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HEADER    HYDROLASE/HYDROLASE INHIBITOR           02-MAY-11   3RT0              
TITLE     CRYSTAL STRUCTURE OF PYL10-HAB1 COMPLEX IN THE ABSENCE OF ABSCISIC    
TITLE    2 ACID (ABA)                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN PHOSPHATASE 2C 16;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 172- 511;                                         
COMPND   5 SYNONYM: ATPP2C16, ATP2C-HA, PROTEIN HYPERSENSITIVE TO ABA 1, PROTEIN
COMPND   6 PHOSPHATASE 2C HAB1, PP2C HAB1;                                      
COMPND   7 EC: 3.1.3.16;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: ABSCISIC ACID RECEPTOR PYL10;                              
COMPND  12 CHAIN: C, D;                                                         
COMPND  13 SYNONYM: ABI1-BINDING PROTEIN 8, PYR1-LIKE PROTEIN 10, REGULATORY    
COMPND  14 COMPONENTS OF ABA RECEPTOR 4;                                        
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: THALE-CRESS;                                        
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: HAB1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE  10 ORGANISM_COMMON: THALE-CRESS;                                        
SOURCE  11 ORGANISM_TAXID: 3702;                                                
SOURCE  12 GENE: PYL10;                                                         
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PYL10-HAB1 BINARY COMPLEX, APO-PYL10 INHIBITS HAB1 DEPHOSPHORYLATION  
KEYWDS   2 ACTIVITY, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.HAO,P.YIN,W.LI,L.WANG,C.YAN,J.WANG,N.YAN                            
REVDAT   1   22-JUN-11 3RT0    0                                                
JRNL        AUTH   Q.HAO,P.YIN,W.LI,L.WANG,C.YAN,Z.LIN,J.Z.WU,J.WANG,S.F.YAN,   
JRNL        AUTH 2 N.YAN                                                        
JRNL        TITL   THE MOLECULAR BASIS OF ABA-INDEPENDENT INHIBITION OF PP2CS   
JRNL        TITL 2 BY A SUBCLASS OF PYL PROTEINS                                
JRNL        REF    MOL.CELL                      V.  42   662 2011              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   21658606                                                     
JRNL        DOI    10.1016/J.MOLCEL.2011.05.011                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.11 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.3_473)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.11                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 55874                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2848                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 32.5031 -  5.7269    0.98     2821   153  0.1825 0.1839        
REMARK   3     2  5.7269 -  4.5496    1.00     2804   158  0.1474 0.1767        
REMARK   3     3  4.5496 -  3.9757    1.00     2795   140  0.1439 0.1872        
REMARK   3     4  3.9757 -  3.6127    1.00     2779   159  0.1547 0.1545        
REMARK   3     5  3.6127 -  3.3540    1.00     2785   146  0.1698 0.1868        
REMARK   3     6  3.3540 -  3.1565    0.99     2756   169  0.1765 0.2072        
REMARK   3     7  3.1565 -  2.9985    0.99     2757   149  0.1843 0.2407        
REMARK   3     8  2.9985 -  2.8681    0.99     2700   157  0.1834 0.2192        
REMARK   3     9  2.8681 -  2.7577    0.98     2738   135  0.1844 0.2064        
REMARK   3    10  2.7577 -  2.6626    0.97     2724   134  0.1822 0.2240        
REMARK   3    11  2.6626 -  2.5794    0.97     2722   145  0.1858 0.2826        
REMARK   3    12  2.5794 -  2.5057    0.95     2602   166  0.1891 0.2546        
REMARK   3    13  2.5057 -  2.4397    0.95     2609   159  0.1899 0.2206        
REMARK   3    14  2.4397 -  2.3802    0.94     2601   140  0.1876 0.2246        
REMARK   3    15  2.3802 -  2.3261    0.94     2628   120  0.1791 0.2188        
REMARK   3    16  2.3261 -  2.2766    0.93     2599   129  0.1796 0.2338        
REMARK   3    17  2.2766 -  2.2311    0.93     2601   119  0.1833 0.2208        
REMARK   3    18  2.2311 -  2.1890    0.90     2484   150  0.1995 0.2865        
REMARK   3    19  2.1890 -  2.1499    0.89     2431   142  0.2001 0.2498        
REMARK   3    20  2.1499 -  2.1135    0.74     2090    78  0.2132 0.2992        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 41.02                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.010           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.43                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.82260                                             
REMARK   3    B22 (A**2) : -3.73850                                             
REMARK   3    B33 (A**2) : 5.56110                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 5.35700                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.020           7881                                  
REMARK   3   ANGLE     :  1.074          10657                                  
REMARK   3   CHIRALITY :  0.071           1200                                  
REMARK   3   PLANARITY :  0.005           1382                                  
REMARK   3   DIHEDRAL  : 17.121           2964                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: all                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  37.9109  15.0621  12.3016              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1137 T22:   0.0984                                     
REMARK   3      T33:   0.1202 T12:  -0.0009                                     
REMARK   3      T13:  -0.0106 T23:   0.0132                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3087 L22:   0.1811                                     
REMARK   3      L33:   0.1284 L12:  -0.0568                                     
REMARK   3      L13:  -0.1667 L23:   0.1248                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0190 S12:  -0.0173 S13:  -0.0316                       
REMARK   3      S21:   0.0023 S22:   0.0057 S23:  -0.0400                       
REMARK   3      S31:  -0.0187 S32:   0.0088 S33:  -0.0197                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3RT0 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-MAY-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065339.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : ROTATED-INCLINED DOUBLE-CRYSTAL    
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58037                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.39900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.160                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3RT2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS, 21% PEG3350, 2% DIOXANE ,    
REMARK 280  PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       41.75150            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   172                                                      
REMARK 465     ASN A   173                                                      
REMARK 465     HIS A   174                                                      
REMARK 465     LEU A   175                                                      
REMARK 465     VAL A   176                                                      
REMARK 465     LYS A   177                                                      
REMARK 465     GLY A   178                                                      
REMARK 465     ARG A   179                                                      
REMARK 465     PRO A   229                                                      
REMARK 465     SER A   230                                                      
REMARK 465     LEU A   231                                                      
REMARK 465     THR A   511                                                      
REMARK 465     SER B   172                                                      
REMARK 465     ASN B   173                                                      
REMARK 465     HIS B   174                                                      
REMARK 465     LEU B   175                                                      
REMARK 465     VAL B   176                                                      
REMARK 465     LYS B   177                                                      
REMARK 465     GLY B   178                                                      
REMARK 465     ARG B   179                                                      
REMARK 465     GLY B   222                                                      
REMARK 465     ASP B   223                                                      
REMARK 465     HIS B   224                                                      
REMARK 465     GLU B   225                                                      
REMARK 465     GLY B   226                                                      
REMARK 465     MET B   227                                                      
REMARK 465     SER B   228                                                      
REMARK 465     PRO B   229                                                      
REMARK 465     LEU B   273                                                      
REMARK 465     SER B   274                                                      
REMARK 465     LYS B   275                                                      
REMARK 465     ARG B   276                                                      
REMARK 465     ASN B   277                                                      
REMARK 465     PHE B   507                                                      
REMARK 465     LYS B   508                                                      
REMARK 465     THR B   509                                                      
REMARK 465     ARG B   510                                                      
REMARK 465     THR B   511                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ASN C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     ASP C     4                                                      
REMARK 465     GLU C     5                                                      
REMARK 465     THR C     6                                                      
REMARK 465     LYS C     7                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     LYS C   181                                                      
REMARK 465     LYS C   182                                                      
REMARK 465     ILE C   183                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ASN D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     ASP D     4                                                      
REMARK 465     GLU D     5                                                      
REMARK 465     THR D     6                                                      
REMARK 465     LYS D     7                                                      
REMARK 465     LYS D     8                                                      
REMARK 465     VAL D     9                                                      
REMARK 465     GLU D    10                                                      
REMARK 465     SER D    11                                                      
REMARK 465     GLU D    12                                                      
REMARK 465     TYR D    13                                                      
REMARK 465     ILE D    14                                                      
REMARK 465     ARG D    19                                                      
REMARK 465     HIS D    20                                                      
REMARK 465     GLU D    21                                                      
REMARK 465     LEU D    22                                                      
REMARK 465     VAL D    23                                                      
REMARK 465     GLU D    24                                                      
REMARK 465     ASP D   128                                                      
REMARK 465     GLY D   129                                                      
REMARK 465     LYS D   181                                                      
REMARK 465     LYS D   182                                                      
REMARK 465     ILE D   183                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU B   376     O    HOH B   682              1.84            
REMARK 500   OE2  GLU B   265     NH1  ARG B   268              1.99            
REMARK 500   NH1  ARG C   173     O    HOH C   213              2.12            
REMARK 500   OE2  GLU C    76     OG1  THR C    89              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   N    VAL C    23     NE2  GLN D    26     1556     2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A 220      -51.40   -120.67                                   
REMARK 500    TRP A 385       86.37   -158.39                                   
REMARK 500    VAL A 393      -65.18    -91.35                                   
REMARK 500    ASN B 198       53.95    -92.38                                   
REMARK 500    ASP B 314      -63.85   -134.34                                   
REMARK 500    TRP B 385       88.69   -154.29                                   
REMARK 500    PHE B 391       29.40     48.05                                   
REMARK 500    VAL B 393      -73.10    -99.28                                   
REMARK 500    GLU C  10      -73.47    -16.51                                   
REMARK 500    GLU C  24      149.27   -178.82                                   
REMARK 500    TYR C  55      -18.94   -150.95                                   
REMARK 500    PRO C  84       46.40    -82.11                                   
REMARK 500    LYS D  16      -70.65    -54.41                                   
REMARK 500    HIS D 100       62.95     66.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 667        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH A 696        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH A 719        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH B 653        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH C 219        DISTANCE =  5.05 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 512  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 243   OD1                                                    
REMARK 620 2 ASP A 432   OD1 125.7                                              
REMARK 620 3 ASP A 492   OD2 162.7  70.3                                        
REMARK 620 4 HOH A 681   O    86.6  97.3  84.6                                  
REMARK 620 5 HOH A 544   O    72.4 161.7  92.2  86.2                            
REMARK 620 6 HOH A 727   O   107.8  73.2  81.9 165.5  99.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 512  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 243   OD2                                                    
REMARK 620 2 ASP B 432   OD1  74.5                                              
REMARK 620 3 ASP B 492   OD2 141.0  70.7                                        
REMARK 620 4 HOH B 673   O    95.7  86.7  99.5                                  
REMARK 620 5 HOH B 674   O    84.2  85.4  76.0 171.9                            
REMARK 620 6 HOH B 675   O   117.5 167.5  98.7  88.6  98.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 512                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 512                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3RT2   RELATED DB: PDB                                   
DBREF  3RT0 A  172   511  UNP    Q9CAJ0   P2C16_ARATH    172    511             
DBREF  3RT0 B  172   511  UNP    Q9CAJ0   P2C16_ARATH    172    511             
DBREF  3RT0 C    1   183  UNP    Q8H1R0   PYL10_ARATH      1    183             
DBREF  3RT0 D    1   183  UNP    Q8H1R0   PYL10_ARATH      1    183             
SEQADV 3RT0 SER A  274  UNP  Q9CAJ0    CYS   274 ENGINEERED MUTATION            
SEQADV 3RT0 SER B  274  UNP  Q9CAJ0    CYS   274 ENGINEERED MUTATION            
SEQADV 3RT0 SER C  162  UNP  Q8H1R0    CYS   162 ENGINEERED MUTATION            
SEQADV 3RT0 SER D  162  UNP  Q8H1R0    CYS   162 ENGINEERED MUTATION            
SEQRES   1 A  340  SER ASN HIS LEU VAL LYS GLY ARG SER VAL TYR GLU LEU          
SEQRES   2 A  340  ASP CYS ILE PRO LEU TRP GLY THR VAL SER ILE GLN GLY          
SEQRES   3 A  340  ASN ARG SER GLU MET GLU ASP ALA PHE ALA VAL SER PRO          
SEQRES   4 A  340  HIS PHE LEU LYS LEU PRO ILE LYS MET LEU MET GLY ASP          
SEQRES   5 A  340  HIS GLU GLY MET SER PRO SER LEU THR HIS LEU THR GLY          
SEQRES   6 A  340  HIS PHE PHE GLY VAL TYR ASP GLY HIS GLY GLY HIS LYS          
SEQRES   7 A  340  VAL ALA ASP TYR CYS ARG ASP ARG LEU HIS PHE ALA LEU          
SEQRES   8 A  340  ALA GLU GLU ILE GLU ARG ILE LYS ASP GLU LEU SER LYS          
SEQRES   9 A  340  ARG ASN THR GLY GLU GLY ARG GLN VAL GLN TRP ASP LYS          
SEQRES  10 A  340  VAL PHE THR SER CYS PHE LEU THR VAL ASP GLY GLU ILE          
SEQRES  11 A  340  GLU GLY LYS ILE GLY ARG ALA VAL VAL GLY SER SER ASP          
SEQRES  12 A  340  LYS VAL LEU GLU ALA VAL ALA SER GLU THR VAL GLY SER          
SEQRES  13 A  340  THR ALA VAL VAL ALA LEU VAL CYS SER SER HIS ILE VAL          
SEQRES  14 A  340  VAL SER ASN CYS GLY ASP SER ARG ALA VAL LEU PHE ARG          
SEQRES  15 A  340  GLY LYS GLU ALA MET PRO LEU SER VAL ASP HIS LYS PRO          
SEQRES  16 A  340  ASP ARG GLU ASP GLU TYR ALA ARG ILE GLU ASN ALA GLY          
SEQRES  17 A  340  GLY LYS VAL ILE GLN TRP GLN GLY ALA ARG VAL PHE GLY          
SEQRES  18 A  340  VAL LEU ALA MET SER ARG SER ILE GLY ASP ARG TYR LEU          
SEQRES  19 A  340  LYS PRO TYR VAL ILE PRO GLU PRO GLU VAL THR PHE MET          
SEQRES  20 A  340  PRO ARG SER ARG GLU ASP GLU CYS LEU ILE LEU ALA SER          
SEQRES  21 A  340  ASP GLY LEU TRP ASP VAL MET ASN ASN GLN GLU VAL CYS          
SEQRES  22 A  340  GLU ILE ALA ARG ARG ARG ILE LEU MET TRP HIS LYS LYS          
SEQRES  23 A  340  ASN GLY ALA PRO PRO LEU ALA GLU ARG GLY LYS GLY ILE          
SEQRES  24 A  340  ASP PRO ALA CYS GLN ALA ALA ALA ASP TYR LEU SER MET          
SEQRES  25 A  340  LEU ALA LEU GLN LYS GLY SER LYS ASP ASN ILE SER ILE          
SEQRES  26 A  340  ILE VAL ILE ASP LEU LYS ALA GLN ARG LYS PHE LYS THR          
SEQRES  27 A  340  ARG THR                                                      
SEQRES   1 B  340  SER ASN HIS LEU VAL LYS GLY ARG SER VAL TYR GLU LEU          
SEQRES   2 B  340  ASP CYS ILE PRO LEU TRP GLY THR VAL SER ILE GLN GLY          
SEQRES   3 B  340  ASN ARG SER GLU MET GLU ASP ALA PHE ALA VAL SER PRO          
SEQRES   4 B  340  HIS PHE LEU LYS LEU PRO ILE LYS MET LEU MET GLY ASP          
SEQRES   5 B  340  HIS GLU GLY MET SER PRO SER LEU THR HIS LEU THR GLY          
SEQRES   6 B  340  HIS PHE PHE GLY VAL TYR ASP GLY HIS GLY GLY HIS LYS          
SEQRES   7 B  340  VAL ALA ASP TYR CYS ARG ASP ARG LEU HIS PHE ALA LEU          
SEQRES   8 B  340  ALA GLU GLU ILE GLU ARG ILE LYS ASP GLU LEU SER LYS          
SEQRES   9 B  340  ARG ASN THR GLY GLU GLY ARG GLN VAL GLN TRP ASP LYS          
SEQRES  10 B  340  VAL PHE THR SER CYS PHE LEU THR VAL ASP GLY GLU ILE          
SEQRES  11 B  340  GLU GLY LYS ILE GLY ARG ALA VAL VAL GLY SER SER ASP          
SEQRES  12 B  340  LYS VAL LEU GLU ALA VAL ALA SER GLU THR VAL GLY SER          
SEQRES  13 B  340  THR ALA VAL VAL ALA LEU VAL CYS SER SER HIS ILE VAL          
SEQRES  14 B  340  VAL SER ASN CYS GLY ASP SER ARG ALA VAL LEU PHE ARG          
SEQRES  15 B  340  GLY LYS GLU ALA MET PRO LEU SER VAL ASP HIS LYS PRO          
SEQRES  16 B  340  ASP ARG GLU ASP GLU TYR ALA ARG ILE GLU ASN ALA GLY          
SEQRES  17 B  340  GLY LYS VAL ILE GLN TRP GLN GLY ALA ARG VAL PHE GLY          
SEQRES  18 B  340  VAL LEU ALA MET SER ARG SER ILE GLY ASP ARG TYR LEU          
SEQRES  19 B  340  LYS PRO TYR VAL ILE PRO GLU PRO GLU VAL THR PHE MET          
SEQRES  20 B  340  PRO ARG SER ARG GLU ASP GLU CYS LEU ILE LEU ALA SER          
SEQRES  21 B  340  ASP GLY LEU TRP ASP VAL MET ASN ASN GLN GLU VAL CYS          
SEQRES  22 B  340  GLU ILE ALA ARG ARG ARG ILE LEU MET TRP HIS LYS LYS          
SEQRES  23 B  340  ASN GLY ALA PRO PRO LEU ALA GLU ARG GLY LYS GLY ILE          
SEQRES  24 B  340  ASP PRO ALA CYS GLN ALA ALA ALA ASP TYR LEU SER MET          
SEQRES  25 B  340  LEU ALA LEU GLN LYS GLY SER LYS ASP ASN ILE SER ILE          
SEQRES  26 B  340  ILE VAL ILE ASP LEU LYS ALA GLN ARG LYS PHE LYS THR          
SEQRES  27 B  340  ARG THR                                                      
SEQRES   1 C  183  MET ASN GLY ASP GLU THR LYS LYS VAL GLU SER GLU TYR          
SEQRES   2 C  183  ILE LYS LYS HIS HIS ARG HIS GLU LEU VAL GLU SER GLN          
SEQRES   3 C  183  CYS SER SER THR LEU VAL LYS HIS ILE LYS ALA PRO LEU          
SEQRES   4 C  183  HIS LEU VAL TRP SER ILE VAL ARG ARG PHE ASP GLU PRO          
SEQRES   5 C  183  GLN LYS TYR LYS PRO PHE ILE SER ARG CYS VAL VAL GLN          
SEQRES   6 C  183  GLY LYS LYS LEU GLU VAL GLY SER VAL ARG GLU VAL ASP          
SEQRES   7 C  183  LEU LYS SER GLY LEU PRO ALA THR LYS SER THR GLU VAL          
SEQRES   8 C  183  LEU GLU ILE LEU ASP ASP ASN GLU HIS ILE LEU GLY ILE          
SEQRES   9 C  183  ARG ILE VAL GLY GLY ASP HIS ARG LEU LYS ASN TYR SER          
SEQRES  10 C  183  SER THR ILE SER LEU HIS SER GLU THR ILE ASP GLY LYS          
SEQRES  11 C  183  THR GLY THR LEU ALA ILE GLU SER PHE VAL VAL ASP VAL          
SEQRES  12 C  183  PRO GLU GLY ASN THR LYS GLU GLU THR CYS PHE PHE VAL          
SEQRES  13 C  183  GLU ALA LEU ILE GLN SER ASN LEU ASN SER LEU ALA ASP          
SEQRES  14 C  183  VAL THR GLU ARG LEU GLN ALA GLU SER MET GLU LYS LYS          
SEQRES  15 C  183  ILE                                                          
SEQRES   1 D  183  MET ASN GLY ASP GLU THR LYS LYS VAL GLU SER GLU TYR          
SEQRES   2 D  183  ILE LYS LYS HIS HIS ARG HIS GLU LEU VAL GLU SER GLN          
SEQRES   3 D  183  CYS SER SER THR LEU VAL LYS HIS ILE LYS ALA PRO LEU          
SEQRES   4 D  183  HIS LEU VAL TRP SER ILE VAL ARG ARG PHE ASP GLU PRO          
SEQRES   5 D  183  GLN LYS TYR LYS PRO PHE ILE SER ARG CYS VAL VAL GLN          
SEQRES   6 D  183  GLY LYS LYS LEU GLU VAL GLY SER VAL ARG GLU VAL ASP          
SEQRES   7 D  183  LEU LYS SER GLY LEU PRO ALA THR LYS SER THR GLU VAL          
SEQRES   8 D  183  LEU GLU ILE LEU ASP ASP ASN GLU HIS ILE LEU GLY ILE          
SEQRES   9 D  183  ARG ILE VAL GLY GLY ASP HIS ARG LEU LYS ASN TYR SER          
SEQRES  10 D  183  SER THR ILE SER LEU HIS SER GLU THR ILE ASP GLY LYS          
SEQRES  11 D  183  THR GLY THR LEU ALA ILE GLU SER PHE VAL VAL ASP VAL          
SEQRES  12 D  183  PRO GLU GLY ASN THR LYS GLU GLU THR CYS PHE PHE VAL          
SEQRES  13 D  183  GLU ALA LEU ILE GLN SER ASN LEU ASN SER LEU ALA ASP          
SEQRES  14 D  183  VAL THR GLU ARG LEU GLN ALA GLU SER MET GLU LYS LYS          
SEQRES  15 D  183  ILE                                                          
HET     MG  A 512       1                                                       
HET     MG  B 512       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   7  HOH   *507(H2 O)                                                    
HELIX    1   1 SER A  180  LEU A  184  5                                   5    
HELIX    2   2 LYS A  218  LEU A  220  5                                   3    
HELIX    3   3 HIS A  248  ARG A  276  1                                  29    
HELIX    4   4 GLY A  281  GLU A  302  1                                  22    
HELIX    5   5 ARG A  368  ALA A  378  1                                  11    
HELIX    6   6 ARG A  403  LYS A  406  5                                   4    
HELIX    7   7 SER A  431  ASP A  436  1                                   6    
HELIX    8   8 ASN A  439  ASN A  458  1                                  20    
HELIX    9   9 PRO A  462  ARG A  466  5                                   5    
HELIX   10  10 ASP A  471  LYS A  488  1                                  18    
HELIX   11  11 SER B  180  LEU B  184  5                                   5    
HELIX   12  12 LYS B  218  LEU B  220  5                                   3    
HELIX   13  13 HIS B  248  LYS B  270  1                                  23    
HELIX   14  14 GLY B  281  GLU B  302  1                                  22    
HELIX   15  15 ARG B  368  ALA B  378  1                                  11    
HELIX   16  16 ARG B  403  LYS B  406  5                                   4    
HELIX   17  17 SER B  431  ASP B  436  1                                   6    
HELIX   18  18 ASN B  439  GLY B  459  1                                  21    
HELIX   19  19 PRO B  462  ARG B  466  5                                   5    
HELIX   20  20 ASP B  471  LYS B  488  1                                  18    
HELIX   21  21 VAL C    9  HIS C   18  1                                  10    
HELIX   22  22 PRO C   38  ARG C   47  1                                  10    
HELIX   23  23 GLU C   51  TYR C   55  5                                   5    
HELIX   24  24 THR C  148  GLU C  180  1                                  33    
HELIX   25  25 PRO D   38  ARG D   47  1                                  10    
HELIX   26  26 GLU D   51  TYR D   55  5                                   5    
HELIX   27  27 THR D  148  GLU D  177  1                                  30    
SHEET    1   A 5 TRP A 190  ILE A 195  0                                        
SHEET    2   A 5 ILE A 494  ASP A 500 -1  O  ILE A 496   N  VAL A 193           
SHEET    3   A 5 ASP A 424  ALA A 430 -1  N  LEU A 429   O  ILE A 497           
SHEET    4   A 5 ARG A 348  ARG A 353 -1  N  PHE A 352   O  GLU A 425           
SHEET    5   A 5 GLU A 356  PRO A 359 -1  O  MET A 358   N  LEU A 351           
SHEET    1   B 4 ASP A 204  PRO A 216  0                                        
SHEET    2   B 4 HIS A 233  HIS A 245 -1  O  TYR A 242   N  ALA A 205           
SHEET    3   B 4 GLY A 326  SER A 327 -1  O  GLY A 326   N  HIS A 245           
SHEET    4   B 4 ILE A 400  GLY A 401 -1  O  ILE A 400   N  SER A 327           
SHEET    1   C 5 ASP A 204  PRO A 216  0                                        
SHEET    2   C 5 HIS A 233  HIS A 245 -1  O  TYR A 242   N  ALA A 205           
SHEET    3   C 5 ALA A 329  VAL A 334 -1  O  ALA A 332   N  PHE A 239           
SHEET    4   C 5 HIS A 338  CYS A 344 -1  O  VAL A 340   N  LEU A 333           
SHEET    5   C 5 GLU A 414  PRO A 419 -1  O  THR A 416   N  VAL A 341           
SHEET    1   D 2 ARG A 307  ALA A 308  0                                        
SHEET    2   D 2 LYS A 315  VAL A 316 -1  O  VAL A 316   N  ARG A 307           
SHEET    1   E 2 VAL A 382  GLN A 384  0                                        
SHEET    2   E 2 ALA A 388  VAL A 390 -1  O  ARG A 389   N  ILE A 383           
SHEET    1   F 5 TRP B 190  ILE B 195  0                                        
SHEET    2   F 5 ILE B 494  ASP B 500 -1  O  ILE B 496   N  VAL B 193           
SHEET    3   F 5 ASP B 424  ALA B 430 -1  N  LEU B 429   O  ILE B 497           
SHEET    4   F 5 ARG B 348  ARG B 353 -1  N  VAL B 350   O  ILE B 428           
SHEET    5   F 5 GLU B 356  PRO B 359 -1  O  MET B 358   N  LEU B 351           
SHEET    1   G 4 ASP B 204  PRO B 216  0                                        
SHEET    2   G 4 HIS B 233  HIS B 245 -1  O  LEU B 234   N  LEU B 215           
SHEET    3   G 4 GLY B 326  SER B 327 -1  O  GLY B 326   N  HIS B 245           
SHEET    4   G 4 ILE B 400  GLY B 401 -1  O  ILE B 400   N  SER B 327           
SHEET    1   H 5 ASP B 204  PRO B 216  0                                        
SHEET    2   H 5 HIS B 233  HIS B 245 -1  O  LEU B 234   N  LEU B 215           
SHEET    3   H 5 ALA B 329  VAL B 334 -1  O  ALA B 332   N  PHE B 239           
SHEET    4   H 5 HIS B 338  CYS B 344 -1  O  SER B 342   N  VAL B 331           
SHEET    5   H 5 GLU B 414  PRO B 419 -1  O  MET B 418   N  ILE B 339           
SHEET    1   I 2 ARG B 307  VAL B 309  0                                        
SHEET    2   I 2 SER B 312  VAL B 316 -1  O  VAL B 316   N  ARG B 307           
SHEET    1   J 2 VAL B 382  GLN B 384  0                                        
SHEET    2   J 2 ALA B 388  VAL B 390 -1  O  ARG B 389   N  ILE B 383           
SHEET    1   K 7 GLN C  26  ILE C  35  0                                        
SHEET    2   K 7 LYS C 130  ASP C 142 -1  O  THR C 133   N  ILE C  35           
SHEET    3   K 7 LYS C 114  ILE C 127 -1  N  HIS C 123   O  LEU C 134           
SHEET    4   K 7 ILE C 101  GLY C 109 -1  N  ILE C 106   O  TYR C 116           
SHEET    5   K 7 LYS C  87  ASP C  96 -1  N  THR C  89   O  VAL C 107           
SHEET    6   K 7 VAL C  74  LEU C  79 -1  N  VAL C  77   O  SER C  88           
SHEET    7   K 7 ILE C  59  VAL C  64 -1  N  VAL C  63   O  GLU C  76           
SHEET    1   L 7 GLN D  26  ILE D  35  0                                        
SHEET    2   L 7 GLY D 132  ASP D 142 -1  O  THR D 133   N  ILE D  35           
SHEET    3   L 7 SER D 117  GLU D 125 -1  N  HIS D 123   O  LEU D 134           
SHEET    4   L 7 ILE D 101  GLY D 109 -1  N  LEU D 102   O  ILE D 120           
SHEET    5   L 7 LYS D  87  ASP D  96 -1  N  ILE D  94   O  GLY D 103           
SHEET    6   L 7 VAL D  74  LEU D  79 -1  N  VAL D  77   O  SER D  88           
SHEET    7   L 7 ILE D  59  VAL D  64 -1  N  SER D  60   O  ASP D  78           
LINK         OD1 ASP A 243                MG    MG A 512     1555   1555  2.65  
LINK         OD2 ASP B 243                MG    MG B 512     1555   1555  2.49  
LINK         OD1 ASP A 432                MG    MG A 512     1555   1555  2.45  
LINK         OD1 ASP B 432                MG    MG B 512     1555   1555  2.43  
LINK         OD2 ASP B 492                MG    MG B 512     1555   1555  2.33  
LINK         OD2 ASP A 492                MG    MG A 512     1555   1555  2.55  
LINK        MG    MG B 512                 O   HOH B 673     1555   1555  2.09  
LINK        MG    MG A 512                 O   HOH A 681     1555   1555  2.33  
LINK        MG    MG B 512                 O   HOH B 674     1555   1555  2.35  
LINK        MG    MG B 512                 O   HOH B 675     1555   1555  2.42  
LINK        MG    MG A 512                 O   HOH A 544     1555   1555  2.43  
LINK        MG    MG A 512                 O   HOH A 727     1555   1555  2.45  
CISPEP   1 LYS A  406    PRO A  407          0        -0.43                     
CISPEP   2 SER B  313    ASP B  314          0         3.65                     
CISPEP   3 LYS B  406    PRO B  407          0         6.72                     
SITE     1 AC1  6 ASP A 243  ASP A 432  ASP A 492  HOH A 544                    
SITE     2 AC1  6 HOH A 681  HOH A 727                                          
SITE     1 AC2  6 ASP B 243  ASP B 432  ASP B 492  HOH B 673                    
SITE     2 AC2  6 HOH B 674  HOH B 675                                          
CRYST1   70.766   83.503   88.544  90.00  97.20  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014131  0.000000  0.001785        0.00000                         
SCALE2      0.000000  0.011976  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011384        0.00000                         
ATOM      1  N   SER A 180      32.313  22.029 -13.662  1.00 55.57           N  
ANISOU    1  N   SER A 180     7265   7178   6672    338     91    150       N  
ATOM      2  CA  SER A 180      32.437  22.711 -12.372  1.00 66.04           C  
ANISOU    2  CA  SER A 180     8598   8468   8028    323     98    166       C  
ATOM      3  C   SER A 180      31.561  22.084 -11.287  1.00 64.97           C  
ANISOU    3  C   SER A 180     8438   8335   7912    310     69    151       C  
ATOM      4  O   SER A 180      30.379  21.807 -11.508  1.00 59.11           O  
ANISOU    4  O   SER A 180     7684   7624   7149    328     47    144       O  
ATOM      5  CB  SER A 180      32.103  24.195 -12.502  1.00 69.73           C  
ANISOU    5  CB  SER A 180     9094   8927   8472    350    121    200       C  
ATOM      6  OG  SER A 180      32.051  24.811 -11.222  1.00 71.23           O  
ANISOU    6  OG  SER A 180     9288   9086   8691    337    125    211       O  
ATOM      7  N   VAL A 181      32.147  21.884 -10.111  1.00 48.88           N  
ANISOU    7  N   VAL A 181     6393   6265   5913    280     68    147       N  
ATOM      8  CA  VAL A 181      31.456  21.221  -9.012  1.00 52.12           C  
ANISOU    8  CA  VAL A 181     6782   6675   6346    265     43    134       C  
ATOM      9  C   VAL A 181      30.255  22.035  -8.521  1.00 51.31           C  
ANISOU    9  C   VAL A 181     6686   6579   6230    284     37    150       C  
ATOM     10  O   VAL A 181      29.249  21.463  -8.118  1.00 47.02           O  
ANISOU   10  O   VAL A 181     6125   6052   5689    284     13    138       O  
ATOM     11  CB  VAL A 181      32.410  20.933  -7.835  1.00 44.85           C  
ANISOU   11  CB  VAL A 181     5854   5719   5467    232     46    129       C  
ATOM     12  CG1 VAL A 181      32.690  22.206  -7.054  1.00 44.83           C  
ANISOU   12  CG1 VAL A 181     5872   5688   5473    230     65    152       C  
ATOM     13  CG2 VAL A 181      31.836  19.849  -6.925  1.00 35.37           C  
ANISOU   13  CG2 VAL A 181     4628   4521   4289    215     19    111       C  
ATOM     14  N   TYR A 182      30.358  23.362  -8.568  1.00 54.87           N  
ANISOU   14  N   TYR A 182     7163   7016   6670    299     60    177       N  
ATOM     15  CA  TYR A 182      29.252  24.231  -8.157  1.00 57.64           C  
ANISOU   15  CA  TYR A 182     7522   7371   7008    319     57    195       C  
ATOM     16  C   TYR A 182      28.127  24.262  -9.184  1.00 62.24           C  
ANISOU   16  C   TYR A 182     8103   7994   7551    354     45    196       C  
ATOM     17  O   TYR A 182      27.182  25.038  -9.059  1.00 69.25           O  
ANISOU   17  O   TYR A 182     8998   8889   8424    376     43    212       O  
ATOM     18  CB  TYR A 182      29.744  25.654  -7.891  1.00 54.30           C  
ANISOU   18  CB  TYR A 182     7126   6918   6589    324     89    223       C  
ATOM     19  CG  TYR A 182      30.749  25.751  -6.769  1.00 59.25           C  
ANISOU   19  CG  TYR A 182     7752   7507   7254    291    100    220       C  
ATOM     20  CD1 TYR A 182      30.337  25.798  -5.440  1.00 54.76           C  
ANISOU   20  CD1 TYR A 182     7173   6925   6707    275     89    217       C  
ATOM     21  CD2 TYR A 182      32.112  25.788  -7.036  1.00 56.76           C  
ANISOU   21  CD2 TYR A 182     7443   7170   6951    275    122    218       C  
ATOM     22  CE1 TYR A 182      31.258  25.880  -4.406  1.00 41.30           C  
ANISOU   22  CE1 TYR A 182     5467   5191   5036    245     97    213       C  
ATOM     23  CE2 TYR A 182      33.040  25.873  -6.012  1.00 55.56           C  
ANISOU   23  CE2 TYR A 182     7289   6988   6835    246    130    212       C  
ATOM     24  CZ  TYR A 182      32.609  25.917  -4.701  1.00 52.91           C  
ANISOU   24  CZ  TYR A 182     6943   6642   6518    232    117    210       C  
ATOM     25  OH  TYR A 182      33.536  25.999  -3.689  1.00 54.96           O  
ANISOU   25  OH  TYR A 182     7198   6874   6809    204    125    203       O  
ATOM     26  N   GLU A 183      28.223  23.400 -10.187  1.00 71.79           N  
ANISOU   26  N   GLU A 183     9302   9232   8745    359     35    178       N  
ATOM     27  CA  GLU A 183      27.290  23.400 -11.304  1.00 68.46           C  
ANISOU   27  CA  GLU A 183     8879   8853   8281    394     24    177       C  
ATOM     28  C   GLU A 183      26.552  22.062 -11.393  1.00 73.68           C  
ANISOU   28  C   GLU A 183     9507   9545   8945    387     -8    141       C  
ATOM     29  O   GLU A 183      25.464  21.976 -11.968  1.00 71.54           O  
ANISOU   29  O   GLU A 183     9226   9312   8645    413    -25    133       O  
ATOM     30  CB  GLU A 183      28.074  23.648 -12.591  1.00 75.50           C  
ANISOU   30  CB  GLU A 183     9788   9754   9146    410     44    185       C  
ATOM     31  CG  GLU A 183      27.357  24.438 -13.663  1.00 85.15           C  
ANISOU   31  CG  GLU A 183    11026  11007  10319    454     49    206       C  
ATOM     32  CD  GLU A 183      28.288  24.813 -14.812  1.00 96.83           C  
ANISOU   32  CD  GLU A 183    12529  12489  11775    468     76    220       C  
ATOM     33  OE1 GLU A 183      28.292  24.091 -15.835  1.00100.60           O  
ANISOU   33  OE1 GLU A 183    12996  13001  12227    477     66    201       O  
ATOM     34  OE2 GLU A 183      29.022  25.822 -14.687  1.00 84.69           O  
ANISOU   34  OE2 GLU A 183    11017  10917  10243    468    108    248       O  
ATOM     35  N   LEU A 184      27.157  21.021 -10.823  1.00 71.45           N  
ANISOU   35  N   LEU A 184     9206   9246   8697    353    -15    118       N  
ATOM     36  CA  LEU A 184      26.611  19.668 -10.900  1.00 62.21           C  
ANISOU   36  CA  LEU A 184     8003   8099   7534    342    -40     83       C  
ATOM     37  C   LEU A 184      25.316  19.494 -10.110  1.00 74.09           C  
ANISOU   37  C   LEU A 184     9491   9614   9047    344    -61     74       C  
ATOM     38  O   LEU A 184      25.078  20.184  -9.111  1.00 69.00           O  
ANISOU   38  O   LEU A 184     8856   8945   8416    340    -57     93       O  
ATOM     39  CB  LEU A 184      27.641  18.640 -10.419  1.00 65.74           C  
ANISOU   39  CB  LEU A 184     8437   8521   8020    305    -38     65       C  
ATOM     40  CG  LEU A 184      28.688  18.132 -11.414  1.00 74.47           C  
ANISOU   40  CG  LEU A 184     9542   9631   9121    300    -28     53       C  
ATOM     41  CD1 LEU A 184      28.288  18.457 -12.854  1.00 68.37           C  
ANISOU   41  CD1 LEU A 184     8777   8899   8301    333    -26     54       C  
ATOM     42  CD2 LEU A 184      30.062  18.694 -11.087  1.00 66.82           C  
ANISOU   42  CD2 LEU A 184     8594   8624   8170    284     -3     73       C  
ATOM     43  N   ASP A 185      24.488  18.560 -10.567  1.00 92.12           N  
ANISOU   43  N   ASP A 185    11747  11930  11323    349    -82     44       N  
ATOM     44  CA  ASP A 185      23.268  18.191  -9.861  1.00 90.91           C  
ANISOU   44  CA  ASP A 185    11574  11787  11182    347   -101     29       C  
ATOM     45  C   ASP A 185      23.583  17.352  -8.628  1.00 83.19           C  
ANISOU   45  C   ASP A 185    10581  10776  10250    310   -104     17       C  
ATOM     46  O   ASP A 185      24.234  16.307  -8.721  1.00 83.25           O  
ANISOU   46  O   ASP A 185    10574  10777  10279    288   -104     -3       O  
ATOM     47  CB  ASP A 185      22.328  17.415 -10.783  1.00102.08           C  
ANISOU   47  CB  ASP A 185    12962  13249  12576    363   -121     -5       C  
ATOM     48  CG  ASP A 185      21.586  18.315 -11.750  1.00113.18           C  
ANISOU   48  CG  ASP A 185    14378  14691  13933    405   -125      7       C  
ATOM     49  OD1 ASP A 185      21.197  19.433 -11.341  1.00112.71           O  
ANISOU   49  OD1 ASP A 185    14338  14623  13865    422   -119     37       O  
ATOM     50  OD2 ASP A 185      21.397  17.906 -12.916  1.00116.83           O  
ANISOU   50  OD2 ASP A 185    14829  15193  14367    422   -133    -13       O  
ATOM     51  N   CYS A 186      23.116  17.811  -7.472  1.00 47.55           N  
ANISOU   51  N   CYS A 186     6072   6243   5753    303   -105     31       N  
ATOM     52  CA  CYS A 186      23.341  17.089  -6.230  1.00 38.45           C  
ANISOU   52  CA  CYS A 186     4908   5061   4641    271   -107     24       C  
ATOM     53  C   CYS A 186      22.129  16.229  -5.883  1.00 33.68           C  
ANISOU   53  C   CYS A 186     4276   4472   4048    267   -125     -3       C  
ATOM     54  O   CYS A 186      21.165  16.711  -5.309  1.00 31.09           O  
ANISOU   54  O   CYS A 186     3948   4147   3719    275   -131      2       O  
ATOM     55  CB  CYS A 186      23.633  18.068  -5.102  1.00 37.39           C  
ANISOU   55  CB  CYS A 186     4796   4894   4519    264    -96     53       C  
ATOM     56  SG  CYS A 186      24.193  17.276  -3.587  1.00 27.40           S  
ANISOU   56  SG  CYS A 186     3521   3592   3299    226    -96     49       S  
ATOM     57  N   ILE A 187      22.174  14.951  -6.243  1.00 30.40           N  
ANISOU   57  N   ILE A 187     3836   4066   3648    254   -132    -34       N  
ATOM     58  CA  ILE A 187      21.069  14.047  -5.945  1.00 28.51           C  
ANISOU   58  CA  ILE A 187     3568   3840   3424    248   -146    -64       C  
ATOM     59  C   ILE A 187      21.271  13.398  -4.577  1.00 23.72           C  
ANISOU   59  C   ILE A 187     2955   3197   2859    218   -142    -62       C  
ATOM     60  O   ILE A 187      22.267  12.713  -4.343  1.00 22.96           O  
ANISOU   60  O   ILE A 187     2858   3080   2787    197   -135    -63       O  
ATOM     61  CB  ILE A 187      20.900  12.970  -7.037  1.00 35.41           C  
ANISOU   61  CB  ILE A 187     4415   4744   4295    250   -153   -101       C  
ATOM     62  CG1 ILE A 187      20.517  13.626  -8.372  1.00 37.02           C  
ANISOU   62  CG1 ILE A 187     4624   4990   4452    284   -159   -103       C  
ATOM     63  CG2 ILE A 187      19.874  11.924  -6.610  1.00 31.89           C  
ANISOU   63  CG2 ILE A 187     3938   4304   3874    238   -163   -135       C  
ATOM     64  CD1 ILE A 187      20.350  12.641  -9.503  1.00 46.95           C  
ANISOU   64  CD1 ILE A 187     5855   6282   5702    287   -167   -143       C  
ATOM     65  N   PRO A 188      20.325  13.627  -3.666  1.00 20.38           N  
ANISOU   65  N   PRO A 188     2529   2769   2444    217   -147    -59       N  
ATOM     66  CA  PRO A 188      20.468  13.158  -2.279  1.00 20.87           C  
ANISOU   66  CA  PRO A 188     2589   2798   2542    191   -143    -53       C  
ATOM     67  C   PRO A 188      20.102  11.680  -2.115  1.00 20.60           C  
ANISOU   67  C   PRO A 188     2526   2763   2539    173   -146    -84       C  
ATOM     68  O   PRO A 188      18.974  11.267  -2.404  1.00 21.75           O  
ANISOU   68  O   PRO A 188     2650   2930   2683    180   -154   -111       O  
ATOM     69  CB  PRO A 188      19.486  14.048  -1.506  1.00 18.30           C  
ANISOU   69  CB  PRO A 188     2272   2472   2209    200   -145    -39       C  
ATOM     70  CG  PRO A 188      18.416  14.404  -2.513  1.00 21.47           C  
ANISOU   70  CG  PRO A 188     2664   2912   2581    228   -156    -55       C  
ATOM     71  CD  PRO A 188      19.099  14.430  -3.875  1.00 21.51           C  
ANISOU   71  CD  PRO A 188     2673   2938   2563    242   -155    -59       C  
ATOM     72  N   LEU A 189      21.070  10.894  -1.663  1.00 17.53           N  
ANISOU   72  N   LEU A 189     2135   2347   2177    151   -138    -82       N  
ATOM     73  CA  LEU A 189      20.899   9.467  -1.450  1.00 20.54           C  
ANISOU   73  CA  LEU A 189     2491   2721   2592    132   -136   -108       C  
ATOM     74  C   LEU A 189      21.060   9.143   0.027  1.00 15.64           C  
ANISOU   74  C   LEU A 189     1875   2065   2001    112   -130    -91       C  
ATOM     75  O   LEU A 189      22.156   9.287   0.570  1.00 15.51           O  
ANISOU   75  O   LEU A 189     1875   2026   1994    103   -124    -68       O  
ATOM     76  CB  LEU A 189      21.955   8.690  -2.236  1.00 19.92           C  
ANISOU   76  CB  LEU A 189     2405   2640   2524    125   -132   -120       C  
ATOM     77  CG  LEU A 189      22.007   8.868  -3.754  1.00 25.36           C  
ANISOU   77  CG  LEU A 189     3090   3363   3183    142   -136   -138       C  
ATOM     78  CD1 LEU A 189      23.068   7.957  -4.366  1.00 23.85           C  
ANISOU   78  CD1 LEU A 189     2889   3165   3008    130   -129   -151       C  
ATOM     79  CD2 LEU A 189      20.656   8.548  -4.339  1.00 21.44           C  
ANISOU   79  CD2 LEU A 189     2570   2900   2678    154   -146   -171       C  
ATOM     80  N   TRP A 190      19.989   8.690   0.679  1.00 17.27           N  
ANISOU   80  N   TRP A 190     2067   2270   2225    107   -130   -104       N  
ATOM     81  CA  TRP A 190      20.062   8.410   2.109  1.00 16.58           C  
ANISOU   81  CA  TRP A 190     1986   2152   2162     89   -123    -86       C  
ATOM     82  C   TRP A 190      19.120   7.306   2.563  1.00 17.04           C  
ANISOU   82  C   TRP A 190     2020   2204   2251     78   -118   -110       C  
ATOM     83  O   TRP A 190      18.158   6.957   1.874  1.00 21.51           O  
ANISOU   83  O   TRP A 190     2564   2791   2816     84   -121   -141       O  
ATOM     84  CB  TRP A 190      19.751   9.671   2.925  1.00 13.53           C  
ANISOU   84  CB  TRP A 190     1621   1761   1757     96   -125    -59       C  
ATOM     85  CG  TRP A 190      18.265   9.888   3.060  1.00 15.41           C  
ANISOU   85  CG  TRP A 190     1849   2016   1991    104   -129    -74       C  
ATOM     86  CD1 TRP A 190      17.458   9.483   4.092  1.00 17.38           C  
ANISOU   86  CD1 TRP A 190     2092   2252   2261     93   -125    -77       C  
ATOM     87  CD2 TRP A 190      17.408  10.547   2.119  1.00 18.24           C  
ANISOU   87  CD2 TRP A 190     2202   2405   2321    126   -139    -88       C  
ATOM     88  NE1 TRP A 190      16.150   9.871   3.856  1.00 20.09           N  
ANISOU   88  NE1 TRP A 190     2424   2616   2593    105   -130    -94       N  
ATOM     89  CE2 TRP A 190      16.095  10.514   2.646  1.00 18.81           C  
ANISOU   89  CE2 TRP A 190     2262   2482   2401    127   -140   -101       C  
ATOM     90  CE3 TRP A 190      17.625  11.164   0.882  1.00 20.15           C  
ANISOU   90  CE3 TRP A 190     2449   2674   2533    147   -146    -90       C  
ATOM     91  CZ2 TRP A 190      15.004  11.069   1.970  1.00 24.02           C  
ANISOU   91  CZ2 TRP A 190     2913   3173   3039    148   -150   -117       C  
ATOM     92  CZ3 TRP A 190      16.538  11.724   0.216  1.00 25.56           C  
ANISOU   92  CZ3 TRP A 190     3127   3391   3195    169   -155   -104       C  
ATOM     93  CH2 TRP A 190      15.247  11.674   0.765  1.00 23.67           C  
ANISOU   93  CH2 TRP A 190     2873   3155   2964    170   -158   -118       C  
ATOM     94  N   GLY A 191      19.404   6.775   3.748  1.00 14.37           N  
ANISOU   94  N   GLY A 191     1686   1836   1939     61   -109    -94       N  
ATOM     95  CA  GLY A 191      18.524   5.814   4.403  1.00 17.25           C  
ANISOU   95  CA  GLY A 191     2032   2188   2333     49    -99   -110       C  
ATOM     96  C   GLY A 191      18.475   6.136   5.890  1.00 21.45           C  
ANISOU   96  C   GLY A 191     2583   2697   2872     41    -94    -81       C  
ATOM     97  O   GLY A 191      19.412   6.742   6.434  1.00 19.64           O  
ANISOU   97  O   GLY A 191     2375   2456   2631     40    -96    -50       O  
ATOM     98  N  ATHR A 192      17.405   5.730   6.562  0.50 14.15           N  
ANISOU   98  N  ATHR A 192     1648   1766   1964     34    -86    -91       N  
ATOM     99  N  BTHR A 192      17.399   5.754   6.559  0.50 14.15           N  
ANISOU   99  N  BTHR A 192     1648   1766   1963     34    -86    -90       N  
ATOM    100  CA ATHR A 192      17.238   6.085   7.962  0.50 17.46           C  
ANISOU  100  CA ATHR A 192     2083   2166   2385     27    -81    -64       C  
ATOM    101  CA BTHR A 192      17.274   6.085   7.968  0.50 17.46           C  
ANISOU  101  CA BTHR A 192     2083   2165   2384     27    -81    -64       C  
ATOM    102  C  ATHR A 192      16.632   4.971   8.788  0.50 17.44           C  
ANISOU  102  C  ATHR A 192     2068   2142   2417     13    -64    -72       C  
ATOM    103  C  BTHR A 192      16.629   4.984   8.790  0.50 17.44           C  
ANISOU  103  C  BTHR A 192     2068   2142   2416     13    -64    -72       C  
ATOM    104  O  ATHR A 192      15.719   4.281   8.339  0.50 15.31           O  
ANISOU  104  O  ATHR A 192     1774   1877   2164     10    -58   -104       O  
ATOM    105  O  BTHR A 192      15.690   4.327   8.350  0.50 15.30           O  
ANISOU  105  O  BTHR A 192     1774   1878   2163     11    -58   -104       O  
ATOM    106  CB ATHR A 192      16.282   7.309   8.154  0.50 17.03           C  
ANISOU  106  CB ATHR A 192     2038   2129   2305     38    -88    -62       C  
ATOM    107  CB BTHR A 192      16.482   7.400   8.179  0.50 17.01           C  
ANISOU  107  CB BTHR A 192     2038   2124   2299     39    -89    -57       C  
ATOM    108  OG1ATHR A 192      16.698   8.407   7.338  0.50 26.00           O  
ANISOU  108  OG1ATHR A 192     3185   3285   3408     54   -101    -55       O  
ATOM    109  OG1BTHR A 192      15.094   7.172   7.921  0.50 26.15           O  
ANISOU  109  OG1BTHR A 192     3176   3295   3464     41    -88    -87       O  
ATOM    110  CG2ATHR A 192      16.299   7.761   9.624  0.50 23.89           C  
ANISOU  110  CG2ATHR A 192     2926   2978   3173     31    -83    -32       C  
ATOM    111  CG2BTHR A 192      16.980   8.482   7.249  0.50 23.92           C  
ANISOU  111  CG2BTHR A 192     2925   3021   3142     55   -102    -51       C  
ATOM    112  N  AVAL A 193      17.144   4.797  10.000  0.50 17.13           N  
ANISOU  112  N  AVAL A 193     2044   2078   2387      4    -56    -42       N  
ATOM    113  N  BVAL A 193      17.150   4.796   9.993  0.50 17.05           N  
ANISOU  113  N  BVAL A 193     2034   2068   2377      4    -56    -42       N  
ATOM    114  CA AVAL A 193      16.502   3.931  10.982  0.50 18.95           C  
ANISOU  114  CA AVAL A 193     2269   2287   2645     -9    -38    -42       C  
ATOM    115  CA BVAL A 193      16.501   3.949  10.985  0.50 18.93           C  
ANISOU  115  CA BVAL A 193     2267   2285   2643     -8    -38    -42       C  
ATOM    116  C  AVAL A 193      16.424   4.672  12.308  0.50 19.60           C  
ANISOU  116  C  AVAL A 193     2373   2360   2713    -10    -37    -12       C  
ATOM    117  C  BVAL A 193      16.392   4.746  12.269  0.50 19.57           C  
ANISOU  117  C  BVAL A 193     2370   2358   2707     -9    -38    -12       C  
ATOM    118  O  AVAL A 193      17.391   5.308  12.730  0.50 20.73           O  
ANISOU  118  O  AVAL A 193     2537   2502   2838     -7    -45     16       O  
ATOM    119  O  BVAL A 193      17.309   5.487  12.628  0.50 20.84           O  
ANISOU  119  O  BVAL A 193     2551   2520   2847     -6    -47     14       O  
ATOM    120  CB AVAL A 193      17.258   2.590  11.167  0.50 19.82           C  
ANISOU  120  CB AVAL A 193     2371   2371   2788    -19    -23    -38       C  
ATOM    121  CB BVAL A 193      17.303   2.655  11.261  0.50 19.82           C  
ANISOU  121  CB BVAL A 193     2373   2370   2786    -18    -24    -34       C  
ATOM    122  CG1AVAL A 193      18.618   2.821  11.801  0.50 17.69           C  
ANISOU  122  CG1AVAL A 193     2123   2089   2508    -18    -29     -1       C  
ATOM    123  CG1BVAL A 193      16.985   2.118  12.653  0.50 22.57           C  
ANISOU  123  CG1BVAL A 193     2730   2694   3154    -28     -6    -15       C  
ATOM    124  CG2AVAL A 193      16.434   1.624  12.010  0.50 21.49           C  
ANISOU  124  CG2AVAL A 193     2574   2560   3032    -30     -1    -42       C  
ATOM    125  CG2BVAL A 193      17.013   1.600  10.197  0.50 19.03           C  
ANISOU  125  CG2BVAL A 193     2245   2273   2714    -22    -16    -71       C  
ATOM    126  N   SER A 194      15.267   4.614  12.952  1.00 17.93           N  
ANISOU  126  N   SER A 194     2158   2145   2510    -15    -27    -19       N  
ATOM    127  CA  SER A 194      15.116   5.208  14.268  1.00 20.84           C  
ANISOU  127  CA  SER A 194     2547   2505   2866    -18    -23      8       C  
ATOM    128  C   SER A 194      14.158   4.335  15.050  1.00 22.57           C  
ANISOU  128  C   SER A 194     2757   2705   3113    -29     -1      1       C  
ATOM    129  O   SER A 194      12.964   4.355  14.802  1.00 20.57           O  
ANISOU  129  O   SER A 194     2490   2460   2868    -30      4    -26       O  
ATOM    130  CB  SER A 194      14.598   6.649  14.172  1.00 21.25           C  
ANISOU  130  CB  SER A 194     2608   2578   2887     -9    -37      7       C  
ATOM    131  OG  SER A 194      14.697   7.314  15.425  1.00 17.09           O  
ANISOU  131  OG  SER A 194     2103   2045   2347    -12    -35     35       O  
ATOM    132  N   ILE A 195      14.695   3.555  15.983  1.00 23.59           N  
ANISOU  132  N   ILE A 195     2895   2810   3258    -37     13     24       N  
ATOM    133  CA  ILE A 195      13.896   2.591  16.726  1.00 24.69           C  
ANISOU  133  CA  ILE A 195     3027   2927   3427    -48     39     20       C  
ATOM    134  C   ILE A 195      14.111   2.702  18.234  1.00 27.49           C  
ANISOU  134  C   ILE A 195     3405   3267   3773    -51     48     57       C  
ATOM    135  O   ILE A 195      15.145   3.194  18.688  1.00 27.64           O  
ANISOU  135  O   ILE A 195     3443   3289   3770    -47     36     86       O  
ATOM    136  CB  ILE A 195      14.254   1.165  16.284  1.00 32.11           C  
ANISOU  136  CB  ILE A 195     3950   3847   4403    -53     54     10       C  
ATOM    137  CG1 ILE A 195      15.724   0.886  16.610  1.00 23.94           C  
ANISOU  137  CG1 ILE A 195     2930   2801   3365    -50     50     43       C  
ATOM    138  CG2 ILE A 195      13.980   0.997  14.788  1.00 26.24           C  
ANISOU  138  CG2 ILE A 195     3180   3120   3668    -50     46    -30       C  
ATOM    139  CD1 ILE A 195      16.260  -0.404  16.037  1.00 27.17           C  
ANISOU  139  CD1 ILE A 195     3323   3193   3809    -53     62     34       C  
ATOM    140  N   GLN A 196      13.134   2.233  19.006  1.00 25.63           N  
ANISOU  140  N   GLN A 196     3167   3016   3555    -60     70     54       N  
ATOM    141  CA  GLN A 196      13.170   2.332  20.465  1.00 24.36           C  
ANISOU  141  CA  GLN A 196     3029   2843   3385    -63     81     87       C  
ATOM    142  C   GLN A 196      14.191   1.361  21.021  1.00 21.45           C  
ANISOU  142  C   GLN A 196     2668   2452   3029    -63     92    116       C  
ATOM    143  O   GLN A 196      14.824   1.622  22.037  1.00 23.84           O  
ANISOU  143  O   GLN A 196     2993   2754   3313    -59     89    150       O  
ATOM    144  CB  GLN A 196      11.776   2.027  21.036  1.00 24.72           C  
ANISOU  144  CB  GLN A 196     3067   2876   3449    -73    106     72       C  
ATOM    145  CG  GLN A 196      11.666   2.036  22.550  1.00 34.23           C  
ANISOU  145  CG  GLN A 196     4294   4068   4646    -77    121    104       C  
ATOM    146  CD  GLN A 196      10.208   2.028  23.008  1.00 45.56           C  
ANISOU  146  CD  GLN A 196     5722   5496   6094    -87    142     85       C  
ATOM    147  OE1 GLN A 196       9.297   2.111  22.188  1.00 42.23           O  
ANISOU  147  OE1 GLN A 196     5278   5082   5684    -89    142     47       O  
ATOM    148  NE2 GLN A 196       9.987   1.936  24.315  1.00 44.65           N  
ANISOU  148  NE2 GLN A 196     5625   5368   5973    -91    161    110       N  
ATOM    149  N   GLY A 197      14.356   0.236  20.339  1.00 27.22           N  
ANISOU  149  N   GLY A 197     3382   3168   3794    -65    104    102       N  
ATOM    150  CA  GLY A 197      15.280  -0.787  20.788  1.00 30.58           C  
ANISOU  150  CA  GLY A 197     3813   3571   4236    -63    116    129       C  
ATOM    151  C   GLY A 197      14.933  -1.315  22.170  1.00 38.63           C  
ANISOU  151  C   GLY A 197     4847   4568   5263    -66    142    157       C  
ATOM    152  O   GLY A 197      13.758  -1.402  22.547  1.00 38.68           O  
ANISOU  152  O   GLY A 197     4850   4567   5281    -74    161    144       O  
ATOM    153  N   ASN A 198      15.965  -1.646  22.939  1.00 37.57           N  
ANISOU  153  N   ASN A 198     4730   4425   5122    -59    142    196       N  
ATOM    154  CA  ASN A 198      15.775  -2.269  24.246  1.00 48.27           C  
ANISOU  154  CA  ASN A 198     6100   5758   6482    -59    167    227       C  
ATOM    155  C   ASN A 198      15.380  -1.296  25.363  1.00 51.73           C  
ANISOU  155  C   ASN A 198     6559   6211   6885    -59    162    244       C  
ATOM    156  O   ASN A 198      15.438  -1.644  26.542  1.00 56.18           O  
ANISOU  156  O   ASN A 198     7140   6763   7442    -56    178    276       O  
ATOM    157  CB  ASN A 198      17.026  -3.061  24.648  1.00 44.25           C  
ANISOU  157  CB  ASN A 198     5600   5235   5980    -48    170    262       C  
ATOM    158  CG  ASN A 198      17.398  -4.133  23.625  1.00 49.76           C  
ANISOU  158  CG  ASN A 198     6275   5913   6717    -49    179    246       C  
ATOM    159  OD1 ASN A 198      18.566  -4.269  23.254  1.00 53.88           O  
ANISOU  159  OD1 ASN A 198     6796   6438   7236    -40    163    257       O  
ATOM    160  ND2 ASN A 198      16.404  -4.890  23.163  1.00 40.53           N  
ANISOU  160  ND2 ASN A 198     5088   4724   5587    -59    206    217       N  
ATOM    161  N   ARG A 199      14.977  -0.088  24.986  1.00 42.35           N  
ANISOU  161  N   ARG A 199     5370   5048   5672    -61    142    224       N  
ATOM    162  CA  ARG A 199      14.620   0.943  25.954  1.00 43.76           C  
ANISOU  162  CA  ARG A 199     5567   5243   5817    -62    135    236       C  
ATOM    163  C   ARG A 199      13.138   0.916  26.321  1.00 45.38           C  
ANISOU  163  C   ARG A 199     5768   5439   6035    -73    159    219       C  
ATOM    164  O   ARG A 199      12.312   0.400  25.572  1.00 44.98           O  
ANISOU  164  O   ARG A 199     5697   5378   6016    -80    173    187       O  
ATOM    165  CB  ARG A 199      14.992   2.324  25.421  1.00 40.44           C  
ANISOU  165  CB  ARG A 199     5149   4853   5365    -59    103    225       C  
ATOM    166  CG  ARG A 199      16.390   2.772  25.789  1.00 43.68           C  
ANISOU  166  CG  ARG A 199     5573   5276   5746    -49     81    253       C  
ATOM    167  CD  ARG A 199      16.360   4.024  26.645  1.00 51.70           C  
ANISOU  167  CD  ARG A 199     6606   6313   6724    -49     69    264       C  
ATOM    168  NE  ARG A 199      17.122   3.853  27.877  1.00 57.10           N  
ANISOU  168  NE  ARG A 199     7308   6998   7389    -44     69    299       N  
ATOM    169  CZ  ARG A 199      16.784   4.389  29.042  1.00 54.25           C  
ANISOU  169  CZ  ARG A 199     6963   6647   7004    -46     74    313       C  
ATOM    170  NH1 ARG A 199      17.536   4.180  30.112  1.00 56.41           N  
ANISOU  170  NH1 ARG A 199     7252   6924   7258    -38     73    346       N  
ATOM    171  NH2 ARG A 199      15.695   5.138  29.137  1.00 60.85           N  
ANISOU  171  NH2 ARG A 199     7798   7488   7833    -55     79    295       N  
ATOM    172  N   SER A 200      12.815   1.491  27.475  1.00 43.04           N  
ANISOU  172  N   SER A 200     5491   5149   5715    -75    163    237       N  
ATOM    173  CA  SER A 200      11.443   1.530  27.971  1.00 52.09           C  
ANISOU  173  CA  SER A 200     6635   6287   6870    -86    187    222       C  
ATOM    174  C   SER A 200      10.584   2.581  27.267  1.00 53.54           C  
ANISOU  174  C   SER A 200     6807   6490   7048    -90    172    186       C  
ATOM    175  O   SER A 200       9.357   2.516  27.313  1.00 51.78           O  
ANISOU  175  O   SER A 200     6574   6260   6842   -100    190    163       O  
ATOM    176  CB  SER A 200      11.432   1.770  29.482  1.00 53.48           C  
ANISOU  176  CB  SER A 200     6836   6463   7021    -85    197    255       C  
ATOM    177  OG  SER A 200      10.160   2.205  29.924  1.00 61.84           O  
ANISOU  177  OG  SER A 200     7895   7521   8080    -96    213    239       O  
ATOM    178  N   GLU A 201      11.231   3.547  26.622  1.00 43.98           N  
ANISOU  178  N   GLU A 201     5595   5303   5812    -83    140    182       N  
ATOM    179  CA  GLU A 201      10.519   4.579  25.869  1.00 47.26           C  
ANISOU  179  CA  GLU A 201     6000   5738   6220    -84    125    151       C  
ATOM    180  C   GLU A 201      11.410   5.253  24.820  1.00 44.76           C  
ANISOU  180  C   GLU A 201     5679   5442   5887    -75     94    145       C  
ATOM    181  O   GLU A 201      12.631   5.268  24.945  1.00 39.18           O  
ANISOU  181  O   GLU A 201     4982   4738   5165    -68     82    168       O  
ATOM    182  CB  GLU A 201       9.884   5.611  26.807  1.00 44.27           C  
ANISOU  182  CB  GLU A 201     5635   5370   5817    -89    126    155       C  
ATOM    183  CG  GLU A 201      10.859   6.561  27.476  1.00 59.11           C  
ANISOU  183  CG  GLU A 201     7534   7266   7657    -83    107    182       C  
ATOM    184  CD  GLU A 201      10.163   7.770  28.086  1.00 67.05           C  
ANISOU  184  CD  GLU A 201     8549   8286   8642    -88    105    177       C  
ATOM    185  OE1 GLU A 201      10.628   8.907  27.857  1.00 56.36           O  
ANISOU  185  OE1 GLU A 201     7200   6951   7263    -83     83    176       O  
ATOM    186  OE2 GLU A 201       9.149   7.583  28.793  1.00 56.87           O  
ANISOU  186  OE2 GLU A 201     7261   6986   7360    -96    127    172       O  
ATOM    187  N   MET A 202      10.787   5.783  23.774  1.00 30.81           N  
ANISOU  187  N   MET A 202     3896   3688   4123    -73     84    113       N  
ATOM    188  CA  MET A 202      11.516   6.393  22.668  1.00 27.25           C  
ANISOU  188  CA  MET A 202     3440   3256   3658    -63     58    106       C  
ATOM    189  C   MET A 202      11.798   7.868  22.924  1.00 31.72           C  
ANISOU  189  C   MET A 202     4021   3841   4189    -58     39    116       C  
ATOM    190  O   MET A 202      10.880   8.664  23.096  1.00 27.91           O  
ANISOU  190  O   MET A 202     3538   3367   3699    -59     40    104       O  
ATOM    191  CB  MET A 202      10.741   6.222  21.360  1.00 31.02           C  
ANISOU  191  CB  MET A 202     3893   3741   4154    -60     55     68       C  
ATOM    192  CG  MET A 202      11.457   6.750  20.125  1.00 34.97           C  
ANISOU  192  CG  MET A 202     4387   4259   4640    -49     31     60       C  
ATOM    193  SD  MET A 202      13.117   6.086  19.911  1.00 24.02           S  
ANISOU  193  SD  MET A 202     3008   2865   3255    -46     24     83       S  
ATOM    194  CE  MET A 202      13.293   6.171  18.136  1.00 29.69           C  
ANISOU  194  CE  MET A 202     3706   3600   3975    -36      7     54       C  
ATOM    195  N   GLU A 203      13.076   8.225  22.950  1.00 22.90           N  
ANISOU  195  N   GLU A 203     2917   2731   3054    -52     24    136       N  
ATOM    196  CA  GLU A 203      13.481   9.604  23.180  1.00 26.38           C  
ANISOU  196  CA  GLU A 203     3371   3188   3464    -48      9    145       C  
ATOM    197  C   GLU A 203      14.349  10.129  22.035  1.00 22.68           C  
ANISOU  197  C   GLU A 203     2899   2731   2985    -39    -11    140       C  
ATOM    198  O   GLU A 203      14.929  11.203  22.131  1.00 22.21           O  
ANISOU  198  O   GLU A 203     2852   2685   2904    -35    -22    148       O  
ATOM    199  CB  GLU A 203      14.221   9.732  24.513  1.00 21.77           C  
ANISOU  199  CB  GLU A 203     2807   2603   2862    -52     11    175       C  
ATOM    200  CG  GLU A 203      13.313   9.733  25.733  1.00 30.01           C  
ANISOU  200  CG  GLU A 203     3858   3640   3904    -61     28    180       C  
ATOM    201  CD  GLU A 203      14.076   9.579  27.035  1.00 34.22           C  
ANISOU  201  CD  GLU A 203     4409   4172   4420    -63     32    210       C  
ATOM    202  OE1 GLU A 203      14.832  10.499  27.401  1.00 34.92           O  
ANISOU  202  OE1 GLU A 203     4509   4276   4483    -61     18    220       O  
ATOM    203  OE2 GLU A 203      13.922   8.534  27.693  1.00 51.63           O  
ANISOU  203  OE2 GLU A 203     6618   6363   6638    -66     49    224       O  
ATOM    204  N   ASP A 204      14.428   9.360  20.955  1.00 24.22           N  
ANISOU  204  N   ASP A 204     3078   2924   3199    -35    -12    125       N  
ATOM    205  CA  ASP A 204      15.192   9.753  19.777  1.00 20.62           C  
ANISOU  205  CA  ASP A 204     2620   2480   2736    -26    -29    119       C  
ATOM    206  C   ASP A 204      14.267  10.347  18.723  1.00 25.44           C  
ANISOU  206  C   ASP A 204     3218   3105   3344    -18    -35     92       C  
ATOM    207  O   ASP A 204      13.121   9.929  18.595  1.00 20.50           O  
ANISOU  207  O   ASP A 204     2577   2477   2733    -20    -26     73       O  
ATOM    208  CB  ASP A 204      15.901   8.540  19.172  1.00 21.38           C  
ANISOU  208  CB  ASP A 204     2705   2566   2852    -26    -28    117       C  
ATOM    209  CG  ASP A 204      17.324   8.377  19.664  1.00 22.01           C  
ANISOU  209  CG  ASP A 204     2797   2641   2925    -26    -33    143       C  
ATOM    210  OD1 ASP A 204      17.679   8.963  20.703  1.00 22.58           O  
ANISOU  210  OD1 ASP A 204     2886   2715   2980    -28    -35    163       O  
ATOM    211  OD2 ASP A 204      18.087   7.644  19.007  1.00 26.67           O  
ANISOU  211  OD2 ASP A 204     3379   3225   3528    -23    -36    142       O  
ATOM    212  N   ALA A 205      14.778  11.309  17.962  1.00 20.30           N  
ANISOU  212  N   ALA A 205     2571   2468   2674     -8    -49     92       N  
ATOM    213  CA  ALA A 205      14.048  11.886  16.838  1.00 23.47           C  
ANISOU  213  CA  ALA A 205     2962   2886   3070      3    -56     70       C  
ATOM    214  C   ALA A 205      15.026  12.245  15.726  1.00 18.10           C  
ANISOU  214  C   ALA A 205     2283   2215   2378     14    -69     71       C  
ATOM    215  O   ALA A 205      16.227  12.327  15.962  1.00 17.29           O  
ANISOU  215  O   ALA A 205     2193   2108   2270     12    -72     90       O  
ATOM    216  CB  ALA A 205      13.265  13.107  17.276  1.00 19.28           C  
ANISOU  216  CB  ALA A 205     2439   2362   2523      7    -56     71       C  
ATOM    217  N   PHE A 206      14.511  12.433  14.520  1.00 15.87           N  
ANISOU  217  N   PHE A 206     1989   1949   2092     26    -76     51       N  
ATOM    218  CA  PHE A 206      15.353  12.732  13.376  1.00 14.53           C  
ANISOU  218  CA  PHE A 206     1821   1790   1911     38    -86     51       C  
ATOM    219  C   PHE A 206      14.560  13.469  12.316  1.00 16.53           C  
ANISOU  219  C   PHE A 206     2067   2064   2149     55    -93     34       C  
ATOM    220  O   PHE A 206      13.335  13.442  12.316  1.00 21.05           O  
ANISOU  220  O   PHE A 206     2627   2644   2726     58    -92     17       O  
ATOM    221  CB  PHE A 206      15.923  11.446  12.783  1.00 13.44           C  
ANISOU  221  CB  PHE A 206     1669   1646   1790     33    -85     41       C  
ATOM    222  CG  PHE A 206      14.963  10.716  11.890  1.00 18.32           C  
ANISOU  222  CG  PHE A 206     2264   2276   2422     37    -85     10       C  
ATOM    223  CD1 PHE A 206      14.870  11.032  10.547  1.00 24.11           C  
ANISOU  223  CD1 PHE A 206     2988   3030   3142     53    -95     -6       C  
ATOM    224  CD2 PHE A 206      14.150   9.719  12.395  1.00 18.29           C  
ANISOU  224  CD2 PHE A 206     2245   2261   2443     26    -74     -4       C  
ATOM    225  CE1 PHE A 206      13.987  10.362   9.726  1.00 24.11           C  
ANISOU  225  CE1 PHE A 206     2965   3045   3153     57    -96    -38       C  
ATOM    226  CE2 PHE A 206      13.266   9.049  11.578  1.00 21.61           C  
ANISOU  226  CE2 PHE A 206     2641   2692   2877     29    -73    -37       C  
ATOM    227  CZ  PHE A 206      13.185   9.370  10.243  1.00 22.94           C  
ANISOU  227  CZ  PHE A 206     2800   2885   3032     44    -85    -55       C  
ATOM    228  N   ALA A 207      15.273  14.118  11.407  1.00 16.43           N  
ANISOU  228  N   ALA A 207     2061   2062   2119     68   -101     40       N  
ATOM    229  CA  ALA A 207      14.643  14.840  10.318  1.00 17.18           C  
ANISOU  229  CA  ALA A 207     2152   2179   2197     88   -108     28       C  
ATOM    230  C   ALA A 207      15.526  14.862   9.080  1.00 18.21           C  
ANISOU  230  C   ALA A 207     2284   2320   2316     99   -114     28       C  
ATOM    231  O   ALA A 207      16.715  15.158   9.154  1.00 17.16           O  
ANISOU  231  O   ALA A 207     2166   2177   2178     96   -112     46       O  
ATOM    232  CB  ALA A 207      14.304  16.252  10.746  1.00 17.12           C  
ANISOU  232  CB  ALA A 207     2160   2172   2172     96   -107     43       C  
ATOM    233  N   VAL A 208      14.926  14.551   7.942  1.00 16.73           N  
ANISOU  233  N   VAL A 208     2080   2154   2124    113   -121      5       N  
ATOM    234  CA  VAL A 208      15.605  14.651   6.665  1.00 14.20           C  
ANISOU  234  CA  VAL A 208     1760   1847   1787    126   -127      3       C  
ATOM    235  C   VAL A 208      14.772  15.528   5.741  1.00 20.74           C  
ANISOU  235  C   VAL A 208     2586   2702   2591    152   -135     -5       C  
ATOM    236  O   VAL A 208      13.578  15.308   5.572  1.00 16.73           O  
ANISOU  236  O   VAL A 208     2060   2210   2086    159   -140    -26       O  
ATOM    237  CB  VAL A 208      15.822  13.272   6.025  1.00 15.01           C  
ANISOU  237  CB  VAL A 208     1842   1954   1907    119   -129    -20       C  
ATOM    238  CG1 VAL A 208      16.456  13.417   4.657  1.00 21.42           C  
ANISOU  238  CG1 VAL A 208     2655   2784   2701    134   -135    -25       C  
ATOM    239  CG2 VAL A 208      16.684  12.405   6.920  1.00 17.11           C  
ANISOU  239  CG2 VAL A 208     2111   2194   2198     96   -121    -10       C  
ATOM    240  N   SER A 209      15.407  16.534   5.157  1.00 18.14           N  
ANISOU  240  N   SER A 209     2275   2378   2239    167   -134     14       N  
ATOM    241  CA  SER A 209      14.719  17.442   4.255  1.00 23.48           C  
ANISOU  241  CA  SER A 209     2953   3079   2890    195   -140     12       C  
ATOM    242  C   SER A 209      15.542  17.661   2.996  1.00 18.22           C  
ANISOU  242  C   SER A 209     2294   2426   2203    211   -142     17       C  
ATOM    243  O   SER A 209      16.391  18.542   2.947  1.00 21.34           O  
ANISOU  243  O   SER A 209     2712   2811   2587    215   -133     42       O  
ATOM    244  CB  SER A 209      14.435  18.774   4.950  1.00 24.25           C  
ANISOU  244  CB  SER A 209     3069   3167   2979    202   -134     35       C  
ATOM    245  OG  SER A 209      13.371  19.458   4.320  1.00 36.14           O  
ANISOU  245  OG  SER A 209     4570   4696   4466    229   -140     30       O  
ATOM    246  N   PRO A 210      15.289  16.844   1.982  1.00 20.30           N  
ANISOU  246  N   PRO A 210     2538   2713   2462    218   -151     -8       N  
ATOM    247  CA  PRO A 210      16.022  16.939   0.719  1.00 23.58           C  
ANISOU  247  CA  PRO A 210     2958   3144   2856    233   -152     -6       C  
ATOM    248  C   PRO A 210      15.649  18.195  -0.053  1.00 24.10           C  
ANISOU  248  C   PRO A 210     3038   3231   2889    266   -154      8       C  
ATOM    249  O   PRO A 210      14.508  18.642   0.018  1.00 25.39           O  
ANISOU  249  O   PRO A 210     3195   3408   3044    281   -160      3       O  
ATOM    250  CB  PRO A 210      15.556  15.698  -0.042  1.00 24.11           C  
ANISOU  250  CB  PRO A 210     2997   3235   2930    233   -162    -43       C  
ATOM    251  CG  PRO A 210      14.207  15.418   0.494  1.00 28.75           C  
ANISOU  251  CG  PRO A 210     3564   3829   3529    231   -168    -62       C  
ATOM    252  CD  PRO A 210      14.242  15.811   1.938  1.00 20.87           C  
ANISOU  252  CD  PRO A 210     2580   2799   2549    214   -159    -41       C  
ATOM    253  N   HIS A 211      16.599  18.744  -0.802  1.00 21.95           N  
ANISOU  253  N   HIS A 211     2784   2958   2597    276   -147     26       N  
ATOM    254  CA  HIS A 211      16.355  19.935  -1.607  1.00 24.22           C  
ANISOU  254  CA  HIS A 211     3088   3264   2853    309   -145     43       C  
ATOM    255  C   HIS A 211      15.666  21.017  -0.787  1.00 32.10           C  
ANISOU  255  C   HIS A 211     4096   4250   3850    317   -140     62       C  
ATOM    256  O   HIS A 211      14.765  21.692  -1.278  1.00 31.19           O  
ANISOU  256  O   HIS A 211     3980   4156   3714    345   -145     64       O  
ATOM    257  CB  HIS A 211      15.479  19.600  -2.815  1.00 27.35           C  
ANISOU  257  CB  HIS A 211     3464   3703   3225    336   -161     20       C  
ATOM    258  CG  HIS A 211      15.924  18.393  -3.579  1.00 33.35           C  
ANISOU  258  CG  HIS A 211     4206   4478   3987    326   -167     -6       C  
ATOM    259  ND1 HIS A 211      16.963  18.426  -4.483  1.00 34.17           N  
ANISOU  259  ND1 HIS A 211     4323   4586   4076    332   -160      1       N  
ATOM    260  CD2 HIS A 211      15.459  17.122  -3.588  1.00 32.52           C  
ANISOU  260  CD2 HIS A 211     4072   4384   3901    312   -177    -42       C  
ATOM    261  CE1 HIS A 211      17.124  17.225  -5.009  1.00 37.30           C  
ANISOU  261  CE1 HIS A 211     4697   4996   4480    321   -167    -28       C  
ATOM    262  NE2 HIS A 211      16.223  16.416  -4.483  1.00 38.32           N  
ANISOU  262  NE2 HIS A 211     4800   5129   4630    309   -177    -55       N  
ATOM    263  N   PHE A 212      16.082  21.176   0.462  1.00 30.06           N  
ANISOU  263  N   PHE A 212     3848   3959   3616    292   -130     74       N  
ATOM    264  CA  PHE A 212      15.404  22.089   1.369  1.00 30.93           C  
ANISOU  264  CA  PHE A 212     3966   4057   3730    294   -125     87       C  
ATOM    265  C   PHE A 212      15.968  23.506   1.360  1.00 32.89           C  
ANISOU  265  C   PHE A 212     4242   4289   3966    307   -107    119       C  
ATOM    266  O   PHE A 212      15.220  24.476   1.390  1.00 34.30           O  
ANISOU  266  O   PHE A 212     4426   4471   4134    327   -104    130       O  
ATOM    267  CB  PHE A 212      15.423  21.537   2.794  1.00 25.30           C  
ANISOU  267  CB  PHE A 212     3246   3318   3047    262   -123     82       C  
ATOM    268  CG  PHE A 212      14.806  22.457   3.804  1.00 32.01           C  
ANISOU  268  CG  PHE A 212     4105   4155   3903    261   -116     94       C  
ATOM    269  CD1 PHE A 212      13.475  22.814   3.713  1.00 35.44           C  
ANISOU  269  CD1 PHE A 212     4529   4606   4330    279   -123     86       C  
ATOM    270  CD2 PHE A 212      15.560  22.970   4.842  1.00 35.27           C  
ANISOU  270  CD2 PHE A 212     4534   4538   4328    241   -102    112       C  
ATOM    271  CE1 PHE A 212      12.907  23.663   4.639  1.00 41.95           C  
ANISOU  271  CE1 PHE A 212     5361   5417   5161    278   -116     97       C  
ATOM    272  CE2 PHE A 212      14.996  23.816   5.771  1.00 33.69           C  
ANISOU  272  CE2 PHE A 212     4341   4327   4134    239    -95    121       C  
ATOM    273  CZ  PHE A 212      13.669  24.164   5.668  1.00 30.61           C  
ANISOU  273  CZ  PHE A 212     3942   3952   3738    257   -101    114       C  
ATOM    274  N   LEU A 213      17.288  23.620   1.335  1.00 35.85           N  
ANISOU  274  N   LEU A 213     4632   4645   4344    294    -95    132       N  
ATOM    275  CA  LEU A 213      17.931  24.917   1.480  1.00 34.02           C  
ANISOU  275  CA  LEU A 213     4426   4393   4108    300    -74    159       C  
ATOM    276  C   LEU A 213      18.530  25.468   0.193  1.00 36.13           C  
ANISOU  276  C   LEU A 213     4708   4668   4350    324    -64    174       C  
ATOM    277  O   LEU A 213      18.853  24.728  -0.731  1.00 38.06           O  
ANISOU  277  O   LEU A 213     4945   4930   4584    329    -72    163       O  
ATOM    278  CB  LEU A 213      19.006  24.851   2.562  1.00 36.39           C  
ANISOU  278  CB  LEU A 213     4733   4660   4432    268    -63    165       C  
ATOM    279  CG  LEU A 213      18.509  24.504   3.964  1.00 33.02           C  
ANISOU  279  CG  LEU A 213     4297   4222   4027    244    -68    156       C  
ATOM    280  CD1 LEU A 213      19.678  24.262   4.895  1.00 34.77           C  
ANISOU  280  CD1 LEU A 213     4523   4418   4268    215    -61    159       C  
ATOM    281  CD2 LEU A 213      17.620  25.612   4.494  1.00 36.02           C  
ANISOU  281  CD2 LEU A 213     4683   4597   4404    256    -61    167       C  
ATOM    282  N   LYS A 214      18.676  26.786   0.160  1.00 27.06           N  
ANISOU  282  N   LYS A 214     3582   3506   3194    339    -44    199       N  
ATOM    283  CA  LYS A 214      19.332  27.474  -0.935  1.00 39.33           C  
ANISOU  283  CA  LYS A 214     5155   5062   4727    361    -28    218       C  
ATOM    284  C   LYS A 214      20.572  28.165  -0.389  1.00 40.24           C  
ANISOU  284  C   LYS A 214     5289   5141   4859    342     -3    234       C  
ATOM    285  O   LYS A 214      20.493  29.271   0.138  1.00 37.86           O  
ANISOU  285  O   LYS A 214     5001   4819   4564    345     15    250       O  
ATOM    286  CB  LYS A 214      18.393  28.501  -1.559  1.00 48.92           C  
ANISOU  286  CB  LYS A 214     6378   6291   5917    400    -24    235       C  
ATOM    287  CG  LYS A 214      18.506  28.607  -3.062  1.00 59.78           C  
ANISOU  287  CG  LYS A 214     7762   7692   7260    432    -23    243       C  
ATOM    288  CD  LYS A 214      17.224  28.167  -3.741  1.00 77.36           C  
ANISOU  288  CD  LYS A 214     9969   9960   9463    459    -49    229       C  
ATOM    289  CE  LYS A 214      16.150  29.236  -3.645  1.00 89.57           C  
ANISOU  289  CE  LYS A 214    11521  11511  10999    489    -46    246       C  
ATOM    290  NZ  LYS A 214      14.809  28.649  -3.372  1.00 94.30           N  
ANISOU  290  NZ  LYS A 214    12093  12136  11600    493    -72    221       N  
ATOM    291  N   LEU A 215      21.714  27.498  -0.505  1.00 30.33           N  
ANISOU  291  N   LEU A 215     4033   3877   3613    322      0    226       N  
ATOM    292  CA  LEU A 215      22.957  28.003   0.059  1.00 27.95           C  
ANISOU  292  CA  LEU A 215     3746   3543   3330    300     22    235       C  
ATOM    293  C   LEU A 215      23.667  28.970  -0.884  1.00 27.51           C  
ANISOU  293  C   LEU A 215     3713   3478   3260    319     49    256       C  
ATOM    294  O   LEU A 215      23.922  28.650  -2.040  1.00 30.74           O  
ANISOU  294  O   LEU A 215     4124   3904   3650    334     48    256       O  
ATOM    295  CB  LEU A 215      23.875  26.838   0.438  1.00 26.74           C  
ANISOU  295  CB  LEU A 215     3580   3385   3196    270     12    217       C  
ATOM    296  CG  LEU A 215      23.204  25.695   1.204  1.00 30.09           C  
ANISOU  296  CG  LEU A 215     3981   3819   3633    253    -13    196       C  
ATOM    297  CD1 LEU A 215      24.103  24.475   1.303  1.00 19.19           C  
ANISOU  297  CD1 LEU A 215     2588   2436   2268    229    -22    180       C  
ATOM    298  CD2 LEU A 215      22.755  26.153   2.581  1.00 32.07           C  
ANISOU  298  CD2 LEU A 215     4231   4054   3900    239    -12    199       C  
ATOM    299  N   PRO A 216      23.978  30.156  -0.373  1.00 31.76           N  
ANISOU  299  N   PRO A 216     4268   3990   3810    317     74    272       N  
ATOM    300  CA  PRO A 216      24.650  31.200  -1.156  1.00 33.78           C  
ANISOU  300  CA  PRO A 216     4548   4232   4057    334    106    294       C  
ATOM    301  C   PRO A 216      26.076  30.793  -1.471  1.00 30.32           C  
ANISOU  301  C   PRO A 216     4113   3780   3627    315    117    288       C  
ATOM    302  O   PRO A 216      26.823  30.452  -0.558  1.00 25.05           O  
ANISOU  302  O   PRO A 216     3437   3096   2985    284    116    274       O  
ATOM    303  CB  PRO A 216      24.639  32.408  -0.212  1.00 32.35           C  
ANISOU  303  CB  PRO A 216     4377   4020   3894    327    130    306       C  
ATOM    304  CG  PRO A 216      23.474  32.153   0.697  1.00 42.09           C  
ANISOU  304  CG  PRO A 216     5595   5264   5133    323    107    296       C  
ATOM    305  CD  PRO A 216      23.485  30.664   0.918  1.00 36.28           C  
ANISOU  305  CD  PRO A 216     4837   4546   4401    304     76    272       C  
ATOM    306  N   ILE A 217      26.443  30.833  -2.745  1.00 33.31           N  
ANISOU  306  N   ILE A 217     4503   4170   3985    335    127    297       N  
ATOM    307  CA  ILE A 217      27.746  30.344  -3.175  1.00 34.20           C  
ANISOU  307  CA  ILE A 217     4617   4274   4105    319    136    289       C  
ATOM    308  C   ILE A 217      28.877  31.040  -2.438  1.00 34.70           C  
ANISOU  308  C   ILE A 217     4689   4299   4196    295    164    291       C  
ATOM    309  O   ILE A 217      29.926  30.439  -2.184  1.00 30.35           O  
ANISOU  309  O   ILE A 217     4130   3738   3663    269    163    275       O  
ATOM    310  CB  ILE A 217      27.935  30.506  -4.684  1.00 43.96           C  
ANISOU  310  CB  ILE A 217     5868   5524   5310    347    148    302       C  
ATOM    311  CG1 ILE A 217      26.740  29.912  -5.411  1.00 48.92           C  
ANISOU  311  CG1 ILE A 217     6486   6194   5908    374    120    298       C  
ATOM    312  CG2 ILE A 217      29.180  29.783  -5.134  1.00 39.97           C  
ANISOU  312  CG2 ILE A 217     5359   5014   4812    329    153    289       C  
ATOM    313  CD1 ILE A 217      26.472  28.499  -4.998  1.00 49.33           C  
ANISOU  313  CD1 ILE A 217     6510   6264   5970    353     86    269       C  
ATOM    314  N   LYS A 218      28.647  32.300  -2.074  1.00 34.40           N  
ANISOU  314  N   LYS A 218     4666   4241   4164    303    189    308       N  
ATOM    315  CA  LYS A 218      29.650  33.080  -1.362  1.00 34.05           C  
ANISOU  315  CA  LYS A 218     4629   4161   4148    281    218    307       C  
ATOM    316  C   LYS A 218      29.953  32.511   0.022  1.00 32.98           C  
ANISOU  316  C   LYS A 218     4474   4018   4040    245    201    284       C  
ATOM    317  O   LYS A 218      30.968  32.846   0.618  1.00 32.14           O  
ANISOU  317  O   LYS A 218     4367   3888   3957    222    219    276       O  
ATOM    318  CB  LYS A 218      29.214  34.538  -1.233  1.00 42.79           C  
ANISOU  318  CB  LYS A 218     5754   5247   5257    298    249    329       C  
ATOM    319  CG  LYS A 218      29.676  35.438  -2.359  1.00 42.53           C  
ANISOU  319  CG  LYS A 218     5747   5201   5213    321    287    352       C  
ATOM    320  CD  LYS A 218      29.334  36.895  -2.032  1.00 70.90           C  
ANISOU  320  CD  LYS A 218     9356   8768   8816    333    321    372       C  
ATOM    321  CE  LYS A 218      30.421  37.860  -2.496  1.00 77.65           C  
ANISOU  321  CE  LYS A 218    10231   9588   9684    333    370    384       C  
ATOM    322  NZ  LYS A 218      30.490  37.988  -3.979  1.00 79.89           N  
ANISOU  322  NZ  LYS A 218    10536   9882   9938    366    385    408       N  
ATOM    323  N   MET A 219      29.068  31.672   0.547  1.00 31.94           N  
ANISOU  323  N   MET A 219     4325   3908   3904    242    167    274       N  
ATOM    324  CA  MET A 219      29.354  30.998   1.815  1.00 33.86           C  
ANISOU  324  CA  MET A 219     4549   4147   4169    210    148    254       C  
ATOM    325  C   MET A 219      30.010  29.632   1.614  1.00 26.80           C  
ANISOU  325  C   MET A 219     3640   3264   3277    195    127    237       C  
ATOM    326  O   MET A 219      30.245  28.901   2.573  1.00 27.23           O  
ANISOU  326  O   MET A 219     3679   3319   3348    172    109    222       O  
ATOM    327  CB  MET A 219      28.090  30.867   2.666  1.00 28.83           C  
ANISOU  327  CB  MET A 219     3903   3522   3531    211    127    252       C  
ATOM    328  CG  MET A 219      27.916  32.008   3.679  1.00 37.09           C  
ANISOU  328  CG  MET A 219     4955   4547   4592    204    146    256       C  
ATOM    329  SD  MET A 219      26.347  31.861   4.555  1.00 41.94           S  
ANISOU  329  SD  MET A 219     5558   5176   5202    208    123    254       S  
ATOM    330  CE  MET A 219      25.269  32.268   3.213  1.00 33.98           C  
ANISOU  330  CE  MET A 219     4561   4185   4166    250    125    274       C  
ATOM    331  N   LEU A 220      30.304  29.305   0.361  1.00 21.66           N  
ANISOU  331  N   LEU A 220     2995   2624   2612    210    130    240       N  
ATOM    332  CA  LEU A 220      30.857  28.008   0.014  1.00 27.01           C  
ANISOU  332  CA  LEU A 220     3658   3314   3291    198    111    224       C  
ATOM    333  C   LEU A 220      32.220  28.118  -0.671  1.00 27.32           C  
ANISOU  333  C   LEU A 220     3706   3339   3337    192    133    223       C  
ATOM    334  O   LEU A 220      33.170  27.468  -0.256  1.00 20.38           O  
ANISOU  334  O   LEU A 220     2815   2452   2478    169    128    208       O  
ATOM    335  CB  LEU A 220      29.882  27.237  -0.872  1.00 21.71           C  
ANISOU  335  CB  LEU A 220     2980   2674   2596    219     89    223       C  
ATOM    336  CG  LEU A 220      28.530  26.900  -0.252  1.00 25.44           C  
ANISOU  336  CG  LEU A 220     3439   3162   3063    224     65    219       C  
ATOM    337  CD1 LEU A 220      27.636  26.296  -1.314  1.00 20.70           C  
ANISOU  337  CD1 LEU A 220     2834   2594   2439    247     48    215       C  
ATOM    338  CD2 LEU A 220      28.696  25.937   0.934  1.00 19.09           C  
ANISOU  338  CD2 LEU A 220     2617   2354   2284    195     45    202       C  
ATOM    339  N   MET A 221      32.308  28.940  -1.712  1.00 27.62           N  
ANISOU  339  N   MET A 221     3763   3373   3358    214    158    239       N  
ATOM    340  CA  MET A 221      33.553  29.090  -2.473  1.00 39.82           C  
ANISOU  340  CA  MET A 221     5318   4905   4907    209    183    239       C  
ATOM    341  C   MET A 221      34.744  29.511  -1.625  1.00 31.51           C  
ANISOU  341  C   MET A 221     4263   3822   3886    182    201    229       C  
ATOM    342  O   MET A 221      34.656  30.444  -0.836  1.00 27.38           O  
ANISOU  342  O   MET A 221     3746   3282   3376    177    216    234       O  
ATOM    343  CB  MET A 221      33.383  30.089  -3.614  1.00 35.97           C  
ANISOU  343  CB  MET A 221     4855   4416   4397    239    212    262       C  
ATOM    344  CG  MET A 221      32.378  29.650  -4.648  1.00 51.46           C  
ANISOU  344  CG  MET A 221     6818   6412   6323    269    194    269       C  
ATOM    345  SD  MET A 221      32.696  30.396  -6.257  1.00 63.25           S  
ANISOU  345  SD  MET A 221     8339   7906   7787    300    227    292       S  
ATOM    346  CE  MET A 221      34.320  29.714  -6.610  1.00 57.14           C  
ANISOU  346  CE  MET A 221     7559   7119   7031    273    238    273       C  
ATOM    347  N   GLY A 222      35.866  28.822  -1.805  1.00 31.94           N  
ANISOU  347  N   GLY A 222     4309   3872   3955    164    201    213       N  
ATOM    348  CA  GLY A 222      37.073  29.168  -1.075  1.00 31.62           C  
ANISOU  348  CA  GLY A 222     4265   3806   3945    139    218    201       C  
ATOM    349  C   GLY A 222      37.819  30.318  -1.731  1.00 37.98           C  
ANISOU  349  C   GLY A 222     5090   4587   4754    144    262    210       C  
ATOM    350  O   GLY A 222      37.567  30.645  -2.892  1.00 29.06           O  
ANISOU  350  O   GLY A 222     3978   3462   3602    168    278    227       O  
ATOM    351  N   ASP A 223      38.742  30.923  -0.992  1.00 36.43           N  
ANISOU  351  N   ASP A 223     4891   4365   4585    123    282    199       N  
ATOM    352  CA  ASP A 223      39.512  32.059  -1.489  1.00 48.86           C  
ANISOU  352  CA  ASP A 223     6483   5913   6170    125    329    205       C  
ATOM    353  C   ASP A 223      40.373  31.707  -2.701  1.00 45.10           C  
ANISOU  353  C   ASP A 223     6013   5434   5689    128    344    204       C  
ATOM    354  O   ASP A 223      40.508  32.502  -3.625  1.00 43.22           O  
ANISOU  354  O   ASP A 223     5798   5184   5441    144    379    220       O  
ATOM    355  CB  ASP A 223      40.390  32.636  -0.377  1.00 45.58           C  
ANISOU  355  CB  ASP A 223     6057   5473   5788     97    344    186       C  
ATOM    356  CG  ASP A 223      39.596  33.009   0.861  1.00 60.04           C  
ANISOU  356  CG  ASP A 223     7882   7307   7625     92    331    185       C  
ATOM    357  OD1 ASP A 223      38.365  32.811   0.862  1.00 68.53           O  
ANISOU  357  OD1 ASP A 223     8960   8400   8678    109    310    200       O  
ATOM    358  OD2 ASP A 223      40.202  33.500   1.836  1.00 60.32           O  
ANISOU  358  OD2 ASP A 223     7907   7325   7686     71    342    168       O  
ATOM    359  N   HIS A 224      40.957  30.514  -2.686  1.00 48.21           N  
ANISOU  359  N   HIS A 224     6389   5840   6090    113    319    184       N  
ATOM    360  CA  HIS A 224      41.855  30.080  -3.752  1.00 51.53           C  
ANISOU  360  CA  HIS A 224     6811   6258   6508    112    332    179       C  
ATOM    361  C   HIS A 224      41.149  29.846  -5.083  1.00 57.79           C  
ANISOU  361  C   HIS A 224     7621   7073   7266    141    331    197       C  
ATOM    362  O   HIS A 224      41.798  29.706  -6.116  1.00 53.31           O  
ANISOU  362  O   HIS A 224     7060   6503   6691    145    349    197       O  
ATOM    363  CB  HIS A 224      42.595  28.810  -3.340  1.00 47.03           C  
ANISOU  363  CB  HIS A 224     6216   5697   5958     89    304    153       C  
ATOM    364  CG  HIS A 224      43.552  29.004  -2.209  1.00 43.79           C  
ANISOU  364  CG  HIS A 224     5790   5268   5582     62    308    132       C  
ATOM    365  ND1 HIS A 224      44.709  29.741  -2.332  1.00 48.73           N  
ANISOU  365  ND1 HIS A 224     6418   5866   6229     50    344    122       N  
ATOM    366  CD2 HIS A 224      43.528  28.554  -0.932  1.00 37.96           C  
ANISOU  366  CD2 HIS A 224     5030   4535   4859     46    280    118       C  
ATOM    367  CE1 HIS A 224      45.355  29.738  -1.180  1.00 44.63           C  
ANISOU  367  CE1 HIS A 224     5880   5339   5739     27    337    100       C  
ATOM    368  NE2 HIS A 224      44.659  29.026  -0.315  1.00 45.47           N  
ANISOU  368  NE2 HIS A 224     5972   5464   5839     25    298     99       N  
ATOM    369  N   GLU A 225      39.823  29.799  -5.055  1.00 63.02           N  
ANISOU  369  N   GLU A 225     8286   7756   7903    161    310    212       N  
ATOM    370  CA  GLU A 225      39.049  29.589  -6.277  1.00 73.57           C  
ANISOU  370  CA  GLU A 225     9634   9117   9202    190    305    228       C  
ATOM    371  C   GLU A 225      38.757  30.907  -6.999  1.00 77.03           C  
ANISOU  371  C   GLU A 225    10102   9544   9621    217    343    256       C  
ATOM    372  O   GLU A 225      38.998  31.990  -6.458  1.00 78.57           O  
ANISOU  372  O   GLU A 225    10307   9711   9834    212    372    264       O  
ATOM    373  CB  GLU A 225      37.749  28.844  -5.964  1.00 71.77           C  
ANISOU  373  CB  GLU A 225     9393   8920   8957    200    264    228       C  
ATOM    374  CG  GLU A 225      37.968  27.486  -5.338  1.00 68.03           C  
ANISOU  374  CG  GLU A 225     8891   8457   8500    177    229    202       C  
ATOM    375  CD  GLU A 225      36.716  26.937  -4.691  1.00 69.36           C  
ANISOU  375  CD  GLU A 225     9045   8647   8660    182    193    201       C  
ATOM    376  OE1 GLU A 225      36.770  26.631  -3.478  1.00 68.71           O  
ANISOU  376  OE1 GLU A 225     8948   8557   8601    161    177    191       O  
ATOM    377  OE2 GLU A 225      35.688  26.818  -5.394  1.00 69.44           O  
ANISOU  377  OE2 GLU A 225     9060   8682   8641    206    182    211       O  
ATOM    378  N   GLY A 226      38.240  30.811  -8.218  1.00 72.80           N  
ANISOU  378  N   GLY A 226     9580   9031   9050    246    344    272       N  
ATOM    379  CA  GLY A 226      37.873  31.994  -8.972  1.00 78.13           C  
ANISOU  379  CA  GLY A 226    10285   9700   9703    276    378    302       C  
ATOM    380  C   GLY A 226      36.656  32.658  -8.361  1.00 78.92           C  
ANISOU  380  C   GLY A 226    10388   9803   9795    293    370    319       C  
ATOM    381  O   GLY A 226      35.962  32.057  -7.546  1.00 75.93           O  
ANISOU  381  O   GLY A 226     9990   9440   9421    284    334    307       O  
ATOM    382  N   MET A 227      36.397  33.899  -8.752  1.00 97.61           N  
ANISOU  382  N   MET A 227    12781  12155  12152    317    405    348       N  
ATOM    383  CA  MET A 227      35.224  34.607  -8.267  1.00 97.80           C  
ANISOU  383  CA  MET A 227    12811  12182  12168    336    400    366       C  
ATOM    384  C   MET A 227      34.037  34.272  -9.164  1.00103.57           C  
ANISOU  384  C   MET A 227    13545  12953  12854    374    376    381       C  
ATOM    385  O   MET A 227      34.170  33.496 -10.108  1.00104.65           O  
ANISOU  385  O   MET A 227    13679  13115  12966    382    364    376       O  
ATOM    386  CB  MET A 227      35.483  36.113  -8.226  1.00101.01           C  
ANISOU  386  CB  MET A 227    13241  12550  12588    346    451    389       C  
ATOM    387  CG  MET A 227      36.955  36.486  -8.043  1.00101.60           C  
ANISOU  387  CG  MET A 227    13320  12587  12698    317    489    376       C  
ATOM    388  SD  MET A 227      37.530  36.443  -6.327  1.00 97.64           S  
ANISOU  388  SD  MET A 227    12793  12061  12246    271    481    344       S  
ATOM    389  CE  MET A 227      36.110  37.113  -5.469  1.00 71.15           C  
ANISOU  389  CE  MET A 227     9437   8709   8887    286    468    359       C  
ATOM    390  N   SER A 228      32.876  34.847  -8.868  1.00161.16           N  
ANISOU  390  N   SER A 228    20842  20254  20136    396    369    398       N  
ATOM    391  CA  SER A 228      31.671  34.560  -9.637  1.00167.87           C  
ANISOU  391  CA  SER A 228    21693  21146  20944    432    343    410       C  
ATOM    392  C   SER A 228      31.288  33.089  -9.514  1.00160.51           C  
ANISOU  392  C   SER A 228    20732  20249  20006    419    294    381       C  
ATOM    393  O   SER A 228      31.708  32.409  -8.579  1.00158.31           O  
ANISOU  393  O   SER A 228    20433  19961  19758    384    277    355       O  
ATOM    394  CB  SER A 228      31.872  34.941 -11.108  1.00 81.59           C  
ANISOU  394  CB  SER A 228    10791  10229   9981    466    369    435       C  
ATOM    395  OG  SER A 228      32.131  33.801 -11.907  1.00 80.85           O  
ANISOU  395  OG  SER A 228    10686  10166   9866    465    346    417       O  
ATOM    396  N   THR A 232      24.527  31.458  -8.424  1.00 53.76           N  
ANISOU  396  N   THR A 232     7133   6878   6415    496    128    354       N  
ATOM    397  CA  THR A 232      23.971  32.231  -7.307  1.00 65.74           C  
ANISOU  397  CA  THR A 232     8651   8372   7955    491    133    363       C  
ATOM    398  C   THR A 232      23.850  31.417  -6.014  1.00 55.14           C  
ANISOU  398  C   THR A 232     7284   7022   6645    452    110    335       C  
ATOM    399  O   THR A 232      24.214  31.890  -4.935  1.00 50.53           O  
ANISOU  399  O   THR A 232     6703   6405   6090    429    124    336       O  
ATOM    400  CB  THR A 232      22.582  32.850  -7.639  1.00 67.20           C  
ANISOU  400  CB  THR A 232     8839   8581   8114    532    124    379       C  
ATOM    401  OG1 THR A 232      21.597  31.812  -7.755  1.00 68.75           O  
ANISOU  401  OG1 THR A 232     9008   8818   8297    537     84    354       O  
ATOM    402  CG2 THR A 232      22.639  33.657  -8.931  1.00 64.56           C  
ANISOU  402  CG2 THR A 232     8529   8257   7744    575    147    410       C  
ATOM    403  N   HIS A 233      23.325  30.203  -6.118  1.00 73.98           N  
ANISOU  403  N   HIS A 233     9646   9439   9025    447     76    309       N  
ATOM    404  CA  HIS A 233      23.191  29.347  -4.941  1.00 63.25           C  
ANISOU  404  CA  HIS A 233     8264   8073   7695    412     55    284       C  
ATOM    405  C   HIS A 233      23.114  27.865  -5.292  1.00 59.07           C  
ANISOU  405  C   HIS A 233     7710   7570   7162    402     27    254       C  
ATOM    406  O   HIS A 233      22.694  27.492  -6.386  1.00 66.84           O  
ANISOU  406  O   HIS A 233     8689   8588   8117    426     15    249       O  
ATOM    407  CB  HIS A 233      21.993  29.777  -4.084  1.00 63.36           C  
ANISOU  407  CB  HIS A 233     8272   8088   7716    418     45    286       C  
ATOM    408  CG  HIS A 233      20.686  29.745  -4.813  1.00 75.55           C  
ANISOU  408  CG  HIS A 233     9807   9669   9230    454     26    285       C  
ATOM    409  ND1 HIS A 233      20.196  28.602  -5.410  1.00 77.20           N  
ANISOU  409  ND1 HIS A 233     9994   9914   9424    458     -2    261       N  
ATOM    410  CD2 HIS A 233      19.768  30.714  -5.041  1.00 82.72           C  
ANISOU  410  CD2 HIS A 233    10724  10585  10121    487     31    305       C  
ATOM    411  CE1 HIS A 233      19.032  28.869  -5.975  1.00 85.92           C  
ANISOU  411  CE1 HIS A 233    11094  11050  10503    493    -15    264       C  
ATOM    412  NE2 HIS A 233      18.750  30.143  -5.766  1.00 91.54           N  
ANISOU  412  NE2 HIS A 233    11825  11745  11213    512      4    292       N  
ATOM    413  N   LEU A 234      23.539  27.026  -4.353  1.00 41.72           N  
ANISOU  413  N   LEU A 234     5498   5359   4995    366     17    235       N  
ATOM    414  CA  LEU A 234      23.505  25.583  -4.523  1.00 30.98           C  
ANISOU  414  CA  LEU A 234     4114   4019   3639    351     -7    206       C  
ATOM    415  C   LEU A 234      22.377  25.024  -3.676  1.00 37.60           C  
ANISOU  415  C   LEU A 234     4931   4867   4489    343    -30    190       C  
ATOM    416  O   LEU A 234      22.082  25.540  -2.595  1.00 33.06           O  
ANISOU  416  O   LEU A 234     4358   4272   3931    333    -26    197       O  
ATOM    417  CB  LEU A 234      24.822  24.971  -4.056  1.00 29.16           C  
ANISOU  417  CB  LEU A 234     3880   3763   3435    317     -1    197       C  
ATOM    418  CG  LEU A 234      25.838  24.513  -5.100  1.00 38.92           C  
ANISOU  418  CG  LEU A 234     5119   5004   4662    317      7    192       C  
ATOM    419  CD1 LEU A 234      25.966  25.548  -6.194  1.00 55.19           C  
ANISOU  419  CD1 LEU A 234     7204   7072   6694    348     27    215       C  
ATOM    420  CD2 LEU A 234      27.186  24.235  -4.457  1.00 34.59           C  
ANISOU  420  CD2 LEU A 234     4573   4426   4145    284     18    188       C  
ATOM    421  N   THR A 235      21.741  23.967  -4.159  1.00 31.84           N  
ANISOU  421  N   THR A 235     4179   4167   3753    347    -53    165       N  
ATOM    422  CA  THR A 235      20.742  23.290  -3.357  1.00 30.49           C  
ANISOU  422  CA  THR A 235     3985   4003   3597    336    -73    146       C  
ATOM    423  C   THR A 235      21.429  22.593  -2.191  1.00 27.51           C  
ANISOU  423  C   THR A 235     3601   3597   3255    298    -72    138       C  
ATOM    424  O   THR A 235      22.480  21.967  -2.361  1.00 29.11           O  
ANISOU  424  O   THR A 235     3802   3790   3468    281    -69    132       O  
ATOM    425  CB  THR A 235      19.960  22.281  -4.187  1.00 38.22           C  
ANISOU  425  CB  THR A 235     4940   5020   4563    348    -94    118       C  
ATOM    426  OG1 THR A 235      19.259  22.983  -5.219  1.00 39.42           O  
ANISOU  426  OG1 THR A 235     5097   5201   4678    386    -97    127       O  
ATOM    427  CG2 THR A 235      18.964  21.520  -3.314  1.00 32.12           C  
ANISOU  427  CG2 THR A 235     4143   4251   3811    333   -111     96       C  
ATOM    428  N   GLY A 236      20.846  22.726  -1.007  1.00 26.28           N  
ANISOU  428  N   GLY A 236     3441   3428   3117    286    -76    138       N  
ATOM    429  CA  GLY A 236      21.369  22.071   0.175  1.00 26.14           C  
ANISOU  429  CA  GLY A 236     3416   3387   3130    253    -77    132       C  
ATOM    430  C   GLY A 236      20.375  21.078   0.746  1.00 23.20           C  
ANISOU  430  C   GLY A 236     3020   3024   2771    243    -94    110       C  
ATOM    431  O   GLY A 236      19.179  21.356   0.808  1.00 23.59           O  
ANISOU  431  O   GLY A 236     3064   3088   2813    257   -101    106       O  
ATOM    432  N   HIS A 237      20.867  19.915   1.160  1.00 14.84           N  
ANISOU  432  N   HIS A 237     1948   1956   1734    219    -99     96       N  
ATOM    433  CA  HIS A 237      20.018  18.912   1.801  1.00 14.37           C  
ANISOU  433  CA  HIS A 237     1867   1901   1693    206   -112     76       C  
ATOM    434  C   HIS A 237      20.278  18.899   3.300  1.00 12.60           C  
ANISOU  434  C   HIS A 237     1647   1649   1491    182   -107     85       C  
ATOM    435  O   HIS A 237      21.416  19.047   3.754  1.00 15.11           O  
ANISOU  435  O   HIS A 237     1976   1947   1818    168    -98     98       O  
ATOM    436  CB  HIS A 237      20.279  17.534   1.196  1.00 17.36           C  
ANISOU  436  CB  HIS A 237     2226   2289   2082    197   -119     52       C  
ATOM    437  CG  HIS A 237      20.317  17.538  -0.301  1.00 18.95           C  
ANISOU  437  CG  HIS A 237     2424   2516   2258    219   -123     44       C  
ATOM    438  ND1 HIS A 237      19.190  17.705  -1.078  1.00 24.24           N  
ANISOU  438  ND1 HIS A 237     3084   3217   2907    243   -132     31       N  
ATOM    439  CD2 HIS A 237      21.352  17.405  -1.164  1.00 23.45           C  
ANISOU  439  CD2 HIS A 237     3000   3088   2821    220   -117     45       C  
ATOM    440  CE1 HIS A 237      19.531  17.671  -2.354  1.00 28.26           C  
ANISOU  440  CE1 HIS A 237     3594   3748   3395    259   -133     26       C  
ATOM    441  NE2 HIS A 237      20.836  17.487  -2.435  1.00 24.97           N  
ANISOU  441  NE2 HIS A 237     3187   3313   2987    245   -123     34       N  
ATOM    442  N   PHE A 238      19.223  18.731   4.077  1.00 15.40           N  
ANISOU  442  N   PHE A 238     1992   2005   1855    178   -112     78       N  
ATOM    443  CA  PHE A 238      19.341  18.809   5.525  1.00 15.58           C  
ANISOU  443  CA  PHE A 238     2020   2005   1895    158   -107     88       C  
ATOM    444  C   PHE A 238      19.155  17.442   6.154  1.00 14.57           C  
ANISOU  444  C   PHE A 238     1874   1871   1790    138   -113     73       C  
ATOM    445  O   PHE A 238      18.233  16.707   5.813  1.00 16.98           O  
ANISOU  445  O   PHE A 238     2161   2191   2100    142   -120     53       O  
ATOM    446  CB  PHE A 238      18.305  19.769   6.084  1.00 15.55           C  
ANISOU  446  CB  PHE A 238     2021   2002   1884    166   -105     94       C  
ATOM    447  CG  PHE A 238      18.282  19.830   7.582  1.00 16.41           C  
ANISOU  447  CG  PHE A 238     2134   2091   2008    146   -100    102       C  
ATOM    448  CD1 PHE A 238      18.979  20.822   8.255  1.00 11.91           C  
ANISOU  448  CD1 PHE A 238     1583   1506   1438    140    -89    120       C  
ATOM    449  CD2 PHE A 238      17.551  18.903   8.318  1.00 13.07           C  
ANISOU  449  CD2 PHE A 238     1696   1667   1602    133   -105     89       C  
ATOM    450  CE1 PHE A 238      18.945  20.900   9.639  1.00 19.23           C  
ANISOU  450  CE1 PHE A 238     2512   2418   2375    122    -85    125       C  
ATOM    451  CE2 PHE A 238      17.522  18.959   9.693  1.00 15.81           C  
ANISOU  451  CE2 PHE A 238     2048   1998   1961    115   -100     96       C  
ATOM    452  CZ  PHE A 238      18.223  19.965  10.365  1.00 18.54           C  
ANISOU  452  CZ  PHE A 238     2412   2331   2302    110    -91    115       C  
ATOM    453  N   PHE A 239      20.044  17.113   7.077  1.00 14.13           N  
ANISOU  453  N   PHE A 239     1824   1795   1751    118   -108     83       N  
ATOM    454  CA  PHE A 239      19.960  15.867   7.825  1.00 14.02           C  
ANISOU  454  CA  PHE A 239     1796   1772   1760    100   -110     74       C  
ATOM    455  C   PHE A 239      20.220  16.151   9.290  1.00 11.20           C  
ANISOU  455  C   PHE A 239     1449   1396   1410     85   -105     90       C  
ATOM    456  O   PHE A 239      21.221  16.786   9.620  1.00 15.22           O  
ANISOU  456  O   PHE A 239     1972   1895   1915     81   -101    106       O  
ATOM    457  CB  PHE A 239      21.029  14.915   7.328  1.00 14.87           C  
ANISOU  457  CB  PHE A 239     1897   1874   1878     93   -111     70       C  
ATOM    458  CG  PHE A 239      20.929  14.606   5.876  1.00 14.31           C  
ANISOU  458  CG  PHE A 239     1816   1822   1799    106   -116     53       C  
ATOM    459  CD1 PHE A 239      21.669  15.324   4.952  1.00 10.15           C  
ANISOU  459  CD1 PHE A 239     1301   1301   1254    118   -113     60       C  
ATOM    460  CD2 PHE A 239      20.098  13.572   5.427  1.00 13.86           C  
ANISOU  460  CD2 PHE A 239     1737   1776   1752    107   -120     28       C  
ATOM    461  CE1 PHE A 239      21.598  15.024   3.596  1.00 12.58           C  
ANISOU  461  CE1 PHE A 239     1600   1629   1551    131   -117     44       C  
ATOM    462  CE2 PHE A 239      20.009  13.266   4.062  1.00 15.87           C  
ANISOU  462  CE2 PHE A 239     1980   2052   1997    119   -125      9       C  
ATOM    463  CZ  PHE A 239      20.773  14.000   3.145  1.00 16.94           C  
ANISOU  463  CZ  PHE A 239     2130   2197   2112    132   -124     18       C  
ATOM    464  N   GLY A 240      19.362  15.659  10.177  1.00 17.22           N  
ANISOU  464  N   GLY A 240     2204   2154   2185     76   -105     86       N  
ATOM    465  CA  GLY A 240      19.527  15.955  11.589  1.00 16.29           C  
ANISOU  465  CA  GLY A 240     2097   2022   2071     63   -100    101       C  
ATOM    466  C   GLY A 240      19.135  14.785  12.458  1.00 17.17           C  
ANISOU  466  C   GLY A 240     2198   2124   2202     49    -98     97       C  
ATOM    467  O   GLY A 240      18.140  14.119  12.193  1.00 19.77           O  
ANISOU  467  O   GLY A 240     2512   2459   2541     51    -98     80       O  
ATOM    468  N   VAL A 241      19.915  14.544  13.506  1.00 13.28           N  
ANISOU  468  N   VAL A 241     1712   1618   1715     37    -95    112       N  
ATOM    469  CA  VAL A 241      19.598  13.492  14.470  1.00 15.07           C  
ANISOU  469  CA  VAL A 241     1933   1834   1960     25    -91    114       C  
ATOM    470  C   VAL A 241      19.570  14.095  15.876  1.00 12.28           C  
ANISOU  470  C   VAL A 241     1593   1475   1599     16    -87    129       C  
ATOM    471  O   VAL A 241      20.486  14.831  16.248  1.00 13.70           O  
ANISOU  471  O   VAL A 241     1784   1654   1767     15    -89    142       O  
ATOM    472  CB  VAL A 241      20.612  12.327  14.385  1.00 17.81           C  
ANISOU  472  CB  VAL A 241     2274   2171   2323     18    -92    117       C  
ATOM    473  CG1 VAL A 241      20.391  11.332  15.535  1.00 16.82           C  
ANISOU  473  CG1 VAL A 241     2145   2031   2213      7    -85    125       C  
ATOM    474  CG2 VAL A 241      20.499  11.619  13.033  1.00 17.30           C  
ANISOU  474  CG2 VAL A 241     2193   2112   2268     25    -94     97       C  
ATOM    475  N   TYR A 242      18.521  13.799  16.643  1.00 10.60           N  
ANISOU  475  N   TYR A 242     1377   1259   1393     11    -81    127       N  
ATOM    476  CA  TYR A 242      18.329  14.410  17.960  1.00 14.27           C  
ANISOU  476  CA  TYR A 242     1854   1721   1848      3    -76    139       C  
ATOM    477  C   TYR A 242      18.187  13.367  19.056  1.00 12.91           C  
ANISOU  477  C   TYR A 242     1680   1537   1688     -8    -69    148       C  
ATOM    478  O   TYR A 242      17.188  12.672  19.144  1.00 13.76           O  
ANISOU  478  O   TYR A 242     1778   1640   1810    -10    -61    138       O  
ATOM    479  CB  TYR A 242      17.112  15.359  17.931  1.00 14.80           C  
ANISOU  479  CB  TYR A 242     1921   1796   1907      8    -73    130       C  
ATOM    480  CG  TYR A 242      17.169  16.254  16.718  1.00 15.46           C  
ANISOU  480  CG  TYR A 242     2005   1890   1980     22    -79    122       C  
ATOM    481  CD1 TYR A 242      18.102  17.268  16.649  1.00  9.91           C  
ANISOU  481  CD1 TYR A 242     1315   1188   1262     25    -80    133       C  
ATOM    482  CD2 TYR A 242      16.324  16.050  15.622  1.00 14.53           C  
ANISOU  482  CD2 TYR A 242     1874   1781   1865     34    -82    105       C  
ATOM    483  CE1 TYR A 242      18.191  18.095  15.510  1.00 20.09           C  
ANISOU  483  CE1 TYR A 242     2607   2486   2542     40    -82    129       C  
ATOM    484  CE2 TYR A 242      16.399  16.858  14.482  1.00 13.13           C  
ANISOU  484  CE2 TYR A 242     1698   1615   1674     50    -87    101       C  
ATOM    485  CZ  TYR A 242      17.344  17.871  14.431  1.00 17.66           C  
ANISOU  485  CZ  TYR A 242     2288   2188   2235     53    -86    115       C  
ATOM    486  OH  TYR A 242      17.446  18.677  13.317  1.00 17.32           O  
ANISOU  486  OH  TYR A 242     2248   2154   2178     69    -88    113       O  
ATOM    487  N   ASP A 243      19.190  13.267  19.905  1.00 14.14           N  
ANISOU  487  N   ASP A 243     1845   1689   1839    -13    -70    166       N  
ATOM    488  CA  ASP A 243      19.184  12.198  20.894  1.00 15.43           C  
ANISOU  488  CA  ASP A 243     2008   1842   2013    -20    -63    178       C  
ATOM    489  C   ASP A 243      18.673  12.765  22.207  1.00 16.06           C  
ANISOU  489  C   ASP A 243     2099   1923   2079    -27    -56    187       C  
ATOM    490  O   ASP A 243      19.437  13.326  22.977  1.00 17.82           O  
ANISOU  490  O   ASP A 243     2333   2152   2286    -29    -61    199       O  
ATOM    491  CB  ASP A 243      20.602  11.611  21.015  1.00 11.44           C  
ANISOU  491  CB  ASP A 243     1504   1332   1509    -20    -69    192       C  
ATOM    492  CG  ASP A 243      20.713  10.491  22.038  1.00 20.11           C  
ANISOU  492  CG  ASP A 243     2604   2419   2617    -24    -61    209       C  
ATOM    493  OD1 ASP A 243      19.746  10.222  22.792  1.00 20.60           O  
ANISOU  493  OD1 ASP A 243     2669   2477   2683    -28    -50    211       O  
ATOM    494  OD2 ASP A 243      21.811   9.900  22.103  1.00 19.90           O  
ANISOU  494  OD2 ASP A 243     2577   2389   2596    -21    -66    221       O  
ATOM    495  N   GLY A 244      17.375  12.611  22.455  1.00 15.09           N  
ANISOU  495  N   GLY A 244     1972   1797   1963    -30    -46    178       N  
ATOM    496  CA  GLY A 244      16.745  13.213  23.615  1.00 15.54           C  
ANISOU  496  CA  GLY A 244     2039   1856   2008    -37    -38    183       C  
ATOM    497  C   GLY A 244      17.142  12.583  24.941  1.00 19.84           C  
ANISOU  497  C   GLY A 244     2593   2396   2549    -43    -32    204       C  
ATOM    498  O   GLY A 244      17.504  11.410  24.988  1.00 16.80           O  
ANISOU  498  O   GLY A 244     2204   2001   2178    -42    -28    213       O  
ATOM    499  N   HIS A 245      17.120  13.385  26.007  1.00 16.11           N  
ANISOU  499  N   HIS A 245     2132   1932   2057    -48    -30    212       N  
ATOM    500  CA  HIS A 245      17.335  12.876  27.356  1.00 21.60           C  
ANISOU  500  CA  HIS A 245     2837   2626   2743    -53    -23    231       C  
ATOM    501  C   HIS A 245      16.389  13.552  28.310  1.00 21.55           C  
ANISOU  501  C   HIS A 245     2838   2624   2725    -60    -13    228       C  
ATOM    502  O   HIS A 245      16.059  14.712  28.137  1.00 20.73           O  
ANISOU  502  O   HIS A 245     2735   2529   2612    -62    -16    216       O  
ATOM    503  CB  HIS A 245      18.782  13.046  27.831  1.00 22.63           C  
ANISOU  503  CB  HIS A 245     2975   2767   2857    -50    -36    247       C  
ATOM    504  CG  HIS A 245      19.353  14.400  27.556  1.00 20.16           C  
ANISOU  504  CG  HIS A 245     2664   2468   2528    -50    -47    238       C  
ATOM    505  ND1 HIS A 245      20.179  14.651  26.479  1.00 23.56           N  
ANISOU  505  ND1 HIS A 245     3089   2900   2964    -44    -58    231       N  
ATOM    506  CD2 HIS A 245      19.205  15.576  28.201  1.00 21.78           C  
ANISOU  506  CD2 HIS A 245     2877   2685   2716    -55    -46    233       C  
ATOM    507  CE1 HIS A 245      20.527  15.923  26.484  1.00 19.97           C  
ANISOU  507  CE1 HIS A 245     2638   2455   2494    -46    -63    223       C  
ATOM    508  NE2 HIS A 245      19.942  16.514  27.512  1.00 21.06           N  
ANISOU  508  NE2 HIS A 245     2783   2599   2619    -53    -56    224       N  
ATOM    509  N   GLY A 246      15.949  12.814  29.323  1.00 23.14           N  
ANISOU  509  N   GLY A 246     3045   2819   2927    -65      1    241       N  
ATOM    510  CA  GLY A 246      15.013  13.355  30.287  1.00 18.95           C  
ANISOU  510  CA  GLY A 246     2522   2292   2385    -73     14    238       C  
ATOM    511  C   GLY A 246      13.603  13.417  29.728  1.00 18.54           C  
ANISOU  511  C   GLY A 246     2460   2230   2353    -77     25    217       C  
ATOM    512  O   GLY A 246      12.722  14.001  30.330  1.00 19.83           O  
ANISOU  512  O   GLY A 246     2627   2396   2511    -84     35    210       O  
ATOM    513  N   GLY A 247      13.389  12.779  28.585  1.00 17.61           N  
ANISOU  513  N   GLY A 247     2330   2104   2259    -72     23    206       N  
ATOM    514  CA  GLY A 247      12.104  12.825  27.926  1.00 21.07           C  
ANISOU  514  CA  GLY A 247     2755   2536   2716    -73     31    182       C  
ATOM    515  C   GLY A 247      12.272  13.038  26.437  1.00 21.47           C  
ANISOU  515  C   GLY A 247     2792   2590   2774    -64     17    165       C  
ATOM    516  O   GLY A 247      13.398  13.102  25.931  1.00 15.31           O  
ANISOU  516  O   GLY A 247     2013   1815   1988    -57      3    173       O  
ATOM    517  N   HIS A 248      11.150  13.161  25.734  1.00 19.36           N  
ANISOU  517  N   HIS A 248     2512   2324   2522    -62     20    142       N  
ATOM    518  CA  HIS A 248      11.161  13.137  24.278  1.00 21.55           C  
ANISOU  518  CA  HIS A 248     2774   2606   2808    -52      9    124       C  
ATOM    519  C   HIS A 248      10.811  14.493  23.659  1.00 21.88           C  
ANISOU  519  C   HIS A 248     2815   2661   2837    -43     -2    112       C  
ATOM    520  O   HIS A 248      10.998  14.680  22.460  1.00 18.21           O  
ANISOU  520  O   HIS A 248     2342   2204   2373    -32    -14    102       O  
ATOM    521  CB  HIS A 248      10.183  12.072  23.762  1.00 20.71           C  
ANISOU  521  CB  HIS A 248     2649   2490   2730    -53     20    104       C  
ATOM    522  CG  HIS A 248       8.757  12.325  24.151  1.00 26.10           C  
ANISOU  522  CG  HIS A 248     3325   3171   3420    -59     32     87       C  
ATOM    523  ND1 HIS A 248       7.893  13.074  23.376  1.00 26.13           N  
ANISOU  523  ND1 HIS A 248     3317   3187   3425    -51     26     63       N  
ATOM    524  CD2 HIS A 248       8.046  11.945  25.240  1.00 28.28           C  
ANISOU  524  CD2 HIS A 248     3605   3435   3704    -70     52     89       C  
ATOM    525  CE1 HIS A 248       6.712  13.136  23.966  1.00 25.76           C  
ANISOU  525  CE1 HIS A 248     3265   3135   3387    -58     40     51       C  
ATOM    526  NE2 HIS A 248       6.777  12.459  25.101  1.00 27.14           N  
ANISOU  526  NE2 HIS A 248     3450   3295   3567    -71     57     66       N  
ATOM    527  N   LYS A 249      10.302  15.424  24.468  1.00 16.89           N  
ANISOU  527  N   LYS A 249     2191   2032   2193    -48      4    113       N  
ATOM    528  CA  LYS A 249       9.697  16.635  23.919  1.00 20.13           C  
ANISOU  528  CA  LYS A 249     2598   2453   2597    -39     -2    100       C  
ATOM    529  C   LYS A 249      10.679  17.588  23.256  1.00 19.25           C  
ANISOU  529  C   LYS A 249     2494   2350   2470    -29    -15    108       C  
ATOM    530  O   LYS A 249      10.312  18.283  22.295  1.00 17.50           O  
ANISOU  530  O   LYS A 249     2266   2136   2246    -16    -22     97       O  
ATOM    531  CB  LYS A 249       8.880  17.386  24.966  1.00 18.07           C  
ANISOU  531  CB  LYS A 249     2344   2191   2331    -48     10     98       C  
ATOM    532  CG  LYS A 249       7.505  16.789  25.222  1.00 28.35           C  
ANISOU  532  CG  LYS A 249     3633   3486   3652    -53     24     81       C  
ATOM    533  CD  LYS A 249       6.799  17.498  26.367  1.00 27.50           C  
ANISOU  533  CD  LYS A 249     3534   3378   3539    -63     37     81       C  
ATOM    534  CE  LYS A 249       5.552  16.731  26.817  1.00 41.85           C  
ANISOU  534  CE  LYS A 249     5341   5185   5376    -73     54     66       C  
ATOM    535  NZ  LYS A 249       4.526  16.674  25.744  1.00 46.94           N  
ANISOU  535  NZ  LYS A 249     5964   5834   6038    -63     51     39       N  
ATOM    536  N   VAL A 250      11.912  17.640  23.760  1.00 10.50           N  
ANISOU  536  N   VAL A 250     1398   1241   1350    -34    -19    126       N  
ATOM    537  CA  VAL A 250      12.899  18.520  23.128  1.00 13.23           C  
ANISOU  537  CA  VAL A 250     1751   1594   1683    -25    -29    131       C  
ATOM    538  C   VAL A 250      13.385  17.963  21.774  1.00 12.10           C  
ANISOU  538  C   VAL A 250     1598   1452   1546    -14    -40    127       C  
ATOM    539  O   VAL A 250      13.324  18.665  20.774  1.00 17.43           O  
ANISOU  539  O   VAL A 250     2271   2134   2217     -1    -45    120       O  
ATOM    540  CB  VAL A 250      14.030  18.936  24.093  1.00 14.82           C  
ANISOU  540  CB  VAL A 250     1966   1796   1870    -34    -29    148       C  
ATOM    541  CG1 VAL A 250      15.157  19.648  23.340  1.00  9.77           C  
ANISOU  541  CG1 VAL A 250     1330   1160   1221    -26    -38    151       C  
ATOM    542  CG2 VAL A 250      13.449  19.838  25.205  1.00 12.64           C  
ANISOU  542  CG2 VAL A 250     1697   1521   1584    -43    -19    147       C  
ATOM    543  N   ALA A 251      13.818  16.701  21.731  1.00 13.60           N  
ANISOU  543  N   ALA A 251     1783   1636   1747    -18    -41    131       N  
ATOM    544  CA  ALA A 251      14.174  16.035  20.463  1.00 13.08           C  
ANISOU  544  CA  ALA A 251     1707   1572   1690     -9    -49    123       C  
ATOM    545  C   ALA A 251      13.076  16.146  19.395  1.00 13.36           C  
ANISOU  545  C   ALA A 251     1728   1616   1731      3    -51    102       C  
ATOM    546  O   ALA A 251      13.364  16.425  18.224  1.00 14.79           O  
ANISOU  546  O   ALA A 251     1905   1806   1908     15    -60     96       O  
ATOM    547  CB  ALA A 251      14.531  14.558  20.708  1.00 12.96           C  
ANISOU  547  CB  ALA A 251     1686   1547   1691    -16    -45    128       C  
ATOM    548  N   ASP A 252      11.824  15.934  19.798  1.00 16.19           N  
ANISOU  548  N   ASP A 252     2079   1973   2100     -1    -43     89       N  
ATOM    549  CA  ASP A 252      10.687  16.147  18.896  1.00 22.80           C  
ANISOU  549  CA  ASP A 252     2900   2820   2942     10    -46     67       C  
ATOM    550  C   ASP A 252      10.593  17.590  18.394  1.00 17.75           C  
ANISOU  550  C   ASP A 252     2267   2192   2285     25    -52     68       C  
ATOM    551  O   ASP A 252      10.402  17.829  17.192  1.00 16.45           O  
ANISOU  551  O   ASP A 252     2094   2040   2116     41    -61     58       O  
ATOM    552  CB  ASP A 252       9.362  15.766  19.565  1.00 22.23           C  
ANISOU  552  CB  ASP A 252     2818   2743   2885      2    -34     53       C  
ATOM    553  CG  ASP A 252       9.228  14.276  19.800  1.00 31.58           C  
ANISOU  553  CG  ASP A 252     3992   3916   4091     -9    -24     46       C  
ATOM    554  OD1 ASP A 252      10.093  13.508  19.324  1.00 33.12           O  
ANISOU  554  OD1 ASP A 252     4184   4107   4291     -9    -28     51       O  
ATOM    555  OD2 ASP A 252       8.245  13.872  20.454  1.00 38.39           O  
ANISOU  555  OD2 ASP A 252     4848   4771   4968    -18    -11     36       O  
ATOM    556  N   TYR A 253      10.702  18.554  19.308  1.00 15.24           N  
ANISOU  556  N   TYR A 253     1964   1870   1956     19    -46     81       N  
ATOM    557  CA  TYR A 253      10.634  19.957  18.886  1.00 15.30           C  
ANISOU  557  CA  TYR A 253     1978   1884   1949     33    -49     84       C  
ATOM    558  C   TYR A 253      11.722  20.244  17.848  1.00 13.84           C  
ANISOU  558  C   TYR A 253     1799   1704   1754     44    -58     92       C  
ATOM    559  O   TYR A 253      11.460  20.876  16.828  1.00 16.27           O  
ANISOU  559  O   TYR A 253     2104   2022   2055     63    -63     88       O  
ATOM    560  CB  TYR A 253      10.756  20.922  20.071  1.00 13.31           C  
ANISOU  560  CB  TYR A 253     1742   1626   1691     22    -39     95       C  
ATOM    561  CG  TYR A 253      10.448  22.356  19.679  1.00 18.88           C  
ANISOU  561  CG  TYR A 253     2451   2335   2386     36    -38     95       C  
ATOM    562  CD1 TYR A 253       9.139  22.759  19.410  1.00 18.07           C  
ANISOU  562  CD1 TYR A 253     2339   2239   2289     47    -36     82       C  
ATOM    563  CD2 TYR A 253      11.465  23.298  19.558  1.00 14.90           C  
ANISOU  563  CD2 TYR A 253     1961   1829   1871     39    -36    109       C  
ATOM    564  CE1 TYR A 253       8.856  24.067  19.041  1.00 27.48           C  
ANISOU  564  CE1 TYR A 253     3536   3433   3473     62    -34     85       C  
ATOM    565  CE2 TYR A 253      11.190  24.620  19.192  1.00 19.26           C  
ANISOU  565  CE2 TYR A 253     2519   2382   2417     53    -31    111       C  
ATOM    566  CZ  TYR A 253       9.890  24.992  18.927  1.00 21.24           C  
ANISOU  566  CZ  TYR A 253     2761   2639   2672     65    -30    100       C  
ATOM    567  OH  TYR A 253       9.624  26.288  18.559  1.00 18.68           O  
ANISOU  567  OH  TYR A 253     2442   2314   2343     80    -24    104       O  
ATOM    568  N   CYS A 254      12.943  19.781  18.121  1.00 13.62           N  
ANISOU  568  N   CYS A 254     1779   1670   1726     35    -59    104       N  
ATOM    569  CA  CYS A 254      14.067  19.896  17.181  1.00 18.15           C  
ANISOU  569  CA  CYS A 254     2357   2247   2293     43    -66    111       C  
ATOM    570  C   CYS A 254      13.726  19.283  15.822  1.00 18.12           C  
ANISOU  570  C   CYS A 254     2339   2254   2292     58    -74     97       C  
ATOM    571  O   CYS A 254      13.996  19.875  14.779  1.00 15.32           O  
ANISOU  571  O   CYS A 254     1986   1907   1926     74    -78     98       O  
ATOM    572  CB  CYS A 254      15.331  19.224  17.741  1.00 14.61           C  
ANISOU  572  CB  CYS A 254     1915   1790   1847     30    -66    123       C  
ATOM    573  SG  CYS A 254      16.098  20.164  19.102  1.00 20.02           S  
ANISOU  573  SG  CYS A 254     2617   2468   2522     16    -59    138       S  
ATOM    574  N   ARG A 255      13.145  18.086  15.845  1.00 15.96           N  
ANISOU  574  N   ARG A 255     2051   1981   2033     52    -75     83       N  
ATOM    575  CA  ARG A 255      12.725  17.429  14.620  1.00 16.80           C  
ANISOU  575  CA  ARG A 255     2140   2099   2144     64    -83     65       C  
ATOM    576  C   ARG A 255      11.759  18.334  13.861  1.00 19.33           C  
ANISOU  576  C   ARG A 255     2455   2435   2453     84    -87     55       C  
ATOM    577  O   ARG A 255      11.904  18.514  12.662  1.00 24.62           O  
ANISOU  577  O   ARG A 255     3121   3119   3112    101    -95     50       O  
ATOM    578  CB  ARG A 255      12.023  16.119  14.925  1.00 18.72           C  
ANISOU  578  CB  ARG A 255     2366   2338   2409     53    -79     49       C  
ATOM    579  CG  ARG A 255      11.194  15.579  13.746  1.00 22.42           C  
ANISOU  579  CG  ARG A 255     2813   2823   2884     65    -85     22       C  
ATOM    580  CD  ARG A 255      10.498  14.284  14.109  1.00 21.21           C  
ANISOU  580  CD  ARG A 255     2641   2662   2756     52    -78      3       C  
ATOM    581  NE  ARG A 255       9.458  14.505  15.112  1.00 22.63           N  
ANISOU  581  NE  ARG A 255     2820   2835   2943     44    -68     -1       N  
ATOM    582  CZ  ARG A 255       9.004  13.562  15.935  1.00 29.10           C  
ANISOU  582  CZ  ARG A 255     3633   3640   3784     28    -55     -7       C  
ATOM    583  NH1 ARG A 255       9.514  12.329  15.896  1.00 23.62           N  
ANISOU  583  NH1 ARG A 255     2932   2935   3108     18    -49     -9       N  
ATOM    584  NH2 ARG A 255       8.047  13.852  16.806  1.00 30.40           N  
ANISOU  584  NH2 ARG A 255     3797   3799   3954     21    -45    -10       N  
ATOM    585  N   ASP A 256      10.779  18.903  14.563  1.00 17.67           N  
ANISOU  585  N   ASP A 256     2245   2224   2245     83    -81     52       N  
ATOM    586  CA  ASP A 256       9.733  19.698  13.912  1.00 22.98           C  
ANISOU  586  CA  ASP A 256     2911   2912   2909    103    -86     41       C  
ATOM    587  C   ASP A 256      10.182  21.091  13.443  1.00 20.33           C  
ANISOU  587  C   ASP A 256     2591   2580   2554    120    -86     59       C  
ATOM    588  O   ASP A 256       9.608  21.632  12.505  1.00 24.79           O  
ANISOU  588  O   ASP A 256     3151   3161   3108    143    -92     53       O  
ATOM    589  CB  ASP A 256       8.505  19.852  14.824  1.00 23.79           C  
ANISOU  589  CB  ASP A 256     3007   3011   3022     96    -78     31       C  
ATOM    590  CG  ASP A 256       7.897  18.498  15.259  1.00 29.20           C  
ANISOU  590  CG  ASP A 256     3675   3691   3729     80    -74     13       C  
ATOM    591  OD1 ASP A 256       7.158  18.487  16.264  1.00 34.20           O  
ANISOU  591  OD1 ASP A 256     4307   4316   4373     68    -64      9       O  
ATOM    592  OD2 ASP A 256       8.145  17.455  14.610  1.00 32.97           O  
ANISOU  592  OD2 ASP A 256     4140   4172   4214     79    -79      1       O  
ATOM    593  N   ARG A 257      11.203  21.661  14.080  1.00 18.69           N  
ANISOU  593  N   ARG A 257     2402   2357   2341    110    -78     79       N  
ATOM    594  CA  ARG A 257      11.479  23.100  13.958  1.00 15.56           C  
ANISOU  594  CA  ARG A 257     2021   1958   1931    122    -72     94       C  
ATOM    595  C   ARG A 257      12.903  23.506  13.541  1.00 21.02           C  
ANISOU  595  C   ARG A 257     2729   2644   2614    123    -69    111       C  
ATOM    596  O   ARG A 257      13.099  24.521  12.854  1.00 17.69           O  
ANISOU  596  O   ARG A 257     2317   2225   2181    140    -65    120       O  
ATOM    597  CB  ARG A 257      11.130  23.779  15.286  1.00 17.44           C  
ANISOU  597  CB  ARG A 257     2267   2183   2175    108    -60     99       C  
ATOM    598  CG  ARG A 257      11.645  25.199  15.454  1.00 18.90           C  
ANISOU  598  CG  ARG A 257     2470   2360   2352    112    -49    115       C  
ATOM    599  CD  ARG A 257      10.710  26.249  14.821  1.00 23.24           C  
ANISOU  599  CD  ARG A 257     3019   2917   2896    137    -47    115       C  
ATOM    600  NE  ARG A 257      11.221  27.603  15.044  1.00 24.74           N  
ANISOU  600  NE  ARG A 257     3225   3094   3081    140    -32    130       N  
ATOM    601  CZ  ARG A 257      11.465  28.494  14.086  1.00 26.34           C  
ANISOU  601  CZ  ARG A 257     3436   3298   3274    162    -27    141       C  
ATOM    602  NH1 ARG A 257      11.206  28.201  12.823  1.00 23.39           N  
ANISOU  602  NH1 ARG A 257     3056   2941   2890    186    -38    140       N  
ATOM    603  NH2 ARG A 257      11.944  29.688  14.403  1.00 24.22           N  
ANISOU  603  NH2 ARG A 257     3182   3014   3005    162    -10    154       N  
ATOM    604  N  ALEU A 258      13.902  22.722  13.934  0.57 17.69           N  
ANISOU  604  N  ALEU A 258     2310   2215   2199    105    -70    114       N  
ATOM    605  N  BLEU A 258      13.891  22.715  13.950  0.43 17.69           N  
ANISOU  605  N  BLEU A 258     2309   2213   2198    105    -70    114       N  
ATOM    606  CA ALEU A 258      15.272  23.200  13.806  0.57 17.02           C  
ANISOU  606  CA ALEU A 258     2239   2121   2107    102    -65    129       C  
ATOM    607  CA BLEU A 258      15.286  23.114  13.801  0.43 17.08           C  
ANISOU  607  CA BLEU A 258     2246   2129   2116    102    -66    128       C  
ATOM    608  C  ALEU A 258      15.677  23.582  12.373  0.57 19.73           C  
ANISOU  608  C  ALEU A 258     2586   2473   2439    124    -67    132       C  
ATOM    609  C  BLEU A 258      15.645  23.575  12.387  0.43 19.66           C  
ANISOU  609  C  BLEU A 258     2577   2464   2430    124    -67    132       C  
ATOM    610  O  ALEU A 258      16.287  24.633  12.159  0.57 16.83           O  
ANISOU  610  O  ALEU A 258     2233   2099   2064    130    -57    145       O  
ATOM    611  O  BLEU A 258      16.196  24.663  12.204  0.43 16.92           O  
ANISOU  611  O  BLEU A 258     2244   2111   2076    130    -57    144       O  
ATOM    612  CB ALEU A 258      16.254  22.207  14.417  0.57 17.84           C  
ANISOU  612  CB ALEU A 258     2342   2217   2220     82    -68    131       C  
ATOM    613  CB BLEU A 258      16.212  21.981  14.239  0.43 17.97           C  
ANISOU  613  CB BLEU A 258     2356   2235   2238     84    -70    129       C  
ATOM    614  CG ALEU A 258      17.609  22.830  14.743  0.57 18.03           C  
ANISOU  614  CG ALEU A 258     2380   2230   2240     74    -61    144       C  
ATOM    615  CG BLEU A 258      17.695  22.343  14.332  0.43 18.00           C  
ANISOU  615  CG BLEU A 258     2371   2229   2238     76    -66    141       C  
ATOM    616  CD1ALEU A 258      18.292  22.084  15.880  0.57 17.42           C  
ANISOU  616  CD1ALEU A 258     2302   2145   2171     53    -63    146       C  
ATOM    617  CD1BLEU A 258      18.357  22.343  12.966  0.43 16.72           C  
ANISOU  617  CD1BLEU A 258     2211   2073   2069     91    -68    142       C  
ATOM    618  CD2ALEU A 258      18.485  22.863  13.506  0.57 17.22           C  
ANISOU  618  CD2ALEU A 258     2281   2131   2133     86    -63    147       C  
ATOM    619  CD2BLEU A 258      17.876  23.682  15.030  0.43 17.26           C  
ANISOU  619  CD2BLEU A 258     2291   2128   2140     73    -53    149       C  
ATOM    620  N   HIS A 259      15.346  22.748  11.387  1.00 20.11           N  
ANISOU  620  N   HIS A 259     2621   2535   2484    135    -78    121       N  
ATOM    621  CA  HIS A 259      15.719  23.082  10.008  1.00 18.93           C  
ANISOU  621  CA  HIS A 259     2476   2397   2321    156    -80    124       C  
ATOM    622  C   HIS A 259      15.016  24.346   9.488  1.00 20.21           C  
ANISOU  622  C   HIS A 259     2645   2566   2468    180    -75    132       C  
ATOM    623  O   HIS A 259      15.613  25.104   8.712  1.00 20.56           O  
ANISOU  623  O   HIS A 259     2702   2610   2500    195    -67    145       O  
ATOM    624  CB  HIS A 259      15.589  21.897   9.037  1.00 15.81           C  
ANISOU  624  CB  HIS A 259     2064   2019   1926    162    -93    108       C  
ATOM    625  CG  HIS A 259      14.231  21.267   9.009  1.00 23.12           C  
ANISOU  625  CG  HIS A 259     2970   2958   2856    166   -102     88       C  
ATOM    626  ND1 HIS A 259      13.731  20.527  10.057  1.00 22.74           N  
ANISOU  626  ND1 HIS A 259     2912   2902   2827    146   -102     78       N  
ATOM    627  CD2 HIS A 259      13.284  21.241   8.042  1.00 26.15           C  
ANISOU  627  CD2 HIS A 259     3341   3365   3231    188   -111     74       C  
ATOM    628  CE1 HIS A 259      12.528  20.080   9.741  1.00 27.56           C  
ANISOU  628  CE1 HIS A 259     3504   3528   3441    154   -109     58       C  
ATOM    629  NE2 HIS A 259      12.232  20.505   8.529  1.00 25.59           N  
ANISOU  629  NE2 HIS A 259     3251   3298   3174    180   -116     54       N  
ATOM    630  N   PHE A 260      13.776  24.580   9.932  1.00 15.07           N  
ANISOU  630  N   PHE A 260     1986   1919   1821    185    -76    124       N  
ATOM    631  CA  PHE A 260      13.060  25.823   9.590  1.00 23.53           C  
ANISOU  631  CA  PHE A 260     3063   2995   2881    208    -70    133       C  
ATOM    632  C   PHE A 260      13.721  27.041  10.231  1.00 21.63           C  
ANISOU  632  C   PHE A 260     2843   2733   2642    202    -51    152       C  
ATOM    633  O   PHE A 260      13.867  28.085   9.599  1.00 21.47           O  
ANISOU  633  O   PHE A 260     2836   2711   2612    222    -41    166       O  
ATOM    634  CB  PHE A 260      11.577  25.755   9.982  1.00 20.26           C  
ANISOU  634  CB  PHE A 260     2634   2590   2472    213    -76    118       C  
ATOM    635  CG  PHE A 260      10.802  24.730   9.217  1.00 26.41           C  
ANISOU  635  CG  PHE A 260     3392   3393   3250    223    -93     97       C  
ATOM    636  CD1 PHE A 260      10.517  24.921   7.869  1.00 25.99           C  
ANISOU  636  CD1 PHE A 260     3335   3363   3178    253   -102     95       C  
ATOM    637  CD2 PHE A 260      10.386  23.562   9.834  1.00 21.11           C  
ANISOU  637  CD2 PHE A 260     2704   2721   2595    203    -99     77       C  
ATOM    638  CE1 PHE A 260       9.817  23.965   7.153  1.00 29.03           C  
ANISOU  638  CE1 PHE A 260     3696   3772   3560    262   -118     71       C  
ATOM    639  CE2 PHE A 260       9.681  22.588   9.118  1.00 28.53           C  
ANISOU  639  CE2 PHE A 260     3621   3682   3537    210   -113     53       C  
ATOM    640  CZ  PHE A 260       9.398  22.791   7.775  1.00 27.64           C  
ANISOU  640  CZ  PHE A 260     3502   3594   3405    240   -123     48       C  
ATOM    641  N   ALA A 261      14.130  26.896  11.486  1.00 18.00           N  
ANISOU  641  N   ALA A 261     2386   2258   2197    175    -46    151       N  
ATOM    642  CA  ALA A 261      14.881  27.951  12.159  1.00 19.32           C  
ANISOU  642  CA  ALA A 261     2570   2405   2367    165    -28    164       C  
ATOM    643  C   ALA A 261      16.184  28.245  11.413  1.00 21.99           C  
ANISOU  643  C   ALA A 261     2920   2737   2699    169    -20    176       C  
ATOM    644  O   ALA A 261      16.593  29.401  11.272  1.00 22.56           O  
ANISOU  644  O   ALA A 261     3005   2796   2768    177     -2    188       O  
ATOM    645  CB  ALA A 261      15.178  27.554  13.611  1.00 20.30           C  
ANISOU  645  CB  ALA A 261     2692   2518   2503    135    -26    159       C  
ATOM    646  N   LEU A 262      16.843  27.190  10.940  1.00 20.72           N  
ANISOU  646  N   LEU A 262     2754   2583   2537    164    -31    171       N  
ATOM    647  CA  LEU A 262      18.106  27.349  10.229  1.00 17.35           C  
ANISOU  647  CA  LEU A 262     2337   2150   2105    166    -24    180       C  
ATOM    648  C   LEU A 262      17.879  28.080   8.901  1.00 23.35           C  
ANISOU  648  C   LEU A 262     3104   2917   2849    197    -18    190       C  
ATOM    649  O   LEU A 262      18.659  28.947   8.527  1.00 20.05           O  
ANISOU  649  O   LEU A 262     2702   2488   2428    203     -1    203       O  
ATOM    650  CB  LEU A 262      18.776  25.992   9.989  1.00 17.71           C  
ANISOU  650  CB  LEU A 262     2373   2202   2154    155    -38    171       C  
ATOM    651  CG  LEU A 262      19.941  25.901   8.991  1.00 20.50           C  
ANISOU  651  CG  LEU A 262     2733   2554   2502    160    -34    176       C  
ATOM    652  CD1 LEU A 262      21.179  26.699   9.432  1.00 19.11           C  
ANISOU  652  CD1 LEU A 262     2570   2358   2332    147    -17    185       C  
ATOM    653  CD2 LEU A 262      20.306  24.455   8.769  1.00 16.02           C  
ANISOU  653  CD2 LEU A 262     2152   1994   1940    150    -49    164       C  
ATOM    654  N   ALA A 263      16.819  27.713   8.191  1.00 17.69           N  
ANISOU  654  N   ALA A 263     2378   2222   2122    217    -32    183       N  
ATOM    655  CA  ALA A 263      16.501  28.375   6.926  1.00 23.36           C  
ANISOU  655  CA  ALA A 263     3102   2952   2821    250    -28    193       C  
ATOM    656  C   ALA A 263      16.189  29.861   7.146  1.00 25.24           C  
ANISOU  656  C   ALA A 263     3355   3176   3058    263     -8    210       C  
ATOM    657  O   ALA A 263      16.552  30.700   6.320  1.00 24.70           O  
ANISOU  657  O   ALA A 263     3302   3105   2979    284      6    227       O  
ATOM    658  CB  ALA A 263      15.339  27.669   6.212  1.00 19.87           C  
ANISOU  658  CB  ALA A 263     2644   2539   2369    269    -48    179       C  
ATOM    659  N   GLU A 264      15.529  30.192   8.255  1.00 22.05           N  
ANISOU  659  N   GLU A 264     2947   2764   2667    251     -5    206       N  
ATOM    660  CA  GLU A 264      15.317  31.609   8.595  1.00 29.69           C  
ANISOU  660  CA  GLU A 264     3928   3714   3639    260     16    220       C  
ATOM    661  C   GLU A 264      16.651  32.343   8.746  1.00 30.47           C  
ANISOU  661  C   GLU A 264     4044   3789   3745    248     40    232       C  
ATOM    662  O   GLU A 264      16.838  33.450   8.242  1.00 28.37           O  
ANISOU  662  O   GLU A 264     3793   3511   3475    266     61    249       O  
ATOM    663  CB  GLU A 264      14.441  31.762   9.849  1.00 25.45           C  
ANISOU  663  CB  GLU A 264     3382   3171   3116    245     16    210       C  
ATOM    664  CG  GLU A 264      12.996  31.377   9.582  1.00 30.74           C  
ANISOU  664  CG  GLU A 264     4036   3862   3780    262     -2    200       C  
ATOM    665  CD  GLU A 264      12.213  30.983  10.832  1.00 38.56           C  
ANISOU  665  CD  GLU A 264     5015   4851   4786    241     -8    184       C  
ATOM    666  OE1 GLU A 264      12.666  31.298  11.958  1.00 42.89           O  
ANISOU  666  OE1 GLU A 264     5568   5380   5346    216      4    184       O  
ATOM    667  OE2 GLU A 264      11.137  30.351  10.680  1.00 30.11           O  
ANISOU  667  OE2 GLU A 264     3928   3799   3715    249    -24    170       O  
ATOM    668  N   GLU A 265      17.595  31.688   9.405  1.00 22.78           N  
ANISOU  668  N   GLU A 265     3067   2807   2781    219     37    223       N  
ATOM    669  CA  GLU A 265      18.862  32.306   9.733  1.00 23.44           C  
ANISOU  669  CA  GLU A 265     3163   2869   2874    204     58    229       C  
ATOM    670  C   GLU A 265      19.739  32.475   8.474  1.00 31.47           C  
ANISOU  670  C   GLU A 265     4192   3885   3881    219     67    240       C  
ATOM    671  O   GLU A 265      20.420  33.486   8.298  1.00 25.30           O  
ANISOU  671  O   GLU A 265     3424   3084   3104    222     93    251       O  
ATOM    672  CB  GLU A 265      19.556  31.463  10.806  1.00 25.74           C  
ANISOU  672  CB  GLU A 265     3446   3158   3178    170     48    214       C  
ATOM    673  CG  GLU A 265      20.257  32.268  11.889  1.00 38.31           C  
ANISOU  673  CG  GLU A 265     5043   4729   4784    149     67    212       C  
ATOM    674  CD  GLU A 265      19.331  33.260  12.604  1.00 37.60           C  
ANISOU  674  CD  GLU A 265     4955   4631   4701    151     80    213       C  
ATOM    675  OE1 GLU A 265      19.735  34.428  12.749  1.00 37.58           O  
ANISOU  675  OE1 GLU A 265     4963   4610   4707    150    105    218       O  
ATOM    676  OE2 GLU A 265      18.219  32.874  13.028  1.00 46.32           O  
ANISOU  676  OE2 GLU A 265     6049   5746   5803    152     66    207       O  
ATOM    677  N   ILE A 266      19.703  31.486   7.590  1.00 23.27           N  
ANISOU  677  N   ILE A 266     3147   2866   2830    229     49    236       N  
ATOM    678  CA  ILE A 266      20.451  31.559   6.342  1.00 27.30           C  
ANISOU  678  CA  ILE A 266     3666   3378   3327    245     56    246       C  
ATOM    679  C   ILE A 266      19.934  32.721   5.496  1.00 33.84           C  
ANISOU  679  C   ILE A 266     4510   4206   4143    278     74    266       C  
ATOM    680  O   ILE A 266      20.717  33.479   4.932  1.00 31.92           O  
ANISOU  680  O   ILE A 266     4283   3947   3897    287     98    281       O  
ATOM    681  CB  ILE A 266      20.365  30.240   5.551  1.00 29.22           C  
ANISOU  681  CB  ILE A 266     3897   3646   3558    250     32    236       C  
ATOM    682  CG1 ILE A 266      21.162  29.149   6.267  1.00 24.90           C  
ANISOU  682  CG1 ILE A 266     3340   3096   3027    218     20    220       C  
ATOM    683  CG2 ILE A 266      20.901  30.427   4.138  1.00 35.40           C  
ANISOU  683  CG2 ILE A 266     4692   4435   4323    272     40    247       C  
ATOM    684  CD1 ILE A 266      21.048  27.768   5.627  1.00 27.93           C  
ANISOU  684  CD1 ILE A 266     3708   3500   3403    220     -3    207       C  
ATOM    685  N   GLU A 267      18.613  32.862   5.442  1.00 30.11           N  
ANISOU  685  N   GLU A 267     4031   3747   3661    298     64    267       N  
ATOM    686  CA  GLU A 267      17.981  33.951   4.712  1.00 38.63           C  
ANISOU  686  CA  GLU A 267     5123   4828   4729    332     78    287       C  
ATOM    687  C   GLU A 267      18.434  35.305   5.246  1.00 42.15           C  
ANISOU  687  C   GLU A 267     5584   5240   5190    328    112    301       C  
ATOM    688  O   GLU A 267      18.681  36.230   4.477  1.00 48.37           O  
ANISOU  688  O   GLU A 267     6390   6018   5971    351    136    322       O  
ATOM    689  CB  GLU A 267      16.461  33.837   4.786  1.00 36.75           C  
ANISOU  689  CB  GLU A 267     4870   4609   4482    350     59    282       C  
ATOM    690  CG  GLU A 267      15.812  33.392   3.485  1.00 55.88           C  
ANISOU  690  CG  GLU A 267     7288   7066   6878    384     41    283       C  
ATOM    691  CD  GLU A 267      15.955  34.420   2.382  1.00 67.10           C  
ANISOU  691  CD  GLU A 267     8728   8485   8280    420     61    310       C  
ATOM    692  OE1 GLU A 267      16.538  35.491   2.645  1.00 58.77           O  
ANISOU  692  OE1 GLU A 267     7693   7401   7237    418     92    328       O  
ATOM    693  OE2 GLU A 267      15.488  34.159   1.255  1.00 62.17           O  
ANISOU  693  OE2 GLU A 267     8102   7890   7630    451     48    314       O  
ATOM    694  N   ARG A 268      18.550  35.418   6.564  1.00 37.45           N  
ANISOU  694  N   ARG A 268     4983   4629   4617    298    116    289       N  
ATOM    695  CA  ARG A 268      19.051  36.649   7.171  1.00 34.98           C  
ANISOU  695  CA  ARG A 268     4683   4285   4323    288    149    297       C  
ATOM    696  C   ARG A 268      20.463  36.961   6.692  1.00 44.75           C  
ANISOU  696  C   ARG A 268     5934   5504   5564    282    172    304       C  
ATOM    697  O   ARG A 268      20.707  38.009   6.102  1.00 51.29           O  
ANISOU  697  O   ARG A 268     6779   6316   6393    300    202    323       O  
ATOM    698  CB  ARG A 268      19.024  36.557   8.692  1.00 38.82           C  
ANISOU  698  CB  ARG A 268     5158   4762   4830    255    147    279       C  
ATOM    699  CG  ARG A 268      17.673  36.895   9.320  1.00 43.87           C  
ANISOU  699  CG  ARG A 268     5790   5405   5473    261    141    276       C  
ATOM    700  CD  ARG A 268      17.599  36.374  10.756  1.00 49.68           C  
ANISOU  700  CD  ARG A 268     6512   6140   6222    227    130    255       C  
ATOM    701  NE  ARG A 268      16.522  37.001  11.520  1.00 61.78           N  
ANISOU  701  NE  ARG A 268     8040   7669   7764    228    135    252       N  
ATOM    702  CZ  ARG A 268      15.247  36.624  11.471  1.00 63.07           C  
ANISOU  702  CZ  ARG A 268     8193   7850   7920    242    116    249       C  
ATOM    703  NH1 ARG A 268      14.880  35.620  10.683  1.00 57.86           N  
ANISOU  703  NH1 ARG A 268     7526   7215   7245    255     91    246       N  
ATOM    704  NH2 ARG A 268      14.337  37.253  12.207  1.00 57.56           N  
ANISOU  704  NH2 ARG A 268     7491   7145   7232    241    123    245       N  
ATOM    705  N   ILE A 269      21.394  36.048   6.936  1.00 33.51           N  
ANISOU  705  N   ILE A 269     4503   4084   4145    257    160    289       N  
ATOM    706  CA  ILE A 269      22.784  36.279   6.574  1.00 38.88           C  
ANISOU  706  CA  ILE A 269     5194   4747   4832    247    181    292       C  
ATOM    707  C   ILE A 269      22.948  36.480   5.067  1.00 37.69           C  
ANISOU  707  C   ILE A 269     5058   4601   4662    278    192    311       C  
ATOM    708  O   ILE A 269      23.778  37.262   4.633  1.00 38.67           O  
ANISOU  708  O   ILE A 269     5197   4704   4792    282    223    322       O  
ATOM    709  CB  ILE A 269      23.691  35.130   7.051  1.00 33.17           C  
ANISOU  709  CB  ILE A 269     4458   4030   4115    217    162    272       C  
ATOM    710  CG1 ILE A 269      25.151  35.560   7.011  1.00 33.85           C  
ANISOU  710  CG1 ILE A 269     4551   4093   4215    202    188    269       C  
ATOM    711  CG2 ILE A 269      23.482  33.894   6.199  1.00 35.26           C  
ANISOU  711  CG2 ILE A 269     4715   4322   4361    228    134    269       C  
ATOM    712  CD1 ILE A 269      26.081  34.602   7.707  1.00 36.36           C  
ANISOU  712  CD1 ILE A 269     4857   4416   4544    171    171    249       C  
ATOM    713  N   LYS A 270      22.149  35.766   4.282  1.00 41.12           N  
ANISOU  713  N   LYS A 270     5486   5064   5072    301    167    314       N  
ATOM    714  CA  LYS A 270      22.171  35.870   2.828  1.00 41.74           C  
ANISOU  714  CA  LYS A 270     5577   5154   5127    333    172    332       C  
ATOM    715  C   LYS A 270      21.879  37.293   2.369  1.00 46.46           C  
ANISOU  715  C   LYS A 270     6196   5735   5723    362    205    358       C  
ATOM    716  O   LYS A 270      22.467  37.789   1.410  1.00 44.82           O  
ANISOU  716  O   LYS A 270     6005   5519   5505    379    228    376       O  
ATOM    717  CB  LYS A 270      21.124  34.926   2.240  1.00 42.07           C  
ANISOU  717  CB  LYS A 270     5606   5233   5145    352    137    326       C  
ATOM    718  CG  LYS A 270      21.220  34.731   0.747  1.00 51.54           C  
ANISOU  718  CG  LYS A 270     6814   6453   6316    383    136    338       C  
ATOM    719  CD  LYS A 270      19.959  34.063   0.217  1.00 67.45           C  
ANISOU  719  CD  LYS A 270     8815   8506   8309    406    104    332       C  
ATOM    720  CE  LYS A 270      18.827  35.078   0.067  1.00 59.68           C  
ANISOU  720  CE  LYS A 270     7836   7524   7314    440    111    350       C  
ATOM    721  NZ  LYS A 270      19.125  36.056  -1.020  1.00 62.71           N  
ANISOU  721  NZ  LYS A 270     8244   7902   7679    473    139    380       N  
ATOM    722  N   ASP A 271      20.960  37.948   3.065  1.00 53.26           N  
ANISOU  722  N   ASP A 271     7054   6590   6593    366    208    361       N  
ATOM    723  CA  ASP A 271      20.580  39.312   2.725  1.00 54.39           C  
ANISOU  723  CA  ASP A 271     7215   6715   6737    394    240    386       C  
ATOM    724  C   ASP A 271      21.653  40.318   3.135  1.00 56.07           C  
ANISOU  724  C   ASP A 271     7442   6887   6976    376    282    391       C  
ATOM    725  O   ASP A 271      21.917  41.275   2.413  1.00 57.23           O  
ANISOU  725  O   ASP A 271     7608   7016   7121    399    316    415       O  
ATOM    726  CB  ASP A 271      19.224  39.659   3.346  1.00 54.66           C  
ANISOU  726  CB  ASP A 271     7239   6754   6773    404    230    386       C  
ATOM    727  CG  ASP A 271      18.093  38.781   2.809  1.00 62.87           C  
ANISOU  727  CG  ASP A 271     8266   7835   7788    427    191    381       C  
ATOM    728  OD1 ASP A 271      18.233  38.238   1.688  1.00 68.44           O  
ANISOU  728  OD1 ASP A 271     8973   8563   8467    447    179    387       O  
ATOM    729  OD2 ASP A 271      17.060  38.639   3.505  1.00 67.15           O  
ANISOU  729  OD2 ASP A 271     8792   8386   8334    424    173    370       O  
ATOM    730  N   GLU A 272      22.286  40.090   4.278  1.00 46.98           N  
ANISOU  730  N   GLU A 272     6280   5723   5849    336    282    368       N  
ATOM    731  CA  GLU A 272      23.367  40.961   4.713  1.00 54.77           C  
ANISOU  731  CA  GLU A 272     7275   6673   6862    316    321    365       C  
ATOM    732  C   GLU A 272      24.567  40.843   3.778  1.00 56.75           C  
ANISOU  732  C   GLU A 272     7537   6916   7107    317    337    372       C  
ATOM    733  O   GLU A 272      25.193  41.841   3.430  1.00 50.83           O  
ANISOU  733  O   GLU A 272     6805   6138   6371    323    378    385       O  
ATOM    734  CB  GLU A 272      23.789  40.638   6.144  1.00 53.71           C  
ANISOU  734  CB  GLU A 272     7123   6532   6751    273    312    336       C  
ATOM    735  CG  GLU A 272      25.257  40.915   6.417  1.00 70.18           C  
ANISOU  735  CG  GLU A 272     9212   8594   8859    246    337    324       C  
ATOM    736  CD  GLU A 272      25.500  41.482   7.800  1.00 83.82           C  
ANISOU  736  CD  GLU A 272    10930  10304  10615    215    351    303       C  
ATOM    737  OE1 GLU A 272      25.978  42.633   7.897  1.00 87.58           O  
ANISOU  737  OE1 GLU A 272    11415  10749  11113    212    392    305       O  
ATOM    738  OE2 GLU A 272      25.217  40.770   8.789  1.00 72.07           O  
ANISOU  738  OE2 GLU A 272     9425   8832   9128    194    322    284       O  
ATOM    739  N   LEU A 273      24.883  39.617   3.376  1.00 44.75           N  
ANISOU  739  N   LEU A 273     6009   5422   5572    311    307    361       N  
ATOM    740  CA  LEU A 273      26.023  39.366   2.499  1.00 45.19           C  
ANISOU  740  CA  LEU A 273     6075   5473   5623    310    319    364       C  
ATOM    741  C   LEU A 273      25.827  39.960   1.113  1.00 52.94           C  
ANISOU  741  C   LEU A 273     7078   6454   6582    351    341    395       C  
ATOM    742  O   LEU A 273      26.799  40.246   0.412  1.00 54.18           O  
ANISOU  742  O   LEU A 273     7249   6596   6741    353    368    403       O  
ATOM    743  CB  LEU A 273      26.278  37.870   2.368  1.00 40.22           C  
ANISOU  743  CB  LEU A 273     5429   4871   4981    297    280    346       C  
ATOM    744  CG  LEU A 273      27.246  37.269   3.379  1.00 50.60           C  
ANISOU  744  CG  LEU A 273     6728   6178   6319    256    272    319       C  
ATOM    745  CD1 LEU A 273      26.915  37.738   4.785  1.00 54.66           C  
ANISOU  745  CD1 LEU A 273     7233   6680   6854    235    274    307       C  
ATOM    746  CD2 LEU A 273      27.203  35.754   3.281  1.00 45.21           C  
ANISOU  746  CD2 LEU A 273     6029   5525   5623    248    231    304       C  
ATOM    747  N   SER A 274      24.568  40.119   0.712  1.00 61.55           N  
ANISOU  747  N   SER A 274     8170   7564   7651    383    328    411       N  
ATOM    748  CA  SER A 274      24.254  40.728  -0.575  1.00 63.07           C  
ANISOU  748  CA  SER A 274     8384   7760   7819    427    346    443       C  
ATOM    749  C   SER A 274      24.497  42.232  -0.523  1.00 68.06           C  
ANISOU  749  C   SER A 274     9037   8353   8471    436    397    465       C  
ATOM    750  O   SER A 274      24.746  42.865  -1.553  1.00 70.48           O  
ANISOU  750  O   SER A 274     9366   8650   8765    465    427    492       O  
ATOM    751  CB  SER A 274      22.803  40.444  -0.978  1.00 65.02           C  
ANISOU  751  CB  SER A 274     8624   8042   8037    460    315    452       C  
ATOM    752  OG  SER A 274      22.634  39.096  -1.387  1.00 68.74           O  
ANISOU  752  OG  SER A 274     9080   8551   8486    458    274    436       O  
ATOM    753  N   LYS A 275      24.431  42.795   0.680  1.00 48.66           N  
ANISOU  753  N   LYS A 275     6572   5872   6046    412    409    452       N  
ATOM    754  CA  LYS A 275      24.578  44.233   0.861  1.00 49.93           C  
ANISOU  754  CA  LYS A 275     6749   5993   6230    419    459    469       C  
ATOM    755  C   LYS A 275      25.986  44.633   1.300  1.00 46.68           C  
ANISOU  755  C   LYS A 275     6340   5545   5851    384    495    453       C  
ATOM    756  O   LYS A 275      26.593  45.522   0.706  1.00 48.34           O  
ANISOU  756  O   LYS A 275     6570   5726   6070    396    540    472       O  
ATOM    757  CB  LYS A 275      23.525  44.737   1.847  1.00 51.52           C  
ANISOU  757  CB  LYS A 275     6940   6190   6446    417    454    465       C  
ATOM    758  CG  LYS A 275      22.129  44.286   1.459  1.00 52.11           C  
ANISOU  758  CG  LYS A 275     7009   6301   6491    450    417    475       C  
ATOM    759  CD  LYS A 275      21.058  44.814   2.394  1.00 54.43           C  
ANISOU  759  CD  LYS A 275     7293   6590   6800    450    414    472       C  
ATOM    760  CE  LYS A 275      19.704  44.213   2.035  1.00 54.24           C  
ANISOU  760  CE  LYS A 275     7258   6605   6746    479    373    476       C  
ATOM    761  NZ  LYS A 275      18.641  44.660   2.972  1.00 65.85           N  
ANISOU  761  NZ  LYS A 275     8716   8071   8231    477    369    470       N  
ATOM    762  N   ARG A 276      26.493  43.972   2.330  1.00 50.63           N  
ANISOU  762  N   ARG A 276     6820   6050   6369    343    474    419       N  
ATOM    763  CA  ARG A 276      27.834  44.243   2.819  1.00 43.83           C  
ANISOU  763  CA  ARG A 276     5956   5160   5538    309    502    399       C  
ATOM    764  C   ARG A 276      28.688  42.995   2.691  1.00 57.77           C  
ANISOU  764  C   ARG A 276     7709   6945   7294    287    473    379       C  
ATOM    765  O   ARG A 276      28.185  41.918   2.382  1.00 56.25           O  
ANISOU  765  O   ARG A 276     7510   6788   7077    296    431    378       O  
ATOM    766  CB  ARG A 276      27.792  44.703   4.275  1.00 35.89           C  
ANISOU  766  CB  ARG A 276     4935   4137   4563    278    508    375       C  
ATOM    767  CG  ARG A 276      27.286  46.118   4.462  1.00 43.76           C  
ANISOU  767  CG  ARG A 276     5943   5103   5580    291    550    390       C  
ATOM    768  CD  ARG A 276      26.206  46.179   5.525  1.00 47.92           C  
ANISOU  768  CD  ARG A 276     6456   5640   6112    285    529    380       C  
ATOM    769  NE  ARG A 276      25.022  46.885   5.049  1.00 53.62           N  
ANISOU  769  NE  ARG A 276     7190   6360   6824    324    539    410       N  
ATOM    770  CZ  ARG A 276      23.775  46.542   5.351  1.00 53.99           C  
ANISOU  770  CZ  ARG A 276     7227   6431   6855    336    506    412       C  
ATOM    771  NH1 ARG A 276      23.539  45.501   6.133  1.00 50.21           N  
ANISOU  771  NH1 ARG A 276     6727   5979   6370    313    462    387       N  
ATOM    772  NH2 ARG A 276      22.762  47.245   4.869  1.00 61.56           N  
ANISOU  772  NH2 ARG A 276     8197   7387   7806    373    517    440       N  
ATOM    773  N   ASN A 277      29.983  43.147   2.929  1.00 67.30           N  
ANISOU  773  N   ASN A 277     8915   8131   8527    260    497    361       N  
ATOM    774  CA  ASN A 277      30.896  42.019   2.886  1.00 61.57           C  
ANISOU  774  CA  ASN A 277     8177   7420   7798    238    472    340       C  
ATOM    775  C   ASN A 277      32.152  42.278   3.694  1.00 58.25           C  
ANISOU  775  C   ASN A 277     7745   6975   7411    200    493    311       C  
ATOM    776  O   ASN A 277      32.975  43.111   3.331  1.00 64.13           O  
ANISOU  776  O   ASN A 277     8502   7690   8175    198    538    314       O  
ATOM    777  CB  ASN A 277      31.268  41.670   1.445  1.00 64.72           C  
ANISOU  777  CB  ASN A 277     8591   7826   8173    261    478    359       C  
ATOM    778  CG  ASN A 277      31.783  40.253   1.306  1.00 69.06           C  
ANISOU  778  CG  ASN A 277     9126   8402   8710    246    439    340       C  
ATOM    779  OD1 ASN A 277      32.987  40.008   1.361  1.00 56.77           O  
ANISOU  779  OD1 ASN A 277     7564   6835   7171    222    449    323       O  
ATOM    780  ND2 ASN A 277      30.868  39.310   1.130  1.00 72.90           N  
ANISOU  780  ND2 ASN A 277     9605   8924   9171    259    396    343       N  
ATOM    781  N   THR A 278      32.291  41.554   4.796  1.00 51.44           N  
ANISOU  781  N   THR A 278     6860   6129   6557    171    461    283       N  
ATOM    782  CA  THR A 278      33.495  41.622   5.601  1.00 52.73           C  
ANISOU  782  CA  THR A 278     7009   6277   6749    136    473    252       C  
ATOM    783  C   THR A 278      34.488  40.617   5.041  1.00 45.23           C  
ANISOU  783  C   THR A 278     6054   5339   5794    127    457    243       C  
ATOM    784  O   THR A 278      34.262  40.040   3.981  1.00 42.60           O  
ANISOU  784  O   THR A 278     5730   5020   5435    149    445    261       O  
ATOM    785  CB  THR A 278      33.196  41.265   7.057  1.00 61.16           C  
ANISOU  785  CB  THR A 278     8055   7360   7825    111    444    228       C  
ATOM    786  OG1 THR A 278      32.277  40.167   7.093  1.00 64.41           O  
ANISOU  786  OG1 THR A 278     8459   7804   8210    121    396    235       O  
ATOM    787  CG2 THR A 278      32.583  42.454   7.783  1.00 60.70           C  
ANISOU  787  CG2 THR A 278     7998   7281   7783    110    470    228       C  
ATOM    788  N   GLY A 279      35.583  40.402   5.756  1.00 51.75           N  
ANISOU  788  N   GLY A 279     6863   6159   6641     96    457    213       N  
ATOM    789  CA  GLY A 279      36.560  39.410   5.348  1.00 47.98           C  
ANISOU  789  CA  GLY A 279     6377   5692   6161     85    441    200       C  
ATOM    790  C   GLY A 279      36.276  38.077   6.009  1.00 50.40           C  
ANISOU  790  C   GLY A 279     6664   6032   6455     75    388    189       C  
ATOM    791  O   GLY A 279      37.144  37.213   6.087  1.00 50.06           O  
ANISOU  791  O   GLY A 279     6607   5997   6416     59    370    172       O  
ATOM    792  N   GLU A 280      35.048  37.919   6.489  1.00 52.46           N  
ANISOU  792  N   GLU A 280     6923   6309   6701     84    364    198       N  
ATOM    793  CA  GLU A 280      34.646  36.723   7.217  1.00 53.57           C  
ANISOU  793  CA  GLU A 280     7046   6478   6830     75    317    188       C  
ATOM    794  C   GLU A 280      34.964  35.434   6.468  1.00 43.41           C  
ANISOU  794  C   GLU A 280     5755   5210   5529     79    290    190       C  
ATOM    795  O   GLU A 280      34.442  35.190   5.386  1.00 49.48           O  
ANISOU  795  O   GLU A 280     6535   5987   6277    103    287    209       O  
ATOM    796  CB  GLU A 280      33.149  36.772   7.539  1.00 58.19           C  
ANISOU  796  CB  GLU A 280     7634   7077   7400     90    300    202       C  
ATOM    797  CG  GLU A 280      32.823  37.308   8.926  1.00 65.14           C  
ANISOU  797  CG  GLU A 280     8504   7953   8294     72    301    188       C  
ATOM    798  CD  GLU A 280      31.341  37.594   9.116  1.00 68.80           C  
ANISOU  798  CD  GLU A 280     8973   8424   8745     90    293    203       C  
ATOM    799  OE1 GLU A 280      30.511  36.747   8.725  1.00 63.90           O  
ANISOU  799  OE1 GLU A 280     8352   7825   8103    105    264    215       O  
ATOM    800  OE2 GLU A 280      31.007  38.669   9.660  1.00 70.36           O  
ANISOU  800  OE2 GLU A 280     9173   8605   8954     87    317    203       O  
ATOM    801  N   GLY A 281      35.815  34.606   7.059  1.00 31.67           N  
ANISOU  801  N   GLY A 281     4250   3731   4052     57    270    168       N  
ATOM    802  CA  GLY A 281      36.035  33.271   6.544  1.00 30.67           C  
ANISOU  802  CA  GLY A 281     4116   3623   3914     59    241    168       C  
ATOM    803  C   GLY A 281      34.725  32.501   6.494  1.00 40.20           C  
ANISOU  803  C   GLY A 281     5322   4854   5099     74    209    180       C  
ATOM    804  O   GLY A 281      33.750  32.827   7.183  1.00 36.14           O  
ANISOU  804  O   GLY A 281     4807   4344   4580     77    203    185       O  
ATOM    805  N  AARG A 282      34.702  31.471   5.663  0.59 29.31           N  
ANISOU  805  N  AARG A 282     3940   3490   3706     83    190    184       N  
ATOM    806  N  BARG A 282      34.701  31.454   5.679  0.41 29.31           N  
ANISOU  806  N  BARG A 282     3940   3489   3706     83    190    184       N  
ATOM    807  CA AARG A 282      33.533  30.616   5.540  0.59 36.20           C  
ANISOU  807  CA AARG A 282     4809   4386   4560     96    160    192       C  
ATOM    808  CA BARG A 282      33.509  30.631   5.548  0.41 36.21           C  
ANISOU  808  CA BARG A 282     4810   4387   4561     97    160    192       C  
ATOM    809  C  AARG A 282      33.168  29.971   6.883  0.59 34.75           C  
ANISOU  809  C  AARG A 282     4609   4213   4383     80    133    181       C  
ATOM    810  C  BARG A 282      33.154  29.921   6.854  0.41 34.76           C  
ANISOU  810  C  BARG A 282     4609   4214   4383     80    132    181       C  
ATOM    811  O  AARG A 282      32.020  30.014   7.318  0.59 30.71           O  
ANISOU  811  O  AARG A 282     4096   3710   3862     87    122    187       O  
ATOM    812  O  BARG A 282      31.991  29.887   7.242  0.41 30.73           O  
ANISOU  812  O  BARG A 282     4099   3715   3864     88    119    187       O  
ATOM    813  CB AARG A 282      33.791  29.531   4.492  0.59 38.00           C  
ANISOU  813  CB AARG A 282     5034   4627   4778    104    146    191       C  
ATOM    814  CB BARG A 282      33.663  29.623   4.409  0.41 38.07           C  
ANISOU  814  CB BARG A 282     5044   4636   4784    107    147    194       C  
ATOM    815  CG AARG A 282      32.901  29.629   3.265  0.59 42.18           C  
ANISOU  815  CG AARG A 282     5575   5168   5282    133    148    208       C  
ATOM    816  CG BARG A 282      33.041  30.083   3.100  0.41 42.27           C  
ANISOU  816  CG BARG A 282     5594   5173   5295    136    160    212       C  
ATOM    817  CD AARG A 282      33.485  30.510   2.176  0.59 31.40           C  
ANISOU  817  CD AARG A 282     4229   3789   3913    146    181    219       C  
ATOM    818  CD BARG A 282      34.081  30.183   2.007  0.41 31.29           C  
ANISOU  818  CD BARG A 282     4213   3774   3904    139    182    213       C  
ATOM    819  NE AARG A 282      33.777  31.864   2.635  0.59 46.32           N  
ANISOU  819  NE AARG A 282     6130   5653   5816    142    214    224       N  
ATOM    820  NE BARG A 282      35.394  29.741   2.470  0.41 45.75           N  
ANISOU  820  NE BARG A 282     6031   5594   5758    113    182    194       N  
ATOM    821  CZ AARG A 282      34.787  32.600   2.170  0.59 53.20           C  
ANISOU  821  CZ AARG A 282     7013   6503   6699    139    248    225       C  
ATOM    822  CZ BARG A 282      36.012  28.646   2.042  0.41 52.51           C  
ANISOU  822  CZ BARG A 282     6877   6459   6615    107    167    184       C  
ATOM    823  NH1AARG A 282      35.593  32.106   1.233  0.59 46.59           N  
ANISOU  823  NH1AARG A 282     6178   5667   5858    140    253    222       N  
ATOM    824  NH1BARG A 282      35.438  27.871   1.136  0.41 46.22           N  
ANISOU  824  NH1BARG A 282     6079   5682   5799    122    151    188       N  
ATOM    825  NH2AARG A 282      34.997  33.824   2.638  0.59 49.03           N  
ANISOU  825  NH2AARG A 282     6494   5951   6186    135    279    227       N  
ATOM    826  NH2BARG A 282      37.204  28.326   2.523  0.41 47.94           N  
ANISOU  826  NH2BARG A 282     6287   5870   6060     84    168    167       N  
ATOM    827  N   GLN A 283      34.149  29.361   7.535  1.00 37.53           N  
ANISOU  827  N   GLN A 283     4946   4564   4749     59    123    165       N  
ATOM    828  CA  GLN A 283      33.871  28.675   8.779  1.00 36.17           C  
ANISOU  828  CA  GLN A 283     4759   4403   4581     45     97    157       C  
ATOM    829  C   GLN A 283      33.232  29.649   9.774  1.00 32.98           C  
ANISOU  829  C   GLN A 283     4359   3994   4178     41    106    157       C  
ATOM    830  O   GLN A 283      32.291  29.297  10.483  1.00 32.75           O  
ANISOU  830  O   GLN A 283     4325   3977   4143     41     89    160       O  
ATOM    831  CB  GLN A 283      35.133  27.998   9.328  1.00 42.69           C  
ANISOU  831  CB  GLN A 283     5570   5228   5422     26     88    141       C  
ATOM    832  CG  GLN A 283      34.852  26.859  10.314  1.00 27.98           C  
ANISOU  832  CG  GLN A 283     3692   3381   3559     17     56    137       C  
ATOM    833  CD  GLN A 283      34.546  27.408  11.677  1.00 34.53           C  
ANISOU  833  CD  GLN A 283     4518   4212   4390      6     55    132       C  
ATOM    834  OE1 GLN A 283      35.009  28.496  12.022  1.00 34.41           O  
ANISOU  834  OE1 GLN A 283     4506   4185   4382     -2     76    125       O  
ATOM    835  NE2 GLN A 283      33.767  26.680  12.457  1.00 28.41           N  
ANISOU  835  NE2 GLN A 283     3736   3449   3608      4     33    136       N  
ATOM    836  N   VAL A 284      33.709  30.884   9.796  1.00 27.69           N  
ANISOU  836  N   VAL A 284     3697   3306   3519     38    136    155       N  
ATOM    837  CA  VAL A 284      33.136  31.898  10.685  1.00 27.10           C  
ANISOU  837  CA  VAL A 284     3625   3225   3448     33    149    154       C  
ATOM    838  C   VAL A 284      31.687  32.267  10.337  1.00 30.17           C  
ANISOU  838  C   VAL A 284     4025   3617   3822     54    150    171       C  
ATOM    839  O   VAL A 284      30.852  32.485  11.229  1.00 25.42           O  
ANISOU  839  O   VAL A 284     3420   3020   3218     51    143    170       O  
ATOM    840  CB  VAL A 284      34.008  33.170  10.728  1.00 38.19           C  
ANISOU  840  CB  VAL A 284     5035   4606   4870     25    186    145       C  
ATOM    841  CG1 VAL A 284      33.285  34.283  11.440  1.00 24.23           C  
ANISOU  841  CG1 VAL A 284     3271   2829   3106     24    203    145       C  
ATOM    842  CG2 VAL A 284      35.375  32.861  11.387  1.00 36.76           C  
ANISOU  842  CG2 VAL A 284     4838   4424   4705      1    182    122       C  
ATOM    843  N   GLN A 285      31.384  32.332   9.044  1.00 25.84           N  
ANISOU  843  N   GLN A 285     3488   3068   3262     76    157    186       N  
ATOM    844  CA  GLN A 285      30.014  32.575   8.599  1.00 31.17           C  
ANISOU  844  CA  GLN A 285     4172   3751   3921     99    155    203       C  
ATOM    845  C   GLN A 285      29.043  31.487   9.088  1.00 25.42           C  
ANISOU  845  C   GLN A 285     3431   3044   3182     99    120    200       C  
ATOM    846  O   GLN A 285      27.982  31.785   9.622  1.00 22.01           O  
ANISOU  846  O   GLN A 285     2999   2617   2747    103    116    203       O  
ATOM    847  CB  GLN A 285      29.965  32.692   7.064  1.00 33.89           C  
ANISOU  847  CB  GLN A 285     4531   4096   4252    124    166    218       C  
ATOM    848  CG  GLN A 285      30.328  34.079   6.528  1.00 36.01           C  
ANISOU  848  CG  GLN A 285     4817   4341   4526    135    206    230       C  
ATOM    849  CD  GLN A 285      30.718  34.073   5.051  1.00 38.13           C  
ANISOU  849  CD  GLN A 285     5098   4608   4781    155    219    243       C  
ATOM    850  OE1 GLN A 285      31.079  33.042   4.493  1.00 43.32           O  
ANISOU  850  OE1 GLN A 285     5750   5280   5431    154    200    238       O  
ATOM    851  NE2 GLN A 285      30.650  35.234   4.418  1.00 46.38           N  
ANISOU  851  NE2 GLN A 285     6162   5636   5824    173    252    260       N  
ATOM    852  N   TRP A 286      29.413  30.225   8.897  1.00 17.11           N  
ANISOU  852  N   TRP A 286     2369   2005   2128     93     97    194       N  
ATOM    853  CA  TRP A 286      28.539  29.111   9.242  1.00 23.28           C  
ANISOU  853  CA  TRP A 286     3138   2805   2902     93     68    191       C  
ATOM    854  C   TRP A 286      28.401  28.977  10.744  1.00 16.69           C  
ANISOU  854  C   TRP A 286     2294   1971   2076     73     58    182       C  
ATOM    855  O   TRP A 286      27.358  28.599  11.253  1.00 13.93           O  
ANISOU  855  O   TRP A 286     1939   1632   1722     75     44    183       O  
ATOM    856  CB  TRP A 286      29.055  27.814   8.621  1.00 15.07           C  
ANISOU  856  CB  TRP A 286     2089   1775   1860     92     50    186       C  
ATOM    857  CG  TRP A 286      28.752  27.773   7.163  1.00 19.47           C  
ANISOU  857  CG  TRP A 286     2654   2341   2403    115     53    194       C  
ATOM    858  CD1 TRP A 286      29.638  27.923   6.124  1.00 16.89           C  
ANISOU  858  CD1 TRP A 286     2335   2008   2074    121     67    197       C  
ATOM    859  CD2 TRP A 286      27.462  27.613   6.574  1.00 19.51           C  
ANISOU  859  CD2 TRP A 286     2659   2362   2392    136     43    200       C  
ATOM    860  NE1 TRP A 286      28.970  27.840   4.930  1.00 18.94           N  
ANISOU  860  NE1 TRP A 286     2601   2282   2315    145     66    205       N  
ATOM    861  CE2 TRP A 286      27.635  27.656   5.177  1.00 22.73           C  
ANISOU  861  CE2 TRP A 286     3075   2776   2786    155     50    206       C  
ATOM    862  CE3 TRP A 286      26.176  27.419   7.095  1.00 18.99           C  
ANISOU  862  CE3 TRP A 286     2587   2307   2321    140     29    199       C  
ATOM    863  CZ2 TRP A 286      26.568  27.520   4.297  1.00 20.97           C  
ANISOU  863  CZ2 TRP A 286     2852   2572   2543    179     41    211       C  
ATOM    864  CZ3 TRP A 286      25.127  27.289   6.226  1.00 22.74           C  
ANISOU  864  CZ3 TRP A 286     3061   2799   2779    163     21    203       C  
ATOM    865  CH2 TRP A 286      25.326  27.331   4.839  1.00 24.44           C  
ANISOU  865  CH2 TRP A 286     3284   3023   2981    183     26    208       C  
ATOM    866  N   ASP A 287      29.468  29.329  11.436  1.00 18.63           N  
ANISOU  866  N   ASP A 287     2538   2207   2335     55     68    173       N  
ATOM    867  CA  ASP A 287      29.478  29.432  12.877  1.00 25.20           C  
ANISOU  867  CA  ASP A 287     3362   3040   3174     37     63    164       C  
ATOM    868  C   ASP A 287      28.357  30.313  13.421  1.00 29.08           C  
ANISOU  868  C   ASP A 287     3858   3529   3661     41     72    168       C  
ATOM    869  O   ASP A 287      27.609  29.923  14.330  1.00 24.39           O  
ANISOU  869  O   ASP A 287     3257   2944   3064     35     57    165       O  
ATOM    870  CB  ASP A 287      30.790  30.061  13.290  1.00 32.24           C  
ANISOU  870  CB  ASP A 287     4251   3919   4078     21     79    152       C  
ATOM    871  CG  ASP A 287      31.439  29.328  14.393  1.00 43.02           C  
ANISOU  871  CG  ASP A 287     5602   5294   5448      2     61    140       C  
ATOM    872  OD1 ASP A 287      31.133  29.640  15.567  1.00 57.37           O  
ANISOU  872  OD1 ASP A 287     7416   7116   7266     -9     59    133       O  
ATOM    873  OD2 ASP A 287      32.251  28.432  14.080  1.00 46.84           O  
ANISOU  873  OD2 ASP A 287     6079   5782   5935     -1     49    137       O  
ATOM    874  N   LYS A 288      28.257  31.523  12.884  1.00 20.56           N  
ANISOU  874  N   LYS A 288     2792   2436   2585     51     98    174       N  
ATOM    875  CA  LYS A 288      27.267  32.472  13.377  1.00 22.49           C  
ANISOU  875  CA  LYS A 288     3040   2675   2829     56    110    177       C  
ATOM    876  C   LYS A 288      25.857  32.058  12.977  1.00 20.69           C  
ANISOU  876  C   LYS A 288     2813   2459   2587     74     95    187       C  
ATOM    877  O   LYS A 288      24.915  32.244  13.736  1.00 24.60           O  
ANISOU  877  O   LYS A 288     3305   2958   3082     72     91    186       O  
ATOM    878  CB  LYS A 288      27.583  33.884  12.888  1.00 34.78           C  
ANISOU  878  CB  LYS A 288     4610   4210   4394     63    145    182       C  
ATOM    879  CG  LYS A 288      26.615  34.433  11.875  1.00 37.43           C  
ANISOU  879  CG  LYS A 288     4958   4543   4720     91    155    200       C  
ATOM    880  CD  LYS A 288      26.697  35.970  11.785  1.00 54.39           C  
ANISOU  880  CD  LYS A 288     7118   6667   6880     96    193    206       C  
ATOM    881  CE  LYS A 288      28.036  36.457  11.211  1.00 49.80           C  
ANISOU  881  CE  LYS A 288     6544   6068   6311     92    219    204       C  
ATOM    882  NZ  LYS A 288      29.161  36.344  12.185  1.00 46.97           N  
ANISOU  882  NZ  LYS A 288     6174   5706   5968     62    219    181       N  
ATOM    883  N   VAL A 289      25.711  31.483  11.790  1.00 17.61           N  
ANISOU  883  N   VAL A 289     2425   2077   2187     92     86    196       N  
ATOM    884  CA  VAL A 289      24.407  31.000  11.352  1.00 14.46           C  
ANISOU  884  CA  VAL A 289     2024   1694   1776    110     70    202       C  
ATOM    885  C   VAL A 289      23.891  29.892  12.263  1.00 19.17           C  
ANISOU  885  C   VAL A 289     2607   2304   2373     96     45    192       C  
ATOM    886  O   VAL A 289      22.735  29.914  12.690  1.00 17.88           O  
ANISOU  886  O   VAL A 289     2440   2147   2207    100     39    192       O  
ATOM    887  CB  VAL A 289      24.467  30.477   9.922  1.00 23.05           C  
ANISOU  887  CB  VAL A 289     3115   2792   2852    130     64    209       C  
ATOM    888  CG1 VAL A 289      23.327  29.519   9.665  1.00 17.93           C  
ANISOU  888  CG1 VAL A 289     2456   2164   2193    140     40    206       C  
ATOM    889  CG2 VAL A 289      24.422  31.644   8.933  1.00 25.46           C  
ANISOU  889  CG2 VAL A 289     3436   3087   3150    153     88    224       C  
ATOM    890  N   PHE A 290      24.737  28.907  12.550  1.00 16.23           N  
ANISOU  890  N   PHE A 290     2227   1936   2005     81     32    185       N  
ATOM    891  CA  PHE A 290      24.293  27.801  13.395  1.00 18.13           C  
ANISOU  891  CA  PHE A 290     2454   2186   2246     69     11    179       C  
ATOM    892  C   PHE A 290      24.160  28.161  14.869  1.00 14.45           C  
ANISOU  892  C   PHE A 290     1986   1718   1786     51     14    173       C  
ATOM    893  O   PHE A 290      23.314  27.619  15.562  1.00 15.73           O  
ANISOU  893  O   PHE A 290     2142   1887   1946     47      2    171       O  
ATOM    894  CB  PHE A 290      25.202  26.586  13.242  1.00 13.84           C  
ANISOU  894  CB  PHE A 290     1904   1649   1708     60     -3    174       C  
ATOM    895  CG  PHE A 290      24.848  25.730  12.077  1.00 16.73           C  
ANISOU  895  CG  PHE A 290     2265   2024   2068     75    -14    175       C  
ATOM    896  CD1 PHE A 290      23.719  24.940  12.110  1.00 15.73           C  
ANISOU  896  CD1 PHE A 290     2130   1909   1938     80    -29    172       C  
ATOM    897  CD2 PHE A 290      25.645  25.716  10.946  1.00 18.63           C  
ANISOU  897  CD2 PHE A 290     2509   2263   2306     83     -9    177       C  
ATOM    898  CE1 PHE A 290      23.395  24.134  11.026  1.00 21.06           C  
ANISOU  898  CE1 PHE A 290     2798   2595   2608     92    -39    169       C  
ATOM    899  CE2 PHE A 290      25.318  24.932   9.864  1.00 19.76           C  
ANISOU  899  CE2 PHE A 290     2648   2418   2442     96    -19    175       C  
ATOM    900  CZ  PHE A 290      24.205  24.129   9.909  1.00 19.85           C  
ANISOU  900  CZ  PHE A 290     2649   2442   2452    101    -35    170       C  
ATOM    901  N   THR A 291      25.018  29.045  15.352  1.00 12.77           N  
ANISOU  901  N   THR A 291     1779   1495   1580     40     29    170       N  
ATOM    902  CA  THR A 291      24.915  29.488  16.733  1.00 20.80           C  
ANISOU  902  CA  THR A 291     2793   2511   2600     24     33    162       C  
ATOM    903  C   THR A 291      23.580  30.208  16.969  1.00 25.78           C  
ANISOU  903  C   THR A 291     3427   3140   3229     31     41    165       C  
ATOM    904  O   THR A 291      22.890  29.939  17.948  1.00 21.96           O  
ANISOU  904  O   THR A 291     2938   2662   2743     22     34    161       O  
ATOM    905  CB  THR A 291      26.095  30.401  17.120  1.00 20.22           C  
ANISOU  905  CB  THR A 291     2721   2427   2535     11     51    154       C  
ATOM    906  OG1 THR A 291      27.295  29.625  17.116  1.00 23.69           O  
ANISOU  906  OG1 THR A 291     3154   2870   2977      2     41    149       O  
ATOM    907  CG2 THR A 291      25.891  31.015  18.512  1.00 21.60           C  
ANISOU  907  CG2 THR A 291     2892   2602   2712     -5     57    144       C  
ATOM    908  N   SER A 292      23.205  31.100  16.062  1.00 16.12           N  
ANISOU  908  N   SER A 292     2212   1908   2005     49     57    172       N  
ATOM    909  CA  SER A 292      21.939  31.813  16.202  1.00 23.00           C  
ANISOU  909  CA  SER A 292     3087   2778   2876     59     65    176       C  
ATOM    910  C   SER A 292      20.768  30.857  16.133  1.00 18.70           C  
ANISOU  910  C   SER A 292     2535   2248   2324     67     44    176       C  
ATOM    911  O   SER A 292      19.810  30.969  16.889  1.00 20.93           O  
ANISOU  911  O   SER A 292     2813   2532   2606     63     43    172       O  
ATOM    912  CB  SER A 292      21.786  32.858  15.091  1.00 26.59           C  
ANISOU  912  CB  SER A 292     3553   3221   3330     81     84    187       C  
ATOM    913  OG  SER A 292      22.869  33.752  15.122  1.00 34.11           O  
ANISOU  913  OG  SER A 292     4512   4157   4292     74    107    185       O  
ATOM    914  N   CYS A 293      20.858  29.913  15.211  1.00 16.36           N  
ANISOU  914  N   CYS A 293     2235   1960   2021     77     29    179       N  
ATOM    915  CA  CYS A 293      19.793  28.961  14.980  1.00 14.99           C  
ANISOU  915  CA  CYS A 293     2052   1801   1843     85     11    177       C  
ATOM    916  C   CYS A 293      19.568  28.024  16.178  1.00 19.80           C  
ANISOU  916  C   CYS A 293     2652   2416   2456     65     -2    169       C  
ATOM    917  O   CYS A 293      18.430  27.758  16.559  1.00 20.25           O  
ANISOU  917  O   CYS A 293     2703   2478   2513     66     -7    165       O  
ATOM    918  CB  CYS A 293      20.111  28.151  13.719  1.00 22.76           C  
ANISOU  918  CB  CYS A 293     3034   2794   2821     98      0    179       C  
ATOM    919  SG  CYS A 293      19.381  26.526  13.697  1.00 29.21           S  
ANISOU  919  SG  CYS A 293     3835   3626   3638     96    -24    170       S  
ATOM    920  N   PHE A 294      20.649  27.514  16.755  1.00 18.98           N  
ANISOU  920  N   PHE A 294     2547   2310   2355     48     -6    167       N  
ATOM    921  CA  PHE A 294      20.538  26.607  17.898  1.00 18.33           C  
ANISOU  921  CA  PHE A 294     2457   2232   2274     31    -16    163       C  
ATOM    922  C   PHE A 294      20.003  27.332  19.141  1.00 17.60           C  
ANISOU  922  C   PHE A 294     2366   2138   2182     20     -7    159       C  
ATOM    923  O   PHE A 294      19.177  26.784  19.883  1.00 17.67           O  
ANISOU  923  O   PHE A 294     2370   2152   2191     14    -13    157       O  
ATOM    924  CB  PHE A 294      21.893  25.943  18.200  1.00 15.22           C  
ANISOU  924  CB  PHE A 294     2061   1839   1883     19    -23    163       C  
ATOM    925  CG  PHE A 294      22.164  24.687  17.392  1.00 15.79           C  
ANISOU  925  CG  PHE A 294     2127   1915   1957     24    -37    165       C  
ATOM    926  CD1 PHE A 294      21.767  24.590  16.060  1.00 16.01           C  
ANISOU  926  CD1 PHE A 294     2154   1946   1983     42    -38    165       C  
ATOM    927  CD2 PHE A 294      22.840  23.611  17.963  1.00 15.58           C  
ANISOU  927  CD2 PHE A 294     2094   1891   1935     13    -48    165       C  
ATOM    928  CE1 PHE A 294      22.028  23.432  15.306  1.00 15.68           C  
ANISOU  928  CE1 PHE A 294     2104   1908   1944     46    -50    163       C  
ATOM    929  CE2 PHE A 294      23.116  22.456  17.221  1.00 17.22           C  
ANISOU  929  CE2 PHE A 294     2295   2101   2147     18    -58    166       C  
ATOM    930  CZ  PHE A 294      22.709  22.366  15.886  1.00 13.81           C  
ANISOU  930  CZ  PHE A 294     1861   1671   1714     33    -59    163       C  
ATOM    931  N   LEU A 295      20.471  28.562  19.329  1.00 17.43           N  
ANISOU  931  N   LEU A 295     2351   2108   2162     17      9    158       N  
ATOM    932  CA  LEU A 295      20.040  29.407  20.432  1.00 23.30           C  
ANISOU  932  CA  LEU A 295     3097   2849   2907      6     21    152       C  
ATOM    933  C   LEU A 295      18.574  29.803  20.278  1.00 22.19           C  
ANISOU  933  C   LEU A 295     2956   2707   2767     17     25    152       C  
ATOM    934  O   LEU A 295      17.840  29.859  21.257  1.00 23.14           O  
ANISOU  934  O   LEU A 295     3073   2830   2887      8     27    147       O  
ATOM    935  CB  LEU A 295      20.919  30.655  20.528  1.00 24.03           C  
ANISOU  935  CB  LEU A 295     3195   2931   3005      1     40    148       C  
ATOM    936  CG  LEU A 295      22.246  30.523  21.281  1.00 42.86           C  
ANISOU  936  CG  LEU A 295     5577   5318   5389    -17     38    141       C  
ATOM    937  CD1 LEU A 295      22.005  30.289  22.759  1.00 39.72           C  
ANISOU  937  CD1 LEU A 295     5175   4931   4986    -35     33    134       C  
ATOM    938  CD2 LEU A 295      23.119  29.420  20.694  1.00 44.08           C  
ANISOU  938  CD2 LEU A 295     5729   5478   5542    -15     22    146       C  
ATOM    939  N   THR A 296      18.152  30.071  19.046  1.00 17.32           N  
ANISOU  939  N   THR A 296     2341   2088   2150     39     27    158       N  
ATOM    940  CA  THR A 296      16.754  30.407  18.792  1.00 20.69           C  
ANISOU  940  CA  THR A 296     2767   2518   2578     53     29    158       C  
ATOM    941  C   THR A 296      15.860  29.230  19.189  1.00 17.84           C  
ANISOU  941  C   THR A 296     2394   2167   2216     49     13    152       C  
ATOM    942  O   THR A 296      14.880  29.394  19.897  1.00 18.38           O  
ANISOU  942  O   THR A 296     2460   2236   2288     44     16    146       O  
ATOM    943  CB  THR A 296      16.519  30.793  17.324  1.00 20.62           C  
ANISOU  943  CB  THR A 296     2761   2508   2566     80     31    167       C  
ATOM    944  OG1 THR A 296      17.268  31.976  17.034  1.00 21.81           O  
ANISOU  944  OG1 THR A 296     2922   2645   2719     84     51    173       O  
ATOM    945  CG2 THR A 296      15.040  31.077  17.058  1.00 23.14           C  
ANISOU  945  CG2 THR A 296     3075   2832   2884     97     30    165       C  
ATOM    946  N   VAL A 297      16.216  28.036  18.745  1.00 16.21           N  
ANISOU  946  N   VAL A 297     2183   1968   2008     49     -2    153       N  
ATOM    947  CA  VAL A 297      15.418  26.868  19.098  1.00 20.72           C  
ANISOU  947  CA  VAL A 297     2743   2547   2581     44    -14    146       C  
ATOM    948  C   VAL A 297      15.368  26.684  20.617  1.00 16.18           C  
ANISOU  948  C   VAL A 297     2169   1970   2008     22    -11    143       C  
ATOM    949  O   VAL A 297      14.308  26.385  21.189  1.00 14.29           O  
ANISOU  949  O   VAL A 297     1924   1733   1772     18    -10    137       O  
ATOM    950  CB  VAL A 297      15.944  25.587  18.409  1.00 22.04           C  
ANISOU  950  CB  VAL A 297     2906   2721   2750     46    -28    147       C  
ATOM    951  CG1 VAL A 297      15.247  24.350  18.987  1.00 18.47           C  
ANISOU  951  CG1 VAL A 297     2442   2271   2303     36    -36    140       C  
ATOM    952  CG2 VAL A 297      15.732  25.686  16.908  1.00 18.22           C  
ANISOU  952  CG2 VAL A 297     2419   2242   2261     69    -33    147       C  
ATOM    953  N   ASP A 298      16.517  26.893  21.262  1.00 17.99           N  
ANISOU  953  N   ASP A 298     2405   2197   2235      8     -8    147       N  
ATOM    954  CA  ASP A 298      16.638  26.747  22.710  1.00 21.44           C  
ANISOU  954  CA  ASP A 298     2842   2635   2668    -11     -5    145       C  
ATOM    955  C   ASP A 298      15.806  27.772  23.499  1.00 19.47           C  
ANISOU  955  C   ASP A 298     2595   2383   2420    -17      9    138       C  
ATOM    956  O   ASP A 298      15.196  27.433  24.513  1.00 20.85           O  
ANISOU  956  O   ASP A 298     2768   2561   2593    -28     10    135       O  
ATOM    957  CB  ASP A 298      18.101  26.818  23.132  1.00 19.53           C  
ANISOU  957  CB  ASP A 298     2604   2394   2422    -22     -6    147       C  
ATOM    958  CG  ASP A 298      18.292  26.635  24.644  1.00 23.09           C  
ANISOU  958  CG  ASP A 298     3056   2852   2866    -40     -6    145       C  
ATOM    959  OD1 ASP A 298      18.202  25.488  25.140  1.00 24.04           O  
ANISOU  959  OD1 ASP A 298     3173   2977   2983    -45    -15    150       O  
ATOM    960  OD2 ASP A 298      18.563  27.636  25.336  1.00 30.62           O  
ANISOU  960  OD2 ASP A 298     4012   3805   3816    -50      5    139       O  
ATOM    961  N   GLY A 299      15.801  29.020  23.046  1.00 15.85           N  
ANISOU  961  N   GLY A 299     2140   1917   1963     -9     21    137       N  
ATOM    962  CA  GLY A 299      15.019  30.054  23.711  1.00 13.33           C  
ANISOU  962  CA  GLY A 299     1823   1594   1649    -13     36    130       C  
ATOM    963  C   GLY A 299      13.531  29.805  23.520  1.00 14.96           C  
ANISOU  963  C   GLY A 299     2023   1801   1859     -3     34    127       C  
ATOM    964  O   GLY A 299      12.739  30.059  24.416  1.00 13.89           O  
ANISOU  964  O   GLY A 299     1886   1666   1727    -13     41    119       O  
ATOM    965  N   GLU A 300      13.147  29.306  22.349  1.00 15.82           N  
ANISOU  965  N   GLU A 300     2128   1914   1970     15     24    130       N  
ATOM    966  CA  GLU A 300      11.748  28.955  22.098  1.00 16.93           C  
ANISOU  966  CA  GLU A 300     2259   2059   2116     25     20    123       C  
ATOM    967  C   GLU A 300      11.283  27.858  23.059  1.00 20.60           C  
ANISOU  967  C   GLU A 300     2717   2527   2581      8     15    117       C  
ATOM    968  O   GLU A 300      10.197  27.932  23.632  1.00 16.50           O  
ANISOU  968  O   GLU A 300     2194   2008   2068      4     21    109       O  
ATOM    969  CB  GLU A 300      11.558  28.495  20.638  1.00 15.26           C  
ANISOU  969  CB  GLU A 300     2042   1854   1903     47      8    125       C  
ATOM    970  CG  GLU A 300      11.574  29.634  19.607  1.00 18.35           C  
ANISOU  970  CG  GLU A 300     2438   2242   2292     70     14    132       C  
ATOM    971  CD  GLU A 300      11.650  29.175  18.156  1.00 22.42           C  
ANISOU  971  CD  GLU A 300     2950   2767   2802     92      2    136       C  
ATOM    972  OE1 GLU A 300      11.816  30.052  17.275  1.00 28.14           O  
ANISOU  972  OE1 GLU A 300     3681   3489   3522    112      8    144       O  
ATOM    973  OE2 GLU A 300      11.563  27.950  17.886  1.00 25.08           O  
ANISOU  973  OE2 GLU A 300     3278   3113   3139     90    -12    130       O  
ATOM    974  N   ILE A 301      12.118  26.835  23.214  1.00 13.03           N  
ANISOU  974  N   ILE A 301     1759   1571   1619     -1      6    122       N  
ATOM    975  CA  ILE A 301      11.840  25.714  24.112  1.00 18.19           C  
ANISOU  975  CA  ILE A 301     2409   2227   2274    -16      3    121       C  
ATOM    976  C   ILE A 301      11.668  26.155  25.574  1.00 20.62           C  
ANISOU  976  C   ILE A 301     2723   2534   2578    -34     15    118       C  
ATOM    977  O   ILE A 301      10.834  25.639  26.320  1.00 17.44           O  
ANISOU  977  O   ILE A 301     2317   2132   2179    -43     19    114       O  
ATOM    978  CB  ILE A 301      12.985  24.704  24.020  1.00 19.78           C  
ANISOU  978  CB  ILE A 301     2613   2431   2473    -20     -7    130       C  
ATOM    979  CG1 ILE A 301      12.872  23.946  22.693  1.00 15.74           C  
ANISOU  979  CG1 ILE A 301     2092   1921   1967     -5    -18    128       C  
ATOM    980  CG2 ILE A 301      12.987  23.785  25.237  1.00 11.14           C  
ANISOU  980  CG2 ILE A 301     1519   1337   1376    -37     -5    133       C  
ATOM    981  CD1 ILE A 301      14.089  23.088  22.347  1.00 15.74           C  
ANISOU  981  CD1 ILE A 301     2094   1922   1965     -6    -27    136       C  
ATOM    982  N   GLU A 302      12.465  27.135  25.965  1.00 20.73           N  
ANISOU  982  N   GLU A 302     2744   2547   2585    -39     21    120       N  
ATOM    983  CA  GLU A 302      12.477  27.626  27.336  1.00 23.48           C  
ANISOU  983  CA  GLU A 302     3097   2897   2926    -57     32    116       C  
ATOM    984  C   GLU A 302      11.338  28.613  27.598  1.00 24.07           C  
ANISOU  984  C   GLU A 302     3170   2967   3008    -57     46    106       C  
ATOM    985  O   GLU A 302      11.078  28.982  28.738  1.00 29.94           O  
ANISOU  985  O   GLU A 302     3916   3712   3748    -72     56    100       O  
ATOM    986  CB  GLU A 302      13.829  28.279  27.620  1.00 25.46           C  
ANISOU  986  CB  GLU A 302     3354   3150   3169    -64     34    119       C  
ATOM    987  CG  GLU A 302      13.957  28.931  28.988  1.00 42.18           C  
ANISOU  987  CG  GLU A 302     5475   5272   5278    -82     45    111       C  
ATOM    988  CD  GLU A 302      15.408  29.270  29.318  1.00 47.64           C  
ANISOU  988  CD  GLU A 302     6169   5970   5961    -90     43    111       C  
ATOM    989  OE1 GLU A 302      15.745  29.418  30.519  1.00 52.91           O  
ANISOU  989  OE1 GLU A 302     6838   6648   6617   -105     46    105       O  
ATOM    990  OE2 GLU A 302      16.207  29.384  28.363  1.00 41.90           O  
ANISOU  990  OE2 GLU A 302     5443   5239   5238    -80     38    115       O  
ATOM    991  N   GLY A 303      10.654  29.023  26.537  1.00 20.92           N  
ANISOU  991  N   GLY A 303     2767   2564   2620    -39     46    104       N  
ATOM    992  CA  GLY A 303       9.589  29.998  26.637  1.00 21.87           C  
ANISOU  992  CA  GLY A 303     2883   2677   2748    -34     59     95       C  
ATOM    993  C   GLY A 303      10.085  31.439  26.742  1.00 25.97           C  
ANISOU  993  C   GLY A 303     3409   3190   3268    -35     73     94       C  
ATOM    994  O   GLY A 303       9.373  32.282  27.254  1.00 22.53           O  
ANISOU  994  O   GLY A 303     2972   2749   2840    -39     87     85       O  
ATOM    995  N   LYS A 304      11.296  31.721  26.257  1.00 18.67           N  
ANISOU  995  N   LYS A 304     2491   2264   2340    -32     71    101       N  
ATOM    996  CA  LYS A 304      11.850  33.077  26.287  1.00 25.68           C  
ANISOU  996  CA  LYS A 304     3384   3142   3232    -33     88     99       C  
ATOM    997  C   LYS A 304      11.721  33.795  24.940  1.00 23.60           C  
ANISOU  997  C   LYS A 304     3121   2869   2975     -8     92    107       C  
ATOM    998  O   LYS A 304      11.869  35.020  24.857  1.00 31.74           O  
ANISOU  998  O   LYS A 304     4156   3888   4014     -4    111    106       O  
ATOM    999  CB  LYS A 304      13.330  33.034  26.678  1.00 25.93           C  
ANISOU  999  CB  LYS A 304     3419   3176   3255    -46     87    100       C  
ATOM   1000  CG  LYS A 304      13.623  32.133  27.864  1.00 35.46           C  
ANISOU 1000  CG  LYS A 304     4626   4397   4451    -66     78     97       C  
ATOM   1001  CD  LYS A 304      13.524  32.860  29.191  1.00 38.08           C  
ANISOU 1001  CD  LYS A 304     4957   4731   4779    -86     93     83       C  
ATOM   1002  CE  LYS A 304      14.921  33.076  29.784  1.00 57.08           C  
ANISOU 1002  CE  LYS A 304     7365   7145   7177   -100     93     78       C  
ATOM   1003  NZ  LYS A 304      15.900  33.621  28.782  1.00 55.86           N  
ANISOU 1003  NZ  LYS A 304     7213   6982   7030    -90     96     82       N  
ATOM   1004  N   ILE A 305      11.461  33.031  23.884  1.00 15.33           N  
ANISOU 1004  N   ILE A 305     2071   1827   1926     10     77    114       N  
ATOM   1005  CA  ILE A 305      11.374  33.595  22.548  1.00 15.08           C  
ANISOU 1005  CA  ILE A 305     2043   1791   1898     37     79    123       C  
ATOM   1006  C   ILE A 305      10.005  33.243  21.997  1.00 16.84           C  
ANISOU 1006  C   ILE A 305     2255   2020   2122     54     70    121       C  
ATOM   1007  O   ILE A 305       9.534  32.102  22.154  1.00 16.69           O  
ANISOU 1007  O   ILE A 305     2228   2011   2101     49     55    115       O  
ATOM   1008  CB  ILE A 305      12.500  33.019  21.638  1.00 16.03           C  
ANISOU 1008  CB  ILE A 305     2167   1914   2010     43     68    133       C  
ATOM   1009  CG1 ILE A 305      13.868  33.452  22.170  1.00 20.35           C  
ANISOU 1009  CG1 ILE A 305     2721   2454   2556     26     78    133       C  
ATOM   1010  CG2 ILE A 305      12.333  33.457  20.164  1.00 14.25           C  
ANISOU 1010  CG2 ILE A 305     1945   1687   1784     73     68    144       C  
ATOM   1011  CD1 ILE A 305      15.049  32.865  21.392  1.00 24.42           C  
ANISOU 1011  CD1 ILE A 305     3241   2973   3066     30     68    141       C  
ATOM   1012  N   GLY A 306       9.349  34.211  21.367  1.00 21.30           N  
ANISOU 1012  N   GLY A 306     2821   2579   2693     76     79    124       N  
ATOM   1013  CA  GLY A 306       8.018  33.971  20.821  1.00 20.49           C  
ANISOU 1013  CA  GLY A 306     2708   2486   2593     95     70    120       C  
ATOM   1014  C   GLY A 306       8.067  32.962  19.681  1.00 27.43           C  
ANISOU 1014  C   GLY A 306     3581   3379   3462    112     49    123       C  
ATOM   1015  O   GLY A 306       8.926  33.045  18.802  1.00 27.47           O  
ANISOU 1015  O   GLY A 306     3594   3384   3460    123     47    135       O  
ATOM   1016  N   ARG A 307       7.162  31.991  19.693  1.00 21.48           N  
ANISOU 1016  N   ARG A 307     2813   2637   2710    112     35    111       N  
ATOM   1017  CA  ARG A 307       7.193  30.963  18.666  1.00 23.38           C  
ANISOU 1017  CA  ARG A 307     3047   2893   2944    125     16    110       C  
ATOM   1018  C   ARG A 307       5.846  30.768  17.970  1.00 31.96           C  
ANISOU 1018  C   ARG A 307     4116   3993   4032    147      6     98       C  
ATOM   1019  O   ARG A 307       4.790  30.802  18.595  1.00 27.29           O  
ANISOU 1019  O   ARG A 307     3516   3403   3452    142      9     85       O  
ATOM   1020  CB  ARG A 307       7.708  29.638  19.237  1.00 24.23           C  
ANISOU 1020  CB  ARG A 307     3151   3003   3052    101      7    104       C  
ATOM   1021  CG  ARG A 307       6.846  29.075  20.337  1.00 26.32           C  
ANISOU 1021  CG  ARG A 307     3408   3267   3326     82     10     90       C  
ATOM   1022  CD  ARG A 307       7.519  27.885  21.007  1.00 23.59           C  
ANISOU 1022  CD  ARG A 307     3063   2921   2980     59      5     90       C  
ATOM   1023  NE  ARG A 307       6.798  27.457  22.197  1.00 19.00           N  
ANISOU 1023  NE  ARG A 307     2477   2336   2406     39     12     80       N  
ATOM   1024  CZ  ARG A 307       5.785  26.598  22.190  1.00 28.16           C  
ANISOU 1024  CZ  ARG A 307     3622   3501   3576     39      8     65       C  
ATOM   1025  NH1 ARG A 307       5.365  26.071  21.045  1.00 22.28           N  
ANISOU 1025  NH1 ARG A 307     2865   2767   2834     57     -4     57       N  
ATOM   1026  NH2 ARG A 307       5.194  26.264  23.330  1.00 25.01           N  
ANISOU 1026  NH2 ARG A 307     3221   3096   3184     20     18     58       N  
ATOM   1027  N   ALA A 308       5.909  30.570  16.661  1.00 34.47           N  
ANISOU 1027  N   ALA A 308     4432   4325   4341    172     -7    102       N  
ATOM   1028  CA  ALA A 308       4.730  30.299  15.859  1.00 38.73           C  
ANISOU 1028  CA  ALA A 308     4953   4883   4879    196    -20     89       C  
ATOM   1029  C   ALA A 308       4.265  28.868  16.073  1.00 36.84           C  
ANISOU 1029  C   ALA A 308     4697   4654   4647    181    -32     68       C  
ATOM   1030  O   ALA A 308       5.075  27.964  16.285  1.00 33.46           O  
ANISOU 1030  O   ALA A 308     4271   4223   4218    162    -36     68       O  
ATOM   1031  CB  ALA A 308       5.039  30.540  14.376  1.00 40.00           C  
ANISOU 1031  CB  ALA A 308     5117   5059   5024    228    -29    100       C  
ATOM   1032  N   VAL A 309       2.955  28.670  16.012  1.00 35.07           N  
ANISOU 1032  N   VAL A 309     4453   4441   4431    189    -38     48       N  
ATOM   1033  CA  VAL A 309       2.357  27.339  16.081  1.00 33.68           C  
ANISOU 1033  CA  VAL A 309     4257   4275   4265    178    -48     25       C  
ATOM   1034  C   VAL A 309       1.766  26.982  14.712  1.00 37.96           C  
ANISOU 1034  C   VAL A 309     4781   4843   4799    207    -66     11       C  
ATOM   1035  O   VAL A 309       1.097  27.811  14.083  1.00 30.75           O  
ANISOU 1035  O   VAL A 309     3862   3941   3879    235    -70     11       O  
ATOM   1036  CB  VAL A 309       1.231  27.307  17.141  1.00 44.53           C  
ANISOU 1036  CB  VAL A 309     5621   5642   5657    163    -39      8       C  
ATOM   1037  CG1 VAL A 309       0.479  25.978  17.100  1.00 44.67           C  
ANISOU 1037  CG1 VAL A 309     5615   5669   5687    155    -46    -20       C  
ATOM   1038  CG2 VAL A 309       1.798  27.596  18.538  1.00 36.51           C  
ANISOU 1038  CG2 VAL A 309     4622   4603   4645    134    -21     19       C  
ATOM   1039  N   VAL A 310       2.006  25.764  14.234  1.00 32.00           N  
ANISOU 1039  N   VAL A 310     4015   4098   4044    202    -77     -2       N  
ATOM   1040  CA  VAL A 310       1.422  25.355  12.956  1.00 34.02           C  
ANISOU 1040  CA  VAL A 310     4250   4382   4293    228    -94    -20       C  
ATOM   1041  C   VAL A 310      -0.101  25.553  12.975  1.00 32.91           C  
ANISOU 1041  C   VAL A 310     4088   4255   4163    240    -98    -44       C  
ATOM   1042  O   VAL A 310      -0.774  25.180  13.937  1.00 29.26           O  
ANISOU 1042  O   VAL A 310     3616   3782   3721    219    -90    -59       O  
ATOM   1043  CB  VAL A 310       1.773  23.889  12.586  1.00 46.85           C  
ANISOU 1043  CB  VAL A 310     5863   6014   5923    215   -103    -37       C  
ATOM   1044  CG1 VAL A 310       1.649  22.977  13.802  1.00 49.70           C  
ANISOU 1044  CG1 VAL A 310     6220   6356   6307    180    -91    -47       C  
ATOM   1045  CG2 VAL A 310       0.874  23.393  11.445  1.00 44.09           C  
ANISOU 1045  CG2 VAL A 310     5485   5696   5570    238   -120    -65       C  
ATOM   1046  N   GLY A 311      -0.625  26.174  11.926  1.00 27.91           N  
ANISOU 1046  N   GLY A 311     3445   3644   3514    276   -111    -45       N  
ATOM   1047  CA  GLY A 311      -2.055  26.383  11.798  1.00 30.20           C  
ANISOU 1047  CA  GLY A 311     3712   3950   3812    293   -117    -69       C  
ATOM   1048  C   GLY A 311      -2.578  27.677  12.400  1.00 35.74           C  
ANISOU 1048  C   GLY A 311     4422   4639   4517    302   -106    -55       C  
ATOM   1049  O   GLY A 311      -3.674  28.132  12.052  1.00 34.75           O  
ANISOU 1049  O   GLY A 311     4280   4530   4393    326   -113    -69       O  
ATOM   1050  N   SER A 312      -1.805  28.255  13.310  1.00 32.44           N  
ANISOU 1050  N   SER A 312     4031   4193   4103    282    -88    -31       N  
ATOM   1051  CA  SER A 312      -2.244  29.431  14.040  1.00 37.61           C  
ANISOU 1051  CA  SER A 312     4694   4832   4766    283    -73    -21       C  
ATOM   1052  C   SER A 312      -1.581  30.705  13.537  1.00 39.36           C  
ANISOU 1052  C   SER A 312     4937   5047   4971    307    -67     12       C  
ATOM   1053  O   SER A 312      -0.410  30.708  13.166  1.00 35.94           O  
ANISOU 1053  O   SER A 312     4522   4609   4524    306    -65     32       O  
ATOM   1054  CB  SER A 312      -1.972  29.258  15.533  1.00 25.69           C  
ANISOU 1054  CB  SER A 312     3194   3294   3273    243    -54    -20       C  
ATOM   1055  OG  SER A 312      -2.081  30.491  16.214  1.00 26.23           O  
ANISOU 1055  OG  SER A 312     3276   3345   3346    243    -37     -6       O  
ATOM   1056  N   SER A 313      -2.348  31.788  13.533  1.00 43.93           N  
ANISOU 1056  N   SER A 313     5514   5625   5553    329    -61     16       N  
ATOM   1057  CA  SER A 313      -1.829  33.092  13.150  1.00 46.81           C  
ANISOU 1057  CA  SER A 313     5900   5979   5906    351    -50     48       C  
ATOM   1058  C   SER A 313      -1.094  33.742  14.319  1.00 44.78           C  
ANISOU 1058  C   SER A 313     5664   5689   5661    322    -25     63       C  
ATOM   1059  O   SER A 313      -0.360  34.712  14.137  1.00 47.38           O  
ANISOU 1059  O   SER A 313     6014   6003   5984    332    -11     89       O  
ATOM   1060  CB  SER A 313      -2.977  33.984  12.687  1.00 44.58           C  
ANISOU 1060  CB  SER A 313     5605   5708   5624    388    -53     47       C  
ATOM   1061  OG  SER A 313      -3.651  33.404  11.583  1.00 43.91           O  
ANISOU 1061  OG  SER A 313     5498   5659   5526    417    -78     30       O  
ATOM   1062  N   ASP A 314      -1.271  33.178  15.509  1.00 34.57           N  
ANISOU 1062  N   ASP A 314     4366   4384   4384    286    -19     46       N  
ATOM   1063  CA  ASP A 314      -0.776  33.791  16.742  1.00 37.77           C  
ANISOU 1063  CA  ASP A 314     4788   4762   4801    258      4     55       C  
ATOM   1064  C   ASP A 314       0.494  33.141  17.307  1.00 39.97           C  
ANISOU 1064  C   ASP A 314     5082   5030   5076    226      8     62       C  
ATOM   1065  O   ASP A 314       0.589  31.915  17.390  1.00 31.17           O  
ANISOU 1065  O   ASP A 314     3959   3924   3961    210     -3     49       O  
ATOM   1066  CB  ASP A 314      -1.883  33.774  17.795  1.00 39.22           C  
ANISOU 1066  CB  ASP A 314     4958   4939   5005    241     12     34       C  
ATOM   1067  CG  ASP A 314      -3.123  34.539  17.350  1.00 50.48           C  
ANISOU 1067  CG  ASP A 314     6370   6374   6438    272     10     27       C  
ATOM   1068  OD1 ASP A 314      -2.969  35.555  16.636  1.00 45.77           O  
ANISOU 1068  OD1 ASP A 314     5782   5777   5834    302     13     48       O  
ATOM   1069  OD2 ASP A 314      -4.248  34.124  17.708  1.00 61.76           O  
ANISOU 1069  OD2 ASP A 314     7777   7810   7880    268      5      2       O  
ATOM   1070  N   LYS A 315       1.462  33.974  17.696  1.00 28.60           N  
ANISOU 1070  N   LYS A 315     3662   3571   3635    217     25     81       N  
ATOM   1071  CA  LYS A 315       2.675  33.515  18.366  1.00 24.39           C  
ANISOU 1071  CA  LYS A 315     3142   3027   3098    187     31     86       C  
ATOM   1072  C   LYS A 315       2.474  33.394  19.870  1.00 28.24           C  
ANISOU 1072  C   LYS A 315     3629   3503   3599    153     43     74       C  
ATOM   1073  O   LYS A 315       1.731  34.168  20.476  1.00 30.21           O  
ANISOU 1073  O   LYS A 315     3875   3743   3859    151     56     69       O  
ATOM   1074  CB  LYS A 315       3.845  34.462  18.089  1.00 27.59           C  
ANISOU 1074  CB  LYS A 315     3568   3418   3498    192     44    109       C  
ATOM   1075  CG  LYS A 315       4.395  34.393  16.663  1.00 30.51           C  
ANISOU 1075  CG  LYS A 315     3942   3799   3851    219     34    123       C  
ATOM   1076  CD  LYS A 315       5.592  35.314  16.509  1.00 28.87           C  
ANISOU 1076  CD  LYS A 315     3755   3574   3641    220     52    144       C  
ATOM   1077  CE  LYS A 315       5.883  35.603  15.045  1.00 49.49           C  
ANISOU 1077  CE  LYS A 315     6373   6194   6237    255     47    161       C  
ATOM   1078  NZ  LYS A 315       6.167  34.365  14.285  1.00 46.72           N  
ANISOU 1078  NZ  LYS A 315     6015   5863   5872    258     24    156       N  
ATOM   1079  N   VAL A 316       3.150  32.422  20.472  1.00 24.53           N  
ANISOU 1079  N   VAL A 316     3163   3032   3126    127     39     72       N  
ATOM   1080  CA  VAL A 316       3.037  32.199  21.900  1.00 26.00           C  
ANISOU 1080  CA  VAL A 316     3350   3210   3320     96     50     62       C  
ATOM   1081  C   VAL A 316       4.397  32.257  22.570  1.00 24.11           C  
ANISOU 1081  C   VAL A 316     3126   2961   3072     74     57     73       C  
ATOM   1082  O   VAL A 316       5.418  31.905  21.976  1.00 23.90           O  
ANISOU 1082  O   VAL A 316     3107   2938   3037     77     49     84       O  
ATOM   1083  CB  VAL A 316       2.405  30.823  22.206  1.00 28.89           C  
ANISOU 1083  CB  VAL A 316     3702   3585   3690     83     40     46       C  
ATOM   1084  CG1 VAL A 316       1.015  30.717  21.585  1.00 30.45           C  
ANISOU 1084  CG1 VAL A 316     3881   3793   3897    103     32     30       C  
ATOM   1085  CG2 VAL A 316       3.324  29.707  21.717  1.00 21.60           C  
ANISOU 1085  CG2 VAL A 316     2781   2668   2757     80     26     52       C  
ATOM   1086  N   LEU A 317       4.386  32.692  23.819  1.00 23.52           N  
ANISOU 1086  N   LEU A 317     3057   2877   3003     51     72     68       N  
ATOM   1087  CA  LEU A 317       5.547  32.671  24.670  1.00 26.22           C  
ANISOU 1087  CA  LEU A 317     3411   3215   3338     28     79     74       C  
ATOM   1088  C   LEU A 317       5.318  31.619  25.752  1.00 31.79           C  
ANISOU 1088  C   LEU A 317     4113   3925   4042      4     77     65       C  
ATOM   1089  O   LEU A 317       4.667  31.885  26.760  1.00 31.70           O  
ANISOU 1089  O   LEU A 317     4099   3910   4035    -11     89     55       O  
ATOM   1090  CB  LEU A 317       5.735  34.040  25.292  1.00 22.33           C  
ANISOU 1090  CB  LEU A 317     2925   2709   2849     21    100     74       C  
ATOM   1091  CG  LEU A 317       7.096  34.417  25.850  1.00 30.03           C  
ANISOU 1091  CG  LEU A 317     3912   3680   3817      4    108     79       C  
ATOM   1092  CD1 LEU A 317       8.194  34.366  24.769  1.00 20.37           C  
ANISOU 1092  CD1 LEU A 317     2695   2457   2588     18    100     93       C  
ATOM   1093  CD2 LEU A 317       6.974  35.817  26.489  1.00 28.41           C  
ANISOU 1093  CD2 LEU A 317     3709   3462   3622     -3    131     73       C  
ATOM   1094  N   GLU A 318       5.855  30.423  25.543  1.00 29.09           N  
ANISOU 1094  N   GLU A 318     3771   3590   3693      0     63     70       N  
ATOM   1095  CA  GLU A 318       5.564  29.301  26.431  1.00 27.08           C  
ANISOU 1095  CA  GLU A 318     3513   3338   3437    -19     62     64       C  
ATOM   1096  C   GLU A 318       6.537  28.135  26.261  1.00 26.01           C  
ANISOU 1096  C   GLU A 318     3381   3207   3294    -24     50     74       C  
ATOM   1097  O   GLU A 318       6.805  27.691  25.141  1.00 23.25           O  
ANISOU 1097  O   GLU A 318     3028   2862   2945     -8     37     78       O  
ATOM   1098  CB  GLU A 318       4.141  28.817  26.177  1.00 29.13           C  
ANISOU 1098  CB  GLU A 318     3758   3600   3711    -12     61     50       C  
ATOM   1099  CG  GLU A 318       3.664  27.756  27.139  1.00 45.69           C  
ANISOU 1099  CG  GLU A 318     5852   5697   5812    -31     65     42       C  
ATOM   1100  CD  GLU A 318       2.209  27.403  26.915  1.00 66.14           C  
ANISOU 1100  CD  GLU A 318     8425   8287   8417    -26     67     24       C  
ATOM   1101  OE1 GLU A 318       1.559  26.915  27.867  1.00 77.44           O  
ANISOU 1101  OE1 GLU A 318     9854   9715   9855    -43     78     15       O  
ATOM   1102  OE2 GLU A 318       1.717  27.614  25.782  1.00 67.93           O  
ANISOU 1102  OE2 GLU A 318     8641   8520   8651     -3     57     18       O  
ATOM   1103  N   ALA A 319       7.033  27.623  27.382  1.00 25.81           N  
ANISOU 1103  N   ALA A 319     3363   3182   3261    -44     54     78       N  
ATOM   1104  CA  ALA A 319       7.965  26.494  27.373  1.00 25.94           C  
ANISOU 1104  CA  ALA A 319     3383   3202   3271    -49     43     88       C  
ATOM   1105  C   ALA A 319       7.402  25.280  26.621  1.00 20.97           C  
ANISOU 1105  C   ALA A 319     2742   2574   2652    -41     34     84       C  
ATOM   1106  O   ALA A 319       6.244  24.911  26.791  1.00 18.72           O  
ANISOU 1106  O   ALA A 319     2448   2287   2378    -43     40     72       O  
ATOM   1107  CB  ALA A 319       8.340  26.122  28.800  1.00 22.17           C  
ANISOU 1107  CB  ALA A 319     2913   2727   2783    -70     50     93       C  
ATOM   1108  N   VAL A 320       8.209  24.643  25.778  1.00 17.64           N  
ANISOU 1108  N   VAL A 320     2319   2154   2227    -33     22     92       N  
ATOM   1109  CA  VAL A 320       7.702  23.443  25.119  1.00 18.52           C  
ANISOU 1109  CA  VAL A 320     2419   2267   2351    -27     15     85       C  
ATOM   1110  C   VAL A 320       7.906  22.189  25.993  1.00 20.07           C  
ANISOU 1110  C   VAL A 320     2617   2459   2549    -43     19     90       C  
ATOM   1111  O   VAL A 320       7.305  21.151  25.750  1.00 21.49           O  
ANISOU 1111  O   VAL A 320     2786   2636   2742    -43     20     83       O  
ATOM   1112  CB  VAL A 320       8.291  23.207  23.693  1.00 25.02           C  
ANISOU 1112  CB  VAL A 320     3238   3096   3174    -10      1     87       C  
ATOM   1113  CG1 VAL A 320       8.723  24.515  23.005  1.00 16.72           C  
ANISOU 1113  CG1 VAL A 320     2193   2047   2114      5     -2     92       C  
ATOM   1114  CG2 VAL A 320       9.395  22.210  23.733  1.00 18.64           C  
ANISOU 1114  CG2 VAL A 320     2434   2286   2362    -16     -6     98       C  
ATOM   1115  N   ALA A 321       8.749  22.287  27.012  1.00 18.02           N  
ANISOU 1115  N   ALA A 321     2371   2199   2277    -56     23    104       N  
ATOM   1116  CA  ALA A 321       9.062  21.125  27.836  1.00 20.62           C  
ANISOU 1116  CA  ALA A 321     2704   2525   2605    -68     26    113       C  
ATOM   1117  C   ALA A 321       9.555  21.565  29.198  1.00 14.42           C  
ANISOU 1117  C   ALA A 321     1932   1744   1803    -82     34    123       C  
ATOM   1118  O   ALA A 321       9.917  22.717  29.382  1.00 18.25           O  
ANISOU 1118  O   ALA A 321     2423   2234   2278    -83     34    122       O  
ATOM   1119  CB  ALA A 321      10.098  20.224  27.160  1.00 14.51           C  
ANISOU 1119  CB  ALA A 321     1929   1751   1832    -62     14    124       C  
ATOM   1120  N   SER A 322       9.565  20.638  30.151  1.00 25.33           N  
ANISOU 1120  N   SER A 322     3319   3123   3182    -92     41    132       N  
ATOM   1121  CA  SER A 322       9.942  20.974  31.511  1.00 22.43           C  
ANISOU 1121  CA  SER A 322     2963   2763   2795   -104     48    141       C  
ATOM   1122  C   SER A 322      11.461  21.117  31.579  1.00 24.75           C  
ANISOU 1122  C   SER A 322     3264   3066   3073   -103     35    154       C  
ATOM   1123  O   SER A 322      12.170  20.717  30.656  1.00 18.57           O  
ANISOU 1123  O   SER A 322     2478   2281   2295    -93     23    159       O  
ATOM   1124  CB  SER A 322       9.401  19.938  32.517  1.00 27.69           C  
ANISOU 1124  CB  SER A 322     3633   3424   3462   -114     62    148       C  
ATOM   1125  OG  SER A 322      10.202  18.762  32.517  1.00 29.24           O  
ANISOU 1125  OG  SER A 322     3833   3618   3657   -111     56    166       O  
ATOM   1126  N   GLU A 323      11.942  21.697  32.673  1.00 18.89           N  
ANISOU 1126  N   GLU A 323     2531   2334   2311   -112     38    157       N  
ATOM   1127  CA  GLU A 323      13.328  22.106  32.804  1.00 17.56           C  
ANISOU 1127  CA  GLU A 323     2366   2177   2127   -111     27    163       C  
ATOM   1128  C   GLU A 323      14.336  20.971  32.759  1.00 16.95           C  
ANISOU 1128  C   GLU A 323     2291   2102   2046   -106     16    181       C  
ATOM   1129  O   GLU A 323      15.527  21.226  32.600  1.00 16.10           O  
ANISOU 1129  O   GLU A 323     2184   2003   1930   -103      4    184       O  
ATOM   1130  CB  GLU A 323      13.531  22.899  34.109  1.00 15.85           C  
ANISOU 1130  CB  GLU A 323     2158   1976   1891   -124     34    160       C  
ATOM   1131  CG  GLU A 323      13.259  22.094  35.371  1.00 20.82           C  
ANISOU 1131  CG  GLU A 323     2794   2610   2505   -131     41    171       C  
ATOM   1132  CD  GLU A 323      13.889  22.709  36.631  1.00 36.50           C  
ANISOU 1132  CD  GLU A 323     4787   4618   4465   -141     42    170       C  
ATOM   1133  OE1 GLU A 323      14.398  23.855  36.551  1.00 24.50           O  
ANISOU 1133  OE1 GLU A 323     3264   3106   2941   -144     40    156       O  
ATOM   1134  OE2 GLU A 323      13.885  22.042  37.699  1.00 26.27           O  
ANISOU 1134  OE2 GLU A 323     3499   3332   3152   -145     47    183       O  
ATOM   1135  N   THR A 324      13.879  19.733  32.932  1.00 15.96           N  
ANISOU 1135  N   THR A 324     2167   1970   1928   -105     21    191       N  
ATOM   1136  CA  THR A 324      14.796  18.597  32.960  1.00 17.49           C  
ANISOU 1136  CA  THR A 324     2362   2164   2120    -99     12    210       C  
ATOM   1137  C   THR A 324      14.902  17.858  31.625  1.00 18.37           C  
ANISOU 1137  C   THR A 324     2465   2262   2253    -89      5    209       C  
ATOM   1138  O   THR A 324      15.575  16.839  31.535  1.00 19.39           O  
ANISOU 1138  O   THR A 324     2593   2388   2385    -84      0    224       O  
ATOM   1139  CB  THR A 324      14.396  17.567  34.028  1.00 21.52           C  
ANISOU 1139  CB  THR A 324     2880   2672   2625   -103     24    226       C  
ATOM   1140  OG1 THR A 324      13.005  17.261  33.881  1.00 20.34           O  
ANISOU 1140  OG1 THR A 324     2727   2508   2494   -107     40    217       O  
ATOM   1141  CG2 THR A 324      14.682  18.094  35.451  1.00 19.20           C  
ANISOU 1141  CG2 THR A 324     2596   2396   2301   -111     27    231       C  
ATOM   1142  N   VAL A 325      14.244  18.358  30.587  1.00 18.80           N  
ANISOU 1142  N   VAL A 325     2510   2310   2322    -86      5    193       N  
ATOM   1143  CA  VAL A 325      14.264  17.666  29.302  1.00 17.94           C  
ANISOU 1143  CA  VAL A 325     2391   2191   2232    -76     -1    190       C  
ATOM   1144  C   VAL A 325      15.236  18.358  28.340  1.00 16.95           C  
ANISOU 1144  C   VAL A 325     2265   2072   2105    -68    -15    186       C  
ATOM   1145  O   VAL A 325      15.294  19.584  28.266  1.00 13.66           O  
ANISOU 1145  O   VAL A 325     1850   1661   1680    -69    -16    178       O  
ATOM   1146  CB  VAL A 325      12.861  17.590  28.677  1.00 19.23           C  
ANISOU 1146  CB  VAL A 325     2546   2347   2415    -75      7    173       C  
ATOM   1147  CG1 VAL A 325      12.890  16.720  27.416  1.00 13.54           C  
ANISOU 1147  CG1 VAL A 325     1813   1619   1714    -65      1    168       C  
ATOM   1148  CG2 VAL A 325      11.861  17.051  29.700  1.00 17.66           C  
ANISOU 1148  CG2 VAL A 325     2348   2141   2219    -84     25    174       C  
ATOM   1149  N   GLY A 326      16.008  17.575  27.601  1.00 15.17           N  
ANISOU 1149  N   GLY A 326     2034   1842   1886    -61    -24    192       N  
ATOM   1150  CA  GLY A 326      16.959  18.160  26.677  1.00 11.37           C  
ANISOU 1150  CA  GLY A 326     1552   1365   1403    -54    -36    189       C  
ATOM   1151  C   GLY A 326      17.168  17.232  25.503  1.00 16.82           C  
ANISOU 1151  C   GLY A 326     2233   2049   2110    -46    -42    188       C  
ATOM   1152  O   GLY A 326      16.520  16.185  25.411  1.00 11.51           O  
ANISOU 1152  O   GLY A 326     1554   1368   1452    -46    -37    187       O  
ATOM   1153  N   SER A 327      18.054  17.628  24.593  1.00 15.99           N  
ANISOU 1153  N   SER A 327     2126   1945   2003    -39    -51    186       N  
ATOM   1154  CA  SER A 327      18.459  16.771  23.476  1.00 18.08           C  
ANISOU 1154  CA  SER A 327     2382   2205   2281    -32    -58    184       C  
ATOM   1155  C   SER A 327      19.801  17.204  22.906  1.00 16.71           C  
ANISOU 1155  C   SER A 327     2211   2036   2103    -27    -67    187       C  
ATOM   1156  O   SER A 327      20.142  18.380  22.959  1.00 15.85           O  
ANISOU 1156  O   SER A 327     2107   1931   1982    -28    -66    184       O  
ATOM   1157  CB  SER A 327      17.425  16.793  22.358  1.00 11.24           C  
ANISOU 1157  CB  SER A 327     1507   1339   1426    -24    -56    168       C  
ATOM   1158  OG  SER A 327      17.798  15.930  21.287  1.00 17.05           O  
ANISOU 1158  OG  SER A 327     2233   2071   2174    -17    -62    164       O  
ATOM   1159  N   THR A 328      20.560  16.241  22.381  1.00 19.44           N  
ANISOU 1159  N   THR A 328     2551   2378   2458    -24    -73    191       N  
ATOM   1160  CA  THR A 328      21.702  16.573  21.542  1.00 22.69           C  
ANISOU 1160  CA  THR A 328     2962   2791   2868    -19    -80    189       C  
ATOM   1161  C   THR A 328      21.147  16.971  20.190  1.00 20.40           C  
ANISOU 1161  C   THR A 328     2667   2501   2582    -10    -80    177       C  
ATOM   1162  O   THR A 328      19.957  16.792  19.904  1.00 14.30           O  
ANISOU 1162  O   THR A 328     1890   1729   1815     -7    -76    168       O  
ATOM   1163  CB  THR A 328      22.616  15.363  21.260  1.00 17.20           C  
ANISOU 1163  CB  THR A 328     2260   2090   2185    -18    -87    196       C  
ATOM   1164  OG1 THR A 328      21.890  14.417  20.463  1.00 19.44           O  
ANISOU 1164  OG1 THR A 328     2534   2368   2485    -14    -84    188       O  
ATOM   1165  CG2 THR A 328      23.092  14.711  22.564  1.00 14.97           C  
ANISOU 1165  CG2 THR A 328     1981   1807   1899    -23    -88    212       C  
ATOM   1166  N   ALA A 329      22.020  17.493  19.346  1.00 15.29           N  
ANISOU 1166  N   ALA A 329     2021   1855   1931     -5    -83    174       N  
ATOM   1167  CA  ALA A 329      21.630  17.812  17.989  1.00 14.59           C  
ANISOU 1167  CA  ALA A 329     1929   1769   1844      7    -83    164       C  
ATOM   1168  C   ALA A 329      22.885  17.704  17.163  1.00 14.59           C  
ANISOU 1168  C   ALA A 329     1929   1768   1846     10    -87    165       C  
ATOM   1169  O   ALA A 329      23.869  18.390  17.442  1.00 18.62           O  
ANISOU 1169  O   ALA A 329     2447   2278   2351      7    -86    170       O  
ATOM   1170  CB  ALA A 329      21.022  19.228  17.907  1.00 12.03           C  
ANISOU 1170  CB  ALA A 329     1613   1449   1508     12    -76    161       C  
ATOM   1171  N   VAL A 330      22.871  16.799  16.192  1.00 15.11           N  
ANISOU 1171  N   VAL A 330     1985   1834   1921     16    -91    159       N  
ATOM   1172  CA  VAL A 330      23.911  16.765  15.193  1.00 16.36           C  
ANISOU 1172  CA  VAL A 330     2143   1992   2081     20    -94    157       C  
ATOM   1173  C   VAL A 330      23.242  16.970  13.837  1.00 17.33           C  
ANISOU 1173  C   VAL A 330     2263   2123   2200     34    -93    146       C  
ATOM   1174  O   VAL A 330      22.326  16.234  13.462  1.00 13.99           O  
ANISOU 1174  O   VAL A 330     1828   1703   1783     37    -96    136       O  
ATOM   1175  CB  VAL A 330      24.727  15.449  15.222  1.00 17.03           C  
ANISOU 1175  CB  VAL A 330     2219   2071   2182     15    -99    159       C  
ATOM   1176  CG1 VAL A 330      23.866  14.288  14.797  1.00 13.37           C  
ANISOU 1176  CG1 VAL A 330     1743   1606   1731     17   -100    150       C  
ATOM   1177  CG2 VAL A 330      25.939  15.580  14.299  1.00 15.87           C  
ANISOU 1177  CG2 VAL A 330     2072   1923   2035     18   -101    156       C  
ATOM   1178  N  AVAL A 331      23.680  17.993  13.113  0.32 14.34           N  
ANISOU 1178  N  AVAL A 331     1892   1747   1810     42    -89    147       N  
ATOM   1179  N  BVAL A 331      23.721  17.969  13.101  0.68 14.33           N  
ANISOU 1179  N  BVAL A 331     1891   1745   1810     42    -89    147       N  
ATOM   1180  CA AVAL A 331      23.074  18.300  11.827  0.32 13.99           C  
ANISOU 1180  CA AVAL A 331     1846   1711   1757     58    -89    139       C  
ATOM   1181  CA BVAL A 331      23.101  18.364  11.848  0.68 13.68           C  
ANISOU 1181  CA BVAL A 331     1808   1673   1718     58    -88    140       C  
ATOM   1182  C  AVAL A 331      24.120  18.416  10.723  0.32 15.98           C  
ANISOU 1182  C  AVAL A 331     2101   1964   2006     64    -87    138       C  
ATOM   1183  C  BVAL A 331      24.129  18.448  10.713  0.68 16.04           C  
ANISOU 1183  C  BVAL A 331     2109   1972   2014     64    -87    139       C  
ATOM   1184  O  AVAL A 331      25.245  18.866  10.951  0.32 15.08           O  
ANISOU 1184  O  AVAL A 331     1995   1842   1893     58    -82    145       O  
ATOM   1185  O  BVAL A 331      25.253  18.920  10.911  0.68 15.00           O  
ANISOU 1185  O  BVAL A 331     1986   1832   1882     59    -82    145       O  
ATOM   1186  CB AVAL A 331      22.225  19.591  11.882  0.32 15.72           C  
ANISOU 1186  CB AVAL A 331     2075   1936   1964     68    -82    142       C  
ATOM   1187  CB BVAL A 331      22.392  19.729  12.000  0.68 15.75           C  
ANISOU 1187  CB BVAL A 331     2081   1937   1966     66    -81    144       C  
ATOM   1188  CG1AVAL A 331      21.209  19.520  13.021  0.32 14.98           C  
ANISOU 1188  CG1AVAL A 331     1979   1841   1874     60    -83    142       C  
ATOM   1189  CG1BVAL A 331      22.032  20.304  10.638  0.68 14.80           C  
ANISOU 1189  CG1BVAL A 331     1963   1828   1834     86    -79    141       C  
ATOM   1190  CG2AVAL A 331      23.118  20.807  12.039  0.32 15.38           C  
ANISOU 1190  CG2AVAL A 331     2046   1884   1913     67    -72    152       C  
ATOM   1191  CG2BVAL A 331      21.160  19.615  12.915  0.68 14.92           C  
ANISOU 1191  CG2BVAL A 331     1971   1833   1864     62    -82    141       C  
ATOM   1192  N   ALA A 332      23.729  18.009   9.523  1.00 13.57           N  
ANISOU 1192  N   ALA A 332     1789   1670   1697     76    -90    128       N  
ATOM   1193  CA  ALA A 332      24.594  18.086   8.354  1.00 16.17           C  
ANISOU 1193  CA  ALA A 332     2121   2002   2022     84    -88    127       C  
ATOM   1194  C   ALA A 332      23.835  18.687   7.182  1.00 16.98           C  
ANISOU 1194  C   ALA A 332     2226   2121   2106    105    -86    123       C  
ATOM   1195  O   ALA A 332      22.710  18.275   6.888  1.00 16.51           O  
ANISOU 1195  O   ALA A 332     2155   2074   2043    113    -93    112       O  
ATOM   1196  CB  ALA A 332      25.129  16.703   7.985  1.00 12.86           C  
ANISOU 1196  CB  ALA A 332     1687   1582   1617     76    -94    116       C  
ATOM   1197  N   LEU A 333      24.450  19.687   6.555  1.00 16.68           N  
ANISOU 1197  N   LEU A 333     2203   2081   2055    114    -76    132       N  
ATOM   1198  CA  LEU A 333      24.027  20.239   5.278  1.00 19.88           C  
ANISOU 1198  CA  LEU A 333     2613   2502   2440    137    -73    132       C  
ATOM   1199  C   LEU A 333      24.939  19.627   4.232  1.00 22.36           C  
ANISOU 1199  C   LEU A 333     2924   2820   2754    138    -73    125       C  
ATOM   1200  O   LEU A 333      26.149  19.681   4.374  1.00 18.05           O  
ANISOU 1200  O   LEU A 333     2383   2259   2216    127    -66    130       O  
ATOM   1201  CB  LEU A 333      24.263  21.750   5.264  1.00 22.77           C  
ANISOU 1201  CB  LEU A 333     2998   2858   2794    146    -57    148       C  
ATOM   1202  CG  LEU A 333      23.180  22.692   5.784  1.00 32.65           C  
ANISOU 1202  CG  LEU A 333     4256   4112   4039    156    -54    156       C  
ATOM   1203  CD1 LEU A 333      22.370  22.030   6.871  1.00 27.64           C  
ANISOU 1203  CD1 LEU A 333     3608   3477   3416    143    -65    147       C  
ATOM   1204  CD2 LEU A 333      23.760  24.035   6.234  1.00 26.23           C  
ANISOU 1204  CD2 LEU A 333     3461   3281   3225    154    -35    171       C  
ATOM   1205  N   VAL A 334      24.371  19.037   3.191  1.00 16.04           N  
ANISOU 1205  N   VAL A 334     2112   2039   1944    151    -81    112       N  
ATOM   1206  CA  VAL A 334      25.186  18.492   2.123  1.00 15.17           C  
ANISOU 1206  CA  VAL A 334     1998   1934   1831    153    -80    104       C  
ATOM   1207  C   VAL A 334      24.808  19.194   0.821  1.00 20.83           C  
ANISOU 1207  C   VAL A 334     2724   2671   2520    179    -76    106       C  
ATOM   1208  O   VAL A 334      23.632  19.429   0.531  1.00 15.74           O  
ANISOU 1208  O   VAL A 334     2076   2046   1860    197    -83    103       O  
ATOM   1209  CB  VAL A 334      25.010  16.960   1.945  1.00 19.81           C  
ANISOU 1209  CB  VAL A 334     2563   2530   2435    143    -92     82       C  
ATOM   1210  CG1 VAL A 334      25.907  16.456   0.819  1.00 20.67           C  
ANISOU 1210  CG1 VAL A 334     2668   2643   2541    145    -89     73       C  
ATOM   1211  CG2 VAL A 334      25.312  16.187   3.257  1.00 13.25           C  
ANISOU 1211  CG2 VAL A 334     1724   1679   1632    120    -95     82       C  
ATOM   1212  N   CYS A 335      25.821  19.582   0.062  1.00 20.01           N  
ANISOU 1212  N   CYS A 335     2632   2564   2407    184    -64    113       N  
ATOM   1213  CA  CYS A 335      25.606  20.076  -1.283  1.00 21.96           C  
ANISOU 1213  CA  CYS A 335     2887   2831   2626    209    -59    116       C  
ATOM   1214  C   CYS A 335      26.739  19.508  -2.136  1.00 22.48           C  
ANISOU 1214  C   CYS A 335     2952   2896   2693    204    -54    108       C  
ATOM   1215  O   CYS A 335      27.502  18.668  -1.674  1.00 18.39           O  
ANISOU 1215  O   CYS A 335     2424   2365   2200    181    -56     99       O  
ATOM   1216  CB  CYS A 335      25.573  21.604  -1.309  1.00 19.98           C  
ANISOU 1216  CB  CYS A 335     2660   2572   2359    226    -43    140       C  
ATOM   1217  SG  CYS A 335      27.110  22.411  -0.837  1.00 21.54           S  
ANISOU 1217  SG  CYS A 335     2877   2736   2571    209    -18    157       S  
ATOM   1218  N   SER A 336      26.842  19.954  -3.378  1.00 20.17           N  
ANISOU 1218  N   SER A 336     2669   2619   2375    225    -46    112       N  
ATOM   1219  CA  SER A 336      27.763  19.329  -4.311  1.00 24.46           C  
ANISOU 1219  CA  SER A 336     3209   3167   2917    221    -42    101       C  
ATOM   1220  C   SER A 336      29.214  19.531  -3.900  1.00 22.17           C  
ANISOU 1220  C   SER A 336     2929   2847   2647    201    -25    110       C  
ATOM   1221  O   SER A 336      30.033  18.644  -4.081  1.00 24.50           O  
ANISOU 1221  O   SER A 336     3214   3137   2959    186    -27     96       O  
ATOM   1222  CB  SER A 336      27.546  19.875  -5.723  1.00 32.32           C  
ANISOU 1222  CB  SER A 336     4215   4187   3876    250    -35    107       C  
ATOM   1223  OG  SER A 336      26.254  19.546  -6.180  1.00 45.17           O  
ANISOU 1223  OG  SER A 336     5829   5848   5484    269    -53     94       O  
ATOM   1224  N   SER A 337      29.523  20.695  -3.336  1.00 20.64           N  
ANISOU 1224  N   SER A 337     2755   2633   2455    201    -10    130       N  
ATOM   1225  CA  SER A 337      30.909  21.044  -3.021  1.00 24.54           C  
ANISOU 1225  CA  SER A 337     3258   3100   2966    185      8    137       C  
ATOM   1226  C   SER A 337      31.335  20.785  -1.575  1.00 20.73           C  
ANISOU 1226  C   SER A 337     2768   2596   2514    159      3    134       C  
ATOM   1227  O   SER A 337      32.528  20.602  -1.295  1.00 19.31           O  
ANISOU 1227  O   SER A 337     2587   2398   2354    141     10    131       O  
ATOM   1228  CB  SER A 337      31.138  22.521  -3.326  1.00 23.35           C  
ANISOU 1228  CB  SER A 337     3133   2938   2800    199     33    158       C  
ATOM   1229  OG  SER A 337      30.239  23.322  -2.573  1.00 25.11           O  
ANISOU 1229  OG  SER A 337     3362   3158   3020    207     32    171       O  
ATOM   1230  N   HIS A 338      30.374  20.783  -0.659  1.00 14.08           N  
ANISOU 1230  N   HIS A 338     1920   1756   1675    158    -10    136       N  
ATOM   1231  CA  HIS A 338      30.710  20.821   0.760  1.00 15.57           C  
ANISOU 1231  CA  HIS A 338     2104   1924   1886    137    -12    138       C  
ATOM   1232  C   HIS A 338      29.764  20.018   1.652  1.00 15.67           C  
ANISOU 1232  C   HIS A 338     2102   1944   1909    130    -32    131       C  
ATOM   1233  O   HIS A 338      28.613  19.763   1.308  1.00 17.00           O  
ANISOU 1233  O   HIS A 338     2265   2131   2065    143    -43    126       O  
ATOM   1234  CB  HIS A 338      30.708  22.267   1.264  1.00 16.14           C  
ANISOU 1234  CB  HIS A 338     2195   1982   1954    141      5    155       C  
ATOM   1235  CG  HIS A 338      31.830  23.087   0.743  1.00 16.38           C  
ANISOU 1235  CG  HIS A 338     2242   1999   1985    141     29    162       C  
ATOM   1236  ND1 HIS A 338      31.800  23.675  -0.503  1.00 18.35           N  
ANISOU 1236  ND1 HIS A 338     2504   2254   2212    162     45    170       N  
ATOM   1237  CD2 HIS A 338      33.043  23.401   1.272  1.00 18.93           C  
ANISOU 1237  CD2 HIS A 338     2567   2300   2327    124     42    160       C  
ATOM   1238  CE1 HIS A 338      32.929  24.318  -0.716  1.00 20.82           C  
ANISOU 1238  CE1 HIS A 338     2830   2549   2533    157     68    174       C  
ATOM   1239  NE2 HIS A 338      33.703  24.173   0.354  1.00 20.29           N  
ANISOU 1239  NE2 HIS A 338     2754   2464   2491    133     67    167       N  
ATOM   1240  N   ILE A 339      30.278  19.641   2.811  1.00 14.11           N  
ANISOU 1240  N   ILE A 339     1898   1732   1733    110    -37    130       N  
ATOM   1241  CA  ILE A 339      29.455  19.141   3.899  1.00 16.35           C  
ANISOU 1241  CA  ILE A 339     2171   2016   2025    102    -51    128       C  
ATOM   1242  C   ILE A 339      29.686  20.120   5.040  1.00 15.82           C  
ANISOU 1242  C   ILE A 339     2115   1935   1963     94    -43    140       C  
ATOM   1243  O   ILE A 339      30.823  20.465   5.342  1.00 17.61           O  
ANISOU 1243  O   ILE A 339     2345   2147   2198     83    -34    142       O  
ATOM   1244  CB  ILE A 339      29.890  17.714   4.320  1.00 13.24           C  
ANISOU 1244  CB  ILE A 339     1760   1619   1654     86    -63    117       C  
ATOM   1245  CG1 ILE A 339      29.689  16.732   3.153  1.00 18.13           C  
ANISOU 1245  CG1 ILE A 339     2366   2251   2271     93    -69    102       C  
ATOM   1246  CG2 ILE A 339      29.157  17.258   5.604  1.00 13.02           C  
ANISOU 1246  CG2 ILE A 339     1724   1588   1636     77    -74    119       C  
ATOM   1247  CD1 ILE A 339      30.390  15.384   3.348  1.00 17.07           C  
ANISOU 1247  CD1 ILE A 339     2215   2109   2161     78    -76     92       C  
ATOM   1248  N   VAL A 340      28.610  20.607   5.636  1.00 15.95           N  
ANISOU 1248  N   VAL A 340     2134   1955   1971     99    -45    145       N  
ATOM   1249  CA  VAL A 340      28.725  21.433   6.826  1.00 15.42           C  
ANISOU 1249  CA  VAL A 340     2074   1876   1910     89    -39    153       C  
ATOM   1250  C   VAL A 340      27.996  20.729   7.969  1.00 17.89           C  
ANISOU 1250  C   VAL A 340     2376   2191   2231     79    -53    150       C  
ATOM   1251  O   VAL A 340      26.816  20.394   7.856  1.00 17.57           O  
ANISOU 1251  O   VAL A 340     2331   2162   2185     87    -61    147       O  
ATOM   1252  CB  VAL A 340      28.099  22.830   6.624  1.00 20.30           C  
ANISOU 1252  CB  VAL A 340     2707   2493   2512    103    -25    163       C  
ATOM   1253  CG1 VAL A 340      28.310  23.687   7.876  1.00 17.07           C  
ANISOU 1253  CG1 VAL A 340     2304   2070   2111     91    -16    168       C  
ATOM   1254  CG2 VAL A 340      28.680  23.515   5.395  1.00 20.64           C  
ANISOU 1254  CG2 VAL A 340     2763   2534   2545    117     -8    168       C  
ATOM   1255  N   VAL A 341      28.698  20.527   9.074  1.00 12.35           N  
ANISOU 1255  N   VAL A 341     1671   1479   1541     62    -56    151       N  
ATOM   1256  CA  VAL A 341      28.128  19.837  10.219  1.00 13.53           C  
ANISOU 1256  CA  VAL A 341     1813   1630   1698     52    -67    151       C  
ATOM   1257  C   VAL A 341      28.123  20.759  11.418  1.00 11.39           C  
ANISOU 1257  C   VAL A 341     1549   1353   1425     44    -61    157       C  
ATOM   1258  O   VAL A 341      29.145  21.371  11.735  1.00 14.43           O  
ANISOU 1258  O   VAL A 341     1938   1731   1813     37    -54    157       O  
ATOM   1259  CB  VAL A 341      28.961  18.556  10.570  1.00 14.96           C  
ANISOU 1259  CB  VAL A 341     1982   1808   1896     41    -77    148       C  
ATOM   1260  CG1 VAL A 341      28.520  17.963  11.907  1.00 14.76           C  
ANISOU 1260  CG1 VAL A 341     1950   1781   1877     31    -85    151       C  
ATOM   1261  CG2 VAL A 341      28.838  17.500   9.480  1.00 12.83           C  
ANISOU 1261  CG2 VAL A 341     1701   1542   1630     47    -83    139       C  
ATOM   1262  N   SER A 342      26.978  20.854  12.084  1.00 10.69           N  
ANISOU 1262  N   SER A 342     1460   1269   1333     45    -64    158       N  
ATOM   1263  CA  SER A 342      26.855  21.616  13.321  1.00 12.99           C  
ANISOU 1263  CA  SER A 342     1756   1556   1622     36    -60    162       C  
ATOM   1264  C   SER A 342      26.488  20.657  14.453  1.00 14.57           C  
ANISOU 1264  C   SER A 342     1948   1759   1828     25    -71    163       C  
ATOM   1265  O   SER A 342      25.526  19.875  14.353  1.00 15.44           O  
ANISOU 1265  O   SER A 342     2052   1874   1940     29    -77    161       O  
ATOM   1266  CB  SER A 342      25.788  22.707  13.202  1.00 17.58           C  
ANISOU 1266  CB  SER A 342     2346   2139   2193     46    -50    164       C  
ATOM   1267  OG  SER A 342      25.581  23.358  14.448  1.00 15.85           O  
ANISOU 1267  OG  SER A 342     2131   1918   1974     35    -45    166       O  
ATOM   1268  N   ASN A 343      27.261  20.688  15.526  1.00 12.66           N  
ANISOU 1268  N   ASN A 343     1707   1516   1589     13    -72    165       N  
ATOM   1269  CA  ASN A 343      27.091  19.666  16.555  1.00 15.25           C  
ANISOU 1269  CA  ASN A 343     2028   1846   1922      5    -83    169       C  
ATOM   1270  C   ASN A 343      26.917  20.252  17.944  1.00 16.53           C  
ANISOU 1270  C   ASN A 343     2193   2010   2076     -5    -80    172       C  
ATOM   1271  O   ASN A 343      27.653  21.147  18.337  1.00 13.30           O  
ANISOU 1271  O   ASN A 343     1788   1601   1663    -10    -75    169       O  
ATOM   1272  CB  ASN A 343      28.294  18.722  16.558  1.00 14.58           C  
ANISOU 1272  CB  ASN A 343     1935   1758   1846      0    -91    170       C  
ATOM   1273  CG  ASN A 343      28.190  17.669  17.663  1.00 19.18           C  
ANISOU 1273  CG  ASN A 343     2511   2342   2432     -6   -100    178       C  
ATOM   1274  OD1 ASN A 343      28.906  17.712  18.658  1.00 18.54           O  
ANISOU 1274  OD1 ASN A 343     2431   2265   2349    -12   -104    182       O  
ATOM   1275  ND2 ASN A 343      27.259  16.752  17.502  1.00 16.37           N  
ANISOU 1275  ND2 ASN A 343     2150   1985   2083     -3   -102    179       N  
ATOM   1276  N   CYS A 344      25.962  19.718  18.692  1.00 12.75           N  
ANISOU 1276  N   CYS A 344     1713   1534   1596     -7    -84    175       N  
ATOM   1277  CA  CYS A 344      25.764  20.127  20.066  1.00 15.01           C  
ANISOU 1277  CA  CYS A 344     2003   1825   1874    -16    -82    178       C  
ATOM   1278  C   CYS A 344      25.455  18.886  20.886  1.00 15.50           C  
ANISOU 1278  C   CYS A 344     2061   1889   1939    -20    -89    186       C  
ATOM   1279  O   CYS A 344      24.340  18.379  20.853  1.00 19.01           O  
ANISOU 1279  O   CYS A 344     2504   2332   2388    -18    -87    187       O  
ATOM   1280  CB  CYS A 344      24.605  21.137  20.150  1.00 20.20           C  
ANISOU 1280  CB  CYS A 344     2666   2483   2525    -15    -72    174       C  
ATOM   1281  SG  CYS A 344      24.385  21.864  21.780  1.00 25.90           S  
ANISOU 1281  SG  CYS A 344     3393   3210   3236    -27    -67    174       S  
ATOM   1282  N   GLY A 345      26.452  18.357  21.587  1.00 13.82           N  
ANISOU 1282  N   GLY A 345     1845   1679   1726    -24    -97    193       N  
ATOM   1283  CA  GLY A 345      26.235  17.174  22.393  1.00 11.98           C  
ANISOU 1283  CA  GLY A 345     1609   1446   1495    -26   -102    204       C  
ATOM   1284  C   GLY A 345      27.196  16.065  22.008  1.00 19.40           C  
ANISOU 1284  C   GLY A 345     2542   2383   2448    -22   -110    210       C  
ATOM   1285  O   GLY A 345      28.277  16.327  21.470  1.00 15.79           O  
ANISOU 1285  O   GLY A 345     2081   1925   1993    -21   -114    205       O  
ATOM   1286  N   ASP A 346      26.799  14.825  22.287  1.00 15.07           N  
ANISOU 1286  N   ASP A 346     1989   1828   1908    -20   -110    220       N  
ATOM   1287  CA  ASP A 346      27.656  13.673  22.034  1.00 21.85           C  
ANISOU 1287  CA  ASP A 346     2840   2681   2780    -16   -117    227       C  
ATOM   1288  C   ASP A 346      27.092  12.702  21.007  1.00 20.18           C  
ANISOU 1288  C   ASP A 346     2621   2457   2589    -12   -112    222       C  
ATOM   1289  O   ASP A 346      27.565  11.575  20.895  1.00 21.12           O  
ANISOU 1289  O   ASP A 346     2733   2568   2722    -10   -114    229       O  
ATOM   1290  CB  ASP A 346      28.012  12.941  23.335  1.00 24.52           C  
ANISOU 1290  CB  ASP A 346     3180   3023   3114    -16   -121    244       C  
ATOM   1291  CG  ASP A 346      26.784  12.410  24.074  1.00 33.68           C  
ANISOU 1291  CG  ASP A 346     4344   4178   4273    -17   -112    254       C  
ATOM   1292  OD1 ASP A 346      25.634  12.574  23.588  1.00 26.32           O  
ANISOU 1292  OD1 ASP A 346     3413   3241   3347    -19   -103    244       O  
ATOM   1293  OD2 ASP A 346      26.993  11.802  25.143  1.00 30.38           O  
ANISOU 1293  OD2 ASP A 346     3929   3763   3850    -15   -113    271       O  
ATOM   1294  N   SER A 347      26.073  13.131  20.269  1.00 16.16           N  
ANISOU 1294  N   SER A 347     2113   1948   2081    -12   -106    210       N  
ATOM   1295  CA  SER A 347      25.770  12.477  19.011  1.00 16.66           C  
ANISOU 1295  CA  SER A 347     2166   2004   2159     -7   -105    199       C  
ATOM   1296  C   SER A 347      26.922  12.827  18.064  1.00 18.34           C  
ANISOU 1296  C   SER A 347     2377   2218   2373     -4   -110    193       C  
ATOM   1297  O   SER A 347      27.816  13.595  18.433  1.00 17.64           O  
ANISOU 1297  O   SER A 347     2294   2136   2274     -6   -114    196       O  
ATOM   1298  CB  SER A 347      24.402  12.895  18.475  1.00 15.40           C  
ANISOU 1298  CB  SER A 347     2006   1848   1998     -6    -98    187       C  
ATOM   1299  OG  SER A 347      23.387  12.519  19.390  1.00 18.73           O  
ANISOU 1299  OG  SER A 347     2429   2266   2421    -10    -92    191       O  
ATOM   1300  N   ARG A 348      26.935  12.259  16.864  1.00 14.31           N  
ANISOU 1300  N   ARG A 348     1858   1704   1875      0   -109    183       N  
ATOM   1301  CA  ARG A 348      28.175  12.292  16.075  1.00 18.97           C  
ANISOU 1301  CA  ARG A 348     2445   2294   2470      2   -113    179       C  
ATOM   1302  C   ARG A 348      27.902  12.172  14.586  1.00 16.77           C  
ANISOU 1302  C   ARG A 348     2160   2016   2197      7   -111    164       C  
ATOM   1303  O   ARG A 348      26.962  11.491  14.175  1.00 15.94           O  
ANISOU 1303  O   ARG A 348     2046   1910   2099      9   -108    155       O  
ATOM   1304  CB  ARG A 348      29.119  11.165  16.531  1.00 13.66           C  
ANISOU 1304  CB  ARG A 348     1764   1612   1812      0   -118    189       C  
ATOM   1305  CG  ARG A 348      30.562  11.294  16.058  1.00 19.60           C  
ANISOU 1305  CG  ARG A 348     2513   2364   2568      0   -123    186       C  
ATOM   1306  CD  ARG A 348      31.432  10.125  16.547  1.00 22.96           C  
ANISOU 1306  CD  ARG A 348     2932   2783   3011      1   -127    197       C  
ATOM   1307  NE  ARG A 348      31.489  10.028  18.001  1.00 24.05           N  
ANISOU 1307  NE  ARG A 348     3073   2923   3141      0   -131    214       N  
ATOM   1308  CZ  ARG A 348      31.807   8.915  18.660  1.00 28.89           C  
ANISOU 1308  CZ  ARG A 348     3682   3529   3767      3   -133    228       C  
ATOM   1309  NH1 ARG A 348      32.118   7.806  17.998  1.00 22.37           N  
ANISOU 1309  NH1 ARG A 348     2844   2690   2964      6   -131    226       N  
ATOM   1310  NH2 ARG A 348      31.835   8.913  19.980  1.00 25.63           N  
ANISOU 1310  NH2 ARG A 348     3274   3122   3342      4   -137    244       N  
ATOM   1311  N   ALA A 349      28.702  12.863  13.778  1.00 17.40           N  
ANISOU 1311  N   ALA A 349     2243   2099   2270     10   -111    158       N  
ATOM   1312  CA  ALA A 349      28.657  12.678  12.332  1.00 14.74           C  
ANISOU 1312  CA  ALA A 349     1900   1765   1936     16   -109    145       C  
ATOM   1313  C   ALA A 349      30.031  12.197  11.895  1.00 15.55           C  
ANISOU 1313  C   ALA A 349     1997   1861   2050     14   -111    143       C  
ATOM   1314  O   ALA A 349      31.042  12.753  12.325  1.00 17.02           O  
ANISOU 1314  O   ALA A 349     2188   2045   2233     11   -112    149       O  
ATOM   1315  CB  ALA A 349      28.303  13.981  11.633  1.00 15.71           C  
ANISOU 1315  CB  ALA A 349     2033   1896   2039     24   -105    140       C  
ATOM   1316  N   VAL A 350      30.068  11.158  11.061  1.00 14.38           N  
ANISOU 1316  N   VAL A 350     1836   1710   1917     15   -111    133       N  
ATOM   1317  CA  VAL A 350      31.332  10.580  10.627  1.00 17.70           C  
ANISOU 1317  CA  VAL A 350     2249   2123   2352     13   -112    131       C  
ATOM   1318  C   VAL A 350      31.349  10.414   9.114  1.00 20.14           C  
ANISOU 1318  C   VAL A 350     2552   2437   2662     17   -108    114       C  
ATOM   1319  O   VAL A 350      30.421   9.831   8.525  1.00 17.36           O  
ANISOU 1319  O   VAL A 350     2192   2090   2314     20   -107    102       O  
ATOM   1320  CB  VAL A 350      31.594   9.207  11.277  1.00 15.16           C  
ANISOU 1320  CB  VAL A 350     1917   1790   2055      8   -114    137       C  
ATOM   1321  CG1 VAL A 350      32.922   8.607  10.744  1.00 15.57           C  
ANISOU 1321  CG1 VAL A 350     1959   1834   2123      7   -115    132       C  
ATOM   1322  CG2 VAL A 350      31.619   9.323  12.782  1.00 19.31           C  
ANISOU 1322  CG2 VAL A 350     2448   2313   2576      5   -118    155       C  
ATOM   1323  N   LEU A 351      32.403  10.940   8.503  1.00 12.02           N  
ANISOU 1323  N   LEU A 351     1528   1408   1629     18   -106    111       N  
ATOM   1324  CA  LEU A 351      32.630  10.844   7.059  1.00 16.78           C  
ANISOU 1324  CA  LEU A 351     2127   2017   2231     22   -101     96       C  
ATOM   1325  C   LEU A 351      33.616   9.711   6.759  1.00 14.91           C  
ANISOU 1325  C   LEU A 351     1876   1770   2019     16   -102     89       C  
ATOM   1326  O   LEU A 351      34.641   9.593   7.417  1.00 17.34           O  
ANISOU 1326  O   LEU A 351     2183   2068   2338     11   -104     98       O  
ATOM   1327  CB  LEU A 351      33.191  12.173   6.534  1.00 14.53           C  
ANISOU 1327  CB  LEU A 351     1857   1737   1928     27    -95     98       C  
ATOM   1328  CG  LEU A 351      33.743  12.296   5.099  1.00 19.41           C  
ANISOU 1328  CG  LEU A 351     2475   2358   2540     31    -87     86       C  
ATOM   1329  CD1 LEU A 351      32.637  12.182   4.062  1.00 15.29           C  
ANISOU 1329  CD1 LEU A 351     1951   1853   2006     42    -87     75       C  
ATOM   1330  CD2 LEU A 351      34.544  13.599   4.880  1.00 19.85           C  
ANISOU 1330  CD2 LEU A 351     2546   2412   2583     33    -77     92       C  
ATOM   1331  N   PHE A 352      33.309   8.875   5.774  1.00 17.86           N  
ANISOU 1331  N   PHE A 352     2238   2147   2402     18    -99     73       N  
ATOM   1332  CA  PHE A 352      34.250   7.842   5.333  1.00 17.95           C  
ANISOU 1332  CA  PHE A 352     2235   2149   2438     12    -97     64       C  
ATOM   1333  C   PHE A 352      34.955   8.369   4.079  1.00 18.87           C  
ANISOU 1333  C   PHE A 352     2355   2272   2544     15    -91     53       C  
ATOM   1334  O   PHE A 352      34.336   8.491   3.015  1.00 20.21           O  
ANISOU 1334  O   PHE A 352     2523   2455   2699     22    -88     39       O  
ATOM   1335  CB  PHE A 352      33.505   6.518   5.041  1.00 16.86           C  
ANISOU 1335  CB  PHE A 352     2078   2008   2320     10    -96     51       C  
ATOM   1336  CG  PHE A 352      34.405   5.288   4.956  1.00 17.93           C  
ANISOU 1336  CG  PHE A 352     2197   2128   2487      4    -93     45       C  
ATOM   1337  CD1 PHE A 352      35.559   5.194   5.713  1.00 20.34           C  
ANISOU 1337  CD1 PHE A 352     2503   2419   2804      0    -96     60       C  
ATOM   1338  CD2 PHE A 352      34.080   4.224   4.119  1.00 24.49           C  
ANISOU 1338  CD2 PHE A 352     3011   2958   3337      1    -87     24       C  
ATOM   1339  CE1 PHE A 352      36.388   4.059   5.648  1.00 26.47           C  
ANISOU 1339  CE1 PHE A 352     3265   3181   3613     -4    -93     56       C  
ATOM   1340  CE2 PHE A 352      34.899   3.091   4.042  1.00 23.95           C  
ANISOU 1340  CE2 PHE A 352     2926   2873   3300     -5    -83     19       C  
ATOM   1341  CZ  PHE A 352      36.058   3.010   4.806  1.00 18.81           C  
ANISOU 1341  CZ  PHE A 352     2278   2207   2662     -7    -86     37       C  
ATOM   1342  N   ARG A 353      36.230   8.729   4.202  1.00 17.14           N  
ANISOU 1342  N   ARG A 353     2139   2043   2329     11    -89     58       N  
ATOM   1343  CA  ARG A 353      36.973   9.227   3.044  1.00 15.82           C  
ANISOU 1343  CA  ARG A 353     1977   1881   2154     13    -81     48       C  
ATOM   1344  C   ARG A 353      38.089   8.258   2.712  1.00 21.85           C  
ANISOU 1344  C   ARG A 353     2725   2632   2944      6    -79     38       C  
ATOM   1345  O   ARG A 353      38.969   8.004   3.534  1.00 17.70           O  
ANISOU 1345  O   ARG A 353     2195   2093   2436      0    -82     46       O  
ATOM   1346  CB  ARG A 353      37.556  10.627   3.283  1.00 21.52           C  
ANISOU 1346  CB  ARG A 353     2716   2601   2858     14    -75     58       C  
ATOM   1347  CG  ARG A 353      38.361  11.180   2.084  1.00 23.64           C  
ANISOU 1347  CG  ARG A 353     2991   2871   3119     16    -62     49       C  
ATOM   1348  CD  ARG A 353      38.695  12.698   2.221  1.00 27.02           C  
ANISOU 1348  CD  ARG A 353     3439   3298   3529     19    -52     59       C  
ATOM   1349  NE  ARG A 353      37.490  13.517   2.113  1.00 25.09           N  
ANISOU 1349  NE  ARG A 353     3208   3066   3259     30    -50     66       N  
ATOM   1350  CZ  ARG A 353      37.435  14.840   2.278  1.00 25.75           C  
ANISOU 1350  CZ  ARG A 353     3309   3149   3326     34    -41     77       C  
ATOM   1351  NH1 ARG A 353      38.531  15.525   2.566  1.00 19.05           N  
ANISOU 1351  NH1 ARG A 353     2466   2288   2484     27    -31     78       N  
ATOM   1352  NH2 ARG A 353      36.272  15.480   2.151  1.00 22.43           N  
ANISOU 1352  NH2 ARG A 353     2899   2739   2883     46    -40     84       N  
ATOM   1353  N   GLY A 354      38.058   7.716   1.507  1.00 20.00           N  
ANISOU 1353  N   GLY A 354     2482   2403   2712      7    -73     20       N  
ATOM   1354  CA  GLY A 354      39.046   6.720   1.135  1.00 25.66           C  
ANISOU 1354  CA  GLY A 354     3183   3109   3458     -1    -70      8       C  
ATOM   1355  C   GLY A 354      38.825   5.521   2.028  1.00 20.52           C  
ANISOU 1355  C   GLY A 354     2517   2446   2835     -5    -77     13       C  
ATOM   1356  O   GLY A 354      37.737   4.957   2.037  1.00 25.01           O  
ANISOU 1356  O   GLY A 354     3079   3019   3405     -4    -78      8       O  
ATOM   1357  N   LYS A 355      39.829   5.148   2.808  1.00 24.84           N  
ANISOU 1357  N   LYS A 355     3059   2977   3404    -10    -80     22       N  
ATOM   1358  CA  LYS A 355      39.666   4.032   3.741  1.00 28.36           C  
ANISOU 1358  CA  LYS A 355     3492   3409   3875    -11    -85     31       C  
ATOM   1359  C   LYS A 355      39.644   4.446   5.207  1.00 24.94           C  
ANISOU 1359  C   LYS A 355     3068   2973   3436     -9    -94     55       C  
ATOM   1360  O   LYS A 355      39.765   3.589   6.080  1.00 27.57           O  
ANISOU 1360  O   LYS A 355     3392   3294   3789     -9    -98     67       O  
ATOM   1361  CB  LYS A 355      40.761   2.978   3.532  1.00 40.62           C  
ANISOU 1361  CB  LYS A 355     5026   4946   5462    -16    -82     24       C  
ATOM   1362  CG  LYS A 355      41.877   3.403   2.597  1.00 39.00           C  
ANISOU 1362  CG  LYS A 355     4821   4741   5255    -19    -76     10       C  
ATOM   1363  CD  LYS A 355      43.156   2.596   2.838  1.00 51.91           C  
ANISOU 1363  CD  LYS A 355     6441   6359   6924    -23    -76     10       C  
ATOM   1364  CE  LYS A 355      43.930   3.134   4.040  1.00 54.63           C  
ANISOU 1364  CE  LYS A 355     6791   6700   7267    -20    -87     29       C  
ATOM   1365  NZ  LYS A 355      45.167   2.349   4.337  1.00 52.06           N  
ANISOU 1365  NZ  LYS A 355     6448   6359   6972    -21    -89     29       N  
ATOM   1366  N   GLU A 356      39.482   5.743   5.482  1.00 22.46           N  
ANISOU 1366  N   GLU A 356     2771   2670   3093     -7    -97     62       N  
ATOM   1367  CA  GLU A 356      39.542   6.252   6.864  1.00 25.08           C  
ANISOU 1367  CA  GLU A 356     3111   3001   3417     -5   -106     82       C  
ATOM   1368  C   GLU A 356      38.272   6.973   7.337  1.00 24.56           C  
ANISOU 1368  C   GLU A 356     3058   2946   3327     -2   -107     91       C  
ATOM   1369  O   GLU A 356      37.741   7.857   6.649  1.00 18.87           O  
ANISOU 1369  O   GLU A 356     2349   2237   2585      1   -102     84       O  
ATOM   1370  CB  GLU A 356      40.726   7.216   7.033  1.00 27.24           C  
ANISOU 1370  CB  GLU A 356     3391   3276   3684     -7   -107     83       C  
ATOM   1371  CG  GLU A 356      42.051   6.724   6.469  1.00 29.13           C  
ANISOU 1371  CG  GLU A 356     3617   3506   3945    -11   -104     72       C  
ATOM   1372  CD  GLU A 356      42.689   5.641   7.328  1.00 37.68           C  
ANISOU 1372  CD  GLU A 356     4686   4578   5055    -10   -112     82       C  
ATOM   1373  OE1 GLU A 356      42.149   5.338   8.426  1.00 36.53           O  
ANISOU 1373  OE1 GLU A 356     4542   4432   4908     -6   -120     99       O  
ATOM   1374  OE2 GLU A 356      43.734   5.096   6.901  1.00 41.14           O  
ANISOU 1374  OE2 GLU A 356     5110   5006   5514    -12   -110     73       O  
ATOM   1375  N   ALA A 357      37.802   6.601   8.522  1.00 18.42           N  
ANISOU 1375  N   ALA A 357     2281   2165   2553     -1   -113    106       N  
ATOM   1376  CA  ALA A 357      36.737   7.325   9.178  1.00 21.31           C  
ANISOU 1376  CA  ALA A 357     2659   2539   2896      1   -115    116       C  
ATOM   1377  C   ALA A 357      37.285   8.699   9.515  1.00 23.42           C  
ANISOU 1377  C   ALA A 357     2941   2815   3144      1   -117    120       C  
ATOM   1378  O   ALA A 357      38.431   8.839   9.935  1.00 28.07           O  
ANISOU 1378  O   ALA A 357     3526   3400   3738     -1   -121    123       O  
ATOM   1379  CB  ALA A 357      36.304   6.607  10.448  1.00 19.62           C  
ANISOU 1379  CB  ALA A 357     2443   2320   2691      2   -120    132       C  
ATOM   1380  N   MET A 358      36.479   9.724   9.302  1.00 18.44           N  
ANISOU 1380  N   MET A 358     2322   2193   2490      3   -113    118       N  
ATOM   1381  CA  MET A 358      36.837  11.069   9.745  1.00 21.12           C  
ANISOU 1381  CA  MET A 358     2675   2538   2812      2   -112    123       C  
ATOM   1382  C   MET A 358      35.647  11.691  10.454  1.00 20.39           C  
ANISOU 1382  C   MET A 358     2593   2453   2702      4   -113    131       C  
ATOM   1383  O   MET A 358      34.716  12.143   9.803  1.00 17.72           O  
ANISOU 1383  O   MET A 358     2262   2121   2351      9   -108    127       O  
ATOM   1384  CB  MET A 358      37.220  11.945   8.559  1.00 20.07           C  
ANISOU 1384  CB  MET A 358     2549   2407   2670      3   -101    111       C  
ATOM   1385  CG  MET A 358      38.350  11.391   7.698  1.00 39.04           C  
ANISOU 1385  CG  MET A 358     4942   4804   5090      1    -98    100       C  
ATOM   1386  SD  MET A 358      39.001  12.614   6.544  1.00 55.29           S  
ANISOU 1386  SD  MET A 358     7011   6862   7134      2    -82     90       S  
ATOM   1387  CE  MET A 358      39.921  13.694   7.646  1.00 39.27           C  
ANISOU 1387  CE  MET A 358     4988   4830   5104     -5    -81     95       C  
ATOM   1388  N   PRO A 359      35.667  11.702  11.787  1.00 21.15           N  
ANISOU 1388  N   PRO A 359     2690   2549   2797      1   -120    143       N  
ATOM   1389  CA  PRO A 359      34.532  12.296  12.501  1.00 23.52           C  
ANISOU 1389  CA  PRO A 359     3000   2856   3080      2   -119    151       C  
ATOM   1390  C   PRO A 359      34.458  13.772  12.135  1.00 24.35           C  
ANISOU 1390  C   PRO A 359     3118   2967   3168      3   -111    146       C  
ATOM   1391  O   PRO A 359      35.505  14.402  12.028  1.00 22.24           O  
ANISOU 1391  O   PRO A 359     2853   2698   2901      0   -108    142       O  
ATOM   1392  CB  PRO A 359      34.894  12.111  13.977  1.00 25.31           C  
ANISOU 1392  CB  PRO A 359     3225   3083   3307     -1   -128    163       C  
ATOM   1393  CG  PRO A 359      36.394  11.849  13.988  1.00 33.54           C  
ANISOU 1393  CG  PRO A 359     4260   4123   4362     -3   -132    161       C  
ATOM   1394  CD  PRO A 359      36.715  11.191  12.687  1.00 21.82           C  
ANISOU 1394  CD  PRO A 359     2767   2630   2892     -1   -128    150       C  
ATOM   1395  N   LEU A 360      33.261  14.294  11.881  1.00 20.16           N  
ANISOU 1395  N   LEU A 360     2596   2441   2623      8   -107    146       N  
ATOM   1396  CA  LEU A 360      33.116  15.705  11.529  1.00 20.50           C  
ANISOU 1396  CA  LEU A 360     2651   2487   2650     11    -97    144       C  
ATOM   1397  C   LEU A 360      32.578  16.514  12.703  1.00 21.33           C  
ANISOU 1397  C   LEU A 360     2765   2597   2745      7    -97    151       C  
ATOM   1398  O   LEU A 360      32.168  17.668  12.542  1.00 26.16           O  
ANISOU 1398  O   LEU A 360     3387   3210   3344     10    -87    150       O  
ATOM   1399  CB  LEU A 360      32.205  15.867  10.316  1.00 15.91           C  
ANISOU 1399  CB  LEU A 360     2073   1911   2060     21    -91    138       C  
ATOM   1400  CG  LEU A 360      32.676  15.217   9.014  1.00 21.74           C  
ANISOU 1400  CG  LEU A 360     2806   2650   2806     25    -90    128       C  
ATOM   1401  CD1 LEU A 360      31.668  15.468   7.913  1.00 18.82           C  
ANISOU 1401  CD1 LEU A 360     2439   2290   2422     37    -86    123       C  
ATOM   1402  CD2 LEU A 360      34.045  15.753   8.608  1.00 19.00           C  
ANISOU 1402  CD2 LEU A 360     2461   2295   2461     21    -82    125       C  
ATOM   1403  N   SER A 361      32.554  15.903  13.881  1.00 13.66           N  
ANISOU 1403  N   SER A 361     1788   1626   1777      2   -106    158       N  
ATOM   1404  CA  SER A 361      32.166  16.607  15.106  1.00 19.72           C  
ANISOU 1404  CA  SER A 361     2562   2398   2533     -2   -106    164       C  
ATOM   1405  C   SER A 361      33.019  16.080  16.237  1.00 18.70           C  
ANISOU 1405  C   SER A 361     2427   2271   2409     -8   -115    169       C  
ATOM   1406  O   SER A 361      33.479  14.956  16.173  1.00 23.75           O  
ANISOU 1406  O   SER A 361     3056   2906   3061     -7   -122    173       O  
ATOM   1407  CB  SER A 361      30.683  16.366  15.443  1.00 17.46           C  
ANISOU 1407  CB  SER A 361     2278   2114   2241      0   -106    168       C  
ATOM   1408  OG  SER A 361      30.402  14.967  15.514  1.00 18.87           O  
ANISOU 1408  OG  SER A 361     2447   2289   2432      1   -113    172       O  
ATOM   1409  N   VAL A 362      33.215  16.890  17.272  1.00 18.61           N  
ANISOU 1409  N   VAL A 362     2419   2265   2387    -14   -115    170       N  
ATOM   1410  CA  VAL A 362      33.933  16.468  18.472  1.00 23.90           C  
ANISOU 1410  CA  VAL A 362     3082   2942   3056    -17   -126    175       C  
ATOM   1411  C   VAL A 362      32.952  16.441  19.644  1.00 25.10           C  
ANISOU 1411  C   VAL A 362     3240   3101   3196    -19   -128    185       C  
ATOM   1412  O   VAL A 362      32.369  17.462  19.969  1.00 17.12           O  
ANISOU 1412  O   VAL A 362     2236   2094   2173    -22   -121    181       O  
ATOM   1413  CB  VAL A 362      35.066  17.459  18.808  1.00 22.60           C  
ANISOU 1413  CB  VAL A 362     2917   2783   2888    -23   -124    164       C  
ATOM   1414  CG1 VAL A 362      35.859  16.999  20.019  1.00 23.27           C  
ANISOU 1414  CG1 VAL A 362     2993   2879   2971    -25   -138    168       C  
ATOM   1415  CG2 VAL A 362      35.973  17.660  17.599  1.00 25.73           C  
ANISOU 1415  CG2 VAL A 362     3309   3170   3296    -23   -118    153       C  
ATOM   1416  N   ASP A 363      32.777  15.281  20.271  1.00 20.38           N  
ANISOU 1416  N   ASP A 363     2639   2504   2602    -16   -136    198       N  
ATOM   1417  CA  ASP A 363      31.799  15.124  21.345  1.00 22.30           C  
ANISOU 1417  CA  ASP A 363     2887   2753   2835    -17   -136    209       C  
ATOM   1418  C   ASP A 363      31.975  16.210  22.401  1.00 22.74           C  
ANISOU 1418  C   ASP A 363     2948   2822   2872    -23   -136    205       C  
ATOM   1419  O   ASP A 363      33.090  16.486  22.850  1.00 22.35           O  
ANISOU 1419  O   ASP A 363     2893   2781   2819    -25   -143    200       O  
ATOM   1420  CB  ASP A 363      31.951  13.751  22.019  1.00 27.85           C  
ANISOU 1420  CB  ASP A 363     3585   3454   3543    -12   -144    225       C  
ATOM   1421  CG  ASP A 363      31.688  12.584  21.064  1.00 32.25           C  
ANISOU 1421  CG  ASP A 363     4136   3996   4122     -7   -141    228       C  
ATOM   1422  OD1 ASP A 363      31.702  12.773  19.818  1.00 24.17           O  
ANISOU 1422  OD1 ASP A 363     3110   2967   3108     -7   -137    215       O  
ATOM   1423  OD2 ASP A 363      31.471  11.461  21.568  1.00 34.15           O  
ANISOU 1423  OD2 ASP A 363     4374   4231   4370     -4   -142    242       O  
ATOM   1424  N   HIS A 364      30.873  16.819  22.814  1.00 16.87           N  
ANISOU 1424  N   HIS A 364     2212   2081   2117    -26   -129    205       N  
ATOM   1425  CA  HIS A 364      30.899  17.766  23.932  1.00 15.66           C  
ANISOU 1425  CA  HIS A 364     2063   1941   1947    -33   -128    200       C  
ATOM   1426  C   HIS A 364      30.777  16.989  25.247  1.00 23.38           C  
ANISOU 1426  C   HIS A 364     3040   2928   2913    -32   -136    215       C  
ATOM   1427  O   HIS A 364      29.670  16.670  25.690  1.00 18.04           O  
ANISOU 1427  O   HIS A 364     2371   2251   2234    -32   -131    224       O  
ATOM   1428  CB  HIS A 364      29.759  18.774  23.780  1.00 13.58           C  
ANISOU 1428  CB  HIS A 364     1807   1674   1678    -37   -115    193       C  
ATOM   1429  CG  HIS A 364      29.971  19.740  22.666  1.00 14.00           C  
ANISOU 1429  CG  HIS A 364     1863   1720   1738    -37   -106    180       C  
ATOM   1430  ND1 HIS A 364      29.077  19.905  21.618  1.00 14.81           N  
ANISOU 1430  ND1 HIS A 364     1970   1812   1847    -31    -97    179       N  
ATOM   1431  CD2 HIS A 364      30.988  20.606  22.409  1.00 18.85           C  
ANISOU 1431  CD2 HIS A 364     2474   2334   2353    -41   -102    168       C  
ATOM   1432  CE1 HIS A 364      29.531  20.816  20.788  1.00 18.22           C  
ANISOU 1432  CE1 HIS A 364     2403   2238   2281    -30    -89    170       C  
ATOM   1433  NE2 HIS A 364      30.692  21.262  21.245  1.00 16.41           N  
ANISOU 1433  NE2 HIS A 364     2171   2014   2051    -37    -90    162       N  
ATOM   1434  N   LYS A 365      31.921  16.656  25.837  1.00 20.67           N  
ANISOU 1434  N   LYS A 365     2690   2597   2566    -29   -147    218       N  
ATOM   1435  CA  LYS A 365      31.966  15.888  27.078  1.00 25.42           C  
ANISOU 1435  CA  LYS A 365     3292   3211   3155    -25   -156    235       C  
ATOM   1436  C   LYS A 365      32.744  16.680  28.109  1.00 24.27           C  
ANISOU 1436  C   LYS A 365     3143   3089   2990    -29   -163    226       C  
ATOM   1437  O   LYS A 365      33.694  17.378  27.771  1.00 21.72           O  
ANISOU 1437  O   LYS A 365     2813   2771   2671    -32   -166    208       O  
ATOM   1438  CB  LYS A 365      32.626  14.528  26.857  1.00 30.61           C  
ANISOU 1438  CB  LYS A 365     3942   3862   3825    -14   -165    250       C  
ATOM   1439  CG  LYS A 365      32.105  13.785  25.639  1.00 38.01           C  
ANISOU 1439  CG  LYS A 365     4879   4776   4786    -12   -157    253       C  
ATOM   1440  CD  LYS A 365      32.121  12.279  25.847  1.00 45.95           C  
ANISOU 1440  CD  LYS A 365     5883   5774   5804     -2   -160    274       C  
ATOM   1441  CE  LYS A 365      30.830  11.833  26.538  1.00 52.94           C  
ANISOU 1441  CE  LYS A 365     6778   6655   6684     -3   -150    287       C  
ATOM   1442  NZ  LYS A 365      30.678  10.350  26.623  1.00 62.49           N  
ANISOU 1442  NZ  LYS A 365     7984   7849   7908      6   -146    307       N  
ATOM   1443  N   PRO A 366      32.332  16.588  29.377  1.00 25.16           N  
ANISOU 1443  N   PRO A 366     3261   3218   3082    -28   -165    235       N  
ATOM   1444  CA  PRO A 366      32.893  17.381  30.469  1.00 22.02           C  
ANISOU 1444  CA  PRO A 366     2859   2846   2662    -32   -172    224       C  
ATOM   1445  C   PRO A 366      34.377  17.117  30.725  1.00 22.06           C  
ANISOU 1445  C   PRO A 366     2851   2867   2664    -26   -189    220       C  
ATOM   1446  O   PRO A 366      35.027  17.952  31.349  1.00 29.02           O  
ANISOU 1446  O   PRO A 366     3724   3770   3531    -31   -194    202       O  
ATOM   1447  CB  PRO A 366      32.076  16.923  31.680  1.00 26.04           C  
ANISOU 1447  CB  PRO A 366     3377   3366   3150    -30   -171    242       C  
ATOM   1448  CG  PRO A 366      30.816  16.411  31.105  1.00 23.90           C  
ANISOU 1448  CG  PRO A 366     3116   3071   2893    -30   -158    254       C  
ATOM   1449  CD  PRO A 366      31.191  15.776  29.825  1.00 25.70           C  
ANISOU 1449  CD  PRO A 366     3338   3278   3147    -25   -159    256       C  
ATOM   1450  N   ASP A 367      34.911  15.977  30.303  1.00 19.87           N  
ANISOU 1450  N   ASP A 367     2569   2582   2400    -14   -197    236       N  
ATOM   1451  CA  ASP A 367      36.346  15.770  30.522  1.00 30.85           C  
ANISOU 1451  CA  ASP A 367     3945   3988   3789     -7   -214    231       C  
ATOM   1452  C   ASP A 367      37.246  16.438  29.469  1.00 24.29           C  
ANISOU 1452  C   ASP A 367     3104   3149   2978    -14   -212    206       C  
ATOM   1453  O   ASP A 367      38.462  16.343  29.563  1.00 24.08           O  
ANISOU 1453  O   ASP A 367     3063   3135   2953     -9   -225    197       O  
ATOM   1454  CB  ASP A 367      36.705  14.295  30.709  1.00 29.36           C  
ANISOU 1454  CB  ASP A 367     3754   3797   3605     11   -225    258       C  
ATOM   1455  CG  ASP A 367      36.081  13.420  29.672  1.00 41.05           C  
ANISOU 1455  CG  ASP A 367     5240   5246   5110     13   -214    272       C  
ATOM   1456  OD1 ASP A 367      35.730  13.954  28.592  1.00 46.87           O  
ANISOU 1456  OD1 ASP A 367     5979   5966   5864      3   -203    256       O  
ATOM   1457  OD2 ASP A 367      35.928  12.209  29.942  1.00 46.98           O  
ANISOU 1457  OD2 ASP A 367     5994   5991   5866     25   -216    297       O  
ATOM   1458  N   ARG A 368      36.651  17.096  28.473  1.00 17.73           N  
ANISOU 1458  N   ARG A 368     2278   2297   2160    -24   -196    195       N  
ATOM   1459  CA  ARG A 368      37.414  18.005  27.611  1.00 16.25           C  
ANISOU 1459  CA  ARG A 368     2084   2104   1988    -32   -190    169       C  
ATOM   1460  C   ARG A 368      37.857  19.178  28.476  1.00 20.61           C  
ANISOU 1460  C   ARG A 368     2629   2678   2524    -41   -190    146       C  
ATOM   1461  O   ARG A 368      37.045  19.747  29.204  1.00 18.21           O  
ANISOU 1461  O   ARG A 368     2333   2383   2204    -47   -184    145       O  
ATOM   1462  CB  ARG A 368      36.542  18.516  26.464  1.00 16.35           C  
ANISOU 1462  CB  ARG A 368     2106   2092   2013    -38   -172    166       C  
ATOM   1463  CG  ARG A 368      36.613  17.670  25.212  1.00 26.69           C  
ANISOU 1463  CG  ARG A 368     3417   3381   3345    -32   -170    174       C  
ATOM   1464  CD  ARG A 368      35.625  18.109  24.151  1.00 24.98           C  
ANISOU 1464  CD  ARG A 368     3210   3145   3136    -35   -154    172       C  
ATOM   1465  NE  ARG A 368      35.743  19.527  23.822  1.00 22.41           N  
ANISOU 1465  NE  ARG A 368     2887   2818   2811    -44   -140    152       N  
ATOM   1466  CZ  ARG A 368      35.077  20.113  22.830  1.00 25.15           C  
ANISOU 1466  CZ  ARG A 368     3243   3150   3164    -45   -125    149       C  
ATOM   1467  NH1 ARG A 368      34.243  19.412  22.062  1.00 22.42           N  
ANISOU 1467  NH1 ARG A 368     2903   2792   2825    -39   -124    161       N  
ATOM   1468  NH2 ARG A 368      35.248  21.403  22.598  1.00 25.66           N  
ANISOU 1468  NH2 ARG A 368     3309   3210   3229    -52   -111    133       N  
ATOM   1469  N   GLU A 369      39.133  19.535  28.399  1.00 18.93           N  
ANISOU 1469  N   GLU A 369     2402   2475   2318    -43   -196    126       N  
ATOM   1470  CA  GLU A 369      39.703  20.535  29.301  1.00 20.07           C  
ANISOU 1470  CA  GLU A 369     2535   2644   2448    -52   -198    100       C  
ATOM   1471  C   GLU A 369      39.037  21.873  29.142  1.00 24.79           C  
ANISOU 1471  C   GLU A 369     3140   3232   3047    -67   -176     82       C  
ATOM   1472  O   GLU A 369      38.757  22.536  30.136  1.00 26.94           O  
ANISOU 1472  O   GLU A 369     3411   3524   3302    -74   -175     71       O  
ATOM   1473  CB  GLU A 369      41.220  20.674  29.107  1.00 27.21           C  
ANISOU 1473  CB  GLU A 369     3419   3557   3364    -52   -206     78       C  
ATOM   1474  CG  GLU A 369      42.023  19.392  29.393  1.00 34.38           C  
ANISOU 1474  CG  GLU A 369     4316   4476   4269    -36   -229     94       C  
ATOM   1475  CD  GLU A 369      41.886  18.873  30.837  1.00 38.64           C  
ANISOU 1475  CD  GLU A 369     4855   5048   4779    -25   -248    108       C  
ATOM   1476  OE1 GLU A 369      41.312  19.580  31.699  1.00 42.51           O  
ANISOU 1476  OE1 GLU A 369     5349   5555   5249    -32   -244    101       O  
ATOM   1477  OE2 GLU A 369      42.356  17.744  31.104  1.00 41.37           O  
ANISOU 1477  OE2 GLU A 369     5196   5402   5123     -8   -265    128       O  
ATOM   1478  N   ASP A 370      38.781  22.278  27.897  1.00 23.55           N  
ANISOU 1478  N   ASP A 370     2990   3048   2911    -71   -158     80       N  
ATOM   1479  CA  ASP A 370      38.034  23.512  27.670  1.00 22.98           C  
ANISOU 1479  CA  ASP A 370     2926   2963   2841    -83   -136     67       C  
ATOM   1480  C   ASP A 370      36.642  23.490  28.352  1.00 19.41           C  
ANISOU 1480  C   ASP A 370     2488   2515   2372    -82   -134     83       C  
ATOM   1481  O   ASP A 370      36.260  24.444  29.036  1.00 23.77           O  
ANISOU 1481  O   ASP A 370     3042   3076   2915    -92   -124     68       O  
ATOM   1482  CB  ASP A 370      37.981  23.906  26.171  1.00 22.26           C  
ANISOU 1482  CB  ASP A 370     2843   2843   2773    -84   -117     65       C  
ATOM   1483  CG  ASP A 370      37.320  22.837  25.262  1.00 25.76           C  
ANISOU 1483  CG  ASP A 370     3296   3269   3222    -72   -121     92       C  
ATOM   1484  OD1 ASP A 370      37.217  21.650  25.638  1.00 23.23           O  
ANISOU 1484  OD1 ASP A 370     2974   2955   2895    -63   -139    110       O  
ATOM   1485  OD2 ASP A 370      36.910  23.196  24.131  1.00 24.80           O  
ANISOU 1485  OD2 ASP A 370     3184   3126   3113    -71   -106     93       O  
ATOM   1486  N   GLU A 371      35.906  22.396  28.199  1.00 21.01           N  
ANISOU 1486  N   GLU A 371     2700   2711   2571    -72   -141    110       N  
ATOM   1487  CA  GLU A 371      34.576  22.292  28.801  1.00 19.88           C  
ANISOU 1487  CA  GLU A 371     2569   2569   2414    -72   -138    124       C  
ATOM   1488  C   GLU A 371      34.629  22.236  30.327  1.00 23.77           C  
ANISOU 1488  C   GLU A 371     3059   3091   2883    -74   -148    123       C  
ATOM   1489  O   GLU A 371      33.820  22.869  31.014  1.00 18.90           O  
ANISOU 1489  O   GLU A 371     2447   2481   2253    -81   -140    119       O  
ATOM   1490  CB  GLU A 371      33.823  21.090  28.239  1.00 17.68           C  
ANISOU 1490  CB  GLU A 371     2299   2275   2142    -62   -141    150       C  
ATOM   1491  CG  GLU A 371      33.456  21.275  26.773  1.00 24.98           C  
ANISOU 1491  CG  GLU A 371     3229   3174   3087    -60   -129    149       C  
ATOM   1492  CD  GLU A 371      32.456  22.417  26.578  1.00 26.06           C  
ANISOU 1492  CD  GLU A 371     3376   3303   3224    -67   -110    141       C  
ATOM   1493  OE1 GLU A 371      32.896  23.584  26.460  1.00 26.26           O  
ANISOU 1493  OE1 GLU A 371     3398   3326   3252    -75    -99    122       O  
ATOM   1494  OE2 GLU A 371      31.231  22.139  26.561  1.00 16.01           O  
ANISOU 1494  OE2 GLU A 371     2111   2022   1948    -65   -106    153       O  
ATOM   1495  N   TYR A 372      35.579  21.475  30.850  1.00 17.88           N  
ANISOU 1495  N   TYR A 372     2302   2363   2129    -65   -167    128       N  
ATOM   1496  CA  TYR A 372      35.751  21.371  32.292  1.00 18.47           C  
ANISOU 1496  CA  TYR A 372     2373   2470   2176    -64   -180    128       C  
ATOM   1497  C   TYR A 372      35.955  22.762  32.893  1.00 21.22           C  
ANISOU 1497  C   TYR A 372     2714   2834   2516    -78   -171     96       C  
ATOM   1498  O   TYR A 372      35.296  23.129  33.868  1.00 20.14           O  
ANISOU 1498  O   TYR A 372     2581   2713   2359    -84   -168     94       O  
ATOM   1499  CB  TYR A 372      36.955  20.477  32.607  1.00 20.45           C  
ANISOU 1499  CB  TYR A 372     2610   2738   2422    -51   -202    135       C  
ATOM   1500  CG  TYR A 372      37.158  20.203  34.087  1.00 25.16           C  
ANISOU 1500  CG  TYR A 372     3202   3370   2986    -44   -217    139       C  
ATOM   1501  CD1 TYR A 372      36.648  19.051  34.673  1.00 32.52           C  
ANISOU 1501  CD1 TYR A 372     4146   4307   3905    -30   -225    173       C  
ATOM   1502  CD2 TYR A 372      37.858  21.096  34.893  1.00 29.85           C  
ANISOU 1502  CD2 TYR A 372     3782   3994   3564    -51   -222    110       C  
ATOM   1503  CE1 TYR A 372      36.826  18.789  36.022  1.00 37.71           C  
ANISOU 1503  CE1 TYR A 372     4800   4998   4529    -22   -238    180       C  
ATOM   1504  CE2 TYR A 372      38.041  20.850  36.243  1.00 37.72           C  
ANISOU 1504  CE2 TYR A 372     4775   5028   4529    -44   -238    114       C  
ATOM   1505  CZ  TYR A 372      37.527  19.689  36.802  1.00 39.96           C  
ANISOU 1505  CZ  TYR A 372     5071   5315   4795    -28   -246    151       C  
ATOM   1506  OH  TYR A 372      37.705  19.422  38.137  1.00 51.27           O  
ANISOU 1506  OH  TYR A 372     6501   6785   6193    -18   -260    157       O  
ATOM   1507  N   ALA A 373      36.866  23.535  32.297  1.00 22.81           N  
ANISOU 1507  N   ALA A 373     2903   3031   2734    -86   -165     70       N  
ATOM   1508  CA  ALA A 373      37.171  24.876  32.776  1.00 21.36           C  
ANISOU 1508  CA  ALA A 373     2710   2860   2548   -101   -154     36       C  
ATOM   1509  C   ALA A 373      35.997  25.828  32.588  1.00 25.00           C  
ANISOU 1509  C   ALA A 373     3183   3302   3013   -112   -130     32       C  
ATOM   1510  O   ALA A 373      35.741  26.680  33.435  1.00 26.43           O  
ANISOU 1510  O   ALA A 373     3361   3499   3183   -123   -122     13       O  
ATOM   1511  CB  ALA A 373      38.416  25.410  32.091  1.00 21.94           C  
ANISOU 1511  CB  ALA A 373     2768   2928   2642   -107   -150     10       C  
ATOM   1512  N   ARG A 374      35.281  25.697  31.478  1.00 25.67           N  
ANISOU 1512  N   ARG A 374     3281   3356   3116   -109   -118     48       N  
ATOM   1513  CA  ARG A 374      34.121  26.553  31.273  1.00 24.01           C  
ANISOU 1513  CA  ARG A 374     3083   3129   2911   -117    -97     46       C  
ATOM   1514  C   ARG A 374      33.129  26.299  32.406  1.00 25.08           C  
ANISOU 1514  C   ARG A 374     3225   3280   3022   -117   -101     57       C  
ATOM   1515  O   ARG A 374      32.650  27.217  33.046  1.00 25.00           O  
ANISOU 1515  O   ARG A 374     3216   3277   3006   -128    -89     41       O  
ATOM   1516  CB  ARG A 374      33.452  26.296  29.916  1.00 27.82           C  
ANISOU 1516  CB  ARG A 374     3578   3579   3412   -109    -87     64       C  
ATOM   1517  CG  ARG A 374      32.245  27.219  29.655  1.00 27.01           C  
ANISOU 1517  CG  ARG A 374     3487   3460   3315   -115    -66     62       C  
ATOM   1518  CD  ARG A 374      31.551  26.928  28.323  1.00 22.23           C  
ANISOU 1518  CD  ARG A 374     2893   2828   2724   -105    -59     80       C  
ATOM   1519  NE  ARG A 374      31.184  25.513  28.154  1.00 22.79           N  
ANISOU 1519  NE  ARG A 374     2969   2900   2792    -93    -75    104       N  
ATOM   1520  CZ  ARG A 374      30.152  24.927  28.748  1.00 21.42           C  
ANISOU 1520  CZ  ARG A 374     2802   2731   2607    -91    -80    119       C  
ATOM   1521  NH1 ARG A 374      29.898  23.637  28.526  1.00 14.54           N  
ANISOU 1521  NH1 ARG A 374     1933   1857   1736    -81    -92    140       N  
ATOM   1522  NH2 ARG A 374      29.372  25.633  29.568  1.00 16.72           N  
ANISOU 1522  NH2 ARG A 374     2210   2141   2001    -99    -70    112       N  
ATOM   1523  N   ILE A 375      32.848  25.033  32.667  1.00 26.06           N  
ANISOU 1523  N   ILE A 375     3355   3410   3135   -106   -117     83       N  
ATOM   1524  CA  ILE A 375      31.880  24.665  33.692  1.00 24.07           C  
ANISOU 1524  CA  ILE A 375     3113   3171   2862   -105   -119     97       C  
ATOM   1525  C   ILE A 375      32.308  25.084  35.100  1.00 28.59           C  
ANISOU 1525  C   ILE A 375     3676   3778   3408   -111   -126     81       C  
ATOM   1526  O   ILE A 375      31.547  25.730  35.821  1.00 24.33           O  
ANISOU 1526  O   ILE A 375     3141   3247   2858   -121   -115     72       O  
ATOM   1527  CB  ILE A 375      31.612  23.171  33.649  1.00 16.85           C  
ANISOU 1527  CB  ILE A 375     2205   2253   1943    -90   -133    130       C  
ATOM   1528  CG1 ILE A 375      30.846  22.832  32.365  1.00 20.46           C  
ANISOU 1528  CG1 ILE A 375     2672   2678   2424    -86   -123    143       C  
ATOM   1529  CG2 ILE A 375      30.834  22.721  34.884  1.00 19.95           C  
ANISOU 1529  CG2 ILE A 375     2607   2664   2312    -89   -135    144       C  
ATOM   1530  CD1 ILE A 375      30.874  21.364  32.023  1.00 12.31           C  
ANISOU 1530  CD1 ILE A 375     1642   1638   1396    -72   -134    170       C  
ATOM   1531  N   GLU A 376      33.528  24.715  35.482  1.00 28.79           N  
ANISOU 1531  N   GLU A 376     3687   3826   3424   -106   -144     75       N  
ATOM   1532  CA  GLU A 376      34.045  25.036  36.808  1.00 32.14           C  
ANISOU 1532  CA  GLU A 376     4101   4289   3822   -109   -154     58       C  
ATOM   1533  C   GLU A 376      34.164  26.541  37.045  1.00 37.71           C  
ANISOU 1533  C   GLU A 376     4797   5000   4532   -128   -137     19       C  
ATOM   1534  O   GLU A 376      33.861  27.013  38.141  1.00 35.83           O  
ANISOU 1534  O   GLU A 376     4556   4786   4271   -136   -135      6       O  
ATOM   1535  CB  GLU A 376      35.378  24.325  37.061  1.00 36.63           C  
ANISOU 1535  CB  GLU A 376     4655   4881   4381    -97   -178     58       C  
ATOM   1536  CG  GLU A 376      35.260  22.781  37.063  1.00 41.93           C  
ANISOU 1536  CG  GLU A 376     5336   5550   5045    -77   -193     98       C  
ATOM   1537  CD  GLU A 376      35.017  22.192  38.462  1.00 56.05           C  
ANISOU 1537  CD  GLU A 376     7128   7371   6796    -68   -206    115       C  
ATOM   1538  OE1 GLU A 376      34.444  21.070  38.572  1.00 44.61           O  
ANISOU 1538  OE1 GLU A 376     5693   5914   5342    -55   -209    150       O  
ATOM   1539  OE2 GLU A 376      35.417  22.851  39.452  1.00 62.21           O  
ANISOU 1539  OE2 GLU A 376     7898   8186   7554    -73   -211     91       O  
ATOM   1540  N   ASN A 377      34.582  27.289  36.020  1.00 35.48           N  
ANISOU 1540  N   ASN A 377     4509   4695   4278   -136   -123      1       N  
ATOM   1541  CA  ASN A 377      34.676  28.749  36.117  1.00 37.38           C  
ANISOU 1541  CA  ASN A 377     4741   4934   4530   -154   -102    -36       C  
ATOM   1542  C   ASN A 377      33.305  29.424  36.238  1.00 39.89           C  
ANISOU 1542  C   ASN A 377     5072   5235   4848   -163    -81    -34       C  
ATOM   1543  O   ASN A 377      33.190  30.555  36.730  1.00 34.32           O  
ANISOU 1543  O   ASN A 377     4360   4536   4145   -178    -64    -63       O  
ATOM   1544  CB  ASN A 377      35.428  29.351  34.918  1.00 37.11           C  
ANISOU 1544  CB  ASN A 377     4700   4874   4528   -158    -89    -52       C  
ATOM   1545  CG  ASN A 377      36.868  28.859  34.806  1.00 48.57           C  
ANISOU 1545  CG  ASN A 377     6134   6340   5981   -152   -107    -61       C  
ATOM   1546  OD1 ASN A 377      37.462  28.370  35.772  1.00 47.00           O  
ANISOU 1546  OD1 ASN A 377     5924   6176   5759   -147   -129    -66       O  
ATOM   1547  ND2 ASN A 377      37.438  28.997  33.611  1.00 47.64           N  
ANISOU 1547  ND2 ASN A 377     6014   6196   5890   -151    -98    -65       N  
ATOM   1548  N   ALA A 378      32.265  28.736  35.781  1.00 32.15           N  
ANISOU 1548  N   ALA A 378     4110   4236   3871   -154    -80     -2       N  
ATOM   1549  CA  ALA A 378      30.913  29.272  35.901  1.00 27.99           C  
ANISOU 1549  CA  ALA A 378     3595   3695   3345   -160    -62      1       C  
ATOM   1550  C   ALA A 378      30.294  28.886  37.242  1.00 31.49           C  
ANISOU 1550  C   ALA A 378     4042   4164   3757   -161    -70      8       C  
ATOM   1551  O   ALA A 378      29.161  29.258  37.543  1.00 36.88           O  
ANISOU 1551  O   ALA A 378     4734   4840   4438   -168    -56     10       O  
ATOM   1552  CB  ALA A 378      30.043  28.800  34.747  1.00 31.16           C  
ANISOU 1552  CB  ALA A 378     4012   4063   3765   -150    -56     28       C  
ATOM   1553  N   GLY A 379      31.034  28.137  38.048  1.00 29.67           N  
ANISOU 1553  N   GLY A 379     3805   3965   3503   -154    -91     12       N  
ATOM   1554  CA  GLY A 379      30.559  27.773  39.373  1.00 28.31           C  
ANISOU 1554  CA  GLY A 379     3637   3822   3298   -154    -98     19       C  
ATOM   1555  C   GLY A 379      29.931  26.395  39.461  1.00 33.73           C  
ANISOU 1555  C   GLY A 379     4338   4504   3972   -139   -109     59       C  
ATOM   1556  O   GLY A 379      29.351  26.044  40.494  1.00 28.73           O  
ANISOU 1556  O   GLY A 379     3713   3890   3314   -138   -111     70       O  
ATOM   1557  N   GLY A 380      30.041  25.615  38.387  1.00 29.91           N  
ANISOU 1557  N   GLY A 380     3860   3996   3509   -127   -114     81       N  
ATOM   1558  CA  GLY A 380      29.512  24.258  38.361  1.00 26.22           C  
ANISOU 1558  CA  GLY A 380     3405   3520   3036   -113   -122    117       C  
ATOM   1559  C   GLY A 380      30.502  23.180  38.767  1.00 27.12           C  
ANISOU 1559  C   GLY A 380     3514   3656   3135    -97   -144    134       C  
ATOM   1560  O   GLY A 380      31.681  23.460  39.006  1.00 33.00           O  
ANISOU 1560  O   GLY A 380     4244   4422   3872    -96   -157    116       O  
ATOM   1561  N   LYS A 381      30.025  21.938  38.827  1.00 25.78           N  
ANISOU 1561  N   LYS A 381     3357   3479   2962    -84   -148    168       N  
ATOM   1562  CA  LYS A 381      30.850  20.818  39.238  1.00 29.16           C  
ANISOU 1562  CA  LYS A 381     3782   3924   3375    -67   -168    189       C  
ATOM   1563  C   LYS A 381      30.860  19.748  38.166  1.00 22.48           C  
ANISOU 1563  C   LYS A 381     2939   3047   2554    -55   -170    213       C  
ATOM   1564  O   LYS A 381      29.831  19.410  37.599  1.00 27.87           O  
ANISOU 1564  O   LYS A 381     3634   3703   3254    -57   -156    226       O  
ATOM   1565  CB  LYS A 381      30.321  20.205  40.536  1.00 25.31           C  
ANISOU 1565  CB  LYS A 381     3306   3458   2855    -59   -169    210       C  
ATOM   1566  CG  LYS A 381      30.287  21.175  41.694  1.00 30.09           C  
ANISOU 1566  CG  LYS A 381     3906   4096   3430    -70   -168    187       C  
ATOM   1567  CD  LYS A 381      31.665  21.767  41.911  1.00 47.24           C  
ANISOU 1567  CD  LYS A 381     6058   6299   5594    -70   -184    159       C  
ATOM   1568  CE  LYS A 381      31.661  22.815  43.015  1.00 51.42           C  
ANISOU 1568  CE  LYS A 381     6580   6862   6095    -83   -182    130       C  
ATOM   1569  NZ  LYS A 381      33.039  23.300  43.306  1.00 65.08           N  
ANISOU 1569  NZ  LYS A 381     8287   8624   7815    -82   -199    101       N  
ATOM   1570  N   VAL A 382      32.027  19.216  37.880  1.00 24.80           N  
ANISOU 1570  N   VAL A 382     3223   3347   2852    -44   -186    217       N  
ATOM   1571  CA  VAL A 382      32.102  18.054  37.034  1.00 21.08           C  
ANISOU 1571  CA  VAL A 382     2756   2852   2403    -31   -189    241       C  
ATOM   1572  C   VAL A 382      32.456  16.911  37.955  1.00 26.56           C  
ANISOU 1572  C   VAL A 382     3451   3563   3075    -13   -202    270       C  
ATOM   1573  O   VAL A 382      33.438  16.979  38.687  1.00 27.73           O  
ANISOU 1573  O   VAL A 382     3590   3744   3202     -5   -219    265       O  
ATOM   1574  CB  VAL A 382      33.171  18.225  35.971  1.00 27.42           C  
ANISOU 1574  CB  VAL A 382     3544   3645   3229    -31   -197    226       C  
ATOM   1575  CG1 VAL A 382      33.376  16.915  35.208  1.00 23.53           C  
ANISOU 1575  CG1 VAL A 382     3052   3130   2756    -17   -201    251       C  
ATOM   1576  CG2 VAL A 382      32.792  19.370  35.038  1.00 22.91           C  
ANISOU 1576  CG2 VAL A 382     2972   3054   2678    -47   -182    200       C  
ATOM   1577  N   ILE A 383      31.647  15.864  37.929  1.00 26.08           N  
ANISOU 1577  N   ILE A 383     3405   3484   3022     -5   -193    300       N  
ATOM   1578  CA  ILE A 383      31.789  14.789  38.888  1.00 25.56           C  
ANISOU 1578  CA  ILE A 383     3345   3433   2934     13   -199    331       C  
ATOM   1579  C   ILE A 383      31.892  13.441  38.206  1.00 28.55           C  
ANISOU 1579  C   ILE A 383     3727   3785   3338     28   -198    359       C  
ATOM   1580  O   ILE A 383      31.146  13.151  37.281  1.00 23.40           O  
ANISOU 1580  O   ILE A 383     3079   3099   2714     21   -184    361       O  
ATOM   1581  CB  ILE A 383      30.595  14.761  39.836  1.00 27.62           C  
ANISOU 1581  CB  ILE A 383     3623   3698   3175     10   -184    344       C  
ATOM   1582  CG1 ILE A 383      30.473  16.104  40.553  1.00 22.75           C  
ANISOU 1582  CG1 ILE A 383     3002   3107   2533     -5   -184    315       C  
ATOM   1583  CG2 ILE A 383      30.739  13.621  40.820  1.00 32.97           C  
ANISOU 1583  CG2 ILE A 383     4310   4389   3830     31   -188    381       C  
ATOM   1584  CD1 ILE A 383      29.188  16.251  41.336  1.00 30.93           C  
ANISOU 1584  CD1 ILE A 383     4054   4144   3553    -13   -166    322       C  
ATOM   1585  N   GLN A 384      32.823  12.618  38.670  1.00 34.73           N  
ANISOU 1585  N   GLN A 384     4505   4582   4110     48   -214    379       N  
ATOM   1586  CA  GLN A 384      32.981  11.278  38.130  1.00 36.70           C  
ANISOU 1586  CA  GLN A 384     4755   4806   4383     63   -212    407       C  
ATOM   1587  C   GLN A 384      31.920  10.358  38.697  1.00 36.24           C  
ANISOU 1587  C   GLN A 384     4715   4734   4321     69   -193    439       C  
ATOM   1588  O   GLN A 384      31.925  10.042  39.892  1.00 38.93           O  
ANISOU 1588  O   GLN A 384     5065   5097   4631     82   -195    461       O  
ATOM   1589  CB  GLN A 384      34.379  10.742  38.428  1.00 40.86           C  
ANISOU 1589  CB  GLN A 384     5270   5354   4900     83   -234    417       C  
ATOM   1590  CG  GLN A 384      35.374  11.071  37.336  1.00 45.62           C  
ANISOU 1590  CG  GLN A 384     5855   5951   5529     79   -246    393       C  
ATOM   1591  CD  GLN A 384      35.123  10.248  36.099  1.00 41.90           C  
ANISOU 1591  CD  GLN A 384     5384   5437   5097     78   -234    402       C  
ATOM   1592  OE1 GLN A 384      35.401  10.676  34.981  1.00 52.58           O  
ANISOU 1592  OE1 GLN A 384     6728   6775   6475     67   -234    379       O  
ATOM   1593  NE2 GLN A 384      34.593   9.048  36.296  1.00 47.19           N  
ANISOU 1593  NE2 GLN A 384     6065   6089   5775     90   -223    435       N  
ATOM   1594  N   TRP A 385      31.015   9.926  37.824  1.00 27.03           N  
ANISOU 1594  N   TRP A 385     3554   3529   3186     61   -174    442       N  
ATOM   1595  CA  TRP A 385      29.872   9.119  38.219  1.00 31.43           C  
ANISOU 1595  CA  TRP A 385     4127   4067   3747     63   -151    467       C  
ATOM   1596  C   TRP A 385      29.357   8.361  37.004  1.00 31.80           C  
ANISOU 1596  C   TRP A 385     4172   4073   3838     59   -136    469       C  
ATOM   1597  O   TRP A 385      28.439   8.819  36.318  1.00 30.96           O  
ANISOU 1597  O   TRP A 385     4066   3949   3748     42   -124    449       O  
ATOM   1598  CB  TRP A 385      28.765  10.023  38.761  1.00 30.49           C  
ANISOU 1598  CB  TRP A 385     4018   3955   3611     46   -138    453       C  
ATOM   1599  CG  TRP A 385      27.815   9.330  39.683  1.00 32.92           C  
ANISOU 1599  CG  TRP A 385     4343   4258   3907     51   -118    481       C  
ATOM   1600  CD1 TRP A 385      26.867   8.403  39.348  1.00 35.08           C  
ANISOU 1600  CD1 TRP A 385     4625   4497   4207     50    -95    497       C  
ATOM   1601  CD2 TRP A 385      27.705   9.524  41.097  1.00 27.82           C  
ANISOU 1601  CD2 TRP A 385     3708   3642   3220     57   -118    494       C  
ATOM   1602  NE1 TRP A 385      26.175   8.004  40.471  1.00 29.13           N  
ANISOU 1602  NE1 TRP A 385     3888   3748   3433     55    -78    520       N  
ATOM   1603  CE2 TRP A 385      26.675   8.681  41.557  1.00 28.27           C  
ANISOU 1603  CE2 TRP A 385     3782   3679   3281     60    -93    520       C  
ATOM   1604  CE3 TRP A 385      28.389  10.321  42.023  1.00 28.89           C  
ANISOU 1604  CE3 TRP A 385     3841   3820   3316     60   -137    484       C  
ATOM   1605  CZ2 TRP A 385      26.317   8.608  42.897  1.00 35.28           C  
ANISOU 1605  CZ2 TRP A 385     4685   4588   4133     66    -85    539       C  
ATOM   1606  CZ3 TRP A 385      28.024  10.259  43.360  1.00 32.32           C  
ANISOU 1606  CZ3 TRP A 385     4289   4278   3713     66   -130    502       C  
ATOM   1607  CH2 TRP A 385      27.001   9.408  43.782  1.00 34.10           C  
ANISOU 1607  CH2 TRP A 385     4533   4483   3942     70   -104    530       C  
ATOM   1608  N   GLN A 386      29.940   7.198  36.752  1.00 33.96           N  
ANISOU 1608  N   GLN A 386     4441   4332   4128     75   -137    491       N  
ATOM   1609  CA  GLN A 386      29.680   6.461  35.528  1.00 34.02           C  
ANISOU 1609  CA  GLN A 386     4443   4303   4178     72   -126    489       C  
ATOM   1610  C   GLN A 386      30.040   7.372  34.351  1.00 31.65           C  
ANISOU 1610  C   GLN A 386     4130   4003   3893     58   -137    453       C  
ATOM   1611  O   GLN A 386      29.230   7.606  33.454  1.00 27.21           O  
ANISOU 1611  O   GLN A 386     3567   3421   3352     44   -126    435       O  
ATOM   1612  CB  GLN A 386      28.221   5.999  35.466  1.00 37.94           C  
ANISOU 1612  CB  GLN A 386     4950   4773   4692     63    -98    494       C  
ATOM   1613  CG  GLN A 386      27.948   4.902  34.431  1.00 45.80           C  
ANISOU 1613  CG  GLN A 386     5939   5731   5731     63    -83    498       C  
ATOM   1614  CD  GLN A 386      26.458   4.681  34.172  1.00 55.57           C  
ANISOU 1614  CD  GLN A 386     7182   6944   6988     50    -56    491       C  
ATOM   1615  OE1 GLN A 386      25.991   4.768  33.027  1.00 48.30           O  
ANISOU 1615  OE1 GLN A 386     6252   6006   6095     39    -51    467       O  
ATOM   1616  NE2 GLN A 386      25.705   4.385  35.235  1.00 51.94           N  
ANISOU 1616  NE2 GLN A 386     6738   6484   6515     52    -38    511       N  
ATOM   1617  N   GLY A 387      31.269   7.888  34.384  1.00 30.80           N  
ANISOU 1617  N   GLY A 387     4013   3918   3773     63   -160    444       N  
ATOM   1618  CA  GLY A 387      31.765   8.841  33.405  1.00 30.17           C  
ANISOU 1618  CA  GLY A 387     3921   3841   3702     51   -170    412       C  
ATOM   1619  C   GLY A 387      31.704  10.240  33.990  1.00 31.62           C  
ANISOU 1619  C   GLY A 387     4106   4051   3857     40   -176    391       C  
ATOM   1620  O   GLY A 387      30.981  10.474  34.966  1.00 29.71           O  
ANISOU 1620  O   GLY A 387     3875   3821   3592     38   -169    398       O  
ATOM   1621  N   ALA A 388      32.445  11.176  33.399  1.00 28.10           N  
ANISOU 1621  N   ALA A 388     3649   3614   3413     33   -187    364       N  
ATOM   1622  CA  ALA A 388      32.432  12.557  33.875  1.00 30.28           C  
ANISOU 1622  CA  ALA A 388     3925   3913   3667     21   -191    340       C  
ATOM   1623  C   ALA A 388      31.081  13.177  33.554  1.00 26.46           C  
ANISOU 1623  C   ALA A 388     3450   3414   3189      5   -172    329       C  
ATOM   1624  O   ALA A 388      30.626  13.135  32.405  1.00 21.31           O  
ANISOU 1624  O   ALA A 388     2797   2737   2562      0   -163    321       O  
ATOM   1625  CB  ALA A 388      33.557  13.356  33.246  1.00 29.56           C  
ANISOU 1625  CB  ALA A 388     3819   3830   3581     16   -203    314       C  
ATOM   1626  N   ARG A 389      30.435  13.739  34.570  1.00 16.94           N  
ANISOU 1626  N   ARG A 389     2254   2225   1959      0   -167    328       N  
ATOM   1627  CA  ARG A 389      29.083  14.255  34.411  1.00 20.93           C  
ANISOU 1627  CA  ARG A 389     2767   2716   2468    -13   -149    320       C  
ATOM   1628  C   ARG A 389      28.917  15.623  35.037  1.00 20.07           C  
ANISOU 1628  C   ARG A 389     2660   2628   2339    -26   -148    298       C  
ATOM   1629  O   ARG A 389      29.487  15.914  36.081  1.00 20.10           O  
ANISOU 1629  O   ARG A 389     2662   2660   2315    -24   -157    297       O  
ATOM   1630  CB  ARG A 389      28.042  13.267  34.981  1.00 16.24           C  
ANISOU 1630  CB  ARG A 389     2185   2111   1873     -9   -135    345       C  
ATOM   1631  CG  ARG A 389      27.849  11.995  34.124  1.00 19.71           C  
ANISOU 1631  CG  ARG A 389     2624   2521   2343     -1   -128    361       C  
ATOM   1632  CD  ARG A 389      26.881  10.952  34.743  1.00 25.31           C  
ANISOU 1632  CD  ARG A 389     3345   3217   3054      4   -111    387       C  
ATOM   1633  NE  ARG A 389      26.862   9.729  33.923  1.00 23.91           N  
ANISOU 1633  NE  ARG A 389     3164   3013   2909     11   -105    399       N  
ATOM   1634  CZ  ARG A 389      25.905   9.398  33.057  1.00 28.70           C  
ANISOU 1634  CZ  ARG A 389     3769   3593   3543      4    -89    391       C  
ATOM   1635  NH1 ARG A 389      24.816  10.157  32.904  1.00 20.41           N  
ANISOU 1635  NH1 ARG A 389     2722   2540   2493     -9    -79    373       N  
ATOM   1636  NH2 ARG A 389      26.022   8.279  32.355  1.00 28.70           N  
ANISOU 1636  NH2 ARG A 389     3763   3570   3571     10    -84    400       N  
ATOM   1637  N   VAL A 390      28.119  16.466  34.397  1.00 19.65           N  
ANISOU 1637  N   VAL A 390     2608   2562   2298    -38   -136    280       N  
ATOM   1638  CA  VAL A 390      27.796  17.772  34.963  1.00 20.66           C  
ANISOU 1638  CA  VAL A 390     2736   2703   2409    -51   -130    259       C  
ATOM   1639  C   VAL A 390      26.935  17.575  36.228  1.00 21.93           C  
ANISOU 1639  C   VAL A 390     2909   2877   2548    -53   -122    271       C  
ATOM   1640  O   VAL A 390      25.826  17.060  36.151  1.00 22.34           O  
ANISOU 1640  O   VAL A 390     2969   2911   2608    -54   -109    283       O  
ATOM   1641  CB  VAL A 390      27.050  18.638  33.944  1.00 18.36           C  
ANISOU 1641  CB  VAL A 390     2445   2392   2138    -61   -117    241       C  
ATOM   1642  CG1 VAL A 390      26.683  19.979  34.554  1.00 21.71           C  
ANISOU 1642  CG1 VAL A 390     2871   2829   2549    -75   -109    220       C  
ATOM   1643  CG2 VAL A 390      27.915  18.840  32.690  1.00 18.23           C  
ANISOU 1643  CG2 VAL A 390     2420   2365   2142    -59   -124    230       C  
ATOM   1644  N   PHE A 391      27.458  17.977  37.382  1.00 23.94           N  
ANISOU 1644  N   PHE A 391     3161   3161   2772    -53   -130    267       N  
ATOM   1645  CA  PHE A 391      26.816  17.677  38.673  1.00 27.63           C  
ANISOU 1645  CA  PHE A 391     3640   3645   3214    -52   -124    282       C  
ATOM   1646  C   PHE A 391      26.501  16.190  38.880  1.00 28.50           C  
ANISOU 1646  C   PHE A 391     3759   3743   3325    -38   -120    317       C  
ATOM   1647  O   PHE A 391      25.614  15.826  39.666  1.00 28.65           O  
ANISOU 1647  O   PHE A 391     3791   3762   3332    -39   -107    331       O  
ATOM   1648  CB  PHE A 391      25.573  18.538  38.879  1.00 24.47           C  
ANISOU 1648  CB  PHE A 391     3246   3238   2813    -68   -105    267       C  
ATOM   1649  CG  PHE A 391      25.888  19.937  39.304  1.00 28.75           C  
ANISOU 1649  CG  PHE A 391     3781   3801   3342    -81   -106    237       C  
ATOM   1650  CD1 PHE A 391      26.093  20.240  40.646  1.00 29.50           C  
ANISOU 1650  CD1 PHE A 391     3877   3930   3402    -83   -110    233       C  
ATOM   1651  CD2 PHE A 391      26.015  20.945  38.367  1.00 29.24           C  
ANISOU 1651  CD2 PHE A 391     3835   3851   3425    -90   -103    212       C  
ATOM   1652  CE1 PHE A 391      26.404  21.527  41.046  1.00 30.72           C  
ANISOU 1652  CE1 PHE A 391     4022   4104   3546    -96   -109    202       C  
ATOM   1653  CE2 PHE A 391      26.321  22.241  38.760  1.00 32.30           C  
ANISOU 1653  CE2 PHE A 391     4214   4254   3802   -103   -100    183       C  
ATOM   1654  CZ  PHE A 391      26.520  22.530  40.103  1.00 29.84           C  
ANISOU 1654  CZ  PHE A 391     3903   3977   3460   -106   -104    176       C  
ATOM   1655  N   GLY A 392      27.251  15.331  38.193  1.00 25.86           N  
ANISOU 1655  N   GLY A 392     3420   3397   3008    -26   -130    330       N  
ATOM   1656  CA  GLY A 392      27.062  13.893  38.293  1.00 24.34           C  
ANISOU 1656  CA  GLY A 392     3235   3191   2823    -12   -126    362       C  
ATOM   1657  C   GLY A 392      25.878  13.375  37.502  1.00 25.25           C  
ANISOU 1657  C   GLY A 392     3356   3270   2968    -17   -106    367       C  
ATOM   1658  O   GLY A 392      25.672  12.167  37.396  1.00 24.89           O  
ANISOU 1658  O   GLY A 392     3314   3206   2936     -7    -99    390       O  
ATOM   1659  N   VAL A 393      25.123  14.291  36.908  1.00 20.56           N  
ANISOU 1659  N   VAL A 393     2760   2666   2386    -32    -98    343       N  
ATOM   1660  CA  VAL A 393      23.884  13.951  36.208  1.00 21.56           C  
ANISOU 1660  CA  VAL A 393     2889   2763   2538    -38    -80    342       C  
ATOM   1661  C   VAL A 393      24.074  13.662  34.718  1.00 22.59           C  
ANISOU 1661  C   VAL A 393     3010   2871   2701    -36    -83    333       C  
ATOM   1662  O   VAL A 393      23.845  12.538  34.266  1.00 25.96           O  
ANISOU 1662  O   VAL A 393     3436   3278   3148    -30    -76    347       O  
ATOM   1663  CB  VAL A 393      22.863  15.097  36.351  1.00 23.03           C  
ANISOU 1663  CB  VAL A 393     3078   2951   2720    -53    -68    320       C  
ATOM   1664  CG1 VAL A 393      21.569  14.776  35.609  1.00 20.91           C  
ANISOU 1664  CG1 VAL A 393     2811   2655   2478    -58    -51    316       C  
ATOM   1665  CG2 VAL A 393      22.603  15.384  37.820  1.00 28.61           C  
ANISOU 1665  CG2 VAL A 393     3795   3680   3395    -57    -63    326       C  
ATOM   1666  N   LEU A 394      24.479  14.688  33.965  1.00 22.79           N  
ANISOU 1666  N   LEU A 394     3028   2901   2731    -42    -91    310       N  
ATOM   1667  CA  LEU A 394      24.538  14.633  32.502  1.00 23.12           C  
ANISOU 1667  CA  LEU A 394     3061   2923   2800    -41    -92    299       C  
ATOM   1668  C   LEU A 394      25.949  14.376  31.975  1.00 20.85           C  
ANISOU 1668  C   LEU A 394     2765   2640   2518    -33   -108    301       C  
ATOM   1669  O   LEU A 394      26.900  15.038  32.388  1.00 22.16           O  
ANISOU 1669  O   LEU A 394     2927   2824   2667    -34   -120    293       O  
ATOM   1670  CB  LEU A 394      23.997  15.946  31.920  1.00 28.43           C  
ANISOU 1670  CB  LEU A 394     3732   3594   3476    -51    -87    275       C  
ATOM   1671  CG  LEU A 394      22.661  15.905  31.172  1.00 34.97           C  
ANISOU 1671  CG  LEU A 394     4561   4403   4324    -55    -74    267       C  
ATOM   1672  CD1 LEU A 394      21.702  14.869  31.741  1.00 29.60           C  
ANISOU 1672  CD1 LEU A 394     3886   3713   3647    -54    -61    282       C  
ATOM   1673  CD2 LEU A 394      22.015  17.273  31.116  1.00 29.17           C  
ANISOU 1673  CD2 LEU A 394     3827   3672   3583    -64    -67    247       C  
ATOM   1674  N   ALA A 395      26.065  13.420  31.055  1.00 16.22           N  
ANISOU 1674  N   ALA A 395     2174   2035   1956    -27   -108    307       N  
ATOM   1675  CA  ALA A 395      27.346  12.999  30.491  1.00 21.61           C  
ANISOU 1675  CA  ALA A 395     2847   2717   2647    -19   -122    309       C  
ATOM   1676  C   ALA A 395      27.810  13.884  29.326  1.00 19.72           C  
ANISOU 1676  C   ALA A 395     2601   2475   2418    -23   -126    286       C  
ATOM   1677  O   ALA A 395      28.919  13.720  28.813  1.00 21.36           O  
ANISOU 1677  O   ALA A 395     2800   2683   2632    -18   -137    284       O  
ATOM   1678  CB  ALA A 395      27.278  11.549  30.040  1.00 16.98           C  
ANISOU 1678  CB  ALA A 395     2258   2111   2084    -10   -117    326       C  
ATOM   1679  N   MET A 396      26.975  14.830  28.910  1.00 18.87           N  
ANISOU 1679  N   MET A 396     2496   2364   2311    -32   -118    270       N  
ATOM   1680  CA  MET A 396      27.376  15.794  27.888  1.00 21.55           C  
ANISOU 1680  CA  MET A 396     2831   2702   2657    -35   -119    251       C  
ATOM   1681  C   MET A 396      27.430  17.203  28.478  1.00 23.20           C  
ANISOU 1681  C   MET A 396     3042   2924   2847    -43   -117    236       C  
ATOM   1682  O   MET A 396      26.718  17.504  29.432  1.00 19.07           O  
ANISOU 1682  O   MET A 396     2526   2410   2311    -48   -111    238       O  
ATOM   1683  CB  MET A 396      26.450  15.736  26.668  1.00 20.50           C  
ANISOU 1683  CB  MET A 396     2697   2550   2542    -35   -110    243       C  
ATOM   1684  CG  MET A 396      25.065  16.311  26.883  1.00 15.27           C  
ANISOU 1684  CG  MET A 396     2040   1886   1875    -40    -98    237       C  
ATOM   1685  SD  MET A 396      24.006  15.232  27.860  1.00 51.37           S  
ANISOU 1685  SD  MET A 396     6617   6454   6447    -41    -90    253       S  
ATOM   1686  CE  MET A 396      23.881  13.807  26.779  1.00 17.61           C  
ANISOU 1686  CE  MET A 396     2334   2159   2199    -33    -88    258       C  
ATOM   1687  N   SER A 397      28.284  18.058  27.920  1.00 17.66           N  
ANISOU 1687  N   SER A 397     2336   2226   2149    -46   -120    221       N  
ATOM   1688  CA  SER A 397      28.466  19.396  28.467  1.00 14.47           C  
ANISOU 1688  CA  SER A 397     1933   1834   1732    -54   -116    205       C  
ATOM   1689  C   SER A 397      27.720  20.434  27.654  1.00 14.67           C  
ANISOU 1689  C   SER A 397     1961   1847   1765    -59   -102    192       C  
ATOM   1690  O   SER A 397      27.680  21.609  28.023  1.00 15.06           O  
ANISOU 1690  O   SER A 397     2013   1903   1807    -66    -95    178       O  
ATOM   1691  CB  SER A 397      29.956  19.735  28.541  1.00 20.17           C  
ANISOU 1691  CB  SER A 397     2645   2567   2451    -55   -126    195       C  
ATOM   1692  OG  SER A 397      30.557  19.602  27.270  1.00 21.47           O  
ANISOU 1692  OG  SER A 397     2805   2718   2633    -51   -126    191       O  
ATOM   1693  N   ARG A 398      27.122  20.004  26.545  1.00 13.26           N  
ANISOU 1693  N   ARG A 398     1784   1652   1601    -52    -99    196       N  
ATOM   1694  CA  ARG A 398      26.261  20.900  25.778  1.00 14.46           C  
ANISOU 1694  CA  ARG A 398     1940   1794   1759    -53    -87    186       C  
ATOM   1695  C   ARG A 398      25.057  20.148  25.277  1.00 15.51           C  
ANISOU 1695  C   ARG A 398     2075   1918   1901    -47    -84    193       C  
ATOM   1696  O   ARG A 398      25.141  18.946  25.036  1.00 14.57           O  
ANISOU 1696  O   ARG A 398     1952   1794   1790    -42    -90    203       O  
ATOM   1697  CB  ARG A 398      27.001  21.494  24.576  1.00 13.16           C  
ANISOU 1697  CB  ARG A 398     1774   1622   1605    -49    -84    177       C  
ATOM   1698  CG  ARG A 398      28.189  22.299  24.986  1.00 13.60           C  
ANISOU 1698  CG  ARG A 398     1826   1686   1656    -56    -84    166       C  
ATOM   1699  CD  ARG A 398      28.780  23.058  23.833  1.00 13.67           C  
ANISOU 1699  CD  ARG A 398     1835   1684   1676    -53    -75    156       C  
ATOM   1700  NE  ARG A 398      30.072  23.630  24.205  1.00 19.16           N  
ANISOU 1700  NE  ARG A 398     2523   2385   2370    -60    -75    144       N  
ATOM   1701  CZ  ARG A 398      30.743  24.521  23.481  1.00 27.72           C  
ANISOU 1701  CZ  ARG A 398     3608   3462   3463    -62    -64    132       C  
ATOM   1702  NH1 ARG A 398      30.227  24.957  22.343  1.00 20.92           N  
ANISOU 1702  NH1 ARG A 398     2754   2586   2610    -55    -52    134       N  
ATOM   1703  NH2 ARG A 398      31.925  24.974  23.900  1.00 19.74           N  
ANISOU 1703  NH2 ARG A 398     2589   2458   2454    -70    -63    118       N  
ATOM   1704  N  ASER A 399      23.942  20.863  25.136  0.51 14.36           N  
ANISOU 1704  N  ASER A 399     1933   1768   1755    -48    -74    187       N  
ATOM   1705  N  BSER A 399      24.042  20.863  25.136  0.12 14.36           N  
ANISOU 1705  N  BSER A 399     1933   1769   1755    -48    -74    187       N  
ATOM   1706  N  CSER A 399      23.954  20.872  25.117  0.37 14.36           N  
ANISOU 1706  N  CSER A 399     1933   1768   1755    -48    -74    187       N  
ATOM   1707  CA ASER A 399      22.741  20.320  24.520  0.51 18.30           C  
ANISOU 1707  CA ASER A 399     2431   2259   2264    -42    -70    188       C  
ATOM   1708  CA BSER A 399      22.841  20.320  24.520  0.12 18.30           C  
ANISOU 1708  CA BSER A 399     2431   2259   2263    -42    -71    188       C  
ATOM   1709  CA CSER A 399      22.705  20.319  24.628  0.37 18.31           C  
ANISOU 1709  CA CSER A 399     2432   2260   2264    -42    -70    189       C  
ATOM   1710  C  ASER A 399      21.696  21.414  24.402  0.51 15.91           C  
ANISOU 1710  C  ASER A 399     2132   1954   1959    -42    -59    179       C  
ATOM   1711  C  BSER A 399      21.796  21.414  24.402  0.12 15.91           C  
ANISOU 1711  C  BSER A 399     2132   1954   1959    -42    -60    179       C  
ATOM   1712  C  CSER A 399      21.676  21.421  24.426  0.37 15.91           C  
ANISOU 1712  C  CSER A 399     2132   1954   1959    -42    -59    179       C  
ATOM   1713  O  ASER A 399      21.869  22.518  24.935  0.51 17.68           O  
ANISOU 1713  O  ASER A 399     2361   2182   2176    -48    -53    173       O  
ATOM   1714  O  BSER A 399      21.969  22.518  24.935  0.12 17.68           O  
ANISOU 1714  O  BSER A 399     2361   2183   2176    -48    -53    173       O  
ATOM   1715  O  CSER A 399      21.834  22.530  24.927  0.37 17.68           O  
ANISOU 1715  O  CSER A 399     2361   2182   2176    -48    -52    173       O  
ATOM   1716  CB ASER A 399      22.174  19.169  25.355  0.51 23.33           C  
ANISOU 1716  CB ASER A 399     3068   2896   2901    -45    -71    199       C  
ATOM   1717  CB BSER A 399      22.274  19.169  25.355  0.12 23.32           C  
ANISOU 1717  CB BSER A 399     3067   2896   2900    -45    -72    199       C  
ATOM   1718  CB CSER A 399      22.157  19.286  25.611  0.37 23.32           C  
ANISOU 1718  CB CSER A 399     3068   2897   2897    -46    -71    199       C  
ATOM   1719  OG ASER A 399      21.582  19.703  26.527  0.51 29.06           O  
ANISOU 1719  OG ASER A 399     3798   3628   3614    -53    -65    198       O  
ATOM   1720  OG BSER A 399      21.682  19.703  26.527  0.12 29.06           O  
ANISOU 1720  OG BSER A 399     3798   3628   3614    -53    -65    198       O  
ATOM   1721  OG CSER A 399      22.315  17.975  25.107  0.37 29.18           O  
ANISOU 1721  OG CSER A 399     3803   3631   3651    -41    -76    206       O  
ATOM   1722  N   ILE A 400      20.619  21.100  23.696  1.00 13.23           N  
ANISOU 1722  N   ILE A 400     1789   1609   1628    -35    -57    177       N  
ATOM   1723  CA  ILE A 400      19.472  21.993  23.542  1.00 15.57           C  
ANISOU 1723  CA  ILE A 400     2088   1904   1924    -32    -48    169       C  
ATOM   1724  C   ILE A 400      18.501  21.697  24.679  1.00 19.10           C  
ANISOU 1724  C   ILE A 400     2536   2353   2369    -40    -42    169       C  
ATOM   1725  O   ILE A 400      18.179  20.537  24.916  1.00 16.72           O  
ANISOU 1725  O   ILE A 400     2230   2049   2072    -42    -45    174       O  
ATOM   1726  CB  ILE A 400      18.700  21.690  22.239  1.00 20.12           C  
ANISOU 1726  CB  ILE A 400     2658   2476   2510    -18    -49    164       C  
ATOM   1727  CG1 ILE A 400      19.639  21.594  21.028  1.00 24.96           C  
ANISOU 1727  CG1 ILE A 400     3269   3088   3126     -9    -55    165       C  
ATOM   1728  CG2 ILE A 400      17.555  22.680  22.039  1.00 14.83           C  
ANISOU 1728  CG2 ILE A 400     1989   1806   1840    -13    -41    156       C  
ATOM   1729  CD1 ILE A 400      20.042  22.899  20.447  1.00 22.40           C  
ANISOU 1729  CD1 ILE A 400     2952   2763   2797     -3    -49    163       C  
ATOM   1730  N   GLY A 401      18.011  22.724  25.366  1.00 19.67           N  
ANISOU 1730  N   GLY A 401     2613   2427   2435    -46    -33    164       N  
ATOM   1731  CA  GLY A 401      17.126  22.493  26.510  1.00 17.93           C  
ANISOU 1731  CA  GLY A 401     2393   2208   2210    -56    -26    164       C  
ATOM   1732  C   GLY A 401      17.912  22.414  27.806  1.00 20.13           C  
ANISOU 1732  C   GLY A 401     2677   2496   2475    -67    -27    170       C  
ATOM   1733  O   GLY A 401      18.891  23.146  27.991  1.00 15.71           O  
ANISOU 1733  O   GLY A 401     2120   1942   1908    -71    -29    168       O  
ATOM   1734  N   ASP A 402      17.476  21.539  28.711  1.00 20.27           N  
ANISOU 1734  N   ASP A 402     2696   2515   2489    -73    -25    178       N  
ATOM   1735  CA  ASP A 402      18.152  21.336  30.000  1.00 18.17           C  
ANISOU 1735  CA  ASP A 402     2436   2262   2207    -82    -27    186       C  
ATOM   1736  C   ASP A 402      18.364  22.615  30.790  1.00 19.71           C  
ANISOU 1736  C   ASP A 402     2634   2467   2388    -91    -22    175       C  
ATOM   1737  O   ASP A 402      19.442  22.812  31.392  1.00 17.32           O  
ANISOU 1737  O   ASP A 402     2332   2178   2071    -95    -28    176       O  
ATOM   1738  CB  ASP A 402      19.519  20.667  29.789  1.00 18.47           C  
ANISOU 1738  CB  ASP A 402     2472   2304   2242    -77    -41    196       C  
ATOM   1739  CG  ASP A 402      19.403  19.252  29.233  1.00 25.99           C  
ANISOU 1739  CG  ASP A 402     3420   3246   3208    -69    -45    207       C  
ATOM   1740  OD1 ASP A 402      18.494  18.492  29.664  1.00 23.85           O  
ANISOU 1740  OD1 ASP A 402     3151   2970   2942    -71    -37    213       O  
ATOM   1741  OD2 ASP A 402      20.225  18.897  28.359  1.00 26.23           O  
ANISOU 1741  OD2 ASP A 402     3446   3273   3246    -62    -54    209       O  
ATOM   1742  N   ARG A 403      17.365  23.491  30.807  1.00 16.62           N  
ANISOU 1742  N   ARG A 403     2243   2071   2000    -94    -10    164       N  
ATOM   1743  CA  ARG A 403      17.542  24.720  31.566  1.00 19.40           C  
ANISOU 1743  CA  ARG A 403     2597   2432   2342   -104     -2    152       C  
ATOM   1744  C   ARG A 403      17.900  24.471  33.038  1.00 16.92           C  
ANISOU 1744  C   ARG A 403     2287   2136   2007   -115     -2    155       C  
ATOM   1745  O   ARG A 403      18.590  25.286  33.637  1.00 21.41           O  
ANISOU 1745  O   ARG A 403     2855   2716   2563   -122     -2    145       O  
ATOM   1746  CB  ARG A 403      16.367  25.703  31.390  1.00 21.70           C  
ANISOU 1746  CB  ARG A 403     2887   2714   2642   -106     13    139       C  
ATOM   1747  CG  ARG A 403      14.986  25.205  31.757  1.00 18.15           C  
ANISOU 1747  CG  ARG A 403     2439   2260   2197   -108     20    140       C  
ATOM   1748  CD  ARG A 403      13.963  26.270  31.350  1.00 16.10           C  
ANISOU 1748  CD  ARG A 403     2176   1991   1950   -106     33    126       C  
ATOM   1749  NE  ARG A 403      12.589  25.938  31.711  1.00 23.06           N  
ANISOU 1749  NE  ARG A 403     3056   2868   2837   -109     42    123       N  
ATOM   1750  CZ  ARG A 403      11.833  25.032  31.087  1.00 25.15           C  
ANISOU 1750  CZ  ARG A 403     3316   3125   3115   -101     39    126       C  
ATOM   1751  NH1 ARG A 403      12.306  24.329  30.057  1.00 18.86           N  
ANISOU 1751  NH1 ARG A 403     2516   2325   2325    -90     27    133       N  
ATOM   1752  NH2 ARG A 403      10.595  24.813  31.498  1.00 18.92           N  
ANISOU 1752  NH2 ARG A 403     2525   2332   2333   -105     49    119       N  
ATOM   1753  N   TYR A 404      17.489  23.340  33.614  1.00 21.30           N  
ANISOU 1753  N   TYR A 404     2845   2692   2556   -114     -3    169       N  
ATOM   1754  CA  TYR A 404      17.853  23.081  35.012  1.00 21.14           C  
ANISOU 1754  CA  TYR A 404     2830   2690   2511   -122     -4    175       C  
ATOM   1755  C   TYR A 404      19.364  23.114  35.241  1.00 23.20           C  
ANISOU 1755  C   TYR A 404     3089   2968   2759   -120    -18    177       C  
ATOM   1756  O   TYR A 404      19.816  23.377  36.351  1.00 26.24           O  
ANISOU 1756  O   TYR A 404     3475   3374   3122   -126    -20    174       O  
ATOM   1757  CB  TYR A 404      17.252  21.781  35.587  1.00 14.65           C  
ANISOU 1757  CB  TYR A 404     2014   1866   1686   -120     -1    194       C  
ATOM   1758  CG  TYR A 404      17.855  20.455  35.129  1.00 22.92           C  
ANISOU 1758  CG  TYR A 404     3061   2907   2739   -109    -11    213       C  
ATOM   1759  CD1 TYR A 404      18.034  20.173  33.776  1.00 19.94           C  
ANISOU 1759  CD1 TYR A 404     2677   2516   2384   -100    -18    212       C  
ATOM   1760  CD2 TYR A 404      18.185  19.460  36.051  1.00 19.43           C  
ANISOU 1760  CD2 TYR A 404     2625   2474   2282   -106    -13    233       C  
ATOM   1761  CE1 TYR A 404      18.532  18.974  33.359  1.00 20.70           C  
ANISOU 1761  CE1 TYR A 404     2772   2605   2489    -91    -26    228       C  
ATOM   1762  CE2 TYR A 404      18.697  18.243  35.637  1.00 21.53           C  
ANISOU 1762  CE2 TYR A 404     2890   2732   2557    -95    -20    251       C  
ATOM   1763  CZ  TYR A 404      18.866  18.006  34.286  1.00 24.02           C  
ANISOU 1763  CZ  TYR A 404     3197   3032   2895    -89    -26    247       C  
ATOM   1764  OH  TYR A 404      19.365  16.806  33.840  1.00 27.30           O  
ANISOU 1764  OH  TYR A 404     3611   3439   3322    -79    -32    263       O  
ATOM   1765  N   LEU A 405      20.138  22.857  34.191  1.00 18.62           N  
ANISOU 1765  N   LEU A 405     2504   2380   2191   -111    -29    180       N  
ATOM   1766  CA  LEU A 405      21.592  22.823  34.318  1.00 21.30           C  
ANISOU 1766  CA  LEU A 405     2838   2733   2520   -108    -43    181       C  
ATOM   1767  C   LEU A 405      22.312  23.945  33.558  1.00 24.14           C  
ANISOU 1767  C   LEU A 405     3191   3090   2890   -110    -43    162       C  
ATOM   1768  O   LEU A 405      23.524  23.883  33.356  1.00 21.68           O  
ANISOU 1768  O   LEU A 405     2874   2786   2576   -107    -54    161       O  
ATOM   1769  CB  LEU A 405      22.130  21.457  33.895  1.00 22.27           C  
ANISOU 1769  CB  LEU A 405     2961   2852   2649    -97    -55    201       C  
ATOM   1770  CG  LEU A 405      21.771  20.305  34.830  1.00 24.00           C  
ANISOU 1770  CG  LEU A 405     3187   3077   2856    -94    -55    221       C  
ATOM   1771  CD1 LEU A 405      22.212  18.994  34.219  1.00 18.71           C  
ANISOU 1771  CD1 LEU A 405     2516   2396   2199    -82    -63    240       C  
ATOM   1772  CD2 LEU A 405      22.397  20.515  36.211  1.00 24.37           C  
ANISOU 1772  CD2 LEU A 405     3235   3151   2873    -97    -60    222       C  
ATOM   1773  N   LYS A 406      21.564  24.958  33.131  1.00 22.58           N  
ANISOU 1773  N   LYS A 406     2995   2882   2704   -115    -29    149       N  
ATOM   1774  CA  LYS A 406      22.161  26.177  32.600  1.00 23.92           C  
ANISOU 1774  CA  LYS A 406     3160   3047   2882   -118    -23    131       C  
ATOM   1775  C   LYS A 406      22.726  26.958  33.781  1.00 26.55           C  
ANISOU 1775  C   LYS A 406     3489   3401   3198   -130    -20    115       C  
ATOM   1776  O   LYS A 406      22.180  26.885  34.875  1.00 27.99           O  
ANISOU 1776  O   LYS A 406     3674   3596   3364   -137    -17    115       O  
ATOM   1777  CB  LYS A 406      21.099  27.033  31.905  1.00 26.10           C  
ANISOU 1777  CB  LYS A 406     3438   3305   3174   -117     -7    124       C  
ATOM   1778  CG  LYS A 406      20.826  26.688  30.437  1.00 27.60           C  
ANISOU 1778  CG  LYS A 406     3628   3476   3382   -103    -10    132       C  
ATOM   1779  CD  LYS A 406      19.467  27.267  30.016  1.00 30.42           C  
ANISOU 1779  CD  LYS A 406     3988   3820   3750   -100      4    129       C  
ATOM   1780  CE  LYS A 406      19.335  27.484  28.525  1.00 30.01           C  
ANISOU 1780  CE  LYS A 406     3935   3753   3713    -86      5    131       C  
ATOM   1781  NZ  LYS A 406      19.723  26.325  27.721  1.00 32.37           N  
ANISOU 1781  NZ  LYS A 406     4232   4050   4016    -76     -9    143       N  
ATOM   1782  N   PRO A 407      23.813  27.720  33.574  1.00 25.75           N  
ANISOU 1782  N   PRO A 407     3380   3303   3100   -134    -20     99       N  
ATOM   1783  CA  PRO A 407      24.597  27.939  32.354  1.00 20.94           C  
ANISOU 1783  CA  PRO A 407     2768   2681   2509   -127    -21     97       C  
ATOM   1784  C   PRO A 407      25.771  26.957  32.239  1.00 26.89           C  
ANISOU 1784  C   PRO A 407     3517   3444   3257   -121    -40    106       C  
ATOM   1785  O   PRO A 407      26.780  27.229  31.561  1.00 25.41           O  
ANISOU 1785  O   PRO A 407     3323   3252   3080   -119    -42     99       O  
ATOM   1786  CB  PRO A 407      25.138  29.350  32.570  1.00 37.79           C  
ANISOU 1786  CB  PRO A 407     4895   4816   4648   -139     -6     71       C  
ATOM   1787  CG  PRO A 407      25.402  29.388  34.060  1.00 34.34           C  
ANISOU 1787  CG  PRO A 407     4453   4407   4187   -150    -11     60       C  
ATOM   1788  CD  PRO A 407      24.324  28.534  34.697  1.00 31.97           C  
ANISOU 1788  CD  PRO A 407     4162   4112   3874   -147    -16     78       C  
ATOM   1789  N   TYR A 408      25.647  25.815  32.899  1.00 22.48           N  
ANISOU 1789  N   TYR A 408     2960   2897   2684   -116    -53    123       N  
ATOM   1790  CA  TYR A 408      26.710  24.819  32.859  1.00 27.49           C  
ANISOU 1790  CA  TYR A 408     3589   3540   3313   -108    -72    134       C  
ATOM   1791  C   TYR A 408      26.657  24.028  31.542  1.00 27.35           C  
ANISOU 1791  C   TYR A 408     3574   3501   3315    -97    -75    149       C  
ATOM   1792  O   TYR A 408      27.656  23.940  30.830  1.00 22.00           O  
ANISOU 1792  O   TYR A 408     2890   2820   2647    -93    -82    146       O  
ATOM   1793  CB  TYR A 408      26.662  23.925  34.107  1.00 22.49           C  
ANISOU 1793  CB  TYR A 408     2959   2929   2657   -106    -82    148       C  
ATOM   1794  CG  TYR A 408      26.472  24.736  35.372  1.00 27.11           C  
ANISOU 1794  CG  TYR A 408     3544   3536   3222   -118    -76    133       C  
ATOM   1795  CD1 TYR A 408      25.310  24.640  36.123  1.00 30.39           C  
ANISOU 1795  CD1 TYR A 408     3968   3953   3626   -122    -67    139       C  
ATOM   1796  CD2 TYR A 408      27.442  25.641  35.784  1.00 31.25           C  
ANISOU 1796  CD2 TYR A 408     4056   4077   3739   -126    -78    108       C  
ATOM   1797  CE1 TYR A 408      25.135  25.409  37.274  1.00 29.40           C  
ANISOU 1797  CE1 TYR A 408     3842   3849   3482   -134    -61    123       C  
ATOM   1798  CE2 TYR A 408      27.275  26.409  36.923  1.00 32.25           C  
ANISOU 1798  CE2 TYR A 408     4181   4225   3848   -138    -71     90       C  
ATOM   1799  CZ  TYR A 408      26.125  26.292  37.662  1.00 31.80           C  
ANISOU 1799  CZ  TYR A 408     4133   4171   3778   -141    -63     98       C  
ATOM   1800  OH  TYR A 408      25.971  27.059  38.795  1.00 42.71           O  
ANISOU 1800  OH  TYR A 408     5512   5575   5141   -154    -57     79       O  
ATOM   1801  N   VAL A 409      25.497  23.483  31.195  1.00 28.32           N  
ANISOU 1801  N   VAL A 409     3704   3611   3445    -92    -71    162       N  
ATOM   1802  CA  VAL A 409      25.339  22.953  29.849  1.00 26.02           C  
ANISOU 1802  CA  VAL A 409     3414   3301   3173    -83    -72    170       C  
ATOM   1803  C   VAL A 409      24.689  24.033  28.993  1.00 25.48           C  
ANISOU 1803  C   VAL A 409     3348   3217   3117    -83    -57    158       C  
ATOM   1804  O   VAL A 409      23.728  24.664  29.417  1.00 32.23           O  
ANISOU 1804  O   VAL A 409     4206   4071   3969    -89    -46    152       O  
ATOM   1805  CB  VAL A 409      24.558  21.607  29.798  1.00 26.91           C  
ANISOU 1805  CB  VAL A 409     3530   3406   3289    -76    -75    189       C  
ATOM   1806  CG1 VAL A 409      24.792  20.786  31.069  1.00 25.89           C  
ANISOU 1806  CG1 VAL A 409     3402   3292   3143    -76    -83    202       C  
ATOM   1807  CG2 VAL A 409      23.091  21.836  29.553  1.00 36.31           C  
ANISOU 1807  CG2 VAL A 409     4725   4585   4486    -77    -63    187       C  
ATOM   1808  N   ILE A 410      25.239  24.265  27.803  1.00 17.71           N  
ANISOU 1808  N   ILE A 410     2361   2222   2146    -77    -57    155       N  
ATOM   1809  CA  ILE A 410      24.806  25.354  26.936  1.00 14.36           C  
ANISOU 1809  CA  ILE A 410     1939   1784   1732    -75    -42    146       C  
ATOM   1810  C   ILE A 410      24.434  24.828  25.554  1.00 20.13           C  
ANISOU 1810  C   ILE A 410     2671   2501   2475    -62    -44    154       C  
ATOM   1811  O   ILE A 410      24.916  23.771  25.138  1.00 18.56           O  
ANISOU 1811  O   ILE A 410     2469   2302   2279    -57    -56    162       O  
ATOM   1812  CB  ILE A 410      25.901  26.408  26.781  1.00 17.21           C  
ANISOU 1812  CB  ILE A 410     2297   2144   2096    -80    -35    131       C  
ATOM   1813  CG1 ILE A 410      27.211  25.750  26.347  1.00 20.01           C  
ANISOU 1813  CG1 ILE A 410     2647   2502   2455    -77    -47    133       C  
ATOM   1814  CG2 ILE A 410      26.123  27.159  28.096  1.00 23.55           C  
ANISOU 1814  CG2 ILE A 410     3098   2962   2888    -94    -30    117       C  
ATOM   1815  CD1 ILE A 410      28.336  26.759  26.107  1.00 21.56           C  
ANISOU 1815  CD1 ILE A 410     2839   2697   2658    -83    -38    116       C  
ATOM   1816  N   PRO A 411      23.570  25.559  24.834  1.00 16.83           N  
ANISOU 1816  N   PRO A 411     2257   2073   2063    -56    -33    151       N  
ATOM   1817  CA  PRO A 411      23.108  25.109  23.511  1.00 17.85           C  
ANISOU 1817  CA  PRO A 411     2387   2193   2201    -42    -35    157       C  
ATOM   1818  C   PRO A 411      24.010  25.536  22.334  1.00 22.46           C  
ANISOU 1818  C   PRO A 411     2972   2770   2792    -35    -32    155       C  
ATOM   1819  O   PRO A 411      23.588  25.412  21.185  1.00 29.11           O  
ANISOU 1819  O   PRO A 411     3815   3606   3639    -22    -31    158       O  
ATOM   1820  CB  PRO A 411      21.745  25.801  23.389  1.00 18.46           C  
ANISOU 1820  CB  PRO A 411     2467   2266   2280    -38    -24    154       C  
ATOM   1821  CG  PRO A 411      21.980  27.123  24.098  1.00 19.25           C  
ANISOU 1821  CG  PRO A 411     2571   2365   2377    -47    -10    145       C  
ATOM   1822  CD  PRO A 411      22.854  26.772  25.285  1.00 20.32           C  
ANISOU 1822  CD  PRO A 411     2703   2512   2504    -61    -17    142       C  
ATOM   1823  N   GLU A 412      25.217  26.015  22.607  1.00 19.69           N  
ANISOU 1823  N   GLU A 412     2619   2420   2441    -42    -29    149       N  
ATOM   1824  CA  GLU A 412      26.114  26.527  21.562  1.00 18.99           C  
ANISOU 1824  CA  GLU A 412     2532   2322   2359    -37    -21    146       C  
ATOM   1825  C   GLU A 412      26.832  25.397  20.825  1.00 21.71           C  
ANISOU 1825  C   GLU A 412     2872   2667   2708    -32    -35    151       C  
ATOM   1826  O   GLU A 412      27.577  24.636  21.429  1.00 20.42           O  
ANISOU 1826  O   GLU A 412     2703   2512   2544    -38    -47    152       O  
ATOM   1827  CB  GLU A 412      27.138  27.499  22.169  1.00 25.20           C  
ANISOU 1827  CB  GLU A 412     3317   3109   3148    -49    -11    133       C  
ATOM   1828  CG  GLU A 412      28.215  28.009  21.188  1.00 43.13           C  
ANISOU 1828  CG  GLU A 412     5589   5370   5429    -46     -1    128       C  
ATOM   1829  CD  GLU A 412      29.166  29.059  21.803  1.00 55.55           C  
ANISOU 1829  CD  GLU A 412     7158   6941   7007    -59     14    111       C  
ATOM   1830  OE1 GLU A 412      29.990  29.638  21.056  1.00 62.25           O  
ANISOU 1830  OE1 GLU A 412     8008   7779   7866    -58     27    105       O  
ATOM   1831  OE2 GLU A 412      29.091  29.308  23.030  1.00 49.15           O  
ANISOU 1831  OE2 GLU A 412     6343   6142   6190    -71     12    101       O  
ATOM   1832  N   PRO A 413      26.608  25.288  19.512  1.00 17.48           N  
ANISOU 1832  N   PRO A 413     2340   2125   2177    -19    -33    155       N  
ATOM   1833  CA  PRO A 413      27.213  24.220  18.702  1.00 16.69           C  
ANISOU 1833  CA  PRO A 413     2234   2025   2082    -13    -44    159       C  
ATOM   1834  C   PRO A 413      28.643  24.555  18.274  1.00 16.46           C  
ANISOU 1834  C   PRO A 413     2204   1991   2058    -16    -39    153       C  
ATOM   1835  O   PRO A 413      29.077  25.697  18.361  1.00 17.13           O  
ANISOU 1835  O   PRO A 413     2293   2070   2145    -20    -24    147       O  
ATOM   1836  CB  PRO A 413      26.327  24.184  17.465  1.00 14.63           C  
ANISOU 1836  CB  PRO A 413     1978   1762   1821      2    -41    163       C  
ATOM   1837  CG  PRO A 413      25.888  25.655  17.296  1.00 16.18           C  
ANISOU 1837  CG  PRO A 413     2183   1951   2014      7    -23    161       C  
ATOM   1838  CD  PRO A 413      25.766  26.199  18.715  1.00 18.89           C  
ANISOU 1838  CD  PRO A 413     2525   2296   2355     -7    -19    157       C  
ATOM   1839  N   GLU A 414      29.362  23.541  17.816  1.00 21.22           N  
ANISOU 1839  N   GLU A 414     2801   2594   2667    -15    -50    155       N  
ATOM   1840  CA  GLU A 414      30.591  23.749  17.073  1.00 19.17           C  
ANISOU 1840  CA  GLU A 414     2540   2328   2414    -15    -44    150       C  
ATOM   1841  C   GLU A 414      30.368  23.288  15.641  1.00 20.05           C  
ANISOU 1841  C   GLU A 414     2654   2436   2528     -2    -44    154       C  
ATOM   1842  O   GLU A 414      29.733  22.258  15.400  1.00 15.82           O  
ANISOU 1842  O   GLU A 414     2113   1905   1992      3    -56    158       O  
ATOM   1843  CB  GLU A 414      31.739  22.992  17.725  1.00 17.70           C  
ANISOU 1843  CB  GLU A 414     2344   2148   2234    -24    -57    146       C  
ATOM   1844  CG  GLU A 414      32.077  23.569  19.084  1.00 32.13           C  
ANISOU 1844  CG  GLU A 414     4168   3983   4057    -36    -57    139       C  
ATOM   1845  CD  GLU A 414      33.343  22.993  19.662  1.00 40.84           C  
ANISOU 1845  CD  GLU A 414     5259   5093   5164    -42    -69    134       C  
ATOM   1846  OE1 GLU A 414      34.425  23.198  19.065  1.00 51.00           O  
ANISOU 1846  OE1 GLU A 414     6542   6375   6460    -44    -64    125       O  
ATOM   1847  OE2 GLU A 414      33.248  22.327  20.710  1.00 40.33           O  
ANISOU 1847  OE2 GLU A 414     5190   5041   5092    -45    -83    139       O  
ATOM   1848  N   VAL A 415      30.882  24.063  14.698  1.00 15.79           N  
ANISOU 1848  N   VAL A 415     2120   1888   1991      3    -29    151       N  
ATOM   1849  CA  VAL A 415      30.644  23.823  13.285  1.00 20.46           C  
ANISOU 1849  CA  VAL A 415     2715   2478   2580     17    -26    155       C  
ATOM   1850  C   VAL A 415      31.894  23.386  12.529  1.00 19.34           C  
ANISOU 1850  C   VAL A 415     2570   2332   2447     16    -25    150       C  
ATOM   1851  O   VAL A 415      32.962  23.985  12.673  1.00 17.86           O  
ANISOU 1851  O   VAL A 415     2383   2138   2267      8    -15    143       O  
ATOM   1852  CB  VAL A 415      30.144  25.093  12.602  1.00 20.72           C  
ANISOU 1852  CB  VAL A 415     2762   2505   2606     28     -6    158       C  
ATOM   1853  CG1 VAL A 415      29.937  24.825  11.105  1.00 22.38           C  
ANISOU 1853  CG1 VAL A 415     2976   2717   2810     45     -5    163       C  
ATOM   1854  CG2 VAL A 415      28.867  25.577  13.270  1.00 20.58           C  
ANISOU 1854  CG2 VAL A 415     2748   2491   2581     31     -6    162       C  
ATOM   1855  N   THR A 416      31.733  22.372  11.689  1.00 14.98           N  
ANISOU 1855  N   THR A 416     2013   1784   1895     23    -35    151       N  
ATOM   1856  CA  THR A 416      32.814  21.872  10.827  1.00 15.15           C  
ANISOU 1856  CA  THR A 416     2030   1801   1924     23    -34    146       C  
ATOM   1857  C   THR A 416      32.501  22.158   9.359  1.00 15.61           C  
ANISOU 1857  C   THR A 416     2097   1860   1974     38    -24    148       C  
ATOM   1858  O   THR A 416      31.439  21.802   8.850  1.00 17.83           O  
ANISOU 1858  O   THR A 416     2378   2150   2246     49    -30    151       O  
ATOM   1859  CB  THR A 416      33.058  20.347  11.042  1.00 17.84           C  
ANISOU 1859  CB  THR A 416     2357   2147   2276     18    -53    144       C  
ATOM   1860  OG1 THR A 416      33.421  20.113  12.410  1.00 22.86           O  
ANISOU 1860  OG1 THR A 416     2986   2784   2917      6    -62    144       O  
ATOM   1861  CG2 THR A 416      34.194  19.831  10.140  1.00 22.37           C  
ANISOU 1861  CG2 THR A 416     2924   2715   2859     17    -51    137       C  
ATOM   1862  N   PHE A 417      33.415  22.830   8.678  1.00 16.74           N  
ANISOU 1862  N   PHE A 417     2247   1994   2119     39     -7    146       N  
ATOM   1863  CA  PHE A 417      33.196  23.171   7.276  1.00 17.55           C  
ANISOU 1863  CA  PHE A 417     2359   2098   2211     55      5    150       C  
ATOM   1864  C   PHE A 417      34.118  22.263   6.458  1.00 18.97           C  
ANISOU 1864  C   PHE A 417     2531   2278   2398     52      2    142       C  
ATOM   1865  O   PHE A 417      35.324  22.303   6.627  1.00 21.25           O  
ANISOU 1865  O   PHE A 417     2817   2557   2701     41      8    135       O  
ATOM   1866  CB  PHE A 417      33.464  24.667   7.057  1.00 19.82           C  
ANISOU 1866  CB  PHE A 417     2663   2373   2495     59     32    155       C  
ATOM   1867  CG  PHE A 417      33.334  25.124   5.625  1.00 23.69           C  
ANISOU 1867  CG  PHE A 417     3166   2864   2972     78     48    162       C  
ATOM   1868  CD1 PHE A 417      34.461  25.220   4.809  1.00 24.33           C  
ANISOU 1868  CD1 PHE A 417     3251   2936   3058     76     63    158       C  
ATOM   1869  CD2 PHE A 417      32.101  25.481   5.104  1.00 24.86           C  
ANISOU 1869  CD2 PHE A 417     3323   3022   3102     97     48    173       C  
ATOM   1870  CE1 PHE A 417      34.359  25.657   3.494  1.00 22.44           C  
ANISOU 1870  CE1 PHE A 417     3024   2697   2803     94     79    167       C  
ATOM   1871  CE2 PHE A 417      31.981  25.918   3.787  1.00 24.09           C  
ANISOU 1871  CE2 PHE A 417     3238   2928   2989    117     62    181       C  
ATOM   1872  CZ  PHE A 417      33.112  26.006   2.977  1.00 26.10           C  
ANISOU 1872  CZ  PHE A 417     3497   3172   3246    116     78    179       C  
ATOM   1873  N   MET A 418      33.551  21.416   5.598  1.00 17.40           N  
ANISOU 1873  N   MET A 418     2328   2090   2192     62     -8    140       N  
ATOM   1874  CA  MET A 418      34.332  20.316   5.018  1.00 16.11           C  
ANISOU 1874  CA  MET A 418     2153   1928   2039     57    -15    131       C  
ATOM   1875  C   MET A 418      34.163  20.208   3.495  1.00 19.28           C  
ANISOU 1875  C   MET A 418     2560   2339   2428     72     -8    129       C  
ATOM   1876  O   MET A 418      33.164  19.689   3.012  1.00 17.91           O  
ANISOU 1876  O   MET A 418     2382   2181   2243     83    -19    127       O  
ATOM   1877  CB  MET A 418      33.921  19.006   5.710  1.00 16.74           C  
ANISOU 1877  CB  MET A 418     2216   2014   2130     50    -37    126       C  
ATOM   1878  CG  MET A 418      34.727  17.780   5.353  1.00 26.61           C  
ANISOU 1878  CG  MET A 418     3452   3262   3396     43    -44    117       C  
ATOM   1879  SD  MET A 418      36.430  17.869   5.940  1.00 38.06           S  
ANISOU 1879  SD  MET A 418     4898   4697   4866     28    -40    112       S  
ATOM   1880  CE  MET A 418      37.208  18.557   4.506  1.00 33.85           C  
ANISOU 1880  CE  MET A 418     4375   4160   4327     33    -18    108       C  
ATOM   1881  N   PRO A 419      35.144  20.714   2.728  1.00 20.62           N  
ANISOU 1881  N   PRO A 419     2737   2500   2597     73     10    128       N  
ATOM   1882  CA  PRO A 419      35.038  20.510   1.283  1.00 19.98           C  
ANISOU 1882  CA  PRO A 419     2660   2430   2502     87     15    125       C  
ATOM   1883  C   PRO A 419      34.959  19.014   0.982  1.00 16.07           C  
ANISOU 1883  C   PRO A 419     2146   1945   2014     83     -3    112       C  
ATOM   1884  O   PRO A 419      35.674  18.211   1.599  1.00 19.59           O  
ANISOU 1884  O   PRO A 419     2578   2382   2482     67    -12    104       O  
ATOM   1885  CB  PRO A 419      36.354  21.094   0.740  1.00 20.30           C  
ANISOU 1885  CB  PRO A 419     2710   2455   2548     83     38    124       C  
ATOM   1886  CG  PRO A 419      36.802  22.078   1.809  1.00 21.29           C  
ANISOU 1886  CG  PRO A 419     2841   2563   2684     72     49    129       C  
ATOM   1887  CD  PRO A 419      36.365  21.453   3.106  1.00 16.37           C  
ANISOU 1887  CD  PRO A 419     2204   1944   2072     61     27    127       C  
ATOM   1888  N   ARG A 420      34.091  18.641   0.050  1.00 16.01           N  
ANISOU 1888  N   ARG A 420     2137   1957   1990     98     -9    108       N  
ATOM   1889  CA  ARG A 420      33.956  17.247  -0.360  1.00 20.85           C  
ANISOU 1889  CA  ARG A 420     2730   2581   2611     94    -23     92       C  
ATOM   1890  C   ARG A 420      35.166  16.783  -1.184  1.00 22.73           C  
ANISOU 1890  C   ARG A 420     2964   2813   2858     88    -15     82       C  
ATOM   1891  O   ARG A 420      35.977  17.599  -1.609  1.00 16.93           O  
ANISOU 1891  O   ARG A 420     2243   2069   2119     89      4     87       O  
ATOM   1892  CB  ARG A 420      32.645  17.047  -1.132  1.00 17.49           C  
ANISOU 1892  CB  ARG A 420     2302   2181   2164    112    -32     87       C  
ATOM   1893  CG  ARG A 420      31.406  17.250  -0.237  1.00 19.83           C  
ANISOU 1893  CG  ARG A 420     2597   2481   2456    116    -43     93       C  
ATOM   1894  CD  ARG A 420      30.087  17.027  -0.967  1.00 19.98           C  
ANISOU 1894  CD  ARG A 420     2609   2526   2456    134    -52     85       C  
ATOM   1895  NE  ARG A 420      30.010  15.704  -1.560  1.00 16.68           N  
ANISOU 1895  NE  ARG A 420     2171   2120   2046    129    -62     64       N  
ATOM   1896  CZ  ARG A 420      28.961  15.242  -2.244  1.00 20.66           C  
ANISOU 1896  CZ  ARG A 420     2663   2649   2537    142    -72     49       C  
ATOM   1897  NH1 ARG A 420      27.887  16.010  -2.427  1.00 18.88           N  
ANISOU 1897  NH1 ARG A 420     2445   2440   2288    161    -74     55       N  
ATOM   1898  NH2 ARG A 420      28.997  14.022  -2.772  1.00 16.57           N  
ANISOU 1898  NH2 ARG A 420     2126   2140   2031    136    -78     26       N  
ATOM   1899  N   SER A 421      35.274  15.470  -1.385  1.00 18.45           N  
ANISOU 1899  N   SER A 421     2403   2275   2332     80    -26     66       N  
ATOM   1900  CA  SER A 421      36.349  14.852  -2.166  1.00 19.25           C  
ANISOU 1900  CA  SER A 421     2497   2372   2444     73    -19     53       C  
ATOM   1901  C   SER A 421      35.819  13.702  -3.035  1.00 23.81           C  
ANISOU 1901  C   SER A 421     3058   2968   3021     77    -28     34       C  
ATOM   1902  O   SER A 421      34.867  13.008  -2.653  1.00 17.68           O  
ANISOU 1902  O   SER A 421     2269   2200   2250     77    -42     28       O  
ATOM   1903  CB  SER A 421      37.440  14.303  -1.236  1.00 17.04           C  
ANISOU 1903  CB  SER A 421     2207   2071   2197     54    -22     51       C  
ATOM   1904  OG  SER A 421      38.455  13.629  -1.977  1.00 22.58           O  
ANISOU 1904  OG  SER A 421     2899   2768   2913     47    -16     37       O  
ATOM   1905  N   ARG A 422      36.446  13.481  -4.188  1.00 23.51           N  
ANISOU 1905  N   ARG A 422     3020   2936   2979     79    -18     23       N  
ATOM   1906  CA  ARG A 422      36.087  12.327  -5.019  1.00 31.12           C  
ANISOU 1906  CA  ARG A 422     3965   3916   3945     79    -25      0       C  
ATOM   1907  C   ARG A 422      36.250  10.998  -4.255  1.00 27.62           C  
ANISOU 1907  C   ARG A 422     3498   3459   3537     62    -37    -11       C  
ATOM   1908  O   ARG A 422      35.575  10.016  -4.554  1.00 29.85           O  
ANISOU 1908  O   ARG A 422     3763   3754   3827     62    -45    -28       O  
ATOM   1909  CB  ARG A 422      36.899  12.309  -6.326  1.00 31.14           C  
ANISOU 1909  CB  ARG A 422     3970   3924   3937     82    -11    -11       C  
ATOM   1910  CG  ARG A 422      36.317  13.171  -7.440  1.00 40.33           C  
ANISOU 1910  CG  ARG A 422     5151   5113   5061    104     -3     -6       C  
ATOM   1911  CD  ARG A 422      37.103  14.470  -7.636  1.00 50.79           C  
ANISOU 1911  CD  ARG A 422     6501   6424   6372    109     18     13       C  
ATOM   1912  NE  ARG A 422      36.298  15.518  -8.266  1.00 61.43           N  
ANISOU 1912  NE  ARG A 422     7868   7791   7680    134     25     28       N  
ATOM   1913  CZ  ARG A 422      36.194  15.700  -9.579  1.00 57.82           C  
ANISOU 1913  CZ  ARG A 422     7419   7356   7193    151     33     24       C  
ATOM   1914  NH1 ARG A 422      36.845  14.899 -10.413  1.00 48.14           N  
ANISOU 1914  NH1 ARG A 422     6183   6136   5973    144     37      4       N  
ATOM   1915  NH2 ARG A 422      35.437  16.683 -10.057  1.00 46.69           N  
ANISOU 1915  NH2 ARG A 422     6028   5964   5749    176     39     41       N  
ATOM   1916  N   GLU A 423      37.134  10.976  -3.259  1.00 25.72           N  
ANISOU 1916  N   GLU A 423     3257   3194   3321     49    -36     -1       N  
ATOM   1917  CA  GLU A 423      37.353   9.775  -2.438  1.00 28.34           C  
ANISOU 1917  CA  GLU A 423     3569   3513   3687     35    -46     -7       C  
ATOM   1918  C   GLU A 423      36.268   9.517  -1.394  1.00 22.75           C  
ANISOU 1918  C   GLU A 423     2857   2805   2983     36    -59      1       C  
ATOM   1919  O   GLU A 423      36.283   8.472  -0.731  1.00 24.67           O  
ANISOU 1919  O   GLU A 423     3084   3037   3253     26    -65     -2       O  
ATOM   1920  CB  GLU A 423      38.668   9.892  -1.657  1.00 27.80           C  
ANISOU 1920  CB  GLU A 423     3501   3420   3640     23    -43      2       C  
ATOM   1921  CG  GLU A 423      39.937   9.551  -2.384  1.00 39.29           C  
ANISOU 1921  CG  GLU A 423     4951   4867   5110     16    -33    -10       C  
ATOM   1922  CD  GLU A 423      41.108   9.474  -1.413  1.00 52.96           C  
ANISOU 1922  CD  GLU A 423     6677   6577   6867      5    -34     -3       C  
ATOM   1923  OE1 GLU A 423      41.155  10.310  -0.471  1.00 44.78           O  
ANISOU 1923  OE1 GLU A 423     5652   5536   5826      5    -37     12       O  
ATOM   1924  OE2 GLU A 423      41.962   8.563  -1.570  1.00 52.03           O  
ANISOU 1924  OE2 GLU A 423     6544   6449   6776     -4    -34    -15       O  
ATOM   1925  N   ASP A 424      35.363  10.467  -1.188  1.00 17.42           N  
ANISOU 1925  N   ASP A 424     2195   2140   2282     46    -61     12       N  
ATOM   1926  CA  ASP A 424      34.369  10.263  -0.140  1.00 16.85           C  
ANISOU 1926  CA  ASP A 424     2119   2067   2215     45    -71     19       C  
ATOM   1927  C   ASP A 424      33.416   9.145  -0.494  1.00 20.13           C  
ANISOU 1927  C   ASP A 424     2515   2493   2639     46    -77      1       C  
ATOM   1928  O   ASP A 424      32.988   9.012  -1.640  1.00 22.95           O  
ANISOU 1928  O   ASP A 424     2868   2871   2983     54    -76    -16       O  
ATOM   1929  CB  ASP A 424      33.577  11.537   0.148  1.00 21.43           C  
ANISOU 1929  CB  ASP A 424     2718   2657   2769     57    -71     34       C  
ATOM   1930  CG  ASP A 424      34.437  12.619   0.774  1.00 20.57           C  
ANISOU 1930  CG  ASP A 424     2626   2534   2656     53    -64     52       C  
ATOM   1931  OD1 ASP A 424      35.439  12.252   1.417  1.00 27.17           O  
ANISOU 1931  OD1 ASP A 424     3457   3353   3513     41    -64     54       O  
ATOM   1932  OD2 ASP A 424      34.127  13.822   0.628  1.00 27.56           O  
ANISOU 1932  OD2 ASP A 424     3529   3425   3519     64    -57     62       O  
ATOM   1933  N   GLU A 425      33.078   8.352   0.508  1.00 15.63           N  
ANISOU 1933  N   GLU A 425     1934   1912   2092     37    -83      3       N  
ATOM   1934  CA  GLU A 425      32.234   7.198   0.304  1.00 21.64           C  
ANISOU 1934  CA  GLU A 425     2675   2678   2869     35    -86    -16       C  
ATOM   1935  C   GLU A 425      30.836   7.403   0.877  1.00 22.32           C  
ANISOU 1935  C   GLU A 425     2762   2773   2945     40    -91    -13       C  
ATOM   1936  O   GLU A 425      29.845   7.207   0.187  1.00 22.08           O  
ANISOU 1936  O   GLU A 425     2722   2762   2906     47    -93    -32       O  
ATOM   1937  CB  GLU A 425      32.880   5.977   0.953  1.00 22.20           C  
ANISOU 1937  CB  GLU A 425     2732   2727   2978     21    -84    -16       C  
ATOM   1938  CG  GLU A 425      34.133   5.489   0.254  1.00 22.06           C  
ANISOU 1938  CG  GLU A 425     2706   2701   2975     16    -78    -26       C  
ATOM   1939  CD  GLU A 425      33.829   4.649  -0.989  1.00 32.20           C  
ANISOU 1939  CD  GLU A 425     3972   3998   4265     15    -74    -56       C  
ATOM   1940  OE1 GLU A 425      34.766   4.395  -1.772  1.00 33.97           O  
ANISOU 1940  OE1 GLU A 425     4191   4219   4495     12    -68    -67       O  
ATOM   1941  OE2 GLU A 425      32.660   4.239  -1.188  1.00 30.66           O  
ANISOU 1941  OE2 GLU A 425     3766   3815   4069     18    -76    -71       O  
ATOM   1942  N   CYS A 426      30.755   7.779   2.149  1.00 14.86           N  
ANISOU 1942  N   CYS A 426     1827   1816   2004     37    -94      8       N  
ATOM   1943  CA  CYS A 426      29.461   7.946   2.777  1.00 13.68           C  
ANISOU 1943  CA  CYS A 426     1678   1672   1847     40    -98     10       C  
ATOM   1944  C   CYS A 426      29.604   8.759   4.047  1.00 18.85           C  
ANISOU 1944  C   CYS A 426     2350   2316   2496     38   -100     36       C  
ATOM   1945  O   CYS A 426      30.709   8.920   4.571  1.00 14.27           O  
ANISOU 1945  O   CYS A 426     1776   1722   1923     32    -99     49       O  
ATOM   1946  CB  CYS A 426      28.842   6.578   3.103  1.00 23.38           C  
ANISOU 1946  CB  CYS A 426     2885   2892   3105     32    -97     -3       C  
ATOM   1947  SG  CYS A 426      29.937   5.502   4.088  1.00 28.63           S  
ANISOU 1947  SG  CYS A 426     3544   3527   3807     18    -93     10       S  
ATOM   1948  N   LEU A 427      28.474   9.265   4.531  1.00 16.54           N  
ANISOU 1948  N   LEU A 427     2063   2031   2192     43   -103     40       N  
ATOM   1949  CA  LEU A 427      28.425  10.094   5.721  1.00 14.39           C  
ANISOU 1949  CA  LEU A 427     1805   1751   1911     41   -104     61       C  
ATOM   1950  C   LEU A 427      27.376   9.482   6.629  1.00 15.57           C  
ANISOU 1950  C   LEU A 427     1947   1896   2072     36   -105     61       C  
ATOM   1951  O   LEU A 427      26.284   9.137   6.178  1.00 17.68           O  
ANISOU 1951  O   LEU A 427     2203   2174   2340     41   -105     45       O  
ATOM   1952  CB  LEU A 427      28.055  11.530   5.327  1.00 12.37           C  
ANISOU 1952  CB  LEU A 427     1565   1508   1625     53   -103     67       C  
ATOM   1953  CG  LEU A 427      27.676  12.495   6.440  1.00 16.49           C  
ANISOU 1953  CG  LEU A 427     2101   2027   2137     53   -103     84       C  
ATOM   1954  CD1 LEU A 427      28.869  12.721   7.341  1.00 11.55           C  
ANISOU 1954  CD1 LEU A 427     1483   1385   1518     43   -102     99       C  
ATOM   1955  CD2 LEU A 427      27.165  13.826   5.847  1.00 13.42           C  
ANISOU 1955  CD2 LEU A 427     1727   1652   1721     67   -100     87       C  
ATOM   1956  N   ILE A 428      27.709   9.308   7.902  1.00 11.94           N  
ANISOU 1956  N   ILE A 428     1492   1422   1624     28   -105     78       N  
ATOM   1957  CA  ILE A 428      26.768   8.713   8.842  1.00 16.57           C  
ANISOU 1957  CA  ILE A 428     2072   2001   2221     23   -104     80       C  
ATOM   1958  C   ILE A 428      26.504   9.624  10.047  1.00 17.01           C  
ANISOU 1958  C   ILE A 428     2144   2056   2264     22   -105     99       C  
ATOM   1959  O   ILE A 428      27.435  10.128  10.666  1.00 18.67           O  
ANISOU 1959  O   ILE A 428     2365   2261   2468     19   -107    115       O  
ATOM   1960  CB  ILE A 428      27.273   7.338   9.329  1.00 23.63           C  
ANISOU 1960  CB  ILE A 428     2954   2877   3146     14   -100     83       C  
ATOM   1961  CG1 ILE A 428      27.424   6.381   8.139  1.00 29.09           C  
ANISOU 1961  CG1 ILE A 428     3628   3569   3854     14    -97     61       C  
ATOM   1962  CG2 ILE A 428      26.300   6.742  10.348  1.00 18.37           C  
ANISOU 1962  CG2 ILE A 428     2284   2202   2491     10    -95     88       C  
ATOM   1963  CD1 ILE A 428      28.707   5.568   8.146  1.00 34.84           C  
ANISOU 1963  CD1 ILE A 428     4351   4283   4605      9    -95     66       C  
ATOM   1964  N   LEU A 429      25.234   9.851  10.356  1.00 14.57           N  
ANISOU 1964  N   LEU A 429     1835   1753   1948     24   -104     96       N  
ATOM   1965  CA  LEU A 429      24.833  10.589  11.556  1.00 15.76           C  
ANISOU 1965  CA  LEU A 429     1998   1902   2088     22   -103    111       C  
ATOM   1966  C   LEU A 429      24.105   9.627  12.464  1.00 16.80           C  
ANISOU 1966  C   LEU A 429     2122   2023   2237     14    -98    113       C  
ATOM   1967  O   LEU A 429      23.254   8.867  12.000  1.00 16.06           O  
ANISOU 1967  O   LEU A 429     2014   1930   2157     14    -94     96       O  
ATOM   1968  CB  LEU A 429      23.865  11.737  11.217  1.00 13.70           C  
ANISOU 1968  CB  LEU A 429     1744   1655   1806     30   -104    106       C  
ATOM   1969  CG  LEU A 429      24.499  13.067  10.836  1.00 17.56           C  
ANISOU 1969  CG  LEU A 429     2248   2150   2274     37   -105    113       C  
ATOM   1970  CD1 LEU A 429      25.294  12.900   9.579  1.00 13.51           C  
ANISOU 1970  CD1 LEU A 429     1731   1641   1760     43   -106    104       C  
ATOM   1971  CD2 LEU A 429      23.413  14.143  10.654  1.00 13.36           C  
ANISOU 1971  CD2 LEU A 429     1722   1630   1723     47   -104    110       C  
ATOM   1972  N   ALA A 430      24.403   9.666  13.754  1.00 13.79           N  
ANISOU 1972  N   ALA A 430     1750   1633   1855      9    -97    132       N  
ATOM   1973  CA  ALA A 430      23.791   8.707  14.657  1.00 15.05           C  
ANISOU 1973  CA  ALA A 430     1906   1782   2032      2    -90    137       C  
ATOM   1974  C   ALA A 430      23.817   9.151  16.111  1.00 13.35           C  
ANISOU 1974  C   ALA A 430     1704   1564   1806     -2    -89    158       C  
ATOM   1975  O   ALA A 430      24.709   9.874  16.533  1.00 11.00           O  
ANISOU 1975  O   ALA A 430     1417   1270   1493     -1    -96    170       O  
ATOM   1976  CB  ALA A 430      24.455   7.318  14.492  1.00 14.48           C  
ANISOU 1976  CB  ALA A 430     1821   1695   1986     -1    -86    138       C  
ATOM   1977  N   SER A 431      22.815   8.703  16.862  1.00 14.40           N  
ANISOU 1977  N   SER A 431     1836   1691   1946     -6    -80    160       N  
ATOM   1978  CA  SER A 431      22.771   8.886  18.301  1.00 15.29           C  
ANISOU 1978  CA  SER A 431     1960   1800   2049    -10    -78    180       C  
ATOM   1979  C   SER A 431      23.735   7.890  18.935  1.00 20.32           C  
ANISOU 1979  C   SER A 431     2597   2425   2698    -11    -76    198       C  
ATOM   1980  O   SER A 431      24.317   7.047  18.249  1.00 17.62           O  
ANISOU 1980  O   SER A 431     2245   2076   2375     -9    -76    194       O  
ATOM   1981  CB  SER A 431      21.351   8.627  18.813  1.00 17.98           C  
ANISOU 1981  CB  SER A 431     2299   2137   2397    -14    -66    175       C  
ATOM   1982  OG  SER A 431      20.948   7.294  18.527  1.00 17.39           O  
ANISOU 1982  OG  SER A 431     2210   2047   2349    -16    -55    167       O  
ATOM   1983  N   ASP A 432      23.882   7.952  20.252  1.00 21.57           N  
ANISOU 1983  N   ASP A 432     2766   2583   2847    -12    -75    218       N  
ATOM   1984  CA  ASP A 432      24.858   7.092  20.913  1.00 25.10           C  
ANISOU 1984  CA  ASP A 432     3213   3021   3301    -10    -76    239       C  
ATOM   1985  C   ASP A 432      24.405   5.631  21.099  1.00 19.67           C  
ANISOU 1985  C   ASP A 432     2518   2314   2641    -10    -60    245       C  
ATOM   1986  O   ASP A 432      25.164   4.809  21.588  1.00 23.04           O  
ANISOU 1986  O   ASP A 432     2945   2731   3077     -6    -59    263       O  
ATOM   1987  CB  ASP A 432      25.341   7.708  22.232  1.00 27.42           C  
ANISOU 1987  CB  ASP A 432     3521   3326   3571     -9    -82    259       C  
ATOM   1988  CG  ASP A 432      24.228   7.876  23.226  1.00 29.39           C  
ANISOU 1988  CG  ASP A 432     3779   3576   3811    -13    -72    265       C  
ATOM   1989  OD1 ASP A 432      23.161   7.250  23.033  1.00 26.26           O  
ANISOU 1989  OD1 ASP A 432     3378   3168   3432    -16    -58    258       O  
ATOM   1990  OD2 ASP A 432      24.426   8.624  24.207  1.00 39.96           O  
ANISOU 1990  OD2 ASP A 432     5130   4928   5127    -14    -77    275       O  
ATOM   1991  N   GLY A 433      23.187   5.309  20.685  1.00 21.73           N  
ANISOU 1991  N   GLY A 433     2772   2569   2917    -15    -48    228       N  
ATOM   1992  CA  GLY A 433      22.749   3.920  20.633  1.00 24.54           C  
ANISOU 1992  CA  GLY A 433     3117   2902   3304    -17    -30    228       C  
ATOM   1993  C   GLY A 433      23.600   3.092  19.679  1.00 23.03           C  
ANISOU 1993  C   GLY A 433     2912   2702   3136    -14    -32    221       C  
ATOM   1994  O   GLY A 433      23.739   1.879  19.827  1.00 22.50           O  
ANISOU 1994  O   GLY A 433     2838   2615   3095    -13    -18    229       O  
ATOM   1995  N   LEU A 434      24.191   3.767  18.703  1.00 20.13           N  
ANISOU 1995  N   LEU A 434     2541   2348   2758    -12    -47    207       N  
ATOM   1996  CA  LEU A 434      25.123   3.146  17.778  1.00 20.54           C  
ANISOU 1996  CA  LEU A 434     2581   2395   2828     -9    -50    200       C  
ATOM   1997  C   LEU A 434      26.560   3.271  18.316  1.00 26.37           C  
ANISOU 1997  C   LEU A 434     3328   3135   3557     -4    -62    222       C  
ATOM   1998  O   LEU A 434      27.244   2.265  18.496  1.00 22.23           O  
ANISOU 1998  O   LEU A 434     2798   2596   3053      0    -57    235       O  
ATOM   1999  CB  LEU A 434      25.019   3.818  16.400  1.00 21.11           C  
ANISOU 1999  CB  LEU A 434     2646   2481   2892    -10    -59    172       C  
ATOM   2000  CG  LEU A 434      25.327   3.078  15.089  1.00 25.53           C  
ANISOU 2000  CG  LEU A 434     3189   3038   3476    -10    -56    151       C  
ATOM   2001  CD1 LEU A 434      26.120   3.949  14.120  1.00 16.48           C  
ANISOU 2001  CD1 LEU A 434     2043   1906   2311     -6    -71    141       C  
ATOM   2002  CD2 LEU A 434      26.004   1.759  15.275  1.00 20.08           C  
ANISOU 2002  CD2 LEU A 434     2490   2326   2815    -10    -47    160       C  
ATOM   2003  N   TRP A 435      27.007   4.505  18.565  1.00 21.09           N  
ANISOU 2003  N   TRP A 435     2671   2484   2859     -2    -76    226       N  
ATOM   2004  CA  TRP A 435      28.406   4.758  18.903  1.00 21.90           C  
ANISOU 2004  CA  TRP A 435     2777   2592   2952      3    -89    240       C  
ATOM   2005  C   TRP A 435      28.895   4.126  20.216  1.00 26.16           C  
ANISOU 2005  C   TRP A 435     3322   3125   3491      8    -89    269       C  
ATOM   2006  O   TRP A 435      30.084   3.868  20.367  1.00 27.18           O  
ANISOU 2006  O   TRP A 435     3449   3254   3623     14    -97    280       O  
ATOM   2007  CB  TRP A 435      28.710   6.261  18.904  1.00 22.66           C  
ANISOU 2007  CB  TRP A 435     2883   2708   3018      2   -102    235       C  
ATOM   2008  CG  TRP A 435      28.260   7.024  17.670  1.00 18.59           C  
ANISOU 2008  CG  TRP A 435     2366   2200   2498     -1   -103    212       C  
ATOM   2009  CD1 TRP A 435      27.360   8.053  17.630  1.00 15.84           C  
ANISOU 2009  CD1 TRP A 435     2025   1862   2131     -2   -102    203       C  
ATOM   2010  CD2 TRP A 435      28.682   6.806  16.311  1.00 18.55           C  
ANISOU 2010  CD2 TRP A 435     2350   2193   2505      0   -104    194       C  
ATOM   2011  NE1 TRP A 435      27.200   8.495  16.332  1.00 19.13           N  
ANISOU 2011  NE1 TRP A 435     2437   2285   2547     -1   -103    184       N  
ATOM   2012  CE2 TRP A 435      28.005   7.754  15.506  1.00 18.02           C  
ANISOU 2012  CE2 TRP A 435     2286   2138   2424      1   -104    177       C  
ATOM   2013  CE3 TRP A 435      29.572   5.909  15.697  1.00 18.87           C  
ANISOU 2013  CE3 TRP A 435     2379   2224   2566      2   -104    191       C  
ATOM   2014  CZ2 TRP A 435      28.193   7.835  14.119  1.00 15.81           C  
ANISOU 2014  CZ2 TRP A 435     1998   1862   2147      3   -105    159       C  
ATOM   2015  CZ3 TRP A 435      29.754   5.985  14.311  1.00 20.89           C  
ANISOU 2015  CZ3 TRP A 435     2627   2483   2827      2   -104    171       C  
ATOM   2016  CH2 TRP A 435      29.060   6.942  13.538  1.00 15.05           C  
ANISOU 2016  CH2 TRP A 435     1891   1757   2070      3   -105    155       C  
ATOM   2017  N   ASP A 436      27.999   3.902  21.172  1.00 23.18           N  
ANISOU 2017  N   ASP A 436     2953   2744   3111      7    -78    282       N  
ATOM   2018  CA  ASP A 436      28.391   3.232  22.410  1.00 27.52           C  
ANISOU 2018  CA  ASP A 436     3509   3288   3660     15    -75    311       C  
ATOM   2019  C   ASP A 436      28.869   1.787  22.189  1.00 29.59           C  
ANISOU 2019  C   ASP A 436     3760   3528   3954     21    -66    321       C  
ATOM   2020  O   ASP A 436      29.554   1.231  23.037  1.00 34.87           O  
ANISOU 2020  O   ASP A 436     4433   4194   4623     31    -67    347       O  
ATOM   2021  CB  ASP A 436      27.260   3.219  23.441  1.00 23.99           C  
ANISOU 2021  CB  ASP A 436     3072   2839   3202     12    -62    323       C  
ATOM   2022  CG  ASP A 436      26.977   4.593  24.040  1.00 36.96           C  
ANISOU 2022  CG  ASP A 436     4728   4504   4811      8    -72    320       C  
ATOM   2023  OD1 ASP A 436      25.853   4.780  24.559  1.00 36.08           O  
ANISOU 2023  OD1 ASP A 436     4623   4392   4693      3    -61    320       O  
ATOM   2024  OD2 ASP A 436      27.859   5.481  24.008  1.00 39.47           O  
ANISOU 2024  OD2 ASP A 436     5048   4840   5110     10    -89    317       O  
ATOM   2025  N   VAL A 437      28.505   1.168  21.072  1.00 26.77           N  
ANISOU 2025  N   VAL A 437     3389   3156   3625     16    -55    301       N  
ATOM   2026  CA  VAL A 437      28.837  -0.248  20.887  1.00 29.18           C  
ANISOU 2026  CA  VAL A 437     3683   3437   3966     20    -42    309       C  
ATOM   2027  C   VAL A 437      29.675  -0.551  19.638  1.00 28.30           C  
ANISOU 2027  C   VAL A 437     3556   3322   3874     19    -47    290       C  
ATOM   2028  O   VAL A 437      30.093  -1.682  19.443  1.00 29.09           O  
ANISOU 2028  O   VAL A 437     3646   3402   4005     23    -37    296       O  
ATOM   2029  CB  VAL A 437      27.565  -1.155  20.937  1.00 33.08           C  
ANISOU 2029  CB  VAL A 437     4173   3909   4485     14    -15    304       C  
ATOM   2030  CG1 VAL A 437      26.846  -0.991  22.276  1.00 25.39           C  
ANISOU 2030  CG1 VAL A 437     3216   2937   3494     16     -7    327       C  
ATOM   2031  CG2 VAL A 437      26.626  -0.843  19.784  1.00 29.65           C  
ANISOU 2031  CG2 VAL A 437     3728   3479   4059      3    -11    268       C  
ATOM   2032  N   MET A 438      29.922   0.454  18.798  1.00 27.56           N  
ANISOU 2032  N   MET A 438     3461   3246   3764     15    -62    269       N  
ATOM   2033  CA  MET A 438      30.835   0.292  17.651  1.00 24.43           C  
ANISOU 2033  CA  MET A 438     3053   2849   3382     14    -68    252       C  
ATOM   2034  C   MET A 438      31.652   1.558  17.441  1.00 25.59           C  
ANISOU 2034  C   MET A 438     3205   3017   3500     15    -88    247       C  
ATOM   2035  O   MET A 438      31.156   2.657  17.671  1.00 25.91           O  
ANISOU 2035  O   MET A 438     3258   3074   3514     12    -94    244       O  
ATOM   2036  CB  MET A 438      30.061  -0.007  16.368  1.00 25.80           C  
ANISOU 2036  CB  MET A 438     3212   3017   3573      6    -58    221       C  
ATOM   2037  CG  MET A 438      29.177  -1.244  16.423  1.00 29.99           C  
ANISOU 2037  CG  MET A 438     3733   3526   4136      3    -35    218       C  
ATOM   2038  SD  MET A 438      28.230  -1.458  14.899  1.00 36.37           S  
ANISOU 2038  SD  MET A 438     4523   4336   4962     -7    -26    175       S  
ATOM   2039  CE  MET A 438      29.526  -1.369  13.675  1.00 34.99           C  
ANISOU 2039  CE  MET A 438     4338   4167   4790     -6    -38    160       C  
ATOM   2040  N   ASN A 439      32.897   1.424  17.002  1.00 22.72           N  
ANISOU 2040  N   ASN A 439     2835   2653   3144     18    -96    246       N  
ATOM   2041  CA  ASN A 439      33.701   2.608  16.734  1.00 26.26           C  
ANISOU 2041  CA  ASN A 439     3288   3119   3570     17   -112    238       C  
ATOM   2042  C   ASN A 439      33.429   3.183  15.334  1.00 28.06           C  
ANISOU 2042  C   ASN A 439     3513   3354   3796     11   -110    210       C  
ATOM   2043  O   ASN A 439      32.727   2.563  14.524  1.00 24.83           O  
ANISOU 2043  O   ASN A 439     3093   2936   3403      7   -100    194       O  
ATOM   2044  CB  ASN A 439      35.204   2.376  17.003  1.00 19.33           C  
ANISOU 2044  CB  ASN A 439     2405   2241   2698     24   -123    248       C  
ATOM   2045  CG  ASN A 439      35.801   1.262  16.159  1.00 26.00           C  
ANISOU 2045  CG  ASN A 439     3234   3068   3577     25   -116    241       C  
ATOM   2046  OD1 ASN A 439      36.451   0.347  16.685  1.00 34.98           O  
ANISOU 2046  OD1 ASN A 439     4365   4194   4733     34   -116    258       O  
ATOM   2047  ND2 ASN A 439      35.617   1.346  14.846  1.00 21.16           N  
ANISOU 2047  ND2 ASN A 439     2614   2454   2973     18   -111    215       N  
ATOM   2048  N   ASN A 440      33.962   4.376  15.081  1.00 24.25           N  
ANISOU 2048  N   ASN A 440     3036   2886   3291     10   -120    203       N  
ATOM   2049  CA  ASN A 440      33.755   5.094  13.829  1.00 24.93           C  
ANISOU 2049  CA  ASN A 440     3123   2981   3370      6   -119    180       C  
ATOM   2050  C   ASN A 440      34.218   4.290  12.601  1.00 25.32           C  
ANISOU 2050  C   ASN A 440     3157   3021   3442      5   -114    163       C  
ATOM   2051  O   ASN A 440      33.520   4.224  11.580  1.00 16.96           O  
ANISOU 2051  O   ASN A 440     2093   1964   2385      2   -107    144       O  
ATOM   2052  CB  ASN A 440      34.500   6.440  13.853  1.00 17.93           C  
ANISOU 2052  CB  ASN A 440     2246   2107   2460      6   -127    179       C  
ATOM   2053  CG  ASN A 440      33.998   7.398  14.957  1.00 22.44           C  
ANISOU 2053  CG  ASN A 440     2831   2689   3006      5   -131    190       C  
ATOM   2054  OD1 ASN A 440      32.883   7.272  15.445  1.00 22.92           O  
ANISOU 2054  OD1 ASN A 440     2897   2751   3063      5   -127    196       O  
ATOM   2055  ND2 ASN A 440      34.840   8.362  15.338  1.00 20.91           N  
ANISOU 2055  ND2 ASN A 440     2643   2505   2797      5   -138    192       N  
ATOM   2056  N   GLN A 441      35.413   3.709  12.694  1.00 17.26           N  
ANISOU 2056  N   GLN A 441     2129   1992   2439      7   -117    169       N  
ATOM   2057  CA  GLN A 441      36.000   2.962  11.565  1.00 24.57           C  
ANISOU 2057  CA  GLN A 441     3039   2907   3387      5   -112    153       C  
ATOM   2058  C   GLN A 441      35.174   1.738  11.160  1.00 19.72           C  
ANISOU 2058  C   GLN A 441     2412   2280   2799      3    -99    144       C  
ATOM   2059  O   GLN A 441      34.975   1.466   9.974  1.00 21.08           O  
ANISOU 2059  O   GLN A 441     2575   2454   2981     -1    -93    121       O  
ATOM   2060  CB  GLN A 441      37.455   2.545  11.849  1.00 19.24           C  
ANISOU 2060  CB  GLN A 441     2357   2225   2728      8   -118    161       C  
ATOM   2061  CG  GLN A 441      38.138   1.808  10.687  1.00 21.60           C  
ANISOU 2061  CG  GLN A 441     2640   2513   3052      5   -112    143       C  
ATOM   2062  CD  GLN A 441      38.435   2.738   9.511  1.00 24.38           C  
ANISOU 2062  CD  GLN A 441     2996   2878   3390      1   -111    122       C  
ATOM   2063  OE1 GLN A 441      38.501   3.952   9.679  1.00 22.57           O  
ANISOU 2063  OE1 GLN A 441     2780   2662   3135      1   -117    124       O  
ATOM   2064  NE2 GLN A 441      38.598   2.171   8.315  1.00 21.79           N  
ANISOU 2064  NE2 GLN A 441     2656   2546   3079     -3   -103    101       N  
ATOM   2065  N   GLU A 442      34.675   1.002  12.136  1.00 22.29           N  
ANISOU 2065  N   GLU A 442     2738   2595   3137      5    -94    161       N  
ATOM   2066  CA  GLU A 442      33.926  -0.196  11.786  1.00 24.73           C  
ANISOU 2066  CA  GLU A 442     3033   2888   3474      2    -78    151       C  
ATOM   2067  C   GLU A 442      32.543   0.153  11.230  1.00 21.98           C  
ANISOU 2067  C   GLU A 442     2685   2550   3115     -3    -73    132       C  
ATOM   2068  O   GLU A 442      32.062  -0.505  10.309  1.00 19.19           O  
ANISOU 2068  O   GLU A 442     2318   2193   2781     -8    -63    108       O  
ATOM   2069  CB  GLU A 442      33.856  -1.181  12.949  1.00 25.08           C  
ANISOU 2069  CB  GLU A 442     3077   2913   3539      6    -71    177       C  
ATOM   2070  CG  GLU A 442      33.115  -0.698  14.156  1.00 32.81           C  
ANISOU 2070  CG  GLU A 442     4072   3898   4496      9    -73    197       C  
ATOM   2071  CD  GLU A 442      33.106  -1.737  15.268  1.00 37.06           C  
ANISOU 2071  CD  GLU A 442     4610   4416   5053     15    -63    224       C  
ATOM   2072  OE1 GLU A 442      33.322  -1.362  16.442  1.00 31.01           O  
ANISOU 2072  OE1 GLU A 442     3858   3657   4269     22    -71    249       O  
ATOM   2073  OE2 GLU A 442      32.883  -2.932  14.961  1.00 48.32           O  
ANISOU 2073  OE2 GLU A 442     6023   5822   6515     14    -45    219       O  
ATOM   2074  N   VAL A 443      31.921   1.205  11.764  1.00 16.77           N  
ANISOU 2074  N   VAL A 443     2041   1905   2426     -2    -80    139       N  
ATOM   2075  CA  VAL A 443      30.648   1.683  11.234  1.00 17.07           C  
ANISOU 2075  CA  VAL A 443     2079   1955   2450     -4    -77    121       C  
ATOM   2076  C   VAL A 443      30.770   2.080   9.761  1.00 18.70           C  
ANISOU 2076  C   VAL A 443     2280   2176   2650     -5    -79     94       C  
ATOM   2077  O   VAL A 443      29.988   1.634   8.919  1.00 18.54           O  
ANISOU 2077  O   VAL A 443     2246   2159   2638     -7    -72     70       O  
ATOM   2078  CB  VAL A 443      30.103   2.874  12.057  1.00 19.10           C  
ANISOU 2078  CB  VAL A 443     2355   2226   2676     -2    -84    134       C  
ATOM   2079  CG1 VAL A 443      29.036   3.604  11.269  1.00 21.82           C  
ANISOU 2079  CG1 VAL A 443     2700   2587   3002     -2    -85    113       C  
ATOM   2080  CG2 VAL A 443      29.552   2.398  13.387  1.00 15.49           C  
ANISOU 2080  CG2 VAL A 443     1903   1757   2225     -2    -78    154       C  
ATOM   2081  N   CYS A 444      31.757   2.913   9.442  1.00 16.43           N  
ANISOU 2081  N   CYS A 444     2001   1897   2345     -2    -89     97       N  
ATOM   2082  CA  CYS A 444      31.966   3.322   8.054  1.00 15.42           C  
ANISOU 2082  CA  CYS A 444     1869   1783   2209     -2    -90     75       C  
ATOM   2083  C   CYS A 444      32.229   2.136   7.134  1.00 17.94           C  
ANISOU 2083  C   CYS A 444     2167   2092   2555     -5    -81     55       C  
ATOM   2084  O   CYS A 444      31.646   2.036   6.058  1.00 18.36           O  
ANISOU 2084  O   CYS A 444     2211   2157   2606     -6    -78     30       O  
ATOM   2085  CB  CYS A 444      33.112   4.329   7.952  1.00 22.00           C  
ANISOU 2085  CB  CYS A 444     2714   2621   3023      1    -97     83       C  
ATOM   2086  SG  CYS A 444      32.710   5.927   8.692  1.00 25.43           S  
ANISOU 2086  SG  CYS A 444     3171   3069   3422      4   -104     98       S  
ATOM   2087  N   GLU A 445      33.111   1.236   7.564  1.00 18.56           N  
ANISOU 2087  N   GLU A 445     2239   2152   2662     -8    -78     65       N  
ATOM   2088  CA  GLU A 445      33.490   0.081   6.745  1.00 24.47           C  
ANISOU 2088  CA  GLU A 445     2967   2889   3441    -12    -69     46       C  
ATOM   2089  C   GLU A 445      32.265  -0.787   6.479  1.00 21.33           C  
ANISOU 2089  C   GLU A 445     2555   2488   3063    -16    -57     27       C  
ATOM   2090  O   GLU A 445      32.064  -1.277   5.369  1.00 22.60           O  
ANISOU 2090  O   GLU A 445     2699   2653   3233    -20    -50     -1       O  
ATOM   2091  CB  GLU A 445      34.571  -0.760   7.443  1.00 21.20           C  
ANISOU 2091  CB  GLU A 445     2548   2453   3056    -12    -67     64       C  
ATOM   2092  CG  GLU A 445      35.996  -0.232   7.267  1.00 32.16           C  
ANISOU 2092  CG  GLU A 445     3941   3843   4437    -10    -76     70       C  
ATOM   2093  CD  GLU A 445      37.009  -0.989   8.120  1.00 36.33           C  
ANISOU 2093  CD  GLU A 445     4463   4351   4989     -7    -76     91       C  
ATOM   2094  OE1 GLU A 445      36.631  -2.017   8.727  1.00 41.86           O  
ANISOU 2094  OE1 GLU A 445     5156   5034   5714     -6    -68    100       O  
ATOM   2095  OE2 GLU A 445      38.178  -0.550   8.192  1.00 37.10           O  
ANISOU 2095  OE2 GLU A 445     4563   4450   5081     -5    -85     97       O  
ATOM   2096  N   ILE A 446      31.440  -0.952   7.503  1.00 13.93           N  
ANISOU 2096  N   ILE A 446     1622   1543   2127    -16    -53     42       N  
ATOM   2097  CA  ILE A 446      30.220  -1.731   7.364  1.00 19.35           C  
ANISOU 2097  CA  ILE A 446     2294   2225   2833    -21    -40     23       C  
ATOM   2098  C   ILE A 446      29.216  -1.041   6.452  1.00 23.25           C  
ANISOU 2098  C   ILE A 446     2786   2745   3303    -20    -44     -3       C  
ATOM   2099  O   ILE A 446      28.661  -1.681   5.563  1.00 22.39           O  
ANISOU 2099  O   ILE A 446     2658   2640   3209    -24    -36    -34       O  
ATOM   2100  CB  ILE A 446      29.617  -2.089   8.728  1.00 19.92           C  
ANISOU 2100  CB  ILE A 446     2373   2281   2915    -21    -32     47       C  
ATOM   2101  CG1 ILE A 446      30.486  -3.165   9.391  1.00 25.65           C  
ANISOU 2101  CG1 ILE A 446     3093   2978   3673    -20    -23     67       C  
ATOM   2102  CG2 ILE A 446      28.188  -2.618   8.582  1.00 19.05           C  
ANISOU 2102  CG2 ILE A 446     2250   2169   2819    -26    -18     25       C  
ATOM   2103  CD1 ILE A 446      30.294  -3.283  10.890  1.00 25.87           C  
ANISOU 2103  CD1 ILE A 446     3136   2994   3701    -16    -20    101       C  
ATOM   2104  N   ALA A 447      29.017   0.268   6.631  1.00 21.68           N  
ANISOU 2104  N   ALA A 447     2605   2564   3066    -13    -57      8       N  
ATOM   2105  CA  ALA A 447      28.067   0.988   5.780  1.00 15.18           C  
ANISOU 2105  CA  ALA A 447     1782   1768   2219     -9    -62    -14       C  
ATOM   2106  C   ALA A 447      28.482   0.870   4.319  1.00 19.86           C  
ANISOU 2106  C   ALA A 447     2363   2375   2809     -8    -63    -41       C  
ATOM   2107  O   ALA A 447      27.669   0.506   3.482  1.00 18.30           O  
ANISOU 2107  O   ALA A 447     2148   2190   2614     -8    -59    -70       O  
ATOM   2108  CB  ALA A 447      27.927   2.455   6.181  1.00 17.45           C  
ANISOU 2108  CB  ALA A 447     2092   2070   2468     -2    -74      4       C  
ATOM   2109  N   ARG A 448      29.734   1.205   4.007  1.00 16.29           N  
ANISOU 2109  N   ARG A 448     1918   1921   2350     -7    -67    -32       N  
ATOM   2110  CA  ARG A 448      30.185   1.133   2.626  1.00 20.77           C  
ANISOU 2110  CA  ARG A 448     2476   2501   2913     -6    -67    -56       C  
ATOM   2111  C   ARG A 448      29.968  -0.275   2.067  1.00 20.20           C  
ANISOU 2111  C   ARG A 448     2378   2422   2877    -14    -55    -84       C  
ATOM   2112  O   ARG A 448      29.502  -0.441   0.942  1.00 16.37           O  
ANISOU 2112  O   ARG A 448     1879   1956   2387    -13    -53   -115       O  
ATOM   2113  CB  ARG A 448      31.667   1.515   2.480  1.00 20.40           C  
ANISOU 2113  CB  ARG A 448     2440   2449   2864     -6    -70    -42       C  
ATOM   2114  CG  ARG A 448      32.174   1.304   1.043  1.00 21.94           C  
ANISOU 2114  CG  ARG A 448     2624   2655   3057     -6    -67    -68       C  
ATOM   2115  CD  ARG A 448      33.650   1.652   0.829  1.00 24.30           C  
ANISOU 2115  CD  ARG A 448     2932   2947   3355     -7    -67    -57       C  
ATOM   2116  NE  ARG A 448      34.424   0.455   0.503  1.00 41.01           N  
ANISOU 2116  NE  ARG A 448     5029   5047   5507    -16    -59    -70       N  
ATOM   2117  CZ  ARG A 448      34.948   0.190  -0.690  1.00 33.62           C  
ANISOU 2117  CZ  ARG A 448     4083   4118   4574    -18    -53    -93       C  
ATOM   2118  NH1 ARG A 448      34.818   1.048  -1.690  1.00 42.34           N  
ANISOU 2118  NH1 ARG A 448     5196   5247   5644    -11    -56   -104       N  
ATOM   2119  NH2 ARG A 448      35.618  -0.933  -0.878  1.00 53.55           N  
ANISOU 2119  NH2 ARG A 448     6589   6625   7135    -26    -45   -105       N  
ATOM   2120  N   ARG A 449      30.319  -1.290   2.843  1.00 22.89           N  
ANISOU 2120  N   ARG A 449     2710   2734   3254    -21    -45    -74       N  
ATOM   2121  CA  ARG A 449      30.193  -2.654   2.333  1.00 24.27           C  
ANISOU 2121  CA  ARG A 449     2859   2897   3467    -30    -30   -100       C  
ATOM   2122  C   ARG A 449      28.739  -3.017   1.995  1.00 22.89           C  
ANISOU 2122  C   ARG A 449     2667   2733   3296    -33    -24   -130       C  
ATOM   2123  O   ARG A 449      28.464  -3.634   0.956  1.00 19.55           O  
ANISOU 2123  O   ARG A 449     2222   2321   2886    -37    -17   -166       O  
ATOM   2124  CB  ARG A 449      30.816  -3.675   3.291  1.00 24.28           C  
ANISOU 2124  CB  ARG A 449     2855   2863   3508    -36    -19    -80       C  
ATOM   2125  CG  ARG A 449      30.875  -5.065   2.686  1.00 39.31           C  
ANISOU 2125  CG  ARG A 449     4731   4750   5454    -45     -1   -108       C  
ATOM   2126  CD  ARG A 449      31.980  -5.926   3.273  1.00 54.56           C  
ANISOU 2126  CD  ARG A 449     6660   6650   7422    -47      8    -87       C  
ATOM   2127  NE  ARG A 449      32.879  -6.387   2.216  1.00 61.81           N  
ANISOU 2127  NE  ARG A 449     7564   7567   8356    -51     12   -109       N  
ATOM   2128  CZ  ARG A 449      34.166  -6.673   2.385  1.00 64.30           C  
ANISOU 2128  CZ  ARG A 449     7879   7865   8687    -51     12    -93       C  
ATOM   2129  NH1 ARG A 449      34.728  -6.555   3.583  1.00 69.81           N  
ANISOU 2129  NH1 ARG A 449     8592   8547   9387    -44      7    -55       N  
ATOM   2130  NH2 ARG A 449      34.897  -7.075   1.353  1.00 67.44           N  
ANISOU 2130  NH2 ARG A 449     8262   8263   9098    -56     17   -117       N  
ATOM   2131  N   ARG A 450      27.809  -2.644   2.865  1.00 18.47           N  
ANISOU 2131  N   ARG A 450     2116   2174   2727    -30    -26   -116       N  
ATOM   2132  CA  ARG A 450      26.405  -2.974   2.616  1.00 18.73           C  
ANISOU 2132  CA  ARG A 450     2132   2217   2766    -33    -19   -145       C  
ATOM   2133  C   ARG A 450      25.839  -2.184   1.436  1.00 22.52           C  
ANISOU 2133  C   ARG A 450     2609   2737   3211    -24    -32   -172       C  
ATOM   2134  O   ARG A 450      24.980  -2.684   0.699  1.00 14.21           O  
ANISOU 2134  O   ARG A 450     1533   1699   2166    -27    -27   -210       O  
ATOM   2135  CB  ARG A 450      25.561  -2.756   3.875  1.00 17.46           C  
ANISOU 2135  CB  ARG A 450     1982   2046   2605    -32    -17   -124       C  
ATOM   2136  CG  ARG A 450      26.175  -3.357   5.134  1.00 22.34           C  
ANISOU 2136  CG  ARG A 450     2609   2629   3249    -36     -7    -91       C  
ATOM   2137  CD  ARG A 450      26.305  -4.877   5.004  1.00 26.46           C  
ANISOU 2137  CD  ARG A 450     3108   3125   3821    -47     15   -107       C  
ATOM   2138  NE  ARG A 450      25.015  -5.478   4.682  1.00 25.31           N  
ANISOU 2138  NE  ARG A 450     2940   2983   3694    -53     29   -142       N  
ATOM   2139  CZ  ARG A 450      24.766  -6.787   4.704  1.00 41.85           C  
ANISOU 2139  CZ  ARG A 450     5013   5053   5836    -64     53   -159       C  
ATOM   2140  NH1 ARG A 450      25.729  -7.652   5.029  1.00 34.64           N  
ANISOU 2140  NH1 ARG A 450     4098   4110   4955    -67     66   -143       N  
ATOM   2141  NH2 ARG A 450      23.549  -7.231   4.397  1.00 32.60           N  
ANISOU 2141  NH2 ARG A 450     3820   3887   4680    -70     66   -195       N  
ATOM   2142  N   ILE A 451      26.311  -0.949   1.255  1.00 14.81           N  
ANISOU 2142  N   ILE A 451     1655   1777   2195    -14    -47   -153       N  
ATOM   2143  CA  ILE A 451      25.866  -0.157   0.109  1.00 17.05           C  
ANISOU 2143  CA  ILE A 451     1938   2097   2442     -2    -58   -174       C  
ATOM   2144  C   ILE A 451      26.342  -0.827  -1.190  1.00 19.59           C  
ANISOU 2144  C   ILE A 451     2240   2430   2772     -5    -54   -206       C  
ATOM   2145  O   ILE A 451      25.574  -1.007  -2.145  1.00 18.59           O  
ANISOU 2145  O   ILE A 451     2094   2330   2637     -2    -55   -242       O  
ATOM   2146  CB  ILE A 451      26.370   1.299   0.181  1.00 22.87           C  
ANISOU 2146  CB  ILE A 451     2705   2847   3139     10    -71   -145       C  
ATOM   2147  CG1 ILE A 451      25.572   2.085   1.243  1.00 21.20           C  
ANISOU 2147  CG1 ILE A 451     2509   2634   2913     14    -77   -122       C  
ATOM   2148  CG2 ILE A 451      26.347   1.946  -1.222  1.00 15.64           C  
ANISOU 2148  CG2 ILE A 451     1789   1965   2189     22    -79   -164       C  
ATOM   2149  CD1 ILE A 451      26.187   3.442   1.639  1.00 19.96           C  
ANISOU 2149  CD1 ILE A 451     2381   2478   2724     23    -86    -89       C  
ATOM   2150  N   LEU A 452      27.615  -1.195  -1.214  1.00 18.87           N  
ANISOU 2150  N   LEU A 452     2152   2320   2698    -12    -49   -195       N  
ATOM   2151  CA  LEU A 452      28.194  -1.888  -2.362  1.00 20.60           C  
ANISOU 2151  CA  LEU A 452     2352   2545   2929    -17    -42   -224       C  
ATOM   2152  C   LEU A 452      27.513  -3.231  -2.649  1.00 21.16           C  
ANISOU 2152  C   LEU A 452     2390   2610   3038    -28    -28   -262       C  
ATOM   2153  O   LEU A 452      27.194  -3.529  -3.797  1.00 25.37           O  
ANISOU 2153  O   LEU A 452     2904   3168   3566    -28    -27   -300       O  
ATOM   2154  CB  LEU A 452      29.689  -2.102  -2.162  1.00 16.32           C  
ANISOU 2154  CB  LEU A 452     1819   1979   2404    -22    -38   -204       C  
ATOM   2155  CG  LEU A 452      30.581  -0.900  -2.483  1.00 22.27           C  
ANISOU 2155  CG  LEU A 452     2596   2743   3120    -13    -49   -183       C  
ATOM   2156  CD1 LEU A 452      32.017  -1.150  -2.003  1.00 22.74           C  
ANISOU 2156  CD1 LEU A 452     2663   2774   3202    -19    -44   -161       C  
ATOM   2157  CD2 LEU A 452      30.553  -0.639  -3.984  1.00 26.09           C  
ANISOU 2157  CD2 LEU A 452     3074   3260   3579     -7    -51   -212       C  
ATOM   2158  N   MET A 453      27.302  -4.042  -1.617  1.00 18.86           N  
ANISOU 2158  N   MET A 453     2093   2287   2785    -37    -16   -252       N  
ATOM   2159  CA  MET A 453      26.593  -5.306  -1.812  1.00 30.25           C  
ANISOU 2159  CA  MET A 453     3504   3721   4268    -49      2   -288       C  
ATOM   2160  C   MET A 453      25.211  -5.087  -2.437  1.00 28.02           C  
ANISOU 2160  C   MET A 453     3206   3473   3967    -45     -3   -324       C  
ATOM   2161  O   MET A 453      24.754  -5.886  -3.257  1.00 20.92           O  
ANISOU 2161  O   MET A 453     2278   2586   3086    -51      6   -369       O  
ATOM   2162  CB  MET A 453      26.435  -6.072  -0.501  1.00 25.05           C  
ANISOU 2162  CB  MET A 453     2845   3023   3649    -57     18   -267       C  
ATOM   2163  CG  MET A 453      27.719  -6.427   0.240  1.00 27.15           C  
ANISOU 2163  CG  MET A 453     3124   3255   3938    -60     23   -231       C  
ATOM   2164  SD  MET A 453      27.219  -7.136   1.821  1.00 36.01           S  
ANISOU 2164  SD  MET A 453     4248   4337   5095    -65     40   -204       S  
ATOM   2165  CE  MET A 453      28.559  -6.747   2.917  1.00 42.00           C  
ANISOU 2165  CE  MET A 453     5036   5075   5849    -58     32   -149       C  
ATOM   2166  N   TRP A 454      24.521  -4.020  -2.041  1.00 14.70           N  
ANISOU 2166  N   TRP A 454     1538   1804   2245    -33    -17   -307       N  
ATOM   2167  CA  TRP A 454      23.213  -3.764  -2.648  1.00 17.42           C  
ANISOU 2167  CA  TRP A 454     1866   2182   2569    -26    -24   -341       C  
ATOM   2168  C   TRP A 454      23.360  -3.517  -4.155  1.00 20.19           C  
ANISOU 2168  C   TRP A 454     2207   2572   2891    -18    -34   -372       C  
ATOM   2169  O   TRP A 454      22.613  -4.089  -4.957  1.00 18.07           O  
ANISOU 2169  O   TRP A 454     1909   2326   2630    -20    -31   -419       O  
ATOM   2170  CB  TRP A 454      22.447  -2.624  -1.957  1.00 14.00           C  
ANISOU 2170  CB  TRP A 454     1455   1761   2105    -14    -38   -316       C  
ATOM   2171  CG  TRP A 454      21.029  -2.460  -2.458  1.00 14.80           C  
ANISOU 2171  CG  TRP A 454     1537   1895   2192     -7    -44   -352       C  
ATOM   2172  CD1 TRP A 454      19.890  -2.944  -1.875  1.00 18.09           C  
ANISOU 2172  CD1 TRP A 454     1938   2304   2632    -14    -34   -369       C  
ATOM   2173  CD2 TRP A 454      20.605  -1.770  -3.643  1.00 16.97           C  
ANISOU 2173  CD2 TRP A 454     1806   2216   2424      9    -60   -375       C  
ATOM   2174  NE1 TRP A 454      18.781  -2.591  -2.619  1.00 18.77           N  
ANISOU 2174  NE1 TRP A 454     2007   2430   2695     -4    -45   -403       N  
ATOM   2175  CE2 TRP A 454      19.197  -1.868  -3.708  1.00 15.57           C  
ANISOU 2175  CE2 TRP A 454     1609   2060   2249     12    -62   -407       C  
ATOM   2176  CE3 TRP A 454      21.279  -1.071  -4.653  1.00 20.56           C  
ANISOU 2176  CE3 TRP A 454     2274   2698   2842     22    -73   -372       C  
ATOM   2177  CZ2 TRP A 454      18.455  -1.306  -4.743  1.00 21.87           C  
ANISOU 2177  CZ2 TRP A 454     2395   2905   3009     29    -78   -435       C  
ATOM   2178  CZ3 TRP A 454      20.538  -0.499  -5.671  1.00 21.79           C  
ANISOU 2178  CZ3 TRP A 454     2420   2900   2959     40    -87   -397       C  
ATOM   2179  CH2 TRP A 454      19.140  -0.617  -5.710  1.00 16.94           C  
ANISOU 2179  CH2 TRP A 454     1785   2308   2345     44    -91   -428       C  
ATOM   2180  N   HIS A 455      24.337  -2.713  -4.552  1.00 15.24           N  
ANISOU 2180  N   HIS A 455     1603   1955   2234     -9    -45   -349       N  
ATOM   2181  CA  HIS A 455      24.518  -2.412  -5.970  1.00 18.45           C  
ANISOU 2181  CA  HIS A 455     2003   2399   2609      1    -53   -375       C  
ATOM   2182  C   HIS A 455      24.989  -3.603  -6.817  1.00 22.71           C  
ANISOU 2182  C   HIS A 455     2513   2936   3178    -12    -39   -413       C  
ATOM   2183  O   HIS A 455      24.644  -3.698  -7.989  1.00 26.18           O  
ANISOU 2183  O   HIS A 455     2936   3412   3601     -7    -43   -451       O  
ATOM   2184  CB  HIS A 455      25.415  -1.190  -6.162  1.00 16.98           C  
ANISOU 2184  CB  HIS A 455     1849   2220   2382     14    -64   -339       C  
ATOM   2185  CG  HIS A 455      24.749   0.100  -5.798  1.00 19.67           C  
ANISOU 2185  CG  HIS A 455     2212   2577   2683     32    -78   -315       C  
ATOM   2186  ND1 HIS A 455      23.872   0.747  -6.639  1.00 22.71           N  
ANISOU 2186  ND1 HIS A 455     2594   3005   3030     50    -91   -333       N  
ATOM   2187  CD2 HIS A 455      24.810   0.846  -4.671  1.00 15.74           C  
ANISOU 2187  CD2 HIS A 455     1740   2060   2181     34    -82   -275       C  
ATOM   2188  CE1 HIS A 455      23.432   1.844  -6.053  1.00 20.05           C  
ANISOU 2188  CE1 HIS A 455     2280   2671   2667     62   -100   -304       C  
ATOM   2189  NE2 HIS A 455      23.985   1.927  -4.858  1.00 24.73           N  
ANISOU 2189  NE2 HIS A 455     2890   3227   3280     52    -95   -269       N  
ATOM   2190  N   LYS A 456      25.758  -4.512  -6.226  1.00 20.19           N  
ANISOU 2190  N   LYS A 456     2190   2576   2905    -29    -23   -404       N  
ATOM   2191  CA  LYS A 456      26.172  -5.731  -6.945  1.00 27.97           C  
ANISOU 2191  CA  LYS A 456     3147   3555   3927    -43     -7   -441       C  
ATOM   2192  C   LYS A 456      24.984  -6.635  -7.282  1.00 24.70           C  
ANISOU 2192  C   LYS A 456     2695   3152   3536    -51      3   -491       C  
ATOM   2193  O   LYS A 456      25.034  -7.425  -8.219  1.00 31.53           O  
ANISOU 2193  O   LYS A 456     3533   4029   4418    -59     12   -535       O  
ATOM   2194  CB  LYS A 456      27.159  -6.555  -6.125  1.00 26.80           C  
ANISOU 2194  CB  LYS A 456     3000   3357   3826    -57      9   -418       C  
ATOM   2195  CG  LYS A 456      28.469  -5.873  -5.824  1.00 31.70           C  
ANISOU 2195  CG  LYS A 456     3650   3963   4431    -52      2   -376       C  
ATOM   2196  CD  LYS A 456      29.401  -6.884  -5.173  1.00 37.20           C  
ANISOU 2196  CD  LYS A 456     4341   4615   5179    -65     19   -362       C  
ATOM   2197  CE  LYS A 456      30.341  -6.238  -4.168  1.00 48.61           C  
ANISOU 2197  CE  LYS A 456     5816   6036   6617    -60     12   -310       C  
ATOM   2198  NZ  LYS A 456      31.711  -6.037  -4.716  1.00 46.56           N  
ANISOU 2198  NZ  LYS A 456     5564   5774   6352    -60     10   -302       N  
ATOM   2199  N   LYS A 457      23.916  -6.532  -6.500  1.00 28.75           N  
ANISOU 2199  N   LYS A 457     3208   3662   4055    -50      2   -488       N  
ATOM   2200  CA  LYS A 457      22.785  -7.442  -6.649  1.00 25.88           C  
ANISOU 2200  CA  LYS A 457     2808   3303   3722    -60     15   -535       C  
ATOM   2201  C   LYS A 457      21.485  -6.769  -7.081  1.00 30.23           C  
ANISOU 2201  C   LYS A 457     3351   3899   4236    -46     -1   -560       C  
ATOM   2202  O   LYS A 457      20.435  -7.402  -7.102  1.00 31.21           O  
ANISOU 2202  O   LYS A 457     3446   4029   4383    -53      8   -599       O  
ATOM   2203  CB  LYS A 457      22.560  -8.212  -5.350  1.00 29.77           C  
ANISOU 2203  CB  LYS A 457     3299   3747   4265    -74     36   -518       C  
ATOM   2204  CG  LYS A 457      23.841  -8.656  -4.668  1.00 32.78           C  
ANISOU 2204  CG  LYS A 457     3696   4083   4676    -82     48   -480       C  
ATOM   2205  CD  LYS A 457      23.549  -9.333  -3.344  1.00 52.12           C  
ANISOU 2205  CD  LYS A 457     6146   6488   7169    -91     68   -459       C  
ATOM   2206  CE  LYS A 457      24.100  -8.536  -2.176  1.00 49.54           C  
ANISOU 2206  CE  LYS A 457     5858   6141   6824    -83     58   -397       C  
ATOM   2207  NZ  LYS A 457      23.103  -7.570  -1.644  1.00 37.86           N  
ANISOU 2207  NZ  LYS A 457     4393   4680   5312    -73     44   -384       N  
ATOM   2208  N   ASN A 458      21.557  -5.491  -7.428  1.00 25.23           N  
ANISOU 2208  N   ASN A 458     2743   3297   3547    -26    -25   -538       N  
ATOM   2209  CA  ASN A 458      20.364  -4.753  -7.825  1.00 27.32           C  
ANISOU 2209  CA  ASN A 458     3002   3605   3772     -9    -42   -556       C  
ATOM   2210  C   ASN A 458      20.628  -3.838  -9.008  1.00 24.59           C  
ANISOU 2210  C   ASN A 458     2667   3307   3370     12    -62   -559       C  
ATOM   2211  O   ASN A 458      21.702  -3.261  -9.122  1.00 28.85           O  
ANISOU 2211  O   ASN A 458     3234   3839   3890     18    -66   -525       O  
ATOM   2212  CB  ASN A 458      19.826  -3.943  -6.639  1.00 24.20           C  
ANISOU 2212  CB  ASN A 458     2632   3196   3367     -2    -49   -516       C  
ATOM   2213  CG  ASN A 458      19.229  -4.825  -5.564  1.00 21.40           C  
ANISOU 2213  CG  ASN A 458     2263   2804   3064    -20    -29   -521       C  
ATOM   2214  OD1 ASN A 458      18.041  -5.143  -5.603  1.00 24.18           O  
ANISOU 2214  OD1 ASN A 458     2591   3171   3427    -22    -26   -556       O  
ATOM   2215  ND2 ASN A 458      20.051  -5.248  -4.616  1.00 19.17           N  
ANISOU 2215  ND2 ASN A 458     1995   2474   2813    -32    -15   -486       N  
ATOM   2216  N   GLY A 459      19.640  -3.698  -9.880  1.00 26.42           N  
ANISOU 2216  N   GLY A 459     2876   3586   3575     25    -74   -599       N  
ATOM   2217  CA  GLY A 459      19.743  -2.764 -10.980  1.00 33.56           C  
ANISOU 2217  CA  GLY A 459     3793   4539   4422     49    -93   -600       C  
ATOM   2218  C   GLY A 459      19.587  -1.350 -10.457  1.00 37.18           C  
ANISOU 2218  C   GLY A 459     4288   5001   4840     70   -109   -551       C  
ATOM   2219  O   GLY A 459      18.823  -1.110  -9.528  1.00 31.98           O  
ANISOU 2219  O   GLY A 459     3632   4328   4189     70   -110   -538       O  
ATOM   2220  N   ALA A 460      20.316  -0.411 -11.047  1.00 32.04           N  
ANISOU 2220  N   ALA A 460     3664   4367   4145     87   -118   -524       N  
ATOM   2221  CA  ALA A 460      20.223   0.979 -10.630  1.00 42.93           C  
ANISOU 2221  CA  ALA A 460     5078   5749   5485    107   -131   -478       C  
ATOM   2222  C   ALA A 460      18.770   1.434 -10.663  1.00 40.24           C  
ANISOU 2222  C   ALA A 460     4725   5442   5123    125   -145   -494       C  
ATOM   2223  O   ALA A 460      18.044   1.138 -11.607  1.00 42.67           O  
ANISOU 2223  O   ALA A 460     5005   5793   5415    135   -154   -538       O  
ATOM   2224  CB  ALA A 460      21.080   1.858 -11.521  1.00 47.12           C  
ANISOU 2224  CB  ALA A 460     5634   6300   5970    125   -136   -456       C  
ATOM   2225  N   PRO A 461      18.349   2.144  -9.623  1.00 43.79           N  
ANISOU 2225  N   PRO A 461     5194   5873   5572    129   -149   -461       N  
ATOM   2226  CA  PRO A 461      16.972   2.636  -9.544  1.00 39.97           C  
ANISOU 2226  CA  PRO A 461     4701   5418   5070    146   -162   -473       C  
ATOM   2227  C   PRO A 461      16.685   3.639 -10.653  1.00 42.84           C  
ANISOU 2227  C   PRO A 461     5072   5833   5374    179   -180   -473       C  
ATOM   2228  O   PRO A 461      17.612   4.255 -11.175  1.00 44.91           O  
ANISOU 2228  O   PRO A 461     5360   6098   5607    190   -181   -446       O  
ATOM   2229  CB  PRO A 461      16.922   3.330  -8.179  1.00 43.16           C  
ANISOU 2229  CB  PRO A 461     5133   5785   5483    143   -159   -427       C  
ATOM   2230  CG  PRO A 461      18.075   2.781  -7.414  1.00 38.88           C  
ANISOU 2230  CG  PRO A 461     4602   5193   4977    118   -143   -403       C  
ATOM   2231  CD  PRO A 461      19.130   2.497  -8.428  1.00 35.73           C  
ANISOU 2231  CD  PRO A 461     4204   4804   4569    117   -140   -411       C  
ATOM   2232  N   PRO A 462      15.416   3.794 -11.009  1.00 45.16           N  
ANISOU 2232  N   PRO A 462     5345   6166   5650    197   -194   -502       N  
ATOM   2233  CA  PRO A 462      15.028   4.731 -12.066  1.00 56.34           C  
ANISOU 2233  CA  PRO A 462     6766   7634   7007    232   -213   -502       C  
ATOM   2234  C   PRO A 462      15.535   6.135 -11.760  1.00 54.47           C  
ANISOU 2234  C   PRO A 462     6574   7384   6737    251   -215   -442       C  
ATOM   2235  O   PRO A 462      15.209   6.695 -10.716  1.00 53.99           O  
ANISOU 2235  O   PRO A 462     6530   7298   6686    250   -214   -413       O  
ATOM   2236  CB  PRO A 462      13.499   4.691 -12.021  1.00 53.34           C  
ANISOU 2236  CB  PRO A 462     6357   7285   6624    244   -226   -536       C  
ATOM   2237  CG  PRO A 462      13.175   3.365 -11.435  1.00 55.87           C  
ANISOU 2237  CG  PRO A 462     6645   7580   7003    211   -212   -575       C  
ATOM   2238  CD  PRO A 462      14.254   3.103 -10.430  1.00 50.97           C  
ANISOU 2238  CD  PRO A 462     6048   6898   6419    184   -193   -537       C  
ATOM   2239  N   LEU A 463      16.333   6.688 -12.664  1.00 95.62           N  
ANISOU 2239  N   LEU A 463    11807  12614  11912    268   -216   -425       N  
ATOM   2240  CA  LEU A 463      16.962   7.986 -12.450  1.00101.50           C  
ANISOU 2240  CA  LEU A 463    12594  13343  12627    284   -214   -369       C  
ATOM   2241  C   LEU A 463      15.983   9.066 -11.995  1.00109.98           C  
ANISOU 2241  C   LEU A 463    13680  14426  13680    307   -224   -346       C  
ATOM   2242  O   LEU A 463      16.311   9.893 -11.147  1.00105.03           O  
ANISOU 2242  O   LEU A 463    13083  13767  13057    306   -218   -303       O  
ATOM   2243  CB  LEU A 463      17.683   8.440 -13.719  1.00 65.97           C  
ANISOU 2243  CB  LEU A 463     8109   8872   8083    305   -214   -361       C  
ATOM   2244  CG  LEU A 463      19.097   8.987 -13.527  1.00 64.69           C  
ANISOU 2244  CG  LEU A 463     7984   8674   7921    297   -198   -317       C  
ATOM   2245  CD1 LEU A 463      19.670   9.465 -14.850  1.00 64.30           C  
ANISOU 2245  CD1 LEU A 463     7948   8657   7825    321   -197   -311       C  
ATOM   2246  CD2 LEU A 463      19.115  10.103 -12.493  1.00 63.39           C  
ANISOU 2246  CD2 LEU A 463     7851   8477   7757    302   -194   -268       C  
ATOM   2247  N   ALA A 464      14.786   9.056 -12.568  1.00 89.00           N  
ANISOU 2247  N   ALA A 464    10998  11816  11002    329   -241   -378       N  
ATOM   2248  CA  ALA A 464      13.794  10.089 -12.288  1.00 95.30           C  
ANISOU 2248  CA  ALA A 464    11804  12629  11776    355   -253   -360       C  
ATOM   2249  C   ALA A 464      13.335  10.095 -10.834  1.00 87.80           C  
ANISOU 2249  C   ALA A 464    10856  11638  10866    335   -247   -348       C  
ATOM   2250  O   ALA A 464      13.185  11.154 -10.229  1.00 88.17           O  
ANISOU 2250  O   ALA A 464    10928  11670  10901    347   -247   -310       O  
ATOM   2251  CB  ALA A 464      12.597   9.940 -13.222  1.00103.90           C  
ANISOU 2251  CB  ALA A 464    12862  13780  12837    382   -273   -403       C  
ATOM   2252  N   GLU A 465      13.108   8.909 -10.283  1.00113.09           N  
ANISOU 2252  N   GLU A 465    14032  14823  14115    305   -241   -382       N  
ATOM   2253  CA  GLU A 465      12.596   8.777  -8.925  1.00114.65           C  
ANISOU 2253  CA  GLU A 465    14228  14984  14351    285   -235   -375       C  
ATOM   2254  C   GLU A 465      13.702   8.828  -7.875  1.00103.13           C  
ANISOU 2254  C   GLU A 465    12798  13469  12919    260   -217   -334       C  
ATOM   2255  O   GLU A 465      13.433   8.743  -6.680  1.00101.32           O  
ANISOU 2255  O   GLU A 465    12571  13207  12720    242   -210   -323       O  
ATOM   2256  CB  GLU A 465      11.801   7.477  -8.787  1.00 77.59           C  
ANISOU 2256  CB  GLU A 465     9491  10295   9695    264   -233   -428       C  
ATOM   2257  CG  GLU A 465      10.443   7.636  -8.116  1.00 77.34           C  
ANISOU 2257  CG  GLU A 465     9444  10268   9675    268   -239   -443       C  
ATOM   2258  CD  GLU A 465       9.634   8.787  -8.686  1.00 78.45           C  
ANISOU 2258  CD  GLU A 465     9589  10451   9768    307   -259   -436       C  
ATOM   2259  OE1 GLU A 465       9.839   9.141  -9.864  1.00 79.38           O  
ANISOU 2259  OE1 GLU A 465     9708  10608   9844    333   -270   -439       O  
ATOM   2260  OE2 GLU A 465       8.791   9.339  -7.949  1.00 78.26           O  
ANISOU 2260  OE2 GLU A 465     9567  10421   9748    313   -262   -426       O  
ATOM   2261  N   ARG A 466      14.944   8.968  -8.324  1.00 46.58           N  
ANISOU 2261  N   ARG A 466     5656   6298   5746    258   -210   -313       N  
ATOM   2262  CA  ARG A 466      16.077   9.001  -7.409  1.00 48.07           C  
ANISOU 2262  CA  ARG A 466     5869   6436   5958    236   -195   -278       C  
ATOM   2263  C   ARG A 466      16.214  10.354  -6.716  1.00 44.69           C  
ANISOU 2263  C   ARG A 466     5476   5990   5512    247   -194   -230       C  
ATOM   2264  O   ARG A 466      16.248  11.395  -7.366  1.00 38.24           O  
ANISOU 2264  O   ARG A 466     4678   5195   4657    274   -199   -211       O  
ATOM   2265  CB  ARG A 466      17.371   8.643  -8.144  1.00 49.47           C  
ANISOU 2265  CB  ARG A 466     6054   6611   6133    229   -188   -276       C  
ATOM   2266  CG  ARG A 466      18.478   8.137  -7.237  1.00 53.93           C  
ANISOU 2266  CG  ARG A 466     6629   7125   6735    199   -172   -257       C  
ATOM   2267  CD  ARG A 466      18.805   6.673  -7.497  1.00 46.07           C  
ANISOU 2267  CD  ARG A 466     5607   6124   5774    177   -165   -292       C  
ATOM   2268  NE  ARG A 466      20.156   6.509  -8.018  1.00 48.98           N  
ANISOU 2268  NE  ARG A 466     5987   6482   6142    170   -157   -283       N  
ATOM   2269  CZ  ARG A 466      21.132   5.849  -7.400  1.00 38.74           C  
ANISOU 2269  CZ  ARG A 466     4692   5146   4880    146   -144   -273       C  
ATOM   2270  NH1 ARG A 466      20.921   5.276  -6.226  1.00 36.32           N  
ANISOU 2270  NH1 ARG A 466     4379   4807   4612    126   -138   -270       N  
ATOM   2271  NH2 ARG A 466      22.325   5.765  -7.964  1.00 44.16           N  
ANISOU 2271  NH2 ARG A 466     5388   5826   5564    142   -137   -267       N  
ATOM   2272  N   GLY A 467      16.287  10.324  -5.389  1.00 36.81           N  
ANISOU 2272  N   GLY A 467     4487   4954   4545    227   -185   -212       N  
ATOM   2273  CA  GLY A 467      16.425  11.535  -4.598  1.00 29.24           C  
ANISOU 2273  CA  GLY A 467     3559   3976   3576    233   -182   -170       C  
ATOM   2274  C   GLY A 467      15.092  12.072  -4.116  1.00 34.66           C  
ANISOU 2274  C   GLY A 467     4239   4672   4256    246   -190   -172       C  
ATOM   2275  O   GLY A 467      15.036  13.147  -3.519  1.00 35.41           O  
ANISOU 2275  O   GLY A 467     4358   4755   4342    254   -188   -141       O  
ATOM   2276  N   LYS A 468      14.023  11.316  -4.368  1.00 37.88           N  
ANISOU 2276  N   LYS A 468     4616   5104   4675    246   -198   -212       N  
ATOM   2277  CA  LYS A 468      12.668  11.702  -3.968  1.00 38.90           C  
ANISOU 2277  CA  LYS A 468     4733   5245   4801    257   -206   -222       C  
ATOM   2278  C   LYS A 468      12.216  11.020  -2.679  1.00 40.87           C  
ANISOU 2278  C   LYS A 468     4972   5464   5093    230   -197   -230       C  
ATOM   2279  O   LYS A 468      11.198  11.382  -2.091  1.00 43.70           O  
ANISOU 2279  O   LYS A 468     5325   5823   5455    234   -200   -232       O  
ATOM   2280  CB  LYS A 468      11.673  11.389  -5.086  1.00 44.61           C  
ANISOU 2280  CB  LYS A 468     5426   6018   5506    278   -221   -263       C  
ATOM   2281  CG  LYS A 468      11.783  12.300  -6.300  1.00 58.26           C  
ANISOU 2281  CG  LYS A 468     7166   7784   7184    314   -233   -252       C  
ATOM   2282  CD  LYS A 468      10.403  12.758  -6.761  1.00 68.78           C  
ANISOU 2282  CD  LYS A 468     8481   9160   8494    344   -250   -272       C  
ATOM   2283  CE  LYS A 468      10.248  12.599  -8.268  1.00 73.11           C  
ANISOU 2283  CE  LYS A 468     9012   9760   9005    370   -264   -299       C  
ATOM   2284  NZ  LYS A 468      11.344  13.279  -9.024  1.00 71.19           N  
ANISOU 2284  NZ  LYS A 468     8800   9521   8728    386   -260   -266       N  
ATOM   2285  N   GLY A 469      12.975  10.019  -2.257  1.00 27.79           N  
ANISOU 2285  N   GLY A 469     3312   3779   3469    202   -185   -233       N  
ATOM   2286  CA  GLY A 469      12.714   9.303  -1.021  1.00 30.73           C  
ANISOU 2286  CA  GLY A 469     3677   4118   3881    176   -173   -236       C  
ATOM   2287  C   GLY A 469      13.987   8.542  -0.672  1.00 25.89           C  
ANISOU 2287  C   GLY A 469     3072   3472   3293    152   -161   -223       C  
ATOM   2288  O   GLY A 469      15.052   8.827  -1.217  1.00 24.82           O  
ANISOU 2288  O   GLY A 469     2952   3336   3141    157   -161   -206       O  
ATOM   2289  N   ILE A 470      13.887   7.565   0.214  1.00 21.00           N  
ANISOU 2289  N   ILE A 470     2441   2824   2713    128   -148   -231       N  
ATOM   2290  CA  ILE A 470      15.066   6.860   0.658  1.00 21.40           C  
ANISOU 2290  CA  ILE A 470     2500   2842   2787    108   -136   -216       C  
ATOM   2291  C   ILE A 470      15.704   6.045  -0.465  1.00 25.68           C  
ANISOU 2291  C   ILE A 470     3026   3397   3334    106   -136   -240       C  
ATOM   2292  O   ILE A 470      15.025   5.544  -1.355  1.00 24.17           O  
ANISOU 2292  O   ILE A 470     2807   3233   3142    112   -140   -279       O  
ATOM   2293  CB  ILE A 470      14.775   5.945   1.854  1.00 23.58           C  
ANISOU 2293  CB  ILE A 470     2768   3085   3105     85   -121   -218       C  
ATOM   2294  CG1 ILE A 470      13.857   4.811   1.422  1.00 29.70           C  
ANISOU 2294  CG1 ILE A 470     3507   3872   3907     77   -115   -265       C  
ATOM   2295  CG2 ILE A 470      14.200   6.746   3.027  1.00 20.82           C  
ANISOU 2295  CG2 ILE A 470     2436   2724   2752     85   -120   -193       C  
ATOM   2296  CD1 ILE A 470      13.943   3.618   2.323  1.00 37.33           C  
ANISOU 2296  CD1 ILE A 470     4464   4801   4919     53    -95   -268       C  
ATOM   2297  N   ASP A 471      17.025   5.945  -0.411  1.00 24.02           N  
ANISOU 2297  N   ASP A 471     2833   3167   3128     98   -130   -217       N  
ATOM   2298  CA  ASP A 471      17.804   5.118  -1.330  1.00 20.21           C  
ANISOU 2298  CA  ASP A 471     2337   2689   2655     93   -127   -237       C  
ATOM   2299  C   ASP A 471      17.866   3.724  -0.728  1.00 22.18           C  
ANISOU 2299  C   ASP A 471     2567   2908   2952     69   -112   -252       C  
ATOM   2300  O   ASP A 471      18.279   3.582   0.422  1.00 21.09           O  
ANISOU 2300  O   ASP A 471     2443   2737   2834     56   -103   -224       O  
ATOM   2301  CB  ASP A 471      19.222   5.694  -1.419  1.00 18.39           C  
ANISOU 2301  CB  ASP A 471     2133   2445   2409     95   -127   -203       C  
ATOM   2302  CG  ASP A 471      20.131   4.883  -2.313  1.00 24.59           C  
ANISOU 2302  CG  ASP A 471     2907   3232   3204     88   -122   -221       C  
ATOM   2303  OD1 ASP A 471      21.211   4.435  -1.836  1.00 23.63           O  
ANISOU 2303  OD1 ASP A 471     2793   3081   3105     73   -113   -204       O  
ATOM   2304  OD2 ASP A 471      19.779   4.727  -3.501  1.00 26.16           O  
ANISOU 2304  OD2 ASP A 471     3089   3464   3387     99   -128   -251       O  
ATOM   2305  N   PRO A 472      17.450   2.689  -1.485  1.00 23.44           N  
ANISOU 2305  N   PRO A 472     2695   3081   3131     63   -107   -295       N  
ATOM   2306  CA  PRO A 472      17.442   1.334  -0.907  1.00 21.43           C  
ANISOU 2306  CA  PRO A 472     2421   2796   2926     41    -88   -310       C  
ATOM   2307  C   PRO A 472      18.817   0.835  -0.437  1.00 17.63           C  
ANISOU 2307  C   PRO A 472     1953   2279   2467     27    -78   -283       C  
ATOM   2308  O   PRO A 472      18.880   0.172   0.609  1.00 18.22           O  
ANISOU 2308  O   PRO A 472     2028   2319   2575     12    -63   -271       O  
ATOM   2309  CB  PRO A 472      16.878   0.464  -2.042  1.00 25.35           C  
ANISOU 2309  CB  PRO A 472     2880   3318   3433     39    -87   -365       C  
ATOM   2310  CG  PRO A 472      16.019   1.426  -2.842  1.00 28.08           C  
ANISOU 2310  CG  PRO A 472     3224   3711   3736     63   -106   -380       C  
ATOM   2311  CD  PRO A 472      16.751   2.748  -2.784  1.00 21.79           C  
ANISOU 2311  CD  PRO A 472     2464   2917   2898     78   -118   -334       C  
ATOM   2312  N   ALA A 473      19.889   1.144  -1.164  1.00 19.83           N  
ANISOU 2312  N   ALA A 473     2242   2565   2726     33    -84   -274       N  
ATOM   2313  CA  ALA A 473      21.223   0.762  -0.706  1.00 19.62           C  
ANISOU 2313  CA  ALA A 473     2229   2506   2719     22    -75   -248       C  
ATOM   2314  C   ALA A 473      21.538   1.372   0.668  1.00 22.08           C  
ANISOU 2314  C   ALA A 473     2568   2791   3029     20    -75   -203       C  
ATOM   2315  O   ALA A 473      21.979   0.683   1.587  1.00 16.97           O  
ANISOU 2315  O   ALA A 473     1923   2112   2414      7    -63   -187       O  
ATOM   2316  CB  ALA A 473      22.283   1.159  -1.730  1.00 15.43           C  
ANISOU 2316  CB  ALA A 473     1707   1991   2166     29    -82   -245       C  
ATOM   2317  N   CYS A 474      21.314   2.671   0.799  1.00 18.03           N  
ANISOU 2317  N   CYS A 474     2076   2294   2480     34    -88   -182       N  
ATOM   2318  CA  CYS A 474      21.519   3.349   2.081  1.00 17.81           C  
ANISOU 2318  CA  CYS A 474     2073   2246   2447     32    -88   -143       C  
ATOM   2319  C   CYS A 474      20.619   2.789   3.182  1.00 18.73           C  
ANISOU 2319  C   CYS A 474     2183   2344   2590     22    -78   -144       C  
ATOM   2320  O   CYS A 474      21.047   2.619   4.327  1.00 14.35           O  
ANISOU 2320  O   CYS A 474     1640   1762   2050     13    -72   -116       O  
ATOM   2321  CB  CYS A 474      21.283   4.851   1.929  1.00 16.07           C  
ANISOU 2321  CB  CYS A 474     1874   2047   2185     49   -101   -127       C  
ATOM   2322  SG  CYS A 474      22.537   5.696   0.949  1.00 19.76           S  
ANISOU 2322  SG  CYS A 474     2360   2527   2622     60   -108   -114       S  
ATOM   2323  N   GLN A 475      19.362   2.509   2.843  1.00 18.89           N  
ANISOU 2323  N   GLN A 475     2182   2381   2615     24    -77   -175       N  
ATOM   2324  CA  GLN A 475      18.439   1.948   3.826  1.00 18.45           C  
ANISOU 2324  CA  GLN A 475     2118   2307   2586     13    -65   -179       C  
ATOM   2325  C   GLN A 475      18.899   0.570   4.307  1.00 17.43           C  
ANISOU 2325  C   GLN A 475     1977   2145   2501     -4    -46   -180       C  
ATOM   2326  O   GLN A 475      18.799   0.262   5.493  1.00 19.76           O  
ANISOU 2326  O   GLN A 475     2280   2413   2814    -12    -34   -159       O  
ATOM   2327  CB  GLN A 475      17.002   1.872   3.284  1.00 22.54           C  
ANISOU 2327  CB  GLN A 475     2612   2850   3102     18    -67   -218       C  
ATOM   2328  CG  GLN A 475      15.981   1.467   4.341  1.00 23.84           C  
ANISOU 2328  CG  GLN A 475     2770   2996   3292      8    -53   -221       C  
ATOM   2329  CD  GLN A 475      15.835   2.528   5.432  1.00 20.48           C  
ANISOU 2329  CD  GLN A 475     2373   2565   2846     12    -58   -184       C  
ATOM   2330  OE1 GLN A 475      15.673   2.216   6.616  1.00 21.37           O  
ANISOU 2330  OE1 GLN A 475     2492   2650   2978      1    -45   -166       O  
ATOM   2331  NE2 GLN A 475      15.891   3.782   5.032  1.00 10.32           N  
ANISOU 2331  NE2 GLN A 475     1101   1301   1520     28    -76   -173       N  
ATOM   2332  N   ALA A 476      19.413  -0.257   3.395  1.00 23.04           N  
ANISOU 2332  N   ALA A 476     2670   2857   3229     -8    -41   -204       N  
ATOM   2333  CA  ALA A 476      19.938  -1.568   3.786  1.00 27.25           C  
ANISOU 2333  CA  ALA A 476     3191   3356   3806    -23    -21   -204       C  
ATOM   2334  C   ALA A 476      21.111  -1.371   4.735  1.00 25.13           C  
ANISOU 2334  C   ALA A 476     2949   3062   3537    -24    -21   -158       C  
ATOM   2335  O   ALA A 476      21.207  -2.038   5.774  1.00 26.88           O  
ANISOU 2335  O   ALA A 476     3173   3253   3786    -33     -7   -139       O  
ATOM   2336  CB  ALA A 476      20.371  -2.389   2.560  1.00 28.35           C  
ANISOU 2336  CB  ALA A 476     3307   3503   3961    -27    -17   -238       C  
ATOM   2337  N   ALA A 477      21.998  -0.443   4.390  1.00 16.12           N  
ANISOU 2337  N   ALA A 477     1827   1935   2365    -15    -38   -139       N  
ATOM   2338  CA  ALA A 477      23.122  -0.128   5.270  1.00 17.52           C  
ANISOU 2338  CA  ALA A 477     2028   2093   2538    -15    -40    -98       C  
ATOM   2339  C   ALA A 477      22.674   0.329   6.678  1.00 18.25           C  
ANISOU 2339  C   ALA A 477     2138   2173   2624    -15    -39    -69       C  
ATOM   2340  O   ALA A 477      23.164  -0.196   7.673  1.00 17.83           O  
ANISOU 2340  O   ALA A 477     2091   2093   2590    -21    -30    -45       O  
ATOM   2341  CB  ALA A 477      24.050   0.892   4.619  1.00 17.43           C  
ANISOU 2341  CB  ALA A 477     2032   2099   2493     -6    -56    -88       C  
ATOM   2342  N   ALA A 478      21.724   1.265   6.767  1.00 14.98           N  
ANISOU 2342  N   ALA A 478     1731   1778   2184     -9    -47    -72       N  
ATOM   2343  CA  ALA A 478      21.242   1.720   8.091  1.00 12.55           C  
ANISOU 2343  CA  ALA A 478     1439   1460   1870    -10    -45    -46       C  
ATOM   2344  C   ALA A 478      20.535   0.589   8.858  1.00 18.84           C  
ANISOU 2344  C   ALA A 478     2223   2232   2703    -21    -25    -51       C  
ATOM   2345  O   ALA A 478      20.710   0.420  10.077  1.00 17.21           O  
ANISOU 2345  O   ALA A 478     2030   2006   2505    -25    -17    -23       O  
ATOM   2346  CB  ALA A 478      20.322   2.946   7.951  1.00 11.46           C  
ANISOU 2346  CB  ALA A 478     1309   1347   1700     -1    -57    -51       C  
ATOM   2347  N   ASP A 479      19.742  -0.200   8.141  1.00 21.79           N  
ANISOU 2347  N   ASP A 479     2571   2610   3099    -26    -15    -88       N  
ATOM   2348  CA  ASP A 479      19.088  -1.365   8.742  1.00 24.56           C  
ANISOU 2348  CA  ASP A 479     2907   2935   3489    -37      9    -97       C  
ATOM   2349  C   ASP A 479      20.116  -2.343   9.340  1.00 23.69           C  
ANISOU 2349  C   ASP A 479     2800   2792   3408    -43     23    -73       C  
ATOM   2350  O   ASP A 479      20.014  -2.754  10.494  1.00 20.58           O  
ANISOU 2350  O   ASP A 479     2416   2374   3029    -47     37    -49       O  
ATOM   2351  CB  ASP A 479      18.243  -2.098   7.695  1.00 23.51           C  
ANISOU 2351  CB  ASP A 479     2742   2813   3378    -42     17   -146       C  
ATOM   2352  CG  ASP A 479      16.968  -1.353   7.337  1.00 33.41           C  
ANISOU 2352  CG  ASP A 479     3988   4095   4610    -36      8   -171       C  
ATOM   2353  OD1 ASP A 479      16.493  -0.535   8.153  1.00 32.78           O  
ANISOU 2353  OD1 ASP A 479     3926   4018   4512    -32      3   -151       O  
ATOM   2354  OD2 ASP A 479      16.425  -1.613   6.241  1.00 37.51           O  
ANISOU 2354  OD2 ASP A 479     4482   4635   5133    -35      6   -212       O  
ATOM   2355  N   TYR A 480      21.096  -2.728   8.536  1.00 20.92           N  
ANISOU 2355  N   TYR A 480     2443   2442   3065    -43     19    -79       N  
ATOM   2356  CA  TYR A 480      22.105  -3.670   9.003  1.00 17.56           C  
ANISOU 2356  CA  TYR A 480     2018   1985   2668    -46     32    -58       C  
ATOM   2357  C   TYR A 480      22.839  -3.128  10.233  1.00 23.68           C  
ANISOU 2357  C   TYR A 480     2821   2751   3425    -41     24    -11       C  
ATOM   2358  O   TYR A 480      23.069  -3.863  11.194  1.00 21.63           O  
ANISOU 2358  O   TYR A 480     2566   2464   3188    -43     39     13       O  
ATOM   2359  CB  TYR A 480      23.092  -4.013   7.884  1.00 20.03           C  
ANISOU 2359  CB  TYR A 480     2319   2304   2988    -46     27    -74       C  
ATOM   2360  CG  TYR A 480      24.067  -5.106   8.250  1.00 17.67           C  
ANISOU 2360  CG  TYR A 480     2016   1972   2725    -50     42    -57       C  
ATOM   2361  CD1 TYR A 480      25.340  -4.805   8.697  1.00 22.58           C  
ANISOU 2361  CD1 TYR A 480     2656   2588   3335    -44     31    -23       C  
ATOM   2362  CD2 TYR A 480      23.709  -6.443   8.148  1.00 31.70           C  
ANISOU 2362  CD2 TYR A 480     3771   3725   4548    -59     68    -77       C  
ATOM   2363  CE1 TYR A 480      26.230  -5.794   9.033  1.00 22.50           C  
ANISOU 2363  CE1 TYR A 480     2642   2550   3357    -45     43     -8       C  
ATOM   2364  CE2 TYR A 480      24.593  -7.441   8.480  1.00 30.72           C  
ANISOU 2364  CE2 TYR A 480     3644   3571   4459    -61     82    -60       C  
ATOM   2365  CZ  TYR A 480      25.850  -7.116   8.920  1.00 30.77           C  
ANISOU 2365  CZ  TYR A 480     3668   3573   4451    -53     69    -25       C  
ATOM   2366  OH  TYR A 480      26.732  -8.113   9.247  1.00 32.04           O  
ANISOU 2366  OH  TYR A 480     3825   3704   4646    -53     83     -7       O  
ATOM   2367  N   LEU A 481      23.202  -1.844  10.214  1.00 20.40           N  
ANISOU 2367  N   LEU A 481     2424   2358   2969    -33      2      2       N  
ATOM   2368  CA  LEU A 481      23.893  -1.252  11.363  1.00 17.39           C  
ANISOU 2368  CA  LEU A 481     2067   1971   2569    -28     -6     43       C  
ATOM   2369  C   LEU A 481      23.042  -1.290  12.627  1.00 17.50           C  
ANISOU 2369  C   LEU A 481     2091   1973   2584    -30      5     60       C  
ATOM   2370  O   LEU A 481      23.567  -1.531  13.719  1.00 20.34           O  
ANISOU 2370  O   LEU A 481     2463   2317   2947    -28      9     92       O  
ATOM   2371  CB  LEU A 481      24.345   0.191  11.088  1.00 14.45           C  
ANISOU 2371  CB  LEU A 481     1711   1624   2155    -21    -29     50       C  
ATOM   2372  CG  LEU A 481      25.473   0.401  10.075  1.00 19.70           C  
ANISOU 2372  CG  LEU A 481     2374   2298   2814    -17    -40     43       C  
ATOM   2373  CD1 LEU A 481      25.536   1.849   9.679  1.00 16.29           C  
ANISOU 2373  CD1 LEU A 481     1956   1891   2342    -10    -57     43       C  
ATOM   2374  CD2 LEU A 481      26.802  -0.064  10.655  1.00 16.24           C  
ANISOU 2374  CD2 LEU A 481     1941   1841   2387    -17    -40     68       C  
ATOM   2375  N   SER A 482      21.742  -1.033  12.511  1.00 16.54           N  
ANISOU 2375  N   SER A 482     1963   1862   2459    -33      9     40       N  
ATOM   2376  CA  SER A 482      20.914  -1.071  13.720  1.00 20.02           C  
ANISOU 2376  CA  SER A 482     2413   2291   2902    -36     21     55       C  
ATOM   2377  C   SER A 482      20.808  -2.500  14.270  1.00 20.77           C  
ANISOU 2377  C   SER A 482     2499   2353   3039    -43     48     61       C  
ATOM   2378  O   SER A 482      20.807  -2.707  15.481  1.00 19.85           O  
ANISOU 2378  O   SER A 482     2397   2220   2924    -42     59     91       O  
ATOM   2379  CB  SER A 482      19.521  -0.445  13.519  1.00 21.84           C  
ANISOU 2379  CB  SER A 482     2638   2538   3120    -38     21     31       C  
ATOM   2380  OG  SER A 482      18.793  -1.103  12.508  1.00 23.79           O  
ANISOU 2380  OG  SER A 482     2860   2789   3391    -43     30     -9       O  
ATOM   2381  N  AMET A 483      20.710  -3.481  13.381  0.47 22.84           N  
ANISOU 2381  N  AMET A 483     2737   2605   3334    -48     61     33       N  
ATOM   2382  N  BMET A 483      20.711  -3.478  13.378  0.53 22.83           N  
ANISOU 2382  N  BMET A 483     2737   2606   3334    -48     61     33       N  
ATOM   2383  CA AMET A 483      20.638  -4.878  13.802  0.47 26.12           C  
ANISOU 2383  CA AMET A 483     3143   2987   3794    -54     91     36       C  
ATOM   2384  CA BMET A 483      20.637  -4.877  13.791  0.53 26.12           C  
ANISOU 2384  CA BMET A 483     3142   2987   3794    -54     91     36       C  
ATOM   2385  C  AMET A 483      21.918  -5.283  14.520  0.47 26.60           C  
ANISOU 2385  C  AMET A 483     3218   3030   3859    -48     91     76       C  
ATOM   2386  C  BMET A 483      21.915  -5.289  14.511  0.53 26.60           C  
ANISOU 2386  C  BMET A 483     3218   3030   3860    -48     91     76       C  
ATOM   2387  O  AMET A 483      21.883  -5.922  15.567  0.47 28.28           O  
ANISOU 2387  O  AMET A 483     3439   3218   4088    -47    110    103       O  
ATOM   2388  O  BMET A 483      21.876  -5.936  15.552  0.53 28.28           O  
ANISOU 2388  O  BMET A 483     3439   3218   4089    -47    110    103       O  
ATOM   2389  CB AMET A 483      20.401  -5.798  12.604  0.47 28.82           C  
ANISOU 2389  CB AMET A 483     3454   3325   4171    -62    104     -6       C  
ATOM   2390  CB BMET A 483      20.395  -5.782  12.583  0.53 28.82           C  
ANISOU 2390  CB BMET A 483     3454   3325   4170    -62    103     -6       C  
ATOM   2391  CG AMET A 483      21.665  -6.443  12.061  0.47 43.37           C  
ANISOU 2391  CG AMET A 483     5290   5157   6031    -60    103     -2       C  
ATOM   2392  CG BMET A 483      19.239  -6.754  12.757  0.53 44.11           C  
ANISOU 2392  CG BMET A 483     5372   5240   6146    -73    135    -29       C  
ATOM   2393  SD AMET A 483      22.149  -7.938  12.950  0.47 80.75           S  
ANISOU 2393  SD AMET A 483    10024   9845  10814    -62    135     26       S  
ATOM   2394  SD BMET A 483      17.675  -5.948  13.164  0.53 81.97           S  
ANISOU 2394  SD BMET A 483    10170  10053  10923    -76    134    -44       S  
ATOM   2395  CE AMET A 483      22.420  -9.057  11.582  0.47 41.73           C  
ANISOU 2395  CE AMET A 483     5048   4892   5915    -70    150    -16       C  
ATOM   2396  CE BMET A 483      17.297  -6.716  14.735  0.53 42.23           C  
ANISOU 2396  CE BMET A 483     5150   4980   5915    -81    168    -11       C  
ATOM   2397  N   LEU A 484      23.048  -4.898  13.944  1.00 18.71           N  
ANISOU 2397  N   LEU A 484     2221   2043   2845    -42     70     80       N  
ATOM   2398  CA  LEU A 484      24.347  -5.189  14.515  1.00 23.49           C  
ANISOU 2398  CA  LEU A 484     2838   2636   3453    -34     66    115       C  
ATOM   2399  C   LEU A 484      24.462  -4.556  15.895  1.00 27.27           C  
ANISOU 2399  C   LEU A 484     3341   3116   3902    -27     59    154       C  
ATOM   2400  O   LEU A 484      24.950  -5.179  16.835  1.00 24.27           O  
ANISOU 2400  O   LEU A 484     2970   2717   3534    -21     69    186       O  
ATOM   2401  CB  LEU A 484      25.433  -4.634  13.597  1.00 25.08           C  
ANISOU 2401  CB  LEU A 484     3038   2855   3637    -30     43    107       C  
ATOM   2402  CG  LEU A 484      26.663  -5.465  13.252  1.00 37.16           C  
ANISOU 2402  CG  LEU A 484     4558   4369   5192    -27     46    114       C  
ATOM   2403  CD1 LEU A 484      26.357  -6.961  13.212  1.00 32.05           C  
ANISOU 2403  CD1 LEU A 484     3893   3689   4595    -33     77    105       C  
ATOM   2404  CD2 LEU A 484      27.233  -4.984  11.929  1.00 33.69           C  
ANISOU 2404  CD2 LEU A 484     4110   3950   4741    -28     30     87       C  
ATOM   2405  N   ALA A 485      24.022  -3.307  16.018  1.00 23.19           N  
ANISOU 2405  N   ALA A 485     2837   2625   3349    -26     42    152       N  
ATOM   2406  CA  ALA A 485      24.103  -2.601  17.298  1.00 22.00           C  
ANISOU 2406  CA  ALA A 485     2710   2481   3169    -21     34    185       C  
ATOM   2407  C   ALA A 485      23.306  -3.333  18.377  1.00 25.90           C  
ANISOU 2407  C   ALA A 485     3209   2953   3680    -23     59    201       C  
ATOM   2408  O   ALA A 485      23.766  -3.488  19.509  1.00 30.47           O  
ANISOU 2408  O   ALA A 485     3803   3524   4251    -16     62    237       O  
ATOM   2409  CB  ALA A 485      23.606  -1.172  17.151  1.00 20.28           C  
ANISOU 2409  CB  ALA A 485     2502   2291   2913    -22     16    174       C  
ATOM   2410  N   LEU A 486      22.104  -3.773  18.027  1.00 26.05           N  
ANISOU 2410  N   LEU A 486     3214   2963   3721    -32     79    175       N  
ATOM   2411  CA  LEU A 486      21.286  -4.536  18.966  1.00 32.30           C  
ANISOU 2411  CA  LEU A 486     4008   3730   4533    -36    107    187       C  
ATOM   2412  C   LEU A 486      22.002  -5.851  19.317  1.00 30.71           C  
ANISOU 2412  C   LEU A 486     3805   3498   4366    -31    127    210       C  
ATOM   2413  O   LEU A 486      22.110  -6.229  20.488  1.00 34.91           O  
ANISOU 2413  O   LEU A 486     4352   4015   4898    -24    140    246       O  
ATOM   2414  CB  LEU A 486      19.904  -4.810  18.368  1.00 28.08           C  
ANISOU 2414  CB  LEU A 486     3456   3193   4021    -48    125    148       C  
ATOM   2415  CG  LEU A 486      18.947  -3.626  18.220  1.00 28.00           C  
ANISOU 2415  CG  LEU A 486     3448   3209   3981    -51    111    128       C  
ATOM   2416  CD1 LEU A 486      17.769  -4.021  17.341  1.00 26.49           C  
ANISOU 2416  CD1 LEU A 486     3231   3017   3816    -61    125     83       C  
ATOM   2417  CD2 LEU A 486      18.464  -3.180  19.590  1.00 35.87           C  
ANISOU 2417  CD2 LEU A 486     4466   4204   4958    -50    117    156       C  
ATOM   2418  N   GLN A 487      22.502  -6.522  18.286  1.00 33.25           N  
ANISOU 2418  N   GLN A 487     4107   3812   4716    -33    130    190       N  
ATOM   2419  CA  GLN A 487      23.276  -7.753  18.441  1.00 32.42           C  
ANISOU 2419  CA  GLN A 487     3996   3676   4645    -28    148    208       C  
ATOM   2420  C   GLN A 487      24.383  -7.562  19.479  1.00 37.08           C  
ANISOU 2420  C   GLN A 487     4608   4268   5212    -12    135    256       C  
ATOM   2421  O   GLN A 487      24.659  -8.452  20.275  1.00 33.94           O  
ANISOU 2421  O   GLN A 487     4217   3846   4835     -4    154    287       O  
ATOM   2422  CB  GLN A 487      23.863  -8.176  17.087  1.00 39.01           C  
ANISOU 2422  CB  GLN A 487     4808   4510   5502    -31    144    178       C  
ATOM   2423  CG  GLN A 487      24.699  -9.458  17.106  1.00 47.17           C  
ANISOU 2423  CG  GLN A 487     5833   5512   6576    -26    163    193       C  
ATOM   2424  CD  GLN A 487      25.275  -9.805  15.735  1.00 53.42           C  
ANISOU 2424  CD  GLN A 487     6602   6306   7390    -32    158    160       C  
ATOM   2425  OE1 GLN A 487      24.544 -10.184  14.816  1.00 60.65           O  
ANISOU 2425  OE1 GLN A 487     7496   7220   8329    -44    171    119       O  
ATOM   2426  NE2 GLN A 487      26.592  -9.675  15.595  1.00 56.95           N  
ANISOU 2426  NE2 GLN A 487     7053   6759   7827    -22    139    177       N  
ATOM   2427  N   LYS A 488      24.987  -6.381  19.492  1.00 31.37           N  
ANISOU 2427  N   LYS A 488     3897   3576   4448     -7    102    262       N  
ATOM   2428  CA  LYS A 488      26.120  -6.122  20.365  1.00 27.63           C  
ANISOU 2428  CA  LYS A 488     3440   3109   3950      8     86    300       C  
ATOM   2429  C   LYS A 488      25.710  -5.603  21.733  1.00 22.64           C  
ANISOU 2429  C   LYS A 488     2831   2485   3288     13     85    329       C  
ATOM   2430  O   LYS A 488      26.549  -5.150  22.495  1.00 32.13           O  
ANISOU 2430  O   LYS A 488     4047   3701   4461     24     68    357       O  
ATOM   2431  CB  LYS A 488      27.093  -5.145  19.702  1.00 27.87           C  
ANISOU 2431  CB  LYS A 488     3470   3166   3953     10     53    290       C  
ATOM   2432  CG  LYS A 488      27.742  -5.717  18.467  1.00 31.80           C  
ANISOU 2432  CG  LYS A 488     3947   3656   4480      7     53    267       C  
ATOM   2433  CD  LYS A 488      28.469  -4.657  17.675  1.00 34.70           C  
ANISOU 2433  CD  LYS A 488     4314   4050   4820      6     24    251       C  
ATOM   2434  CE  LYS A 488      29.231  -5.295  16.538  1.00 33.02           C  
ANISOU 2434  CE  LYS A 488     4082   3828   4635      5     25    232       C  
ATOM   2435  NZ  LYS A 488      30.340  -6.131  17.076  1.00 40.88           N  
ANISOU 2435  NZ  LYS A 488     5078   4806   5650     16     29    260       N  
ATOM   2436  N   GLY A 489      24.420  -5.658  22.035  1.00 32.44           N  
ANISOU 2436  N   GLY A 489     4074   3719   4534      4    105    321       N  
ATOM   2437  CA  GLY A 489      23.956  -5.363  23.379  1.00 37.07           C  
ANISOU 2437  CA  GLY A 489     4681   4308   5097      8    111    349       C  
ATOM   2438  C   GLY A 489      23.554  -3.927  23.667  1.00 40.81           C  
ANISOU 2438  C   GLY A 489     5166   4812   5526      4     90    342       C  
ATOM   2439  O   GLY A 489      23.305  -3.566  24.821  1.00 36.78           O  
ANISOU 2439  O   GLY A 489     4674   4308   4991      8     91    366       O  
ATOM   2440  N   SER A 490      23.476  -3.099  22.631  1.00 28.36           N  
ANISOU 2440  N   SER A 490     3581   3255   3940     -3     71    310       N  
ATOM   2441  CA  SER A 490      23.000  -1.731  22.824  1.00 27.64           C  
ANISOU 2441  CA  SER A 490     3499   3190   3811     -8     54    301       C  
ATOM   2442  C   SER A 490      21.649  -1.739  23.543  1.00 26.97           C  
ANISOU 2442  C   SER A 490     3420   3099   3727    -15     75    301       C  
ATOM   2443  O   SER A 490      20.681  -2.321  23.065  1.00 24.63           O  
ANISOU 2443  O   SER A 490     3112   2788   3460    -24     95    278       O  
ATOM   2444  CB  SER A 490      22.866  -1.002  21.486  1.00 26.63           C  
ANISOU 2444  CB  SER A 490     3358   3080   3680    -14     38    265       C  
ATOM   2445  OG  SER A 490      22.443   0.337  21.674  1.00 24.37           O  
ANISOU 2445  OG  SER A 490     3082   2817   3359    -16     23    258       O  
ATOM   2446  N   LYS A 491      21.586  -1.086  24.693  1.00 31.96           N  
ANISOU 2446  N   LYS A 491     4072   3743   4328    -11     70    323       N  
ATOM   2447  CA  LYS A 491      20.333  -0.999  25.434  1.00 45.70           C  
ANISOU 2447  CA  LYS A 491     5820   5478   6065    -19     89    323       C  
ATOM   2448  C   LYS A 491      19.735   0.415  25.364  1.00 48.64           C  
ANISOU 2448  C   LYS A 491     6197   5877   6408    -25     73    305       C  
ATOM   2449  O   LYS A 491      19.177   0.921  26.341  1.00 53.79           O  
ANISOU 2449  O   LYS A 491     6864   6536   7040    -27     77    316       O  
ATOM   2450  CB  LYS A 491      20.548  -1.438  26.890  1.00 56.83           C  
ANISOU 2450  CB  LYS A 491     7249   6880   7464    -10    102    364       C  
ATOM   2451  CG  LYS A 491      22.008  -1.374  27.348  1.00 67.74           C  
ANISOU 2451  CG  LYS A 491     8640   8274   8825      5     81    394       C  
ATOM   2452  CD  LYS A 491      22.261  -0.219  28.311  1.00 80.70           C  
ANISOU 2452  CD  LYS A 491    10299   9944  10419      8     62    408       C  
ATOM   2453  CE  LYS A 491      22.411  -0.704  29.752  1.00 89.16           C  
ANISOU 2453  CE  LYS A 491    11388  11013  11476     19     74    448       C  
ATOM   2454  NZ  LYS A 491      21.161  -1.310  30.295  1.00 84.49           N  
ANISOU 2454  NZ  LYS A 491    10802  10399  10900     13    108    453       N  
ATOM   2455  N   ASP A 492      19.845   1.044  24.198  1.00 47.29           N  
ANISOU 2455  N   ASP A 492     6014   5719   6234    -28     55    277       N  
ATOM   2456  CA  ASP A 492      19.404   2.427  24.030  1.00 35.55           C  
ANISOU 2456  CA  ASP A 492     4531   4256   4719    -31     39    261       C  
ATOM   2457  C   ASP A 492      18.579   2.618  22.756  1.00 30.00           C  
ANISOU 2457  C   ASP A 492     3811   3558   4032    -37     38    223       C  
ATOM   2458  O   ASP A 492      18.534   1.731  21.904  1.00 34.05           O  
ANISOU 2458  O   ASP A 492     4306   4058   4573    -38     46    206       O  
ATOM   2459  CB  ASP A 492      20.623   3.329  23.974  1.00 35.11           C  
ANISOU 2459  CB  ASP A 492     4484   4222   4636    -24     12    270       C  
ATOM   2460  CG  ASP A 492      20.291   4.764  24.280  1.00 44.37           C  
ANISOU 2460  CG  ASP A 492     5666   5416   5776    -27      0    265       C  
ATOM   2461  OD1 ASP A 492      19.085   5.087  24.442  1.00 44.56           O  
ANISOU 2461  OD1 ASP A 492     5690   5440   5799    -34     10    252       O  
ATOM   2462  OD2 ASP A 492      21.245   5.564  24.368  1.00 38.97           O  
ANISOU 2462  OD2 ASP A 492     4989   4749   5069    -23    -19    272       O  
ATOM   2463  N   ASN A 493      17.928   3.771  22.618  1.00 24.00           N  
ANISOU 2463  N   ASN A 493     3053   2816   3251    -39     28    208       N  
ATOM   2464  CA  ASN A 493      17.341   4.118  21.334  1.00 19.33           C  
ANISOU 2464  CA  ASN A 493     2445   2234   2665    -40     22    174       C  
ATOM   2465  C   ASN A 493      18.448   4.229  20.291  1.00 15.42           C  
ANISOU 2465  C   ASN A 493     1944   1747   2167    -34      4    169       C  
ATOM   2466  O   ASN A 493      19.541   4.697  20.579  1.00 16.61           O  
ANISOU 2466  O   ASN A 493     2107   1905   2299    -29    -10    188       O  
ATOM   2467  CB  ASN A 493      16.563   5.431  21.395  1.00 18.37           C  
ANISOU 2467  CB  ASN A 493     2330   2132   2520    -41     13    163       C  
ATOM   2468  CG  ASN A 493      15.561   5.481  22.544  1.00 25.21           C  
ANISOU 2468  CG  ASN A 493     3204   2991   3385    -48     30    169       C  
ATOM   2469  OD1 ASN A 493      15.387   6.523  23.177  1.00 23.00           O  
ANISOU 2469  OD1 ASN A 493     2936   2723   3079    -48     23    176       O  
ATOM   2470  ND2 ASN A 493      14.892   4.366  22.805  1.00 21.93           N  
ANISOU 2470  ND2 ASN A 493     2780   2556   2998    -54     53    165       N  
ATOM   2471  N   ILE A 494      18.153   3.802  19.074  1.00 16.79           N  
ANISOU 2471  N   ILE A 494     2100   1922   2360    -34      5    141       N  
ATOM   2472  CA  ILE A 494      19.141   3.790  18.008  1.00 19.89           C  
ANISOU 2472  CA  ILE A 494     2485   2321   2752    -29     -9    134       C  
ATOM   2473  C   ILE A 494      18.605   4.545  16.805  1.00 15.99           C  
ANISOU 2473  C   ILE A 494     1981   1847   2247    -25    -20    106       C  
ATOM   2474  O   ILE A 494      17.620   4.136  16.193  1.00 19.74           O  
ANISOU 2474  O   ILE A 494     2439   2323   2738    -27    -13     78       O  
ATOM   2475  CB  ILE A 494      19.455   2.345  17.574  1.00 18.16           C  
ANISOU 2475  CB  ILE A 494     2250   2082   2569    -31      4    128       C  
ATOM   2476  CG1 ILE A 494      20.090   1.566  18.722  1.00 18.69           C  
ANISOU 2476  CG1 ILE A 494     2328   2128   2646    -31     15    161       C  
ATOM   2477  CG2 ILE A 494      20.339   2.325  16.326  1.00 19.47           C  
ANISOU 2477  CG2 ILE A 494     2406   2256   2736    -27     -9    115       C  
ATOM   2478  CD1 ILE A 494      19.893   0.077  18.581  1.00 25.30           C  
ANISOU 2478  CD1 ILE A 494     3149   2939   3523    -36     38    155       C  
ATOM   2479  N   SER A 495      19.260   5.647  16.465  1.00 15.43           N  
ANISOU 2479  N   SER A 495     1920   1792   2149    -19    -38    111       N  
ATOM   2480  CA  SER A 495      18.898   6.408  15.284  1.00 18.59           C  
ANISOU 2480  CA  SER A 495     2314   2213   2536    -12    -49     88       C  
ATOM   2481  C   SER A 495      20.128   6.633  14.403  1.00 17.87           C  
ANISOU 2481  C   SER A 495     2225   2129   2438     -6    -61     90       C  
ATOM   2482  O   SER A 495      21.187   7.057  14.875  1.00 16.68           O  
ANISOU 2482  O   SER A 495     2087   1976   2274     -5    -68    111       O  
ATOM   2483  CB  SER A 495      18.253   7.743  15.676  1.00 20.26           C  
ANISOU 2483  CB  SER A 495     2538   2439   2722     -8    -55     92       C  
ATOM   2484  OG  SER A 495      17.067   7.520  16.429  1.00 21.69           O  
ANISOU 2484  OG  SER A 495     2717   2614   2912    -14    -43     87       O  
ATOM   2485  N   ILE A 496      19.963   6.359  13.118  1.00 14.48           N  
ANISOU 2485  N   ILE A 496     1779   1708   2013     -2    -64     65       N  
ATOM   2486  CA  ILE A 496      21.063   6.348  12.187  1.00 15.00           C  
ANISOU 2486  CA  ILE A 496     1844   1779   2077      3    -72     63       C  
ATOM   2487  C   ILE A 496      20.575   6.878  10.853  1.00 16.55           C  
ANISOU 2487  C   ILE A 496     2031   1997   2259     12    -79     39       C  
ATOM   2488  O   ILE A 496      19.532   6.451  10.343  1.00 18.09           O  
ANISOU 2488  O   ILE A 496     2209   2199   2463     13    -76     14       O  
ATOM   2489  CB  ILE A 496      21.573   4.904  11.919  1.00 15.81           C  
ANISOU 2489  CB  ILE A 496     1930   1865   2211     -4    -63     57       C  
ATOM   2490  CG1 ILE A 496      21.833   4.129  13.212  1.00 15.55           C  
ANISOU 2490  CG1 ILE A 496     1903   1808   2196    -11    -52     79       C  
ATOM   2491  CG2 ILE A 496      22.835   4.939  11.104  1.00 15.60           C  
ANISOU 2491  CG2 ILE A 496     1904   1841   2181      0    -71     57       C  
ATOM   2492  CD1 ILE A 496      22.328   2.695  12.963  1.00 17.74           C  
ANISOU 2492  CD1 ILE A 496     2166   2067   2508    -16    -41     75       C  
ATOM   2493  N   ILE A 497      21.339   7.792  10.275  1.00 14.50           N  
ANISOU 2493  N   ILE A 497     1783   1749   1977     20    -89     45       N  
ATOM   2494  CA  ILE A 497      21.098   8.207   8.906  1.00 14.51           C  
ANISOU 2494  CA  ILE A 497     1777   1771   1964     31    -96     25       C  
ATOM   2495  C   ILE A 497      22.348   7.887   8.109  1.00 14.47           C  
ANISOU 2495  C   ILE A 497     1771   1765   1962     32    -98     25       C  
ATOM   2496  O   ILE A 497      23.441   8.377   8.447  1.00 12.85           O  
ANISOU 2496  O   ILE A 497     1581   1553   1749     30   -100     45       O  
ATOM   2497  CB  ILE A 497      20.827   9.718   8.835  1.00 17.51           C  
ANISOU 2497  CB  ILE A 497     2174   2167   2314     43   -102     34       C  
ATOM   2498  CG1 ILE A 497      19.569  10.090   9.635  1.00 11.39           C  
ANISOU 2498  CG1 ILE A 497     1399   1392   1535     42   -100     34       C  
ATOM   2499  CG2 ILE A 497      20.716  10.188   7.375  1.00 12.34           C  
ANISOU 2499  CG2 ILE A 497     1515   1535   1640     58   -109     18       C  
ATOM   2500  CD1 ILE A 497      19.350  11.651   9.702  1.00 16.30           C  
ANISOU 2500  CD1 ILE A 497     2039   2026   2129     53   -105     46       C  
ATOM   2501  N   VAL A 498      22.207   7.060   7.070  1.00 14.17           N  
ANISOU 2501  N   VAL A 498     1713   1734   1936     32    -97     -1       N  
ATOM   2502  CA  VAL A 498      23.331   6.762   6.166  1.00 12.70           C  
ANISOU 2502  CA  VAL A 498     1524   1549   1752     33    -98     -5       C  
ATOM   2503  C   VAL A 498      23.172   7.528   4.840  1.00 15.81           C  
ANISOU 2503  C   VAL A 498     1919   1970   2119     48   -105    -19       C  
ATOM   2504  O   VAL A 498      22.117   7.474   4.203  1.00 19.61           O  
ANISOU 2504  O   VAL A 498     2387   2470   2593     55   -108    -42       O  
ATOM   2505  CB  VAL A 498      23.450   5.260   5.869  1.00 14.97           C  
ANISOU 2505  CB  VAL A 498     1790   1825   2073     23    -90    -24       C  
ATOM   2506  CG1 VAL A 498      24.406   5.021   4.702  1.00 16.02           C  
ANISOU 2506  CG1 VAL A 498     1917   1965   2205     25    -91    -36       C  
ATOM   2507  CG2 VAL A 498      23.928   4.519   7.111  1.00 13.78           C  
ANISOU 2507  CG2 VAL A 498     1642   1646   1948     12    -82     -4       C  
ATOM   2508  N   ILE A 499      24.220   8.231   4.429  1.00 13.00           N  
ANISOU 2508  N   ILE A 499     1578   1615   1746     52   -107     -6       N  
ATOM   2509  CA  ILE A 499      24.182   9.078   3.227  1.00 17.78           C  
ANISOU 2509  CA  ILE A 499     2189   2244   2323     68   -112    -13       C  
ATOM   2510  C   ILE A 499      25.270   8.653   2.245  1.00 18.57           C  
ANISOU 2510  C   ILE A 499     2285   2346   2426     67   -109    -22       C  
ATOM   2511  O   ILE A 499      26.447   8.656   2.590  1.00 19.67           O  
ANISOU 2511  O   ILE A 499     2432   2467   2574     59   -106     -7       O  
ATOM   2512  CB  ILE A 499      24.388  10.575   3.589  1.00 14.68           C  
ANISOU 2512  CB  ILE A 499     1821   1852   1904     77   -113     12       C  
ATOM   2513  CG1 ILE A 499      23.254  11.085   4.492  1.00 16.88           C  
ANISOU 2513  CG1 ILE A 499     2104   2132   2178     79   -114     18       C  
ATOM   2514  CG2 ILE A 499      24.488  11.446   2.332  1.00 16.97           C  
ANISOU 2514  CG2 ILE A 499     2120   2164   2165     94   -114      9       C  
ATOM   2515  CD1 ILE A 499      23.632  12.355   5.246  1.00 21.39           C  
ANISOU 2515  CD1 ILE A 499     2697   2694   2734     80   -112     44       C  
ATOM   2516  N   ASP A 500      24.887   8.289   1.025  1.00 15.62           N  
ANISOU 2516  N   ASP A 500     1897   1994   2045     75   -111    -47       N  
ATOM   2517  CA  ASP A 500      25.872   7.829   0.034  1.00 16.41           C  
ANISOU 2517  CA  ASP A 500     1991   2096   2148     73   -108    -58       C  
ATOM   2518  C   ASP A 500      26.427   9.026  -0.723  1.00 22.21           C  
ANISOU 2518  C   ASP A 500     2746   2844   2851     87   -108    -46       C  
ATOM   2519  O   ASP A 500      25.670   9.778  -1.322  1.00 17.20           O  
ANISOU 2519  O   ASP A 500     2116   2232   2187    104   -112    -49       O  
ATOM   2520  CB  ASP A 500      25.228   6.811  -0.933  1.00 17.20           C  
ANISOU 2520  CB  ASP A 500     2065   2215   2257     74   -109    -95       C  
ATOM   2521  CG  ASP A 500      26.228   6.163  -1.888  1.00 24.22           C  
ANISOU 2521  CG  ASP A 500     2944   3104   3154     69   -104   -110       C  
ATOM   2522  OD1 ASP A 500      27.452   6.436  -1.782  1.00 22.39           O  
ANISOU 2522  OD1 ASP A 500     2726   2856   2924     64   -100    -91       O  
ATOM   2523  OD2 ASP A 500      25.777   5.373  -2.757  1.00 20.57           O  
ANISOU 2523  OD2 ASP A 500     2459   2659   2697     69   -104   -142       O  
ATOM   2524  N   LEU A 501      27.746   9.204  -0.694  1.00 18.18           N  
ANISOU 2524  N   LEU A 501     2246   2316   2344     81   -102    -32       N  
ATOM   2525  CA  LEU A 501      28.367  10.355  -1.347  1.00 21.18           C  
ANISOU 2525  CA  LEU A 501     2647   2704   2697     93    -98    -19       C  
ATOM   2526  C   LEU A 501      28.939  10.074  -2.738  1.00 24.81           C  
ANISOU 2526  C   LEU A 501     3101   3178   3147     98    -93    -36       C  
ATOM   2527  O   LEU A 501      29.465  10.980  -3.370  1.00 22.34           O  
ANISOU 2527  O   LEU A 501     2806   2871   2812    108    -87    -25       O  
ATOM   2528  CB  LEU A 501      29.458  10.969  -0.466  1.00 14.97           C  
ANISOU 2528  CB  LEU A 501     1878   1893   1918     84    -92      6       C  
ATOM   2529  CG  LEU A 501      28.929  11.534   0.853  1.00 20.43           C  
ANISOU 2529  CG  LEU A 501     2578   2573   2610     81    -95     24       C  
ATOM   2530  CD1 LEU A 501      30.074  11.795   1.812  1.00 14.90           C  
ANISOU 2530  CD1 LEU A 501     1888   1849   1924     69    -91     43       C  
ATOM   2531  CD2 LEU A 501      28.100  12.790   0.575  1.00 15.14           C  
ANISOU 2531  CD2 LEU A 501     1924   1920   1909     99    -95     33       C  
ATOM   2532  N   LYS A 502      28.861   8.830  -3.203  1.00 24.21           N  
ANISOU 2532  N   LYS A 502     3002   3106   3090     90    -95    -62       N  
ATOM   2533  CA  LYS A 502      29.270   8.534  -4.572  1.00 31.59           C  
ANISOU 2533  CA  LYS A 502     3929   4059   4013     95    -91    -82       C  
ATOM   2534  C   LYS A 502      28.141   8.846  -5.543  1.00 28.22           C  
ANISOU 2534  C   LYS A 502     3498   3669   3554    115    -98    -98       C  
ATOM   2535  O   LYS A 502      26.997   8.454  -5.337  1.00 30.17           O  
ANISOU 2535  O   LYS A 502     3730   3929   3805    117   -106   -112       O  
ATOM   2536  CB  LYS A 502      29.689   7.069  -4.729  1.00 28.86           C  
ANISOU 2536  CB  LYS A 502     3559   3703   3702     78    -88   -106       C  
ATOM   2537  CG  LYS A 502      30.975   6.688  -4.028  1.00 29.12           C  
ANISOU 2537  CG  LYS A 502     3595   3704   3766     61    -82    -92       C  
ATOM   2538  CD  LYS A 502      32.180   7.324  -4.707  1.00 34.16           C  
ANISOU 2538  CD  LYS A 502     4249   4341   4391     64    -74    -84       C  
ATOM   2539  CE  LYS A 502      33.475   6.833  -4.081  1.00 31.70           C  
ANISOU 2539  CE  LYS A 502     3936   3998   4112     47    -68    -76       C  
ATOM   2540  NZ  LYS A 502      34.667   7.277  -4.840  1.00 35.68           N  
ANISOU 2540  NZ  LYS A 502     4449   4500   4607     48    -58    -74       N  
ATOM   2541  N   ALA A 503      28.479   9.535  -6.620  1.00 33.01           N  
ANISOU 2541  N   ALA A 503     4117   4295   4129    130    -94    -95       N  
ATOM   2542  CA  ALA A 503      27.511   9.806  -7.678  1.00 40.02           C  
ANISOU 2542  CA  ALA A 503     5000   5222   4982    153   -101   -111       C  
ATOM   2543  C   ALA A 503      26.920   8.495  -8.203  1.00 32.38           C  
ANISOU 2543  C   ALA A 503     4001   4274   4030    146   -107   -151       C  
ATOM   2544  O   ALA A 503      25.706   8.335  -8.336  1.00 35.26           O  
ANISOU 2544  O   ALA A 503     4349   4662   4385    156   -117   -169       O  
ATOM   2545  CB  ALA A 503      28.191  10.572  -8.814  1.00 40.52           C  
ANISOU 2545  CB  ALA A 503     5082   5300   5012    169    -92   -102       C  
ATOM   2546  N   GLN A 504      27.798   7.547  -8.485  1.00 27.14           N  
ANISOU 2546  N   GLN A 504     3324   3598   3391    129   -100   -167       N  
ATOM   2547  CA  GLN A 504      27.365   6.288  -9.055  1.00 35.91           C  
ANISOU 2547  CA  GLN A 504     4402   4724   4519    122   -102   -208       C  
ATOM   2548  C   GLN A 504      28.289   5.181  -8.586  1.00 32.52           C  
ANISOU 2548  C   GLN A 504     3959   4260   4135     96    -93   -215       C  
ATOM   2549  O   GLN A 504      29.430   5.425  -8.188  1.00 27.96           O  
ANISOU 2549  O   GLN A 504     3398   3656   3568     87    -85   -192       O  
ATOM   2550  CB  GLN A 504      27.361   6.373 -10.587  1.00 40.03           C  
ANISOU 2550  CB  GLN A 504     4920   5285   5006    137   -103   -230       C  
ATOM   2551  CG  GLN A 504      28.702   6.771 -11.174  1.00 45.90           C  
ANISOU 2551  CG  GLN A 504     5682   6019   5738    137    -91   -215       C  
ATOM   2552  CD  GLN A 504      28.917   6.217 -12.579  1.00 67.69           C  
ANISOU 2552  CD  GLN A 504     8427   8810   8483    141    -88   -248       C  
ATOM   2553  OE1 GLN A 504      30.039   5.848 -12.955  1.00 67.48           O  
ANISOU 2553  OE1 GLN A 504     8400   8769   8469    129    -76   -252       O  
ATOM   2554  NE2 GLN A 504      27.842   6.156 -13.362  1.00 61.99           N  
ANISOU 2554  NE2 GLN A 504     7689   8130   7732    158    -99   -273       N  
ATOM   2555  N   ARG A 505      27.798   3.955  -8.619  1.00 35.87           N  
ANISOU 2555  N   ARG A 505     4354   4686   4589     84    -92   -247       N  
ATOM   2556  CA  ARG A 505      28.628   2.842  -8.204  1.00 34.13           C  
ANISOU 2556  CA  ARG A 505     4120   4434   4415     61    -82   -254       C  
ATOM   2557  C   ARG A 505      28.551   1.681  -9.199  1.00 31.02           C  
ANISOU 2557  C   ARG A 505     3695   4055   4036     53    -77   -299       C  
ATOM   2558  O   ARG A 505      27.828   0.723  -8.986  1.00 32.00           O  
ANISOU 2558  O   ARG A 505     3793   4177   4188     44    -75   -325       O  
ATOM   2559  CB  ARG A 505      28.247   2.411  -6.786  1.00 27.29           C  
ANISOU 2559  CB  ARG A 505     3250   3536   3582     49    -81   -241       C  
ATOM   2560  CG  ARG A 505      28.430   3.534  -5.723  1.00 28.89           C  
ANISOU 2560  CG  ARG A 505     3483   3723   3772     54    -86   -197       C  
ATOM   2561  CD  ARG A 505      28.218   2.972  -4.331  1.00 26.69           C  
ANISOU 2561  CD  ARG A 505     3200   3413   3529     41    -83   -184       C  
ATOM   2562  NE  ARG A 505      28.441   3.907  -3.232  1.00 24.82           N  
ANISOU 2562  NE  ARG A 505     2989   3159   3283     43    -87   -146       N  
ATOM   2563  CZ  ARG A 505      29.557   3.948  -2.511  1.00 27.87           C  
ANISOU 2563  CZ  ARG A 505     3387   3518   3685     35    -83   -122       C  
ATOM   2564  NH1 ARG A 505      30.565   3.136  -2.805  1.00 28.49           N  
ANISOU 2564  NH1 ARG A 505     3454   3581   3788     24    -76   -130       N  
ATOM   2565  NH2 ARG A 505      29.677   4.800  -1.493  1.00 17.18           N  
ANISOU 2565  NH2 ARG A 505     2053   2152   2322     37    -86    -91       N  
ATOM   2566  N   LYS A 506      29.293   1.791 -10.294  1.00 35.91           N  
ANISOU 2566  N   LYS A 506     4317   4690   4637     57    -73   -309       N  
ATOM   2567  CA  LYS A 506      29.343   0.735 -11.314  1.00 41.17           C  
ANISOU 2567  CA  LYS A 506     4954   5373   5316     49    -67   -353       C  
ATOM   2568  C   LYS A 506      30.568  -0.175 -11.159  1.00 34.99           C  
ANISOU 2568  C   LYS A 506     4163   4554   4576     28    -52   -356       C  
ATOM   2569  O   LYS A 506      31.602   0.239 -10.638  1.00 32.18           O  
ANISOU 2569  O   LYS A 506     3828   4171   4227     24    -48   -324       O  
ATOM   2570  CB  LYS A 506      29.309   1.352 -12.714  1.00 45.46           C  
ANISOU 2570  CB  LYS A 506     5503   5959   5809     68    -71   -367       C  
ATOM   2571  CG  LYS A 506      28.076   2.224 -12.965  1.00 48.07           C  
ANISOU 2571  CG  LYS A 506     5840   6329   6096     92    -85   -365       C  
ATOM   2572  CD  LYS A 506      26.787   1.422 -12.825  1.00 48.22           C  
ANISOU 2572  CD  LYS A 506     5826   6362   6132     89    -92   -401       C  
ATOM   2573  CE  LYS A 506      25.563   2.320 -12.901  1.00 51.85           C  
ANISOU 2573  CE  LYS A 506     6293   6856   6551    113   -108   -397       C  
ATOM   2574  NZ  LYS A 506      25.511   3.071 -14.178  1.00 62.01           N  
ANISOU 2574  NZ  LYS A 506     7589   8189   7784    138   -114   -402       N  
ATOM   2575  N   PHE A 507      30.440  -1.421 -11.607  1.00 43.57           N  
ANISOU 2575  N   PHE A 507     5217   5642   5694     15    -44   -396       N  
ATOM   2576  CA  PHE A 507      31.512  -2.400 -11.466  1.00 37.71           C  
ANISOU 2576  CA  PHE A 507     4463   4866   4998     -5    -29   -401       C  
ATOM   2577  C   PHE A 507      32.130  -2.767 -12.809  1.00 51.62           C  
ANISOU 2577  C   PHE A 507     6212   6648   6752     -8    -22   -433       C  
ATOM   2578  O   PHE A 507      31.637  -3.651 -13.520  1.00 48.80           O  
ANISOU 2578  O   PHE A 507     5826   6310   6407    -14    -17   -478       O  
ATOM   2579  CB  PHE A 507      30.997  -3.653 -10.751  1.00 38.63           C  
ANISOU 2579  CB  PHE A 507     4553   4958   5167    -21    -21   -419       C  
ATOM   2580  CG  PHE A 507      30.400  -3.369  -9.413  1.00 33.54           C  
ANISOU 2580  CG  PHE A 507     3920   4293   4532    -20    -26   -389       C  
ATOM   2581  CD1 PHE A 507      31.207  -3.221  -8.299  1.00 37.48           C  
ANISOU 2581  CD1 PHE A 507     4437   4753   5049    -25    -24   -348       C  
ATOM   2582  CD2 PHE A 507      29.034  -3.221  -9.269  1.00 34.98           C  
ANISOU 2582  CD2 PHE A 507     4094   4495   4700    -12    -34   -401       C  
ATOM   2583  CE1 PHE A 507      30.655  -2.941  -7.061  1.00 37.04           C  
ANISOU 2583  CE1 PHE A 507     4394   4682   5000    -23    -29   -321       C  
ATOM   2584  CE2 PHE A 507      28.480  -2.939  -8.041  1.00 31.57           C  
ANISOU 2584  CE2 PHE A 507     3674   4045   4276    -11    -38   -374       C  
ATOM   2585  CZ  PHE A 507      29.286  -2.796  -6.937  1.00 30.51           C  
ANISOU 2585  CZ  PHE A 507     3559   3873   4160    -16    -35   -333       C  
ATOM   2586  N   LYS A 508      33.216  -2.087 -13.154  1.00 52.97           N  
ANISOU 2586  N   LYS A 508     6407   6816   6904     -4    -19   -412       N  
ATOM   2587  CA  LYS A 508      33.909  -2.373 -14.400  1.00 65.89           C  
ANISOU 2587  CA  LYS A 508     8034   8470   8532     -7    -10   -439       C  
ATOM   2588  C   LYS A 508      34.548  -3.765 -14.361  1.00 58.34           C  
ANISOU 2588  C   LYS A 508     7050   7485   7633    -30      5   -465       C  
ATOM   2589  O   LYS A 508      35.240  -4.120 -13.403  1.00 51.07           O  
ANISOU 2589  O   LYS A 508     6132   6521   6752    -41     11   -442       O  
ATOM   2590  CB  LYS A 508      34.960  -1.307 -14.693  1.00 71.26           C  
ANISOU 2590  CB  LYS A 508     8746   9148   9182      1     -8   -409       C  
ATOM   2591  CG  LYS A 508      35.483  -1.381 -16.112  1.00 85.57           C  
ANISOU 2591  CG  LYS A 508    10554  10988  10973      3      1   -436       C  
ATOM   2592  CD  LYS A 508      36.820  -0.689 -16.256  1.00 91.08           C  
ANISOU 2592  CD  LYS A 508    11277  11668  11662      3     11   -410       C  
ATOM   2593  CE  LYS A 508      37.576  -1.288 -17.421  1.00 93.48           C  
ANISOU 2593  CE  LYS A 508    11566  11981  11969     -6     25   -442       C  
ATOM   2594  NZ  LYS A 508      37.591  -2.779 -17.326  1.00 95.17           N  
ANISOU 2594  NZ  LYS A 508    11744  12179  12237    -27     32   -478       N  
ATOM   2595  N   THR A 509      34.300  -4.550 -15.402  1.00 68.54           N  
ANISOU 2595  N   THR A 509     8313   8800   8928    -36     12   -512       N  
ATOM   2596  CA  THR A 509      34.789  -5.920 -15.464  1.00 64.93           C  
ANISOU 2596  CA  THR A 509     7826   8317   8526    -57     29   -541       C  
ATOM   2597  C   THR A 509      34.989  -6.367 -16.906  1.00 64.44           C  
ANISOU 2597  C   THR A 509     7745   8288   8453    -61     37   -587       C  
ATOM   2598  O   THR A 509      34.608  -5.664 -17.841  1.00 64.38           O  
ANISOU 2598  O   THR A 509     7745   8324   8392    -46     28   -598       O  
ATOM   2599  CB  THR A 509      33.801  -6.889 -14.801  1.00 59.76           C  
ANISOU 2599  CB  THR A 509     7144   7649   7912    -67     32   -560       C  
ATOM   2600  OG1 THR A 509      32.580  -6.906 -15.547  1.00 62.14           O  
ANISOU 2600  OG1 THR A 509     7428   7995   8185    -59     25   -598       O  
ATOM   2601  CG2 THR A 509      33.505  -6.460 -13.378  1.00 56.69           C  
ANISOU 2601  CG2 THR A 509     6775   7232   7532    -63     24   -516       C  
ATOM   2602  N   ARG A 510      35.588  -7.543 -17.066  1.00 94.23           N  
ANISOU 2602  N   ARG A 510    11491  12036  12275    -81     54   -614       N  
ATOM   2603  CA  ARG A 510      35.810  -8.135 -18.379  1.00 94.88           C  
ANISOU 2603  CA  ARG A 510    11550  12145  12355    -89     65   -663       C  
ATOM   2604  C   ARG A 510      37.219  -8.708 -18.509  1.00 94.81           C  
ANISOU 2604  C   ARG A 510    11537  12102  12384   -105     82   -664       C  
ATOM   2605  O   ARG A 510      37.583  -9.649 -17.808  1.00 94.34           O  
ANISOU 2605  O   ARG A 510    11462  12000  12385   -121     94   -663       O  
ATOM   2606  CB  ARG A 510      35.552  -7.116 -19.485  1.00 85.71           C  
ANISOU 2606  CB  ARG A 510    10405  11038  11123    -69     54   -669       C  
ATOM   2607  CG  ARG A 510      34.871  -7.700 -20.709  1.00 86.46           C  
ANISOU 2607  CG  ARG A 510    10469  11180  11202    -70     56   -728       C  
ATOM   2608  CD  ARG A 510      33.367  -7.549 -20.623  1.00 86.55           C  
ANISOU 2608  CD  ARG A 510    10469  11224  11190    -57     40   -743       C  
ATOM   2609  NE  ARG A 510      32.795  -7.087 -21.882  1.00 87.57           N  
ANISOU 2609  NE  ARG A 510    10596  11418  11260    -39     30   -772       N  
ATOM   2610  CZ  ARG A 510      32.893  -7.744 -23.031  1.00 88.28           C  
ANISOU 2610  CZ  ARG A 510    10658  11538  11346    -46     39   -824       C  
ATOM   2611  NH1 ARG A 510      33.543  -8.897 -23.086  1.00 88.04           N  
ANISOU 2611  NH1 ARG A 510    10602  11478  11371    -72     59   -852       N  
ATOM   2612  NH2 ARG A 510      32.340  -7.250 -24.129  1.00 89.29           N  
ANISOU 2612  NH2 ARG A 510    10786  11728  11414    -27     27   -847       N  
TER    2613      ARG A 510                                                      
ATOM   2614  N   SER B 180      43.892  24.727  37.677  1.00 43.06           N  
ANISOU 2614  N   SER B 180     5326   5829   5206    -80   -269    -89       N  
ATOM   2615  CA  SER B 180      43.738  25.225  36.311  1.00 52.45           C  
ANISOU 2615  CA  SER B 180     6523   6971   6435    -93   -243    -94       C  
ATOM   2616  C   SER B 180      44.687  24.519  35.339  1.00 47.21           C  
ANISOU 2616  C   SER B 180     5851   6291   5796    -83   -252    -88       C  
ATOM   2617  O   SER B 180      45.905  24.526  35.529  1.00 43.48           O  
ANISOU 2617  O   SER B 180     5354   5840   5326    -81   -266   -113       O  
ATOM   2618  CB  SER B 180      43.962  26.739  36.253  1.00 57.55           C  
ANISOU 2618  CB  SER B 180     7156   7614   7097   -117   -219   -142       C  
ATOM   2619  OG  SER B 180      44.038  27.202  34.910  1.00 52.80           O  
ANISOU 2619  OG  SER B 180     6559   6969   6533   -127   -195   -147       O  
ATOM   2620  N   VAL B 181      44.118  23.915  34.299  1.00 47.28           N  
ANISOU 2620  N   VAL B 181     5880   6262   5823    -78   -243    -56       N  
ATOM   2621  CA  VAL B 181      44.897  23.145  33.329  1.00 42.65           C  
ANISOU 2621  CA  VAL B 181     5288   5657   5259    -69   -250    -46       C  
ATOM   2622  C   VAL B 181      46.122  23.897  32.821  1.00 44.46           C  
ANISOU 2622  C   VAL B 181     5495   5885   5514    -80   -242    -88       C  
ATOM   2623  O   VAL B 181      47.184  23.302  32.653  1.00 38.46           O  
ANISOU 2623  O   VAL B 181     4719   5134   4762    -71   -259    -92       O  
ATOM   2624  CB  VAL B 181      44.046  22.718  32.118  1.00 38.99           C  
ANISOU 2624  CB  VAL B 181     4848   5150   4816    -68   -234    -17       C  
ATOM   2625  CG1 VAL B 181      43.582  23.942  31.331  1.00 37.58           C  
ANISOU 2625  CG1 VAL B 181     4678   4944   4658    -87   -203    -36       C  
ATOM   2626  CG2 VAL B 181      44.839  21.764  31.223  1.00 38.20           C  
ANISOU 2626  CG2 VAL B 181     4742   5035   4737    -56   -244     -5       C  
ATOM   2627  N   TYR B 182      45.974  25.201  32.587  1.00 40.19           N  
ANISOU 2627  N   TYR B 182     4952   5331   4985   -101   -216   -118       N  
ATOM   2628  CA  TYR B 182      47.070  26.003  32.051  1.00 53.45           C  
ANISOU 2628  CA  TYR B 182     6612   7004   6693   -114   -203   -158       C  
ATOM   2629  C   TYR B 182      48.279  26.039  32.991  1.00 52.03           C  
ANISOU 2629  C   TYR B 182     6400   6866   6502   -112   -224   -192       C  
ATOM   2630  O   TYR B 182      49.387  26.354  32.566  1.00 55.88           O  
ANISOU 2630  O   TYR B 182     6867   7353   7013   -118   -220   -223       O  
ATOM   2631  CB  TYR B 182      46.601  27.428  31.721  1.00 51.50           C  
ANISOU 2631  CB  TYR B 182     6371   6735   6461   -136   -167   -183       C  
ATOM   2632  CG  TYR B 182      45.489  27.496  30.691  1.00 48.71           C  
ANISOU 2632  CG  TYR B 182     6047   6341   6121   -137   -145   -154       C  
ATOM   2633  CD1 TYR B 182      45.734  27.210  29.351  1.00 46.29           C  
ANISOU 2633  CD1 TYR B 182     5748   6000   5840   -134   -134   -142       C  
ATOM   2634  CD2 TYR B 182      44.202  27.852  31.056  1.00 45.58           C  
ANISOU 2634  CD2 TYR B 182     5669   5940   5710   -140   -135   -139       C  
ATOM   2635  CE1 TYR B 182      44.719  27.268  28.407  1.00 46.45           C  
ANISOU 2635  CE1 TYR B 182     5793   5987   5869   -133   -116   -116       C  
ATOM   2636  CE2 TYR B 182      43.182  27.910  30.122  1.00 52.80           C  
ANISOU 2636  CE2 TYR B 182     6608   6819   6635   -139   -117   -113       C  
ATOM   2637  CZ  TYR B 182      43.443  27.620  28.800  1.00 49.09           C  
ANISOU 2637  CZ  TYR B 182     6144   6319   6188   -135   -107   -102       C  
ATOM   2638  OH  TYR B 182      42.423  27.685  27.873  1.00 47.13           O  
ANISOU 2638  OH  TYR B 182     5919   6039   5947   -132    -91    -78       O  
ATOM   2639  N   GLU B 183      48.062  25.702  34.258  1.00 43.08           N  
ANISOU 2639  N   GLU B 183     5263   5773   5333   -102   -247   -186       N  
ATOM   2640  CA  GLU B 183      49.111  25.781  35.274  1.00 44.97           C  
ANISOU 2640  CA  GLU B 183     5472   6060   5556    -98   -270   -218       C  
ATOM   2641  C   GLU B 183      49.827  24.461  35.524  1.00 46.05           C  
ANISOU 2641  C   GLU B 183     5598   6219   5680    -72   -304   -196       C  
ATOM   2642  O   GLU B 183      50.746  24.394  36.339  1.00 56.63           O  
ANISOU 2642  O   GLU B 183     6912   7601   7005    -64   -327   -220       O  
ATOM   2643  CB  GLU B 183      48.519  26.308  36.581  1.00 43.99           C  
ANISOU 2643  CB  GLU B 183     5345   5971   5397   -102   -274   -230       C  
ATOM   2644  CG  GLU B 183      47.836  27.652  36.400  1.00 54.42           C  
ANISOU 2644  CG  GLU B 183     6675   7271   6733   -128   -239   -254       C  
ATOM   2645  CD  GLU B 183      47.013  28.075  37.601  1.00 63.33           C  
ANISOU 2645  CD  GLU B 183     7808   8428   7828   -132   -240   -258       C  
ATOM   2646  OE1 GLU B 183      46.706  27.215  38.459  1.00 65.73           O  
ANISOU 2646  OE1 GLU B 183     8117   8762   8095   -114   -266   -230       O  
ATOM   2647  OE2 GLU B 183      46.672  29.275  37.683  1.00 76.17           O  
ANISOU 2647  OE2 GLU B 183     9432  10046   9464   -154   -214   -288       O  
ATOM   2648  N   LEU B 184      49.413  23.406  34.831  1.00 41.61           N  
ANISOU 2648  N   LEU B 184     5056   5629   5124    -58   -308   -151       N  
ATOM   2649  CA  LEU B 184      50.015  22.101  35.050  1.00 42.16           C  
ANISOU 2649  CA  LEU B 184     5119   5716   5185    -32   -338   -126       C  
ATOM   2650  C   LEU B 184      51.328  21.953  34.285  1.00 46.36           C  
ANISOU 2650  C   LEU B 184     5627   6239   5747    -31   -342   -148       C  
ATOM   2651  O   LEU B 184      51.515  22.554  33.225  1.00 39.64           O  
ANISOU 2651  O   LEU B 184     4777   5354   4929    -49   -317   -167       O  
ATOM   2652  CB  LEU B 184      49.033  20.994  34.679  1.00 44.86           C  
ANISOU 2652  CB  LEU B 184     5490   6031   5523    -18   -339    -70       C  
ATOM   2653  CG  LEU B 184      47.866  20.891  35.667  1.00 57.46           C  
ANISOU 2653  CG  LEU B 184     7106   7644   7084    -13   -341    -46       C  
ATOM   2654  CD1 LEU B 184      46.583  20.435  34.987  1.00 54.72           C  
ANISOU 2654  CD1 LEU B 184     6790   7257   6745    -14   -324     -7       C  
ATOM   2655  CD2 LEU B 184      48.232  19.953  36.816  1.00 61.46           C  
ANISOU 2655  CD2 LEU B 184     7604   8193   7557     13   -373    -25       C  
ATOM   2656  N   ASP B 185      52.243  21.168  34.849  1.00 52.51           N  
ANISOU 2656  N   ASP B 185     6386   7050   6514    -11   -373   -147       N  
ATOM   2657  CA  ASP B 185      53.508  20.862  34.197  1.00 56.25           C  
ANISOU 2657  CA  ASP B 185     6837   7520   7016     -6   -380   -165       C  
ATOM   2658  C   ASP B 185      53.270  19.866  33.073  1.00 52.05           C  
ANISOU 2658  C   ASP B 185     6324   6945   6508      2   -374   -126       C  
ATOM   2659  O   ASP B 185      52.634  18.832  33.270  1.00 53.17           O  
ANISOU 2659  O   ASP B 185     6484   7084   6635     20   -385    -81       O  
ATOM   2660  CB  ASP B 185      54.505  20.273  35.196  1.00 71.82           C  
ANISOU 2660  CB  ASP B 185     8781   9541   8966     17   -416   -173       C  
ATOM   2661  CG  ASP B 185      54.691  21.149  36.429  1.00 88.97           C  
ANISOU 2661  CG  ASP B 185    10933  11763  11108     11   -426   -210       C  
ATOM   2662  OD1 ASP B 185      54.423  22.372  36.356  1.00 79.09           O  
ANISOU 2662  OD1 ASP B 185     9682  10505   9865    -15   -401   -245       O  
ATOM   2663  OD2 ASP B 185      55.112  20.609  37.475  1.00107.01           O  
ANISOU 2663  OD2 ASP B 185    13203  14094  13360     34   -458   -205       O  
ATOM   2664  N   CYS B 186      53.783  20.177  31.893  1.00 37.66           N  
ANISOU 2664  N   CYS B 186     4496   5090   4723    -12   -355   -145       N  
ATOM   2665  CA  CYS B 186      53.569  19.332  30.734  1.00 35.89           C  
ANISOU 2665  CA  CYS B 186     4288   4825   4522     -7   -347   -114       C  
ATOM   2666  C   CYS B 186      54.821  18.511  30.447  1.00 36.22           C  
ANISOU 2666  C   CYS B 186     4307   4872   4584      8   -365   -119       C  
ATOM   2667  O   CYS B 186      55.711  18.969  29.729  1.00 38.74           O  
ANISOU 2667  O   CYS B 186     4609   5178   4931     -5   -354   -152       O  
ATOM   2668  CB  CYS B 186      53.233  20.214  29.537  1.00 35.64           C  
ANISOU 2668  CB  CYS B 186     4270   4752   4519    -31   -311   -129       C  
ATOM   2669  SG  CYS B 186      52.605  19.340  28.109  1.00 32.82           S  
ANISOU 2669  SG  CYS B 186     3939   4347   4185    -27   -296    -90       S  
ATOM   2670  N   ILE B 187      54.893  17.305  31.014  1.00 31.61           N  
ANISOU 2670  N   ILE B 187     3721   4305   3983     34   -392    -86       N  
ATOM   2671  CA  ILE B 187      56.078  16.451  30.880  1.00 26.16           C  
ANISOU 2671  CA  ILE B 187     3008   3623   3308     52   -413    -88       C  
ATOM   2672  C   ILE B 187      56.016  15.657  29.581  1.00 26.43           C  
ANISOU 2672  C   ILE B 187     3054   3612   3375     52   -400    -65       C  
ATOM   2673  O   ILE B 187      55.157  14.786  29.416  1.00 28.12           O  
ANISOU 2673  O   ILE B 187     3292   3809   3586     63   -398    -22       O  
ATOM   2674  CB  ILE B 187      56.200  15.485  32.078  1.00 30.87           C  
ANISOU 2674  CB  ILE B 187     3599   4258   3873     83   -446    -59       C  
ATOM   2675  CG1 ILE B 187      56.258  16.277  33.391  1.00 43.17           C  
ANISOU 2675  CG1 ILE B 187     5143   5864   5394     83   -460    -84       C  
ATOM   2676  CG2 ILE B 187      57.418  14.589  31.928  1.00 35.87           C  
ANISOU 2676  CG2 ILE B 187     4207   4899   4524    103   -468    -60       C  
ATOM   2677  CD1 ILE B 187      55.746  15.509  34.604  1.00 43.12           C  
ANISOU 2677  CD1 ILE B 187     5146   5890   5346    110   -484    -45       C  
ATOM   2678  N   PRO B 188      56.925  15.948  28.646  1.00 24.79           N  
ANISOU 2678  N   PRO B 188     2831   3387   3202     40   -388    -95       N  
ATOM   2679  CA  PRO B 188      56.792  15.345  27.316  1.00 18.57           C  
ANISOU 2679  CA  PRO B 188     2055   2555   2444     37   -372    -78       C  
ATOM   2680  C   PRO B 188      57.220  13.889  27.305  1.00 25.04           C  
ANISOU 2680  C   PRO B 188     2868   3373   3272     62   -392    -48       C  
ATOM   2681  O   PRO B 188      58.347  13.558  27.704  1.00 26.11           O  
ANISOU 2681  O   PRO B 188     2975   3532   3412     76   -414    -63       O  
ATOM   2682  CB  PRO B 188      57.741  16.191  26.452  1.00 18.32           C  
ANISOU 2682  CB  PRO B 188     2007   2509   2444     16   -353   -124       C  
ATOM   2683  CG  PRO B 188      58.778  16.691  27.422  1.00 21.85           C  
ANISOU 2683  CG  PRO B 188     2422   2998   2883     19   -372   -161       C  
ATOM   2684  CD  PRO B 188      58.072  16.873  28.730  1.00 23.55           C  
ANISOU 2684  CD  PRO B 188     2644   3248   3058     28   -388   -149       C  
ATOM   2685  N   LEU B 189      56.328  13.028  26.828  1.00 24.34           N  
ANISOU 2685  N   LEU B 189     2803   3258   3187     68   -385     -8       N  
ATOM   2686  CA  LEU B 189      56.597  11.600  26.728  1.00 16.98           C  
ANISOU 2686  CA  LEU B 189     1867   2317   2266     91   -399     23       C  
ATOM   2687  C   LEU B 189      56.458  11.164  25.278  1.00 19.27           C  
ANISOU 2687  C   LEU B 189     2168   2564   2591     81   -378     28       C  
ATOM   2688  O   LEU B 189      55.337  11.115  24.750  1.00 18.83           O  
ANISOU 2688  O   LEU B 189     2137   2483   2533     73   -360     48       O  
ATOM   2689  CB  LEU B 189      55.592  10.820  27.581  1.00 22.09           C  
ANISOU 2689  CB  LEU B 189     2534   2974   2886    110   -410     68       C  
ATOM   2690  CG  LEU B 189      55.495  11.185  29.058  1.00 26.87           C  
ANISOU 2690  CG  LEU B 189     3135   3622   3451    121   -429     70       C  
ATOM   2691  CD1 LEU B 189      54.476  10.302  29.738  1.00 29.84           C  
ANISOU 2691  CD1 LEU B 189     3533   4000   3804    139   -434    118       C  
ATOM   2692  CD2 LEU B 189      56.850  11.010  29.705  1.00 32.17           C  
ANISOU 2692  CD2 LEU B 189     3774   4329   4120    139   -457     51       C  
ATOM   2693  N   TRP B 190      57.571  10.833  24.628  1.00 18.47           N  
ANISOU 2693  N   TRP B 190     2045   2454   2519     82   -380     10       N  
ATOM   2694  CA  TRP B 190      57.526  10.475  23.211  1.00 15.51           C  
ANISOU 2694  CA  TRP B 190     1677   2038   2176     71   -358     11       C  
ATOM   2695  C   TRP B 190      58.575   9.429  22.846  1.00 25.71           C  
ANISOU 2695  C   TRP B 190     2948   3324   3498     86   -369     12       C  
ATOM   2696  O   TRP B 190      59.551   9.235  23.569  1.00 24.26           O  
ANISOU 2696  O   TRP B 190     2738   3165   3312    101   -392      2       O  
ATOM   2697  CB  TRP B 190      57.746  11.719  22.337  1.00 13.97           C  
ANISOU 2697  CB  TRP B 190     1483   1830   1994     44   -333    -27       C  
ATOM   2698  CG  TRP B 190      59.187  12.033  22.171  1.00 20.94           C  
ANISOU 2698  CG  TRP B 190     2336   2721   2900     40   -337    -65       C  
ATOM   2699  CD1 TRP B 190      59.988  11.664  21.134  1.00 20.85           C  
ANISOU 2699  CD1 TRP B 190     2312   2687   2922     36   -328    -79       C  
ATOM   2700  CD2 TRP B 190      60.019  12.748  23.083  1.00 22.77           C  
ANISOU 2700  CD2 TRP B 190     2544   2987   3121     41   -352    -97       C  
ATOM   2701  NE1 TRP B 190      61.267  12.109  21.336  1.00 25.77           N  
ANISOU 2701  NE1 TRP B 190     2906   3326   3558     33   -335   -117       N  
ATOM   2702  CE2 TRP B 190      61.318  12.775  22.536  1.00 22.52           C  
ANISOU 2702  CE2 TRP B 190     2486   2951   3121     36   -350   -130       C  
ATOM   2703  CE3 TRP B 190      59.799  13.366  24.318  1.00 19.91           C  
ANISOU 2703  CE3 TRP B 190     2178   2660   2727     44   -366   -103       C  
ATOM   2704  CZ2 TRP B 190      62.392  13.403  23.166  1.00 28.16           C  
ANISOU 2704  CZ2 TRP B 190     3170   3695   3836     35   -362   -170       C  
ATOM   2705  CZ3 TRP B 190      60.868  13.991  24.949  1.00 25.57           C  
ANISOU 2705  CZ3 TRP B 190     2864   3407   3443     43   -379   -143       C  
ATOM   2706  CH2 TRP B 190      62.148  14.005  24.370  1.00 30.10           C  
ANISOU 2706  CH2 TRP B 190     3412   3976   4049     39   -377   -176       C  
ATOM   2707  N   GLY B 191      58.373   8.768  21.707  1.00 22.98           N  
ANISOU 2707  N   GLY B 191     2611   2944   3179     81   -353     22       N  
ATOM   2708  CA  GLY B 191      59.339   7.822  21.178  1.00 23.50           C  
ANISOU 2708  CA  GLY B 191     2656   2996   3276     91   -358     20       C  
ATOM   2709  C   GLY B 191      59.311   8.003  19.681  1.00 27.94           C  
ANISOU 2709  C   GLY B 191     3226   3524   3866     70   -330      4       C  
ATOM   2710  O   GLY B 191      58.318   8.503  19.147  1.00 22.57           O  
ANISOU 2710  O   GLY B 191     2570   2829   3176     55   -311      9       O  
ATOM   2711  N   THR B 192      60.383   7.609  19.001  1.00 20.60           N  
ANISOU 2711  N   THR B 192     2276   2584   2969     69   -329    -14       N  
ATOM   2712  CA  THR B 192      60.498   7.852  17.574  1.00 20.53           C  
ANISOU 2712  CA  THR B 192     2272   2544   2984     49   -302    -34       C  
ATOM   2713  C   THR B 192      61.229   6.742  16.823  1.00 22.97           C  
ANISOU 2713  C   THR B 192     2565   2833   3329     56   -301    -33       C  
ATOM   2714  O   THR B 192      62.254   6.246  17.276  1.00 23.50           O  
ANISOU 2714  O   THR B 192     2607   2912   3411     70   -319    -40       O  
ATOM   2715  CB  THR B 192      61.279   9.153  17.302  1.00 27.39           C  
ANISOU 2715  CB  THR B 192     3130   3419   3858     30   -290    -77       C  
ATOM   2716  OG1 THR B 192      60.804  10.192  18.171  1.00 34.25           O  
ANISOU 2716  OG1 THR B 192     4007   4310   4695     25   -293    -82       O  
ATOM   2717  CG2 THR B 192      61.086   9.576  15.865  1.00 21.75           C  
ANISOU 2717  CG2 THR B 192     2430   2674   3159      9   -258    -91       C  
ATOM   2718  N  AVAL B 193      60.703   6.373  15.662  0.57 21.08           N  
ANISOU 2718  N  AVAL B 193     2341   2565   3105     46   -279    -27       N  
ATOM   2719  N  BVAL B 193      60.720   6.416  15.646  0.43 21.06           N  
ANISOU 2719  N  BVAL B 193     2338   2563   3102     45   -279    -29       N  
ATOM   2720  CA AVAL B 193      61.439   5.547  14.726  0.57 20.93           C  
ANISOU 2720  CA AVAL B 193     2307   2524   3122     45   -272    -36       C  
ATOM   2721  CA BVAL B 193      61.412   5.544  14.723  0.43 20.93           C  
ANISOU 2721  CA BVAL B 193     2307   2523   3121     45   -272    -36       C  
ATOM   2722  C  AVAL B 193      61.475   6.286  13.400  0.57 25.20           C  
ANISOU 2722  C  AVAL B 193     2857   3046   3674     21   -242    -62       C  
ATOM   2723  C  BVAL B 193      61.459   6.238  13.370  0.43 25.20           C  
ANISOU 2723  C  BVAL B 193     2857   3044   3674     21   -242    -62       C  
ATOM   2724  O  AVAL B 193      60.491   6.910  12.992  0.57 21.26           O  
ANISOU 2724  O  AVAL B 193     2383   2540   3155      9   -226    -58       O  
ATOM   2725  O  BVAL B 193      60.451   6.749  12.900  0.43 21.24           O  
ANISOU 2725  O  BVAL B 193     2380   2535   3154     10   -226    -55       O  
ATOM   2726  CB AVAL B 193      60.800   4.153  14.555  0.57 33.39           C  
ANISOU 2726  CB AVAL B 193     3890   4084   4711     58   -273     -3       C  
ATOM   2727  CB BVAL B 193      60.696   4.190  14.578  0.43 33.37           C  
ANISOU 2727  CB BVAL B 193     3890   4082   4706     58   -273     -1       C  
ATOM   2728  CG1AVAL B 193      59.351   4.290  14.176  0.57 29.84           C  
ANISOU 2728  CG1AVAL B 193     3471   3624   4243     50   -258     15       C  
ATOM   2729  CG1BVAL B 193      61.264   3.413  13.407  0.43 30.01           C  
ANISOU 2729  CG1BVAL B 193     3453   3630   4318     53   -259    -13       C  
ATOM   2730  CG2AVAL B 193      61.556   3.337  13.493  0.57 30.99           C  
ANISOU 2730  CG2AVAL B 193     3571   3757   4448     56   -262    -15       C  
ATOM   2731  CG2BVAL B 193      60.819   3.388  15.861  0.43 31.82           C  
ANISOU 2731  CG2BVAL B 193     3683   3903   4503     85   -300     26       C  
ATOM   2732  N   SER B 194      62.633   6.270  12.751  1.00 25.65           N  
ANISOU 2732  N   SER B 194     2894   3093   3759     14   -235    -91       N  
ATOM   2733  CA  SER B 194      62.741   6.790  11.397  1.00 26.63           C  
ANISOU 2733  CA  SER B 194     3026   3196   3896     -7   -205   -113       C  
ATOM   2734  C   SER B 194      63.736   5.929  10.626  1.00 30.12           C  
ANISOU 2734  C   SER B 194     3447   3621   4377     -7   -201   -128       C  
ATOM   2735  O   SER B 194      64.942   6.069  10.788  1.00 34.58           O  
ANISOU 2735  O   SER B 194     3987   4191   4961     -7   -206   -153       O  
ATOM   2736  CB  SER B 194      63.179   8.252  11.398  1.00 21.30           C  
ANISOU 2736  CB  SER B 194     2351   2529   3212    -23   -192   -144       C  
ATOM   2737  OG  SER B 194      63.055   8.817  10.096  1.00 24.34           O  
ANISOU 2737  OG  SER B 194     2753   2894   3604    -42   -160   -159       O  
ATOM   2738  N   ILE B 195      63.218   5.042   9.786  1.00 27.29           N  
ANISOU 2738  N   ILE B 195     3098   3242   4030     -7   -190   -114       N  
ATOM   2739  CA  ILE B 195      64.049   4.046   9.123  1.00 27.85           C  
ANISOU 2739  CA  ILE B 195     3147   3295   4138     -5   -187   -123       C  
ATOM   2740  C   ILE B 195      63.873   4.056   7.613  1.00 29.57           C  
ANISOU 2740  C   ILE B 195     3376   3490   4367    -23   -157   -137       C  
ATOM   2741  O   ILE B 195      62.797   4.386   7.090  1.00 29.08           O  
ANISOU 2741  O   ILE B 195     3340   3424   4284    -31   -143   -127       O  
ATOM   2742  CB  ILE B 195      63.746   2.636   9.632  1.00 31.03           C  
ANISOU 2742  CB  ILE B 195     3543   3695   4553     16   -204    -93       C  
ATOM   2743  CG1 ILE B 195      62.274   2.299   9.413  1.00 26.92           C  
ANISOU 2743  CG1 ILE B 195     3049   3167   4013     15   -196    -65       C  
ATOM   2744  CG2 ILE B 195      64.114   2.500  11.112  1.00 29.97           C  
ANISOU 2744  CG2 ILE B 195     3394   3584   4408     37   -235    -79       C  
ATOM   2745  CD1 ILE B 195      61.917   0.875   9.806  1.00 26.24           C  
ANISOU 2745  CD1 ILE B 195     2957   3072   3942     34   -207    -36       C  
ATOM   2746  N   GLN B 196      64.940   3.680   6.917  1.00 29.09           N  
ANISOU 2746  N   GLN B 196     3296   3417   4341    -28   -148   -161       N  
ATOM   2747  CA  GLN B 196      64.936   3.633   5.460  1.00 25.76           C  
ANISOU 2747  CA  GLN B 196     2881   2974   3931    -45   -119   -177       C  
ATOM   2748  C   GLN B 196      63.969   2.578   4.952  1.00 26.44           C  
ANISOU 2748  C   GLN B 196     2979   3049   4020    -41   -116   -156       C  
ATOM   2749  O   GLN B 196      63.339   2.762   3.909  1.00 24.90           O  
ANISOU 2749  O   GLN B 196     2801   2845   3815    -53    -94   -160       O  
ATOM   2750  CB  GLN B 196      66.347   3.355   4.920  1.00 32.65           C  
ANISOU 2750  CB  GLN B 196     3728   3836   4843    -51   -112   -208       C  
ATOM   2751  CG  GLN B 196      66.464   3.463   3.389  1.00 31.03           C  
ANISOU 2751  CG  GLN B 196     3530   3610   4648    -70    -79   -229       C  
ATOM   2752  CD  GLN B 196      67.913   3.404   2.899  1.00 40.17           C  
ANISOU 2752  CD  GLN B 196     4662   4757   5843    -78    -69   -263       C  
ATOM   2753  OE1 GLN B 196      68.830   3.862   3.583  1.00 35.95           O  
ANISOU 2753  OE1 GLN B 196     4109   4232   5318    -76    -80   -280       O  
ATOM   2754  NE2 GLN B 196      68.118   2.838   1.713  1.00 33.61           N  
ANISOU 2754  NE2 GLN B 196     3828   3908   5033    -88    -48   -276       N  
ATOM   2755  N   GLY B 197      63.858   1.474   5.691  1.00 24.06           N  
ANISOU 2755  N   GLY B 197     2665   2747   3731    -23   -135   -133       N  
ATOM   2756  CA  GLY B 197      62.983   0.382   5.307  1.00 29.69           C  
ANISOU 2756  CA  GLY B 197     3384   3447   4451    -18   -131   -114       C  
ATOM   2757  C   GLY B 197      63.462  -0.315   4.045  1.00 36.03           C  
ANISOU 2757  C   GLY B 197     4174   4228   5286    -29   -111   -135       C  
ATOM   2758  O   GLY B 197      64.661  -0.405   3.785  1.00 42.18           O  
ANISOU 2758  O   GLY B 197     4933   5001   6092    -32   -109   -157       O  
ATOM   2759  N   ASN B 198      62.520  -0.799   3.249  1.00 41.21           N  
ANISOU 2759  N   ASN B 198     4844   4875   5939    -35    -97   -130       N  
ATOM   2760  CA  ASN B 198      62.849  -1.528   2.034  1.00 46.58           C  
ANISOU 2760  CA  ASN B 198     5514   5537   6649    -45    -77   -150       C  
ATOM   2761  C   ASN B 198      62.910  -0.605   0.837  1.00 46.64           C  
ANISOU 2761  C   ASN B 198     5534   5545   6641    -64    -53   -175       C  
ATOM   2762  O   ASN B 198      62.233  -0.844  -0.164  1.00 56.51           O  
ANISOU 2762  O   ASN B 198     6795   6790   7885    -73    -36   -181       O  
ATOM   2763  CB  ASN B 198      61.824  -2.637   1.768  1.00 43.53           C  
ANISOU 2763  CB  ASN B 198     5130   5141   6270    -41    -73   -134       C  
ATOM   2764  CG  ASN B 198      61.872  -3.739   2.808  1.00 50.53           C  
ANISOU 2764  CG  ASN B 198     6001   6020   7179    -22    -90   -109       C  
ATOM   2765  OD1 ASN B 198      60.834  -4.228   3.263  1.00 54.87           O  
ANISOU 2765  OD1 ASN B 198     6560   6569   7720    -14    -95    -85       O  
ATOM   2766  ND2 ASN B 198      63.080  -4.139   3.190  1.00 53.62           N  
ANISOU 2766  ND2 ASN B 198     6367   6405   7600    -13   -100   -115       N  
ATOM   2767  N   ARG B 199      63.710   0.452   0.939  1.00 43.19           N  
ANISOU 2767  N   ARG B 199     5097   5115   6197    -70    -51   -191       N  
ATOM   2768  CA  ARG B 199      63.901   1.377  -0.174  1.00 46.24           C  
ANISOU 2768  CA  ARG B 199     5497   5500   6572    -88    -25   -214       C  
ATOM   2769  C   ARG B 199      65.368   1.736  -0.310  1.00 40.14           C  
ANISOU 2769  C   ARG B 199     4706   4721   5825    -95    -18   -242       C  
ATOM   2770  O   ARG B 199      66.106   1.713   0.670  1.00 36.94           O  
ANISOU 2770  O   ARG B 199     4281   4319   5433    -87    -37   -242       O  
ATOM   2771  CB  ARG B 199      63.054   2.637  -0.008  1.00 47.01           C  
ANISOU 2771  CB  ARG B 199     5624   5612   6626    -90    -21   -204       C  
ATOM   2772  CG  ARG B 199      62.501   3.132  -1.329  1.00 54.84           C  
ANISOU 2772  CG  ARG B 199     6637   6602   7597   -103      5   -214       C  
ATOM   2773  CD  ARG B 199      61.422   4.168  -1.134  1.00 47.69           C  
ANISOU 2773  CD  ARG B 199     5760   5710   6649   -101      7   -197       C  
ATOM   2774  NE  ARG B 199      61.970   5.416  -0.611  1.00 57.46           N  
ANISOU 2774  NE  ARG B 199     7003   6953   7876   -105      9   -204       N  
ATOM   2775  CZ  ARG B 199      61.406   6.605  -0.793  1.00 55.32           C  
ANISOU 2775  CZ  ARG B 199     6757   6689   7574   -108     22   -200       C  
ATOM   2776  NH1 ARG B 199      61.966   7.696  -0.280  1.00 48.16           N  
ANISOU 2776  NH1 ARG B 199     5851   5784   6663   -113     27   -208       N  
ATOM   2777  NH2 ARG B 199      60.276   6.700  -1.493  1.00 58.94           N  
ANISOU 2777  NH2 ARG B 199     7237   7152   8005   -107     32   -188       N  
ATOM   2778  N   SER B 200      65.786   2.053  -1.529  1.00 33.98           N  
ANISOU 2778  N   SER B 200     3929   3931   5051   -111      9   -267       N  
ATOM   2779  CA  SER B 200      67.207   2.242  -1.821  1.00 44.37           C  
ANISOU 2779  CA  SER B 200     5225   5238   6397   -120     20   -297       C  
ATOM   2780  C   SER B 200      67.801   3.515  -1.225  1.00 44.97           C  
ANISOU 2780  C   SER B 200     5302   5321   6462   -124     20   -308       C  
ATOM   2781  O   SER B 200      69.024   3.626  -1.084  1.00 44.52           O  
ANISOU 2781  O   SER B 200     5223   5260   6434   -128     22   -332       O  
ATOM   2782  CB  SER B 200      67.455   2.211  -3.333  1.00 47.17           C  
ANISOU 2782  CB  SER B 200     5584   5579   6758   -136     52   -321       C  
ATOM   2783  OG  SER B 200      66.656   3.175  -3.997  1.00 58.28           O  
ANISOU 2783  OG  SER B 200     7023   6993   8128   -144     72   -317       O  
ATOM   2784  N   GLU B 201      66.945   4.479  -0.896  1.00 37.80           N  
ANISOU 2784  N   GLU B 201     4419   4426   5516   -123     21   -293       N  
ATOM   2785  CA  GLU B 201      67.399   5.743  -0.311  1.00 41.92           C  
ANISOU 2785  CA  GLU B 201     4945   4956   6029   -128     23   -304       C  
ATOM   2786  C   GLU B 201      66.481   6.226   0.822  1.00 38.97           C  
ANISOU 2786  C   GLU B 201     4584   4600   5623   -117      2   -277       C  
ATOM   2787  O   GLU B 201      65.277   5.927   0.840  1.00 36.66           O  
ANISOU 2787  O   GLU B 201     4310   4312   5306   -110     -5   -251       O  
ATOM   2788  CB  GLU B 201      67.549   6.814  -1.396  1.00 49.41           C  
ANISOU 2788  CB  GLU B 201     5913   5896   6967   -145     60   -322       C  
ATOM   2789  CG  GLU B 201      68.602   6.448  -2.449  1.00 57.61           C  
ANISOU 2789  CG  GLU B 201     6936   6916   8038   -157     83   -352       C  
ATOM   2790  CD  GLU B 201      68.924   7.585  -3.412  1.00 75.81           C  
ANISOU 2790  CD  GLU B 201     9258   9212  10335   -174    122   -371       C  
ATOM   2791  OE1 GLU B 201      70.102   7.698  -3.827  1.00 70.97           O  
ANISOU 2791  OE1 GLU B 201     8629   8586   9751   -185    140   -401       O  
ATOM   2792  OE2 GLU B 201      68.002   8.356  -3.768  1.00 76.06           O  
ANISOU 2792  OE2 GLU B 201     9322   9248  10331   -175    137   -356       O  
ATOM   2793  N   MET B 202      67.061   6.957   1.771  1.00 32.97           N  
ANISOU 2793  N   MET B 202     3813   3850   4863   -116     -8   -287       N  
ATOM   2794  CA  MET B 202      66.324   7.512   2.904  1.00 29.93           C  
ANISOU 2794  CA  MET B 202     3440   3484   4449   -107    -27   -267       C  
ATOM   2795  C   MET B 202      65.958   8.958   2.633  1.00 36.00           C  
ANISOU 2795  C   MET B 202     4232   4253   5192   -119     -4   -273       C  
ATOM   2796  O   MET B 202      66.852   9.794   2.486  1.00 32.31           O  
ANISOU 2796  O   MET B 202     3758   3782   4738   -131     14   -301       O  
ATOM   2797  CB  MET B 202      67.166   7.454   4.183  1.00 28.95           C  
ANISOU 2797  CB  MET B 202     3287   3374   4338    -97    -54   -275       C  
ATOM   2798  CG  MET B 202      66.463   8.074   5.398  1.00 34.94           C  
ANISOU 2798  CG  MET B 202     4056   4155   5066    -89    -74   -257       C  
ATOM   2799  SD  MET B 202      64.825   7.332   5.692  1.00 27.42           S  
ANISOU 2799  SD  MET B 202     3128   3208   4085    -74    -89   -211       S  
ATOM   2800  CE  MET B 202      64.569   7.690   7.440  1.00 26.25           C  
ANISOU 2800  CE  MET B 202     2975   3087   3913    -60   -121   -196       C  
ATOM   2801  N   GLU B 203      64.657   9.266   2.584  1.00 29.96           N  
ANISOU 2801  N   GLU B 203     3496   3494   4394   -115     -2   -248       N  
ATOM   2802  CA  GLU B 203      64.222  10.657   2.368  1.00 28.94           C  
ANISOU 2802  CA  GLU B 203     3391   3365   4240   -124     21   -250       C  
ATOM   2803  C   GLU B 203      63.193  11.189   3.380  1.00 25.82           C  
ANISOU 2803  C   GLU B 203     3011   2985   3813   -116      5   -227       C  
ATOM   2804  O   GLU B 203      62.655  12.274   3.200  1.00 22.02           O  
ANISOU 2804  O   GLU B 203     2551   2504   3310   -122     24   -224       O  
ATOM   2805  CB  GLU B 203      63.713  10.878   0.940  1.00 21.44           C  
ANISOU 2805  CB  GLU B 203     2466   2402   3278   -132     52   -248       C  
ATOM   2806  CG  GLU B 203      64.736  10.532  -0.141  1.00 35.57           C  
ANISOU 2806  CG  GLU B 203     4244   4175   5097   -142     74   -273       C  
ATOM   2807  CD  GLU B 203      64.103  10.370  -1.518  1.00 37.08           C  
ANISOU 2807  CD  GLU B 203     4457   4358   5274   -145     97   -266       C  
ATOM   2808  OE1 GLU B 203      62.974   9.835  -1.601  1.00 37.16           O  
ANISOU 2808  OE1 GLU B 203     4480   4376   5263   -135     84   -243       O  
ATOM   2809  OE2 GLU B 203      64.735  10.772  -2.519  1.00 38.88           O  
ANISOU 2809  OE2 GLU B 203     4690   4573   5511   -156    127   -286       O  
ATOM   2810  N   ASP B 204      62.921  10.424   4.428  1.00 23.93           N  
ANISOU 2810  N   ASP B 204     2760   2760   3572   -103    -28   -210       N  
ATOM   2811  CA  ASP B 204      62.148  10.930   5.551  1.00 23.75           C  
ANISOU 2811  CA  ASP B 204     2746   2755   3523    -95    -44   -192       C  
ATOM   2812  C   ASP B 204      63.112  11.662   6.482  1.00 26.57           C  
ANISOU 2812  C   ASP B 204     3084   3122   3888    -99    -51   -215       C  
ATOM   2813  O   ASP B 204      64.315  11.397   6.487  1.00 26.06           O  
ANISOU 2813  O   ASP B 204     2993   3055   3852   -102    -53   -239       O  
ATOM   2814  CB  ASP B 204      61.512   9.781   6.349  1.00 18.85           C  
ANISOU 2814  CB  ASP B 204     2121   2145   2896    -79    -76   -164       C  
ATOM   2815  CG  ASP B 204      60.219   9.238   5.730  1.00 17.42           C  
ANISOU 2815  CG  ASP B 204     1961   1958   2698    -75    -72   -139       C  
ATOM   2816  OD1 ASP B 204      59.864   9.611   4.595  1.00 18.91           O  
ANISOU 2816  OD1 ASP B 204     2167   2136   2880    -83    -47   -144       O  
ATOM   2817  OD2 ASP B 204      59.565   8.401   6.399  1.00 19.59           O  
ANISOU 2817  OD2 ASP B 204     2235   2240   2968    -62    -93   -116       O  
ATOM   2818  N   ALA B 205      62.567  12.564   7.283  1.00 17.17           N  
ANISOU 2818  N   ALA B 205     1904   1946   2675    -99    -54   -210       N  
ATOM   2819  CA  ALA B 205      63.300  13.235   8.351  1.00 23.33           C  
ANISOU 2819  CA  ALA B 205     2665   2742   3458   -101    -65   -230       C  
ATOM   2820  C   ALA B 205      62.276  13.616   9.410  1.00 21.90           C  
ANISOU 2820  C   ALA B 205     2497   2578   3244    -93    -81   -209       C  
ATOM   2821  O   ALA B 205      61.080  13.610   9.126  1.00 23.58           O  
ANISOU 2821  O   ALA B 205     2736   2788   3436    -90    -76   -183       O  
ATOM   2822  CB  ALA B 205      64.012  14.485   7.811  1.00 21.61           C  
ANISOU 2822  CB  ALA B 205     2448   2512   3253   -119    -31   -264       C  
ATOM   2823  N   PHE B 206      62.730  13.953  10.617  1.00 21.94           N  
ANISOU 2823  N   PHE B 206     2483   2605   3246    -90   -100   -221       N  
ATOM   2824  CA  PHE B 206      61.827  14.312  11.708  1.00 19.18           C  
ANISOU 2824  CA  PHE B 206     2145   2276   2867    -83   -116   -203       C  
ATOM   2825  C   PHE B 206      62.567  15.231  12.660  1.00 20.20           C  
ANISOU 2825  C   PHE B 206     2254   2424   2996    -89   -121   -233       C  
ATOM   2826  O   PHE B 206      63.798  15.248  12.670  1.00 24.22           O  
ANISOU 2826  O   PHE B 206     2737   2935   3531    -93   -121   -263       O  
ATOM   2827  CB  PHE B 206      61.353  13.060  12.482  1.00 12.44           C  
ANISOU 2827  CB  PHE B 206     1287   1437   2003    -63   -150   -171       C  
ATOM   2828  CG  PHE B 206      62.409  12.482  13.377  1.00 25.73           C  
ANISOU 2828  CG  PHE B 206     2938   3139   3699    -51   -178   -183       C  
ATOM   2829  CD1 PHE B 206      62.493  12.856  14.709  1.00 29.12           C  
ANISOU 2829  CD1 PHE B 206     3356   3598   4111    -44   -200   -186       C  
ATOM   2830  CD2 PHE B 206      63.351  11.585  12.875  1.00 27.23           C  
ANISOU 2830  CD2 PHE B 206     3108   3320   3920    -47   -182   -192       C  
ATOM   2831  CE1 PHE B 206      63.497  12.335  15.540  1.00 34.65           C  
ANISOU 2831  CE1 PHE B 206     4026   4320   4822    -31   -227   -198       C  
ATOM   2832  CE2 PHE B 206      64.358  11.058  13.699  1.00 28.09           C  
ANISOU 2832  CE2 PHE B 206     3185   3447   4041    -34   -209   -202       C  
ATOM   2833  CZ  PHE B 206      64.429  11.436  15.031  1.00 30.59           C  
ANISOU 2833  CZ  PHE B 206     3491   3795   4337    -25   -232   -205       C  
ATOM   2834  N   ALA B 207      61.821  15.983  13.467  1.00 18.27           N  
ANISOU 2834  N   ALA B 207     2021   2194   2727    -89   -124   -226       N  
ATOM   2835  CA  ALA B 207      62.414  16.755  14.560  1.00 21.85           C  
ANISOU 2835  CA  ALA B 207     2454   2671   3177    -93   -133   -254       C  
ATOM   2836  C   ALA B 207      61.539  16.726  15.807  1.00 21.97           C  
ANISOU 2836  C   ALA B 207     2475   2712   3159    -81   -158   -232       C  
ATOM   2837  O   ALA B 207      60.317  16.808  15.734  1.00 21.85           O  
ANISOU 2837  O   ALA B 207     2487   2692   3122    -80   -153   -203       O  
ATOM   2838  CB  ALA B 207      62.671  18.197  14.140  1.00 18.68           C  
ANISOU 2838  CB  ALA B 207     2057   2257   2784   -114    -97   -285       C  
ATOM   2839  N   VAL B 208      62.180  16.582  16.951  1.00 17.96           N  
ANISOU 2839  N   VAL B 208     1942   2235   2648    -73   -185   -245       N  
ATOM   2840  CA  VAL B 208      61.492  16.644  18.218  1.00 18.18           C  
ANISOU 2840  CA  VAL B 208     1973   2292   2644    -62   -208   -229       C  
ATOM   2841  C   VAL B 208      62.238  17.642  19.095  1.00 26.60           C  
ANISOU 2841  C   VAL B 208     3015   3383   3708    -71   -211   -270       C  
ATOM   2842  O   VAL B 208      63.463  17.580  19.215  1.00 24.86           O  
ANISOU 2842  O   VAL B 208     2764   3172   3508    -71   -218   -301       O  
ATOM   2843  CB  VAL B 208      61.465  15.285  18.906  1.00 22.55           C  
ANISOU 2843  CB  VAL B 208     2518   2863   3187    -38   -244   -200       C  
ATOM   2844  CG1 VAL B 208      60.930  15.446  20.318  1.00 21.80           C  
ANISOU 2844  CG1 VAL B 208     2423   2802   3059    -27   -267   -188       C  
ATOM   2845  CG2 VAL B 208      60.624  14.287  18.093  1.00 21.01           C  
ANISOU 2845  CG2 VAL B 208     2346   2642   2994    -30   -240   -160       C  
ATOM   2846  N   SER B 209      61.514  18.583  19.687  1.00 20.34           N  
ANISOU 2846  N   SER B 209     2235   2600   2894    -78   -203   -272       N  
ATOM   2847  CA  SER B 209      62.159  19.548  20.556  1.00 24.14           C  
ANISOU 2847  CA  SER B 209     2692   3107   3373    -88   -205   -313       C  
ATOM   2848  C   SER B 209      61.320  19.828  21.789  1.00 25.36           C  
ANISOU 2848  C   SER B 209     2854   3291   3492    -81   -222   -301       C  
ATOM   2849  O   SER B 209      60.439  20.674  21.760  1.00 24.83           O  
ANISOU 2849  O   SER B 209     2808   3214   3413    -93   -201   -297       O  
ATOM   2850  CB  SER B 209      62.471  20.826  19.787  1.00 29.11           C  
ANISOU 2850  CB  SER B 209     3323   3711   4026   -113   -163   -349       C  
ATOM   2851  OG  SER B 209      63.431  21.591  20.488  1.00 42.89           O  
ANISOU 2851  OG  SER B 209     5037   5479   5781   -123   -163   -397       O  
ATOM   2852  N   PRO B 210      61.590  19.100  22.885  1.00 21.69           N  
ANISOU 2852  N   PRO B 210     2370   2862   3008    -61   -260   -293       N  
ATOM   2853  CA  PRO B 210      60.817  19.249  24.121  1.00 21.21           C  
ANISOU 2853  CA  PRO B 210     2316   2832   2910    -53   -279   -279       C  
ATOM   2854  C   PRO B 210      61.135  20.578  24.809  1.00 24.87           C  
ANISOU 2854  C   PRO B 210     2762   3317   3369    -70   -269   -325       C  
ATOM   2855  O   PRO B 210      62.253  21.078  24.690  1.00 29.68           O  
ANISOU 2855  O   PRO B 210     3344   3931   4002    -80   -262   -369       O  
ATOM   2856  CB  PRO B 210      61.289  18.064  24.971  1.00 23.87           C  
ANISOU 2856  CB  PRO B 210     2634   3202   3234    -26   -320   -262       C  
ATOM   2857  CG  PRO B 210      62.676  17.799  24.503  1.00 25.65           C  
ANISOU 2857  CG  PRO B 210     2830   3425   3492    -25   -323   -292       C  
ATOM   2858  CD  PRO B 210      62.691  18.131  23.028  1.00 25.11           C  
ANISOU 2858  CD  PRO B 210     2775   3310   3455    -45   -286   -299       C  
ATOM   2859  N   HIS B 211      60.156  21.144  25.505  1.00 27.80           N  
ANISOU 2859  N   HIS B 211     3150   3700   3713    -73   -267   -315       N  
ATOM   2860  CA  HIS B 211      60.314  22.438  26.164  1.00 32.85           C  
ANISOU 2860  CA  HIS B 211     3775   4357   4348    -91   -254   -358       C  
ATOM   2861  C   HIS B 211      60.913  23.468  25.215  1.00 30.98           C  
ANISOU 2861  C   HIS B 211     3533   4091   4149   -116   -215   -398       C  
ATOM   2862  O   HIS B 211      61.706  24.314  25.617  1.00 26.20           O  
ANISOU 2862  O   HIS B 211     2899   3500   3554   -129   -207   -447       O  
ATOM   2863  CB  HIS B 211      61.189  22.296  27.410  1.00 30.44           C  
ANISOU 2863  CB  HIS B 211     3434   4104   4028    -79   -288   -386       C  
ATOM   2864  CG  HIS B 211      60.710  21.255  28.368  1.00 33.04           C  
ANISOU 2864  CG  HIS B 211     3768   4465   4320    -52   -326   -346       C  
ATOM   2865  ND1 HIS B 211      59.616  21.445  29.190  1.00 47.24           N  
ANISOU 2865  ND1 HIS B 211     5586   6279   6083    -49   -332   -324       N  
ATOM   2866  CD2 HIS B 211      61.166  20.007  28.634  1.00 30.88           C  
ANISOU 2866  CD2 HIS B 211     3485   4209   4040    -26   -359   -322       C  
ATOM   2867  CE1 HIS B 211      59.424  20.363  29.922  1.00 35.95           C  
ANISOU 2867  CE1 HIS B 211     4158   4875   4626    -22   -365   -289       C  
ATOM   2868  NE2 HIS B 211      60.357  19.478  29.609  1.00 31.19           N  
ANISOU 2868  NE2 HIS B 211     3538   4273   4040     -7   -382   -286       N  
ATOM   2869  N   PHE B 212      60.551  23.382  23.944  1.00 26.62           N  
ANISOU 2869  N   PHE B 212     3004   3494   3615   -122   -189   -377       N  
ATOM   2870  CA  PHE B 212      61.159  24.255  22.963  1.00 34.05           C  
ANISOU 2870  CA  PHE B 212     3942   4405   4592   -143   -149   -410       C  
ATOM   2871  C   PHE B 212      60.547  25.654  22.984  1.00 31.67           C  
ANISOU 2871  C   PHE B 212     3654   4089   4291   -163   -114   -426       C  
ATOM   2872  O   PHE B 212      61.249  26.647  22.840  1.00 34.48           O  
ANISOU 2872  O   PHE B 212     3993   4436   4671   -182    -87   -471       O  
ATOM   2873  CB  PHE B 212      61.048  23.641  21.567  1.00 28.53           C  
ANISOU 2873  CB  PHE B 212     3264   3666   3911   -141   -134   -382       C  
ATOM   2874  CG  PHE B 212      61.632  24.497  20.477  1.00 26.46           C  
ANISOU 2874  CG  PHE B 212     3001   3368   3683   -161    -91   -411       C  
ATOM   2875  CD1 PHE B 212      62.992  24.757  20.440  1.00 31.99           C  
ANISOU 2875  CD1 PHE B 212     3669   4074   4413   -171    -85   -458       C  
ATOM   2876  CD2 PHE B 212      60.826  25.020  19.486  1.00 27.43           C  
ANISOU 2876  CD2 PHE B 212     3157   3455   3810   -170    -56   -392       C  
ATOM   2877  CE1 PHE B 212      63.540  25.527  19.441  1.00 30.03           C  
ANISOU 2877  CE1 PHE B 212     3421   3791   4198   -190    -43   -485       C  
ATOM   2878  CE2 PHE B 212      61.370  25.799  18.473  1.00 29.47           C  
ANISOU 2878  CE2 PHE B 212     3417   3680   4100   -187    -14   -416       C  
ATOM   2879  CZ  PHE B 212      62.733  26.047  18.452  1.00 32.95           C  
ANISOU 2879  CZ  PHE B 212     3826   4124   4570   -197     -6   -462       C  
ATOM   2880  N   LEU B 213      59.237  25.725  23.176  1.00 27.60           N  
ANISOU 2880  N   LEU B 213     3168   3570   3749   -159   -113   -391       N  
ATOM   2881  CA  LEU B 213      58.513  26.984  23.060  1.00 35.12           C  
ANISOU 2881  CA  LEU B 213     4137   4503   4703   -176    -78   -400       C  
ATOM   2882  C   LEU B 213      57.970  27.540  24.374  1.00 32.25           C  
ANISOU 2882  C   LEU B 213     3769   4172   4313   -179    -89   -410       C  
ATOM   2883  O   LEU B 213      57.524  26.799  25.243  1.00 35.68           O  
ANISOU 2883  O   LEU B 213     4204   4636   4716   -163   -124   -387       O  
ATOM   2884  CB  LEU B 213      57.339  26.813  22.088  1.00 38.64           C  
ANISOU 2884  CB  LEU B 213     4624   4916   5143   -172    -61   -354       C  
ATOM   2885  CG  LEU B 213      57.689  26.474  20.639  1.00 40.93           C  
ANISOU 2885  CG  LEU B 213     4924   5169   5457   -172    -41   -343       C  
ATOM   2886  CD1 LEU B 213      56.429  26.181  19.844  1.00 39.87           C  
ANISOU 2886  CD1 LEU B 213     4827   5011   5310   -164    -32   -297       C  
ATOM   2887  CD2 LEU B 213      58.471  27.600  19.996  1.00 33.13           C  
ANISOU 2887  CD2 LEU B 213     3928   4156   4503   -193      1   -383       C  
ATOM   2888  N   LYS B 214      57.997  28.862  24.490  1.00 34.90           N  
ANISOU 2888  N   LYS B 214     4100   4499   4662   -199    -56   -444       N  
ATOM   2889  CA  LYS B 214      57.225  29.572  25.505  1.00 38.46           C  
ANISOU 2889  CA  LYS B 214     4554   4970   5091   -205    -56   -450       C  
ATOM   2890  C   LYS B 214      56.026  30.199  24.800  1.00 37.94           C  
ANISOU 2890  C   LYS B 214     4524   4866   5026   -210    -22   -422       C  
ATOM   2891  O   LYS B 214      56.180  31.159  24.059  1.00 37.19           O  
ANISOU 2891  O   LYS B 214     4434   4738   4957   -226     19   -441       O  
ATOM   2892  CB  LYS B 214      58.065  30.672  26.156  1.00 39.06           C  
ANISOU 2892  CB  LYS B 214     4596   5061   5183   -224    -40   -512       C  
ATOM   2893  CG  LYS B 214      58.374  30.429  27.623  1.00 51.90           C  
ANISOU 2893  CG  LYS B 214     6195   6744   6782   -217    -78   -534       C  
ATOM   2894  CD  LYS B 214      59.638  29.608  27.808  1.00 61.94           C  
ANISOU 2894  CD  LYS B 214     7434   8042   8059   -207   -110   -553       C  
ATOM   2895  CE  LYS B 214      60.882  30.486  27.707  1.00 76.07           C  
ANISOU 2895  CE  LYS B 214     9188   9830   9884   -227    -86   -617       C  
ATOM   2896  NZ  LYS B 214      62.147  29.711  27.899  1.00 73.12           N  
ANISOU 2896  NZ  LYS B 214     8780   9485   9518   -216   -117   -639       N  
ATOM   2897  N   LEU B 215      54.835  29.655  25.012  1.00 28.52           N  
ANISOU 2897  N   LEU B 215     3356   3676   3803   -197    -39   -378       N  
ATOM   2898  CA  LEU B 215      53.663  30.125  24.269  1.00 32.76           C  
ANISOU 2898  CA  LEU B 215     3927   4179   4340   -199    -11   -349       C  
ATOM   2899  C   LEU B 215      52.868  31.194  25.008  1.00 28.81           C  
ANISOU 2899  C   LEU B 215     3432   3683   3829   -210      6   -360       C  
ATOM   2900  O   LEU B 215      52.427  30.975  26.128  1.00 33.33           O  
ANISOU 2900  O   LEU B 215     4001   4289   4375   -205    -20   -356       O  
ATOM   2901  CB  LEU B 215      52.751  28.948  23.921  1.00 23.03           C  
ANISOU 2901  CB  LEU B 215     2721   2944   3087   -179    -34   -295       C  
ATOM   2902  CG  LEU B 215      53.412  27.869  23.068  1.00 25.16           C  
ANISOU 2902  CG  LEU B 215     2988   3204   3368   -168    -47   -281       C  
ATOM   2903  CD1 LEU B 215      52.508  26.642  22.970  1.00 19.90           C  
ANISOU 2903  CD1 LEU B 215     2341   2540   2679   -149    -73   -232       C  
ATOM   2904  CD2 LEU B 215      53.717  28.413  21.688  1.00 18.84           C  
ANISOU 2904  CD2 LEU B 215     2199   2364   2598   -177     -9   -287       C  
ATOM   2905  N   PRO B 216      52.672  32.359  24.373  1.00 37.25           N  
ANISOU 2905  N   PRO B 216     4513   4719   4921   -224     50   -372       N  
ATOM   2906  CA  PRO B 216      51.873  33.398  25.030  1.00 34.00           C  
ANISOU 2906  CA  PRO B 216     4107   4308   4503   -235     69   -382       C  
ATOM   2907  C   PRO B 216      50.519  32.823  25.409  1.00 38.36           C  
ANISOU 2907  C   PRO B 216     4683   4871   5022   -221     47   -338       C  
ATOM   2908  O   PRO B 216      49.856  32.195  24.583  1.00 36.08           O  
ANISOU 2908  O   PRO B 216     4419   4563   4728   -208     43   -297       O  
ATOM   2909  CB  PRO B 216      51.719  34.467  23.947  1.00 34.36           C  
ANISOU 2909  CB  PRO B 216     4170   4308   4579   -246    120   -385       C  
ATOM   2910  CG  PRO B 216      52.870  34.249  23.025  1.00 45.81           C  
ANISOU 2910  CG  PRO B 216     5610   5741   6056   -248    131   -399       C  
ATOM   2911  CD  PRO B 216      53.135  32.769  23.038  1.00 38.69           C  
ANISOU 2911  CD  PRO B 216     4704   4861   5136   -230     86   -376       C  
ATOM   2912  N   ILE B 217      50.124  33.031  26.660  1.00 29.44           N  
ANISOU 2912  N   ILE B 217     3544   3772   3870   -224     32   -349       N  
ATOM   2913  CA  ILE B 217      48.918  32.433  27.192  1.00 28.50           C  
ANISOU 2913  CA  ILE B 217     3443   3667   3718   -211      9   -312       C  
ATOM   2914  C   ILE B 217      47.681  32.835  26.378  1.00 30.53           C  
ANISOU 2914  C   ILE B 217     3733   3888   3978   -209     34   -280       C  
ATOM   2915  O   ILE B 217      46.734  32.060  26.248  1.00 22.29           O  
ANISOU 2915  O   ILE B 217     2710   2844   2915   -195     17   -240       O  
ATOM   2916  CB  ILE B 217      48.752  32.793  28.684  1.00 31.66           C  
ANISOU 2916  CB  ILE B 217     3827   4105   4096   -218     -5   -335       C  
ATOM   2917  CG1 ILE B 217      47.567  32.050  29.295  1.00 31.51           C  
ANISOU 2917  CG1 ILE B 217     3827   4103   4042   -204    -31   -296       C  
ATOM   2918  CG2 ILE B 217      48.597  34.304  28.853  1.00 37.11           C  
ANISOU 2918  CG2 ILE B 217     4513   4781   4804   -239     34   -370       C  
ATOM   2919  CD1 ILE B 217      47.707  30.557  29.269  1.00 45.79           C  
ANISOU 2919  CD1 ILE B 217     5639   5927   5833   -184    -68   -263       C  
ATOM   2920  N   LYS B 218      47.700  34.038  25.816  1.00 28.98           N  
ANISOU 2920  N   LYS B 218     3542   3662   3808   -222     76   -298       N  
ATOM   2921  CA  LYS B 218      46.599  34.503  24.986  1.00 29.05           C  
ANISOU 2921  CA  LYS B 218     3581   3637   3822   -218    103   -269       C  
ATOM   2922  C   LYS B 218      46.362  33.639  23.736  1.00 31.74           C  
ANISOU 2922  C   LYS B 218     3942   3957   4163   -201     97   -230       C  
ATOM   2923  O   LYS B 218      45.249  33.567  23.219  1.00 34.33           O  
ANISOU 2923  O   LYS B 218     4295   4269   4481   -191    102   -196       O  
ATOM   2924  CB  LYS B 218      46.828  35.949  24.573  1.00 40.97           C  
ANISOU 2924  CB  LYS B 218     5089   5116   5362   -234    151   -296       C  
ATOM   2925  CG  LYS B 218      45.846  36.927  25.194  1.00 60.13           C  
ANISOU 2925  CG  LYS B 218     7523   7539   7784   -241    171   -300       C  
ATOM   2926  CD  LYS B 218      45.897  38.285  24.489  1.00 61.47           C  
ANISOU 2926  CD  LYS B 218     7699   7668   7987   -252    224   -315       C  
ATOM   2927  CE  LYS B 218      44.784  39.207  24.965  1.00 60.67           C  
ANISOU 2927  CE  LYS B 218     7609   7559   7884   -257    245   -313       C  
ATOM   2928  NZ  LYS B 218      44.817  40.505  24.230  1.00 78.34           N  
ANISOU 2928  NZ  LYS B 218     9855   9754  10155   -265    299   -323       N  
ATOM   2929  N   MET B 219      47.402  32.978  23.249  1.00 26.15           N  
ANISOU 2929  N   MET B 219     3222   3249   3464   -199     87   -236       N  
ATOM   2930  CA  MET B 219      47.233  32.113  22.087  1.00 27.60           C  
ANISOU 2930  CA  MET B 219     3424   3416   3648   -184     81   -202       C  
ATOM   2931  C   MET B 219      46.468  30.823  22.425  1.00 26.25           C  
ANISOU 2931  C   MET B 219     3260   3264   3448   -168     42   -167       C  
ATOM   2932  O   MET B 219      46.093  30.079  21.534  1.00 25.78           O  
ANISOU 2932  O   MET B 219     3217   3192   3387   -155     36   -138       O  
ATOM   2933  CB  MET B 219      48.586  31.778  21.457  1.00 21.19           C  
ANISOU 2933  CB  MET B 219     2597   2598   2858   -186     82   -220       C  
ATOM   2934  CG  MET B 219      49.323  32.997  20.898  1.00 27.68           C  
ANISOU 2934  CG  MET B 219     3413   3393   3712   -202    126   -251       C  
ATOM   2935  SD  MET B 219      50.738  32.504  19.889  1.00 41.14           S  
ANISOU 2935  SD  MET B 219     5105   5084   5441   -203    132   -265       S  
ATOM   2936  CE  MET B 219      49.951  32.375  18.279  1.00 32.83           C  
ANISOU 2936  CE  MET B 219     4089   3996   4389   -189    153   -222       C  
ATOM   2937  N   LEU B 220      46.232  30.567  23.710  1.00 27.61           N  
ANISOU 2937  N   LEU B 220     3423   3468   3600   -168     17   -171       N  
ATOM   2938  CA  LEU B 220      45.600  29.313  24.125  1.00 27.05           C  
ANISOU 2938  CA  LEU B 220     3358   3416   3504   -153    -18   -139       C  
ATOM   2939  C   LEU B 220      44.281  29.473  24.869  1.00 30.44           C  
ANISOU 2939  C   LEU B 220     3801   3854   3911   -151    -22   -123       C  
ATOM   2940  O   LEU B 220      43.382  28.641  24.745  1.00 26.43           O  
ANISOU 2940  O   LEU B 220     3309   3346   3389   -139    -37    -90       O  
ATOM   2941  CB  LEU B 220      46.581  28.503  24.974  1.00 21.80           C  
ANISOU 2941  CB  LEU B 220     2669   2783   2831   -150    -50   -152       C  
ATOM   2942  CG  LEU B 220      47.870  28.188  24.210  1.00 33.49           C  
ANISOU 2942  CG  LEU B 220     4135   4255   4335   -150    -49   -167       C  
ATOM   2943  CD1 LEU B 220      48.924  27.637  25.135  1.00 33.47           C  
ANISOU 2943  CD1 LEU B 220     4105   4286   4326   -148    -77   -187       C  
ATOM   2944  CD2 LEU B 220      47.581  27.226  23.065  1.00 19.20           C  
ANISOU 2944  CD2 LEU B 220     2342   2424   2529   -137    -53   -134       C  
ATOM   2945  N   MET B 221      44.170  30.533  25.658  1.00 32.65           N  
ANISOU 2945  N   MET B 221     4075   4142   4190   -164     -7   -148       N  
ATOM   2946  CA  MET B 221      43.041  30.679  26.574  1.00 40.06           C  
ANISOU 2946  CA  MET B 221     5021   5094   5105   -164    -13   -137       C  
ATOM   2947  C   MET B 221      41.692  30.900  25.894  1.00 40.43           C  
ANISOU 2947  C   MET B 221     5095   5116   5152   -158      3   -109       C  
ATOM   2948  O   MET B 221      41.411  31.991  25.409  1.00 38.52           O  
ANISOU 2948  O   MET B 221     4860   4850   4925   -165     34   -117       O  
ATOM   2949  CB  MET B 221      43.312  31.809  27.549  1.00 41.70           C  
ANISOU 2949  CB  MET B 221     5213   5316   5314   -181      0   -175       C  
ATOM   2950  CG  MET B 221      44.149  31.379  28.734  1.00 58.02           C  
ANISOU 2950  CG  MET B 221     7255   7424   7365   -183    -28   -197       C  
ATOM   2951  SD  MET B 221      43.740  32.395  30.167  1.00 90.41           S  
ANISOU 2951  SD  MET B 221    11347  11553  11453   -198    -21   -227       S  
ATOM   2952  CE  MET B 221      41.956  32.407  30.036  1.00 63.12           C  
ANISOU 2952  CE  MET B 221     7922   8078   7984   -192    -13   -188       C  
ATOM   2953  N   SER B 230      48.968  35.301  37.108  1.00 90.00           N  
ANISOU 2953  N   SER B 230    11092  11757  11348   -265    -75   -531       N  
ATOM   2954  CA  SER B 230      50.396  35.038  37.221  1.00 90.27           C  
ANISOU 2954  CA  SER B 230    11093  11818  11388   -263    -93   -566       C  
ATOM   2955  C   SER B 230      50.902  34.229  36.031  1.00 89.92           C  
ANISOU 2955  C   SER B 230    11058  11743  11364   -249    -98   -536       C  
ATOM   2956  O   SER B 230      52.081  34.293  35.684  1.00 90.05           O  
ANISOU 2956  O   SER B 230    11050  11761  11404   -253    -98   -568       O  
ATOM   2957  CB  SER B 230      50.707  34.302  38.524  1.00 80.66           C  
ANISOU 2957  CB  SER B 230     9857  10665  10125   -247   -138   -570       C  
ATOM   2958  OG  SER B 230      49.520  34.015  39.240  1.00 80.64           O  
ANISOU 2958  OG  SER B 230     9878  10677  10086   -239   -149   -536       O  
ATOM   2959  N   LEU B 231      50.006  33.469  35.412  1.00 93.00           N  
ANISOU 2959  N   LEU B 231    11482  12106  11747   -234   -103   -478       N  
ATOM   2960  CA  LEU B 231      50.357  32.669  34.245  1.00 92.83           C  
ANISOU 2960  CA  LEU B 231    11472  12054  11744   -222   -107   -447       C  
ATOM   2961  C   LEU B 231      50.434  33.540  32.997  1.00 92.53           C  
ANISOU 2961  C   LEU B 231    11443  11964  11750   -238    -63   -458       C  
ATOM   2962  O   LEU B 231      49.438  34.102  32.550  1.00 92.37           O  
ANISOU 2962  O   LEU B 231    11448  11911  11739   -244    -35   -440       O  
ATOM   2963  CB  LEU B 231      49.354  31.532  34.040  1.00 82.76           C  
ANISOU 2963  CB  LEU B 231    10229  10771  10445   -201   -127   -384       C  
ATOM   2964  CG  LEU B 231      49.922  30.118  34.172  1.00 83.07           C  
ANISOU 2964  CG  LEU B 231    10263  10833  10467   -177   -167   -359       C  
ATOM   2965  CD1 LEU B 231      48.977  29.097  33.563  1.00 82.92           C  
ANISOU 2965  CD1 LEU B 231    10277  10789  10440   -160   -174   -299       C  
ATOM   2966  CD2 LEU B 231      51.302  30.024  33.542  1.00 83.25           C  
ANISOU 2966  CD2 LEU B 231    10262  10852  10518   -178   -168   -386       C  
ATOM   2967  N   THR B 232      51.633  33.641  32.446  1.00 43.26           N  
ANISOU 2967  N   THR B 232     5182   5716   5539   -243    -56   -487       N  
ATOM   2968  CA  THR B 232      51.898  34.476  31.283  1.00 46.96           C  
ANISOU 2968  CA  THR B 232     5655   6136   6050   -258    -12   -501       C  
ATOM   2969  C   THR B 232      52.217  33.625  30.056  1.00 47.74           C  
ANISOU 2969  C   THR B 232     5769   6207   6164   -245    -16   -469       C  
ATOM   2970  O   THR B 232      51.905  33.999  28.929  1.00 42.40           O  
ANISOU 2970  O   THR B 232     5114   5486   5512   -249     17   -454       O  
ATOM   2971  CB  THR B 232      53.063  35.447  31.555  1.00 54.73           C  
ANISOU 2971  CB  THR B 232     6604   7130   7062   -279      8   -568       C  
ATOM   2972  OG1 THR B 232      53.246  36.310  30.430  1.00 57.43           O  
ANISOU 2972  OG1 THR B 232     6954   7422   7447   -294     56   -579       O  
ATOM   2973  CG2 THR B 232      54.345  34.680  31.813  1.00 61.94           C  
ANISOU 2973  CG2 THR B 232     7486   8076   7973   -270    -25   -589       C  
ATOM   2974  N   HIS B 233      52.835  32.475  30.296  1.00 51.88           N  
ANISOU 2974  N   HIS B 233     6281   6759   6673   -229    -55   -459       N  
ATOM   2975  CA  HIS B 233      53.255  31.563  29.236  1.00 45.41           C  
ANISOU 2975  CA  HIS B 233     5469   5917   5866   -216    -62   -432       C  
ATOM   2976  C   HIS B 233      53.023  30.090  29.576  1.00 45.34           C  
ANISOU 2976  C   HIS B 233     5467   5932   5827   -191   -106   -390       C  
ATOM   2977  O   HIS B 233      52.992  29.711  30.742  1.00 46.20           O  
ANISOU 2977  O   HIS B 233     5564   6083   5905   -182   -136   -392       O  
ATOM   2978  CB  HIS B 233      54.741  31.756  28.928  1.00 46.64           C  
ANISOU 2978  CB  HIS B 233     5594   6074   6052   -225    -56   -476       C  
ATOM   2979  CG  HIS B 233      55.078  33.101  28.367  1.00 57.06           C  
ANISOU 2979  CG  HIS B 233     6908   7362   7409   -249     -7   -515       C  
ATOM   2980  ND1 HIS B 233      55.250  34.217  29.161  1.00 62.10           N  
ANISOU 2980  ND1 HIS B 233     7526   8016   8054   -267     11   -563       N  
ATOM   2981  CD2 HIS B 233      55.278  33.510  27.092  1.00 53.68           C  
ANISOU 2981  CD2 HIS B 233     6493   6888   7016   -256     30   -513       C  
ATOM   2982  CE1 HIS B 233      55.540  35.256  28.396  1.00 57.70           C  
ANISOU 2982  CE1 HIS B 233     6969   7420   7535   -286     58   -588       C  
ATOM   2983  NE2 HIS B 233      55.560  34.854  27.137  1.00 58.11           N  
ANISOU 2983  NE2 HIS B 233     7041   7433   7603   -279     71   -557       N  
ATOM   2984  N   LEU B 234      52.873  29.265  28.542  1.00 33.52           N  
ANISOU 2984  N   LEU B 234     3989   4407   4338   -179   -108   -353       N  
ATOM   2985  CA  LEU B 234      52.869  27.811  28.692  1.00 32.47           C  
ANISOU 2985  CA  LEU B 234     3860   4291   4186   -156   -146   -317       C  
ATOM   2986  C   LEU B 234      54.026  27.229  27.887  1.00 30.31           C  
ANISOU 2986  C   LEU B 234     3571   4006   3937   -152   -150   -325       C  
ATOM   2987  O   LEU B 234      54.308  27.702  26.789  1.00 25.18           O  
ANISOU 2987  O   LEU B 234     2928   3322   3319   -163   -120   -335       O  
ATOM   2988  CB  LEU B 234      51.562  27.226  28.173  1.00 32.56           C  
ANISOU 2988  CB  LEU B 234     3907   4278   4185   -146   -144   -264       C  
ATOM   2989  CG  LEU B 234      50.526  26.784  29.201  1.00 44.14           C  
ANISOU 2989  CG  LEU B 234     5386   5770   5615   -135   -166   -236       C  
ATOM   2990  CD1 LEU B 234      49.810  27.998  29.737  1.00 45.06           C  
ANISOU 2990  CD1 LEU B 234     5509   5888   5726   -151   -144   -255       C  
ATOM   2991  CD2 LEU B 234      49.538  25.799  28.569  1.00 41.38           C  
ANISOU 2991  CD2 LEU B 234     5065   5397   5258   -121   -171   -185       C  
ATOM   2992  N   THR B 235      54.697  26.218  28.429  1.00 28.09           N  
ANISOU 2992  N   THR B 235     3273   3757   3645   -135   -187   -321       N  
ATOM   2993  CA  THR B 235      55.769  25.545  27.702  1.00 30.37           C  
ANISOU 2993  CA  THR B 235     3546   4036   3957   -129   -194   -326       C  
ATOM   2994  C   THR B 235      55.163  24.721  26.549  1.00 28.29           C  
ANISOU 2994  C   THR B 235     3312   3736   3702   -120   -188   -280       C  
ATOM   2995  O   THR B 235      54.099  24.129  26.694  1.00 24.01           O  
ANISOU 2995  O   THR B 235     2793   3191   3138   -108   -198   -240       O  
ATOM   2996  CB  THR B 235      56.624  24.653  28.643  1.00 32.82           C  
ANISOU 2996  CB  THR B 235     3828   4390   4251   -110   -236   -331       C  
ATOM   2997  OG1 THR B 235      57.730  24.107  27.918  1.00 36.78           O  
ANISOU 2997  OG1 THR B 235     4313   4881   4780   -106   -240   -342       O  
ATOM   2998  CG2 THR B 235      55.796  23.513  29.208  1.00 37.88           C  
ANISOU 2998  CG2 THR B 235     4487   5046   4859    -87   -265   -281       C  
ATOM   2999  N   GLY B 236      55.825  24.694  25.401  1.00 35.35           N  
ANISOU 2999  N   GLY B 236     4203   4600   4628   -125   -170   -289       N  
ATOM   3000  CA  GLY B 236      55.308  23.938  24.268  1.00 28.03           C  
ANISOU 3000  CA  GLY B 236     3300   3640   3708   -117   -164   -251       C  
ATOM   3001  C   GLY B 236      56.340  22.981  23.703  1.00 28.33           C  
ANISOU 3001  C   GLY B 236     3323   3675   3767   -108   -177   -252       C  
ATOM   3002  O   GLY B 236      57.510  23.339  23.562  1.00 31.95           O  
ANISOU 3002  O   GLY B 236     3757   4136   4248   -117   -171   -290       O  
ATOM   3003  N   HIS B 237      55.906  21.765  23.377  1.00 20.09           N  
ANISOU 3003  N   HIS B 237     2292   2624   2716    -91   -194   -212       N  
ATOM   3004  CA  HIS B 237      56.793  20.755  22.822  1.00 20.65           C  
ANISOU 3004  CA  HIS B 237     2350   2689   2806    -81   -206   -209       C  
ATOM   3005  C   HIS B 237      56.576  20.653  21.327  1.00 19.70           C  
ANISOU 3005  C   HIS B 237     2249   2529   2708    -88   -180   -197       C  
ATOM   3006  O   HIS B 237      55.430  20.665  20.863  1.00 19.82           O  
ANISOU 3006  O   HIS B 237     2292   2525   2712    -88   -168   -169       O  
ATOM   3007  CB  HIS B 237      56.532  19.406  23.493  1.00 18.48           C  
ANISOU 3007  CB  HIS B 237     2075   2434   2512    -58   -242   -173       C  
ATOM   3008  CG  HIS B 237      56.473  19.485  24.990  1.00 20.81           C  
ANISOU 3008  CG  HIS B 237     2359   2771   2778    -49   -267   -177       C  
ATOM   3009  ND1 HIS B 237      57.527  19.939  25.752  1.00 20.38           N  
ANISOU 3009  ND1 HIS B 237     2273   2747   2724    -51   -279   -215       N  
ATOM   3010  CD2 HIS B 237      55.488  19.164  25.864  1.00 23.24           C  
ANISOU 3010  CD2 HIS B 237     2680   3095   3053    -38   -282   -147       C  
ATOM   3011  CE1 HIS B 237      57.194  19.899  27.032  1.00 26.89           C  
ANISOU 3011  CE1 HIS B 237     3093   3607   3515    -41   -302   -209       C  
ATOM   3012  NE2 HIS B 237      55.962  19.429  27.126  1.00 24.72           N  
ANISOU 3012  NE2 HIS B 237     2847   3324   3221    -33   -303   -167       N  
ATOM   3013  N   PHE B 238      57.673  20.554  20.576  1.00 19.94           N  
ANISOU 3013  N   PHE B 238     2263   2546   2767    -93   -172   -219       N  
ATOM   3014  CA  PHE B 238      57.611  20.514  19.113  1.00 15.23           C  
ANISOU 3014  CA  PHE B 238     1683   1912   2192    -99   -145   -212       C  
ATOM   3015  C   PHE B 238      57.903  19.130  18.531  1.00 21.93           C  
ANISOU 3015  C   PHE B 238     2529   2753   3052    -85   -161   -191       C  
ATOM   3016  O   PHE B 238      58.896  18.473  18.873  1.00 24.64           O  
ANISOU 3016  O   PHE B 238     2846   3111   3406    -77   -181   -203       O  
ATOM   3017  CB  PHE B 238      58.561  21.557  18.501  1.00 16.38           C  
ANISOU 3017  CB  PHE B 238     1816   2042   2364   -118   -114   -254       C  
ATOM   3018  CG  PHE B 238      58.619  21.526  16.998  1.00 16.46           C  
ANISOU 3018  CG  PHE B 238     1842   2016   2395   -124    -85   -248       C  
ATOM   3019  CD1 PHE B 238      57.958  22.480  16.251  1.00 16.54           C  
ANISOU 3019  CD1 PHE B 238     1877   2001   2405   -135    -50   -245       C  
ATOM   3020  CD2 PHE B 238      59.330  20.522  16.329  1.00 20.24           C  
ANISOU 3020  CD2 PHE B 238     2310   2486   2893   -118    -93   -246       C  
ATOM   3021  CE1 PHE B 238      58.007  22.461  14.868  1.00 17.47           C  
ANISOU 3021  CE1 PHE B 238     2009   2089   2538   -139    -23   -239       C  
ATOM   3022  CE2 PHE B 238      59.369  20.488  14.939  1.00 17.91           C  
ANISOU 3022  CE2 PHE B 238     2029   2160   2614   -124    -66   -242       C  
ATOM   3023  CZ  PHE B 238      58.703  21.458  14.211  1.00 20.88           C  
ANISOU 3023  CZ  PHE B 238     2431   2514   2987   -134    -32   -238       C  
ATOM   3024  N   PHE B 239      57.029  18.696  17.631  1.00 17.84           N  
ANISOU 3024  N   PHE B 239     2035   2212   2531    -83   -150   -162       N  
ATOM   3025  CA  PHE B 239      57.155  17.404  16.975  1.00 18.68           C  
ANISOU 3025  CA  PHE B 239     2141   2307   2649    -71   -160   -141       C  
ATOM   3026  C   PHE B 239      56.851  17.586  15.510  1.00 17.67           C  
ANISOU 3026  C   PHE B 239     2033   2148   2534    -80   -131   -138       C  
ATOM   3027  O   PHE B 239      55.808  18.123  15.162  1.00 19.36           O  
ANISOU 3027  O   PHE B 239     2271   2351   2733    -84   -114   -124       O  
ATOM   3028  CB  PHE B 239      56.154  16.409  17.550  1.00 14.59           C  
ANISOU 3028  CB  PHE B 239     1635   1799   2110    -55   -184   -103       C  
ATOM   3029  CG  PHE B 239      56.254  16.235  19.033  1.00 21.43           C  
ANISOU 3029  CG  PHE B 239     2487   2697   2957    -44   -212   -100       C  
ATOM   3030  CD1 PHE B 239      55.392  16.903  19.881  1.00 16.79           C  
ANISOU 3030  CD1 PHE B 239     1912   2125   2343    -46   -214    -94       C  
ATOM   3031  CD2 PHE B 239      57.200  15.385  19.581  1.00 17.83           C  
ANISOU 3031  CD2 PHE B 239     2007   2259   2509    -30   -238   -103       C  
ATOM   3032  CE1 PHE B 239      55.474  16.725  21.257  1.00 18.53           C  
ANISOU 3032  CE1 PHE B 239     2120   2378   2543    -35   -240    -91       C  
ATOM   3033  CE2 PHE B 239      57.288  15.211  20.950  1.00 20.47           C  
ANISOU 3033  CE2 PHE B 239     2329   2627   2823    -18   -265    -98       C  
ATOM   3034  CZ  PHE B 239      56.428  15.890  21.790  1.00 18.11           C  
ANISOU 3034  CZ  PHE B 239     2042   2343   2495    -20   -266    -93       C  
ATOM   3035  N   GLY B 240      57.740  17.118  14.648  1.00 16.14           N  
ANISOU 3035  N   GLY B 240     1828   1940   2366    -82   -124   -150       N  
ATOM   3036  CA  GLY B 240      57.530  17.258  13.224  1.00 16.71           C  
ANISOU 3036  CA  GLY B 240     1918   1984   2448    -89    -95   -147       C  
ATOM   3037  C   GLY B 240      58.045  16.064  12.445  1.00 17.59           C  
ANISOU 3037  C   GLY B 240     2020   2084   2580    -83   -101   -143       C  
ATOM   3038  O   GLY B 240      59.067  15.472  12.794  1.00 18.92           O  
ANISOU 3038  O   GLY B 240     2163   2260   2766    -79   -118   -156       O  
ATOM   3039  N   VAL B 241      57.321  15.702  11.391  1.00 17.20           N  
ANISOU 3039  N   VAL B 241     1991   2017   2528    -82    -88   -124       N  
ATOM   3040  CA  VAL B 241      57.752  14.630  10.503  1.00 14.69           C  
ANISOU 3040  CA  VAL B 241     1666   1686   2230    -79    -89   -122       C  
ATOM   3041  C   VAL B 241      57.714  15.151   9.074  1.00 16.12           C  
ANISOU 3041  C   VAL B 241     1862   1845   2416    -89    -55   -130       C  
ATOM   3042  O   VAL B 241      56.718  15.749   8.655  1.00 14.10           O  
ANISOU 3042  O   VAL B 241     1631   1584   2141    -91    -40   -117       O  
ATOM   3043  CB  VAL B 241      56.849  13.384  10.596  1.00 16.88           C  
ANISOU 3043  CB  VAL B 241     1950   1966   2499    -65   -108    -91       C  
ATOM   3044  CG1 VAL B 241      57.272  12.380   9.537  1.00 14.15           C  
ANISOU 3044  CG1 VAL B 241     1597   1604   2176    -64   -103    -92       C  
ATOM   3045  CG2 VAL B 241      56.892  12.761  11.990  1.00 10.52           C  
ANISOU 3045  CG2 VAL B 241     1130   1181   1688    -52   -140    -78       C  
ATOM   3046  N   TYR B 242      58.793  14.916   8.332  1.00 15.58           N  
ANISOU 3046  N   TYR B 242     1781   1765   2375    -96    -44   -151       N  
ATOM   3047  CA  TYR B 242      58.939  15.424   6.970  1.00 15.62           C  
ANISOU 3047  CA  TYR B 242     1800   1750   2387   -106    -10   -161       C  
ATOM   3048  C   TYR B 242      59.222  14.294   5.967  1.00 19.75           C  
ANISOU 3048  C   TYR B 242     2318   2261   2926   -103     -9   -160       C  
ATOM   3049  O   TYR B 242      60.309  13.718   5.941  1.00 18.56           O  
ANISOU 3049  O   TYR B 242     2144   2108   2802   -105    -15   -177       O  
ATOM   3050  CB  TYR B 242      60.033  16.502   6.929  1.00 17.69           C  
ANISOU 3050  CB  TYR B 242     2052   2004   2665   -120     13   -194       C  
ATOM   3051  CG  TYR B 242      59.906  17.441   8.104  1.00 17.17           C  
ANISOU 3051  CG  TYR B 242     1983   1952   2587   -122      8   -201       C  
ATOM   3052  CD1 TYR B 242      58.884  18.400   8.148  1.00 15.12           C  
ANISOU 3052  CD1 TYR B 242     1749   1692   2305   -123     22   -187       C  
ATOM   3053  CD2 TYR B 242      60.755  17.333   9.201  1.00 19.54           C  
ANISOU 3053  CD2 TYR B 242     2255   2269   2900   -122    -14   -220       C  
ATOM   3054  CE1 TYR B 242      58.733  19.243   9.258  1.00 18.10           C  
ANISOU 3054  CE1 TYR B 242     2123   2082   2672   -126     18   -194       C  
ATOM   3055  CE2 TYR B 242      60.616  18.178  10.307  1.00 18.91           C  
ANISOU 3055  CE2 TYR B 242     2172   2206   2808   -124    -20   -228       C  
ATOM   3056  CZ  TYR B 242      59.607  19.125  10.324  1.00 22.72           C  
ANISOU 3056  CZ  TYR B 242     2680   2686   3269   -127     -3   -216       C  
ATOM   3057  OH  TYR B 242      59.473  19.949  11.409  1.00 19.62           O  
ANISOU 3057  OH  TYR B 242     2282   2308   2865   -131     -8   -225       O  
ATOM   3058  N   ASP B 243      58.228  14.006   5.135  1.00 17.34           N  
ANISOU 3058  N   ASP B 243     2034   1951   2605    -99     -1   -141       N  
ATOM   3059  CA  ASP B 243      58.285  12.927   4.154  1.00 21.54           C  
ANISOU 3059  CA  ASP B 243     2562   2473   3148    -97      0   -138       C  
ATOM   3060  C   ASP B 243      58.748  13.475   2.800  1.00 18.18           C  
ANISOU 3060  C   ASP B 243     2146   2032   2729   -107     35   -155       C  
ATOM   3061  O   ASP B 243      57.969  14.054   2.042  1.00 21.73           O  
ANISOU 3061  O   ASP B 243     2621   2479   3157   -107     54   -145       O  
ATOM   3062  CB  ASP B 243      56.896  12.296   4.017  1.00 19.10           C  
ANISOU 3062  CB  ASP B 243     2269   2171   2819    -87    -11   -111       C  
ATOM   3063  CG  ASP B 243      56.884  11.060   3.117  1.00 21.84           C  
ANISOU 3063  CG  ASP B 243     2608   2510   3179    -84    -11   -110       C  
ATOM   3064  OD1 ASP B 243      57.886  10.827   2.413  1.00 23.49           O  
ANISOU 3064  OD1 ASP B 243     2807   2709   3411    -91      1   -130       O  
ATOM   3065  OD2 ASP B 243      55.855  10.338   3.108  1.00 16.60           O  
ANISOU 3065  OD2 ASP B 243     1951   1851   2504    -76    -23    -92       O  
ATOM   3066  N   GLY B 244      60.022  13.300   2.489  1.00 17.29           N  
ANISOU 3066  N   GLY B 244     2015   1910   2646   -115     43   -179       N  
ATOM   3067  CA  GLY B 244      60.566  13.903   1.283  1.00 21.23           C  
ANISOU 3067  CA  GLY B 244     2523   2392   3151   -126     79   -197       C  
ATOM   3068  C   GLY B 244      60.203  13.130   0.028  1.00 19.59           C  
ANISOU 3068  C   GLY B 244     2324   2179   2941   -124     88   -191       C  
ATOM   3069  O   GLY B 244      59.916  11.934   0.082  1.00 20.79           O  
ANISOU 3069  O   GLY B 244     2466   2336   3098   -117     67   -182       O  
ATOM   3070  N   HIS B 245      60.190  13.823  -1.103  1.00 20.86           N  
ANISOU 3070  N   HIS B 245     2504   2330   3091   -129    121   -195       N  
ATOM   3071  CA  HIS B 245      60.068  13.160  -2.391  1.00 22.23           C  
ANISOU 3071  CA  HIS B 245     2684   2499   3264   -129    133   -196       C  
ATOM   3072  C   HIS B 245      60.931  13.858  -3.436  1.00 25.34           C  
ANISOU 3072  C   HIS B 245     3084   2876   3666   -140    172   -216       C  
ATOM   3073  O   HIS B 245      61.115  15.079  -3.399  1.00 22.60           O  
ANISOU 3073  O   HIS B 245     2752   2523   3314   -144    195   -220       O  
ATOM   3074  CB  HIS B 245      58.617  13.106  -2.862  1.00 20.76           C  
ANISOU 3074  CB  HIS B 245     2522   2324   3043   -117    131   -172       C  
ATOM   3075  CG  HIS B 245      57.912  14.424  -2.792  1.00 25.24           C  
ANISOU 3075  CG  HIS B 245     3115   2894   3581   -114    146   -158       C  
ATOM   3076  ND1 HIS B 245      57.043  14.752  -1.772  1.00 29.22           N  
ANISOU 3076  ND1 HIS B 245     3626   3409   4069   -106    127   -140       N  
ATOM   3077  CD2 HIS B 245      57.939  15.495  -3.621  1.00 26.92           C  
ANISOU 3077  CD2 HIS B 245     3350   3098   3779   -115    181   -159       C  
ATOM   3078  CE1 HIS B 245      56.574  15.974  -1.971  1.00 23.06           C  
ANISOU 3078  CE1 HIS B 245     2869   2627   3266   -104    149   -132       C  
ATOM   3079  NE2 HIS B 245      57.106  16.445  -3.085  1.00 28.58           N  
ANISOU 3079  NE2 HIS B 245     3578   3313   3966   -109    182   -142       N  
ATOM   3080  N   GLY B 246      61.451  13.064  -4.370  1.00 23.11           N  
ANISOU 3080  N   GLY B 246     2793   2588   3399   -144    180   -229       N  
ATOM   3081  CA  GLY B 246      62.273  13.569  -5.447  1.00 22.06           C  
ANISOU 3081  CA  GLY B 246     2667   2439   3275   -154    218   -248       C  
ATOM   3082  C   GLY B 246      63.716  13.778  -5.007  1.00 21.96           C  
ANISOU 3082  C   GLY B 246     2630   2413   3300   -168    225   -277       C  
ATOM   3083  O   GLY B 246      64.560  14.126  -5.820  1.00 28.83           O  
ANISOU 3083  O   GLY B 246     3501   3268   4184   -178    257   -297       O  
ATOM   3084  N   GLY B 247      63.990  13.559  -3.722  1.00 21.12           N  
ANISOU 3084  N   GLY B 247     2502   2313   3210   -166    196   -280       N  
ATOM   3085  CA  GLY B 247      65.289  13.850  -3.138  1.00 24.19           C  
ANISOU 3085  CA  GLY B 247     2866   2694   3633   -177    199   -308       C  
ATOM   3086  C   GLY B 247      65.140  13.975  -1.633  1.00 32.62           C  
ANISOU 3086  C   GLY B 247     3920   3776   4700   -171    168   -302       C  
ATOM   3087  O   GLY B 247      64.032  13.870  -1.107  1.00 29.01           O  
ANISOU 3087  O   GLY B 247     3476   3332   4216   -159    147   -275       O  
ATOM   3088  N   HIS B 248      66.248  14.207  -0.942  1.00 24.63           N  
ANISOU 3088  N   HIS B 248     2881   2761   3715   -178    164   -328       N  
ATOM   3089  CA  HIS B 248      66.251  14.218   0.508  1.00 27.30           C  
ANISOU 3089  CA  HIS B 248     3203   3116   4054   -172    132   -326       C  
ATOM   3090  C   HIS B 248      66.483  15.610   1.091  1.00 28.69           C  
ANISOU 3090  C   HIS B 248     3382   3292   4227   -180    148   -341       C  
ATOM   3091  O   HIS B 248      66.332  15.805   2.296  1.00 24.65           O  
ANISOU 3091  O   HIS B 248     2860   2797   3709   -175    124   -338       O  
ATOM   3092  CB  HIS B 248      67.326  13.261   1.033  1.00 31.60           C  
ANISOU 3092  CB  HIS B 248     3710   3665   4633   -170    108   -345       C  
ATOM   3093  CG  HIS B 248      68.724  13.672   0.682  1.00 38.56           C  
ANISOU 3093  CG  HIS B 248     4571   4532   5548   -185    131   -384       C  
ATOM   3094  ND1 HIS B 248      69.497  14.473   1.497  1.00 35.53           N  
ANISOU 3094  ND1 HIS B 248     4168   4153   5178   -192    132   -411       N  
ATOM   3095  CD2 HIS B 248      69.487  13.397  -0.406  1.00 35.95           C  
ANISOU 3095  CD2 HIS B 248     4235   4183   5241   -195    156   -404       C  
ATOM   3096  CE1 HIS B 248      70.677  14.665   0.935  1.00 37.92           C  
ANISOU 3096  CE1 HIS B 248     4454   4440   5513   -206    157   -445       C  
ATOM   3097  NE2 HIS B 248      70.692  14.028  -0.223  1.00 36.78           N  
ANISOU 3097  NE2 HIS B 248     4319   4281   5374   -208    172   -441       N  
ATOM   3098  N   LYS B 249      66.858  16.573   0.252  1.00 24.82           N  
ANISOU 3098  N   LYS B 249     2905   2782   3742   -193    191   -356       N  
ATOM   3099  CA  LYS B 249      67.371  17.841   0.776  1.00 26.67           C  
ANISOU 3099  CA  LYS B 249     3135   3013   3986   -205    211   -379       C  
ATOM   3100  C   LYS B 249      66.312  18.757   1.385  1.00 21.41           C  
ANISOU 3100  C   LYS B 249     2491   2354   3289   -200    211   -359       C  
ATOM   3101  O   LYS B 249      66.602  19.510   2.321  1.00 23.23           O  
ANISOU 3101  O   LYS B 249     2710   2592   3526   -205    210   -376       O  
ATOM   3102  CB  LYS B 249      68.196  18.585  -0.268  1.00 25.91           C  
ANISOU 3102  CB  LYS B 249     3044   2890   3909   -221    261   -404       C  
ATOM   3103  CG  LYS B 249      69.604  18.008  -0.455  1.00 30.99           C  
ANISOU 3103  CG  LYS B 249     3655   3527   4594   -230    262   -440       C  
ATOM   3104  CD  LYS B 249      70.357  18.775  -1.551  1.00 38.49           C  
ANISOU 3104  CD  LYS B 249     4613   4448   5562   -247    315   -464       C  
ATOM   3105  CE  LYS B 249      71.686  18.111  -1.892  1.00 52.75           C  
ANISOU 3105  CE  LYS B 249     6388   6245   7408   -257    318   -498       C  
ATOM   3106  NZ  LYS B 249      72.548  17.961  -0.681  1.00 58.85           N  
ANISOU 3106  NZ  LYS B 249     7120   7032   8208   -258    289   -527       N  
ATOM   3107  N   VAL B 250      65.088  18.688   0.868  1.00 23.70           N  
ANISOU 3107  N   VAL B 250     2812   2646   3547   -190    213   -325       N  
ATOM   3108  CA  VAL B 250      64.006  19.501   1.405  1.00 16.76           C  
ANISOU 3108  CA  VAL B 250     1955   1775   2639   -184    212   -303       C  
ATOM   3109  C   VAL B 250      63.558  19.023   2.775  1.00 21.54           C  
ANISOU 3109  C   VAL B 250     2546   2405   3235   -175    168   -293       C  
ATOM   3110  O   VAL B 250      63.393  19.836   3.682  1.00 22.79           O  
ANISOU 3110  O   VAL B 250     2702   2570   3387   -177    166   -298       O  
ATOM   3111  CB  VAL B 250      62.849  19.632   0.424  1.00 19.67           C  
ANISOU 3111  CB  VAL B 250     2359   2138   2977   -175    228   -272       C  
ATOM   3112  CG1 VAL B 250      61.679  20.386   1.066  1.00 14.23           C  
ANISOU 3112  CG1 VAL B 250     1690   1458   2258   -168    223   -249       C  
ATOM   3113  CG2 VAL B 250      63.343  20.364  -0.823  1.00 16.62           C  
ANISOU 3113  CG2 VAL B 250     1989   1727   2597   -184    277   -283       C  
ATOM   3114  N   ALA B 251      63.386  17.713   2.936  1.00 21.20           N  
ANISOU 3114  N   ALA B 251     2491   2374   3191   -164    134   -280       N  
ATOM   3115  CA  ALA B 251      63.070  17.140   4.246  1.00 23.35           C  
ANISOU 3115  CA  ALA B 251     2748   2668   3455   -153     92   -269       C  
ATOM   3116  C   ALA B 251      64.127  17.464   5.291  1.00 27.35           C  
ANISOU 3116  C   ALA B 251     3225   3185   3983   -159     81   -299       C  
ATOM   3117  O   ALA B 251      63.793  17.827   6.432  1.00 27.26           O  
ANISOU 3117  O   ALA B 251     3208   3191   3958   -156     63   -296       O  
ATOM   3118  CB  ALA B 251      62.884  15.619   4.157  1.00 18.19           C  
ANISOU 3118  CB  ALA B 251     2086   2022   2805   -141     63   -252       C  
ATOM   3119  N   ASP B 252      65.397  17.305   4.917  1.00 24.32           N  
ANISOU 3119  N   ASP B 252     2818   2791   3631   -168     92   -330       N  
ATOM   3120  CA  ASP B 252      66.496  17.609   5.831  1.00 26.82           C  
ANISOU 3120  CA  ASP B 252     3102   3119   3971   -174     83   -364       C  
ATOM   3121  C   ASP B 252      66.510  19.081   6.235  1.00 21.30           C  
ANISOU 3121  C   ASP B 252     2408   2418   3268   -187    107   -382       C  
ATOM   3122  O   ASP B 252      66.804  19.413   7.388  1.00 26.12           O  
ANISOU 3122  O   ASP B 252     2998   3047   3879   -187     89   -399       O  
ATOM   3123  CB  ASP B 252      67.855  17.236   5.222  1.00 26.09           C  
ANISOU 3123  CB  ASP B 252     2984   3013   3915   -183     94   -396       C  
ATOM   3124  CG  ASP B 252      68.015  15.743   5.018  1.00 35.82           C  
ANISOU 3124  CG  ASP B 252     4204   4249   5158   -171     67   -383       C  
ATOM   3125  OD1 ASP B 252      67.289  14.956   5.664  1.00 36.77           O  
ANISOU 3125  OD1 ASP B 252     4326   4386   5260   -155     34   -354       O  
ATOM   3126  OD2 ASP B 252      68.876  15.353   4.208  1.00 46.82           O  
ANISOU 3126  OD2 ASP B 252     5585   5626   6578   -178     82   -402       O  
ATOM   3127  N   TYR B 253      66.222  19.968   5.286  1.00 18.56           N  
ANISOU 3127  N   TYR B 253     2087   2047   2917   -197    149   -381       N  
ATOM   3128  CA  TYR B 253      66.180  21.392   5.607  1.00 22.93           C  
ANISOU 3128  CA  TYR B 253     2648   2595   3470   -208    177   -397       C  
ATOM   3129  C   TYR B 253      65.053  21.671   6.619  1.00 22.92           C  
ANISOU 3129  C   TYR B 253     2659   2614   3437   -199    155   -373       C  
ATOM   3130  O   TYR B 253      65.234  22.434   7.567  1.00 24.00           O  
ANISOU 3130  O   TYR B 253     2782   2761   3575   -205    153   -393       O  
ATOM   3131  CB  TYR B 253      66.017  22.242   4.344  1.00 17.75           C  
ANISOU 3131  CB  TYR B 253     2022   1909   2815   -217    229   -394       C  
ATOM   3132  CG  TYR B 253      66.200  23.726   4.599  1.00 25.78           C  
ANISOU 3132  CG  TYR B 253     3042   2913   3840   -231    265   -416       C  
ATOM   3133  CD1 TYR B 253      67.474  24.275   4.782  1.00 27.79           C  
ANISOU 3133  CD1 TYR B 253     3270   3160   4131   -248    286   -462       C  
ATOM   3134  CD2 TYR B 253      65.105  24.584   4.642  1.00 18.38           C  
ANISOU 3134  CD2 TYR B 253     2135   1972   2878   -228    281   -392       C  
ATOM   3135  CE1 TYR B 253      67.635  25.634   5.015  1.00 31.40           C  
ANISOU 3135  CE1 TYR B 253     3728   3603   4598   -262    322   -484       C  
ATOM   3136  CE2 TYR B 253      65.260  25.928   4.874  1.00 24.03           C  
ANISOU 3136  CE2 TYR B 253     2853   2673   3603   -241    316   -412       C  
ATOM   3137  CZ  TYR B 253      66.522  26.452   5.059  1.00 28.93           C  
ANISOU 3137  CZ  TYR B 253     3447   3285   4261   -258    338   -458       C  
ATOM   3138  OH  TYR B 253      66.656  27.804   5.287  1.00 36.69           O  
ANISOU 3138  OH  TYR B 253     4432   4253   5257   -272    377   -479       O  
ATOM   3139  N   CYS B 254      63.904  21.027   6.423  1.00 20.77           N  
ANISOU 3139  N   CYS B 254     2409   2347   3137   -184    137   -333       N  
ATOM   3140  CA  CYS B 254      62.776  21.165   7.344  1.00 22.34           C  
ANISOU 3140  CA  CYS B 254     2619   2565   3305   -175    115   -309       C  
ATOM   3141  C   CYS B 254      63.162  20.725   8.760  1.00 25.39           C  
ANISOU 3141  C   CYS B 254     2975   2979   3692   -169     75   -320       C  
ATOM   3142  O   CYS B 254      62.903  21.431   9.740  1.00 27.50           O  
ANISOU 3142  O   CYS B 254     3239   3261   3949   -172     69   -326       O  
ATOM   3143  CB  CYS B 254      61.574  20.342   6.847  1.00 19.80           C  
ANISOU 3143  CB  CYS B 254     2321   2244   2958   -160    100   -267       C  
ATOM   3144  SG  CYS B 254      60.718  21.055   5.420  1.00 21.16           S  
ANISOU 3144  SG  CYS B 254     2533   2391   3113   -161    142   -247       S  
ATOM   3145  N   ARG B 255      63.776  19.550   8.851  1.00 21.83           N  
ANISOU 3145  N   ARG B 255     2503   2537   3255   -162     48   -322       N  
ATOM   3146  CA  ARG B 255      64.262  19.028  10.114  1.00 23.48           C  
ANISOU 3146  CA  ARG B 255     2682   2775   3466   -154     10   -331       C  
ATOM   3147  C   ARG B 255      65.164  20.027  10.846  1.00 21.68           C  
ANISOU 3147  C   ARG B 255     2429   2555   3252   -166     18   -374       C  
ATOM   3148  O   ARG B 255      65.065  20.172  12.060  1.00 28.61           O  
ANISOU 3148  O   ARG B 255     3294   3460   4117   -161     -7   -378       O  
ATOM   3149  CB  ARG B 255      65.033  17.727   9.887  1.00 23.10           C  
ANISOU 3149  CB  ARG B 255     2612   2728   3438   -145    -12   -333       C  
ATOM   3150  CG  ARG B 255      65.872  17.295  11.099  1.00 26.87           C  
ANISOU 3150  CG  ARG B 255     3053   3233   3923   -136    -47   -351       C  
ATOM   3151  CD  ARG B 255      66.769  16.111  10.790  1.00 24.69           C  
ANISOU 3151  CD  ARG B 255     2754   2955   3673   -129    -63   -356       C  
ATOM   3152  NE  ARG B 255      67.736  16.402   9.739  1.00 33.68           N  
ANISOU 3152  NE  ARG B 255     3884   4069   4843   -144    -31   -387       N  
ATOM   3153  CZ  ARG B 255      68.246  15.478   8.935  1.00 38.32           C  
ANISOU 3153  CZ  ARG B 255     4464   4643   5453   -142    -30   -387       C  
ATOM   3154  NH1 ARG B 255      67.852  14.215   9.049  1.00 39.60           N  
ANISOU 3154  NH1 ARG B 255     4627   4811   5610   -125    -58   -356       N  
ATOM   3155  NH2 ARG B 255      69.136  15.818   8.011  1.00 36.51           N  
ANISOU 3155  NH2 ARG B 255     4228   4393   5253   -157      1   -417       N  
ATOM   3156  N   ASP B 256      66.043  20.703  10.109  1.00 28.69           N  
ANISOU 3156  N   ASP B 256     3311   3422   4168   -183     53   -406       N  
ATOM   3157  CA  ASP B 256      66.992  21.650  10.710  1.00 28.72           C  
ANISOU 3157  CA  ASP B 256     3288   3432   4192   -197     66   -452       C  
ATOM   3158  C   ASP B 256      66.375  23.011  11.071  1.00 27.71           C  
ANISOU 3158  C   ASP B 256     3176   3301   4051   -208     91   -458       C  
ATOM   3159  O   ASP B 256      66.705  23.601  12.096  1.00 30.66           O  
ANISOU 3159  O   ASP B 256     3528   3695   4427   -213     83   -486       O  
ATOM   3160  CB  ASP B 256      68.175  21.889   9.770  1.00 24.74           C  
ANISOU 3160  CB  ASP B 256     2770   2903   3726   -212     99   -487       C  
ATOM   3161  CG  ASP B 256      69.034  20.653   9.575  1.00 35.54           C  
ANISOU 3161  CG  ASP B 256     4114   4277   5114   -204     74   -493       C  
ATOM   3162  OD1 ASP B 256      69.620  20.519   8.474  1.00 34.25           O  
ANISOU 3162  OD1 ASP B 256     3952   4088   4974   -213    101   -504       O  
ATOM   3163  OD2 ASP B 256      69.115  19.817  10.507  1.00 42.04           O  
ANISOU 3163  OD2 ASP B 256     4917   5128   5928   -188     30   -486       O  
ATOM   3164  N   ARG B 257      65.480  23.496  10.217  1.00 17.98           N  
ANISOU 3164  N   ARG B 257     1980   2044   2806   -210    121   -432       N  
ATOM   3165  CA  ARG B 257      65.097  24.901  10.218  1.00 20.98           C  
ANISOU 3165  CA  ARG B 257     2376   2411   3185   -223    158   -442       C  
ATOM   3166  C   ARG B 257      63.663  25.190  10.722  1.00 25.98           C  
ANISOU 3166  C   ARG B 257     3036   3054   3783   -214    148   -407       C  
ATOM   3167  O   ARG B 257      63.412  26.228  11.342  1.00 22.28           O  
ANISOU 3167  O   ARG B 257     2567   2587   3310   -222    162   -420       O  
ATOM   3168  CB  ARG B 257      65.273  25.451   8.793  1.00 21.39           C  
ANISOU 3168  CB  ARG B 257     2449   2424   3253   -233    208   -443       C  
ATOM   3169  CG  ARG B 257      64.699  26.847   8.550  1.00 26.77           C  
ANISOU 3169  CG  ARG B 257     3156   3084   3931   -243    253   -441       C  
ATOM   3170  CD  ARG B 257      65.596  27.958   9.134  1.00 27.53           C  
ANISOU 3170  CD  ARG B 257     3227   3176   4056   -262    279   -491       C  
ATOM   3171  NE  ARG B 257      65.042  29.287   8.847  1.00 29.78           N  
ANISOU 3171  NE  ARG B 257     3537   3436   4340   -271    325   -488       N  
ATOM   3172  CZ  ARG B 257      64.787  30.212   9.767  1.00 28.72           C  
ANISOU 3172  CZ  ARG B 257     3397   3311   4206   -279    332   -504       C  
ATOM   3173  NH1 ARG B 257      65.043  29.969  11.052  1.00 23.56           N  
ANISOU 3173  NH1 ARG B 257     2712   2691   3548   -279    294   -526       N  
ATOM   3174  NH2 ARG B 257      64.285  31.378   9.401  1.00 25.43           N  
ANISOU 3174  NH2 ARG B 257     3004   2867   3791   -285    377   -499       N  
ATOM   3175  N  ALEU B 258      62.733  24.280  10.460  0.54 19.38           N  
ANISOU 3175  N  ALEU B 258     2219   2222   2921   -198    125   -365       N  
ATOM   3176  N  BLEU B 258      62.724  24.306  10.400  0.46 19.40           N  
ANISOU 3176  N  BLEU B 258     2223   2223   2924   -198    127   -364       N  
ATOM   3177  CA ALEU B 258      61.302  24.593  10.608  0.54 19.41           C  
ANISOU 3177  CA ALEU B 258     2254   2228   2894   -190    124   -330       C  
ATOM   3178  CA BLEU B 258      61.305  24.600  10.592  0.46 19.41           C  
ANISOU 3178  CA BLEU B 258     2253   2227   2894   -190    125   -330       C  
ATOM   3179  C  ALEU B 258      60.893  25.066  11.990  0.54 20.23           C  
ANISOU 3179  C  ALEU B 258     2348   2356   2982   -190    106   -336       C  
ATOM   3180  C  BLEU B 258      60.908  25.073  11.987  0.46 20.23           C  
ANISOU 3180  C  BLEU B 258     2348   2356   2983   -190    106   -336       C  
ATOM   3181  O  ALEU B 258      60.196  26.079  12.125  0.54 23.62           O  
ANISOU 3181  O  ALEU B 258     2794   2778   3401   -195    127   -332       O  
ATOM   3182  O  BLEU B 258      60.236  26.090  12.125  0.46 23.65           O  
ANISOU 3182  O  BLEU B 258     2797   2781   3406   -195    128   -333       O  
ATOM   3183  CB ALEU B 258      60.424  23.411  10.179  0.54 18.46           C  
ANISOU 3183  CB ALEU B 258     2151   2111   2752   -172     99   -288       C  
ATOM   3184  CB BLEU B 258      60.419  23.431  10.163  0.46 18.44           C  
ANISOU 3184  CB BLEU B 258     2148   2108   2749   -172    100   -288       C  
ATOM   3185  CG ALEU B 258      58.911  23.610   9.966  0.54 25.70           C  
ANISOU 3185  CG ALEU B 258     3101   3025   3639   -163    103   -250       C  
ATOM   3186  CG BLEU B 258      58.964  23.849   9.927  0.46 25.72           C  
ANISOU 3186  CG BLEU B 258     3105   3025   3644   -165    110   -254       C  
ATOM   3187  CD1ALEU B 258      58.154  23.775  11.267  0.54 20.88           C  
ANISOU 3187  CD1ALEU B 258     2490   2439   3007   -158     78   -241       C  
ATOM   3188  CD1BLEU B 258      58.291  22.969   8.897  0.46 19.42           C  
ANISOU 3188  CD1BLEU B 258     2328   2219   2834   -153    105   -222       C  
ATOM   3189  CD2ALEU B 258      58.649  24.793   9.065  0.54 28.20           C  
ANISOU 3189  CD2ALEU B 258     3442   3315   3958   -171    149   -250       C  
ATOM   3190  CD2BLEU B 258      58.183  23.856  11.226  0.46 29.21           C  
ANISOU 3190  CD2BLEU B 258     3545   3492   4063   -159     81   -243       C  
ATOM   3191  N   HIS B 259      61.305  24.338  13.019  1.00 18.10           N  
ANISOU 3191  N   HIS B 259     2052   2116   2709   -183     66   -344       N  
ATOM   3192  CA  HIS B 259      60.915  24.718  14.364  1.00 20.02           C  
ANISOU 3192  CA  HIS B 259     2287   2387   2934   -182     46   -349       C  
ATOM   3193  C   HIS B 259      61.483  26.080  14.754  1.00 26.53           C  
ANISOU 3193  C   HIS B 259     3096   3207   3775   -201     75   -392       C  
ATOM   3194  O   HIS B 259      60.828  26.831  15.473  1.00 25.47           O  
ANISOU 3194  O   HIS B 259     2969   3083   3627   -204     78   -392       O  
ATOM   3195  CB  HIS B 259      61.268  23.636  15.398  1.00 22.03           C  
ANISOU 3195  CB  HIS B 259     2516   2676   3179   -168     -3   -348       C  
ATOM   3196  CG  HIS B 259      62.695  23.181  15.345  1.00 22.98           C  
ANISOU 3196  CG  HIS B 259     2603   2802   3327   -170    -12   -380       C  
ATOM   3197  ND1 HIS B 259      63.255  22.628  14.215  1.00 21.18           N  
ANISOU 3197  ND1 HIS B 259     2376   2551   3121   -171      1   -379       N  
ATOM   3198  CD2 HIS B 259      63.663  23.166  16.293  1.00 26.17           C  
ANISOU 3198  CD2 HIS B 259     2971   3233   3740   -171    -32   -414       C  
ATOM   3199  CE1 HIS B 259      64.515  22.311  14.462  1.00 31.05           C  
ANISOU 3199  CE1 HIS B 259     3591   3812   4394   -173    -11   -411       C  
ATOM   3200  NE2 HIS B 259      64.786  22.620  15.718  1.00 24.18           N  
ANISOU 3200  NE2 HIS B 259     2698   2973   3516   -172    -32   -433       N  
ATOM   3201  N   PHE B 260      62.681  26.412  14.267  1.00 17.06           N  
ANISOU 3201  N   PHE B 260     1878   1994   2610   -214     98   -429       N  
ATOM   3202  CA  PHE B 260      63.236  27.733  14.548  1.00 25.42           C  
ANISOU 3202  CA  PHE B 260     2924   3046   3690   -234    132   -472       C  
ATOM   3203  C   PHE B 260      62.457  28.829  13.827  1.00 26.74           C  
ANISOU 3203  C   PHE B 260     3124   3180   3856   -242    179   -459       C  
ATOM   3204  O   PHE B 260      62.254  29.896  14.383  1.00 23.44           O  
ANISOU 3204  O   PHE B 260     2705   2762   3441   -253    198   -477       O  
ATOM   3205  CB  PHE B 260      64.737  27.818  14.223  1.00 25.78           C  
ANISOU 3205  CB  PHE B 260     2938   3084   3773   -247    147   -518       C  
ATOM   3206  CG  PHE B 260      65.615  27.092  15.220  1.00 21.20           C  
ANISOU 3206  CG  PHE B 260     2318   2542   3196   -241    103   -544       C  
ATOM   3207  CD1 PHE B 260      65.679  27.511  16.539  1.00 24.57           C  
ANISOU 3207  CD1 PHE B 260     2721   3001   3612   -243     84   -569       C  
ATOM   3208  CD2 PHE B 260      66.364  25.995  14.837  1.00 21.76           C  
ANISOU 3208  CD2 PHE B 260     2373   2615   3278   -232     82   -543       C  
ATOM   3209  CE1 PHE B 260      66.474  26.844  17.467  1.00 30.52           C  
ANISOU 3209  CE1 PHE B 260     3438   3793   4365   -234     42   -591       C  
ATOM   3210  CE2 PHE B 260      67.167  25.320  15.756  1.00 27.10           C  
ANISOU 3210  CE2 PHE B 260     3013   3328   3957   -223     42   -564       C  
ATOM   3211  CZ  PHE B 260      67.220  25.739  17.074  1.00 26.13           C  
ANISOU 3211  CZ  PHE B 260     2867   3240   3821   -223     21   -588       C  
ATOM   3212  N   ALA B 261      62.009  28.572  12.602  1.00 22.63           N  
ANISOU 3212  N   ALA B 261     2632   2632   3333   -236    197   -427       N  
ATOM   3213  CA  ALA B 261      61.228  29.579  11.895  1.00 24.37           C  
ANISOU 3213  CA  ALA B 261     2886   2823   3550   -239    240   -410       C  
ATOM   3214  C   ALA B 261      59.923  29.828  12.647  1.00 27.85           C  
ANISOU 3214  C   ALA B 261     3344   3279   3960   -231    224   -383       C  
ATOM   3215  O   ALA B 261      59.448  30.972  12.755  1.00 24.17           O  
ANISOU 3215  O   ALA B 261     2890   2799   3495   -239    255   -387       O  
ATOM   3216  CB  ALA B 261      60.962  29.154  10.460  1.00 21.20           C  
ANISOU 3216  CB  ALA B 261     2512   2396   3146   -231    257   -379       C  
ATOM   3217  N   LEU B 262      59.354  28.751  13.186  1.00 23.11           N  
ANISOU 3217  N   LEU B 262     2743   2705   3333   -216    177   -357       N  
ATOM   3218  CA  LEU B 262      58.149  28.871  13.992  1.00 21.26           C  
ANISOU 3218  CA  LEU B 262     2522   2488   3069   -208    159   -334       C  
ATOM   3219  C   LEU B 262      58.413  29.762  15.220  1.00 24.29           C  
ANISOU 3219  C   LEU B 262     2884   2889   3457   -221    161   -369       C  
ATOM   3220  O   LEU B 262      57.642  30.673  15.510  1.00 19.18           O  
ANISOU 3220  O   LEU B 262     2250   2235   2802   -225    180   -365       O  
ATOM   3221  CB  LEU B 262      57.643  27.496  14.431  1.00 18.09           C  
ANISOU 3221  CB  LEU B 262     2119   2112   2641   -190    110   -304       C  
ATOM   3222  CG  LEU B 262      56.501  27.482  15.446  1.00 25.32           C  
ANISOU 3222  CG  LEU B 262     3044   3050   3527   -182     86   -283       C  
ATOM   3223  CD1 LEU B 262      55.288  28.161  14.854  1.00 17.66           C  
ANISOU 3223  CD1 LEU B 262     2107   2058   2544   -180    112   -256       C  
ATOM   3224  CD2 LEU B 262      56.170  26.054  15.887  1.00 16.48           C  
ANISOU 3224  CD2 LEU B 262     1920   1954   2387   -165     40   -256       C  
ATOM   3225  N   ALA B 263      59.498  29.492  15.938  1.00 19.92           N  
ANISOU 3225  N   ALA B 263     2295   2357   2916   -226    141   -405       N  
ATOM   3226  CA  ALA B 263      59.831  30.292  17.118  1.00 26.33           C  
ANISOU 3226  CA  ALA B 263     3082   3190   3732   -239    141   -444       C  
ATOM   3227  C   ALA B 263      59.953  31.776  16.773  1.00 25.86           C  
ANISOU 3227  C   ALA B 263     3027   3100   3697   -258    196   -470       C  
ATOM   3228  O   ALA B 263      59.529  32.632  17.555  1.00 26.83           O  
ANISOU 3228  O   ALA B 263     3147   3231   3815   -266    205   -484       O  
ATOM   3229  CB  ALA B 263      61.109  29.784  17.773  1.00 24.22           C  
ANISOU 3229  CB  ALA B 263     2773   2951   3478   -241    114   -482       C  
ATOM   3230  N   GLU B 264      60.510  32.074  15.597  1.00 26.99           N  
ANISOU 3230  N   GLU B 264     3179   3210   3868   -265    234   -477       N  
ATOM   3231  CA  GLU B 264      60.671  33.468  15.148  1.00 28.26           C  
ANISOU 3231  CA  GLU B 264     3346   3336   4056   -282    291   -499       C  
ATOM   3232  C   GLU B 264      59.322  34.132  14.914  1.00 32.59           C  
ANISOU 3232  C   GLU B 264     3931   3867   4586   -277    313   -463       C  
ATOM   3233  O   GLU B 264      59.111  35.294  15.268  1.00 26.15           O  
ANISOU 3233  O   GLU B 264     3116   3040   3782   -289    345   -482       O  
ATOM   3234  CB  GLU B 264      61.518  33.542  13.869  1.00 32.03           C  
ANISOU 3234  CB  GLU B 264     3827   3779   4563   -289    328   -508       C  
ATOM   3235  CG  GLU B 264      62.942  33.031  14.053  1.00 30.55           C  
ANISOU 3235  CG  GLU B 264     3602   3606   4401   -297    314   -550       C  
ATOM   3236  CD  GLU B 264      63.701  32.813  12.734  1.00 33.12           C  
ANISOU 3236  CD  GLU B 264     3933   3899   4750   -300    342   -551       C  
ATOM   3237  OE1 GLU B 264      63.212  33.233  11.659  1.00 31.83           O  
ANISOU 3237  OE1 GLU B 264     3804   3702   4588   -298    380   -524       O  
ATOM   3238  OE2 GLU B 264      64.793  32.206  12.788  1.00 29.21           O  
ANISOU 3238  OE2 GLU B 264     3409   3415   4273   -304    326   -579       O  
ATOM   3239  N   GLU B 265      58.409  33.378  14.314  1.00 33.87           N  
ANISOU 3239  N   GLU B 265     4121   4026   4721   -258    295   -414       N  
ATOM   3240  CA  GLU B 265      57.063  33.858  14.058  1.00 33.82           C  
ANISOU 3240  CA  GLU B 265     4150   4007   4695   -249    309   -376       C  
ATOM   3241  C   GLU B 265      56.353  34.164  15.369  1.00 42.33           C  
ANISOU 3241  C   GLU B 265     5220   5110   5754   -250    288   -380       C  
ATOM   3242  O   GLU B 265      55.690  35.188  15.498  1.00 38.20           O  
ANISOU 3242  O   GLU B 265     4711   4573   5232   -254    317   -378       O  
ATOM   3243  CB  GLU B 265      56.270  32.827  13.256  1.00 35.60           C  
ANISOU 3243  CB  GLU B 265     4400   4232   4894   -228    287   -327       C  
ATOM   3244  CG  GLU B 265      55.557  33.390  12.049  1.00 39.68           C  
ANISOU 3244  CG  GLU B 265     4953   4715   5407   -220    325   -296       C  
ATOM   3245  CD  GLU B 265      56.485  34.142  11.117  1.00 48.62           C  
ANISOU 3245  CD  GLU B 265     6088   5814   6573   -231    376   -317       C  
ATOM   3246  OE1 GLU B 265      57.490  33.555  10.670  1.00 45.18           O  
ANISOU 3246  OE1 GLU B 265     5637   5376   6152   -235    372   -333       O  
ATOM   3247  OE2 GLU B 265      56.207  35.319  10.826  1.00 62.18           O  
ANISOU 3247  OE2 GLU B 265     7820   7504   8300   -236    420   -318       O  
ATOM   3248  N   ILE B 266      56.499  33.274  16.343  1.00 22.90           N  
ANISOU 3248  N   ILE B 266     2738   2688   3276   -245    240   -385       N  
ATOM   3249  CA  ILE B 266      55.888  33.492  17.642  1.00 32.59           C  
ANISOU 3249  CA  ILE B 266     3956   3942   4483   -246    218   -390       C  
ATOM   3250  C   ILE B 266      56.470  34.732  18.303  1.00 35.04           C  
ANISOU 3250  C   ILE B 266     4245   4251   4817   -268    248   -440       C  
ATOM   3251  O   ILE B 266      55.738  35.564  18.826  1.00 42.90           O  
ANISOU 3251  O   ILE B 266     5247   5245   5807   -273    262   -441       O  
ATOM   3252  CB  ILE B 266      56.052  32.276  18.554  1.00 31.28           C  
ANISOU 3252  CB  ILE B 266     3771   3818   4295   -236    162   -387       C  
ATOM   3253  CG1 ILE B 266      55.140  31.150  18.078  1.00 26.77           C  
ANISOU 3253  CG1 ILE B 266     3225   3249   3697   -215    135   -335       C  
ATOM   3254  CG2 ILE B 266      55.737  32.646  19.988  1.00 30.35           C  
ANISOU 3254  CG2 ILE B 266     3638   3732   4160   -241    144   -405       C  
ATOM   3255  CD1 ILE B 266      55.244  29.907  18.904  1.00 24.99           C  
ANISOU 3255  CD1 ILE B 266     2984   3060   3451   -203     84   -326       C  
ATOM   3256  N   GLU B 267      57.789  34.871  18.274  1.00 41.84           N  
ANISOU 3256  N   GLU B 267     5077   5112   5707   -281    258   -483       N  
ATOM   3257  CA  GLU B 267      58.428  36.025  18.900  1.00 46.91           C  
ANISOU 3257  CA  GLU B 267     5694   5753   6375   -303    287   -536       C  
ATOM   3258  C   GLU B 267      57.878  37.354  18.382  1.00 49.04           C  
ANISOU 3258  C   GLU B 267     5986   5982   6663   -313    344   -534       C  
ATOM   3259  O   GLU B 267      57.768  38.315  19.137  1.00 48.89           O  
ANISOU 3259  O   GLU B 267     5956   5966   6653   -327    363   -564       O  
ATOM   3260  CB  GLU B 267      59.947  35.968  18.749  1.00 45.63           C  
ANISOU 3260  CB  GLU B 267     5499   5592   6246   -315    295   -583       C  
ATOM   3261  CG  GLU B 267      60.648  35.280  19.910  1.00 59.60           C  
ANISOU 3261  CG  GLU B 267     7230   7411   8005   -314    246   -613       C  
ATOM   3262  CD  GLU B 267      60.783  36.173  21.130  1.00 64.22           C  
ANISOU 3262  CD  GLU B 267     7788   8020   8593   -330    250   -659       C  
ATOM   3263  OE1 GLU B 267      60.210  37.279  21.129  1.00 62.97           O  
ANISOU 3263  OE1 GLU B 267     7642   7839   8444   -341    289   -664       O  
ATOM   3264  OE2 GLU B 267      61.463  35.769  22.092  1.00 65.93           O  
ANISOU 3264  OE2 GLU B 267     7970   8279   8803   -330    215   -691       O  
ATOM   3265  N   ARG B 268      57.506  37.390  17.108  1.00 51.31           N  
ANISOU 3265  N   ARG B 268     6307   6234   6956   -304    371   -499       N  
ATOM   3266  CA  ARG B 268      56.928  38.588  16.515  1.00 49.16           C  
ANISOU 3266  CA  ARG B 268     6060   5922   6698   -309    426   -489       C  
ATOM   3267  C   ARG B 268      55.493  38.827  16.989  1.00 63.47           C  
ANISOU 3267  C   ARG B 268     7894   7740   8481   -298    416   -456       C  
ATOM   3268  O   ARG B 268      55.205  39.845  17.612  1.00 73.02           O  
ANISOU 3268  O   ARG B 268     9099   8945   9701   -310    440   -477       O  
ATOM   3269  CB  ARG B 268      56.990  38.514  14.989  1.00 45.65           C  
ANISOU 3269  CB  ARG B 268     5643   5439   6262   -300    456   -459       C  
ATOM   3270  CG  ARG B 268      58.401  38.601  14.436  1.00 49.07           C  
ANISOU 3270  CG  ARG B 268     6057   5855   6731   -314    482   -496       C  
ATOM   3271  CD  ARG B 268      58.419  38.496  12.924  1.00 51.05           C  
ANISOU 3271  CD  ARG B 268     6338   6071   6988   -304    512   -464       C  
ATOM   3272  NE  ARG B 268      59.414  37.531  12.463  1.00 60.12           N  
ANISOU 3272  NE  ARG B 268     7471   7227   8144   -303    493   -475       N  
ATOM   3273  CZ  ARG B 268      59.138  36.485  11.690  1.00 60.43           C  
ANISOU 3273  CZ  ARG B 268     7528   7270   8162   -286    468   -437       C  
ATOM   3274  NH1 ARG B 268      57.895  36.269  11.285  1.00 62.52           N  
ANISOU 3274  NH1 ARG B 268     7826   7533   8395   -267    459   -387       N  
ATOM   3275  NH2 ARG B 268      60.103  35.657  11.322  1.00 52.33           N  
ANISOU 3275  NH2 ARG B 268     6486   6250   7147   -287    453   -450       N  
ATOM   3276  N   ILE B 269      54.598  37.889  16.699  1.00 59.56           N  
ANISOU 3276  N   ILE B 269     7422   7257   7953   -277    382   -408       N  
ATOM   3277  CA  ILE B 269      53.206  38.003  17.140  1.00 58.11           C  
ANISOU 3277  CA  ILE B 269     7257   7080   7740   -267    369   -377       C  
ATOM   3278  C   ILE B 269      53.187  38.244  18.641  1.00 68.93           C  
ANISOU 3278  C   ILE B 269     8602   8484   9104   -278    349   -408       C  
ATOM   3279  O   ILE B 269      52.203  38.731  19.198  1.00 66.26           O  
ANISOU 3279  O   ILE B 269     8275   8150   8753   -277    351   -398       O  
ATOM   3280  CB  ILE B 269      52.383  36.726  16.838  1.00 49.71           C  
ANISOU 3280  CB  ILE B 269     6214   6034   6642   -244    326   -328       C  
ATOM   3281  CG1 ILE B 269      50.893  37.064  16.699  1.00 60.14           C  
ANISOU 3281  CG1 ILE B 269     7564   7345   7941   -231    332   -290       C  
ATOM   3282  CG2 ILE B 269      52.600  35.677  17.925  1.00 48.37           C  
ANISOU 3282  CG2 ILE B 269     6020   5909   6451   -242    271   -337       C  
ATOM   3283  CD1 ILE B 269      49.984  35.858  16.461  1.00 51.10           C  
ANISOU 3283  CD1 ILE B 269     6436   6217   6762   -210    291   -245       C  
ATOM   3284  N   LYS B 270      54.314  37.958  19.282  1.00 83.69           N  
ANISOU 3284  N   LYS B 270    10437  10377  10984   -290    331   -449       N  
ATOM   3285  CA  LYS B 270      54.470  38.168  20.716  1.00 84.97           C  
ANISOU 3285  CA  LYS B 270    10570  10575  11139   -301    311   -485       C  
ATOM   3286  C   LYS B 270      53.945  39.526  21.167  1.00 91.94           C  
ANISOU 3286  C   LYS B 270    11455  11443  12035   -315    349   -504       C  
ATOM   3287  O   LYS B 270      53.589  39.704  22.330  1.00 91.60           O  
ANISOU 3287  O   LYS B 270    11398  11430  11977   -320    331   -520       O  
ATOM   3288  CB  LYS B 270      55.938  38.026  21.114  1.00 81.08           C  
ANISOU 3288  CB  LYS B 270    10037  10101  10667   -314    303   -536       C  
ATOM   3289  CG  LYS B 270      56.153  37.528  22.528  1.00 77.95           C  
ANISOU 3289  CG  LYS B 270     9612   9758  10248   -315    256   -560       C  
ATOM   3290  CD  LYS B 270      55.592  36.133  22.709  1.00 80.03           C  
ANISOU 3290  CD  LYS B 270     9887  10049  10472   -291    202   -515       C  
ATOM   3291  CE  LYS B 270      56.585  35.236  23.422  1.00 95.51           C  
ANISOU 3291  CE  LYS B 270    11814  12051  12425   -287    159   -538       C  
ATOM   3292  NZ  LYS B 270      57.942  35.839  23.438  1.00 98.13           N  
ANISOU 3292  NZ  LYS B 270    12112  12381  12793   -306    181   -596       N  
ATOM   3293  N   ASP B 271      53.899  40.482  20.246  1.00103.61           N  
ANISOU 3293  N   ASP B 271    12950  12876  13541   -321    403   -502       N  
ATOM   3294  CA  ASP B 271      53.417  41.820  20.566  1.00107.06           C  
ANISOU 3294  CA  ASP B 271    13391  13292  13996   -334    446   -518       C  
ATOM   3295  C   ASP B 271      51.946  41.980  20.200  1.00100.70           C  
ANISOU 3295  C   ASP B 271    12622  12469  13169   -317    452   -467       C  
ATOM   3296  O   ASP B 271      51.603  42.667  19.240  1.00 94.61           O  
ANISOU 3296  O   ASP B 271    11876  11656  12414   -313    495   -446       O  
ATOM   3297  CB  ASP B 271      54.271  42.884  19.870  1.00118.10           C  
ANISOU 3297  CB  ASP B 271    14784  14649  15442   -350    508   -550       C  
ATOM   3298  CG  ASP B 271      53.694  43.321  18.539  1.00126.09           C  
ANISOU 3298  CG  ASP B 271    15835  15612  16462   -338    550   -507       C  
ATOM   3299  OD1 ASP B 271      53.780  42.543  17.565  1.00112.49           O  
ANISOU 3299  OD1 ASP B 271    14130  13882  14730   -323    538   -474       O  
ATOM   3300  OD2 ASP B 271      53.160  44.447  18.465  1.00128.79           O  
ANISOU 3300  OD2 ASP B 271    16190  15924  16821   -343    594   -507       O  
ATOM   3301  N   GLU B 272      51.082  41.335  20.976  1.00 96.17           N  
ANISOU 3301  N   GLU B 272    12052  11929  12559   -307    408   -446       N  
ATOM   3302  CA  GLU B 272      49.646  41.385  20.739  1.00 94.78           C  
ANISOU 3302  CA  GLU B 272    11908  11743  12361   -291    407   -399       C  
ATOM   3303  C   GLU B 272      48.923  42.012  21.924  1.00 95.42           C  
ANISOU 3303  C   GLU B 272    11982  11840  12434   -300    406   -414       C  
ATOM   3304  O   GLU B 272      49.151  41.633  23.072  1.00 96.56           O  
ANISOU 3304  O   GLU B 272    12102  12024  12563   -307    372   -439       O  
ATOM   3305  CB  GLU B 272      49.099  39.981  20.483  1.00 83.91           C  
ANISOU 3305  CB  GLU B 272    10547  10388  10949   -269    358   -355       C  
ATOM   3306  CG  GLU B 272      49.170  39.067  21.692  1.00 85.03           C  
ANISOU 3306  CG  GLU B 272    10667  10577  11063   -269    305   -365       C  
ATOM   3307  CD  GLU B 272      49.207  37.602  21.313  1.00 84.43           C  
ANISOU 3307  CD  GLU B 272    10596  10518  10963   -251    262   -333       C  
ATOM   3308  OE1 GLU B 272      50.127  36.895  21.769  1.00 85.42           O  
ANISOU 3308  OE1 GLU B 272    10698  10670  11087   -254    233   -354       O  
ATOM   3309  OE2 GLU B 272      48.317  37.155  20.563  1.00 83.05           O  
ANISOU 3309  OE2 GLU B 272    10450  10331  10774   -234    257   -289       O  
ATOM   3310  N   THR B 278      40.984  44.349  18.096  1.00118.82           N  
ANISOU 3310  N   THR B 278    15139  14662  15346   -186    506   -153       N  
ATOM   3311  CA  THR B 278      41.025  43.561  16.871  1.00118.49           C  
ANISOU 3311  CA  THR B 278    15116  14617  15290   -165    494   -120       C  
ATOM   3312  C   THR B 278      40.033  42.406  16.933  1.00118.12           C  
ANISOU 3312  C   THR B 278    15077  14599  15205   -148    443    -89       C  
ATOM   3313  O   THR B 278      39.431  42.034  15.925  1.00117.84           O  
ANISOU 3313  O   THR B 278    15062  14557  15154   -125    439    -53       O  
ATOM   3314  CB  THR B 278      42.447  43.025  16.618  1.00108.62           C  
ANISOU 3314  CB  THR B 278    13850  13371  14050   -177    489   -142       C  
ATOM   3315  OG1 THR B 278      42.861  42.218  17.726  1.00108.75           O  
ANISOU 3315  OG1 THR B 278    13840  13424  14054   -191    446   -168       O  
ATOM   3316  CG2 THR B 278      43.454  44.165  16.618  1.00109.03           C  
ANISOU 3316  CG2 THR B 278    13890  13394  14141   -196    540   -178       C  
ATOM   3317  N   GLY B 279      39.868  41.844  18.126  1.00 69.22           N  
ANISOU 3317  N   GLY B 279     8865   8437   8997   -159    407   -104       N  
ATOM   3318  CA  GLY B 279      38.966  40.727  18.328  1.00 68.91           C  
ANISOU 3318  CA  GLY B 279     8831   8426   8925   -146    361    -79       C  
ATOM   3319  C   GLY B 279      39.328  39.517  17.489  1.00 68.65           C  
ANISOU 3319  C   GLY B 279     8804   8403   8878   -133    334    -60       C  
ATOM   3320  O   GLY B 279      38.453  38.745  17.099  1.00 68.35           O  
ANISOU 3320  O   GLY B 279     8778   8375   8817   -116    309    -30       O  
ATOM   3321  N   GLU B 280      40.618  39.347  17.212  1.00 62.32           N  
ANISOU 3321  N   GLU B 280     7990   7598   8091   -143    340    -80       N  
ATOM   3322  CA  GLU B 280      41.076  38.232  16.392  1.00 49.93           C  
ANISOU 3322  CA  GLU B 280     6424   6036   6512   -133    318    -65       C  
ATOM   3323  C   GLU B 280      41.325  36.993  17.245  1.00 47.70           C  
ANISOU 3323  C   GLU B 280     6124   5789   6213   -139    270    -73       C  
ATOM   3324  O   GLU B 280      42.202  36.983  18.107  1.00 58.37           O  
ANISOU 3324  O   GLU B 280     7453   7154   7573   -156    263   -104       O  
ATOM   3325  CB  GLU B 280      42.337  38.616  15.615  1.00 41.99           C  
ANISOU 3325  CB  GLU B 280     5415   5008   5531   -140    348    -81       C  
ATOM   3326  CG  GLU B 280      42.082  39.602  14.484  1.00 45.96           C  
ANISOU 3326  CG  GLU B 280     5942   5475   6046   -128    394    -63       C  
ATOM   3327  CD  GLU B 280      43.206  39.639  13.469  1.00 42.05           C  
ANISOU 3327  CD  GLU B 280     5449   4960   5569   -129    419    -69       C  
ATOM   3328  OE1 GLU B 280      44.380  39.606  13.881  1.00 44.75           O  
ANISOU 3328  OE1 GLU B 280     5769   5305   5929   -149    421   -103       O  
ATOM   3329  OE2 GLU B 280      42.915  39.700  12.259  1.00 32.48           O  
ANISOU 3329  OE2 GLU B 280     4259   3731   4351   -111    435    -41       O  
ATOM   3330  N   GLY B 281      40.542  35.951  16.995  1.00 34.57           N  
ANISOU 3330  N   GLY B 281     4469   4140   4526   -123    238    -44       N  
ATOM   3331  CA  GLY B 281      40.592  34.742  17.793  1.00 29.24           C  
ANISOU 3331  CA  GLY B 281     3781   3496   3834   -125    194    -45       C  
ATOM   3332  C   GLY B 281      41.812  33.864  17.592  1.00 25.26           C  
ANISOU 3332  C   GLY B 281     3262   3000   3335   -129    177    -57       C  
ATOM   3333  O   GLY B 281      42.670  34.138  16.758  1.00 22.56           O  
ANISOU 3333  O   GLY B 281     2921   2641   3011   -131    199    -65       O  
ATOM   3334  N   ARG B 282      41.866  32.795  18.376  1.00 27.46           N  
ANISOU 3334  N   ARG B 282     3528   3307   3600   -130    139    -56       N  
ATOM   3335  CA  ARG B 282      42.973  31.847  18.377  1.00 27.67           C  
ANISOU 3335  CA  ARG B 282     3538   3345   3629   -132    118    -67       C  
ATOM   3336  C   ARG B 282      43.220  31.142  17.037  1.00 22.38           C  
ANISOU 3336  C   ARG B 282     2878   2662   2963   -120    118    -49       C  
ATOM   3337  O   ARG B 282      44.366  30.997  16.625  1.00 22.70           O  
ANISOU 3337  O   ARG B 282     2908   2698   3020   -126    123    -65       O  
ATOM   3338  CB  ARG B 282      42.794  30.834  19.510  1.00 22.94           C  
ANISOU 3338  CB  ARG B 282     2926   2777   3011   -131     78    -63       C  
ATOM   3339  CG  ARG B 282      43.184  31.408  20.882  1.00 33.16           C  
ANISOU 3339  CG  ARG B 282     4203   4092   4306   -146     76    -93       C  
ATOM   3340  CD  ARG B 282      42.596  30.574  22.023  1.00 32.21           C  
ANISOU 3340  CD  ARG B 282     4078   4000   4160   -142     41    -81       C  
ATOM   3341  NE  ARG B 282      41.172  30.360  21.812  1.00 29.43           N  
ANISOU 3341  NE  ARG B 282     3747   3643   3793   -131     38    -51       N  
ATOM   3342  CZ  ARG B 282      40.402  29.577  22.564  1.00 33.35           C  
ANISOU 3342  CZ  ARG B 282     4244   4158   4268   -125     13    -34       C  
ATOM   3343  NH1 ARG B 282      40.914  28.913  23.602  1.00 26.54           N  
ANISOU 3343  NH1 ARG B 282     3366   3322   3394   -127    -13    -41       N  
ATOM   3344  NH2 ARG B 282      39.112  29.465  22.273  1.00 31.28           N  
ANISOU 3344  NH2 ARG B 282     4000   3888   3996   -116     14    -10       N  
ATOM   3345  N   GLN B 283      42.158  30.708  16.362  1.00 21.78           N  
ANISOU 3345  N   GLN B 283     2820   2582   2873   -105    112    -19       N  
ATOM   3346  CA  GLN B 283      42.320  30.058  15.065  1.00 23.35           C  
ANISOU 3346  CA  GLN B 283     3028   2771   3073    -94    112     -4       C  
ATOM   3347  C   GLN B 283      43.083  30.978  14.117  1.00 27.47           C  
ANISOU 3347  C   GLN B 283     3555   3267   3614    -97    150    -15       C  
ATOM   3348  O   GLN B 283      43.979  30.540  13.392  1.00 20.91           O  
ANISOU 3348  O   GLN B 283     2720   2431   2794    -98    152    -20       O  
ATOM   3349  CB  GLN B 283      40.968  29.685  14.439  1.00 26.35           C  
ANISOU 3349  CB  GLN B 283     3426   3150   3435    -76    106     26       C  
ATOM   3350  CG  GLN B 283      41.107  28.982  13.069  1.00 25.36           C  
ANISOU 3350  CG  GLN B 283     3309   3018   3309    -64    105     40       C  
ATOM   3351  CD  GLN B 283      41.769  27.606  13.199  1.00 28.56           C  
ANISOU 3351  CD  GLN B 283     3699   3436   3716    -66     76     37       C  
ATOM   3352  OE1 GLN B 283      41.348  26.796  14.010  1.00 24.50           O  
ANISOU 3352  OE1 GLN B 283     3177   2939   3192    -65     48     43       O  
ATOM   3353  NE2 GLN B 283      42.804  27.347  12.402  1.00 22.75           N  
ANISOU 3353  NE2 GLN B 283     2958   2692   2994    -68     84     28       N  
ATOM   3354  N   VAL B 284      42.728  32.259  14.144  1.00 23.86           N  
ANISOU 3354  N   VAL B 284     3108   2794   3163   -100    181    -18       N  
ATOM   3355  CA  VAL B 284      43.311  33.235  13.240  1.00 25.78           C  
ANISOU 3355  CA  VAL B 284     3361   3011   3425   -102    223    -25       C  
ATOM   3356  C   VAL B 284      44.771  33.487  13.589  1.00 29.29           C  
ANISOU 3356  C   VAL B 284     3784   3451   3893   -120    234    -59       C  
ATOM   3357  O   VAL B 284      45.605  33.590  12.697  1.00 28.97           O  
ANISOU 3357  O   VAL B 284     3746   3394   3869   -122    255    -65       O  
ATOM   3358  CB  VAL B 284      42.518  34.571  13.262  1.00 33.21           C  
ANISOU 3358  CB  VAL B 284     4317   3934   4369    -99    256    -19       C  
ATOM   3359  CG1 VAL B 284      43.313  35.692  12.598  1.00 26.25           C  
ANISOU 3359  CG1 VAL B 284     3440   3021   3511   -105    303    -31       C  
ATOM   3360  CG2 VAL B 284      41.153  34.396  12.611  1.00 33.39           C  
ANISOU 3360  CG2 VAL B 284     4362   3957   4370    -77    250     16       C  
ATOM   3361  N   GLN B 285      45.083  33.590  14.881  1.00 13.82           N  
ANISOU 3361  N   GLN B 285     1804   1508   1937   -135    220    -83       N  
ATOM   3362  CA  GLN B 285      46.477  33.756  15.307  1.00 20.80           C  
ANISOU 3362  CA  GLN B 285     2664   2394   2843   -152    226   -120       C  
ATOM   3363  C   GLN B 285      47.353  32.583  14.852  1.00 20.53           C  
ANISOU 3363  C   GLN B 285     2619   2369   2812   -150    203   -121       C  
ATOM   3364  O   GLN B 285      48.472  32.770  14.360  1.00 18.89           O  
ANISOU 3364  O   GLN B 285     2403   2149   2627   -158    222   -142       O  
ATOM   3365  CB  GLN B 285      46.582  33.863  16.830  1.00 22.38           C  
ANISOU 3365  CB  GLN B 285     2843   2620   3040   -165    207   -144       C  
ATOM   3366  CG  GLN B 285      45.706  34.923  17.472  1.00 28.97           C  
ANISOU 3366  CG  GLN B 285     3684   3451   3872   -170    225   -147       C  
ATOM   3367  CD  GLN B 285      45.819  34.929  18.991  1.00 39.61           C  
ANISOU 3367  CD  GLN B 285     5009   4828   5213   -182    203   -171       C  
ATOM   3368  OE1 GLN B 285      44.822  35.055  19.697  1.00 42.47           O  
ANISOU 3368  OE1 GLN B 285     5377   5201   5557   -179    194   -161       O  
ATOM   3369  NE2 GLN B 285      47.041  34.789  19.497  1.00 43.68           N  
ANISOU 3369  NE2 GLN B 285     5499   5357   5741   -194    196   -205       N  
ATOM   3370  N   TRP B 286      46.846  31.370  15.037  1.00 17.60           N  
ANISOU 3370  N   TRP B 286     2248   2018   2419   -138    165   -101       N  
ATOM   3371  CA  TRP B 286      47.630  30.179  14.695  1.00 17.54           C  
ANISOU 3371  CA  TRP B 286     2229   2019   2415   -135    141   -101       C  
ATOM   3372  C   TRP B 286      47.790  30.009  13.193  1.00 13.46           C  
ANISOU 3372  C   TRP B 286     1728   1482   1905   -127    160    -87       C  
ATOM   3373  O   TRP B 286      48.842  29.579  12.728  1.00 17.79           O  
ANISOU 3373  O   TRP B 286     2265   2026   2468   -131    161   -101       O  
ATOM   3374  CB  TRP B 286      47.053  28.921  15.351  1.00 15.77           C  
ANISOU 3374  CB  TRP B 286     2001   1822   2170   -126     97    -83       C  
ATOM   3375  CG  TRP B 286      47.379  28.839  16.821  1.00 17.67           C  
ANISOU 3375  CG  TRP B 286     2220   2088   2406   -134     75   -102       C  
ATOM   3376  CD1 TRP B 286      46.520  29.016  17.871  1.00 21.99           C  
ANISOU 3376  CD1 TRP B 286     2768   2651   2935   -134     62    -96       C  
ATOM   3377  CD2 TRP B 286      48.669  28.591  17.396  1.00 15.37           C  
ANISOU 3377  CD2 TRP B 286     1901   1810   2127   -143     63   -130       C  
ATOM   3378  NE1 TRP B 286      47.191  28.862  19.069  1.00 19.13           N  
ANISOU 3378  NE1 TRP B 286     2382   2314   2571   -142     43   -118       N  
ATOM   3379  CE2 TRP B 286      48.507  28.606  18.803  1.00 21.30           C  
ANISOU 3379  CE2 TRP B 286     2640   2590   2866   -147     42   -140       C  
ATOM   3380  CE3 TRP B 286      49.936  28.350  16.857  1.00 21.32           C  
ANISOU 3380  CE3 TRP B 286     2641   2558   2903   -148     68   -150       C  
ATOM   3381  CZ2 TRP B 286      49.574  28.392  19.673  1.00 25.19           C  
ANISOU 3381  CZ2 TRP B 286     3104   3104   3363   -153     24   -168       C  
ATOM   3382  CZ3 TRP B 286      51.002  28.135  17.728  1.00 28.36           C  
ANISOU 3382  CZ3 TRP B 286     3503   3470   3802   -155     51   -179       C  
ATOM   3383  CH2 TRP B 286      50.813  28.157  19.119  1.00 25.69           C  
ANISOU 3383  CH2 TRP B 286     3152   3161   3448   -157     28   -187       C  
ATOM   3384  N   ASP B 287      46.751  30.333  12.432  1.00 22.05           N  
ANISOU 3384  N   ASP B 287     2840   2557   2980   -115    174    -61       N  
ATOM   3385  CA  ASP B 287      46.857  30.350  10.968  1.00 26.61           C  
ANISOU 3385  CA  ASP B 287     3435   3115   3561   -106    197    -48       C  
ATOM   3386  C   ASP B 287      47.999  31.260  10.491  1.00 24.50           C  
ANISOU 3386  C   ASP B 287     3165   2824   3320   -118    236    -72       C  
ATOM   3387  O   ASP B 287      48.797  30.858   9.647  1.00 21.57           O  
ANISOU 3387  O   ASP B 287     2792   2445   2960   -118    244    -76       O  
ATOM   3388  CB  ASP B 287      45.548  30.801  10.313  1.00 27.71           C  
ANISOU 3388  CB  ASP B 287     3602   3246   3682    -90    210    -19       C  
ATOM   3389  CG  ASP B 287      44.435  29.782  10.464  1.00 40.28           C  
ANISOU 3389  CG  ASP B 287     5197   4858   5250    -76    174      5       C  
ATOM   3390  OD1 ASP B 287      43.255  30.144  10.241  1.00 40.03           O  
ANISOU 3390  OD1 ASP B 287     5182   4825   5202    -64    179     26       O  
ATOM   3391  OD2 ASP B 287      44.738  28.623  10.815  1.00 31.74           O  
ANISOU 3391  OD2 ASP B 287     4100   3793   4166    -78    142      2       O  
ATOM   3392  N   LYS B 288      48.082  32.458  11.055  1.00 21.88           N  
ANISOU 3392  N   LYS B 288     2831   2482   3001   -129    263    -88       N  
ATOM   3393  CA  LYS B 288      49.139  33.403  10.711  1.00 23.68           C  
ANISOU 3393  CA  LYS B 288     3054   2686   3257   -142    304   -114       C  
ATOM   3394  C   LYS B 288      50.535  32.873  11.058  1.00 24.12           C  
ANISOU 3394  C   LYS B 288     3081   2749   3333   -157    292   -147       C  
ATOM   3395  O   LYS B 288      51.432  32.878  10.222  1.00 25.95           O  
ANISOU 3395  O   LYS B 288     3312   2965   3583   -161    313   -158       O  
ATOM   3396  CB  LYS B 288      48.890  34.747  11.397  1.00 22.30           C  
ANISOU 3396  CB  LYS B 288     2880   2499   3094   -152    333   -128       C  
ATOM   3397  CG  LYS B 288      47.702  35.524  10.831  1.00 36.56           C  
ANISOU 3397  CG  LYS B 288     4716   4288   4888   -137    358    -98       C  
ATOM   3398  CD  LYS B 288      47.519  36.866  11.538  1.00 34.61           C  
ANISOU 3398  CD  LYS B 288     4468   4027   4656   -148    389   -114       C  
ATOM   3399  CE  LYS B 288      46.222  37.554  11.135  1.00 31.73           C  
ANISOU 3399  CE  LYS B 288     4130   3649   4277   -131    408    -82       C  
ATOM   3400  NZ  LYS B 288      46.461  38.842  10.440  1.00 28.06           N  
ANISOU 3400  NZ  LYS B 288     3680   3147   3834   -131    465    -83       N  
ATOM   3401  N  AVAL B 289      50.680  32.352  12.267  0.34 17.83           N  
ANISOU 3401  N  AVAL B 289     2262   1980   2532   -163    257   -162       N  
ATOM   3402  N  BVAL B 289      50.667  32.375  12.273  0.66 17.83           N  
ANISOU 3402  N  BVAL B 289     2262   1980   2532   -163    257   -162       N  
ATOM   3403  CA AVAL B 289      51.989  31.927  12.728  0.34 17.32           C  
ANISOU 3403  CA AVAL B 289     2167   1927   2485   -176    244   -195       C  
ATOM   3404  CA BVAL B 289      51.940  31.898  12.778  0.66 17.32           C  
ANISOU 3404  CA BVAL B 289     2167   1928   2484   -176    242   -195       C  
ATOM   3405  C  AVAL B 289      52.493  30.769  11.878  0.34 21.42           C  
ANISOU 3405  C  AVAL B 289     2686   2447   3006   -168    227   -185       C  
ATOM   3406  C  BVAL B 289      52.481  30.768  11.915  0.66 21.44           C  
ANISOU 3406  C  BVAL B 289     2688   2451   3008   -168    227   -186       C  
ATOM   3407  O  AVAL B 289      53.627  30.793  11.392  0.34 22.30           O  
ANISOU 3407  O  AVAL B 289     2785   2547   3140   -177    244   -208       O  
ATOM   3408  O  BVAL B 289      53.628  30.806  11.477  0.66 22.35           O  
ANISOU 3408  O  BVAL B 289     2790   2555   3147   -177    243   -209       O  
ATOM   3409  CB AVAL B 289      51.994  31.541  14.218  0.34 25.11           C  
ANISOU 3409  CB AVAL B 289     3131   2947   3463   -181    206   -210       C  
ATOM   3410  CB BVAL B 289      51.821  31.418  14.232  0.66 25.00           C  
ANISOU 3410  CB BVAL B 289     3120   2936   3445   -178    201   -204       C  
ATOM   3411  CG1AVAL B 289      50.702  30.889  14.607  0.34 34.79           C  
ANISOU 3411  CG1AVAL B 289     4371   4191   4658   -166    175   -176       C  
ATOM   3412  CG1BVAL B 289      52.940  30.459  14.566  0.66 35.99           C  
ANISOU 3412  CG1BVAL B 289     4483   4346   4844   -181    173   -224       C  
ATOM   3413  CG2AVAL B 289      53.131  30.600  14.514  0.34 29.20           C  
ANISOU 3413  CG2AVAL B 289     3621   3483   3990   -184    179   -230       C  
ATOM   3414  CG2BVAL B 289      51.823  32.602  15.181  0.66 29.12           C  
ANISOU 3414  CG2BVAL B 289     3631   3458   3974   -192    220   -231       C  
ATOM   3415  N   PHE B 290      51.644  29.767  11.671  1.00 15.12           N  
ANISOU 3415  N   PHE B 290     1899   1662   2184   -152    198   -153       N  
ATOM   3416  CA  PHE B 290      52.069  28.576  10.952  1.00 16.47           C  
ANISOU 3416  CA  PHE B 290     2067   1836   2356   -145    180   -145       C  
ATOM   3417  C   PHE B 290      52.183  28.750   9.444  1.00 14.17           C  
ANISOU 3417  C   PHE B 290     1795   1520   2070   -141    211   -134       C  
ATOM   3418  O   PHE B 290      53.056  28.151   8.814  1.00 16.81           O  
ANISOU 3418  O   PHE B 290     2120   1848   2417   -143    211   -143       O  
ATOM   3419  CB  PHE B 290      51.156  27.396  11.277  1.00 17.40           C  
ANISOU 3419  CB  PHE B 290     2188   1975   2449   -131    139   -117       C  
ATOM   3420  CG  PHE B 290      51.657  26.561  12.411  1.00 16.86           C  
ANISOU 3420  CG  PHE B 290     2093   1931   2380   -134    101   -129       C  
ATOM   3421  CD1 PHE B 290      52.875  25.895  12.302  1.00 17.75           C  
ANISOU 3421  CD1 PHE B 290     2184   2048   2512   -138     92   -148       C  
ATOM   3422  CD2 PHE B 290      50.946  26.474  13.584  1.00 14.18           C  
ANISOU 3422  CD2 PHE B 290     1751   1614   2024   -131     77   -122       C  
ATOM   3423  CE1 PHE B 290      53.353  25.122  13.342  1.00 21.23           C  
ANISOU 3423  CE1 PHE B 290     2601   2512   2952   -137     57   -157       C  
ATOM   3424  CE2 PHE B 290      51.415  25.715  14.649  1.00 18.97           C  
ANISOU 3424  CE2 PHE B 290     2335   2246   2628   -131     44   -131       C  
ATOM   3425  CZ  PHE B 290      52.612  25.030  14.527  1.00 25.63           C  
ANISOU 3425  CZ  PHE B 290     3156   3092   3489   -133     33   -147       C  
ATOM   3426  N   THR B 291      51.279  29.532   8.858  1.00 18.42           N  
ANISOU 3426  N   THR B 291     2360   2043   2597   -133    237   -113       N  
ATOM   3427  CA  THR B 291      51.359  29.788   7.428  1.00 17.97           C  
ANISOU 3427  CA  THR B 291     2324   1964   2542   -126    269   -102       C  
ATOM   3428  C   THR B 291      52.639  30.549   7.098  1.00 20.25           C  
ANISOU 3428  C   THR B 291     2604   2230   2861   -141    307   -131       C  
ATOM   3429  O   THR B 291      53.358  30.165   6.190  1.00 23.88           O  
ANISOU 3429  O   THR B 291     3064   2679   3331   -142    318   -136       O  
ATOM   3430  CB  THR B 291      50.143  30.549   6.898  1.00 18.32           C  
ANISOU 3430  CB  THR B 291     2397   1997   2566   -112    289    -73       C  
ATOM   3431  OG1 THR B 291      48.968  29.770   7.130  1.00 19.71           O  
ANISOU 3431  OG1 THR B 291     2580   2195   2715    -98    254    -48       O  
ATOM   3432  CG2 THR B 291      50.281  30.804   5.404  1.00 22.09           C  
ANISOU 3432  CG2 THR B 291     2897   2455   3043   -103    323    -60       C  
ATOM   3433  N  ASER B 292      52.912  31.616   7.847  0.52 19.62           N  
ANISOU 3433  N  ASER B 292     2516   2142   2797   -155    328   -153       N  
ATOM   3434  N  BSER B 292      52.936  31.618   7.835  0.48 19.64           N  
ANISOU 3434  N  BSER B 292     2518   2144   2800   -155    329   -154       N  
ATOM   3435  CA ASER B 292      54.128  32.402   7.640  0.52 23.42           C  
ANISOU 3435  CA ASER B 292     2987   2601   3312   -172    367   -186       C  
ATOM   3436  CA BSER B 292      54.149  32.381   7.544  0.48 23.37           C  
ANISOU 3436  CA BSER B 292     2981   2593   3305   -171    368   -185       C  
ATOM   3437  C  ASER B 292      55.384  31.558   7.834  0.52 23.59           C  
ANISOU 3437  C  ASER B 292     2978   2632   3351   -182    347   -215       C  
ATOM   3438  C  BSER B 292      55.433  31.606   7.874  0.48 23.65           C  
ANISOU 3438  C  BSER B 292     2984   2639   3361   -184    348   -217       C  
ATOM   3439  O  ASER B 292      56.344  31.674   7.077  0.52 23.25           O  
ANISOU 3439  O  ASER B 292     2932   2571   3330   -190    374   -232       O  
ATOM   3440  O  BSER B 292      56.464  31.817   7.242  0.48 23.39           O  
ANISOU 3440  O  BSER B 292     2946   2588   3353   -193    376   -238       O  
ATOM   3441  CB ASER B 292      54.175  33.601   8.594  0.52 26.47           C  
ANISOU 3441  CB ASER B 292     3364   2980   3712   -185    389   -210       C  
ATOM   3442  CB BSER B 292      54.138  33.752   8.229  0.48 26.17           C  
ANISOU 3442  CB BSER B 292     3334   2934   3676   -183    400   -205       C  
ATOM   3443  OG ASER B 292      53.035  34.429   8.448  0.52 24.65           O  
ANISOU 3443  OG ASER B 292     3159   2738   3467   -175    409   -184       O  
ATOM   3444  OG BSER B 292      54.097  33.626   9.630  0.48 27.05           O  
ANISOU 3444  OG BSER B 292     3422   3072   3785   -192    369   -223       O  
ATOM   3445  N   CYS B 293      55.367  30.718   8.865  1.00 23.60           N  
ANISOU 3445  N   CYS B 293     2958   2664   3345   -182    301   -221       N  
ATOM   3446  CA  CYS B 293      56.479  29.820   9.174  1.00 20.43           C  
ANISOU 3446  CA  CYS B 293     2527   2277   2959   -189    275   -246       C  
ATOM   3447  C   CYS B 293      56.736  28.854   8.011  1.00 21.63           C  
ANISOU 3447  C   CYS B 293     2687   2423   3110   -181    271   -231       C  
ATOM   3448  O   CYS B 293      57.862  28.697   7.562  1.00 21.01           O  
ANISOU 3448  O   CYS B 293     2593   2333   3055   -190    284   -254       O  
ATOM   3449  CB  CYS B 293      56.175  29.018  10.459  1.00 23.49           C  
ANISOU 3449  CB  CYS B 293     2896   2699   3330   -185    224   -244       C  
ATOM   3450  SG  CYS B 293      57.058  27.462  10.606  1.00 35.28           S  
ANISOU 3450  SG  CYS B 293     4363   4213   4830   -181    182   -251       S  
ATOM   3451  N   PHE B 294      55.691  28.195   7.529  1.00 24.66           N  
ANISOU 3451  N   PHE B 294     3091   2812   3467   -164    254   -194       N  
ATOM   3452  CA  PHE B 294      55.855  27.294   6.391  1.00 20.19           C  
ANISOU 3452  CA  PHE B 294     2532   2241   2899   -156    251   -181       C  
ATOM   3453  C   PHE B 294      56.331  28.032   5.129  1.00 22.19           C  
ANISOU 3453  C   PHE B 294     2802   2465   3165   -160    300   -185       C  
ATOM   3454  O   PHE B 294      57.241  27.574   4.422  1.00 21.18           O  
ANISOU 3454  O   PHE B 294     2666   2328   3054   -165    309   -198       O  
ATOM   3455  CB  PHE B 294      54.564  26.525   6.107  1.00 15.84           C  
ANISOU 3455  CB  PHE B 294     1999   1702   2316   -138    226   -143       C  
ATOM   3456  CG  PHE B 294      54.354  25.311   6.990  1.00 13.79           C  
ANISOU 3456  CG  PHE B 294     1722   1470   2049   -133    177   -138       C  
ATOM   3457  CD1 PHE B 294      54.570  25.376   8.370  1.00 16.64           C  
ANISOU 3457  CD1 PHE B 294     2061   1847   2413   -139    156   -153       C  
ATOM   3458  CD2 PHE B 294      53.884  24.121   6.448  1.00 12.71           C  
ANISOU 3458  CD2 PHE B 294     1589   1340   1899   -121    155   -117       C  
ATOM   3459  CE1 PHE B 294      54.331  24.263   9.190  1.00 15.16           C  
ANISOU 3459  CE1 PHE B 294     1860   1683   2216   -132    113   -144       C  
ATOM   3460  CE2 PHE B 294      53.643  23.010   7.252  1.00 15.35           C  
ANISOU 3460  CE2 PHE B 294     1908   1695   2227   -115    114   -110       C  
ATOM   3461  CZ  PHE B 294      53.880  23.071   8.620  1.00 18.61           C  
ANISOU 3461  CZ  PHE B 294     2304   2125   2644   -120     93   -122       C  
ATOM   3462  N   LEU B 295      55.712  29.168   4.842  1.00 25.15           N  
ANISOU 3462  N   LEU B 295     3200   2823   3532   -157    334   -173       N  
ATOM   3463  CA  LEU B 295      56.068  29.933   3.654  1.00 27.39           C  
ANISOU 3463  CA  LEU B 295     3503   3077   3825   -158    384   -172       C  
ATOM   3464  C   LEU B 295      57.489  30.488   3.757  1.00 28.62           C  
ANISOU 3464  C   LEU B 295     3639   3215   4019   -179    414   -212       C  
ATOM   3465  O   LEU B 295      58.159  30.697   2.744  1.00 27.55           O  
ANISOU 3465  O   LEU B 295     3511   3058   3898   -183    449   -218       O  
ATOM   3466  CB  LEU B 295      55.069  31.064   3.427  1.00 25.48           C  
ANISOU 3466  CB  LEU B 295     3291   2822   3569   -149    414   -148       C  
ATOM   3467  CG  LEU B 295      53.732  30.717   2.777  1.00 33.58           C  
ANISOU 3467  CG  LEU B 295     4343   3857   4557   -125    401   -107       C  
ATOM   3468  CD1 LEU B 295      53.817  30.919   1.297  1.00 40.25           C  
ANISOU 3468  CD1 LEU B 295     5213   4684   5396   -115    435    -91       C  
ATOM   3469  CD2 LEU B 295      53.265  29.298   3.105  1.00 31.44           C  
ANISOU 3469  CD2 LEU B 295     4061   3617   4269   -118    347    -97       C  
ATOM   3470  N   THR B 296      57.956  30.725   4.977  1.00 24.57           N  
ANISOU 3470  N   THR B 296     3099   2712   3523   -193    401   -241       N  
ATOM   3471  CA  THR B 296      59.318  31.236   5.165  1.00 26.47           C  
ANISOU 3471  CA  THR B 296     3316   2939   3802   -213    427   -285       C  
ATOM   3472  C   THR B 296      60.311  30.130   4.815  1.00 27.13           C  
ANISOU 3472  C   THR B 296     3379   3030   3900   -217    407   -301       C  
ATOM   3473  O   THR B 296      61.276  30.341   4.079  1.00 29.21           O  
ANISOU 3473  O   THR B 296     3638   3272   4188   -227    440   -321       O  
ATOM   3474  CB  THR B 296      59.551  31.760   6.611  1.00 30.47           C  
ANISOU 3474  CB  THR B 296     3796   3459   4321   -226    415   -316       C  
ATOM   3475  OG1 THR B 296      58.851  32.997   6.787  1.00 29.19           O  
ANISOU 3475  OG1 THR B 296     3653   3282   4156   -227    447   -309       O  
ATOM   3476  CG2 THR B 296      61.029  31.990   6.891  1.00 27.62           C  
ANISOU 3476  CG2 THR B 296     3402   3092   3999   -247    430   -366       C  
ATOM   3477  N   VAL B 297      60.063  28.938   5.334  1.00 22.59           N  
ANISOU 3477  N   VAL B 297     2791   2483   3309   -208    356   -291       N  
ATOM   3478  CA  VAL B 297      60.900  27.798   4.994  1.00 24.79           C  
ANISOU 3478  CA  VAL B 297     3051   2769   3601   -209    335   -302       C  
ATOM   3479  C   VAL B 297      60.889  27.572   3.482  1.00 23.19           C  
ANISOU 3479  C   VAL B 297     2870   2545   3394   -203    361   -285       C  
ATOM   3480  O   VAL B 297      61.947  27.431   2.854  1.00 27.31           O  
ANISOU 3480  O   VAL B 297     3382   3053   3941   -212    380   -307       O  
ATOM   3481  CB  VAL B 297      60.457  26.534   5.748  1.00 24.75           C  
ANISOU 3481  CB  VAL B 297     3032   2795   3577   -197    277   -287       C  
ATOM   3482  CG1 VAL B 297      61.183  25.310   5.206  1.00 19.69           C  
ANISOU 3482  CG1 VAL B 297     2376   2157   2948   -195    260   -292       C  
ATOM   3483  CG2 VAL B 297      60.709  26.720   7.246  1.00 22.59           C  
ANISOU 3483  CG2 VAL B 297     2731   2543   3308   -203    252   -310       C  
ATOM   3484  N   ASP B 298      59.695  27.594   2.896  1.00 27.68           N  
ANISOU 3484  N   ASP B 298     3471   3114   3932   -187    363   -247       N  
ATOM   3485  CA  ASP B 298      59.544  27.360   1.466  1.00 25.90           C  
ANISOU 3485  CA  ASP B 298     3269   2875   3696   -179    385   -227       C  
ATOM   3486  C   ASP B 298      60.312  28.357   0.617  1.00 26.29           C  
ANISOU 3486  C   ASP B 298     3330   2893   3767   -189    442   -243       C  
ATOM   3487  O   ASP B 298      60.885  27.990  -0.395  1.00 27.23           O  
ANISOU 3487  O   ASP B 298     3452   3001   3893   -190    459   -246       O  
ATOM   3488  CB  ASP B 298      58.083  27.422   1.059  1.00 27.33           C  
ANISOU 3488  CB  ASP B 298     3482   3063   3840   -159    380   -186       C  
ATOM   3489  CG  ASP B 298      57.887  27.114  -0.411  1.00 28.30           C  
ANISOU 3489  CG  ASP B 298     3627   3177   3947   -148    398   -167       C  
ATOM   3490  OD1 ASP B 298      57.943  25.920  -0.770  1.00 27.90           O  
ANISOU 3490  OD1 ASP B 298     3569   3141   3893   -144    371   -164       O  
ATOM   3491  OD2 ASP B 298      57.673  28.054  -1.207  1.00 33.91           O  
ANISOU 3491  OD2 ASP B 298     4364   3869   4651   -143    440   -155       O  
ATOM   3492  N   GLY B 299      60.286  29.625   1.010  1.00 23.84           N  
ANISOU 3492  N   GLY B 299     3026   2567   3467   -196    474   -251       N  
ATOM   3493  CA  GLY B 299      60.992  30.659   0.273  1.00 25.23           C  
ANISOU 3493  CA  GLY B 299     3212   2710   3665   -207    533   -265       C  
ATOM   3494  C   GLY B 299      62.503  30.567   0.421  1.00 25.45           C  
ANISOU 3494  C   GLY B 299     3208   2727   3733   -228    545   -311       C  
ATOM   3495  O   GLY B 299      63.244  30.907  -0.497  1.00 24.51           O  
ANISOU 3495  O   GLY B 299     3096   2583   3633   -235    588   -322       O  
ATOM   3496  N   GLU B 300      62.961  30.118   1.583  1.00 27.08           N  
ANISOU 3496  N   GLU B 300     3380   2955   3954   -237    508   -338       N  
ATOM   3497  CA  GLU B 300      64.385  29.930   1.819  1.00 26.97           C  
ANISOU 3497  CA  GLU B 300     3332   2937   3979   -255    511   -383       C  
ATOM   3498  C   GLU B 300      64.902  28.822   0.910  1.00 32.95           C  
ANISOU 3498  C   GLU B 300     4085   3695   4738   -252    501   -381       C  
ATOM   3499  O   GLU B 300      66.012  28.905   0.370  1.00 26.17           O  
ANISOU 3499  O   GLU B 300     3215   2818   3911   -266    530   -410       O  
ATOM   3500  CB  GLU B 300      64.654  29.592   3.292  1.00 28.86           C  
ANISOU 3500  CB  GLU B 300     3534   3205   4225   -261    467   -408       C  
ATOM   3501  CG  GLU B 300      64.541  30.792   4.219  1.00 28.37           C  
ANISOU 3501  CG  GLU B 300     3466   3140   4173   -271    485   -427       C  
ATOM   3502  CD  GLU B 300      64.500  30.434   5.700  1.00 36.38           C  
ANISOU 3502  CD  GLU B 300     4451   4190   5183   -272    436   -443       C  
ATOM   3503  OE1 GLU B 300      64.343  31.367   6.525  1.00 34.03           O  
ANISOU 3503  OE1 GLU B 300     4146   3893   4889   -280    447   -459       O  
ATOM   3504  OE2 GLU B 300      64.606  29.231   6.045  1.00 31.31           O  
ANISOU 3504  OE2 GLU B 300     3793   3574   4532   -263    388   -438       O  
ATOM   3505  N  AILE B 301      64.106  27.776   0.717  0.20 27.61           N  
ANISOU 3505  N  AILE B 301     3418   3039   4032   -235    462   -349       N  
ATOM   3506  N  BILE B 301      64.063  27.802   0.738  0.80 27.54           N  
ANISOU 3506  N  BILE B 301     3411   3031   4022   -235    462   -348       N  
ATOM   3507  CA AILE B 301      64.568  26.659  -0.104  0.20 28.15           C  
ANISOU 3507  CA AILE B 301     3482   3110   4104   -232    451   -348       C  
ATOM   3508  CA BILE B 301      64.379  26.631  -0.070  0.80 28.20           C  
ANISOU 3508  CA BILE B 301     3492   3119   4106   -230    447   -343       C  
ATOM   3509  C  AILE B 301      64.524  26.981  -1.601  0.20 27.84           C  
ANISOU 3509  C  AILE B 301     3473   3046   4058   -229    496   -333       C  
ATOM   3510  C  BILE B 301      64.498  26.986  -1.550  0.80 27.83           C  
ANISOU 3510  C  BILE B 301     3472   3046   4057   -229    495   -333       C  
ATOM   3511  O  AILE B 301      65.347  26.485  -2.366  0.20 28.05           O  
ANISOU 3511  O  AILE B 301     3492   3063   4101   -235    508   -348       O  
ATOM   3512  O  BILE B 301      65.407  26.540  -2.236  0.80 27.92           O  
ANISOU 3512  O  BILE B 301     3474   3047   4088   -237    508   -351       O  
ATOM   3513  CB AILE B 301      63.814  25.341   0.200  0.20 26.43           C  
ANISOU 3513  CB AILE B 301     3261   2921   3861   -216    395   -323       C  
ATOM   3514  CB BILE B 301      63.307  25.535   0.127  0.80 25.54           C  
ANISOU 3514  CB BILE B 301     3161   2809   3736   -211    398   -309       C  
ATOM   3515  CG1AILE B 301      62.631  25.151  -0.747  0.20 24.63           C  
ANISOU 3515  CG1AILE B 301     3068   2694   3596   -199    399   -281       C  
ATOM   3516  CG1BILE B 301      63.514  24.866   1.489  0.80 26.27           C  
ANISOU 3516  CG1BILE B 301     3220   2926   3835   -212    349   -323       C  
ATOM   3517  CG2AILE B 301      63.399  25.272   1.662  0.20 26.25           C  
ANISOU 3517  CG2AILE B 301     3220   2922   3831   -213    356   -323       C  
ATOM   3518  CG2BILE B 301      63.361  24.504  -1.001  0.80 22.01           C  
ANISOU 3518  CG2BILE B 301     2720   2362   3282   -204    393   -297       C  
ATOM   3519  CD1AILE B 301      62.984  24.372  -1.991  0.20 24.16           C  
ANISOU 3519  CD1AILE B 301     3014   2628   3538   -197    408   -279       C  
ATOM   3520  CD1BILE B 301      62.405  23.931   1.912  0.80 23.77           C  
ANISOU 3520  CD1BILE B 301     2908   2635   3488   -195    303   -290       C  
ATOM   3521  N   GLU B 302      63.564  27.803  -2.017  1.00 26.02           N  
ANISOU 3521  N   GLU B 302     3277   2806   3802   -219    521   -303       N  
ATOM   3522  CA  GLU B 302      63.496  28.228  -3.405  1.00 30.63           C  
ANISOU 3522  CA  GLU B 302     3893   3368   4376   -213    567   -287       C  
ATOM   3523  C   GLU B 302      64.535  29.312  -3.731  1.00 35.99           C  
ANISOU 3523  C   GLU B 302     4572   4013   5089   -231    626   -315       C  
ATOM   3524  O   GLU B 302      64.747  29.634  -4.894  1.00 41.35           O  
ANISOU 3524  O   GLU B 302     5273   4671   5767   -229    668   -307       O  
ATOM   3525  CB  GLU B 302      62.096  28.756  -3.709  1.00 31.79           C  
ANISOU 3525  CB  GLU B 302     4076   3519   4484   -193    573   -244       C  
ATOM   3526  CG  GLU B 302      61.864  29.138  -5.163  1.00 46.52           C  
ANISOU 3526  CG  GLU B 302     5977   5367   6330   -182    615   -220       C  
ATOM   3527  CD  GLU B 302      60.511  29.806  -5.379  1.00 60.30           C  
ANISOU 3527  CD  GLU B 302     7757   7116   8039   -160    623   -179       C  
ATOM   3528  OE1 GLU B 302      60.128  30.032  -6.557  1.00 56.92           O  
ANISOU 3528  OE1 GLU B 302     7360   6681   7587   -145    651   -154       O  
ATOM   3529  OE2 GLU B 302      59.835  30.103  -4.364  1.00 52.98           O  
ANISOU 3529  OE2 GLU B 302     6826   6200   7106   -158    601   -173       O  
ATOM   3530  N   GLY B 303      65.167  29.878  -2.705  1.00 34.73           N  
ANISOU 3530  N   GLY B 303     4387   3849   4961   -248    629   -348       N  
ATOM   3531  CA  GLY B 303      66.149  30.940  -2.898  1.00 37.95           C  
ANISOU 3531  CA  GLY B 303     4791   4224   5406   -266    686   -380       C  
ATOM   3532  C   GLY B 303      65.547  32.325  -3.118  1.00 42.60           C  
ANISOU 3532  C   GLY B 303     5411   4788   5988   -262    736   -361       C  
ATOM   3533  O   GLY B 303      66.101  33.146  -3.845  1.00 40.87           O  
ANISOU 3533  O   GLY B 303     5206   4536   5788   -271    794   -369       O  
ATOM   3534  N   LYS B 304      64.409  32.596  -2.486  1.00 36.91           N  
ANISOU 3534  N   LYS B 304     4702   4082   5240   -249    714   -335       N  
ATOM   3535  CA  LYS B 304      63.765  33.904  -2.599  1.00 34.20           C  
ANISOU 3535  CA  LYS B 304     4387   3716   4890   -244    757   -316       C  
ATOM   3536  C   LYS B 304      63.785  34.640  -1.258  1.00 32.98           C  
ANISOU 3536  C   LYS B 304     4211   3563   4756   -257    754   -341       C  
ATOM   3537  O   LYS B 304      63.367  35.793  -1.153  1.00 30.45           O  
ANISOU 3537  O   LYS B 304     3908   3222   4439   -256    791   -333       O  
ATOM   3538  CB  LYS B 304      62.335  33.742  -3.115  1.00 36.62           C  
ANISOU 3538  CB  LYS B 304     4729   4036   5148   -216    742   -262       C  
ATOM   3539  CG  LYS B 304      62.245  32.958  -4.407  1.00 44.33           C  
ANISOU 3539  CG  LYS B 304     5726   5017   6102   -202    741   -238       C  
ATOM   3540  CD  LYS B 304      61.522  33.748  -5.488  1.00 55.74           C  
ANISOU 3540  CD  LYS B 304     7215   6443   7520   -182    785   -199       C  
ATOM   3541  CE  LYS B 304      60.012  33.639  -5.342  1.00 57.86           C  
ANISOU 3541  CE  LYS B 304     7504   6736   7746   -157    753   -158       C  
ATOM   3542  NZ  LYS B 304      59.290  34.550  -6.276  1.00 64.78           N  
ANISOU 3542  NZ  LYS B 304     8421   7595   8597   -136    796   -119       N  
ATOM   3543  N   ILE B 305      64.283  33.954  -0.237  1.00 32.37           N  
ANISOU 3543  N   ILE B 305     4096   3512   4693   -268    709   -372       N  
ATOM   3544  CA  ILE B 305      64.392  34.515   1.098  1.00 32.91           C  
ANISOU 3544  CA  ILE B 305     4138   3588   4778   -281    699   -401       C  
ATOM   3545  C   ILE B 305      65.777  34.185   1.636  1.00 37.23           C  
ANISOU 3545  C   ILE B 305     4641   4140   5364   -303    690   -456       C  
ATOM   3546  O   ILE B 305      66.230  33.042   1.544  1.00 33.48           O  
ANISOU 3546  O   ILE B 305     4149   3684   4888   -301    654   -461       O  
ATOM   3547  CB  ILE B 305      63.316  33.934   2.051  1.00 32.90           C  
ANISOU 3547  CB  ILE B 305     4134   3624   4743   -267    639   -379       C  
ATOM   3548  CG1 ILE B 305      61.919  34.361   1.614  1.00 31.82           C  
ANISOU 3548  CG1 ILE B 305     4037   3482   4570   -247    648   -329       C  
ATOM   3549  CG2 ILE B 305      63.561  34.371   3.484  1.00 35.77           C  
ANISOU 3549  CG2 ILE B 305     4466   4002   5124   -282    624   -414       C  
ATOM   3550  CD1 ILE B 305      60.811  33.828   2.522  1.00 32.51           C  
ANISOU 3550  CD1 ILE B 305     4123   3603   4625   -233    593   -307       C  
ATOM   3551  N   GLY B 306      66.446  35.186   2.198  1.00 37.31           N  
ANISOU 3551  N   GLY B 306     4633   4134   5410   -323    724   -496       N  
ATOM   3552  CA  GLY B 306      67.806  35.030   2.674  1.00 35.56           C  
ANISOU 3552  CA  GLY B 306     4367   3915   5228   -344    722   -553       C  
ATOM   3553  C   GLY B 306      67.995  34.014   3.780  1.00 36.83           C  
ANISOU 3553  C   GLY B 306     4491   4120   5381   -342    654   -570       C  
ATOM   3554  O   GLY B 306      67.235  33.968   4.750  1.00 42.60           O  
ANISOU 3554  O   GLY B 306     5219   4878   6090   -335    618   -559       O  
ATOM   3555  N   ARG B 307      69.020  33.192   3.631  1.00 35.96           N  
ANISOU 3555  N   ARG B 307     4354   4018   5291   -349    637   -596       N  
ATOM   3556  CA  ARG B 307      69.350  32.211   4.644  1.00 36.54           C  
ANISOU 3556  CA  ARG B 307     4391   4131   5361   -346    575   -614       C  
ATOM   3557  C   ARG B 307      70.849  32.174   4.847  1.00 37.33           C  
ANISOU 3557  C   ARG B 307     4448   4230   5505   -365    583   -672       C  
ATOM   3558  O   ARG B 307      71.618  32.434   3.925  1.00 42.26           O  
ANISOU 3558  O   ARG B 307     5075   4823   6158   -377    628   -690       O  
ATOM   3559  CB  ARG B 307      68.839  30.830   4.248  1.00 28.13           C  
ANISOU 3559  CB  ARG B 307     3338   3086   4265   -325    529   -573       C  
ATOM   3560  CG  ARG B 307      69.511  30.249   3.025  1.00 36.67           C  
ANISOU 3560  CG  ARG B 307     4424   4149   5360   -327    547   -573       C  
ATOM   3561  CD  ARG B 307      68.891  28.920   2.658  1.00 29.37           C  
ANISOU 3561  CD  ARG B 307     3511   3243   4404   -307    503   -533       C  
ATOM   3562  NE  ARG B 307      69.425  28.390   1.412  1.00 35.25           N  
ANISOU 3562  NE  ARG B 307     4265   3970   5160   -308    523   -531       N  
ATOM   3563  CZ  ARG B 307      70.473  27.581   1.337  1.00 27.21           C  
ANISOU 3563  CZ  ARG B 307     3216   2957   4166   -314    508   -559       C  
ATOM   3564  NH1 ARG B 307      71.105  27.214   2.439  1.00 30.50           N  
ANISOU 3564  NH1 ARG B 307     3592   3397   4599   -318    471   -590       N  
ATOM   3565  NH2 ARG B 307      70.886  27.143   0.161  1.00 42.35           N  
ANISOU 3565  NH2 ARG B 307     5143   4856   6091   -315    529   -555       N  
ATOM   3566  N   ALA B 308      71.260  31.847   6.061  1.00 38.67           N  
ANISOU 3566  N   ALA B 308     4579   4434   5680   -367    541   -703       N  
ATOM   3567  CA  ALA B 308      72.672  31.744   6.372  1.00 47.68           C  
ANISOU 3567  CA  ALA B 308     5675   5581   6862   -383    541   -761       C  
ATOM   3568  C   ALA B 308      73.281  30.641   5.522  1.00 50.19           C  
ANISOU 3568  C   ALA B 308     5988   5894   7187   -378    529   -755       C  
ATOM   3569  O   ALA B 308      72.730  29.546   5.419  1.00 51.14           O  
ANISOU 3569  O   ALA B 308     6120   6034   7279   -359    486   -717       O  
ATOM   3570  CB  ALA B 308      72.874  31.454   7.848  1.00 48.23           C  
ANISOU 3570  CB  ALA B 308     5704   5694   6926   -381    488   -788       C  
ATOM   3571  N   VAL B 309      74.415  30.934   4.901  1.00 48.05           N  
ANISOU 3571  N   VAL B 309     5702   5598   6958   -396    569   -795       N  
ATOM   3572  CA  VAL B 309      75.121  29.931   4.112  1.00 56.23           C  
ANISOU 3572  CA  VAL B 309     6730   6629   8007   -393    561   -796       C  
ATOM   3573  C   VAL B 309      76.623  29.971   4.412  1.00 58.87           C  
ANISOU 3573  C   VAL B 309     7015   6965   8389   -411    568   -862       C  
ATOM   3574  O   VAL B 309      77.178  31.037   4.667  1.00 61.82           O  
ANISOU 3574  O   VAL B 309     7372   7323   8794   -431    607   -905       O  
ATOM   3575  CB  VAL B 309      74.852  30.130   2.608  1.00 53.03           C  
ANISOU 3575  CB  VAL B 309     6367   6185   7598   -394    611   -766       C  
ATOM   3576  CG1 VAL B 309      76.071  29.764   1.777  1.00 57.42           C  
ANISOU 3576  CG1 VAL B 309     6905   6720   8190   -406    635   -797       C  
ATOM   3577  CG2 VAL B 309      73.630  29.325   2.189  1.00 50.90           C  
ANISOU 3577  CG2 VAL B 309     6134   5926   7281   -370    580   -703       C  
ATOM   3578  N   VAL B 310      77.267  28.810   4.375  1.00 57.02           N  
ANISOU 3578  N   VAL B 310     6755   6748   8162   -404    531   -870       N  
ATOM   3579  CA  VAL B 310      78.698  28.724   4.631  1.00 58.74           C  
ANISOU 3579  CA  VAL B 310     6923   6969   8425   -419    532   -931       C  
ATOM   3580  C   VAL B 310      79.490  29.546   3.623  1.00 64.93           C  
ANISOU 3580  C   VAL B 310     7712   7707   9250   -443    604   -963       C  
ATOM   3581  O   VAL B 310      79.119  29.642   2.454  1.00 65.11           O  
ANISOU 3581  O   VAL B 310     7774   7698   9265   -443    642   -931       O  
ATOM   3582  CB  VAL B 310      79.198  27.273   4.575  1.00 54.11           C  
ANISOU 3582  CB  VAL B 310     6316   6405   7841   -405    484   -927       C  
ATOM   3583  CG1 VAL B 310      80.535  27.149   5.279  1.00 51.92           C  
ANISOU 3583  CG1 VAL B 310     5980   6146   7603   -414    467   -991       C  
ATOM   3584  CG2 VAL B 310      78.175  26.333   5.191  1.00 62.86           C  
ANISOU 3584  CG2 VAL B 310     7436   7547   8903   -378    422   -877       C  
ATOM   3585  N   GLY B 311      80.590  30.130   4.086  1.00112.24           N  
ANISOU 3585  N   GLY B 311    13662  13698  15286   -463    623  -1028       N  
ATOM   3586  CA  GLY B 311      81.460  30.912   3.227  1.00113.50           C  
ANISOU 3586  CA  GLY B 311    13820  13814  15491   -488    693  -1066       C  
ATOM   3587  C   GLY B 311      80.901  32.289   2.948  1.00113.49           C  
ANISOU 3587  C   GLY B 311    13852  13779  15490   -500    755  -1058       C  
ATOM   3588  O   GLY B 311      81.553  33.124   2.323  1.00113.74           O  
ANISOU 3588  O   GLY B 311    13885  13772  15560   -521    820  -1089       O  
ATOM   3589  N   SER B 312      79.681  32.526   3.416  1.00127.87           N  
ANISOU 3589  N   SER B 312    15700  15613  17270   -486    736  -1016       N  
ATOM   3590  CA  SER B 312      79.029  33.808   3.216  1.00133.55           C  
ANISOU 3590  CA  SER B 312    16453  16303  17988   -494    790  -1003       C  
ATOM   3591  C   SER B 312      78.551  34.389   4.536  1.00135.08           C  
ANISOU 3591  C   SER B 312    16630  16523  18170   -494    767  -1016       C  
ATOM   3592  O   SER B 312      77.822  33.745   5.286  1.00140.84           O  
ANISOU 3592  O   SER B 312    17360  17292  18862   -475    707   -988       O  
ATOM   3593  CB  SER B 312      77.852  33.666   2.251  1.00 80.43           C  
ANISOU 3593  CB  SER B 312     9784   9557  11218   -476    802   -931       C  
ATOM   3594  OG  SER B 312      77.899  34.658   1.242  1.00 79.93           O  
ANISOU 3594  OG  SER B 312     9752   9444  11172   -488    878   -926       O  
ATOM   3595  N   SER B 313      78.977  35.613   4.814  1.00164.29           N  
ANISOU 3595  N   SER B 313    20315  20201  21905   -517    818  -1062       N  
ATOM   3596  CA  SER B 313      78.515  36.335   5.984  1.00172.30           C  
ANISOU 3596  CA  SER B 313    21317  21237  22913   -520    806  -1078       C  
ATOM   3597  C   SER B 313      77.671  37.500   5.500  1.00177.23           C  
ANISOU 3597  C   SER B 313    21986  21820  23533   -524    867  -1049       C  
ATOM   3598  O   SER B 313      78.199  38.489   4.993  1.00185.93           O  
ANISOU 3598  O   SER B 313    23089  22880  24675   -545    937  -1078       O  
ATOM   3599  CB  SER B 313      79.698  36.837   6.811  1.00105.50           C  
ANISOU 3599  CB  SER B 313    12799  12788  14500   -543    815  -1160       C  
ATOM   3600  OG  SER B 313      80.114  38.120   6.379  1.00106.00           O  
ANISOU 3600  OG  SER B 313    12865  12804  14607   -569    895  -1194       O  
ATOM   3601  N   ASP B 314      76.356  37.367   5.628  1.00102.84           N  
ANISOU 3601  N   ASP B 314    12600  12411  14063   -503    841   -990       N  
ATOM   3602  CA  ASP B 314      75.760  36.204   6.272  1.00106.89           C  
ANISOU 3602  CA  ASP B 314    13109  12973  14532   -480    761   -958       C  
ATOM   3603  C   ASP B 314      74.572  35.597   5.515  1.00 95.60           C  
ANISOU 3603  C   ASP B 314    11730  11539  13054   -455    744   -882       C  
ATOM   3604  O   ASP B 314      74.651  34.445   5.066  1.00 90.34           O  
ANISOU 3604  O   ASP B 314    11066  10886  12371   -441    710   -859       O  
ATOM   3605  CB  ASP B 314      75.386  36.512   7.721  1.00106.98           C  
ANISOU 3605  CB  ASP B 314    13096  13022  14530   -480    725   -977       C  
ATOM   3606  CG  ASP B 314      75.394  35.272   8.592  1.00110.80           C  
ANISOU 3606  CG  ASP B 314    13554  13560  14987   -463    644   -973       C  
ATOM   3607  OD1 ASP B 314      76.167  34.337   8.284  1.00104.90           O  
ANISOU 3607  OD1 ASP B 314    12786  12821  14248   -459    620   -983       O  
ATOM   3608  OD2 ASP B 314      74.629  35.233   9.581  1.00110.28           O  
ANISOU 3608  OD2 ASP B 314    13486  13527  14889   -452    604   -959       O  
ATOM   3609  N   LYS B 315      73.484  36.356   5.376  1.00 56.29           N  
ANISOU 3609  N   LYS B 315     6790   6544   8054   -449    770   -844       N  
ATOM   3610  CA  LYS B 315      72.270  35.837   4.732  1.00 59.52           C  
ANISOU 3610  CA  LYS B 315     7245   6954   8415   -424    752   -774       C  
ATOM   3611  C   LYS B 315      72.231  36.101   3.228  1.00 56.37           C  
ANISOU 3611  C   LYS B 315     6886   6511   8020   -422    808   -745       C  
ATOM   3612  O   LYS B 315      72.366  37.241   2.791  1.00 61.79           O  
ANISOU 3612  O   LYS B 315     7588   7159   8731   -434    873   -755       O  
ATOM   3613  CB  LYS B 315      71.002  36.397   5.388  1.00 52.80           C  
ANISOU 3613  CB  LYS B 315     6416   6113   7534   -414    742   -743       C  
ATOM   3614  CG  LYS B 315      70.700  35.839   6.772  1.00 48.90           C  
ANISOU 3614  CG  LYS B 315     5893   5668   7017   -407    676   -751       C  
ATOM   3615  CD  LYS B 315      69.292  36.206   7.205  1.00 39.11           C  
ANISOU 3615  CD  LYS B 315     4683   4437   5741   -393    664   -709       C  
ATOM   3616  CE  LYS B 315      68.916  35.484   8.493  1.00 52.34           C  
ANISOU 3616  CE  LYS B 315     6336   6163   7389   -383    595   -709       C  
ATOM   3617  NZ  LYS B 315      67.434  35.327   8.640  1.00 57.96           N  
ANISOU 3617  NZ  LYS B 315     7082   6887   8056   -363    570   -653       N  
ATOM   3618  N   VAL B 316      72.026  35.045   2.442  1.00 49.99           N  
ANISOU 3618  N   VAL B 316     6096   5710   7188   -406    783   -709       N  
ATOM   3619  CA  VAL B 316      72.018  35.170   0.982  1.00 45.80           C  
ANISOU 3619  CA  VAL B 316     5602   5144   6656   -402    831   -682       C  
ATOM   3620  C   VAL B 316      70.913  34.346   0.305  1.00 48.29           C  
ANISOU 3620  C   VAL B 316     5955   5472   6922   -376    800   -619       C  
ATOM   3621  O   VAL B 316      70.387  33.385   0.883  1.00 38.78           O  
ANISOU 3621  O   VAL B 316     4742   4305   5689   -362    737   -601       O  
ATOM   3622  CB  VAL B 316      73.390  34.804   0.371  1.00 51.46           C  
ANISOU 3622  CB  VAL B 316     6295   5845   7412   -418    852   -722       C  
ATOM   3623  CG1 VAL B 316      74.499  35.608   1.037  1.00 58.05           C  
ANISOU 3623  CG1 VAL B 316     7090   6669   8299   -445    882   -789       C  
ATOM   3624  CG2 VAL B 316      73.666  33.327   0.517  1.00 42.76           C  
ANISOU 3624  CG2 VAL B 316     5170   4778   6297   -409    788   -721       C  
ATOM   3625  N   LEU B 317      70.563  34.739  -0.919  1.00 49.88           N  
ANISOU 3625  N   LEU B 317     6197   5643   7112   -368    847   -586       N  
ATOM   3626  CA  LEU B 317      69.547  34.045  -1.695  1.00 47.18           C  
ANISOU 3626  CA  LEU B 317     5890   5312   6723   -343    825   -530       C  
ATOM   3627  C   LEU B 317      70.167  32.855  -2.419  1.00 51.28           C  
ANISOU 3627  C   LEU B 317     6402   5840   7244   -342    805   -533       C  
ATOM   3628  O   LEU B 317      71.015  33.031  -3.296  1.00 51.98           O  
ANISOU 3628  O   LEU B 317     6492   5900   7357   -353    850   -550       O  
ATOM   3629  CB  LEU B 317      68.903  35.000  -2.703  1.00 42.01           C  
ANISOU 3629  CB  LEU B 317     5284   4625   6054   -334    883   -493       C  
ATOM   3630  CG  LEU B 317      67.549  35.606  -2.324  1.00 50.43           C  
ANISOU 3630  CG  LEU B 317     6377   5696   7087   -317    877   -454       C  
ATOM   3631  CD1 LEU B 317      67.508  35.993  -0.855  1.00 48.35           C  
ANISOU 3631  CD1 LEU B 317     6083   5448   6838   -328    854   -483       C  
ATOM   3632  CD2 LEU B 317      67.204  36.800  -3.219  1.00 44.81           C  
ANISOU 3632  CD2 LEU B 317     5706   4946   6375   -311    947   -429       C  
ATOM   3633  N   GLU B 318      69.744  31.649  -2.052  1.00 38.58           N  
ANISOU 3633  N   GLU B 318     4782   4267   5610   -329    741   -517       N  
ATOM   3634  CA  GLU B 318      70.281  30.429  -2.664  1.00 40.75           C  
ANISOU 3634  CA  GLU B 318     5045   4550   5886   -327    718   -520       C  
ATOM   3635  C   GLU B 318      69.440  29.172  -2.399  1.00 34.64           C  
ANISOU 3635  C   GLU B 318     4272   3813   5076   -307    653   -488       C  
ATOM   3636  O   GLU B 318      69.259  28.771  -1.247  1.00 32.96           O  
ANISOU 3636  O   GLU B 318     4036   3628   4860   -305    605   -495       O  
ATOM   3637  CB  GLU B 318      71.704  30.174  -2.170  1.00 33.83           C  
ANISOU 3637  CB  GLU B 318     4123   3674   5056   -347    714   -576       C  
ATOM   3638  CG  GLU B 318      72.420  29.099  -2.954  1.00 50.16           C  
ANISOU 3638  CG  GLU B 318     6180   5743   7134   -349    705   -584       C  
ATOM   3639  CD  GLU B 318      73.791  28.809  -2.400  1.00 61.46           C  
ANISOU 3639  CD  GLU B 318     7563   7177   8611   -367    696   -640       C  
ATOM   3640  OE1 GLU B 318      74.018  27.667  -1.946  1.00 67.99           O  
ANISOU 3640  OE1 GLU B 318     8363   8031   9437   -361    643   -646       O  
ATOM   3641  OE2 GLU B 318      74.639  29.726  -2.415  1.00 68.22           O  
ANISOU 3641  OE2 GLU B 318     8407   8008   9504   -387    743   -679       O  
ATOM   3642  N   ALA B 319      68.964  28.551  -3.475  1.00 28.93           N  
ANISOU 3642  N   ALA B 319     3575   3090   4327   -294    653   -455       N  
ATOM   3643  CA  ALA B 319      68.184  27.316  -3.418  1.00 30.44           C  
ANISOU 3643  CA  ALA B 319     3769   3312   4487   -276    598   -426       C  
ATOM   3644  C   ALA B 319      68.866  26.224  -2.609  1.00 30.00           C  
ANISOU 3644  C   ALA B 319     3670   3277   4450   -280    548   -452       C  
ATOM   3645  O   ALA B 319      70.035  25.930  -2.834  1.00 35.60           O  
ANISOU 3645  O   ALA B 319     4355   3978   5193   -294    559   -486       O  
ATOM   3646  CB  ALA B 319      67.909  26.815  -4.839  1.00 30.74           C  
ANISOU 3646  CB  ALA B 319     3834   3343   4504   -266    613   -400       C  
ATOM   3647  N   VAL B 320      68.149  25.607  -1.668  1.00 33.34           N  
ANISOU 3647  N   VAL B 320     4084   3730   4853   -268    496   -436       N  
ATOM   3648  CA  VAL B 320      68.746  24.487  -0.934  1.00 31.49           C  
ANISOU 3648  CA  VAL B 320     3812   3519   4635   -269    448   -455       C  
ATOM   3649  C   VAL B 320      68.639  23.138  -1.683  1.00 33.96           C  
ANISOU 3649  C   VAL B 320     4126   3838   4938   -259    424   -437       C  
ATOM   3650  O   VAL B 320      69.307  22.167  -1.327  1.00 31.13           O  
ANISOU 3650  O   VAL B 320     3736   3491   4599   -259    393   -455       O  
ATOM   3651  CB  VAL B 320      68.246  24.355   0.550  1.00 36.36           C  
ANISOU 3651  CB  VAL B 320     4411   4164   5240   -262    401   -451       C  
ATOM   3652  CG1 VAL B 320      67.514  25.623   1.023  1.00 31.74           C  
ANISOU 3652  CG1 VAL B 320     3845   3574   4639   -262    421   -442       C  
ATOM   3653  CG2 VAL B 320      67.407  23.106   0.745  1.00 27.41           C  
ANISOU 3653  CG2 VAL B 320     3281   3055   4079   -243    351   -418       C  
ATOM   3654  N   ALA B 321      67.825  23.096  -2.733  1.00 23.75           N  
ANISOU 3654  N   ALA B 321     2868   2539   3617   -249    441   -405       N  
ATOM   3655  CA  ALA B 321      67.662  21.874  -3.516  1.00 26.66           C  
ANISOU 3655  CA  ALA B 321     3239   2915   3976   -240    423   -391       C  
ATOM   3656  C   ALA B 321      67.160  22.199  -4.918  1.00 22.99           C  
ANISOU 3656  C   ALA B 321     2812   2436   3489   -235    461   -369       C  
ATOM   3657  O   ALA B 321      66.693  23.300  -5.163  1.00 23.66           O  
ANISOU 3657  O   ALA B 321     2923   2509   3558   -233    493   -355       O  
ATOM   3658  CB  ALA B 321      66.713  20.893  -2.798  1.00 24.72           C  
ANISOU 3658  CB  ALA B 321     2988   2697   3706   -224    368   -365       C  
ATOM   3659  N   SER B 322      67.259  21.240  -5.835  1.00 29.13           N  
ANISOU 3659  N   SER B 322     3590   3215   4263   -232    457   -365       N  
ATOM   3660  CA  SER B 322      66.822  21.463  -7.208  1.00 28.12           C  
ANISOU 3660  CA  SER B 322     3495   3078   4110   -226    491   -346       C  
ATOM   3661  C   SER B 322      65.302  21.562  -7.248  1.00 31.72           C  
ANISOU 3661  C   SER B 322     3980   3551   4520   -206    475   -305       C  
ATOM   3662  O   SER B 322      64.631  21.209  -6.286  1.00 25.42           O  
ANISOU 3662  O   SER B 322     3174   2772   3713   -198    435   -293       O  
ATOM   3663  CB  SER B 322      67.300  20.330  -8.128  1.00 44.49           C  
ANISOU 3663  CB  SER B 322     5559   5152   6192   -228    487   -355       C  
ATOM   3664  OG  SER B 322      66.402  19.228  -8.091  1.00 42.56           O  
ANISOU 3664  OG  SER B 322     5314   4931   5924   -213    445   -333       O  
ATOM   3665  N   GLU B 323      64.763  22.016  -8.374  1.00 33.95           N  
ANISOU 3665  N   GLU B 323     4296   3828   4775   -197    507   -284       N  
ATOM   3666  CA  GLU B 323      63.363  22.402  -8.446  1.00 35.57           C  
ANISOU 3666  CA  GLU B 323     4531   4047   4938   -177    500   -247       C  
ATOM   3667  C   GLU B 323      62.355  21.264  -8.330  1.00 33.02           C  
ANISOU 3667  C   GLU B 323     4205   3752   4590   -163    453   -227       C  
ATOM   3668  O   GLU B 323      61.154  21.517  -8.191  1.00 29.34           O  
ANISOU 3668  O   GLU B 323     3758   3300   4091   -147    440   -199       O  
ATOM   3669  CB  GLU B 323      63.088  23.219  -9.716  1.00 34.99           C  
ANISOU 3669  CB  GLU B 323     4495   3961   4840   -169    548   -229       C  
ATOM   3670  CG  GLU B 323      63.223  22.456 -11.018  1.00 46.44           C  
ANISOU 3670  CG  GLU B 323     5952   5415   6276   -165    557   -228       C  
ATOM   3671  CD  GLU B 323      62.743  23.264 -12.225  1.00 54.52           C  
ANISOU 3671  CD  GLU B 323     7016   6434   7266   -151    600   -204       C  
ATOM   3672  OE1 GLU B 323      62.098  24.319 -12.029  1.00 53.20           O  
ANISOU 3672  OE1 GLU B 323     6872   6261   7081   -140    616   -181       O  
ATOM   3673  OE2 GLU B 323      63.013  22.842 -13.372  1.00 57.34           O  
ANISOU 3673  OE2 GLU B 323     7381   6792   7614   -149    617   -206       O  
ATOM   3674  N   THR B 324      62.828  20.023  -8.388  1.00 22.74           N  
ANISOU 3674  N   THR B 324     2877   2458   3304   -168    427   -243       N  
ATOM   3675  CA  THR B 324      61.923  18.886  -8.397  1.00 28.15           C  
ANISOU 3675  CA  THR B 324     3558   3167   3969   -156    388   -227       C  
ATOM   3676  C   THR B 324      61.914  18.161  -7.060  1.00 28.85           C  
ANISOU 3676  C   THR B 324     3619   3267   4076   -158    343   -232       C  
ATOM   3677  O   THR B 324      61.325  17.090  -6.943  1.00 28.89           O  
ANISOU 3677  O   THR B 324     3614   3288   4073   -150    309   -223       O  
ATOM   3678  CB  THR B 324      62.286  17.842  -9.481  1.00 34.48           C  
ANISOU 3678  CB  THR B 324     4353   3971   4775   -158    390   -238       C  
ATOM   3679  OG1 THR B 324      63.611  17.349  -9.241  1.00 29.96           O  
ANISOU 3679  OG1 THR B 324     3752   3386   4247   -175    390   -269       O  
ATOM   3680  CG2 THR B 324      62.211  18.441 -10.878  1.00 33.19           C  
ANISOU 3680  CG2 THR B 324     4221   3802   4589   -153    433   -230       C  
ATOM   3681  N   VAL B 325      62.574  18.709  -6.051  1.00 20.32           N  
ANISOU 3681  N   VAL B 325     2523   2178   3020   -168    342   -247       N  
ATOM   3682  CA  VAL B 325      62.542  18.040  -4.756  1.00 21.24           C  
ANISOU 3682  CA  VAL B 325     2613   2308   3149   -167    298   -250       C  
ATOM   3683  C   VAL B 325      61.628  18.756  -3.764  1.00 17.49           C  
ANISOU 3683  C   VAL B 325     2149   1843   2654   -159    285   -231       C  
ATOM   3684  O   VAL B 325      61.618  19.984  -3.680  1.00 21.79           O  
ANISOU 3684  O   VAL B 325     2708   2377   3194   -163    312   -231       O  
ATOM   3685  CB  VAL B 325      63.963  17.702  -4.205  1.00 27.26           C  
ANISOU 3685  CB  VAL B 325     3341   3062   3955   -181    293   -283       C  
ATOM   3686  CG1 VAL B 325      65.002  18.641  -4.768  1.00 36.15           C  
ANISOU 3686  CG1 VAL B 325     4469   4166   5102   -196    338   -308       C  
ATOM   3687  CG2 VAL B 325      63.995  17.626  -2.670  1.00 20.23           C  
ANISOU 3687  CG2 VAL B 325     2428   2184   3073   -180    258   -286       C  
ATOM   3688  N   GLY B 326      60.822  17.979  -3.054  1.00 21.41           N  
ANISOU 3688  N   GLY B 326     2639   2359   3138   -149    245   -214       N  
ATOM   3689  CA  GLY B 326      59.901  18.556  -2.089  1.00 20.66           C  
ANISOU 3689  CA  GLY B 326     2553   2274   3023   -142    231   -196       C  
ATOM   3690  C   GLY B 326      59.772  17.693  -0.856  1.00 20.99           C  
ANISOU 3690  C   GLY B 326     2572   2332   3072   -138    187   -193       C  
ATOM   3691  O   GLY B 326      60.506  16.716  -0.704  1.00 21.64           O  
ANISOU 3691  O   GLY B 326     2629   2415   3177   -141    169   -207       O  
ATOM   3692  N   SER B 327      58.830  18.049   0.017  1.00 18.04           N  
ANISOU 3692  N   SER B 327     2206   1971   2678   -131    170   -175       N  
ATOM   3693  CA  SER B 327      58.577  17.287   1.220  1.00 16.75           C  
ANISOU 3693  CA  SER B 327     2025   1824   2516   -125    130   -169       C  
ATOM   3694  C   SER B 327      57.216  17.652   1.821  1.00 18.95           C  
ANISOU 3694  C   SER B 327     2321   2114   2763   -115    117   -143       C  
ATOM   3695  O   SER B 327      56.795  18.809   1.747  1.00 18.28           O  
ANISOU 3695  O   SER B 327     2256   2026   2665   -116    139   -138       O  
ATOM   3696  CB  SER B 327      59.663  17.577   2.241  1.00 19.37           C  
ANISOU 3696  CB  SER B 327     2331   2156   2872   -135    123   -193       C  
ATOM   3697  OG  SER B 327      59.490  16.792   3.401  1.00 20.00           O  
ANISOU 3697  OG  SER B 327     2393   2253   2952   -128     85   -186       O  
ATOM   3698  N   THR B 328      56.534  16.673   2.418  1.00 17.08           N  
ANISOU 3698  N   THR B 328     2078   1893   2520   -106     84   -127       N  
ATOM   3699  CA  THR B 328      55.400  16.981   3.277  1.00 18.20           C  
ANISOU 3699  CA  THR B 328     2230   2047   2637    -98     69   -106       C  
ATOM   3700  C   THR B 328      55.938  17.534   4.583  1.00 23.11           C  
ANISOU 3700  C   THR B 328     2837   2674   3267   -104     59   -118       C  
ATOM   3701  O   THR B 328      57.107  17.360   4.908  1.00 19.37           O  
ANISOU 3701  O   THR B 328     2342   2200   2819   -111     56   -140       O  
ATOM   3702  CB  THR B 328      54.583  15.737   3.683  1.00 19.41           C  
ANISOU 3702  CB  THR B 328     2379   2214   2784    -88     37    -87       C  
ATOM   3703  OG1 THR B 328      55.348  14.979   4.626  1.00 23.77           O  
ANISOU 3703  OG1 THR B 328     2905   2772   3356    -88     13    -95       O  
ATOM   3704  CG2 THR B 328      54.211  14.875   2.482  1.00 17.57           C  
ANISOU 3704  CG2 THR B 328     2151   1978   2549    -83     41    -82       C  
ATOM   3705  N   ALA B 329      55.072  18.180   5.347  1.00 17.35           N  
ANISOU 3705  N   ALA B 329     2120   1954   2518   -101     54   -105       N  
ATOM   3706  CA  ALA B 329      55.416  18.510   6.717  1.00 20.98           C  
ANISOU 3706  CA  ALA B 329     2563   2425   2981   -104     38   -115       C  
ATOM   3707  C   ALA B 329      54.167  18.385   7.563  1.00 17.73           C  
ANISOU 3707  C   ALA B 329     2162   2030   2546    -95     17    -91       C  
ATOM   3708  O   ALA B 329      53.156  19.028   7.291  1.00 19.08           O  
ANISOU 3708  O   ALA B 329     2356   2199   2697    -91     29    -76       O  
ATOM   3709  CB  ALA B 329      56.011  19.930   6.824  1.00 15.68           C  
ANISOU 3709  CB  ALA B 329     1894   1745   2318   -116     67   -136       C  
ATOM   3710  N   VAL B 330      54.235  17.540   8.576  1.00 17.20           N  
ANISOU 3710  N   VAL B 330     2078   1977   2480    -89    -14    -86       N  
ATOM   3711  CA  VAL B 330      53.207  17.536   9.596  1.00 16.57           C  
ANISOU 3711  CA  VAL B 330     2005   1913   2379    -82    -33    -67       C  
ATOM   3712  C   VAL B 330      53.889  17.902  10.919  1.00 20.28           C  
ANISOU 3712  C   VAL B 330     2455   2397   2852    -86    -47    -82       C  
ATOM   3713  O   VAL B 330      54.910  17.312  11.281  1.00 19.28           O  
ANISOU 3713  O   VAL B 330     2306   2277   2743    -86    -62    -95       O  
ATOM   3714  CB  VAL B 330      52.458  16.189   9.659  1.00 14.96           C  
ANISOU 3714  CB  VAL B 330     1802   1715   2169    -70    -57    -43       C  
ATOM   3715  CG1 VAL B 330      53.365  15.076  10.193  1.00 16.67           C  
ANISOU 3715  CG1 VAL B 330     1993   1937   2404    -66    -80    -47       C  
ATOM   3716  CG2 VAL B 330      51.197  16.316  10.481  1.00 14.58           C  
ANISOU 3716  CG2 VAL B 330     1766   1679   2096    -64    -68    -22       C  
ATOM   3717  N   VAL B 331      53.357  18.922  11.593  1.00 12.91           N  
ANISOU 3717  N   VAL B 331     1531   1471   1903    -90    -41    -82       N  
ATOM   3718  CA  VAL B 331      53.939  19.429  12.826  1.00 18.10           C  
ANISOU 3718  CA  VAL B 331     2171   2145   2561    -94    -52   -101       C  
ATOM   3719  C   VAL B 331      52.875  19.503  13.905  1.00 17.63           C  
ANISOU 3719  C   VAL B 331     2120   2102   2476    -88    -69    -82       C  
ATOM   3720  O   VAL B 331      51.768  19.969  13.659  1.00 18.93           O  
ANISOU 3720  O   VAL B 331     2307   2262   2625    -87    -57    -66       O  
ATOM   3721  CB  VAL B 331      54.520  20.865  12.653  1.00 19.30           C  
ANISOU 3721  CB  VAL B 331     2323   2287   2724   -109    -21   -129       C  
ATOM   3722  CG1 VAL B 331      54.924  21.440  14.005  1.00 21.60           C  
ANISOU 3722  CG1 VAL B 331     2597   2599   3012   -115    -32   -149       C  
ATOM   3723  CG2 VAL B 331      55.718  20.866  11.713  1.00 16.27           C  
ANISOU 3723  CG2 VAL B 331     1929   1887   2368   -117     -2   -152       C  
ATOM   3724  N   ALA B 332      53.222  19.071  15.106  1.00 17.62           N  
ANISOU 3724  N   ALA B 332     2101   2123   2471    -84    -96    -85       N  
ATOM   3725  CA  ALA B 332      52.330  19.223  16.251  1.00 17.35           C  
ANISOU 3725  CA  ALA B 332     2073   2108   2412    -79   -111    -71       C  
ATOM   3726  C   ALA B 332      53.046  19.921  17.381  1.00 18.73           C  
ANISOU 3726  C   ALA B 332     2229   2304   2585    -85   -117    -96       C  
ATOM   3727  O   ALA B 332      54.217  19.643  17.663  1.00 21.63           O  
ANISOU 3727  O   ALA B 332     2572   2681   2967    -85   -129   -116       O  
ATOM   3728  CB  ALA B 332      51.822  17.891  16.725  1.00 13.94           C  
ANISOU 3728  CB  ALA B 332     1641   1687   1970    -64   -138    -42       C  
ATOM   3729  N   LEU B 333      52.320  20.825  18.020  1.00 20.41           N  
ANISOU 3729  N   LEU B 333     2451   2524   2780    -90   -111    -97       N  
ATOM   3730  CA  LEU B 333      52.742  21.502  19.240  1.00 20.77           C  
ANISOU 3730  CA  LEU B 333     2480   2593   2818    -96   -119   -120       C  
ATOM   3731  C   LEU B 333      51.863  20.984  20.361  1.00 20.97           C  
ANISOU 3731  C   LEU B 333     2511   2642   2816    -85   -144    -96       C  
ATOM   3732  O   LEU B 333      50.642  21.042  20.262  1.00 26.16           O  
ANISOU 3732  O   LEU B 333     3190   3291   3458    -83   -138    -73       O  
ATOM   3733  CB  LEU B 333      52.461  22.985  19.109  1.00 22.48           C  
ANISOU 3733  CB  LEU B 333     2706   2799   3036   -111    -87   -139       C  
ATOM   3734  CG  LEU B 333      53.598  23.934  18.764  1.00 39.66           C  
ANISOU 3734  CG  LEU B 333     4866   4965   5237   -126    -63   -179       C  
ATOM   3735  CD1 LEU B 333      54.434  23.342  17.648  1.00 30.91           C  
ANISOU 3735  CD1 LEU B 333     3753   3838   4152   -125    -57   -182       C  
ATOM   3736  CD2 LEU B 333      53.022  25.299  18.390  1.00 26.65           C  
ANISOU 3736  CD2 LEU B 333     3237   3298   3592   -139    -26   -186       C  
ATOM   3737  N   VAL B 334      52.467  20.490  21.428  1.00 13.19           N  
ANISOU 3737  N   VAL B 334     1505   1685   1823    -77   -171   -102       N  
ATOM   3738  CA  VAL B 334      51.691  19.981  22.552  1.00 14.19           C  
ANISOU 3738  CA  VAL B 334     1637   1835   1922    -65   -194    -78       C  
ATOM   3739  C   VAL B 334      51.961  20.827  23.788  1.00 17.94           C  
ANISOU 3739  C   VAL B 334     2097   2339   2380    -71   -201   -103       C  
ATOM   3740  O   VAL B 334      53.112  21.060  24.161  1.00 18.96           O  
ANISOU 3740  O   VAL B 334     2201   2485   2518    -74   -208   -134       O  
ATOM   3741  CB  VAL B 334      52.053  18.526  22.863  1.00 16.25           C  
ANISOU 3741  CB  VAL B 334     1887   2106   2180    -46   -223    -57       C  
ATOM   3742  CG1 VAL B 334      51.285  18.031  24.088  1.00 16.82           C  
ANISOU 3742  CG1 VAL B 334     1965   2202   2222    -34   -245    -32       C  
ATOM   3743  CG2 VAL B 334      51.775  17.645  21.648  1.00 14.07           C  
ANISOU 3743  CG2 VAL B 334     1623   1801   1921    -42   -216    -35       C  
ATOM   3744  N   CYS B 335      50.909  21.334  24.405  1.00 16.54           N  
ANISOU 3744  N   CYS B 335     1935   2169   2182    -74   -197    -94       N  
ATOM   3745  CA  CYS B 335      51.086  21.955  25.705  1.00 17.91           C  
ANISOU 3745  CA  CYS B 335     2094   2375   2336    -78   -207   -115       C  
ATOM   3746  C   CYS B 335      50.032  21.377  26.630  1.00 23.93           C  
ANISOU 3746  C   CYS B 335     2871   3155   3068    -66   -225    -83       C  
ATOM   3747  O   CYS B 335      49.316  20.449  26.255  1.00 22.96           O  
ANISOU 3747  O   CYS B 335     2764   3017   2941    -55   -230    -47       O  
ATOM   3748  CB  CYS B 335      50.979  23.473  25.617  1.00 22.95           C  
ANISOU 3748  CB  CYS B 335     2734   3005   2981    -98   -178   -146       C  
ATOM   3749  SG  CYS B 335      49.368  24.086  25.010  1.00 25.15           S  
ANISOU 3749  SG  CYS B 335     3047   3253   3254   -105   -150   -122       S  
ATOM   3750  N  ASER B 336      49.958  21.920  27.837  0.47 18.90           N  
ANISOU 3750  N  ASER B 336     2226   2549   2408    -68   -234    -97       N  
ATOM   3751  N  BSER B 336      49.961  21.889  27.851  0.53 18.91           N  
ANISOU 3751  N  BSER B 336     2226   2550   2408    -68   -234    -96       N  
ATOM   3752  CA ASER B 336      49.092  21.401  28.888  0.47 25.58           C  
ANISOU 3752  CA ASER B 336     3082   3417   3222    -57   -251    -70       C  
ATOM   3753  CA BSER B 336      49.073  21.317  28.854  0.53 25.56           C  
ANISOU 3753  CA BSER B 336     3080   3412   3219    -55   -252    -67       C  
ATOM   3754  C  ASER B 336      47.619  21.393  28.460  0.47 27.76           C  
ANISOU 3754  C  ASER B 336     3387   3666   3492    -59   -235    -40       C  
ATOM   3755  C  BSER B 336      47.597  21.389  28.467  0.53 27.75           C  
ANISOU 3755  C  BSER B 336     3387   3666   3492    -59   -235    -40       C  
ATOM   3756  O  ASER B 336      46.884  20.435  28.712  0.47 21.28           O  
ANISOU 3756  O  ASER B 336     2580   2846   2658    -45   -247     -5       O  
ATOM   3757  O  BSER B 336      46.834  20.477  28.765  0.53 21.30           O  
ANISOU 3757  O  BSER B 336     2584   2850   2660    -46   -247     -5       O  
ATOM   3758  CB ASER B 336      49.259  22.270  30.138  0.47 33.44           C  
ANISOU 3758  CB ASER B 336     4063   4448   4196    -64   -257    -98       C  
ATOM   3759  CB BSER B 336      49.298  21.972  30.217  0.53 33.49           C  
ANISOU 3759  CB BSER B 336     4069   4457   4199    -59   -263    -92       C  
ATOM   3760  OG ASER B 336      49.117  21.500  31.317  0.47 49.55           O  
ANISOU 3760  OG ASER B 336     6101   6522   6204    -46   -285    -79       O  
ATOM   3761  OG BSER B 336      48.955  23.343  30.184  0.53 48.94           O  
ANISOU 3761  OG BSER B 336     6028   6406   6160    -80   -237   -120       O  
ATOM   3762  N   SER B 337      47.198  22.468  27.799  1.00 26.10           N  
ANISOU 3762  N   SER B 337     3188   3434   3296    -75   -207    -55       N  
ATOM   3763  CA  SER B 337      45.795  22.664  27.482  1.00 20.20           C  
ANISOU 3763  CA  SER B 337     2466   2667   2543    -78   -191    -33       C  
ATOM   3764  C   SER B 337      45.393  22.250  26.064  1.00 20.93           C  
ANISOU 3764  C   SER B 337     2574   2724   2655    -76   -178    -13       C  
ATOM   3765  O   SER B 337      44.217  21.966  25.816  1.00 13.62           O  
ANISOU 3765  O   SER B 337     1667   1784   1722    -72   -173     12       O  
ATOM   3766  CB  SER B 337      45.442  24.131  27.690  1.00 26.49           C  
ANISOU 3766  CB  SER B 337     3265   3462   3339    -96   -168    -58       C  
ATOM   3767  OG  SER B 337      46.196  24.945  26.812  1.00 23.08           O  
ANISOU 3767  OG  SER B 337     2826   3010   2934   -107   -146    -86       O  
ATOM   3768  N   HIS B 338      46.357  22.232  25.143  1.00 18.36           N  
ANISOU 3768  N   HIS B 338     2239   2383   2353    -78   -171    -27       N  
ATOM   3769  CA  HIS B 338      46.047  22.111  23.719  1.00 18.03           C  
ANISOU 3769  CA  HIS B 338     2212   2309   2330    -78   -154    -16       C  
ATOM   3770  C   HIS B 338      47.032  21.284  22.887  1.00 18.81           C  
ANISOU 3770  C   HIS B 338     2299   2398   2449    -72   -160    -16       C  
ATOM   3771  O   HIS B 338      48.205  21.123  23.235  1.00 18.11           O  
ANISOU 3771  O   HIS B 338     2190   2324   2368    -72   -172    -35       O  
ATOM   3772  CB  HIS B 338      45.949  23.509  23.079  1.00 16.11           C  
ANISOU 3772  CB  HIS B 338     1975   2047   2099    -93   -122    -37       C  
ATOM   3773  CG  HIS B 338      44.707  24.250  23.446  1.00 20.79           C  
ANISOU 3773  CG  HIS B 338     2585   2639   2677    -97   -110    -29       C  
ATOM   3774  ND1 HIS B 338      44.617  25.029  24.581  1.00 23.57           N  
ANISOU 3774  ND1 HIS B 338     2930   3010   3016   -105   -109    -47       N  
ATOM   3775  CD2 HIS B 338      43.494  24.314  22.842  1.00 17.20           C  
ANISOU 3775  CD2 HIS B 338     2151   2165   2218    -94    -98     -8       C  
ATOM   3776  CE1 HIS B 338      43.402  25.546  24.660  1.00 23.04           C  
ANISOU 3776  CE1 HIS B 338     2881   2936   2939   -108    -97    -35       C  
ATOM   3777  NE2 HIS B 338      42.701  25.126  23.619  1.00 26.46           N  
ANISOU 3777  NE2 HIS B 338     3331   3346   3378   -100    -90    -12       N  
ATOM   3778  N   ILE B 339      46.529  20.776  21.767  1.00 17.95           N  
ANISOU 3778  N   ILE B 339     2206   2266   2351    -68   -151      3       N  
ATOM   3779  CA  ILE B 339      47.377  20.294  20.693  1.00 18.20           C  
ANISOU 3779  CA  ILE B 339     2230   2281   2404    -67   -147     -2       C  
ATOM   3780  C   ILE B 339      47.113  21.154  19.451  1.00 15.19           C  
ANISOU 3780  C   ILE B 339     1863   1873   2035    -75   -117     -9       C  
ATOM   3781  O   ILE B 339      45.980  21.354  19.061  1.00 16.72           O  
ANISOU 3781  O   ILE B 339     2075   2056   2220    -73   -107      7       O  
ATOM   3782  CB  ILE B 339      47.072  18.831  20.359  1.00 16.58           C  
ANISOU 3782  CB  ILE B 339     2028   2071   2202    -53   -163     25       C  
ATOM   3783  CG1 ILE B 339      47.263  17.968  21.605  1.00 17.16           C  
ANISOU 3783  CG1 ILE B 339     2089   2168   2262    -42   -191     37       C  
ATOM   3784  CG2 ILE B 339      47.936  18.354  19.189  1.00 17.89           C  
ANISOU 3784  CG2 ILE B 339     2187   2219   2392    -53   -157     18       C  
ATOM   3785  CD1 ILE B 339      46.750  16.582  21.444  1.00 22.27           C  
ANISOU 3785  CD1 ILE B 339     2742   2809   2910    -28   -203     67       C  
ATOM   3786  N   VAL B 340      48.161  21.680  18.842  1.00 14.39           N  
ANISOU 3786  N   VAL B 340     1752   1762   1953    -83   -102    -33       N  
ATOM   3787  CA  VAL B 340      47.996  22.435  17.614  1.00 17.36           C  
ANISOU 3787  CA  VAL B 340     2142   2113   2340    -89    -72    -37       C  
ATOM   3788  C   VAL B 340      48.741  21.724  16.502  1.00 14.67           C  
ANISOU 3788  C   VAL B 340     1797   1758   2019    -86    -69    -38       C  
ATOM   3789  O   VAL B 340      49.930  21.425  16.622  1.00 14.84           O  
ANISOU 3789  O   VAL B 340     1799   1785   2055    -89    -76    -56       O  
ATOM   3790  CB  VAL B 340      48.504  23.883  17.764  1.00 19.00           C  
ANISOU 3790  CB  VAL B 340     2346   2316   2556   -104    -47    -67       C  
ATOM   3791  CG1 VAL B 340      48.164  24.690  16.507  1.00 18.51           C  
ANISOU 3791  CG1 VAL B 340     2304   2227   2504   -107    -13    -64       C  
ATOM   3792  CG2 VAL B 340      47.875  24.539  18.999  1.00 13.76           C  
ANISOU 3792  CG2 VAL B 340     1683   1671   1876   -107    -51    -70       C  
ATOM   3793  N   VAL B 341      48.036  21.410  15.432  1.00 17.37           N  
ANISOU 3793  N   VAL B 341     2157   2084   2360    -80    -60    -20       N  
ATOM   3794  CA  VAL B 341      48.666  20.672  14.344  1.00 15.17           C  
ANISOU 3794  CA  VAL B 341     1874   1793   2097    -78    -57    -20       C  
ATOM   3795  C   VAL B 341      48.689  21.526  13.097  1.00 16.22           C  
ANISOU 3795  C   VAL B 341     2021   1905   2237    -82    -25    -27       C  
ATOM   3796  O   VAL B 341      47.681  22.113  12.715  1.00 19.67           O  
ANISOU 3796  O   VAL B 341     2477   2334   2661    -79    -11    -14       O  
ATOM   3797  CB  VAL B 341      47.961  19.322  14.082  1.00 19.17           C  
ANISOU 3797  CB  VAL B 341     2385   2301   2599    -66    -76      5       C  
ATOM   3798  CG1 VAL B 341      48.338  18.761  12.708  1.00 17.58           C  
ANISOU 3798  CG1 VAL B 341     2184   2083   2412    -64    -66      4       C  
ATOM   3799  CG2 VAL B 341      48.296  18.317  15.196  1.00 16.12           C  
ANISOU 3799  CG2 VAL B 341     1982   1933   2212    -60   -106     10       C  
ATOM   3800  N   SER B 342      49.859  21.620  12.478  1.00 15.66           N  
ANISOU 3800  N   SER B 342     1940   1823   2187    -89    -12    -46       N  
ATOM   3801  CA  SER B 342      49.959  22.308  11.212  1.00 17.45           C  
ANISOU 3801  CA  SER B 342     2181   2029   2421    -92     20    -50       C  
ATOM   3802  C   SER B 342      50.357  21.291  10.161  1.00 16.13           C  
ANISOU 3802  C   SER B 342     2012   1854   2264    -87     17    -46       C  
ATOM   3803  O   SER B 342      51.385  20.608  10.285  1.00 13.49           O  
ANISOU 3803  O   SER B 342     1657   1523   1947    -90      6    -60       O  
ATOM   3804  CB  SER B 342      50.978  23.450  11.284  1.00 19.67           C  
ANISOU 3804  CB  SER B 342     2454   2300   2719   -106     46    -79       C  
ATOM   3805  OG  SER B 342      51.078  24.128  10.041  1.00 19.63           O  
ANISOU 3805  OG  SER B 342     2465   2272   2720   -107     80    -80       O  
ATOM   3806  N   ASN B 343      49.547  21.185   9.121  1.00 13.93           N  
ANISOU 3806  N   ASN B 343     1752   1567   1974    -79     28    -29       N  
ATOM   3807  CA  ASN B 343      49.793  20.144   8.126  1.00 15.75           C  
ANISOU 3807  CA  ASN B 343     1980   1793   2212    -75     24    -26       C  
ATOM   3808  C   ASN B 343      49.906  20.646   6.692  1.00 16.44           C  
ANISOU 3808  C   ASN B 343     2082   1864   2300    -74     54    -27       C  
ATOM   3809  O   ASN B 343      49.112  21.478   6.249  1.00 18.31           O  
ANISOU 3809  O   ASN B 343     2340   2096   2521    -69     73    -17       O  
ATOM   3810  CB  ASN B 343      48.693  19.079   8.202  1.00 12.08           C  
ANISOU 3810  CB  ASN B 343     1518   1338   1733    -63      1     -3       C  
ATOM   3811  CG  ASN B 343      48.903  17.981   7.175  1.00 22.52           C  
ANISOU 3811  CG  ASN B 343     2836   2656   3064    -59     -2     -2       C  
ATOM   3812  OD1 ASN B 343      48.190  17.901   6.170  1.00 20.79           O  
ANISOU 3812  OD1 ASN B 343     2632   2435   2834    -53      7      7       O  
ATOM   3813  ND2 ASN B 343      49.927  17.165   7.394  1.00 14.47           N  
ANISOU 3813  ND2 ASN B 343     1796   1636   2065    -63    -15    -13       N  
ATOM   3814  N   CYS B 344      50.885  20.121   5.965  1.00 19.06           N  
ANISOU 3814  N   CYS B 344     2404   2187   2649    -78     60    -40       N  
ATOM   3815  CA  CYS B 344      51.064  20.431   4.556  1.00 19.47           C  
ANISOU 3815  CA  CYS B 344     2470   2226   2702    -77     88    -42       C  
ATOM   3816  C   CYS B 344      51.427  19.150   3.779  1.00 22.90           C  
ANISOU 3816  C   CYS B 344     2894   2660   3146    -75     78    -44       C  
ATOM   3817  O   CYS B 344      52.535  18.643   3.908  1.00 18.49           O  
ANISOU 3817  O   CYS B 344     2317   2099   2611    -82     73    -61       O  
ATOM   3818  CB  CYS B 344      52.193  21.451   4.394  1.00 21.86           C  
ANISOU 3818  CB  CYS B 344     2770   2513   3023    -89    118    -64       C  
ATOM   3819  SG  CYS B 344      52.426  21.986   2.677  1.00 30.29           S  
ANISOU 3819  SG  CYS B 344     3859   3562   4089    -87    159    -64       S  
ATOM   3820  N   GLY B 345      50.497  18.619   2.992  1.00 22.43           N  
ANISOU 3820  N   GLY B 345     2846   2606   3069    -64     75    -29       N  
ATOM   3821  CA  GLY B 345      50.753  17.372   2.287  1.00 20.14           C  
ANISOU 3821  CA  GLY B 345     2546   2317   2789    -63     65    -32       C  
ATOM   3822  C   GLY B 345      49.942  16.195   2.821  1.00 23.26           C  
ANISOU 3822  C   GLY B 345     2932   2725   3180    -56     34    -20       C  
ATOM   3823  O   GLY B 345      48.835  16.379   3.350  1.00 20.04           O  
ANISOU 3823  O   GLY B 345     2533   2326   2753    -49     24     -4       O  
ATOM   3824  N   ASP B 346      50.494  14.983   2.698  1.00 21.67           N  
ANISOU 3824  N   ASP B 346     2712   2523   2998    -58     21    -27       N  
ATOM   3825  CA  ASP B 346      49.763  13.769   3.066  1.00 19.24           C  
ANISOU 3825  CA  ASP B 346     2395   2224   2691    -51     -3    -16       C  
ATOM   3826  C   ASP B 346      50.407  12.902   4.162  1.00 21.58           C  
ANISOU 3826  C   ASP B 346     2669   2520   3009    -53    -26    -18       C  
ATOM   3827  O   ASP B 346      50.020  11.764   4.334  1.00 21.41           O  
ANISOU 3827  O   ASP B 346     2638   2501   2995    -48    -42    -10       O  
ATOM   3828  CB  ASP B 346      49.405  12.909   1.841  1.00 22.54           C  
ANISOU 3828  CB  ASP B 346     2813   2642   3109    -47      1    -19       C  
ATOM   3829  CG  ASP B 346      50.639  12.387   1.093  1.00 34.89           C  
ANISOU 3829  CG  ASP B 346     4364   4195   4697    -55     11    -37       C  
ATOM   3830  OD1 ASP B 346      51.780  12.677   1.521  1.00 30.74           O  
ANISOU 3830  OD1 ASP B 346     3828   3662   4191    -62     14    -49       O  
ATOM   3831  OD2 ASP B 346      50.465  11.671   0.077  1.00 31.40           O  
ANISOU 3831  OD2 ASP B 346     3920   3754   4258    -53     15    -43       O  
ATOM   3832  N   SER B 347      51.370  13.430   4.910  1.00 21.26           N  
ANISOU 3832  N   SER B 347     2620   2479   2980    -59    -27    -27       N  
ATOM   3833  CA  SER B 347      51.677  12.809   6.193  1.00 20.93           C  
ANISOU 3833  CA  SER B 347     2561   2444   2949    -57    -52    -23       C  
ATOM   3834  C   SER B 347      50.513  13.153   7.118  1.00 19.83           C  
ANISOU 3834  C   SER B 347     2434   2316   2786    -51    -63     -4       C  
ATOM   3835  O   SER B 347      49.620  13.917   6.739  1.00 21.04           O  
ANISOU 3835  O   SER B 347     2606   2471   2919    -50    -51      2       O  
ATOM   3836  CB  SER B 347      52.998  13.311   6.748  1.00 22.57           C  
ANISOU 3836  CB  SER B 347     2753   2651   3173    -64    -51    -42       C  
ATOM   3837  OG  SER B 347      53.997  13.117   5.778  1.00 24.95           O  
ANISOU 3837  OG  SER B 347     3046   2940   3495    -70    -36    -60       O  
ATOM   3838  N   ARG B 348      50.495  12.603   8.320  1.00 17.83           N  
ANISOU 3838  N   ARG B 348     2169   2071   2534    -46    -85      5       N  
ATOM   3839  CA  ARG B 348      49.270  12.665   9.098  1.00 21.05           C  
ANISOU 3839  CA  ARG B 348     2588   2489   2921    -40    -95     25       C  
ATOM   3840  C   ARG B 348      49.539  12.692  10.597  1.00 20.05           C  
ANISOU 3840  C   ARG B 348     2451   2375   2791    -38   -115     30       C  
ATOM   3841  O   ARG B 348      50.483  12.061  11.069  1.00 20.48           O  
ANISOU 3841  O   ARG B 348     2487   2431   2862    -35   -127     25       O  
ATOM   3842  CB  ARG B 348      48.390  11.450   8.717  1.00 24.54           C  
ANISOU 3842  CB  ARG B 348     3030   2928   3365    -33   -102     39       C  
ATOM   3843  CG  ARG B 348      46.935  11.526   9.132  1.00 28.30           C  
ANISOU 3843  CG  ARG B 348     3520   3411   3820    -28   -107     57       C  
ATOM   3844  CD  ARG B 348      46.196  10.235   8.718  1.00 27.57           C  
ANISOU 3844  CD  ARG B 348     3425   3315   3736    -22   -111     66       C  
ATOM   3845  NE  ARG B 348      46.211  10.036   7.269  1.00 31.57           N  
ANISOU 3845  NE  ARG B 348     3933   3815   4249    -25    -97     53       N  
ATOM   3846  CZ  ARG B 348      45.955   8.876   6.669  1.00 30.20           C  
ANISOU 3846  CZ  ARG B 348     3750   3635   4089    -23    -98     52       C  
ATOM   3847  NH1 ARG B 348      45.677   7.798   7.389  1.00 21.31           N  
ANISOU 3847  NH1 ARG B 348     2615   2507   2976    -18   -110     64       N  
ATOM   3848  NH2 ARG B 348      45.975   8.794   5.345  1.00 21.13           N  
ANISOU 3848  NH2 ARG B 348     2602   2483   2942    -25    -85     39       N  
ATOM   3849  N   ALA B 349      48.706  13.426  11.343  1.00 19.94           N  
ANISOU 3849  N   ALA B 349     2450   2371   2756    -37   -116     39       N  
ATOM   3850  CA  ALA B 349      48.747  13.399  12.796  1.00 16.33           C  
ANISOU 3850  CA  ALA B 349     1985   1928   2290    -33   -135     46       C  
ATOM   3851  C   ALA B 349      47.424  12.855  13.339  1.00 19.19           C  
ANISOU 3851  C   ALA B 349     2359   2296   2638    -26   -145     70       C  
ATOM   3852  O   ALA B 349      46.348  13.341  12.971  1.00 21.00           O  
ANISOU 3852  O   ALA B 349     2605   2524   2852    -27   -134     76       O  
ATOM   3853  CB  ALA B 349      49.028  14.802  13.363  1.00 17.64           C  
ANISOU 3853  CB  ALA B 349     2155   2103   2446    -41   -128     32       C  
ATOM   3854  N   VAL B 350      47.498  11.864  14.224  1.00 15.61           N  
ANISOU 3854  N   VAL B 350     1895   1849   2187    -17   -163     84       N  
ATOM   3855  CA  VAL B 350      46.286  11.190  14.698  1.00 14.49           C  
ANISOU 3855  CA  VAL B 350     1762   1709   2035    -10   -170    107       C  
ATOM   3856  C   VAL B 350      46.211  11.165  16.212  1.00 17.75           C  
ANISOU 3856  C   VAL B 350     2172   2138   2433     -4   -186    120       C  
ATOM   3857  O   VAL B 350      47.157  10.730  16.880  1.00 19.44           O  
ANISOU 3857  O   VAL B 350     2372   2361   2655      2   -201    120       O  
ATOM   3858  CB  VAL B 350      46.196   9.735  14.146  1.00 18.83           C  
ANISOU 3858  CB  VAL B 350     2304   2246   2606     -3   -172    117       C  
ATOM   3859  CG1 VAL B 350      44.987   8.998  14.736  1.00 16.68           C  
ANISOU 3859  CG1 VAL B 350     2038   1973   2325      4   -177    139       C  
ATOM   3860  CG2 VAL B 350      46.102   9.745  12.634  1.00 12.18           C  
ANISOU 3860  CG2 VAL B 350     1465   1390   1774     -9   -156    104       C  
ATOM   3861  N   LEU B 351      45.086  11.644  16.743  1.00 14.89           N  
ANISOU 3861  N   LEU B 351     1825   1783   2051     -5   -185    130       N  
ATOM   3862  CA  LEU B 351      44.823  11.631  18.172  1.00 18.10           C  
ANISOU 3862  CA  LEU B 351     2232   2206   2439      1   -198    143       C  
ATOM   3863  C   LEU B 351      44.013  10.402  18.489  1.00 19.30           C  
ANISOU 3863  C   LEU B 351     2387   2352   2594     11   -203    168       C  
ATOM   3864  O   LEU B 351      43.074  10.089  17.772  1.00 20.50           O  
ANISOU 3864  O   LEU B 351     2548   2491   2750      9   -192    173       O  
ATOM   3865  CB  LEU B 351      44.020  12.874  18.579  1.00 20.88           C  
ANISOU 3865  CB  LEU B 351     2598   2567   2768     -6   -191    139       C  
ATOM   3866  CG  LEU B 351      43.546  12.941  20.036  1.00 19.02           C  
ANISOU 3866  CG  LEU B 351     2366   2350   2512     -2   -202    153       C  
ATOM   3867  CD1 LEU B 351      44.749  12.880  20.961  1.00 14.63           C  
ANISOU 3867  CD1 LEU B 351     1794   1813   1954      3   -219    147       C  
ATOM   3868  CD2 LEU B 351      42.722  14.219  20.296  1.00 19.69           C  
ANISOU 3868  CD2 LEU B 351     2464   2441   2576    -11   -192    146       C  
ATOM   3869  N   PHE B 352      44.362   9.702  19.562  1.00 19.97           N  
ANISOU 3869  N   PHE B 352     2465   2448   2676     22   -218    184       N  
ATOM   3870  CA  PHE B 352      43.506   8.626  20.070  1.00 17.52           C  
ANISOU 3870  CA  PHE B 352     2159   2131   2365     31   -220    210       C  
ATOM   3871  C   PHE B 352      42.714   9.163  21.260  1.00 19.10           C  
ANISOU 3871  C   PHE B 352     2372   2349   2538     32   -223    221       C  
ATOM   3872  O   PHE B 352      43.266   9.369  22.334  1.00 22.88           O  
ANISOU 3872  O   PHE B 352     2846   2847   3002     38   -237    225       O  
ATOM   3873  CB  PHE B 352      44.334   7.399  20.497  1.00 21.66           C  
ANISOU 3873  CB  PHE B 352     2670   2654   2905     46   -231    225       C  
ATOM   3874  CG  PHE B 352      43.529   6.098  20.593  1.00 25.44           C  
ANISOU 3874  CG  PHE B 352     3152   3116   3396     54   -226    250       C  
ATOM   3875  CD1 PHE B 352      42.383   5.901  19.822  1.00 22.70           C  
ANISOU 3875  CD1 PHE B 352     2815   2753   3057     47   -210    249       C  
ATOM   3876  CD2 PHE B 352      43.929   5.075  21.447  1.00 28.46           C  
ANISOU 3876  CD2 PHE B 352     3529   3501   3784     71   -235    273       C  
ATOM   3877  CE1 PHE B 352      41.651   4.708  19.911  1.00 26.38           C  
ANISOU 3877  CE1 PHE B 352     3283   3203   3537     53   -202    269       C  
ATOM   3878  CE2 PHE B 352      43.196   3.865  21.538  1.00 27.59           C  
ANISOU 3878  CE2 PHE B 352     3422   3372   3688     79   -226    297       C  
ATOM   3879  CZ  PHE B 352      42.070   3.686  20.774  1.00 24.21           C  
ANISOU 3879  CZ  PHE B 352     3002   2927   3270     69   -209    293       C  
ATOM   3880  N   ARG B 353      41.424   9.400  21.073  1.00 23.88           N  
ANISOU 3880  N   ARG B 353     2991   2947   3135     26   -212    225       N  
ATOM   3881  CA  ARG B 353      40.587   9.922  22.159  1.00 21.55           C  
ANISOU 3881  CA  ARG B 353     2708   2666   2814     25   -213    235       C  
ATOM   3882  C   ARG B 353      39.610   8.856  22.599  1.00 22.32           C  
ANISOU 3882  C   ARG B 353     2812   2755   2914     33   -209    259       C  
ATOM   3883  O   ARG B 353      38.759   8.422  21.813  1.00 22.47           O  
ANISOU 3883  O   ARG B 353     2836   2756   2946     29   -197    260       O  
ATOM   3884  CB  ARG B 353      39.833  11.183  21.723  1.00 20.70           C  
ANISOU 3884  CB  ARG B 353     2611   2559   2695     13   -201    219       C  
ATOM   3885  CG  ARG B 353      38.834  11.680  22.761  1.00 27.54           C  
ANISOU 3885  CG  ARG B 353     3490   3438   3538     11   -200    227       C  
ATOM   3886  CD  ARG B 353      38.482  13.132  22.545  1.00 23.10           C  
ANISOU 3886  CD  ARG B 353     2935   2880   2963     -1   -191    209       C  
ATOM   3887  NE  ARG B 353      39.658  13.989  22.677  1.00 21.91           N  
ANISOU 3887  NE  ARG B 353     2775   2741   2809     -5   -196    190       N  
ATOM   3888  CZ  ARG B 353      39.631  15.316  22.594  1.00 23.48           C  
ANISOU 3888  CZ  ARG B 353     2978   2944   2999    -15   -187    172       C  
ATOM   3889  NH1 ARG B 353      38.477  15.952  22.391  1.00 17.36           N  
ANISOU 3889  NH1 ARG B 353     2216   2163   2217    -20   -174    172       N  
ATOM   3890  NH2 ARG B 353      40.757  16.009  22.736  1.00 17.93           N  
ANISOU 3890  NH2 ARG B 353     2265   2251   2298    -20   -190    152       N  
ATOM   3891  N   GLY B 354      39.747   8.413  23.846  1.00 27.67           N  
ANISOU 3891  N   GLY B 354     3490   3445   3578     43   -219    279       N  
ATOM   3892  CA  GLY B 354      38.926   7.321  24.349  1.00 32.81           C  
ANISOU 3892  CA  GLY B 354     4147   4085   4233     52   -213    305       C  
ATOM   3893  C   GLY B 354      39.148   6.069  23.526  1.00 34.59           C  
ANISOU 3893  C   GLY B 354     4364   4287   4490     58   -207    312       C  
ATOM   3894  O   GLY B 354      40.232   5.482  23.571  1.00 37.38           O  
ANISOU 3894  O   GLY B 354     4706   4642   4857     68   -216    317       O  
ATOM   3895  N   LYS B 355      38.135   5.661  22.761  1.00 31.44           N  
ANISOU 3895  N   LYS B 355     3969   3868   4107     51   -191    310       N  
ATOM   3896  CA  LYS B 355      38.266   4.483  21.914  1.00 27.24           C  
ANISOU 3896  CA  LYS B 355     3428   3314   3608     54   -183    312       C  
ATOM   3897  C   LYS B 355      38.237   4.806  20.410  1.00 26.51           C  
ANISOU 3897  C   LYS B 355     3331   3212   3531     43   -176    285       C  
ATOM   3898  O   LYS B 355      38.143   3.901  19.580  1.00 26.93           O  
ANISOU 3898  O   LYS B 355     3376   3246   3611     43   -167    282       O  
ATOM   3899  CB  LYS B 355      37.206   3.424  22.278  1.00 35.63           C  
ANISOU 3899  CB  LYS B 355     4497   4360   4683     58   -168    332       C  
ATOM   3900  CG  LYS B 355      35.763   3.791  21.939  1.00 36.64           C  
ANISOU 3900  CG  LYS B 355     4633   4482   4805     47   -155    322       C  
ATOM   3901  CD  LYS B 355      34.806   2.672  22.397  1.00 38.80           C  
ANISOU 3901  CD  LYS B 355     4910   4737   5093     51   -138    341       C  
ATOM   3902  CE  LYS B 355      33.335   2.970  22.076  1.00 42.81           C  
ANISOU 3902  CE  LYS B 355     5425   5241   5599     40   -124    329       C  
ATOM   3903  NZ  LYS B 355      33.027   2.925  20.615  1.00 40.01           N  
ANISOU 3903  NZ  LYS B 355     5061   4876   5265     31   -118    303       N  
ATOM   3904  N   GLU B 356      38.330   6.087  20.061  1.00 22.41           N  
ANISOU 3904  N   GLU B 356     2816   2705   2995     34   -179    266       N  
ATOM   3905  CA  GLU B 356      38.244   6.501  18.658  1.00 22.91           C  
ANISOU 3905  CA  GLU B 356     2876   2761   3067     25   -172    243       C  
ATOM   3906  C   GLU B 356      39.490   7.221  18.186  1.00 23.23           C  
ANISOU 3906  C   GLU B 356     2910   2808   3107     22   -178    227       C  
ATOM   3907  O   GLU B 356      39.988   8.121  18.864  1.00 22.24           O  
ANISOU 3907  O   GLU B 356     2788   2699   2964     21   -186    224       O  
ATOM   3908  CB  GLU B 356      37.055   7.445  18.446  1.00 20.04           C  
ANISOU 3908  CB  GLU B 356     2526   2403   2686     17   -164    234       C  
ATOM   3909  CG  GLU B 356      35.745   6.961  19.091  1.00 30.66           C  
ANISOU 3909  CG  GLU B 356     3878   3744   4027     18   -157    249       C  
ATOM   3910  CD  GLU B 356      35.074   5.862  18.278  1.00 30.06           C  
ANISOU 3910  CD  GLU B 356     3796   3650   3977     18   -145    246       C  
ATOM   3911  OE1 GLU B 356      35.561   5.572  17.159  1.00 28.33           O  
ANISOU 3911  OE1 GLU B 356     3567   3423   3774     16   -143    232       O  
ATOM   3912  OE2 GLU B 356      34.060   5.299  18.752  1.00 33.83           O  
ANISOU 3912  OE2 GLU B 356     4276   4120   4456     19   -137    256       O  
ATOM   3913  N   ALA B 357      39.964   6.850  16.999  1.00 21.32           N  
ANISOU 3913  N   ALA B 357     2660   2555   2886     20   -173    213       N  
ATOM   3914  CA  ALA B 357      40.990   7.630  16.326  1.00 25.66           C  
ANISOU 3914  CA  ALA B 357     3205   3109   3437     15   -175    194       C  
ATOM   3915  C   ALA B 357      40.369   8.936  15.817  1.00 25.59           C  
ANISOU 3915  C   ALA B 357     3209   3107   3409      7   -166    181       C  
ATOM   3916  O   ALA B 357      39.203   8.975  15.432  1.00 30.97           O  
ANISOU 3916  O   ALA B 357     3899   3785   4085      5   -158    181       O  
ATOM   3917  CB  ALA B 357      41.601   6.848  15.183  1.00 25.90           C  
ANISOU 3917  CB  ALA B 357     3223   3125   3493     14   -169    183       C  
ATOM   3918  N   MET B 358      41.143  10.013  15.854  1.00 20.43           N  
ANISOU 3918  N   MET B 358     2557   2462   2746      2   -167    169       N  
ATOM   3919  CA  MET B 358      40.692  11.303  15.348  1.00 25.67           C  
ANISOU 3919  CA  MET B 358     3231   3128   3394     -5   -157    157       C  
ATOM   3920  C   MET B 358      41.835  11.985  14.618  1.00 17.73           C  
ANISOU 3920  C   MET B 358     2221   2120   2394    -10   -151    138       C  
ATOM   3921  O   MET B 358      42.727  12.556  15.253  1.00 18.15           O  
ANISOU 3921  O   MET B 358     2269   2181   2445    -12   -156    132       O  
ATOM   3922  CB  MET B 358      40.213  12.198  16.497  1.00 19.43           C  
ANISOU 3922  CB  MET B 358     2451   2351   2581     -6   -160    162       C  
ATOM   3923  CG  MET B 358      39.137  11.580  17.381  1.00 31.72           C  
ANISOU 3923  CG  MET B 358     4012   3910   4130     -2   -165    181       C  
ATOM   3924  SD  MET B 358      38.517  12.781  18.574  1.00 49.83           S  
ANISOU 3924  SD  MET B 358     6318   6220   6397     -6   -165    183       S  
ATOM   3925  CE  MET B 358      37.184  13.560  17.644  1.00 42.65           C  
ANISOU 3925  CE  MET B 358     5422   5305   5480     -9   -150    177       C  
ATOM   3926  N   PRO B 359      41.818  11.938  13.281  1.00 24.38           N  
ANISOU 3926  N   PRO B 359     3065   2953   3245    -11   -140    128       N  
ATOM   3927  CA  PRO B 359      42.949  12.573  12.590  1.00 22.69           C  
ANISOU 3927  CA  PRO B 359     2847   2735   3038    -16   -132    111       C  
ATOM   3928  C   PRO B 359      42.898  14.062  12.833  1.00 22.39           C  
ANISOU 3928  C   PRO B 359     2820   2702   2984    -22   -122    104       C  
ATOM   3929  O   PRO B 359      41.817  14.628  12.793  1.00 22.40           O  
ANISOU 3929  O   PRO B 359     2835   2706   2969    -21   -116    110       O  
ATOM   3930  CB  PRO B 359      42.709  12.239  11.108  1.00 24.02           C  
ANISOU 3930  CB  PRO B 359     3018   2894   3215    -16   -120    104       C  
ATOM   3931  CG  PRO B 359      41.248  11.820  11.030  1.00 29.72           C  
ANISOU 3931  CG  PRO B 359     3746   3617   3927    -11   -121    115       C  
ATOM   3932  CD  PRO B 359      40.913  11.226  12.367  1.00 24.27           C  
ANISOU 3932  CD  PRO B 359     3053   2932   3236     -8   -134    130       C  
ATOM   3933  N   LEU B 360      44.036  14.684  13.107  1.00 19.47           N  
ANISOU 3933  N   LEU B 360     2444   2336   2620    -27   -121     91       N  
ATOM   3934  CA  LEU B 360      44.030  16.113  13.369  1.00 20.94           C  
ANISOU 3934  CA  LEU B 360     2638   2524   2793    -33   -109     82       C  
ATOM   3935  C   LEU B 360      44.447  16.883  12.120  1.00 24.89           C  
ANISOU 3935  C   LEU B 360     3145   3013   3299    -38    -87     69       C  
ATOM   3936  O   LEU B 360      44.653  18.099  12.172  1.00 22.48           O  
ANISOU 3936  O   LEU B 360     2847   2706   2990    -43    -72     59       O  
ATOM   3937  CB  LEU B 360      44.923  16.461  14.566  1.00 17.73           C  
ANISOU 3937  CB  LEU B 360     2220   2130   2388    -38   -119     73       C  
ATOM   3938  CG  LEU B 360      44.560  15.793  15.909  1.00 22.27           C  
ANISOU 3938  CG  LEU B 360     2790   2720   2954    -32   -140     88       C  
ATOM   3939  CD1 LEU B 360      45.455  16.331  17.034  1.00 23.06           C  
ANISOU 3939  CD1 LEU B 360     2878   2835   3050    -36   -149     76       C  
ATOM   3940  CD2 LEU B 360      43.102  16.021  16.248  1.00 22.52           C  
ANISOU 3940  CD2 LEU B 360     2837   2753   2966    -30   -138    103       C  
ATOM   3941  N   SER B 361      44.555  16.172  10.997  1.00 19.76           N  
ANISOU 3941  N   SER B 361     2494   2355   2659    -34    -83     68       N  
ATOM   3942  CA  SER B 361      44.897  16.800   9.721  1.00 19.31           C  
ANISOU 3942  CA  SER B 361     2445   2287   2605    -37    -61     58       C  
ATOM   3943  C   SER B 361      44.113  16.143   8.598  1.00 20.12           C  
ANISOU 3943  C   SER B 361     2554   2386   2703    -29    -58     65       C  
ATOM   3944  O   SER B 361      43.835  14.958   8.656  1.00 19.34           O  
ANISOU 3944  O   SER B 361     2447   2291   2612    -26    -72     71       O  
ATOM   3945  CB  SER B 361      46.408  16.685   9.438  1.00 16.11           C  
ANISOU 3945  CB  SER B 361     2026   1875   2222    -43    -57     40       C  
ATOM   3946  OG  SER B 361      46.828  15.321   9.338  1.00 21.28           O  
ANISOU 3946  OG  SER B 361     2665   2529   2892    -41    -72     41       O  
ATOM   3947  N   VAL B 362      43.756  16.922   7.581  1.00 23.56           N  
ANISOU 3947  N   VAL B 362     3005   2818   3128    -26    -39     63       N  
ATOM   3948  CA  VAL B 362      43.076  16.392   6.406  1.00 25.16           C  
ANISOU 3948  CA  VAL B 362     3213   3022   3325    -18    -35     67       C  
ATOM   3949  C   VAL B 362      44.083  16.365   5.258  1.00 26.20           C  
ANISOU 3949  C   VAL B 362     3343   3145   3468    -21    -20     54       C  
ATOM   3950  O   VAL B 362      44.655  17.383   4.936  1.00 18.40           O  
ANISOU 3950  O   VAL B 362     2363   2150   2478    -24     -1     48       O  
ATOM   3951  CB  VAL B 362      41.864  17.277   6.007  1.00 29.53           C  
ANISOU 3951  CB  VAL B 362     3786   3581   3854    -10    -25     76       C  
ATOM   3952  CG1 VAL B 362      41.185  16.729   4.757  1.00 29.79           C  
ANISOU 3952  CG1 VAL B 362     3822   3619   3878      0    -23     77       C  
ATOM   3953  CG2 VAL B 362      40.858  17.396   7.159  1.00 34.98           C  
ANISOU 3953  CG2 VAL B 362     4478   4278   4534     -8    -38     88       C  
ATOM   3954  N   ASP B 363      44.305  15.201   4.654  1.00 24.03           N  
ANISOU 3954  N   ASP B 363     3056   2870   3204    -21    -27     49       N  
ATOM   3955  CA  ASP B 363      45.314  15.059   3.593  1.00 21.59           C  
ANISOU 3955  CA  ASP B 363     2743   2552   2907    -24    -13     35       C  
ATOM   3956  C   ASP B 363      45.072  16.041   2.431  1.00 24.35           C  
ANISOU 3956  C   ASP B 363     3112   2901   3238    -19     11     35       C  
ATOM   3957  O   ASP B 363      43.930  16.217   1.972  1.00 21.64           O  
ANISOU 3957  O   ASP B 363     2781   2567   2874     -8     12     44       O  
ATOM   3958  CB  ASP B 363      45.322  13.627   3.031  1.00 25.05           C  
ANISOU 3958  CB  ASP B 363     3167   2991   3359    -23    -23     29       C  
ATOM   3959  CG  ASP B 363      45.650  12.555   4.087  1.00 32.41           C  
ANISOU 3959  CG  ASP B 363     4081   3922   4313    -27    -44     32       C  
ATOM   3960  OD1 ASP B 363      45.645  12.825   5.308  1.00 23.63           O  
ANISOU 3960  OD1 ASP B 363     2966   2812   3199    -28    -55     39       O  
ATOM   3961  OD2 ASP B 363      45.907  11.409   3.674  1.00 33.51           O  
ANISOU 3961  OD2 ASP B 363     4205   4057   4468    -27    -49     26       O  
ATOM   3962  N   HIS B 364      46.138  16.675   1.951  1.00 17.52           N  
ANISOU 3962  N   HIS B 364     2249   2024   2381    -25     31     24       N  
ATOM   3963  CA  HIS B 364      46.030  17.530   0.770  1.00 18.50           C  
ANISOU 3963  CA  HIS B 364     2394   2147   2490    -19     57     25       C  
ATOM   3964  C   HIS B 364      46.188  16.686  -0.487  1.00 21.85           C  
ANISOU 3964  C   HIS B 364     2814   2574   2914    -16     60     17       C  
ATOM   3965  O   HIS B 364      47.306  16.460  -0.963  1.00 17.83           O  
ANISOU 3965  O   HIS B 364     2297   2055   2422    -24     71      3       O  
ATOM   3966  CB  HIS B 364      47.073  18.642   0.811  1.00 15.03           C  
ANISOU 3966  CB  HIS B 364     1960   1692   2060    -27     82     17       C  
ATOM   3967  CG  HIS B 364      46.842  19.623   1.915  1.00 16.96           C  
ANISOU 3967  CG  HIS B 364     2209   1933   2301    -30     83     23       C  
ATOM   3968  ND1 HIS B 364      47.752  19.826   2.934  1.00 17.71           N  
ANISOU 3968  ND1 HIS B 364     2290   2022   2416    -42     79     11       N  
ATOM   3969  CD2 HIS B 364      45.794  20.435   2.179  1.00 17.60           C  
ANISOU 3969  CD2 HIS B 364     2307   2020   2363    -21     86     38       C  
ATOM   3970  CE1 HIS B 364      47.278  20.739   3.763  1.00 20.45           C  
ANISOU 3970  CE1 HIS B 364     2644   2370   2755    -42     82     17       C  
ATOM   3971  NE2 HIS B 364      46.087  21.120   3.331  1.00 19.42           N  
ANISOU 3971  NE2 HIS B 364     2533   2245   2602    -30     87     34       N  
ATOM   3972  N   LYS B 365      45.069  16.172  -0.986  1.00 17.06           N  
ANISOU 3972  N   LYS B 365     2210   1982   2290     -4     51     24       N  
ATOM   3973  CA  LYS B 365      45.085  15.386  -2.211  1.00 21.85           C  
ANISOU 3973  CA  LYS B 365     2813   2596   2894     -1     54     14       C  
ATOM   3974  C   LYS B 365      44.285  16.105  -3.280  1.00 19.27           C  
ANISOU 3974  C   LYS B 365     2507   2281   2534     15     69     22       C  
ATOM   3975  O   LYS B 365      43.299  16.762  -2.989  1.00 23.73           O  
ANISOU 3975  O   LYS B 365     3084   2854   3079     25     66     37       O  
ATOM   3976  CB  LYS B 365      44.550  13.975  -1.975  1.00 25.80           C  
ANISOU 3976  CB  LYS B 365     3294   3105   3404     -2     30     10       C  
ATOM   3977  CG  LYS B 365      45.432  13.139  -1.070  1.00 27.12           C  
ANISOU 3977  CG  LYS B 365     3440   3259   3604    -14     17      3       C  
ATOM   3978  CD  LYS B 365      45.010  11.677  -1.079  1.00 43.19           C  
ANISOU 3978  CD  LYS B 365     5456   5300   5652    -15      0     -3       C  
ATOM   3979  CE  LYS B 365      44.533  11.227   0.300  1.00 50.83           C  
ANISOU 3979  CE  LYS B 365     6416   6267   6630    -16    -21      9       C  
ATOM   3980  NZ  LYS B 365      45.165   9.947   0.763  1.00 53.95           N  
ANISOU 3980  NZ  LYS B 365     6790   6653   7057    -22    -33      3       N  
ATOM   3981  N   PRO B 366      44.723  15.980  -4.528  1.00 21.77           N  
ANISOU 3981  N   PRO B 366     2827   2601   2845     17     84     13       N  
ATOM   3982  CA  PRO B 366      44.157  16.719  -5.656  1.00 26.10           C  
ANISOU 3982  CA  PRO B 366     3397   3160   3361     34    101     22       C  
ATOM   3983  C   PRO B 366      42.704  16.363  -5.932  1.00 21.76           C  
ANISOU 3983  C   PRO B 366     2847   2635   2785     50     84     27       C  
ATOM   3984  O   PRO B 366      42.054  17.070  -6.699  1.00 30.83           O  
ANISOU 3984  O   PRO B 366     4013   3796   3903     67     95     38       O  
ATOM   3985  CB  PRO B 366      45.034  16.286  -6.843  1.00 22.29           C  
ANISOU 3985  CB  PRO B 366     2911   2676   2881     30    117      7       C  
ATOM   3986  CG  PRO B 366      46.216  15.707  -6.268  1.00 22.63           C  
ANISOU 3986  CG  PRO B 366     2935   2701   2961     11    114     -8       C  
ATOM   3987  CD  PRO B 366      45.906  15.197  -4.909  1.00 18.21           C  
ANISOU 3987  CD  PRO B 366     2361   2140   2420      4     88     -5       C  
ATOM   3988  N   ASP B 367      42.181  15.290  -5.350  1.00 20.77           N  
ANISOU 3988  N   ASP B 367     2702   2516   2673     45     60     20       N  
ATOM   3989  CA  ASP B 367      40.786  14.994  -5.628  1.00 23.25           C  
ANISOU 3989  CA  ASP B 367     3015   2854   2964     59     45     23       C  
ATOM   3990  C   ASP B 367      39.788  15.614  -4.630  1.00 21.56           C  
ANISOU 3990  C   ASP B 367     2809   2642   2742     65     35     39       C  
ATOM   3991  O   ASP B 367      38.593  15.479  -4.804  1.00 21.39           O  
ANISOU 3991  O   ASP B 367     2787   2640   2702     78     24     41       O  
ATOM   3992  CB  ASP B 367      40.548  13.504  -5.823  1.00 27.80           C  
ANISOU 3992  CB  ASP B 367     3568   3440   3556     53     28      4       C  
ATOM   3993  CG  ASP B 367      41.013  12.692  -4.660  1.00 38.26           C  
ANISOU 3993  CG  ASP B 367     4874   4747   4916     36     15      0       C  
ATOM   3994  OD1 ASP B 367      41.377  13.299  -3.628  1.00 42.50           O  
ANISOU 3994  OD1 ASP B 367     5416   5269   5461     30     15     12       O  
ATOM   3995  OD2 ASP B 367      41.015  11.448  -4.782  1.00 52.04           O  
ANISOU 3995  OD2 ASP B 367     6600   6495   6680     29      5    -15       O  
ATOM   3996  N   ARG B 368      40.286  16.301  -3.606  1.00 22.69           N  
ANISOU 3996  N   ARG B 368     2958   2767   2898     57     39     49       N  
ATOM   3997  CA  ARG B 368      39.446  17.220  -2.837  1.00 20.86           C  
ANISOU 3997  CA  ARG B 368     2738   2535   2652     64     37     66       C  
ATOM   3998  C   ARG B 368      38.928  18.289  -3.784  1.00 22.25           C  
ANISOU 3998  C   ARG B 368     2936   2721   2797     84     55     77       C  
ATOM   3999  O   ARG B 368      39.709  18.868  -4.538  1.00 22.70           O  
ANISOU 3999  O   ARG B 368     3005   2770   2849     86     77     79       O  
ATOM   4000  CB  ARG B 368      40.270  17.889  -1.728  1.00 18.63           C  
ANISOU 4000  CB  ARG B 368     2458   2231   2388     51     44     71       C  
ATOM   4001  CG  ARG B 368      40.192  17.180  -0.395  1.00 21.72           C  
ANISOU 4001  CG  ARG B 368     2833   2620   2801     38     22     69       C  
ATOM   4002  CD  ARG B 368      41.169  17.739   0.630  1.00 28.83           C  
ANISOU 4002  CD  ARG B 368     3732   3502   3719     25     28     69       C  
ATOM   4003  NE  ARG B 368      41.113  19.195   0.780  1.00 20.76           N  
ANISOU 4003  NE  ARG B 368     2729   2474   2686     29     47     79       N  
ATOM   4004  CZ  ARG B 368      41.835  19.865   1.677  1.00 28.08           C  
ANISOU 4004  CZ  ARG B 368     3655   3387   3626     18     54     78       C  
ATOM   4005  NH1 ARG B 368      42.654  19.205   2.495  1.00 21.66           N  
ANISOU 4005  NH1 ARG B 368     2825   2569   2837      4     41     68       N  
ATOM   4006  NH2 ARG B 368      41.751  21.191   1.752  1.00 21.06           N  
ANISOU 4006  NH2 ARG B 368     2783   2490   2729     21     74     85       N  
ATOM   4007  N   GLU B 369      37.626  18.570  -3.741  1.00 20.46           N  
ANISOU 4007  N   GLU B 369     2714   2510   2549     99     46     87       N  
ATOM   4008  CA  GLU B 369      37.024  19.524  -4.673  1.00 23.39           C  
ANISOU 4008  CA  GLU B 369     3106   2894   2887    122     60    100       C  
ATOM   4009  C   GLU B 369      37.640  20.929  -4.584  1.00 28.14           C  
ANISOU 4009  C   GLU B 369     3730   3475   3487    124     88    115       C  
ATOM   4010  O   GLU B 369      37.823  21.600  -5.606  1.00 28.61           O  
ANISOU 4010  O   GLU B 369     3807   3537   3528    139    109    124       O  
ATOM   4011  CB  GLU B 369      35.499  19.586  -4.501  1.00 27.75           C  
ANISOU 4011  CB  GLU B 369     3657   3466   3420    138     43    106       C  
ATOM   4012  CG  GLU B 369      34.772  18.222  -4.688  1.00 33.44           C  
ANISOU 4012  CG  GLU B 369     4355   4207   4142    137     19     88       C  
ATOM   4013  CD  GLU B 369      34.819  17.718  -6.131  1.00 39.00           C  
ANISOU 4013  CD  GLU B 369     5057   4934   4829    148     21     75       C  
ATOM   4014  OE1 GLU B 369      35.292  18.484  -7.003  1.00 37.64           O  
ANISOU 4014  OE1 GLU B 369     4902   4761   4638    160     42     84       O  
ATOM   4015  OE2 GLU B 369      34.393  16.565  -6.393  1.00 36.78           O  
ANISOU 4015  OE2 GLU B 369     4755   4668   4552    145      5     56       O  
ATOM   4016  N   ASP B 370      37.974  21.377  -3.378  1.00 19.92           N  
ANISOU 4016  N   ASP B 370     2687   2414   2466    110     89    119       N  
ATOM   4017  CA  ASP B 370      38.564  22.704  -3.252  1.00 24.36           C  
ANISOU 4017  CA  ASP B 370     3268   2956   3031    110    118    130       C  
ATOM   4018  C   ASP B 370      39.946  22.734  -3.926  1.00 25.46           C  
ANISOU 4018  C   ASP B 370     3411   3081   3183    100    140    122       C  
ATOM   4019  O   ASP B 370      40.267  23.664  -4.689  1.00 21.67           O  
ANISOU 4019  O   ASP B 370     2950   2592   2691    111    170    131       O  
ATOM   4020  CB  ASP B 370      38.594  23.195  -1.783  1.00 20.76           C  
ANISOU 4020  CB  ASP B 370     2808   2484   2593     96    115    132       C  
ATOM   4021  CG  ASP B 370      39.438  22.301  -0.848  1.00 24.40           C  
ANISOU 4021  CG  ASP B 370     3248   2938   3084     72     98    116       C  
ATOM   4022  OD1 ASP B 370      39.494  21.066  -1.046  1.00 23.92           O  
ANISOU 4022  OD1 ASP B 370     3172   2888   3030     67     79    105       O  
ATOM   4023  OD2 ASP B 370      40.045  22.839   0.109  1.00 23.55           O  
ANISOU 4023  OD2 ASP B 370     3139   2814   2994     58    105    113       O  
ATOM   4024  N   GLU B 371      40.750  21.707  -3.660  1.00 20.80           N  
ANISOU 4024  N   GLU B 371     2801   2487   2616     82    128    103       N  
ATOM   4025  CA  GLU B 371      42.097  21.607  -4.246  1.00 19.39           C  
ANISOU 4025  CA  GLU B 371     2620   2294   2452     71    147     92       C  
ATOM   4026  C   GLU B 371      41.999  21.431  -5.753  1.00 21.43           C  
ANISOU 4026  C   GLU B 371     2889   2567   2687     86    158     93       C  
ATOM   4027  O   GLU B 371      42.746  22.044  -6.512  1.00 18.02           O  
ANISOU 4027  O   GLU B 371     2470   2123   2252     88    187     94       O  
ATOM   4028  CB  GLU B 371      42.888  20.462  -3.614  1.00 19.23           C  
ANISOU 4028  CB  GLU B 371     2576   2270   2462     50    128     73       C  
ATOM   4029  CG  GLU B 371      43.248  20.708  -2.135  1.00 18.78           C  
ANISOU 4029  CG  GLU B 371     2509   2199   2428     35    120     71       C  
ATOM   4030  CD  GLU B 371      44.207  21.881  -1.974  1.00 29.68           C  
ANISOU 4030  CD  GLU B 371     3899   3557   3820     27    149     69       C  
ATOM   4031  OE1 GLU B 371      43.731  23.043  -1.910  1.00 23.33           O  
ANISOU 4031  OE1 GLU B 371     3114   2748   3004     36    167     83       O  
ATOM   4032  OE2 GLU B 371      45.441  21.645  -1.946  1.00 23.76           O  
ANISOU 4032  OE2 GLU B 371     3138   2794   3094     12    157     53       O  
ATOM   4033  N   TYR B 372      41.044  20.616  -6.182  1.00 20.06           N  
ANISOU 4033  N   TYR B 372     2707   2418   2495     98    136     90       N  
ATOM   4034  CA  TYR B 372      40.813  20.406  -7.601  1.00 22.79           C  
ANISOU 4034  CA  TYR B 372     3060   2783   2815    114    143     89       C  
ATOM   4035  C   TYR B 372      40.484  21.732  -8.299  1.00 27.44           C  
ANISOU 4035  C   TYR B 372     3678   3373   3374    136    169    111       C  
ATOM   4036  O   TYR B 372      41.050  22.053  -9.339  1.00 28.30           O  
ANISOU 4036  O   TYR B 372     3801   3481   3471    144    194    114       O  
ATOM   4037  CB  TYR B 372      39.702  19.370  -7.827  1.00 24.57           C  
ANISOU 4037  CB  TYR B 372     3271   3038   3027    123    114     81       C  
ATOM   4038  CG  TYR B 372      39.538  18.991  -9.280  1.00 26.71           C  
ANISOU 4038  CG  TYR B 372     3544   3333   3271    137    118     74       C  
ATOM   4039  CD1 TYR B 372      40.259  17.937  -9.829  1.00 32.88           C  
ANISOU 4039  CD1 TYR B 372     4310   4117   4067    125    116     52       C  
ATOM   4040  CD2 TYR B 372      38.683  19.707 -10.111  1.00 37.96           C  
ANISOU 4040  CD2 TYR B 372     4987   4779   4657    165    125     89       C  
ATOM   4041  CE1 TYR B 372      40.125  17.600 -11.161  1.00 36.16           C  
ANISOU 4041  CE1 TYR B 372     4726   4555   4456    138    120     43       C  
ATOM   4042  CE2 TYR B 372      38.544  19.379 -11.447  1.00 45.82           C  
ANISOU 4042  CE2 TYR B 372     5984   5799   5624    180    129     82       C  
ATOM   4043  CZ  TYR B 372      39.269  18.324 -11.968  1.00 41.38           C  
ANISOU 4043  CZ  TYR B 372     5406   5240   5076    166    126     58       C  
ATOM   4044  OH  TYR B 372      39.125  17.988 -13.296  1.00 52.47           O  
ANISOU 4044  OH  TYR B 372     6812   6673   6452    180    130     49       O  
ATOM   4045  N   ALA B 373      39.590  22.517  -7.704  1.00 24.50           N  
ANISOU 4045  N   ALA B 373     3315   3001   2991    148    167    129       N  
ATOM   4046  CA  ALA B 373      39.198  23.794  -8.295  1.00 23.03           C  
ANISOU 4046  CA  ALA B 373     3157   2814   2779    171    192    152       C  
ATOM   4047  C   ALA B 373      40.342  24.808  -8.254  1.00 26.75           C  
ANISOU 4047  C   ALA B 373     3644   3253   3267    162    230    159       C  
ATOM   4048  O   ALA B 373      40.549  25.552  -9.215  1.00 21.99           O  
ANISOU 4048  O   ALA B 373     3063   2647   2645    178    260    173       O  
ATOM   4049  CB  ALA B 373      37.958  24.340  -7.625  1.00 24.70           C  
ANISOU 4049  CB  ALA B 373     3373   3033   2980    185    180    167       C  
ATOM   4050  N   ARG B 374      41.102  24.817  -7.161  1.00 21.39           N  
ANISOU 4050  N   ARG B 374     2953   2550   2623    137    230    148       N  
ATOM   4051  CA  ARG B 374      42.258  25.698  -7.064  1.00 23.99           C  
ANISOU 4051  CA  ARG B 374     3293   2849   2973    125    265    147       C  
ATOM   4052  C   ARG B 374      43.243  25.436  -8.214  1.00 31.45           C  
ANISOU 4052  C   ARG B 374     4243   3790   3917    123    287    139       C  
ATOM   4053  O   ARG B 374      43.694  26.353  -8.925  1.00 28.19           O  
ANISOU 4053  O   ARG B 374     3852   3363   3497    131    324    151       O  
ATOM   4054  CB  ARG B 374      42.964  25.528  -5.710  1.00 21.65           C  
ANISOU 4054  CB  ARG B 374     2977   2534   2714     97    256    130       C  
ATOM   4055  CG  ARG B 374      44.201  26.414  -5.577  1.00 22.69           C  
ANISOU 4055  CG  ARG B 374     3115   2634   2870     82    292    124       C  
ATOM   4056  CD  ARG B 374      44.872  26.287  -4.216  1.00 23.64           C  
ANISOU 4056  CD  ARG B 374     3215   2741   3025     56    281    106       C  
ATOM   4057  NE  ARG B 374      45.278  24.912  -3.913  1.00 20.67           N  
ANISOU 4057  NE  ARG B 374     2814   2377   2664     42    249     87       N  
ATOM   4058  CZ  ARG B 374      46.311  24.295  -4.487  1.00 24.40           C  
ANISOU 4058  CZ  ARG B 374     3277   2844   3150     32    255     71       C  
ATOM   4059  NH1 ARG B 374      46.608  23.040  -4.151  1.00 23.42           N  
ANISOU 4059  NH1 ARG B 374     3129   2729   3041     20    226     55       N  
ATOM   4060  NH2 ARG B 374      47.037  24.925  -5.407  1.00 18.99           N  
ANISOU 4060  NH2 ARG B 374     2606   2143   2465     33    292     71       N  
ATOM   4061  N   ILE B 375      43.561  24.168  -8.414  1.00 20.27           N  
ANISOU 4061  N   ILE B 375     2806   2387   2508    112    264    119       N  
ATOM   4062  CA  ILE B 375      44.551  23.796  -9.424  1.00 23.49           C  
ANISOU 4062  CA  ILE B 375     3215   2791   2919    107    282    107       C  
ATOM   4063  C   ILE B 375      44.099  24.092 -10.862  1.00 26.08           C  
ANISOU 4063  C   ILE B 375     3565   3138   3207    133    300    122       C  
ATOM   4064  O   ILE B 375      44.878  24.599 -11.662  1.00 27.22           O  
ANISOU 4064  O   ILE B 375     3725   3269   3349    135    334    125       O  
ATOM   4065  CB  ILE B 375      44.973  22.320  -9.257  1.00 18.96           C  
ANISOU 4065  CB  ILE B 375     2613   2227   2366     89    254     82       C  
ATOM   4066  CG1 ILE B 375      45.806  22.167  -7.981  1.00 18.40           C  
ANISOU 4066  CG1 ILE B 375     2522   2133   2334     63    246     68       C  
ATOM   4067  CG2 ILE B 375      45.751  21.826 -10.484  1.00 24.96           C  
ANISOU 4067  CG2 ILE B 375     3373   2990   3121     87    270     70       C  
ATOM   4068  CD1 ILE B 375      45.831  20.756  -7.445  1.00 21.12           C  
ANISOU 4068  CD1 ILE B 375     2839   2488   2698     50    211     50       C  
ATOM   4069  N   GLU B 376      42.850  23.767 -11.180  1.00 31.90           N  
ANISOU 4069  N   GLU B 376     4303   3905   3913    154    276    131       N  
ATOM   4070  CA  GLU B 376      42.292  24.013 -12.513  1.00 34.53           C  
ANISOU 4070  CA  GLU B 376     4655   4263   4204    183    287    145       C  
ATOM   4071  C   GLU B 376      42.119  25.501 -12.793  1.00 42.21           C  
ANISOU 4071  C   GLU B 376     5659   5221   5158    204    322    175       C  
ATOM   4072  O   GLU B 376      42.515  25.995 -13.851  1.00 46.71           O  
ANISOU 4072  O   GLU B 376     6249   5789   5708    218    353    186       O  
ATOM   4073  CB  GLU B 376      40.959  23.277 -12.684  1.00 34.64           C  
ANISOU 4073  CB  GLU B 376     4657   4315   4191    200    251    143       C  
ATOM   4074  CG  GLU B 376      41.078  21.758 -12.474  1.00 47.68           C  
ANISOU 4074  CG  GLU B 376     6276   5978   5861    180    219    113       C  
ATOM   4075  CD  GLU B 376      41.034  20.951 -13.776  1.00 58.64           C  
ANISOU 4075  CD  GLU B 376     7659   7396   7225    190    215     99       C  
ATOM   4076  OE1 GLU B 376      41.830  19.989 -13.914  1.00 58.80           O  
ANISOU 4076  OE1 GLU B 376     7662   7412   7268    169    211     75       O  
ATOM   4077  OE2 GLU B 376      40.187  21.258 -14.648  1.00 62.38           O  
ANISOU 4077  OE2 GLU B 376     8146   7898   7657    218    216    111       O  
ATOM   4078  N  AASN B 377      41.543  26.224 -11.839  0.55 33.39           N  
ANISOU 4078  N  AASN B 377     4546   4093   4049    206    319    189       N  
ATOM   4079  N  BASN B 377      41.561  26.225 -11.829  0.45 33.40           N  
ANISOU 4079  N  BASN B 377     4546   4093   4050    206    320    188       N  
ATOM   4080  CA AASN B 377      41.427  27.673 -11.965  0.55 35.65           C  
ANISOU 4080  CA AASN B 377     4861   4361   4325    224    355    216       C  
ATOM   4081  CA BASN B 377      41.438  27.671 -11.951  0.45 35.66           C  
ANISOU 4081  CA BASN B 377     4861   4361   4326    223    355    216       C  
ATOM   4082  C  AASN B 377      42.782  28.350 -12.186  0.55 40.62           C  
ANISOU 4082  C  AASN B 377     5503   4954   4977    210    400    215       C  
ATOM   4083  C  BASN B 377      42.786  28.324 -12.233  0.45 40.64           C  
ANISOU 4083  C  BASN B 377     5505   4957   4978    210    400    215       C  
ATOM   4084  O  AASN B 377      42.849  29.447 -12.734  0.55 42.83           O  
ANISOU 4084  O  AASN B 377     5811   5220   5244    227    439    239       O  
ATOM   4085  O  BASN B 377      42.851  29.379 -12.858  0.45 42.89           O  
ANISOU 4085  O  BASN B 377     5818   5229   5248    229    438    239       O  
ATOM   4086  CB AASN B 377      40.699  28.271 -10.757  0.55 40.04           C  
ANISOU 4086  CB AASN B 377     5414   4907   4893    223    345    226       C  
ATOM   4087  CB BASN B 377      40.812  28.280 -10.697  0.45 40.05           C  
ANISOU 4087  CB BASN B 377     5414   4905   4897    220    346    224       C  
ATOM   4088  CG AASN B 377      39.244  27.813 -10.669  0.55 52.58           C  
ANISOU 4088  CG AASN B 377     6993   6529   6454    242    307    231       C  
ATOM   4089  CG BASN B 377      40.669  29.792 -10.790  0.45 53.33           C  
ANISOU 4089  CG BASN B 377     7125   6565   6574    238    386    253       C  
ATOM   4090  OD1AASN B 377      38.748  27.105 -11.552  0.55 51.67           O  
ANISOU 4090  OD1AASN B 377     6875   6446   6311    258    290    228       O  
ATOM   4091  OD1BASN B 377      39.810  30.302 -11.507  0.45 52.63           O  
ANISOU 4091  OD1BASN B 377     7055   6492   6449    270    392    277       O  
ATOM   4092  ND2AASN B 377      38.561  28.201  -9.593  0.55 57.47           N  
ANISOU 4092  ND2AASN B 377     7609   7143   7085    240    295    236       N  
ATOM   4093  ND2BASN B 377      41.514  30.514 -10.063  0.45 58.12           N  
ANISOU 4093  ND2BASN B 377     7733   7134   7214    217    413    248       N  
ATOM   4094  N   ALA B 378      43.863  27.695 -11.774  1.00 32.94           N  
ANISOU 4094  N   ALA B 378     4510   3966   4038    179    397    188       N  
ATOM   4095  CA  ALA B 378      45.203  28.231 -12.027  1.00 36.58           C  
ANISOU 4095  CA  ALA B 378     4981   4396   4524    163    439    182       C  
ATOM   4096  C   ALA B 378      45.804  27.752 -13.357  1.00 33.32           C  
ANISOU 4096  C   ALA B 378     4574   3992   4094    168    454    177       C  
ATOM   4097  O   ALA B 378      46.953  28.051 -13.665  1.00 37.75           O  
ANISOU 4097  O   ALA B 378     5141   4527   4675    154    488    168       O  
ATOM   4098  CB  ALA B 378      46.148  27.907 -10.863  1.00 34.25           C  
ANISOU 4098  CB  ALA B 378     4660   4077   4275    128    431    155       C  
ATOM   4099  N   GLY B 379      45.028  27.008 -14.138  1.00 32.90           N  
ANISOU 4099  N   GLY B 379     4519   3976   4006    187    430    179       N  
ATOM   4100  CA  GLY B 379      45.492  26.521 -15.426  1.00 31.20           C  
ANISOU 4100  CA  GLY B 379     4310   3774   3770    193    442    173       C  
ATOM   4101  C   GLY B 379      46.124  25.133 -15.393  1.00 38.62           C  
ANISOU 4101  C   GLY B 379     5220   4723   4732    168    417    139       C  
ATOM   4102  O   GLY B 379      46.612  24.642 -16.410  1.00 32.15           O  
ANISOU 4102  O   GLY B 379     4401   3913   3900    169    427    129       O  
ATOM   4103  N   GLY B 380      46.121  24.489 -14.231  1.00 29.98           N  
ANISOU 4103  N   GLY B 380     4098   3623   3668    147    385    121       N  
ATOM   4104  CA  GLY B 380      46.749  23.186 -14.105  1.00 28.25           C  
ANISOU 4104  CA  GLY B 380     3850   3408   3474    124    363     91       C  
ATOM   4105  C   GLY B 380      45.795  22.049 -14.403  1.00 31.63           C  
ANISOU 4105  C   GLY B 380     4262   3874   3881    133    324     82       C  
ATOM   4106  O   GLY B 380      44.630  22.279 -14.704  1.00 31.23           O  
ANISOU 4106  O   GLY B 380     4222   3849   3796    158    313     98       O  
ATOM   4107  N   LYS B 381      46.287  20.820 -14.294  1.00 28.10           N  
ANISOU 4107  N   LYS B 381     3788   3430   3458    113    304     55       N  
ATOM   4108  CA  LYS B 381      45.489  19.635 -14.593  1.00 37.82           C  
ANISOU 4108  CA  LYS B 381     5000   4694   4675    118    271     41       C  
ATOM   4109  C   LYS B 381      45.636  18.572 -13.510  1.00 28.94           C  
ANISOU 4109  C   LYS B 381     3845   3563   3590     95    240     21       C  
ATOM   4110  O   LYS B 381      46.717  18.346 -12.976  1.00 26.34           O  
ANISOU 4110  O   LYS B 381     3502   3207   3296     73    245      8       O  
ATOM   4111  CB  LYS B 381      45.882  19.051 -15.956  1.00 43.51           C  
ANISOU 4111  CB  LYS B 381     5720   5432   5378    122    282     26       C  
ATOM   4112  CG  LYS B 381      45.263  19.773 -17.144  1.00 50.09           C  
ANISOU 4112  CG  LYS B 381     6581   6289   6160    153    300     46       C  
ATOM   4113  CD  LYS B 381      43.797  19.378 -17.331  1.00 57.77           C  
ANISOU 4113  CD  LYS B 381     7548   7302   7100    174    268     48       C  
ATOM   4114  CE  LYS B 381      43.079  20.318 -18.300  1.00 68.64           C  
ANISOU 4114  CE  LYS B 381     8954   8702   8424    210    285     74       C  
ATOM   4115  NZ  LYS B 381      42.839  21.684 -17.718  1.00 60.03           N  
ANISOU 4115  NZ  LYS B 381     7888   7590   7331    222    302    107       N  
ATOM   4116  N   VAL B 382      44.536  17.927 -13.172  1.00 25.17           N  
ANISOU 4116  N   VAL B 382     3353   3107   3102    102    208     19       N  
ATOM   4117  CA  VAL B 382      44.582  16.807 -12.252  1.00 24.82           C  
ANISOU 4117  CA  VAL B 382     3280   3058   3092     83    179      1       C  
ATOM   4118  C   VAL B 382      44.184  15.557 -13.018  1.00 33.28           C  
ANISOU 4118  C   VAL B 382     4333   4157   4157     84    163    -20       C  
ATOM   4119  O   VAL B 382      43.127  15.517 -13.647  1.00 25.35           O  
ANISOU 4119  O   VAL B 382     3331   3181   3118    103    154    -17       O  
ATOM   4120  CB  VAL B 382      43.639  17.020 -11.072  1.00 26.69           C  
ANISOU 4120  CB  VAL B 382     3513   3295   3331     86    157     15       C  
ATOM   4121  CG1 VAL B 382      43.621  15.776 -10.176  1.00 27.77           C  
ANISOU 4121  CG1 VAL B 382     3621   3430   3501     69    129     -2       C  
ATOM   4122  CG2 VAL B 382      44.075  18.247 -10.286  1.00 24.63           C  
ANISOU 4122  CG2 VAL B 382     3270   3009   3080     83    175     32       C  
ATOM   4123  N   ILE B 383      45.038  14.540 -12.975  1.00 22.14           N  
ANISOU 4123  N   ILE B 383     2900   2735   2779     64    159    -43       N  
ATOM   4124  CA  ILE B 383      44.782  13.327 -13.736  1.00 29.89           C  
ANISOU 4124  CA  ILE B 383     3861   3737   3758     63    147    -67       C  
ATOM   4125  C   ILE B 383      44.739  12.114 -12.824  1.00 27.60           C  
ANISOU 4125  C   ILE B 383     3542   3440   3507     46    122    -82       C  
ATOM   4126  O   ILE B 383      45.637  11.931 -11.998  1.00 27.87           O  
ANISOU 4126  O   ILE B 383     3566   3446   3576     28    122    -83       O  
ATOM   4127  CB  ILE B 383      45.877  13.119 -14.800  1.00 31.03           C  
ANISOU 4127  CB  ILE B 383     4006   3878   3906     55    171    -83       C  
ATOM   4128  CG1 ILE B 383      45.915  14.310 -15.760  1.00 29.53           C  
ANISOU 4128  CG1 ILE B 383     3847   3695   3676     73    199    -66       C  
ATOM   4129  CG2 ILE B 383      45.641  11.825 -15.575  1.00 38.46           C  
ANISOU 4129  CG2 ILE B 383     4925   4842   4848     52    159   -111       C  
ATOM   4130  CD1 ILE B 383      47.115  14.288 -16.688  1.00 41.57           C  
ANISOU 4130  CD1 ILE B 383     5377   5211   5206     65    227    -78       C  
ATOM   4131  N   GLN B 384      43.707  11.283 -12.969  1.00 27.69           N  
ANISOU 4131  N   GLN B 384     3538   3474   3510     51    102    -93       N  
ATOM   4132  CA  GLN B 384      43.650  10.018 -12.225  1.00 28.17           C  
ANISOU 4132  CA  GLN B 384     3570   3526   3608     36     82   -109       C  
ATOM   4133  C   GLN B 384      44.656   9.015 -12.804  1.00 33.83           C  
ANISOU 4133  C   GLN B 384     4267   4234   4351     20     90   -134       C  
ATOM   4134  O   GLN B 384      44.456   8.483 -13.894  1.00 37.35           O  
ANISOU 4134  O   GLN B 384     4705   4701   4784     23     94   -154       O  
ATOM   4135  CB  GLN B 384      42.233   9.438 -12.238  1.00 34.17           C  
ANISOU 4135  CB  GLN B 384     4317   4311   4353     46     62   -116       C  
ATOM   4136  CG  GLN B 384      42.033   8.261 -11.275  1.00 34.45           C  
ANISOU 4136  CG  GLN B 384     4326   4334   4428     31     43   -126       C  
ATOM   4137  CD  GLN B 384      42.065   8.682  -9.802  1.00 34.49           C  
ANISOU 4137  CD  GLN B 384     4337   4317   4450     27     34   -103       C  
ATOM   4138  OE1 GLN B 384      41.599   9.764  -9.440  1.00 32.93           O  
ANISOU 4138  OE1 GLN B 384     4160   4123   4230     38     35    -81       O  
ATOM   4139  NE2 GLN B 384      42.622   7.825  -8.954  1.00 34.74           N  
ANISOU 4139  NE2 GLN B 384     4350   4326   4522     11     27   -107       N  
ATOM   4140  N   TRP B 385      45.739   8.763 -12.073  1.00 31.01           N  
ANISOU 4140  N   TRP B 385     3902   3848   4034      3     93   -135       N  
ATOM   4141  CA  TRP B 385      46.814   7.896 -12.553  1.00 19.87           C  
ANISOU 4141  CA  TRP B 385     2473   2425   2652    -12    102   -158       C  
ATOM   4142  C   TRP B 385      47.545   7.296 -11.358  1.00 18.63           C  
ANISOU 4142  C   TRP B 385     2298   2239   2542    -28     92   -157       C  
ATOM   4143  O   TRP B 385      48.501   7.878 -10.844  1.00 18.05           O  
ANISOU 4143  O   TRP B 385     2231   2145   2483    -34    100   -148       O  
ATOM   4144  CB  TRP B 385      47.781   8.707 -13.420  1.00 25.24           C  
ANISOU 4144  CB  TRP B 385     3170   3100   3319    -12    129   -158       C  
ATOM   4145  CG  TRP B 385      48.633   7.878 -14.332  1.00 33.76           C  
ANISOU 4145  CG  TRP B 385     4234   4177   4415    -24    142   -185       C  
ATOM   4146  CD1 TRP B 385      49.754   7.170 -13.998  1.00 25.06           C  
ANISOU 4146  CD1 TRP B 385     3112   3050   3358    -42    144   -199       C  
ATOM   4147  CD2 TRP B 385      48.442   7.683 -15.741  1.00 32.74           C  
ANISOU 4147  CD2 TRP B 385     4107   4072   4259    -18    154   -203       C  
ATOM   4148  NE1 TRP B 385      50.261   6.545 -15.106  1.00 29.21           N  
ANISOU 4148  NE1 TRP B 385     3628   3582   3888    -49    158   -225       N  
ATOM   4149  CE2 TRP B 385      49.484   6.848 -16.185  1.00 29.80           C  
ANISOU 4149  CE2 TRP B 385     3716   3688   3919    -35    165   -228       C  
ATOM   4150  CE3 TRP B 385      47.496   8.143 -16.660  1.00 34.39           C  
ANISOU 4150  CE3 TRP B 385     4331   4315   4419      1    157   -200       C  
ATOM   4151  CZ2 TRP B 385      49.598   6.454 -17.518  1.00 38.23           C  
ANISOU 4151  CZ2 TRP B 385     4781   4775   4971    -35    179   -251       C  
ATOM   4152  CZ3 TRP B 385      47.617   7.750 -17.985  1.00 37.77           C  
ANISOU 4152  CZ3 TRP B 385     4757   4765   4830      3    169   -222       C  
ATOM   4153  CH2 TRP B 385      48.659   6.912 -18.399  1.00 32.91           C  
ANISOU 4153  CH2 TRP B 385     4123   4135   4246    -16    181   -248       C  
ATOM   4154  N   GLN B 386      47.059   6.152 -10.888  1.00 30.46           N  
ANISOU 4154  N   GLN B 386     3774   3738   4064    -32     74   -166       N  
ATOM   4155  CA  GLN B 386      47.518   5.581  -9.630  1.00 34.53           C  
ANISOU 4155  CA  GLN B 386     4273   4228   4618    -42     62   -160       C  
ATOM   4156  C   GLN B 386      47.263   6.601  -8.532  1.00 28.54           C  
ANISOU 4156  C   GLN B 386     3532   3465   3848    -36     54   -132       C  
ATOM   4157  O   GLN B 386      48.188   7.060  -7.871  1.00 26.58           O  
ANISOU 4157  O   GLN B 386     3286   3198   3615    -42     57   -124       O  
ATOM   4158  CB  GLN B 386      49.004   5.237  -9.699  1.00 37.48           C  
ANISOU 4158  CB  GLN B 386     4635   4579   5025    -55     73   -171       C  
ATOM   4159  CG  GLN B 386      49.342   4.187 -10.737  1.00 47.10           C  
ANISOU 4159  CG  GLN B 386     5835   5801   6261    -63     82   -200       C  
ATOM   4160  CD  GLN B 386      50.217   3.088 -10.182  1.00 61.55           C  
ANISOU 4160  CD  GLN B 386     7638   7606   8140    -76     77   -209       C  
ATOM   4161  OE1 GLN B 386      50.988   3.306  -9.249  1.00 61.42           O  
ANISOU 4161  OE1 GLN B 386     7620   7571   8146    -79     73   -197       O  
ATOM   4162  NE2 GLN B 386      50.102   1.895 -10.752  1.00 72.67           N  
ANISOU 4162  NE2 GLN B 386     9025   9016   9569    -81     79   -232       N  
ATOM   4163  N   GLY B 387      45.995   6.955  -8.358  1.00 28.23           N  
ANISOU 4163  N   GLY B 387     3503   3443   3782    -24     44   -121       N  
ATOM   4164  CA  GLY B 387      45.610   8.090  -7.531  1.00 24.79           C  
ANISOU 4164  CA  GLY B 387     3086   3005   3326    -17     40    -96       C  
ATOM   4165  C   GLY B 387      45.532   9.373  -8.355  1.00 27.40           C  
ANISOU 4165  C   GLY B 387     3443   3347   3620     -6     58    -89       C  
ATOM   4166  O   GLY B 387      46.198   9.509  -9.394  1.00 26.02           O  
ANISOU 4166  O   GLY B 387     3272   3174   3439     -7     76   -100       O  
ATOM   4167  N   ALA B 388      44.709  10.312  -7.899  1.00 28.15           N  
ANISOU 4167  N   ALA B 388     3555   3449   3690      5     54    -69       N  
ATOM   4168  CA  ALA B 388      44.632  11.642  -8.502  1.00 27.52           C  
ANISOU 4168  CA  ALA B 388     3503   3377   3578     17     72    -57       C  
ATOM   4169  C   ALA B 388      45.982  12.322  -8.369  1.00 18.80           C  
ANISOU 4169  C   ALA B 388     2406   2249   2488      7     91    -55       C  
ATOM   4170  O   ALA B 388      46.529  12.389  -7.281  1.00 18.51           O  
ANISOU 4170  O   ALA B 388     2363   2195   2477     -3     85    -51       O  
ATOM   4171  CB  ALA B 388      43.558  12.476  -7.808  1.00 25.22           C  
ANISOU 4171  CB  ALA B 388     3226   3093   3264     29     64    -35       C  
ATOM   4172  N   ARG B 389      46.519  12.828  -9.471  1.00 19.94           N  
ANISOU 4172  N   ARG B 389     2564   2395   2619     10    115    -59       N  
ATOM   4173  CA  ARG B 389      47.843  13.449  -9.452  1.00 21.71           C  
ANISOU 4173  CA  ARG B 389     2794   2596   2860      0    138    -61       C  
ATOM   4174  C   ARG B 389      47.894  14.776 -10.186  1.00 23.58           C  
ANISOU 4174  C   ARG B 389     3060   2833   3067     11    166    -48       C  
ATOM   4175  O   ARG B 389      47.274  14.935 -11.232  1.00 26.21           O  
ANISOU 4175  O   ARG B 389     3405   3186   3367     26    174    -45       O  
ATOM   4176  CB  ARG B 389      48.903  12.500 -10.043  1.00 21.54           C  
ANISOU 4176  CB  ARG B 389     2753   2566   2864    -14    144    -85       C  
ATOM   4177  CG  ARG B 389      49.274  11.354  -9.109  1.00 21.24           C  
ANISOU 4177  CG  ARG B 389     2687   2517   2865    -28    122    -96       C  
ATOM   4178  CD  ARG B 389      50.268  10.351  -9.719  1.00 18.89           C  
ANISOU 4178  CD  ARG B 389     2370   2212   2596    -41    128   -120       C  
ATOM   4179  NE  ARG B 389      50.347   9.175  -8.859  1.00 17.12           N  
ANISOU 4179  NE  ARG B 389     2120   1981   2406    -49    105   -126       N  
ATOM   4180  CZ  ARG B 389      51.302   8.961  -7.952  1.00 25.08           C  
ANISOU 4180  CZ  ARG B 389     3113   2968   3448    -59     99   -129       C  
ATOM   4181  NH1 ARG B 389      52.311   9.826  -7.808  1.00 21.73           N  
ANISOU 4181  NH1 ARG B 389     2696   2529   3031    -66    115   -129       N  
ATOM   4182  NH2 ARG B 389      51.262   7.868  -7.196  1.00 18.50           N  
ANISOU 4182  NH2 ARG B 389     2258   2130   2642    -63     79   -131       N  
ATOM   4183  N   VAL B 390      48.663  15.717  -9.648  1.00 20.34           N  
ANISOU 4183  N   VAL B 390     2658   2401   2670      4    183    -42       N  
ATOM   4184  CA  VAL B 390      48.842  17.006 -10.303  1.00 20.67           C  
ANISOU 4184  CA  VAL B 390     2728   2437   2690     13    216    -29       C  
ATOM   4185  C   VAL B 390      49.661  16.730 -11.562  1.00 26.04           C  
ANISOU 4185  C   VAL B 390     3409   3115   3368     10    239    -44       C  
ATOM   4186  O   VAL B 390      50.776  16.225 -11.480  1.00 23.08           O  
ANISOU 4186  O   VAL B 390     3018   2724   3026     -8    243    -63       O  
ATOM   4187  CB  VAL B 390      49.563  18.021  -9.387  1.00 18.12           C  
ANISOU 4187  CB  VAL B 390     2411   2087   2387      3    231    -24       C  
ATOM   4188  CG1 VAL B 390      49.810  19.335 -10.114  1.00 19.54           C  
ANISOU 4188  CG1 VAL B 390     2619   2257   2549     12    270    -11       C  
ATOM   4189  CG2 VAL B 390      48.739  18.271  -8.111  1.00 14.38           C  
ANISOU 4189  CG2 VAL B 390     1934   1616   1913      6    208    -10       C  
ATOM   4190  N   PHE B 391      49.087  17.032 -12.721  1.00 24.32           N  
ANISOU 4190  N   PHE B 391     3211   2917   3114     28    252    -35       N  
ATOM   4191  CA  PHE B 391      49.696  16.693 -14.007  1.00 30.95           C  
ANISOU 4191  CA  PHE B 391     4053   3762   3945     27    272    -49       C  
ATOM   4192  C   PHE B 391      50.179  15.240 -14.084  1.00 29.75           C  
ANISOU 4192  C   PHE B 391     3870   3612   3821     11    254    -77       C  
ATOM   4193  O   PHE B 391      51.126  14.949 -14.807  1.00 36.72           O  
ANISOU 4193  O   PHE B 391     4749   4488   4716      1    273    -94       O  
ATOM   4194  CB  PHE B 391      50.867  17.636 -14.330  1.00 29.01           C  
ANISOU 4194  CB  PHE B 391     3823   3489   3710     20    312    -48       C  
ATOM   4195  CG  PHE B 391      50.437  19.007 -14.811  1.00 33.31           C  
ANISOU 4195  CG  PHE B 391     4403   4035   4221     40    340    -22       C  
ATOM   4196  CD1 PHE B 391      50.008  19.196 -16.118  1.00 43.00           C  
ANISOU 4196  CD1 PHE B 391     5648   5282   5405     60    356    -13       C  
ATOM   4197  CD2 PHE B 391      50.471  20.098 -13.959  1.00 36.54           C  
ANISOU 4197  CD2 PHE B 391     4823   4422   4639     39    352     -6       C  
ATOM   4198  CE1 PHE B 391      49.613  20.453 -16.568  1.00 44.02           C  
ANISOU 4198  CE1 PHE B 391     5811   5412   5504     81    384     15       C  
ATOM   4199  CE2 PHE B 391      50.069  21.357 -14.395  1.00 39.75           C  
ANISOU 4199  CE2 PHE B 391     5261   4826   5016     59    380     20       C  
ATOM   4200  CZ  PHE B 391      49.641  21.535 -15.704  1.00 40.08           C  
ANISOU 4200  CZ  PHE B 391     5323   4888   5016     81    396     32       C  
ATOM   4201  N   GLY B 392      49.532  14.330 -13.358  1.00 29.11           N  
ANISOU 4201  N   GLY B 392     3768   3540   3751      8    221    -82       N  
ATOM   4202  CA  GLY B 392      49.922  12.922 -13.391  1.00 26.53           C  
ANISOU 4202  CA  GLY B 392     3412   3215   3454     -6    205   -107       C  
ATOM   4203  C   GLY B 392      51.211  12.611 -12.626  1.00 21.38           C  
ANISOU 4203  C   GLY B 392     2741   2532   2849    -28    207   -120       C  
ATOM   4204  O   GLY B 392      51.662  11.485 -12.575  1.00 26.39           O  
ANISOU 4204  O   GLY B 392     3352   3164   3513    -40    196   -139       O  
ATOM   4205  N   VAL B 393      51.789  13.628 -12.004  1.00 28.28           N  
ANISOU 4205  N   VAL B 393     3626   3386   3731    -32    220   -109       N  
ATOM   4206  CA  VAL B 393      53.044  13.491 -11.293  1.00 25.56           C  
ANISOU 4206  CA  VAL B 393     3266   3016   3429    -50    223   -122       C  
ATOM   4207  C   VAL B 393      52.873  13.336  -9.773  1.00 27.75           C  
ANISOU 4207  C   VAL B 393     3529   3287   3728    -55    196   -115       C  
ATOM   4208  O   VAL B 393      53.068  12.252  -9.227  1.00 27.83           O  
ANISOU 4208  O   VAL B 393     3515   3295   3765    -62    174   -125       O  
ATOM   4209  CB  VAL B 393      53.940  14.702 -11.598  1.00 28.94           C  
ANISOU 4209  CB  VAL B 393     3712   3425   3858    -54    259   -121       C  
ATOM   4210  CG1 VAL B 393      55.182  14.686 -10.738  1.00 29.59           C  
ANISOU 4210  CG1 VAL B 393     3776   3483   3984    -73    260   -135       C  
ATOM   4211  CG2 VAL B 393      54.287  14.728 -13.076  1.00 39.40           C  
ANISOU 4211  CG2 VAL B 393     5049   4755   5167    -52    287   -129       C  
ATOM   4212  N   LEU B 394      52.519  14.418  -9.091  1.00 26.29           N  
ANISOU 4212  N   LEU B 394     3360   3098   3530    -49    199    -97       N  
ATOM   4213  CA  LEU B 394      52.487  14.413  -7.625  1.00 30.17           C  
ANISOU 4213  CA  LEU B 394     3840   3584   4041    -54    177    -92       C  
ATOM   4214  C   LEU B 394      51.138  14.002  -7.043  1.00 25.28           C  
ANISOU 4214  C   LEU B 394     3219   2981   3404    -43    148    -76       C  
ATOM   4215  O   LEU B 394      50.100  14.549  -7.411  1.00 22.45           O  
ANISOU 4215  O   LEU B 394     2880   2636   3013    -29    151    -61       O  
ATOM   4216  CB  LEU B 394      52.854  15.795  -7.096  1.00 27.51           C  
ANISOU 4216  CB  LEU B 394     3518   3232   3703    -56    195    -84       C  
ATOM   4217  CG  LEU B 394      53.972  15.899  -6.065  1.00 37.94           C  
ANISOU 4217  CG  LEU B 394     4821   4536   5060    -71    193    -97       C  
ATOM   4218  CD1 LEU B 394      55.206  15.126  -6.521  1.00 37.02           C  
ANISOU 4218  CD1 LEU B 394     4685   4409   4974    -84    199   -121       C  
ATOM   4219  CD2 LEU B 394      54.298  17.367  -5.824  1.00 38.08           C  
ANISOU 4219  CD2 LEU B 394     4856   4540   5075    -74    219    -93       C  
ATOM   4220  N   ALA B 395      51.170  13.062  -6.100  1.00 21.32           N  
ANISOU 4220  N   ALA B 395     2695   2478   2926    -49    122    -80       N  
ATOM   4221  CA  ALA B 395      49.962  12.583  -5.433  1.00 15.76           C  
ANISOU 4221  CA  ALA B 395     1988   1787   2212    -41     96    -67       C  
ATOM   4222  C   ALA B 395      49.422  13.528  -4.354  1.00 20.42           C  
ANISOU 4222  C   ALA B 395     2590   2378   2791    -37     89    -49       C  
ATOM   4223  O   ALA B 395      48.359  13.284  -3.785  1.00 22.27           O  
ANISOU 4223  O   ALA B 395     2824   2623   3014    -29     70    -37       O  
ATOM   4224  CB  ALA B 395      50.205  11.181  -4.817  1.00 20.84           C  
ANISOU 4224  CB  ALA B 395     2604   2428   2887    -48     73    -76       C  
ATOM   4225  N  AMET B 396      50.148  14.591  -4.051  0.57 24.78           N  
ANISOU 4225  N  AMET B 396     3151   2918   3347    -42    106    -49       N  
ATOM   4226  N  BMET B 396      50.168  14.587  -4.059  0.43 24.76           N  
ANISOU 4226  N  BMET B 396     3148   2915   3345    -42    106    -49       N  
ATOM   4227  CA AMET B 396      49.628  15.560  -3.092  0.57 22.92           C  
ANISOU 4227  CA AMET B 396     2927   2682   3101    -38    103    -34       C  
ATOM   4228  CA BMET B 396      49.727  15.584  -3.083  0.43 22.91           C  
ANISOU 4228  CA BMET B 396     2925   2680   3101    -39    104    -35       C  
ATOM   4229  C  AMET B 396      49.503  16.926  -3.745  0.57 21.79           C  
ANISOU 4229  C  AMET B 396     2810   2535   2936    -32    133    -26       C  
ATOM   4230  C  BMET B 396      49.494  16.926  -3.772  0.43 21.82           C  
ANISOU 4230  C  BMET B 396     2813   2539   2939    -32    133    -26       C  
ATOM   4231  O  AMET B 396      50.202  17.228  -4.703  0.57 23.23           O  
ANISOU 4231  O  AMET B 396     2998   2709   3118    -34    158    -34       O  
ATOM   4232  O  BMET B 396      50.114  17.213  -4.790  0.43 23.28           O  
ANISOU 4232  O  BMET B 396     3007   2717   3123    -33    158    -33       O  
ATOM   4233  CB AMET B 396      50.495  15.617  -1.838  0.57 22.84           C  
ANISOU 4233  CB AMET B 396     2900   2660   3116    -50     94    -40       C  
ATOM   4234  CB BMET B 396      50.744  15.725  -1.944  0.43 22.88           C  
ANISOU 4234  CB BMET B 396     2906   2663   3125    -52     99    -43       C  
ATOM   4235  CG AMET B 396      51.847  16.250  -2.040  0.57 22.62           C  
ANISOU 4235  CG AMET B 396     2871   2616   3108    -61    117    -57       C  
ATOM   4236  CG BMET B 396      52.144  16.166  -2.367  0.43 22.73           C  
ANISOU 4236  CG BMET B 396     2883   2628   3126    -63    123    -62       C  
ATOM   4237  SD AMET B 396      52.962  15.779  -0.709  0.57 27.34           S  
ANISOU 4237  SD AMET B 396     3439   3207   3741    -74     98    -71       S  
ATOM   4238  SD BMET B 396      53.173  14.882  -3.127  0.43 26.31           S  
ANISOU 4238  SD BMET B 396     3315   3075   3607    -71    122    -83       S  
ATOM   4239  CE AMET B 396      53.235  14.047  -1.105  0.57 25.45           C  
ANISOU 4239  CE AMET B 396     3177   2970   3521    -74     79    -79       C  
ATOM   4240  CE BMET B 396      53.116  13.577  -1.897  0.43 22.97           C  
ANISOU 4240  CE BMET B 396     2864   2658   3205    -73     83    -82       C  
ATOM   4241  N   SER B 397      48.589  17.738  -3.232  1.00 18.76           N  
ANISOU 4241  N   SER B 397     2440   2156   2531    -23    131     -9       N  
ATOM   4242  CA  SER B 397      48.282  19.035  -3.839  1.00 18.62           C  
ANISOU 4242  CA  SER B 397     2449   2135   2492    -14    160      3       C  
ATOM   4243  C   SER B 397      49.031  20.166  -3.141  1.00 17.32           C  
ANISOU 4243  C   SER B 397     2288   1951   2342    -24    179      0       C  
ATOM   4244  O   SER B 397      49.010  21.311  -3.579  1.00 17.17           O  
ANISOU 4244  O   SER B 397     2290   1923   2312    -18    208      8       O  
ATOM   4245  CB  SER B 397      46.774  19.290  -3.790  1.00 19.75           C  
ANISOU 4245  CB  SER B 397     2605   2295   2605      3    148     23       C  
ATOM   4246  OG  SER B 397      46.270  19.174  -2.462  1.00 20.76           O  
ANISOU 4246  OG  SER B 397     2724   2426   2739      0    125     28       O  
ATOM   4247  N   ARG B 398      49.691  19.833  -2.044  1.00 14.50           N  
ANISOU 4247  N   ARG B 398     1910   1588   2010    -37    163    -12       N  
ATOM   4248  CA  ARG B 398      50.448  20.816  -1.292  1.00 22.49           C  
ANISOU 4248  CA  ARG B 398     2921   2585   3039    -49    179    -21       C  
ATOM   4249  C   ARG B 398      51.688  20.167  -0.756  1.00 21.84           C  
ANISOU 4249  C   ARG B 398     2813   2497   2990    -64    169    -43       C  
ATOM   4250  O   ARG B 398      51.657  19.004  -0.367  1.00 18.39           O  
ANISOU 4250  O   ARG B 398     2358   2070   2561    -65    140    -45       O  
ATOM   4251  CB  ARG B 398      49.621  21.380  -0.123  1.00 19.16           C  
ANISOU 4251  CB  ARG B 398     2503   2169   2609    -46    166     -9       C  
ATOM   4252  CG  ARG B 398      48.363  22.083  -0.586  1.00 21.52           C  
ANISOU 4252  CG  ARG B 398     2826   2474   2877    -29    176     14       C  
ATOM   4253  CD  ARG B 398      47.752  22.909   0.502  1.00 20.02           C  
ANISOU 4253  CD  ARG B 398     2641   2284   2682    -29    173     22       C  
ATOM   4254  NE  ARG B 398      46.437  23.384   0.113  1.00 18.25           N  
ANISOU 4254  NE  ARG B 398     2438   2069   2429    -11    176     44       N  
ATOM   4255  CZ  ARG B 398      45.732  24.263   0.809  1.00 26.66           C  
ANISOU 4255  CZ  ARG B 398     3511   3132   3485     -8    179     54       C  
ATOM   4256  NH1 ARG B 398      46.227  24.763   1.937  1.00 19.82           N  
ANISOU 4256  NH1 ARG B 398     2635   2258   2637    -22    180     43       N  
ATOM   4257  NH2 ARG B 398      44.535  24.638   0.374  1.00 18.83           N  
ANISOU 4257  NH2 ARG B 398     2537   2148   2467     10    181     74       N  
ATOM   4258  N   SER B 399      52.785  20.913  -0.753  1.00 15.23           N  
ANISOU 4258  N   SER B 399     1972   1642   2172    -76    194    -60       N  
ATOM   4259  CA  SER B 399      53.957  20.473  -0.015  1.00 23.94           C  
ANISOU 4259  CA  SER B 399     3049   2741   3306    -90    183    -83       C  
ATOM   4260  C   SER B 399      54.975  21.599   0.031  1.00 19.83           C  
ANISOU 4260  C   SER B 399     2528   2202   2805   -103    216   -102       C  
ATOM   4261  O   SER B 399      54.751  22.661  -0.541  1.00 23.06           O  
ANISOU 4261  O   SER B 399     2959   2599   3204   -100    249    -95       O  
ATOM   4262  CB  SER B 399      54.584  19.239  -0.664  1.00 24.25           C  
ANISOU 4262  CB  SER B 399     3073   2782   3361    -93    173    -94       C  
ATOM   4263  OG  SER B 399      55.264  19.624  -1.841  1.00 37.43           O  
ANISOU 4263  OG  SER B 399     4751   4436   5035    -97    207   -104       O  
ATOM   4264  N   ILE B 400      56.070  21.362   0.740  1.00 17.21           N  
ANISOU 4264  N   ILE B 400     2171   1868   2502   -116    207   -126       N  
ATOM   4265  CA  ILE B 400      57.179  22.300   0.820  1.00 18.79           C  
ANISOU 4265  CA  ILE B 400     2364   2050   2726   -130    237   -151       C  
ATOM   4266  C   ILE B 400      58.140  21.963  -0.306  1.00 23.63           C  
ANISOU 4266  C   ILE B 400     2974   2649   3356   -136    259   -167       C  
ATOM   4267  O   ILE B 400      58.484  20.794  -0.486  1.00 20.85           O  
ANISOU 4267  O   ILE B 400     2605   2304   3013   -136    238   -172       O  
ATOM   4268  CB  ILE B 400      57.970  22.117   2.123  1.00 23.69           C  
ANISOU 4268  CB  ILE B 400     2953   2678   3369   -140    215   -174       C  
ATOM   4269  CG1 ILE B 400      57.047  22.142   3.347  1.00 22.99           C  
ANISOU 4269  CG1 ILE B 400     2863   2608   3262   -134    185   -159       C  
ATOM   4270  CG2 ILE B 400      59.038  23.188   2.240  1.00 21.01           C  
ANISOU 4270  CG2 ILE B 400     2606   2322   3055   -156    248   -204       C  
ATOM   4271  CD1 ILE B 400      56.434  23.465   3.586  1.00 20.79           C  
ANISOU 4271  CD1 ILE B 400     2604   2324   2972   -134    208   -153       C  
ATOM   4272  N   GLY B 401      58.589  22.983  -1.033  1.00 20.60           N  
ANISOU 4272  N   GLY B 401     2605   2245   2979   -142    303   -174       N  
ATOM   4273  CA  GLY B 401      59.468  22.803  -2.177  1.00 22.01           C  
ANISOU 4273  CA  GLY B 401     2784   2408   3172   -148    330   -188       C  
ATOM   4274  C   GLY B 401      58.688  22.601  -3.467  1.00 27.61           C  
ANISOU 4274  C   GLY B 401     3520   3119   3852   -134    343   -164       C  
ATOM   4275  O   GLY B 401      57.666  23.246  -3.694  1.00 29.00           O  
ANISOU 4275  O   GLY B 401     3722   3298   4000   -122    352   -139       O  
ATOM   4276  N   ASP B 402      59.174  21.703  -4.322  1.00 32.28           N  
ANISOU 4276  N   ASP B 402     4105   3710   4449   -136    342   -172       N  
ATOM   4277  CA  ASP B 402      58.495  21.386  -5.583  1.00 24.99           C  
ANISOU 4277  CA  ASP B 402     3204   2793   3498   -123    351   -152       C  
ATOM   4278  C   ASP B 402      58.223  22.613  -6.449  1.00 28.72           C  
ANISOU 4278  C   ASP B 402     3709   3252   3951   -116    396   -138       C  
ATOM   4279  O   ASP B 402      57.199  22.699  -7.132  1.00 25.48           O  
ANISOU 4279  O   ASP B 402     3323   2853   3506    -98    398   -113       O  
ATOM   4280  CB  ASP B 402      57.197  20.626  -5.298  1.00 26.26           C  
ANISOU 4280  CB  ASP B 402     3368   2979   3632   -107    312   -130       C  
ATOM   4281  CG  ASP B 402      57.451  19.257  -4.691  1.00 29.65           C  
ANISOU 4281  CG  ASP B 402     3766   3419   4079   -112    272   -141       C  
ATOM   4282  OD1 ASP B 402      58.302  18.524  -5.230  1.00 34.18           O  
ANISOU 4282  OD1 ASP B 402     4326   3989   4674   -120    275   -159       O  
ATOM   4283  OD2 ASP B 402      56.810  18.907  -3.675  1.00 32.63           O  
ANISOU 4283  OD2 ASP B 402     4136   3811   4453   -107    239   -131       O  
ATOM   4284  N   ARG B 403      59.153  23.557  -6.433  1.00 24.03           N  
ANISOU 4284  N   ARG B 403     3116   2634   3380   -128    433   -155       N  
ATOM   4285  CA  ARG B 403      58.960  24.803  -7.159  1.00 25.35           C  
ANISOU 4285  CA  ARG B 403     3315   2784   3533   -122    480   -140       C  
ATOM   4286  C   ARG B 403      58.626  24.567  -8.635  1.00 25.60           C  
ANISOU 4286  C   ARG B 403     3370   2820   3536   -108    498   -123       C  
ATOM   4287  O   ARG B 403      57.950  25.385  -9.249  1.00 27.54           O  
ANISOU 4287  O   ARG B 403     3647   3063   3754    -92    524    -99       O  
ATOM   4288  CB  ARG B 403      60.166  25.743  -6.988  1.00 33.31           C  
ANISOU 4288  CB  ARG B 403     4317   3763   4577   -141    521   -166       C  
ATOM   4289  CG  ARG B 403      61.152  25.705  -8.139  1.00 34.84           C  
ANISOU 4289  CG  ARG B 403     4515   3938   4784   -149    559   -181       C  
ATOM   4290  CD  ARG B 403      62.459  26.422  -7.788  1.00 43.45           C  
ANISOU 4290  CD  ARG B 403     5590   5000   5918   -171    594   -215       C  
ATOM   4291  NE  ARG B 403      63.062  25.812  -6.611  1.00 40.18           N  
ANISOU 4291  NE  ARG B 403     5138   4596   5534   -185    556   -243       N  
ATOM   4292  CZ  ARG B 403      64.309  25.367  -6.529  1.00 34.26           C  
ANISOU 4292  CZ  ARG B 403     4359   3838   4821   -203    558   -278       C  
ATOM   4293  NH1 ARG B 403      65.144  25.469  -7.556  1.00 36.62           N  
ANISOU 4293  NH1 ARG B 403     4664   4116   5134   -211    597   -292       N  
ATOM   4294  NH2 ARG B 403      64.725  24.824  -5.396  1.00 36.09           N  
ANISOU 4294  NH2 ARG B 403     4557   4081   5074   -211    520   -300       N  
ATOM   4295  N   TYR B 404      59.069  23.448  -9.208  1.00 24.51           N  
ANISOU 4295  N   TYR B 404     3219   2691   3404   -112    485   -137       N  
ATOM   4296  CA  TYR B 404      58.699  23.163 -10.600  1.00 26.83           C  
ANISOU 4296  CA  TYR B 404     3533   2993   3667    -98    499   -122       C  
ATOM   4297  C   TYR B 404      57.188  23.000 -10.801  1.00 30.56           C  
ANISOU 4297  C   TYR B 404     4023   3493   4096    -74    475    -92       C  
ATOM   4298  O   TYR B 404      56.694  23.106 -11.924  1.00 24.48           O  
ANISOU 4298  O   TYR B 404     3277   2732   3293    -58    491    -75       O  
ATOM   4299  CB  TYR B 404      59.435  21.937 -11.170  1.00 33.64           C  
ANISOU 4299  CB  TYR B 404     4376   3862   4546   -108    488   -145       C  
ATOM   4300  CG  TYR B 404      58.862  20.600 -10.744  1.00 30.47           C  
ANISOU 4300  CG  TYR B 404     3952   3485   4140   -105    436   -146       C  
ATOM   4301  CD1 TYR B 404      58.911  20.207  -9.419  1.00 31.42           C  
ANISOU 4301  CD1 TYR B 404     4047   3608   4283   -112    401   -154       C  
ATOM   4302  CD2 TYR B 404      58.289  19.725 -11.669  1.00 34.26           C  
ANISOU 4302  CD2 TYR B 404     4436   3986   4595    -94    424   -139       C  
ATOM   4303  CE1 TYR B 404      58.412  18.994  -9.007  1.00 29.92           C  
ANISOU 4303  CE1 TYR B 404     3838   3438   4092   -109    358   -153       C  
ATOM   4304  CE2 TYR B 404      57.767  18.491 -11.261  1.00 31.41           C  
ANISOU 4304  CE2 TYR B 404     4054   3645   4235    -92    380   -142       C  
ATOM   4305  CZ  TYR B 404      57.841  18.140  -9.922  1.00 34.41           C  
ANISOU 4305  CZ  TYR B 404     4411   4024   4639   -100    348   -147       C  
ATOM   4306  OH  TYR B 404      57.354  16.936  -9.451  1.00 36.84           O  
ANISOU 4306  OH  TYR B 404     4699   4349   4951    -97    308   -148       O  
ATOM   4307  N   LEU B 405      56.445  22.745  -9.731  1.00 23.92           N  
ANISOU 4307  N   LEU B 405     3171   2666   3253    -71    437    -85       N  
ATOM   4308  CA  LEU B 405      54.991  22.600  -9.873  1.00 23.72           C  
ANISOU 4308  CA  LEU B 405     3160   2665   3188    -49    415    -58       C  
ATOM   4309  C   LEU B 405      54.174  23.740  -9.255  1.00 24.93           C  
ANISOU 4309  C   LEU B 405     3332   2815   3326    -39    421    -35       C  
ATOM   4310  O   LEU B 405      52.949  23.651  -9.156  1.00 26.70           O  
ANISOU 4310  O   LEU B 405     3564   3059   3522    -22    399    -15       O  
ATOM   4311  CB  LEU B 405      54.520  21.246  -9.339  1.00 33.47           C  
ANISOU 4311  CB  LEU B 405     4370   3922   4425    -50    365    -64       C  
ATOM   4312  CG  LEU B 405      54.750  20.072 -10.293  1.00 33.18           C  
ANISOU 4312  CG  LEU B 405     4323   3898   4386    -51    357    -76       C  
ATOM   4313  CD1 LEU B 405      54.468  18.740  -9.613  1.00 30.79           C  
ANISOU 4313  CD1 LEU B 405     3993   3611   4096    -56    312    -85       C  
ATOM   4314  CD2 LEU B 405      53.903  20.225 -11.542  1.00 32.07           C  
ANISOU 4314  CD2 LEU B 405     4208   3775   4203    -30    370    -58       C  
ATOM   4315  N   LYS B 406      54.848  24.806  -8.835  1.00 27.44           N  
ANISOU 4315  N   LYS B 406     3653   3106   3665    -49    453    -41       N  
ATOM   4316  CA  LYS B 406      54.147  26.017  -8.416  1.00 35.42           C  
ANISOU 4316  CA  LYS B 406     4685   4110   4664    -39    469    -21       C  
ATOM   4317  C   LYS B 406      53.560  26.658  -9.677  1.00 36.22           C  
ANISOU 4317  C   LYS B 406     4821   4212   4730    -16    500      6       C  
ATOM   4318  O   LYS B 406      54.184  26.613 -10.738  1.00 33.82           O  
ANISOU 4318  O   LYS B 406     4526   3901   4423    -16    528      2       O  
ATOM   4319  CB  LYS B 406      55.100  26.971  -7.691  1.00 31.21           C  
ANISOU 4319  CB  LYS B 406     4144   3546   4167    -58    498    -39       C  
ATOM   4320  CG  LYS B 406      55.641  26.427  -6.363  1.00 34.33           C  
ANISOU 4320  CG  LYS B 406     4506   3945   4595    -78    465    -65       C  
ATOM   4321  CD  LYS B 406      56.865  27.216  -5.878  1.00 36.96           C  
ANISOU 4321  CD  LYS B 406     4827   4250   4966    -99    496    -92       C  
ATOM   4322  CE  LYS B 406      56.731  27.654  -4.420  1.00 47.55           C  
ANISOU 4322  CE  LYS B 406     6153   5593   6323   -108    479   -101       C  
ATOM   4323  NZ  LYS B 406      56.723  26.536  -3.427  1.00 33.87           N  
ANISOU 4323  NZ  LYS B 406     4390   3882   4598   -114    427   -113       N  
ATOM   4324  N   PRO B 407      52.351  27.236  -9.578  1.00 31.03           N  
ANISOU 4324  N   PRO B 407     4183   3565   4044      5    496     34       N  
ATOM   4325  CA  PRO B 407      51.540  27.465  -8.372  1.00 33.35           C  
ANISOU 4325  CA  PRO B 407     4468   3865   4337      6    469     41       C  
ATOM   4326  C   PRO B 407      50.511  26.371  -8.087  1.00 26.66           C  
ANISOU 4326  C   PRO B 407     3609   3051   3471     15    418     47       C  
ATOM   4327  O   PRO B 407      49.585  26.617  -7.317  1.00 30.93           O  
ANISOU 4327  O   PRO B 407     4151   3600   4002     22    399     59       O  
ATOM   4328  CB  PRO B 407      50.768  28.729  -8.747  1.00 29.92           C  
ANISOU 4328  CB  PRO B 407     4067   3423   3880     28    500     71       C  
ATOM   4329  CG  PRO B 407      50.462  28.495 -10.199  1.00 35.45           C  
ANISOU 4329  CG  PRO B 407     4786   4137   4544     49    512     88       C  
ATOM   4330  CD  PRO B 407      51.708  27.811 -10.774  1.00 30.66           C  
ANISOU 4330  CD  PRO B 407     4168   3523   3958     32    522     63       C  
ATOM   4331  N   TYR B 408      50.648  25.210  -8.717  1.00 32.04           N  
ANISOU 4331  N   TYR B 408     4279   3749   4145     15    399     37       N  
ATOM   4332  CA  TYR B 408      49.645  24.155  -8.617  1.00 29.93           C  
ANISOU 4332  CA  TYR B 408     4001   3512   3860     24    355     41       C  
ATOM   4333  C   TYR B 408      49.732  23.445  -7.270  1.00 32.09           C  
ANISOU 4333  C   TYR B 408     4246   3788   4159      8    319     27       C  
ATOM   4334  O   TYR B 408      48.715  23.152  -6.642  1.00 21.23           O  
ANISOU 4334  O   TYR B 408     2866   2429   2771     15    289     36       O  
ATOM   4335  CB  TYR B 408      49.788  23.174  -9.783  1.00 25.21           C  
ANISOU 4335  CB  TYR B 408     3400   2931   3249     29    351     34       C  
ATOM   4336  CG  TYR B 408      49.894  23.902 -11.106  1.00 35.83           C  
ANISOU 4336  CG  TYR B 408     4773   4273   4569     44    390     47       C  
ATOM   4337  CD1 TYR B 408      51.085  23.927 -11.819  1.00 35.61           C  
ANISOU 4337  CD1 TYR B 408     4747   4228   4556     33    421     33       C  
ATOM   4338  CD2 TYR B 408      48.814  24.613 -11.609  1.00 34.68           C  
ANISOU 4338  CD2 TYR B 408     4652   4139   4384     71    398     75       C  
ATOM   4339  CE1 TYR B 408      51.181  24.608 -13.018  1.00 39.00           C  
ANISOU 4339  CE1 TYR B 408     5203   4653   4960     48    459     47       C  
ATOM   4340  CE2 TYR B 408      48.899  25.296 -12.803  1.00 38.70           C  
ANISOU 4340  CE2 TYR B 408     5189   4647   4868     88    435     90       C  
ATOM   4341  CZ  TYR B 408      50.083  25.293 -13.503  1.00 37.30           C  
ANISOU 4341  CZ  TYR B 408     5014   4452   4705     76    466     77       C  
ATOM   4342  OH  TYR B 408      50.161  25.981 -14.695  1.00 51.79           O  
ANISOU 4342  OH  TYR B 408     6879   6285   6513     94    505     94       O  
ATOM   4343  N   VAL B 409      50.949  23.168  -6.822  1.00 28.57           N  
ANISOU 4343  N   VAL B 409     3781   3327   3748    -14    322      3       N  
ATOM   4344  CA  VAL B 409      51.112  22.742  -5.451  1.00 31.56           C  
ANISOU 4344  CA  VAL B 409     4136   3706   4151    -28    292     -8       C  
ATOM   4345  C   VAL B 409      51.719  23.922  -4.701  1.00 30.42           C  
ANISOU 4345  C   VAL B 409     3993   3539   4026    -39    316    -14       C  
ATOM   4346  O   VAL B 409      52.526  24.677  -5.260  1.00 34.32           O  
ANISOU 4346  O   VAL B 409     4497   4012   4530    -44    355    -21       O  
ATOM   4347  CB  VAL B 409      51.882  21.381  -5.332  1.00 36.98           C  
ANISOU 4347  CB  VAL B 409     4793   4396   4861    -41    268    -30       C  
ATOM   4348  CG1 VAL B 409      52.291  20.885  -6.688  1.00 32.11           C  
ANISOU 4348  CG1 VAL B 409     4180   3780   4238    -39    284    -37       C  
ATOM   4349  CG2 VAL B 409      53.057  21.462  -4.390  1.00 28.84           C  
ANISOU 4349  CG2 VAL B 409     3742   3350   3867    -61    268    -52       C  
ATOM   4350  N   ILE B 410      51.261  24.123  -3.472  1.00 24.18           N  
ANISOU 4350  N   ILE B 410     3196   2753   3240    -42    296    -12       N  
ATOM   4351  CA  ILE B 410      51.645  25.278  -2.675  1.00 18.94           C  
ANISOU 4351  CA  ILE B 410     2533   2071   2592    -51    317    -18       C  
ATOM   4352  C   ILE B 410      52.071  24.824  -1.300  1.00 22.55           C  
ANISOU 4352  C   ILE B 410     2962   2534   3072    -67    287    -36       C  
ATOM   4353  O   ILE B 410      51.663  23.748  -0.851  1.00 20.77           O  
ANISOU 4353  O   ILE B 410     2722   2326   2842    -64    249    -34       O  
ATOM   4354  CB  ILE B 410      50.487  26.283  -2.530  1.00 25.03           C  
ANISOU 4354  CB  ILE B 410     3328   2844   3341    -36    327      6       C  
ATOM   4355  CG1 ILE B 410      49.236  25.588  -1.983  1.00 19.53           C  
ANISOU 4355  CG1 ILE B 410     2627   2172   2623    -25    286     21       C  
ATOM   4356  CG2 ILE B 410      50.174  26.938  -3.865  1.00 28.60           C  
ANISOU 4356  CG2 ILE B 410     3809   3289   3771    -19    362     25       C  
ATOM   4357  CD1 ILE B 410      48.064  26.523  -1.794  1.00 27.08           C  
ANISOU 4357  CD1 ILE B 410     3602   3129   3556    -11    293     44       C  
ATOM   4358  N   PRO B 411      52.889  25.650  -0.619  1.00 23.80           N  
ANISOU 4358  N   PRO B 411     3112   2676   3255    -81    306    -55       N  
ATOM   4359  CA  PRO B 411      53.419  25.343   0.716  1.00 22.68           C  
ANISOU 4359  CA  PRO B 411     2943   2541   3135    -96    281    -75       C  
ATOM   4360  C   PRO B 411      52.459  25.681   1.867  1.00 26.95           C  
ANISOU 4360  C   PRO B 411     3484   3093   3662    -92    261    -64       C  
ATOM   4361  O   PRO B 411      52.832  25.494   3.026  1.00 28.97           O  
ANISOU 4361  O   PRO B 411     3718   3357   3931   -102    239    -79       O  
ATOM   4362  CB  PRO B 411      54.668  26.231   0.797  1.00 28.06           C  
ANISOU 4362  CB  PRO B 411     3617   3200   3846   -113    315   -102       C  
ATOM   4363  CG  PRO B 411      54.320  27.419  -0.079  1.00 25.71           C  
ANISOU 4363  CG  PRO B 411     3349   2883   3538   -105    361    -87       C  
ATOM   4364  CD  PRO B 411      53.524  26.847  -1.209  1.00 23.43           C  
ANISOU 4364  CD  PRO B 411     3080   2603   3219    -86    356    -61       C  
ATOM   4365  N   GLU B 412      51.247  26.139   1.556  1.00 20.04           N  
ANISOU 4365  N   GLU B 412     2633   2222   2761    -76    266    -38       N  
ATOM   4366  CA  GLU B 412      50.330  26.676   2.567  1.00 23.96           C  
ANISOU 4366  CA  GLU B 412     3133   2726   3246    -73    255    -28       C  
ATOM   4367  C   GLU B 412      49.658  25.582   3.428  1.00 18.49           C  
ANISOU 4367  C   GLU B 412     2426   2058   2543    -70    208    -21       C  
ATOM   4368  O   GLU B 412      48.933  24.738   2.913  1.00 21.49           O  
ANISOU 4368  O   GLU B 412     2811   2450   2905    -58    189     -5       O  
ATOM   4369  CB  GLU B 412      49.290  27.561   1.867  1.00 24.85           C  
ANISOU 4369  CB  GLU B 412     3275   2833   3336    -57    279     -2       C  
ATOM   4370  CG  GLU B 412      48.213  28.135   2.750  1.00 33.28           C  
ANISOU 4370  CG  GLU B 412     4349   3907   4390    -51    270     10       C  
ATOM   4371  CD  GLU B 412      47.158  28.890   1.943  1.00 45.21           C  
ANISOU 4371  CD  GLU B 412     5889   5413   5877    -31    291     37       C  
ATOM   4372  OE1 GLU B 412      45.945  28.667   2.186  1.00 34.71           O  
ANISOU 4372  OE1 GLU B 412     4564   4099   4525    -19    269     56       O  
ATOM   4373  OE2 GLU B 412      47.549  29.694   1.059  1.00 40.68           O  
ANISOU 4373  OE2 GLU B 412     5331   4819   5306    -28    330     41       O  
ATOM   4374  N   PRO B 413      49.921  25.580   4.742  1.00 19.25           N  
ANISOU 4374  N   PRO B 413     2503   2161   2650    -80    190    -34       N  
ATOM   4375  CA  PRO B 413      49.399  24.502   5.595  1.00 20.45           C  
ANISOU 4375  CA  PRO B 413     2642   2334   2793    -77    148    -27       C  
ATOM   4376  C   PRO B 413      47.960  24.737   6.007  1.00 17.07           C  
ANISOU 4376  C   PRO B 413     2228   1917   2342    -66    137     -5       C  
ATOM   4377  O   PRO B 413      47.453  25.843   5.842  1.00 18.50           O  
ANISOU 4377  O   PRO B 413     2426   2089   2514    -63    161      2       O  
ATOM   4378  CB  PRO B 413      50.284  24.594   6.838  1.00 17.29           C  
ANISOU 4378  CB  PRO B 413     2218   1939   2412    -92    137    -50       C  
ATOM   4379  CG  PRO B 413      50.611  26.056   6.931  1.00 18.28           C  
ANISOU 4379  CG  PRO B 413     2350   2049   2547   -100    172    -64       C  
ATOM   4380  CD  PRO B 413      50.789  26.505   5.493  1.00 19.01           C  
ANISOU 4380  CD  PRO B 413     2462   2121   2641    -96    208    -58       C  
ATOM   4381  N   GLU B 414      47.309  23.700   6.530  1.00 22.66           N  
ANISOU 4381  N   GLU B 414     2928   2642   3039    -61    103      5       N  
ATOM   4382  CA  GLU B 414      46.071  23.876   7.292  1.00 26.43           C  
ANISOU 4382  CA  GLU B 414     3413   3132   3499    -54     90     21       C  
ATOM   4383  C   GLU B 414      46.313  23.567   8.766  1.00 20.86           C  
ANISOU 4383  C   GLU B 414     2689   2438   2799    -63     65     12       C  
ATOM   4384  O   GLU B 414      47.019  22.614   9.103  1.00 16.28           O  
ANISOU 4384  O   GLU B 414     2090   1865   2229    -67     45      4       O  
ATOM   4385  CB  GLU B 414      44.923  23.026   6.722  1.00 27.72           C  
ANISOU 4385  CB  GLU B 414     3584   3304   3643    -40     73     41       C  
ATOM   4386  CG  GLU B 414      44.247  23.676   5.514  1.00 31.09           C  
ANISOU 4386  CG  GLU B 414     4034   3724   4054    -27     96     54       C  
ATOM   4387  CD  GLU B 414      43.159  22.805   4.890  1.00 41.31           C  
ANISOU 4387  CD  GLU B 414     5333   5032   5330    -13     80     69       C  
ATOM   4388  OE1 GLU B 414      41.970  22.986   5.238  1.00 47.85           O  
ANISOU 4388  OE1 GLU B 414     6170   5870   6143     -4     71     82       O  
ATOM   4389  OE2 GLU B 414      43.496  21.939   4.053  1.00 34.84           O  
ANISOU 4389  OE2 GLU B 414     4509   4214   4513    -11     75     66       O  
ATOM   4390  N   VAL B 415      45.712  24.377   9.636  1.00 20.27           N  
ANISOU 4390  N   VAL B 415     2619   2367   2715    -65     68     14       N  
ATOM   4391  CA  VAL B 415      45.998  24.327  11.065  1.00 19.23           C  
ANISOU 4391  CA  VAL B 415     2470   2248   2586    -74     49      3       C  
ATOM   4392  C   VAL B 415      44.786  23.890  11.888  1.00 20.51           C  
ANISOU 4392  C   VAL B 415     2636   2426   2730    -67     26     21       C  
ATOM   4393  O   VAL B 415      43.689  24.447  11.767  1.00 18.33           O  
ANISOU 4393  O   VAL B 415     2377   2149   2440    -61     35     35       O  
ATOM   4394  CB  VAL B 415      46.470  25.701  11.583  1.00 25.21           C  
ANISOU 4394  CB  VAL B 415     3227   2999   3353    -85     73    -16       C  
ATOM   4395  CG1 VAL B 415      46.656  25.665  13.079  1.00 25.73           C  
ANISOU 4395  CG1 VAL B 415     3276   3083   3418    -93     53    -28       C  
ATOM   4396  CG2 VAL B 415      47.762  26.121  10.878  1.00 15.43           C  
ANISOU 4396  CG2 VAL B 415     1982   1743   2137    -94     98    -37       C  
ATOM   4397  N   THR B 416      45.018  22.919  12.762  1.00 15.45           N  
ANISOU 4397  N   THR B 416     1980   1801   2090    -68     -2     21       N  
ATOM   4398  CA  THR B 416      43.979  22.371  13.629  1.00 14.61           C  
ANISOU 4398  CA  THR B 416     1875   1709   1967    -62    -24     38       C  
ATOM   4399  C   THR B 416      44.300  22.714  15.081  1.00 20.08           C  
ANISOU 4399  C   THR B 416     2555   2416   2657    -70    -35     27       C  
ATOM   4400  O   THR B 416      45.381  22.414  15.580  1.00 19.14           O  
ANISOU 4400  O   THR B 416     2419   2305   2548    -75    -45     12       O  
ATOM   4401  CB  THR B 416      43.838  20.843  13.451  1.00 17.10           C  
ANISOU 4401  CB  THR B 416     2184   2030   2283    -54    -47     51       C  
ATOM   4402  OG1 THR B 416      43.374  20.569  12.123  1.00 23.17           O  
ANISOU 4402  OG1 THR B 416     2964   2788   3051    -46    -38     59       O  
ATOM   4403  CG2 THR B 416      42.820  20.264  14.445  1.00 22.64           C  
ANISOU 4403  CG2 THR B 416     2886   2745   2970    -49    -68     67       C  
ATOM   4404  N   PHE B 417      43.350  23.355  15.745  1.00 16.55           N  
ANISOU 4404  N   PHE B 417     2118   1975   2195    -70    -32     32       N  
ATOM   4405  CA  PHE B 417      43.524  23.808  17.119  1.00 22.46           C  
ANISOU 4405  CA  PHE B 417     2857   2739   2938    -78    -40     21       C  
ATOM   4406  C   PHE B 417      42.646  22.927  18.001  1.00 17.49           C  
ANISOU 4406  C   PHE B 417     2228   2126   2292    -71    -65     40       C  
ATOM   4407  O   PHE B 417      41.431  23.042  17.954  1.00 19.23           O  
ANISOU 4407  O   PHE B 417     2463   2344   2501    -66    -62     55       O  
ATOM   4408  CB  PHE B 417      43.110  25.280  17.206  1.00 23.85           C  
ANISOU 4408  CB  PHE B 417     3043   2907   3112    -85    -14     11       C  
ATOM   4409  CG  PHE B 417      43.262  25.891  18.576  1.00 24.25           C  
ANISOU 4409  CG  PHE B 417     3083   2974   3157    -95    -18     -5       C  
ATOM   4410  CD1 PHE B 417      42.166  26.000  19.430  1.00 26.23           C  
ANISOU 4410  CD1 PHE B 417     3341   3236   3390    -94    -26      6       C  
ATOM   4411  CD2 PHE B 417      44.484  26.384  18.999  1.00 24.08           C  
ANISOU 4411  CD2 PHE B 417     3044   2958   3149   -106    -13    -34       C  
ATOM   4412  CE1 PHE B 417      42.302  26.582  20.694  1.00 33.79           C  
ANISOU 4412  CE1 PHE B 417     4288   4211   4341   -103    -29    -11       C  
ATOM   4413  CE2 PHE B 417      44.628  26.954  20.268  1.00 29.99           C  
ANISOU 4413  CE2 PHE B 417     3780   3725   3891   -116    -18    -52       C  
ATOM   4414  CZ  PHE B 417      43.538  27.062  21.109  1.00 23.42           C  
ANISOU 4414  CZ  PHE B 417     2955   2903   3039   -114    -25    -40       C  
ATOM   4415  N   MET B 418      43.255  22.035  18.783  1.00 19.26           N  
ANISOU 4415  N   MET B 418     2437   2366   2516    -69    -88     40       N  
ATOM   4416  CA  MET B 418      42.503  20.974  19.468  1.00 17.78           C  
ANISOU 4416  CA  MET B 418     2251   2190   2315    -60   -110     62       C  
ATOM   4417  C   MET B 418      42.645  21.022  21.004  1.00 19.55           C  
ANISOU 4417  C   MET B 418     2465   2438   2524    -62   -126     58       C  
ATOM   4418  O   MET B 418      43.701  20.712  21.540  1.00 25.76           O  
ANISOU 4418  O   MET B 418     3235   3238   3314    -62   -140     47       O  
ATOM   4419  CB  MET B 418      42.967  19.613  18.944  1.00 16.89           C  
ANISOU 4419  CB  MET B 418     2130   2073   2213    -52   -124     72       C  
ATOM   4420  CG  MET B 418      42.193  18.408  19.480  1.00 25.46           C  
ANISOU 4420  CG  MET B 418     3218   3165   3289    -42   -142     96       C  
ATOM   4421  SD  MET B 418      40.412  18.529  19.141  1.00 36.16           S  
ANISOU 4421  SD  MET B 418     4593   4512   4632    -39   -133    114       S  
ATOM   4422  CE  MET B 418      40.353  18.815  17.377  1.00 25.81           C  
ANISOU 4422  CE  MET B 418     3291   3181   3335    -38   -113    108       C  
ATOM   4423  N   PRO B 419      41.588  21.430  21.716  1.00 16.60           N  
ANISOU 4423  N   PRO B 419     2101   2071   2133    -64   -125     65       N  
ATOM   4424  CA  PRO B 419      41.719  21.356  23.176  1.00 21.78           C  
ANISOU 4424  CA  PRO B 419     2750   2754   2773    -64   -141     63       C  
ATOM   4425  C   PRO B 419      41.864  19.901  23.603  1.00 18.66           C  
ANISOU 4425  C   PRO B 419     2348   2367   2373    -52   -165     84       C  
ATOM   4426  O   PRO B 419      41.280  19.009  22.990  1.00 16.62           O  
ANISOU 4426  O   PRO B 419     2098   2097   2121    -44   -166    104       O  
ATOM   4427  CB  PRO B 419      40.409  21.964  23.710  1.00 19.23           C  
ANISOU 4427  CB  PRO B 419     2440   2432   2433    -67   -133     70       C  
ATOM   4428  CG  PRO B 419      39.522  22.190  22.524  1.00 22.43           C  
ANISOU 4428  CG  PRO B 419     2862   2814   2847    -66   -115     80       C  
ATOM   4429  CD  PRO B 419      40.293  21.976  21.263  1.00 16.96           C  
ANISOU 4429  CD  PRO B 419     2165   2104   2173    -64   -109     75       C  
ATOM   4430  N   ARG B 420      42.669  19.664  24.627  1.00 14.25           N  
ANISOU 4430  N   ARG B 420     1776   1833   1807    -49   -182     77       N  
ATOM   4431  CA  ARG B 420      42.921  18.303  25.101  1.00 21.83           C  
ANISOU 4431  CA  ARG B 420     2729   2803   2763    -35   -204     98       C  
ATOM   4432  C   ARG B 420      41.760  17.750  25.922  1.00 18.02           C  
ANISOU 4432  C   ARG B 420     2259   2328   2261    -28   -210    124       C  
ATOM   4433  O   ARG B 420      40.817  18.473  26.230  1.00 16.89           O  
ANISOU 4433  O   ARG B 420     2128   2185   2106    -35   -199    123       O  
ATOM   4434  CB  ARG B 420      44.238  18.252  25.880  1.00 16.44           C  
ANISOU 4434  CB  ARG B 420     2025   2145   2077    -31   -221     82       C  
ATOM   4435  CG  ARG B 420      45.448  18.593  24.990  1.00 19.85           C  
ANISOU 4435  CG  ARG B 420     2443   2567   2533    -37   -215     57       C  
ATOM   4436  CD  ARG B 420      46.774  18.558  25.759  1.00 20.73           C  
ANISOU 4436  CD  ARG B 420     2529   2704   2642    -34   -233     38       C  
ATOM   4437  NE  ARG B 420      47.064  17.228  26.289  1.00 20.56           N  
ANISOU 4437  NE  ARG B 420     2502   2695   2616    -15   -257     61       N  
ATOM   4438  CZ  ARG B 420      48.131  16.916  27.025  1.00 26.18           C  
ANISOU 4438  CZ  ARG B 420     3192   3432   3322     -6   -278     52       C  
ATOM   4439  NH1 ARG B 420      49.037  17.835  27.337  1.00 24.18           N  
ANISOU 4439  NH1 ARG B 420     2921   3197   3071    -15   -278     16       N  
ATOM   4440  NH2 ARG B 420      48.285  15.677  27.456  1.00 25.21           N  
ANISOU 4440  NH2 ARG B 420     3066   3317   3195     13   -297     78       N  
ATOM   4441  N   SER B 421      41.839  16.466  26.268  1.00 20.62           N  
ANISOU 4441  N   SER B 421     2586   2660   2588    -14   -225    147       N  
ATOM   4442  CA  SER B 421      40.805  15.793  27.060  1.00 18.19           C  
ANISOU 4442  CA  SER B 421     2290   2357   2264     -6   -229    174       C  
ATOM   4443  C   SER B 421      41.421  14.741  27.964  1.00 20.79           C  
ANISOU 4443  C   SER B 421     2610   2704   2585     10   -249    191       C  
ATOM   4444  O   SER B 421      42.396  14.099  27.592  1.00 22.67           O  
ANISOU 4444  O   SER B 421     2836   2940   2839     18   -258    192       O  
ATOM   4445  CB  SER B 421      39.778  15.115  26.146  1.00 18.85           C  
ANISOU 4445  CB  SER B 421     2386   2413   2362     -5   -217    191       C  
ATOM   4446  OG  SER B 421      38.856  14.341  26.897  1.00 20.98           O  
ANISOU 4446  OG  SER B 421     2666   2685   2620      3   -220    217       O  
ATOM   4447  N   ARG B 422      40.849  14.555  29.146  1.00 21.43           N  
ANISOU 4447  N   ARG B 422     2698   2802   2641     16   -255    207       N  
ATOM   4448  CA  ARG B 422      41.303  13.498  30.029  1.00 23.49           C  
ANISOU 4448  CA  ARG B 422     2954   3080   2891     35   -272    230       C  
ATOM   4449  C   ARG B 422      41.160  12.137  29.357  1.00 30.77           C  
ANISOU 4449  C   ARG B 422     3879   3976   3836     46   -270    255       C  
ATOM   4450  O   ARG B 422      41.820  11.186  29.745  1.00 31.95           O  
ANISOU 4450  O   ARG B 422     4021   4133   3987     63   -283    272       O  
ATOM   4451  CB  ARG B 422      40.528  13.521  31.349  1.00 34.54           C  
ANISOU 4451  CB  ARG B 422     4364   4499   4259     39   -275    246       C  
ATOM   4452  CG  ARG B 422      41.259  14.220  32.488  1.00 41.64           C  
ANISOU 4452  CG  ARG B 422     5252   5438   5130     41   -290    229       C  
ATOM   4453  CD  ARG B 422      40.653  15.577  32.804  1.00 51.79           C  
ANISOU 4453  CD  ARG B 422     6543   6734   6402     22   -279    205       C  
ATOM   4454  NE  ARG B 422      40.819  15.916  34.219  1.00 66.73           N  
ANISOU 4454  NE  ARG B 422     8431   8664   8259     26   -291    201       N  
ATOM   4455  CZ  ARG B 422      40.623  17.130  34.735  1.00 61.73           C  
ANISOU 4455  CZ  ARG B 422     7796   8049   7611     12   -285    175       C  
ATOM   4456  NH1 ARG B 422      40.257  18.142  33.956  1.00 50.80           N  
ANISOU 4456  NH1 ARG B 422     6415   6645   6244     -8   -267    152       N  
ATOM   4457  NH2 ARG B 422      40.800  17.334  36.035  1.00 61.85           N  
ANISOU 4457  NH2 ARG B 422     7806   8102   7593     17   -298    171       N  
ATOM   4458  N   GLU B 423      40.300  12.051  28.343  1.00 24.55           N  
ANISOU 4458  N   GLU B 423     3102   3160   3067     37   -253    257       N  
ATOM   4459  CA  GLU B 423      40.085  10.803  27.607  1.00 28.88           C  
ANISOU 4459  CA  GLU B 423     3651   3682   3639     45   -248    276       C  
ATOM   4460  C   GLU B 423      41.245  10.463  26.654  1.00 30.97           C  
ANISOU 4460  C   GLU B 423     3900   3936   3929     47   -253    264       C  
ATOM   4461  O   GLU B 423      41.325   9.342  26.126  1.00 24.51           O  
ANISOU 4461  O   GLU B 423     3079   3100   3134     56   -251    279       O  
ATOM   4462  CB  GLU B 423      38.808  10.897  26.763  1.00 30.82           C  
ANISOU 4462  CB  GLU B 423     3910   3904   3896     34   -229    275       C  
ATOM   4463  CG  GLU B 423      37.490  10.606  27.445  1.00 43.92           C  
ANISOU 4463  CG  GLU B 423     5584   5561   5543     35   -220    294       C  
ATOM   4464  CD  GLU B 423      36.363  10.418  26.416  1.00 62.99           C  
ANISOU 4464  CD  GLU B 423     8007   7950   7976     27   -202    293       C  
ATOM   4465  OE1 GLU B 423      36.158  11.341  25.583  1.00 53.26           O  
ANISOU 4465  OE1 GLU B 423     6776   6714   6748     16   -196    271       O  
ATOM   4466  OE2 GLU B 423      35.710   9.342  26.422  1.00 55.93           O  
ANISOU 4466  OE2 GLU B 423     7117   7041   7094     33   -195    312       O  
ATOM   4467  N   ASP B 424      42.107  11.445  26.398  1.00 21.01           N  
ANISOU 4467  N   ASP B 424     2629   2686   2668     39   -257    237       N  
ATOM   4468  CA  ASP B 424      43.169  11.297  25.407  1.00 23.47           C  
ANISOU 4468  CA  ASP B 424     2926   2987   3004     38   -258    221       C  
ATOM   4469  C   ASP B 424      44.219  10.270  25.815  1.00 29.16           C  
ANISOU 4469  C   ASP B 424     3632   3715   3733     55   -275    233       C  
ATOM   4470  O   ASP B 424      44.676  10.267  26.956  1.00 28.52           O  
ANISOU 4470  O   ASP B 424     3545   3660   3631     66   -291    239       O  
ATOM   4471  CB  ASP B 424      43.847  12.641  25.139  1.00 18.77           C  
ANISOU 4471  CB  ASP B 424     2324   2401   2407     25   -256    188       C  
ATOM   4472  CG  ASP B 424      42.977  13.574  24.302  1.00 23.74           C  
ANISOU 4472  CG  ASP B 424     2966   3014   3038      9   -236    176       C  
ATOM   4473  OD1 ASP B 424      42.159  13.083  23.490  1.00 22.84           O  
ANISOU 4473  OD1 ASP B 424     2863   2880   2936      9   -225    187       O  
ATOM   4474  OD2 ASP B 424      43.105  14.795  24.462  1.00 24.34           O  
ANISOU 4474  OD2 ASP B 424     3043   3100   3105     -2   -230    154       O  
ATOM   4475  N   GLU B 425      44.600   9.414  24.869  1.00 18.12           N  
ANISOU 4475  N   GLU B 425     2227   2295   2363     59   -272    237       N  
ATOM   4476  CA  GLU B 425      45.544   8.334  25.129  1.00 24.68           C  
ANISOU 4476  CA  GLU B 425     3044   3128   3206     76   -286    250       C  
ATOM   4477  C   GLU B 425      46.932   8.623  24.548  1.00 25.40           C  
ANISOU 4477  C   GLU B 425     3115   3222   3314     74   -293    224       C  
ATOM   4478  O   GLU B 425      47.944   8.542  25.247  1.00 24.79           O  
ANISOU 4478  O   GLU B 425     3023   3166   3231     85   -311    221       O  
ATOM   4479  CB  GLU B 425      44.999   7.034  24.537  1.00 20.18           C  
ANISOU 4479  CB  GLU B 425     2478   2529   2660     83   -275    273       C  
ATOM   4480  CG  GLU B 425      43.788   6.474  25.289  1.00 27.61           C  
ANISOU 4480  CG  GLU B 425     3436   3467   3587     90   -269    302       C  
ATOM   4481  CD  GLU B 425      44.187   5.669  26.514  1.00 37.93           C  
ANISOU 4481  CD  GLU B 425     4740   4790   4883    112   -283    330       C  
ATOM   4482  OE1 GLU B 425      43.281   5.167  27.214  1.00 42.87           O  
ANISOU 4482  OE1 GLU B 425     5379   5413   5497    119   -277    356       O  
ATOM   4483  OE2 GLU B 425      45.409   5.540  26.776  1.00 32.64           O  
ANISOU 4483  OE2 GLU B 425     4053   4134   4214    123   -300    326       O  
ATOM   4484  N   CYS B 426      46.973   8.954  23.262  1.00 23.31           N  
ANISOU 4484  N   CYS B 426     2850   2936   3069     60   -278    205       N  
ATOM   4485  CA  CYS B 426      48.243   9.156  22.572  1.00 18.06           C  
ANISOU 4485  CA  CYS B 426     2168   2269   2425     56   -281    180       C  
ATOM   4486  C   CYS B 426      48.028   9.875  21.251  1.00 23.41           C  
ANISOU 4486  C   CYS B 426     2852   2927   3115     38   -260    159       C  
ATOM   4487  O   CYS B 426      46.913   9.951  20.744  1.00 20.63           O  
ANISOU 4487  O   CYS B 426     2516   2561   2761     31   -246    166       O  
ATOM   4488  CB  CYS B 426      48.943   7.822  22.327  1.00 28.77           C  
ANISOU 4488  CB  CYS B 426     3511   3615   3807     71   -288    194       C  
ATOM   4489  SG  CYS B 426      47.891   6.625  21.487  1.00 37.29           S  
ANISOU 4489  SG  CYS B 426     4602   4660   4906     72   -272    217       S  
ATOM   4490  N   LEU B 427      49.114  10.399  20.710  1.00 17.22           N  
ANISOU 4490  N   LEU B 427     2054   2143   2345     31   -259    132       N  
ATOM   4491  CA  LEU B 427      49.099  11.173  19.492  1.00 18.78           C  
ANISOU 4491  CA  LEU B 427     2258   2325   2554     15   -239    111       C  
ATOM   4492  C   LEU B 427      50.204  10.590  18.626  1.00 19.51           C  
ANISOU 4492  C   LEU B 427     2334   2405   2676     16   -238     98       C  
ATOM   4493  O   LEU B 427      51.353  10.445  19.070  1.00 19.43           O  
ANISOU 4493  O   LEU B 427     2304   2406   2673     21   -252     88       O  
ATOM   4494  CB  LEU B 427      49.374  12.658  19.799  1.00 14.88           C  
ANISOU 4494  CB  LEU B 427     1763   1844   2046      2   -233     85       C  
ATOM   4495  CG  LEU B 427      49.609  13.570  18.581  1.00 22.40           C  
ANISOU 4495  CG  LEU B 427     2720   2780   3011    -13   -211     62       C  
ATOM   4496  CD1 LEU B 427      48.355  13.708  17.706  1.00 13.64           C  
ANISOU 4496  CD1 LEU B 427     1632   1653   1897    -18   -193     73       C  
ATOM   4497  CD2 LEU B 427      50.099  14.948  19.009  1.00 16.22           C  
ANISOU 4497  CD2 LEU B 427     1933   2010   2221    -24   -204     35       C  
ATOM   4498  N   ILE B 428      49.865  10.239  17.394  1.00 19.13           N  
ANISOU 4498  N   ILE B 428     2291   2333   2643     10   -223     98       N  
ATOM   4499  CA  ILE B 428      50.846   9.664  16.495  1.00 18.28           C  
ANISOU 4499  CA  ILE B 428     2169   2211   2563     10   -220     86       C  
ATOM   4500  C   ILE B 428      51.041  10.555  15.273  1.00 18.84           C  
ANISOU 4500  C   ILE B 428     2247   2271   2643     -5   -198     62       C  
ATOM   4501  O   ILE B 428      50.071  10.898  14.612  1.00 17.30           O  
ANISOU 4501  O   ILE B 428     2068   2066   2438    -11   -183     66       O  
ATOM   4502  CB  ILE B 428      50.412   8.231  16.074  1.00 22.75           C  
ANISOU 4502  CB  ILE B 428     2736   2762   3147     19   -220    107       C  
ATOM   4503  CG1 ILE B 428      50.463   7.295  17.284  1.00 26.53           C  
ANISOU 4503  CG1 ILE B 428     3207   3250   3623     36   -240    131       C  
ATOM   4504  CG2 ILE B 428      51.321   7.673  14.988  1.00 17.00           C  
ANISOU 4504  CG2 ILE B 428     1993   2016   2449     16   -213     92       C  
ATOM   4505  CD1 ILE B 428      49.124   7.059  17.963  1.00 31.65           C  
ANISOU 4505  CD1 ILE B 428     3872   3902   4251     41   -240    157       C  
ATOM   4506  N   LEU B 429      52.277  10.972  14.995  1.00 18.07           N  
ANISOU 4506  N   LEU B 429     2134   2173   2560    -11   -195     38       N  
ATOM   4507  CA  LEU B 429      52.582  11.568  13.699  1.00 16.47           C  
ANISOU 4507  CA  LEU B 429     1936   1955   2369    -24   -172     17       C  
ATOM   4508  C   LEU B 429      53.398  10.561  12.903  1.00 20.30           C  
ANISOU 4508  C   LEU B 429     2406   2426   2883    -22   -172     11       C  
ATOM   4509  O   LEU B 429      54.248   9.865  13.457  1.00 21.54           O  
ANISOU 4509  O   LEU B 429     2543   2588   3053    -13   -188     11       O  
ATOM   4510  CB  LEU B 429      53.394  12.869  13.795  1.00 18.88           C  
ANISOU 4510  CB  LEU B 429     2235   2265   2673    -35   -162    -11       C  
ATOM   4511  CG  LEU B 429      53.234  13.995  14.810  1.00 21.55           C  
ANISOU 4511  CG  LEU B 429     2577   2621   2991    -40   -164    -18       C  
ATOM   4512  CD1 LEU B 429      53.694  15.341  14.183  1.00 16.44           C  
ANISOU 4512  CD1 LEU B 429     1933   1965   2349    -55   -138    -45       C  
ATOM   4513  CD2 LEU B 429      51.850  14.111  15.380  1.00 17.20           C  
ANISOU 4513  CD2 LEU B 429     2045   2077   2414    -35   -168      6       C  
ATOM   4514  N   ALA B 430      53.165  10.481  11.601  1.00 17.26           N  
ANISOU 4514  N   ALA B 430     2028   2023   2505    -28   -153      6       N  
ATOM   4515  CA  ALA B 430      53.901   9.503  10.805  1.00 17.89           C  
ANISOU 4515  CA  ALA B 430     2094   2089   2614    -27   -151      0       C  
ATOM   4516  C   ALA B 430      53.864   9.862   9.336  1.00 18.27           C  
ANISOU 4516  C   ALA B 430     2152   2122   2667    -38   -126    -15       C  
ATOM   4517  O   ALA B 430      52.961  10.571   8.890  1.00 16.33           O  
ANISOU 4517  O   ALA B 430     1926   1875   2401    -42   -113    -11       O  
ATOM   4518  CB  ALA B 430      53.331   8.083  11.027  1.00 16.88           C  
ANISOU 4518  CB  ALA B 430     1962   1957   2493    -15   -164     23       C  
ATOM   4519  N   SER B 431      54.857   9.392   8.586  1.00 19.15           N  
ANISOU 4519  N   SER B 431     2249   2222   2805    -42   -120    -31       N  
ATOM   4520  CA  SER B 431      54.822   9.518   7.134  1.00 20.34           C  
ANISOU 4520  CA  SER B 431     2409   2359   2960    -50    -96    -43       C  
ATOM   4521  C   SER B 431      53.959   8.390   6.573  1.00 21.17           C  
ANISOU 4521  C   SER B 431     2517   2458   3069    -45    -98    -29       C  
ATOM   4522  O   SER B 431      53.544   7.497   7.315  1.00 18.66           O  
ANISOU 4522  O   SER B 431     2193   2143   2753    -35   -115    -11       O  
ATOM   4523  CB  SER B 431      56.232   9.400   6.550  1.00 20.70           C  
ANISOU 4523  CB  SER B 431     2435   2394   3034    -57    -87    -68       C  
ATOM   4524  OG  SER B 431      56.768   8.130   6.855  1.00 21.85           O  
ANISOU 4524  OG  SER B 431     2561   2538   3205    -49   -104    -64       O  
ATOM   4525  N   ASP B 432      53.711   8.414   5.266  1.00 26.43           N  
ANISOU 4525  N   ASP B 432     3192   3116   3734    -50    -79    -37       N  
ATOM   4526  CA  ASP B 432      52.824   7.425   4.661  1.00 28.84           C  
ANISOU 4526  CA  ASP B 432     3500   3417   4041    -47    -78    -28       C  
ATOM   4527  C   ASP B 432      53.467   6.046   4.568  1.00 30.68           C  
ANISOU 4527  C   ASP B 432     3710   3639   4306    -44    -85    -32       C  
ATOM   4528  O   ASP B 432      52.799   5.079   4.212  1.00 32.43           O  
ANISOU 4528  O   ASP B 432     3929   3856   4535    -41    -85    -26       O  
ATOM   4529  CB  ASP B 432      52.310   7.877   3.296  1.00 27.39           C  
ANISOU 4529  CB  ASP B 432     3332   3232   3843    -52    -57    -37       C  
ATOM   4530  CG  ASP B 432      53.427   8.146   2.311  1.00 27.22           C  
ANISOU 4530  CG  ASP B 432     3305   3202   3836    -61    -39    -60       C  
ATOM   4531  OD1 ASP B 432      54.579   7.708   2.562  1.00 28.93           O  
ANISOU 4531  OD1 ASP B 432     3502   3411   4080    -63    -43    -71       O  
ATOM   4532  OD2 ASP B 432      53.147   8.789   1.280  1.00 33.56           O  
ANISOU 4532  OD2 ASP B 432     4123   4004   4622    -64    -19    -67       O  
ATOM   4533  N   GLY B 433      54.757   5.956   4.884  1.00 26.47           N  
ANISOU 4533  N   GLY B 433     3159   3103   3796    -45    -90    -43       N  
ATOM   4534  CA  GLY B 433      55.369   4.654   5.093  1.00 25.28           C  
ANISOU 4534  CA  GLY B 433     2987   2943   3677    -39   -100    -42       C  
ATOM   4535  C   GLY B 433      54.505   3.791   6.014  1.00 32.19           C  
ANISOU 4535  C   GLY B 433     3861   3821   4550    -27   -116    -15       C  
ATOM   4536  O   GLY B 433      54.428   2.569   5.850  1.00 21.82           O  
ANISOU 4536  O   GLY B 433     2535   2495   3259    -22   -118    -10       O  
ATOM   4537  N   LEU B 434      53.844   4.448   6.973  1.00 29.15           N  
ANISOU 4537  N   LEU B 434     3489   3449   4138    -22   -127      1       N  
ATOM   4538  CA  LEU B 434      52.966   3.806   7.949  1.00 21.60           C  
ANISOU 4538  CA  LEU B 434     2536   2496   3175    -11   -140     27       C  
ATOM   4539  C   LEU B 434      51.518   3.777   7.465  1.00 29.96           C  
ANISOU 4539  C   LEU B 434     3612   3555   4216    -13   -131     34       C  
ATOM   4540  O   LEU B 434      50.867   2.743   7.510  1.00 26.09           O  
ANISOU 4540  O   LEU B 434     3119   3057   3738     -8   -132     46       O  
ATOM   4541  CB  LEU B 434      52.982   4.594   9.264  1.00 26.28           C  
ANISOU 4541  CB  LEU B 434     3134   3106   3746     -5   -156     38       C  
ATOM   4542  CG  LEU B 434      52.557   3.905  10.566  1.00 31.59           C  
ANISOU 4542  CG  LEU B 434     3804   3785   4414      9   -173     66       C  
ATOM   4543  CD1 LEU B 434      51.828   4.858  11.523  1.00 23.87           C  
ANISOU 4543  CD1 LEU B 434     2843   2825   3402     11   -181     77       C  
ATOM   4544  CD2 LEU B 434      51.756   2.649  10.318  1.00 27.57           C  
ANISOU 4544  CD2 LEU B 434     3295   3262   3920     14   -169     81       C  
ATOM   4545  N   TRP B 435      51.002   4.921   7.029  1.00 22.49           N  
ANISOU 4545  N   TRP B 435     2683   2617   3244    -21   -122     28       N  
ATOM   4546  CA  TRP B 435      49.571   5.022   6.766  1.00 19.10           C  
ANISOU 4546  CA  TRP B 435     2271   2192   2795    -20   -116     36       C  
ATOM   4547  C   TRP B 435      49.160   4.286   5.498  1.00 27.63           C  
ANISOU 4547  C   TRP B 435     3347   3263   3886    -24   -103     25       C  
ATOM   4548  O   TRP B 435      47.994   3.956   5.326  1.00 25.11           O  
ANISOU 4548  O   TRP B 435     3035   2946   3559    -23   -101     31       O  
ATOM   4549  CB  TRP B 435      49.123   6.475   6.686  1.00 20.63           C  
ANISOU 4549  CB  TRP B 435     2484   2397   2957    -25   -110     34       C  
ATOM   4550  CG  TRP B 435      49.506   7.298   7.868  1.00 19.01           C  
ANISOU 4550  CG  TRP B 435     2282   2202   2740    -23   -120     40       C  
ATOM   4551  CD1 TRP B 435      50.341   8.381   7.876  1.00 20.45           C  
ANISOU 4551  CD1 TRP B 435     2465   2387   2917    -29   -115     27       C  
ATOM   4552  CD2 TRP B 435      49.077   7.110   9.216  1.00 17.98           C  
ANISOU 4552  CD2 TRP B 435     2152   2080   2601    -15   -137     60       C  
ATOM   4553  NE1 TRP B 435      50.457   8.879   9.154  1.00 21.48           N  
ANISOU 4553  NE1 TRP B 435     2596   2530   3037    -26   -128     34       N  
ATOM   4554  CE2 TRP B 435      49.690   8.111  10.000  1.00 18.85           C  
ANISOU 4554  CE2 TRP B 435     2262   2201   2700    -17   -142     56       C  
ATOM   4555  CE3 TRP B 435      48.238   6.184   9.846  1.00 20.70           C  
ANISOU 4555  CE3 TRP B 435     2496   2423   2946     -7   -146     80       C  
ATOM   4556  CZ2 TRP B 435      49.481   8.227  11.376  1.00 17.59           C  
ANISOU 4556  CZ2 TRP B 435     2103   2053   2526    -10   -158     71       C  
ATOM   4557  CZ3 TRP B 435      48.030   6.295  11.214  1.00 21.87           C  
ANISOU 4557  CZ3 TRP B 435     2646   2582   3082      0   -160     97       C  
ATOM   4558  CH2 TRP B 435      48.648   7.313  11.965  1.00 22.90           C  
ANISOU 4558  CH2 TRP B 435     2777   2725   3198     -1   -167     93       C  
ATOM   4559  N   ASP B 436      50.108   4.029   4.605  1.00 28.65           N  
ANISOU 4559  N   ASP B 436     3466   3384   4035    -30    -94      6       N  
ATOM   4560  CA  ASP B 436      49.765   3.327   3.375  1.00 33.39           C  
ANISOU 4560  CA  ASP B 436     4062   3979   4646    -34    -81     -8       C  
ATOM   4561  C   ASP B 436      49.400   1.858   3.592  1.00 31.38           C  
ANISOU 4561  C   ASP B 436     3792   3713   4418    -30    -85     -1       C  
ATOM   4562  O   ASP B 436      48.742   1.263   2.745  1.00 32.21           O  
ANISOU 4562  O   ASP B 436     3894   3816   4528    -33    -75    -12       O  
ATOM   4563  CB  ASP B 436      50.858   3.470   2.317  1.00 29.62           C  
ANISOU 4563  CB  ASP B 436     3577   3495   4182    -42    -68    -31       C  
ATOM   4564  CG  ASP B 436      50.733   4.774   1.539  1.00 39.00           C  
ANISOU 4564  CG  ASP B 436     4784   4693   5341    -47    -54    -40       C  
ATOM   4565  OD1 ASP B 436      51.679   5.142   0.807  1.00 38.08           O  
ANISOU 4565  OD1 ASP B 436     4665   4571   5231    -54    -42    -57       O  
ATOM   4566  OD2 ASP B 436      49.678   5.439   1.667  1.00 36.11           O  
ANISOU 4566  OD2 ASP B 436     4436   4338   4946    -44    -55    -30       O  
ATOM   4567  N   VAL B 437      49.811   1.283   4.723  1.00 26.03           N  
ANISOU 4567  N   VAL B 437     3104   3028   3756    -22    -98     15       N  
ATOM   4568  CA  VAL B 437      49.503  -0.120   5.015  1.00 23.71           C  
ANISOU 4568  CA  VAL B 437     2797   2721   3491    -17    -98     25       C  
ATOM   4569  C   VAL B 437      48.654  -0.338   6.285  1.00 34.52           C  
ANISOU 4569  C   VAL B 437     4173   4093   4851     -7   -109     52       C  
ATOM   4570  O   VAL B 437      48.258  -1.466   6.587  1.00 26.65           O  
ANISOU 4570  O   VAL B 437     3167   3083   3875     -2   -107     63       O  
ATOM   4571  CB  VAL B 437      50.789  -1.000   5.081  1.00 33.69           C  
ANISOU 4571  CB  VAL B 437     4039   3970   4793    -14   -100     21       C  
ATOM   4572  CG1 VAL B 437      51.560  -0.919   3.763  1.00 31.88           C  
ANISOU 4572  CG1 VAL B 437     3801   3736   4576    -25    -87     -8       C  
ATOM   4573  CG2 VAL B 437      51.687  -0.598   6.262  1.00 26.78           C  
ANISOU 4573  CG2 VAL B 437     3160   3100   3914     -5   -117     35       C  
ATOM   4574  N   MET B 438      48.383   0.727   7.036  1.00 29.01           N  
ANISOU 4574  N   MET B 438     3490   3410   4121     -5   -118     63       N  
ATOM   4575  CA  MET B 438      47.560   0.610   8.246  1.00 27.01           C  
ANISOU 4575  CA  MET B 438     3246   3162   3856      4   -128     89       C  
ATOM   4576  C   MET B 438      46.630   1.797   8.405  1.00 31.66           C  
ANISOU 4576  C   MET B 438     3856   3767   4408      1   -129     91       C  
ATOM   4577  O   MET B 438      46.997   2.924   8.060  1.00 26.47           O  
ANISOU 4577  O   MET B 438     3205   3119   3732     -5   -128     80       O  
ATOM   4578  CB  MET B 438      48.442   0.463   9.484  1.00 28.80           C  
ANISOU 4578  CB  MET B 438     3466   3389   4088     15   -143    107       C  
ATOM   4579  CG  MET B 438      49.245  -0.828   9.509  1.00 34.96           C  
ANISOU 4579  CG  MET B 438     4225   4152   4906     22   -143    110       C  
ATOM   4580  SD  MET B 438      50.289  -0.961  10.964  1.00 45.55           S  
ANISOU 4580  SD  MET B 438     5558   5500   6251     39   -164    132       S  
ATOM   4581  CE  MET B 438      49.070  -0.911  12.256  1.00 37.98           C  
ANISOU 4581  CE  MET B 438     4616   4549   5265     48   -170    163       C  
ATOM   4582  N   ASN B 439      45.423   1.566   8.919  1.00 25.27           N  
ANISOU 4582  N   ASN B 439     3054   2958   3588      4   -129    105       N  
ATOM   4583  CA  ASN B 439      44.512   2.686   9.102  1.00 22.97           C  
ANISOU 4583  CA  ASN B 439     2781   2682   3263      1   -129    108       C  
ATOM   4584  C   ASN B 439      44.646   3.317  10.487  1.00 21.29           C  
ANISOU 4584  C   ASN B 439     2578   2481   3032      7   -143    126       C  
ATOM   4585  O   ASN B 439      45.248   2.726  11.397  1.00 20.51           O  
ANISOU 4585  O   ASN B 439     2469   2378   2944     15   -152    141       O  
ATOM   4586  CB  ASN B 439      43.052   2.348   8.728  1.00 27.33           C  
ANISOU 4586  CB  ASN B 439     3340   3235   3811      0   -121    107       C  
ATOM   4587  CG  ASN B 439      42.398   1.334   9.671  1.00 29.62           C  
ANISOU 4587  CG  ASN B 439     3627   3515   4114      6   -122    127       C  
ATOM   4588  OD1 ASN B 439      41.693   0.421   9.223  1.00 38.26           O  
ANISOU 4588  OD1 ASN B 439     4713   4598   5226      4   -111    121       O  
ATOM   4589  ND2 ASN B 439      42.613   1.496  10.969  1.00 21.72           N  
ANISOU 4589  ND2 ASN B 439     2631   2518   3105     13   -133    148       N  
ATOM   4590  N   ASN B 440      44.098   4.520  10.624  1.00 20.56           N  
ANISOU 4590  N   ASN B 440     2500   2401   2910      4   -143    125       N  
ATOM   4591  CA  ASN B 440      44.222   5.304  11.854  1.00 23.53           C  
ANISOU 4591  CA  ASN B 440     2884   2790   3265      7   -154    138       C  
ATOM   4592  C   ASN B 440      43.787   4.535  13.094  1.00 18.98           C  
ANISOU 4592  C   ASN B 440     2308   2214   2691     17   -163    162       C  
ATOM   4593  O   ASN B 440      44.477   4.537  14.111  1.00 21.92           O  
ANISOU 4593  O   ASN B 440     2675   2593   3060     23   -175    173       O  
ATOM   4594  CB  ASN B 440      43.405   6.590  11.758  1.00 20.56           C  
ANISOU 4594  CB  ASN B 440     2526   2426   2860      2   -150    133       C  
ATOM   4595  CG  ASN B 440      43.818   7.458  10.590  1.00 25.31           C  
ANISOU 4595  CG  ASN B 440     3131   3028   3458     -5   -139    113       C  
ATOM   4596  OD1 ASN B 440      44.950   7.376  10.100  1.00 22.62           O  
ANISOU 4596  OD1 ASN B 440     2780   2682   3131     -8   -137    101       O  
ATOM   4597  ND2 ASN B 440      42.895   8.299  10.130  1.00 21.56           N  
ANISOU 4597  ND2 ASN B 440     2671   2560   2962     -7   -131    109       N  
ATOM   4598  N   GLN B 441      42.635   3.882  13.008  1.00 14.13           N  
ANISOU 4598  N   GLN B 441     1697   1592   2080     17   -155    169       N  
ATOM   4599  CA  GLN B 441      42.102   3.188  14.174  1.00 19.34           C  
ANISOU 4599  CA  GLN B 441     2358   2249   2740     26   -159    194       C  
ATOM   4600  C   GLN B 441      43.038   2.083  14.645  1.00 20.08           C  
ANISOU 4600  C   GLN B 441     2438   2333   2859     36   -165    207       C  
ATOM   4601  O   GLN B 441      43.293   1.938  15.847  1.00 24.64           O  
ANISOU 4601  O   GLN B 441     3017   2917   3429     46   -175    228       O  
ATOM   4602  CB  GLN B 441      40.708   2.595  13.899  1.00 15.42           C  
ANISOU 4602  CB  GLN B 441     1866   1744   2249     23   -147    196       C  
ATOM   4603  CG  GLN B 441      40.070   1.938  15.145  1.00 17.12           C  
ANISOU 4603  CG  GLN B 441     2086   1955   2464     31   -147    222       C  
ATOM   4604  CD  GLN B 441      39.591   2.981  16.184  1.00 23.81           C  
ANISOU 4604  CD  GLN B 441     2948   2820   3277     32   -155    233       C  
ATOM   4605  OE1 GLN B 441      39.440   4.152  15.867  1.00 19.73           O  
ANISOU 4605  OE1 GLN B 441     2441   2317   2740     25   -157    219       O  
ATOM   4606  NE2 GLN B 441      39.358   2.542  17.421  1.00 23.31           N  
ANISOU 4606  NE2 GLN B 441     2890   2758   3209     41   -158    257       N  
ATOM   4607  N   GLU B 442      43.532   1.280  13.714  1.00 21.46           N  
ANISOU 4607  N   GLU B 442     2599   2492   3063     34   -157    196       N  
ATOM   4608  CA  GLU B 442      44.381   0.169  14.134  1.00 26.43           C  
ANISOU 4608  CA  GLU B 442     3214   3110   3719     45   -161    209       C  
ATOM   4609  C   GLU B 442      45.743   0.614  14.677  1.00 22.74           C  
ANISOU 4609  C   GLU B 442     2740   2655   3246     52   -177    210       C  
ATOM   4610  O   GLU B 442      46.233   0.029  15.642  1.00 23.59           O  
ANISOU 4610  O   GLU B 442     2842   2763   3359     66   -187    231       O  
ATOM   4611  CB  GLU B 442      44.498  -0.928  13.068  1.00 29.23           C  
ANISOU 4611  CB  GLU B 442     3555   3443   4110     42   -147    197       C  
ATOM   4612  CG  GLU B 442      45.138  -0.541  11.753  1.00 34.54           C  
ANISOU 4612  CG  GLU B 442     4219   4115   4789     31   -143    167       C  
ATOM   4613  CD  GLU B 442      45.307  -1.747  10.815  1.00 47.11           C  
ANISOU 4613  CD  GLU B 442     5794   5685   6419     28   -129    156       C  
ATOM   4614  OE1 GLU B 442      45.269  -1.558   9.574  1.00 38.09           O  
ANISOU 4614  OE1 GLU B 442     4650   4543   5281     17   -120    130       O  
ATOM   4615  OE2 GLU B 442      45.482  -2.883  11.323  1.00 56.62           O  
ANISOU 4615  OE2 GLU B 442     6990   6874   7651     38   -126    172       O  
ATOM   4616  N   VAL B 443      46.324   1.662  14.087  1.00 17.26           N  
ANISOU 4616  N   VAL B 443     2045   1970   2541     43   -180    188       N  
ATOM   4617  CA  VAL B 443      47.568   2.242  14.599  1.00 18.54           C  
ANISOU 4617  CA  VAL B 443     2201   2147   2698     47   -195    183       C  
ATOM   4618  C   VAL B 443      47.415   2.724  16.040  1.00 21.39           C  
ANISOU 4618  C   VAL B 443     2569   2527   3031     56   -209    202       C  
ATOM   4619  O   VAL B 443      48.279   2.491  16.880  1.00 22.72           O  
ANISOU 4619  O   VAL B 443     2727   2704   3200     68   -224    211       O  
ATOM   4620  CB  VAL B 443      48.050   3.437  13.749  1.00 16.10           C  
ANISOU 4620  CB  VAL B 443     1893   1845   2379     33   -190    155       C  
ATOM   4621  CG1 VAL B 443      49.259   4.111  14.414  1.00 21.77           C  
ANISOU 4621  CG1 VAL B 443     2602   2578   3090     36   -205    148       C  
ATOM   4622  CG2 VAL B 443      48.381   3.011  12.330  1.00 18.78           C  
ANISOU 4622  CG2 VAL B 443     2225   2168   2744     25   -177    135       C  
ATOM   4623  N   CYS B 444      46.321   3.426  16.322  1.00 21.28           N  
ANISOU 4623  N   CYS B 444     2573   2522   2991     50   -205    205       N  
ATOM   4624  CA  CYS B 444      46.078   3.918  17.675  1.00 20.99           C  
ANISOU 4624  CA  CYS B 444     2545   2505   2927     57   -217    221       C  
ATOM   4625  C   CYS B 444      45.868   2.778  18.677  1.00 23.11           C  
ANISOU 4625  C   CYS B 444     2811   2769   3200     74   -223    252       C  
ATOM   4626  O   CYS B 444      46.407   2.799  19.784  1.00 22.47           O  
ANISOU 4626  O   CYS B 444     2727   2705   3106     86   -238    266       O  
ATOM   4627  CB  CYS B 444      44.858   4.837  17.690  1.00 28.86           C  
ANISOU 4627  CB  CYS B 444     3559   3508   3898     47   -210    218       C  
ATOM   4628  SG  CYS B 444      45.112   6.477  16.954  1.00 26.89           S  
ANISOU 4628  SG  CYS B 444     3316   3268   3634     31   -205    188       S  
ATOM   4629  N   GLU B 445      45.061   1.796  18.294  1.00 18.57           N  
ANISOU 4629  N   GLU B 445     2239   2174   2644     74   -209    263       N  
ATOM   4630  CA  GLU B 445      44.777   0.674  19.180  1.00 29.31           C  
ANISOU 4630  CA  GLU B 445     3600   3526   4012     90   -208    294       C  
ATOM   4631  C   GLU B 445      46.084  -0.036  19.508  1.00 25.60           C  
ANISOU 4631  C   GLU B 445     3113   3056   3560    106   -220    303       C  
ATOM   4632  O   GLU B 445      46.370  -0.309  20.666  1.00 28.67           O  
ANISOU 4632  O   GLU B 445     3502   3455   3936    123   -231    327       O  
ATOM   4633  CB  GLU B 445      43.755  -0.292  18.549  1.00 22.76           C  
ANISOU 4633  CB  GLU B 445     2772   2670   3206     86   -187    298       C  
ATOM   4634  CG  GLU B 445      42.329   0.239  18.608  1.00 32.45           C  
ANISOU 4634  CG  GLU B 445     4016   3900   4414     75   -178    297       C  
ATOM   4635  CD  GLU B 445      41.330  -0.604  17.829  1.00 38.27           C  
ANISOU 4635  CD  GLU B 445     4751   4614   5175     69   -157    292       C  
ATOM   4636  OE1 GLU B 445      41.757  -1.550  17.132  1.00 34.90           O  
ANISOU 4636  OE1 GLU B 445     4311   4168   4781     70   -149    287       O  
ATOM   4637  OE2 GLU B 445      40.113  -0.305  17.903  1.00 31.42           O  
ANISOU 4637  OE2 GLU B 445     3896   3748   4295     62   -148    291       O  
ATOM   4638  N   ILE B 446      46.890  -0.287  18.483  1.00 16.91           N  
ANISOU 4638  N   ILE B 446     1997   1942   2485    101   -217    283       N  
ATOM   4639  CA  ILE B 446      48.188  -0.923  18.686  1.00 22.20           C  
ANISOU 4639  CA  ILE B 446     2648   2611   3174    115   -228    288       C  
ATOM   4640  C   ILE B 446      49.107  -0.095  19.587  1.00 27.04           C  
ANISOU 4640  C   ILE B 446     3258   3254   3763    124   -251    286       C  
ATOM   4641  O   ILE B 446      49.668  -0.626  20.549  1.00 23.04           O  
ANISOU 4641  O   ILE B 446     2744   2757   3254    144   -264    308       O  
ATOM   4642  CB  ILE B 446      48.877  -1.244  17.346  1.00 23.99           C  
ANISOU 4642  CB  ILE B 446     2860   2819   3434    106   -219    263       C  
ATOM   4643  CG1 ILE B 446      48.107  -2.336  16.610  1.00 22.97           C  
ANISOU 4643  CG1 ILE B 446     2731   2662   3336    102   -198    267       C  
ATOM   4644  CG2 ILE B 446      50.308  -1.706  17.561  1.00 26.85           C  
ANISOU 4644  CG2 ILE B 446     3203   3184   3816    120   -233    264       C  
ATOM   4645  CD1 ILE B 446      48.307  -2.298  15.118  1.00 24.86           C  
ANISOU 4645  CD1 ILE B 446     2962   2889   3596     85   -186    236       C  
ATOM   4646  N   ALA B 447      49.246   1.201  19.296  1.00 19.06           N  
ANISOU 4646  N   ALA B 447     2250   2260   2733    108   -254    260       N  
ATOM   4647  CA  ALA B 447      50.158   2.052  20.066  1.00 18.44           C  
ANISOU 4647  CA  ALA B 447     2164   2209   2633    113   -274    251       C  
ATOM   4648  C   ALA B 447      49.795   2.021  21.539  1.00 22.19           C  
ANISOU 4648  C   ALA B 447     2647   2705   3078    129   -287    278       C  
ATOM   4649  O   ALA B 447      50.658   1.869  22.411  1.00 21.79           O  
ANISOU 4649  O   ALA B 447     2585   2675   3021    146   -306    286       O  
ATOM   4650  CB  ALA B 447      50.159   3.497  19.539  1.00 21.03           C  
ANISOU 4650  CB  ALA B 447     2497   2548   2945     93   -270    220       C  
ATOM   4651  N   ARG B 448      48.511   2.182  21.817  1.00 19.68           N  
ANISOU 4651  N   ARG B 448     2349   2385   2743    124   -277    291       N  
ATOM   4652  CA  ARG B 448      48.045   2.184  23.189  1.00 22.65           C  
ANISOU 4652  CA  ARG B 448     2736   2781   3090    137   -286    317       C  
ATOM   4653  C   ARG B 448      48.301   0.831  23.885  1.00 26.77           C  
ANISOU 4653  C   ARG B 448     3252   3296   3623    163   -291    352       C  
ATOM   4654  O   ARG B 448      48.774   0.801  25.017  1.00 25.44           O  
ANISOU 4654  O   ARG B 448     3081   3152   3434    181   -309    368       O  
ATOM   4655  CB  ARG B 448      46.567   2.553  23.247  1.00 23.52           C  
ANISOU 4655  CB  ARG B 448     2867   2885   3183    125   -272    323       C  
ATOM   4656  CG  ARG B 448      46.008   2.550  24.647  1.00 34.37           C  
ANISOU 4656  CG  ARG B 448     4253   4278   4526    138   -278    349       C  
ATOM   4657  CD  ARG B 448      44.505   2.742  24.637  1.00 41.43           C  
ANISOU 4657  CD  ARG B 448     5167   5163   5411    126   -261    355       C  
ATOM   4658  NE  ARG B 448      43.936   2.442  25.944  1.00 48.77           N  
ANISOU 4658  NE  ARG B 448     6109   6105   6317    140   -264    386       N  
ATOM   4659  CZ  ARG B 448      43.519   1.233  26.304  1.00 53.71           C  
ANISOU 4659  CZ  ARG B 448     6740   6714   6955    154   -254    417       C  
ATOM   4660  NH1 ARG B 448      43.601   0.222  25.449  1.00 46.77           N  
ANISOU 4660  NH1 ARG B 448     5854   5805   6114    155   -241    420       N  
ATOM   4661  NH2 ARG B 448      43.018   1.036  27.518  1.00 53.95           N  
ANISOU 4661  NH2 ARG B 448     6783   6756   6961    167   -255    445       N  
ATOM   4662  N   ARG B 449      47.981  -0.275  23.213  1.00 25.84           N  
ANISOU 4662  N   ARG B 449     3134   3147   3539    164   -274    363       N  
ATOM   4663  CA  ARG B 449      48.261  -1.612  23.747  1.00 25.84           C  
ANISOU 4663  CA  ARG B 449     3128   3134   3555    188   -274    396       C  
ATOM   4664  C   ARG B 449      49.740  -1.817  24.077  1.00 28.60           C  
ANISOU 4664  C   ARG B 449     3457   3499   3911    207   -296    396       C  
ATOM   4665  O   ARG B 449      50.091  -2.352  25.126  1.00 28.14           O  
ANISOU 4665  O   ARG B 449     3397   3454   3842    233   -308    425       O  
ATOM   4666  CB  ARG B 449      47.846  -2.684  22.740  1.00 36.48           C  
ANISOU 4666  CB  ARG B 449     4473   4443   4945    183   -251    398       C  
ATOM   4667  CG  ARG B 449      46.513  -3.342  23.038  1.00 48.40           C  
ANISOU 4667  CG  ARG B 449     5999   5933   6457    184   -230    423       C  
ATOM   4668  CD  ARG B 449      46.395  -4.708  22.358  1.00 46.43           C  
ANISOU 4668  CD  ARG B 449     5742   5646   6254    187   -209    432       C  
ATOM   4669  NE  ARG B 449      46.537  -4.631  20.904  1.00 45.48           N  
ANISOU 4669  NE  ARG B 449     5611   5510   6161    167   -199    397       N  
ATOM   4670  CZ  ARG B 449      45.545  -4.333  20.069  1.00 39.28           C  
ANISOU 4670  CZ  ARG B 449     4832   4714   5377    145   -183    377       C  
ATOM   4671  NH1 ARG B 449      44.334  -4.072  20.542  1.00 43.95           N  
ANISOU 4671  NH1 ARG B 449     5442   5309   5949    140   -175    387       N  
ATOM   4672  NH2 ARG B 449      45.765  -4.286  18.761  1.00 40.31           N  
ANISOU 4672  NH2 ARG B 449     4952   4833   5530    130   -176    347       N  
ATOM   4673  N  AARG B 450      50.604  -1.408  23.158  0.54 22.57           N  
ANISOU 4673  N  AARG B 450     2678   2734   3165    195   -300    363       N  
ATOM   4674  N  BARG B 450      50.602  -1.393  23.161  0.46 22.57           N  
ANISOU 4674  N  BARG B 450     2678   2734   3164    195   -300    363       N  
ATOM   4675  CA AARG B 450      52.043  -1.558  23.337  0.54 22.66           C  
ANISOU 4675  CA AARG B 450     2666   2758   3185    210   -319    356       C  
ATOM   4676  CA BARG B 450      52.042  -1.537  23.330  0.46 22.64           C  
ANISOU 4676  CA BARG B 450     2663   2756   3182    210   -319    356       C  
ATOM   4677  C  AARG B 450      52.587  -0.705  24.483  0.54 26.06           C  
ANISOU 4677  C  AARG B 450     3093   3231   3577    221   -344    354       C  
ATOM   4678  C  BARG B 450      52.547  -0.722  24.512  0.46 26.08           C  
ANISOU 4678  C  BARG B 450     3097   3234   3579    221   -344    355       C  
ATOM   4679  O  AARG B 450      53.465  -1.143  25.223  0.54 26.93           O  
ANISOU 4679  O  AARG B 450     3189   3358   3684    245   -363    367       O  
ATOM   4680  O  BARG B 450      53.345  -1.203  25.309  0.46 27.02           O  
ANISOU 4680  O  BARG B 450     3202   3369   3694    247   -362    372       O  
ATOM   4681  CB AARG B 450      52.766  -1.251  22.021  0.54 19.83           C  
ANISOU 4681  CB AARG B 450     2293   2387   2855    192   -314    319       C  
ATOM   4682  CB BARG B 450      52.773  -1.128  22.054  0.46 19.80           C  
ANISOU 4682  CB BARG B 450     2290   2386   2849    191   -315    317       C  
ATOM   4683  CG AARG B 450      52.635  -2.352  20.969  0.54 23.90           C  
ANISOU 4683  CG AARG B 450     2804   2865   3414    188   -293    321       C  
ATOM   4684  CG BARG B 450      52.777  -2.198  20.984  0.46 23.86           C  
ANISOU 4684  CG BARG B 450     2796   2862   3406    187   -296    318       C  
ATOM   4685  CD AARG B 450      53.648  -3.459  21.273  0.54 34.97           C  
ANISOU 4685  CD AARG B 450     4186   4259   4842    213   -302    339       C  
ATOM   4686  CD BARG B 450      53.651  -3.369  21.390  0.46 35.00           C  
ANISOU 4686  CD BARG B 450     4190   4267   4841    214   -304    340       C  
ATOM   4687  NE AARG B 450      54.255  -3.207  22.582  0.54 49.88           N  
ANISOU 4687  NE AARG B 450     6069   6182   6701    236   -328    354       N  
ATOM   4688  NE BARG B 450      53.002  -4.646  21.116  0.46 49.40           N  
ANISOU 4688  NE BARG B 450     6019   6057   6694    220   -283    364       N  
ATOM   4689  CZ AARG B 450      55.403  -3.720  23.023  0.54 52.38           C  
ANISOU 4689  CZ AARG B 450     6366   6509   7029    260   -346    362       C  
ATOM   4690  CZ BARG B 450      53.631  -5.817  21.095  0.46 51.86           C  
ANISOU 4690  CZ BARG B 450     6315   6349   7039    239   -281    381       C  
ATOM   4691  NH1AARG B 450      56.116  -4.548  22.263  0.54 44.30           N  
ANISOU 4691  NH1AARG B 450     5324   5460   6047    264   -339    357       N  
ATOM   4692  NH1BARG B 450      54.933  -5.878  21.335  0.46 44.19           N  
ANISOU 4692  NH1BARG B 450     5323   5392   6075    255   -301    376       N  
ATOM   4693  NH2AARG B 450      55.833  -3.395  24.239  0.54 41.67           N  
ANISOU 4693  NH2AARG B 450     5006   5188   5639    280   -370    374       N  
ATOM   4694  NH2BARG B 450      52.956  -6.926  20.835  0.46 40.63           N  
ANISOU 4694  NH2BARG B 450     4898   4894   5645    242   -258    401       N  
ATOM   4695  N   ILE B 451      52.078   0.514  24.622  1.00 21.48           N  
ANISOU 4695  N   ILE B 451     2524   2669   2968    203   -345    335       N  
ATOM   4696  CA  ILE B 451      52.410   1.343  25.780  1.00 24.00           C  
ANISOU 4696  CA  ILE B 451     2842   3030   3249    211   -367    332       C  
ATOM   4697  C   ILE B 451      51.953   0.671  27.088  1.00 30.26           C  
ANISOU 4697  C   ILE B 451     3644   3836   4016    237   -374    374       C  
ATOM   4698  O   ILE B 451      52.677   0.647  28.085  1.00 29.46           O  
ANISOU 4698  O   ILE B 451     3533   3766   3895    259   -397    383       O  
ATOM   4699  CB  ILE B 451      51.774   2.755  25.671  1.00 22.66           C  
ANISOU 4699  CB  ILE B 451     2684   2872   3055    185   -361    305       C  
ATOM   4700  CG1 ILE B 451      52.449   3.564  24.558  1.00 24.89           C  
ANISOU 4700  CG1 ILE B 451     2954   3147   3355    164   -356    263       C  
ATOM   4701  CG2 ILE B 451      51.865   3.500  27.001  1.00 23.93           C  
ANISOU 4701  CG2 ILE B 451     2845   3074   3173    194   -380    306       C  
ATOM   4702  CD1 ILE B 451      51.689   4.836  24.152  1.00 23.11           C  
ANISOU 4702  CD1 ILE B 451     2743   2923   3114    137   -342    240       C  
ATOM   4703  N   LEU B 452      50.747   0.123  27.084  1.00 18.81           N  
ANISOU 4703  N   LEU B 452     2215   2363   2568    235   -355    400       N  
ATOM   4704  CA  LEU B 452      50.231  -0.523  28.285  1.00 28.55           C  
ANISOU 4704  CA  LEU B 452     3461   3605   3779    258   -357    441       C  
ATOM   4705  C   LEU B 452      51.041  -1.772  28.632  1.00 29.73           C  
ANISOU 4705  C   LEU B 452     3598   3749   3947    290   -365    471       C  
ATOM   4706  O   LEU B 452      51.409  -1.972  29.791  1.00 38.00           O  
ANISOU 4706  O   LEU B 452     4645   4825   4968    317   -382    495       O  
ATOM   4707  CB  LEU B 452      48.746  -0.844  28.130  1.00 26.73           C  
ANISOU 4707  CB  LEU B 452     3255   3349   3553    247   -330    459       C  
ATOM   4708  CG  LEU B 452      47.872   0.412  28.152  1.00 25.35           C  
ANISOU 4708  CG  LEU B 452     3095   3187   3351    223   -326    438       C  
ATOM   4709  CD1 LEU B 452      46.428   0.063  27.798  1.00 32.75           C  
ANISOU 4709  CD1 LEU B 452     4052   4094   4297    210   -299    450       C  
ATOM   4710  CD2 LEU B 452      47.947   1.054  29.526  1.00 25.43           C  
ANISOU 4710  CD2 LEU B 452     3109   3238   3314    234   -345    446       C  
ATOM   4711  N   MET B 453      51.363  -2.564  27.615  1.00 28.06           N  
ANISOU 4711  N   MET B 453     3377   3504   3781    287   -352    468       N  
ATOM   4712  CA  MET B 453      52.228  -3.723  27.784  1.00 33.54           C  
ANISOU 4712  CA  MET B 453     4056   4189   4498    316   -358    492       C  
ATOM   4713  C   MET B 453      53.540  -3.331  28.453  1.00 36.93           C  
ANISOU 4713  C   MET B 453     4465   4659   4909    335   -391    482       C  
ATOM   4714  O   MET B 453      53.951  -3.949  29.430  1.00 36.20           O  
ANISOU 4714  O   MET B 453     4368   4582   4802    368   -405    514       O  
ATOM   4715  CB  MET B 453      52.520  -4.376  26.431  1.00 29.57           C  
ANISOU 4715  CB  MET B 453     3541   3647   4048    304   -341    476       C  
ATOM   4716  CG  MET B 453      51.356  -5.140  25.826  1.00 35.99           C  
ANISOU 4716  CG  MET B 453     4369   4418   4887    293   -309    491       C  
ATOM   4717  SD  MET B 453      51.867  -6.133  24.409  1.00 60.82           S  
ANISOU 4717  SD  MET B 453     7496   7521   8094    286   -291    477       S  
ATOM   4718  CE  MET B 453      50.418  -6.046  23.371  1.00 45.36           C  
ANISOU 4718  CE  MET B 453     5554   5532   6150    253   -260    460       C  
ATOM   4719  N   TRP B 454      54.201  -2.304  27.924  1.00 28.22           N  
ANISOU 4719  N   TRP B 454     3347   3571   3805    316   -402    438       N  
ATOM   4720  CA  TRP B 454      55.487  -1.889  28.463  1.00 26.03           C  
ANISOU 4720  CA  TRP B 454     3046   3332   3513    331   -432    421       C  
ATOM   4721  C   TRP B 454      55.392  -1.544  29.941  1.00 32.72           C  
ANISOU 4721  C   TRP B 454     3899   4223   4310    352   -453    440       C  
ATOM   4722  O   TRP B 454      56.219  -1.976  30.737  1.00 30.40           O  
ANISOU 4722  O   TRP B 454     3591   3955   4006    383   -475    455       O  
ATOM   4723  CB  TRP B 454      56.080  -0.703  27.702  1.00 24.08           C  
ANISOU 4723  CB  TRP B 454     2785   3094   3272    303   -436    368       C  
ATOM   4724  CG  TRP B 454      57.469  -0.378  28.172  1.00 25.28           C  
ANISOU 4724  CG  TRP B 454     2908   3282   3417    318   -465    347       C  
ATOM   4725  CD1 TRP B 454      58.645  -0.738  27.568  1.00 26.42           C  
ANISOU 4725  CD1 TRP B 454     3025   3418   3594    324   -472    328       C  
ATOM   4726  CD2 TRP B 454      57.834   0.341  29.354  1.00 23.38           C  
ANISOU 4726  CD2 TRP B 454     2659   3090   3132    331   -491    340       C  
ATOM   4727  NE1 TRP B 454      59.716  -0.271  28.294  1.00 27.35           N  
ANISOU 4727  NE1 TRP B 454     3120   3578   3694    338   -501    310       N  
ATOM   4728  CE2 TRP B 454      59.242   0.391  29.409  1.00 29.28           C  
ANISOU 4728  CE2 TRP B 454     3375   3860   3890    344   -514    316       C  
ATOM   4729  CE3 TRP B 454      57.104   0.960  30.386  1.00 37.42           C  
ANISOU 4729  CE3 TRP B 454     4454   4898   4865    332   -497    349       C  
ATOM   4730  CZ2 TRP B 454      59.945   1.033  30.436  1.00 35.40           C  
ANISOU 4730  CZ2 TRP B 454     4133   4686   4631    358   -543    299       C  
ATOM   4731  CZ3 TRP B 454      57.799   1.595  31.416  1.00 35.02           C  
ANISOU 4731  CZ3 TRP B 454     4134   4646   4526    346   -525    334       C  
ATOM   4732  CH2 TRP B 454      59.206   1.628  31.427  1.00 28.81           C  
ANISOU 4732  CH2 TRP B 454     3315   3882   3751    358   -548    309       C  
ATOM   4733  N   HIS B 455      54.385  -0.762  30.306  1.00 29.06           N  
ANISOU 4733  N   HIS B 455     3457   3770   3816    335   -445    437       N  
ATOM   4734  CA  HIS B 455      54.215  -0.354  31.693  1.00 35.31           C  
ANISOU 4734  CA  HIS B 455     4255   4604   4558    352   -463    452       C  
ATOM   4735  C   HIS B 455      53.919  -1.547  32.592  1.00 39.16           C  
ANISOU 4735  C   HIS B 455     4754   5090   5035    387   -463    507       C  
ATOM   4736  O   HIS B 455      54.437  -1.643  33.700  1.00 39.00           O  
ANISOU 4736  O   HIS B 455     4727   5108   4982    416   -486    524       O  
ATOM   4737  CB  HIS B 455      53.107   0.691  31.812  1.00 25.41           C  
ANISOU 4737  CB  HIS B 455     3022   3356   3278    325   -451    437       C  
ATOM   4738  CG  HIS B 455      53.558   2.083  31.499  1.00 35.38           C  
ANISOU 4738  CG  HIS B 455     4271   4640   4532    299   -460    386       C  
ATOM   4739  ND1 HIS B 455      54.032   2.943  32.463  1.00 30.75           N  
ANISOU 4739  ND1 HIS B 455     3675   4102   3907    305   -483    368       N  
ATOM   4740  CD2 HIS B 455      53.614   2.760  30.329  1.00 33.46           C  
ANISOU 4740  CD2 HIS B 455     4024   4376   4314    269   -447    349       C  
ATOM   4741  CE1 HIS B 455      54.355   4.094  31.902  1.00 28.32           C  
ANISOU 4741  CE1 HIS B 455     3357   3800   3605    278   -481    321       C  
ATOM   4742  NE2 HIS B 455      54.111   4.009  30.607  1.00 35.34           N  
ANISOU 4742  NE2 HIS B 455     4250   4647   4532    256   -459    310       N  
ATOM   4743  N   LYS B 456      53.083  -2.455  32.106  1.00 30.72           N  
ANISOU 4743  N   LYS B 456     3702   3977   3994    385   -435    535       N  
ATOM   4744  CA  LYS B 456      52.707  -3.626  32.886  1.00 31.75           C  
ANISOU 4744  CA  LYS B 456     3847   4099   4120    416   -428    589       C  
ATOM   4745  C   LYS B 456      53.937  -4.471  33.229  1.00 40.22           C  
ANISOU 4745  C   LYS B 456     4897   5181   5202    454   -447    609       C  
ATOM   4746  O   LYS B 456      54.126  -4.898  34.371  1.00 40.71           O  
ANISOU 4746  O   LYS B 456     4963   5270   5235    488   -461    644       O  
ATOM   4747  CB  LYS B 456      51.691  -4.457  32.111  1.00 36.12           C  
ANISOU 4747  CB  LYS B 456     4416   4597   4711    403   -391    607       C  
ATOM   4748  CG  LYS B 456      50.924  -5.457  32.950  1.00 44.12           C  
ANISOU 4748  CG  LYS B 456     5451   5597   5716    428   -375    661       C  
ATOM   4749  CD  LYS B 456      51.489  -6.852  32.801  1.00 50.68           C  
ANISOU 4749  CD  LYS B 456     6273   6400   6585    456   -367    694       C  
ATOM   4750  CE  LYS B 456      50.439  -7.891  33.143  1.00 61.79           C  
ANISOU 4750  CE  LYS B 456     7703   7773   8002    467   -335    740       C  
ATOM   4751  NZ  LYS B 456      49.256  -7.769  32.249  1.00 65.63           N  
ANISOU 4751  NZ  LYS B 456     8202   8221   8512    430   -304    722       N  
ATOM   4752  N   LYS B 457      54.784  -4.708  32.237  1.00 36.40           N  
ANISOU 4752  N   LYS B 457     4391   4678   4760    447   -449    585       N  
ATOM   4753  CA  LYS B 457      55.929  -5.570  32.462  1.00 39.53           C  
ANISOU 4753  CA  LYS B 457     4767   5080   5173    482   -465    603       C  
ATOM   4754  C   LYS B 457      57.086  -4.858  33.157  1.00 39.82           C  
ANISOU 4754  C   LYS B 457     4780   5172   5178    498   -504    581       C  
ATOM   4755  O   LYS B 457      57.803  -5.477  33.934  1.00 41.45           O  
ANISOU 4755  O   LYS B 457     4976   5401   5374    538   -523    608       O  
ATOM   4756  CB  LYS B 457      56.383  -6.264  31.169  1.00 44.21           C  
ANISOU 4756  CB  LYS B 457     5344   5627   5826    472   -449    590       C  
ATOM   4757  CG  LYS B 457      57.053  -5.369  30.163  1.00 42.48           C  
ANISOU 4757  CG  LYS B 457     5105   5411   5624    442   -457    533       C  
ATOM   4758  CD  LYS B 457      57.695  -6.201  29.047  1.00 47.23           C  
ANISOU 4758  CD  LYS B 457     5689   5974   6283    440   -445    525       C  
ATOM   4759  CE  LYS B 457      58.830  -7.066  29.569  1.00 43.34           C  
ANISOU 4759  CE  LYS B 457     5174   5492   5801    481   -464    548       C  
ATOM   4760  NZ  LYS B 457      59.490  -7.848  28.474  1.00 54.99           N  
ANISOU 4760  NZ  LYS B 457     6631   6929   7334    478   -452    537       N  
ATOM   4761  N   ASN B 458      57.248  -3.561  32.917  1.00 42.18           N  
ANISOU 4761  N   ASN B 458     5070   5494   5461    470   -514    532       N  
ATOM   4762  CA  ASN B 458      58.394  -2.832  33.470  1.00 36.66           C  
ANISOU 4762  CA  ASN B 458     4344   4846   4737    481   -549    501       C  
ATOM   4763  C   ASN B 458      58.124  -1.947  34.686  1.00 44.54           C  
ANISOU 4763  C   ASN B 458     5349   5897   5676    486   -568    498       C  
ATOM   4764  O   ASN B 458      59.042  -1.653  35.462  1.00 44.97           O  
ANISOU 4764  O   ASN B 458     5382   6001   5704    508   -599    487       O  
ATOM   4765  CB  ASN B 458      59.078  -2.006  32.379  1.00 38.48           C  
ANISOU 4765  CB  ASN B 458     4554   5071   4997    448   -550    443       C  
ATOM   4766  CG  ASN B 458      59.714  -2.868  31.317  1.00 38.21           C  
ANISOU 4766  CG  ASN B 458     4504   4996   5018    450   -540    441       C  
ATOM   4767  OD1 ASN B 458      60.742  -3.495  31.555  1.00 48.72           O  
ANISOU 4767  OD1 ASN B 458     5813   6339   6360    479   -558    449       O  
ATOM   4768  ND2 ASN B 458      59.105  -2.910  30.136  1.00 34.62           N  
ANISOU 4768  ND2 ASN B 458     4061   4496   4597    419   -510    430       N  
ATOM   4769  N   GLY B 459      56.877  -1.511  34.845  1.00 45.05           N  
ANISOU 4769  N   GLY B 459     5443   5954   5721    466   -549    505       N  
ATOM   4770  CA  GLY B 459      56.544  -0.527  35.860  1.00 50.04           C  
ANISOU 4770  CA  GLY B 459     6081   6632   6299    463   -563    495       C  
ATOM   4771  C   GLY B 459      56.847   0.887  35.383  1.00 50.55           C  
ANISOU 4771  C   GLY B 459     6131   6713   6363    427   -568    433       C  
ATOM   4772  O   GLY B 459      57.352   1.085  34.273  1.00 46.27           O  
ANISOU 4772  O   GLY B 459     5575   6146   5860    406   -561    401       O  
ATOM   4773  N   ALA B 460      56.547   1.877  36.215  1.00 62.61           N  
ANISOU 4773  N   ALA B 460     7662   8280   7846    420   -578    416       N  
ATOM   4774  CA  ALA B 460      56.798   3.267  35.844  1.00 60.48           C  
ANISOU 4774  CA  ALA B 460     7380   8026   7576    386   -579    358       C  
ATOM   4775  C   ALA B 460      58.279   3.616  35.979  1.00 63.77           C  
ANISOU 4775  C   ALA B 460     7758   8478   7993    396   -608    321       C  
ATOM   4776  O   ALA B 460      58.940   3.188  36.930  1.00 61.49           O  
ANISOU 4776  O   ALA B 460     7454   8229   7679    432   -636    336       O  
ATOM   4777  CB  ALA B 460      55.951   4.206  36.679  1.00 65.67           C  
ANISOU 4777  CB  ALA B 460     8053   8710   8188    373   -578    352       C  
ATOM   4778  N   PRO B 461      58.810   4.391  35.019  1.00 72.36           N  
ANISOU 4778  N   PRO B 461     8829   9553   9112    367   -601    271       N  
ATOM   4779  CA  PRO B 461      60.189   4.879  35.116  1.00 70.68           C  
ANISOU 4779  CA  PRO B 461     8578   9374   8903    371   -626    227       C  
ATOM   4780  C   PRO B 461      60.288   5.903  36.244  1.00 65.84           C  
ANISOU 4780  C   PRO B 461     7955   8818   8242    371   -645    200       C  
ATOM   4781  O   PRO B 461      59.261   6.460  36.647  1.00 64.76           O  
ANISOU 4781  O   PRO B 461     7842   8686   8079    357   -633    205       O  
ATOM   4782  CB  PRO B 461      60.423   5.564  33.759  1.00 67.45           C  
ANISOU 4782  CB  PRO B 461     8162   8930   8537    333   -604    183       C  
ATOM   4783  CG  PRO B 461      59.275   5.132  32.872  1.00 62.57           C  
ANISOU 4783  CG  PRO B 461     7576   8256   7940    316   -572    212       C  
ATOM   4784  CD  PRO B 461      58.135   4.884  33.806  1.00 64.59           C  
ANISOU 4784  CD  PRO B 461     7861   8523   8159    328   -570    253       C  
ATOM   4785  N   PRO B 462      61.506   6.134  36.759  1.00 59.23           N  
ANISOU 4785  N   PRO B 462     7082   8026   7395    387   -675    169       N  
ATOM   4786  CA  PRO B 462      61.767   7.153  37.787  1.00 49.10           C  
ANISOU 4786  CA  PRO B 462     5782   6802   6070    386   -694    133       C  
ATOM   4787  C   PRO B 462      61.367   8.536  37.278  1.00 53.40           C  
ANISOU 4787  C   PRO B 462     6332   7335   6624    340   -671     85       C  
ATOM   4788  O   PRO B 462      61.781   8.918  36.181  1.00 42.67           O  
ANISOU 4788  O   PRO B 462     4961   5943   5306    315   -655     52       O  
ATOM   4789  CB  PRO B 462      63.286   7.091  37.969  1.00 54.22           C  
ANISOU 4789  CB  PRO B 462     6388   7487   6727    406   -725    100       C  
ATOM   4790  CG  PRO B 462      63.686   5.727  37.485  1.00 53.22           C  
ANISOU 4790  CG  PRO B 462     6261   7331   6631    433   -728    140       C  
ATOM   4791  CD  PRO B 462      62.722   5.388  36.386  1.00 59.29           C  
ANISOU 4791  CD  PRO B 462     7061   8032   7434    409   -691    165       C  
ATOM   4792  N   LEU B 463      60.581   9.273  38.060  1.00 68.43           N  
ANISOU 4792  N   LEU B 463     8249   9263   8488    330   -668     81       N  
ATOM   4793  CA  LEU B 463      60.034  10.554  37.615  1.00 64.79           C  
ANISOU 4793  CA  LEU B 463     7796   8786   8035    288   -643     42       C  
ATOM   4794  C   LEU B 463      61.115  11.594  37.357  1.00 67.19           C  
ANISOU 4794  C   LEU B 463     8063   9109   8356    268   -647    -26       C  
ATOM   4795  O   LEU B 463      60.919  12.524  36.575  1.00 67.29           O  
ANISOU 4795  O   LEU B 463     8079   9093   8393    232   -621    -59       O  
ATOM   4796  CB  LEU B 463      59.020  11.089  38.624  1.00 68.81           C  
ANISOU 4796  CB  LEU B 463     8326   9323   8498    284   -641     52       C  
ATOM   4797  CG  LEU B 463      58.008  10.053  39.105  1.00 73.67           C  
ANISOU 4797  CG  LEU B 463     8974   9927   9089    308   -639    118       C  
ATOM   4798  CD1 LEU B 463      58.508   9.387  40.385  1.00 80.39           C  
ANISOU 4798  CD1 LEU B 463     9814  10834   9898    351   -673    142       C  
ATOM   4799  CD2 LEU B 463      56.650  10.692  39.326  1.00 69.46           C  
ANISOU 4799  CD2 LEU B 463     8471   9383   8536    285   -616    126       C  
ATOM   4800  N   ALA B 464      62.258  11.426  38.012  1.00 53.34           N  
ANISOU 4800  N   ALA B 464     6275   7402   6590    292   -679    -46       N  
ATOM   4801  CA  ALA B 464      63.378  12.342  37.845  1.00 58.00           C  
ANISOU 4801  CA  ALA B 464     6825   8013   7198    276   -685   -113       C  
ATOM   4802  C   ALA B 464      63.917  12.386  36.413  1.00 58.13           C  
ANISOU 4802  C   ALA B 464     6834   7979   7273    253   -663   -135       C  
ATOM   4803  O   ALA B 464      64.445  13.405  35.980  1.00 49.95           O  
ANISOU 4803  O   ALA B 464     5778   6941   6259    225   -650   -191       O  
ATOM   4804  CB  ALA B 464      64.492  11.993  38.818  1.00 69.38           C  
ANISOU 4804  CB  ALA B 464     8230   9517   8616    311   -726   -127       C  
ATOM   4805  N   GLU B 465      63.803  11.289  35.673  1.00 62.80           N  
ANISOU 4805  N   GLU B 465     7441   8531   7890    266   -657    -93       N  
ATOM   4806  CA  GLU B 465      64.334  11.300  34.314  1.00 64.85           C  
ANISOU 4806  CA  GLU B 465     7693   8744   8203    246   -636   -114       C  
ATOM   4807  C   GLU B 465      63.263  11.400  33.223  1.00 53.22           C  
ANISOU 4807  C   GLU B 465     6257   7211   6753    218   -598    -94       C  
ATOM   4808  O   GLU B 465      63.584  11.460  32.032  1.00 57.49           O  
ANISOU 4808  O   GLU B 465     6795   7712   7336    199   -577   -110       O  
ATOM   4809  CB  GLU B 465      65.283  10.119  34.079  1.00 75.03           C  
ANISOU 4809  CB  GLU B 465     8963  10030   9515    275   -656    -97       C  
ATOM   4810  CG  GLU B 465      66.594  10.226  34.870  1.00 82.53           C  
ANISOU 4810  CG  GLU B 465     9867  11036  10454    297   -691   -133       C  
ATOM   4811  CD  GLU B 465      67.311  11.566  34.671  1.00 88.96           C  
ANISOU 4811  CD  GLU B 465    10652  11864  11283    265   -683   -207       C  
ATOM   4812  OE1 GLU B 465      67.693  11.887  33.521  1.00 84.59           O  
ANISOU 4812  OE1 GLU B 465    10094  11272  10776    239   -658   -235       O  
ATOM   4813  OE2 GLU B 465      67.494  12.298  35.669  1.00 83.99           O  
ANISOU 4813  OE2 GLU B 465    10004  11286  10620    267   -700   -238       O  
ATOM   4814  N   ARG B 466      62.003  11.459  33.634  1.00 52.29           N  
ANISOU 4814  N   ARG B 466     6172   7090   6607    216   -589    -61       N  
ATOM   4815  CA  ARG B 466      60.903  11.598  32.687  1.00 54.74           C  
ANISOU 4815  CA  ARG B 466     6516   7349   6934    191   -555    -43       C  
ATOM   4816  C   ARG B 466      60.888  12.979  32.038  1.00 49.60           C  
ANISOU 4816  C   ARG B 466     5863   6682   6300    153   -528    -92       C  
ATOM   4817  O   ARG B 466      60.925  13.998  32.727  1.00 44.62           O  
ANISOU 4817  O   ARG B 466     5223   6083   5649    142   -530   -125       O  
ATOM   4818  CB  ARG B 466      59.565  11.334  33.378  1.00 45.47           C  
ANISOU 4818  CB  ARG B 466     5375   6177   5724    199   -552      2       C  
ATOM   4819  CG  ARG B 466      59.376   9.900  33.832  1.00 51.61           C  
ANISOU 4819  CG  ARG B 466     6163   6957   6491    235   -569     58       C  
ATOM   4820  CD  ARG B 466      57.931   9.470  33.706  1.00 40.04           C  
ANISOU 4820  CD  ARG B 466     4737   5460   5018    232   -549    103       C  
ATOM   4821  NE  ARG B 466      57.715   8.617  32.544  1.00 47.00           N  
ANISOU 4821  NE  ARG B 466     5631   6290   5939    229   -531    127       N  
ATOM   4822  CZ  ARG B 466      56.560   8.030  32.258  1.00 42.96           C  
ANISOU 4822  CZ  ARG B 466     5149   5746   5429    228   -512    166       C  
ATOM   4823  NH1 ARG B 466      55.514   8.207  33.050  1.00 36.20           N  
ANISOU 4823  NH1 ARG B 466     4315   4902   4538    229   -509    187       N  
ATOM   4824  NH2 ARG B 466      56.449   7.268  31.181  1.00 55.95           N  
ANISOU 4824  NH2 ARG B 466     6801   7346   7110    225   -497    181       N  
ATOM   4825  N   GLY B 467      60.829  13.003  30.711  1.00 42.44           N  
ANISOU 4825  N   GLY B 467     4965   5727   5431    134   -502    -95       N  
ATOM   4826  CA  GLY B 467      60.716  14.247  29.979  1.00 40.10           C  
ANISOU 4826  CA  GLY B 467     4672   5409   5153     99   -472   -134       C  
ATOM   4827  C   GLY B 467      62.033  14.713  29.402  1.00 40.86           C  
ANISOU 4827  C   GLY B 467     4737   5505   5283     87   -468   -184       C  
ATOM   4828  O   GLY B 467      62.078  15.700  28.670  1.00 44.71           O  
ANISOU 4828  O   GLY B 467     5226   5970   5792     59   -439   -217       O  
ATOM   4829  N   LYS B 468      63.108  13.997  29.717  1.00 52.08           N  
ANISOU 4829  N   LYS B 468     6129   6948   6711    109   -495   -189       N  
ATOM   4830  CA  LYS B 468      64.439  14.433  29.316  1.00 52.74           C  
ANISOU 4830  CA  LYS B 468     6178   7037   6825    100   -494   -241       C  
ATOM   4831  C   LYS B 468      64.905  13.843  27.981  1.00 53.47           C  
ANISOU 4831  C   LYS B 468     6270   7084   6961     95   -478   -237       C  
ATOM   4832  O   LYS B 468      65.708  14.447  27.267  1.00 69.31           O  
ANISOU 4832  O   LYS B 468     8258   9077   9000     75   -461   -280       O  
ATOM   4833  CB  LYS B 468      65.443  14.169  30.441  1.00 62.35           C  
ANISOU 4833  CB  LYS B 468     7357   8308   8024    125   -532   -259       C  
ATOM   4834  CG  LYS B 468      65.107  14.931  31.717  1.00 58.81           C  
ANISOU 4834  CG  LYS B 468     6905   7907   7533    126   -546   -274       C  
ATOM   4835  CD  LYS B 468      66.254  14.910  32.711  1.00 77.84           C  
ANISOU 4835  CD  LYS B 468     9273  10375   9929    147   -581   -306       C  
ATOM   4836  CE  LYS B 468      65.991  15.862  33.874  1.00 79.68           C  
ANISOU 4836  CE  LYS B 468     9498  10655  10123    142   -590   -333       C  
ATOM   4837  NZ  LYS B 468      67.205  16.052  34.722  1.00 89.84           N  
ANISOU 4837  NZ  LYS B 468    10738  11999  11399    156   -622   -379       N  
ATOM   4838  N   GLY B 469      64.394  12.667  27.645  1.00 40.66           N  
ANISOU 4838  N   GLY B 469     4668   5440   5342    111   -481   -187       N  
ATOM   4839  CA  GLY B 469      64.674  12.048  26.362  1.00 33.94           C  
ANISOU 4839  CA  GLY B 469     3819   4545   4530    106   -464   -181       C  
ATOM   4840  C   GLY B 469      63.520  11.118  26.059  1.00 28.01           C  
ANISOU 4840  C   GLY B 469     3103   3766   3773    115   -458   -125       C  
ATOM   4841  O   GLY B 469      62.459  11.246  26.663  1.00 30.42           O  
ANISOU 4841  O   GLY B 469     3432   4080   4047    118   -459    -99       O  
ATOM   4842  N   ILE B 470      63.725  10.193  25.134  1.00 28.95           N  
ANISOU 4842  N   ILE B 470     3224   3853   3923    120   -451   -108       N  
ATOM   4843  CA  ILE B 470      62.752   9.144  24.849  1.00 30.67           C  
ANISOU 4843  CA  ILE B 470     3469   4044   4140    131   -446    -57       C  
ATOM   4844  C   ILE B 470      62.118   8.546  26.107  1.00 34.28           C  
ANISOU 4844  C   ILE B 470     3936   4529   4560    157   -469    -17       C  
ATOM   4845  O   ILE B 470      62.798   8.313  27.108  1.00 37.18           O  
ANISOU 4845  O   ILE B 470     4282   4934   4912    180   -498    -19       O  
ATOM   4846  CB  ILE B 470      63.422   7.988  24.095  1.00 36.58           C  
ANISOU 4846  CB  ILE B 470     4205   4769   4925    143   -448    -47       C  
ATOM   4847  CG1 ILE B 470      63.389   8.238  22.588  1.00 38.59           C  
ANISOU 4847  CG1 ILE B 470     4469   4981   5213    116   -415    -64       C  
ATOM   4848  CG2 ILE B 470      62.741   6.668  24.429  1.00 44.29           C  
ANISOU 4848  CG2 ILE B 470     5197   5737   5894    168   -457      7       C  
ATOM   4849  CD1 ILE B 470      64.044   9.520  22.182  1.00 38.20           C  
ANISOU 4849  CD1 ILE B 470     4406   4935   5173     91   -400   -115       C  
ATOM   4850  N   ASP B 471      60.809   8.313  26.044  1.00 27.78           N  
ANISOU 4850  N   ASP B 471     3145   3687   3723    155   -456     18       N  
ATOM   4851  CA  ASP B 471      60.091   7.473  27.001  1.00 22.43           C  
ANISOU 4851  CA  ASP B 471     2482   3023   3019    180   -471     65       C  
ATOM   4852  C   ASP B 471      60.074   6.058  26.421  1.00 31.05           C  
ANISOU 4852  C   ASP B 471     3577   4083   4138    196   -468     99       C  
ATOM   4853  O   ASP B 471      59.635   5.855  25.284  1.00 21.64           O  
ANISOU 4853  O   ASP B 471     2398   2852   2972    180   -444    101       O  
ATOM   4854  CB  ASP B 471      58.672   8.007  27.168  1.00 28.52           C  
ANISOU 4854  CB  ASP B 471     3284   3787   3763    166   -455     80       C  
ATOM   4855  CG  ASP B 471      57.736   7.029  27.849  1.00 35.49           C  
ANISOU 4855  CG  ASP B 471     4188   4669   4627    187   -460    132       C  
ATOM   4856  OD1 ASP B 471      56.832   6.496  27.160  1.00 32.82           O  
ANISOU 4856  OD1 ASP B 471     3871   4295   4302    181   -440    156       O  
ATOM   4857  OD2 ASP B 471      57.878   6.816  29.077  1.00 40.52           O  
ANISOU 4857  OD2 ASP B 471     4820   5343   5235    210   -483    147       O  
ATOM   4858  N   PRO B 472      60.576   5.070  27.189  1.00 38.60           N  
ANISOU 4858  N   PRO B 472     4521   5057   5090    229   -491    125       N  
ATOM   4859  CA  PRO B 472      60.707   3.694  26.684  1.00 34.64           C  
ANISOU 4859  CA  PRO B 472     4018   4525   4618    246   -488    155       C  
ATOM   4860  C   PRO B 472      59.387   3.086  26.191  1.00 29.67           C  
ANISOU 4860  C   PRO B 472     3419   3858   3994    239   -464    190       C  
ATOM   4861  O   PRO B 472      59.375   2.406  25.156  1.00 26.30           O  
ANISOU 4861  O   PRO B 472     2995   3395   3604    233   -447    195       O  
ATOM   4862  CB  PRO B 472      61.234   2.921  27.905  1.00 40.53           C  
ANISOU 4862  CB  PRO B 472     4750   5304   5345    285   -518    183       C  
ATOM   4863  CG  PRO B 472      61.969   3.960  28.708  1.00 40.12           C  
ANISOU 4863  CG  PRO B 472     4677   5301   5267    285   -540    146       C  
ATOM   4864  CD  PRO B 472      61.122   5.211  28.552  1.00 38.82           C  
ANISOU 4864  CD  PRO B 472     4531   5134   5083    253   -522    124       C  
ATOM   4865  N   ALA B 473      58.300   3.323  26.915  1.00 30.05           N  
ANISOU 4865  N   ALA B 473     3491   3917   4009    240   -462    213       N  
ATOM   4866  CA  ALA B 473      56.990   2.797  26.510  1.00 30.04           C  
ANISOU 4866  CA  ALA B 473     3519   3883   4013    233   -439    243       C  
ATOM   4867  C   ALA B 473      56.621   3.293  25.108  1.00 28.05           C  
ANISOU 4867  C   ALA B 473     3275   3598   3785    201   -412    217       C  
ATOM   4868  O   ALA B 473      56.240   2.500  24.233  1.00 23.35           O  
ANISOU 4868  O   ALA B 473     2687   2967   3218    197   -395    230       O  
ATOM   4869  CB  ALA B 473      55.908   3.181  27.526  1.00 24.20           C  
ANISOU 4869  CB  ALA B 473     2801   3162   3231    235   -440    264       C  
ATOM   4870  N   CYS B 474      56.756   4.603  24.890  1.00 30.10           N  
ANISOU 4870  N   CYS B 474     3533   3870   4035    178   -409    180       N  
ATOM   4871  CA  CYS B 474      56.458   5.194  23.582  1.00 26.54           C  
ANISOU 4871  CA  CYS B 474     3090   3390   3603    149   -384    156       C  
ATOM   4872  C   CYS B 474      57.423   4.698  22.531  1.00 25.11           C  
ANISOU 4872  C   CYS B 474     2891   3188   3463    147   -379    139       C  
ATOM   4873  O   CYS B 474      57.033   4.470  21.389  1.00 20.83           O  
ANISOU 4873  O   CYS B 474     2358   2614   2943    132   -357    136       O  
ATOM   4874  CB  CYS B 474      56.507   6.733  23.616  1.00 27.42           C  
ANISOU 4874  CB  CYS B 474     3202   3519   3697    128   -380    120       C  
ATOM   4875  SG  CYS B 474      55.284   7.518  24.662  1.00 28.09           S  
ANISOU 4875  SG  CYS B 474     3310   3626   3737    124   -380    133       S  
ATOM   4876  N   GLN B 475      58.694   4.554  22.902  1.00 29.45           N  
ANISOU 4876  N   GLN B 475     3413   3755   4020    160   -398    125       N  
ATOM   4877  CA  GLN B 475      59.668   3.987  21.967  1.00 28.21           C  
ANISOU 4877  CA  GLN B 475     3236   3578   3904    159   -394    109       C  
ATOM   4878  C   GLN B 475      59.289   2.547  21.595  1.00 23.32           C  
ANISOU 4878  C   GLN B 475     2623   2930   3308    173   -387    144       C  
ATOM   4879  O   GLN B 475      59.345   2.164  20.433  1.00 25.22           O  
ANISOU 4879  O   GLN B 475     2863   3140   3580    161   -369    136       O  
ATOM   4880  CB  GLN B 475      61.094   4.052  22.519  1.00 29.61           C  
ANISOU 4880  CB  GLN B 475     3382   3783   4087    174   -418     88       C  
ATOM   4881  CG  GLN B 475      62.154   3.698  21.482  1.00 24.91           C  
ANISOU 4881  CG  GLN B 475     2764   3166   3534    168   -411     64       C  
ATOM   4882  CD  GLN B 475      62.173   4.678  20.311  1.00 30.93           C  
ANISOU 4882  CD  GLN B 475     3532   3910   4310    135   -385     27       C  
ATOM   4883  OE1 GLN B 475      62.155   4.280  19.138  1.00 25.27           O  
ANISOU 4883  OE1 GLN B 475     2818   3160   3621    123   -365     23       O  
ATOM   4884  NE2 GLN B 475      62.210   5.964  20.626  1.00 22.13           N  
ANISOU 4884  NE2 GLN B 475     2418   2816   3174    120   -384      0       N  
ATOM   4885  N   ALA B 476      58.886   1.758  22.583  1.00 22.55           N  
ANISOU 4885  N   ALA B 476     2531   2842   3196    198   -399    183       N  
ATOM   4886  CA  ALA B 476      58.477   0.391  22.306  1.00 26.99           C  
ANISOU 4886  CA  ALA B 476     3099   3374   3781    211   -390    217       C  
ATOM   4887  C   ALA B 476      57.320   0.404  21.300  1.00 30.13           C  
ANISOU 4887  C   ALA B 476     3520   3741   4188    188   -361    218       C  
ATOM   4888  O   ALA B 476      57.298  -0.398  20.379  1.00 27.59           O  
ANISOU 4888  O   ALA B 476     3195   3388   3900    184   -346    220       O  
ATOM   4889  CB  ALA B 476      58.069  -0.320  23.586  1.00 33.32           C  
ANISOU 4889  CB  ALA B 476     3908   4191   4560    241   -404    260       C  
ATOM   4890  N   ALA B 477      56.359   1.315  21.481  1.00 28.09           N  
ANISOU 4890  N   ALA B 477     3282   3490   3899    173   -355    215       N  
ATOM   4891  CA  ALA B 477      55.215   1.376  20.575  1.00 22.71           C  
ANISOU 4891  CA  ALA B 477     2622   2784   3224    153   -330    215       C  
ATOM   4892  C   ALA B 477      55.643   1.720  19.146  1.00 25.36           C  
ANISOU 4892  C   ALA B 477     2950   3099   3585    131   -314    181       C  
ATOM   4893  O   ALA B 477      55.230   1.043  18.198  1.00 21.13           O  
ANISOU 4893  O   ALA B 477     2419   2535   3074    124   -296    184       O  
ATOM   4894  CB  ALA B 477      54.152   2.355  21.077  1.00 24.21           C  
ANISOU 4894  CB  ALA B 477     2834   2989   3377    142   -327    217       C  
ATOM   4895  N   ALA B 478      56.478   2.753  18.988  1.00 23.30           N  
ANISOU 4895  N   ALA B 478     2678   2854   3320    120   -318    148       N  
ATOM   4896  CA  ALA B 478      56.951   3.130  17.655  1.00 23.71           C  
ANISOU 4896  CA  ALA B 478     2725   2888   3397    100   -302    116       C  
ATOM   4897  C   ALA B 478      57.754   2.010  16.987  1.00 25.04           C  
ANISOU 4897  C   ALA B 478     2875   3036   3605    107   -299    115       C  
ATOM   4898  O   ALA B 478      57.554   1.715  15.805  1.00 25.72           O  
ANISOU 4898  O   ALA B 478     2964   3096   3712     94   -279    105       O  
ATOM   4899  CB  ALA B 478      57.749   4.457  17.683  1.00 18.41           C  
ANISOU 4899  CB  ALA B 478     2044   2235   2715     87   -305     80       C  
ATOM   4900  N   ASP B 479      58.660   1.394  17.740  1.00 23.19           N  
ANISOU 4900  N   ASP B 479     2620   2813   3379    128   -319    123       N  
ATOM   4901  CA  ASP B 479      59.453   0.279  17.210  1.00 28.10           C  
ANISOU 4901  CA  ASP B 479     3221   3414   4040    138   -318    124       C  
ATOM   4902  C   ASP B 479      58.528  -0.798  16.648  1.00 26.06           C  
ANISOU 4902  C   ASP B 479     2976   3126   3801    138   -300    148       C  
ATOM   4903  O   ASP B 479      58.682  -1.245  15.510  1.00 28.53           O  
ANISOU 4903  O   ASP B 479     3284   3414   4144    127   -283    134       O  
ATOM   4904  CB  ASP B 479      60.337  -0.328  18.301  1.00 30.70           C  
ANISOU 4904  CB  ASP B 479     3530   3762   4371    167   -344    140       C  
ATOM   4905  CG  ASP B 479      61.492   0.585  18.698  1.00 37.65           C  
ANISOU 4905  CG  ASP B 479     4391   4672   5244    166   -361    108       C  
ATOM   4906  OD1 ASP B 479      61.933   1.391  17.852  1.00 37.77           O  
ANISOU 4906  OD1 ASP B 479     4401   4682   5269    144   -349     72       O  
ATOM   4907  OD2 ASP B 479      61.955   0.501  19.857  1.00 44.25           O  
ANISOU 4907  OD2 ASP B 479     5214   5535   6063    189   -386    120       O  
ATOM   4908  N   TYR B 480      57.556  -1.186  17.457  1.00 22.48           N  
ANISOU 4908  N   TYR B 480     2538   2675   3328    150   -303    181       N  
ATOM   4909  CA  TYR B 480      56.580  -2.191  17.062  1.00 30.50           C  
ANISOU 4909  CA  TYR B 480     3565   3663   4359    151   -285    204       C  
ATOM   4910  C   TYR B 480      55.768  -1.783  15.823  1.00 26.34           C  
ANISOU 4910  C   TYR B 480     3052   3119   3835    124   -261    184       C  
ATOM   4911  O   TYR B 480      55.617  -2.570  14.896  1.00 27.03           O  
ANISOU 4911  O   TYR B 480     3135   3181   3952    118   -244    180       O  
ATOM   4912  CB  TYR B 480      55.667  -2.527  18.250  1.00 27.88           C  
ANISOU 4912  CB  TYR B 480     3249   3340   4003    168   -291    242       C  
ATOM   4913  CG  TYR B 480      54.722  -3.670  17.984  1.00 30.02           C  
ANISOU 4913  CG  TYR B 480     3530   3582   4295    171   -271    266       C  
ATOM   4914  CD1 TYR B 480      53.427  -3.432  17.557  1.00 31.67           C  
ANISOU 4914  CD1 TYR B 480     3759   3781   4493    154   -254    266       C  
ATOM   4915  CD2 TYR B 480      55.132  -4.995  18.147  1.00 43.85           C  
ANISOU 4915  CD2 TYR B 480     5269   5314   6078    191   -269    288       C  
ATOM   4916  CE1 TYR B 480      52.552  -4.471  17.299  1.00 36.60           C  
ANISOU 4916  CE1 TYR B 480     4389   4379   5138    155   -234    283       C  
ATOM   4917  CE2 TYR B 480      54.266  -6.048  17.893  1.00 42.21           C  
ANISOU 4917  CE2 TYR B 480     5067   5077   5893    192   -248    308       C  
ATOM   4918  CZ  TYR B 480      52.976  -5.778  17.466  1.00 47.07           C  
ANISOU 4918  CZ  TYR B 480     5702   5684   6498    174   -230    304       C  
ATOM   4919  OH  TYR B 480      52.095  -6.799  17.201  1.00 46.33           O  
ANISOU 4919  OH  TYR B 480     5613   5562   6428    173   -208    319       O  
ATOM   4920  N   LEU B 481      55.245  -0.558  15.799  1.00 24.14           N  
ANISOU 4920  N   LEU B 481     2790   2856   3526    109   -260    170       N  
ATOM   4921  CA  LEU B 481      54.471  -0.115  14.642  1.00 24.92           C  
ANISOU 4921  CA  LEU B 481     2902   2942   3624     87   -239    153       C  
ATOM   4922  C   LEU B 481      55.282  -0.217  13.355  1.00 19.82           C  
ANISOU 4922  C   LEU B 481     2242   2281   3007     74   -227    123       C  
ATOM   4923  O   LEU B 481      54.760  -0.634  12.323  1.00 22.60           O  
ANISOU 4923  O   LEU B 481     2598   2614   3374     64   -208    116       O  
ATOM   4924  CB  LEU B 481      53.935   1.319  14.822  1.00 22.89           C  
ANISOU 4924  CB  LEU B 481     2662   2704   3329     74   -239    142       C  
ATOM   4925  CG  LEU B 481      52.740   1.481  15.763  1.00 22.74           C  
ANISOU 4925  CG  LEU B 481     2663   2696   3281     80   -243    167       C  
ATOM   4926  CD1 LEU B 481      52.435   2.945  16.022  1.00 25.29           C  
ANISOU 4926  CD1 LEU B 481     2999   3040   3571     68   -245    154       C  
ATOM   4927  CD2 LEU B 481      51.513   0.753  15.207  1.00 18.69           C  
ANISOU 4927  CD2 LEU B 481     2161   2162   2776     76   -226    179       C  
ATOM   4928  N   SER B 482      56.553   0.174  13.409  1.00 21.84           N  
ANISOU 4928  N   SER B 482     2481   2546   3271     75   -237    104       N  
ATOM   4929  CA  SER B 482      57.389   0.141  12.211  1.00 25.55           C  
ANISOU 4929  CA  SER B 482     2937   3001   3768     63   -224     75       C  
ATOM   4930  C   SER B 482      57.640  -1.296  11.721  1.00 25.70           C  
ANISOU 4930  C   SER B 482     2942   2996   3827     70   -217     82       C  
ATOM   4931  O   SER B 482      57.596  -1.565  10.525  1.00 23.43           O  
ANISOU 4931  O   SER B 482     2652   2690   3558     57   -198     65       O  
ATOM   4932  CB  SER B 482      58.721   0.870  12.422  1.00 20.23           C  
ANISOU 4932  CB  SER B 482     2247   2343   3098     62   -235     51       C  
ATOM   4933  OG  SER B 482      59.510   0.243  13.410  1.00 24.81           O  
ANISOU 4933  OG  SER B 482     2807   2931   3687     84   -256     64       O  
ATOM   4934  N   MET B 483      57.919  -2.205  12.645  1.00 32.94           N  
ANISOU 4934  N   MET B 483     3848   3913   4756     92   -231    107       N  
ATOM   4935  CA  MET B 483      58.184  -3.586  12.260  1.00 39.31           C  
ANISOU 4935  CA  MET B 483     4640   4695   5603    101   -223    115       C  
ATOM   4936  C   MET B 483      56.904  -4.193  11.697  1.00 35.48           C  
ANISOU 4936  C   MET B 483     4169   4189   5122     93   -203    125       C  
ATOM   4937  O   MET B 483      56.923  -4.917  10.708  1.00 33.71           O  
ANISOU 4937  O   MET B 483     3936   3943   4928     85   -186    113       O  
ATOM   4938  CB  MET B 483      58.713  -4.386  13.450  1.00 41.49           C  
ANISOU 4938  CB  MET B 483     4903   4975   5888    129   -242    144       C  
ATOM   4939  CG  MET B 483      57.660  -5.127  14.235  1.00 60.54           C  
ANISOU 4939  CG  MET B 483     7329   7382   8292    144   -241    183       C  
ATOM   4940  SD  MET B 483      57.256  -6.744  13.538  1.00 77.13           S  
ANISOU 4940  SD  MET B 483     9423   9443  10441    147   -216    195       S  
ATOM   4941  CE  MET B 483      55.849  -7.192  14.562  1.00 60.96           C  
ANISOU 4941  CE  MET B 483     7397   7392   8371    159   -213    237       C  
ATOM   4942  N   LEU B 484      55.778  -3.853  12.308  1.00 32.89           N  
ANISOU 4942  N   LEU B 484     3862   3872   4764     94   -205    144       N  
ATOM   4943  CA  LEU B 484      54.483  -4.305  11.820  1.00 32.84           C  
ANISOU 4943  CA  LEU B 484     3868   3850   4759     86   -186    151       C  
ATOM   4944  C   LEU B 484      54.209  -3.779  10.402  1.00 26.29           C  
ANISOU 4944  C   LEU B 484     3044   3015   3929     62   -169    118       C  
ATOM   4945  O   LEU B 484      53.666  -4.491   9.561  1.00 25.20           O  
ANISOU 4945  O   LEU B 484     2904   2859   3811     54   -151    111       O  
ATOM   4946  CB  LEU B 484      53.389  -3.865  12.795  1.00 29.73           C  
ANISOU 4946  CB  LEU B 484     3496   3470   4329     91   -192    175       C  
ATOM   4947  CG  LEU B 484      51.987  -4.440  12.641  1.00 36.47           C  
ANISOU 4947  CG  LEU B 484     4362   4310   5184     87   -176    187       C  
ATOM   4948  CD1 LEU B 484      52.032  -5.966  12.595  1.00 40.02           C  
ANISOU 4948  CD1 LEU B 484     4798   4731   5675     97   -164    202       C  
ATOM   4949  CD2 LEU B 484      51.102  -3.951  13.790  1.00 33.28           C  
ANISOU 4949  CD2 LEU B 484     3978   3923   4745     94   -185    212       C  
ATOM   4950  N   ALA B 485      54.584  -2.533  10.134  1.00 28.69           N  
ANISOU 4950  N   ALA B 485     3353   3336   4210     51   -173     98       N  
ATOM   4951  CA  ALA B 485      54.401  -1.971   8.797  1.00 29.72           C  
ANISOU 4951  CA  ALA B 485     3490   3464   4338     31   -156     69       C  
ATOM   4952  C   ALA B 485      55.306  -2.656   7.761  1.00 25.25           C  
ANISOU 4952  C   ALA B 485     2904   2880   3809     25   -145     47       C  
ATOM   4953  O   ALA B 485      54.916  -2.866   6.607  1.00 25.64           O  
ANISOU 4953  O   ALA B 485     2955   2920   3867     12   -127     30       O  
ATOM   4954  CB  ALA B 485      54.648  -0.458   8.807  1.00 23.81           C  
ANISOU 4954  CB  ALA B 485     2753   2736   3558     22   -161     55       C  
ATOM   4955  N   LEU B 486      56.525  -2.990   8.169  1.00 30.08           N  
ANISOU 4955  N   LEU B 486     3497   3490   4443     35   -155     47       N  
ATOM   4956  CA  LEU B 486      57.420  -3.742   7.292  1.00 32.13           C  
ANISOU 4956  CA  LEU B 486     3736   3731   4742     31   -145     27       C  
ATOM   4957  C   LEU B 486      56.775  -5.088   6.966  1.00 34.71           C  
ANISOU 4957  C   LEU B 486     4056   4035   5096     33   -132     37       C  
ATOM   4958  O   LEU B 486      56.646  -5.479   5.798  1.00 29.16           O  
ANISOU 4958  O   LEU B 486     3349   3320   4412     20   -113     16       O  
ATOM   4959  CB  LEU B 486      58.779  -3.940   7.960  1.00 31.16           C  
ANISOU 4959  CB  LEU B 486     3591   3610   4638     44   -161     28       C  
ATOM   4960  CG  LEU B 486      59.667  -2.696   8.023  1.00 30.46           C  
ANISOU 4960  CG  LEU B 486     3501   3540   4533     37   -169      7       C  
ATOM   4961  CD1 LEU B 486      60.880  -2.962   8.898  1.00 31.16           C  
ANISOU 4961  CD1 LEU B 486     3567   3635   4639     55   -189     11       C  
ATOM   4962  CD2 LEU B 486      60.082  -2.258   6.612  1.00 27.81           C  
ANISOU 4962  CD2 LEU B 486     3163   3196   4207     16   -149    -28       C  
ATOM   4963  N   GLN B 487      56.347  -5.782   8.016  1.00 37.56           N  
ANISOU 4963  N   GLN B 487     4418   4393   5461     51   -140     69       N  
ATOM   4964  CA  GLN B 487      55.653  -7.059   7.895  1.00 43.66           C  
ANISOU 4964  CA  GLN B 487     5185   5142   6260     55   -126     81       C  
ATOM   4965  C   GLN B 487      54.509  -7.010   6.883  1.00 44.79           C  
ANISOU 4965  C   GLN B 487     5341   5282   6397     37   -106     65       C  
ATOM   4966  O   GLN B 487      54.329  -7.935   6.096  1.00 46.64           O  
ANISOU 4966  O   GLN B 487     5563   5496   6662     30    -88     52       O  
ATOM   4967  CB  GLN B 487      55.103  -7.470   9.260  1.00 47.86           C  
ANISOU 4967  CB  GLN B 487     5725   5676   6783     75   -136    121       C  
ATOM   4968  CG  GLN B 487      55.195  -8.945   9.566  1.00 53.85           C  
ANISOU 4968  CG  GLN B 487     6470   6408   7584     90   -128    141       C  
ATOM   4969  CD  GLN B 487      54.870  -9.255  11.013  1.00 65.81           C  
ANISOU 4969  CD  GLN B 487     7993   7927   9086    113   -139    182       C  
ATOM   4970  OE1 GLN B 487      55.764  -9.449  11.832  1.00 69.68           O  
ANISOU 4970  OE1 GLN B 487     8472   8421   9580    134   -156    200       O  
ATOM   4971  NE2 GLN B 487      53.584  -9.297  11.335  1.00 69.18           N  
ANISOU 4971  NE2 GLN B 487     8436   8352   9495    111   -131    198       N  
ATOM   4972  N   LYS B 488      53.739  -5.928   6.914  1.00 35.97           N  
ANISOU 4972  N   LYS B 488     4245   4185   5239     29   -110     63       N  
ATOM   4973  CA  LYS B 488      52.556  -5.790   6.068  1.00 31.17           C  
ANISOU 4973  CA  LYS B 488     3648   3578   4618     15    -95     50       C  
ATOM   4974  C   LYS B 488      52.893  -5.374   4.639  1.00 33.48           C  
ANISOU 4974  C   LYS B 488     3938   3873   4911     -2    -83     14       C  
ATOM   4975  O   LYS B 488      52.000  -5.096   3.831  1.00 32.88           O  
ANISOU 4975  O   LYS B 488     3871   3803   4818    -13    -72      0       O  
ATOM   4976  CB  LYS B 488      51.573  -4.794   6.690  1.00 34.78           C  
ANISOU 4976  CB  LYS B 488     4128   4055   5030     16   -104     63       C  
ATOM   4977  CG  LYS B 488      50.885  -5.297   7.948  1.00 36.37           C  
ANISOU 4977  CG  LYS B 488     4336   4254   5230     30   -110     97       C  
ATOM   4978  CD  LYS B 488      50.224  -4.141   8.695  1.00 37.92           C  
ANISOU 4978  CD  LYS B 488     4554   4473   5381     31   -123    109       C  
ATOM   4979  CE  LYS B 488      49.333  -4.625   9.826  1.00 44.26           C  
ANISOU 4979  CE  LYS B 488     5366   5273   6179     43   -125    140       C  
ATOM   4980  NZ  LYS B 488      48.036  -5.170   9.317  1.00 54.47           N  
ANISOU 4980  NZ  LYS B 488     6662   6555   7478     35   -108    136       N  
ATOM   4981  N   GLY B 489      54.183  -5.319   4.333  1.00 32.61           N  
ANISOU 4981  N   GLY B 489     3813   3758   4817     -3    -84      0       N  
ATOM   4982  CA  GLY B 489      54.611  -5.061   2.976  1.00 32.60           C  
ANISOU 4982  CA  GLY B 489     3808   3758   4822    -19    -70    -33       C  
ATOM   4983  C   GLY B 489      54.929  -3.626   2.607  1.00 31.34           C  
ANISOU 4983  C   GLY B 489     3662   3616   4628    -27    -72    -46       C  
ATOM   4984  O   GLY B 489      55.085  -3.327   1.427  1.00 29.14           O  
ANISOU 4984  O   GLY B 489     3385   3339   4348    -40    -57    -71       O  
ATOM   4985  N   SER B 490      55.039  -2.734   3.593  1.00 25.72           N  
ANISOU 4985  N   SER B 490     2962   2919   3892    -20    -88    -30       N  
ATOM   4986  CA  SER B 490      55.405  -1.356   3.272  1.00 26.79           C  
ANISOU 4986  CA  SER B 490     3110   3068   4000    -29    -86    -44       C  
ATOM   4987  C   SER B 490      56.780  -1.307   2.597  1.00 32.17           C  
ANISOU 4987  C   SER B 490     3776   3742   4705    -36    -79    -69       C  
ATOM   4988  O   SER B 490      57.758  -1.862   3.117  1.00 27.91           O  
ANISOU 4988  O   SER B 490     3217   3195   4194    -29    -88    -67       O  
ATOM   4989  CB  SER B 490      55.398  -0.459   4.510  1.00 24.18           C  
ANISOU 4989  CB  SER B 490     2791   2754   3644    -21   -104    -26       C  
ATOM   4990  OG  SER B 490      55.794   0.851   4.146  1.00 25.28           O  
ANISOU 4990  OG  SER B 490     2941   2904   3762    -30    -99    -42       O  
ATOM   4991  N   LYS B 491      56.843  -0.647   1.441  1.00 26.87           N  
ANISOU 4991  N   LYS B 491     3114   3075   4023    -50    -62    -91       N  
ATOM   4992  CA  LYS B 491      58.076  -0.529   0.663  1.00 34.54           C  
ANISOU 4992  CA  LYS B 491     4072   4037   5014    -59    -50   -117       C  
ATOM   4993  C   LYS B 491      58.643   0.898   0.699  1.00 40.37           C  
ANISOU 4993  C   LYS B 491     4822   4787   5731    -65    -47   -127       C  
ATOM   4994  O   LYS B 491      59.355   1.315  -0.220  1.00 46.68           O  
ANISOU 4994  O   LYS B 491     5620   5582   6536    -76    -30   -150       O  
ATOM   4995  CB  LYS B 491      57.831  -0.909  -0.807  1.00 37.38           C  
ANISOU 4995  CB  LYS B 491     4432   4391   5379    -71    -28   -139       C  
ATOM   4996  CG  LYS B 491      56.843  -2.052  -1.062  1.00 47.10           C  
ANISOU 4996  CG  LYS B 491     5658   5616   6620    -68    -26   -134       C  
ATOM   4997  CD  LYS B 491      57.515  -3.414  -0.998  1.00 45.62           C  
ANISOU 4997  CD  LYS B 491     5443   5408   6480    -65    -25   -138       C  
ATOM   4998  CE  LYS B 491      56.589  -4.530  -1.517  1.00 54.93           C  
ANISOU 4998  CE  LYS B 491     6617   6581   7675    -67    -15   -141       C  
ATOM   4999  NZ  LYS B 491      55.306  -4.685  -0.743  1.00 49.54           N  
ANISOU 4999  NZ  LYS B 491     5945   5903   6975    -59    -25   -117       N  
ATOM   5000  N   ASP B 492      58.326   1.653   1.743  1.00 36.17           N  
ANISOU 5000  N   ASP B 492     4301   4268   5176    -58    -61   -110       N  
ATOM   5001  CA  ASP B 492      58.669   3.075   1.776  1.00 23.67           C  
ANISOU 5001  CA  ASP B 492     2730   2693   3569    -65    -56   -119       C  
ATOM   5002  C   ASP B 492      59.516   3.336   3.014  1.00 24.81           C  
ANISOU 5002  C   ASP B 492     2861   2843   3722    -58    -74   -115       C  
ATOM   5003  O   ASP B 492      59.614   2.464   3.881  1.00 27.62           O  
ANISOU 5003  O   ASP B 492     3203   3199   4093    -45    -93   -100       O  
ATOM   5004  CB  ASP B 492      57.377   3.894   1.815  1.00 32.53           C  
ANISOU 5004  CB  ASP B 492     3879   3828   4651    -64    -53   -104       C  
ATOM   5005  CG  ASP B 492      57.598   5.367   1.531  1.00 32.92           C  
ANISOU 5005  CG  ASP B 492     3946   3884   4679    -72    -39   -115       C  
ATOM   5006  OD1 ASP B 492      58.738   5.768   1.223  1.00 39.93           O  
ANISOU 5006  OD1 ASP B 492     4824   4765   5582    -80    -29   -135       O  
ATOM   5007  OD2 ASP B 492      56.613   6.129   1.592  1.00 32.15           O  
ANISOU 5007  OD2 ASP B 492     3870   3796   4550    -71    -36   -103       O  
ATOM   5008  N   ASN B 493      60.130   4.516   3.104  1.00 22.67           N  
ANISOU 5008  N   ASN B 493     2594   2578   3441    -65    -68   -130       N  
ATOM   5009  CA  ASN B 493      60.695   4.968   4.370  1.00 23.41           C  
ANISOU 5009  CA  ASN B 493     2677   2683   3533    -58    -87   -127       C  
ATOM   5010  C   ASN B 493      59.564   5.016   5.396  1.00 21.88           C  
ANISOU 5010  C   ASN B 493     2498   2503   3312    -47   -104    -98       C  
ATOM   5011  O   ASN B 493      58.418   5.293   5.044  1.00 21.58           O  
ANISOU 5011  O   ASN B 493     2482   2467   3250    -49    -96    -87       O  
ATOM   5012  CB  ASN B 493      61.320   6.368   4.232  1.00 23.01           C  
ANISOU 5012  CB  ASN B 493     2633   2637   3474    -70    -73   -149       C  
ATOM   5013  CG  ASN B 493      62.401   6.438   3.153  1.00 27.02           C  
ANISOU 5013  CG  ASN B 493     3129   3130   4007    -83    -51   -179       C  
ATOM   5014  OD1 ASN B 493      62.565   7.466   2.488  1.00 31.56           O  
ANISOU 5014  OD1 ASN B 493     3717   3701   4573    -95    -27   -195       O  
ATOM   5015  ND2 ASN B 493      63.132   5.347   2.975  1.00 23.14           N  
ANISOU 5015  ND2 ASN B 493     2615   2629   3549    -79    -57   -186       N  
ATOM   5016  N   ILE B 494      59.885   4.762   6.659  1.00 20.11           N  
ANISOU 5016  N   ILE B 494     2261   2290   3091    -34   -128    -87       N  
ATOM   5017  CA  ILE B 494      58.893   4.813   7.726  1.00 22.41           C  
ANISOU 5017  CA  ILE B 494     2564   2595   3356    -24   -145    -60       C  
ATOM   5018  C   ILE B 494      59.351   5.707   8.881  1.00 25.53           C  
ANISOU 5018  C   ILE B 494     2954   3010   3736    -20   -159    -63       C  
ATOM   5019  O   ILE B 494      60.372   5.442   9.521  1.00 23.15           O  
ANISOU 5019  O   ILE B 494     2630   2714   3450    -13   -175    -70       O  
ATOM   5020  CB  ILE B 494      58.614   3.399   8.278  1.00 24.40           C  
ANISOU 5020  CB  ILE B 494     2806   2843   3622     -8   -160    -35       C  
ATOM   5021  CG1 ILE B 494      58.035   2.499   7.176  1.00 27.14           C  
ANISOU 5021  CG1 ILE B 494     3157   3171   3985    -12   -145    -34       C  
ATOM   5022  CG2 ILE B 494      57.702   3.466   9.495  1.00 20.58           C  
ANISOU 5022  CG2 ILE B 494     2334   2374   3112      4   -177     -7       C  
ATOM   5023  CD1 ILE B 494      58.346   1.000   7.371  1.00 27.31           C  
ANISOU 5023  CD1 ILE B 494     3159   3180   4039      0   -153    -22       C  
ATOM   5024  N   SER B 495      58.589   6.766   9.146  1.00 20.56           N  
ANISOU 5024  N   SER B 495     2345   2391   3076    -26   -155    -59       N  
ATOM   5025  CA  SER B 495      58.871   7.619  10.281  1.00 22.65           C  
ANISOU 5025  CA  SER B 495     2606   2675   3324    -23   -168    -63       C  
ATOM   5026  C   SER B 495      57.628   7.773  11.147  1.00 21.51           C  
ANISOU 5026  C   SER B 495     2480   2544   3149    -16   -178    -36       C  
ATOM   5027  O   SER B 495      56.537   8.034  10.650  1.00 21.47           O  
ANISOU 5027  O   SER B 495     2497   2533   3128    -21   -166    -26       O  
ATOM   5028  CB  SER B 495      59.415   8.970   9.825  1.00 24.24           C  
ANISOU 5028  CB  SER B 495     2810   2876   3523    -40   -148    -92       C  
ATOM   5029  OG  SER B 495      60.528   8.772   8.965  1.00 28.74           O  
ANISOU 5029  OG  SER B 495     3364   3432   4123    -47   -136   -117       O  
ATOM   5030  N   ILE B 496      57.810   7.578  12.447  1.00 15.03           N  
ANISOU 5030  N   ILE B 496     1649   1741   2319     -3   -202    -25       N  
ATOM   5031  CA  ILE B 496      56.711   7.560  13.379  1.00 15.77           C  
ANISOU 5031  CA  ILE B 496     1758   1848   2387      6   -213      2       C  
ATOM   5032  C   ILE B 496      57.145   8.236  14.653  1.00 21.80           C  
ANISOU 5032  C   ILE B 496     2512   2637   3133     11   -231     -4       C  
ATOM   5033  O   ILE B 496      58.211   7.920  15.185  1.00 20.14           O  
ANISOU 5033  O   ILE B 496     2278   2437   2935     20   -247    -12       O  
ATOM   5034  CB  ILE B 496      56.313   6.130  13.751  1.00 18.63           C  
ANISOU 5034  CB  ILE B 496     2117   2205   2757     23   -226     31       C  
ATOM   5035  CG1 ILE B 496      56.068   5.285  12.500  1.00 17.56           C  
ANISOU 5035  CG1 ILE B 496     1983   2044   2644     18   -210     32       C  
ATOM   5036  CG2 ILE B 496      55.046   6.137  14.616  1.00 19.95           C  
ANISOU 5036  CG2 ILE B 496     2302   2382   2895     30   -233     59       C  
ATOM   5037  CD1 ILE B 496      55.618   3.863  12.824  1.00 20.72           C  
ANISOU 5037  CD1 ILE B 496     2379   2435   3057     33   -218     60       C  
ATOM   5038  N   ILE B 497      56.317   9.155  15.148  1.00 17.18           N  
ANISOU 5038  N   ILE B 497     1945   2064   2520      6   -228      1       N  
ATOM   5039  CA  ILE B 497      56.490   9.687  16.495  1.00 18.36           C  
ANISOU 5039  CA  ILE B 497     2088   2241   2648     12   -246      0       C  
ATOM   5040  C   ILE B 497      55.282   9.282  17.312  1.00 18.30           C  
ANISOU 5040  C   ILE B 497     2097   2242   2616     23   -257     33       C  
ATOM   5041  O   ILE B 497      54.148   9.595  16.937  1.00 19.63           O  
ANISOU 5041  O   ILE B 497     2287   2400   2771     16   -243     43       O  
ATOM   5042  CB  ILE B 497      56.604  11.241  16.507  1.00 13.35           C  
ANISOU 5042  CB  ILE B 497     1457   1613   2001     -5   -233    -28       C  
ATOM   5043  CG1 ILE B 497      57.699  11.709  15.544  1.00 19.86           C  
ANISOU 5043  CG1 ILE B 497     2269   2425   2852    -18   -215    -61       C  
ATOM   5044  CG2 ILE B 497      56.857  11.750  17.935  1.00 16.73           C  
ANISOU 5044  CG2 ILE B 497     1875   2073   2408      1   -252    -33       C  
ATOM   5045  CD1 ILE B 497      57.886  13.199  15.491  1.00 19.68           C  
ANISOU 5045  CD1 ILE B 497     2250   2405   2823    -35   -197    -89       C  
ATOM   5046  N   VAL B 498      55.505   8.577  18.417  1.00 12.46           N  
ANISOU 5046  N   VAL B 498     1346   1519   1869     42   -280     50       N  
ATOM   5047  CA  VAL B 498      54.405   8.228  19.311  1.00 13.71           C  
ANISOU 5047  CA  VAL B 498     1519   1686   2002     52   -289     82       C  
ATOM   5048  C   VAL B 498      54.486   9.101  20.565  1.00 18.58           C  
ANISOU 5048  C   VAL B 498     2134   2335   2590     55   -303     76       C  
ATOM   5049  O   VAL B 498      55.524   9.179  21.201  1.00 21.62           O  
ANISOU 5049  O   VAL B 498     2497   2741   2975     62   -320     62       O  
ATOM   5050  CB  VAL B 498      54.419   6.722  19.698  1.00 15.55           C  
ANISOU 5050  CB  VAL B 498     1747   1915   2247     74   -302    113       C  
ATOM   5051  CG1 VAL B 498      53.359   6.415  20.746  1.00 18.51           C  
ANISOU 5051  CG1 VAL B 498     2138   2301   2595     86   -309    145       C  
ATOM   5052  CG2 VAL B 498      54.205   5.849  18.477  1.00 17.18           C  
ANISOU 5052  CG2 VAL B 498     1956   2089   2482     70   -286    118       C  
ATOM   5053  N   ILE B 499      53.394   9.769  20.911  1.00 14.13           N  
ANISOU 5053  N   ILE B 499     1591   1777   2002     47   -296     83       N  
ATOM   5054  CA  ILE B 499      53.366  10.645  22.085  1.00 15.96           C  
ANISOU 5054  CA  ILE B 499     1821   2038   2204     47   -306     75       C  
ATOM   5055  C   ILE B 499      52.310  10.183  23.084  1.00 22.71           C  
ANISOU 5055  C   ILE B 499     2691   2904   3033     60   -316    109       C  
ATOM   5056  O   ILE B 499      51.124  10.085  22.740  1.00 21.81           O  
ANISOU 5056  O   ILE B 499     2599   2774   2915     55   -302    126       O  
ATOM   5057  CB  ILE B 499      53.038  12.098  21.678  1.00 14.10           C  
ANISOU 5057  CB  ILE B 499     1596   1800   1962     25   -286     49       C  
ATOM   5058  CG1 ILE B 499      54.103  12.640  20.719  1.00 18.92           C  
ANISOU 5058  CG1 ILE B 499     2192   2399   2599     12   -274     15       C  
ATOM   5059  CG2 ILE B 499      52.923  12.989  22.922  1.00 16.66           C  
ANISOU 5059  CG2 ILE B 499     1918   2155   2257     24   -296     40       C  
ATOM   5060  CD1 ILE B 499      53.600  13.783  19.821  1.00 21.33           C  
ANISOU 5060  CD1 ILE B 499     2513   2686   2905     -8   -245     -1       C  
ATOM   5061  N   ASP B 500      52.732   9.892  24.315  1.00 21.87           N  
ANISOU 5061  N   ASP B 500     2574   2828   2909     77   -338    118       N  
ATOM   5062  CA  ASP B 500      51.809   9.456  25.373  1.00 15.68           C  
ANISOU 5062  CA  ASP B 500     1804   2056   2098     90   -347    150       C  
ATOM   5063  C   ASP B 500      51.148  10.677  26.029  1.00 20.52           C  
ANISOU 5063  C   ASP B 500     2427   2688   2680     78   -343    138       C  
ATOM   5064  O   ASP B 500      51.833  11.550  26.555  1.00 20.04           O  
ANISOU 5064  O   ASP B 500     2352   2652   2608     73   -351    111       O  
ATOM   5065  CB  ASP B 500      52.546   8.612  26.429  1.00 23.25           C  
ANISOU 5065  CB  ASP B 500     2747   3040   3047    117   -373    168       C  
ATOM   5066  CG  ASP B 500      51.591   7.941  27.423  1.00 29.33           C  
ANISOU 5066  CG  ASP B 500     3534   3819   3792    133   -378    208       C  
ATOM   5067  OD1 ASP B 500      50.392   8.278  27.402  1.00 24.87           O  
ANISOU 5067  OD1 ASP B 500     2991   3244   3216    122   -363    217       O  
ATOM   5068  OD2 ASP B 500      52.031   7.082  28.231  1.00 28.24           O  
ANISOU 5068  OD2 ASP B 500     3388   3697   3647    158   -396    231       O  
ATOM   5069  N   LEU B 501      49.816  10.719  26.011  1.00 24.32           N  
ANISOU 5069  N   LEU B 501     2932   3157   3150     72   -330    157       N  
ATOM   5070  CA  LEU B 501      49.068  11.874  26.512  1.00 24.16           C  
ANISOU 5070  CA  LEU B 501     2924   3150   3106     59   -322    146       C  
ATOM   5071  C   LEU B 501      48.464  11.680  27.912  1.00 29.48           C  
ANISOU 5071  C   LEU B 501     3606   3850   3746     71   -335    169       C  
ATOM   5072  O   LEU B 501      47.927  12.629  28.490  1.00 26.67           O  
ANISOU 5072  O   LEU B 501     3257   3508   3367     61   -331    158       O  
ATOM   5073  CB  LEU B 501      47.972  12.271  25.517  1.00 20.26           C  
ANISOU 5073  CB  LEU B 501     2451   2627   2621     42   -297    147       C  
ATOM   5074  CG  LEU B 501      48.467  12.812  24.170  1.00 21.49           C  
ANISOU 5074  CG  LEU B 501     2602   2761   2802     27   -281    121       C  
ATOM   5075  CD1 LEU B 501      47.310  13.008  23.202  1.00 12.67           C  
ANISOU 5075  CD1 LEU B 501     1506   1617   1691     17   -260    128       C  
ATOM   5076  CD2 LEU B 501      49.244  14.123  24.380  1.00 16.43           C  
ANISOU 5076  CD2 LEU B 501     1949   2137   2157     15   -279     84       C  
ATOM   5077  N   LYS B 502      48.536  10.456  28.436  1.00 25.34           N  
ANISOU 5077  N   LYS B 502     3081   3329   3219     93   -348    200       N  
ATOM   5078  CA  LYS B 502      48.155  10.171  29.825  1.00 29.80           C  
ANISOU 5078  CA  LYS B 502     3651   3921   3750    109   -361    224       C  
ATOM   5079  C   LYS B 502      49.284  10.552  30.792  1.00 30.64           C  
ANISOU 5079  C   LYS B 502     3736   4069   3836    120   -385    206       C  
ATOM   5080  O   LYS B 502      50.443  10.215  30.565  1.00 33.10           O  
ANISOU 5080  O   LYS B 502     4027   4386   4164    129   -398    195       O  
ATOM   5081  CB  LYS B 502      47.839   8.681  29.992  1.00 29.93           C  
ANISOU 5081  CB  LYS B 502     3675   3923   3773    131   -363    266       C  
ATOM   5082  CG  LYS B 502      46.624   8.220  29.235  1.00 30.48           C  
ANISOU 5082  CG  LYS B 502     3765   3956   3859    122   -340    284       C  
ATOM   5083  CD  LYS B 502      45.343   8.529  29.998  1.00 36.85           C  
ANISOU 5083  CD  LYS B 502     4593   4770   4639    118   -332    299       C  
ATOM   5084  CE  LYS B 502      44.123   8.071  29.199  1.00 34.36           C  
ANISOU 5084  CE  LYS B 502     4296   4419   4342    109   -309    313       C  
ATOM   5085  NZ  LYS B 502      42.873   8.076  30.000  1.00 36.57           N  
ANISOU 5085  NZ  LYS B 502     4595   4702   4599    109   -300    333       N  
ATOM   5086  N   ALA B 503      48.951  11.238  31.877  1.00 49.98           N  
ANISOU 5086  N   ALA B 503     6189   6550   6251    119   -391    201       N  
ATOM   5087  CA  ALA B 503      49.972  11.615  32.856  1.00 51.76           C  
ANISOU 5087  CA  ALA B 503     6392   6820   6455    129   -415    181       C  
ATOM   5088  C   ALA B 503      50.477  10.395  33.635  1.00 52.29           C  
ANISOU 5088  C   ALA B 503     6453   6907   6510    162   -438    214       C  
ATOM   5089  O   ALA B 503      51.679  10.262  33.879  1.00 58.26           O  
ANISOU 5089  O   ALA B 503     7183   7685   7266    176   -458    199       O  
ATOM   5090  CB  ALA B 503      49.452  12.695  33.802  1.00 47.52           C  
ANISOU 5090  CB  ALA B 503     5860   6312   5883    118   -415    164       C  
ATOM   5091  N   GLN B 504      49.560   9.502  34.005  1.00 47.18           N  
ANISOU 5091  N   GLN B 504     5827   6248   5852    176   -432    257       N  
ATOM   5092  CA  GLN B 504      49.937   8.251  34.669  1.00 48.51           C  
ANISOU 5092  CA  GLN B 504     5992   6427   6012    209   -449    295       C  
ATOM   5093  C   GLN B 504      49.268   7.045  34.026  1.00 45.09           C  
ANISOU 5093  C   GLN B 504     5577   5951   5606    216   -431    334       C  
ATOM   5094  O   GLN B 504      48.155   7.133  33.513  1.00 49.49           O  
ANISOU 5094  O   GLN B 504     6154   6479   6172    198   -409    340       O  
ATOM   5095  CB  GLN B 504      49.550   8.276  36.149  1.00 58.60           C  
ANISOU 5095  CB  GLN B 504     7279   7745   7242    225   -461    315       C  
ATOM   5096  CG  GLN B 504      49.609   9.634  36.823  1.00 51.64           C  
ANISOU 5096  CG  GLN B 504     6390   6902   6330    210   -468    277       C  
ATOM   5097  CD  GLN B 504      49.437   9.529  38.331  1.00 75.71           C  
ANISOU 5097  CD  GLN B 504     9442   9995   9329    231   -484    296       C  
ATOM   5098  OE1 GLN B 504      49.352   8.428  38.882  1.00 85.18           O  
ANISOU 5098  OE1 GLN B 504    10651  11198  10517    259   -491    339       O  
ATOM   5099  NE2 GLN B 504      49.387  10.673  39.006  1.00 67.13           N  
ANISOU 5099  NE2 GLN B 504     8350   8943   8214    218   -489    264       N  
ATOM   5100  N   ARG B 505      49.945   5.907  34.069  1.00 47.50           N  
ANISOU 5100  N   ARG B 505     5873   6252   5924    241   -442    358       N  
ATOM   5101  CA  ARG B 505      49.320   4.653  33.681  1.00 54.34           C  
ANISOU 5101  CA  ARG B 505     6754   7080   6813    252   -426    398       C  
ATOM   5102  C   ARG B 505      49.599   3.578  34.726  1.00 62.19           C  
ANISOU 5102  C   ARG B 505     7749   8092   7789    289   -439    441       C  
ATOM   5103  O   ARG B 505      50.576   2.841  34.627  1.00 73.41           O  
ANISOU 5103  O   ARG B 505     9153   9513   9226    310   -452    450       O  
ATOM   5104  CB  ARG B 505      49.808   4.209  32.306  1.00 45.45           C  
ANISOU 5104  CB  ARG B 505     5617   5916   5734    243   -416    386       C  
ATOM   5105  CG  ARG B 505      49.440   5.165  31.177  1.00 38.04           C  
ANISOU 5105  CG  ARG B 505     4682   4958   4815    209   -399    350       C  
ATOM   5106  CD  ARG B 505      49.949   4.624  29.867  1.00 27.17           C  
ANISOU 5106  CD  ARG B 505     3294   3546   3482    203   -391    341       C  
ATOM   5107  NE  ARG B 505      49.596   5.443  28.713  1.00 29.51           N  
ANISOU 5107  NE  ARG B 505     3594   3821   3796    173   -373    310       N  
ATOM   5108  CZ  ARG B 505      48.411   5.426  28.118  1.00 28.57           C  
ANISOU 5108  CZ  ARG B 505     3494   3676   3685    158   -351    316       C  
ATOM   5109  NH1 ARG B 505      47.441   4.647  28.584  1.00 29.04           N  
ANISOU 5109  NH1 ARG B 505     3571   3725   3739    168   -342    351       N  
ATOM   5110  NH2 ARG B 505      48.195   6.195  27.060  1.00 21.94           N  
ANISOU 5110  NH2 ARG B 505     2657   2820   2859    134   -337    288       N  
ATOM   5111  N   LYS B 506      48.739   3.504  35.734  1.00 69.39           N  
ANISOU 5111  N   LYS B 506     8681   9017   8667    297   -435    468       N  
ATOM   5112  CA  LYS B 506      48.908   2.526  36.802  1.00 86.17           C  
ANISOU 5112  CA  LYS B 506    10810  11160  10770    334   -445    512       C  
ATOM   5113  C   LYS B 506      47.770   1.508  36.824  1.00 90.67           C  
ANISOU 5113  C   LYS B 506    11407  11693  11351    340   -418    557       C  
ATOM   5114  O   LYS B 506      47.148   1.228  35.798  1.00100.00           O  
ANISOU 5114  O   LYS B 506    12595  12830  12569    321   -394    554       O  
ATOM   5115  CB  LYS B 506      49.001   3.228  38.153  1.00 91.93           C  
ANISOU 5115  CB  LYS B 506    11540  11944  11444    344   -465    509       C  
ATOM   5116  CG  LYS B 506      49.747   2.426  39.201  1.00 98.57           C  
ANISOU 5116  CG  LYS B 506    12374  12819  12260    387   -488    542       C  
ATOM   5117  CD  LYS B 506      51.079   3.076  39.532  1.00 96.56           C  
ANISOU 5117  CD  LYS B 506    12088  12612  11988    396   -521    507       C  
ATOM   5118  CE  LYS B 506      51.860   3.419  38.271  1.00 94.91           C  
ANISOU 5118  CE  LYS B 506    11857  12381  11824    375   -522    466       C  
ATOM   5119  NZ  LYS B 506      53.059   4.249  38.573  1.00 90.15           N  
ANISOU 5119  NZ  LYS B 506    11223  11825  11205    376   -551    423       N  
TER    5120      LYS B 506                                                      
ATOM   5121  N   VAL C   9      49.002  23.127  45.451  1.00 99.30           N  
ANISOU 5121  N   VAL C   9    12306  13334  12089     25   -462   -176       N  
ATOM   5122  CA  VAL C   9      49.655  22.804  46.713  1.00100.43           C  
ANISOU 5122  CA  VAL C   9    12430  13545  12185     49   -496   -183       C  
ATOM   5123  C   VAL C   9      48.702  22.078  47.654  1.00 99.75           C  
ANISOU 5123  C   VAL C   9    12371  13478  12051     69   -503   -134       C  
ATOM   5124  O   VAL C   9      48.201  21.000  47.339  1.00 99.26           O  
ANISOU 5124  O   VAL C   9    12336  13388  11992     87   -503    -77       O  
ATOM   5125  CB  VAL C   9      50.176  24.070  47.411  1.00 91.68           C  
ANISOU 5125  CB  VAL C   9    11289  12482  11065     29   -496   -252       C  
ATOM   5126  CG1 VAL C   9      51.589  23.850  47.926  1.00 93.30           C  
ANISOU 5126  CG1 VAL C   9    11456  12742  11254     49   -531   -282       C  
ATOM   5127  CG2 VAL C   9      50.125  25.252  46.461  1.00 91.72           C  
ANISOU 5127  CG2 VAL C   9    11287  12443  11119     -8   -462   -295       C  
ATOM   5128  N   GLU C  10      48.454  22.680  48.811  1.00108.79           N  
ANISOU 5128  N   GLU C  10    13510  14671  13156     65   -508   -157       N  
ATOM   5129  CA  GLU C  10      47.569  22.092  49.807  1.00108.23           C  
ANISOU 5129  CA  GLU C  10    13464  14623  13037     83   -513   -115       C  
ATOM   5130  C   GLU C  10      46.698  20.990  49.214  1.00106.97           C  
ANISOU 5130  C   GLU C  10    13342  14412  12891     96   -501    -47       C  
ATOM   5131  O   GLU C  10      46.920  19.809  49.468  1.00107.07           O  
ANISOU 5131  O   GLU C  10    13363  14434  12884    128   -520     -2       O  
ATOM   5132  CB  GLU C  10      46.685  23.168  50.434  1.00 97.93           C  
ANISOU 5132  CB  GLU C  10    12164  13329  11715     56   -492   -143       C  
ATOM   5133  CG  GLU C  10      46.889  23.349  51.927  1.00 98.52           C  
ANISOU 5133  CG  GLU C  10    12225  13479  11730     69   -513   -161       C  
ATOM   5134  CD  GLU C  10      45.580  23.413  52.685  1.00 97.65           C  
ANISOU 5134  CD  GLU C  10    12145  13372  11587     63   -497   -137       C  
ATOM   5135  OE1 GLU C  10      45.160  24.526  53.063  1.00 97.84           O  
ANISOU 5135  OE1 GLU C  10    12161  13406  11607     36   -479   -179       O  
ATOM   5136  OE2 GLU C  10      44.970  22.346  52.904  1.00 96.91           O  
ANISOU 5136  OE2 GLU C  10    12080  13268  11472     87   -500    -77       O  
ATOM   5137  N   SER C  11      45.705  21.386  48.426  1.00106.77           N  
ANISOU 5137  N   SER C  11    13338  14331  12898     70   -469    -41       N  
ATOM   5138  CA  SER C  11      44.739  20.443  47.873  1.00116.25           C  
ANISOU 5138  CA  SER C  11    14573  15483  14112     78   -455     17       C  
ATOM   5139  C   SER C  11      45.363  19.454  46.894  1.00113.02           C  
ANISOU 5139  C   SER C  11    14164  15043  13736     95   -463     44       C  
ATOM   5140  O   SER C  11      44.816  18.377  46.659  1.00115.29           O  
ANISOU 5140  O   SER C  11    14476  15302  14027    112   -460     96       O  
ATOM   5141  CB  SER C  11      43.587  21.190  47.197  1.00 75.68           C  
ANISOU 5141  CB  SER C  11     9455  10296   9004     46   -419     10       C  
ATOM   5142  OG  SER C  11      42.699  21.731  48.159  1.00 75.37           O  
ANISOU 5142  OG  SER C  11     9426  10279   8932     36   -409      4       O  
ATOM   5143  N   GLU C  12      46.505  19.822  46.326  1.00151.14           N  
ANISOU 5143  N   GLU C  12    18964  19874  18589     90   -473      7       N  
ATOM   5144  CA  GLU C  12      47.186  18.957  45.371  1.00147.63           C  
ANISOU 5144  CA  GLU C  12    18515  19400  18178    105   -481     28       C  
ATOM   5145  C   GLU C  12      47.968  17.865  46.085  1.00145.48           C  
ANISOU 5145  C   GLU C  12    18234  19167  17875    143   -514     55       C  
ATOM   5146  O   GLU C  12      47.791  16.679  45.813  1.00147.01           O  
ANISOU 5146  O   GLU C  12    18445  19337  18075    165   -516    106       O  
ATOM   5147  CB  GLU C  12      48.115  19.773  44.474  1.00100.73           C  
ANISOU 5147  CB  GLU C  12    12549  13447  12278     84   -477    -23       C  
ATOM   5148  CG  GLU C  12      47.514  20.126  43.125  1.00 99.87           C  
ANISOU 5148  CG  GLU C  12    12455  13274  12217     59   -445    -22       C  
ATOM   5149  CD  GLU C  12      48.084  21.405  42.549  1.00100.62           C  
ANISOU 5149  CD  GLU C  12    12528  13362  12342     31   -431    -81       C  
ATOM   5150  OE1 GLU C  12      48.822  22.105  43.272  1.00101.81           O  
ANISOU 5150  OE1 GLU C  12    12652  13557  12476     27   -443   -125       O  
ATOM   5151  OE2 GLU C  12      47.794  21.707  41.373  1.00100.10           O  
ANISOU 5151  OE2 GLU C  12    12472  13246  12317     13   -407    -83       O  
ATOM   5152  N   TYR C  13      48.835  18.271  47.005  1.00 54.56           N  
ANISOU 5152  N   TYR C  13     6691   7712   6328    152   -538     22       N  
ATOM   5153  CA  TYR C  13      49.606  17.325  47.792  1.00 53.56           C  
ANISOU 5153  CA  TYR C  13     6554   7631   6167    192   -571     46       C  
ATOM   5154  C   TYR C  13      48.679  16.293  48.419  1.00 55.12           C  
ANISOU 5154  C   TYR C  13     6785   7826   6333    216   -570    110       C  
ATOM   5155  O   TYR C  13      49.007  15.112  48.495  1.00 57.36           O  
ANISOU 5155  O   TYR C  13     7073   8110   6610    249   -584    154       O  
ATOM   5156  CB  TYR C  13      50.377  18.055  48.889  1.00 54.07           C  
ANISOU 5156  CB  TYR C  13     6586   7767   6192    196   -595     -2       C  
ATOM   5157  CG  TYR C  13      51.428  19.013  48.379  1.00 59.11           C  
ANISOU 5157  CG  TYR C  13     7187   8413   6861    175   -599    -68       C  
ATOM   5158  CD1 TYR C  13      52.124  18.756  47.206  1.00 61.29           C  
ANISOU 5158  CD1 TYR C  13     7452   8650   7186    172   -596    -73       C  
ATOM   5159  CD2 TYR C  13      51.726  20.175  49.075  1.00 53.91           C  
ANISOU 5159  CD2 TYR C  13     6502   7799   6181    157   -602   -128       C  
ATOM   5160  CE1 TYR C  13      53.087  19.631  46.742  1.00 61.68           C  
ANISOU 5160  CE1 TYR C  13     7468   8705   7265    152   -596   -134       C  
ATOM   5161  CE2 TYR C  13      52.684  21.052  48.621  1.00 60.38           C  
ANISOU 5161  CE2 TYR C  13     7286   8623   7031    137   -602   -190       C  
ATOM   5162  CZ  TYR C  13      53.363  20.778  47.456  1.00 61.06           C  
ANISOU 5162  CZ  TYR C  13     7364   8670   7167    134   -598   -192       C  
ATOM   5163  OH  TYR C  13      54.318  21.656  47.007  1.00 64.49           O  
ANISOU 5163  OH  TYR C  13     7763   9107   7633    114   -595   -255       O  
ATOM   5164  N   ILE C  14      47.520  16.752  48.873  1.00 52.71           N  
ANISOU 5164  N   ILE C  14     6502   7517   6009    200   -549    115       N  
ATOM   5165  CA  ILE C  14      46.554  15.885  49.532  1.00 53.41           C  
ANISOU 5165  CA  ILE C  14     6623   7603   6067    219   -543    172       C  
ATOM   5166  C   ILE C  14      45.937  14.892  48.557  1.00 54.88           C  
ANISOU 5166  C   ILE C  14     6836   7725   6292    223   -524    221       C  
ATOM   5167  O   ILE C  14      45.747  13.724  48.885  1.00 53.22           O  
ANISOU 5167  O   ILE C  14     6643   7511   6067    252   -528    274       O  
ATOM   5168  CB  ILE C  14      45.432  16.702  50.194  1.00 42.79           C  
ANISOU 5168  CB  ILE C  14     5294   6267   4697    197   -523    160       C  
ATOM   5169  CG1 ILE C  14      45.800  17.027  51.642  1.00 45.16           C  
ANISOU 5169  CG1 ILE C  14     5580   6642   4936    212   -546    143       C  
ATOM   5170  CG2 ILE C  14      44.118  15.948  50.128  1.00 54.09           C  
ANISOU 5170  CG2 ILE C  14     6764   7657   6130    200   -499    215       C  
ATOM   5171  CD1 ILE C  14      45.571  18.466  52.022  1.00 44.88           C  
ANISOU 5171  CD1 ILE C  14     5531   6630   4891    179   -536     84       C  
ATOM   5172  N   LYS C  15      45.629  15.363  47.356  1.00106.58           N  
ANISOU 5172  N   LYS C  15    13386  14222  12889    194   -502    202       N  
ATOM   5173  CA  LYS C  15      45.016  14.520  46.339  1.00106.98           C  
ANISOU 5173  CA  LYS C  15    13458  14210  12978    193   -482    241       C  
ATOM   5174  C   LYS C  15      45.980  13.451  45.844  1.00109.27           C  
ANISOU 5174  C   LYS C  15    13739  14491  13288    220   -499    264       C  
ATOM   5175  O   LYS C  15      45.575  12.495  45.189  1.00122.92           O  
ANISOU 5175  O   LYS C  15    15484  16176  15043    227   -487    303       O  
ATOM   5176  CB  LYS C  15      44.539  15.368  45.159  1.00 73.31           C  
ANISOU 5176  CB  LYS C  15     9197   9899   8759    157   -457    212       C  
ATOM   5177  CG  LYS C  15      43.047  15.659  45.156  1.00 72.12           C  
ANISOU 5177  CG  LYS C  15     9074   9721   8609    137   -428    224       C  
ATOM   5178  CD  LYS C  15      42.656  16.492  43.944  1.00 71.36           C  
ANISOU 5178  CD  LYS C  15     8978   9579   8556    105   -405    196       C  
ATOM   5179  CE  LYS C  15      41.597  17.526  44.296  1.00 70.52           C  
ANISOU 5179  CE  LYS C  15     8882   9472   8439     80   -384    177       C  
ATOM   5180  NZ  LYS C  15      41.554  18.642  43.306  1.00 70.10           N  
ANISOU 5180  NZ  LYS C  15     8822   9391   8422     50   -367    137       N  
ATOM   5181  N   LYS C  16      47.259  13.616  46.153  1.00 94.39           N  
ANISOU 5181  N   LYS C  16    11824  12648  11393    233   -527    238       N  
ATOM   5182  CA  LYS C  16      48.276  12.705  45.644  1.00 94.90           C  
ANISOU 5182  CA  LYS C  16    11873  12705  11478    257   -544    253       C  
ATOM   5183  C   LYS C  16      48.842  11.767  46.706  1.00 95.14           C  
ANISOU 5183  C   LYS C  16    11900  12780  11468    300   -572    288       C  
ATOM   5184  O   LYS C  16      49.209  10.634  46.406  1.00105.52           O  
ANISOU 5184  O   LYS C  16    13217  14077  12798    326   -578    325       O  
ATOM   5185  CB  LYS C  16      49.402  13.490  44.965  1.00 62.20           C  
ANISOU 5185  CB  LYS C  16     7698   8569   7365    241   -554    198       C  
ATOM   5186  CG  LYS C  16      50.517  13.930  45.895  1.00 63.44           C  
ANISOU 5186  CG  LYS C  16     7823   8793   7489    255   -586    163       C  
ATOM   5187  CD  LYS C  16      51.864  13.884  45.188  1.00 64.53           C  
ANISOU 5187  CD  LYS C  16     7929   8931   7659    259   -602    134       C  
ATOM   5188  CE  LYS C  16      52.950  14.566  46.005  1.00 65.78           C  
ANISOU 5188  CE  LYS C  16     8050   9154   7789    265   -631     85       C  
ATOM   5189  NZ  LYS C  16      53.900  15.324  45.143  1.00 66.37           N  
ANISOU 5189  NZ  LYS C  16     8094   9219   7905    243   -629     29       N  
ATOM   5190  N   HIS C  17      48.916  12.237  47.945  1.00 56.53           N  
ANISOU 5190  N   HIS C  17     7004   7949   6526    309   -588    275       N  
ATOM   5191  CA  HIS C  17      49.522  11.451  49.011  1.00 53.94           C  
ANISOU 5191  CA  HIS C  17     6670   7671   6154    353   -616    304       C  
ATOM   5192  C   HIS C  17      48.519  10.970  50.052  1.00 49.96           C  
ANISOU 5192  C   HIS C  17     6198   7181   5605    370   -607    351       C  
ATOM   5193  O   HIS C  17      48.752   9.973  50.726  1.00 51.19           O  
ANISOU 5193  O   HIS C  17     6360   7358   5731    409   -621    396       O  
ATOM   5194  CB  HIS C  17      50.617  12.260  49.707  1.00 55.50           C  
ANISOU 5194  CB  HIS C  17     6830   7937   6321    357   -647    252       C  
ATOM   5195  CG  HIS C  17      51.854  12.440  48.886  1.00 62.79           C  
ANISOU 5195  CG  HIS C  17     7719   8856   7282    353   -662    214       C  
ATOM   5196  ND1 HIS C  17      52.530  11.383  48.317  1.00 55.35           N  
ANISOU 5196  ND1 HIS C  17     6771   7892   6366    379   -673    243       N  
ATOM   5197  CD2 HIS C  17      52.542  13.554  48.545  1.00 56.46           C  
ANISOU 5197  CD2 HIS C  17     6886   8067   6498    327   -667    148       C  
ATOM   5198  CE1 HIS C  17      53.579  11.839  47.657  1.00 65.29           C  
ANISOU 5198  CE1 HIS C  17     7997   9152   7656    368   -684    197       C  
ATOM   5199  NE2 HIS C  17      53.609  13.153  47.780  1.00 67.69           N  
ANISOU 5199  NE2 HIS C  17     8286   9477   7957    336   -680    138       N  
ATOM   5200  N   HIS C  18      47.410  11.685  50.193  1.00 42.47           N  
ANISOU 5200  N   HIS C  18     5267   6220   4649    340   -583    340       N  
ATOM   5201  CA  HIS C  18      46.468  11.398  51.266  1.00 38.23           C  
ANISOU 5201  CA  HIS C  18     4758   5702   4066    353   -574    377       C  
ATOM   5202  C   HIS C  18      45.063  11.070  50.781  1.00 43.08           C  
ANISOU 5202  C   HIS C  18     5408   6256   4705    335   -536    410       C  
ATOM   5203  O   HIS C  18      44.081  11.388  51.445  1.00 42.36           O  
ANISOU 5203  O   HIS C  18     5336   6172   4586    325   -520    416       O  
ATOM   5204  CB  HIS C  18      46.435  12.561  52.255  1.00 31.30           C  
ANISOU 5204  CB  HIS C  18     3868   4882   3143    339   -583    332       C  
ATOM   5205  CG  HIS C  18      47.790  12.981  52.728  1.00 38.34           C  
ANISOU 5205  CG  HIS C  18     4720   5835   4010    354   -619    292       C  
ATOM   5206  ND1 HIS C  18      48.341  12.527  53.906  1.00 34.26           N  
ANISOU 5206  ND1 HIS C  18     4197   5383   3437    393   -648    309       N  
ATOM   5207  CD2 HIS C  18      48.714  13.799  52.172  1.00 35.25           C  
ANISOU 5207  CD2 HIS C  18     4295   5453   3646    335   -632    233       C  
ATOM   5208  CE1 HIS C  18      49.542  13.054  54.059  1.00 35.78           C  
ANISOU 5208  CE1 HIS C  18     4351   5623   3623    398   -678    261       C  
ATOM   5209  NE2 HIS C  18      49.792  13.830  53.021  1.00 36.64           N  
ANISOU 5209  NE2 HIS C  18     4441   5697   3781    362   -667    214       N  
ATOM   5210  N   ARG C  19      44.972  10.421  49.627  1.00138.89           N  
ANISOU 5210  N   ARG C  19    17549  18331  16892    331   -522    429       N  
ATOM   5211  CA  ARG C  19      43.679  10.016  49.093  1.00137.67           C  
ANISOU 5211  CA  ARG C  19    17425  18118  16764    315   -487    459       C  
ATOM   5212  C   ARG C  19      43.458   8.523  49.295  1.00138.60           C  
ANISOU 5212  C   ARG C  19    17564  18216  16881    349   -480    525       C  
ATOM   5213  O   ARG C  19      43.914   7.703  48.501  1.00139.41           O  
ANISOU 5213  O   ARG C  19    17663  18286  17021    361   -480    543       O  
ATOM   5214  CB  ARG C  19      43.568  10.374  47.612  1.00 92.18           C  
ANISOU 5214  CB  ARG C  19    11659  12304  11063    284   -471    433       C  
ATOM   5215  CG  ARG C  19      42.743  11.618  47.340  1.00 91.26           C  
ANISOU 5215  CG  ARG C  19    11546  12175  10955    244   -452    393       C  
ATOM   5216  CD  ARG C  19      41.275  11.278  47.156  1.00 90.71           C  
ANISOU 5216  CD  ARG C  19    11507  12061  10897    232   -419    423       C  
ATOM   5217  NE  ARG C  19      40.445  12.472  47.016  1.00 89.91           N  
ANISOU 5217  NE  ARG C  19    11410  11952  10799    197   -401    388       N  
ATOM   5218  CZ  ARG C  19      40.707  13.639  47.596  1.00 89.82           C  
ANISOU 5218  CZ  ARG C  19    11384  11982  10763    183   -411    345       C  
ATOM   5219  NH1 ARG C  19      41.781  13.777  48.360  1.00 90.48           N  
ANISOU 5219  NH1 ARG C  19    11446  12119  10814    201   -439    330       N  
ATOM   5220  NH2 ARG C  19      39.893  14.669  47.412  1.00 89.16           N  
ANISOU 5220  NH2 ARG C  19    11305  11885  10688    151   -391    316       N  
ATOM   5221  N   HIS C  20      42.759   8.180  50.370  1.00115.56           N  
ANISOU 5221  N   HIS C  20    14669  15317  13920    365   -471    559       N  
ATOM   5222  CA  HIS C  20      42.454   6.788  50.679  1.00116.59           C  
ANISOU 5222  CA  HIS C  20    14824  15428  14048    397   -460    624       C  
ATOM   5223  C   HIS C  20      40.964   6.507  50.520  1.00115.55           C  
ANISOU 5223  C   HIS C  20    14723  15247  13932    379   -420    649       C  
ATOM   5224  O   HIS C  20      40.126   7.337  50.871  1.00114.21           O  
ANISOU 5224  O   HIS C  20    14563  15086  13746    354   -407    628       O  
ATOM   5225  CB  HIS C  20      42.907   6.444  52.099  1.00107.81           C  
ANISOU 5225  CB  HIS C  20    13714  14377  12872    437   -481    651       C  
ATOM   5226  CG  HIS C  20      43.955   7.365  52.640  1.00108.11           C  
ANISOU 5226  CG  HIS C  20    13720  14482  12875    440   -517    605       C  
ATOM   5227  ND1 HIS C  20      43.650   8.484  53.385  1.00107.79           N  
ANISOU 5227  ND1 HIS C  20    13676  14484  12795    421   -521    568       N  
ATOM   5228  CD2 HIS C  20      45.305   7.334  52.545  1.00108.83           C  
ANISOU 5228  CD2 HIS C  20    13780  14604  12965    459   -551    587       C  
ATOM   5229  CE1 HIS C  20      44.767   9.102  53.724  1.00108.34           C  
ANISOU 5229  CE1 HIS C  20    13714  14609  12843    428   -555    527       C  
ATOM   5230  NE2 HIS C  20      45.786   8.425  53.228  1.00108.96           N  
ANISOU 5230  NE2 HIS C  20    13776  14683  12944    452   -574    538       N  
ATOM   5231  N   GLU C  21      40.642   5.329  49.998  1.00181.24           N  
ANISOU 5231  N   GLU C  21    23059  23518  22286    392   -400    692       N  
ATOM   5232  CA  GLU C  21      39.254   4.922  49.827  1.00180.56           C  
ANISOU 5232  CA  GLU C  21    23001  23384  22219    377   -361    717       C  
ATOM   5233  C   GLU C  21      38.779   4.141  51.045  1.00181.51           C  
ANISOU 5233  C   GLU C  21    23147  23520  22298    406   -348    770       C  
ATOM   5234  O   GLU C  21      39.281   3.057  51.330  1.00183.28           O  
ANISOU 5234  O   GLU C  21    23376  23744  22517    443   -352    815       O  
ATOM   5235  CB  GLU C  21      39.098   4.075  48.564  1.00121.53           C  
ANISOU 5235  CB  GLU C  21    15527  15844  14806    371   -342    732       C  
ATOM   5236  CG  GLU C  21      38.469   4.812  47.396  1.00120.48           C  
ANISOU 5236  CG  GLU C  21    15389  15672  14717    329   -327    691       C  
ATOM   5237  CD  GLU C  21      39.175   4.531  46.086  1.00120.82           C  
ANISOU 5237  CD  GLU C  21    15413  15683  14810    325   -333    676       C  
ATOM   5238  OE1 GLU C  21      39.666   3.396  45.907  1.00121.96           O  
ANISOU 5238  OE1 GLU C  21    15557  15810  14973    350   -334    711       O  
ATOM   5239  OE2 GLU C  21      39.239   5.442  45.235  1.00120.02           O  
ANISOU 5239  OE2 GLU C  21    15298  15573  14732    295   -337    631       O  
ATOM   5240  N   LEU C  22      37.812   4.701  51.762  1.00130.88           N  
ANISOU 5240  N   LEU C  22    16752  17121  15855    391   -333    766       N  
ATOM   5241  CA  LEU C  22      37.288   4.072  52.966  1.00131.71           C  
ANISOU 5241  CA  LEU C  22    16883  17243  15917    417   -318    813       C  
ATOM   5242  C   LEU C  22      36.309   2.959  52.626  1.00131.80           C  
ANISOU 5242  C   LEU C  22    16922  17193  15965    419   -277    858       C  
ATOM   5243  O   LEU C  22      35.395   3.150  51.826  1.00130.89           O  
ANISOU 5243  O   LEU C  22    16811  17030  15890    386   -252    841       O  
ATOM   5244  CB  LEU C  22      36.601   5.109  53.854  1.00 71.19           C  
ANISOU 5244  CB  LEU C  22     9227   9615   8208    397   -315    789       C  
ATOM   5245  CG  LEU C  22      37.303   6.459  54.006  1.00 70.21           C  
ANISOU 5245  CG  LEU C  22     9075   9542   8059    381   -347    730       C  
ATOM   5246  CD1 LEU C  22      36.522   7.357  54.948  1.00 69.49           C  
ANISOU 5246  CD1 LEU C  22     8994   9485   7925    364   -338    710       C  
ATOM   5247  CD2 LEU C  22      38.727   6.269  54.498  1.00 70.99           C  
ANISOU 5247  CD2 LEU C  22     9153   9695   8126    417   -386    733       C  
ATOM   5248  N   VAL C  23      36.501   1.795  53.241  1.00147.75           N  
ANISOU 5248  N   VAL C  23    18957  19211  17968    458   -270    915       N  
ATOM   5249  CA  VAL C  23      35.609   0.667  53.012  1.00147.76           C  
ANISOU 5249  CA  VAL C  23    18984  19155  18005    462   -228    960       C  
ATOM   5250  C   VAL C  23      34.168   1.149  52.930  1.00147.46           C  
ANISOU 5250  C   VAL C  23    18962  19087  17978    425   -194    944       C  
ATOM   5251  O   VAL C  23      33.354   0.568  52.214  1.00147.22           O  
ANISOU 5251  O   VAL C  23    18942  18999  17997    410   -161    954       O  
ATOM   5252  CB  VAL C  23      35.722  -0.393  54.119  1.00138.39           C  
ANISOU 5252  CB  VAL C  23    17820  17983  16781    508   -218   1025       C  
ATOM   5253  CG1 VAL C  23      34.406  -0.511  54.872  1.00138.53           C  
ANISOU 5253  CG1 VAL C  23    17869  17988  16779    500   -180   1049       C  
ATOM   5254  CG2 VAL C  23      36.119  -1.736  53.526  1.00138.51           C  
ANISOU 5254  CG2 VAL C  23    17835  17952  16840    533   -206   1067       C  
ATOM   5255  N   GLU C  24      33.856   2.214  53.661  1.00162.18           N  
ANISOU 5255  N   GLU C  24    20827  20994  19798    410   -203    916       N  
ATOM   5256  CA  GLU C  24      32.513   2.782  53.613  1.00161.89           C  
ANISOU 5256  CA  GLU C  24    20805  20935  19771    374   -173    896       C  
ATOM   5257  C   GLU C  24      32.327   4.021  54.491  1.00161.95           C  
ANISOU 5257  C   GLU C  24    20811  20996  19727    359   -186    863       C  
ATOM   5258  O   GLU C  24      32.962   4.167  55.535  1.00162.38           O  
ANISOU 5258  O   GLU C  24    20865  21108  19725    384   -208    872       O  
ATOM   5259  CB  GLU C  24      31.471   1.720  53.976  1.00152.10           C  
ANISOU 5259  CB  GLU C  24    19596  19654  18541    383   -129    946       C  
ATOM   5260  CG  GLU C  24      30.613   1.265  52.804  1.00151.69           C  
ANISOU 5260  CG  GLU C  24    19546  19531  18557    358    -96    941       C  
ATOM   5261  CD  GLU C  24      30.308   2.389  51.827  1.00151.11           C  
ANISOU 5261  CD  GLU C  24    19454  19447  18514    317   -105    880       C  
ATOM   5262  OE1 GLU C  24      30.634   3.555  52.136  1.00151.03           O  
ANISOU 5262  OE1 GLU C  24    19432  19482  18472    305   -131    843       O  
ATOM   5263  OE2 GLU C  24      29.743   2.104  50.751  1.00150.75           O  
ANISOU 5263  OE2 GLU C  24    19405  19350  18524    297    -85    870       O  
ATOM   5264  N   SER C  25      31.440   4.902  54.041  1.00100.02           N  
ANISOU 5264  N   SER C  25    12966  13134  11904    320   -172    823       N  
ATOM   5265  CA  SER C  25      31.037   6.091  54.781  1.00100.03           C  
ANISOU 5265  CA  SER C  25    12967  13176  11866    300   -177    789       C  
ATOM   5266  C   SER C  25      29.658   6.495  54.271  1.00 99.64           C  
ANISOU 5266  C   SER C  25    12926  13081  11850    262   -143    769       C  
ATOM   5267  O   SER C  25      29.180   5.931  53.293  1.00 99.35           O  
ANISOU 5267  O   SER C  25    12892  12988  11867    252   -123    776       O  
ATOM   5268  CB  SER C  25      32.039   7.225  54.574  1.00 89.90           C  
ANISOU 5268  CB  SER C  25    11653  11934  10570    289   -215    738       C  
ATOM   5269  OG  SER C  25      32.621   7.623  55.803  1.00 90.34           O  
ANISOU 5269  OG  SER C  25    11706  12058  10562    308   -238    736       O  
ATOM   5270  N   GLN C  26      29.017   7.461  54.921  1.00 62.90           N  
ANISOU 5270  N   GLN C  26     8278   8453   7168    241   -138    743       N  
ATOM   5271  CA  GLN C  26      27.683   7.874  54.500  1.00 70.45           C  
ANISOU 5271  CA  GLN C  26     9243   9370   8156    207   -106    723       C  
ATOM   5272  C   GLN C  26      27.528   9.382  54.661  1.00 68.33           C  
ANISOU 5272  C   GLN C  26     8960   9131   7871    178   -118    669       C  
ATOM   5273  O   GLN C  26      27.969   9.942  55.661  1.00 71.05           O  
ANISOU 5273  O   GLN C  26     9302   9531   8163    185   -135    659       O  
ATOM   5274  CB  GLN C  26      26.616   7.160  55.336  1.00 65.76           C  
ANISOU 5274  CB  GLN C  26     8680   8762   7546    214    -69    763       C  
ATOM   5275  CG  GLN C  26      26.227   5.782  54.821  1.00 67.66           C  
ANISOU 5275  CG  GLN C  26     8934   8945   7827    227    -41    806       C  
ATOM   5276  CD  GLN C  26      24.808   5.398  55.193  1.00 77.05           C  
ANISOU 5276  CD  GLN C  26    10148  10102   9025    215      4    824       C  
ATOM   5277  OE1 GLN C  26      24.071   4.845  54.380  1.00 69.83           O  
ANISOU 5277  OE1 GLN C  26     9238   9133   8163    202     30    828       O  
ATOM   5278  NE2 GLN C  26      24.420   5.689  56.429  1.00 71.42           N  
ANISOU 5278  NE2 GLN C  26     9451   9423   8261    219     13    833       N  
ATOM   5279  N   CYS C  27      26.903  10.041  53.689  1.00 50.50           N  
ANISOU 5279  N   CYS C  27     6693   6838   5656    146   -108    634       N  
ATOM   5280  CA  CYS C  27      26.701  11.482  53.796  1.00 40.35           C  
ANISOU 5280  CA  CYS C  27     5395   5576   4361    118   -114    583       C  
ATOM   5281  C   CYS C  27      25.213  11.797  53.887  1.00 42.69           C  
ANISOU 5281  C   CYS C  27     5706   5844   4670     93    -80    575       C  
ATOM   5282  O   CYS C  27      24.380  10.929  53.644  1.00 37.26           O  
ANISOU 5282  O   CYS C  27     5035   5115   4008     94    -52    603       O  
ATOM   5283  CB  CYS C  27      27.305  12.187  52.586  1.00 49.87           C  
ANISOU 5283  CB  CYS C  27     6576   6769   5604    102   -133    543       C  
ATOM   5284  SG  CYS C  27      26.544  11.730  51.022  1.00 48.30           S  
ANISOU 5284  SG  CYS C  27     6377   6497   5476     86   -112    545       S  
ATOM   5285  N   SER C  28      24.874  13.035  54.232  1.00 46.67           N  
ANISOU 5285  N   SER C  28     6203   6371   5158     69    -80    535       N  
ATOM   5286  CA  SER C  28      23.475  13.390  54.378  1.00 43.50           C  
ANISOU 5286  CA  SER C  28     5814   5946   4768     45    -49    525       C  
ATOM   5287  C   SER C  28      23.293  14.876  54.102  1.00 42.35           C  
ANISOU 5287  C   SER C  28     5651   5809   4631     15    -54    471       C  
ATOM   5288  O   SER C  28      24.223  15.659  54.276  1.00 44.05           O  
ANISOU 5288  O   SER C  28     5849   6063   4826     15    -79    443       O  
ATOM   5289  CB  SER C  28      22.996  13.031  55.791  1.00 41.71           C  
ANISOU 5289  CB  SER C  28     5610   5746   4492     56    -32    552       C  
ATOM   5290  OG  SER C  28      21.710  13.567  56.052  1.00 52.42           O  
ANISOU 5290  OG  SER C  28     6976   7088   5855     31     -3    535       O  
ATOM   5291  N   SER C  29      22.095  15.260  53.667  1.00 40.67           N  
ANISOU 5291  N   SER C  29     5443   5561   4449     -9    -28    455       N  
ATOM   5292  CA  SER C  29      21.795  16.661  53.388  1.00 30.65           C  
ANISOU 5292  CA  SER C  29     4159   4295   3193    -37    -29    406       C  
ATOM   5293  C   SER C  29      20.290  16.892  53.423  1.00 39.31           C  
ANISOU 5293  C   SER C  29     5267   5362   4308    -58      4    399       C  
ATOM   5294  O   SER C  29      19.510  15.942  53.547  1.00 41.10           O  
ANISOU 5294  O   SER C  29     5512   5562   4542    -52     27    431       O  
ATOM   5295  CB  SER C  29      22.371  17.075  52.027  1.00 43.20           C  
ANISOU 5295  CB  SER C  29     5728   5862   4823    -43    -45    383       C  
ATOM   5296  OG  SER C  29      22.313  18.481  51.836  1.00 39.29           O  
ANISOU 5296  OG  SER C  29     5218   5376   4336    -66    -47    336       O  
ATOM   5297  N   THR C  30      19.890  18.153  53.309  1.00 36.51           N  
ANISOU 5297  N   THR C  30     4901   5010   3961    -82      8    357       N  
ATOM   5298  CA  THR C  30      18.485  18.537  53.370  1.00 32.93           C  
ANISOU 5298  CA  THR C  30     4455   4532   3525   -103     38    345       C  
ATOM   5299  C   THR C  30      18.167  19.624  52.345  1.00 41.40           C  
ANISOU 5299  C   THR C  30     5512   5581   4639   -125     38    306       C  
ATOM   5300  O   THR C  30      18.981  20.520  52.112  1.00 39.50           O  
ANISOU 5300  O   THR C  30     5253   5359   4396   -130     19    277       O  
ATOM   5301  CB  THR C  30      18.131  19.060  54.777  1.00 42.72           C  
ANISOU 5301  CB  THR C  30     5704   5810   4719   -111     48    336       C  
ATOM   5302  OG1 THR C  30      18.344  18.018  55.739  1.00 47.61           O  
ANISOU 5302  OG1 THR C  30     6341   6450   5299    -89     50    376       O  
ATOM   5303  CG2 THR C  30      16.676  19.528  54.843  1.00 39.21           C  
ANISOU 5303  CG2 THR C  30     5265   5339   4294   -135     79    320       C  
ATOM   5304  N   LEU C  31      16.987  19.543  51.734  1.00 38.46           N  
ANISOU 5304  N   LEU C  31     5143   5167   4302   -136     61    304       N  
ATOM   5305  CA  LEU C  31      16.510  20.590  50.827  1.00 32.74           C  
ANISOU 5305  CA  LEU C  31     4404   4420   3614   -155     64    269       C  
ATOM   5306  C   LEU C  31      15.099  21.055  51.152  1.00 32.47           C  
ANISOU 5306  C   LEU C  31     4377   4371   3591   -174     93    255       C  
ATOM   5307  O   LEU C  31      14.313  20.332  51.765  1.00 33.42           O  
ANISOU 5307  O   LEU C  31     4513   4484   3702   -173    113    276       O  
ATOM   5308  CB  LEU C  31      16.552  20.122  49.375  1.00 32.24           C  
ANISOU 5308  CB  LEU C  31     4335   4318   3596   -149     59    276       C  
ATOM   5309  CG  LEU C  31      17.922  19.742  48.831  1.00 39.22           C  
ANISOU 5309  CG  LEU C  31     5211   5212   4480   -132     32    286       C  
ATOM   5310  CD1 LEU C  31      18.222  18.286  49.185  1.00 40.07           C  
ANISOU 5310  CD1 LEU C  31     5331   5319   4573   -111     30    328       C  
ATOM   5311  CD2 LEU C  31      17.945  19.953  47.332  1.00 37.02           C  
ANISOU 5311  CD2 LEU C  31     4921   4901   4246   -135     26    274       C  
ATOM   5312  N   VAL C  32      14.775  22.253  50.690  1.00 30.84           N  
ANISOU 5312  N   VAL C  32     4157   4156   3405   -191     95    219       N  
ATOM   5313  CA  VAL C  32      13.516  22.895  51.017  1.00 30.81           C  
ANISOU 5313  CA  VAL C  32     4155   4141   3411   -210    120    200       C  
ATOM   5314  C   VAL C  32      12.939  23.568  49.777  1.00 34.35           C  
ANISOU 5314  C   VAL C  32     4591   4555   3906   -219    125    178       C  
ATOM   5315  O   VAL C  32      13.673  23.964  48.881  1.00 36.41           O  
ANISOU 5315  O   VAL C  32     4840   4811   4183   -214    107    168       O  
ATOM   5316  CB  VAL C  32      13.724  23.935  52.131  1.00 36.89           C  
ANISOU 5316  CB  VAL C  32     4921   4949   4146   -223    122    174       C  
ATOM   5317  CG1 VAL C  32      12.634  24.969  52.115  1.00 42.99           C  
ANISOU 5317  CG1 VAL C  32     5688   5707   4940   -244    143    143       C  
ATOM   5318  CG2 VAL C  32      13.817  23.248  53.491  1.00 37.93           C  
ANISOU 5318  CG2 VAL C  32     5069   5113   4230   -216    127    196       C  
ATOM   5319  N   LYS C  33      11.621  23.682  49.718  1.00 24.52           N  
ANISOU 5319  N   LYS C  33     3349   3286   2682   -230    148    171       N  
ATOM   5320  CA  LYS C  33      10.977  24.303  48.578  1.00 26.46           C  
ANISOU 5320  CA  LYS C  33     3582   3501   2970   -236    152    151       C  
ATOM   5321  C   LYS C  33       9.622  24.824  48.983  1.00 32.17           C  
ANISOU 5321  C   LYS C  33     4307   4212   3705   -252    178    133       C  
ATOM   5322  O   LYS C  33       8.828  24.094  49.572  1.00 31.98           O  
ANISOU 5322  O   LYS C  33     4294   4181   3675   -254    196    147       O  
ATOM   5323  CB  LYS C  33      10.805  23.288  47.453  1.00 24.67           C  
ANISOU 5323  CB  LYS C  33     3356   3243   2773   -222    148    171       C  
ATOM   5324  CG  LYS C  33       9.995  23.806  46.278  1.00 28.81           C  
ANISOU 5324  CG  LYS C  33     3869   3737   3340   -226    153    153       C  
ATOM   5325  CD  LYS C  33      10.847  24.678  45.383  1.00 27.31           C  
ANISOU 5325  CD  LYS C  33     3667   3549   3162   -223    134    138       C  
ATOM   5326  CE  LYS C  33      10.013  25.275  44.273  1.00 31.89           C  
ANISOU 5326  CE  LYS C  33     4236   4101   3779   -224    140    121       C  
ATOM   5327  NZ  LYS C  33      10.846  26.092  43.346  1.00 35.80           N  
ANISOU 5327  NZ  LYS C  33     4720   4595   4285   -219    125    110       N  
ATOM   5328  N   HIS C  34       9.339  26.085  48.672  1.00 23.63           N  
ANISOU 5328  N   HIS C  34     3212   3125   2639   -263    182    103       N  
ATOM   5329  CA  HIS C  34       7.997  26.591  48.909  1.00 29.56           C  
ANISOU 5329  CA  HIS C  34     3963   3862   3407   -277    206     85       C  
ATOM   5330  C   HIS C  34       7.125  26.411  47.675  1.00 32.28           C  
ANISOU 5330  C   HIS C  34     4301   4170   3796   -272    210     84       C  
ATOM   5331  O   HIS C  34       7.504  26.775  46.561  1.00 29.46           O  
ANISOU 5331  O   HIS C  34     3933   3800   3460   -264    196     79       O  
ATOM   5332  CB  HIS C  34       7.986  28.052  49.351  1.00 28.02           C  
ANISOU 5332  CB  HIS C  34     3758   3679   3208   -293    213     52       C  
ATOM   5333  CG  HIS C  34       6.603  28.610  49.525  1.00 37.67           C  
ANISOU 5333  CG  HIS C  34     4978   4885   4452   -307    238     32       C  
ATOM   5334  ND1 HIS C  34       5.871  28.439  50.684  1.00 34.76           N  
ANISOU 5334  ND1 HIS C  34     4617   4525   4063   -319    259     30       N  
ATOM   5335  CD2 HIS C  34       5.814  29.315  48.682  1.00 37.29           C  
ANISOU 5335  CD2 HIS C  34     4918   4810   4442   -309    245     15       C  
ATOM   5336  CE1 HIS C  34       4.691  29.021  50.544  1.00 32.55           C  
ANISOU 5336  CE1 HIS C  34     4332   4225   3812   -330    278     10       C  
ATOM   5337  NE2 HIS C  34       4.629  29.557  49.338  1.00 31.19           N  
ANISOU 5337  NE2 HIS C  34     4146   4030   3673   -323    270      1       N  
ATOM   5338  N   ILE C  35       5.944  25.860  47.891  1.00 29.82           N  
ANISOU 5338  N   ILE C  35     3993   3841   3496   -277    230     87       N  
ATOM   5339  CA  ILE C  35       5.033  25.567  46.807  1.00 30.50           C  
ANISOU 5339  CA  ILE C  35     4072   3896   3622   -272    234     84       C  
ATOM   5340  C   ILE C  35       3.777  26.386  46.990  1.00 32.57           C  
ANISOU 5340  C   ILE C  35     4326   4145   3903   -285    255     59       C  
ATOM   5341  O   ILE C  35       3.212  26.425  48.080  1.00 32.74           O  
ANISOU 5341  O   ILE C  35     4356   4175   3910   -298    275     54       O  
ATOM   5342  CB  ILE C  35       4.665  24.105  46.856  1.00 25.92           C  
ANISOU 5342  CB  ILE C  35     3501   3303   3045   -265    242    109       C  
ATOM   5343  CG1 ILE C  35       5.929  23.266  46.677  1.00 26.05           C  
ANISOU 5343  CG1 ILE C  35     3524   3330   3044   -251    222    135       C  
ATOM   5344  CG2 ILE C  35       3.597  23.792  45.820  1.00 26.14           C  
ANISOU 5344  CG2 ILE C  35     3518   3300   3115   -262    249    100       C  
ATOM   5345  CD1 ILE C  35       5.778  21.833  47.149  1.00 30.52           C  
ANISOU 5345  CD1 ILE C  35     4104   3890   3602   -245    233    164       C  
ATOM   5346  N   LYS C  36       3.331  27.049  45.934  1.00 28.99           N  
ANISOU 5346  N   LYS C  36     3859   3674   3482   -281    252     42       N  
ATOM   5347  CA  LYS C  36       2.172  27.910  46.071  1.00 32.74           C  
ANISOU 5347  CA  LYS C  36     4325   4138   3976   -292    271     17       C  
ATOM   5348  C   LYS C  36       0.888  27.124  45.896  1.00 34.17           C  
ANISOU 5348  C   LYS C  36     4504   4298   4181   -293    287     17       C  
ATOM   5349  O   LYS C  36       0.124  27.364  44.961  1.00 29.69           O  
ANISOU 5349  O   LYS C  36     3924   3712   3647   -287    287      4       O  
ATOM   5350  CB  LYS C  36       2.222  29.078  45.085  1.00 34.91           C  
ANISOU 5350  CB  LYS C  36     4586   4403   4274   -286    262      0       C  
ATOM   5351  CG  LYS C  36       3.406  30.011  45.263  1.00 37.10           C  
ANISOU 5351  CG  LYS C  36     4864   4700   4534   -288    251     -6       C  
ATOM   5352  CD  LYS C  36       3.404  31.069  44.145  1.00 45.81           C  
ANISOU 5352  CD  LYS C  36     5953   5788   5665   -279    246    -19       C  
ATOM   5353  CE  LYS C  36       4.626  31.966  44.197  1.00 47.98           C  
ANISOU 5353  CE  LYS C  36     6226   6076   5927   -281    237    -26       C  
ATOM   5354  NZ  LYS C  36       5.883  31.219  43.889  1.00 40.43           N  
ANISOU 5354  NZ  LYS C  36     5277   5133   4954   -271    215     -5       N  
ATOM   5355  N   ALA C  37       0.655  26.190  46.817  1.00 31.06           N  
ANISOU 5355  N   ALA C  37     4124   3908   3771   -300    301     30       N  
ATOM   5356  CA  ALA C  37      -0.571  25.400  46.824  1.00 24.66           C  
ANISOU 5356  CA  ALA C  37     3311   3076   2982   -303    322     28       C  
ATOM   5357  C   ALA C  37      -0.868  24.895  48.243  1.00 20.57           C  
ANISOU 5357  C   ALA C  37     2810   2567   2439   -317    346     37       C  
ATOM   5358  O   ALA C  37       0.053  24.703  49.042  1.00 25.78           O  
ANISOU 5358  O   ALA C  37     3484   3250   3062   -317    341     54       O  
ATOM   5359  CB  ALA C  37      -0.457  24.232  45.837  1.00 26.13           C  
ANISOU 5359  CB  ALA C  37     3495   3247   3187   -288    311     45       C  
ATOM   5360  N   PRO C  38      -2.155  24.685  48.558  1.00 20.81           N  
ANISOU 5360  N   PRO C  38     2837   2581   2488   -328    372     24       N  
ATOM   5361  CA  PRO C  38      -2.562  24.233  49.902  1.00 26.09           C  
ANISOU 5361  CA  PRO C  38     3523   3257   3135   -342    399     31       C  
ATOM   5362  C   PRO C  38      -1.977  22.860  50.174  1.00 27.65           C  
ANISOU 5362  C   PRO C  38     3737   3455   3315   -333    400     65       C  
ATOM   5363  O   PRO C  38      -1.860  22.048  49.253  1.00 22.10           O  
ANISOU 5363  O   PRO C  38     3029   2736   2633   -320    391     77       O  
ATOM   5364  CB  PRO C  38      -4.088  24.102  49.802  1.00 29.66           C  
ANISOU 5364  CB  PRO C  38     3964   3682   3623   -351    426     10       C  
ATOM   5365  CG  PRO C  38      -4.478  24.631  48.455  1.00 34.47           C  
ANISOU 5365  CG  PRO C  38     4550   4276   4270   -342    410    -10       C  
ATOM   5366  CD  PRO C  38      -3.258  24.616  47.584  1.00 24.18           C  
ANISOU 5366  CD  PRO C  38     3247   2982   2960   -325    377      5       C  
ATOM   5367  N   LEU C  39      -1.631  22.584  51.424  1.00 25.73           N  
ANISOU 5367  N   LEU C  39     3512   3231   3032   -338    412     82       N  
ATOM   5368  CA  LEU C  39      -0.931  21.352  51.741  1.00 23.07           C  
ANISOU 5368  CA  LEU C  39     3193   2898   2674   -327    412    118       C  
ATOM   5369  C   LEU C  39      -1.758  20.097  51.378  1.00 27.69           C  
ANISOU 5369  C   LEU C  39     3779   3451   3291   -324    434    129       C  
ATOM   5370  O   LEU C  39      -1.192  19.068  51.026  1.00 25.66           O  
ANISOU 5370  O   LEU C  39     3528   3186   3035   -311    427    155       O  
ATOM   5371  CB  LEU C  39      -0.492  21.346  53.217  1.00 28.84           C  
ANISOU 5371  CB  LEU C  39     3945   3659   3354   -332    423    134       C  
ATOM   5372  CG  LEU C  39       0.343  20.179  53.761  1.00 28.82           C  
ANISOU 5372  CG  LEU C  39     3963   3668   3320   -317    422    175       C  
ATOM   5373  CD1 LEU C  39       1.076  20.589  55.035  1.00 29.29           C  
ANISOU 5373  CD1 LEU C  39     4037   3769   3324   -319    418    184       C  
ATOM   5374  CD2 LEU C  39      -0.508  18.942  54.033  1.00 35.44           C  
ANISOU 5374  CD2 LEU C  39     4813   4478   4173   -318    455    194       C  
ATOM   5375  N   HIS C  40      -3.083  20.172  51.432  1.00 22.77           N  
ANISOU 5375  N   HIS C  40     3148   2806   2697   -338    460    106       N  
ATOM   5376  CA  HIS C  40      -3.856  18.957  51.172  1.00 26.21           C  
ANISOU 5376  CA  HIS C  40     3584   3211   3162   -337    485    114       C  
ATOM   5377  C   HIS C  40      -3.654  18.489  49.729  1.00 26.98           C  
ANISOU 5377  C   HIS C  40     3665   3291   3295   -323    464    112       C  
ATOM   5378  O   HIS C  40      -3.527  17.295  49.471  1.00 26.42           O  
ANISOU 5378  O   HIS C  40     3599   3205   3236   -315    471    132       O  
ATOM   5379  CB  HIS C  40      -5.341  19.152  51.492  1.00 24.13           C  
ANISOU 5379  CB  HIS C  40     3314   2929   2927   -355    518     86       C  
ATOM   5380  CG  HIS C  40      -6.089  19.922  50.448  1.00 27.62           C  
ANISOU 5380  CG  HIS C  40     3728   3358   3409   -358    507     49       C  
ATOM   5381  ND1 HIS C  40      -6.350  21.269  50.568  1.00 37.66           N  
ANISOU 5381  ND1 HIS C  40     4990   4642   4678   -366    501     23       N  
ATOM   5382  CD2 HIS C  40      -6.620  19.532  49.269  1.00 24.57           C  
ANISOU 5382  CD2 HIS C  40     3322   2949   3065   -351    502     35       C  
ATOM   5383  CE1 HIS C  40      -7.017  21.681  49.499  1.00 24.17           C  
ANISOU 5383  CE1 HIS C  40     3257   2918   3008   -363    492     -4       C  
ATOM   5384  NE2 HIS C  40      -7.194  20.650  48.698  1.00 28.39           N  
ANISOU 5384  NE2 HIS C  40     3785   3433   3569   -354    491      2       N  
ATOM   5385  N   LEU C  41      -3.620  19.440  48.795  1.00 26.06           N  
ANISOU 5385  N   LEU C  41     3529   3178   3194   -320    439     89       N  
ATOM   5386  CA  LEU C  41      -3.396  19.136  47.386  1.00 26.15           C  
ANISOU 5386  CA  LEU C  41     3524   3177   3234   -306    416     85       C  
ATOM   5387  C   LEU C  41      -1.957  18.666  47.164  1.00 22.69           C  
ANISOU 5387  C   LEU C  41     3095   2752   2772   -291    391    116       C  
ATOM   5388  O   LEU C  41      -1.716  17.701  46.433  1.00 25.37           O  
ANISOU 5388  O   LEU C  41     3431   3077   3130   -280    386    128       O  
ATOM   5389  CB  LEU C  41      -3.692  20.371  46.529  1.00 31.90           C  
ANISOU 5389  CB  LEU C  41     4231   3908   3981   -305    397     55       C  
ATOM   5390  CG  LEU C  41      -3.458  20.319  45.018  1.00 33.72           C  
ANISOU 5390  CG  LEU C  41     4444   4132   4238   -289    371     48       C  
ATOM   5391  CD1 LEU C  41      -4.057  19.071  44.415  1.00 47.37           C  
ANISOU 5391  CD1 LEU C  41     6164   5837   5999   -286    383     47       C  
ATOM   5392  CD2 LEU C  41      -4.032  21.569  44.349  1.00 33.37           C  
ANISOU 5392  CD2 LEU C  41     4380   4087   4211   -288    360     17       C  
ATOM   5393  N   VAL C  42      -0.995  19.340  47.790  1.00 19.92           N  
ANISOU 5393  N   VAL C  42     2756   2429   2383   -289    376    126       N  
ATOM   5394  CA  VAL C  42       0.385  18.885  47.693  1.00 25.18           C  
ANISOU 5394  CA  VAL C  42     3432   3110   3025   -275    353    154       C  
ATOM   5395  C   VAL C  42       0.497  17.449  48.224  1.00 28.63           C  
ANISOU 5395  C   VAL C  42     3886   3537   3456   -270    372    186       C  
ATOM   5396  O   VAL C  42       1.149  16.599  47.616  1.00 26.34           O  
ANISOU 5396  O   VAL C  42     3595   3240   3173   -256    361    205       O  
ATOM   5397  CB  VAL C  42       1.387  19.819  48.428  1.00 24.77           C  
ANISOU 5397  CB  VAL C  42     3389   3092   2930   -276    337    158       C  
ATOM   5398  CG1 VAL C  42       2.801  19.249  48.335  1.00 21.42           C  
ANISOU 5398  CG1 VAL C  42     2973   2683   2483   -259    314    187       C  
ATOM   5399  CG2 VAL C  42       1.349  21.230  47.856  1.00 20.99           C  
ANISOU 5399  CG2 VAL C  42     2894   2620   2461   -280    320    128       C  
ATOM   5400  N   TRP C  43      -0.161  17.175  49.347  1.00 21.12           N  
ANISOU 5400  N   TRP C  43     2948   2585   2492   -281    403    192       N  
ATOM   5401  CA  TRP C  43      -0.032  15.864  49.974  1.00 21.79           C  
ANISOU 5401  CA  TRP C  43     3052   2661   2568   -275    425    225       C  
ATOM   5402  C   TRP C  43      -0.733  14.788  49.153  1.00 19.15           C  
ANISOU 5402  C   TRP C  43     2708   2289   2280   -273    442    224       C  
ATOM   5403  O   TRP C  43      -0.270  13.654  49.097  1.00 19.14           O  
ANISOU 5403  O   TRP C  43     2715   2276   2280   -262    447    252       O  
ATOM   5404  CB  TRP C  43      -0.564  15.895  51.410  1.00 22.00           C  
ANISOU 5404  CB  TRP C  43     3097   2695   2566   -286    456    232       C  
ATOM   5405  CG  TRP C  43      -0.540  14.563  52.107  1.00 21.37           C  
ANISOU 5405  CG  TRP C  43     3039   2604   2477   -280    483    268       C  
ATOM   5406  CD1 TRP C  43      -1.623  13.829  52.497  1.00 28.01           C  
ANISOU 5406  CD1 TRP C  43     3885   3417   3339   -289    525    269       C  
ATOM   5407  CD2 TRP C  43       0.618  13.804  52.489  1.00 21.15           C  
ANISOU 5407  CD2 TRP C  43     3029   2590   2418   -261    473    309       C  
ATOM   5408  NE1 TRP C  43      -1.212  12.669  53.098  1.00 26.60           N  
ANISOU 5408  NE1 TRP C  43     3729   3234   3145   -278    543    310       N  
ATOM   5409  CE2 TRP C  43       0.152  12.624  53.109  1.00 26.85           C  
ANISOU 5409  CE2 TRP C  43     3768   3291   3144   -259    511    336       C  
ATOM   5410  CE3 TRP C  43       2.000  14.004  52.363  1.00 17.09           C  
ANISOU 5410  CE3 TRP C  43     2516   2104   1874   -245    437    325       C  
ATOM   5411  CZ2 TRP C  43       1.026  11.643  53.607  1.00 26.48           C  
ANISOU 5411  CZ2 TRP C  43     3741   3249   3070   -240    513    381       C  
ATOM   5412  CZ3 TRP C  43       2.861  13.040  52.860  1.00 24.99           C  
ANISOU 5412  CZ3 TRP C  43     3535   3113   2849   -227    437    367       C  
ATOM   5413  CH2 TRP C  43       2.370  11.866  53.477  1.00 28.61           C  
ANISOU 5413  CH2 TRP C  43     4011   3548   3310   -224    475    396       C  
ATOM   5414  N   SER C  44      -1.835  15.157  48.491  1.00 25.28           N  
ANISOU 5414  N   SER C  44     3464   3047   3094   -284    450    189       N  
ATOM   5415  CA  SER C  44      -2.565  14.213  47.643  1.00 24.65           C  
ANISOU 5415  CA  SER C  44     3370   2934   3061   -283    465    179       C  
ATOM   5416  C   SER C  44      -1.678  13.693  46.523  1.00 26.31           C  
ANISOU 5416  C   SER C  44     3572   3142   3284   -267    438    190       C  
ATOM   5417  O   SER C  44      -1.867  12.574  46.053  1.00 23.71           O  
ANISOU 5417  O   SER C  44     3238   2788   2983   -263    452    196       O  
ATOM   5418  CB  SER C  44      -3.845  14.835  47.066  1.00 26.68           C  
ANISOU 5418  CB  SER C  44     3605   3178   3355   -295    472    136       C  
ATOM   5419  OG  SER C  44      -3.566  15.757  46.023  1.00 33.99           O  
ANISOU 5419  OG  SER C  44     4512   4115   4288   -288    438    116       O  
ATOM   5420  N   ILE C  45      -0.708  14.508  46.099  1.00 22.67           N  
ANISOU 5420  N   ILE C  45     3107   2704   2802   -258    401    190       N  
ATOM   5421  CA  ILE C  45       0.284  14.083  45.110  1.00 20.92           C  
ANISOU 5421  CA  ILE C  45     2879   2482   2586   -242    374    202       C  
ATOM   5422  C   ILE C  45       1.406  13.266  45.760  1.00 20.73           C  
ANISOU 5422  C   ILE C  45     2877   2468   2534   -230    372    243       C  
ATOM   5423  O   ILE C  45       1.723  12.165  45.330  1.00 24.61           O  
ANISOU 5423  O   ILE C  45     3368   2942   3041   -221    376    260       O  
ATOM   5424  CB  ILE C  45       0.922  15.307  44.377  1.00 22.80           C  
ANISOU 5424  CB  ILE C  45     3106   2742   2815   -236    337    186       C  
ATOM   5425  CG1 ILE C  45      -0.125  16.069  43.565  1.00 25.90           C  
ANISOU 5425  CG1 ILE C  45     3477   3126   3238   -243    335    148       C  
ATOM   5426  CG2 ILE C  45       2.078  14.877  43.506  1.00 20.14           C  
ANISOU 5426  CG2 ILE C  45     2766   2408   2478   -220    310    202       C  
ATOM   5427  CD1 ILE C  45      -0.998  15.197  42.727  1.00 31.92           C  
ANISOU 5427  CD1 ILE C  45     4222   3861   4043   -242    349    134       C  
ATOM   5428  N   VAL C  46       2.000  13.807  46.813  1.00 20.98           N  
ANISOU 5428  N   VAL C  46     2925   2526   2522   -230    367    258       N  
ATOM   5429  CA  VAL C  46       3.157  13.166  47.434  1.00 20.16           C  
ANISOU 5429  CA  VAL C  46     2840   2437   2385   -216    360    297       C  
ATOM   5430  C   VAL C  46       2.862  11.795  48.048  1.00 25.75           C  
ANISOU 5430  C   VAL C  46     3564   3123   3098   -213    394    326       C  
ATOM   5431  O   VAL C  46       3.700  10.892  47.984  1.00 24.75           O  
ANISOU 5431  O   VAL C  46     3444   2993   2965   -197    389    356       O  
ATOM   5432  CB  VAL C  46       3.786  14.073  48.503  1.00 20.74           C  
ANISOU 5432  CB  VAL C  46     2926   2546   2407   -218    349    303       C  
ATOM   5433  CG1 VAL C  46       4.809  13.288  49.329  1.00 22.31           C  
ANISOU 5433  CG1 VAL C  46     3145   2761   2570   -202    347    344       C  
ATOM   5434  CG2 VAL C  46       4.420  15.276  47.835  1.00 22.51           C  
ANISOU 5434  CG2 VAL C  46     3136   2791   2627   -217    314    281       C  
ATOM   5435  N   ARG C  47       1.677  11.637  48.636  1.00 16.52           N  
ANISOU 5435  N   ARG C  47     2399   1937   1940   -227    430    317       N  
ATOM   5436  CA  ARG C  47       1.328  10.385  49.302  1.00 20.51           C  
ANISOU 5436  CA  ARG C  47     2921   2420   2450   -225    468    345       C  
ATOM   5437  C   ARG C  47       1.252   9.190  48.350  1.00 21.73           C  
ANISOU 5437  C   ARG C  47     3065   2541   2650   -218    478    350       C  
ATOM   5438  O   ARG C  47       1.394   8.046  48.782  1.00 22.43           O  
ANISOU 5438  O   ARG C  47     3169   2612   2741   -210    502    382       O  
ATOM   5439  CB  ARG C  47       0.022  10.527  50.102  1.00 21.77           C  
ANISOU 5439  CB  ARG C  47     3087   2569   2616   -243    507    331       C  
ATOM   5440  CG  ARG C  47      -1.241  10.547  49.282  1.00 17.57           C  
ANISOU 5440  CG  ARG C  47     2532   2007   2137   -258    523    292       C  
ATOM   5441  CD  ARG C  47      -2.457  10.613  50.199  1.00 26.20           C  
ANISOU 5441  CD  ARG C  47     3633   3089   3234   -276    563    281       C  
ATOM   5442  NE  ARG C  47      -2.432   9.569  51.231  1.00 29.91           N  
ANISOU 5442  NE  ARG C  47     4128   3547   3688   -272    600    319       N  
ATOM   5443  CZ  ARG C  47      -2.916   8.341  51.061  1.00 30.63           C  
ANISOU 5443  CZ  ARG C  47     4221   3603   3816   -272    634    328       C  
ATOM   5444  NH1 ARG C  47      -2.846   7.454  52.043  1.00 35.96           N  
ANISOU 5444  NH1 ARG C  47     4921   4267   4473   -266    668    366       N  
ATOM   5445  NH2 ARG C  47      -3.463   7.996  49.894  1.00 31.78           N  
ANISOU 5445  NH2 ARG C  47     4340   3721   4013   -276    635    300       N  
ATOM   5446  N   ARG C  48       1.065   9.452  47.057  1.00 30.38           N  
ANISOU 5446  N   ARG C  48     4135   3627   3780   -220    458    320       N  
ATOM   5447  CA  ARG C  48       0.942   8.374  46.069  1.00 25.00           C  
ANISOU 5447  CA  ARG C  48     3440   2915   3143   -215    467    317       C  
ATOM   5448  C   ARG C  48       2.283   7.716  45.706  1.00 23.23           C  
ANISOU 5448  C   ARG C  48     3222   2696   2910   -196    445    348       C  
ATOM   5449  O   ARG C  48       2.785   7.863  44.586  1.00 20.96           O  
ANISOU 5449  O   ARG C  48     2917   2411   2637   -190    416    335       O  
ATOM   5450  CB  ARG C  48       0.223   8.870  44.819  1.00 24.16           C  
ANISOU 5450  CB  ARG C  48     3304   2800   3075   -224    454    273       C  
ATOM   5451  CG  ARG C  48      -1.173   9.443  45.094  1.00 27.59           C  
ANISOU 5451  CG  ARG C  48     3730   3227   3525   -242    477    240       C  
ATOM   5452  CD  ARG C  48      -2.142   8.381  45.604  1.00 28.39           C  
ANISOU 5452  CD  ARG C  48     3836   3296   3654   -252    526    242       C  
ATOM   5453  NE  ARG C  48      -2.098   7.158  44.796  1.00 39.65           N  
ANISOU 5453  NE  ARG C  48     5251   4694   5120   -246    537    244       N  
ATOM   5454  CZ  ARG C  48      -2.821   6.949  43.698  1.00 40.07           C  
ANISOU 5454  CZ  ARG C  48     5276   4729   5218   -252    538    208       C  
ATOM   5455  NH1 ARG C  48      -3.652   7.886  43.253  1.00 36.39           N  
ANISOU 5455  NH1 ARG C  48     4790   4271   4764   -261    528    168       N  
ATOM   5456  NH2 ARG C  48      -2.709   5.801  43.035  1.00 33.47           N  
ANISOU 5456  NH2 ARG C  48     4431   3869   4417   -247    550    210       N  
ATOM   5457  N   PHE C  49       2.840   6.971  46.666  1.00 24.23           N  
ANISOU 5457  N   PHE C  49     3371   2823   3011   -185    461    390       N  
ATOM   5458  CA  PHE C  49       4.085   6.216  46.481  1.00 26.81           C  
ANISOU 5458  CA  PHE C  49     3705   3152   3329   -165    445    424       C  
ATOM   5459  C   PHE C  49       3.999   5.351  45.238  1.00 20.94           C  
ANISOU 5459  C   PHE C  49     2942   2377   2636   -163    448    412       C  
ATOM   5460  O   PHE C  49       5.001   5.091  44.564  1.00 26.46           O  
ANISOU 5460  O   PHE C  49     3636   3082   3337   -149    423    422       O  
ATOM   5461  CB  PHE C  49       4.350   5.346  47.727  1.00 28.74           C  
ANISOU 5461  CB  PHE C  49     3978   3393   3549   -154    474    470       C  
ATOM   5462  CG  PHE C  49       5.422   4.294  47.554  1.00 28.25           C  
ANISOU 5462  CG  PHE C  49     3923   3324   3488   -132    468    507       C  
ATOM   5463  CD1 PHE C  49       6.759   4.596  47.791  1.00 32.42           C  
ANISOU 5463  CD1 PHE C  49     4458   3885   3975   -115    433    530       C  
ATOM   5464  CD2 PHE C  49       5.087   2.994  47.195  1.00 31.75           C  
ANISOU 5464  CD2 PHE C  49     4364   3726   3975   -130    501    518       C  
ATOM   5465  CE1 PHE C  49       7.751   3.621  47.659  1.00 35.76           C  
ANISOU 5465  CE1 PHE C  49     4887   4301   4400    -93    428    565       C  
ATOM   5466  CE2 PHE C  49       6.074   2.005  47.059  1.00 30.79           C  
ANISOU 5466  CE2 PHE C  49     4248   3595   3855   -109    498    554       C  
ATOM   5467  CZ  PHE C  49       7.406   2.322  47.292  1.00 34.18           C  
ANISOU 5467  CZ  PHE C  49     4686   4059   4243    -90    461    578       C  
ATOM   5468  N   ASP C  50       2.795   4.890  44.938  1.00 23.34           N  
ANISOU 5468  N   ASP C  50     3234   2650   2982   -177    481    389       N  
ATOM   5469  CA  ASP C  50       2.602   3.975  43.823  1.00 29.55           C  
ANISOU 5469  CA  ASP C  50     4001   3406   3819   -176    490    375       C  
ATOM   5470  C   ASP C  50       2.604   4.693  42.476  1.00 29.64           C  
ANISOU 5470  C   ASP C  50     3985   3428   3848   -179    454    335       C  
ATOM   5471  O   ASP C  50       2.614   4.042  41.432  1.00 25.96           O  
ANISOU 5471  O   ASP C  50     3500   2944   3419   -177    453    322       O  
ATOM   5472  CB  ASP C  50       1.307   3.175  43.992  1.00 29.48           C  
ANISOU 5472  CB  ASP C  50     3988   3361   3853   -191    539    361       C  
ATOM   5473  CG  ASP C  50       0.071   4.056  44.022  1.00 36.82           C  
ANISOU 5473  CG  ASP C  50     4905   4293   4790   -210    546    321       C  
ATOM   5474  OD1 ASP C  50      -0.952   3.648  43.440  1.00 43.63           O  
ANISOU 5474  OD1 ASP C  50     5747   5130   5699   -222    569    288       O  
ATOM   5475  OD2 ASP C  50       0.114   5.151  44.631  1.00 37.27           O  
ANISOU 5475  OD2 ASP C  50     4973   4380   4810   -213    530    320       O  
ATOM   5476  N   GLU C  51       2.612   6.026  42.502  1.00 26.09           N  
ANISOU 5476  N   GLU C  51     3533   3009   3372   -183    427    318       N  
ATOM   5477  CA  GLU C  51       2.617   6.799  41.264  1.00 30.37           C  
ANISOU 5477  CA  GLU C  51     4051   3562   3926   -184    394    284       C  
ATOM   5478  C   GLU C  51       3.533   8.022  41.280  1.00 22.83           C  
ANISOU 5478  C   GLU C  51     3100   2642   2931   -177    354    287       C  
ATOM   5479  O   GLU C  51       3.067   9.154  41.160  1.00 20.74           O  
ANISOU 5479  O   GLU C  51     2829   2392   2659   -185    342    262       O  
ATOM   5480  CB  GLU C  51       1.187   7.198  40.905  1.00 30.41           C  
ANISOU 5480  CB  GLU C  51     4038   3556   3961   -200    409    242       C  
ATOM   5481  CG  GLU C  51       0.375   6.030  40.416  1.00 41.53           C  
ANISOU 5481  CG  GLU C  51     5431   4931   5419   -206    441    227       C  
ATOM   5482  CD  GLU C  51      -1.025   6.417  40.006  1.00 52.89           C  
ANISOU 5482  CD  GLU C  51     6848   6361   6888   -220    453    182       C  
ATOM   5483  OE1 GLU C  51      -1.533   7.436  40.522  1.00 54.58           O  
ANISOU 5483  OE1 GLU C  51     7065   6590   7082   -228    450    170       O  
ATOM   5484  OE2 GLU C  51      -1.615   5.694  39.176  1.00 56.39           O  
ANISOU 5484  OE2 GLU C  51     7269   6784   7374   -224    466    156       O  
ATOM   5485  N   PRO C  52       4.845   7.794  41.443  1.00 24.43           N  
ANISOU 5485  N   PRO C  52     3315   2858   3109   -163    335    318       N  
ATOM   5486  CA  PRO C  52       5.763   8.931  41.539  1.00 26.30           C  
ANISOU 5486  CA  PRO C  52     3557   3129   3308   -158    300    320       C  
ATOM   5487  C   PRO C  52       5.859   9.704  40.216  1.00 23.85           C  
ANISOU 5487  C   PRO C  52     3224   2825   3012   -157    271    290       C  
ATOM   5488  O   PRO C  52       6.273  10.861  40.247  1.00 23.98           O  
ANISOU 5488  O   PRO C  52     3242   2866   3004   -157    247    282       O  
ATOM   5489  CB  PRO C  52       7.103   8.277  41.901  1.00 25.90           C  
ANISOU 5489  CB  PRO C  52     3519   3086   3235   -141    289    359       C  
ATOM   5490  CG  PRO C  52       7.005   6.903  41.318  1.00 23.09           C  
ANISOU 5490  CG  PRO C  52     3157   2698   2917   -136    307    367       C  
ATOM   5491  CD  PRO C  52       5.554   6.508  41.564  1.00 27.01           C  
ANISOU 5491  CD  PRO C  52     3651   3169   3442   -151    346    351       C  
ATOM   5492  N   GLN C  53       5.483   9.095  39.100  1.00 22.90           N  
ANISOU 5492  N   GLN C  53     3086   2685   2930   -157    273    272       N  
ATOM   5493  CA  GLN C  53       5.556   9.781  37.816  1.00 26.46           C  
ANISOU 5493  CA  GLN C  53     3517   3143   3393   -154    247    245       C  
ATOM   5494  C   GLN C  53       4.593  10.965  37.749  1.00 27.72           C  
ANISOU 5494  C   GLN C  53     3668   3312   3552   -163    245    215       C  
ATOM   5495  O   GLN C  53       4.620  11.739  36.798  1.00 27.75           O  
ANISOU 5495  O   GLN C  53     3659   3325   3561   -160    223    194       O  
ATOM   5496  CB  GLN C  53       5.302   8.811  36.660  1.00 25.79           C  
ANISOU 5496  CB  GLN C  53     3413   3037   3349   -151    251    231       C  
ATOM   5497  CG  GLN C  53       3.900   8.246  36.619  1.00 42.77           C  
ANISOU 5497  CG  GLN C  53     5552   5164   5534   -162    283    208       C  
ATOM   5498  CD  GLN C  53       3.776   6.938  37.374  1.00 30.43           C  
ANISOU 5498  CD  GLN C  53     4001   3578   3986   -165    317    231       C  
ATOM   5499  OE1 GLN C  53       2.972   6.083  37.020  1.00 33.60           O  
ANISOU 5499  OE1 GLN C  53     4388   3953   4424   -171    342    215       O  
ATOM   5500  NE2 GLN C  53       4.574   6.779  38.418  1.00 36.58           N  
ANISOU 5500  NE2 GLN C  53     4803   4362   4733   -159    320    269       N  
ATOM   5501  N   LYS C  54       3.746  11.105  38.764  1.00 28.25           N  
ANISOU 5501  N   LYS C  54     3745   3376   3614   -175    269    213       N  
ATOM   5502  CA  LYS C  54       2.831  12.241  38.823  1.00 28.65           C  
ANISOU 5502  CA  LYS C  54     3788   3434   3664   -184    269    186       C  
ATOM   5503  C   LYS C  54       3.618  13.547  38.894  1.00 29.06           C  
ANISOU 5503  C   LYS C  54     3845   3513   3684   -180    242    187       C  
ATOM   5504  O   LYS C  54       3.118  14.605  38.522  1.00 26.18           O  
ANISOU 5504  O   LYS C  54     3471   3156   3322   -183    233    163       O  
ATOM   5505  CB  LYS C  54       1.911  12.132  40.036  1.00 30.34           C  
ANISOU 5505  CB  LYS C  54     4013   3640   3875   -198    302    187       C  
ATOM   5506  CG  LYS C  54       0.696  11.248  39.844  1.00 38.51           C  
ANISOU 5506  CG  LYS C  54     5035   4647   4949   -206    333    170       C  
ATOM   5507  CD  LYS C  54       0.053  10.929  41.192  1.00 37.41           C  
ANISOU 5507  CD  LYS C  54     4913   4499   4802   -218    368    182       C  
ATOM   5508  CE  LYS C  54      -1.462  11.067  41.136  1.00 46.49           C  
ANISOU 5508  CE  LYS C  54     6048   5634   5982   -232    392    147       C  
ATOM   5509  NZ  LYS C  54      -2.080  10.258  40.049  1.00 58.56           N  
ANISOU 5509  NZ  LYS C  54     7552   7140   7557   -231    400    123       N  
ATOM   5510  N   TYR C  55       4.848  13.472  39.388  1.00 24.70           N  
ANISOU 5510  N   TYR C  55     3307   2974   3102   -173    229    214       N  
ATOM   5511  CA  TYR C  55       5.644  14.678  39.541  1.00 20.94           C  
ANISOU 5511  CA  TYR C  55     2836   2524   2597   -171    205    214       C  
ATOM   5512  C   TYR C  55       7.154  14.482  39.436  1.00 21.85           C  
ANISOU 5512  C   TYR C  55     2957   2652   2692   -159    183    237       C  
ATOM   5513  O   TYR C  55       7.878  15.450  39.225  1.00 26.15           O  
ANISOU 5513  O   TYR C  55     3500   3215   3220   -156    161    231       O  
ATOM   5514  CB  TYR C  55       5.301  15.397  40.850  1.00 23.59           C  
ANISOU 5514  CB  TYR C  55     3185   2873   2906   -182    218    214       C  
ATOM   5515  CG  TYR C  55       5.941  14.804  42.090  1.00 23.05           C  
ANISOU 5515  CG  TYR C  55     3136   2814   2807   -181    227    246       C  
ATOM   5516  CD1 TYR C  55       7.163  15.277  42.551  1.00 21.48           C  
ANISOU 5516  CD1 TYR C  55     2947   2642   2574   -175    206    260       C  
ATOM   5517  CD2 TYR C  55       5.313  13.785  42.807  1.00 27.63           C  
ANISOU 5517  CD2 TYR C  55     3727   3379   3394   -185    257    260       C  
ATOM   5518  CE1 TYR C  55       7.755  14.752  43.685  1.00 28.12           C  
ANISOU 5518  CE1 TYR C  55     3805   3496   3384   -171    212    288       C  
ATOM   5519  CE2 TYR C  55       5.900  13.248  43.965  1.00 24.76           C  
ANISOU 5519  CE2 TYR C  55     3383   3025   2998   -180    265    292       C  
ATOM   5520  CZ  TYR C  55       7.121  13.736  44.392  1.00 30.67           C  
ANISOU 5520  CZ  TYR C  55     4139   3803   3710   -172    241    306       C  
ATOM   5521  OH  TYR C  55       7.730  13.232  45.521  1.00 38.46           O  
ANISOU 5521  OH  TYR C  55     5145   4805   4663   -165    247    337       O  
ATOM   5522  N   LYS C  56       7.641  13.255  39.603  1.00 21.16           N  
ANISOU 5522  N   LYS C  56     2877   2556   2607   -152    189    262       N  
ATOM   5523  CA  LYS C  56       9.072  13.007  39.435  1.00 21.00           C  
ANISOU 5523  CA  LYS C  56     2861   2547   2571   -139    167    282       C  
ATOM   5524  C   LYS C  56       9.382  12.920  37.944  1.00 24.29           C  
ANISOU 5524  C   LYS C  56     3260   2955   3012   -132    149    269       C  
ATOM   5525  O   LYS C  56       8.952  11.977  37.258  1.00 20.39           O  
ANISOU 5525  O   LYS C  56     2758   2441   2550   -130    159    266       O  
ATOM   5526  CB  LYS C  56       9.505  11.746  40.181  1.00 23.34           C  
ANISOU 5526  CB  LYS C  56     3171   2837   2861   -132    180    316       C  
ATOM   5527  CG  LYS C  56       9.295  11.835  41.690  1.00 29.01           C  
ANISOU 5527  CG  LYS C  56     3907   3567   3547   -137    197    332       C  
ATOM   5528  CD  LYS C  56      10.199  10.865  42.437  1.00 36.37           C  
ANISOU 5528  CD  LYS C  56     4855   4504   4459   -123    199    370       C  
ATOM   5529  CE  LYS C  56      10.040  11.007  43.937  1.00 41.64           C  
ANISOU 5529  CE  LYS C  56     5542   5189   5091   -126    214    387       C  
ATOM   5530  NZ  LYS C  56      11.005  10.118  44.649  1.00 56.81           N  
ANISOU 5530  NZ  LYS C  56     7478   7119   6989   -109    212    426       N  
ATOM   5531  N   PRO C  57      10.130  13.913  37.429  1.00 24.94           N  
ANISOU 5531  N   PRO C  57     3339   3055   3083   -129    124    259       N  
ATOM   5532  CA  PRO C  57      10.277  14.094  35.970  1.00 26.21           C  
ANISOU 5532  CA  PRO C  57     3483   3209   3265   -122    108    243       C  
ATOM   5533  C   PRO C  57      11.169  13.060  35.271  1.00 23.01           C  
ANISOU 5533  C   PRO C  57     3074   2797   2872   -111     98    257       C  
ATOM   5534  O   PRO C  57      11.095  12.923  34.047  1.00 25.39           O  
ANISOU 5534  O   PRO C  57     3362   3090   3196   -107     91    242       O  
ATOM   5535  CB  PRO C  57      10.879  15.505  35.842  1.00 15.41           C  
ANISOU 5535  CB  PRO C  57     2115   1862   1877   -122     89    232       C  
ATOM   5536  CG  PRO C  57      11.641  15.690  37.141  1.00 27.85           C  
ANISOU 5536  CG  PRO C  57     3705   3456   3419   -124     87    250       C  
ATOM   5537  CD  PRO C  57      10.806  14.973  38.196  1.00 22.01           C  
ANISOU 5537  CD  PRO C  57     2976   2709   2678   -131    112    262       C  
ATOM   5538  N   PHE C  58      11.984  12.323  36.017  1.00 23.80           N  
ANISOU 5538  N   PHE C  58     3186   2900   2958   -106     99    284       N  
ATOM   5539  CA  PHE C  58      12.851  11.343  35.374  1.00 26.10           C  
ANISOU 5539  CA  PHE C  58     3473   3183   3263    -95     91    298       C  
ATOM   5540  C   PHE C  58      12.273   9.920  35.290  1.00 33.60           C  
ANISOU 5540  C   PHE C  58     4420   4106   4241    -95    114    306       C  
ATOM   5541  O   PHE C  58      12.926   9.022  34.767  1.00 27.25           O  
ANISOU 5541  O   PHE C  58     3611   3291   3450    -86    110    317       O  
ATOM   5542  CB  PHE C  58      14.229  11.325  36.039  1.00 30.58           C  
ANISOU 5542  CB  PHE C  58     4050   3767   3800    -87     76    322       C  
ATOM   5543  CG  PHE C  58      15.067  12.528  35.706  1.00 31.70           C  
ANISOU 5543  CG  PHE C  58     4188   3931   3925    -86     51    310       C  
ATOM   5544  CD1 PHE C  58      15.507  12.737  34.409  1.00 35.34           C  
ANISOU 5544  CD1 PHE C  58     4638   4389   4402    -81     36    296       C  
ATOM   5545  CD2 PHE C  58      15.404  13.448  36.681  1.00 26.61           C  
ANISOU 5545  CD2 PHE C  58     3552   3309   3248    -89     45    311       C  
ATOM   5546  CE1 PHE C  58      16.282  13.848  34.091  1.00 27.28           C  
ANISOU 5546  CE1 PHE C  58     3614   3384   3367    -81     17    285       C  
ATOM   5547  CE2 PHE C  58      16.171  14.555  36.373  1.00 24.83           C  
ANISOU 5547  CE2 PHE C  58     3323   3102   3010    -90     26    298       C  
ATOM   5548  CZ  PHE C  58      16.609  14.753  35.075  1.00 25.36           C  
ANISOU 5548  CZ  PHE C  58     3378   3162   3094    -85     13    286       C  
ATOM   5549  N   ILE C  59      11.060   9.715  35.799  1.00 26.11           N  
ANISOU 5549  N   ILE C  59     3474   3145   3302   -104    139    300       N  
ATOM   5550  CA  ILE C  59      10.477   8.371  35.816  1.00 28.02           C  
ANISOU 5550  CA  ILE C  59     3713   3359   3573   -105    166    307       C  
ATOM   5551  C   ILE C  59       9.671   8.066  34.561  1.00 24.26           C  
ANISOU 5551  C   ILE C  59     3216   2867   3135   -109    170    277       C  
ATOM   5552  O   ILE C  59       8.678   8.724  34.282  1.00 29.76           O  
ANISOU 5552  O   ILE C  59     3903   3565   3839   -117    173    250       O  
ATOM   5553  CB  ILE C  59       9.609   8.147  37.059  1.00 31.62           C  
ANISOU 5553  CB  ILE C  59     4182   3808   4022   -113    195    318       C  
ATOM   5554  CG1 ILE C  59      10.469   8.307  38.317  1.00 25.72           C  
ANISOU 5554  CG1 ILE C  59     3456   3080   3234   -107    190    350       C  
ATOM   5555  CG2 ILE C  59       8.935   6.761  36.987  1.00 30.29           C  
ANISOU 5555  CG2 ILE C  59     4011   3609   3890   -115    227    322       C  
ATOM   5556  CD1 ILE C  59       9.798   7.900  39.584  1.00 34.69           C  
ANISOU 5556  CD1 ILE C  59     4609   4210   4360   -112    220    367       C  
ATOM   5557  N   SER C  60      10.112   7.073  33.797  1.00 26.82           N  
ANISOU 5557  N   SER C  60     3531   3177   3484   -103    170    280       N  
ATOM   5558  CA  SER C  60       9.397   6.707  32.584  1.00 30.11           C  
ANISOU 5558  CA  SER C  60     3926   3580   3937   -106    175    249       C  
ATOM   5559  C   SER C  60       8.334   5.677  32.901  1.00 35.48           C  
ANISOU 5559  C   SER C  60     4600   4233   4647   -114    210    244       C  
ATOM   5560  O   SER C  60       7.312   5.614  32.229  1.00 31.07           O  
ANISOU 5560  O   SER C  60     4024   3666   4116   -121    219    212       O  
ATOM   5561  CB  SER C  60      10.340   6.162  31.524  1.00 29.51           C  
ANISOU 5561  CB  SER C  60     3838   3500   3873    -96    159    250       C  
ATOM   5562  OG  SER C  60      10.913   4.954  31.952  1.00 40.27           O  
ANISOU 5562  OG  SER C  60     5207   4846   5246    -92    173    277       O  
ATOM   5563  N   ARG C  61       8.570   4.858  33.917  1.00 29.14           N  
ANISOU 5563  N   ARG C  61     3814   3416   3842   -113    232    275       N  
ATOM   5564  CA  ARG C  61       7.618   3.812  34.264  1.00 42.67           C  
ANISOU 5564  CA  ARG C  61     5525   5100   5587   -121    271    273       C  
ATOM   5565  C   ARG C  61       7.742   3.390  35.719  1.00 39.59           C  
ANISOU 5565  C   ARG C  61     5160   4704   5179   -119    294    311       C  
ATOM   5566  O   ARG C  61       8.838   3.360  36.274  1.00 37.58           O  
ANISOU 5566  O   ARG C  61     4922   4461   4896   -108    281    344       O  
ATOM   5567  CB  ARG C  61       7.804   2.600  33.348  1.00 38.28           C  
ANISOU 5567  CB  ARG C  61     4952   4521   5070   -118    281    266       C  
ATOM   5568  CG  ARG C  61       6.867   1.447  33.647  1.00 57.45           C  
ANISOU 5568  CG  ARG C  61     7376   6916   7537   -127    324    262       C  
ATOM   5569  CD  ARG C  61       7.509   0.109  33.323  1.00 60.99           C  
ANISOU 5569  CD  ARG C  61     7821   7339   8014   -120    339    278       C  
ATOM   5570  NE  ARG C  61       7.515  -0.159  31.890  1.00 71.27           N  
ANISOU 5570  NE  ARG C  61     9094   8638   9345   -121    327    244       N  
ATOM   5571  CZ  ARG C  61       6.801  -1.114  31.305  1.00 82.77           C  
ANISOU 5571  CZ  ARG C  61    10530  10069  10849   -130    354    218       C  
ATOM   5572  NH1 ARG C  61       6.017  -1.898  32.033  1.00 85.40           N  
ANISOU 5572  NH1 ARG C  61    10868  10374  11207   -138    397    223       N  
ATOM   5573  NH2 ARG C  61       6.870  -1.286  29.992  1.00 73.39           N  
ANISOU 5573  NH2 ARG C  61     9317   8884   9683   -130    340    186       N  
ATOM   5574  N   CYS C  62       6.615   3.060  36.336  1.00 32.14           N  
ANISOU 5574  N   CYS C  62     4220   3743   4251   -130    328    305       N  
ATOM   5575  CA  CYS C  62       6.638   2.585  37.717  1.00 27.03           C  
ANISOU 5575  CA  CYS C  62     3597   3086   3587   -129    355    341       C  
ATOM   5576  C   CYS C  62       5.634   1.453  37.944  1.00 34.18           C  
ANISOU 5576  C   CYS C  62     4500   3955   4533   -138    402    338       C  
ATOM   5577  O   CYS C  62       4.447   1.591  37.667  1.00 29.30           O  
ANISOU 5577  O   CYS C  62     3867   3327   3939   -152    419    303       O  
ATOM   5578  CB  CYS C  62       6.360   3.734  38.683  1.00 32.60           C  
ANISOU 5578  CB  CYS C  62     4317   3816   4252   -134    348    344       C  
ATOM   5579  SG  CYS C  62       6.402   3.250  40.416  1.00 33.38           S  
ANISOU 5579  SG  CYS C  62     4448   3911   4323   -130    379    389       S  
ATOM   5580  N   VAL C  63       6.122   0.333  38.463  1.00 32.47           N  
ANISOU 5580  N   VAL C  63     4297   3718   4324   -128    426    373       N  
ATOM   5581  CA  VAL C  63       5.288  -0.844  38.679  1.00 29.51           C  
ANISOU 5581  CA  VAL C  63     3920   3303   3990   -136    475    374       C  
ATOM   5582  C   VAL C  63       5.355  -1.258  40.145  1.00 34.19           C  
ANISOU 5582  C   VAL C  63     4543   3888   4559   -130    504    419       C  
ATOM   5583  O   VAL C  63       6.444  -1.433  40.703  1.00 32.01           O  
ANISOU 5583  O   VAL C  63     4286   3624   4253   -112    492    460       O  
ATOM   5584  CB  VAL C  63       5.773  -2.015  37.813  1.00 33.92           C  
ANISOU 5584  CB  VAL C  63     4463   3835   4588   -129    483    375       C  
ATOM   5585  CG1 VAL C  63       5.100  -3.306  38.246  1.00 43.68           C  
ANISOU 5585  CG1 VAL C  63     5703   5029   5866   -135    539    385       C  
ATOM   5586  CG2 VAL C  63       5.524  -1.729  36.340  1.00 35.89           C  
ANISOU 5586  CG2 VAL C  63     4681   4091   4866   -137    461    326       C  
ATOM   5587  N   VAL C  64       4.180  -1.424  40.743  1.00 36.42           N  
ANISOU 5587  N   VAL C  64     4829   4152   4857   -144    543    409       N  
ATOM   5588  CA  VAL C  64       4.046  -1.900  42.112  1.00 44.59           C  
ANISOU 5588  CA  VAL C  64     5893   5174   5874   -139    579    450       C  
ATOM   5589  C   VAL C  64       3.280  -3.219  42.130  1.00 46.44           C  
ANISOU 5589  C   VAL C  64     6124   5361   6162   -146    635    449       C  
ATOM   5590  O   VAL C  64       2.127  -3.279  41.710  1.00 46.87           O  
ANISOU 5590  O   VAL C  64     6159   5396   6254   -165    658    408       O  
ATOM   5591  CB  VAL C  64       3.284  -0.891  42.985  1.00 44.46           C  
ANISOU 5591  CB  VAL C  64     5889   5178   5827   -151    582    441       C  
ATOM   5592  CG1 VAL C  64       2.982  -1.492  44.343  1.00 54.66           C  
ANISOU 5592  CG1 VAL C  64     7209   6453   7105   -148    627    479       C  
ATOM   5593  CG2 VAL C  64       4.072   0.395  43.127  1.00 41.43           C  
ANISOU 5593  CG2 VAL C  64     5511   4841   5391   -144    532    444       C  
ATOM   5594  N   GLN C  65       3.922  -4.275  42.615  1.00 91.96           N  
ANISOU 5594  N   GLN C  65    11907  11105  11930   -131    658    494       N  
ATOM   5595  CA  GLN C  65       3.278  -5.581  42.689  1.00 92.29           C  
ANISOU 5595  CA  GLN C  65    11946  11096  12023   -136    716    498       C  
ATOM   5596  C   GLN C  65       2.697  -5.821  44.075  1.00 94.03           C  
ANISOU 5596  C   GLN C  65    12196  11303  12227   -137    760    530       C  
ATOM   5597  O   GLN C  65       3.396  -5.709  45.079  1.00 95.36           O  
ANISOU 5597  O   GLN C  65    12395  11491  12348   -119    754    577       O  
ATOM   5598  CB  GLN C  65       4.266  -6.692  42.331  1.00 82.14           C  
ANISOU 5598  CB  GLN C  65    10662   9790  10759   -118    721    529       C  
ATOM   5599  CG  GLN C  65       4.783  -6.630  40.903  1.00 80.65           C  
ANISOU 5599  CG  GLN C  65    10442   9608  10592   -119    685    496       C  
ATOM   5600  CD  GLN C  65       6.041  -7.449  40.704  1.00 80.73           C  
ANISOU 5600  CD  GLN C  65    10458   9610  10606    -97    677    533       C  
ATOM   5601  OE1 GLN C  65       7.129  -6.904  40.520  1.00 80.85           O  
ANISOU 5601  OE1 GLN C  65    10476   9658  10586    -82    631    547       O  
ATOM   5602  NE2 GLN C  65       5.900  -8.768  40.744  1.00 80.74           N  
ANISOU 5602  NE2 GLN C  65    10460   9566  10653    -94    725    548       N  
ATOM   5603  N   GLY C  66       1.411  -6.150  44.125  1.00 89.85           N  
ANISOU 5603  N   GLY C  66    11657  10743  11738   -157    805    501       N  
ATOM   5604  CA  GLY C  66       0.738  -6.391  45.388  1.00 91.51           C  
ANISOU 5604  CA  GLY C  66    11895  10938  11938   -161    853    526       C  
ATOM   5605  C   GLY C  66       0.222  -5.107  46.006  1.00 91.83           C  
ANISOU 5605  C   GLY C  66    11942  11013  11935   -172    834    512       C  
ATOM   5606  O   GLY C  66      -0.011  -4.126  45.301  1.00 90.59           O  
ANISOU 5606  O   GLY C  66    11764  10882  11775   -183    796    469       O  
ATOM   5607  N   LYS C  67       0.041  -5.112  47.323  1.00111.78           N  
ANISOU 5607  N   LYS C  67    14501  13541  14429   -168    862    547       N  
ATOM   5608  CA  LYS C  67      -0.429  -3.924  48.024  1.00112.33           C  
ANISOU 5608  CA  LYS C  67    14580  13644  14456   -178    848    536       C  
ATOM   5609  C   LYS C  67       0.306  -2.704  47.488  1.00111.07           C  
ANISOU 5609  C   LYS C  67    14410  13533  14260   -173    781    519       C  
ATOM   5610  O   LYS C  67       1.536  -2.649  47.502  1.00110.59           O  
ANISOU 5610  O   LYS C  67    14359  13496  14166   -152    747    550       O  
ATOM   5611  CB  LYS C  67      -0.226  -4.058  49.534  1.00104.66           C  
ANISOU 5611  CB  LYS C  67    13649  12680  13437   -165    873    589       C  
ATOM   5612  CG  LYS C  67       0.997  -4.862  49.935  1.00105.78           C  
ANISOU 5612  CG  LYS C  67    13814  12822  13556   -135    872    649       C  
ATOM   5613  CD  LYS C  67       1.000  -5.152  51.428  1.00108.48           C  
ANISOU 5613  CD  LYS C  67    14195  13165  13857   -122    907    701       C  
ATOM   5614  CE  LYS C  67      -0.209  -5.981  51.835  1.00109.40           C  
ANISOU 5614  CE  LYS C  67    14318  13232  14016   -138    978    699       C  
ATOM   5615  NZ  LYS C  67      -0.166  -6.366  53.272  1.00110.73           N  
ANISOU 5615  NZ  LYS C  67    14527  13400  14145   -123   1016    754       N  
ATOM   5616  N   LYS C  68      -0.456  -1.733  47.003  1.00 75.64           N  
ANISOU 5616  N   LYS C  68     9901   9060   9780   -192    763    469       N  
ATOM   5617  CA  LYS C  68       0.125  -0.575  46.341  1.00 73.46           C  
ANISOU 5617  CA  LYS C  68     9610   8823   9477   -190    703    447       C  
ATOM   5618  C   LYS C  68       0.548   0.520  47.310  1.00 64.67           C  
ANISOU 5618  C   LYS C  68     8518   7753   8300   -185    678    465       C  
ATOM   5619  O   LYS C  68       1.596   1.134  47.135  1.00 57.93           O  
ANISOU 5619  O   LYS C  68     7666   6933   7412   -172    632    475       O  
ATOM   5620  CB  LYS C  68      -0.847  -0.016  45.301  1.00 76.40           C  
ANISOU 5620  CB  LYS C  68     9948   9192   9887   -209    694    386       C  
ATOM   5621  CG  LYS C  68      -1.165  -0.984  44.176  1.00 66.79           C  
ANISOU 5621  CG  LYS C  68     8705   7941   8732   -214    710    361       C  
ATOM   5622  CD  LYS C  68      -0.581  -0.509  42.860  1.00 64.97           C  
ANISOU 5622  CD  LYS C  68     8449   7730   8506   -209    660    335       C  
ATOM   5623  CE  LYS C  68      -1.135  -1.309  41.695  1.00 70.60           C  
ANISOU 5623  CE  LYS C  68     9130   8414   9281   -217    675    297       C  
ATOM   5624  NZ  LYS C  68      -1.368  -2.731  42.067  1.00 70.82           N  
ANISOU 5624  NZ  LYS C  68     9165   8397   9346   -218    730    317       N  
ATOM   5625  N   LEU C  69      -0.267   0.765  48.329  1.00 63.69           N  
ANISOU 5625  N   LEU C  69     8409   7627   8161   -196    708    467       N  
ATOM   5626  CA  LEU C  69      -0.002   1.866  49.247  1.00 52.85           C  
ANISOU 5626  CA  LEU C  69     7054   6296   6730   -195    687    477       C  
ATOM   5627  C   LEU C  69      -0.040   1.478  50.721  1.00 52.24           C  
ANISOU 5627  C   LEU C  69     7012   6219   6618   -189    722    520       C  
ATOM   5628  O   LEU C  69      -1.066   1.617  51.380  1.00 58.90           O  
ANISOU 5628  O   LEU C  69     7862   7053   7465   -205    757    509       O  
ATOM   5629  CB  LEU C  69      -0.978   3.014  48.987  1.00 52.95           C  
ANISOU 5629  CB  LEU C  69     7048   6320   6750   -217    677    426       C  
ATOM   5630  CG  LEU C  69      -0.393   4.214  48.242  1.00 51.70           C  
ANISOU 5630  CG  LEU C  69     6873   6197   6574   -215    621    402       C  
ATOM   5631  CD1 LEU C  69      -1.258   5.448  48.439  1.00 38.38           C  
ANISOU 5631  CD1 LEU C  69     5178   4527   4879   -233    616    365       C  
ATOM   5632  CD2 LEU C  69       1.026   4.470  48.704  1.00 41.49           C  
ANISOU 5632  CD2 LEU C  69     5598   4938   5228   -195    587    439       C  
ATOM   5633  N   GLU C  70       1.091   1.010  51.235  1.00 45.88           N  
ANISOU 5633  N   GLU C  70     6227   5427   5777   -165    713    569       N  
ATOM   5634  CA  GLU C  70       1.227   0.741  52.660  1.00 48.41           C  
ANISOU 5634  CA  GLU C  70     6583   5758   6053   -154    739    613       C  
ATOM   5635  C   GLU C  70       2.661   0.342  52.991  1.00 46.25           C  
ANISOU 5635  C   GLU C  70     6327   5507   5741   -123    714    663       C  
ATOM   5636  O   GLU C  70       3.374  -0.189  52.143  1.00 41.63           O  
ANISOU 5636  O   GLU C  70     5729   4911   5178   -111    696    669       O  
ATOM   5637  CB  GLU C  70       0.240  -0.339  53.108  1.00 51.18           C  
ANISOU 5637  CB  GLU C  70     6945   6061   6439   -161    805    626       C  
ATOM   5638  CG  GLU C  70       0.711  -1.764  52.890  1.00 53.36           C  
ANISOU 5638  CG  GLU C  70     7228   6301   6744   -143    830    663       C  
ATOM   5639  CD  GLU C  70      -0.188  -2.779  53.571  1.00 70.99           C  
ANISOU 5639  CD  GLU C  70     9479   8490   9004   -148    900    683       C  
ATOM   5640  OE1 GLU C  70       0.331  -3.617  54.337  1.00 73.92           O  
ANISOU 5640  OE1 GLU C  70     9879   8854   9355   -126    925    738       O  
ATOM   5641  OE2 GLU C  70      -1.415  -2.735  53.342  1.00 58.67           O  
ANISOU 5641  OE2 GLU C  70     7905   6903   7485   -173    932    643       O  
ATOM   5642  N   VAL C  71       3.084   0.610  54.221  1.00 45.84           N  
ANISOU 5642  N   VAL C  71     6302   5488   5629   -110    713    697       N  
ATOM   5643  CA  VAL C  71       4.448   0.318  54.631  1.00 44.33           C  
ANISOU 5643  CA  VAL C  71     6126   5325   5394    -80    687    743       C  
ATOM   5644  C   VAL C  71       4.851  -1.081  54.200  1.00 50.21           C  
ANISOU 5644  C   VAL C  71     6873   6030   6174    -61    708    776       C  
ATOM   5645  O   VAL C  71       4.155  -2.054  54.487  1.00 50.35           O  
ANISOU 5645  O   VAL C  71     6903   6007   6222    -63    762    794       O  
ATOM   5646  CB  VAL C  71       4.642   0.492  56.142  1.00 45.98           C  
ANISOU 5646  CB  VAL C  71     6367   5566   5537    -67    698    780       C  
ATOM   5647  CG1 VAL C  71       6.057   0.113  56.537  1.00 42.93           C  
ANISOU 5647  CG1 VAL C  71     5995   5210   5107    -32    671    828       C  
ATOM   5648  CG2 VAL C  71       4.354   1.922  56.534  1.00 36.15           C  
ANISOU 5648  CG2 VAL C  71     5117   4363   4256    -85    673    745       C  
ATOM   5649  N   GLY C  72       5.969  -1.170  53.485  1.00 45.50           N  
ANISOU 5649  N   GLY C  72     6264   5445   5578    -45    668    782       N  
ATOM   5650  CA  GLY C  72       6.425  -2.434  52.946  1.00 41.11           C  
ANISOU 5650  CA  GLY C  72     5706   4853   5060    -29    684    809       C  
ATOM   5651  C   GLY C  72       6.195  -2.559  51.451  1.00 40.19           C  
ANISOU 5651  C   GLY C  72     5557   4709   5006    -44    674    766       C  
ATOM   5652  O   GLY C  72       6.821  -3.389  50.806  1.00 40.35           O  
ANISOU 5652  O   GLY C  72     5570   4708   5054    -31    672    781       O  
ATOM   5653  N   SER C  73       5.299  -1.744  50.898  1.00 37.00           N  
ANISOU 5653  N   SER C  73     5132   4303   4622    -72    668    713       N  
ATOM   5654  CA  SER C  73       5.090  -1.741  49.449  1.00 31.45           C  
ANISOU 5654  CA  SER C  73     4397   3581   3973    -86    654    670       C  
ATOM   5655  C   SER C  73       6.405  -1.518  48.707  1.00 30.41           C  
ANISOU 5655  C   SER C  73     4253   3474   3829    -70    602    673       C  
ATOM   5656  O   SER C  73       7.293  -0.785  49.167  1.00 26.05           O  
ANISOU 5656  O   SER C  73     3708   2964   3224    -57    564    687       O  
ATOM   5657  CB  SER C  73       4.062  -0.681  49.030  1.00 39.50           C  
ANISOU 5657  CB  SER C  73     5396   4607   5004   -113    646    614       C  
ATOM   5658  OG  SER C  73       2.732  -1.132  49.233  1.00 50.48           O  
ANISOU 5658  OG  SER C  73     6786   5961   6431   -132    697    598       O  
ATOM   5659  N   VAL C  74       6.515  -2.155  47.548  1.00 35.61           N  
ANISOU 5659  N   VAL C  74     4890   4104   4537    -71    601    658       N  
ATOM   5660  CA  VAL C  74       7.726  -2.099  46.754  1.00 34.67           C  
ANISOU 5660  CA  VAL C  74     4758   4002   4415    -56    557    660       C  
ATOM   5661  C   VAL C  74       7.422  -1.631  45.334  1.00 36.15           C  
ANISOU 5661  C   VAL C  74     4913   4185   4640    -73    535    607       C  
ATOM   5662  O   VAL C  74       6.533  -2.176  44.674  1.00 34.37           O  
ANISOU 5662  O   VAL C  74     4670   3923   4465    -88    563    580       O  
ATOM   5663  CB  VAL C  74       8.414  -3.471  46.729  1.00 37.83           C  
ANISOU 5663  CB  VAL C  74     5166   4374   4836    -35    577    701       C  
ATOM   5664  CG1 VAL C  74       9.570  -3.467  45.755  1.00 32.89           C  
ANISOU 5664  CG1 VAL C  74     4523   3759   4215    -23    535    697       C  
ATOM   5665  CG2 VAL C  74       8.899  -3.836  48.129  1.00 40.52           C  
ANISOU 5665  CG2 VAL C  74     5539   4726   5129    -12    592    758       C  
ATOM   5666  N   ARG C  75       8.139  -0.599  44.882  1.00 31.93           N  
ANISOU 5666  N   ARG C  75     4367   3686   4077    -72    485    591       N  
ATOM   5667  CA  ARG C  75       7.941  -0.067  43.539  1.00 27.16           C  
ANISOU 5667  CA  ARG C  75     3734   3083   3502    -85    460    543       C  
ATOM   5668  C   ARG C  75       9.205  -0.233  42.722  1.00 27.15           C  
ANISOU 5668  C   ARG C  75     3723   3091   3503    -70    425    550       C  
ATOM   5669  O   ARG C  75      10.309   0.013  43.212  1.00 27.09           O  
ANISOU 5669  O   ARG C  75     3728   3111   3455    -53    399    579       O  
ATOM   5670  CB  ARG C  75       7.486   1.407  43.559  1.00 29.41           C  
ANISOU 5670  CB  ARG C  75     4014   3399   3763    -99    435    510       C  
ATOM   5671  CG  ARG C  75       8.578   2.439  43.880  1.00 25.32           C  
ANISOU 5671  CG  ARG C  75     3502   2925   3191    -89    391    520       C  
ATOM   5672  CD  ARG C  75       7.993   3.859  44.017  1.00 24.26           C  
ANISOU 5672  CD  ARG C  75     3364   2817   3037   -105    375    487       C  
ATOM   5673  NE  ARG C  75       8.988   4.823  44.476  1.00 28.44           N  
ANISOU 5673  NE  ARG C  75     3902   3388   3517    -96    339    496       N  
ATOM   5674  CZ  ARG C  75       8.703   6.029  44.965  1.00 29.79           C  
ANISOU 5674  CZ  ARG C  75     4075   3585   3659   -107    328    478       C  
ATOM   5675  NH1 ARG C  75       7.444   6.436  45.071  1.00 23.67           N  
ANISOU 5675  NH1 ARG C  75     3296   2800   2898   -125    349    452       N  
ATOM   5676  NH2 ARG C  75       9.680   6.830  45.365  1.00 29.98           N  
ANISOU 5676  NH2 ARG C  75     4104   3647   3641    -99    297    485       N  
ATOM   5677  N   GLU C  76       9.014  -0.673  41.483  1.00 29.92           N  
ANISOU 5677  N   GLU C  76     4050   3419   3899    -76    425    523       N  
ATOM   5678  CA  GLU C  76      10.082  -0.831  40.510  1.00 38.17           C  
ANISOU 5678  CA  GLU C  76     5081   4469   4953    -65    394    521       C  
ATOM   5679  C   GLU C  76      10.011   0.303  39.493  1.00 33.96           C  
ANISOU 5679  C   GLU C  76     4527   3958   4418    -76    358    478       C  
ATOM   5680  O   GLU C  76       9.022   0.469  38.786  1.00 30.59           O  
ANISOU 5680  O   GLU C  76     4082   3519   4022    -92    367    440       O  
ATOM   5681  CB  GLU C  76       9.957  -2.176  39.778  1.00 40.59           C  
ANISOU 5681  CB  GLU C  76     5374   4734   5313    -64    422    520       C  
ATOM   5682  CG  GLU C  76      11.025  -3.219  40.138  1.00 50.12           C  
ANISOU 5682  CG  GLU C  76     6593   5929   6520    -42    429    567       C  
ATOM   5683  CD  GLU C  76      12.441  -2.648  40.166  1.00 56.27           C  
ANISOU 5683  CD  GLU C  76     7377   6744   7258    -24    382    585       C  
ATOM   5684  OE1 GLU C  76      13.081  -2.506  39.093  1.00 60.34           O  
ANISOU 5684  OE1 GLU C  76     7875   7266   7787    -23    354    566       O  
ATOM   5685  OE2 GLU C  76      12.917  -2.339  41.277  1.00 56.25           O  
ANISOU 5685  OE2 GLU C  76     7397   6766   7210    -12    375    618       O  
ATOM   5686  N   VAL C  77      11.080   1.075  39.412  1.00 36.32           N  
ANISOU 5686  N   VAL C  77     4828   4289   4683    -66    318    484       N  
ATOM   5687  CA  VAL C  77      11.070   2.261  38.586  1.00 35.17           C  
ANISOU 5687  CA  VAL C  77     4666   4166   4530    -75    285    448       C  
ATOM   5688  C   VAL C  77      12.044   2.124  37.429  1.00 35.47           C  
ANISOU 5688  C   VAL C  77     4689   4206   4581    -66    257    440       C  
ATOM   5689  O   VAL C  77      13.171   1.681  37.612  1.00 33.86           O  
ANISOU 5689  O   VAL C  77     4492   4007   4366    -51    246    469       O  
ATOM   5690  CB  VAL C  77      11.431   3.495  39.421  1.00 36.30           C  
ANISOU 5690  CB  VAL C  77     4824   4347   4623    -74    262    454       C  
ATOM   5691  CG1 VAL C  77      11.724   4.674  38.522  1.00 33.51           C  
ANISOU 5691  CG1 VAL C  77     4455   4015   4261    -78    227    423       C  
ATOM   5692  CG2 VAL C  77      10.303   3.814  40.418  1.00 36.86           C  
ANISOU 5692  CG2 VAL C  77     4907   4417   4683    -86    288    451       C  
ATOM   5693  N   ASP C  78      11.584   2.476  36.235  1.00 29.96           N  
ANISOU 5693  N   ASP C  78     3970   3506   3908    -76    248    402       N  
ATOM   5694  CA  ASP C  78      12.460   2.645  35.087  1.00 30.15           C  
ANISOU 5694  CA  ASP C  78     3979   3539   3938    -70    218    390       C  
ATOM   5695  C   ASP C  78      12.639   4.131  34.824  1.00 34.09           C  
ANISOU 5695  C   ASP C  78     4475   4069   4408    -73    186    370       C  
ATOM   5696  O   ASP C  78      11.672   4.907  34.880  1.00 26.36           O  
ANISOU 5696  O   ASP C  78     3494   3095   3426    -85    190    347       O  
ATOM   5697  CB  ASP C  78      11.873   1.971  33.854  1.00 41.65           C  
ANISOU 5697  CB  ASP C  78     5413   4972   5442    -77    229    360       C  
ATOM   5698  CG  ASP C  78      12.017   0.473  33.898  1.00 53.07           C  
ANISOU 5698  CG  ASP C  78     6857   6386   6920    -72    257    379       C  
ATOM   5699  OD1 ASP C  78      11.078  -0.198  34.382  1.00 63.87           O  
ANISOU 5699  OD1 ASP C  78     8228   7730   8311    -79    293    380       O  
ATOM   5700  OD2 ASP C  78      13.077  -0.032  33.460  1.00 63.84           O  
ANISOU 5700  OD2 ASP C  78     8218   7748   8290    -60    245    392       O  
ATOM   5701  N   LEU C  79      13.875   4.527  34.537  1.00 22.05           N  
ANISOU 5701  N   LEU C  79     2950   2562   2864    -63    156    378       N  
ATOM   5702  CA  LEU C  79      14.195   5.933  34.402  1.00 29.38           C  
ANISOU 5702  CA  LEU C  79     3879   3519   3763    -66    128    364       C  
ATOM   5703  C   LEU C  79      14.317   6.323  32.936  1.00 31.09           C  
ANISOU 5703  C   LEU C  79     4077   3739   3998    -67    110    335       C  
ATOM   5704  O   LEU C  79      14.609   5.489  32.083  1.00 26.19           O  
ANISOU 5704  O   LEU C  79     3445   3103   3404    -63    111    331       O  
ATOM   5705  CB  LEU C  79      15.496   6.250  35.144  1.00 29.85           C  
ANISOU 5705  CB  LEU C  79     3952   3603   3788    -55    108    390       C  
ATOM   5706  CG  LEU C  79      15.527   5.929  36.643  1.00 31.48           C  
ANISOU 5706  CG  LEU C  79     4178   3815   3969    -50    123    421       C  
ATOM   5707  CD1 LEU C  79      16.933   6.008  37.188  1.00 32.43           C  
ANISOU 5707  CD1 LEU C  79     4307   3958   4059    -35    101    446       C  
ATOM   5708  CD2 LEU C  79      14.616   6.883  37.403  1.00 27.35           C  
ANISOU 5708  CD2 LEU C  79     3663   3304   3424    -62    130    410       C  
ATOM   5709  N   LYS C  80      14.086   7.597  32.652  1.00 31.05           N  
ANISOU 5709  N   LYS C  80     4069   3751   3978    -72     94    314       N  
ATOM   5710  CA  LYS C  80      14.321   8.137  31.317  1.00 26.45           C  
ANISOU 5710  CA  LYS C  80     3471   3174   3404    -70     75    290       C  
ATOM   5711  C   LYS C  80      15.827   8.222  31.045  1.00 30.92           C  
ANISOU 5711  C   LYS C  80     4039   3752   3956    -60     52    303       C  
ATOM   5712  O   LYS C  80      16.638   8.226  31.981  1.00 26.64           O  
ANISOU 5712  O   LYS C  80     3510   3221   3392    -55     46    327       O  
ATOM   5713  CB  LYS C  80      13.643   9.506  31.187  1.00 23.38           C  
ANISOU 5713  CB  LYS C  80     3081   2800   3002    -77     68    267       C  
ATOM   5714  CG  LYS C  80      12.113   9.411  31.243  1.00 28.99           C  
ANISOU 5714  CG  LYS C  80     3786   3499   3731    -86     89    248       C  
ATOM   5715  CD  LYS C  80      11.427  10.766  31.309  1.00 29.11           C  
ANISOU 5715  CD  LYS C  80     3801   3528   3731    -92     84    229       C  
ATOM   5716  CE  LYS C  80       9.906  10.597  31.415  1.00 25.71           C  
ANISOU 5716  CE  LYS C  80     3363   3086   3321   -101    106    210       C  
ATOM   5717  NZ  LYS C  80       9.172  11.877  31.664  1.00 33.88           N  
ANISOU 5717  NZ  LYS C  80     4398   4132   4342   -106    104    194       N  
ATOM   5718  N   SER C  81      16.210   8.287  29.773  1.00 26.52           N  
ANISOU 5718  N   SER C  81     3469   3195   3414    -57     38    287       N  
ATOM   5719  CA  SER C  81      17.630   8.272  29.428  1.00 27.38           C  
ANISOU 5719  CA  SER C  81     3577   3311   3514    -48     18    297       C  
ATOM   5720  C   SER C  81      18.356   9.547  29.867  1.00 23.60           C  
ANISOU 5720  C   SER C  81     3107   2857   3003    -47      0    299       C  
ATOM   5721  O   SER C  81      17.735  10.594  30.068  1.00 20.12           O  
ANISOU 5721  O   SER C  81     2669   2426   2549    -54      0    286       O  
ATOM   5722  CB  SER C  81      17.838   8.017  27.935  1.00 35.75           C  
ANISOU 5722  CB  SER C  81     4622   4365   4598    -45     10    279       C  
ATOM   5723  OG  SER C  81      17.633   9.199  27.195  1.00 36.19           O  
ANISOU 5723  OG  SER C  81     4673   4434   4644    -47     -2    257       O  
ATOM   5724  N   GLY C  82      19.665   9.433  30.070  1.00 31.56           N  
ANISOU 5724  N   GLY C  82     4118   3873   3999    -40    -14    315       N  
ATOM   5725  CA  GLY C  82      20.482  10.584  30.413  1.00 34.91           C  
ANISOU 5725  CA  GLY C  82     4547   4321   4396    -40    -32    313       C  
ATOM   5726  C   GLY C  82      21.080  10.533  31.803  1.00 40.49           C  
ANISOU 5726  C   GLY C  82     5266   5042   5077    -36    -34    336       C  
ATOM   5727  O   GLY C  82      22.066  11.220  32.081  1.00 34.44           O  
ANISOU 5727  O   GLY C  82     4501   4296   4290    -34    -50    336       O  
ATOM   5728  N   LEU C  83      20.479   9.731  32.680  1.00 35.36           N  
ANISOU 5728  N   LEU C  83     4624   4385   4427    -35    -17    354       N  
ATOM   5729  CA  LEU C  83      20.978   9.572  34.038  1.00 27.64           C  
ANISOU 5729  CA  LEU C  83     3659   3422   3422    -29    -18    378       C  
ATOM   5730  C   LEU C  83      22.044   8.497  34.098  1.00 30.90           C  
ANISOU 5730  C   LEU C  83     4070   3831   3839    -15    -25    402       C  
ATOM   5731  O   LEU C  83      22.115   7.641  33.221  1.00 27.35           O  
ANISOU 5731  O   LEU C  83     3612   3361   3419    -11    -21    402       O  
ATOM   5732  CB  LEU C  83      19.835   9.159  34.955  1.00 36.63           C  
ANISOU 5732  CB  LEU C  83     4808   4552   4558    -34      5    389       C  
ATOM   5733  CG  LEU C  83      19.197  10.270  35.780  1.00 38.29           C  
ANISOU 5733  CG  LEU C  83     5026   4780   4743    -44      9    378       C  
ATOM   5734  CD1 LEU C  83      19.462  11.622  35.150  1.00 34.25           C  
ANISOU 5734  CD1 LEU C  83     4506   4282   4224    -51     -8    351       C  
ATOM   5735  CD2 LEU C  83      17.710  10.004  35.911  1.00 37.53           C  
ANISOU 5735  CD2 LEU C  83     4933   4666   4662    -54     34    372       C  
ATOM   5736  N   PRO C  84      22.864   8.513  35.160  1.00 30.46           N  
ANISOU 5736  N   PRO C  84     4022   3797   3755     -6    -35    422       N  
ATOM   5737  CA  PRO C  84      23.802   7.402  35.382  1.00 29.82           C  
ANISOU 5737  CA  PRO C  84     3942   3713   3677     11    -39    449       C  
ATOM   5738  C   PRO C  84      23.112   6.220  36.070  1.00 42.31           C  
ANISOU 5738  C   PRO C  84     5534   5275   5267     18    -14    477       C  
ATOM   5739  O   PRO C  84      23.641   5.665  37.035  1.00 53.09           O  
ANISOU 5739  O   PRO C  84     6908   6650   6612     32    -14    506       O  
ATOM   5740  CB  PRO C  84      24.850   8.015  36.307  1.00 30.20           C  
ANISOU 5740  CB  PRO C  84     3992   3795   3686     19    -60    456       C  
ATOM   5741  CG  PRO C  84      24.106   9.079  37.072  1.00 29.04           C  
ANISOU 5741  CG  PRO C  84     3854   3666   3514      7    -55    444       C  
ATOM   5742  CD  PRO C  84      22.975   9.563  36.190  1.00 23.35           C  
ANISOU 5742  CD  PRO C  84     3129   2926   2816     -9    -43    418       C  
ATOM   5743  N   ALA C  85      21.934   5.854  35.577  1.00 33.25           N  
ANISOU 5743  N   ALA C  85     4385   4101   4146      7      9    467       N  
ATOM   5744  CA  ALA C  85      21.138   4.781  36.162  1.00 37.79           C  
ANISOU 5744  CA  ALA C  85     4970   4654   4735     10     38    489       C  
ATOM   5745  C   ALA C  85      19.969   4.542  35.219  1.00 34.46           C  
ANISOU 5745  C   ALA C  85     4538   4204   4350     -4     58    465       C  
ATOM   5746  O   ALA C  85      19.628   5.417  34.443  1.00 24.57           O  
ANISOU 5746  O   ALA C  85     3276   2957   3101    -15     48    434       O  
ATOM   5747  CB  ALA C  85      20.635   5.186  37.535  1.00 32.08           C  
ANISOU 5747  CB  ALA C  85     4264   3948   3977      8     48    502       C  
ATOM   5748  N   THR C  86      19.364   3.363  35.257  1.00 27.50           N  
ANISOU 5748  N   THR C  86     3658   3294   3496     -3     85    477       N  
ATOM   5749  CA  THR C  86      18.227   3.104  34.380  1.00 28.33           C  
ANISOU 5749  CA  THR C  86     3751   3374   3638    -16    104    451       C  
ATOM   5750  C   THR C  86      17.034   2.545  35.136  1.00 27.92           C  
ANISOU 5750  C   THR C  86     3710   3304   3597    -23    139    459       C  
ATOM   5751  O   THR C  86      15.909   2.572  34.637  1.00 30.46           O  
ANISOU 5751  O   THR C  86     4021   3610   3941    -36    155    433       O  
ATOM   5752  CB  THR C  86      18.581   2.131  33.261  1.00 30.72           C  
ANISOU 5752  CB  THR C  86     4039   3654   3980    -13    107    445       C  
ATOM   5753  OG1 THR C  86      18.849   0.842  33.821  1.00 32.71           O  
ANISOU 5753  OG1 THR C  86     4297   3885   4246     -1    128    477       O  
ATOM   5754  CG2 THR C  86      19.804   2.609  32.507  1.00 34.01           C  
ANISOU 5754  CG2 THR C  86     4447   4088   4389     -6     75    438       C  
ATOM   5755  N   LYS C  87      17.284   2.022  36.330  1.00 25.02           N  
ANISOU 5755  N   LYS C  87     3359   2936   3211    -12    151    495       N  
ATOM   5756  CA  LYS C  87      16.211   1.447  37.148  1.00 31.63           C  
ANISOU 5756  CA  LYS C  87     4208   3754   4056    -17    188    507       C  
ATOM   5757  C   LYS C  87      16.528   1.506  38.633  1.00 32.45           C  
ANISOU 5757  C   LYS C  87     4335   3876   4118     -6    191    543       C  
ATOM   5758  O   LYS C  87      17.682   1.652  39.035  1.00 31.72           O  
ANISOU 5758  O   LYS C  87     4249   3807   3997     10    168    564       O  
ATOM   5759  CB  LYS C  87      15.912   0.000  36.737  1.00 28.32           C  
ANISOU 5759  CB  LYS C  87     3783   3295   3683    -14    219    516       C  
ATOM   5760  CG  LYS C  87      17.127  -0.933  36.753  1.00 36.30           C  
ANISOU 5760  CG  LYS C  87     4795   4298   4698      6    214    548       C  
ATOM   5761  CD  LYS C  87      16.806  -2.260  36.063  1.00 45.50           C  
ANISOU 5761  CD  LYS C  87     5949   5422   5917      5    244    546       C  
ATOM   5762  CE  LYS C  87      17.730  -3.385  36.522  1.00 50.88           C  
ANISOU 5762  CE  LYS C  87     6639   6089   6604     26    254    589       C  
ATOM   5763  NZ  LYS C  87      19.175  -3.061  36.380  1.00 60.42           N  
ANISOU 5763  NZ  LYS C  87     7845   7323   7787     42    216    601       N  
ATOM   5764  N   SER C  88      15.484   1.400  39.442  1.00 26.92           N  
ANISOU 5764  N   SER C  88     3647   3166   3415    -13    221    549       N  
ATOM   5765  CA  SER C  88      15.617   1.510  40.883  1.00 28.64           C  
ANISOU 5765  CA  SER C  88     3888   3402   3591     -4    227    581       C  
ATOM   5766  C   SER C  88      14.497   0.729  41.563  1.00 35.77           C  
ANISOU 5766  C   SER C  88     4804   4277   4510     -9    272    595       C  
ATOM   5767  O   SER C  88      13.369   0.694  41.068  1.00 33.01           O  
ANISOU 5767  O   SER C  88     4444   3905   4193    -27    293    567       O  
ATOM   5768  CB  SER C  88      15.545   2.981  41.299  1.00 33.16           C  
ANISOU 5768  CB  SER C  88     4463   4012   4124    -13    204    561       C  
ATOM   5769  OG  SER C  88      15.896   3.152  42.661  1.00 37.26           O  
ANISOU 5769  OG  SER C  88     5003   4557   4598     -3    203    590       O  
ATOM   5770  N   THR C  89      14.829   0.098  42.683  1.00 30.32           N  
ANISOU 5770  N   THR C  89     4134   3588   3797      8    288    638       N  
ATOM   5771  CA  THR C  89      13.857  -0.579  43.526  1.00 28.24           C  
ANISOU 5771  CA  THR C  89     3888   3302   3541      5    333    657       C  
ATOM   5772  C   THR C  89      13.763   0.184  44.829  1.00 34.67           C  
ANISOU 5772  C   THR C  89     4722   4149   4301      7    329    671       C  
ATOM   5773  O   THR C  89      14.775   0.423  45.496  1.00 34.92           O  
ANISOU 5773  O   THR C  89     4764   4214   4290     25    305    696       O  
ATOM   5774  CB  THR C  89      14.293  -2.009  43.846  1.00 33.15           C  
ANISOU 5774  CB  THR C  89     4520   3896   4179     26    359    701       C  
ATOM   5775  OG1 THR C  89      14.559  -2.702  42.623  1.00 38.57           O  
ANISOU 5775  OG1 THR C  89     5186   4555   4914     25    358    688       O  
ATOM   5776  CG2 THR C  89      13.200  -2.743  44.630  1.00 32.96           C  
ANISOU 5776  CG2 THR C  89     4513   3841   4169     21    411    719       C  
ATOM   5777  N   GLU C  90      12.546   0.568  45.196  1.00 31.49           N  
ANISOU 5777  N   GLU C  90     4324   3740   3901    -12    353    653       N  
ATOM   5778  CA  GLU C  90      12.342   1.357  46.392  1.00 31.67           C  
ANISOU 5778  CA  GLU C  90     4364   3794   3875    -13    352    660       C  
ATOM   5779  C   GLU C  90      11.215   0.762  47.243  1.00 30.55           C  
ANISOU 5779  C   GLU C  90     4241   3628   3740    -20    402    676       C  
ATOM   5780  O   GLU C  90      10.241   0.231  46.721  1.00 29.09           O  
ANISOU 5780  O   GLU C  90     4047   3405   3602    -34    433    658       O  
ATOM   5781  CB  GLU C  90      12.035   2.806  46.002  1.00 28.81           C  
ANISOU 5781  CB  GLU C  90     3988   3457   3501    -33    325    616       C  
ATOM   5782  CG  GLU C  90      13.246   3.506  45.380  1.00 38.67           C  
ANISOU 5782  CG  GLU C  90     5223   4735   4734    -25    277    604       C  
ATOM   5783  CD  GLU C  90      12.895   4.489  44.275  1.00 44.84           C  
ANISOU 5783  CD  GLU C  90     5983   5518   5536    -44    257    557       C  
ATOM   5784  OE1 GLU C  90      11.687   4.729  44.045  1.00 41.04           O  
ANISOU 5784  OE1 GLU C  90     5496   5020   5077    -63    278    531       O  
ATOM   5785  OE2 GLU C  90      13.842   5.022  43.635  1.00 40.09           O  
ANISOU 5785  OE2 GLU C  90     5370   4936   4927    -39    222    546       O  
ATOM   5786  N   VAL C  91      11.368   0.849  48.555  1.00 20.88           N  
ANISOU 5786  N   VAL C  91     3039   2425   2467     -9    409    707       N  
ATOM   5787  CA  VAL C  91      10.356   0.327  49.465  1.00 27.81           C  
ANISOU 5787  CA  VAL C  91     3938   3283   3347    -14    458    725       C  
ATOM   5788  C   VAL C  91       9.821   1.496  50.273  1.00 28.08           C  
ANISOU 5788  C   VAL C  91     3979   3349   3341    -28    453    707       C  
ATOM   5789  O   VAL C  91      10.582   2.383  50.689  1.00 23.54           O  
ANISOU 5789  O   VAL C  91     3406   2819   2718    -21    417    706       O  
ATOM   5790  CB  VAL C  91      10.930  -0.777  50.400  1.00 32.06           C  
ANISOU 5790  CB  VAL C  91     4501   3816   3864     15    480    784       C  
ATOM   5791  CG1 VAL C  91      12.027  -0.212  51.294  1.00 31.75           C  
ANISOU 5791  CG1 VAL C  91     4475   3830   3759     36    445    809       C  
ATOM   5792  CG2 VAL C  91       9.820  -1.416  51.243  1.00 37.05           C  
ANISOU 5792  CG2 VAL C  91     5153   4418   4504      9    536    803       C  
ATOM   5793  N   LEU C  92       8.507   1.523  50.455  1.00 27.61           N  
ANISOU 5793  N   LEU C  92     3921   3266   3302    -49    489    688       N  
ATOM   5794  CA  LEU C  92       7.886   2.531  51.303  1.00 27.24           C  
ANISOU 5794  CA  LEU C  92     3883   3245   3221    -63    492    672       C  
ATOM   5795  C   LEU C  92       8.157   2.201  52.770  1.00 36.62           C  
ANISOU 5795  C   LEU C  92     5103   4454   4358    -46    509    718       C  
ATOM   5796  O   LEU C  92       7.784   1.135  53.251  1.00 36.20           O  
ANISOU 5796  O   LEU C  92     5067   4371   4317    -37    552    751       O  
ATOM   5797  CB  LEU C  92       6.384   2.583  51.036  1.00 29.26           C  
ANISOU 5797  CB  LEU C  92     4130   3468   3518    -90    527    638       C  
ATOM   5798  CG  LEU C  92       5.554   3.542  51.886  1.00 28.39           C  
ANISOU 5798  CG  LEU C  92     4029   3378   3381   -107    538    620       C  
ATOM   5799  CD1 LEU C  92       6.062   4.971  51.769  1.00 27.13           C  
ANISOU 5799  CD1 LEU C  92     3857   3262   3188   -113    491    592       C  
ATOM   5800  CD2 LEU C  92       4.091   3.445  51.476  1.00 37.29           C  
ANISOU 5800  CD2 LEU C  92     5143   4467   4557   -132    573    585       C  
ATOM   5801  N   GLU C  93       8.816   3.116  53.470  1.00 39.21           N  
ANISOU 5801  N   GLU C  93     5437   4832   4629    -39    478    721       N  
ATOM   5802  CA  GLU C  93       9.146   2.909  54.869  1.00 42.30           C  
ANISOU 5802  CA  GLU C  93     5857   5251   4965    -21    489    762       C  
ATOM   5803  C   GLU C  93       8.178   3.638  55.783  1.00 42.75           C  
ANISOU 5803  C   GLU C  93     5925   5322   4997    -40    510    746       C  
ATOM   5804  O   GLU C  93       7.779   3.105  56.814  1.00 47.13           O  
ANISOU 5804  O   GLU C  93     6505   5873   5529    -33    546    778       O  
ATOM   5805  CB  GLU C  93      10.587   3.334  55.174  1.00 40.05           C  
ANISOU 5805  CB  GLU C  93     5571   5016   4628      2    441    777       C  
ATOM   5806  CG  GLU C  93      11.632   2.437  54.526  1.00 48.54           C  
ANISOU 5806  CG  GLU C  93     6642   6080   5722     26    425    804       C  
ATOM   5807  CD  GLU C  93      12.948   2.390  55.295  1.00 54.75           C  
ANISOU 5807  CD  GLU C  93     7439   6912   6451     57    396    840       C  
ATOM   5808  OE1 GLU C  93      13.504   3.463  55.626  1.00 50.67           O  
ANISOU 5808  OE1 GLU C  93     6916   6444   5892     55    359    820       O  
ATOM   5809  OE2 GLU C  93      13.427   1.264  55.561  1.00 53.39           O  
ANISOU 5809  OE2 GLU C  93     7281   6727   6277     84    410    887       O  
ATOM   5810  N   ILE C  94       7.793   4.852  55.404  1.00 37.40           N  
ANISOU 5810  N   ILE C  94     5229   4659   4323    -64    490    697       N  
ATOM   5811  CA  ILE C  94       6.905   5.653  56.239  1.00 33.70           C  
ANISOU 5811  CA  ILE C  94     4768   4205   3831    -83    507    678       C  
ATOM   5812  C   ILE C  94       5.818   6.321  55.407  1.00 38.89           C  
ANISOU 5812  C   ILE C  94     5403   4838   4535   -113    513    626       C  
ATOM   5813  O   ILE C  94       6.102   6.988  54.414  1.00 34.81           O  
ANISOU 5813  O   ILE C  94     4863   4326   4038   -120    480    593       O  
ATOM   5814  CB  ILE C  94       7.684   6.744  56.985  1.00 32.11           C  
ANISOU 5814  CB  ILE C  94     4569   4063   3567    -79    471    672       C  
ATOM   5815  CG1 ILE C  94       8.719   6.121  57.922  1.00 38.80           C  
ANISOU 5815  CG1 ILE C  94     5438   4941   4362    -47    464    723       C  
ATOM   5816  CG2 ILE C  94       6.732   7.663  57.754  1.00 29.94           C  
ANISOU 5816  CG2 ILE C  94     4299   3804   3273   -102    489    645       C  
ATOM   5817  CD1 ILE C  94       9.640   7.141  58.556  1.00 41.09           C  
ANISOU 5817  CD1 ILE C  94     5726   5293   4592    -40    424    714       C  
ATOM   5818  N   LEU C  95       4.569   6.137  55.806  1.00 25.34           N  
ANISOU 5818  N   LEU C  95     3695   3096   2837   -130    557    618       N  
ATOM   5819  CA  LEU C  95       3.481   6.860  55.167  1.00 26.59           C  
ANISOU 5819  CA  LEU C  95     3832   3236   3033   -158    563    567       C  
ATOM   5820  C   LEU C  95       2.562   7.428  56.236  1.00 38.09           C  
ANISOU 5820  C   LEU C  95     5302   4704   4467   -175    591    557       C  
ATOM   5821  O   LEU C  95       1.589   6.783  56.637  1.00 33.44           O  
ANISOU 5821  O   LEU C  95     4723   4084   3897   -184    637    563       O  
ATOM   5822  CB  LEU C  95       2.714   5.931  54.243  1.00 35.72           C  
ANISOU 5822  CB  LEU C  95     4977   4340   4256   -165    591    559       C  
ATOM   5823  CG  LEU C  95       1.368   6.431  53.722  1.00 38.96           C  
ANISOU 5823  CG  LEU C  95     5367   4726   4709   -193    609    510       C  
ATOM   5824  CD1 LEU C  95       1.551   7.613  52.766  1.00 30.54           C  
ANISOU 5824  CD1 LEU C  95     4274   3679   3651   -201    565    468       C  
ATOM   5825  CD2 LEU C  95       0.617   5.269  53.056  1.00 41.35           C  
ANISOU 5825  CD2 LEU C  95     5661   4976   5072   -197    645    508       C  
ATOM   5826  N   ASP C  96       2.872   8.628  56.712  1.00 32.80           N  
ANISOU 5826  N   ASP C  96     4630   4077   3756   -181    564    539       N  
ATOM   5827  CA  ASP C  96       2.113   9.196  57.821  1.00 35.93           C  
ANISOU 5827  CA  ASP C  96     5040   4489   4124   -196    589    530       C  
ATOM   5828  C   ASP C  96       1.072  10.198  57.328  1.00 35.29           C  
ANISOU 5828  C   ASP C  96     4937   4397   4075   -224    591    476       C  
ATOM   5829  O   ASP C  96       1.397  11.328  56.969  1.00 29.47           O  
ANISOU 5829  O   ASP C  96     4182   3684   3330   -231    556    446       O  
ATOM   5830  CB  ASP C  96       3.050   9.826  58.859  1.00 39.15           C  
ANISOU 5830  CB  ASP C  96     5461   4952   4462   -184    564    544       C  
ATOM   5831  CG  ASP C  96       2.341  10.153  60.179  1.00 49.98           C  
ANISOU 5831  CG  ASP C  96     6852   6341   5797   -196    596    545       C  
ATOM   5832  OD1 ASP C  96       3.020  10.222  61.230  1.00 56.86           O  
ANISOU 5832  OD1 ASP C  96     7743   7254   6608   -181    589    571       O  
ATOM   5833  OD2 ASP C  96       1.106  10.344  60.166  1.00 48.39           O  
ANISOU 5833  OD2 ASP C  96     6647   6113   5627   -219    627    519       O  
ATOM   5834  N   ASP C  97      -0.185   9.774  57.310  1.00 27.84           N  
ANISOU 5834  N   ASP C  97     3992   3415   3170   -240    633    464       N  
ATOM   5835  CA  ASP C  97      -1.277  10.654  56.909  1.00 32.70           C  
ANISOU 5835  CA  ASP C  97     4587   4018   3817   -265    639    415       C  
ATOM   5836  C   ASP C  97      -1.716  11.637  58.000  1.00 34.24           C  
ANISOU 5836  C   ASP C  97     4792   4243   3976   -281    649    399       C  
ATOM   5837  O   ASP C  97      -2.559  12.499  57.755  1.00 33.24           O  
ANISOU 5837  O   ASP C  97     4648   4110   3871   -301    651    357       O  
ATOM   5838  CB  ASP C  97      -2.470   9.844  56.408  1.00 35.25           C  
ANISOU 5838  CB  ASP C  97     4904   4291   4200   -277    679    403       C  
ATOM   5839  CG  ASP C  97      -2.251   9.315  55.012  1.00 34.20           C  
ANISOU 5839  CG  ASP C  97     4748   4131   4114   -270    662    395       C  
ATOM   5840  OD1 ASP C  97      -2.283  10.129  54.063  1.00 34.93           O  
ANISOU 5840  OD1 ASP C  97     4816   4229   4228   -276    631    359       O  
ATOM   5841  OD2 ASP C  97      -2.042   8.095  54.853  1.00 31.06           O  
ANISOU 5841  OD2 ASP C  97     4358   3708   3733   -258    680    424       O  
ATOM   5842  N   ASN C  98      -1.134  11.512  59.190  1.00 30.12           N  
ANISOU 5842  N   ASN C  98     4296   3752   3397   -270    653    431       N  
ATOM   5843  CA  ASN C  98      -1.433  12.424  60.294  1.00 39.78           C  
ANISOU 5843  CA  ASN C  98     5528   5007   4579   -283    662    418       C  
ATOM   5844  C   ASN C  98      -0.490  13.613  60.282  1.00 34.81           C  
ANISOU 5844  C   ASN C  98     4888   4424   3915   -281    614    400       C  
ATOM   5845  O   ASN C  98      -0.894  14.745  60.561  1.00 35.68           O  
ANISOU 5845  O   ASN C  98     4988   4552   4017   -299    611    364       O  
ATOM   5846  CB  ASN C  98      -1.290  11.710  61.641  1.00 36.20           C  
ANISOU 5846  CB  ASN C  98     5109   4569   4077   -272    691    461       C  
ATOM   5847  CG  ASN C  98      -2.144  10.476  61.732  1.00 43.57           C  
ANISOU 5847  CG  ASN C  98     6056   5455   5043   -272    742    483       C  
ATOM   5848  OD1 ASN C  98      -3.312  10.487  61.333  1.00 39.29           O  
ANISOU 5848  OD1 ASN C  98     5502   4876   4550   -293    770    453       O  
ATOM   5849  ND2 ASN C  98      -1.569   9.395  62.244  1.00 46.00           N  
ANISOU 5849  ND2 ASN C  98     6389   5762   5326   -249    756    535       N  
ATOM   5850  N   GLU C  99       0.770  13.331  59.968  1.00 42.74           N  
ANISOU 5850  N   GLU C  99     5892   5447   4899   -258    580    424       N  
ATOM   5851  CA  GLU C  99       1.849  14.312  60.028  1.00 46.21           C  
ANISOU 5851  CA  GLU C  99     6323   5933   5303   -253    536    412       C  
ATOM   5852  C   GLU C  99       2.324  14.729  58.633  1.00 44.04           C  
ANISOU 5852  C   GLU C  99     6021   5647   5064   -252    499    389       C  
ATOM   5853  O   GLU C  99       3.120  15.657  58.494  1.00 35.44           O  
ANISOU 5853  O   GLU C  99     4920   4589   3956   -251    464    372       O  
ATOM   5854  CB  GLU C  99       3.034  13.715  60.784  1.00 47.59           C  
ANISOU 5854  CB  GLU C  99     6518   6142   5423   -227    522    456       C  
ATOM   5855  CG  GLU C  99       2.696  13.154  62.152  1.00 58.20           C  
ANISOU 5855  CG  GLU C  99     7891   7498   6724   -222    558    487       C  
ATOM   5856  CD  GLU C  99       2.808  14.198  63.247  1.00 69.89           C  
ANISOU 5856  CD  GLU C  99     9375   9028   8150   -231    552    468       C  
ATOM   5857  OE1 GLU C  99       3.625  13.992  64.173  1.00 75.66           O  
ANISOU 5857  OE1 GLU C  99    10123   9800   8822   -212    543    497       O  
ATOM   5858  OE2 GLU C  99       2.083  15.220  63.179  1.00 55.44           O  
ANISOU 5858  OE2 GLU C  99     7531   7197   6337   -257    557    424       O  
ATOM   5859  N   HIS C 100       1.857  14.015  57.611  1.00 39.51           N  
ANISOU 5859  N   HIS C 100     5438   5029   4544   -251    509    390       N  
ATOM   5860  CA  HIS C 100       2.206  14.317  56.226  1.00 31.82           C  
ANISOU 5860  CA  HIS C 100     4439   4042   3608   -249    478    369       C  
ATOM   5861  C   HIS C 100       3.692  14.136  56.011  1.00 31.58           C  
ANISOU 5861  C   HIS C 100     4410   4037   3551   -227    440    393       C  
ATOM   5862  O   HIS C 100       4.411  15.070  55.628  1.00 29.83           O  
ANISOU 5862  O   HIS C 100     4174   3839   3320   -227    406    373       O  
ATOM   5863  CB  HIS C 100       1.797  15.742  55.869  1.00 32.94           C  
ANISOU 5863  CB  HIS C 100     4561   4193   3762   -268    464    322       C  
ATOM   5864  CG  HIS C 100       0.428  16.109  56.341  1.00 32.17           C  
ANISOU 5864  CG  HIS C 100     4463   4080   3679   -290    498    298       C  
ATOM   5865  ND1 HIS C 100      -0.718  15.636  55.737  1.00 36.27           N  
ANISOU 5865  ND1 HIS C 100     4974   4558   4249   -300    524    285       N  
ATOM   5866  CD2 HIS C 100       0.020  16.891  57.364  1.00 33.94           C  
ANISOU 5866  CD2 HIS C 100     4695   4327   3875   -305    512    283       C  
ATOM   5867  CE1 HIS C 100      -1.774  16.115  56.367  1.00 36.49           C  
ANISOU 5867  CE1 HIS C 100     5003   4582   4280   -319    552    263       C  
ATOM   5868  NE2 HIS C 100      -1.355  16.879  57.358  1.00 40.48           N  
ANISOU 5868  NE2 HIS C 100     5518   5125   4737   -323    546    262       N  
ATOM   5869  N   ILE C 101       4.141  12.920  56.267  1.00 26.75           N  
ANISOU 5869  N   ILE C 101     3815   3419   2930   -208    450    435       N  
ATOM   5870  CA  ILE C 101       5.533  12.550  56.095  1.00 28.20           C  
ANISOU 5870  CA  ILE C 101     4000   3623   3090   -184    418    461       C  
ATOM   5871  C   ILE C 101       5.576  11.301  55.234  1.00 32.50           C  
ANISOU 5871  C   ILE C 101     4544   4129   3677   -171    426    484       C  
ATOM   5872  O   ILE C 101       4.741  10.406  55.387  1.00 35.15           O  
ANISOU 5872  O   ILE C 101     4890   4430   4034   -174    464    498       O  
ATOM   5873  CB  ILE C 101       6.200  12.256  57.442  1.00 32.16           C  
ANISOU 5873  CB  ILE C 101     4526   4162   3531   -168    420    497       C  
ATOM   5874  CG1 ILE C 101       6.196  13.512  58.316  1.00 31.13           C  
ANISOU 5874  CG1 ILE C 101     4395   4075   3359   -181    411    471       C  
ATOM   5875  CG2 ILE C 101       7.629  11.745  57.236  1.00 27.74           C  
ANISOU 5875  CG2 ILE C 101     3967   3622   2951   -141    388    526       C  
ATOM   5876  CD1 ILE C 101       6.601  13.242  59.748  1.00 37.77           C  
ANISOU 5876  CD1 ILE C 101     5260   4954   4137   -167    420    501       C  
ATOM   5877  N   LEU C 102       6.534  11.252  54.314  1.00 24.51           N  
ANISOU 5877  N   LEU C 102     3518   3119   2675   -159    392    485       N  
ATOM   5878  CA  LEU C 102       6.726  10.072  53.481  1.00 32.76           C  
ANISOU 5878  CA  LEU C 102     4561   4130   3758   -146    397    506       C  
ATOM   5879  C   LEU C 102       8.194   9.681  53.463  1.00 33.10           C  
ANISOU 5879  C   LEU C 102     4606   4195   3773   -121    366    536       C  
ATOM   5880  O   LEU C 102       9.058  10.490  53.116  1.00 31.34           O  
ANISOU 5880  O   LEU C 102     4371   4000   3536   -118    329    519       O  
ATOM   5881  CB  LEU C 102       6.243  10.320  52.053  1.00 32.15           C  
ANISOU 5881  CB  LEU C 102     4458   4023   3735   -158    389    471       C  
ATOM   5882  CG  LEU C 102       6.293   9.080  51.154  1.00 41.31           C  
ANISOU 5882  CG  LEU C 102     5614   5146   4938   -148    398    487       C  
ATOM   5883  CD1 LEU C 102       5.004   8.282  51.274  1.00 41.66           C  
ANISOU 5883  CD1 LEU C 102     5662   5149   5016   -159    445    487       C  
ATOM   5884  CD2 LEU C 102       6.558   9.456  49.703  1.00 41.77           C  
ANISOU 5884  CD2 LEU C 102     5646   5195   5031   -151    369    458       C  
ATOM   5885  N   GLY C 103       8.471   8.436  53.834  1.00 27.07           N  
ANISOU 5885  N   GLY C 103     3860   3418   3006   -102    384    579       N  
ATOM   5886  CA  GLY C 103       9.834   7.945  53.902  1.00 23.51           C  
ANISOU 5886  CA  GLY C 103     3414   2989   2531    -75    358    611       C  
ATOM   5887  C   GLY C 103       9.986   6.733  53.017  1.00 32.00           C  
ANISOU 5887  C   GLY C 103     4484   4023   3650    -63    367    631       C  
ATOM   5888  O   GLY C 103       9.126   5.846  52.986  1.00 34.46           O  
ANISOU 5888  O   GLY C 103     4804   4295   3993    -67    406    642       O  
ATOM   5889  N   ILE C 104      11.090   6.711  52.285  1.00 32.50           N  
ANISOU 5889  N   ILE C 104     4535   4096   3717    -50    332    632       N  
ATOM   5890  CA  ILE C 104      11.384   5.644  51.356  1.00 24.00           C  
ANISOU 5890  CA  ILE C 104     3452   2985   2683    -39    336    647       C  
ATOM   5891  C   ILE C 104      12.814   5.160  51.575  1.00 30.56           C  
ANISOU 5891  C   ILE C 104     4287   3838   3485    -10    310    682       C  
ATOM   5892  O   ILE C 104      13.630   5.872  52.154  1.00 29.43           O  
ANISOU 5892  O   ILE C 104     4146   3741   3296     -2    281    682       O  
ATOM   5893  CB  ILE C 104      11.216   6.149  49.909  1.00 37.03           C  
ANISOU 5893  CB  ILE C 104     5075   4618   4377    -55    317    605       C  
ATOM   5894  CG1 ILE C 104       9.899   5.657  49.328  1.00 39.74           C  
ANISOU 5894  CG1 ILE C 104     5411   4915   4772    -72    353    588       C  
ATOM   5895  CG2 ILE C 104      12.398   5.761  49.022  1.00 42.64           C  
ANISOU 5895  CG2 ILE C 104     5773   5328   5100    -39    287    613       C  
ATOM   5896  CD1 ILE C 104       8.867   6.739  49.219  1.00 36.95           C  
ANISOU 5896  CD1 ILE C 104     5049   4565   4427    -97    356    546       C  
ATOM   5897  N   ARG C 105      13.106   3.949  51.107  1.00 34.40           N  
ANISOU 5897  N   ARG C 105     4775   4294   4002      5    322    709       N  
ATOM   5898  CA  ARG C 105      14.474   3.441  51.068  1.00 33.44           C  
ANISOU 5898  CA  ARG C 105     4653   4188   3864     33    296    739       C  
ATOM   5899  C   ARG C 105      14.743   2.762  49.727  1.00 32.10           C  
ANISOU 5899  C   ARG C 105     4465   3982   3748     34    292    732       C  
ATOM   5900  O   ARG C 105      13.895   2.037  49.218  1.00 32.13           O  
ANISOU 5900  O   ARG C 105     4468   3942   3799     25    324    729       O  
ATOM   5901  CB  ARG C 105      14.705   2.451  52.211  1.00 36.31           C  
ANISOU 5901  CB  ARG C 105     5043   4554   4198     58    319    793       C  
ATOM   5902  CG  ARG C 105      15.778   1.406  51.922  1.00 40.48           C  
ANISOU 5902  CG  ARG C 105     5572   5074   4735     87    309    830       C  
ATOM   5903  CD  ARG C 105      16.130   0.625  53.187  1.00 55.01           C  
ANISOU 5903  CD  ARG C 105     7439   6927   6534    117    326    885       C  
ATOM   5904  NE  ARG C 105      16.471   1.532  54.280  1.00 65.17           N  
ANISOU 5904  NE  ARG C 105     8736   8272   7756    122    305    886       N  
ATOM   5905  CZ  ARG C 105      17.711   1.868  54.632  1.00 63.35           C  
ANISOU 5905  CZ  ARG C 105     8501   8088   7481    144    264    895       C  
ATOM   5906  NH1 ARG C 105      18.756   1.354  53.994  1.00 57.07           N  
ANISOU 5906  NH1 ARG C 105     7694   7289   6701    163    241    907       N  
ATOM   5907  NH2 ARG C 105      17.905   2.715  55.635  1.00 60.13           N  
ANISOU 5907  NH2 ARG C 105     8100   7732   7015    145    248    890       N  
ATOM   5908  N   ILE C 106      15.923   2.984  49.159  1.00 30.05           N  
ANISOU 5908  N   ILE C 106     4193   3742   3484     45    253    728       N  
ATOM   5909  CA  ILE C 106      16.285   2.322  47.914  1.00 33.45           C  
ANISOU 5909  CA  ILE C 106     4607   4142   3963     48    248    723       C  
ATOM   5910  C   ILE C 106      16.992   0.998  48.203  1.00 36.43           C  
ANISOU 5910  C   ILE C 106     4994   4505   4342     77    259    772       C  
ATOM   5911  O   ILE C 106      17.952   0.959  48.967  1.00 36.07           O  
ANISOU 5911  O   ILE C 106     4958   4492   4254    100    240    801       O  
ATOM   5912  CB  ILE C 106      17.210   3.191  47.048  1.00 32.45           C  
ANISOU 5912  CB  ILE C 106     4458   4038   3834     45    203    694       C  
ATOM   5913  CG1 ILE C 106      16.539   4.523  46.711  1.00 35.22           C  
ANISOU 5913  CG1 ILE C 106     4797   4400   4183     19    193    647       C  
ATOM   5914  CG2 ILE C 106      17.597   2.436  45.788  1.00 37.84           C  
ANISOU 5914  CG2 ILE C 106     5124   4689   4564     49    199    690       C  
ATOM   5915  CD1 ILE C 106      17.370   5.405  45.793  1.00 39.24           C  
ANISOU 5915  CD1 ILE C 106     5286   4928   4695     15    153    617       C  
ATOM   5916  N   VAL C 107      16.526  -0.077  47.582  1.00 28.63           N  
ANISOU 5916  N   VAL C 107     4003   3469   3405     76    289    780       N  
ATOM   5917  CA  VAL C 107      16.997  -1.416  47.922  1.00 35.67           C  
ANISOU 5917  CA  VAL C 107     4908   4340   4305    102    310    828       C  
ATOM   5918  C   VAL C 107      17.528  -2.186  46.726  1.00 42.41           C  
ANISOU 5918  C   VAL C 107     5743   5163   5208    107    305    825       C  
ATOM   5919  O   VAL C 107      17.928  -3.345  46.860  1.00 44.39           O  
ANISOU 5919  O   VAL C 107     6001   5390   5474    128    323    863       O  
ATOM   5920  CB  VAL C 107      15.874  -2.257  48.579  1.00 40.91           C  
ANISOU 5920  CB  VAL C 107     5592   4968   4985     99    365    852       C  
ATOM   5921  CG1 VAL C 107      15.507  -1.683  49.943  1.00 33.59           C  
ANISOU 5921  CG1 VAL C 107     4687   4073   4003    101    372    866       C  
ATOM   5922  CG2 VAL C 107      14.648  -2.332  47.662  1.00 31.79           C  
ANISOU 5922  CG2 VAL C 107     4421   3771   3886     69    392    812       C  
ATOM   5923  N   GLY C 108      17.522  -1.555  45.556  1.00 32.55           N  
ANISOU 5923  N   GLY C 108     4470   3913   3984     88    282    780       N  
ATOM   5924  CA  GLY C 108      17.944  -2.232  44.343  1.00 40.42           C  
ANISOU 5924  CA  GLY C 108     5448   4881   5028     89    279    771       C  
ATOM   5925  C   GLY C 108      18.054  -1.269  43.183  1.00 37.42           C  
ANISOU 5925  C   GLY C 108     5044   4512   4660     71    246    722       C  
ATOM   5926  O   GLY C 108      17.691  -0.109  43.326  1.00 29.59           O  
ANISOU 5926  O   GLY C 108     4051   3547   3645     56    231    696       O  
ATOM   5927  N   GLY C 109      18.555  -1.751  42.046  1.00 45.93           N  
ANISOU 5927  N   GLY C 109     6104   5572   5776     72    237    711       N  
ATOM   5928  CA  GLY C 109      18.722  -0.925  40.860  1.00 45.15           C  
ANISOU 5928  CA  GLY C 109     5983   5482   5690     57    208    668       C  
ATOM   5929  C   GLY C 109      20.175  -0.770  40.440  1.00 50.19           C  
ANISOU 5929  C   GLY C 109     6612   6142   6318     72    170    672       C  
ATOM   5930  O   GLY C 109      21.079  -1.282  41.101  1.00 49.00           O  
ANISOU 5930  O   GLY C 109     6470   6001   6147     95    164    708       O  
ATOM   5931  N   ASP C 110      20.410  -0.057  39.344  1.00 41.81           N  
ANISOU 5931  N   ASP C 110     5531   5088   5268     60    146    635       N  
ATOM   5932  CA  ASP C 110      21.768   0.071  38.820  1.00 48.67           C  
ANISOU 5932  CA  ASP C 110     6388   5972   6131     72    112    635       C  
ATOM   5933  C   ASP C 110      22.374   1.445  39.057  1.00 47.76           C  
ANISOU 5933  C   ASP C 110     6272   5901   5974     69     77    618       C  
ATOM   5934  O   ASP C 110      23.233   1.896  38.296  1.00 51.45           O  
ANISOU 5934  O   ASP C 110     6725   6380   6444     69     49    600       O  
ATOM   5935  CB  ASP C 110      21.831  -0.291  37.331  1.00 41.88           C  
ANISOU 5935  CB  ASP C 110     5508   5088   5317     63    111    609       C  
ATOM   5936  CG  ASP C 110      20.970   0.611  36.475  1.00 37.41           C  
ANISOU 5936  CG  ASP C 110     4930   4522   4763     40    107    564       C  
ATOM   5937  OD1 ASP C 110      20.858   0.335  35.262  1.00 37.97           O  
ANISOU 5937  OD1 ASP C 110     4984   4573   4869     32    108    541       O  
ATOM   5938  OD2 ASP C 110      20.407   1.591  37.015  1.00 37.73           O  
ANISOU 5938  OD2 ASP C 110     4978   4582   4775     30    104    553       O  
ATOM   5939  N   HIS C 111      21.924   2.115  40.106  1.00 47.90           N  
ANISOU 5939  N   HIS C 111     6304   5941   5955     65     79    622       N  
ATOM   5940  CA  HIS C 111      22.523   3.380  40.491  1.00 48.12           C  
ANISOU 5940  CA  HIS C 111     6330   6010   5942     63     48    607       C  
ATOM   5941  C   HIS C 111      23.696   3.098  41.419  1.00 52.78           C  
ANISOU 5941  C   HIS C 111     6928   6629   6498     88     31    640       C  
ATOM   5942  O   HIS C 111      24.046   1.940  41.657  1.00 58.67           O  
ANISOU 5942  O   HIS C 111     7679   7359   7252    107     42    674       O  
ATOM   5943  CB  HIS C 111      21.491   4.229  41.207  1.00 45.21           C  
ANISOU 5943  CB  HIS C 111     5973   5655   5551     48     60    595       C  
ATOM   5944  CG  HIS C 111      20.666   3.445  42.173  1.00 55.94           C  
ANISOU 5944  CG  HIS C 111     7349   6999   6905     52     93    624       C  
ATOM   5945  ND1 HIS C 111      19.449   2.898  41.835  1.00 61.18           N  
ANISOU 5945  ND1 HIS C 111     8015   7626   7605     40    126    618       N  
ATOM   5946  CD2 HIS C 111      20.909   3.076  43.453  1.00 55.02           C  
ANISOU 5946  CD2 HIS C 111     7252   6900   6754     69     99    659       C  
ATOM   5947  CE1 HIS C 111      18.962   2.243  42.876  1.00 56.81           C  
ANISOU 5947  CE1 HIS C 111     7480   7066   7040     47    154    648       C  
ATOM   5948  NE2 HIS C 111      19.829   2.332  43.867  1.00 62.29           N  
ANISOU 5948  NE2 HIS C 111     8185   7791   7690     66    138    676       N  
ATOM   5949  N   ARG C 112      24.301   4.155  41.944  1.00 43.19           N  
ANISOU 5949  N   ARG C 112     5712   5455   5243     88      5    628       N  
ATOM   5950  CA  ARG C 112      25.411   3.997  42.872  1.00 45.66           C  
ANISOU 5950  CA  ARG C 112     6029   5801   5518    112    -15    655       C  
ATOM   5951  C   ARG C 112      25.053   4.649  44.204  1.00 45.02           C  
ANISOU 5951  C   ARG C 112     5964   5754   5389    112    -13    660       C  
ATOM   5952  O   ARG C 112      25.896   5.233  44.887  1.00 41.16           O  
ANISOU 5952  O   ARG C 112     5472   5306   4860    121    -38    659       O  
ATOM   5953  CB  ARG C 112      26.697   4.583  42.281  1.00 43.24           C  
ANISOU 5953  CB  ARG C 112     5704   5517   5208    116    -50    634       C  
ATOM   5954  CG  ARG C 112      27.160   3.893  40.992  1.00 42.97           C  
ANISOU 5954  CG  ARG C 112     5655   5451   5219    118    -52    630       C  
ATOM   5955  CD  ARG C 112      28.601   4.268  40.648  1.00 49.07           C  
ANISOU 5955  CD  ARG C 112     6411   6248   5984    127    -87    619       C  
ATOM   5956  NE  ARG C 112      28.861   5.655  41.013  1.00 43.61           N  
ANISOU 5956  NE  ARG C 112     5716   5595   5260    116   -107    591       N  
ATOM   5957  CZ  ARG C 112      29.942   6.079  41.658  1.00 39.51           C  
ANISOU 5957  CZ  ARG C 112     5190   5114   4706    129   -133    591       C  
ATOM   5958  NH1 ARG C 112      30.908   5.237  42.001  1.00 39.69           N  
ANISOU 5958  NH1 ARG C 112     5211   5147   4723    155   -145    619       N  
ATOM   5959  NH2 ARG C 112      30.058   7.362  41.946  1.00 38.52           N  
ANISOU 5959  NH2 ARG C 112     5060   5020   4555    116   -147    561       N  
ATOM   5960  N   LEU C 113      23.776   4.548  44.552  1.00 40.29           N  
ANISOU 5960  N   LEU C 113     5377   5136   4794     99     17    663       N  
ATOM   5961  CA  LEU C 113      23.258   5.098  45.795  1.00 38.37           C  
ANISOU 5961  CA  LEU C 113     5149   4920   4509     97     25    667       C  
ATOM   5962  C   LEU C 113      22.897   3.960  46.747  1.00 48.26           C  
ANISOU 5962  C   LEU C 113     6424   6162   5751    115     52    714       C  
ATOM   5963  O   LEU C 113      21.760   3.487  46.758  1.00 51.00           O  
ANISOU 5963  O   LEU C 113     6781   6477   6120    105     87    720       O  
ATOM   5964  CB  LEU C 113      22.025   5.957  45.509  1.00 39.57           C  
ANISOU 5964  CB  LEU C 113     5300   5060   4673     67     40    633       C  
ATOM   5965  CG  LEU C 113      22.303   7.220  44.695  1.00 35.96           C  
ANISOU 5965  CG  LEU C 113     4824   4616   4221     50     15    588       C  
ATOM   5966  CD1 LEU C 113      21.005   7.936  44.333  1.00 33.32           C  
ANISOU 5966  CD1 LEU C 113     4489   4265   3905     24     33    558       C  
ATOM   5967  CD2 LEU C 113      23.248   8.135  45.470  1.00 27.32           C  
ANISOU 5967  CD2 LEU C 113     3727   3572   3081     55    -13    580       C  
ATOM   5968  N   LYS C 114      23.872   3.517  47.533  1.00 39.63           N  
ANISOU 5968  N   LYS C 114     5337   5096   4624    143     38    746       N  
ATOM   5969  CA  LYS C 114      23.680   2.378  48.424  1.00 51.79           C  
ANISOU 5969  CA  LYS C 114     6899   6627   6153    166     64    796       C  
ATOM   5970  C   LYS C 114      23.212   2.798  49.812  1.00 45.68           C  
ANISOU 5970  C   LYS C 114     6144   5885   5328    168     73    808       C  
ATOM   5971  O   LYS C 114      23.630   3.829  50.333  1.00 37.16           O  
ANISOU 5971  O   LYS C 114     5060   4851   4207    165     47    788       O  
ATOM   5972  CB  LYS C 114      24.966   1.555  48.526  1.00 49.46           C  
ANISOU 5972  CB  LYS C 114     6601   6341   5850    199     46    830       C  
ATOM   5973  CG  LYS C 114      24.877   0.389  49.494  1.00 62.74           C  
ANISOU 5973  CG  LYS C 114     8306   8016   7517    227     72    886       C  
ATOM   5974  CD  LYS C 114      26.086  -0.518  49.378  1.00 73.23           C  
ANISOU 5974  CD  LYS C 114     9629   9345   8849    260     56    918       C  
ATOM   5975  CE  LYS C 114      25.707  -1.871  48.801  1.00 80.21           C  
ANISOU 5975  CE  LYS C 114    10518  10171   9787    267     92    946       C  
ATOM   5976  NZ  LYS C 114      26.329  -2.987  49.562  1.00 83.92           N  
ANISOU 5976  NZ  LYS C 114    11002  10641  10241    306    100   1003       N  
ATOM   5977  N   ASN C 115      22.342   1.988  50.408  1.00 45.15           N  
ANISOU 5977  N   ASN C 115     6099   5794   5264    173    112    840       N  
ATOM   5978  CA  ASN C 115      21.764   2.314  51.705  1.00 44.14           C  
ANISOU 5978  CA  ASN C 115     5991   5691   5088    173    127    852       C  
ATOM   5979  C   ASN C 115      21.107   3.693  51.717  1.00 35.08           C  
ANISOU 5979  C   ASN C 115     4836   4562   3929    142    120    804       C  
ATOM   5980  O   ASN C 115      21.158   4.406  52.715  1.00 32.76           O  
ANISOU 5980  O   ASN C 115     4550   4311   3586    143    111    800       O  
ATOM   5981  CB  ASN C 115      22.811   2.198  52.815  1.00 48.17           C  
ANISOU 5981  CB  ASN C 115     6510   6251   5540    206    105    885       C  
ATOM   5982  CG  ASN C 115      23.009   0.764  53.290  1.00 59.53           C  
ANISOU 5982  CG  ASN C 115     7968   7671   6979    239    128    944       C  
ATOM   5983  OD1 ASN C 115      22.295   0.285  54.177  1.00 61.05           O  
ANISOU 5983  OD1 ASN C 115     8186   7857   7155    247    162    975       O  
ATOM   5984  ND2 ASN C 115      23.976   0.074  52.699  1.00 46.31           N  
ANISOU 5984  ND2 ASN C 115     6283   5987   5326    260    112    961       N  
ATOM   5985  N   TYR C 116      20.486   4.055  50.595  1.00 40.20           N  
ANISOU 5985  N   TYR C 116     5470   5179   4625    115    125    768       N  
ATOM   5986  CA  TYR C 116      19.804   5.340  50.458  1.00 34.51           C  
ANISOU 5986  CA  TYR C 116     4741   4468   3901     86    121    722       C  
ATOM   5987  C   TYR C 116      18.439   5.275  51.116  1.00 36.32           C  
ANISOU 5987  C   TYR C 116     4988   4682   4130     72    160    726       C  
ATOM   5988  O   TYR C 116      17.617   4.426  50.773  1.00 34.49           O  
ANISOU 5988  O   TYR C 116     4763   4406   3937     67    194    737       O  
ATOM   5989  CB  TYR C 116      19.608   5.687  48.977  1.00 31.34           C  
ANISOU 5989  CB  TYR C 116     4317   4037   3551     65    114    684       C  
ATOM   5990  CG  TYR C 116      18.958   7.039  48.725  1.00 34.34           C  
ANISOU 5990  CG  TYR C 116     4687   4427   3932     37    108    638       C  
ATOM   5991  CD1 TYR C 116      19.729   8.144  48.361  1.00 32.01           C  
ANISOU 5991  CD1 TYR C 116     4376   4161   3625     31     74    606       C  
ATOM   5992  CD2 TYR C 116      17.578   7.211  48.840  1.00 27.43           C  
ANISOU 5992  CD2 TYR C 116     3820   3531   3072     17    139    625       C  
ATOM   5993  CE1 TYR C 116      19.151   9.389  48.127  1.00 21.82           C  
ANISOU 5993  CE1 TYR C 116     3076   2877   2336      6     71    565       C  
ATOM   5994  CE2 TYR C 116      16.990   8.458  48.607  1.00 34.03           C  
ANISOU 5994  CE2 TYR C 116     4646   4374   3909     -7    134    583       C  
ATOM   5995  CZ  TYR C 116      17.784   9.540  48.245  1.00 29.05           C  
ANISOU 5995  CZ  TYR C 116     4000   3772   3267    -12    100    555       C  
ATOM   5996  OH  TYR C 116      17.213  10.769  48.011  1.00 29.58           O  
ANISOU 5996  OH  TYR C 116     4057   3844   3337    -35     98    515       O  
ATOM   5997  N   SER C 117      18.198   6.172  52.058  1.00 27.85           N  
ANISOU 5997  N   SER C 117     3923   3646   3014     64    157    714       N  
ATOM   5998  CA  SER C 117      16.858   6.359  52.569  1.00 38.64           C  
ANISOU 5998  CA  SER C 117     5302   4998   4382     45    192    706       C  
ATOM   5999  C   SER C 117      16.604   7.859  52.589  1.00 37.33           C  
ANISOU 5999  C   SER C 117     5124   4859   4201     20    175    659       C  
ATOM   6000  O   SER C 117      17.547   8.650  52.676  1.00 32.11           O  
ANISOU 6000  O   SER C 117     4452   4237   3513     24    140    643       O  
ATOM   6001  CB  SER C 117      16.710   5.736  53.962  1.00 36.46           C  
ANISOU 6001  CB  SER C 117     5053   4737   4063     63    215    749       C  
ATOM   6002  OG  SER C 117      17.417   6.495  54.928  1.00 44.99           O  
ANISOU 6002  OG  SER C 117     6135   5875   5083     71    189    747       O  
ATOM   6003  N   SER C 118      15.339   8.254  52.483  1.00 37.03           N  
ANISOU 6003  N   SER C 118     5087   4798   4185     -4    200    636       N  
ATOM   6004  CA  SER C 118      15.004   9.675  52.416  1.00 34.44           C  
ANISOU 6004  CA  SER C 118     4746   4490   3850    -28    188    591       C  
ATOM   6005  C   SER C 118      13.643   9.949  53.019  1.00 34.01           C  
ANISOU 6005  C   SER C 118     4702   4424   3795    -48    222    580       C  
ATOM   6006  O   SER C 118      12.824   9.047  53.168  1.00 37.48           O  
ANISOU 6006  O   SER C 118     5155   4831   4254    -47    257    601       O  
ATOM   6007  CB  SER C 118      15.032  10.179  50.970  1.00 34.83           C  
ANISOU 6007  CB  SER C 118     4772   4517   3944    -42    171    556       C  
ATOM   6008  OG  SER C 118      13.854   9.796  50.274  1.00 34.81           O  
ANISOU 6008  OG  SER C 118     4767   4470   3989    -56    199    546       O  
ATOM   6009  N   THR C 119      13.411  11.210  53.349  1.00 33.03           N  
ANISOU 6009  N   THR C 119     4572   4326   3652    -65    214    546       N  
ATOM   6010  CA  THR C 119      12.223  11.605  54.069  1.00 41.22           C  
ANISOU 6010  CA  THR C 119     5619   5360   4682    -84    243    534       C  
ATOM   6011  C   THR C 119      11.724  12.931  53.534  1.00 34.82           C  
ANISOU 6011  C   THR C 119     4791   4551   3890   -109    235    485       C  
ATOM   6012  O   THR C 119      12.494  13.874  53.424  1.00 29.80           O  
ANISOU 6012  O   THR C 119     4141   3943   3236   -111    206    463       O  
ATOM   6013  CB  THR C 119      12.539  11.751  55.571  1.00 41.96           C  
ANISOU 6013  CB  THR C 119     5730   5499   4713    -75    245    552       C  
ATOM   6014  OG1 THR C 119      12.891  10.465  56.105  1.00 45.95           O  
ANISOU 6014  OG1 THR C 119     6255   6001   5201    -49    257    602       O  
ATOM   6015  CG2 THR C 119      11.337  12.279  56.326  1.00 38.71           C  
ANISOU 6015  CG2 THR C 119     5328   5087   4292    -96    275    535       C  
ATOM   6016  N   ILE C 120      10.444  12.998  53.179  1.00 27.42           N  
ANISOU 6016  N   ILE C 120     3850   3579   2988   -128    262    467       N  
ATOM   6017  CA  ILE C 120       9.851  14.281  52.832  1.00 26.75           C  
ANISOU 6017  CA  ILE C 120     3751   3496   2918   -151    258    422       C  
ATOM   6018  C   ILE C 120       8.694  14.625  53.748  1.00 28.24           C  
ANISOU 6018  C   ILE C 120     3950   3685   3096   -168    289    412       C  
ATOM   6019  O   ILE C 120       7.819  13.796  53.988  1.00 32.50           O  
ANISOU 6019  O   ILE C 120     4502   4198   3651   -170    322    428       O  
ATOM   6020  CB  ILE C 120       9.375  14.339  51.363  1.00 30.76           C  
ANISOU 6020  CB  ILE C 120     4240   3967   3482   -159    255    400       C  
ATOM   6021  CG1 ILE C 120       8.705  15.689  51.081  1.00 27.50           C  
ANISOU 6021  CG1 ILE C 120     3813   3555   3081   -180    254    357       C  
ATOM   6022  CG2 ILE C 120       8.424  13.177  51.045  1.00 35.04           C  
ANISOU 6022  CG2 ILE C 120     4787   4465   4060   -159    287    415       C  
ATOM   6023  CD1 ILE C 120       8.646  16.050  49.590  1.00 27.09           C  
ANISOU 6023  CD1 ILE C 120     3739   3480   3072   -183    238    333       C  
ATOM   6024  N   SER C 121       8.696  15.853  54.258  1.00 25.21           N  
ANISOU 6024  N   SER C 121     3560   3330   2687   -181    281    384       N  
ATOM   6025  CA  SER C 121       7.610  16.328  55.104  1.00 26.37           C  
ANISOU 6025  CA  SER C 121     3715   3479   2825   -200    310    368       C  
ATOM   6026  C   SER C 121       7.034  17.630  54.577  1.00 30.60           C  
ANISOU 6026  C   SER C 121     4232   4010   3386   -221    306    322       C  
ATOM   6027  O   SER C 121       7.737  18.451  53.988  1.00 31.60           O  
ANISOU 6027  O   SER C 121     4342   4150   3515   -221    278    302       O  
ATOM   6028  CB  SER C 121       8.069  16.481  56.560  1.00 31.36           C  
ANISOU 6028  CB  SER C 121     4363   4156   3395   -195    311    382       C  
ATOM   6029  OG  SER C 121       9.201  17.320  56.669  1.00 39.93           O  
ANISOU 6029  OG  SER C 121     5437   5282   4452   -190    277    368       O  
ATOM   6030  N   LEU C 122       5.740  17.802  54.787  1.00 23.96           N  
ANISOU 6030  N   LEU C 122     3391   3148   2563   -238    336    307       N  
ATOM   6031  CA  LEU C 122       5.027  18.978  54.329  1.00 26.96           C  
ANISOU 6031  CA  LEU C 122     3754   3519   2969   -258    337    265       C  
ATOM   6032  C   LEU C 122       4.610  19.813  55.525  1.00 33.29           C  
ANISOU 6032  C   LEU C 122     4562   4348   3739   -274    352    247       C  
ATOM   6033  O   LEU C 122       4.274  19.283  56.578  1.00 30.06           O  
ANISOU 6033  O   LEU C 122     4172   3947   3303   -274    375    265       O  
ATOM   6034  CB  LEU C 122       3.796  18.580  53.511  1.00 22.27           C  
ANISOU 6034  CB  LEU C 122     3153   2881   2428   -266    358    255       C  
ATOM   6035  CG  LEU C 122       4.073  17.673  52.304  1.00 28.42           C  
ANISOU 6035  CG  LEU C 122     3924   3632   3241   -251    347    269       C  
ATOM   6036  CD1 LEU C 122       2.846  17.573  51.402  1.00 24.96           C  
ANISOU 6036  CD1 LEU C 122     3472   3155   2855   -261    364    248       C  
ATOM   6037  CD2 LEU C 122       5.312  18.149  51.502  1.00 23.50           C  
ANISOU 6037  CD2 LEU C 122     3289   3025   2615   -240    308    266       C  
ATOM   6038  N   HIS C 123       4.644  21.126  55.350  1.00 31.51           N  
ANISOU 6038  N   HIS C 123     4320   4134   3517   -287    340    211       N  
ATOM   6039  CA  HIS C 123       4.298  22.066  56.398  1.00 34.62           C  
ANISOU 6039  CA  HIS C 123     4716   4553   3885   -304    353    188       C  
ATOM   6040  C   HIS C 123       3.589  23.243  55.763  1.00 38.44           C  
ANISOU 6040  C   HIS C 123     5180   5020   4405   -321    356    147       C  
ATOM   6041  O   HIS C 123       3.993  23.724  54.697  1.00 33.18           O  
ANISOU 6041  O   HIS C 123     4498   4345   3766   -317    334    134       O  
ATOM   6042  CB  HIS C 123       5.560  22.556  57.099  1.00 34.02           C  
ANISOU 6042  CB  HIS C 123     4641   4525   3759   -298    329    188       C  
ATOM   6043  CG  HIS C 123       6.450  21.450  57.558  1.00 38.88           C  
ANISOU 6043  CG  HIS C 123     5273   5160   4339   -276    319    229       C  
ATOM   6044  ND1 HIS C 123       6.435  20.966  58.849  1.00 41.43           N  
ANISOU 6044  ND1 HIS C 123     5617   5509   4617   -272    335    250       N  
ATOM   6045  CD2 HIS C 123       7.362  20.706  56.889  1.00 36.38           C  
ANISOU 6045  CD2 HIS C 123     4957   4840   4028   -255    297    254       C  
ATOM   6046  CE1 HIS C 123       7.309  19.981  58.958  1.00 45.20           C  
ANISOU 6046  CE1 HIS C 123     6105   5998   5071   -248    321    288       C  
ATOM   6047  NE2 HIS C 123       7.884  19.802  57.781  1.00 43.43           N  
ANISOU 6047  NE2 HIS C 123     5868   5755   4878   -238    298    290       N  
ATOM   6048  N   SER C 124       2.527  23.699  56.412  1.00 25.94           N  
ANISOU 6048  N   SER C 124     3599   3433   2825   -339    383    127       N  
ATOM   6049  CA  SER C 124       1.781  24.850  55.941  1.00 30.47           C  
ANISOU 6049  CA  SER C 124     4153   3991   3432   -355    389     89       C  
ATOM   6050  C   SER C 124       2.606  26.129  56.116  1.00 37.08           C  
ANISOU 6050  C   SER C 124     4979   4858   4251   -361    370     63       C  
ATOM   6051  O   SER C 124       3.286  26.310  57.127  1.00 36.55           O  
ANISOU 6051  O   SER C 124     4919   4829   4138   -363    366     65       O  
ATOM   6052  CB  SER C 124       0.464  24.960  56.698  1.00 34.13           C  
ANISOU 6052  CB  SER C 124     4623   4445   3902   -374    425     75       C  
ATOM   6053  OG  SER C 124      -0.340  25.977  56.133  1.00 55.33           O  
ANISOU 6053  OG  SER C 124     7288   7110   6625   -387    431     39       O  
ATOM   6054  N   GLU C 125       2.555  27.009  55.120  1.00 42.42           N  
ANISOU 6054  N   GLU C 125     5637   5519   4964   -364    359     39       N  
ATOM   6055  CA  GLU C 125       3.332  28.241  55.155  1.00 45.02           C  
ANISOU 6055  CA  GLU C 125     5952   5869   5282   -369    344     14       C  
ATOM   6056  C   GLU C 125       2.768  29.308  54.238  1.00 45.07           C  
ANISOU 6056  C   GLU C 125     5940   5850   5334   -376    347    -16       C  
ATOM   6057  O   GLU C 125       2.647  29.114  53.027  1.00 42.62           O  
ANISOU 6057  O   GLU C 125     5623   5513   5059   -365    336    -10       O  
ATOM   6058  CB  GLU C 125       4.786  27.982  54.777  1.00 45.64           C  
ANISOU 6058  CB  GLU C 125     6031   5968   5343   -353    313     30       C  
ATOM   6059  CG  GLU C 125       5.642  29.233  54.785  1.00 47.10           C  
ANISOU 6059  CG  GLU C 125     6201   6175   5521   -359    299      2       C  
ATOM   6060  CD  GLU C 125       7.051  28.963  54.292  1.00 58.90           C  
ANISOU 6060  CD  GLU C 125     7692   7683   7003   -343    268     16       C  
ATOM   6061  OE1 GLU C 125       7.194  28.294  53.242  1.00 56.28           O  
ANISOU 6061  OE1 GLU C 125     7361   7328   6695   -328    256     36       O  
ATOM   6062  OE2 GLU C 125       8.016  29.407  54.956  1.00 58.80           O  
ANISOU 6062  OE2 GLU C 125     7676   7707   6957   -345    257      5       O  
ATOM   6063  N   THR C 126       2.453  30.449  54.828  1.00 34.70           N  
ANISOU 6063  N   THR C 126     4619   4548   4020   -394    360    -48       N  
ATOM   6064  CA  THR C 126       1.843  31.542  54.104  1.00 31.74           C  
ANISOU 6064  CA  THR C 126     4226   4148   3686   -401    367    -76       C  
ATOM   6065  C   THR C 126       2.909  32.549  53.737  1.00 34.73           C  
ANISOU 6065  C   THR C 126     4592   4539   4064   -400    350    -92       C  
ATOM   6066  O   THR C 126       3.730  32.930  54.576  1.00 38.60           O  
ANISOU 6066  O   THR C 126     5083   5063   4520   -407    345   -102       O  
ATOM   6067  CB  THR C 126       0.768  32.190  54.972  1.00 37.02           C  
ANISOU 6067  CB  THR C 126     4892   4815   4357   -422    397   -102       C  
ATOM   6068  OG1 THR C 126      -0.160  31.175  55.380  1.00 44.66           O  
ANISOU 6068  OG1 THR C 126     5873   5772   5323   -424    415    -86       O  
ATOM   6069  CG2 THR C 126       0.027  33.309  54.212  1.00 38.80           C  
ANISOU 6069  CG2 THR C 126     5099   5013   4629   -428    406   -131       C  
ATOM   6070  N   ILE C 127       2.924  32.964  52.478  1.00 32.21           N  
ANISOU 6070  N   ILE C 127     4261   4194   3782   -390    340    -96       N  
ATOM   6071  CA  ILE C 127       3.907  33.947  52.040  1.00 35.27           C  
ANISOU 6071  CA  ILE C 127     4637   4589   4175   -389    327   -111       C  
ATOM   6072  C   ILE C 127       3.295  34.906  51.035  1.00 40.21           C  
ANISOU 6072  C   ILE C 127     5249   5183   4847   -388    334   -129       C  
ATOM   6073  O   ILE C 127       2.632  34.486  50.084  1.00 41.14           O  
ANISOU 6073  O   ILE C 127     5365   5273   4993   -375    332   -116       O  
ATOM   6074  CB  ILE C 127       5.153  33.284  51.428  1.00 37.05           C  
ANISOU 6074  CB  ILE C 127     4866   4824   4388   -371    298    -87       C  
ATOM   6075  CG1 ILE C 127       5.937  32.535  52.506  1.00 38.40           C  
ANISOU 6075  CG1 ILE C 127     5049   5032   4510   -371    290    -73       C  
ATOM   6076  CG2 ILE C 127       6.039  34.332  50.779  1.00 39.75           C  
ANISOU 6076  CG2 ILE C 127     5195   5165   4745   -370    289   -105       C  
ATOM   6077  CD1 ILE C 127       7.018  31.635  51.962  1.00 43.07           C  
ANISOU 6077  CD1 ILE C 127     5645   5629   5088   -352    263    -45       C  
ATOM   6078  N   ASP C 128       3.520  36.195  51.263  1.00 43.71           N  
ANISOU 6078  N   ASP C 128     5680   5631   5298   -400    344   -158       N  
ATOM   6079  CA  ASP C 128       2.982  37.246  50.403  1.00 49.53           C  
ANISOU 6079  CA  ASP C 128     6403   6337   6078   -398    355   -175       C  
ATOM   6080  C   ASP C 128       1.456  37.200  50.404  1.00 48.40           C  
ANISOU 6080  C   ASP C 128     6259   6172   5960   -401    374   -180       C  
ATOM   6081  O   ASP C 128       0.803  37.561  49.421  1.00 55.36           O  
ANISOU 6081  O   ASP C 128     7132   7024   6878   -391    376   -181       O  
ATOM   6082  CB  ASP C 128       3.528  37.127  48.976  1.00 52.45           C  
ANISOU 6082  CB  ASP C 128     6770   6689   6469   -376    335   -157       C  
ATOM   6083  CG  ASP C 128       3.791  38.479  48.335  1.00 59.45           C  
ANISOU 6083  CG  ASP C 128     7644   7560   7385   -375    342   -177       C  
ATOM   6084  OD1 ASP C 128       3.408  39.510  48.931  1.00 59.04           O  
ANISOU 6084  OD1 ASP C 128     7584   7508   7343   -391    364   -205       O  
ATOM   6085  OD2 ASP C 128       4.374  38.509  47.230  1.00 66.60           O  
ANISOU 6085  OD2 ASP C 128     8547   8453   8305   -359    327   -164       O  
ATOM   6086  N   GLY C 129       0.894  36.752  51.522  1.00 36.19           N  
ANISOU 6086  N   GLY C 129     4721   4640   4392   -416    388   -183       N  
ATOM   6087  CA  GLY C 129      -0.543  36.725  51.700  1.00 37.14           C  
ANISOU 6087  CA  GLY C 129     4839   4741   4533   -423    409   -192       C  
ATOM   6088  C   GLY C 129      -1.227  35.504  51.101  1.00 46.52           C  
ANISOU 6088  C   GLY C 129     6032   5911   5731   -409    403   -168       C  
ATOM   6089  O   GLY C 129      -2.441  35.357  51.211  1.00 41.60           O  
ANISOU 6089  O   GLY C 129     5407   5272   5128   -414    421   -175       O  
ATOM   6090  N   LYS C 130      -0.459  34.626  50.466  1.00 44.92           N  
ANISOU 6090  N   LYS C 130     5837   5711   5519   -392    380   -141       N  
ATOM   6091  CA  LYS C 130      -1.046  33.430  49.862  1.00 45.92           C  
ANISOU 6091  CA  LYS C 130     5969   5821   5659   -379    375   -119       C  
ATOM   6092  C   LYS C 130      -0.612  32.178  50.611  1.00 44.67           C  
ANISOU 6092  C   LYS C 130     5828   5682   5465   -380    372    -95       C  
ATOM   6093  O   LYS C 130       0.590  31.922  50.785  1.00 38.86           O  
ANISOU 6093  O   LYS C 130     5099   4966   4699   -375    354    -81       O  
ATOM   6094  CB  LYS C 130      -0.674  33.333  48.381  1.00 47.43           C  
ANISOU 6094  CB  LYS C 130     6153   5996   5873   -357    353   -107       C  
ATOM   6095  CG  LYS C 130      -0.532  34.698  47.714  1.00 60.61           C  
ANISOU 6095  CG  LYS C 130     7808   7655   7567   -354    352   -125       C  
ATOM   6096  CD  LYS C 130      -1.102  34.718  46.304  1.00 79.04           C  
ANISOU 6096  CD  LYS C 130    10132   9964   9937   -334    343   -122       C  
ATOM   6097  CE  LYS C 130      -2.328  35.627  46.216  1.00 81.90           C  
ANISOU 6097  CE  LYS C 130    10481  10307  10331   -338    363   -145       C  
ATOM   6098  NZ  LYS C 130      -2.885  35.696  44.833  1.00 92.81           N  
ANISOU 6098  NZ  LYS C 130    11851  11666  11745   -315    353   -142       N  
ATOM   6099  N   THR C 131      -1.594  31.411  51.074  1.00 45.20           N  
ANISOU 6099  N   THR C 131     5900   5739   5533   -386    390    -91       N  
ATOM   6100  CA  THR C 131      -1.315  30.190  51.820  1.00 43.89           C  
ANISOU 6100  CA  THR C 131     5753   5587   5335   -386    392    -66       C  
ATOM   6101  C   THR C 131      -0.829  29.088  50.872  1.00 37.88           C  
ANISOU 6101  C   THR C 131     4996   4816   4581   -366    371    -37       C  
ATOM   6102  O   THR C 131      -1.431  28.840  49.830  1.00 43.14           O  
ANISOU 6102  O   THR C 131     5652   5457   5283   -356    368    -38       O  
ATOM   6103  CB  THR C 131      -2.535  29.746  52.655  1.00 49.04           C  
ANISOU 6103  CB  THR C 131     6411   6231   5989   -400    422    -71       C  
ATOM   6104  OG1 THR C 131      -2.959  30.837  53.484  1.00 52.82           O  
ANISOU 6104  OG1 THR C 131     6886   6720   6464   -419    441   -100       O  
ATOM   6105  CG2 THR C 131      -2.181  28.556  53.548  1.00 45.46           C  
ANISOU 6105  CG2 THR C 131     5980   5794   5499   -399    428    -43       C  
ATOM   6106  N   GLY C 132       0.291  28.469  51.228  1.00 32.15           N  
ANISOU 6106  N   GLY C 132     4282   4112   3821   -359    357    -14       N  
ATOM   6107  CA  GLY C 132       0.895  27.428  50.419  1.00 29.38           C  
ANISOU 6107  CA  GLY C 132     3935   3754   3474   -340    338     13       C  
ATOM   6108  C   GLY C 132       1.561  26.399  51.308  1.00 24.56           C  
ANISOU 6108  C   GLY C 132     3344   3163   2825   -337    337     42       C  
ATOM   6109  O   GLY C 132       1.163  26.215  52.456  1.00 28.39           O  
ANISOU 6109  O   GLY C 132     3840   3659   3286   -348    358     43       O  
ATOM   6110  N   THR C 133       2.604  25.758  50.797  1.00 28.48           N  
ANISOU 6110  N   THR C 133     3843   3665   3312   -321    314     65       N  
ATOM   6111  CA  THR C 133       3.206  24.629  51.480  1.00 25.31           C  
ANISOU 6111  CA  THR C 133     3459   3279   2879   -313    313     96       C  
ATOM   6112  C   THR C 133       4.718  24.677  51.407  1.00 26.22           C  
ANISOU 6112  C   THR C 133     3576   3420   2968   -301    284    109       C  
ATOM   6113  O   THR C 133       5.274  24.995  50.374  1.00 28.32           O  
ANISOU 6113  O   THR C 133     3830   3678   3252   -292    264    104       O  
ATOM   6114  CB  THR C 133       2.733  23.288  50.845  1.00 27.00           C  
ANISOU 6114  CB  THR C 133     3678   3464   3118   -302    319    119       C  
ATOM   6115  OG1 THR C 133       1.305  23.272  50.750  1.00 26.14           O  
ANISOU 6115  OG1 THR C 133     3563   3329   3039   -313    345    103       O  
ATOM   6116  CG2 THR C 133       3.198  22.124  51.663  1.00 26.42           C  
ANISOU 6116  CG2 THR C 133     3624   3402   3013   -294    325    153       C  
ATOM   6117  N   LEU C 134       5.368  24.329  52.508  1.00 26.53           N  
ANISOU 6117  N   LEU C 134     3629   3489   2963   -299    284    124       N  
ATOM   6118  CA  LEU C 134       6.808  24.187  52.546  1.00 23.87           C  
ANISOU 6118  CA  LEU C 134     3292   3178   2598   -285    257    139       C  
ATOM   6119  C   LEU C 134       7.177  22.715  52.542  1.00 34.18           C  
ANISOU 6119  C   LEU C 134     4613   4480   3895   -268    253    178       C  
ATOM   6120  O   LEU C 134       6.889  21.991  53.502  1.00 30.39           O  
ANISOU 6120  O   LEU C 134     4149   4008   3390   -267    270    198       O  
ATOM   6121  CB  LEU C 134       7.367  24.820  53.816  1.00 30.42           C  
ANISOU 6121  CB  LEU C 134     4126   4050   3381   -293    256    128       C  
ATOM   6122  CG  LEU C 134       8.884  24.698  53.901  1.00 33.79           C  
ANISOU 6122  CG  LEU C 134     4551   4508   3778   -279    227    140       C  
ATOM   6123  CD1 LEU C 134       9.496  25.387  52.689  1.00 31.46           C  
ANISOU 6123  CD1 LEU C 134     4238   4201   3512   -276    206    122       C  
ATOM   6124  CD2 LEU C 134       9.423  25.291  55.193  1.00 39.63           C  
ANISOU 6124  CD2 LEU C 134     5293   5295   4470   -286    225    127       C  
ATOM   6125  N   ALA C 135       7.814  22.266  51.465  1.00 30.04           N  
ANISOU 6125  N   ALA C 135     4082   3942   3390   -253    233    190       N  
ATOM   6126  CA  ALA C 135       8.269  20.888  51.387  1.00 30.53           C  
ANISOU 6126  CA  ALA C 135     4156   3999   3447   -236    229    227       C  
ATOM   6127  C   ALA C 135       9.730  20.762  51.817  1.00 34.41           C  
ANISOU 6127  C   ALA C 135     4650   4525   3900   -222    204    242       C  
ATOM   6128  O   ALA C 135      10.591  21.519  51.384  1.00 29.08           O  
ANISOU 6128  O   ALA C 135     3962   3864   3224   -221    181    226       O  
ATOM   6129  CB  ALA C 135       8.064  20.324  49.978  1.00 31.08           C  
ANISOU 6129  CB  ALA C 135     4215   4031   3561   -228    224    231       C  
ATOM   6130  N   ILE C 136      10.003  19.785  52.667  1.00 23.46           N  
ANISOU 6130  N   ILE C 136     3280   3151   2482   -210    209    274       N  
ATOM   6131  CA  ILE C 136      11.349  19.551  53.137  1.00 23.59           C  
ANISOU 6131  CA  ILE C 136     3299   3203   2460   -194    186    292       C  
ATOM   6132  C   ILE C 136      11.713  18.106  52.883  1.00 27.14           C  
ANISOU 6132  C   ILE C 136     3759   3638   2914   -173    184    333       C  
ATOM   6133  O   ILE C 136      10.983  17.192  53.272  1.00 33.50           O  
ANISOU 6133  O   ILE C 136     4580   4425   3722   -170    209    356       O  
ATOM   6134  CB  ILE C 136      11.457  19.839  54.636  1.00 31.55           C  
ANISOU 6134  CB  ILE C 136     4319   4253   3417   -197    192    293       C  
ATOM   6135  CG1 ILE C 136      11.171  21.322  54.893  1.00 27.49           C  
ANISOU 6135  CG1 ILE C 136     3792   3755   2900   -219    194    249       C  
ATOM   6136  CG2 ILE C 136      12.824  19.423  55.156  1.00 28.11           C  
ANISOU 6136  CG2 ILE C 136     3887   3856   2940   -176    167    314       C  
ATOM   6137  CD1 ILE C 136      10.623  21.621  56.269  1.00 35.27           C  
ANISOU 6137  CD1 ILE C 136     4788   4765   3847   -230    214    243       C  
ATOM   6138  N   GLU C 137      12.836  17.895  52.217  1.00 26.02           N  
ANISOU 6138  N   GLU C 137     3609   3501   2776   -158    157    340       N  
ATOM   6139  CA  GLU C 137      13.268  16.546  51.911  1.00 29.57           C  
ANISOU 6139  CA  GLU C 137     4067   3935   3233   -138    154    378       C  
ATOM   6140  C   GLU C 137      14.717  16.370  52.317  1.00 34.89           C  
ANISOU 6140  C   GLU C 137     4740   4646   3870   -118    126    394       C  
ATOM   6141  O   GLU C 137      15.560  17.220  52.030  1.00 39.54           O  
ANISOU 6141  O   GLU C 137     5314   5256   4453   -120    101    370       O  
ATOM   6142  CB  GLU C 137      13.053  16.231  50.429  1.00 24.87           C  
ANISOU 6142  CB  GLU C 137     3459   3299   2690   -138    152    372       C  
ATOM   6143  CG  GLU C 137      13.555  14.866  50.007  1.00 31.05           C  
ANISOU 6143  CG  GLU C 137     4248   4065   3486   -118    149    407       C  
ATOM   6144  CD  GLU C 137      12.916  14.361  48.713  1.00 42.78           C  
ANISOU 6144  CD  GLU C 137     5725   5506   5024   -121    158    402       C  
ATOM   6145  OE1 GLU C 137      12.053  15.071  48.146  1.00 47.05           O  
ANISOU 6145  OE1 GLU C 137     6256   6031   5591   -138    166    372       O  
ATOM   6146  OE2 GLU C 137      13.275  13.247  48.264  1.00 44.48           O  
ANISOU 6146  OE2 GLU C 137     5942   5702   5255   -106    158    427       O  
ATOM   6147  N   SER C 138      14.994  15.280  53.022  1.00 32.75           N  
ANISOU 6147  N   SER C 138     4486   4383   3574    -99    132    433       N  
ATOM   6148  CA  SER C 138      16.349  14.962  53.445  1.00 27.29           C  
ANISOU 6148  CA  SER C 138     3795   3727   2848    -77    106    453       C  
ATOM   6149  C   SER C 138      16.638  13.541  53.031  1.00 34.94           C  
ANISOU 6149  C   SER C 138     4772   4671   3834    -55    109    493       C  
ATOM   6150  O   SER C 138      15.720  12.780  52.727  1.00 34.57           O  
ANISOU 6150  O   SER C 138     4734   4583   3817    -58    136    508       O  
ATOM   6151  CB  SER C 138      16.488  15.107  54.962  1.00 35.98           C  
ANISOU 6151  CB  SER C 138     4908   4873   3890    -71    109    463       C  
ATOM   6152  OG  SER C 138      15.804  14.073  55.643  1.00 39.63           O  
ANISOU 6152  OG  SER C 138     5394   5322   4342    -62    138    500       O  
ATOM   6153  N   PHE C 139      17.915  13.179  53.012  1.00 30.03           N  
ANISOU 6153  N   PHE C 139     4145   4070   3195    -33     82    510       N  
ATOM   6154  CA  PHE C 139      18.304  11.832  52.657  1.00 31.76           C  
ANISOU 6154  CA  PHE C 139     4371   4267   3429    -11     84    549       C  
ATOM   6155  C   PHE C 139      19.562  11.448  53.415  1.00 37.95           C  
ANISOU 6155  C   PHE C 139     5159   5093   4169     17     61    575       C  
ATOM   6156  O   PHE C 139      20.231  12.298  54.003  1.00 36.40           O  
ANISOU 6156  O   PHE C 139     4955   4942   3934     17     38    556       O  
ATOM   6157  CB  PHE C 139      18.597  11.745  51.161  1.00 29.47           C  
ANISOU 6157  CB  PHE C 139     4064   3945   3189    -14     72    535       C  
ATOM   6158  CG  PHE C 139      19.767  12.577  50.741  1.00 31.30           C  
ANISOU 6158  CG  PHE C 139     4276   4204   3413    -13     36    510       C  
ATOM   6159  CD1 PHE C 139      21.025  12.009  50.597  1.00 32.86           C  
ANISOU 6159  CD1 PHE C 139     4468   4415   3602      9     12    529       C  
ATOM   6160  CD2 PHE C 139      19.620  13.936  50.521  1.00 29.39           C  
ANISOU 6160  CD2 PHE C 139     4020   3974   3173    -35     28    467       C  
ATOM   6161  CE1 PHE C 139      22.111  12.784  50.218  1.00 34.92           C  
ANISOU 6161  CE1 PHE C 139     4709   4701   3858      9    -20    503       C  
ATOM   6162  CE2 PHE C 139      20.703  14.711  50.144  1.00 31.89           C  
ANISOU 6162  CE2 PHE C 139     4318   4314   3484    -35     -2    442       C  
ATOM   6163  CZ  PHE C 139      21.941  14.138  49.994  1.00 27.46           C  
ANISOU 6163  CZ  PHE C 139     3752   3767   2916    -14    -26    459       C  
ATOM   6164  N   VAL C 140      19.878  10.160  53.365  1.00 26.39           N  
ANISOU 6164  N   VAL C 140     3705   3611   2711     40     66    617       N  
ATOM   6165  CA  VAL C 140      21.116   9.641  53.899  1.00 32.88           C  
ANISOU 6165  CA  VAL C 140     4528   4467   3497     71     43    646       C  
ATOM   6166  C   VAL C 140      21.550   8.535  52.962  1.00 36.87           C  
ANISOU 6166  C   VAL C 140     5030   4935   4042     87     42    671       C  
ATOM   6167  O   VAL C 140      20.735   7.694  52.581  1.00 40.50           O  
ANISOU 6167  O   VAL C 140     5500   5350   4538     84     72    690       O  
ATOM   6168  CB  VAL C 140      20.896   9.063  55.299  1.00 42.18           C  
ANISOU 6168  CB  VAL C 140     5731   5668   4628     89     60    684       C  
ATOM   6169  CG1 VAL C 140      21.930   7.989  55.602  1.00 39.27           C  
ANISOU 6169  CG1 VAL C 140     5369   5313   4240    127     47    730       C  
ATOM   6170  CG2 VAL C 140      20.939  10.177  56.337  1.00 41.40           C  
ANISOU 6170  CG2 VAL C 140     5630   5622   4476     80     49    659       C  
ATOM   6171  N   VAL C 141      22.824   8.523  52.582  1.00 26.50           N  
ANISOU 6171  N   VAL C 141     3702   3641   2726    102      9    670       N  
ATOM   6172  CA  VAL C 141      23.296   7.507  51.659  1.00 30.59           C  
ANISOU 6172  CA  VAL C 141     4214   4124   3283    116      7    691       C  
ATOM   6173  C   VAL C 141      24.785   7.210  51.844  1.00 32.41           C  
ANISOU 6173  C   VAL C 141     4436   4389   3490    145    -26    707       C  
ATOM   6174  O   VAL C 141      25.524   8.035  52.379  1.00 31.14           O  
ANISOU 6174  O   VAL C 141     4266   4277   3291    148    -53    688       O  
ATOM   6175  CB  VAL C 141      23.065   7.961  50.200  1.00 27.68           C  
ANISOU 6175  CB  VAL C 141     3828   3722   2968     93      4    654       C  
ATOM   6176  CG1 VAL C 141      23.964   9.135  49.871  1.00 25.04           C  
ANISOU 6176  CG1 VAL C 141     3471   3420   2622     85    -31    615       C  
ATOM   6177  CG2 VAL C 141      23.308   6.815  49.234  1.00 30.27           C  
ANISOU 6177  CG2 VAL C 141     4151   4008   3340    104     10    675       C  
ATOM   6178  N   ASP C 142      25.210   6.030  51.389  1.00 35.12           N  
ANISOU 6178  N   ASP C 142     4781   4704   3858    166    -23    740       N  
ATOM   6179  CA  ASP C 142      26.624   5.684  51.323  1.00 37.66           C  
ANISOU 6179  CA  ASP C 142     5091   5050   4168    192    -54    753       C  
ATOM   6180  C   ASP C 142      27.329   6.413  50.186  1.00 39.69           C  
ANISOU 6180  C   ASP C 142     5321   5306   4453    178    -81    711       C  
ATOM   6181  O   ASP C 142      26.887   6.359  49.034  1.00 33.87           O  
ANISOU 6181  O   ASP C 142     4577   4527   3765    160    -71    695       O  
ATOM   6182  CB  ASP C 142      26.809   4.179  51.125  1.00 37.03           C  
ANISOU 6182  CB  ASP C 142     5021   4937   4113    218    -38    801       C  
ATOM   6183  CG  ASP C 142      26.273   3.359  52.290  1.00 54.86           C  
ANISOU 6183  CG  ASP C 142     7307   7196   6342    239    -11    849       C  
ATOM   6184  OD1 ASP C 142      25.876   3.955  53.308  1.00 50.22           O  
ANISOU 6184  OD1 ASP C 142     6731   6642   5710    235     -7    846       O  
ATOM   6185  OD2 ASP C 142      26.262   2.112  52.193  1.00 57.59           O  
ANISOU 6185  OD2 ASP C 142     7664   7509   6710    259     10    891       O  
ATOM   6186  N   VAL C 143      28.422   7.090  50.528  1.00 38.18           N  
ANISOU 6186  N   VAL C 143     5115   5163   4229    186   -116    694       N  
ATOM   6187  CA  VAL C 143      29.342   7.644  49.544  1.00 36.51           C  
ANISOU 6187  CA  VAL C 143     4878   4953   4041    178   -143    660       C  
ATOM   6188  C   VAL C 143      29.991   6.501  48.758  1.00 45.50           C  
ANISOU 6188  C   VAL C 143     6011   6062   5214    198   -146    686       C  
ATOM   6189  O   VAL C 143      30.693   5.669  49.335  1.00 43.48           O  
ANISOU 6189  O   VAL C 143     5759   5822   4938    229   -155    722       O  
ATOM   6190  CB  VAL C 143      30.452   8.468  50.221  1.00 35.61           C  
ANISOU 6190  CB  VAL C 143     4748   4900   3882    187   -178    638       C  
ATOM   6191  CG1 VAL C 143      31.481   8.918  49.194  1.00 43.09           C  
ANISOU 6191  CG1 VAL C 143     5670   5847   4857    181   -203    606       C  
ATOM   6192  CG2 VAL C 143      29.864   9.668  50.940  1.00 39.59           C  
ANISOU 6192  CG2 VAL C 143     5255   5434   4355    165   -175    607       C  
ATOM   6193  N   PRO C 144      29.769   6.468  47.433  1.00 32.20           N  
ANISOU 6193  N   PRO C 144     4317   4335   3582    180   -139    667       N  
ATOM   6194  CA  PRO C 144      30.288   5.382  46.591  1.00 37.63           C  
ANISOU 6194  CA  PRO C 144     4999   4990   4308    195   -139    688       C  
ATOM   6195  C   PRO C 144      31.803   5.482  46.372  1.00 41.17           C  
ANISOU 6195  C   PRO C 144     5427   5466   4750    211   -174    680       C  
ATOM   6196  O   PRO C 144      32.417   6.500  46.686  1.00 37.81           O  
ANISOU 6196  O   PRO C 144     4988   5081   4296    206   -199    650       O  
ATOM   6197  CB  PRO C 144      29.553   5.599  45.272  1.00 36.06           C  
ANISOU 6197  CB  PRO C 144     4794   4747   4160    167   -123    661       C  
ATOM   6198  CG  PRO C 144      29.352   7.091  45.219  1.00 32.58           C  
ANISOU 6198  CG  PRO C 144     4345   4329   3706    142   -134    616       C  
ATOM   6199  CD  PRO C 144      29.046   7.484  46.647  1.00 30.30           C  
ANISOU 6199  CD  PRO C 144     4070   4078   3366    146   -132    624       C  
ATOM   6200  N   GLU C 145      32.394   4.427  45.826  1.00 61.23           N  
ANISOU 6200  N   GLU C 145     7962   7983   7318    230   -175    704       N  
ATOM   6201  CA  GLU C 145      33.837   4.380  45.649  1.00 69.78           C  
ANISOU 6201  CA  GLU C 145     9026   9089   8397    248   -208    699       C  
ATOM   6202  C   GLU C 145      34.303   5.394  44.606  1.00 65.27           C  
ANISOU 6202  C   GLU C 145     8432   8518   7848    224   -225    649       C  
ATOM   6203  O   GLU C 145      33.728   5.497  43.520  1.00 66.05           O  
ANISOU 6203  O   GLU C 145     8530   8579   7988    202   -210    631       O  
ATOM   6204  CB  GLU C 145      34.272   2.978  45.239  1.00 79.38           C  
ANISOU 6204  CB  GLU C 145    10242  10274   9644    272   -201    737       C  
ATOM   6205  CG  GLU C 145      35.760   2.753  45.344  1.00 87.58           C  
ANISOU 6205  CG  GLU C 145    11264  11342  10671    299   -233    742       C  
ATOM   6206  CD  GLU C 145      36.219   1.605  44.475  1.00109.18           C  
ANISOU 6206  CD  GLU C 145    13993  14038  13453    312   -227    763       C  
ATOM   6207  OE1 GLU C 145      37.208   0.934  44.841  1.00121.77           O  
ANISOU 6207  OE1 GLU C 145    15580  15648  15037    344   -243    788       O  
ATOM   6208  OE2 GLU C 145      35.586   1.378  43.419  1.00109.69           O  
ANISOU 6208  OE2 GLU C 145    14057  14057  13564    291   -206    752       O  
ATOM   6209  N   GLY C 146      35.343   6.147  44.950  1.00 53.73           N  
ANISOU 6209  N   GLY C 146     6954   7101   6359    229   -255    626       N  
ATOM   6210  CA  GLY C 146      35.911   7.127  44.044  1.00 49.57           C  
ANISOU 6210  CA  GLY C 146     6406   6577   5852    208   -271    579       C  
ATOM   6211  C   GLY C 146      35.404   8.545  44.247  1.00 46.69           C  
ANISOU 6211  C   GLY C 146     6040   6231   5469    181   -270    540       C  
ATOM   6212  O   GLY C 146      35.960   9.494  43.690  1.00 46.73           O  
ANISOU 6212  O   GLY C 146     6027   6245   5484    165   -283    500       O  
ATOM   6213  N   ASN C 147      34.353   8.698  45.049  1.00 41.55           N  
ANISOU 6213  N   ASN C 147     5408   5585   4795    175   -252    550       N  
ATOM   6214  CA  ASN C 147      33.739  10.006  45.232  1.00 38.61           C  
ANISOU 6214  CA  ASN C 147     5034   5226   4410    148   -247    514       C  
ATOM   6215  C   ASN C 147      33.856  10.550  46.644  1.00 39.75           C  
ANISOU 6215  C   ASN C 147     5182   5423   4500    154   -258    510       C  
ATOM   6216  O   ASN C 147      34.165   9.823  47.581  1.00 39.52           O  
ANISOU 6216  O   ASN C 147     5159   5417   4438    181   -264    543       O  
ATOM   6217  CB  ASN C 147      32.272   9.966  44.802  1.00 38.83           C  
ANISOU 6217  CB  ASN C 147     5080   5213   4462    128   -216    517       C  
ATOM   6218  CG  ASN C 147      32.116   9.647  43.335  1.00 36.80           C  
ANISOU 6218  CG  ASN C 147     4816   4908   4257    118   -206    510       C  
ATOM   6219  OD1 ASN C 147      31.849   8.513  42.964  1.00 30.87           O  
ANISOU 6219  OD1 ASN C 147     4073   4126   3530    128   -193    540       O  
ATOM   6220  ND2 ASN C 147      32.314  10.651  42.486  1.00 33.56           N  
ANISOU 6220  ND2 ASN C 147     4392   4494   3865     98   -213    471       N  
ATOM   6221  N   THR C 148      33.600  11.839  46.796  1.00 38.39           N  
ANISOU 6221  N   THR C 148     5002   5267   4316    131   -258    471       N  
ATOM   6222  CA  THR C 148      33.654  12.447  48.108  1.00 36.37           C  
ANISOU 6222  CA  THR C 148     4747   5062   4009    133   -266    461       C  
ATOM   6223  C   THR C 148      32.259  12.655  48.673  1.00 41.92           C  
ANISOU 6223  C   THR C 148     5472   5756   4700    119   -239    468       C  
ATOM   6224  O   THR C 148      31.255  12.476  47.978  1.00 41.64           O  
ANISOU 6224  O   THR C 148     5447   5675   4698    104   -215    474       O  
ATOM   6225  CB  THR C 148      34.345  13.800  48.062  1.00 35.84           C  
ANISOU 6225  CB  THR C 148     4657   5026   3936    116   -283    409       C  
ATOM   6226  OG1 THR C 148      33.601  14.671  47.202  1.00 36.68           O  
ANISOU 6226  OG1 THR C 148     4762   5098   4074     85   -265    379       O  
ATOM   6227  CG2 THR C 148      35.775  13.660  47.546  1.00 36.16           C  
ANISOU 6227  CG2 THR C 148     4674   5078   3987    129   -310    398       C  
ATOM   6228  N   LYS C 149      32.218  13.048  49.941  1.00 41.53           N  
ANISOU 6228  N   LYS C 149     5426   5752   4602    123   -244    466       N  
ATOM   6229  CA  LYS C 149      30.986  13.444  50.612  1.00 46.68           C  
ANISOU 6229  CA  LYS C 149     6095   6403   5236    108   -220    465       C  
ATOM   6230  C   LYS C 149      30.282  14.575  49.862  1.00 44.74           C  
ANISOU 6230  C   LYS C 149     5844   6133   5022     73   -206    423       C  
ATOM   6231  O   LYS C 149      29.077  14.494  49.583  1.00 40.20           O  
ANISOU 6231  O   LYS C 149     5284   5522   4467     59   -180    430       O  
ATOM   6232  CB  LYS C 149      31.305  13.887  52.044  1.00 45.70           C  
ANISOU 6232  CB  LYS C 149     5970   6340   5052    117   -233    458       C  
ATOM   6233  CG  LYS C 149      30.107  14.363  52.855  1.00 55.24           C  
ANISOU 6233  CG  LYS C 149     7195   7555   6238    100   -209    454       C  
ATOM   6234  CD  LYS C 149      30.409  14.300  54.353  1.00 57.25           C  
ANISOU 6234  CD  LYS C 149     7455   7868   6429    120   -220    466       C  
ATOM   6235  CE  LYS C 149      29.154  13.955  55.155  1.00 66.84           C  
ANISOU 6235  CE  LYS C 149     8698   9076   7623    118   -190    493       C  
ATOM   6236  NZ  LYS C 149      29.483  13.321  56.466  1.00 71.28           N  
ANISOU 6236  NZ  LYS C 149     9272   9684   8126    148   -198    527       N  
ATOM   6237  N  AGLU C 150      31.020  15.638  49.540  0.42 39.48           N  
ANISOU 6237  N  AGLU C 150     5155   5484   4360     60   -222    380       N  
ATOM   6238  N  BGLU C 150      31.052  15.613  49.547  0.58 39.48           N  
ANISOU 6238  N  BGLU C 150     5156   5486   4360     60   -223    381       N  
ATOM   6239  CA AGLU C 150      30.427  16.791  48.854  0.42 37.70           C  
ANISOU 6239  CA AGLU C 150     4923   5237   4163     28   -208    341       C  
ATOM   6240  CA BGLU C 150      30.566  16.799  48.853  0.58 37.76           C  
ANISOU 6240  CA BGLU C 150     4929   5248   4170     30   -211    340       C  
ATOM   6241  C  AGLU C 150      29.942  16.437  47.449  0.42 36.44           C  
ANISOU 6241  C  AGLU C 150     4768   5022   4057     21   -195    348       C  
ATOM   6242  C  BGLU C 150      29.988  16.453  47.479  0.58 36.45           C  
ANISOU 6242  C  BGLU C 150     4769   5025   4057     21   -196    347       C  
ATOM   6243  O  AGLU C 150      28.857  16.848  47.039  0.42 38.03           O  
ANISOU 6243  O  AGLU C 150     4977   5193   4279      2   -173    339       O  
ATOM   6244  O  BGLU C 150      28.890  16.879  47.125  0.58 38.07           O  
ANISOU 6244  O  BGLU C 150     4982   5203   4282      2   -174    338       O  
ATOM   6245  CB AGLU C 150      31.390  17.987  48.801  0.42 39.87           C  
ANISOU 6245  CB AGLU C 150     5173   5542   4434     17   -226    293       C  
ATOM   6246  CB BGLU C 150      31.710  17.810  48.700  0.58 39.78           C  
ANISOU 6246  CB BGLU C 150     5158   5532   4424     22   -232    296       C  
ATOM   6247  CG AGLU C 150      30.844  19.244  49.485  0.42 38.87           C  
ANISOU 6247  CG AGLU C 150     5044   5438   4289     -6   -215    257       C  
ATOM   6248  CG BGLU C 150      32.334  18.287  50.021  0.58 40.25           C  
ANISOU 6248  CG BGLU C 150     5208   5654   4433     29   -249    279       C  
ATOM   6249  CD AGLU C 150      31.364  20.542  48.883  0.42 42.23           C  
ANISOU 6249  CD AGLU C 150     5446   5863   4736    -28   -218    206       C  
ATOM   6250  CD BGLU C 150      33.072  17.187  50.787  0.58 40.62           C  
ANISOU 6250  CD BGLU C 150     5258   5733   4444     63   -269    315       C  
ATOM   6251  OE1AGLU C 150      30.619  21.546  48.918  0.42 35.89           O  
ANISOU 6251  OE1AGLU C 150     4644   5052   3940    -51   -200    179       O  
ATOM   6252  OE1BGLU C 150      33.608  16.247  50.159  0.58 40.17           O  
ANISOU 6252  OE1BGLU C 150     5201   5657   4407     81   -279    341       O  
ATOM   6253  OE2AGLU C 150      32.513  20.566  48.382  0.42 43.15           O  
ANISOU 6253  OE2AGLU C 150     5544   5986   4863    -21   -237    193       O  
ATOM   6254  OE2BGLU C 150      33.114  17.270  52.032  0.58 40.96           O  
ANISOU 6254  OE2BGLU C 150     5303   5822   4438     72   -276    317       O  
ATOM   6255  N   GLU C 151      30.748  15.683  46.711  1.00 36.20           N  
ANISOU 6255  N   GLU C 151     4731   4977   4047     36   -208    363       N  
ATOM   6256  CA  GLU C 151      30.340  15.264  45.378  1.00 34.46           C  
ANISOU 6256  CA  GLU C 151     4512   4706   3874     30   -196    370       C  
ATOM   6257  C   GLU C 151      29.016  14.506  45.441  1.00 38.78           C  
ANISOU 6257  C   GLU C 151     5082   5223   4432     30   -170    399       C  
ATOM   6258  O   GLU C 151      28.114  14.753  44.638  1.00 31.20           O  
ANISOU 6258  O   GLU C 151     4124   4227   3502     13   -152    389       O  
ATOM   6259  CB  GLU C 151      31.413  14.379  44.741  1.00 36.85           C  
ANISOU 6259  CB  GLU C 151     4806   5001   4194     50   -213    386       C  
ATOM   6260  CG  GLU C 151      32.596  15.136  44.132  1.00 35.58           C  
ANISOU 6260  CG  GLU C 151     4621   4852   4043     45   -233    352       C  
ATOM   6261  CD  GLU C 151      33.634  14.185  43.543  1.00 47.87           C  
ANISOU 6261  CD  GLU C 151     6169   6401   5617     65   -249    369       C  
ATOM   6262  OE1 GLU C 151      33.646  12.993  43.942  1.00 42.75           O  
ANISOU 6262  OE1 GLU C 151     5532   5752   4961     87   -250    408       O  
ATOM   6263  OE2 GLU C 151      34.430  14.622  42.677  1.00 51.81           O  
ANISOU 6263  OE2 GLU C 151     6652   6895   6140     58   -259    344       O  
ATOM   6264  N   THR C 152      28.907  13.588  46.402  1.00 32.74           N  
ANISOU 6264  N   THR C 152     4331   4471   3639     49   -167    435       N  
ATOM   6265  CA  THR C 152      27.721  12.749  46.539  1.00 27.95           C  
ANISOU 6265  CA  THR C 152     3745   3834   3042     50   -141    465       C  
ATOM   6266  C   THR C 152      26.482  13.585  46.801  1.00 27.34           C  
ANISOU 6266  C   THR C 152     3675   3750   2962     26   -120    445       C  
ATOM   6267  O   THR C 152      25.423  13.307  46.246  1.00 31.32           O  
ANISOU 6267  O   THR C 152     4187   4217   3496     16    -97    449       O  
ATOM   6268  CB  THR C 152      27.915  11.660  47.609  1.00 32.25           C  
ANISOU 6268  CB  THR C 152     4303   4395   3554     76   -140    508       C  
ATOM   6269  OG1 THR C 152      29.022  10.832  47.229  1.00 32.27           O  
ANISOU 6269  OG1 THR C 152     4298   4398   3566     99   -158    528       O  
ATOM   6270  CG2 THR C 152      26.664  10.782  47.733  1.00 31.48           C  
ANISOU 6270  CG2 THR C 152     4227   4263   3470     76   -108    539       C  
ATOM   6271  N   CYS C 153      26.634  14.637  47.600  1.00 30.71           N  
ANISOU 6271  N   CYS C 153     4097   4215   3356     17   -127    420       N  
ATOM   6272  CA  CYS C 153      25.541  15.561  47.903  1.00 32.72           C  
ANISOU 6272  CA  CYS C 153     4357   4467   3609     -6   -108    397       C  
ATOM   6273  C   CYS C 153      25.178  16.537  46.775  1.00 34.17           C  
ANISOU 6273  C   CYS C 153     4529   4625   3830    -29   -103    361       C  
ATOM   6274  O   CYS C 153      24.023  16.956  46.664  1.00 31.65           O  
ANISOU 6274  O   CYS C 153     4217   4286   3524    -46    -82    350       O  
ATOM   6275  CB  CYS C 153      25.844  16.328  49.194  1.00 39.39           C  
ANISOU 6275  CB  CYS C 153     5199   5362   4404     -8   -116    381       C  
ATOM   6276  SG  CYS C 153      25.829  15.253  50.657  1.00 59.51           S  
ANISOU 6276  SG  CYS C 153     7767   7940   6903     17   -114    426       S  
ATOM   6277  N   PHE C 154      26.155  16.913  45.952  1.00 28.98           N  
ANISOU 6277  N   PHE C 154     3855   3968   3189    -29   -121    342       N  
ATOM   6278  CA  PHE C 154      25.855  17.683  44.745  1.00 31.42           C  
ANISOU 6278  CA  PHE C 154     4155   4248   3536    -46   -115    315       C  
ATOM   6279  C   PHE C 154      24.944  16.897  43.805  1.00 23.89           C  
ANISOU 6279  C   PHE C 154     3210   3249   2619    -46    -99    333       C  
ATOM   6280  O   PHE C 154      23.941  17.405  43.331  1.00 29.15           O  
ANISOU 6280  O   PHE C 154     3878   3893   3306    -61    -82    319       O  
ATOM   6281  CB  PHE C 154      27.142  18.075  44.012  1.00 30.00           C  
ANISOU 6281  CB  PHE C 154     3956   4074   3368    -43   -136    296       C  
ATOM   6282  CG  PHE C 154      27.763  19.343  44.528  1.00 36.11           C  
ANISOU 6282  CG  PHE C 154     4716   4882   4122    -55   -145    260       C  
ATOM   6283  CD1 PHE C 154      26.993  20.485  44.699  1.00 39.74           C  
ANISOU 6283  CD1 PHE C 154     5175   5340   4583    -75   -129    233       C  
ATOM   6284  CD2 PHE C 154      29.111  19.388  44.867  1.00 36.71           C  
ANISOU 6284  CD2 PHE C 154     4778   4991   4180    -44   -168    252       C  
ATOM   6285  CE1 PHE C 154      27.560  21.664  45.183  1.00 39.97           C  
ANISOU 6285  CE1 PHE C 154     5191   5399   4597    -87   -135    197       C  
ATOM   6286  CE2 PHE C 154      29.683  20.562  45.358  1.00 39.48           C  
ANISOU 6286  CE2 PHE C 154     5114   5374   4515    -56   -175    214       C  
ATOM   6287  CZ  PHE C 154      28.904  21.698  45.515  1.00 43.20           C  
ANISOU 6287  CZ  PHE C 154     5585   5842   4989    -78   -157    186       C  
ATOM   6288  N   PHE C 155      25.311  15.652  43.539  1.00 25.32           N  
ANISOU 6288  N   PHE C 155     3395   3418   2809    -28   -103    363       N  
ATOM   6289  CA  PHE C 155      24.518  14.776  42.701  1.00 26.88           C  
ANISOU 6289  CA  PHE C 155     3598   3574   3041    -27    -87    380       C  
ATOM   6290  C   PHE C 155      23.090  14.621  43.258  1.00 27.53           C  
ANISOU 6290  C   PHE C 155     3695   3643   3121    -36    -61    388       C  
ATOM   6291  O   PHE C 155      22.117  14.977  42.597  1.00 27.38           O  
ANISOU 6291  O   PHE C 155     3676   3600   3128    -50    -47    372       O  
ATOM   6292  CB  PHE C 155      25.229  13.427  42.592  1.00 23.89           C  
ANISOU 6292  CB  PHE C 155     3221   3188   2667     -5    -95    412       C  
ATOM   6293  CG  PHE C 155      24.481  12.384  41.800  1.00 27.52           C  
ANISOU 6293  CG  PHE C 155     3686   3607   3163     -3    -77    430       C  
ATOM   6294  CD1 PHE C 155      24.206  12.572  40.456  1.00 26.56           C  
ANISOU 6294  CD1 PHE C 155     3556   3458   3079    -13    -75    411       C  
ATOM   6295  CD2 PHE C 155      24.093  11.184  42.400  1.00 29.56           C  
ANISOU 6295  CD2 PHE C 155     3958   3855   3418      9    -62    465       C  
ATOM   6296  CE1 PHE C 155      23.529  11.592  39.717  1.00 28.08           C  
ANISOU 6296  CE1 PHE C 155     3750   3614   3304    -11    -59    423       C  
ATOM   6297  CE2 PHE C 155      23.415  10.201  41.676  1.00 33.75           C  
ANISOU 6297  CE2 PHE C 155     4492   4347   3985     10    -44    478       C  
ATOM   6298  CZ  PHE C 155      23.128  10.401  40.340  1.00 33.22           C  
ANISOU 6298  CZ  PHE C 155     4413   4254   3954     -1    -43    455       C  
ATOM   6299  N   VAL C 156      22.968  14.114  44.482  1.00 25.04           N  
ANISOU 6299  N   VAL C 156     3393   3347   2774    -27    -55    411       N  
ATOM   6300  CA  VAL C 156      21.652  13.843  45.058  1.00 21.92           C  
ANISOU 6300  CA  VAL C 156     3013   2938   2377    -34    -28    421       C  
ATOM   6301  C   VAL C 156      20.787  15.096  45.130  1.00 22.15           C  
ANISOU 6301  C   VAL C 156     3040   2969   2407    -57    -18    388       C  
ATOM   6302  O   VAL C 156      19.604  15.056  44.795  1.00 29.32           O  
ANISOU 6302  O   VAL C 156     3952   3850   3338    -68      3    384       O  
ATOM   6303  CB  VAL C 156      21.762  13.216  46.464  1.00 28.61           C  
ANISOU 6303  CB  VAL C 156     3876   3810   3185    -20    -24    452       C  
ATOM   6304  CG1 VAL C 156      20.384  12.867  47.000  1.00 28.37           C  
ANISOU 6304  CG1 VAL C 156     3861   3761   3156    -28      8    463       C  
ATOM   6305  CG2 VAL C 156      22.626  11.994  46.417  1.00 25.92           C  
ANISOU 6305  CG2 VAL C 156     3537   3467   2844      5    -33    486       C  
ATOM   6306  N   GLU C 157      21.373  16.204  45.575  1.00 21.64           N  
ANISOU 6306  N   GLU C 157     2968   2937   2318    -63    -32    364       N  
ATOM   6307  CA  GLU C 157      20.620  17.452  45.696  1.00 28.49           C  
ANISOU 6307  CA  GLU C 157     3832   3807   3186    -84    -22    332       C  
ATOM   6308  C   GLU C 157      20.170  17.956  44.337  1.00 29.07           C  
ANISOU 6308  C   GLU C 157     3896   3849   3301    -95    -18    311       C  
ATOM   6309  O   GLU C 157      19.114  18.567  44.229  1.00 27.55           O  
ANISOU 6309  O   GLU C 157     3705   3643   3122   -110     -2    295       O  
ATOM   6310  CB  GLU C 157      21.430  18.544  46.398  1.00 27.92           C  
ANISOU 6310  CB  GLU C 157     3751   3776   3083    -90    -37    308       C  
ATOM   6311  CG  GLU C 157      21.741  18.253  47.861  1.00 29.53           C  
ANISOU 6311  CG  GLU C 157     3964   4018   3239    -81    -40    323       C  
ATOM   6312  CD  GLU C 157      22.735  19.240  48.442  1.00 49.79           C  
ANISOU 6312  CD  GLU C 157     6516   6627   5776    -84    -59    296       C  
ATOM   6313  OE1 GLU C 157      22.769  20.402  47.976  1.00 50.33           O  
ANISOU 6313  OE1 GLU C 157     6571   6692   5859   -100    -59    261       O  
ATOM   6314  OE2 GLU C 157      23.493  18.849  49.357  1.00 49.18           O  
ANISOU 6314  OE2 GLU C 157     6440   6585   5660    -69    -73    310       O  
ATOM   6315  N   ALA C 158      20.975  17.706  43.304  1.00 28.16           N  
ANISOU 6315  N   ALA C 158     3770   3722   3206    -87    -33    312       N  
ATOM   6316  CA  ALA C 158      20.560  18.034  41.953  1.00 29.14           C  
ANISOU 6316  CA  ALA C 158     3887   3817   3369    -93    -30    296       C  
ATOM   6317  C   ALA C 158      19.276  17.277  41.657  1.00 26.48           C  
ANISOU 6317  C   ALA C 158     3558   3449   3055    -95     -9    308       C  
ATOM   6318  O   ALA C 158      18.300  17.864  41.219  1.00 29.01           O  
ANISOU 6318  O   ALA C 158     3875   3753   3392   -107      3    290       O  
ATOM   6319  CB  ALA C 158      21.647  17.668  40.939  1.00 25.13           C  
ANISOU 6319  CB  ALA C 158     3369   3302   2878    -83    -48    299       C  
ATOM   6320  N   LEU C 159      19.287  15.971  41.908  1.00 19.90           N  
ANISOU 6320  N   LEU C 159     2732   2608   2221    -83     -5    338       N  
ATOM   6321  CA  LEU C 159      18.112  15.135  41.678  1.00 26.04           C  
ANISOU 6321  CA  LEU C 159     3517   3356   3022    -85     17    349       C  
ATOM   6322  C   LEU C 159      16.909  15.586  42.526  1.00 23.39           C  
ANISOU 6322  C   LEU C 159     3190   3022   2676    -98     39    341       C  
ATOM   6323  O   LEU C 159      15.808  15.809  42.010  1.00 24.61           O  
ANISOU 6323  O   LEU C 159     3341   3155   2855   -108     54    326       O  
ATOM   6324  CB  LEU C 159      18.435  13.657  41.944  1.00 27.61           C  
ANISOU 6324  CB  LEU C 159     3723   3546   3221    -69     21    384       C  
ATOM   6325  CG  LEU C 159      19.568  13.042  41.108  1.00 29.36           C  
ANISOU 6325  CG  LEU C 159     3936   3762   3456    -55      3    393       C  
ATOM   6326  CD1 LEU C 159      19.854  11.598  41.518  1.00 32.13           C  
ANISOU 6326  CD1 LEU C 159     4297   4105   3807    -38      9    430       C  
ATOM   6327  CD2 LEU C 159      19.253  13.137  39.619  1.00 29.37           C  
ANISOU 6327  CD2 LEU C 159     3926   3738   3497    -60      2    374       C  
ATOM   6328  N   ILE C 160      17.130  15.747  43.822  1.00 23.86           N  
ANISOU 6328  N   ILE C 160     3259   3109   2699    -98     40    350       N  
ATOM   6329  CA  ILE C 160      16.043  16.127  44.709  1.00 22.16           C  
ANISOU 6329  CA  ILE C 160     3052   2896   2470   -110     61    343       C  
ATOM   6330  C   ILE C 160      15.454  17.499  44.381  1.00 21.97           C  
ANISOU 6330  C   ILE C 160     3020   2872   2457   -128     64    308       C  
ATOM   6331  O   ILE C 160      14.235  17.679  44.391  1.00 22.34           O  
ANISOU 6331  O   ILE C 160     3068   2902   2518   -139     84    297       O  
ATOM   6332  CB  ILE C 160      16.491  16.108  46.169  1.00 28.61           C  
ANISOU 6332  CB  ILE C 160     3881   3747   3241   -105     60    358       C  
ATOM   6333  CG1 ILE C 160      16.730  14.663  46.634  1.00 32.52           C  
ANISOU 6333  CG1 ILE C 160     4390   4239   3729    -87     67    398       C  
ATOM   6334  CG2 ILE C 160      15.465  16.830  47.032  1.00 23.79           C  
ANISOU 6334  CG2 ILE C 160     3277   3145   2617   -122     80    343       C  
ATOM   6335  CD1 ILE C 160      17.215  14.557  48.071  1.00 29.97           C  
ANISOU 6335  CD1 ILE C 160     4079   3952   3355    -78     65    417       C  
ATOM   6336  N   GLN C 161      16.312  18.474  44.092  1.00 25.92           N  
ANISOU 6336  N   GLN C 161     3509   3390   2951   -130     45    288       N  
ATOM   6337  CA  GLN C 161      15.824  19.806  43.738  1.00 22.72           C  
ANISOU 6337  CA  GLN C 161     3095   2981   2556   -144     49    255       C  
ATOM   6338  C   GLN C 161      14.944  19.756  42.480  1.00 23.95           C  
ANISOU 6338  C   GLN C 161     3244   3103   2753   -147     57    247       C  
ATOM   6339  O   GLN C 161      13.907  20.411  42.405  1.00 27.65           O  
ANISOU 6339  O   GLN C 161     3711   3561   3234   -158     71    229       O  
ATOM   6340  CB  GLN C 161      16.994  20.770  43.533  1.00 35.39           C  
ANISOU 6340  CB  GLN C 161     4688   4607   4152   -145     29    237       C  
ATOM   6341  CG  GLN C 161      16.577  22.219  43.266  1.00 34.15           C  
ANISOU 6341  CG  GLN C 161     4523   4448   4006   -160     35    204       C  
ATOM   6342  CD  GLN C 161      16.017  22.913  44.500  1.00 43.84           C  
ANISOU 6342  CD  GLN C 161     5754   5693   5209   -174     49    191       C  
ATOM   6343  OE1 GLN C 161      16.627  22.884  45.567  1.00 46.85           O  
ANISOU 6343  OE1 GLN C 161     6139   6106   5556   -173     43    194       O  
ATOM   6344  NE2 GLN C 161      14.843  23.533  44.357  1.00 36.88           N  
ANISOU 6344  NE2 GLN C 161     4872   4796   4346   -185     67    175       N  
ATOM   6345  N   SER C 162      15.360  18.971  41.495  1.00 22.90           N  
ANISOU 6345  N   SER C 162     3106   2954   2640   -135     47    258       N  
ATOM   6346  CA  SER C 162      14.537  18.749  40.312  1.00 22.80           C  
ANISOU 6346  CA  SER C 162     3087   2912   2664   -135     54    251       C  
ATOM   6347  C   SER C 162      13.187  18.151  40.695  1.00 26.16           C  
ANISOU 6347  C   SER C 162     3519   3321   3100   -141     77    255       C  
ATOM   6348  O   SER C 162      12.143  18.532  40.144  1.00 23.19           O  
ANISOU 6348  O   SER C 162     3137   2929   2747   -147     88    238       O  
ATOM   6349  CB  SER C 162      15.252  17.807  39.350  1.00 19.05           C  
ANISOU 6349  CB  SER C 162     2608   2425   2205   -121     41    265       C  
ATOM   6350  OG  SER C 162      16.410  18.415  38.810  1.00 27.97           O  
ANISOU 6350  OG  SER C 162     3730   3566   3331   -117     21    258       O  
ATOM   6351  N   ASN C 163      13.196  17.199  41.627  1.00 16.89           N  
ANISOU 6351  N   ASN C 163     2357   2151   1911   -137     87    279       N  
ATOM   6352  CA  ASN C 163      11.922  16.611  42.062  1.00 23.45           C  
ANISOU 6352  CA  ASN C 163     3195   2964   2752   -144    113    283       C  
ATOM   6353  C   ASN C 163      11.021  17.642  42.709  1.00 16.68           C  
ANISOU 6353  C   ASN C 163     2337   2113   1886   -159    127    262       C  
ATOM   6354  O   ASN C 163       9.853  17.755  42.341  1.00 19.56           O  
ANISOU 6354  O   ASN C 163     2698   2460   2276   -167    142    247       O  
ATOM   6355  CB  ASN C 163      12.118  15.364  42.942  1.00 22.53           C  
ANISOU 6355  CB  ASN C 163     3093   2848   2621   -136    124    316       C  
ATOM   6356  CG  ASN C 163      12.737  14.210  42.169  1.00 27.03           C  
ANISOU 6356  CG  ASN C 163     3659   3402   3210   -121    117    335       C  
ATOM   6357  OD1 ASN C 163      12.575  14.116  40.944  1.00 26.80           O  
ANISOU 6357  OD1 ASN C 163     3616   3354   3211   -121    112    322       O  
ATOM   6358  ND2 ASN C 163      13.457  13.332  42.871  1.00 30.35           N  
ANISOU 6358  ND2 ASN C 163     4090   3830   3610   -109    117    365       N  
ATOM   6359  N   LEU C 164      11.581  18.444  43.614  1.00 21.48           N  
ANISOU 6359  N   LEU C 164     2951   2750   2462   -163    120    259       N  
ATOM   6360  CA  LEU C 164      10.810  19.471  44.307  1.00 22.52           C  
ANISOU 6360  CA  LEU C 164     3083   2889   2583   -179    134    237       C  
ATOM   6361  C   LEU C 164      10.292  20.551  43.365  1.00 24.63           C  
ANISOU 6361  C   LEU C 164     3336   3145   2877   -185    132    208       C  
ATOM   6362  O   LEU C 164       9.150  20.980  43.491  1.00 21.44           O  
ANISOU 6362  O   LEU C 164     2931   2731   2486   -196    149    192       O  
ATOM   6363  CB  LEU C 164      11.621  20.095  45.452  1.00 19.68           C  
ANISOU 6363  CB  LEU C 164     2729   2565   2182   -182    126    237       C  
ATOM   6364  CG  LEU C 164      12.022  19.093  46.534  1.00 24.38           C  
ANISOU 6364  CG  LEU C 164     3341   3177   2747   -173    130    267       C  
ATOM   6365  CD1 LEU C 164      12.964  19.740  47.542  1.00 21.16           C  
ANISOU 6365  CD1 LEU C 164     2934   2808   2296   -174    117    264       C  
ATOM   6366  CD2 LEU C 164      10.775  18.501  47.228  1.00 27.16           C  
ANISOU 6366  CD2 LEU C 164     3704   3514   3100   -180    160    276       C  
ATOM   6367  N   ASN C 165      11.129  20.995  42.429  1.00 21.98           N  
ANISOU 6367  N   ASN C 165     2991   2810   2549   -179    111    201       N  
ATOM   6368  CA  ASN C 165      10.702  21.980  41.444  1.00 21.97           C  
ANISOU 6368  CA  ASN C 165     2978   2797   2572   -181    110    178       C  
ATOM   6369  C   ASN C 165       9.509  21.474  40.649  1.00 21.04           C  
ANISOU 6369  C   ASN C 165     2855   2653   2488   -180    121    173       C  
ATOM   6370  O   ASN C 165       8.579  22.213  40.376  1.00 24.14           O  
ANISOU 6370  O   ASN C 165     3240   3037   2896   -186    130    154       O  
ATOM   6371  CB  ASN C 165      11.852  22.343  40.491  1.00 16.25           C  
ANISOU 6371  CB  ASN C 165     2246   2077   1853   -172     88    176       C  
ATOM   6372  CG  ASN C 165      12.904  23.222  41.158  1.00 24.62           C  
ANISOU 6372  CG  ASN C 165     3306   3162   2886   -176     78    168       C  
ATOM   6373  OD1 ASN C 165      12.713  23.695  42.277  1.00 26.74           O  
ANISOU 6373  OD1 ASN C 165     3579   3447   3133   -187     88    161       O  
ATOM   6374  ND2 ASN C 165      14.007  23.459  40.465  1.00 23.89           N  
ANISOU 6374  ND2 ASN C 165     3208   3074   2796   -169     61    167       N  
ATOM   6375  N   SER C 166       9.549  20.206  40.266  1.00 21.20           N  
ANISOU 6375  N   SER C 166     2876   2661   2518   -171    120    191       N  
ATOM   6376  CA  SER C 166       8.455  19.631  39.498  1.00 21.74           C  
ANISOU 6376  CA  SER C 166     2937   2706   2619   -170    131    184       C  
ATOM   6377  C   SER C 166       7.216  19.491  40.376  1.00 20.20           C  
ANISOU 6377  C   SER C 166     2746   2503   2426   -182    156    179       C  
ATOM   6378  O   SER C 166       6.098  19.735  39.924  1.00 20.91           O  
ANISOU 6378  O   SER C 166     2827   2579   2540   -186    167    160       O  
ATOM   6379  CB  SER C 166       8.849  18.268  38.923  1.00 19.82           C  
ANISOU 6379  CB  SER C 166     2693   2450   2388   -159    126    203       C  
ATOM   6380  OG  SER C 166       7.814  17.759  38.093  1.00 20.27           O  
ANISOU 6380  OG  SER C 166     2739   2485   2477   -158    136    191       O  
ATOM   6381  N   LEU C 167       7.418  19.100  41.632  1.00 17.55           N  
ANISOU 6381  N   LEU C 167     2425   2179   2065   -187    167    195       N  
ATOM   6382  CA  LEU C 167       6.295  18.965  42.555  1.00 16.62           C  
ANISOU 6382  CA  LEU C 167     2313   2055   1946   -199    193    192       C  
ATOM   6383  C   LEU C 167       5.597  20.310  42.615  1.00 21.85           C  
ANISOU 6383  C   LEU C 167     2969   2722   2613   -209    198    163       C  
ATOM   6384  O   LEU C 167       4.369  20.401  42.526  1.00 21.33           O  
ANISOU 6384  O   LEU C 167     2896   2640   2568   -217    215    147       O  
ATOM   6385  CB  LEU C 167       6.756  18.544  43.959  1.00 16.10           C  
ANISOU 6385  CB  LEU C 167     2266   2007   1846   -201    202    214       C  
ATOM   6386  CG  LEU C 167       5.662  18.447  45.042  1.00 24.13           C  
ANISOU 6386  CG  LEU C 167     3291   3019   2856   -214    232    212       C  
ATOM   6387  CD1 LEU C 167       4.535  17.505  44.615  1.00 19.40           C  
ANISOU 6387  CD1 LEU C 167     2689   2390   2293   -216    254    210       C  
ATOM   6388  CD2 LEU C 167       6.257  17.999  46.377  1.00 18.99           C  
ANISOU 6388  CD2 LEU C 167     2660   2389   2165   -212    238    237       C  
ATOM   6389  N   ALA C 168       6.387  21.368  42.750  1.00 21.00           N  
ANISOU 6389  N   ALA C 168     2860   2633   2486   -210    183    156       N  
ATOM   6390  CA  ALA C 168       5.806  22.692  42.878  1.00 23.00           C  
ANISOU 6390  CA  ALA C 168     3106   2889   2742   -221    189    131       C  
ATOM   6391  C   ALA C 168       5.042  23.063  41.601  1.00 25.48           C  
ANISOU 6391  C   ALA C 168     3406   3184   3093   -215    187    112       C  
ATOM   6392  O   ALA C 168       3.943  23.610  41.649  1.00 27.58           O  
ANISOU 6392  O   ALA C 168     3664   3440   3373   -223    201     93       O  
ATOM   6393  CB  ALA C 168       6.896  23.709  43.191  1.00 23.30           C  
ANISOU 6393  CB  ALA C 168     3145   2950   2757   -222    175    125       C  
ATOM   6394  N   ASP C 169       5.618  22.750  40.450  1.00 29.46           N  
ANISOU 6394  N   ASP C 169     3902   3681   3608   -202    169    118       N  
ATOM   6395  CA  ASP C 169       4.972  23.127  39.200  1.00 31.62           C  
ANISOU 6395  CA  ASP C 169     4162   3941   3912   -194    164    102       C  
ATOM   6396  C   ASP C 169       3.677  22.355  38.985  1.00 34.27           C  
ANISOU 6396  C   ASP C 169     4489   4258   4272   -195    180     95       C  
ATOM   6397  O   ASP C 169       2.656  22.931  38.601  1.00 30.99           O  
ANISOU 6397  O   ASP C 169     4064   3835   3877   -196    186     74       O  
ATOM   6398  CB  ASP C 169       5.926  22.953  38.017  1.00 32.81           C  
ANISOU 6398  CB  ASP C 169     4308   4091   4068   -179    142    110       C  
ATOM   6399  CG  ASP C 169       7.023  24.013  37.999  1.00 50.98           C  
ANISOU 6399  CG  ASP C 169     6611   6406   6352   -177    129    109       C  
ATOM   6400  OD1 ASP C 169       6.793  25.124  38.536  1.00 54.85           O  
ANISOU 6400  OD1 ASP C 169     7101   6902   6837   -186    137     95       O  
ATOM   6401  OD2 ASP C 169       8.117  23.744  37.449  1.00 54.11           O  
ANISOU 6401  OD2 ASP C 169     7008   6807   6743   -168    112    120       O  
ATOM   6402  N   VAL C 170       3.710  21.052  39.254  1.00 24.11           N  
ANISOU 6402  N   VAL C 170     3209   2966   2986   -195    186    111       N  
ATOM   6403  CA  VAL C 170       2.511  20.234  39.073  1.00 24.83           C  
ANISOU 6403  CA  VAL C 170     3292   3038   3104   -198    204    102       C  
ATOM   6404  C   VAL C 170       1.373  20.692  39.977  1.00 28.39           C  
ANISOU 6404  C   VAL C 170     3744   3486   3557   -213    227     86       C  
ATOM   6405  O   VAL C 170       0.252  20.884  39.514  1.00 28.32           O  
ANISOU 6405  O   VAL C 170     3721   3465   3573   -214    235     64       O  
ATOM   6406  CB  VAL C 170       2.788  18.717  39.278  1.00 26.50           C  
ANISOU 6406  CB  VAL C 170     3512   3241   3318   -196    211    123       C  
ATOM   6407  CG1 VAL C 170       1.490  17.944  39.373  1.00 29.51           C  
ANISOU 6407  CG1 VAL C 170     3885   3602   3725   -204    237    112       C  
ATOM   6408  CG2 VAL C 170       3.632  18.177  38.146  1.00 24.71           C  
ANISOU 6408  CG2 VAL C 170     3279   3012   3099   -182    190    132       C  
ATOM   6409  N   THR C 171       1.655  20.879  41.264  1.00 24.92           N  
ANISOU 6409  N   THR C 171     3320   3058   3090   -224    238     97       N  
ATOM   6410  CA  THR C 171       0.587  21.199  42.210  1.00 23.37           C  
ANISOU 6410  CA  THR C 171     3126   2859   2894   -239    263     83       C  
ATOM   6411  C   THR C 171       0.055  22.622  42.006  1.00 26.54           C  
ANISOU 6411  C   THR C 171     3517   3264   3304   -242    261     57       C  
ATOM   6412  O   THR C 171      -1.128  22.893  42.213  1.00 21.95           O  
ANISOU 6412  O   THR C 171     2928   2673   2740   -251    279     38       O  
ATOM   6413  CB  THR C 171       1.022  20.976  43.663  1.00 24.77           C  
ANISOU 6413  CB  THR C 171     3324   3051   3038   -249    276    102       C  
ATOM   6414  OG1 THR C 171       2.120  21.841  43.970  1.00 23.22           O  
ANISOU 6414  OG1 THR C 171     3133   2877   2812   -247    258    106       O  
ATOM   6415  CG2 THR C 171       1.439  19.513  43.876  1.00 22.07           C  
ANISOU 6415  CG2 THR C 171     2993   2701   2691   -243    282    130       C  
ATOM   6416  N   GLU C 172       0.932  23.529  41.589  1.00 31.38           N  
ANISOU 6416  N   GLU C 172     4128   3889   3906   -236    241     57       N  
ATOM   6417  CA  GLU C 172       0.498  24.889  41.281  1.00 27.95           C  
ANISOU 6417  CA  GLU C 172     3683   3454   3481   -236    240     35       C  
ATOM   6418  C   GLU C 172      -0.423  24.917  40.062  1.00 29.95           C  
ANISOU 6418  C   GLU C 172     3919   3692   3770   -225    236     18       C  
ATOM   6419  O   GLU C 172      -1.431  25.615  40.060  1.00 35.10           O  
ANISOU 6419  O   GLU C 172     4561   4339   4438   -229    247     -3       O  
ATOM   6420  CB  GLU C 172       1.705  25.831  41.123  1.00 28.77           C  
ANISOU 6420  CB  GLU C 172     3790   3573   3567   -232    222     38       C  
ATOM   6421  CG  GLU C 172       2.485  25.985  42.437  1.00 29.43           C  
ANISOU 6421  CG  GLU C 172     3889   3677   3617   -244    227     47       C  
ATOM   6422  CD  GLU C 172       3.797  26.744  42.304  1.00 37.83           C  
ANISOU 6422  CD  GLU C 172     4955   4756   4663   -240    209     50       C  
ATOM   6423  OE1 GLU C 172       4.064  27.323  41.220  1.00 38.90           O  
ANISOU 6423  OE1 GLU C 172     5081   4885   4814   -229    196     45       O  
ATOM   6424  OE2 GLU C 172       4.565  26.759  43.297  1.00 30.89           O  
ANISOU 6424  OE2 GLU C 172     4086   3897   3755   -248    209     57       O  
ATOM   6425  N   ARG C 173      -0.091  24.146  39.032  1.00 34.44           N  
ANISOU 6425  N   ARG C 173     4481   4255   4348   -211    221     27       N  
ATOM   6426  CA  ARG C 173      -0.965  24.039  37.866  1.00 35.49           C  
ANISOU 6426  CA  ARG C 173     4596   4378   4512   -200    217     11       C  
ATOM   6427  C   ARG C 173      -2.329  23.494  38.290  1.00 45.68           C  
ANISOU 6427  C   ARG C 173     5879   5656   5823   -210    239     -5       C  
ATOM   6428  O   ARG C 173      -3.370  24.050  37.929  1.00 41.02           O  
ANISOU 6428  O   ARG C 173     5273   5060   5253   -207    244    -28       O  
ATOM   6429  CB  ARG C 173      -0.351  23.136  36.796  1.00 38.06           C  
ANISOU 6429  CB  ARG C 173     4917   4701   4843   -185    199     22       C  
ATOM   6430  CG  ARG C 173      -1.173  23.050  35.508  1.00 52.43           C  
ANISOU 6430  CG  ARG C 173     6716   6514   6691   -171    191      3       C  
ATOM   6431  CD  ARG C 173      -0.775  21.844  34.642  1.00 55.34           C  
ANISOU 6431  CD  ARG C 173     7080   6879   7068   -161    180     11       C  
ATOM   6432  NE  ARG C 173       0.678  21.669  34.566  1.00 66.32           N  
ANISOU 6432  NE  ARG C 173     8484   8278   8438   -157    165     35       N  
ATOM   6433  CZ  ARG C 173       1.335  20.587  34.984  1.00 56.53           C  
ANISOU 6433  CZ  ARG C 173     7254   7035   7190   -161    167     54       C  
ATOM   6434  NH1 ARG C 173       0.674  19.558  35.502  1.00 49.63           N  
ANISOU 6434  NH1 ARG C 173     6379   6149   6327   -171    187     53       N  
ATOM   6435  NH2 ARG C 173       2.659  20.530  34.879  1.00 62.81           N  
ANISOU 6435  NH2 ARG C 173     8059   7838   7966   -156    152     74       N  
ATOM   6436  N   LEU C 174      -2.316  22.405  39.060  1.00 38.93           N  
ANISOU 6436  N   LEU C 174     5034   4796   4962   -220    254      7       N  
ATOM   6437  CA  LEU C 174      -3.551  21.815  39.570  1.00 40.30           C  
ANISOU 6437  CA  LEU C 174     5201   4955   5154   -232    281     -7       C  
ATOM   6438  C   LEU C 174      -4.398  22.826  40.331  1.00 39.35           C  
ANISOU 6438  C   LEU C 174     5080   4836   5035   -244    297    -26       C  
ATOM   6439  O   LEU C 174      -5.600  22.937  40.104  1.00 44.33           O  
ANISOU 6439  O   LEU C 174     5694   5457   5692   -246    308    -50       O  
ATOM   6440  CB  LEU C 174      -3.251  20.612  40.461  1.00 33.64           C  
ANISOU 6440  CB  LEU C 174     4375   4107   4300   -242    298     14       C  
ATOM   6441  CG  LEU C 174      -2.803  19.409  39.640  1.00 41.67           C  
ANISOU 6441  CG  LEU C 174     5388   5116   5329   -231    289     26       C  
ATOM   6442  CD1 LEU C 174      -2.334  18.279  40.542  1.00 45.27           C  
ANISOU 6442  CD1 LEU C 174     5862   5567   5770   -237    305     52       C  
ATOM   6443  CD2 LEU C 174      -3.946  18.949  38.737  1.00 48.00           C  
ANISOU 6443  CD2 LEU C 174     6166   5903   6169   -228    295     -1       C  
ATOM   6444  N   GLN C 175      -3.760  23.559  41.233  1.00 28.94           N  
ANISOU 6444  N   GLN C 175     3777   3531   3689   -253    298    -16       N  
ATOM   6445  CA  GLN C 175      -4.434  24.593  42.011  1.00 35.62           C  
ANISOU 6445  CA  GLN C 175     4622   4379   4533   -265    314    -34       C  
ATOM   6446  C   GLN C 175      -5.026  25.692  41.128  1.00 38.37           C  
ANISOU 6446  C   GLN C 175     4952   4724   4904   -255    305    -57       C  
ATOM   6447  O   GLN C 175      -6.106  26.200  41.408  1.00 33.22           O  
ANISOU 6447  O   GLN C 175     4289   4065   4268   -263    321    -79       O  
ATOM   6448  CB  GLN C 175      -3.465  25.199  43.027  1.00 36.51           C  
ANISOU 6448  CB  GLN C 175     4753   4509   4609   -274    314    -21       C  
ATOM   6449  CG  GLN C 175      -4.034  26.352  43.828  1.00 33.11           C  
ANISOU 6449  CG  GLN C 175     4321   4083   4176   -288    330    -40       C  
ATOM   6450  CD  GLN C 175      -5.082  25.903  44.823  1.00 40.73           C  
ANISOU 6450  CD  GLN C 175     5290   5041   5146   -306    360    -49       C  
ATOM   6451  OE1 GLN C 175      -5.533  26.684  45.654  1.00 52.39           O  
ANISOU 6451  OE1 GLN C 175     6768   6521   6618   -320    376    -64       O  
ATOM   6452  NE2 GLN C 175      -5.472  24.641  44.748  1.00 38.07           N  
ANISOU 6452  NE2 GLN C 175     4954   4691   4819   -305    370    -41       N  
ATOM   6453  N   ALA C 176      -4.319  26.056  40.064  1.00 35.01           N  
ANISOU 6453  N   ALA C 176     4521   4303   4478   -238    280    -51       N  
ATOM   6454  CA  ALA C 176      -4.831  27.046  39.108  1.00 43.68           C  
ANISOU 6454  CA  ALA C 176     5601   5398   5596   -224    270    -68       C  
ATOM   6455  C   ALA C 176      -6.101  26.558  38.401  1.00 49.64           C  
ANISOU 6455  C   ALA C 176     6336   6141   6382   -216    274    -89       C  
ATOM   6456  O   ALA C 176      -7.075  27.302  38.254  1.00 48.30           O  
ANISOU 6456  O   ALA C 176     6152   5967   6232   -214    280   -110       O  
ATOM   6457  CB  ALA C 176      -3.769  27.400  38.081  1.00 36.07           C  
ANISOU 6457  CB  ALA C 176     4639   4441   4624   -205    245    -55       C  
ATOM   6458  N   GLU C 177      -6.073  25.310  37.948  1.00 50.27           N  
ANISOU 6458  N   GLU C 177     6413   6218   6470   -212    270    -83       N  
ATOM   6459  CA  GLU C 177      -7.223  24.718  37.279  1.00 62.20           C  
ANISOU 6459  CA  GLU C 177     7902   7720   8011   -207    273   -105       C  
ATOM   6460  C   GLU C 177      -8.419  24.640  38.228  1.00 69.55           C  
ANISOU 6460  C   GLU C 177     8828   8640   8957   -225    302   -125       C  
ATOM   6461  O   GLU C 177      -9.554  24.910  37.830  1.00 69.77           O  
ANISOU 6461  O   GLU C 177     8836   8664   9011   -221    307   -151       O  
ATOM   6462  CB  GLU C 177      -6.874  23.327  36.758  1.00 55.37           C  
ANISOU 6462  CB  GLU C 177     7036   6852   7151   -203    268    -96       C  
ATOM   6463  CG  GLU C 177      -5.789  23.316  35.691  1.00 57.68           C  
ANISOU 6463  CG  GLU C 177     7330   7153   7433   -184    239    -80       C  
ATOM   6464  CD  GLU C 177      -5.410  21.900  35.270  1.00 66.84           C  
ANISOU 6464  CD  GLU C 177     8490   8309   8599   -182    236    -71       C  
ATOM   6465  OE1 GLU C 177      -6.155  20.957  35.637  1.00 54.08           O  
ANISOU 6465  OE1 GLU C 177     6867   6681   7000   -193    256    -81       O  
ATOM   6466  OE2 GLU C 177      -4.372  21.732  34.585  1.00 67.17           O  
ANISOU 6466  OE2 GLU C 177     8535   8357   8628   -170    216    -55       O  
ATOM   6467  N   SER C 178      -8.151  24.265  39.478  1.00 57.14           N  
ANISOU 6467  N   SER C 178     7275   7066   7368   -245    322   -112       N  
ATOM   6468  CA  SER C 178      -9.177  24.198  40.514  1.00 59.41           C  
ANISOU 6468  CA  SER C 178     7563   7345   7665   -264    353   -128       C  
ATOM   6469  C   SER C 178      -9.891  25.538  40.697  1.00 70.37           C  
ANISOU 6469  C   SER C 178     8941   8734   9061   -266    358   -149       C  
ATOM   6470  O   SER C 178     -11.120  25.606  40.681  1.00 79.14           O  
ANISOU 6470  O   SER C 178    10035   9836  10200   -270    372   -176       O  
ATOM   6471  CB  SER C 178      -8.562  23.740  41.840  1.00 60.63           C  
ANISOU 6471  CB  SER C 178     7744   7502   7792   -282    371   -105       C  
ATOM   6472  OG  SER C 178      -8.990  24.561  42.914  1.00 65.45           O  
ANISOU 6472  OG  SER C 178     8361   8115   8393   -298    390   -115       O  
ATOM   6473  N   MET C 179      -9.114  26.601  40.874  1.00 64.30           N  
ANISOU 6473  N   MET C 179     8183   7976   8272   -264    347   -139       N  
ATOM   6474  CA  MET C 179      -9.668  27.947  40.981  1.00 73.41           C  
ANISOU 6474  CA  MET C 179     9328   9130   9435   -264    351   -157       C  
ATOM   6475  C   MET C 179     -10.698  28.233  39.889  1.00 80.32           C  
ANISOU 6475  C   MET C 179    10177   9999  10344   -246    343   -181       C  
ATOM   6476  O   MET C 179     -11.652  28.982  40.103  1.00 83.12           O  
ANISOU 6476  O   MET C 179    10518  10348  10716   -249    355   -203       O  
ATOM   6477  CB  MET C 179      -8.555  28.996  40.923  1.00 74.47           C  
ANISOU 6477  CB  MET C 179     9473   9275   9547   -258    336   -143       C  
ATOM   6478  CG  MET C 179      -7.612  28.981  42.121  1.00 74.80           C  
ANISOU 6478  CG  MET C 179     9538   9328   9555   -276    345   -126       C  
ATOM   6479  SD  MET C 179      -8.480  29.089  43.698  1.00 88.77           S  
ANISOU 6479  SD  MET C 179    11314  11095  11321   -304    380   -141       S  
ATOM   6480  CE  MET C 179      -9.484  30.551  43.437  1.00 83.04           C  
ANISOU 6480  CE  MET C 179    10568  10361  10624   -301    387   -171       C  
ATOM   6481  N   GLU C 180     -10.498  27.637  38.719  1.00 76.79           N  
ANISOU 6481  N   GLU C 180     9719   9553   9903   -227    322   -177       N  
ATOM   6482  CA  GLU C 180     -11.397  27.853  37.591  1.00 76.99           C  
ANISOU 6482  CA  GLU C 180     9719   9579   9957   -207    310   -198       C  
ATOM   6483  C   GLU C 180     -12.438  26.745  37.457  1.00 80.48           C  
ANISOU 6483  C   GLU C 180    10143  10012  10424   -212    321   -220       C  
ATOM   6484  O   GLU C 180     -13.420  26.709  38.202  1.00 80.88           O  
ANISOU 6484  O   GLU C 180    10187  10053  10491   -228    346   -240       O  
ATOM   6485  CB  GLU C 180     -10.595  28.013  36.297  1.00 78.16           C  
ANISOU 6485  CB  GLU C 180     9864   9736  10097   -181    280   -184       C  
ATOM   6486  CG  GLU C 180      -9.609  29.167  36.355  1.00 83.14           C  
ANISOU 6486  CG  GLU C 180    10510  10372  10707   -175    271   -166       C  
ATOM   6487  CD  GLU C 180     -10.204  30.395  37.034  1.00 94.73           C  
ANISOU 6487  CD  GLU C 180    11975  11835  12182   -183    287   -179       C  
ATOM   6488  OE1 GLU C 180      -9.461  31.108  37.743  1.00 93.63           O  
ANISOU 6488  OE1 GLU C 180    11853  11698  12024   -194    294   -168       O  
ATOM   6489  OE2 GLU C 180     -11.419  30.646  36.863  1.00 98.11           O  
ANISOU 6489  OE2 GLU C 180    12383  12258  12635   -178    295   -203       O  
TER    6490      GLU C 180                                                      
ATOM   6491  N   LYS D  15      25.970  19.676 -24.543  1.00192.52           N  
ANISOU 6491  N   LYS D  15    24543  25023  23584    618    -33     36       N  
ATOM   6492  CA  LYS D  15      26.775  18.567 -24.046  1.00192.34           C  
ANISOU 6492  CA  LYS D  15    24499  24970  23613    569    -31      2       C  
ATOM   6493  C   LYS D  15      25.909  17.353 -23.733  1.00192.60           C  
ANISOU 6493  C   LYS D  15    24486  25028  23667    552    -65    -48       C  
ATOM   6494  O   LYS D  15      26.325  16.214 -23.932  1.00192.85           O  
ANISOU 6494  O   LYS D  15    24492  25063  23719    524    -69    -88       O  
ATOM   6495  CB  LYS D  15      27.556  18.989 -22.801  1.00113.03           C  
ANISOU 6495  CB  LYS D  15    14471  14856  13620    537    -12     28       C  
ATOM   6496  CG  LYS D  15      28.630  20.033 -23.065  1.00113.09           C  
ANISOU 6496  CG  LYS D  15    14519  14830  13618    544     26     70       C  
ATOM   6497  CD  LYS D  15      29.349  20.423 -21.785  1.00112.73           C  
ANISOU 6497  CD  LYS D  15    14487  14720  13627    512     44     90       C  
ATOM   6498  CE  LYS D  15      30.438  21.449 -22.052  1.00112.89           C  
ANISOU 6498  CE  LYS D  15    14546  14707  13642    517     84    128       C  
ATOM   6499  NZ  LYS D  15      31.135  21.858 -20.801  1.00112.63           N  
ANISOU 6499  NZ  LYS D  15    14521  14612  13659    487    100    143       N  
ATOM   6500  N   LYS D  16      24.701  17.606 -23.241  1.00190.30           N  
ANISOU 6500  N   LYS D  16    24183  24751  23370    569    -86    -47       N  
ATOM   6501  CA  LYS D  16      23.784  16.535 -22.871  1.00190.68           C  
ANISOU 6501  CA  LYS D  16    24187  24820  23441    554   -116    -94       C  
ATOM   6502  C   LYS D  16      23.554  15.564 -24.021  1.00191.39           C  
ANISOU 6502  C   LYS D  16    24248  24966  23504    560   -130   -142       C  
ATOM   6503  O   LYS D  16      24.010  14.422 -23.982  1.00191.65           O  
ANISOU 6503  O   LYS D  16    24257  24992  23570    526   -131   -180       O  
ATOM   6504  CB  LYS D  16      22.449  17.117 -22.405  1.00117.26           C  
ANISOU 6504  CB  LYS D  16    14884  15539  14130    580   -136    -84       C  
ATOM   6505  CG  LYS D  16      22.532  17.902 -21.105  1.00116.77           C  
ANISOU 6505  CG  LYS D  16    14843  15422  14103    568   -125    -47       C  
ATOM   6506  CD  LYS D  16      21.179  18.471 -20.715  1.00116.81           C  
ANISOU 6506  CD  LYS D  16    14842  15446  14095    595   -144    -39       C  
ATOM   6507  CE  LYS D  16      21.257  19.235 -19.404  1.00116.35           C  
ANISOU 6507  CE  LYS D  16    14803  15333  14072    582   -132     -4       C  
ATOM   6508  NZ  LYS D  16      19.942  19.819 -19.021  1.00116.43           N  
ANISOU 6508  NZ  LYS D  16    14807  15360  14070    608   -150      3       N  
ATOM   6509  N   HIS D  17      22.841  16.022 -25.044  1.00113.96           N  
ANISOU 6509  N   HIS D  17    14445  15218  13638    604   -142   -140       N  
ATOM   6510  CA  HIS D  17      22.522  15.176 -26.187  1.00114.72           C  
ANISOU 6510  CA  HIS D  17    14512  15376  13701    615   -157   -187       C  
ATOM   6511  C   HIS D  17      23.744  14.889 -27.053  1.00114.72           C  
ANISOU 6511  C   HIS D  17    14524  15374  13689    604   -135   -190       C  
ATOM   6512  O   HIS D  17      23.892  13.786 -27.578  1.00115.28           O  
ANISOU 6512  O   HIS D  17    14566  15470  13767    586   -142   -238       O  
ATOM   6513  CB  HIS D  17      21.411  15.804 -27.029  1.00105.16           C  
ANISOU 6513  CB  HIS D  17    13301  14230  12425    669   -177   -182       C  
ATOM   6514  CG  HIS D  17      20.054  15.695 -26.410  1.00105.50           C  
ANISOU 6514  CG  HIS D  17    13315  14291  12479    677   -205   -201       C  
ATOM   6515  ND1 HIS D  17      19.655  14.596 -25.681  1.00105.85           N  
ANISOU 6515  ND1 HIS D  17    13321  14324  12575    640   -220   -247       N  
ATOM   6516  CD2 HIS D  17      19.003  16.549 -26.409  1.00105.66           C  
ANISOU 6516  CD2 HIS D  17    13342  14339  12467    718   -221   -180       C  
ATOM   6517  CE1 HIS D  17      18.417  14.776 -25.258  1.00106.19           C  
ANISOU 6517  CE1 HIS D  17    13346  14386  12616    657   -242   -255       C  
ATOM   6518  NE2 HIS D  17      17.998  15.954 -25.686  1.00106.06           N  
ANISOU 6518  NE2 HIS D  17    13355  14394  12549    704   -244   -215       N  
ATOM   6519  N   HIS D  18      24.618  15.880 -27.203  1.00 84.26           N  
ANISOU 6519  N   HIS D  18    10710  11488   9816    615   -107   -140       N  
ATOM   6520  CA  HIS D  18      25.815  15.706 -28.016  1.00 84.28           C  
ANISOU 6520  CA  HIS D  18    10728  11487   9808    606    -82   -140       C  
ATOM   6521  C   HIS D  18      27.076  15.928 -27.186  1.00 83.69           C  
ANISOU 6521  C   HIS D  18    10677  11339   9784    570    -53   -113       C  
ATOM   6522  O   HIS D  18      27.868  15.007 -26.985  1.00 83.76           O  
ANISOU 6522  O   HIS D  18    10670  11322   9834    531    -46   -140       O  
ATOM   6523  CB  HIS D  18      25.800  16.660 -29.212  1.00 74.44           C  
ANISOU 6523  CB  HIS D  18     9513  10281   8490    655    -71   -108       C  
ATOM   6524  CG  HIS D  18      24.668  16.424 -30.162  1.00 75.10           C  
ANISOU 6524  CG  HIS D  18     9573  10444   8517    693   -100   -137       C  
ATOM   6525  ND1 HIS D  18      23.553  17.232 -30.208  1.00 75.22           N  
ANISOU 6525  ND1 HIS D  18     9595  10492   8495    737   -118   -114       N  
ATOM   6526  CD2 HIS D  18      24.481  15.472 -31.106  1.00 75.77           C  
ANISOU 6526  CD2 HIS D  18     9627  10584   8577    694   -115   -187       C  
ATOM   6527  CE1 HIS D  18      22.726  16.787 -31.135  1.00 75.92           C  
ANISOU 6527  CE1 HIS D  18     9656  10653   8537    764   -143   -150       C  
ATOM   6528  NE2 HIS D  18      23.264  15.720 -31.696  1.00 76.26           N  
ANISOU 6528  NE2 HIS D  18     9676  10712   8586    738   -142   -196       N  
ATOM   6529  N   SER D  25      43.211   1.991 -29.976  1.00 63.69           N  
ANISOU 6529  N   SER D  25     7906   8465   7829     62    175   -546       N  
ATOM   6530  CA  SER D  25      43.591   1.549 -28.636  1.00 68.22           C  
ANISOU 6530  CA  SER D  25     8467   8982   8470     39    170   -537       C  
ATOM   6531  C   SER D  25      44.897   2.194 -28.163  1.00 64.54           C  
ANISOU 6531  C   SER D  25     8027   8467   8028     28    191   -503       C  
ATOM   6532  O   SER D  25      45.299   2.040 -27.009  1.00 58.27           O  
ANISOU 6532  O   SER D  25     7229   7627   7285     13    187   -488       O  
ATOM   6533  CB  SER D  25      43.725   0.026 -28.600  1.00 64.87           C  
ANISOU 6533  CB  SER D  25     7999   8548   8099     11    168   -585       C  
ATOM   6534  OG  SER D  25      44.823  -0.409 -29.387  1.00 71.13           O  
ANISOU 6534  OG  SER D  25     8785   9334   8905     -6    192   -609       O  
ATOM   6535  N   GLN D  26      45.555   2.918 -29.061  1.00 52.92           N  
ANISOU 6535  N   GLN D  26     6582   7006   6520     37    214   -493       N  
ATOM   6536  CA  GLN D  26      46.844   3.505 -28.753  1.00 54.42           C  
ANISOU 6536  CA  GLN D  26     6794   7151   6733     26    237   -468       C  
ATOM   6537  C   GLN D  26      46.889   4.965 -29.168  1.00 55.65           C  
ANISOU 6537  C   GLN D  26     6994   7318   6834     52    253   -428       C  
ATOM   6538  O   GLN D  26      46.401   5.326 -30.234  1.00 60.30           O  
ANISOU 6538  O   GLN D  26     7595   7951   7364     74    257   -431       O  
ATOM   6539  CB  GLN D  26      47.958   2.726 -29.450  1.00 52.42           C  
ANISOU 6539  CB  GLN D  26     6524   6886   6506      3    259   -502       C  
ATOM   6540  CG  GLN D  26      47.654   2.404 -30.893  1.00 61.97           C  
ANISOU 6540  CG  GLN D  26     7728   8149   7671     12    267   -535       C  
ATOM   6541  CD  GLN D  26      48.818   1.749 -31.595  1.00 66.43           C  
ANISOU 6541  CD  GLN D  26     8280   8701   8261    -11    292   -566       C  
ATOM   6542  OE1 GLN D  26      49.697   1.162 -30.958  1.00 65.48           O  
ANISOU 6542  OE1 GLN D  26     8142   8535   8202    -37    298   -574       O  
ATOM   6543  NE2 GLN D  26      48.840   1.855 -32.921  1.00 76.67           N  
ANISOU 6543  NE2 GLN D  26     9584  10039   9508     -1    307   -584       N  
ATOM   6544  N   CYS D  27      47.482   5.805 -28.323  1.00 42.66           N  
ANISOU 6544  N   CYS D  27     5371   5630   5208     49    262   -391       N  
ATOM   6545  CA  CYS D  27      47.549   7.225 -28.617  1.00 35.22           C  
ANISOU 6545  CA  CYS D  27     4471   4691   4221     73    280   -352       C  
ATOM   6546  C   CYS D  27      48.969   7.705 -28.925  1.00 40.86           C  
ANISOU 6546  C   CYS D  27     5204   5372   4948     60    316   -344       C  
ATOM   6547  O   CYS D  27      49.949   6.996 -28.716  1.00 38.12           O  
ANISOU 6547  O   CYS D  27     4838   4994   4651     32    325   -365       O  
ATOM   6548  CB  CYS D  27      46.963   8.030 -27.463  1.00 41.92           C  
ANISOU 6548  CB  CYS D  27     5334   5521   5072     84    265   -314       C  
ATOM   6549  SG  CYS D  27      47.963   7.966 -25.968  1.00 41.95           S  
ANISOU 6549  SG  CYS D  27     5330   5459   5149     55    266   -302       S  
ATOM   6550  N   SER D  28      49.070   8.939 -29.398  1.00 40.12           N  
ANISOU 6550  N   SER D  28     5149   5283   4812     81    339   -311       N  
ATOM   6551  CA  SER D  28      50.335   9.454 -29.844  1.00 37.26           C  
ANISOU 6551  CA  SER D  28     4807   4894   4456     72    377   -305       C  
ATOM   6552  C   SER D  28      50.276  10.953 -29.852  1.00 44.45           C  
ANISOU 6552  C   SER D  28     5760   5797   5332     96    398   -259       C  
ATOM   6553  O   SER D  28      49.222  11.546 -30.084  1.00 40.90           O  
ANISOU 6553  O   SER D  28     5328   5381   4833    126    388   -237       O  
ATOM   6554  CB  SER D  28      50.637   8.944 -31.252  1.00 46.54           C  
ANISOU 6554  CB  SER D  28     5978   6102   5603     72    395   -334       C  
ATOM   6555  OG  SER D  28      51.816   9.540 -31.769  1.00 44.71           O  
ANISOU 6555  OG  SER D  28     5769   5845   5372     66    436   -326       O  
ATOM   6556  N   SER D  29      51.417  11.569 -29.597  1.00 35.64           N  
ANISOU 6556  N   SER D  29     4660   4638   4243     82    429   -246       N  
ATOM   6557  CA  SER D  29      51.504  13.007 -29.632  1.00 36.73           C  
ANISOU 6557  CA  SER D  29     4839   4762   4354    101    456   -204       C  
ATOM   6558  C   SER D  29      52.936  13.383 -29.955  1.00 32.53           C  
ANISOU 6558  C   SER D  29     4321   4194   3846     84    499   -206       C  
ATOM   6559  O   SER D  29      53.828  12.542 -29.903  1.00 35.96           O  
ANISOU 6559  O   SER D  29     4731   4609   4324     55    503   -238       O  
ATOM   6560  CB  SER D  29      51.059  13.608 -28.296  1.00 44.75           C  
ANISOU 6560  CB  SER D  29     5858   5752   5391    104    439   -177       C  
ATOM   6561  OG  SER D  29      51.046  15.028 -28.354  1.00 52.07           O  
ANISOU 6561  OG  SER D  29     6825   6668   6291    125    466   -136       O  
ATOM   6562  N   THR D  30      53.141  14.642 -30.318  1.00 33.70           N  
ANISOU 6562  N   THR D  30     4508   4332   3965    101    534   -172       N  
ATOM   6563  CA  THR D  30      54.454  15.140 -30.686  1.00 35.99           C  
ANISOU 6563  CA  THR D  30     4815   4587   4274     87    581   -172       C  
ATOM   6564  C   THR D  30      54.724  16.438 -29.952  1.00 34.64           C  
ANISOU 6564  C   THR D  30     4670   4376   4115     91    604   -136       C  
ATOM   6565  O   THR D  30      53.838  17.280 -29.825  1.00 38.00           O  
ANISOU 6565  O   THR D  30     5118   4813   4506    119    600   -102       O  
ATOM   6566  CB  THR D  30      54.553  15.398 -32.206  1.00 38.85           C  
ANISOU 6566  CB  THR D  30     5202   4979   4581    106    613   -169       C  
ATOM   6567  OG1 THR D  30      54.328  14.173 -32.921  1.00 40.38           O  
ANISOU 6567  OG1 THR D  30     5369   5212   4762    100    593   -207       O  
ATOM   6568  CG2 THR D  30      55.928  15.979 -32.574  1.00 38.76           C  
ANISOU 6568  CG2 THR D  30     5209   4927   4589     90    666   -167       C  
ATOM   6569  N   LEU D  31      55.954  16.599 -29.478  1.00 33.24           N  
ANISOU 6569  N   LEU D  31     4488   4152   3991     64    628   -146       N  
ATOM   6570  CA  LEU D  31      56.357  17.809 -28.779  1.00 33.92           C  
ANISOU 6570  CA  LEU D  31     4596   4197   4096     63    654   -119       C  
ATOM   6571  C   LEU D  31      57.611  18.411 -29.404  1.00 38.83           C  
ANISOU 6571  C   LEU D  31     5237   4786   4729     52    710   -121       C  
ATOM   6572  O   LEU D  31      58.442  17.697 -29.970  1.00 36.03           O  
ANISOU 6572  O   LEU D  31     4868   4429   4392     32    723   -151       O  
ATOM   6573  CB  LEU D  31      56.576  17.519 -27.292  1.00 38.69           C  
ANISOU 6573  CB  LEU D  31     5172   4771   4759     40    626   -130       C  
ATOM   6574  CG  LEU D  31      55.318  17.072 -26.543  1.00 43.43           C  
ANISOU 6574  CG  LEU D  31     5756   5396   5350     51    575   -124       C  
ATOM   6575  CD1 LEU D  31      55.132  15.550 -26.613  1.00 36.13           C  
ANISOU 6575  CD1 LEU D  31     4793   4495   4438     38    538   -159       C  
ATOM   6576  CD2 LEU D  31      55.361  17.543 -25.101  1.00 42.63           C  
ANISOU 6576  CD2 LEU D  31     5648   5263   5288     41    562   -112       C  
ATOM   6577  N   VAL D  32      57.744  19.728 -29.293  1.00 39.13           N  
ANISOU 6577  N   VAL D  32     5308   4799   4761     63    746    -88       N  
ATOM   6578  CA  VAL D  32      58.841  20.437 -29.925  1.00 35.74           C  
ANISOU 6578  CA  VAL D  32     4902   4340   4339     56    805    -86       C  
ATOM   6579  C   VAL D  32      59.479  21.428 -28.965  1.00 44.82           C  
ANISOU 6579  C   VAL D  32     6058   5437   5533     42    831    -75       C  
ATOM   6580  O   VAL D  32      58.785  22.081 -28.193  1.00 49.57           O  
ANISOU 6580  O   VAL D  32     6668   6034   6131     55    817    -50       O  
ATOM   6581  CB  VAL D  32      58.351  21.174 -31.177  1.00 44.64           C  
ANISOU 6581  CB  VAL D  32     6071   5491   5398     91    838    -54       C  
ATOM   6582  CG1 VAL D  32      59.431  22.047 -31.725  1.00 54.16           C  
ANISOU 6582  CG1 VAL D  32     7304   6660   6613     84    903    -46       C  
ATOM   6583  CG2 VAL D  32      57.879  20.183 -32.232  1.00 39.23           C  
ANISOU 6583  CG2 VAL D  32     5378   4859   4670    102    818    -71       C  
ATOM   6584  N   LYS D  33      60.803  21.542 -29.018  1.00 34.14           N  
ANISOU 6584  N   LYS D  33     4701   4048   4224     16    868    -96       N  
ATOM   6585  CA  LYS D  33      61.523  22.447 -28.132  1.00 36.11           C  
ANISOU 6585  CA  LYS D  33     4953   4248   4520     -1    895    -93       C  
ATOM   6586  C   LYS D  33      62.701  23.107 -28.856  1.00 45.07           C  
ANISOU 6586  C   LYS D  33     6108   5349   5669    -12    961    -98       C  
ATOM   6587  O   LYS D  33      63.580  22.424 -29.375  1.00 33.73           O  
ANISOU 6587  O   LYS D  33     4657   3908   4252    -32    973   -130       O  
ATOM   6588  CB  LYS D  33      62.026  21.673 -26.915  1.00 33.35           C  
ANISOU 6588  CB  LYS D  33     4559   3881   4231    -31    857   -127       C  
ATOM   6589  CG  LYS D  33      62.786  22.506 -25.902  1.00 32.54           C  
ANISOU 6589  CG  LYS D  33     4451   3732   4178    -50    879   -131       C  
ATOM   6590  CD  LYS D  33      61.877  23.490 -25.185  1.00 34.89           C  
ANISOU 6590  CD  LYS D  33     4769   4028   4461    -30    873    -96       C  
ATOM   6591  CE  LYS D  33      62.684  24.384 -24.238  1.00 41.17           C  
ANISOU 6591  CE  LYS D  33     5560   4777   5307    -50    900   -103       C  
ATOM   6592  NZ  LYS D  33      61.961  25.636 -23.859  1.00 43.01           N  
ANISOU 6592  NZ  LYS D  33     5820   4999   5521    -30    916    -66       N  
ATOM   6593  N   HIS D  34      62.713  24.436 -28.882  1.00 52.28           N  
ANISOU 6593  N   HIS D  34     7055   6235   6574      1   1006    -68       N  
ATOM   6594  CA  HIS D  34      63.822  25.186 -29.456  1.00 47.34           C  
ANISOU 6594  CA  HIS D  34     6449   5570   5966    -10   1073    -70       C  
ATOM   6595  C   HIS D  34      64.888  25.431 -28.393  1.00 47.52           C  
ANISOU 6595  C   HIS D  34     6447   5546   6062    -45   1085    -99       C  
ATOM   6596  O   HIS D  34      64.604  25.981 -27.334  1.00 45.51           O  
ANISOU 6596  O   HIS D  34     6187   5276   5829    -46   1073    -90       O  
ATOM   6597  CB  HIS D  34      63.327  26.518 -30.037  1.00 55.56           C  
ANISOU 6597  CB  HIS D  34     7541   6605   6965     22   1121    -22       C  
ATOM   6598  CG  HIS D  34      62.154  26.375 -30.959  1.00 66.23           C  
ANISOU 6598  CG  HIS D  34     8916   8006   8241     61   1104      9       C  
ATOM   6599  ND1 HIS D  34      62.268  26.462 -32.331  1.00 68.69           N  
ANISOU 6599  ND1 HIS D  34     9257   8335   8507     78   1141     22       N  
ATOM   6600  CD2 HIS D  34      60.847  26.133 -30.704  1.00 68.34           C  
ANISOU 6600  CD2 HIS D  34     9181   8314   8470     86   1054     29       C  
ATOM   6601  CE1 HIS D  34      61.079  26.286 -32.879  1.00 66.81           C  
ANISOU 6601  CE1 HIS D  34     9033   8146   8205    114   1113     47       C  
ATOM   6602  NE2 HIS D  34      60.198  26.086 -31.915  1.00 63.38           N  
ANISOU 6602  NE2 HIS D  34     8580   7727   7775    119   1060     52       N  
ATOM   6603  N   ILE D  35      66.116  25.010 -28.670  1.00 45.38           N  
ANISOU 6603  N   ILE D  35     6159   5254   5830    -73   1109   -136       N  
ATOM   6604  CA  ILE D  35      67.188  25.099 -27.686  1.00 43.52           C  
ANISOU 6604  CA  ILE D  35     5893   4978   5665   -107   1115   -170       C  
ATOM   6605  C   ILE D  35      68.256  26.090 -28.138  1.00 45.94           C  
ANISOU 6605  C   ILE D  35     6220   5239   5997   -120   1191   -174       C  
ATOM   6606  O   ILE D  35      68.625  26.126 -29.310  1.00 46.08           O  
ANISOU 6606  O   ILE D  35     6259   5256   5992   -116   1232   -171       O  
ATOM   6607  CB  ILE D  35      67.846  23.729 -27.453  1.00 42.80           C  
ANISOU 6607  CB  ILE D  35     5756   4894   5610   -134   1078   -215       C  
ATOM   6608  CG1 ILE D  35      66.795  22.674 -27.093  1.00 41.11           C  
ANISOU 6608  CG1 ILE D  35     5523   4725   5373   -122   1007   -212       C  
ATOM   6609  CG2 ILE D  35      68.909  23.812 -26.358  1.00 38.52           C  
ANISOU 6609  CG2 ILE D  35     5181   4315   5140   -166   1079   -250       C  
ATOM   6610  CD1 ILE D  35      67.401  21.338 -26.688  1.00 35.10           C  
ANISOU 6610  CD1 ILE D  35     4715   3968   4653   -147    969   -254       C  
ATOM   6611  N   LYS D  36      68.755  26.889 -27.202  1.00 48.16           N  
ANISOU 6611  N   LYS D  36     6493   5481   6324   -135   1210   -182       N  
ATOM   6612  CA  LYS D  36      69.801  27.857 -27.515  1.00 48.24           C  
ANISOU 6612  CA  LYS D  36     6518   5444   6366   -150   1283   -191       C  
ATOM   6613  C   LYS D  36      71.181  27.235 -27.314  1.00 47.81           C  
ANISOU 6613  C   LYS D  36     6426   5367   6373   -188   1289   -245       C  
ATOM   6614  O   LYS D  36      71.960  27.649 -26.453  1.00 38.37           O  
ANISOU 6614  O   LYS D  36     5208   4138   5234   -212   1302   -272       O  
ATOM   6615  CB  LYS D  36      69.628  29.133 -26.687  1.00 52.34           C  
ANISOU 6615  CB  LYS D  36     7050   5932   6905   -147   1307   -173       C  
ATOM   6616  CG  LYS D  36      68.425  29.966 -27.125  1.00 53.62           C  
ANISOU 6616  CG  LYS D  36     7257   6107   7007   -108   1321   -117       C  
ATOM   6617  CD  LYS D  36      68.350  31.326 -26.422  1.00 72.84           C  
ANISOU 6617  CD  LYS D  36     9707   8504   9464   -106   1357   -100       C  
ATOM   6618  CE  LYS D  36      67.713  31.240 -25.031  1.00 73.05           C  
ANISOU 6618  CE  LYS D  36     9708   8542   9507   -109   1300   -103       C  
ATOM   6619  NZ  LYS D  36      68.667  30.811 -23.964  1.00 65.19           N  
ANISOU 6619  NZ  LYS D  36     8664   7529   8577   -146   1279   -155       N  
ATOM   6620  N   ALA D  37      71.462  26.216 -28.118  1.00 46.34           N  
ANISOU 6620  N   ALA D  37     6230   5201   6175   -193   1279   -262       N  
ATOM   6621  CA  ALA D  37      72.738  25.518 -28.074  1.00 35.42           C  
ANISOU 6621  CA  ALA D  37     4811   3801   4846   -226   1284   -313       C  
ATOM   6622  C   ALA D  37      72.970  24.851 -29.421  1.00 38.57           C  
ANISOU 6622  C   ALA D  37     5221   4217   5216   -224   1302   -319       C  
ATOM   6623  O   ALA D  37      72.013  24.543 -30.130  1.00 37.31           O  
ANISOU 6623  O   ALA D  37     5084   4095   4996   -198   1285   -290       O  
ATOM   6624  CB  ALA D  37      72.743  24.487 -26.943  1.00 39.21           C  
ANISOU 6624  CB  ALA D  37     5241   4297   5360   -240   1213   -342       C  
ATOM   6625  N   PRO D  38      74.247  24.639 -29.784  1.00 36.39           N  
ANISOU 6625  N   PRO D  38     4930   3915   4983   -251   1338   -357       N  
ATOM   6626  CA  PRO D  38      74.614  24.018 -31.062  1.00 39.84           C  
ANISOU 6626  CA  PRO D  38     5375   4364   5399   -253   1361   -368       C  
ATOM   6627  C   PRO D  38      74.214  22.546 -31.131  1.00 39.46           C  
ANISOU 6627  C   PRO D  38     5297   4357   5337   -253   1297   -384       C  
ATOM   6628  O   PRO D  38      74.413  21.812 -30.156  1.00 32.01           O  
ANISOU 6628  O   PRO D  38     4312   3416   4435   -269   1248   -411       O  
ATOM   6629  CB  PRO D  38      76.142  24.104 -31.074  1.00 41.21           C  
ANISOU 6629  CB  PRO D  38     5527   4493   5637   -288   1405   -413       C  
ATOM   6630  CG  PRO D  38      76.507  25.034 -29.975  1.00 45.92           C  
ANISOU 6630  CG  PRO D  38     6114   5054   6280   -300   1419   -420       C  
ATOM   6631  CD  PRO D  38      75.427  24.957 -28.968  1.00 34.70           C  
ANISOU 6631  CD  PRO D  38     4684   3657   4841   -283   1357   -397       C  
ATOM   6632  N   LEU D  39      73.680  22.134 -32.280  1.00 28.08           N  
ANISOU 6632  N   LEU D  39     3879   2950   3840   -235   1300   -368       N  
ATOM   6633  CA  LEU D  39      73.296  20.750 -32.537  1.00 33.93           C  
ANISOU 6633  CA  LEU D  39     4595   3732   4565   -234   1248   -385       C  
ATOM   6634  C   LEU D  39      74.310  19.725 -32.026  1.00 34.49           C  
ANISOU 6634  C   LEU D  39     4615   3788   4702   -267   1225   -436       C  
ATOM   6635  O   LEU D  39      73.928  18.723 -31.433  1.00 29.64           O  
ANISOU 6635  O   LEU D  39     3968   3196   4099   -269   1166   -449       O  
ATOM   6636  CB  LEU D  39      73.025  20.541 -34.030  1.00 37.33           C  
ANISOU 6636  CB  LEU D  39     5055   4190   4937   -218   1274   -373       C  
ATOM   6637  CG  LEU D  39      72.695  19.125 -34.507  1.00 41.77           C  
ANISOU 6637  CG  LEU D  39     5593   4795   5482   -219   1230   -395       C  
ATOM   6638  CD1 LEU D  39      71.388  18.647 -33.889  1.00 36.18           C  
ANISOU 6638  CD1 LEU D  39     4875   4126   4746   -199   1164   -375       C  
ATOM   6639  CD2 LEU D  39      72.614  19.066 -36.028  1.00 41.99           C  
ANISOU 6639  CD2 LEU D  39     5651   4848   5455   -206   1267   -387       C  
ATOM   6640  N   HIS D  40      75.597  19.972 -32.244  1.00 41.96           N  
ANISOU 6640  N   HIS D  40     5553   4696   5694   -293   1273   -467       N  
ATOM   6641  CA  HIS D  40      76.609  18.984 -31.877  1.00 40.87           C  
ANISOU 6641  CA  HIS D  40     5367   4546   5618   -323   1255   -517       C  
ATOM   6642  C   HIS D  40      76.670  18.747 -30.365  1.00 40.16           C  
ANISOU 6642  C   HIS D  40     5237   4446   5575   -332   1204   -530       C  
ATOM   6643  O   HIS D  40      77.002  17.647 -29.913  1.00 36.60           O  
ANISOU 6643  O   HIS D  40     4745   4003   5160   -346   1163   -561       O  
ATOM   6644  CB  HIS D  40      77.987  19.382 -32.397  1.00 39.66           C  
ANISOU 6644  CB  HIS D  40     5213   4352   5505   -348   1319   -548       C  
ATOM   6645  CG  HIS D  40      78.619  20.500 -31.633  1.00 41.71           C  
ANISOU 6645  CG  HIS D  40     5473   4568   5807   -360   1352   -552       C  
ATOM   6646  ND1 HIS D  40      78.422  21.826 -31.955  1.00 38.13           N  
ANISOU 6646  ND1 HIS D  40     5063   4095   5328   -347   1406   -519       N  
ATOM   6647  CD2 HIS D  40      79.448  20.491 -30.562  1.00 39.31           C  
ANISOU 6647  CD2 HIS D  40     5129   4236   5569   -383   1340   -585       C  
ATOM   6648  CE1 HIS D  40      79.107  22.585 -31.119  1.00 40.31           C  
ANISOU 6648  CE1 HIS D  40     5326   4332   5655   -364   1427   -535       C  
ATOM   6649  NE2 HIS D  40      79.735  21.800 -30.261  1.00 36.94           N  
ANISOU 6649  NE2 HIS D  40     4849   3902   5284   -386   1387   -576       N  
ATOM   6650  N   LEU D  41      76.359  19.787 -29.597  1.00 39.07           N  
ANISOU 6650  N   LEU D  41     5113   4293   5438   -324   1210   -507       N  
ATOM   6651  CA  LEU D  41      76.378  19.727 -28.134  1.00 41.33           C  
ANISOU 6651  CA  LEU D  41     5367   4573   5765   -331   1166   -517       C  
ATOM   6652  C   LEU D  41      75.090  19.086 -27.585  1.00 40.16           C  
ANISOU 6652  C   LEU D  41     5214   4464   5583   -310   1099   -492       C  
ATOM   6653  O   LEU D  41      75.119  18.297 -26.636  1.00 35.28           O  
ANISOU 6653  O   LEU D  41     4557   3852   4995   -317   1047   -509       O  
ATOM   6654  CB  LEU D  41      76.541  21.142 -27.567  1.00 42.92           C  
ANISOU 6654  CB  LEU D  41     5587   4742   5980   -332   1202   -504       C  
ATOM   6655  CG  LEU D  41      76.724  21.330 -26.063  1.00 48.52           C  
ANISOU 6655  CG  LEU D  41     6264   5439   6734   -341   1169   -517       C  
ATOM   6656  CD1 LEU D  41      77.537  20.192 -25.450  1.00 45.29           C  
ANISOU 6656  CD1 LEU D  41     5801   5030   6378   -362   1130   -562       C  
ATOM   6657  CD2 LEU D  41      77.377  22.687 -25.790  1.00 49.85           C  
ANISOU 6657  CD2 LEU D  41     6444   5565   6931   -352   1225   -523       C  
ATOM   6658  N   VAL D  42      73.959  19.435 -28.184  1.00 23.12           N  
ANISOU 6658  N   VAL D  42     3093   2331   3361   -283   1100   -451       N  
ATOM   6659  CA  VAL D  42      72.696  18.849 -27.778  1.00 29.74           C  
ANISOU 6659  CA  VAL D  42     3928   3207   4164   -262   1041   -428       C  
ATOM   6660  C   VAL D  42      72.716  17.340 -28.068  1.00 35.14           C  
ANISOU 6660  C   VAL D  42     4581   3917   4855   -269   1002   -454       C  
ATOM   6661  O   VAL D  42      72.374  16.525 -27.207  1.00 23.50           O  
ANISOU 6661  O   VAL D  42     3076   2456   3397   -270    948   -461       O  
ATOM   6662  CB  VAL D  42      71.517  19.534 -28.490  1.00 29.97           C  
ANISOU 6662  CB  VAL D  42     4004   3261   4122   -231   1054   -382       C  
ATOM   6663  CG1 VAL D  42      70.210  18.893 -28.098  1.00 29.15           C  
ANISOU 6663  CG1 VAL D  42     3894   3197   3984   -210    993   -362       C  
ATOM   6664  CG2 VAL D  42      71.503  21.019 -28.163  1.00 33.19           C  
ANISOU 6664  CG2 VAL D  42     4442   3641   4529   -224   1093   -357       C  
ATOM   6665  N   TRP D  43      73.155  16.967 -29.268  1.00 31.55           N  
ANISOU 6665  N   TRP D  43     4133   3466   4387   -275   1033   -469       N  
ATOM   6666  CA  TRP D  43      73.204  15.557 -29.639  1.00 23.51           C  
ANISOU 6666  CA  TRP D  43     3087   2471   3377   -283   1003   -495       C  
ATOM   6667  C   TRP D  43      74.174  14.739 -28.789  1.00 29.85           C  
ANISOU 6667  C   TRP D  43     3840   3253   4251   -308    979   -535       C  
ATOM   6668  O   TRP D  43      73.947  13.545 -28.577  1.00 26.09           O  
ANISOU 6668  O   TRP D  43     3334   2795   3786   -311    935   -550       O  
ATOM   6669  CB  TRP D  43      73.508  15.387 -31.128  1.00 33.34           C  
ANISOU 6669  CB  TRP D  43     4349   3724   4593   -284   1044   -505       C  
ATOM   6670  CG  TRP D  43      73.620  13.958 -31.558  1.00 30.33           C  
ANISOU 6670  CG  TRP D  43     3937   3364   4222   -294   1018   -536       C  
ATOM   6671  CD1 TRP D  43      74.751  13.315 -31.971  1.00 35.38           C  
ANISOU 6671  CD1 TRP D  43     4553   3986   4904   -319   1038   -577       C  
ATOM   6672  CD2 TRP D  43      72.563  12.982 -31.599  1.00 30.77           C  
ANISOU 6672  CD2 TRP D  43     3982   3460   4248   -281    968   -531       C  
ATOM   6673  NE1 TRP D  43      74.464  12.000 -32.281  1.00 35.23           N  
ANISOU 6673  NE1 TRP D  43     4508   3994   4884   -322   1004   -597       N  
ATOM   6674  CE2 TRP D  43      73.132  11.772 -32.057  1.00 31.15           C  
ANISOU 6674  CE2 TRP D  43     3999   3513   4325   -299    962   -570       C  
ATOM   6675  CE3 TRP D  43      71.189  13.020 -31.301  1.00 29.19           C  
ANISOU 6675  CE3 TRP D  43     3794   3293   4004   -255    930   -498       C  
ATOM   6676  CZ2 TRP D  43      72.371  10.602 -32.226  1.00 31.10           C  
ANISOU 6676  CZ2 TRP D  43     3973   3541   4303   -293    920   -578       C  
ATOM   6677  CZ3 TRP D  43      70.438  11.859 -31.463  1.00 28.55           C  
ANISOU 6677  CZ3 TRP D  43     3693   3246   3907   -249    888   -508       C  
ATOM   6678  CH2 TRP D  43      71.034  10.663 -31.928  1.00 27.81           C  
ANISOU 6678  CH2 TRP D  43     3567   3155   3842   -268    884   -547       C  
ATOM   6679  N   SER D  44      75.248  15.353 -28.291  1.00 26.10           N  
ANISOU 6679  N   SER D  44     3355   2739   3823   -327   1006   -554       N  
ATOM   6680  CA  SER D  44      76.163  14.591 -27.444  1.00 28.50           C  
ANISOU 6680  CA  SER D  44     3610   3025   4193   -348    981   -591       C  
ATOM   6681  C   SER D  44      75.533  14.282 -26.085  1.00 24.45           C  
ANISOU 6681  C   SER D  44     3076   2524   3692   -340    921   -579       C  
ATOM   6682  O   SER D  44      76.003  13.408 -25.349  1.00 27.33           O  
ANISOU 6682  O   SER D  44     3399   2885   4101   -351    886   -603       O  
ATOM   6683  CB  SER D  44      77.503  15.305 -27.256  1.00 33.07           C  
ANISOU 6683  CB  SER D  44     4180   3563   4823   -371   1025   -618       C  
ATOM   6684  OG  SER D  44      77.313  16.621 -26.768  1.00 33.37           O  
ANISOU 6684  OG  SER D  44     4242   3585   4852   -364   1047   -596       O  
ATOM   6685  N   ILE D  45      74.476  15.001 -25.747  1.00 27.07           N  
ANISOU 6685  N   ILE D  45     3434   2869   3981   -319    910   -541       N  
ATOM   6686  CA  ILE D  45      73.749  14.703 -24.512  1.00 29.63           C  
ANISOU 6686  CA  ILE D  45     3742   3207   4310   -309    854   -526       C  
ATOM   6687  C   ILE D  45      72.570  13.756 -24.760  1.00 24.71           C  
ANISOU 6687  C   ILE D  45     3118   2621   3647   -292    812   -510       C  
ATOM   6688  O   ILE D  45      72.406  12.770 -24.064  1.00 24.23           O  
ANISOU 6688  O   ILE D  45     3027   2571   3609   -294    766   -519       O  
ATOM   6689  CB  ILE D  45      73.270  15.979 -23.811  1.00 35.21           C  
ANISOU 6689  CB  ILE D  45     4472   3906   5001   -298    861   -498       C  
ATOM   6690  CG1 ILE D  45      74.471  16.715 -23.204  1.00 34.57           C  
ANISOU 6690  CG1 ILE D  45     4377   3788   4971   -318    890   -522       C  
ATOM   6691  CG2 ILE D  45      72.225  15.650 -22.745  1.00 26.26           C  
ANISOU 6691  CG2 ILE D  45     3329   2795   3855   -283    804   -476       C  
ATOM   6692  CD1 ILE D  45      74.078  17.655 -22.092  1.00 45.49           C  
ANISOU 6692  CD1 ILE D  45     5766   5164   6355   -311    879   -504       C  
ATOM   6693  N   VAL D  46      71.774  14.059 -25.775  1.00 24.40           N  
ANISOU 6693  N   VAL D  46     3115   2604   3551   -275    830   -487       N  
ATOM   6694  CA  VAL D  46      70.648  13.214 -26.171  1.00 27.77           C  
ANISOU 6694  CA  VAL D  46     3543   3069   3939   -259    796   -474       C  
ATOM   6695  C   VAL D  46      71.039  11.764 -26.500  1.00 31.42           C  
ANISOU 6695  C   VAL D  46     3970   3539   4428   -273    777   -508       C  
ATOM   6696  O   VAL D  46      70.334  10.829 -26.131  1.00 28.05           O  
ANISOU 6696  O   VAL D  46     3525   3134   3999   -267    733   -507       O  
ATOM   6697  CB  VAL D  46      69.915  13.823 -27.379  1.00 25.41           C  
ANISOU 6697  CB  VAL D  46     3287   2792   3574   -240    826   -449       C  
ATOM   6698  CG1 VAL D  46      68.978  12.818 -28.009  1.00 29.90           C  
ANISOU 6698  CG1 VAL D  46     3852   3402   4106   -227    796   -449       C  
ATOM   6699  CG2 VAL D  46      69.141  15.056 -26.943  1.00 32.42           C  
ANISOU 6699  CG2 VAL D  46     4207   3680   4429   -220    831   -409       C  
ATOM   6700  N   ARG D  47      72.159  11.578 -27.192  1.00 23.28           N  
ANISOU 6700  N   ARG D  47     2931   2490   3424   -292    812   -538       N  
ATOM   6701  CA  ARG D  47      72.548  10.248 -27.645  1.00 27.99           C  
ANISOU 6701  CA  ARG D  47     3497   3094   4045   -305    800   -571       C  
ATOM   6702  C   ARG D  47      72.980   9.307 -26.506  1.00 21.10           C  
ANISOU 6702  C   ARG D  47     2578   2208   3231   -316    759   -591       C  
ATOM   6703  O   ARG D  47      73.121   8.105 -26.722  1.00 27.43           O  
ANISOU 6703  O   ARG D  47     3351   3016   4053   -324    741   -614       O  
ATOM   6704  CB  ARG D  47      73.669  10.346 -28.693  1.00 27.46           C  
ANISOU 6704  CB  ARG D  47     3432   3008   3992   -322    852   -599       C  
ATOM   6705  CG  ARG D  47      75.058  10.587 -28.110  1.00 22.48           C  
ANISOU 6705  CG  ARG D  47     2779   2337   3425   -345    870   -625       C  
ATOM   6706  CD  ARG D  47      76.108  10.694 -29.226  1.00 27.58           C  
ANISOU 6706  CD  ARG D  47     3430   2966   4083   -363    925   -653       C  
ATOM   6707  NE  ARG D  47      76.197   9.470 -30.024  1.00 24.99           N  
ANISOU 6707  NE  ARG D  47     3083   2654   3759   -370    918   -679       N  
ATOM   6708  CZ  ARG D  47      76.850   8.382 -29.633  1.00 29.91           C  
ANISOU 6708  CZ  ARG D  47     3662   3267   4436   -386    896   -711       C  
ATOM   6709  NH1 ARG D  47      76.885   7.303 -30.407  1.00 39.84           N  
ANISOU 6709  NH1 ARG D  47     4904   4539   5696   -393    893   -735       N  
ATOM   6710  NH2 ARG D  47      77.478   8.374 -28.464  1.00 29.23           N  
ANISOU 6710  NH2 ARG D  47     3548   3156   4403   -394    876   -721       N  
ATOM   6711  N   ARG D  48      73.187   9.845 -25.304  1.00 29.14           N  
ANISOU 6711  N   ARG D  48     3588   3208   4275   -317    744   -582       N  
ATOM   6712  CA  ARG D  48      73.714   9.041 -24.204  1.00 31.00           C  
ANISOU 6712  CA  ARG D  48     3782   3431   4566   -326    707   -600       C  
ATOM   6713  C   ARG D  48      72.641   8.141 -23.575  1.00 30.08           C  
ANISOU 6713  C   ARG D  48     3651   3338   4439   -312    654   -584       C  
ATOM   6714  O   ARG D  48      72.145   8.404 -22.469  1.00 23.83           O  
ANISOU 6714  O   ARG D  48     2858   2549   3647   -302    624   -563       O  
ATOM   6715  CB  ARG D  48      74.386   9.925 -23.143  1.00 28.35           C  
ANISOU 6715  CB  ARG D  48     3440   3070   4262   -332    711   -600       C  
ATOM   6716  CG  ARG D  48      75.617  10.696 -23.645  1.00 30.77           C  
ANISOU 6716  CG  ARG D  48     3752   3348   4593   -349    764   -624       C  
ATOM   6717  CD  ARG D  48      76.718   9.747 -24.130  1.00 36.75           C  
ANISOU 6717  CD  ARG D  48     4476   4091   5396   -369    774   -665       C  
ATOM   6718  NE  ARG D  48      77.154   8.824 -23.078  1.00 40.94           N  
ANISOU 6718  NE  ARG D  48     4963   4617   5977   -373    731   -681       N  
ATOM   6719  CZ  ARG D  48      78.097   9.097 -22.177  1.00 44.49           C  
ANISOU 6719  CZ  ARG D  48     5387   5044   6473   -383    728   -700       C  
ATOM   6720  NH1 ARG D  48      78.717  10.274 -22.188  1.00 41.83           N  
ANISOU 6720  NH1 ARG D  48     5064   4687   6143   -392    766   -706       N  
ATOM   6721  NH2 ARG D  48      78.413   8.198 -21.255  1.00 36.42           N  
ANISOU 6721  NH2 ARG D  48     4325   4021   5491   -383    687   -712       N  
ATOM   6722  N   PHE D  49      72.313   7.066 -24.288  1.00 26.28           N  
ANISOU 6722  N   PHE D  49     3159   2875   3951   -312    646   -596       N  
ATOM   6723  CA  PHE D  49      71.281   6.129 -23.860  1.00 25.32           C  
ANISOU 6723  CA  PHE D  49     3024   2775   3821   -301    601   -585       C  
ATOM   6724  C   PHE D  49      71.665   5.505 -22.518  1.00 26.45           C  
ANISOU 6724  C   PHE D  49     3132   2903   4015   -304    565   -590       C  
ATOM   6725  O   PHE D  49      70.794   5.163 -21.705  1.00 25.83           O  
ANISOU 6725  O   PHE D  49     3048   2837   3929   -291    527   -569       O  
ATOM   6726  CB  PHE D  49      71.053   5.092 -24.961  1.00 27.50           C  
ANISOU 6726  CB  PHE D  49     3292   3069   4088   -304    606   -605       C  
ATOM   6727  CG  PHE D  49      70.223   3.909 -24.545  1.00 27.84           C  
ANISOU 6727  CG  PHE D  49     3312   3129   4137   -298    564   -604       C  
ATOM   6728  CD1 PHE D  49      68.842   3.915 -24.715  1.00 24.88           C  
ANISOU 6728  CD1 PHE D  49     2956   2786   3713   -280    547   -582       C  
ATOM   6729  CD2 PHE D  49      70.824   2.783 -24.010  1.00 22.66           C  
ANISOU 6729  CD2 PHE D  49     2616   2456   3537   -308    545   -625       C  
ATOM   6730  CE1 PHE D  49      68.075   2.824 -24.347  1.00 31.06           C  
ANISOU 6730  CE1 PHE D  49     3717   3582   4504   -275    512   -583       C  
ATOM   6731  CE2 PHE D  49      70.052   1.677 -23.626  1.00 27.60           C  
ANISOU 6731  CE2 PHE D  49     3221   3094   4172   -302    510   -623       C  
ATOM   6732  CZ  PHE D  49      68.683   1.699 -23.803  1.00 25.93           C  
ANISOU 6732  CZ  PHE D  49     3028   2913   3912   -286    495   -603       C  
ATOM   6733  N   ASP D  50      72.972   5.404 -22.272  1.00 29.95           N  
ANISOU 6733  N   ASP D  50     3551   3319   4509   -320    577   -616       N  
ATOM   6734  CA  ASP D  50      73.500   4.933 -20.984  1.00 29.34           C  
ANISOU 6734  CA  ASP D  50     3440   3227   4482   -322    544   -621       C  
ATOM   6735  C   ASP D  50      73.407   5.939 -19.814  1.00 27.18           C  
ANISOU 6735  C   ASP D  50     3175   2948   4204   -314    531   -599       C  
ATOM   6736  O   ASP D  50      73.557   5.558 -18.650  1.00 36.34           O  
ANISOU 6736  O   ASP D  50     4311   4104   5394   -310    498   -596       O  
ATOM   6737  CB  ASP D  50      74.958   4.513 -21.145  1.00 30.75           C  
ANISOU 6737  CB  ASP D  50     3587   3379   4716   -340    562   -658       C  
ATOM   6738  CG  ASP D  50      75.863   5.684 -21.495  1.00 41.51           C  
ANISOU 6738  CG  ASP D  50     4965   4724   6082   -352    605   -671       C  
ATOM   6739  OD1 ASP D  50      76.959   5.777 -20.903  1.00 47.26           O  
ANISOU 6739  OD1 ASP D  50     5668   5430   6857   -362    607   -692       O  
ATOM   6740  OD2 ASP D  50      75.480   6.514 -22.355  1.00 37.90           O  
ANISOU 6740  OD2 ASP D  50     4544   4274   5582   -350    637   -660       O  
ATOM   6741  N   GLU D  51      73.181   7.218 -20.103  1.00 26.54           N  
ANISOU 6741  N   GLU D  51     3128   2867   4087   -311    558   -584       N  
ATOM   6742  CA  GLU D  51      73.136   8.220 -19.033  1.00 30.20           C  
ANISOU 6742  CA  GLU D  51     3599   3325   4549   -305    550   -568       C  
ATOM   6743  C   GLU D  51      72.004   9.231 -19.240  1.00 37.21           C  
ANISOU 6743  C   GLU D  51     4529   4229   5380   -291    559   -534       C  
ATOM   6744  O   GLU D  51      72.249  10.426 -19.442  1.00 31.88           O  
ANISOU 6744  O   GLU D  51     3878   3543   4692   -293    592   -529       O  
ATOM   6745  CB  GLU D  51      74.487   8.944 -18.883  1.00 34.02           C  
ANISOU 6745  CB  GLU D  51     4073   3782   5071   -322    580   -593       C  
ATOM   6746  CG  GLU D  51      75.683   7.989 -18.769  1.00 48.14           C  
ANISOU 6746  CG  GLU D  51     5819   5554   6917   -336    574   -629       C  
ATOM   6747  CD  GLU D  51      76.832   8.526 -17.917  1.00 56.61           C  
ANISOU 6747  CD  GLU D  51     6869   6606   8034   -346    579   -651       C  
ATOM   6748  OE1 GLU D  51      76.770   9.689 -17.466  1.00 52.94           O  
ANISOU 6748  OE1 GLU D  51     6421   6137   7557   -345    590   -641       O  
ATOM   6749  OE2 GLU D  51      77.803   7.768 -17.690  1.00 60.79           O  
ANISOU 6749  OE2 GLU D  51     7361   7123   8612   -355    570   -680       O  
ATOM   6750  N   PRO D  52      70.748   8.758 -19.189  1.00 24.42           N  
ANISOU 6750  N   PRO D  52     2918   2635   3727   -275    530   -510       N  
ATOM   6751  CA  PRO D  52      69.641   9.705 -19.346  1.00 27.89           C  
ANISOU 6751  CA  PRO D  52     3396   3090   4112   -259    535   -477       C  
ATOM   6752  C   PRO D  52      69.556  10.704 -18.171  1.00 25.19           C  
ANISOU 6752  C   PRO D  52     3060   2740   3772   -255    526   -460       C  
ATOM   6753  O   PRO D  52      68.986  11.780 -18.358  1.00 25.62           O  
ANISOU 6753  O   PRO D  52     3147   2798   3790   -245    545   -438       O  
ATOM   6754  CB  PRO D  52      68.409   8.793 -19.420  1.00 26.96           C  
ANISOU 6754  CB  PRO D  52     3276   2999   3967   -245    501   -462       C  
ATOM   6755  CG  PRO D  52      68.815   7.559 -18.701  1.00 23.99           C  
ANISOU 6755  CG  PRO D  52     2860   2617   3637   -252    469   -479       C  
ATOM   6756  CD  PRO D  52      70.280   7.374 -19.017  1.00 25.99           C  
ANISOU 6756  CD  PRO D  52     3093   2847   3937   -271    493   -513       C  
ATOM   6757  N   GLN D  53      70.138  10.372 -17.025  1.00 27.19           N  
ANISOU 6757  N   GLN D  53     3283   2982   4066   -260    501   -471       N  
ATOM   6758  CA  GLN D  53      70.106  11.270 -15.876  1.00 32.74           C  
ANISOU 6758  CA  GLN D  53     3988   3679   4773   -257    491   -459       C  
ATOM   6759  C   GLN D  53      70.852  12.582 -16.119  1.00 42.01           C  
ANISOU 6759  C   GLN D  53     5179   4833   5952   -267    536   -468       C  
ATOM   6760  O   GLN D  53      70.773  13.500 -15.308  1.00 38.00           O  
ANISOU 6760  O   GLN D  53     4677   4319   5442   -265    536   -458       O  
ATOM   6761  CB  GLN D  53      70.639  10.575 -14.621  1.00 30.72           C  
ANISOU 6761  CB  GLN D  53     3694   3420   4560   -260    454   -471       C  
ATOM   6762  CG  GLN D  53      72.079  10.130 -14.718  1.00 43.91           C  
ANISOU 6762  CG  GLN D  53     5332   5069   6280   -277    465   -508       C  
ATOM   6763  CD  GLN D  53      72.218   8.736 -15.287  1.00 33.95           C  
ANISOU 6763  CD  GLN D  53     4051   3812   5037   -279    454   -521       C  
ATOM   6764  OE1 GLN D  53      72.937   7.902 -14.745  1.00 44.15           O  
ANISOU 6764  OE1 GLN D  53     5307   5096   6371   -284    433   -539       O  
ATOM   6765  NE2 GLN D  53      71.531   8.478 -16.389  1.00 34.32           N  
ANISOU 6765  NE2 GLN D  53     4118   3869   5051   -276    467   -513       N  
ATOM   6766  N   LYS D  54      71.570  12.669 -17.235  1.00 38.57           N  
ANISOU 6766  N   LYS D  54     4748   4383   5522   -278    576   -487       N  
ATOM   6767  CA  LYS D  54      72.227  13.926 -17.613  1.00 43.23           C  
ANISOU 6767  CA  LYS D  54     5358   4952   6115   -288    626   -494       C  
ATOM   6768  C   LYS D  54      71.235  15.080 -17.735  1.00 37.25           C  
ANISOU 6768  C   LYS D  54     4642   4202   5311   -273    642   -460       C  
ATOM   6769  O   LYS D  54      71.535  16.206 -17.358  1.00 46.56           O  
ANISOU 6769  O   LYS D  54     5831   5363   6496   -277    667   -459       O  
ATOM   6770  CB  LYS D  54      73.005  13.778 -18.925  1.00 45.02           C  
ANISOU 6770  CB  LYS D  54     5590   5167   6350   -300    669   -516       C  
ATOM   6771  CG  LYS D  54      74.418  13.235 -18.776  1.00 43.88           C  
ANISOU 6771  CG  LYS D  54     5407   5001   6263   -321    674   -558       C  
ATOM   6772  CD  LYS D  54      75.105  13.139 -20.146  1.00 51.42           C  
ANISOU 6772  CD  LYS D  54     6371   5945   7223   -333    720   -578       C  
ATOM   6773  CE  LYS D  54      76.581  12.831 -20.011  1.00 52.90           C  
ANISOU 6773  CE  LYS D  54     6523   6108   7469   -354    733   -621       C  
ATOM   6774  NZ  LYS D  54      76.809  11.586 -19.237  1.00 55.20           N  
ANISOU 6774  NZ  LYS D  54     6772   6407   7796   -355    684   -636       N  
ATOM   6775  N   TYR D  55      70.051  14.801 -18.266  1.00 32.33           N  
ANISOU 6775  N   TYR D  55     4040   3602   4641   -255    629   -433       N  
ATOM   6776  CA  TYR D  55      69.050  15.847 -18.418  1.00 32.33           C  
ANISOU 6776  CA  TYR D  55     4078   3611   4594   -239    643   -398       C  
ATOM   6777  C   TYR D  55      67.637  15.454 -17.968  1.00 34.40           C  
ANISOU 6777  C   TYR D  55     4347   3902   4821   -219    599   -369       C  
ATOM   6778  O   TYR D  55      66.755  16.305 -17.918  1.00 39.20           O  
ANISOU 6778  O   TYR D  55     4984   4518   5394   -204    604   -340       O  
ATOM   6779  CB  TYR D  55      69.036  16.367 -19.856  1.00 31.51           C  
ANISOU 6779  CB  TYR D  55     4009   3506   4458   -234    691   -391       C  
ATOM   6780  CG  TYR D  55      68.419  15.422 -20.857  1.00 29.70           C  
ANISOU 6780  CG  TYR D  55     3784   3303   4197   -225    680   -387       C  
ATOM   6781  CD1 TYR D  55      67.104  15.596 -21.284  1.00 30.00           C  
ANISOU 6781  CD1 TYR D  55     3850   3370   4181   -202    670   -356       C  
ATOM   6782  CD2 TYR D  55      69.148  14.359 -21.385  1.00 30.17           C  
ANISOU 6782  CD2 TYR D  55     3819   3362   4283   -239    679   -418       C  
ATOM   6783  CE1 TYR D  55      66.529  14.741 -22.209  1.00 33.87           C  
ANISOU 6783  CE1 TYR D  55     4343   3887   4641   -194    660   -356       C  
ATOM   6784  CE2 TYR D  55      68.572  13.483 -22.310  1.00 29.75           C  
ANISOU 6784  CE2 TYR D  55     3768   3334   4201   -232    670   -418       C  
ATOM   6785  CZ  TYR D  55      67.269  13.681 -22.716  1.00 32.47           C  
ANISOU 6785  CZ  TYR D  55     4140   3708   4490   -209    660   -388       C  
ATOM   6786  OH  TYR D  55      66.690  12.829 -23.631  1.00 43.45           O  
ANISOU 6786  OH  TYR D  55     5531   5127   5852   -202    650   -391       O  
ATOM   6787  N   LYS D  56      67.417  14.179 -17.652  1.00 33.26           N  
ANISOU 6787  N   LYS D  56     4175   3773   4689   -219    557   -377       N  
ATOM   6788  CA  LYS D  56      66.103  13.743 -17.184  1.00 33.61           C  
ANISOU 6788  CA  LYS D  56     4222   3843   4704   -202    517   -353       C  
ATOM   6789  C   LYS D  56      66.045  13.768 -15.657  1.00 33.33           C  
ANISOU 6789  C   LYS D  56     4167   3804   4692   -202    482   -348       C  
ATOM   6790  O   LYS D  56      66.665  12.939 -14.976  1.00 28.51           O  
ANISOU 6790  O   LYS D  56     3523   3188   4120   -212    458   -367       O  
ATOM   6791  CB  LYS D  56      65.733  12.367 -17.738  1.00 33.39           C  
ANISOU 6791  CB  LYS D  56     4179   3835   4673   -200    494   -361       C  
ATOM   6792  CG  LYS D  56      65.546  12.342 -19.243  1.00 33.83           C  
ANISOU 6792  CG  LYS D  56     4256   3903   4696   -196    523   -363       C  
ATOM   6793  CD  LYS D  56      65.207  10.947 -19.745  1.00 38.21           C  
ANISOU 6793  CD  LYS D  56     4791   4477   5251   -196    500   -376       C  
ATOM   6794  CE  LYS D  56      65.368  10.858 -21.256  1.00 40.13           C  
ANISOU 6794  CE  LYS D  56     5048   4728   5469   -197    534   -388       C  
ATOM   6795  NZ  LYS D  56      64.177  10.260 -21.923  1.00 52.55           N  
ANISOU 6795  NZ  LYS D  56     6629   6337   7001   -181    516   -379       N  
ATOM   6796  N   PRO D  57      65.299  14.740 -15.114  1.00 30.49           N  
ANISOU 6796  N   PRO D  57     3830   3449   4308   -191    481   -323       N  
ATOM   6797  CA  PRO D  57      65.268  15.019 -13.672  1.00 38.16           C  
ANISOU 6797  CA  PRO D  57     4787   4416   5297   -192    455   -319       C  
ATOM   6798  C   PRO D  57      64.644  13.909 -12.821  1.00 32.58           C  
ANISOU 6798  C   PRO D  57     4058   3727   4595   -185    404   -312       C  
ATOM   6799  O   PRO D  57      64.938  13.837 -11.632  1.00 31.67           O  
ANISOU 6799  O   PRO D  57     3922   3607   4504   -189    380   -317       O  
ATOM   6800  CB  PRO D  57      64.407  16.277 -13.582  1.00 37.60           C  
ANISOU 6800  CB  PRO D  57     4749   4348   5189   -179    470   -290       C  
ATOM   6801  CG  PRO D  57      63.517  16.199 -14.774  1.00 43.03           C  
ANISOU 6801  CG  PRO D  57     5464   5053   5833   -164    480   -272       C  
ATOM   6802  CD  PRO D  57      64.353  15.587 -15.862  1.00 37.73           C  
ANISOU 6802  CD  PRO D  57     4786   4377   5175   -175    502   -296       C  
ATOM   6803  N   PHE D  58      63.804  13.059 -13.406  1.00 34.56           N  
ANISOU 6803  N   PHE D  58     4312   3997   4823   -176    388   -303       N  
ATOM   6804  CA  PHE D  58      63.103  12.045 -12.612  1.00 32.42           C  
ANISOU 6804  CA  PHE D  58     4023   3741   4556   -169    343   -295       C  
ATOM   6805  C   PHE D  58      63.875  10.727 -12.449  1.00 38.91           C  
ANISOU 6805  C   PHE D  58     4808   4556   5419   -179    326   -318       C  
ATOM   6806  O   PHE D  58      63.404   9.795 -11.795  1.00 39.10           O  
ANISOU 6806  O   PHE D  58     4815   4590   5452   -173    291   -313       O  
ATOM   6807  CB  PHE D  58      61.701  11.806 -13.183  1.00 31.82           C  
ANISOU 6807  CB  PHE D  58     3965   3690   4436   -153    333   -274       C  
ATOM   6808  CG  PHE D  58      60.760  12.953 -12.947  1.00 40.40           C  
ANISOU 6808  CG  PHE D  58     5081   4784   5485   -139    337   -247       C  
ATOM   6809  CD1 PHE D  58      60.808  13.661 -11.751  1.00 40.02           C  
ANISOU 6809  CD1 PHE D  58     5032   4728   5447   -140    328   -238       C  
ATOM   6810  CD2 PHE D  58      59.846  13.336 -13.917  1.00 47.79           C  
ANISOU 6810  CD2 PHE D  58     6045   5738   6377   -125    351   -231       C  
ATOM   6811  CE1 PHE D  58      59.956  14.725 -11.520  1.00 41.71           C  
ANISOU 6811  CE1 PHE D  58     5272   4947   5629   -128    334   -213       C  
ATOM   6812  CE2 PHE D  58      58.989  14.400 -13.696  1.00 54.22           C  
ANISOU 6812  CE2 PHE D  58     6885   6558   7158   -111    356   -205       C  
ATOM   6813  CZ  PHE D  58      59.045  15.099 -12.493  1.00 49.66           C  
ANISOU 6813  CZ  PHE D  58     6307   5969   6593   -113    348   -196       C  
ATOM   6814  N   ILE D  59      65.064  10.660 -13.036  1.00 32.84           N  
ANISOU 6814  N   ILE D  59     4029   3772   4678   -193    351   -344       N  
ATOM   6815  CA  ILE D  59      65.879   9.457 -12.979  1.00 33.15           C  
ANISOU 6815  CA  ILE D  59     4034   3803   4759   -202    338   -368       C  
ATOM   6816  C   ILE D  59      66.900   9.513 -11.855  1.00 28.95           C  
ANISOU 6816  C   ILE D  59     3476   3255   4267   -210    326   -381       C  
ATOM   6817  O   ILE D  59      67.651  10.472 -11.741  1.00 39.47           O  
ANISOU 6817  O   ILE D  59     4812   4574   5610   -218    349   -392       O  
ATOM   6818  CB  ILE D  59      66.588   9.215 -14.331  1.00 37.78           C  
ANISOU 6818  CB  ILE D  59     4621   4381   5352   -213    371   -392       C  
ATOM   6819  CG1 ILE D  59      65.538   8.974 -15.419  1.00 35.15           C  
ANISOU 6819  CG1 ILE D  59     4309   4069   4977   -204    378   -380       C  
ATOM   6820  CG2 ILE D  59      67.555   8.038 -14.233  1.00 33.89           C  
ANISOU 6820  CG2 ILE D  59     4091   3877   4908   -224    361   -418       C  
ATOM   6821  CD1 ILE D  59      66.121   8.743 -16.780  1.00 44.24           C  
ANISOU 6821  CD1 ILE D  59     5463   5216   6129   -213    410   -402       C  
ATOM   6822  N   SER D  60      66.926   8.477 -11.027  1.00 32.02           N  
ANISOU 6822  N   SER D  60     3837   3647   4680   -206    291   -382       N  
ATOM   6823  CA  SER D  60      67.878   8.411  -9.933  1.00 36.54           C  
ANISOU 6823  CA  SER D  60     4383   4210   5291   -210    275   -394       C  
ATOM   6824  C   SER D  60      69.066   7.525 -10.283  1.00 47.90           C  
ANISOU 6824  C   SER D  60     5790   5634   6774   -221    279   -424       C  
ATOM   6825  O   SER D  60      70.190   7.782  -9.850  1.00 58.13           O  
ANISOU 6825  O   SER D  60     7067   6918   8103   -229    284   -445       O  
ATOM   6826  CB  SER D  60      67.209   7.920  -8.647  1.00 26.08           C  
ANISOU 6826  CB  SER D  60     3047   2898   3965   -197    233   -372       C  
ATOM   6827  OG  SER D  60      67.134   6.512  -8.606  1.00 43.30           O  
ANISOU 6827  OG  SER D  60     5207   5080   6166   -193    211   -373       O  
ATOM   6828  N   ARG D  61      68.814   6.484 -11.073  1.00 42.63           N  
ANISOU 6828  N   ARG D  61     5118   4969   6111   -221    279   -427       N  
ATOM   6829  CA  ARG D  61      69.859   5.550 -11.476  1.00 39.99           C  
ANISOU 6829  CA  ARG D  61     4754   4621   5819   -231    284   -455       C  
ATOM   6830  C   ARG D  61      69.576   4.987 -12.857  1.00 40.23           C  
ANISOU 6830  C   ARG D  61     4793   4653   5840   -236    305   -465       C  
ATOM   6831  O   ARG D  61      68.416   4.837 -13.246  1.00 35.31           O  
ANISOU 6831  O   ARG D  61     4189   4046   5182   -228    301   -447       O  
ATOM   6832  CB  ARG D  61      69.933   4.376 -10.506  1.00 42.06           C  
ANISOU 6832  CB  ARG D  61     4985   4883   6112   -222    247   -451       C  
ATOM   6833  CG  ARG D  61      70.722   4.615  -9.240  1.00 53.39           C  
ANISOU 6833  CG  ARG D  61     6399   6314   7574   -219    227   -454       C  
ATOM   6834  CD  ARG D  61      71.235   3.274  -8.754  1.00 65.20           C  
ANISOU 6834  CD  ARG D  61     7859   7803   9110   -213    203   -461       C  
ATOM   6835  NE  ARG D  61      70.784   2.207  -9.650  1.00 66.42           N  
ANISOU 6835  NE  ARG D  61     8013   7956   9269   -215    208   -462       N  
ATOM   6836  CZ  ARG D  61      71.431   1.063  -9.859  1.00 75.59           C  
ANISOU 6836  CZ  ARG D  61     9145   9105  10471   -217    205   -478       C  
ATOM   6837  NH1 ARG D  61      70.932   0.161 -10.695  1.00 74.94           N  
ANISOU 6837  NH1 ARG D  61     9062   9022  10391   -219    212   -481       N  
ATOM   6838  NH2 ARG D  61      72.578   0.820  -9.237  1.00 79.80           N  
ANISOU 6838  NH2 ARG D  61     9648   9627  11045   -217    195   -494       N  
ATOM   6839  N   CYS D  62      70.639   4.659 -13.583  1.00 29.04           N  
ANISOU 6839  N   CYS D  62     3360   3221   4453   -250    328   -494       N  
ATOM   6840  CA  CYS D  62      70.521   3.944 -14.844  1.00 28.42           C  
ANISOU 6840  CA  CYS D  62     3282   3144   4372   -256    346   -508       C  
ATOM   6841  C   CYS D  62      71.683   2.954 -14.988  1.00 36.24           C  
ANISOU 6841  C   CYS D  62     4236   4116   5416   -267    348   -539       C  
ATOM   6842  O   CYS D  62      72.834   3.299 -14.710  1.00 40.14           O  
ANISOU 6842  O   CYS D  62     4715   4594   5941   -276    358   -558       O  
ATOM   6843  CB  CYS D  62      70.513   4.936 -16.006  1.00 32.09           C  
ANISOU 6843  CB  CYS D  62     3779   3611   4804   -263    387   -513       C  
ATOM   6844  SG  CYS D  62      70.240   4.205 -17.635  1.00 31.11           S  
ANISOU 6844  SG  CYS D  62     3661   3496   4665   -269    411   -530       S  
ATOM   6845  N   VAL D  63      71.386   1.725 -15.405  1.00 37.00           N  
ANISOU 6845  N   VAL D  63     4317   4215   5525   -267    340   -545       N  
ATOM   6846  CA  VAL D  63      72.427   0.716 -15.651  1.00 35.13           C  
ANISOU 6846  CA  VAL D  63     4047   3961   5341   -277    344   -574       C  
ATOM   6847  C   VAL D  63      72.246   0.058 -17.011  1.00 38.45           C  
ANISOU 6847  C   VAL D  63     4469   4385   5756   -286    367   -593       C  
ATOM   6848  O   VAL D  63      71.120  -0.266 -17.411  1.00 30.19           O  
ANISOU 6848  O   VAL D  63     3436   3356   4678   -280    362   -581       O  
ATOM   6849  CB  VAL D  63      72.460  -0.390 -14.562  1.00 41.84           C  
ANISOU 6849  CB  VAL D  63     4865   4805   6228   -266    308   -566       C  
ATOM   6850  CG1 VAL D  63      72.811   0.206 -13.212  1.00 46.71           C  
ANISOU 6850  CG1 VAL D  63     5475   5419   6852   -257    285   -552       C  
ATOM   6851  CG2 VAL D  63      71.127  -1.134 -14.488  1.00 41.99           C  
ANISOU 6851  CG2 VAL D  63     4890   4838   6225   -255    288   -544       C  
ATOM   6852  N   VAL D  64      73.367  -0.146 -17.694  1.00 33.18           N  
ANISOU 6852  N   VAL D  64     3785   3701   5121   -301    393   -625       N  
ATOM   6853  CA  VAL D  64      73.417  -0.878 -18.948  1.00 35.41           C  
ANISOU 6853  CA  VAL D  64     4062   3983   5407   -313    416   -649       C  
ATOM   6854  C   VAL D  64      74.471  -1.971 -18.822  1.00 41.52           C  
ANISOU 6854  C   VAL D  64     4795   4736   6245   -321    413   -676       C  
ATOM   6855  O   VAL D  64      75.326  -1.912 -17.942  1.00 43.31           O  
ANISOU 6855  O   VAL D  64     5002   4947   6508   -319    400   -679       O  
ATOM   6856  CB  VAL D  64      73.789   0.039 -20.121  1.00 32.97           C  
ANISOU 6856  CB  VAL D  64     3778   3676   5072   -325    458   -665       C  
ATOM   6857  CG1 VAL D  64      72.641   0.970 -20.450  1.00 37.89           C  
ANISOU 6857  CG1 VAL D  64     4443   4324   5631   -315    463   -638       C  
ATOM   6858  CG2 VAL D  64      75.045   0.826 -19.797  1.00 36.18           C  
ANISOU 6858  CG2 VAL D  64     4178   4061   5506   -334    474   -679       C  
ATOM   6859  N   GLN D  65      74.421  -2.965 -19.699  1.00 80.93           N  
ANISOU 6859  N   GLN D  65     9774   9727  11251   -329    424   -697       N  
ATOM   6860  CA  GLN D  65      75.390  -4.054 -19.646  1.00 81.06           C  
ANISOU 6860  CA  GLN D  65     9750   9721  11329   -337    424   -723       C  
ATOM   6861  C   GLN D  65      76.810  -3.561 -19.931  1.00 81.48           C  
ANISOU 6861  C   GLN D  65     9793   9755  11412   -351    449   -751       C  
ATOM   6862  O   GLN D  65      77.734  -3.829 -19.165  1.00 81.20           O  
ANISOU 6862  O   GLN D  65     9728   9701  11422   -350    437   -759       O  
ATOM   6863  CB  GLN D  65      75.004  -5.171 -20.614  1.00 71.82           C  
ANISOU 6863  CB  GLN D  65     8568   8554  10165   -344    435   -743       C  
ATOM   6864  CG  GLN D  65      74.685  -6.488 -19.929  1.00 70.97           C  
ANISOU 6864  CG  GLN D  65     8432   8439  10097   -335    407   -736       C  
ATOM   6865  CD  GLN D  65      74.634  -7.647 -20.902  1.00 71.40           C  
ANISOU 6865  CD  GLN D  65     8466   8490  10173   -347    424   -765       C  
ATOM   6866  OE1 GLN D  65      75.354  -7.664 -21.900  1.00 72.25           O  
ANISOU 6866  OE1 GLN D  65     8569   8592  10292   -364    455   -797       O  
ATOM   6867  NE2 GLN D  65      73.780  -8.620 -20.618  1.00 70.85           N  
ANISOU 6867  NE2 GLN D  65     8385   8423  10112   -339    407   -755       N  
ATOM   6868  N   GLY D  66      76.972  -2.835 -21.031  1.00 50.50           N  
ANISOU 6868  N   GLY D  66     5892   5836   7460   -364    486   -766       N  
ATOM   6869  CA  GLY D  66      78.264  -2.290 -21.400  1.00 50.97           C  
ANISOU 6869  CA  GLY D  66     5945   5877   7545   -380    516   -794       C  
ATOM   6870  C   GLY D  66      78.170  -0.851 -21.870  1.00 51.30           C  
ANISOU 6870  C   GLY D  66     6026   5926   7540   -384    544   -787       C  
ATOM   6871  O   GLY D  66      77.079  -0.344 -22.121  1.00 51.35           O  
ANISOU 6871  O   GLY D  66     6064   5953   7492   -374    544   -762       O  
ATOM   6872  N   LYS D  67      79.316  -0.189 -21.991  1.00111.08           N  
ANISOU 6872  N   LYS D  67    13592  13479  15135   -396    571   -809       N  
ATOM   6873  CA  LYS D  67      79.341   1.201 -22.425  1.00111.41           C  
ANISOU 6873  CA  LYS D  67    13669  13522  15139   -401    603   -803       C  
ATOM   6874  C   LYS D  67      79.128   1.310 -23.929  1.00112.68           C  
ANISOU 6874  C   LYS D  67    13856  13692  15267   -411    643   -814       C  
ATOM   6875  O   LYS D  67      78.843   2.387 -24.451  1.00113.16           O  
ANISOU 6875  O   LYS D  67    13953  13760  15284   -410    670   -801       O  
ATOM   6876  CB  LYS D  67      80.651   1.878 -22.017  1.00101.37           C  
ANISOU 6876  CB  LYS D  67    12383  12227  13907   -412    620   -825       C  
ATOM   6877  CG  LYS D  67      80.619   2.494 -20.625  1.00100.43           C  
ANISOU 6877  CG  LYS D  67    12260  12107  13792   -400    591   -805       C  
ATOM   6878  CD  LYS D  67      81.578   3.668 -20.507  1.00100.67           C  
ANISOU 6878  CD  LYS D  67    12294  12120  13837   -412    620   -823       C  
ATOM   6879  CE  LYS D  67      82.079   3.833 -19.080  1.00100.14           C  
ANISOU 6879  CE  LYS D  67    12200  12048  13802   -405    588   -823       C  
ATOM   6880  NZ  LYS D  67      83.382   4.560 -19.016  1.00100.69           N  
ANISOU 6880  NZ  LYS D  67    12254  12096  13908   -421    617   -857       N  
ATOM   6881  N   LYS D  68      79.262   0.185 -24.622  1.00 82.42           N  
ANISOU 6881  N   LYS D  68    10003   9859  11454   -419    647   -837       N  
ATOM   6882  CA  LYS D  68      79.051   0.149 -26.062  1.00 83.89           C  
ANISOU 6882  CA  LYS D  68    10209  10058  11608   -428    682   -850       C  
ATOM   6883  C   LYS D  68      77.584   0.396 -26.397  1.00 84.28           C  
ANISOU 6883  C   LYS D  68    10292  10140  11590   -412    672   -819       C  
ATOM   6884  O   LYS D  68      76.734  -0.463 -26.176  1.00 84.07           O  
ANISOU 6884  O   LYS D  68    10255  10129  11558   -402    642   -810       O  
ATOM   6885  CB  LYS D  68      79.507  -1.191 -26.640  1.00 74.54           C  
ANISOU 6885  CB  LYS D  68     8992   8867  10464   -440    686   -884       C  
ATOM   6886  CG  LYS D  68      79.968  -1.116 -28.087  1.00 76.22           C  
ANISOU 6886  CG  LYS D  68     9215   9080  10665   -457    733   -913       C  
ATOM   6887  CD  LYS D  68      79.718  -2.426 -28.820  1.00 77.17           C  
ANISOU 6887  CD  LYS D  68     9314   9210  10796   -464    732   -936       C  
ATOM   6888  CE  LYS D  68      80.212  -3.618 -28.013  1.00 76.17           C  
ANISOU 6888  CE  LYS D  68     9139   9063  10737   -466    703   -951       C  
ATOM   6889  NZ  LYS D  68      81.696  -3.747 -28.054  1.00 76.23           N  
ANISOU 6889  NZ  LYS D  68     9120   9040  10805   -483    724   -985       N  
ATOM   6890  N   LEU D  69      77.298   1.579 -26.926  1.00 54.39           N  
ANISOU 6890  N   LEU D  69     6547   6364   7755   -408    700   -803       N  
ATOM   6891  CA  LEU D  69      75.947   1.938 -27.329  1.00 62.15           C  
ANISOU 6891  CA  LEU D  69     7564   7380   8672   -392    694   -774       C  
ATOM   6892  C   LEU D  69      75.663   1.410 -28.726  1.00 63.97           C  
ANISOU 6892  C   LEU D  69     7801   7630   8873   -397    717   -793       C  
ATOM   6893  O   LEU D  69      76.302   1.817 -29.692  1.00 70.93           O  
ANISOU 6893  O   LEU D  69     8697   8507   9748   -408    759   -810       O  
ATOM   6894  CB  LEU D  69      75.772   3.456 -27.317  1.00 67.05           C  
ANISOU 6894  CB  LEU D  69     8225   8001   9251   -383    715   -747       C  
ATOM   6895  CG  LEU D  69      75.271   4.115 -26.034  1.00 61.95           C  
ANISOU 6895  CG  LEU D  69     7587   7354   8599   -369    685   -715       C  
ATOM   6896  CD1 LEU D  69      75.860   3.438 -24.812  1.00 60.76           C  
ANISOU 6896  CD1 LEU D  69     7395   7184   8509   -373    652   -725       C  
ATOM   6897  CD2 LEU D  69      75.600   5.597 -26.046  1.00 58.30           C  
ANISOU 6897  CD2 LEU D  69     7155   6879   8118   -369    718   -702       C  
ATOM   6898  N   GLU D  70      74.698   0.507 -28.828  1.00 37.79           N  
ANISOU 6898  N   GLU D  70     4476   4338   5543   -389    690   -790       N  
ATOM   6899  CA  GLU D  70      74.314  -0.058 -30.110  1.00 40.13           C  
ANISOU 6899  CA  GLU D  70     4777   4660   5811   -393    707   -810       C  
ATOM   6900  C   GLU D  70      72.843  -0.432 -30.084  1.00 41.67           C  
ANISOU 6900  C   GLU D  70     4979   4889   5964   -375    676   -791       C  
ATOM   6901  O   GLU D  70      72.270  -0.638 -29.019  1.00 35.93           O  
ANISOU 6901  O   GLU D  70     4243   4162   5248   -364    639   -770       O  
ATOM   6902  CB  GLU D  70      75.157  -1.294 -30.413  1.00 41.84           C  
ANISOU 6902  CB  GLU D  70     4952   4859   6085   -412    713   -852       C  
ATOM   6903  CG  GLU D  70      76.133  -1.654 -29.308  1.00 54.77           C  
ANISOU 6903  CG  GLU D  70     6556   6461   7794   -420    697   -860       C  
ATOM   6904  CD  GLU D  70      76.523  -3.117 -29.325  1.00 69.72           C  
ANISOU 6904  CD  GLU D  70     8405   8342   9742   -432    686   -892       C  
ATOM   6905  OE1 GLU D  70      76.770  -3.682 -28.240  1.00 68.32           O  
ANISOU 6905  OE1 GLU D  70     8199   8145   9613   -429    657   -888       O  
ATOM   6906  OE2 GLU D  70      76.584  -3.702 -30.424  1.00 78.69           O  
ANISOU 6906  OE2 GLU D  70     9536   9488  10874   -443    709   -921       O  
ATOM   6907  N   VAL D  71      72.232  -0.517 -31.259  1.00 34.27           N  
ANISOU 6907  N   VAL D  71     4057   3984   4978   -372    692   -800       N  
ATOM   6908  CA  VAL D  71      70.852  -0.970 -31.349  1.00 35.51           C  
ANISOU 6908  CA  VAL D  71     4217   4178   5097   -357    664   -789       C  
ATOM   6909  C   VAL D  71      70.722  -2.306 -30.611  1.00 43.05           C  
ANISOU 6909  C   VAL D  71     5130   5122   6106   -362    632   -804       C  
ATOM   6910  O   VAL D  71      71.570  -3.186 -30.766  1.00 32.62           O  
ANISOU 6910  O   VAL D  71     3778   3781   4837   -380    641   -836       O  
ATOM   6911  CB  VAL D  71      70.407  -1.133 -32.814  1.00 40.99           C  
ANISOU 6911  CB  VAL D  71     4924   4909   5741   -356    687   -808       C  
ATOM   6912  CG1 VAL D  71      69.012  -1.763 -32.890  1.00 36.54           C  
ANISOU 6912  CG1 VAL D  71     4355   4383   5146   -343    657   -806       C  
ATOM   6913  CG2 VAL D  71      70.433   0.223 -33.525  1.00 38.45           C  
ANISOU 6913  CG2 VAL D  71     4648   4599   5361   -346    720   -788       C  
ATOM   6914  N   GLY D  72      69.681  -2.445 -29.792  1.00 38.36           N  
ANISOU 6914  N   GLY D  72     4536   4540   5501   -347    595   -779       N  
ATOM   6915  CA  GLY D  72      69.490  -3.661 -29.020  1.00 35.83           C  
ANISOU 6915  CA  GLY D  72     4177   4206   5229   -350    566   -788       C  
ATOM   6916  C   GLY D  72      70.023  -3.582 -27.600  1.00 33.69           C  
ANISOU 6916  C   GLY D  72     3892   3901   5005   -348    544   -768       C  
ATOM   6917  O   GLY D  72      69.820  -4.508 -26.808  1.00 35.06           O  
ANISOU 6917  O   GLY D  72     4038   4063   5218   -347    517   -768       O  
ATOM   6918  N   SER D  73      70.703  -2.486 -27.267  1.00 31.74           N  
ANISOU 6918  N   SER D  73     3665   3639   4756   -348    556   -753       N  
ATOM   6919  CA  SER D  73      71.157  -2.270 -25.893  1.00 28.57           C  
ANISOU 6919  CA  SER D  73     3253   3211   4392   -344    534   -734       C  
ATOM   6920  C   SER D  73      69.963  -2.117 -24.971  1.00 23.66           C  
ANISOU 6920  C   SER D  73     2641   2603   3744   -325    498   -699       C  
ATOM   6921  O   SER D  73      68.959  -1.496 -25.331  1.00 22.74           O  
ANISOU 6921  O   SER D  73     2554   2514   3570   -312    498   -680       O  
ATOM   6922  CB  SER D  73      72.028  -1.011 -25.774  1.00 33.27           C  
ANISOU 6922  CB  SER D  73     3868   3789   4983   -347    556   -726       C  
ATOM   6923  OG  SER D  73      73.196  -1.107 -26.569  1.00 41.19           O  
ANISOU 6923  OG  SER D  73     4863   4777   6013   -365    591   -759       O  
ATOM   6924  N   VAL D  74      70.083  -2.665 -23.768  1.00 23.26           N  
ANISOU 6924  N   VAL D  74     2567   2535   3737   -321    469   -689       N  
ATOM   6925  CA  VAL D  74      68.998  -2.595 -22.805  1.00 24.79           C  
ANISOU 6925  CA  VAL D  74     2768   2739   3911   -304    436   -656       C  
ATOM   6926  C   VAL D  74      69.467  -1.822 -21.598  1.00 19.98           C  
ANISOU 6926  C   VAL D  74     2163   2113   3316   -298    422   -633       C  
ATOM   6927  O   VAL D  74      70.578  -2.016 -21.123  1.00 26.73           O  
ANISOU 6927  O   VAL D  74     2997   2943   4218   -306    423   -645       O  
ATOM   6928  CB  VAL D  74      68.584  -3.995 -22.347  1.00 28.44           C  
ANISOU 6928  CB  VAL D  74     3199   3198   4411   -303    412   -663       C  
ATOM   6929  CG1 VAL D  74      67.568  -3.917 -21.198  1.00 21.25           C  
ANISOU 6929  CG1 VAL D  74     2294   2294   3486   -285    378   -628       C  
ATOM   6930  CG2 VAL D  74      68.048  -4.788 -23.521  1.00 26.73           C  
ANISOU 6930  CG2 VAL D  74     2975   3000   4181   -310    425   -689       C  
ATOM   6931  N   ARG D  75      68.622  -0.936 -21.095  1.00 17.41           N  
ANISOU 6931  N   ARG D  75     1865   1802   2948   -284    409   -601       N  
ATOM   6932  CA  ARG D  75      68.954  -0.221 -19.882  1.00 19.01           C  
ANISOU 6932  CA  ARG D  75     2070   1991   3161   -277    393   -580       C  
ATOM   6933  C   ARG D  75      67.855  -0.449 -18.862  1.00 20.15           C  
ANISOU 6933  C   ARG D  75     2216   2147   3294   -261    357   -550       C  
ATOM   6934  O   ARG D  75      66.713  -0.718 -19.221  1.00 20.01           O  
ANISOU 6934  O   ARG D  75     2208   2150   3245   -254    350   -543       O  
ATOM   6935  CB  ARG D  75      69.156   1.272 -20.158  1.00 22.18           C  
ANISOU 6935  CB  ARG D  75     2505   2395   3528   -277    417   -569       C  
ATOM   6936  CG  ARG D  75      67.865   2.058 -20.429  1.00 21.13           C  
ANISOU 6936  CG  ARG D  75     2408   2290   3332   -262    416   -543       C  
ATOM   6937  CD  ARG D  75      68.174   3.557 -20.635  1.00 23.54           C  
ANISOU 6937  CD  ARG D  75     2745   2592   3609   -261    443   -531       C  
ATOM   6938  NE  ARG D  75      66.976   4.336 -20.927  1.00 23.86           N  
ANISOU 6938  NE  ARG D  75     2819   2656   3589   -246    443   -504       N  
ATOM   6939  CZ  ARG D  75      66.984   5.505 -21.558  1.00 29.76           C  
ANISOU 6939  CZ  ARG D  75     3599   3407   4299   -242    473   -495       C  
ATOM   6940  NH1 ARG D  75      68.137   6.033 -21.975  1.00 24.38           N  
ANISOU 6940  NH1 ARG D  75     2921   2705   3636   -256    507   -511       N  
ATOM   6941  NH2 ARG D  75      65.841   6.145 -21.778  1.00 28.40           N  
ANISOU 6941  NH2 ARG D  75     3457   3259   4074   -225    470   -469       N  
ATOM   6942  N   GLU D  76      68.217  -0.367 -17.592  1.00 23.12           N  
ANISOU 6942  N   GLU D  76     2580   2508   3697   -256    335   -536       N  
ATOM   6943  CA  GLU D  76      67.261  -0.466 -16.504  1.00 29.49           C  
ANISOU 6943  CA  GLU D  76     3389   3323   4492   -241    303   -507       C  
ATOM   6944  C   GLU D  76      67.339   0.814 -15.694  1.00 27.07           C  
ANISOU 6944  C   GLU D  76     3103   3017   4166   -235    298   -485       C  
ATOM   6945  O   GLU D  76      68.392   1.160 -15.178  1.00 25.67           O  
ANISOU 6945  O   GLU D  76     2915   2823   4017   -240    300   -492       O  
ATOM   6946  CB  GLU D  76      67.588  -1.675 -15.623  1.00 29.47           C  
ANISOU 6946  CB  GLU D  76     3351   3304   4540   -239    279   -508       C  
ATOM   6947  CG  GLU D  76      66.535  -2.766 -15.647  1.00 46.78           C  
ANISOU 6947  CG  GLU D  76     5535   5506   6733   -233    264   -503       C  
ATOM   6948  CD  GLU D  76      65.708  -2.814 -14.362  1.00 63.01           C  
ANISOU 6948  CD  GLU D  76     7593   7566   8782   -217    232   -470       C  
ATOM   6949  OE1 GLU D  76      66.264  -3.207 -13.308  1.00 69.48           O  
ANISOU 6949  OE1 GLU D  76     8394   8370   9637   -212    214   -462       O  
ATOM   6950  OE2 GLU D  76      64.507  -2.459 -14.404  1.00 50.83           O  
ANISOU 6950  OE2 GLU D  76     6073   6044   7198   -209    225   -453       O  
ATOM   6951  N   VAL D  77      66.240   1.544 -15.593  1.00 28.66           N  
ANISOU 6951  N   VAL D  77     3332   3237   4321   -224    292   -460       N  
ATOM   6952  CA  VAL D  77      66.303   2.788 -14.843  1.00 26.60           C  
ANISOU 6952  CA  VAL D  77     3089   2974   4042   -218    290   -441       C  
ATOM   6953  C   VAL D  77      65.453   2.732 -13.584  1.00 23.66           C  
ANISOU 6953  C   VAL D  77     2718   2611   3663   -204    255   -413       C  
ATOM   6954  O   VAL D  77      64.408   2.092 -13.559  1.00 24.44           O  
ANISOU 6954  O   VAL D  77     2816   2721   3747   -196    239   -402       O  
ATOM   6955  CB  VAL D  77      66.003   4.050 -15.721  1.00 33.82           C  
ANISOU 6955  CB  VAL D  77     4041   3900   4910   -218    319   -436       C  
ATOM   6956  CG1 VAL D  77      66.011   3.716 -17.211  1.00 36.71           C  
ANISOU 6956  CG1 VAL D  77     4411   4273   5262   -225    345   -456       C  
ATOM   6957  CG2 VAL D  77      64.719   4.727 -15.309  1.00 33.03           C  
ANISOU 6957  CG2 VAL D  77     3967   3819   4765   -203    305   -405       C  
ATOM   6958  N   ASP D  78      65.955   3.359 -12.528  1.00 25.57           N  
ANISOU 6958  N   ASP D  78     2957   2843   3915   -202    245   -404       N  
ATOM   6959  CA  ASP D  78      65.203   3.538 -11.297  1.00 29.57           C  
ANISOU 6959  CA  ASP D  78     3468   3358   4410   -189    216   -376       C  
ATOM   6960  C   ASP D  78      64.795   4.999 -11.234  1.00 27.55           C  
ANISOU 6960  C   ASP D  78     3243   3110   4114   -186    227   -361       C  
ATOM   6961  O   ASP D  78      65.621   5.878 -11.462  1.00 27.67           O  
ANISOU 6961  O   ASP D  78     3264   3115   4132   -194    250   -373       O  
ATOM   6962  CB  ASP D  78      66.068   3.189 -10.085  1.00 30.30           C  
ANISOU 6962  CB  ASP D  78     3532   3437   4542   -188    194   -378       C  
ATOM   6963  CG  ASP D  78      66.532   1.748 -10.099  1.00 46.06           C  
ANISOU 6963  CG  ASP D  78     5497   5423   6581   -189    184   -391       C  
ATOM   6964  OD1 ASP D  78      67.760   1.511 -10.040  1.00 54.16           O  
ANISOU 6964  OD1 ASP D  78     6500   6433   7645   -197    189   -412       O  
ATOM   6965  OD2 ASP D  78      65.667   0.848 -10.163  1.00 42.64           O  
ANISOU 6965  OD2 ASP D  78     5061   4996   6145   -183    172   -382       O  
ATOM   6966  N   LEU D  79      63.525   5.264 -10.946  1.00 30.08           N  
ANISOU 6966  N   LEU D  79     3583   3448   4399   -174    213   -336       N  
ATOM   6967  CA  LEU D  79      63.057   6.646 -10.878  1.00 27.54           C  
ANISOU 6967  CA  LEU D  79     3291   3133   4040   -169    224   -320       C  
ATOM   6968  C   LEU D  79      63.133   7.179  -9.460  1.00 28.94           C  
ANISOU 6968  C   LEU D  79     3465   3308   4224   -165    204   -306       C  
ATOM   6969  O   LEU D  79      63.114   6.420  -8.501  1.00 20.35           O  
ANISOU 6969  O   LEU D  79     2356   2219   3155   -160    176   -300       O  
ATOM   6970  CB  LEU D  79      61.618   6.762 -11.367  1.00 26.27           C  
ANISOU 6970  CB  LEU D  79     3153   2993   3834   -158    222   -301       C  
ATOM   6971  CG  LEU D  79      61.346   6.464 -12.840  1.00 34.37           C  
ANISOU 6971  CG  LEU D  79     4189   4029   4842   -160    243   -313       C  
ATOM   6972  CD1 LEU D  79      59.851   6.469 -13.092  1.00 34.25           C  
ANISOU 6972  CD1 LEU D  79     4191   4038   4785   -146    232   -295       C  
ATOM   6973  CD2 LEU D  79      62.052   7.476 -13.731  1.00 33.70           C  
ANISOU 6973  CD2 LEU D  79     4122   3937   4745   -166    280   -323       C  
ATOM   6974  N   LYS D  80      63.209   8.496  -9.326  1.00 34.66           N  
ANISOU 6974  N   LYS D  80     4210   4031   4930   -166    220   -300       N  
ATOM   6975  CA  LYS D  80      63.121   9.109  -8.006  1.00 32.42           C  
ANISOU 6975  CA  LYS D  80     3925   3749   4646   -161    202   -287       C  
ATOM   6976  C   LYS D  80      61.716   8.925  -7.401  1.00 29.85           C  
ANISOU 6976  C   LYS D  80     3610   3440   4292   -147    176   -259       C  
ATOM   6977  O   LYS D  80      60.742   8.646  -8.104  1.00 25.51           O  
ANISOU 6977  O   LYS D  80     3074   2902   3716   -141    177   -249       O  
ATOM   6978  CB  LYS D  80      63.506  10.582  -8.078  1.00 35.90           C  
ANISOU 6978  CB  LYS D  80     4384   4181   5074   -166    230   -290       C  
ATOM   6979  CG  LYS D  80      65.000  10.792  -8.302  1.00 38.32           C  
ANISOU 6979  CG  LYS D  80     4675   4470   5417   -181    252   -319       C  
ATOM   6980  CD  LYS D  80      65.344  12.262  -8.438  1.00 42.10           C  
ANISOU 6980  CD  LYS D  80     5172   4937   5886   -188    285   -323       C  
ATOM   6981  CE  LYS D  80      66.779  12.439  -8.926  1.00 39.85           C  
ANISOU 6981  CE  LYS D  80     4874   4633   5636   -204    313   -355       C  
ATOM   6982  NZ  LYS D  80      66.893  13.672  -9.756  1.00 45.08           N  
ANISOU 6982  NZ  LYS D  80     5564   5284   6281   -209    358   -357       N  
ATOM   6983  N   SER D  81      61.629   9.082  -6.089  1.00 23.81           N  
ANISOU 6983  N   SER D  81     2837   2678   3531   -142    153   -247       N  
ATOM   6984  CA  SER D  81      60.405   8.831  -5.337  1.00 25.62           C  
ANISOU 6984  CA  SER D  81     3073   2921   3739   -130    126   -222       C  
ATOM   6985  C   SER D  81      59.285   9.840  -5.640  1.00 23.97           C  
ANISOU 6985  C   SER D  81     2896   2723   3487   -123    137   -204       C  
ATOM   6986  O   SER D  81      59.544  10.956  -6.083  1.00 20.23           O  
ANISOU 6986  O   SER D  81     2440   2245   3002   -127    163   -207       O  
ATOM   6987  CB  SER D  81      60.755   8.914  -3.863  1.00 26.83           C  
ANISOU 6987  CB  SER D  81     3212   3075   3908   -127    103   -217       C  
ATOM   6988  OG  SER D  81      61.333  10.186  -3.615  1.00 24.46           O  
ANISOU 6988  OG  SER D  81     2919   2770   3605   -134    119   -225       O  
ATOM   6989  N   GLY D  82      58.044   9.449  -5.376  1.00 26.32           N  
ANISOU 6989  N   GLY D  82     3201   3035   3764   -113    118   -184       N  
ATOM   6990  CA  GLY D  82      56.917  10.359  -5.527  1.00 32.76           C  
ANISOU 6990  CA  GLY D  82     4044   3862   4541   -104    124   -166       C  
ATOM   6991  C   GLY D  82      56.181  10.277  -6.853  1.00 36.89           C  
ANISOU 6991  C   GLY D  82     4584   4396   5038    -99    139   -165       C  
ATOM   6992  O   GLY D  82      55.163  10.943  -7.056  1.00 32.50           O  
ANISOU 6992  O   GLY D  82     4050   3852   4447    -89    142   -148       O  
ATOM   6993  N   LEU D  83      56.693   9.463  -7.770  1.00 31.41           N  
ANISOU 6993  N   LEU D  83     3878   3698   4358   -105    148   -183       N  
ATOM   6994  CA  LEU D  83      56.079   9.324  -9.087  1.00 27.35           C  
ANISOU 6994  CA  LEU D  83     3377   3197   3819   -100    162   -186       C  
ATOM   6995  C   LEU D  83      55.193   8.078  -9.134  1.00 24.09           C  
ANISOU 6995  C   LEU D  83     2950   2797   3407    -95    140   -186       C  
ATOM   6996  O   LEU D  83      55.363   7.164  -8.332  1.00 17.80           O  
ANISOU 6996  O   LEU D  83     2131   1993   2638    -98    120   -188       O  
ATOM   6997  CB  LEU D  83      57.166   9.223 -10.164  1.00 32.74           C  
ANISOU 6997  CB  LEU D  83     4055   3870   4516   -111    189   -209       C  
ATOM   6998  CG  LEU D  83      57.723  10.509 -10.794  1.00 35.25           C  
ANISOU 6998  CG  LEU D  83     4396   4180   4818   -113    223   -210       C  
ATOM   6999  CD1 LEU D  83      57.367  11.721  -9.975  1.00 31.26           C  
ANISOU 6999  CD1 LEU D  83     3908   3673   4297   -107    223   -190       C  
ATOM   7000  CD2 LEU D  83      59.238  10.390 -10.963  1.00 32.28           C  
ANISOU 7000  CD2 LEU D  83     4004   3783   4480   -129    240   -234       C  
ATOM   7001  N   PRO D  84      54.261   8.030 -10.094  1.00 20.45           N  
ANISOU 7001  N   PRO D  84     2501   2355   2914    -87    146   -185       N  
ATOM   7002  CA  PRO D  84      53.417   6.844 -10.261  1.00 24.88           C  
ANISOU 7002  CA  PRO D  84     3047   2928   3477    -84    129   -191       C  
ATOM   7003  C   PRO D  84      54.184   5.598 -10.721  1.00 31.83           C  
ANISOU 7003  C   PRO D  84     3901   3799   4394    -95    131   -216       C  
ATOM   7004  O   PRO D  84      53.585   4.530 -10.757  1.00 44.75           O  
ANISOU 7004  O   PRO D  84     5522   5441   6040    -95    119   -222       O  
ATOM   7005  CB  PRO D  84      52.412   7.250 -11.347  1.00 21.94           C  
ANISOU 7005  CB  PRO D  84     2695   2581   3061    -73    138   -189       C  
ATOM   7006  CG  PRO D  84      52.840   8.590 -11.865  1.00 27.42           C  
ANISOU 7006  CG  PRO D  84     3415   3273   3731    -70    163   -182       C  
ATOM   7007  CD  PRO D  84      54.093   9.013 -11.179  1.00 25.20           C  
ANISOU 7007  CD  PRO D  84     3129   2966   3480    -81    171   -183       C  
ATOM   7008  N   ALA D  85      55.474   5.726 -11.012  1.00 25.96           N  
ANISOU 7008  N   ALA D  85     3152   3039   3672   -106    148   -230       N  
ATOM   7009  CA  ALA D  85      56.303   4.578 -11.366  1.00 30.62           C  
ANISOU 7009  CA  ALA D  85     3716   3618   4302   -117    151   -254       C  
ATOM   7010  C   ALA D  85      57.580   4.547 -10.527  1.00 24.61           C  
ANISOU 7010  C   ALA D  85     2939   2832   3579   -126    149   -257       C  
ATOM   7011  O   ALA D  85      57.928   5.535  -9.887  1.00 27.71           O  
ANISOU 7011  O   ALA D  85     3343   3219   3967   -125    150   -246       O  
ATOM   7012  CB  ALA D  85      56.639   4.602 -12.843  1.00 24.87           C  
ANISOU 7012  CB  ALA D  85     2994   2896   3561   -122    177   -275       C  
ATOM   7013  N   THR D  86      58.273   3.414 -10.531  1.00 22.96           N  
ANISOU 7013  N   THR D  86     2703   2610   3411   -134    145   -274       N  
ATOM   7014  CA  THR D  86      59.521   3.284  -9.785  1.00 23.00           C  
ANISOU 7014  CA  THR D  86     2690   2595   3455   -140    141   -280       C  
ATOM   7015  C   THR D  86      60.670   2.735 -10.629  1.00 24.85           C  
ANISOU 7015  C   THR D  86     2905   2815   3720   -153    160   -308       C  
ATOM   7016  O   THR D  86      61.833   2.967 -10.320  1.00 20.31           O  
ANISOU 7016  O   THR D  86     2320   2225   3171   -159    165   -318       O  
ATOM   7017  CB  THR D  86      59.362   2.397  -8.531  1.00 30.32           C  
ANISOU 7017  CB  THR D  86     3597   3516   4410   -134    113   -267       C  
ATOM   7018  OG1 THR D  86      59.214   1.027  -8.922  1.00 33.56           O  
ANISOU 7018  OG1 THR D  86     3986   3921   4845   -136    110   -279       O  
ATOM   7019  CG2 THR D  86      58.156   2.827  -7.712  1.00 35.68           C  
ANISOU 7019  CG2 THR D  86     4292   4208   5059   -122     95   -239       C  
ATOM   7020  N   LYS D  87      60.344   2.001 -11.687  1.00 19.97           N  
ANISOU 7020  N   LYS D  87     2283   2204   3101   -156    170   -324       N  
ATOM   7021  CA  LYS D  87      61.375   1.396 -12.523  1.00 30.15           C  
ANISOU 7021  CA  LYS D  87     3555   3481   4421   -169    189   -353       C  
ATOM   7022  C   LYS D  87      60.936   1.181 -13.971  1.00 27.02           C  
ANISOU 7022  C   LYS D  87     3166   3100   4002   -173    209   -371       C  
ATOM   7023  O   LYS D  87      59.746   1.144 -14.271  1.00 23.65           O  
ANISOU 7023  O   LYS D  87     2751   2693   3543   -165    203   -363       O  
ATOM   7024  CB  LYS D  87      61.857   0.081 -11.909  1.00 24.97           C  
ANISOU 7024  CB  LYS D  87     2865   2808   3815   -171    173   -360       C  
ATOM   7025  CG  LYS D  87      60.914  -1.080 -12.111  1.00 34.25           C  
ANISOU 7025  CG  LYS D  87     4028   3989   4995   -168    164   -362       C  
ATOM   7026  CD  LYS D  87      61.244  -2.208 -11.158  1.00 48.05           C  
ANISOU 7026  CD  LYS D  87     5748   5718   6790   -165    146   -358       C  
ATOM   7027  CE  LYS D  87      62.018  -1.695  -9.958  1.00 46.96           C  
ANISOU 7027  CE  LYS D  87     5607   5570   6666   -160    132   -342       C  
ATOM   7028  NZ  LYS D  87      63.473  -1.972 -10.082  1.00 53.17           N  
ANISOU 7028  NZ  LYS D  87     6372   6337   7494   -169    141   -363       N  
ATOM   7029  N   SER D  88      61.914   1.039 -14.860  1.00 20.67           N  
ANISOU 7029  N   SER D  88     2353   2285   3213   -185    232   -397       N  
ATOM   7030  CA  SER D  88      61.650   0.900 -16.280  1.00 25.68           C  
ANISOU 7030  CA  SER D  88     2996   2937   3826   -189    254   -416       C  
ATOM   7031  C   SER D  88      62.789   0.151 -16.971  1.00 29.41           C  
ANISOU 7031  C   SER D  88     3445   3393   4337   -205    272   -448       C  
ATOM   7032  O   SER D  88      63.964   0.337 -16.635  1.00 24.17           O  
ANISOU 7032  O   SER D  88     2771   2707   3705   -213    279   -455       O  
ATOM   7033  CB  SER D  88      61.471   2.287 -16.908  1.00 31.76           C  
ANISOU 7033  CB  SER D  88     3801   3720   4548   -184    274   -406       C  
ATOM   7034  OG  SER D  88      60.905   2.211 -18.205  1.00 34.44           O  
ANISOU 7034  OG  SER D  88     4151   4082   4852   -183    290   -418       O  
ATOM   7035  N   THR D  89      62.429  -0.705 -17.923  1.00 17.20           N  
ANISOU 7035  N   THR D  89     1888   1858   2790   -209    280   -470       N  
ATOM   7036  CA  THR D  89      63.405  -1.381 -18.766  1.00 15.95           C  
ANISOU 7036  CA  THR D  89     1710   1688   2663   -225    301   -503       C  
ATOM   7037  C   THR D  89      63.166  -0.929 -20.202  1.00 22.92           C  
ANISOU 7037  C   THR D  89     2613   2593   3503   -227    328   -517       C  
ATOM   7038  O   THR D  89      62.035  -0.941 -20.683  1.00 23.31           O  
ANISOU 7038  O   THR D  89     2674   2670   3513   -218    323   -514       O  
ATOM   7039  CB  THR D  89      63.257  -2.906 -18.684  1.00 21.51           C  
ANISOU 7039  CB  THR D  89     2381   2385   3408   -230    290   -520       C  
ATOM   7040  OG1 THR D  89      63.243  -3.311 -17.310  1.00 21.64           O  
ANISOU 7040  OG1 THR D  89     2383   2384   3457   -223    264   -500       O  
ATOM   7041  CG2 THR D  89      64.410  -3.620 -19.442  1.00 19.70           C  
ANISOU 7041  CG2 THR D  89     2128   2138   3219   -246    312   -555       C  
ATOM   7042  N   GLU D  90      64.232  -0.527 -20.883  1.00 21.27           N  
ANISOU 7042  N   GLU D  90     2407   2373   3300   -238    355   -534       N  
ATOM   7043  CA  GLU D  90      64.107   0.111 -22.185  1.00 24.57           C  
ANISOU 7043  CA  GLU D  90     2850   2812   3673   -238    383   -543       C  
ATOM   7044  C   GLU D  90      65.168  -0.422 -23.140  1.00 27.15           C  
ANISOU 7044  C   GLU D  90     3160   3128   4026   -256    411   -579       C  
ATOM   7045  O   GLU D  90      66.268  -0.791 -22.720  1.00 25.70           O  
ANISOU 7045  O   GLU D  90     2955   2915   3894   -268    414   -592       O  
ATOM   7046  CB  GLU D  90      64.179   1.639 -22.006  1.00 27.01           C  
ANISOU 7046  CB  GLU D  90     3194   3121   3948   -230    395   -517       C  
ATOM   7047  CG  GLU D  90      63.209   2.098 -20.869  1.00 30.38           C  
ANISOU 7047  CG  GLU D  90     3632   3554   4357   -214    365   -482       C  
ATOM   7048  CD  GLU D  90      63.249   3.599 -20.522  1.00 39.19           C  
ANISOU 7048  CD  GLU D  90     4779   4666   5443   -205    375   -456       C  
ATOM   7049  OE1 GLU D  90      64.211   4.302 -20.896  1.00 36.20           O  
ANISOU 7049  OE1 GLU D  90     4411   4274   5070   -214    404   -463       O  
ATOM   7050  OE2 GLU D  90      62.297   4.072 -19.855  1.00 41.46           O  
ANISOU 7050  OE2 GLU D  90     5081   4965   5705   -191    355   -429       O  
ATOM   7051  N   VAL D  91      64.818  -0.505 -24.416  1.00 15.03           N  
ANISOU 7051  N   VAL D  91     1635   1617   2457   -257    430   -596       N  
ATOM   7052  CA  VAL D  91      65.741  -0.990 -25.423  1.00 19.37           C  
ANISOU 7052  CA  VAL D  91     2172   2161   3028   -274    459   -631       C  
ATOM   7053  C   VAL D  91      65.964   0.105 -26.465  1.00 22.12           C  
ANISOU 7053  C   VAL D  91     2554   2522   3328   -272    492   -629       C  
ATOM   7054  O   VAL D  91      65.030   0.807 -26.867  1.00 19.01           O  
ANISOU 7054  O   VAL D  91     2190   2158   2877   -256    493   -610       O  
ATOM   7055  CB  VAL D  91      65.233  -2.305 -26.108  1.00 19.05           C  
ANISOU 7055  CB  VAL D  91     2106   2138   2995   -280    454   -661       C  
ATOM   7056  CG1 VAL D  91      63.928  -2.057 -26.879  1.00 19.72           C  
ANISOU 7056  CG1 VAL D  91     2211   2266   3015   -265    452   -656       C  
ATOM   7057  CG2 VAL D  91      66.292  -2.895 -27.029  1.00 19.79           C  
ANISOU 7057  CG2 VAL D  91     2181   2219   3118   -299    483   -700       C  
ATOM   7058  N   LEU D  92      67.216   0.243 -26.881  1.00 17.45           N  
ANISOU 7058  N   LEU D  92     1958   1909   2763   -287    522   -649       N  
ATOM   7059  CA  LEU D  92      67.605   1.213 -27.892  1.00 21.42           C  
ANISOU 7059  CA  LEU D  92     2492   2419   3228   -288    560   -649       C  
ATOM   7060  C   LEU D  92      67.267   0.660 -29.271  1.00 24.23           C  
ANISOU 7060  C   LEU D  92     2848   2805   3555   -290    576   -675       C  
ATOM   7061  O   LEU D  92      67.861  -0.307 -29.713  1.00 23.89           O  
ANISOU 7061  O   LEU D  92     2777   2754   3547   -307    585   -709       O  
ATOM   7062  CB  LEU D  92      69.106   1.476 -27.782  1.00 21.41           C  
ANISOU 7062  CB  LEU D  92     2482   2380   3273   -305    585   -664       C  
ATOM   7063  CG  LEU D  92      69.738   2.476 -28.747  1.00 27.79           C  
ANISOU 7063  CG  LEU D  92     3319   3186   4053   -309    631   -667       C  
ATOM   7064  CD1 LEU D  92      69.022   3.817 -28.674  1.00 23.01           C  
ANISOU 7064  CD1 LEU D  92     2756   2595   3393   -290    636   -629       C  
ATOM   7065  CD2 LEU D  92      71.229   2.622 -28.430  1.00 24.07           C  
ANISOU 7065  CD2 LEU D  92     2832   2675   3637   -329    651   -686       C  
ATOM   7066  N   GLU D  93      66.310   1.279 -29.947  1.00 23.78           N  
ANISOU 7066  N   GLU D  93     2822   2784   3431   -273    581   -658       N  
ATOM   7067  CA  GLU D  93      65.845   0.790 -31.232  1.00 30.76           C  
ANISOU 7067  CA  GLU D  93     3706   3703   4278   -272    592   -682       C  
ATOM   7068  C   GLU D  93      66.490   1.519 -32.401  1.00 34.31           C  
ANISOU 7068  C   GLU D  93     4182   4158   4695   -274    637   -688       C  
ATOM   7069  O   GLU D  93      66.708   0.941 -33.461  1.00 33.42           O  
ANISOU 7069  O   GLU D  93     4061   4063   4576   -283    655   -719       O  
ATOM   7070  CB  GLU D  93      64.325   0.903 -31.312  1.00 28.14           C  
ANISOU 7070  CB  GLU D  93     3388   3414   3892   -249    568   -663       C  
ATOM   7071  CG  GLU D  93      63.610  -0.112 -30.427  1.00 33.26           C  
ANISOU 7071  CG  GLU D  93     4004   4061   4571   -249    528   -667       C  
ATOM   7072  CD  GLU D  93      62.129  -0.217 -30.747  1.00 42.55           C  
ANISOU 7072  CD  GLU D  93     5189   5284   5696   -230    507   -661       C  
ATOM   7073  OE1 GLU D  93      61.510   0.839 -30.988  1.00 38.93           O  
ANISOU 7073  OE1 GLU D  93     4764   4847   5179   -210    510   -633       O  
ATOM   7074  OE2 GLU D  93      61.589  -1.352 -30.772  1.00 39.69           O  
ANISOU 7074  OE2 GLU D  93     4796   4934   5352   -235    489   -686       O  
ATOM   7075  N   ILE D  94      66.779   2.796 -32.206  1.00 24.82           N  
ANISOU 7075  N   ILE D  94     3012   2942   3474   -266    655   -658       N  
ATOM   7076  CA  ILE D  94      67.397   3.591 -33.252  1.00 31.16           C  
ANISOU 7076  CA  ILE D  94     3845   3747   4248   -267    701   -659       C  
ATOM   7077  C   ILE D  94      68.456   4.469 -32.623  1.00 30.17           C  
ANISOU 7077  C   ILE D  94     3729   3577   4156   -276    723   -647       C  
ATOM   7078  O   ILE D  94      68.186   5.167 -31.639  1.00 25.51           O  
ANISOU 7078  O   ILE D  94     3150   2974   3568   -266    707   -617       O  
ATOM   7079  CB  ILE D  94      66.374   4.494 -33.945  1.00 34.50           C  
ANISOU 7079  CB  ILE D  94     4309   4209   4590   -240    708   -630       C  
ATOM   7080  CG1 ILE D  94      65.330   3.658 -34.683  1.00 42.19           C  
ANISOU 7080  CG1 ILE D  94     5272   5232   5526   -230    689   -647       C  
ATOM   7081  CG2 ILE D  94      67.071   5.450 -34.914  1.00 35.44           C  
ANISOU 7081  CG2 ILE D  94     4462   4324   4679   -239    759   -624       C  
ATOM   7082  CD1 ILE D  94      64.205   4.486 -35.287  1.00 34.67           C  
ANISOU 7082  CD1 ILE D  94     4357   4323   4493   -199    689   -617       C  
ATOM   7083  N   LEU D  95      69.663   4.403 -33.170  1.00 25.97           N  
ANISOU 7083  N   LEU D  95     3191   3023   3653   -296    758   -673       N  
ATOM   7084  CA  LEU D  95      70.729   5.331 -32.822  1.00 32.22           C  
ANISOU 7084  CA  LEU D  95     3994   3775   4471   -306    789   -666       C  
ATOM   7085  C   LEU D  95      71.378   5.810 -34.118  1.00 35.39           C  
ANISOU 7085  C   LEU D  95     4421   4179   4849   -311    842   -678       C  
ATOM   7086  O   LEU D  95      72.296   5.171 -34.642  1.00 30.66           O  
ANISOU 7086  O   LEU D  95     3800   3566   4283   -333    862   -714       O  
ATOM   7087  CB  LEU D  95      71.764   4.664 -31.924  1.00 22.76           C  
ANISOU 7087  CB  LEU D  95     2756   2538   3352   -328    777   -691       C  
ATOM   7088  CG  LEU D  95      73.032   5.486 -31.678  1.00 31.86           C  
ANISOU 7088  CG  LEU D  95     3914   3650   4540   -342    811   -695       C  
ATOM   7089  CD1 LEU D  95      72.680   6.838 -31.109  1.00 26.53           C  
ANISOU 7089  CD1 LEU D  95     3272   2969   3839   -327    816   -656       C  
ATOM   7090  CD2 LEU D  95      73.984   4.754 -30.751  1.00 34.03           C  
ANISOU 7090  CD2 LEU D  95     4145   3892   4891   -361    793   -721       C  
ATOM   7091  N   ASP D  96      70.884   6.921 -34.652  1.00 25.74           N  
ANISOU 7091  N   ASP D  96     3242   2972   3566   -292    865   -646       N  
ATOM   7092  CA  ASP D  96      71.394   7.414 -35.928  1.00 33.95           C  
ANISOU 7092  CA  ASP D  96     4309   4017   4574   -294    918   -653       C  
ATOM   7093  C   ASP D  96      72.383   8.551 -35.716  1.00 35.02           C  
ANISOU 7093  C   ASP D  96     4465   4110   4731   -302    960   -642       C  
ATOM   7094  O   ASP D  96      71.985   9.703 -35.548  1.00 30.73           O  
ANISOU 7094  O   ASP D  96     3956   3564   4155   -284    973   -605       O  
ATOM   7095  CB  ASP D  96      70.262   7.876 -36.838  1.00 32.48           C  
ANISOU 7095  CB  ASP D  96     4160   3877   4304   -265    922   -626       C  
ATOM   7096  CG  ASP D  96      70.695   7.977 -38.293  1.00 46.96           C  
ANISOU 7096  CG  ASP D  96     6014   5726   6102   -267    970   -641       C  
ATOM   7097  OD1 ASP D  96      69.814   7.878 -39.179  1.00 49.45           O  
ANISOU 7097  OD1 ASP D  96     6346   6089   6354   -247    966   -634       O  
ATOM   7098  OD2 ASP D  96      71.917   8.135 -38.544  1.00 40.60           O  
ANISOU 7098  OD2 ASP D  96     5206   4887   5333   -289   1009   -660       O  
ATOM   7099  N   ASP D  97      73.671   8.214 -35.725  1.00 34.01           N  
ANISOU 7099  N   ASP D  97     4314   3948   4661   -329    983   -676       N  
ATOM   7100  CA  ASP D  97      74.728   9.184 -35.450  1.00 32.74           C  
ANISOU 7100  CA  ASP D  97     4164   3744   4533   -342   1024   -675       C  
ATOM   7101  C   ASP D  97      75.057  10.062 -36.651  1.00 42.49           C  
ANISOU 7101  C   ASP D  97     5440   4978   5726   -338   1085   -666       C  
ATOM   7102  O   ASP D  97      75.935  10.920 -36.566  1.00 41.32           O  
ANISOU 7102  O   ASP D  97     5304   4793   5601   -348   1126   -666       O  
ATOM   7103  CB  ASP D  97      75.996   8.488 -34.938  1.00 30.96           C  
ANISOU 7103  CB  ASP D  97     3895   3481   4388   -372   1023   -716       C  
ATOM   7104  CG  ASP D  97      76.001   8.325 -33.420  1.00 31.86           C  
ANISOU 7104  CG  ASP D  97     3980   3576   4550   -374    979   -712       C  
ATOM   7105  OD1 ASP D  97      75.774   9.328 -32.701  1.00 30.12           O  
ANISOU 7105  OD1 ASP D  97     3779   3344   4322   -363    978   -683       O  
ATOM   7106  OD2 ASP D  97      76.236   7.197 -32.938  1.00 27.19           O  
ANISOU 7106  OD2 ASP D  97     3346   2981   4002   -385    945   -738       O  
ATOM   7107  N   ASN D  98      74.353   9.850 -37.761  1.00 33.57           N  
ANISOU 7107  N   ASN D  98     4330   3889   4534   -322   1091   -660       N  
ATOM   7108  CA  ASN D  98      74.559  10.658 -38.951  1.00 37.55           C  
ANISOU 7108  CA  ASN D  98     4877   4399   4990   -315   1148   -648       C  
ATOM   7109  C   ASN D  98      73.470  11.710 -39.078  1.00 40.90           C  
ANISOU 7109  C   ASN D  98     5347   4848   5346   -280   1151   -596       C  
ATOM   7110  O   ASN D  98      73.751  12.860 -39.401  1.00 44.75           O  
ANISOU 7110  O   ASN D  98     5872   5317   5813   -272   1198   -572       O  
ATOM   7111  CB  ASN D  98      74.642   9.780 -40.208  1.00 38.57           C  
ANISOU 7111  CB  ASN D  98     5000   4560   5095   -321   1161   -678       C  
ATOM   7112  CG  ASN D  98      75.815   8.802 -40.162  1.00 39.52           C  
ANISOU 7112  CG  ASN D  98     5077   4653   5286   -356   1166   -730       C  
ATOM   7113  OD1 ASN D  98      76.959   9.193 -39.920  1.00 35.90           O  
ANISOU 7113  OD1 ASN D  98     4613   4150   4878   -376   1200   -745       O  
ATOM   7114  ND2 ASN D  98      75.531   7.521 -40.376  1.00 40.21           N  
ANISOU 7114  ND2 ASN D  98     5131   4766   5381   -363   1134   -760       N  
ATOM   7115  N   GLU D  99      72.229  11.320 -38.796  1.00 44.20           N  
ANISOU 7115  N   GLU D  99     5760   5304   5729   -259   1100   -580       N  
ATOM   7116  CA  GLU D  99      71.093  12.237 -38.903  1.00 40.31           C  
ANISOU 7116  CA  GLU D  99     5308   4838   5170   -224   1097   -531       C  
ATOM   7117  C   GLU D  99      70.568  12.734 -37.546  1.00 33.61           C  
ANISOU 7117  C   GLU D  99     4456   3974   4341   -215   1062   -504       C  
ATOM   7118  O   GLU D  99      69.631  13.519 -37.500  1.00 30.82           O  
ANISOU 7118  O   GLU D  99     4134   3638   3939   -186   1057   -463       O  
ATOM   7119  CB  GLU D  99      69.942  11.587 -39.686  1.00 48.53           C  
ANISOU 7119  CB  GLU D  99     6352   5941   6148   -202   1068   -530       C  
ATOM   7120  CG  GLU D  99      70.366  10.705 -40.866  1.00 53.78           C  
ANISOU 7120  CG  GLU D  99     7005   6628   6801   -215   1086   -569       C  
ATOM   7121  CD  GLU D  99      71.231  11.438 -41.888  1.00 71.49           C  
ANISOU 7121  CD  GLU D  99     9282   8857   9027   -218   1153   -566       C  
ATOM   7122  OE1 GLU D  99      72.093  10.778 -42.516  1.00 75.86           O  
ANISOU 7122  OE1 GLU D  99     9817   9404   9604   -242   1176   -606       O  
ATOM   7123  OE2 GLU D  99      71.047  12.665 -42.072  1.00 72.84           O  
ANISOU 7123  OE2 GLU D  99     9496   9021   9159   -196   1185   -525       O  
ATOM   7124  N   HIS D 100      71.160  12.258 -36.456  1.00 31.79           N  
ANISOU 7124  N   HIS D 100     4188   3711   4180   -238   1038   -526       N  
ATOM   7125  CA  HIS D 100      70.792  12.708 -35.113  1.00 32.42           C  
ANISOU 7125  CA  HIS D 100     4262   3773   4283   -233   1007   -504       C  
ATOM   7126  C   HIS D 100      69.375  12.313 -34.689  1.00 32.06           C  
ANISOU 7126  C   HIS D 100     4212   3767   4203   -211    952   -484       C  
ATOM   7127  O   HIS D 100      68.530  13.170 -34.438  1.00 27.08           O  
ANISOU 7127  O   HIS D 100     3609   3146   3534   -186    947   -445       O  
ATOM   7128  CB  HIS D 100      70.973  14.222 -34.997  1.00 27.23           C  
ANISOU 7128  CB  HIS D 100     3644   3089   3613   -223   1049   -470       C  
ATOM   7129  CG  HIS D 100      72.315  14.701 -35.454  1.00 34.83           C  
ANISOU 7129  CG  HIS D 100     4614   4013   4608   -244   1109   -489       C  
ATOM   7130  ND1 HIS D 100      72.509  15.326 -36.665  1.00 33.62           N  
ANISOU 7130  ND1 HIS D 100     4499   3863   4413   -235   1164   -477       N  
ATOM   7131  CD2 HIS D 100      73.531  14.637 -34.864  1.00 35.27           C  
ANISOU 7131  CD2 HIS D 100     4642   4024   4733   -274   1123   -519       C  
ATOM   7132  CE1 HIS D 100      73.786  15.633 -36.799  1.00 40.39           C  
ANISOU 7132  CE1 HIS D 100     5353   4679   5314   -260   1211   -500       C  
ATOM   7133  NE2 HIS D 100      74.429  15.225 -35.721  1.00 42.42           N  
ANISOU 7133  NE2 HIS D 100     5570   4908   5641   -284   1186   -527       N  
ATOM   7134  N   ILE D 101      69.135  11.009 -34.599  1.00 30.76           N  
ANISOU 7134  N   ILE D 101     4010   3621   4054   -219    913   -512       N  
ATOM   7135  CA  ILE D 101      67.837  10.468 -34.211  1.00 28.27           C  
ANISOU 7135  CA  ILE D 101     3685   3342   3713   -202    860   -501       C  
ATOM   7136  C   ILE D 101      68.009   9.323 -33.225  1.00 28.11           C  
ANISOU 7136  C   ILE D 101     3618   3310   3754   -221    817   -527       C  
ATOM   7137  O   ILE D 101      68.778   8.399 -33.467  1.00 25.58           O  
ANISOU 7137  O   ILE D 101     3268   2980   3473   -243    821   -565       O  
ATOM   7138  CB  ILE D 101      67.078   9.945 -35.424  1.00 31.54           C  
ANISOU 7138  CB  ILE D 101     4107   3807   4069   -187    858   -507       C  
ATOM   7139  CG1 ILE D 101      66.869  11.070 -36.440  1.00 41.00           C  
ANISOU 7139  CG1 ILE D 101     5355   5021   5202   -164    901   -478       C  
ATOM   7140  CG2 ILE D 101      65.742   9.332 -34.993  1.00 30.75           C  
ANISOU 7140  CG2 ILE D 101     3993   3744   3948   -170    804   -500       C  
ATOM   7141  CD1 ILE D 101      66.319  10.601 -37.755  1.00 42.30           C  
ANISOU 7141  CD1 ILE D 101     5528   5236   5308   -150    905   -488       C  
ATOM   7142  N   LEU D 102      67.287   9.396 -32.113  1.00 30.11           N  
ANISOU 7142  N   LEU D 102     3864   3564   4014   -211    778   -507       N  
ATOM   7143  CA  LEU D 102      67.344   8.382 -31.063  1.00 33.93           C  
ANISOU 7143  CA  LEU D 102     4306   4036   4551   -225    735   -525       C  
ATOM   7144  C   LEU D 102      65.963   7.754 -30.871  1.00 29.71           C  
ANISOU 7144  C   LEU D 102     3763   3539   3987   -207    690   -515       C  
ATOM   7145  O   LEU D 102      64.981   8.461 -30.681  1.00 30.45           O  
ANISOU 7145  O   LEU D 102     3881   3651   4038   -185    679   -482       O  
ATOM   7146  CB  LEU D 102      67.804   9.020 -29.756  1.00 24.91           C  
ANISOU 7146  CB  LEU D 102     3159   2856   3450   -230    728   -510       C  
ATOM   7147  CG  LEU D 102      67.987   8.085 -28.568  1.00 31.15           C  
ANISOU 7147  CG  LEU D 102     3908   3631   4297   -243    687   -525       C  
ATOM   7148  CD1 LEU D 102      69.248   7.275 -28.758  1.00 31.53           C  
ANISOU 7148  CD1 LEU D 102     3924   3655   4400   -269    701   -565       C  
ATOM   7149  CD2 LEU D 102      68.056   8.876 -27.276  1.00 30.10           C  
ANISOU 7149  CD2 LEU D 102     3778   3474   4185   -240    675   -503       C  
ATOM   7150  N   GLY D 103      65.883   6.427 -30.936  1.00 28.89           N  
ANISOU 7150  N   GLY D 103     3624   3446   3908   -219    667   -546       N  
ATOM   7151  CA  GLY D 103      64.603   5.743 -30.823  1.00 27.78           C  
ANISOU 7151  CA  GLY D 103     3472   3340   3742   -205    628   -543       C  
ATOM   7152  C   GLY D 103      64.630   4.687 -29.733  1.00 30.52           C  
ANISOU 7152  C   GLY D 103     3779   3670   4147   -217    590   -557       C  
ATOM   7153  O   GLY D 103      65.490   3.798 -29.731  1.00 25.23           O  
ANISOU 7153  O   GLY D 103     3079   2981   3528   -238    594   -589       O  
ATOM   7154  N   ILE D 104      63.692   4.785 -28.796  1.00 31.75           N  
ANISOU 7154  N   ILE D 104     3934   3832   4295   -204    556   -533       N  
ATOM   7155  CA  ILE D 104      63.629   3.852 -27.663  1.00 28.38           C  
ANISOU 7155  CA  ILE D 104     3473   3390   3920   -212    520   -540       C  
ATOM   7156  C   ILE D 104      62.280   3.147 -27.554  1.00 27.47           C  
ANISOU 7156  C   ILE D 104     3347   3307   3784   -200    486   -538       C  
ATOM   7157  O   ILE D 104      61.269   3.672 -28.022  1.00 29.97           O  
ANISOU 7157  O   ILE D 104     3687   3656   4044   -180    484   -522       O  
ATOM   7158  CB  ILE D 104      63.925   4.576 -26.335  1.00 26.81           C  
ANISOU 7158  CB  ILE D 104     3280   3162   3747   -211    509   -514       C  
ATOM   7159  CG1 ILE D 104      65.425   4.603 -26.080  1.00 33.96           C  
ANISOU 7159  CG1 ILE D 104     4171   4028   4705   -232    530   -531       C  
ATOM   7160  CG2 ILE D 104      63.218   3.912 -25.173  1.00 41.91           C  
ANISOU 7160  CG2 ILE D 104     5169   5073   5681   -207    467   -505       C  
ATOM   7161  CD1 ILE D 104      66.030   5.942 -26.239  1.00 30.70           C  
ANISOU 7161  CD1 ILE D 104     3788   3599   4278   -231    563   -516       C  
ATOM   7162  N   ARG D 105      62.282   1.957 -26.946  1.00 25.21           N  
ANISOU 7162  N   ARG D 105     3025   3010   3545   -211    462   -556       N  
ATOM   7163  CA  ARG D 105      61.054   1.234 -26.615  1.00 28.92           C  
ANISOU 7163  CA  ARG D 105     3480   3502   4006   -202    430   -555       C  
ATOM   7164  C   ARG D 105      61.105   0.738 -25.170  1.00 20.30           C  
ANISOU 7164  C   ARG D 105     2366   2383   2965   -206    401   -545       C  
ATOM   7165  O   ARG D 105      62.113   0.199 -24.722  1.00 20.58           O  
ANISOU 7165  O   ARG D 105     2379   2387   3055   -222    403   -559       O  
ATOM   7166  CB  ARG D 105      60.831   0.054 -27.573  1.00 27.24           C  
ANISOU 7166  CB  ARG D 105     3243   3312   3797   -210    432   -594       C  
ATOM   7167  CG  ARG D 105      59.654  -0.841 -27.184  1.00 32.55           C  
ANISOU 7167  CG  ARG D 105     3894   4002   4471   -204    401   -600       C  
ATOM   7168  CD  ARG D 105      59.375  -1.940 -28.224  1.00 36.92           C  
ANISOU 7168  CD  ARG D 105     4424   4581   5024   -213    407   -642       C  
ATOM   7169  NE  ARG D 105      58.919  -1.362 -29.484  1.00 45.05           N  
ANISOU 7169  NE  ARG D 105     5476   5652   5988   -201    423   -647       N  
ATOM   7170  CZ  ARG D 105      57.643  -1.114 -29.771  1.00 53.03           C  
ANISOU 7170  CZ  ARG D 105     6499   6704   6947   -181    408   -638       C  
ATOM   7171  NH1 ARG D 105      56.700  -1.416 -28.886  1.00 44.81           N  
ANISOU 7171  NH1 ARG D 105     5447   5665   5915   -174    377   -627       N  
ATOM   7172  NH2 ARG D 105      57.308  -0.572 -30.941  1.00 47.30           N  
ANISOU 7172  NH2 ARG D 105     5795   6018   6160   -168    423   -642       N  
ATOM   7173  N   ILE D 106      60.018   0.930 -24.433  1.00 23.14           N  
ANISOU 7173  N   ILE D 106     2732   2754   3305   -191    374   -520       N  
ATOM   7174  CA  ILE D 106      59.942   0.433 -23.061  1.00 18.78           C  
ANISOU 7174  CA  ILE D 106     2160   2179   2796   -193    346   -509       C  
ATOM   7175  C   ILE D 106      59.489  -1.017 -23.099  1.00 21.22           C  
ANISOU 7175  C   ILE D 106     2436   2494   3134   -200    332   -533       C  
ATOM   7176  O   ILE D 106      58.486  -1.325 -23.731  1.00 24.22           O  
ANISOU 7176  O   ILE D 106     2815   2905   3482   -193    327   -543       O  
ATOM   7177  CB  ILE D 106      58.953   1.266 -22.217  1.00 21.90           C  
ANISOU 7177  CB  ILE D 106     2577   2584   3159   -175    325   -472       C  
ATOM   7178  CG1 ILE D 106      59.478   2.693 -22.033  1.00 23.83           C  
ANISOU 7178  CG1 ILE D 106     2852   2817   3384   -170    341   -447       C  
ATOM   7179  CG2 ILE D 106      58.714   0.615 -20.870  1.00 19.53           C  
ANISOU 7179  CG2 ILE D 106     2256   2267   2899   -176    296   -461       C  
ATOM   7180  CD1 ILE D 106      58.571   3.566 -21.199  1.00 26.49           C  
ANISOU 7180  CD1 ILE D 106     3210   3161   3692   -153    323   -412       C  
ATOM   7181  N   VAL D 107      60.236  -1.906 -22.446  1.00 26.02           N  
ANISOU 7181  N   VAL D 107     3014   3070   3801   -213    326   -545       N  
ATOM   7182  CA  VAL D 107      59.938  -3.341 -22.479  1.00 24.99           C  
ANISOU 7182  CA  VAL D 107     2850   2939   3707   -221    317   -569       C  
ATOM   7183  C   VAL D 107      59.800  -3.967 -21.093  1.00 23.50           C  
ANISOU 7183  C   VAL D 107     2642   2725   3561   -219    292   -553       C  
ATOM   7184  O   VAL D 107      59.881  -5.187 -20.948  1.00 20.08           O  
ANISOU 7184  O   VAL D 107     2179   2279   3173   -227    288   -571       O  
ATOM   7185  CB  VAL D 107      61.021  -4.135 -23.261  1.00 21.17           C  
ANISOU 7185  CB  VAL D 107     2342   2440   3261   -239    340   -607       C  
ATOM   7186  CG1 VAL D 107      61.085  -3.666 -24.723  1.00 22.39           C  
ANISOU 7186  CG1 VAL D 107     2515   2622   3372   -242    366   -626       C  
ATOM   7187  CG2 VAL D 107      62.372  -3.990 -22.583  1.00 17.57           C  
ANISOU 7187  CG2 VAL D 107     1879   1946   2850   -248    345   -601       C  
ATOM   7188  N   GLY D 108      59.574  -3.148 -20.071  1.00 20.19           N  
ANISOU 7188  N   GLY D 108     2241   2301   3129   -207    275   -518       N  
ATOM   7189  CA  GLY D 108      59.368  -3.694 -18.738  1.00 24.46           C  
ANISOU 7189  CA  GLY D 108     2766   2822   3704   -203    251   -500       C  
ATOM   7190  C   GLY D 108      59.345  -2.583 -17.708  1.00 28.91           C  
ANISOU 7190  C   GLY D 108     3353   3381   4251   -192    237   -464       C  
ATOM   7191  O   GLY D 108      59.620  -1.437 -18.053  1.00 23.09           O  
ANISOU 7191  O   GLY D 108     2641   2651   3481   -190    250   -455       O  
ATOM   7192  N   GLY D 109      59.026  -2.916 -16.458  1.00 21.99           N  
ANISOU 7192  N   GLY D 109     2467   2492   3395   -186    214   -443       N  
ATOM   7193  CA  GLY D 109      58.908  -1.911 -15.405  1.00 25.02           C  
ANISOU 7193  CA  GLY D 109     2872   2874   3763   -175    199   -410       C  
ATOM   7194  C   GLY D 109      57.504  -1.849 -14.823  1.00 26.86           C  
ANISOU 7194  C   GLY D 109     3114   3123   3969   -162    179   -388       C  
ATOM   7195  O   GLY D 109      56.633  -2.603 -15.244  1.00 27.26           O  
ANISOU 7195  O   GLY D 109     3155   3187   4016   -162    177   -400       O  
ATOM   7196  N   ASP D 110      57.302  -0.986 -13.833  1.00 30.03           N  
ANISOU 7196  N   ASP D 110     3532   3523   4355   -153    165   -359       N  
ATOM   7197  CA  ASP D 110      56.040  -0.935 -13.100  1.00 28.64           C  
ANISOU 7197  CA  ASP D 110     3364   3358   4158   -141    145   -336       C  
ATOM   7198  C   ASP D 110      55.198   0.295 -13.427  1.00 38.52           C  
ANISOU 7198  C   ASP D 110     4647   4635   5354   -131    147   -322       C  
ATOM   7199  O   ASP D 110      54.339   0.694 -12.647  1.00 34.65           O  
ANISOU 7199  O   ASP D 110     4168   4152   4845   -121    131   -299       O  
ATOM   7200  CB  ASP D 110      56.294  -1.006 -11.594  1.00 30.52           C  
ANISOU 7200  CB  ASP D 110     3596   3577   4422   -137    125   -313       C  
ATOM   7201  CG  ASP D 110      57.078   0.186 -11.080  1.00 31.61           C  
ANISOU 7201  CG  ASP D 110     3750   3710   4552   -136    127   -299       C  
ATOM   7202  OD1 ASP D 110      57.326   0.252  -9.861  1.00 39.06           O  
ANISOU 7202  OD1 ASP D 110     4689   4641   5511   -131    110   -280       O  
ATOM   7203  OD2 ASP D 110      57.447   1.053 -11.892  1.00 22.33           O  
ANISOU 7203  OD2 ASP D 110     2591   2540   3353   -139    145   -306       O  
ATOM   7204  N   HIS D 111      55.450   0.896 -14.581  1.00 30.91           N  
ANISOU 7204  N   HIS D 111     3697   3683   4363   -133    168   -334       N  
ATOM   7205  CA  HIS D 111      54.645   2.011 -15.041  1.00 36.13           C  
ANISOU 7205  CA  HIS D 111     4389   4369   4971   -121    172   -320       C  
ATOM   7206  C   HIS D 111      53.420   1.439 -15.738  1.00 38.02           C  
ANISOU 7206  C   HIS D 111     4624   4636   5186   -114    167   -332       C  
ATOM   7207  O   HIS D 111      53.287   0.228 -15.864  1.00 33.58           O  
ANISOU 7207  O   HIS D 111     4035   4071   4651   -122    163   -352       O  
ATOM   7208  CB  HIS D 111      55.443   2.865 -16.015  1.00 35.54           C  
ANISOU 7208  CB  HIS D 111     4332   4296   4877   -124    200   -328       C  
ATOM   7209  CG  HIS D 111      56.272   2.062 -16.963  1.00 43.63           C  
ANISOU 7209  CG  HIS D 111     5338   5314   5924   -137    217   -360       C  
ATOM   7210  ND1 HIS D 111      55.773   1.566 -18.146  1.00 45.16           N  
ANISOU 7210  ND1 HIS D 111     5528   5533   6098   -137    226   -381       N  
ATOM   7211  CD2 HIS D 111      57.556   1.644 -16.889  1.00 42.93           C  
ANISOU 7211  CD2 HIS D 111     5232   5201   5879   -151    227   -375       C  
ATOM   7212  CE1 HIS D 111      56.720   0.888 -18.769  1.00 37.60           C  
ANISOU 7212  CE1 HIS D 111     4552   4563   5170   -151    242   -409       C  
ATOM   7213  NE2 HIS D 111      57.811   0.920 -18.026  1.00 48.84           N  
ANISOU 7213  NE2 HIS D 111     5967   5956   6633   -160    243   -405       N  
ATOM   7214  N   ARG D 112      52.526   2.305 -16.191  1.00 34.68           N  
ANISOU 7214  N   ARG D 112     4225   4240   4713   -101    168   -321       N  
ATOM   7215  CA  ARG D 112      51.333   1.841 -16.882  1.00 43.08           C  
ANISOU 7215  CA  ARG D 112     5284   5334   5750    -93    162   -334       C  
ATOM   7216  C   ARG D 112      51.397   2.181 -18.365  1.00 41.52           C  
ANISOU 7216  C   ARG D 112     5098   5162   5515    -89    182   -351       C  
ATOM   7217  O   ARG D 112      50.375   2.398 -19.008  1.00 46.54           O  
ANISOU 7217  O   ARG D 112     5742   5830   6109    -76    179   -353       O  
ATOM   7218  CB  ARG D 112      50.076   2.426 -16.239  1.00 38.71           C  
ANISOU 7218  CB  ARG D 112     4745   4796   5166    -77    143   -309       C  
ATOM   7219  CG  ARG D 112      49.699   1.768 -14.917  1.00 44.31           C  
ANISOU 7219  CG  ARG D 112     5438   5488   5909    -80    122   -299       C  
ATOM   7220  CD  ARG D 112      48.265   2.085 -14.518  1.00 41.70           C  
ANISOU 7220  CD  ARG D 112     5117   5178   5549    -66    105   -284       C  
ATOM   7221  NE  ARG D 112      47.925   3.477 -14.781  1.00 34.56           N  
ANISOU 7221  NE  ARG D 112     4243   4290   4597    -51    110   -263       N  
ATOM   7222  CZ  ARG D 112      46.738   3.888 -15.210  1.00 41.31           C  
ANISOU 7222  CZ  ARG D 112     5110   5175   5410    -36    104   -260       C  
ATOM   7223  NH1 ARG D 112      45.768   3.014 -15.424  1.00 42.55           N  
ANISOU 7223  NH1 ARG D 112     5248   5351   5568    -34     92   -278       N  
ATOM   7224  NH2 ARG D 112      46.522   5.175 -15.428  1.00 42.21           N  
ANISOU 7224  NH2 ARG D 112     5252   5300   5483    -21    110   -238       N  
ATOM   7225  N   LEU D 113      52.609   2.223 -18.905  1.00 39.05           N  
ANISOU 7225  N   LEU D 113     4785   4835   5218   -101    203   -363       N  
ATOM   7226  CA  LEU D 113      52.785   2.543 -20.310  1.00 35.51           C  
ANISOU 7226  CA  LEU D 113     4348   4408   4735    -98    225   -379       C  
ATOM   7227  C   LEU D 113      53.199   1.285 -21.071  1.00 34.81           C  
ANISOU 7227  C   LEU D 113     4231   4321   4674   -113    233   -418       C  
ATOM   7228  O   LEU D 113      54.387   0.978 -21.168  1.00 46.73           O  
ANISOU 7228  O   LEU D 113     5730   5807   6219   -128    248   -431       O  
ATOM   7229  CB  LEU D 113      53.848   3.638 -20.464  1.00 37.87           C  
ANISOU 7229  CB  LEU D 113     4672   4690   5028    -99    249   -365       C  
ATOM   7230  CG  LEU D 113      53.673   4.932 -19.660  1.00 43.21           C  
ANISOU 7230  CG  LEU D 113     5376   5358   5685    -88    246   -328       C  
ATOM   7231  CD1 LEU D 113      54.939   5.787 -19.727  1.00 33.63           C  
ANISOU 7231  CD1 LEU D 113     4177   4120   4481    -95    273   -322       C  
ATOM   7232  CD2 LEU D 113      52.444   5.740 -20.117  1.00 29.71           C  
ANISOU 7232  CD2 LEU D 113     3691   3682   3916    -65    243   -310       C  
ATOM   7233  N   LYS D 114      52.224   0.548 -21.598  1.00 30.27           N  
ANISOU 7233  N   LYS D 114     3641   3775   4085   -109    224   -438       N  
ATOM   7234  CA  LYS D 114      52.515  -0.660 -22.372  1.00 32.59           C  
ANISOU 7234  CA  LYS D 114     3906   4073   4404   -124    233   -479       C  
ATOM   7235  C   LYS D 114      52.765  -0.317 -23.836  1.00 26.46           C  
ANISOU 7235  C   LYS D 114     3142   3324   3588   -121    256   -498       C  
ATOM   7236  O   LYS D 114      52.099   0.556 -24.403  1.00 32.89           O  
ANISOU 7236  O   LYS D 114     3981   4170   4346   -103    257   -485       O  
ATOM   7237  CB  LYS D 114      51.361  -1.668 -22.301  1.00 38.59           C  
ANISOU 7237  CB  LYS D 114     4640   4851   5171   -123    215   -498       C  
ATOM   7238  CG  LYS D 114      50.775  -1.898 -20.919  1.00 42.45           C  
ANISOU 7238  CG  LYS D 114     5123   5322   5686   -120    192   -477       C  
ATOM   7239  CD  LYS D 114      51.538  -2.960 -20.143  1.00 44.40           C  
ANISOU 7239  CD  LYS D 114     5342   5529   6000   -138    191   -484       C  
ATOM   7240  CE  LYS D 114      52.533  -2.333 -19.176  1.00 44.98           C  
ANISOU 7240  CE  LYS D 114     5428   5568   6095   -139    191   -454       C  
ATOM   7241  NZ  LYS D 114      53.149  -3.360 -18.288  1.00 47.77           N  
ANISOU 7241  NZ  LYS D 114     5754   5885   6510   -151    186   -457       N  
ATOM   7242  N   ASN D 115      53.714  -1.024 -24.448  1.00 28.35           N  
ANISOU 7242  N   ASN D 115     3363   3552   3857   -139    274   -528       N  
ATOM   7243  CA  ASN D 115      54.021  -0.834 -25.861  1.00 33.34           C  
ANISOU 7243  CA  ASN D 115     4003   4209   4454   -139    297   -549       C  
ATOM   7244  C   ASN D 115      54.376   0.601 -26.204  1.00 30.73           C  
ANISOU 7244  C   ASN D 115     3712   3883   4080   -126    314   -520       C  
ATOM   7245  O   ASN D 115      54.028   1.121 -27.268  1.00 34.24           O  
ANISOU 7245  O   ASN D 115     4176   4362   4471   -112    327   -523       O  
ATOM   7246  CB  ASN D 115      52.860  -1.331 -26.710  1.00 36.10           C  
ANISOU 7246  CB  ASN D 115     4343   4606   4769   -130    289   -574       C  
ATOM   7247  CG  ASN D 115      52.956  -2.807 -26.987  1.00 46.67           C  
ANISOU 7247  CG  ASN D 115     5640   5941   6150   -149    290   -618       C  
ATOM   7248  OD1 ASN D 115      53.328  -3.214 -28.085  1.00 66.11           O  
ANISOU 7248  OD1 ASN D 115     8093   8420   8605   -157    308   -651       O  
ATOM   7249  ND2 ASN D 115      52.658  -3.623 -25.983  1.00 43.42           N  
ANISOU 7249  ND2 ASN D 115     5205   5507   5787   -156    273   -619       N  
ATOM   7250  N   TYR D 116      55.065   1.241 -25.270  1.00 24.13           N  
ANISOU 7250  N   TYR D 116     2888   3011   3268   -129    316   -493       N  
ATOM   7251  CA  TYR D 116      55.508   2.604 -25.450  1.00 23.17           C  
ANISOU 7251  CA  TYR D 116     2803   2885   3115   -119    336   -466       C  
ATOM   7252  C   TYR D 116      56.740   2.600 -26.326  1.00 29.50           C  
ANISOU 7252  C   TYR D 116     3606   3675   3926   -133    368   -486       C  
ATOM   7253  O   TYR D 116      57.682   1.850 -26.071  1.00 25.26           O  
ANISOU 7253  O   TYR D 116     3045   3110   3444   -153    373   -506       O  
ATOM   7254  CB  TYR D 116      55.855   3.223 -24.092  1.00 21.89           C  
ANISOU 7254  CB  TYR D 116     2649   2688   2980   -120    326   -435       C  
ATOM   7255  CG  TYR D 116      56.315   4.661 -24.149  1.00 22.04           C  
ANISOU 7255  CG  TYR D 116     2703   2697   2973   -112    348   -408       C  
ATOM   7256  CD1 TYR D 116      55.423   5.695 -23.910  1.00 23.36           C  
ANISOU 7256  CD1 TYR D 116     2899   2880   3097    -90    341   -375       C  
ATOM   7257  CD2 TYR D 116      57.642   4.990 -24.438  1.00 23.56           C  
ANISOU 7257  CD2 TYR D 116     2901   2864   3187   -125    377   -415       C  
ATOM   7258  CE1 TYR D 116      55.820   7.014 -23.955  1.00 27.15           C  
ANISOU 7258  CE1 TYR D 116     3411   3349   3557    -82    364   -350       C  
ATOM   7259  CE2 TYR D 116      58.056   6.328 -24.489  1.00 24.70           C  
ANISOU 7259  CE2 TYR D 116     3078   2998   3310   -118    401   -391       C  
ATOM   7260  CZ  TYR D 116      57.129   7.333 -24.237  1.00 27.33           C  
ANISOU 7260  CZ  TYR D 116     3439   3345   3601    -97    394   -358       C  
ATOM   7261  OH  TYR D 116      57.475   8.661 -24.261  1.00 29.29           O  
ANISOU 7261  OH  TYR D 116     3719   3581   3830    -89    419   -333       O  
ATOM   7262  N   SER D 117      56.737   3.436 -27.357  1.00 28.75           N  
ANISOU 7262  N   SER D 117     3540   3602   3781   -121    392   -480       N  
ATOM   7263  CA  SER D 117      57.961   3.705 -28.101  1.00 27.91           C  
ANISOU 7263  CA  SER D 117     3442   3481   3681   -133    427   -492       C  
ATOM   7264  C   SER D 117      57.998   5.175 -28.471  1.00 34.33           C  
ANISOU 7264  C   SER D 117     4298   4298   4447   -116    451   -460       C  
ATOM   7265  O   SER D 117      56.955   5.790 -28.722  1.00 32.50           O  
ANISOU 7265  O   SER D 117     4088   4097   4162    -92    443   -438       O  
ATOM   7266  CB  SER D 117      58.089   2.803 -29.332  1.00 30.69           C  
ANISOU 7266  CB  SER D 117     3777   3857   4026   -142    440   -532       C  
ATOM   7267  OG  SER D 117      57.075   3.076 -30.275  1.00 34.20           O  
ANISOU 7267  OG  SER D 117     4238   4351   4406   -121    439   -530       O  
ATOM   7268  N   SER D 118      59.194   5.752 -28.444  1.00 30.08           N  
ANISOU 7268  N   SER D 118     3771   3727   3931   -127    480   -456       N  
ATOM   7269  CA  SER D 118      59.366   7.157 -28.787  1.00 34.36           C  
ANISOU 7269  CA  SER D 118     4354   4267   4436   -113    509   -427       C  
ATOM   7270  C   SER D 118      60.566   7.377 -29.700  1.00 34.62           C  
ANISOU 7270  C   SER D 118     4396   4285   4474   -126    552   -443       C  
ATOM   7271  O   SER D 118      61.435   6.510 -29.833  1.00 35.07           O  
ANISOU 7271  O   SER D 118     4425   4325   4573   -149    558   -475       O  
ATOM   7272  CB  SER D 118      59.483   8.033 -27.537  1.00 27.18           C  
ANISOU 7272  CB  SER D 118     3456   3326   3547   -112    502   -396       C  
ATOM   7273  OG  SER D 118      60.537   7.597 -26.702  1.00 28.67           O  
ANISOU 7273  OG  SER D 118     3619   3475   3800   -135    500   -411       O  
ATOM   7274  N   THR D 119      60.589   8.553 -30.316  1.00 29.53           N  
ANISOU 7274  N   THR D 119     3789   3645   3785   -111    583   -418       N  
ATOM   7275  CA  THR D 119      61.622   8.957 -31.248  1.00 31.57           C  
ANISOU 7275  CA  THR D 119     4064   3892   4039   -119    629   -427       C  
ATOM   7276  C   THR D 119      61.945  10.414 -30.994  1.00 31.15           C  
ANISOU 7276  C   THR D 119     4047   3813   3975   -110    658   -393       C  
ATOM   7277  O   THR D 119      61.045  11.251 -30.954  1.00 33.31           O  
ANISOU 7277  O   THR D 119     4348   4104   4204    -85    654   -359       O  
ATOM   7278  CB  THR D 119      61.103   8.875 -32.696  1.00 37.59           C  
ANISOU 7278  CB  THR D 119     4843   4700   4740   -103    643   -434       C  
ATOM   7279  OG1 THR D 119      60.863   7.508 -33.046  1.00 40.91           O  
ANISOU 7279  OG1 THR D 119     5229   5144   5172   -113    621   -472       O  
ATOM   7280  CG2 THR D 119      62.110   9.485 -33.665  1.00 36.19           C  
ANISOU 7280  CG2 THR D 119     4690   4510   4551   -108    696   -436       C  
ATOM   7281  N   ILE D 120      63.220  10.734 -30.818  1.00 29.19           N  
ANISOU 7281  N   ILE D 120     3798   3525   3770   -130    689   -402       N  
ATOM   7282  CA  ILE D 120      63.607  12.131 -30.818  1.00 30.51           C  
ANISOU 7282  CA  ILE D 120     4000   3668   3924   -123    727   -374       C  
ATOM   7283  C   ILE D 120      64.523  12.382 -32.006  1.00 30.35           C  
ANISOU 7283  C   ILE D 120     3997   3641   3893   -130    778   -387       C  
ATOM   7284  O   ILE D 120      65.412  11.582 -32.282  1.00 33.29           O  
ANISOU 7284  O   ILE D 120     4344   4001   4302   -154    786   -422       O  
ATOM   7285  CB  ILE D 120      64.268  12.577 -29.484  1.00 28.93           C  
ANISOU 7285  CB  ILE D 120     3789   3422   3779   -138    723   -369       C  
ATOM   7286  CG1 ILE D 120      64.843  13.989 -29.614  1.00 36.41           C  
ANISOU 7286  CG1 ILE D 120     4771   4342   4721   -135    772   -347       C  
ATOM   7287  CG2 ILE D 120      65.370  11.619 -29.063  1.00 28.63           C  
ANISOU 7287  CG2 ILE D 120     3712   3359   3808   -169    717   -408       C  
ATOM   7288  CD1 ILE D 120      65.058  14.677 -28.279  1.00 32.72           C  
ANISOU 7288  CD1 ILE D 120     4300   3841   4290   -141    764   -334       C  
ATOM   7289  N   SER D 121      64.275  13.471 -32.730  1.00 30.38           N  
ANISOU 7289  N   SER D 121     4043   3654   3847   -109    813   -357       N  
ATOM   7290  CA  SER D 121      65.191  13.938 -33.775  1.00 31.74           C  
ANISOU 7290  CA  SER D 121     4238   3813   4009   -115    869   -362       C  
ATOM   7291  C   SER D 121      65.659  15.366 -33.485  1.00 34.74           C  
ANISOU 7291  C   SER D 121     4650   4155   4395   -111    911   -333       C  
ATOM   7292  O   SER D 121      64.897  16.171 -32.950  1.00 36.29           O  
ANISOU 7292  O   SER D 121     4866   4353   4570    -90    901   -298       O  
ATOM   7293  CB  SER D 121      64.535  13.865 -35.155  1.00 34.71           C  
ANISOU 7293  CB  SER D 121     4637   4236   4314    -91    881   -356       C  
ATOM   7294  OG  SER D 121      63.391  14.694 -35.240  1.00 35.47           O  
ANISOU 7294  OG  SER D 121     4766   4360   4353    -56    874   -314       O  
ATOM   7295  N   LEU D 122      66.905  15.678 -33.835  1.00 31.32           N  
ANISOU 7295  N   LEU D 122     4221   3687   3992   -131    958   -349       N  
ATOM   7296  CA  LEU D 122      67.427  17.030 -33.652  1.00 30.29           C  
ANISOU 7296  CA  LEU D 122     4120   3518   3869   -129   1005   -325       C  
ATOM   7297  C   LEU D 122      67.714  17.686 -34.991  1.00 40.69           C  
ANISOU 7297  C   LEU D 122     5478   4840   5144   -117   1064   -312       C  
ATOM   7298  O   LEU D 122      68.104  17.014 -35.944  1.00 36.47           O  
ANISOU 7298  O   LEU D 122     4938   4321   4599   -125   1077   -336       O  
ATOM   7299  CB  LEU D 122      68.688  17.023 -32.798  1.00 25.98           C  
ANISOU 7299  CB  LEU D 122     3547   2922   3400   -163   1017   -354       C  
ATOM   7300  CG  LEU D 122      68.552  16.293 -31.464  1.00 31.84           C  
ANISOU 7300  CG  LEU D 122     4248   3660   4189   -176    960   -369       C  
ATOM   7301  CD1 LEU D 122      69.853  16.397 -30.699  1.00 22.16           C  
ANISOU 7301  CD1 LEU D 122     2998   2387   3035   -206    976   -397       C  
ATOM   7302  CD2 LEU D 122      67.380  16.867 -30.657  1.00 25.96           C  
ANISOU 7302  CD2 LEU D 122     3517   2928   3418   -152    929   -332       C  
ATOM   7303  N   HIS D 123      67.519  19.000 -35.054  1.00 37.63           N  
ANISOU 7303  N   HIS D 123     5130   4437   4731    -98   1100   -273       N  
ATOM   7304  CA  HIS D 123      67.698  19.749 -36.291  1.00 39.92           C  
ANISOU 7304  CA  HIS D 123     5463   4730   4975    -82   1158   -252       C  
ATOM   7305  C   HIS D 123      68.290  21.126 -36.019  1.00 45.80           C  
ANISOU 7305  C   HIS D 123     6236   5424   5740    -83   1214   -229       C  
ATOM   7306  O   HIS D 123      67.746  21.895 -35.226  1.00 40.77           O  
ANISOU 7306  O   HIS D 123     5610   4776   5104    -70   1205   -201       O  
ATOM   7307  CB  HIS D 123      66.358  19.929 -37.003  1.00 44.69           C  
ANISOU 7307  CB  HIS D 123     6097   5387   5498    -40   1143   -216       C  
ATOM   7308  CG  HIS D 123      65.556  18.676 -37.106  1.00 42.88           C  
ANISOU 7308  CG  HIS D 123     5839   5208   5247    -36   1084   -235       C  
ATOM   7309  ND1 HIS D 123      65.721  17.766 -38.129  1.00 49.64           N  
ANISOU 7309  ND1 HIS D 123     6685   6096   6082    -41   1084   -264       N  
ATOM   7310  CD2 HIS D 123      64.580  18.171 -36.311  1.00 42.28           C  
ANISOU 7310  CD2 HIS D 123     5740   5155   5170    -28   1023   -233       C  
ATOM   7311  CE1 HIS D 123      64.880  16.761 -37.963  1.00 45.66           C  
ANISOU 7311  CE1 HIS D 123     6153   5632   5565    -36   1028   -279       C  
ATOM   7312  NE2 HIS D 123      64.177  16.982 -36.863  1.00 36.73           N  
ANISOU 7312  NE2 HIS D 123     5013   4495   4446    -29    990   -260       N  
ATOM   7313  N   SER D 124      69.394  21.446 -36.685  1.00 46.15           N  
ANISOU 7313  N   SER D 124     6294   5439   5803    -99   1273   -243       N  
ATOM   7314  CA  SER D 124      69.966  22.775 -36.559  1.00 45.86           C  
ANISOU 7314  CA  SER D 124     6286   5354   5784   -100   1334   -222       C  
ATOM   7315  C   SER D 124      68.952  23.828 -37.042  1.00 49.30           C  
ANISOU 7315  C   SER D 124     6773   5808   6153    -58   1354   -164       C  
ATOM   7316  O   SER D 124      68.242  23.610 -38.026  1.00 46.99           O  
ANISOU 7316  O   SER D 124     6501   5560   5793    -30   1350   -145       O  
ATOM   7317  CB  SER D 124      71.277  22.869 -37.340  1.00 46.44           C  
ANISOU 7317  CB  SER D 124     6365   5396   5882   -124   1397   -247       C  
ATOM   7318  OG  SER D 124      72.084  23.916 -36.824  1.00 56.56           O  
ANISOU 7318  OG  SER D 124     7656   6621   7212   -139   1446   -246       O  
ATOM   7319  N   GLU D 125      68.872  24.952 -36.329  1.00 55.10           N  
ANISOU 7319  N   GLU D 125     7524   6508   6905    -52   1376   -138       N  
ATOM   7320  CA  GLU D 125      67.985  26.057 -36.706  1.00 68.04           C  
ANISOU 7320  CA  GLU D 125     9210   8154   8487    -11   1401    -82       C  
ATOM   7321  C   GLU D 125      68.537  27.404 -36.218  1.00 77.60           C  
ANISOU 7321  C   GLU D 125    10442   9306   9735    -17   1458    -64       C  
ATOM   7322  O   GLU D 125      69.591  27.461 -35.581  1.00 76.11           O  
ANISOU 7322  O   GLU D 125    10230   9074   9616    -53   1476    -98       O  
ATOM   7323  CB  GLU D 125      66.593  25.859 -36.110  1.00 66.45           C  
ANISOU 7323  CB  GLU D 125     9002   7993   8252     15   1335    -58       C  
ATOM   7324  CG  GLU D 125      66.527  26.246 -34.640  1.00 65.05           C  
ANISOU 7324  CG  GLU D 125     8805   7785   8128      1   1312    -61       C  
ATOM   7325  CD  GLU D 125      65.120  26.215 -34.084  1.00 65.77           C  
ANISOU 7325  CD  GLU D 125     8894   7911   8183     29   1256    -33       C  
ATOM   7326  OE1 GLU D 125      64.945  26.588 -32.902  1.00 63.80           O  
ANISOU 7326  OE1 GLU D 125     8632   7641   7970     21   1236    -31       O  
ATOM   7327  OE2 GLU D 125      64.193  25.821 -34.826  1.00 67.87           O  
ANISOU 7327  OE2 GLU D 125     9173   8228   8386     58   1231    -15       O  
ATOM   7328  N   THR D 126      67.825  28.479 -36.535  1.00102.41           N  
ANISOU 7328  N   THR D 126    13629  12449  12833     19   1488    -12       N  
ATOM   7329  CA  THR D 126      68.230  29.819 -36.127  1.00106.30           C  
ANISOU 7329  CA  THR D 126    14145  12886  13358     17   1546      8       C  
ATOM   7330  C   THR D 126      67.021  30.731 -35.953  1.00105.68           C  
ANISOU 7330  C   THR D 126    14099  12819  13235     58   1542     64       C  
ATOM   7331  O   THR D 126      66.017  30.588 -36.649  1.00104.73           O  
ANISOU 7331  O   THR D 126    14000  12747  13044     95   1521     96       O  
ATOM   7332  CB  THR D 126      69.180  30.457 -37.150  1.00111.00           C  
ANISOU 7332  CB  THR D 126    14774  13448  13953     13   1631     14       C  
ATOM   7333  OG1 THR D 126      68.497  31.510 -37.841  1.00108.53           O  
ANISOU 7333  OG1 THR D 126    14515  13139  13584     56   1674     73       O  
ATOM   7334  CG2 THR D 126      69.656  29.422 -38.157  1.00107.64           C  
ANISOU 7334  CG2 THR D 126    14340  13051  13508      3   1629    -15       C  
ATOM   7335  N   ILE D 127      67.126  31.673 -35.021  1.00183.39           N  
ANISOU 7335  N   ILE D 127    23943  22618  23120     51   1562     73       N  
ATOM   7336  CA  ILE D 127      66.049  32.623 -34.768  1.00183.68           C  
ANISOU 7336  CA  ILE D 127    24009  22657  23123     87   1563    124       C  
ATOM   7337  C   ILE D 127      66.414  33.585 -33.644  1.00181.71           C  
ANISOU 7337  C   ILE D 127    23754  22353  22936     69   1589    121       C  
ATOM   7338  O   ILE D 127      65.662  33.747 -32.683  1.00180.19           O  
ANISOU 7338  O   ILE D 127    23549  22167  22750     75   1547    130       O  
ATOM   7339  CB  ILE D 127      64.735  31.903 -34.408  1.00 95.40           C  
ANISOU 7339  CB  ILE D 127    12812  11534  11901    109   1480    134       C  
ATOM   7340  CG1 ILE D 127      64.837  30.412 -34.736  1.00 94.92           C  
ANISOU 7340  CG1 ILE D 127    12718  11517  11830     95   1428     96       C  
ATOM   7341  CG2 ILE D 127      63.563  32.538 -35.143  1.00 96.56           C  
ANISOU 7341  CG2 ILE D 127    13003  11712  11972    163   1488    194       C  
ATOM   7342  CD1 ILE D 127      64.550  29.507 -33.559  1.00 93.01           C  
ANISOU 7342  CD1 ILE D 127    12427  11290  11622     73   1354     63       C  
ATOM   7343  N   LYS D 130      69.355  33.607 -33.806  1.00202.55           N  
ANISOU 7343  N   LYS D 130    26365  24902  25694    -11   1688     37       N  
ATOM   7344  CA  LYS D 130      70.645  32.925 -33.810  1.00201.68           C  
ANISOU 7344  CA  LYS D 130    26221  24771  25636    -53   1698    -19       C  
ATOM   7345  C   LYS D 130      70.511  31.470 -34.251  1.00202.34           C  
ANISOU 7345  C   LYS D 130    26280  24907  25693    -56   1640    -42       C  
ATOM   7346  O   LYS D 130      69.403  30.960 -34.428  1.00203.27           O  
ANISOU 7346  O   LYS D 130    26403  25076  25755    -29   1587    -19       O  
ATOM   7347  CB  LYS D 130      71.287  32.993 -32.424  1.00112.27           C  
ANISOU 7347  CB  LYS D 130    14853  13413  14390    -90   1682    -61       C  
ATOM   7348  CG  LYS D 130      71.694  34.395 -31.996  1.00111.82           C  
ANISOU 7348  CG  LYS D 130    14813  13297  14374    -97   1748    -52       C  
ATOM   7349  CD  LYS D 130      72.300  34.394 -30.604  1.00109.62           C  
ANISOU 7349  CD  LYS D 130    14488  12992  14170   -133   1726    -98       C  
ATOM   7350  CE  LYS D 130      72.728  35.791 -30.185  1.00109.28           C  
ANISOU 7350  CE  LYS D 130    14460  12891  14170   -142   1795    -93       C  
ATOM   7351  NZ  LYS D 130      73.303  35.807 -28.812  1.00107.37           N  
ANISOU 7351  NZ  LYS D 130    14170  12627  13998   -176   1772   -141       N  
ATOM   7352  N   THR D 131      71.650  30.810 -34.432  1.00 95.03           N  
ANISOU 7352  N   THR D 131    12663  11302  12144    -91   1651    -90       N  
ATOM   7353  CA  THR D 131      71.670  29.418 -34.860  1.00 95.61           C  
ANISOU 7353  CA  THR D 131    12710  11418  12201    -99   1603   -118       C  
ATOM   7354  C   THR D 131      71.689  28.480 -33.659  1.00 92.93           C  
ANISOU 7354  C   THR D 131    12315  11089  11904   -123   1530   -157       C  
ATOM   7355  O   THR D 131      72.659  28.436 -32.906  1.00 90.96           O  
ANISOU 7355  O   THR D 131    12033  10804  11723   -157   1536   -197       O  
ATOM   7356  CB  THR D 131      72.888  29.119 -35.747  1.00 86.77           C  
ANISOU 7356  CB  THR D 131    11590  10279  11101   -123   1653   -150       C  
ATOM   7357  OG1 THR D 131      72.647  29.603 -37.073  1.00 89.92           O  
ANISOU 7357  OG1 THR D 131    12039  10688  11439    -94   1705   -112       O  
ATOM   7358  CG2 THR D 131      73.149  27.625 -35.798  1.00 86.42           C  
ANISOU 7358  CG2 THR D 131    11503  10266  11067   -143   1599   -194       C  
ATOM   7359  N   GLY D 132      70.611  27.730 -33.483  1.00 42.42           N  
ANISOU 7359  N   GLY D 132     5908   4741   5468   -103   1462   -145       N  
ATOM   7360  CA  GLY D 132      70.522  26.807 -32.371  1.00 47.62           C  
ANISOU 7360  CA  GLY D 132     6518   5414   6163   -122   1392   -177       C  
ATOM   7361  C   GLY D 132      70.094  25.421 -32.797  1.00 44.76           C  
ANISOU 7361  C   GLY D 132     6134   5100   5772   -119   1337   -192       C  
ATOM   7362  O   GLY D 132      70.434  24.956 -33.883  1.00 41.33           O  
ANISOU 7362  O   GLY D 132     5708   4680   5316   -119   1358   -202       O  
ATOM   7363  N   THR D 133      69.338  24.761 -31.929  1.00 43.57           N  
ANISOU 7363  N   THR D 133     5956   4976   5621   -116   1268   -195       N  
ATOM   7364  CA  THR D 133      68.861  23.401 -32.197  1.00 37.78           C  
ANISOU 7364  CA  THR D 133     5199   4289   4867   -114   1213   -211       C  
ATOM   7365  C   THR D 133      67.371  23.243 -31.918  1.00 37.84           C  
ANISOU 7365  C   THR D 133     5212   4340   4826    -83   1159   -180       C  
ATOM   7366  O   THR D 133      66.885  23.648 -30.867  1.00 34.01           O  
ANISOU 7366  O   THR D 133     4722   3847   4355    -79   1135   -167       O  
ATOM   7367  CB  THR D 133      69.606  22.372 -31.337  1.00 36.10           C  
ANISOU 7367  CB  THR D 133     4933   4066   4718   -148   1174   -260       C  
ATOM   7368  OG1 THR D 133      71.006  22.443 -31.621  1.00 27.71           O  
ANISOU 7368  OG1 THR D 133     3861   2965   3701   -177   1221   -293       O  
ATOM   7369  CG2 THR D 133      69.096  20.960 -31.622  1.00 36.77           C  
ANISOU 7369  CG2 THR D 133     4993   4195   4783   -146   1120   -276       C  
ATOM   7370  N   LEU D 134      66.656  22.642 -32.865  1.00 32.71           N  
ANISOU 7370  N   LEU D 134     4572   3736   4119    -62   1142   -171       N  
ATOM   7371  CA  LEU D 134      65.262  22.272 -32.675  1.00 33.73           C  
ANISOU 7371  CA  LEU D 134     4700   3911   4204    -36   1087   -150       C  
ATOM   7372  C   LEU D 134      65.121  20.778 -32.301  1.00 42.63           C  
ANISOU 7372  C   LEU D 134     5782   5065   5352    -52   1027   -187       C  
ATOM   7373  O   LEU D 134      65.559  19.895 -33.046  1.00 35.30           O  
ANISOU 7373  O   LEU D 134     4840   4152   4423    -64   1028   -215       O  
ATOM   7374  CB  LEU D 134      64.474  22.558 -33.946  1.00 36.16           C  
ANISOU 7374  CB  LEU D 134     5047   4258   4434      1   1105   -118       C  
ATOM   7375  CG  LEU D 134      63.099  21.899 -33.974  1.00 39.29           C  
ANISOU 7375  CG  LEU D 134     5435   4710   4783     26   1045   -107       C  
ATOM   7376  CD1 LEU D 134      62.213  22.535 -32.925  1.00 39.12           C  
ANISOU 7376  CD1 LEU D 134     5417   4684   4761     41   1019    -78       C  
ATOM   7377  CD2 LEU D 134      62.472  22.017 -35.339  1.00 38.15           C  
ANISOU 7377  CD2 LEU D 134     5324   4610   4563     60   1061    -84       C  
ATOM   7378  N   ALA D 135      64.512  20.501 -31.150  1.00 39.84           N  
ANISOU 7378  N   ALA D 135     5406   4716   5017    -53    976   -186       N  
ATOM   7379  CA  ALA D 135      64.286  19.126 -30.707  1.00 31.29           C  
ANISOU 7379  CA  ALA D 135     4280   3656   3953    -66    919   -216       C  
ATOM   7380  C   ALA D 135      62.835  18.719 -30.893  1.00 38.65           C  
ANISOU 7380  C   ALA D 135     5215   4638   4831    -38    875   -198       C  
ATOM   7381  O   ALA D 135      61.923  19.406 -30.436  1.00 43.13           O  
ANISOU 7381  O   ALA D 135     5800   5213   5375    -16    863   -165       O  
ATOM   7382  CB  ALA D 135      64.690  18.964 -29.262  1.00 30.49           C  
ANISOU 7382  CB  ALA D 135     4147   3525   3914    -89    892   -232       C  
ATOM   7383  N   ILE D 136      62.621  17.599 -31.574  1.00 32.24           N  
ANISOU 7383  N   ILE D 136     4386   3861   4002    -39    854   -221       N  
ATOM   7384  CA  ILE D 136      61.283  17.057 -31.731  1.00 24.30           C  
ANISOU 7384  CA  ILE D 136     3376   2904   2951    -16    809   -212       C  
ATOM   7385  C   ILE D 136      61.212  15.655 -31.131  1.00 33.10           C  
ANISOU 7385  C   ILE D 136     4445   4030   4104    -36    760   -247       C  
ATOM   7386  O   ILE D 136      62.031  14.797 -31.453  1.00 29.75           O  
ANISOU 7386  O   ILE D 136     3997   3599   3710    -60    765   -283       O  
ATOM   7387  CB  ILE D 136      60.894  16.960 -33.208  1.00 35.41           C  
ANISOU 7387  CB  ILE D 136     4806   4355   4295      6    827   -208       C  
ATOM   7388  CG1 ILE D 136      61.251  18.254 -33.943  1.00 37.22           C  
ANISOU 7388  CG1 ILE D 136     5081   4568   4493     22    886   -176       C  
ATOM   7389  CG2 ILE D 136      59.407  16.655 -33.344  1.00 32.63           C  
ANISOU 7389  CG2 ILE D 136     4454   4055   3891     35    784   -194       C  
ATOM   7390  CD1 ILE D 136      60.983  18.183 -35.434  1.00 35.00           C  
ANISOU 7390  CD1 ILE D 136     4822   4328   4147     44    907   -172       C  
ATOM   7391  N   GLU D 137      60.225  15.424 -30.268  1.00 34.77           N  
ANISOU 7391  N   GLU D 137     4643   4255   4314    -27    714   -237       N  
ATOM   7392  CA  GLU D 137      60.015  14.107 -29.674  1.00 39.47           C  
ANISOU 7392  CA  GLU D 137     5196   4861   4942    -43    668   -266       C  
ATOM   7393  C   GLU D 137      58.582  13.613 -29.836  1.00 36.85           C  
ANISOU 7393  C   GLU D 137     4859   4576   4565    -20    628   -260       C  
ATOM   7394  O   GLU D 137      57.624  14.298 -29.476  1.00 34.90           O  
ANISOU 7394  O   GLU D 137     4630   4342   4289      3    615   -229       O  
ATOM   7395  CB  GLU D 137      60.422  14.081 -28.192  1.00 33.99           C  
ANISOU 7395  CB  GLU D 137     4479   4129   4306    -62    648   -269       C  
ATOM   7396  CG  GLU D 137      60.254  12.691 -27.550  1.00 34.16           C  
ANISOU 7396  CG  GLU D 137     4457   4157   4364    -77    602   -297       C  
ATOM   7397  CD  GLU D 137      61.101  12.498 -26.296  1.00 48.80           C  
ANISOU 7397  CD  GLU D 137     6286   5972   6285   -101    591   -309       C  
ATOM   7398  OE1 GLU D 137      61.794  13.464 -25.884  1.00 48.56           O  
ANISOU 7398  OE1 GLU D 137     6270   5910   6272   -107    618   -298       O  
ATOM   7399  OE2 GLU D 137      61.080  11.377 -25.729  1.00 43.45           O  
ANISOU 7399  OE2 GLU D 137     5573   5294   5640   -114    558   -330       O  
ATOM   7400  N   SER D 138      58.445  12.417 -30.389  1.00 27.85           N  
ANISOU 7400  N   SER D 138     3694   3464   3425    -27    610   -292       N  
ATOM   7401  CA  SER D 138      57.141  11.803 -30.547  1.00 32.41           C  
ANISOU 7401  CA  SER D 138     4261   4087   3968    -10    572   -294       C  
ATOM   7402  C   SER D 138      57.078  10.471 -29.808  1.00 26.21           C  
ANISOU 7402  C   SER D 138     3430   3297   3230    -31    534   -326       C  
ATOM   7403  O   SER D 138      58.095   9.863 -29.501  1.00 29.23           O  
ANISOU 7403  O   SER D 138     3789   3649   3666    -58    539   -350       O  
ATOM   7404  CB  SER D 138      56.832  11.579 -32.029  1.00 33.57           C  
ANISOU 7404  CB  SER D 138     4418   4278   4059      6    586   -305       C  
ATOM   7405  OG  SER D 138      57.762  10.677 -32.607  1.00 34.02           O  
ANISOU 7405  OG  SER D 138     4453   4329   4144    -19    600   -345       O  
ATOM   7406  N   PHE D 139      55.867  10.020 -29.535  1.00 23.85           N  
ANISOU 7406  N   PHE D 139     3120   3030   2914    -18    496   -324       N  
ATOM   7407  CA  PHE D 139      55.669   8.735 -28.903  1.00 34.00           C  
ANISOU 7407  CA  PHE D 139     4364   4314   4240    -35    462   -352       C  
ATOM   7408  C   PHE D 139      54.394   8.087 -29.416  1.00 29.58           C  
ANISOU 7408  C   PHE D 139     3792   3803   3642    -19    435   -364       C  
ATOM   7409  O   PHE D 139      53.515   8.754 -29.941  1.00 29.62           O  
ANISOU 7409  O   PHE D 139     3822   3843   3590      9    434   -344       O  
ATOM   7410  CB  PHE D 139      55.580   8.897 -27.389  1.00 25.93           C  
ANISOU 7410  CB  PHE D 139     3333   3260   3258    -41    439   -334       C  
ATOM   7411  CG  PHE D 139      54.332   9.598 -26.930  1.00 25.18           C  
ANISOU 7411  CG  PHE D 139     3256   3184   3126    -16    418   -302       C  
ATOM   7412  CD1 PHE D 139      53.170   8.888 -26.699  1.00 28.43           C  
ANISOU 7412  CD1 PHE D 139     3650   3625   3529     -8    383   -310       C  
ATOM   7413  CD2 PHE D 139      54.327  10.969 -26.722  1.00 30.33           C  
ANISOU 7413  CD2 PHE D 139     3943   3824   3756     -1    437   -266       C  
ATOM   7414  CE1 PHE D 139      52.016   9.528 -26.269  1.00 27.91           C  
ANISOU 7414  CE1 PHE D 139     3598   3576   3429     15    364   -282       C  
ATOM   7415  CE2 PHE D 139      53.181  11.615 -26.295  1.00 34.51           C  
ANISOU 7415  CE2 PHE D 139     4487   4369   4254     22    419   -237       C  
ATOM   7416  CZ  PHE D 139      52.024  10.890 -26.068  1.00 24.14           C  
ANISOU 7416  CZ  PHE D 139     3155   3086   2930     31    381   -245       C  
ATOM   7417  N   VAL D 140      54.325   6.775 -29.280  1.00 27.67           N  
ANISOU 7417  N   VAL D 140     3513   3566   3434    -36    414   -399       N  
ATOM   7418  CA  VAL D 140      53.076   6.048 -29.392  1.00 33.16           C  
ANISOU 7418  CA  VAL D 140     4189   4300   4109    -25    383   -413       C  
ATOM   7419  C   VAL D 140      53.013   5.090 -28.200  1.00 32.21           C  
ANISOU 7419  C   VAL D 140     4035   4155   4050    -44    355   -426       C  
ATOM   7420  O   VAL D 140      54.051   4.560 -27.767  1.00 25.25           O  
ANISOU 7420  O   VAL D 140     3135   3236   3223    -68    362   -440       O  
ATOM   7421  CB  VAL D 140      53.002   5.244 -30.691  1.00 37.72           C  
ANISOU 7421  CB  VAL D 140     4752   4916   4664    -27    390   -452       C  
ATOM   7422  CG1 VAL D 140      54.357   4.704 -31.030  1.00 44.51           C  
ANISOU 7422  CG1 VAL D 140     5599   5748   5566    -54    416   -478       C  
ATOM   7423  CG2 VAL D 140      52.009   4.094 -30.545  1.00 36.36           C  
ANISOU 7423  CG2 VAL D 140     4545   4770   4501    -29    357   -481       C  
ATOM   7424  N   VAL D 141      51.810   4.885 -27.666  1.00 27.58           N  
ANISOU 7424  N   VAL D 141     3440   3588   3453    -32    324   -420       N  
ATOM   7425  CA  VAL D 141      51.623   4.044 -26.487  1.00 23.09           C  
ANISOU 7425  CA  VAL D 141     2842   2995   2936    -47    298   -426       C  
ATOM   7426  C   VAL D 141      50.174   3.523 -26.382  1.00 27.50           C  
ANISOU 7426  C   VAL D 141     3385   3588   3476    -35    269   -435       C  
ATOM   7427  O   VAL D 141      49.246   4.142 -26.900  1.00 28.39           O  
ANISOU 7427  O   VAL D 141     3515   3738   3534    -11    264   -423       O  
ATOM   7428  CB  VAL D 141      51.992   4.839 -25.205  1.00 28.52           C  
ANISOU 7428  CB  VAL D 141     3545   3644   3649    -48    295   -390       C  
ATOM   7429  CG1 VAL D 141      50.959   5.940 -24.938  1.00 19.21           C  
ANISOU 7429  CG1 VAL D 141     2393   2482   2422    -22    285   -355       C  
ATOM   7430  CG2 VAL D 141      52.138   3.896 -23.989  1.00 23.29           C  
ANISOU 7430  CG2 VAL D 141     2851   2951   3047    -66    274   -398       C  
ATOM   7431  N   ASP D 142      49.998   2.373 -25.738  1.00 33.03           N  
ANISOU 7431  N   ASP D 142     4051   4275   4223    -51    251   -456       N  
ATOM   7432  CA  ASP D 142      48.667   1.859 -25.414  1.00 33.67           C  
ANISOU 7432  CA  ASP D 142     4115   4380   4297    -42    224   -463       C  
ATOM   7433  C   ASP D 142      48.015   2.689 -24.313  1.00 38.46           C  
ANISOU 7433  C   ASP D 142     4740   4977   4895    -28    207   -424       C  
ATOM   7434  O   ASP D 142      48.659   3.008 -23.314  1.00 36.57           O  
ANISOU 7434  O   ASP D 142     4507   4698   4688    -37    207   -401       O  
ATOM   7435  CB  ASP D 142      48.766   0.421 -24.919  1.00 33.85           C  
ANISOU 7435  CB  ASP D 142     4097   4383   4379    -64    214   -494       C  
ATOM   7436  CG  ASP D 142      49.143  -0.549 -26.012  1.00 37.54           C  
ANISOU 7436  CG  ASP D 142     4541   4866   4856    -78    228   -539       C  
ATOM   7437  OD1 ASP D 142      49.460  -0.085 -27.129  1.00 41.01           O  
ANISOU 7437  OD1 ASP D 142     4996   5329   5256    -71    246   -546       O  
ATOM   7438  OD2 ASP D 142      49.093  -1.775 -25.756  1.00 37.55           O  
ANISOU 7438  OD2 ASP D 142     4508   4856   4904    -95    223   -567       O  
ATOM   7439  N   VAL D 143      46.744   3.045 -24.488  1.00 36.36           N  
ANISOU 7439  N   VAL D 143     4481   4747   4586     -7    191   -417       N  
ATOM   7440  CA  VAL D 143      46.003   3.681 -23.405  1.00 43.15           C  
ANISOU 7440  CA  VAL D 143     5353   5598   5442      5    173   -384       C  
ATOM   7441  C   VAL D 143      45.735   2.643 -22.315  1.00 39.43           C  
ANISOU 7441  C   VAL D 143     4853   5105   5024    -11    154   -394       C  
ATOM   7442  O   VAL D 143      45.129   1.604 -22.570  1.00 39.04           O  
ANISOU 7442  O   VAL D 143     4775   5073   4987    -17    144   -426       O  
ATOM   7443  CB  VAL D 143      44.676   4.298 -23.886  1.00 46.63           C  
ANISOU 7443  CB  VAL D 143     5808   6085   5823     33    160   -376       C  
ATOM   7444  CG1 VAL D 143      43.934   4.937 -22.719  1.00 43.32           C  
ANISOU 7444  CG1 VAL D 143     5400   5654   5404     44    142   -343       C  
ATOM   7445  CG2 VAL D 143      44.932   5.319 -24.980  1.00 44.82           C  
ANISOU 7445  CG2 VAL D 143     5610   5879   5539     53    180   -362       C  
ATOM   7446  N   PRO D 144      46.207   2.913 -21.092  1.00 39.38           N  
ANISOU 7446  N   PRO D 144     4852   5059   5051    -19    150   -368       N  
ATOM   7447  CA  PRO D 144      46.058   1.919 -20.029  1.00 41.22           C  
ANISOU 7447  CA  PRO D 144     5059   5268   5336    -34    135   -375       C  
ATOM   7448  C   PRO D 144      44.599   1.782 -19.606  1.00 41.53           C  
ANISOU 7448  C   PRO D 144     5091   5328   5360    -22    113   -373       C  
ATOM   7449  O   PRO D 144      43.823   2.732 -19.746  1.00 32.26           O  
ANISOU 7449  O   PRO D 144     3938   4177   4140     -2    107   -354       O  
ATOM   7450  CB  PRO D 144      46.880   2.516 -18.885  1.00 35.53           C  
ANISOU 7450  CB  PRO D 144     4353   4507   4642    -40    136   -343       C  
ATOM   7451  CG  PRO D 144      46.796   3.982 -19.102  1.00 39.31           C  
ANISOU 7451  CG  PRO D 144     4867   4996   5074    -22    143   -314       C  
ATOM   7452  CD  PRO D 144      46.799   4.168 -20.599  1.00 45.20           C  
ANISOU 7452  CD  PRO D 144     5620   5774   5778    -13    159   -331       C  
ATOM   7453  N   GLU D 145      44.251   0.603 -19.097  1.00 62.49           N  
ANISOU 7453  N   GLU D 145     7716   7972   8056    -35    103   -393       N  
ATOM   7454  CA  GLU D 145      42.919   0.313 -18.565  1.00 70.91           C  
ANISOU 7454  CA  GLU D 145     8772   9053   9119    -27     83   -394       C  
ATOM   7455  C   GLU D 145      42.493   1.271 -17.444  1.00 69.18           C  
ANISOU 7455  C   GLU D 145     8575   8821   8888    -16     71   -353       C  
ATOM   7456  O   GLU D 145      43.092   1.299 -16.363  1.00 63.21           O  
ANISOU 7456  O   GLU D 145     7822   8029   8165    -25     69   -332       O  
ATOM   7457  CB  GLU D 145      42.887  -1.120 -18.042  1.00 77.67           C  
ANISOU 7457  CB  GLU D 145     9592   9886  10031    -46     81   -417       C  
ATOM   7458  CG  GLU D 145      41.713  -1.421 -17.145  1.00 90.82           C  
ANISOU 7458  CG  GLU D 145    11249  11552  11706    -42     64   -412       C  
ATOM   7459  CD  GLU D 145      40.775  -2.423 -17.766  1.00103.32           C  
ANISOU 7459  CD  GLU D 145    12802  13161  13294    -46     62   -454       C  
ATOM   7460  OE1 GLU D 145      40.755  -3.583 -17.301  1.00116.51           O  
ANISOU 7460  OE1 GLU D 145    14444  14809  15014    -61     64   -471       O  
ATOM   7461  OE2 GLU D 145      40.067  -2.051 -18.725  1.00104.95           O  
ANISOU 7461  OE2 GLU D 145    13010  13410  13455    -32     59   -470       O  
ATOM   7462  N   GLY D 146      41.451   2.050 -17.708  1.00 50.28           N  
ANISOU 7462  N   GLY D 146     6196   6459   6448      4     62   -343       N  
ATOM   7463  CA  GLY D 146      40.944   2.988 -16.725  1.00 51.73           C  
ANISOU 7463  CA  GLY D 146     6401   6635   6619     16     51   -307       C  
ATOM   7464  C   GLY D 146      41.041   4.425 -17.191  1.00 63.64           C  
ANISOU 7464  C   GLY D 146     7944   8157   8078     35     59   -281       C  
ATOM   7465  O   GLY D 146      40.367   5.312 -16.655  1.00 61.13           O  
ANISOU 7465  O   GLY D 146     7644   7844   7738     49     50   -255       O  
ATOM   7466  N   ASN D 147      41.872   4.667 -18.201  1.00 43.72           N  
ANISOU 7466  N   ASN D 147     5431   5642   5540     35     77   -288       N  
ATOM   7467  CA  ASN D 147      42.077   6.030 -18.657  1.00 41.22           C  
ANISOU 7467  CA  ASN D 147     5148   5333   5180     52     89   -262       C  
ATOM   7468  C   ASN D 147      41.558   6.332 -20.055  1.00 42.11           C  
ANISOU 7468  C   ASN D 147     5268   5491   5240     73     94   -274       C  
ATOM   7469  O   ASN D 147      41.207   5.436 -20.828  1.00 45.47           O  
ANISOU 7469  O   ASN D 147     5672   5944   5662     71     90   -308       O  
ATOM   7470  CB  ASN D 147      43.556   6.417 -18.550  1.00 46.07           C  
ANISOU 7470  CB  ASN D 147     5775   5913   5815     39    110   -250       C  
ATOM   7471  CG  ASN D 147      44.022   6.525 -17.112  1.00 39.13           C  
ANISOU 7471  CG  ASN D 147     4896   4994   4977     27    104   -230       C  
ATOM   7472  OD1 ASN D 147      44.611   5.598 -16.569  1.00 37.46           O  
ANISOU 7472  OD1 ASN D 147     4663   4759   4811      7    101   -243       O  
ATOM   7473  ND2 ASN D 147      43.738   7.656 -16.484  1.00 38.73           N  
ANISOU 7473  ND2 ASN D 147     4870   4938   4909     38    103   -198       N  
ATOM   7474  N   THR D 148      41.525   7.619 -20.362  1.00 45.20           N  
ANISOU 7474  N   THR D 148     5693   5892   5591     93    104   -245       N  
ATOM   7475  CA  THR D 148      41.159   8.094 -21.675  1.00 47.66           C  
ANISOU 7475  CA  THR D 148     6019   6245   5847    116    112   -248       C  
ATOM   7476  C   THR D 148      42.408   8.521 -22.435  1.00 53.37           C  
ANISOU 7476  C   THR D 148     6761   6956   6563    112    142   -243       C  
ATOM   7477  O   THR D 148      43.388   8.976 -21.839  1.00 48.62           O  
ANISOU 7477  O   THR D 148     6172   6315   5989    100    157   -225       O  
ATOM   7478  CB  THR D 148      40.258   9.301 -21.547  1.00 51.66           C  
ANISOU 7478  CB  THR D 148     6551   6767   6310    145    107   -215       C  
ATOM   7479  OG1 THR D 148      40.974  10.333 -20.865  1.00 55.96           O  
ANISOU 7479  OG1 THR D 148     7122   7274   6865    143    123   -179       O  
ATOM   7480  CG2 THR D 148      39.008   8.935 -20.745  1.00 53.05           C  
ANISOU 7480  CG2 THR D 148     6709   6954   6495    148     79   -219       C  
ATOM   7481  N   LYS D 149      42.366   8.379 -23.754  1.00 60.55           N  
ANISOU 7481  N   LYS D 149     7670   7901   7435    123    151   -262       N  
ATOM   7482  CA  LYS D 149      43.468   8.805 -24.607  1.00 63.18           C  
ANISOU 7482  CA  LYS D 149     8022   8227   7755    122    181   -258       C  
ATOM   7483  C   LYS D 149      43.877  10.252 -24.320  1.00 59.26           C  
ANISOU 7483  C   LYS D 149     7564   7707   7244    134    201   -214       C  
ATOM   7484  O   LYS D 149      45.060  10.599 -24.367  1.00 60.14           O  
ANISOU 7484  O   LYS D 149     7689   7788   7373    122    227   -207       O  
ATOM   7485  CB  LYS D 149      43.091   8.625 -26.083  1.00 62.50           C  
ANISOU 7485  CB  LYS D 149     7937   8193   7619    140    186   -279       C  
ATOM   7486  CG  LYS D 149      43.965   9.386 -27.072  1.00 66.74           C  
ANISOU 7486  CG  LYS D 149     8502   8731   8125    149    219   -266       C  
ATOM   7487  CD  LYS D 149      43.302  10.682 -27.542  1.00 74.70           C  
ANISOU 7487  CD  LYS D 149     9546   9765   9071    186    225   -229       C  
ATOM   7488  CE  LYS D 149      44.122  11.357 -28.637  1.00 84.40           C  
ANISOU 7488  CE  LYS D 149    10805  10999  10267    196    261   -217       C  
ATOM   7489  NZ  LYS D 149      43.479  12.603 -29.152  1.00 97.24           N  
ANISOU 7489  NZ  LYS D 149    12466  12649  11831    236    269   -180       N  
ATOM   7490  N   GLU D 150      42.897  11.095 -24.021  1.00 51.77           N  
ANISOU 7490  N   GLU D 150     6633   6773   6265    159    190   -187       N  
ATOM   7491  CA  GLU D 150      43.181  12.497 -23.739  1.00 60.86           C  
ANISOU 7491  CA  GLU D 150     7820   7902   7401    172    210   -145       C  
ATOM   7492  C   GLU D 150      43.992  12.627 -22.451  1.00 50.33           C  
ANISOU 7492  C   GLU D 150     6485   6516   6123    147    214   -134       C  
ATOM   7493  O   GLU D 150      44.923  13.430 -22.373  1.00 53.52           O  
ANISOU 7493  O   GLU D 150     6911   6890   6535    142    242   -116       O  
ATOM   7494  CB  GLU D 150      41.885  13.311 -23.649  1.00 69.04           C  
ANISOU 7494  CB  GLU D 150     8872   8964   8396    204    196   -119       C  
ATOM   7495  CG  GLU D 150      42.094  14.823 -23.670  1.00 71.64           C  
ANISOU 7495  CG  GLU D 150     9242   9278   8701    224    222    -76       C  
ATOM   7496  CD  GLU D 150      40.788  15.602 -23.581  1.00 90.56           C  
ANISOU 7496  CD  GLU D 150    11652  11700  11057    257    208    -51       C  
ATOM   7497  OE1 GLU D 150      39.868  15.324 -24.381  1.00 89.34           O  
ANISOU 7497  OE1 GLU D 150    11490  11593  10860    279    192    -62       O  
ATOM   7498  OE2 GLU D 150      40.684  16.491 -22.707  1.00 94.84           O  
ANISOU 7498  OE2 GLU D 150    12210  12215  11610    260    212    -21       O  
ATOM   7499  N   GLU D 151      43.630  11.833 -21.449  1.00 48.13           N  
ANISOU 7499  N   GLU D 151     6180   6226   5881    131    188   -147       N  
ATOM   7500  CA  GLU D 151      44.383  11.780 -20.200  1.00 50.60           C  
ANISOU 7500  CA  GLU D 151     6486   6494   6246    107    188   -141       C  
ATOM   7501  C   GLU D 151      45.814  11.295 -20.436  1.00 47.56           C  
ANISOU 7501  C   GLU D 151     6092   6083   5895     83    207   -159       C  
ATOM   7502  O   GLU D 151      46.773  11.886 -19.938  1.00 49.28           O  
ANISOU 7502  O   GLU D 151     6322   6266   6136     72    225   -146       O  
ATOM   7503  CB  GLU D 151      43.684  10.867 -19.190  1.00 46.52           C  
ANISOU 7503  CB  GLU D 151     5941   5975   5759     96    156   -153       C  
ATOM   7504  CG  GLU D 151      42.491  11.523 -18.489  1.00 53.61           C  
ANISOU 7504  CG  GLU D 151     6848   6882   6637    114    139   -129       C  
ATOM   7505  CD  GLU D 151      41.619  10.520 -17.745  1.00 51.63           C  
ANISOU 7505  CD  GLU D 151     6570   6639   6410    107    109   -146       C  
ATOM   7506  OE1 GLU D 151      41.999   9.328 -17.664  1.00 46.96           O  
ANISOU 7506  OE1 GLU D 151     5950   6039   5852     87    103   -173       O  
ATOM   7507  OE2 GLU D 151      40.544  10.923 -17.244  1.00 63.12           O  
ANISOU 7507  OE2 GLU D 151     8029   8105   7848    121     94   -131       O  
ATOM   7508  N   THR D 152      45.946  10.217 -21.199  1.00 35.83           N  
ANISOU 7508  N   THR D 152     4585   4615   4414     74    205   -192       N  
ATOM   7509  CA  THR D 152      47.245   9.597 -21.449  1.00 36.34           C  
ANISOU 7509  CA  THR D 152     4637   4657   4515     51    221   -214       C  
ATOM   7510  C   THR D 152      48.186  10.554 -22.180  1.00 40.19           C  
ANISOU 7510  C   THR D 152     5153   5133   4984     54    257   -201       C  
ATOM   7511  O   THR D 152      49.356  10.694 -21.806  1.00 36.44           O  
ANISOU 7511  O   THR D 152     4678   4623   4544     36    274   -201       O  
ATOM   7512  CB  THR D 152      47.087   8.292 -22.241  1.00 41.63           C  
ANISOU 7512  CB  THR D 152     5278   5351   5188     43    213   -253       C  
ATOM   7513  OG1 THR D 152      46.115   7.461 -21.597  1.00 38.33           O  
ANISOU 7513  OG1 THR D 152     4835   4943   4785     41    183   -264       O  
ATOM   7514  CG2 THR D 152      48.421   7.536 -22.328  1.00 36.90           C  
ANISOU 7514  CG2 THR D 152     4662   4724   4635     16    228   -276       C  
ATOM   7515  N   CYS D 153      47.679  11.230 -23.208  1.00 34.84           N  
ANISOU 7515  N   CYS D 153     4499   4488   4252     79    269   -190       N  
ATOM   7516  CA  CYS D 153      48.510  12.183 -23.924  1.00 39.06           C  
ANISOU 7516  CA  CYS D 153     5063   5011   4767     85    307   -174       C  
ATOM   7517  C   CYS D 153      48.959  13.270 -22.977  1.00 36.50           C  
ANISOU 7517  C   CYS D 153     4759   4649   4462     82    320   -144       C  
ATOM   7518  O   CYS D 153      50.123  13.627 -22.950  1.00 38.62           O  
ANISOU 7518  O   CYS D 153     5034   4885   4754     67    347   -144       O  
ATOM   7519  CB  CYS D 153      47.779  12.772 -25.129  1.00 45.12           C  
ANISOU 7519  CB  CYS D 153     5854   5820   5468    116    316   -162       C  
ATOM   7520  SG  CYS D 153      47.664  11.619 -26.508  1.00 55.57           S  
ANISOU 7520  SG  CYS D 153     7157   7188   6768    116    313   -203       S  
ATOM   7521  N   PHE D 154      48.025  13.777 -22.184  1.00 44.23           N  
ANISOU 7521  N   PHE D 154     5743   5630   5431     96    301   -122       N  
ATOM   7522  CA  PHE D 154      48.341  14.794 -21.197  1.00 47.11           C  
ANISOU 7522  CA  PHE D 154     6124   5960   5814     93    311    -95       C  
ATOM   7523  C   PHE D 154      49.458  14.352 -20.258  1.00 41.70           C  
ANISOU 7523  C   PHE D 154     5420   5236   5189     62    311   -110       C  
ATOM   7524  O   PHE D 154      50.372  15.124 -19.959  1.00 42.73           O  
ANISOU 7524  O   PHE D 154     5563   5334   5337     53    337   -101       O  
ATOM   7525  CB  PHE D 154      47.103  15.128 -20.376  1.00 52.62           C  
ANISOU 7525  CB  PHE D 154     6825   6669   6499    108    285    -76       C  
ATOM   7526  CG  PHE D 154      46.580  16.500 -20.623  1.00 63.31           C  
ANISOU 7526  CG  PHE D 154     8212   8028   7813    135    302    -41       C  
ATOM   7527  CD1 PHE D 154      45.340  16.688 -21.217  1.00 68.37           C  
ANISOU 7527  CD1 PHE D 154     8864   8710   8406    165    290    -30       C  
ATOM   7528  CD2 PHE D 154      47.338  17.609 -20.276  1.00 64.86           C  
ANISOU 7528  CD2 PHE D 154     8431   8189   8022    131    333    -20       C  
ATOM   7529  CE1 PHE D 154      44.859  17.960 -21.452  1.00 70.76           C  
ANISOU 7529  CE1 PHE D 154     9198   9016   8672    192    307      4       C  
ATOM   7530  CE2 PHE D 154      46.867  18.883 -20.507  1.00 72.70           C  
ANISOU 7530  CE2 PHE D 154     9457   9185   8982    157    352     13       C  
ATOM   7531  CZ  PHE D 154      45.622  19.061 -21.097  1.00 81.87           C  
ANISOU 7531  CZ  PHE D 154    10628  10385  10093    188    339     26       C  
ATOM   7532  N   PHE D 155      49.364  13.108 -19.795  1.00 36.45           N  
ANISOU 7532  N   PHE D 155     4722   4573   4554     46    283   -134       N  
ATOM   7533  CA  PHE D 155      50.340  12.534 -18.871  1.00 30.58           C  
ANISOU 7533  CA  PHE D 155     3956   3796   3866     20    278   -148       C  
ATOM   7534  C   PHE D 155      51.721  12.392 -19.523  1.00 30.65           C  
ANISOU 7534  C   PHE D 155     3963   3787   3896      3    307   -167       C  
ATOM   7535  O   PHE D 155      52.708  12.890 -18.993  1.00 31.34           O  
ANISOU 7535  O   PHE D 155     4054   3842   4013    -10    323   -164       O  
ATOM   7536  CB  PHE D 155      49.834  11.188 -18.341  1.00 26.97           C  
ANISOU 7536  CB  PHE D 155     3466   3348   3434     10    244   -168       C  
ATOM   7537  CG  PHE D 155      50.827  10.453 -17.471  1.00 31.96           C  
ANISOU 7537  CG  PHE D 155     4073   3948   4122    -14    238   -183       C  
ATOM   7538  CD1 PHE D 155      50.902  10.702 -16.108  1.00 36.46           C  
ANISOU 7538  CD1 PHE D 155     4639   4497   4718    -20    224   -169       C  
ATOM   7539  CD2 PHE D 155      51.676   9.504 -18.014  1.00 23.96           C  
ANISOU 7539  CD2 PHE D 155     3039   2929   3135    -31    245   -211       C  
ATOM   7540  CE1 PHE D 155      51.818  10.016 -15.303  1.00 29.59           C  
ANISOU 7540  CE1 PHE D 155     3745   3601   3897    -40    216   -182       C  
ATOM   7541  CE2 PHE D 155      52.585   8.807 -17.216  1.00 31.27           C  
ANISOU 7541  CE2 PHE D 155     3942   3828   4114    -51    238   -224       C  
ATOM   7542  CZ  PHE D 155      52.657   9.065 -15.860  1.00 27.46           C  
ANISOU 7542  CZ  PHE D 155     3455   3324   3654    -55    223   -208       C  
ATOM   7543  N   VAL D 156      51.788  11.725 -20.673  1.00 31.64           N  
ANISOU 7543  N   VAL D 156     4082   3933   4006      4    314   -188       N  
ATOM   7544  CA  VAL D 156      53.065  11.567 -21.375  1.00 31.62           C  
ANISOU 7544  CA  VAL D 156     4078   3914   4022    -12    343   -207       C  
ATOM   7545  C   VAL D 156      53.610  12.922 -21.812  1.00 33.48           C  
ANISOU 7545  C   VAL D 156     4348   4136   4237     -4    381   -186       C  
ATOM   7546  O   VAL D 156      54.781  13.238 -21.581  1.00 31.45           O  
ANISOU 7546  O   VAL D 156     4090   3846   4012    -21    404   -191       O  
ATOM   7547  CB  VAL D 156      52.938  10.671 -22.612  1.00 32.96           C  
ANISOU 7547  CB  VAL D 156     4236   4113   4173    -11    345   -233       C  
ATOM   7548  CG1 VAL D 156      54.316  10.485 -23.283  1.00 29.82           C  
ANISOU 7548  CG1 VAL D 156     3835   3696   3798    -29    376   -254       C  
ATOM   7549  CG2 VAL D 156      52.350   9.339 -22.229  1.00 24.77           C  
ANISOU 7549  CG2 VAL D 156     3165   3089   3157    -19    311   -255       C  
ATOM   7550  N   GLU D 157      52.746  13.726 -22.424  1.00 37.82           N  
ANISOU 7550  N   GLU D 157     4925   4710   4734     22    389   -163       N  
ATOM   7551  CA  GLU D 157      53.137  15.057 -22.871  1.00 41.91           C  
ANISOU 7551  CA  GLU D 157     5479   5216   5231     33    428   -139       C  
ATOM   7552  C   GLU D 157      53.796  15.834 -21.747  1.00 41.00           C  
ANISOU 7552  C   GLU D 157     5367   5059   5152     20    439   -127       C  
ATOM   7553  O   GLU D 157      54.812  16.498 -21.951  1.00 38.80           O  
ANISOU 7553  O   GLU D 157     5102   4754   4888     11    475   -126       O  
ATOM   7554  CB  GLU D 157      51.932  15.835 -23.381  1.00 44.19           C  
ANISOU 7554  CB  GLU D 157     5795   5535   5460     66    428   -110       C  
ATOM   7555  CG  GLU D 157      51.444  15.421 -24.755  1.00 46.44           C  
ANISOU 7555  CG  GLU D 157     6085   5863   5698     84    430   -118       C  
ATOM   7556  CD  GLU D 157      50.214  16.198 -25.158  1.00 53.41           C  
ANISOU 7556  CD  GLU D 157     6993   6778   6523    119    426    -88       C  
ATOM   7557  OE1 GLU D 157      49.693  16.951 -24.305  1.00 58.02           O  
ANISOU 7557  OE1 GLU D 157     7587   7349   7108    129    419    -63       O  
ATOM   7558  OE2 GLU D 157      49.767  16.060 -26.312  1.00 57.53           O  
ANISOU 7558  OE2 GLU D 157     7524   7338   6998    139    430    -91       O  
ATOM   7559  N   ALA D 158      53.206  15.745 -20.560  1.00 37.17           N  
ANISOU 7559  N   ALA D 158     4870   4570   4683     19    407   -119       N  
ATOM   7560  CA  ALA D 158      53.744  16.428 -19.391  1.00 43.36           C  
ANISOU 7560  CA  ALA D 158     5654   5319   5502      7    412   -110       C  
ATOM   7561  C   ALA D 158      55.149  15.929 -19.086  1.00 36.95           C  
ANISOU 7561  C   ALA D 158     4820   4478   4741    -21    422   -137       C  
ATOM   7562  O   ALA D 158      56.056  16.723 -18.838  1.00 34.07           O  
ANISOU 7562  O   ALA D 158     4464   4084   4398    -31    450   -135       O  
ATOM   7563  CB  ALA D 158      52.837  16.226 -18.190  1.00 33.71           C  
ANISOU 7563  CB  ALA D 158     4419   4103   4287     10    374   -101       C  
ATOM   7564  N   LEU D 159      55.333  14.615 -19.101  1.00 36.18           N  
ANISOU 7564  N   LEU D 159     4692   4388   4665    -34    399   -163       N  
ATOM   7565  CA  LEU D 159      56.650  14.069 -18.822  1.00 40.24           C  
ANISOU 7565  CA  LEU D 159     5184   4876   5230    -59    405   -189       C  
ATOM   7566  C   LEU D 159      57.668  14.466 -19.900  1.00 36.04           C  
ANISOU 7566  C   LEU D 159     4665   4331   4696    -66    449   -199       C  
ATOM   7567  O   LEU D 159      58.782  14.872 -19.591  1.00 34.52           O  
ANISOU 7567  O   LEU D 159     4469   4109   4538    -82    471   -209       O  
ATOM   7568  CB  LEU D 159      56.586  12.554 -18.647  1.00 37.57           C  
ANISOU 7568  CB  LEU D 159     4811   4548   4917    -70    374   -212       C  
ATOM   7569  CG  LEU D 159      55.886  12.066 -17.373  1.00 41.93           C  
ANISOU 7569  CG  LEU D 159     5345   5102   5484    -69    334   -205       C  
ATOM   7570  CD1 LEU D 159      56.133  10.580 -17.193  1.00 48.76           C  
ANISOU 7570  CD1 LEU D 159     6175   5967   6384    -82    311   -230       C  
ATOM   7571  CD2 LEU D 159      56.352  12.846 -16.136  1.00 40.30           C  
ANISOU 7571  CD2 LEU D 159     5141   4870   5303    -75    333   -193       C  
ATOM   7572  N   ILE D 160      57.271  14.378 -21.161  1.00 28.66           N  
ANISOU 7572  N   ILE D 160     3746   3423   3723    -53    463   -199       N  
ATOM   7573  CA  ILE D 160      58.183  14.727 -22.248  1.00 34.66           C  
ANISOU 7573  CA  ILE D 160     4520   4172   4476    -58    506   -208       C  
ATOM   7574  C   ILE D 160      58.538  16.211 -22.231  1.00 40.09           C  
ANISOU 7574  C   ILE D 160     5239   4837   5156    -52    545   -185       C  
ATOM   7575  O   ILE D 160      59.702  16.572 -22.403  1.00 38.98           O  
ANISOU 7575  O   ILE D 160     5101   4668   5042    -68    578   -197       O  
ATOM   7576  CB  ILE D 160      57.644  14.296 -23.617  1.00 38.40           C  
ANISOU 7576  CB  ILE D 160     5003   4682   4905    -43    511   -212       C  
ATOM   7577  CG1 ILE D 160      57.657  12.772 -23.700  1.00 27.13           C  
ANISOU 7577  CG1 ILE D 160     3539   3268   3500    -57    483   -245       C  
ATOM   7578  CG2 ILE D 160      58.495  14.884 -24.746  1.00 39.03           C  
ANISOU 7578  CG2 ILE D 160     5106   4753   4972    -45    561   -215       C  
ATOM   7579  CD1 ILE D 160      56.998  12.212 -24.927  1.00 35.78           C  
ANISOU 7579  CD1 ILE D 160     4638   4404   4553    -44    481   -254       C  
ATOM   7580  N   GLN D 161      57.554  17.074 -21.994  1.00 42.11           N  
ANISOU 7580  N   GLN D 161     5519   5103   5378    -30    541   -153       N  
ATOM   7581  CA  GLN D 161      57.849  18.501 -21.879  1.00 43.62           C  
ANISOU 7581  CA  GLN D 161     5740   5270   5566    -24    579   -131       C  
ATOM   7582  C   GLN D 161      58.894  18.735 -20.801  1.00 43.83           C  
ANISOU 7582  C   GLN D 161     5748   5256   5648    -49    585   -145       C  
ATOM   7583  O   GLN D 161      59.896  19.417 -21.028  1.00 46.92           O  
ANISOU 7583  O   GLN D 161     6149   5619   6059    -60    626   -151       O  
ATOM   7584  CB  GLN D 161      56.594  19.325 -21.571  1.00 49.09           C  
ANISOU 7584  CB  GLN D 161     6455   5976   6221      2    569    -95       C  
ATOM   7585  CG  GLN D 161      56.026  20.075 -22.772  1.00 55.55           C  
ANISOU 7585  CG  GLN D 161     7310   6813   6982     30    597    -69       C  
ATOM   7586  CD  GLN D 161      57.061  20.961 -23.457  1.00 66.82           C  
ANISOU 7586  CD  GLN D 161     8762   8213   8415     26    655    -65       C  
ATOM   7587  OE1 GLN D 161      57.085  21.077 -24.687  1.00 66.78           O  
ANISOU 7587  OE1 GLN D 161     8778   8222   8374     40    682    -59       O  
ATOM   7588  NE2 GLN D 161      57.924  21.589 -22.660  1.00 70.06           N  
ANISOU 7588  NE2 GLN D 161     9168   8582   8868      7    676    -70       N  
ATOM   7589  N   SER D 162      58.671  18.170 -19.623  1.00 36.00           N  
ANISOU 7589  N   SER D 162     4730   4265   4684    -58    544   -153       N  
ATOM   7590  CA  SER D 162      59.626  18.387 -18.547  1.00 39.75           C  
ANISOU 7590  CA  SER D 162     5186   4708   5209    -80    546   -167       C  
ATOM   7591  C   SER D 162      61.009  17.984 -19.043  1.00 38.77           C  
ANISOU 7591  C   SER D 162     5048   4564   5120   -102    571   -198       C  
ATOM   7592  O   SER D 162      62.007  18.659 -18.775  1.00 35.38           O  
ANISOU 7592  O   SER D 162     4618   4105   4721   -116    600   -209       O  
ATOM   7593  CB  SER D 162      59.253  17.576 -17.310  1.00 40.93           C  
ANISOU 7593  CB  SER D 162     5305   4864   5381    -86    496   -174       C  
ATOM   7594  OG  SER D 162      57.849  17.469 -17.178  1.00 46.83           O  
ANISOU 7594  OG  SER D 162     6062   5639   6092    -65    467   -151       O  
ATOM   7595  N   ASN D 163      61.059  16.873 -19.771  1.00 36.17           N  
ANISOU 7595  N   ASN D 163     4704   4252   4787   -104    559   -215       N  
ATOM   7596  CA  ASN D 163      62.331  16.350 -20.252  1.00 42.93           C  
ANISOU 7596  CA  ASN D 163     5543   5091   5677   -125    579   -247       C  
ATOM   7597  C   ASN D 163      63.008  17.306 -21.238  1.00 33.19           C  
ANISOU 7597  C   ASN D 163     4338   3841   4433   -126    636   -245       C  
ATOM   7598  O   ASN D 163      64.182  17.618 -21.081  1.00 34.43           O  
ANISOU 7598  O   ASN D 163     4486   3967   4628   -145    663   -264       O  
ATOM   7599  CB  ASN D 163      62.158  14.946 -20.844  1.00 35.77           C  
ANISOU 7599  CB  ASN D 163     4615   4207   4768   -128    556   -266       C  
ATOM   7600  CG  ASN D 163      61.914  13.891 -19.772  1.00 39.55           C  
ANISOU 7600  CG  ASN D 163     5060   4692   5277   -134    507   -276       C  
ATOM   7601  OD1 ASN D 163      62.416  14.001 -18.649  1.00 37.84           O  
ANISOU 7601  OD1 ASN D 163     4826   4455   5097   -145    495   -281       O  
ATOM   7602  ND2 ASN D 163      61.141  12.865 -20.114  1.00 34.82           N  
ANISOU 7602  ND2 ASN D 163     4449   4119   4661   -127    480   -280       N  
ATOM   7603  N   LEU D 164      62.255  17.777 -22.229  1.00 26.05           N  
ANISOU 7603  N   LEU D 164     3465   2956   3475   -104    654   -221       N  
ATOM   7604  CA  LEU D 164      62.762  18.756 -23.185  1.00 35.26           C  
ANISOU 7604  CA  LEU D 164     4665   4108   4626   -100    710   -213       C  
ATOM   7605  C   LEU D 164      63.223  20.049 -22.515  1.00 38.64           C  
ANISOU 7605  C   LEU D 164     5105   4500   5075   -105    741   -202       C  
ATOM   7606  O   LEU D 164      64.288  20.577 -22.845  1.00 35.60           O  
ANISOU 7606  O   LEU D 164     4727   4086   4714   -120    786   -215       O  
ATOM   7607  CB  LEU D 164      61.709  19.066 -24.245  1.00 35.45           C  
ANISOU 7607  CB  LEU D 164     4722   4164   4584    -71    719   -184       C  
ATOM   7608  CG  LEU D 164      61.475  17.867 -25.155  1.00 43.62           C  
ANISOU 7608  CG  LEU D 164     5744   5231   5598    -69    701   -202       C  
ATOM   7609  CD1 LEU D 164      60.367  18.148 -26.148  1.00 38.36           C  
ANISOU 7609  CD1 LEU D 164     5107   4602   4864    -37    704   -175       C  
ATOM   7610  CD2 LEU D 164      62.781  17.498 -25.867  1.00 42.74           C  
ANISOU 7610  CD2 LEU D 164     5623   5102   5515    -91    734   -232       C  
ATOM   7611  N   ASN D 165      62.422  20.558 -21.580  1.00 45.98           N  
ANISOU 7611  N   ASN D 165     6040   5433   5998    -94    719   -180       N  
ATOM   7612  CA  ASN D 165      62.776  21.789 -20.872  1.00 39.97           C  
ANISOU 7612  CA  ASN D 165     5290   4639   5258    -99    747   -171       C  
ATOM   7613  C   ASN D 165      64.063  21.618 -20.078  1.00 39.32           C  
ANISOU 7613  C   ASN D 165     5175   4527   5237   -129    750   -206       C  
ATOM   7614  O   ASN D 165      64.892  22.522 -20.021  1.00 40.77           O  
ANISOU 7614  O   ASN D 165     5367   4679   5446   -141    793   -214       O  
ATOM   7615  CB  ASN D 165      61.643  22.266 -19.955  1.00 36.49           C  
ANISOU 7615  CB  ASN D 165     4856   4210   4800    -83    718   -144       C  
ATOM   7616  CG  ASN D 165      60.398  22.692 -20.725  1.00 48.19           C  
ANISOU 7616  CG  ASN D 165     6372   5718   6221    -51    721   -107       C  
ATOM   7617  OD1 ASN D 165      60.468  23.036 -21.906  1.00 51.55           O  
ANISOU 7617  OD1 ASN D 165     6823   6146   6616    -39    758    -96       O  
ATOM   7618  ND2 ASN D 165      59.252  22.672 -20.053  1.00 46.89           N  
ANISOU 7618  ND2 ASN D 165     6206   5573   6036    -35    683    -88       N  
ATOM   7619  N   SER D 166      64.234  20.460 -19.457  1.00 34.48           N  
ANISOU 7619  N   SER D 166     4526   3924   4650   -142    705   -229       N  
ATOM   7620  CA  SER D 166      65.468  20.212 -18.739  1.00 35.80           C  
ANISOU 7620  CA  SER D 166     4661   4066   4875   -168    705   -264       C  
ATOM   7621  C   SER D 166      66.634  20.095 -19.717  1.00 35.33           C  
ANISOU 7621  C   SER D 166     4601   3990   4835   -183    747   -289       C  
ATOM   7622  O   SER D 166      67.746  20.523 -19.415  1.00 38.84           O  
ANISOU 7622  O   SER D 166     5033   4404   5321   -203    774   -313       O  
ATOM   7623  CB  SER D 166      65.367  18.956 -17.887  1.00 34.77           C  
ANISOU 7623  CB  SER D 166     4493   3952   4766   -174    649   -279       C  
ATOM   7624  OG  SER D 166      66.582  18.733 -17.183  1.00 30.38           O  
ANISOU 7624  OG  SER D 166     3904   3373   4264   -197    648   -312       O  
ATOM   7625  N   LEU D 167      66.378  19.508 -20.884  1.00 28.27           N  
ANISOU 7625  N   LEU D 167     3718   3114   3911   -175    752   -286       N  
ATOM   7626  CA  LEU D 167      67.427  19.350 -21.892  1.00 36.91           C  
ANISOU 7626  CA  LEU D 167     4812   4194   5019   -189    793   -310       C  
ATOM   7627  C   LEU D 167      67.911  20.726 -22.337  1.00 36.96           C  
ANISOU 7627  C   LEU D 167     4849   4171   5024   -190    854   -300       C  
ATOM   7628  O   LEU D 167      69.112  20.994 -22.375  1.00 34.35           O  
ANISOU 7628  O   LEU D 167     4508   3809   4733   -211    889   -327       O  
ATOM   7629  CB  LEU D 167      66.915  18.568 -23.105  1.00 33.62           C  
ANISOU 7629  CB  LEU D 167     4405   3806   4562   -177    789   -305       C  
ATOM   7630  CG  LEU D 167      67.944  18.368 -24.220  1.00 33.30           C  
ANISOU 7630  CG  LEU D 167     4366   3753   4532   -191    831   -329       C  
ATOM   7631  CD1 LEU D 167      69.100  17.486 -23.744  1.00 29.72           C  
ANISOU 7631  CD1 LEU D 167     3870   3283   4140   -219    818   -372       C  
ATOM   7632  CD2 LEU D 167      67.270  17.788 -25.451  1.00 27.71           C  
ANISOU 7632  CD2 LEU D 167     3675   3080   3775   -176    829   -320       C  
ATOM   7633  N   ALA D 168      66.956  21.587 -22.672  1.00 33.96           N  
ANISOU 7633  N   ALA D 168     4507   3800   4597   -166    869   -262       N  
ATOM   7634  CA  ALA D 168      67.237  22.978 -23.001  1.00 43.39           C  
ANISOU 7634  CA  ALA D 168     5734   4966   5787   -162    928   -246       C  
ATOM   7635  C   ALA D 168      68.112  23.622 -21.928  1.00 45.33           C  
ANISOU 7635  C   ALA D 168     5960   5175   6088   -184    942   -267       C  
ATOM   7636  O   ALA D 168      69.186  24.165 -22.225  1.00 46.65           O  
ANISOU 7636  O   ALA D 168     6130   5310   6287   -201    992   -286       O  
ATOM   7637  CB  ALA D 168      65.941  23.746 -23.167  1.00 36.53           C  
ANISOU 7637  CB  ALA D 168     4901   4114   4865   -131    929   -200       C  
ATOM   7638  N   ASP D 169      67.654  23.550 -20.682  1.00 39.65           N  
ANISOU 7638  N   ASP D 169     5221   4463   5381   -184    899   -265       N  
ATOM   7639  CA  ASP D 169      68.401  24.079 -19.546  1.00 38.48           C  
ANISOU 7639  CA  ASP D 169     5050   4286   5283   -204    903   -288       C  
ATOM   7640  C   ASP D 169      69.827  23.530 -19.465  1.00 42.19           C  
ANISOU 7640  C   ASP D 169     5485   4737   5806   -233    912   -335       C  
ATOM   7641  O   ASP D 169      70.791  24.275 -19.330  1.00 44.34           O  
ANISOU 7641  O   ASP D 169     5755   4977   6117   -250    954   -356       O  
ATOM   7642  CB  ASP D 169      67.650  23.766 -18.249  1.00 48.99           C  
ANISOU 7642  CB  ASP D 169     6361   5637   6615   -199    845   -281       C  
ATOM   7643  CG  ASP D 169      68.392  24.235 -17.002  1.00 59.38           C  
ANISOU 7643  CG  ASP D 169     7651   6930   7981   -219    844   -307       C  
ATOM   7644  OD1 ASP D 169      67.713  24.690 -16.057  1.00 78.11           O  
ANISOU 7644  OD1 ASP D 169    10024   9308  10348   -211    823   -292       O  
ATOM   7645  OD2 ASP D 169      69.642  24.143 -16.952  1.00 63.13           O  
ANISOU 7645  OD2 ASP D 169     8102   7383   8501   -242    864   -344       O  
ATOM   7646  N   VAL D 170      69.962  22.217 -19.531  1.00 39.58           N  
ANISOU 7646  N   VAL D 170     5129   4427   5484   -238    873   -352       N  
ATOM   7647  CA  VAL D 170      71.264  21.611 -19.349  1.00 40.97           C  
ANISOU 7647  CA  VAL D 170     5268   4586   5712   -263    874   -396       C  
ATOM   7648  C   VAL D 170      72.255  21.967 -20.461  1.00 42.95           C  
ANISOU 7648  C   VAL D 170     5531   4812   5976   -276    935   -414       C  
ATOM   7649  O   VAL D 170      73.416  22.285 -20.183  1.00 37.18           O  
ANISOU 7649  O   VAL D 170     4781   4052   5293   -298    962   -447       O  
ATOM   7650  CB  VAL D 170      71.136  20.100 -19.177  1.00 37.69           C  
ANISOU 7650  CB  VAL D 170     4821   4196   5301   -264    819   -408       C  
ATOM   7651  CG1 VAL D 170      72.485  19.439 -19.310  1.00 36.91           C  
ANISOU 7651  CG1 VAL D 170     4690   4082   5252   -287    828   -452       C  
ATOM   7652  CG2 VAL D 170      70.509  19.800 -17.819  1.00 31.52           C  
ANISOU 7652  CG2 VAL D 170     4020   3432   4524   -257    763   -400       C  
ATOM   7653  N   THR D 171      71.793  21.937 -21.710  1.00 42.19           N  
ANISOU 7653  N   THR D 171     5468   4728   5837   -262    958   -392       N  
ATOM   7654  CA  THR D 171      72.672  22.201 -22.851  1.00 42.66           C  
ANISOU 7654  CA  THR D 171     5541   4764   5902   -273   1017   -406       C  
ATOM   7655  C   THR D 171      73.022  23.681 -22.990  1.00 42.77           C  
ANISOU 7655  C   THR D 171     5583   4744   5923   -275   1080   -397       C  
ATOM   7656  O   THR D 171      74.151  24.020 -23.319  1.00 39.49           O  
ANISOU 7656  O   THR D 171     5163   4297   5543   -295   1127   -425       O  
ATOM   7657  CB  THR D 171      72.092  21.665 -24.181  1.00 37.97           C  
ANISOU 7657  CB  THR D 171     4972   4197   5257   -256   1022   -387       C  
ATOM   7658  OG1 THR D 171      70.821  22.278 -24.443  1.00 32.73           O  
ANISOU 7658  OG1 THR D 171     4347   3554   4536   -227   1021   -341       O  
ATOM   7659  CG2 THR D 171      71.929  20.139 -24.121  1.00 39.71           C  
ANISOU 7659  CG2 THR D 171     5160   4447   5480   -259    967   -405       C  
ATOM   7660  N   GLU D 172      72.055  24.554 -22.730  1.00 50.68           N  
ANISOU 7660  N   GLU D 172     6614   5750   6892   -254   1083   -360       N  
ATOM   7661  CA  GLU D 172      72.317  25.988 -22.709  1.00 56.63           C  
ANISOU 7661  CA  GLU D 172     7393   6469   7656   -256   1142   -350       C  
ATOM   7662  C   GLU D 172      73.360  26.342 -21.651  1.00 55.66           C  
ANISOU 7662  C   GLU D 172     7235   6316   7599   -284   1149   -390       C  
ATOM   7663  O   GLU D 172      74.213  27.207 -21.863  1.00 52.63           O  
ANISOU 7663  O   GLU D 172     6858   5894   7245   -299   1208   -406       O  
ATOM   7664  CB  GLU D 172      71.021  26.779 -22.508  1.00 50.28           C  
ANISOU 7664  CB  GLU D 172     6622   5677   6807   -228   1136   -302       C  
ATOM   7665  CG  GLU D 172      70.296  27.058 -23.821  1.00 55.60           C  
ANISOU 7665  CG  GLU D 172     7342   6364   7420   -201   1165   -262       C  
ATOM   7666  CD  GLU D 172      68.792  27.200 -23.661  1.00 59.66           C  
ANISOU 7666  CD  GLU D 172     7877   6909   7881   -169   1130   -218       C  
ATOM   7667  OE1 GLU D 172      68.336  27.684 -22.602  1.00 69.12           O  
ANISOU 7667  OE1 GLU D 172     9069   8103   9089   -166   1110   -209       O  
ATOM   7668  OE2 GLU D 172      68.059  26.817 -24.597  1.00 59.65           O  
ANISOU 7668  OE2 GLU D 172     7898   6938   7826   -146   1122   -193       O  
ATOM   7669  N   ARG D 173      73.304  25.657 -20.519  1.00 56.85           N  
ANISOU 7669  N   ARG D 173     7348   6483   7771   -290   1090   -408       N  
ATOM   7670  CA  ARG D 173      74.259  25.910 -19.456  1.00 54.48           C  
ANISOU 7670  CA  ARG D 173     7010   6160   7529   -315   1089   -448       C  
ATOM   7671  C   ARG D 173      75.650  25.454 -19.878  1.00 60.63           C  
ANISOU 7671  C   ARG D 173     7763   6919   8354   -340   1114   -494       C  
ATOM   7672  O   ARG D 173      76.629  26.171 -19.677  1.00 65.32           O  
ANISOU 7672  O   ARG D 173     8347   7480   8992   -360   1156   -524       O  
ATOM   7673  CB  ARG D 173      73.831  25.207 -18.166  1.00 55.28           C  
ANISOU 7673  CB  ARG D 173     7079   6288   7639   -312   1017   -453       C  
ATOM   7674  CG  ARG D 173      74.610  25.646 -16.940  1.00 66.37           C  
ANISOU 7674  CG  ARG D 173     8448   7675   9095   -332   1014   -489       C  
ATOM   7675  CD  ARG D 173      74.507  24.617 -15.827  1.00 72.43           C  
ANISOU 7675  CD  ARG D 173     9175   8470   9875   -333    942   -503       C  
ATOM   7676  NE  ARG D 173      75.052  23.324 -16.235  1.00 71.96           N  
ANISOU 7676  NE  ARG D 173     9091   8422   9828   -339    918   -523       N  
ATOM   7677  CZ  ARG D 173      74.338  22.206 -16.334  1.00 70.51           C  
ANISOU 7677  CZ  ARG D 173     8904   8269   9617   -325    869   -505       C  
ATOM   7678  NH1 ARG D 173      73.043  22.215 -16.041  1.00 66.14           N  
ANISOU 7678  NH1 ARG D 173     8370   7739   9021   -304    838   -467       N  
ATOM   7679  NH2 ARG D 173      74.925  21.077 -16.715  1.00 69.79           N  
ANISOU 7679  NH2 ARG D 173     8789   8183   9544   -333    853   -527       N  
ATOM   7680  N   LEU D 174      75.737  24.261 -20.463  1.00 45.99           N  
ANISOU 7680  N   LEU D 174     5897   5085   6490   -339   1088   -500       N  
ATOM   7681  CA  LEU D 174      77.021  23.725 -20.924  1.00 45.45           C  
ANISOU 7681  CA  LEU D 174     5804   5000   6464   -363   1109   -543       C  
ATOM   7682  C   LEU D 174      77.610  24.591 -22.033  1.00 50.66           C  
ANISOU 7682  C   LEU D 174     6494   5627   7125   -370   1188   -545       C  
ATOM   7683  O   LEU D 174      78.832  24.631 -22.231  1.00 44.63           O  
ANISOU 7683  O   LEU D 174     5712   4837   6408   -394   1223   -585       O  
ATOM   7684  CB  LEU D 174      76.867  22.287 -21.432  1.00 50.63           C  
ANISOU 7684  CB  LEU D 174     6447   5685   7106   -358   1069   -546       C  
ATOM   7685  CG  LEU D 174      76.506  21.173 -20.443  1.00 48.17           C  
ANISOU 7685  CG  LEU D 174     6099   5402   6802   -354    994   -552       C  
ATOM   7686  CD1 LEU D 174      76.278  19.874 -21.193  1.00 45.59           C  
ANISOU 7686  CD1 LEU D 174     5766   5099   6457   -349    967   -551       C  
ATOM   7687  CD2 LEU D 174      77.584  20.999 -19.377  1.00 46.45           C  
ANISOU 7687  CD2 LEU D 174     5833   5169   6646   -375    977   -595       C  
ATOM   7688  N   GLN D 175      76.721  25.264 -22.762  1.00 40.87           N  
ANISOU 7688  N   GLN D 175     5304   4392   5835   -348   1216   -500       N  
ATOM   7689  CA  GLN D 175      77.099  26.153 -23.855  1.00 50.93           C  
ANISOU 7689  CA  GLN D 175     6614   5636   7100   -349   1293   -492       C  
ATOM   7690  C   GLN D 175      77.803  27.409 -23.336  1.00 54.30           C  
ANISOU 7690  C   GLN D 175     7040   6020   7571   -366   1345   -509       C  
ATOM   7691  O   GLN D 175      78.907  27.730 -23.769  1.00 58.63           O  
ANISOU 7691  O   GLN D 175     7584   6536   8158   -387   1399   -540       O  
ATOM   7692  CB  GLN D 175      75.868  26.532 -24.675  1.00 41.81           C  
ANISOU 7692  CB  GLN D 175     5510   4500   5874   -317   1304   -436       C  
ATOM   7693  CG  GLN D 175      76.095  27.675 -25.647  1.00 52.86           C  
ANISOU 7693  CG  GLN D 175     6954   5869   7261   -312   1385   -417       C  
ATOM   7694  CD  GLN D 175      76.942  27.273 -26.842  1.00 56.37           C  
ANISOU 7694  CD  GLN D 175     7404   6304   7709   -324   1426   -436       C  
ATOM   7695  OE1 GLN D 175      76.923  27.940 -27.874  1.00 58.64           O  
ANISOU 7695  OE1 GLN D 175     7733   6578   7970   -314   1486   -412       O  
ATOM   7696  NE2 GLN D 175      77.690  26.182 -26.708  1.00 49.25           N  
ANISOU 7696  NE2 GLN D 175     6461   5410   6843   -345   1397   -478       N  
ATOM   7697  N   ALA D 176      77.158  28.111 -22.408  1.00 51.00           N  
ANISOU 7697  N   ALA D 176     6626   5602   7149   -357   1330   -492       N  
ATOM   7698  CA  ALA D 176      77.781  29.245 -21.735  1.00 52.42           C  
ANISOU 7698  CA  ALA D 176     6798   5744   7375   -374   1372   -513       C  
ATOM   7699  C   ALA D 176      79.050  28.794 -21.030  1.00 63.71           C  
ANISOU 7699  C   ALA D 176     8174   7162   8871   -405   1360   -575       C  
ATOM   7700  O   ALA D 176      80.073  29.483 -21.071  1.00 60.14           O  
ANISOU 7700  O   ALA D 176     7713   6672   8465   -427   1416   -608       O  
ATOM   7701  CB  ALA D 176      76.822  29.867 -20.737  1.00 47.52           C  
ANISOU 7701  CB  ALA D 176     6184   5133   6739   -359   1345   -488       C  
ATOM   7702  N   GLU D 177      78.978  27.633 -20.381  1.00 75.88           N  
ANISOU 7702  N   GLU D 177     9679   8736  10417   -406   1289   -589       N  
ATOM   7703  CA  GLU D 177      80.128  27.084 -19.670  1.00 75.23           C  
ANISOU 7703  CA  GLU D 177     9543   8648  10394   -431   1269   -645       C  
ATOM   7704  C   GLU D 177      81.308  26.837 -20.608  1.00 80.18           C  
ANISOU 7704  C   GLU D 177    10162   9251  11053   -451   1315   -680       C  
ATOM   7705  O   GLU D 177      82.435  26.641 -20.154  1.00 81.86           O  
ANISOU 7705  O   GLU D 177    10333   9450  11321   -475   1317   -731       O  
ATOM   7706  CB  GLU D 177      79.750  25.798 -18.919  1.00 77.08           C  
ANISOU 7706  CB  GLU D 177     9743   8922  10621   -423   1184   -648       C  
ATOM   7707  CG  GLU D 177      78.966  26.032 -17.622  1.00 80.50           C  
ANISOU 7707  CG  GLU D 177    10168   9375  11045   -412   1136   -633       C  
ATOM   7708  CD  GLU D 177      78.563  24.741 -16.920  1.00 80.09           C  
ANISOU 7708  CD  GLU D 177    10086   9361  10985   -403   1056   -631       C  
ATOM   7709  OE1 GLU D 177      78.021  23.835 -17.589  1.00 75.84           O  
ANISOU 7709  OE1 GLU D 177     9559   8844  10413   -390   1033   -609       O  
ATOM   7710  OE2 GLU D 177      78.784  24.632 -15.695  1.00 88.12           O  
ANISOU 7710  OE2 GLU D 177    11066  10386  12028   -409   1018   -653       O  
ATOM   7711  N   SER D 178      81.049  26.850 -21.916  1.00 64.07           N  
ANISOU 7711  N   SER D 178     8162   7207   8976   -442   1353   -653       N  
ATOM   7712  CA  SER D 178      82.110  26.641 -22.900  1.00 74.77           C  
ANISOU 7712  CA  SER D 178     9513   8539  10355   -460   1401   -682       C  
ATOM   7713  C   SER D 178      82.678  27.962 -23.435  1.00 79.64           C  
ANISOU 7713  C   SER D 178    10158   9110  10992   -471   1490   -687       C  
ATOM   7714  O   SER D 178      83.829  28.014 -23.878  1.00 78.91           O  
ANISOU 7714  O   SER D 178    10052   8990  10942   -495   1535   -726       O  
ATOM   7715  CB  SER D 178      81.626  25.761 -24.058  1.00 65.90           C  
ANISOU 7715  CB  SER D 178     8414   7441   9184   -445   1391   -657       C  
ATOM   7716  OG  SER D 178      80.716  26.457 -24.893  1.00 64.16           O  
ANISOU 7716  OG  SER D 178     8249   7222   8907   -422   1426   -605       O  
ATOM   7717  N   MET D 179      81.869  29.022 -23.385  1.00 87.33           N  
ANISOU 7717  N   MET D 179    11170  10076  11936   -455   1515   -647       N  
ATOM   7718  CA  MET D 179      82.313  30.353 -23.806  1.00 97.12           C  
ANISOU 7718  CA  MET D 179    12437  11269  13194   -463   1601   -647       C  
ATOM   7719  C   MET D 179      83.502  30.833 -22.977  1.00102.08           C  
ANISOU 7719  C   MET D 179    13023  11865  13899   -495   1625   -706       C  
ATOM   7720  O   MET D 179      84.053  31.902 -23.231  1.00107.47           O  
ANISOU 7720  O   MET D 179    13720  12504  14609   -508   1699   -718       O  
ATOM   7721  CB  MET D 179      81.171  31.374 -23.719  1.00 92.47           C  
ANISOU 7721  CB  MET D 179    11892  10679  12563   -438   1616   -594       C  
ATOM   7722  CG  MET D 179      80.060  31.172 -24.744  1.00 95.07           C  
ANISOU 7722  CG  MET D 179    12270  11035  12818   -405   1612   -534       C  
ATOM   7723  SD  MET D 179      80.690  30.731 -26.378  1.00113.39           S  
ANISOU 7723  SD  MET D 179    14614  13347  15122   -408   1663   -536       S  
ATOM   7724  CE  MET D 179      79.304  31.184 -27.428  1.00 96.82           C  
ANISOU 7724  CE  MET D 179    12583  11269  12936   -365   1681   -459       C  
ATOM   7725  N   GLU D 180      83.890  30.038 -21.985  1.00101.07           N  
ANISOU 7725  N   GLU D 180    12843  11758  13803   -507   1563   -745       N  
ATOM   7726  CA  GLU D 180      85.018  30.366 -21.124  1.00 98.55           C  
ANISOU 7726  CA  GLU D 180    12477  11415  13554   -537   1575   -805       C  
ATOM   7727  C   GLU D 180      85.676  29.095 -20.599  1.00 99.62           C  
ANISOU 7727  C   GLU D 180    12557  11575  13719   -548   1513   -848       C  
ATOM   7728  O   GLU D 180      86.838  29.106 -20.199  1.00 99.45           O  
ANISOU 7728  O   GLU D 180    12493  11536  13758   -574   1525   -905       O  
ATOM   7729  CB  GLU D 180      84.561  31.243 -19.955  1.00 99.26           C  
ANISOU 7729  CB  GLU D 180    12560  11503  13652   -534   1564   -802       C  
ATOM   7730  CG  GLU D 180      83.754  32.470 -20.372  1.00104.07           C  
ANISOU 7730  CG  GLU D 180    13223  12090  14229   -518   1618   -755       C  
ATOM   7731  CD  GLU D 180      83.872  33.613 -19.387  1.00 95.93           C  
ANISOU 7731  CD  GLU D 180    12179  11035  13234   -529   1642   -774       C  
ATOM   7732  OE1 GLU D 180      83.182  34.639 -19.579  1.00 91.85           O  
ANISOU 7732  OE1 GLU D 180    11704  10501  12695   -516   1683   -736       O  
ATOM   7733  OE2 GLU D 180      84.661  33.490 -18.425  1.00 93.37           O  
ANISOU 7733  OE2 GLU D 180    11804  10712  12961   -551   1620   -829       O  
TER    7734      GLU D 180                                                      
HETATM 7735 MG    MG A 512      20.882   7.962  23.571  1.00 16.64          MG  
ANISOU 7735 MG    MG A 512     2165   1952   2207    -26    -41    242      MG  
HETATM 7736 MG    MG B 512      56.746   8.446   1.763  1.00 19.85          MG  
ANISOU 7736 MG    MG B 512     2338   2246   2959    -79    -19   -109      MG  
HETATM 7737  O   HOH A 513       9.087  14.937  27.498  1.00 11.06           O  
ANISOU 7737  O   HOH A 513     1471   1278   1454    -77     42    129       O  
HETATM 7738  O   HOH A 514      25.587  15.997  19.433  0.99 16.93           O  
ANISOU 7738  O   HOH A 514     2224   2058   2152    -10   -100    191       O  
HETATM 7739  O   HOH A 515      24.081  10.789  21.381  1.00 20.65           O  
ANISOU 7739  O   HOH A 515     2675   2497   2676    -15    -89    224       O  
HETATM 7740  O   HOH A 516      14.969  19.299  12.297  1.00 15.90           O  
ANISOU 7740  O   HOH A 516     2052   2000   1990     98    -92     90       O  
HETATM 7741  O   HOH A 517      23.468  11.091  24.804  1.00 20.92           O  
ANISOU 7741  O   HOH A 517     2732   2541   2675    -23    -80    259       O  
HETATM 7742  O   HOH A 518      12.140  13.646   8.166  1.00 17.01           O  
ANISOU 7742  O   HOH A 518     2073   2206   2182    113   -123    -45       O  
HETATM 7743  O   HOH A 519      11.761  11.220  14.393  1.00 17.37           O  
ANISOU 7743  O   HOH A 519     2139   2144   2317     22    -62      0       O  
HETATM 7744  O   HOH A 520      17.681   8.930  -1.461  1.00 15.09           O  
ANISOU 7744  O   HOH A 520     1755   2073   1905    146   -151   -164       O  
HETATM 7745  O   HOH A 521      23.878  12.141  -1.355  1.00 20.68           O  
ANISOU 7745  O   HOH A 521     2583   2705   2570    142   -120    -27       O  
HETATM 7746  O   HOH A 522      34.996  10.288  17.376  1.00 21.38           O  
ANISOU 7746  O   HOH A 522     2721   2587   2815      2   -148    205       O  
HETATM 7747  O   HOH A 523      21.034  12.382  24.980  1.00 22.53           O  
ANISOU 7747  O   HOH A 523     2942   2749   2871    -33    -63    237       O  
HETATM 7748  O   HOH A 524      17.879   5.749  -5.058  1.00 24.35           O  
ANISOU 7748  O   HOH A 524     2842   3314   3096    140   -153   -289       O  
HETATM 7749  O   HOH A 525      17.347   9.321  23.237  1.00 23.79           O  
ANISOU 7749  O   HOH A 525     3063   2864   3112    -37    -21    196       O  
HETATM 7750  O   HOH A 526      13.566  21.591  28.338  0.81 13.06           O  
ANISOU 7750  O   HOH A 526     1774   1585   1605    -71      0    154       O  
HETATM 7751  O   HOH A 527      19.907   2.047  -3.998  0.87 21.96           O  
ANISOU 7751  O   HOH A 527     2502   2916   2926     66   -108   -316       O  
HETATM 7752  O   HOH A 528      18.219  16.301  31.471  1.00 25.71           O  
ANISOU 7752  O   HOH A 528     3395   3202   3170    -73    -27    246       O  
HETATM 7753  O   HOH A 529      30.398  14.526  18.133  1.00 21.04           O  
ANISOU 7753  O   HOH A 529     2724   2569   2700     -8   -122    192       O  
HETATM 7754  O   HOH A 530      31.068  19.885  14.221  0.91 15.79           O  
ANISOU 7754  O   HOH A 530     2092   1901   2008      5    -75    157       O  
HETATM 7755  O   HOH A 531       8.241  29.973  23.490  1.00 21.00           O  
ANISOU 7755  O   HOH A 531     2758   2570   2651     23     40     96       O  
HETATM 7756  O   HOH A 532      24.321  21.040  -4.382  1.00 30.76           O  
ANISOU 7756  O   HOH A 532     4013   4012   3661    282    -59    119       O  
HETATM 7757  O   HOH A 533      13.982  15.510  24.488  1.00 17.69           O  
ANISOU 7757  O   HOH A 533     2317   2140   2265    -43    -22    158       O  
HETATM 7758  O   HOH A 534      11.354  13.097  10.719  1.00 24.16           O  
ANISOU 7758  O   HOH A 534     2983   3074   3124     79   -101    -35       O  
HETATM 7759  O   HOH A 535      32.294  26.380  15.639  0.88 20.13           O  
ANISOU 7759  O   HOH A 535     2675   2424   2549    -15      4    134       O  
HETATM 7760  O   HOH A 536      12.423  14.813  32.792  1.00 27.03           O  
ANISOU 7760  O   HOH A 536     3562   3322   3385    -98     51    226       O  
HETATM 7761  O   HOH A 537      12.131  20.077  37.671  0.96 19.98           O  
ANISOU 7761  O   HOH A 537     2706   2507   2380   -142     68    200       O  
HETATM 7762  O   HOH A 538      35.640  14.816  22.880  1.00 24.01           O  
ANISOU 7762  O   HOH A 538     3080   2996   3049    -14   -167    207       O  
HETATM 7763  O   HOH A 539      37.519  30.877   4.117  1.00 38.00           O  
ANISOU 7763  O   HOH A 539     5039   4571   4828     68    217    165       O  
HETATM 7764  O   HOH A 540      32.772  19.618  16.642  1.00 33.02           O  
ANISOU 7764  O   HOH A 540     4263   4089   4195    -15    -89    156       O  
HETATM 7765  O   HOH A 541      11.148  18.956  35.404  1.00 24.83           O  
ANISOU 7765  O   HOH A 541     3302   3084   3048   -129     67    192       O  
HETATM 7766  O   HOH A 542      16.677   8.032  -3.825  1.00 22.78           O  
ANISOU 7766  O   HOH A 542     2681   3116   2857    168   -165   -236       O  
HETATM 7767  O   HOH A 543       7.769  18.566  21.460  1.00 21.93           O  
ANISOU 7767  O   HOH A 543     2801   2707   2826     -2    -18     57       O  
HETATM 7768  O   HOH A 544      18.676   8.066  24.588  1.00 32.51           O  
ANISOU 7768  O   HOH A 544     4179   3956   4218    -37    -16    235       O  
HETATM 7769  O   HOH A 545      16.022  25.620  26.717  1.00 19.96           O  
ANISOU 7769  O   HOH A 545     2656   2462   2465    -58     -1    142       O  
HETATM 7770  O   HOH A 546      31.096  12.142  29.986  1.00 30.00           O  
ANISOU 7770  O   HOH A 546     3884   3796   3717      4   -162    316       O  
HETATM 7771  O   HOH A 547      25.126  13.940  -2.544  1.00 40.47           O  
ANISOU 7771  O   HOH A 547     5126   5218   5032    165   -108      3       O  
HETATM 7772  O   HOH A 548       9.280  14.949  10.678  1.00 29.91           O  
ANISOU 7772  O   HOH A 548     3708   3828   3829    105   -109    -46       O  
HETATM 7773  O   HOH A 549      25.149   3.469  -9.314  1.00 32.61           O  
ANISOU 7773  O   HOH A 549     3901   4334   4157    101   -110   -305       O  
HETATM 7774  O   HOH A 550      14.807   6.113  25.930  1.00 35.03           O  
ANISOU 7774  O   HOH A 550     4488   4231   4592    -58     54    218       O  
HETATM 7775  O   HOH A 551       9.012  26.584  11.917  1.00 24.64           O  
ANISOU 7775  O   HOH A 551     3174   3138   3050    206    -68    102       O  
HETATM 7776  O   HOH A 552      32.503  10.924  -3.751  1.00 23.06           O  
ANISOU 7776  O   HOH A 552     2909   2926   2927     87    -66    -16       O  
HETATM 7777  O   HOH A 553       9.870   9.642  17.600  1.00 47.77           O  
ANISOU 7777  O   HOH A 553     5987   5945   6217    -18    -13      3       O  
HETATM 7778  O   HOH A 554      14.825  23.996  28.767  1.00 25.69           O  
ANISOU 7778  O   HOH A 554     3383   3195   3185    -77      3    148       O  
HETATM 7779  O   HOH A 555      12.269   8.723  15.594  1.00 24.80           O  
ANISOU 7779  O   HOH A 555     3072   3043   3308     -6    -35      7       O  
HETATM 7780  O   HOH A 556      21.155  24.248  27.249  0.86 26.08           O  
ANISOU 7780  O   HOH A 556     3431   3258   3218    -69    -35    161       O  
HETATM 7781  O   HOH A 557      26.019   5.839  -5.627  0.92 26.32           O  
ANISOU 7781  O   HOH A 557     3183   3449   3370     95   -108   -178       O  
HETATM 7782  O   HOH A 558      23.911  11.516  -5.892  1.00 29.18           O  
ANISOU 7782  O   HOH A 558     3634   3874   3580    186   -127    -88       O  
HETATM 7783  O   HOH A 559      34.770  25.231  25.646  0.95 30.61           O  
ANISOU 7783  O   HOH A 559     3936   3869   3824    -87    -80     83       O  
HETATM 7784  O   HOH A 560       9.829  22.745  34.716  1.00 23.55           O  
ANISOU 7784  O   HOH A 560     3127   2927   2894   -136     73    138       O  
HETATM 7785  O   HOH A 561       6.513  15.873  21.385  1.00 26.56           O  
ANISOU 7785  O   HOH A 561     3355   3281   3456    -17     -4     27       O  
HETATM 7786  O   HOH A 562      18.403  -0.955  21.924  1.00 35.58           O  
ANISOU 7786  O   HOH A 562     4482   4200   4839    -42     92    211       O  
HETATM 7787  O   HOH A 563      40.385   7.714  11.322  0.93 24.98           O  
ANISOU 7787  O   HOH A 563     3116   2998   3377     -1   -136    136       O  
HETATM 7788  O   HOH A 564      12.465  19.167   1.747  1.00 32.40           O  
ANISOU 7788  O   HOH A 564     4070   4287   3953    277   -163     -3       O  
HETATM 7789  O   HOH A 565       8.303  17.964  29.632  0.96 38.40           O  
ANISOU 7789  O   HOH A 565     4957   4758   4876    -92     53    127       O  
HETATM 7790  O   HOH A 566      32.039  13.512  -2.877  1.00 31.60           O  
ANISOU 7790  O   HOH A 566     4033   4002   3970    106    -58     29       O  
HETATM 7791  O   HOH A 567      32.018   2.449  -5.423  1.00 26.42           O  
ANISOU 7791  O   HOH A 567     3174   3342   3522     22    -64   -176       O  
HETATM 7792  O   HOH A 568      20.308  -4.779   5.760  1.00 30.49           O  
ANISOU 7792  O   HOH A 568     3581   3668   4337    -57     42   -188       O  
HETATM 7793  O   HOH A 569      13.200   3.214  11.495  1.00 32.96           O  
ANISOU 7793  O   HOH A 569     4006   4062   4457    -20    -11    -99       O  
HETATM 7794  O   HOH A 570       6.137  16.279  16.772  1.00 38.21           O  
ANISOU 7794  O   HOH A 570     4786   4813   4920     45    -52    -23       O  
HETATM 7795  O   HOH A 571      40.780  13.394  -0.801  1.00 31.95           O  
ANISOU 7795  O   HOH A 571     4075   3920   4146     21    -12     35       O  
HETATM 7796  O   HOH A 572      37.666  -1.023  13.618  1.00 44.30           O  
ANISOU 7796  O   HOH A 572     5507   5348   5976     23   -101    207       O  
HETATM 7797  O   HOH A 573      36.936   6.041  -2.126  0.95 26.11           O  
ANISOU 7797  O   HOH A 573     3225   3215   3479     13    -60    -45       O  
HETATM 7798  O   HOH A 574      10.371  10.989  11.880  1.00 30.43           O  
ANISOU 7798  O   HOH A 574     3751   3841   3971     48    -79    -61       O  
HETATM 7799  O   HOH A 575      40.293  22.106  32.305  0.89 27.43           O  
ANISOU 7799  O   HOH A 575     3445   3651   3326    -65   -212     57       O  
HETATM 7800  O   HOH A 576      30.504  -3.724  21.162  1.00 33.77           O  
ANISOU 7800  O   HOH A 576     4244   3957   4630     42    -11    353       O  
HETATM 7801  O   HOH A 577      22.686  -0.326  -9.083  1.00 28.41           O  
ANISOU 7801  O   HOH A 577     3257   3802   3734     58    -95   -432       O  
HETATM 7802  O   HOH A 578       5.870  26.211  18.472  1.00 31.15           O  
ANISOU 7802  O   HOH A 578     3982   3909   3942    101    -27     63       O  
HETATM 7803  O   HOH A 579      25.797  10.748  -3.942  1.00 32.60           O  
ANISOU 7803  O   HOH A 579     4076   4234   4078    139   -112    -63       O  
HETATM 7804  O   HOH A 580      16.242  -1.775  -8.553  1.00 42.38           O  
ANISOU 7804  O   HOH A 580     4904   5653   5548     62   -108   -589       O  
HETATM 7805  O   HOH A 581      33.337   6.566  35.888  1.00 37.46           O  
ANISOU 7805  O   HOH A 581     4850   4795   4586    106   -188    491       O  
HETATM 7806  O   HOH A 582      35.937  23.476  10.015  0.92 24.46           O  
ANISOU 7806  O   HOH A 582     3215   2954   3125      9      5    128       O  
HETATM 7807  O   HOH A 583       1.668  31.151  15.094  1.00 29.44           O  
ANISOU 7807  O   HOH A 583     3742   3734   3712    247    -31     63       O  
HETATM 7808  O   HOH A 584       2.052  33.280  25.166  1.00 25.76           O  
ANISOU 7808  O   HOH A 584     3323   3155   3310     40     92     40       O  
HETATM 7809  O   HOH A 585      12.306  11.281   6.340  1.00 31.85           O  
ANISOU 7809  O   HOH A 585     3907   4106   4087    109   -127   -100       O  
HETATM 7810  O   HOH A 586      23.290  -4.565   1.641  0.96 31.78           O  
ANISOU 7810  O   HOH A 586     3722   3891   4462    -46      7   -241       O  
HETATM 7811  O   HOH A 587      14.208  32.694  13.361  1.00 38.60           O  
ANISOU 7811  O   HOH A 587     5047   4798   4821    184     40    195       O  
HETATM 7812  O   HOH A 588      27.145   7.805  25.644  1.00 47.62           O  
ANISOU 7812  O   HOH A 588     6102   5908   6082      1    -98    316       O  
HETATM 7813  O   HOH A 589      10.384  17.424  10.504  1.00 30.76           O  
ANISOU 7813  O   HOH A 589     3857   3937   3892    129   -113      1       O  
HETATM 7814  O   HOH A 590      16.398  -7.026  -4.156  0.99 33.16           O  
ANISOU 7814  O   HOH A 590     3683   4253   4664    -56     19   -598       O  
HETATM 7815  O   HOH A 591      25.738  34.120  16.260  0.86 30.14           O  
ANISOU 7815  O   HOH A 591     4003   3639   3810     29    126    159       O  
HETATM 7816  O   HOH A 592      32.061   6.366  38.566  1.00 43.66           O  
ANISOU 7816  O   HOH A 592     5668   5613   5307    120   -171    536       O  
HETATM 7817  O   HOH A 593      30.071  31.344  17.826  1.00 48.18           O  
ANISOU 7817  O   HOH A 593     6251   5952   6103    -28     77    119       O  
HETATM 7818  O   HOH A 594      10.479  32.366  16.695  1.00 42.04           O  
ANISOU 7818  O   HOH A 594     5448   5241   5286    149     31    153       O  
HETATM 7819  O   HOH A 595       7.196  19.283  19.052  1.00 30.85           O  
ANISOU 7819  O   HOH A 595     3910   3862   3949     35    -39     35       O  
HETATM 7820  O   HOH A 596      29.263  -7.697  10.131  1.00 32.51           O  
ANISOU 7820  O   HOH A 596     3911   3754   4686    -35     58     56       O  
HETATM 7821  O   HOH A 597      44.538  16.619  29.752  1.00 38.16           O  
ANISOU 7821  O   HOH A 597     4760   4980   4758      6   -282    120       O  
HETATM 7822  O   HOH A 598       9.124  35.846  17.450  1.00 40.35           O  
ANISOU 7822  O   HOH A 598     5245   4991   5094    169     83    164       O  
HETATM 7823  O   HOH A 599      24.392   0.973 -10.541  1.00 42.81           O  
ANISOU 7823  O   HOH A 599     5120   5652   5495     79   -102   -402       O  
HETATM 7824  O   HOH A 600      33.978  12.796  17.755  1.00 43.39           O  
ANISOU 7824  O   HOH A 600     5530   5392   5564     -5   -140    194       O  
HETATM 7825  O   HOH A 601      10.373  10.759  19.737  0.98 33.75           O  
ANISOU 7825  O   HOH A 601     4251   4158   4416    -28     -7     49       O  
HETATM 7826  O   HOH A 602      23.967   8.381  30.501  1.00 29.60           O  
ANISOU 7826  O   HOH A 602     3868   3648   3730     -9    -59    363       O  
HETATM 7827  O   HOH A 603      32.881  29.793  32.410  1.00 33.84           O  
ANISOU 7827  O   HOH A 603     4327   4372   4157   -151    -46     -8       O  
HETATM 7828  O   HOH A 604      29.094  28.525  30.117  1.00 37.15           O  
ANISOU 7828  O   HOH A 604     4795   4726   4595   -122    -32     68       O  
HETATM 7829  O   HOH A 605      16.545  14.178  -7.036  0.92 32.92           O  
ANISOU 7829  O   HOH A 605     4068   4510   3932    313   -193   -130       O  
HETATM 7830  O   HOH A 606      19.646  -5.935   8.174  1.00 37.14           O  
ANISOU 7830  O   HOH A 606     4433   4447   5231    -70     83   -147       O  
HETATM 7831  O   HOH A 607      23.202  29.209  29.584  1.00 46.21           O  
ANISOU 7831  O   HOH A 607     5977   5826   5753   -110      8    100       O  
HETATM 7832  O   HOH A 608      31.234  19.368  18.567  0.85 40.29           O  
ANISOU 7832  O   HOH A 608     5186   5020   5101    -20    -97    168       O  
HETATM 7833  O   HOH A 609      37.403   2.705   0.649  1.00 46.95           O  
ANISOU 7833  O   HOH A 609     5820   5794   6226    -11    -67    -32       O  
HETATM 7834  O   HOH A 610      11.930  13.139   4.124  1.00 41.36           O  
ANISOU 7834  O   HOH A 610     5117   5371   5227    163   -152   -103       O  
HETATM 7835  O   HOH A 611       9.922  28.984   8.093  0.91 30.85           O  
ANISOU 7835  O   HOH A 611     3993   3953   3776    301    -64    150       O  
HETATM 7836  O   HOH A 612      31.198   3.977 -10.561  0.92 36.66           O  
ANISOU 7836  O   HOH A 612     4474   4774   4682     74    -66   -245       O  
HETATM 7837  O   HOH A 613      32.173  14.068  -0.563  0.68 23.61           O  
ANISOU 7837  O   HOH A 613     3029   2959   2981     89    -62     54       O  
HETATM 7838  O   HOH A 614       8.856  31.496  12.464  1.00 47.82           O  
ANISOU 7838  O   HOH A 614     6158   6030   5980    244    -13    157       O  
HETATM 7839  O   HOH A 615      25.991  24.753  42.916  1.00 44.75           O  
ANISOU 7839  O   HOH A 615     5785   5930   5288   -138    -87    123       O  
HETATM 7840  O   HOH A 616      34.023  -1.047   3.295  1.00 30.76           O  
ANISOU 7840  O   HOH A 616     3724   3699   4264    -22    -53    -29       O  
HETATM 7841  O   HOH A 617      13.986  36.841  23.828  1.00 39.62           O  
ANISOU 7841  O   HOH A 617     5170   4862   5023      4    141    115       O  
HETATM 7842  O   HOH A 618      34.745  25.943  17.744  1.00 55.52           O  
ANISOU 7842  O   HOH A 618     7130   6921   7043    -46    -14    107       O  
HETATM 7843  O   HOH A 619       7.228  11.204  20.377  0.82 36.22           O  
ANISOU 7843  O   HOH A 619     4540   4473   4747    -35     15      5       O  
HETATM 7844  O   HOH A 620      31.118   9.378  29.418  0.85 41.41           O  
ANISOU 7844  O   HOH A 620     5326   5205   5203     23   -154    354       O  
HETATM 7845  O   HOH A 621      16.277  31.212  13.465  1.00 29.93           O  
ANISOU 7845  O   HOH A 621     3949   3700   3722    152     28    190       O  
HETATM 7846  O   HOH A 622       7.285  11.063  17.714  1.00 36.06           O  
ANISOU 7846  O   HOH A 622     4489   4484   4729    -10    -12    -34       O  
HETATM 7847  O   HOH A 623      35.627  24.719  -2.827  1.00 47.88           O  
ANISOU 7847  O   HOH A 623     6277   5952   5962    154    119    172       O  
HETATM 7848  O   HOH A 624      16.694  -1.441   1.244  0.92 25.91           O  
ANISOU 7848  O   HOH A 624     2954   3280   3612     -8    -36   -328       O  
HETATM 7849  O   HOH A 625      35.171  13.153  20.345  1.00 36.33           O  
ANISOU 7849  O   HOH A 625     4635   4520   4650     -7   -157    209       O  
HETATM 7850  O   HOH A 626       7.654  11.483  13.140  1.00 42.65           O  
ANISOU 7850  O   HOH A 626     5282   5389   5534     43    -65    -88       O  
HETATM 7851  O   HOH A 627      25.788  30.909  29.152  0.85 42.57           O  
ANISOU 7851  O   HOH A 627     5504   5364   5307   -121     23     67       O  
HETATM 7852  O   HOH A 628      34.416  -4.550 -10.468  1.00 37.48           O  
ANISOU 7852  O   HOH A 628     4415   4736   5090    -48      5   -389       O  
HETATM 7853  O   HOH A 629      -0.829  23.238  15.460  0.85 50.06           O  
ANISOU 7853  O   HOH A 629     6241   6392   6389    164    -74    -83       O  
HETATM 7854  O   HOH A 630      40.574  -1.161  12.346  1.00 52.03           O  
ANISOU 7854  O   HOH A 630     6463   6323   6983     24   -114    187       O  
HETATM 7855  O   HOH A 631      11.157   7.197   0.895  1.00 39.75           O  
ANISOU 7855  O   HOH A 631     4775   5216   5113    128   -148   -282       O  
HETATM 7856  O   HOH A 632      30.668  43.560   6.262  0.82 41.64           O  
ANISOU 7856  O   HOH A 632     5621   4857   5342    176    496    290       O  
HETATM 7857  O   HOH A 633      16.276  -4.089  -7.200  1.00 33.92           O  
ANISOU 7857  O   HOH A 633     3797   4500   4589     11    -61   -616       O  
HETATM 7858  O   HOH A 634      10.592   2.042  17.651  0.96 36.82           O  
ANISOU 7858  O   HOH A 634     4537   4448   5004    -66     82    -28       O  
HETATM 7859  O   HOH A 635      37.274  27.391  28.655  1.00 38.55           O  
ANISOU 7859  O   HOH A 635     4899   4936   4812   -121    -81      4       O  
HETATM 7860  O   HOH A 636      26.054   9.931  26.763  0.88 33.04           O  
ANISOU 7860  O   HOH A 636     4273   4088   4192    -11    -97    305       O  
HETATM 7861  O   HOH A 637      19.311  -6.668  -2.114  1.00 39.63           O  
ANISOU 7861  O   HOH A 637     4582   4980   5494    -61     28   -461       O  
HETATM 7862  O   HOH A 638      25.862   7.067  27.589  1.00 42.89           O  
ANISOU 7862  O   HOH A 638     5521   5305   5472      2    -77    347       O  
HETATM 7863  O   HOH A 639      30.711  -8.817 -15.387  0.87 27.92           O  
ANISOU 7863  O   HOH A 639     3028   3664   3916    -79     38   -674       O  
HETATM 7864  O   HOH A 640      37.597  34.937   9.554  1.00 37.56           O  
ANISOU 7864  O   HOH A 640     4960   4469   4843      0    272    112       O  
HETATM 7865  O   HOH A 641      19.763  40.310   7.209  0.77 34.81           O  
ANISOU 7865  O   HOH A 641     4703   4188   4337    308    250    336       O  
HETATM 7866  O   HOH A 642       8.106  27.165   9.104  0.99 55.05           O  
ANISOU 7866  O   HOH A 642     7015   7036   6865    276    -88    101       O  
HETATM 7867  O   HOH A 643      12.314  -1.109  18.610  1.00 39.54           O  
ANISOU 7867  O   HOH A 643     4885   4720   5421    -80    134     16       O  
HETATM 7868  O   HOH A 644      35.638  -3.620  -1.129  1.00 56.16           O  
ANISOU 7868  O   HOH A 644     6873   6921   7545    -43    -21   -139       O  
HETATM 7869  O   HOH A 645      37.186  -7.929   3.807  1.00 57.07           O  
ANISOU 7869  O   HOH A 645     6962   6888   7833    -43     16    -35       O  
HETATM 7870  O   HOH A 646      14.801  35.258   7.841  0.77 34.35           O  
ANISOU 7870  O   HOH A 646     4556   4270   4225    317     77    270       O  
HETATM 7871  O   HOH A 647       7.971  24.134  12.389  1.00 41.78           O  
ANISOU 7871  O   HOH A 647     5309   5322   5244    180    -86     60       O  
HETATM 7872  O   HOH A 648      35.546  21.805 -10.240  1.00 42.45           O  
ANISOU 7872  O   HOH A 648     5591   5389   5150    232    117    139       O  
HETATM 7873  O   HOH A 649      29.935  16.286  -5.499  0.91 32.40           O  
ANISOU 7873  O   HOH A 649     4176   4172   3964    180    -47     49       O  
HETATM 7874  O   HOH A 650      35.906  17.014  13.598  1.00 42.08           O  
ANISOU 7874  O   HOH A 650     5382   5217   5388     -9    -98    142       O  
HETATM 7875  O   HOH A 651      20.030  -5.354   0.852  1.00 49.19           O  
ANISOU 7875  O   HOH A 651     5869   6133   6690    -54     22   -337       O  
HETATM 7876  O   HOH A 652      21.639  25.715  -7.988  1.00 55.30           O  
ANISOU 7876  O   HOH A 652     7192   7203   6616    449    -30    207       O  
HETATM 7877  O   HOH A 653      19.974  46.910   4.893  1.00 47.75           O  
ANISOU 7877  O   HOH A 653     6435   5685   6023    421    461    456       O  
HETATM 7878  O   HOH A 654      12.513  27.512  34.346  1.00 46.73           O  
ANISOU 7878  O   HOH A 654     6062   5885   5808   -140     65    104       O  
HETATM 7879  O   HOH A 655      23.638  10.125  28.002  0.77 30.14           O  
ANISOU 7879  O   HOH A 655     3920   3716   3815    -22    -71    307       O  
HETATM 7880  O   HOH A 656       8.937  11.407  28.097  1.00 38.47           O  
ANISOU 7880  O   HOH A 656     4935   4711   4973    -88     77    144       O  
HETATM 7881  O   HOH A 657      29.108  12.382  -5.729  0.79 40.03           O  
ANISOU 7881  O   HOH A 657     5066   5160   4982    149    -81    -27       O  
HETATM 7882  O   HOH A 658      15.935  25.163  38.356  1.00 49.69           O  
ANISOU 7882  O   HOH A 658     6455   6337   6087   -160     36    142       O  
HETATM 7883  O   HOH A 659      16.216  -3.402  -1.928  1.00 43.33           O  
ANISOU 7883  O   HOH A 659     5074   5543   5846    -15    -29   -459       O  
HETATM 7884  O   HOH A 660      36.917  35.768   2.050  1.00 73.71           O  
ANISOU 7884  O   HOH A 660     9641   9018   9347    124    365    226       O  
HETATM 7885  O   HOH A 661       5.836  19.627  23.198  1.00 44.56           O  
ANISOU 7885  O   HOH A 661     5667   5566   5697    -17      5     45       O  
HETATM 7886  O   HOH A 662      38.007  13.939  11.156  1.00 40.03           O  
ANISOU 7886  O   HOH A 662     5090   4939   5179     -5   -106    127       O  
HETATM 7887  O   HOH A 663      29.138  -2.222  25.999  1.00 55.28           O  
ANISOU 7887  O   HOH A 663     7035   6723   7246     62    -13    443       O  
HETATM 7888  O   HOH A 664      36.161  25.746   0.201  1.00 38.18           O  
ANISOU 7888  O   HOH A 664     5040   4685   4782    115    122    168       O  
HETATM 7889  O   HOH A 665      24.704  13.707  -6.958  1.00 38.12           O  
ANISOU 7889  O   HOH A 665     4813   5017   4652    222   -114    -44       O  
HETATM 7890  O   HOH A 666      24.074 -11.299  20.500  1.00 49.68           O  
ANISOU 7890  O   HOH A 666     6189   5758   6929     -7    233    295       O  
HETATM 7891  O   HOH A 667       9.635   8.607  10.832  0.92 36.82           O  
ANISOU 7891  O   HOH A 667     4510   4651   4828     37    -68   -120       O  
HETATM 7892  O   HOH A 668       7.146  15.677  12.830  1.00 52.02           O  
ANISOU 7892  O   HOH A 668     6507   6612   6648     91    -91    -52       O  
HETATM 7893  O   HOH A 669      31.905   1.088  -7.579  1.00 44.06           O  
ANISOU 7893  O   HOH A 669     5370   5609   5762     18    -55   -242       O  
HETATM 7894  O   HOH A 670       7.427  23.756  14.967  1.00 42.91           O  
ANISOU 7894  O   HOH A 670     5454   5436   5415    133    -68     55       O  
HETATM 7895  O   HOH A 671      26.801  -3.282  25.371  1.00 58.79           O  
ANISOU 7895  O   HOH A 671     7471   7125   7740     42     37    418       O  
HETATM 7896  O   HOH A 672       8.025  23.829  31.831  0.85 36.48           O  
ANISOU 7896  O   HOH A 672     4737   4543   4580   -110     68    105       O  
HETATM 7897  O   HOH A 673      37.890  23.192   6.231  1.00 48.07           O  
ANISOU 7897  O   HOH A 673     6215   5928   6121     24     40    120       O  
HETATM 7898  O   HOH A 674      36.313  23.880  13.054  1.00 56.80           O  
ANISOU 7898  O   HOH A 674     7295   7058   7227    -17    -10    118       O  
HETATM 7899  O   HOH A 675       8.451  29.837  15.561  1.00 36.68           O  
ANISOU 7899  O   HOH A 675     4731   4605   4602    168    -14    124       O  
HETATM 7900  O   HOH A 676      29.362   6.793  22.458  1.00 41.74           O  
ANISOU 7900  O   HOH A 676     5326   5143   5390      8   -113    288       O  
HETATM 7901  O   HOH A 677       4.525  15.176  23.047  1.00 44.16           O  
ANISOU 7901  O   HOH A 677     5574   5491   5713    -40     30      7       O  
HETATM 7902  O   HOH A 678       2.008  29.568  11.808  1.00 37.75           O  
ANISOU 7902  O   HOH A 678     4773   4847   4724    302    -77     54       O  
HETATM 7903  O   HOH A 679      31.026  27.936  17.580  1.00 48.34           O  
ANISOU 7903  O   HOH A 679     6252   6000   6114    -27     17    128       O  
HETATM 7904  O   HOH A 680      42.375   6.850   2.614  1.00 49.38           O  
ANISOU 7904  O   HOH A 680     6180   6078   6504    -15    -73     23       O  
HETATM 7905  O   HOH A 681      19.823   6.964  21.749  1.00 21.62           O  
ANISOU 7905  O   HOH A 681     2770   2569   2877    -27    -30    207       O  
HETATM 7906  O   HOH A 682      34.028  30.159  14.090  0.77 36.81           O  
ANISOU 7906  O   HOH A 682     4812   4488   4688    -16     91    116       O  
HETATM 7907  O   HOH A 683      12.170  28.434   7.188  0.94 29.46           O  
ANISOU 7907  O   HOH A 683     3835   3770   3589    291    -59    164       O  
HETATM 7908  O   HOH A 684       2.939  33.104  13.419  1.00 41.08           O  
ANISOU 7908  O   HOH A 684     5248   5202   5157    297    -19    112       O  
HETATM 7909  O   HOH A 685      22.197  -6.194   0.134  1.00 57.24           O  
ANISOU 7909  O   HOH A 685     6887   7129   7731    -61     29   -327       O  
HETATM 7910  O   HOH A 686       9.127  16.392  31.989  0.73 18.82           O  
ANISOU 7910  O   HOH A 686     2502   2273   2377   -109     73    167       O  
HETATM 7911  O   HOH A 687       7.808  26.514  16.913  1.00 42.16           O  
ANISOU 7911  O   HOH A 687     5395   5309   5316    120    -36     87       O  
HETATM 7912  O   HOH A 688      34.335  32.393  14.665  0.98 34.91           O  
ANISOU 7912  O   HOH A 688     4576   4223   4464    -28    137    101       O  
HETATM 7913  O   HOH A 689      15.275   4.867  -5.675  1.00 37.13           O  
ANISOU 7913  O   HOH A 689     4399   4986   4723    150   -165   -371       O  
HETATM 7914  O   HOH A 690      15.318  39.201  22.766  1.00 43.70           O  
ANISOU 7914  O   HOH A 690     5700   5341   5563     18    189    123       O  
HETATM 7915  O   HOH A 691      15.138   0.158  -6.449  0.87 33.85           O  
ANISOU 7915  O   HOH A 691     3873   4548   4441     80   -122   -512       O  
HETATM 7916  O   HOH A 692       8.989   9.452  21.183  1.00 41.88           O  
ANISOU 7916  O   HOH A 692     5273   5160   5479    -49     29     42       O  
HETATM 7917  O   HOH A 693      14.691  26.386  35.417  0.90 38.25           O  
ANISOU 7917  O   HOH A 693     4995   4840   4700   -146     44    123       O  
HETATM 7918  O   HOH A 694       6.330  29.026  29.832  1.00 44.85           O  
ANISOU 7918  O   HOH A 694     5782   5590   5669    -77     85     64       O  
HETATM 7919  O   HOH A 695      16.899  -6.232  -1.578  0.87 37.97           O  
ANISOU 7919  O   HOH A 695     4355   4794   5278    -56     25   -492       O  
HETATM 7920  O   HOH A 696       7.807  14.531   8.245  0.88 36.15           O  
ANISOU 7920  O   HOH A 696     4452   4675   4608    142   -131   -105       O  
HETATM 7921  O   HOH A 697      33.354   7.593  40.605  1.00 55.46           O  
ANISOU 7921  O   HOH A 697     7159   7194   6720    136   -210    530       O  
HETATM 7922  O   HOH A 698      22.278  31.278  31.314  1.00 52.04           O  
ANISOU 7922  O   HOH A 698     6713   6571   6487   -134     39     68       O  
HETATM 7923  O   HOH A 699      12.855   5.696   9.986  1.00 48.13           O  
ANISOU 7923  O   HOH A 699     5936   6044   6307     13    -53   -108       O  
HETATM 7924  O   HOH A 700      23.505   4.190  24.358  0.82 32.18           O  
ANISOU 7924  O   HOH A 700     4125   3877   4224     -9    -29    302       O  
HETATM 7925  O   HOH A 701      37.786  25.686  22.881  1.00 46.56           O  
ANISOU 7925  O   HOH A 701     5941   5857   5895    -87    -61     54       O  
HETATM 7926  O   HOH A 702      14.233  -7.237  -5.819  0.99 34.92           O  
ANISOU 7926  O   HOH A 702     3838   4558   4870    -47      6   -711       O  
HETATM 7927  O   HOH A 703      10.591  20.280   5.238  1.00 45.73           O  
ANISOU 7927  O   HOH A 703     5765   5926   5685    245   -147     12       O  
HETATM 7928  O   HOH A 704      31.789   4.814  -7.332  1.00 41.13           O  
ANISOU 7928  O   HOH A 704     5073   5264   5290     58    -69   -169       O  
HETATM 7929  O   HOH A 705      34.451   2.347  -3.828  0.97 36.11           O  
ANISOU 7929  O   HOH A 705     4418   4508   4794      4    -57   -130       O  
HETATM 7930  O   HOH A 706      22.786  24.525  40.360  1.00 48.39           O  
ANISOU 7930  O   HOH A 706     6270   6287   5829   -143    -44    147       O  
HETATM 7931  O   HOH A 707       1.067  37.145  17.591  1.00 40.16           O  
ANISOU 7931  O   HOH A 707     5143   5003   5111    255     66    111       O  
HETATM 7932  O   HOH A 708       8.094   6.117  23.950  1.00 43.41           O  
ANISOU 7932  O   HOH A 708     5471   5283   5740    -85    108     66       O  
HETATM 7933  O   HOH A 709      34.355  10.157  31.718  0.84 36.46           O  
ANISOU 7933  O   HOH A 709     4684   4653   4516     46   -204    360       O  
HETATM 7934  O   HOH A 710       4.705  19.764  15.694  0.98 39.77           O  
ANISOU 7934  O   HOH A 710     4988   5045   5077     97    -69    -23       O  
HETATM 7935  O   HOH A 711      14.117   9.414   5.902  1.00 38.25           O  
ANISOU 7935  O   HOH A 711     4710   4894   4929     86   -118   -104       O  
HETATM 7936  O   HOH A 712      29.118   7.522 -15.420  0.97 55.60           O  
ANISOU 7936  O   HOH A 712     6920   7357   6849    189    -83   -253       O  
HETATM 7937  O   HOH A 713      21.356  29.628  27.397  1.00 49.38           O  
ANISOU 7937  O   HOH A 713     6388   6193   6180    -85     22    113       O  
HETATM 7938  O   HOH A 714      23.881   1.729  23.496  1.00 37.59           O  
ANISOU 7938  O   HOH A 714     4789   4521   4972     -4     -6    306       O  
HETATM 7939  O   HOH A 715      35.124  20.530  15.977  1.00 43.60           O  
ANISOU 7939  O   HOH A 715     5597   5420   5548    -22    -77    138       O  
HETATM 7940  O   HOH A 716       7.336   6.871  20.797  1.00 48.09           O  
ANISOU 7940  O   HOH A 716     6016   5918   6338    -65     69     -7       O  
HETATM 7941  O   HOH A 717      -1.126  37.330  18.435  1.00 38.87           O  
ANISOU 7941  O   HOH A 717     4952   4843   4972    257     66     80       O  
HETATM 7942  O   HOH A 718      -0.652  35.511  20.705  1.00 48.32           O  
ANISOU 7942  O   HOH A 718     6147   6033   6177    177     68     50       O  
HETATM 7943  O   HOH A 719       6.564  24.862   8.710  0.79 31.20           O  
ANISOU 7943  O   HOH A 719     3944   4051   3858    270   -118     45       O  
HETATM 7944  O   HOH A 720      26.524  15.645  -5.408  1.00 64.63           O  
ANISOU 7944  O   HOH A 720     8224   8309   8023    207    -85     22       O  
HETATM 7945  O   HOH A 721      17.128  30.354   3.775  0.85 39.50           O  
ANISOU 7945  O   HOH A 721     5184   5009   4815    326      1    238       O  
HETATM 7946  O   HOH A 722      38.397  17.949   2.416  0.89 20.48           O  
ANISOU 7946  O   HOH A 722     2678   2464   2637     37     -3     93       O  
HETATM 7947  O   HOH A 723      24.202   4.973  -6.981  1.00 28.02           O  
ANISOU 7947  O   HOH A 723     3355   3719   3572    108   -118   -242       O  
HETATM 7948  O   HOH A 724      23.357   4.129  -3.434  1.00 24.35           O  
ANISOU 7948  O   HOH A 724     2889   3176   3187     72   -109   -207       O  
HETATM 7949  O   HOH A 725      10.366   4.420  15.801  1.00 44.48           O  
ANISOU 7949  O   HOH A 725     5503   5484   5915    -41     28    -56       O  
HETATM 7950  O   HOH A 726      11.332  -1.847  22.001  1.00 47.11           O  
ANISOU 7950  O   HOH A 726     5883   5624   6393    -93    195     79       O  
HETATM 7951  O   HOH A 727      22.260   8.454  25.534  0.93 29.42           O  
ANISOU 7951  O   HOH A 727     3805   3586   3789    -23    -52    280       O  
HETATM 7952  O   HOH A 728      40.706  34.802  -7.276  1.00 58.82           O  
ANISOU 7952  O   HOH A 728     7856   7130   7362    217    496    291       O  
HETATM 7953  O   HOH A 729      -1.862  30.836   9.274  1.00 47.71           O  
ANISOU 7953  O   HOH A 729     5975   6192   5962    421   -119     20       O  
HETATM 7954  O   HOH A 730      34.392  19.623  39.595  0.57 46.05           O  
ANISOU 7954  O   HOH A 730     5884   6116   5495    -32   -224    190       O  
HETATM 7955  O   HOH A 731      18.365  27.456  35.740  1.00 66.01           O  
ANISOU 7955  O   HOH A 731     8504   8390   8189   -150     21    111       O  
HETATM 7956  O   HOH A 732      31.248  29.648  25.026  1.00 49.51           O  
ANISOU 7956  O   HOH A 732     6366   6215   6231    -99      5     66       O  
HETATM 7957  O   HOH A 733      24.718  -9.855  13.006  0.90 77.81           O  
ANISOU 7957  O   HOH A 733     9645   9420  10500    -52    153     66       O  
HETATM 7958  O   HOH B 513      40.956  24.074  14.460  1.00 16.89           O  
ANISOU 7958  O   HOH B 513     2199   2002   2218    -55     -9     63       O  
HETATM 7959  O   HOH B 514      60.195   9.875   2.037  1.00 27.06           O  
ANISOU 7959  O   HOH B 514     3216   3144   3923   -101      3   -168       O  
HETATM 7960  O   HOH B 515      36.389  13.976  25.668  1.00 24.84           O  
ANISOU 7960  O   HOH B 515     3179   3136   3124     -3   -192    232       O  
HETATM 7961  O   HOH B 516      51.602  16.378   5.485  1.00 22.18           O  
ANISOU 7961  O   HOH B 516     2759   2593   3076    -70      7    -38       O  
HETATM 7962  O   HOH B 517      63.275  16.399   0.137  1.00 18.61           O  
ANISOU 7962  O   HOH B 517     2185   2020   2865   -162    165   -267       O  
HETATM 7963  O   HOH B 518      53.340  13.931  26.401  1.00 22.85           O  
ANISOU 7963  O   HOH B 518     2678   3032   2971     42   -343     27       O  
HETATM 7964  O   HOH B 519      65.657  13.022  10.640  1.00 18.66           O  
ANISOU 7964  O   HOH B 519     2000   2192   2898    -89   -116   -278       O  
HETATM 7965  O   HOH B 520      63.297  22.159  -3.900  0.91 19.42           O  
ANISOU 7965  O   HOH B 520     2412   2034   2933   -188    391   -271       O  
HETATM 7966  O   HOH B 521      53.883  11.406   0.680  1.00 25.99           O  
ANISOU 7966  O   HOH B 521     3193   3042   3640    -75     20    -81       O  
HETATM 7967  O   HOH B 522      46.813  14.671   6.787  1.00 21.23           O  
ANISOU 7967  O   HOH B 522     2666   2508   2894    -38    -49     33       O  
HETATM 7968  O   HOH B 523      45.820  20.385  10.293  1.00 20.73           O  
ANISOU 7968  O   HOH B 523     2641   2457   2779    -55    -14     30       O  
HETATM 7969  O   HOH B 524      61.765  20.993  12.137  1.00 20.93           O  
ANISOU 7969  O   HOH B 524     2398   2482   3073   -152      4   -300       O  
HETATM 7970  O   HOH B 525      56.250  12.893   0.035  1.00 25.70           O  
ANISOU 7970  O   HOH B 525     3150   2983   3631    -95     62   -121       O  
HETATM 7971  O   HOH B 526      58.322   4.077  29.736  1.00 37.77           O  
ANISOU 7971  O   HOH B 526     4466   4987   4899    274   -507    227       O  
HETATM 7972  O   HOH B 527      53.541  11.284   3.957  0.93 22.46           O  
ANISOU 7972  O   HOH B 527     2728   2612   3192    -65    -32    -56       O  
HETATM 7973  O   HOH B 528      61.554  24.161  -4.585  1.00 26.11           O  
ANISOU 7973  O   HOH B 528     3324   2870   3727   -170    442   -223       O  
HETATM 7974  O   HOH B 529      42.771  10.202   7.877  1.00 24.77           O  
ANISOU 7974  O   HOH B 529     3098   2971   3344    -14   -103     83       O  
HETATM 7975  O   HOH B 530      52.209  15.631  27.669  1.00 35.44           O  
ANISOU 7975  O   HOH B 530     4288   4656   4522     25   -334     11       O  
HETATM 7976  O   HOH B 531      46.301  11.544  -4.857  1.00 24.59           O  
ANISOU 7976  O   HOH B 531     3108   2950   3285    -14     47    -40       O  
HETATM 7977  O   HOH B 532      44.319  40.322  10.328  0.90 28.39           O  
ANISOU 7977  O   HOH B 532     3759   3167   3860   -106    499    -38       O  
HETATM 7978  O   HOH B 533      45.082  15.299  25.622  0.88 29.48           O  
ANISOU 7978  O   HOH B 533     3664   3789   3748      1   -253    126       O  
HETATM 7979  O   HOH B 534      44.404  26.745   8.712  1.00 28.94           O  
ANISOU 7979  O   HOH B 534     3758   3441   3797    -55    124     31       O  
HETATM 7980  O   HOH B 535      59.885  11.386  26.897  0.93 28.14           O  
ANISOU 7980  O   HOH B 535     3205   3770   3717    109   -436    -41       O  
HETATM 7981  O   HOH B 536      64.098  15.159  -8.385  0.98 46.32           O  
ANISOU 7981  O   HOH B 536     5771   5472   6358   -179    328   -288       O  
HETATM 7982  O   HOH B 537      38.486  19.041  22.053  0.89 22.27           O  
ANISOU 7982  O   HOH B 537     2847   2786   2829    -41   -145    132       O  
HETATM 7983  O   HOH B 538      51.336   9.845  -1.572  1.00 34.16           O  
ANISOU 7983  O   HOH B 538     4245   4095   4639    -60     23    -69       O  
HETATM 7984  O   HOH B 539      55.295  24.457  -3.025  1.00 29.95           O  
ANISOU 7984  O   HOH B 539     3879   3432   4067    -96    344    -90       O  
HETATM 7985  O   HOH B 540      47.220  27.821  -6.231  1.00 32.06           O  
ANISOU 7985  O   HOH B 540     4314   3757   4109     51    380    100       O  
HETATM 7986  O   HOH B 541      51.705   7.733  30.761  1.00 29.19           O  
ANISOU 7986  O   HOH B 541     3512   3887   3692    179   -425    244       O  
HETATM 7987  O   HOH B 542      44.733  26.698   3.289  0.96 35.91           O  
ANISOU 7987  O   HOH B 542     4693   4292   4659    -15    194     62       O  
HETATM 7988  O   HOH B 543      53.511   8.511  -5.418  1.00 34.52           O  
ANISOU 7988  O   HOH B 543     4271   4124   4721    -79     76   -131       O  
HETATM 7989  O   HOH B 544      59.863  -0.193   3.777  0.84 25.96           O  
ANISOU 7989  O   HOH B 544     2959   2963   3942    -31   -100    -89       O  
HETATM 7990  O   HOH B 545      67.740  31.102   0.082  0.88 26.98           O  
ANISOU 7990  O   HOH B 545     3307   2862   4083   -303    637   -476       O  
HETATM 7991  O   HOH B 546      51.590  12.392  29.191  1.00 34.07           O  
ANISOU 7991  O   HOH B 546     4126   4502   4318     86   -380    110       O  
HETATM 7992  O   HOH B 547      39.235  14.071  13.588  1.00 32.85           O  
ANISOU 7992  O   HOH B 547     4173   4038   4272    -13   -124    136       O  
HETATM 7993  O   HOH B 548      44.742  12.297  28.891  1.00 28.04           O  
ANISOU 7993  O   HOH B 548     3483   3658   3515     56   -304    211       O  
HETATM 7994  O   HOH B 549      46.519  -3.159   8.126  0.65 25.86           O  
ANISOU 7994  O   HOH B 549     3067   2964   3793     13   -104    104       O  
HETATM 7995  O   HOH B 550      41.581  14.687   1.942  0.87 23.12           O  
ANISOU 7995  O   HOH B 550     2962   2779   3044      6    -18     55       O  
HETATM 7996  O   HOH B 551      65.440  18.722 -10.865  1.00 37.61           O  
ANISOU 7996  O   HOH B 551     4738   4312   5242   -197    484   -303       O  
HETATM 7997  O   HOH B 552      37.251   4.935  14.768  0.93 34.90           O  
ANISOU 7997  O   HOH B 552     4376   4241   4644     14   -141    200       O  
HETATM 7998  O   HOH B 553      46.711  18.170  30.325  1.00 38.95           O  
ANISOU 7998  O   HOH B 553     4819   5122   4858     -7   -294     51       O  
HETATM 7999  O   HOH B 554      65.255  15.724  16.841  1.00 30.57           O  
ANISOU 7999  O   HOH B 554     3465   3843   4306    -68   -206   -308       O  
HETATM 8000  O   HOH B 555      69.055  20.123   3.083  1.00 31.25           O  
ANISOU 8000  O   HOH B 555     3666   3602   4605   -230    223   -455       O  
HETATM 8001  O   HOH B 556      50.470   7.916  -0.344  1.00 32.96           O  
ANISOU 8001  O   HOH B 556     4069   3946   4510    -53    -14    -55       O  
HETATM 8002  O   HOH B 557      40.941   4.648  11.000  1.00 33.61           O  
ANISOU 8002  O   HOH B 557     4176   4062   4531      4   -135    140       O  
HETATM 8003  O   HOH B 558      52.278  23.355  28.940  1.00 30.34           O  
ANISOU 8003  O   HOH B 558     3614   4047   3866    -85   -240   -188       O  
HETATM 8004  O   HOH B 559      44.205  19.808   8.244  0.91 26.74           O  
ANISOU 8004  O   HOH B 559     3427   3213   3520    -36     -4     54       O  
HETATM 8005  O   HOH B 560      70.578  27.866   5.592  0.90 24.97           O  
ANISOU 8005  O   HOH B 560     2847   2758   3882   -315    403   -617       O  
HETATM 8006  O   HOH B 561      38.508  -1.322  16.015  1.00 45.38           O  
ANISOU 8006  O   HOH B 561     5654   5486   6103     44   -115    260       O  
HETATM 8007  O   HOH B 562      57.556  32.056   0.794  1.00 38.87           O  
ANISOU 8007  O   HOH B 562     5003   4449   5318   -167    528   -181       O  
HETATM 8008  O   HOH B 563      39.426  32.452  20.245  0.94 36.34           O  
ANISOU 8008  O   HOH B 563     4660   4464   4682   -124    103    -31       O  
HETATM 8009  O   HOH B 564      40.154  26.300  24.040  1.00 36.16           O  
ANISOU 8009  O   HOH B 564     4589   4564   4584   -104    -67      7       O  
HETATM 8010  O   HOH B 565      64.317  21.231  23.128  1.00 46.40           O  
ANISOU 8010  O   HOH B 565     5425   6014   6190    -98   -233   -428       O  
HETATM 8011  O   HOH B 566      37.858   0.753  20.157  1.00 60.02           O  
ANISOU 8011  O   HOH B 566     7555   7394   7858     62   -146    324       O  
HETATM 8012  O   HOH B 567      66.907  32.740   7.122  1.00 37.24           O  
ANISOU 8012  O   HOH B 567     4490   4278   5382   -325    505   -572       O  
HETATM 8013  O   HOH B 568      52.820   5.144 -14.860  1.00 31.09           O  
ANISOU 8013  O   HOH B 568     3825   3769   4218    -85    172   -260       O  
HETATM 8014  O   HOH B 569      41.230  28.409   9.647  1.00 43.23           O  
ANISOU 8014  O   HOH B 569     5601   5258   5568    -36    131     67       O  
HETATM 8015  O   HOH B 570      37.501   7.735  14.088  1.00 31.91           O  
ANISOU 8015  O   HOH B 570     4016   3888   4222      5   -143    177       O  
HETATM 8016  O   HOH B 571      65.505  10.332   9.691  1.00 31.10           O  
ANISOU 8016  O   HOH B 571     3571   3747   4499    -67   -136   -237       O  
HETATM 8017  O   HOH B 572      41.103  24.464  34.109  1.00 38.88           O  
ANISOU 8017  O   HOH B 572     4866   5156   4751    -91   -205    -17       O  
HETATM 8018  O   HOH B 573      39.911  11.064  -7.486  1.00 36.16           O  
ANISOU 8018  O   HOH B 573     4588   4530   4619     52     14    -41       O  
HETATM 8019  O   HOH B 574      36.281  20.886  -7.873  1.00 35.89           O  
ANISOU 8019  O   HOH B 574     4729   4517   4389    180     95    120       O  
HETATM 8020  O   HOH B 575      65.926  15.057  14.442  0.90 18.09           O  
ANISOU 8020  O   HOH B 575     1891   2205   2776    -82   -166   -314       O  
HETATM 8021  O   HOH B 576      42.559  26.115   1.920  1.00 35.73           O  
ANISOU 8021  O   HOH B 576     4694   4294   4588     21    177     98       O  
HETATM 8022  O   HOH B 577      68.656  18.745  -4.838  0.95 28.86           O  
ANISOU 8022  O   HOH B 577     3480   3203   4282   -237    380   -404       O  
HETATM 8023  O   HOH B 578      60.677  10.606  29.339  1.00 41.22           O  
ANISOU 8023  O   HOH B 578     4831   5509   5322    160   -498    -23       O  
HETATM 8024  O   HOH B 579      67.152  11.639   7.294  1.00 46.88           O  
ANISOU 8024  O   HOH B 579     5565   5701   6545   -108    -64   -306       O  
HETATM 8025  O   HOH B 580      58.737  16.258  -7.035  1.00 46.92           O  
ANISOU 8025  O   HOH B 580     5921   5610   6296   -120    266   -175       O  
HETATM 8026  O   HOH B 581      58.207  -3.022  20.765  0.96 37.58           O  
ANISOU 8026  O   HOH B 581     4435   4626   5218    232   -353    269       O  
HETATM 8027  O   HOH B 582      65.441   0.231   7.599  1.00 39.27           O  
ANISOU 8027  O   HOH B 582     4542   4686   5694     14   -182   -120       O  
HETATM 8028  O   HOH B 583      67.367   2.890   8.583  1.00 46.05           O  
ANISOU 8028  O   HOH B 583     5378   5585   6534      0   -194   -180       O  
HETATM 8029  O   HOH B 584      54.382   4.639   0.975  1.00 34.09           O  
ANISOU 8029  O   HOH B 584     4125   4045   4782    -62    -41    -81       O  
HETATM 8030  O   HOH B 585      48.959  14.450  30.574  0.90 47.55           O  
ANISOU 8030  O   HOH B 585     5875   6229   5963     57   -355    108       O  
HETATM 8031  O   HOH B 586      65.337  19.115  17.107  1.00 43.14           O  
ANISOU 8031  O   HOH B 586     5060   5435   5897   -115   -145   -383       O  
HETATM 8032  O   HOH B 587      65.589  31.312  15.070  1.00 40.87           O  
ANISOU 8032  O   HOH B 587     4821   4972   5738   -299    242   -624       O  
HETATM 8033  O   HOH B 588      43.624   3.463  29.287  0.98 47.52           O  
ANISOU 8033  O   HOH B 588     5970   6020   6065    164   -292    420       O  
HETATM 8034  O   HOH B 589      45.940   3.962  31.047  1.00 34.54           O  
ANISOU 8034  O   HOH B 589     4299   4448   4376    197   -343    416       O  
HETATM 8035  O   HOH B 590      69.474  29.866  -5.854  1.00 46.44           O  
ANISOU 8035  O   HOH B 590     5848   5245   6554   -300    772   -445       O  
HETATM 8036  O   HOH B 591      53.193  13.454  30.774  1.00 28.71           O  
ANISOU 8036  O   HOH B 591     3406   3894   3609     92   -412     60       O  
HETATM 8037  O   HOH B 592      52.723   5.708  34.721  1.00 47.52           O  
ANISOU 8037  O   HOH B 592     5820   6315   5922    279   -495    332       O  
HETATM 8038  O   HOH B 593      67.569   2.060  11.075  1.00 61.60           O  
ANISOU 8038  O   HOH B 593     7324   7594   8488     46   -252   -141       O  
HETATM 8039  O   HOH B 594      40.695   6.562  27.571  1.00 39.98           O  
ANISOU 8039  O   HOH B 594     5047   5048   5097     91   -252    351       O  
HETATM 8040  O   HOH B 595      64.127  10.052  -4.988  0.80 28.26           O  
ANISOU 8040  O   HOH B 595     3368   3218   4150   -160    163   -285       O  
HETATM 8041  O   HOH B 596      45.221  14.747  28.038  1.00 35.69           O  
ANISOU 8041  O   HOH B 596     4444   4627   4492     21   -285    146       O  
HETATM 8042  O   HOH B 597      43.718   5.574  -9.738  1.00 42.77           O  
ANISOU 8042  O   HOH B 597     5324   5331   5595    -12     32   -151       O  
HETATM 8043  O   HOH B 598      56.750  -4.229  26.558  1.00 47.34           O  
ANISOU 8043  O   HOH B 598     5713   5954   6322    345   -410    430       O  
HETATM 8044  O   HOH B 599      32.362  15.082  -5.058  1.00 37.34           O  
ANISOU 8044  O   HOH B 599     4790   4755   4642    138    -36     37       O  
HETATM 8045  O   HOH B 600      64.753   6.683  19.425  1.00 37.65           O  
ANISOU 8045  O   HOH B 600     4331   4775   5197    100   -376    -83       O  
HETATM 8046  O   HOH B 601      67.481  10.792  -2.699  0.96 33.87           O  
ANISOU 8046  O   HOH B 601     4007   3915   4946   -177    149   -347       O  
HETATM 8047  O   HOH B 602      68.716   6.963   8.232  1.00 49.55           O  
ANISOU 8047  O   HOH B 602     5825   6047   6954    -52   -150   -273       O  
HETATM 8048  O   HOH B 603      70.578  12.946   7.528  1.00 50.09           O  
ANISOU 8048  O   HOH B 603     5900   6109   7024   -135    -42   -415       O  
HETATM 8049  O   HOH B 604      44.795   6.348   4.086  1.00 38.65           O  
ANISOU 8049  O   HOH B 604     4802   4695   5187    -22    -84     31       O  
HETATM 8050  O   HOH B 605      42.284  13.021   5.381  0.70 23.26           O  
ANISOU 8050  O   HOH B 605     2944   2786   3106    -11    -62     66       O  
HETATM 8051  O   HOH B 606      58.044  -4.875   3.800  0.99 40.95           O  
ANISOU 8051  O   HOH B 606     4829   4809   5924     -6    -93    -42       O  
HETATM 8052  O   HOH B 607      43.395  29.094  -8.494  0.74 23.86           O  
ANISOU 8052  O   HOH B 607     3345   2773   2948    149    386    189       O  
HETATM 8053  O   HOH B 608      40.200  16.344 -14.845  1.00 62.44           O  
ANISOU 8053  O   HOH B 608     8052   7953   7720    165    134      6       O  
HETATM 8054  O   HOH B 609      61.162  34.234   9.848  1.00 42.66           O  
ANISOU 8054  O   HOH B 609     5261   5017   5932   -280    443   -441       O  
HETATM 8055  O   HOH B 610      53.411  -6.984  29.091  1.00 41.10           O  
ANISOU 8055  O   HOH B 610     4999   5121   5498    405   -360    594       O  
HETATM 8056  O   HOH B 611      51.231  29.743  -1.153  1.00 51.88           O  
ANISOU 8056  O   HOH B 611     6743   6187   6781    -57    411     -8       O  
HETATM 8057  O   HOH B 612      35.493   7.249  22.772  1.00 55.15           O  
ANISOU 8057  O   HOH B 612     6998   6877   7079     30   -172    295       O  
HETATM 8058  O   HOH B 613      66.569  10.257  24.200  1.00 34.61           O  
ANISOU 8058  O   HOH B 613     3872   4570   4708    114   -456   -188       O  
HETATM 8059  O   HOH B 614      55.210   1.885  38.479  1.00 80.22           O  
ANISOU 8059  O   HOH B 614     9929  10564   9987    449   -585    472       O  
HETATM 8060  O   HOH B 615      40.987   2.900  24.203  1.00 48.16           O  
ANISOU 8060  O   HOH B 615     6059   5984   6256     99   -217    363       O  
HETATM 8061  O   HOH B 616      67.144   8.649  10.886  1.00 50.70           O  
ANISOU 8061  O   HOH B 616     5996   6251   7018    -38   -186   -243       O  
HETATM 8062  O   HOH B 617      53.798  25.236  30.953  1.00 41.16           O  
ANISOU 8062  O   HOH B 617     4925   5490   5223   -106   -247   -288       O  
HETATM 8063  O   HOH B 618      41.588  11.666 -14.528  1.00 48.88           O  
ANISOU 8063  O   HOH B 618     6235   6224   6114     92     93    -93       O  
HETATM 8064  O   HOH B 619      70.728   6.108   2.898  0.95 68.04           O  
ANISOU 8064  O   HOH B 619     8161   8292   9401   -110    -38   -353       O  
HETATM 8065  O   HOH B 620      57.204  36.457   8.082  1.00 56.30           O  
ANISOU 8065  O   HOH B 620     7115   6681   7598   -238    528   -311       O  
HETATM 8066  O   HOH B 621      61.607  -0.395  -2.627  0.99 66.25           O  
ANISOU 8066  O   HOH B 621     8052   8023   9098    -98      8   -213       O  
HETATM 8067  O   HOH B 622      67.360  14.782  -6.339  1.00 51.20           O  
ANISOU 8067  O   HOH B 622     6303   6064   7087   -210    309   -362       O  
HETATM 8068  O   HOH B 623      64.250  -3.548   6.076  0.99 51.78           O  
ANISOU 8068  O   HOH B 623     6117   6205   7351     25   -155    -82       O  
HETATM 8069  O   HOH B 624      46.692  32.036  37.950  1.00 65.73           O  
ANISOU 8069  O   HOH B 624     8085   8714   8174   -203   -156   -378       O  
HETATM 8070  O   HOH B 625      43.472  -3.724  16.624  1.00 49.53           O  
ANISOU 8070  O   HOH B 625     6132   5985   6703     86   -142    296       O  
HETATM 8071  O   HOH B 626      50.690  17.288  29.793  1.00 47.90           O  
ANISOU 8071  O   HOH B 626     5882   6282   6036     13   -333      2       O  
HETATM 8072  O   HOH B 627      67.175  12.837  12.995  1.00 41.00           O  
ANISOU 8072  O   HOH B 627     4769   5076   5733    -69   -173   -308       O  
HETATM 8073  O   HOH B 628      70.403  13.076   4.806  0.80 44.96           O  
ANISOU 8073  O   HOH B 628     5288   5405   6390   -160     27   -417       O  
HETATM 8074  O   HOH B 629      54.134  36.370  13.267  1.00 48.88           O  
ANISOU 8074  O   HOH B 629     6136   5855   6582   -236    393   -311       O  
HETATM 8075  O   HOH B 630      67.560   4.854  11.335  1.00 55.30           O  
ANISOU 8075  O   HOH B 630     6542   6823   7645     15   -237   -185       O  
HETATM 8076  O   HOH B 631      61.370  36.967  15.511  1.00 45.85           O  
ANISOU 8076  O   HOH B 631     5556   5510   6354   -333    414   -591       O  
HETATM 8077  O   HOH B 632      33.300   0.179  20.367  1.00 37.05           O  
ANISOU 8077  O   HOH B 632     4667   4457   4953     42    -94    322       O  
HETATM 8078  O   HOH B 633      38.090  22.919 -14.256  1.00 45.75           O  
ANISOU 8078  O   HOH B 633     6068   5811   5506    266    209    157       O  
HETATM 8079  O   HOH B 634      33.218   6.449  21.164  0.87 35.37           O  
ANISOU 8079  O   HOH B 634     4496   4340   4605     20   -143    282       O  
HETATM 8080  O   HOH B 635      62.760  37.725   0.468  1.00 59.98           O  
ANISOU 8080  O   HOH B 635     7641   6946   8201   -269    823   -352       O  
HETATM 8081  O   HOH B 636      54.268   2.229   2.170  1.00 43.33           O  
ANISOU 8081  O   HOH B 636     5263   5201   5998    -48    -67    -61       O  
HETATM 8082  O   HOH B 637      44.480  -0.554  22.471  1.00 40.24           O  
ANISOU 8082  O   HOH B 637     4997   4927   5364    134   -223    374       O  
HETATM 8083  O   HOH B 638      54.455   6.263  29.046  0.96 20.48           O  
ANISOU 8083  O   HOH B 638     2357   2754   2670    197   -440    223       O  
HETATM 8084  O   HOH B 639      60.570  25.977  -2.579  1.00 28.85           O  
ANISOU 8084  O   HOH B 639     3676   3217   4066   -169    440   -213       O  
HETATM 8085  O   HOH B 640      65.032   4.801  14.320  1.00 29.92           O  
ANISOU 8085  O   HOH B 640     3368   3663   4339     54   -289    -99       O  
HETATM 8086  O   HOH B 641      45.650  19.635   5.882  0.88 29.86           O  
ANISOU 8086  O   HOH B 641     3823   3589   3933    -37     27     37       O  
HETATM 8087  O   HOH B 642      49.392  -5.394  19.693  1.00 37.28           O  
ANISOU 8087  O   HOH B 642     4525   4460   5180    178   -216    370       O  
HETATM 8088  O   HOH B 643      53.660  30.406  -1.555  0.80 29.90           O  
ANISOU 8088  O   HOH B 643     3945   3363   4054    -88    470    -54       O  
HETATM 8089  O   HOH B 644      49.567  -1.492  34.580  1.00 52.60           O  
ANISOU 8089  O   HOH B 644     6550   6779   6655    374   -406    591       O  
HETATM 8090  O   HOH B 645      37.241  20.515  19.604  1.00 38.38           O  
ANISOU 8090  O   HOH B 645     4910   4792   4880    -43   -106    124       O  
HETATM 8091  O   HOH B 646      65.196  13.663  18.525  1.00 33.47           O  
ANISOU 8091  O   HOH B 646     3813   4256   4649    -20   -277   -260       O  
HETATM 8092  O   HOH B 647      69.743  20.964   5.612  0.80 32.69           O  
ANISOU 8092  O   HOH B 647     3799   3824   4799   -233    186   -499       O  
HETATM 8093  O   HOH B 648      59.374  30.596  22.049  1.00 35.69           O  
ANISOU 8093  O   HOH B 648     4200   4512   4848   -237     43   -499       O  
HETATM 8094  O   HOH B 649      52.259  15.412  31.896  1.00 43.85           O  
ANISOU 8094  O   HOH B 649     5333   5844   5485     66   -400     26       O  
HETATM 8095  O   HOH B 650      68.602  11.053   4.323  1.00 45.90           O  
ANISOU 8095  O   HOH B 650     5435   5523   6480   -135     -3   -347       O  
HETATM 8096  O   HOH B 651      57.541  -6.123   1.121  1.00 52.56           O  
ANISOU 8096  O   HOH B 651     6285   6253   7432    -34    -48    -90       O  
HETATM 8097  O   HOH B 652      53.039  36.211  10.513  1.00 41.13           O  
ANISOU 8097  O   HOH B 652     5222   4827   5580   -202    432   -232       O  
HETATM 8098  O   HOH B 653      63.250  -2.292  10.950  1.00 47.73           O  
ANISOU 8098  O   HOH B 653     5626   5773   6734     85   -239      5       O  
HETATM 8099  O   HOH B 654      68.761  28.281   7.135  1.00 44.23           O  
ANISOU 8099  O   HOH B 654     5305   5233   6268   -299    362   -578       O  
HETATM 8100  O   HOH B 655      67.169  10.141  -5.996  1.00 60.77           O  
ANISOU 8100  O   HOH B 655     7447   7300   8342   -190    209   -354       O  
HETATM 8101  O   HOH B 656      65.187   4.864  16.905  1.00 47.91           O  
ANISOU 8101  O   HOH B 656     5629   6000   6574     91   -341    -76       O  
HETATM 8102  O   HOH B 657      57.492  30.986  -6.190  1.00 52.94           O  
ANISOU 8102  O   HOH B 657     6899   6197   7019   -105    634    -87       O  
HETATM 8103  O   HOH B 658      43.633  27.416   6.154  1.00 54.59           O  
ANISOU 8103  O   HOH B 658     7045   6670   7026    -28    165     59       O  
HETATM 8104  O   HOH B 659      64.311  -1.970   8.155  1.00 46.74           O  
ANISOU 8104  O   HOH B 659     5488   5613   6656     42   -193    -64       O  
HETATM 8105  O   HOH B 660      40.816  14.146 -12.921  1.00 47.71           O  
ANISOU 8105  O   HOH B 660     6130   6053   5943    113     97    -31       O  
HETATM 8106  O   HOH B 661      55.309  27.716  31.984  1.00 53.16           O  
ANISOU 8106  O   HOH B 661     6386   7050   6762   -146   -221   -411       O  
HETATM 8107  O   HOH B 662      69.750   5.550   6.289  1.00 49.53           O  
ANISOU 8107  O   HOH B 662     5804   6003   7012    -62   -123   -294       O  
HETATM 8108  O   HOH B 663      66.630  19.171  14.292  0.91 42.93           O  
ANISOU 8108  O   HOH B 663     5037   5337   5938   -142    -80   -413       O  
HETATM 8109  O   HOH B 664      64.688   1.253  19.732  1.00 53.36           O  
ANISOU 8109  O   HOH B 664     6308   6717   7247    190   -410     49       O  
HETATM 8110  O   HOH B 665      43.826  39.428  19.514  1.00 64.12           O  
ANISOU 8110  O   HOH B 665     8143   7865   8357   -203    329   -193       O  
HETATM 8111  O   HOH B 666      41.726  20.919   8.548  0.64 34.66           O  
ANISOU 8111  O   HOH B 666     4458   4225   4487    -22      1     79       O  
HETATM 8112  O   HOH B 667      70.368  17.489   3.155  1.00 41.37           O  
ANISOU 8112  O   HOH B 667     4894   4900   5925   -215    163   -467       O  
HETATM 8113  O   HOH B 668      49.351  -1.910  32.012  1.00 42.19           O  
ANISOU 8113  O   HOH B 668     5223   5383   5425    333   -372    555       O  
HETATM 8114  O   HOH B 669      42.538  23.941 -16.069  1.00 46.14           O  
ANISOU 8114  O   HOH B 669     6160   5780   5591    229    329    154       O  
HETATM 8115  O   HOH B 670      65.090  15.185  20.824  0.98 44.30           O  
ANISOU 8115  O   HOH B 670     5167   5694   5971    -19   -302   -290       O  
HETATM 8116  O   HOH B 671      42.083  -0.207   5.846  1.00 61.47           O  
ANISOU 8116  O   HOH B 671     7630   7534   8194    -12    -87     58       O  
HETATM 8117  O   HOH B 672      65.603  15.721  23.288  1.00 47.95           O  
ANISOU 8117  O   HOH B 672     5591   6237   6391      0   -351   -317       O  
HETATM 8118  O   HOH B 673      55.779   8.978  -0.009  1.00 38.38           O  
ANISOU 8118  O   HOH B 673     4713   4593   5277    -82     12   -111       O  
HETATM 8119  O   HOH B 674      57.559   7.674   3.829  1.00 36.87           O  
ANISOU 8119  O   HOH B 674     4462   4409   5139    -68    -58   -100       O  
HETATM 8120  O   HOH B 675      58.861   8.776   0.636  1.00 38.45           O  
ANISOU 8120  O   HOH B 675     4676   4583   5352    -96     11   -152       O  
HETATM 8121  O   HOH B 676      67.995  16.161  -2.908  1.00 23.59           O  
ANISOU 8121  O   HOH B 676     2766   2584   3615   -212    264   -381       O  
HETATM 8122  O   HOH B 677      63.464  34.514   7.184  1.00 43.84           O  
ANISOU 8122  O   HOH B 677     5414   5094   6148   -299    538   -475       O  
HETATM 8123  O   HOH B 678      53.239   2.462  35.056  1.00 59.95           O  
ANISOU 8123  O   HOH B 678     7396   7858   7524    351   -503    432       O  
HETATM 8124  O   HOH B 679      63.774  10.802  29.504  1.00 62.23           O  
ANISOU 8124  O   HOH B 679     7409   8218   8017    174   -535   -104       O  
HETATM 8125  O   HOH B 680      59.723   8.111  30.655  0.88 38.18           O  
ANISOU 8125  O   HOH B 680     4471   5134   4902    223   -528     85       O  
HETATM 8126  O   HOH B 681      44.750   4.781 -12.344  1.00 44.32           O  
ANISOU 8126  O   HOH B 681     5506   5547   5785    -19     61   -201       O  
HETATM 8127  O   HOH B 682      41.948  18.252 -14.502  1.00 47.82           O  
ANISOU 8127  O   HOH B 682     6240   6045   5885    157    188     39       O  
HETATM 8128  O   HOH C 184      -4.172  11.272  46.443  0.92 27.82           O  
ANISOU 8128  O   HOH C 184     3751   3255   3566   -286    527    171       O  
HETATM 8129  O   HOH C 185      12.846  12.106  38.760  1.00 32.48           O  
ANISOU 8129  O   HOH C 185     4318   4027   3995   -104    109    331       O  
HETATM 8130  O   HOH C 186       9.809  21.750  37.112  0.99 33.56           O  
ANISOU 8130  O   HOH C 186     4413   4208   4130   -154     90    157       O  
HETATM 8131  O   HOH C 187       6.822  27.758  43.846  1.00 36.03           O  
ANISOU 8131  O   HOH C 187     4741   4584   4364   -249    187     58       O  
HETATM 8132  O   HOH C 188      31.205   2.204  42.395  1.00 43.99           O  
ANISOU 8132  O   HOH C 188     5772   5645   5296    206   -116    710       O  
HETATM 8133  O   HOH C 189      18.886   6.832  32.316  1.00 33.79           O  
ANISOU 8133  O   HOH C 189     4420   4125   4293    -34     32    372       O  
HETATM 8134  O   HOH C 190       5.891  26.140  58.362  1.00 51.34           O  
ANISOU 8134  O   HOH C 190     6803   6788   5917   -342    323     88       O  
HETATM 8135  O   HOH C 191      11.456  27.853  47.734  1.00 34.89           O  
ANISOU 8135  O   HOH C 191     4615   4573   4069   -261    148     70       O  
HETATM 8136  O   HOH C 192      -3.422   4.408  52.337  1.00 42.92           O  
ANISOU 8136  O   HOH C 192     5825   5066   5417   -258    762    418       O  
HETATM 8137  O   HOH C 193      26.200   4.511  47.481  0.92 40.18           O  
ANISOU 8137  O   HOH C 193     5380   5234   4653    162    -32    725       O  
HETATM 8138  O   HOH C 194       8.272   9.131  46.247  1.00 36.02           O  
ANISOU 8138  O   HOH C 194     4868   4444   4373   -131    298    434       O  
HETATM 8139  O   HOH C 195      -4.724   5.351  49.807  0.89 27.32           O  
ANISOU 8139  O   HOH C 195     3777   3073   3532   -283    726    312       O  
HETATM 8140  O   HOH C 196      -1.332   2.966  40.656  1.00 51.56           O  
ANISOU 8140  O   HOH C 196     6691   6112   6788   -223    548    221       O  
HETATM 8141  O   HOH C 197      33.955  17.745  42.098  1.00 40.12           O  
ANISOU 8141  O   HOH C 197     5155   5417   4673      3   -241    253       O  
HETATM 8142  O   HOH C 198      23.740   6.422  40.222  1.00 39.90           O  
ANISOU 8142  O   HOH C 198     5270   5042   4847     45    -17    544       O  
HETATM 8143  O   HOH C 199      25.883  21.176  47.896  1.00 55.79           O  
ANISOU 8143  O   HOH C 199     7225   7446   6527    -87   -113    225       O  
HETATM 8144  O   HOH C 200      19.476  22.782  45.619  1.00 44.95           O  
ANISOU 8144  O   HOH C 200     5884   5911   5284   -154     -2    197       O  
HETATM 8145  O   HOH C 201      19.368   0.395  51.343  1.00 66.82           O  
ANISOU 8145  O   HOH C 201     8890   8452   8048    157    228    885       O  
HETATM 8146  O   HOH C 202      23.455  19.991  43.372  1.00 30.32           O  
ANISOU 8146  O   HOH C 202     4014   4054   3453    -95    -73    255       O  
HETATM 8147  O   HOH C 203       7.843  27.259  40.454  1.00 51.86           O  
ANISOU 8147  O   HOH C 203     6731   6558   6417   -210    146     76       O  
HETATM 8148  O   HOH C 204       5.074  17.471  58.347  0.82 30.12           O  
ANISOU 8148  O   HOH C 204     4223   3987   3236   -245    392    340       O  
HETATM 8149  O   HOH C 205       5.739  33.028  56.391  1.00 54.94           O  
ANISOU 8149  O   HOH C 205     7158   7215   6501   -412    326   -108       O  
HETATM 8150  O   HOH C 206      -4.699  10.141  43.961  0.91 35.89           O  
ANISOU 8150  O   HOH C 206     4724   4240   4672   -278    516    130       O  
HETATM 8151  O   HOH C 207       9.094  25.116  40.557  0.96 42.02           O  
ANISOU 8151  O   HOH C 207     5495   5321   5148   -198    126    115       O  
HETATM 8152  O   HOH C 208       0.551  11.640  64.878  1.00 54.44           O  
ANISOU 8152  O   HOH C 208     7483   6997   6203   -231    686    544       O  
HETATM 8153  O   HOH C 209       3.230  33.226  47.830  1.00 40.56           O  
ANISOU 8153  O   HOH C 209     5292   5171   4947   -337    295    -74       O  
HETATM 8154  O   HOH C 210      -1.271  24.955  53.154  1.00 31.02           O  
ANISOU 8154  O   HOH C 210     4184   3953   3649   -364    416     45       O  
HETATM 8155  O   HOH C 211       1.572  22.240  58.778  1.00 44.51           O  
ANISOU 8155  O   HOH C 211     5994   5801   5117   -344    440    168       O  
HETATM 8156  O   HOH C 212      14.329  25.937  46.657  1.00 46.54           O  
ANISOU 8156  O   HOH C 212     6092   6067   5525   -221     92    121       O  
HETATM 8157  O   HOH C 213      -0.830  19.591  36.997  1.00 53.38           O  
ANISOU 8157  O   HOH C 213     6857   6614   6810   -193    224     39       O  
HETATM 8158  O   HOH C 214      27.948  19.260  48.512  1.00 40.48           O  
ANISOU 8158  O   HOH C 214     5282   5551   4548    -38   -157    274       O  
HETATM 8159  O   HOH C 215       4.571  -4.160  46.759  1.00 47.13           O  
ANISOU 8159  O   HOH C 215     6329   5461   6118    -96    700    630       O  
HETATM 8160  O   HOH C 216       3.646  10.774  43.703  1.00 37.96           O  
ANISOU 8160  O   HOH C 216     5050   4625   4749   -191    338    291       O  
HETATM 8161  O   HOH C 217      -0.870   7.228  58.787  1.00 45.61           O  
ANISOU 8161  O   HOH C 217     6296   5615   5420   -223    730    546       O  
HETATM 8162  O   HOH C 218      -4.626  15.450  51.222  1.00 32.53           O  
ANISOU 8162  O   HOH C 218     4405   3950   4007   -329    547    164       O  
HETATM 8163  O   HOH C 219      22.166  21.837  40.542  1.00 43.31           O  
ANISOU 8163  O   HOH C 219     5645   5630   5180   -120    -50    207       O  
HETATM 8164  O   HOH C 220       7.905  31.628  56.190  0.88 51.94           O  
ANISOU 8164  O   HOH C 220     6788   6873   6074   -380    277    -63       O  
HETATM 8165  O   HOH C 221      -1.886   5.848  56.360  1.00 37.43           O  
ANISOU 8165  O   HOH C 221     5216   4484   4520   -235    753    510       O  
HETATM 8166  O   HOH C 222       0.111  27.259  37.032  0.93 34.59           O  
ANISOU 8166  O   HOH C 222     4479   4279   4386   -184    193      1       O  
HETATM 8167  O   HOH C 223      16.572  21.383  38.989  1.00 52.31           O  
ANISOU 8167  O   HOH C 223     6803   6672   6400   -137     19    208       O  
HETATM 8168  O   HOH C 224      -7.705  20.757  39.703  1.00 55.85           O  
ANISOU 8168  O   HOH C 224     7126   6881   7213   -255    345    -82       O  
HETATM 8169  O   HOH C 225      16.064  25.273  41.270  1.00 36.85           O  
ANISOU 8169  O   HOH C 225     4839   4758   4402   -179     45    140       O  
HETATM 8170  O   HOH C 226      -2.841   6.326  62.687  1.00 47.95           O  
ANISOU 8170  O   HOH C 226     6678   5907   5633   -236    875    609       O  
HETATM 8171  O   HOH C 227       5.862  29.379  41.487  1.00 47.01           O  
ANISOU 8171  O   HOH C 227     6107   5935   5819   -235    186     31       O  
HETATM 8172  O   HOH C 228       2.061  25.629  37.246  0.91 35.19           O  
ANISOU 8172  O   HOH C 228     4575   4366   4430   -184    175     38       O  
HETATM 8173  O   HOH C 229      19.688  -4.234  42.100  1.00 63.35           O  
ANISOU 8173  O   HOH C 229     8316   7730   8024    113    268    781       O  
HETATM 8174  O   HOH C 230      37.200  11.222  40.955  1.00 65.92           O  
ANISOU 8174  O   HOH C 230     8415   8643   7987    122   -296    410       O  
HETATM 8175  O   HOH C 231       3.930  27.129  38.470  1.00 47.83           O  
ANISOU 8175  O   HOH C 231     6193   5992   5988   -196    171     46       O  
HETATM 8176  O   HOH C 232       6.113  14.552  35.844  1.00 52.99           O  
ANISOU 8176  O   HOH C 232     6852   6569   6712   -148    160    180       O  
HETATM 8177  O   HOH C 233       1.160   9.357  63.272  1.00 56.12           O  
ANISOU 8177  O   HOH C 233     7697   7137   6489   -195    690    603       O  
HETATM 8178  O   HOH C 234      -1.690  18.336  60.515  1.00 52.88           O  
ANISOU 8178  O   HOH C 234     7121   6771   6201   -349    581    249       O  
HETATM 8179  O   HOH C 235      12.661   6.657  55.770  1.00 55.60           O  
ANISOU 8179  O   HOH C 235     7513   7129   6482     -2    322    714       O  
HETATM 8180  O   HOH C 236       1.758  -0.709  39.265  1.00 51.36           O  
ANISOU 8180  O   HOH C 236     6668   6031   6814   -181    555    302       O  
HETATM 8181  O   HOH C 237      15.299  -2.334  39.617  1.00 58.04           O  
ANISOU 8181  O   HOH C 237     7597   7014   7441     10    306    614       O  
HETATM 8182  O   HOH C 238      19.593   4.143  54.603  1.00 58.06           O  
ANISOU 8182  O   HOH C 238     7796   7521   6744    141    167    834       O  
HETATM 8183  O   HOH C 239      23.709  12.140  29.994  0.98 17.52           O  
ANISOU 8183  O   HOH C 239     2340   2157   2162    -30    -78    308       O  
HETATM 8184  O   HOH C 240       8.321  18.649  35.713  0.94 23.18           O  
ANISOU 8184  O   HOH C 240     3086   2852   2871   -142    104    169       O  
HETATM 8185  O   HOH C 241       7.941  11.253  34.766  1.00 35.83           O  
ANISOU 8185  O   HOH C 241     4675   4366   4571   -127    157    224       O  
HETATM 8186  O   HOH D 184      77.108  21.897 -34.362  1.00 32.92           O  
ANISOU 8186  O   HOH D 184     4483   3490   4535   -301   1445   -458       O  
HETATM 8187  O   HOH D 185      77.106  13.029 -37.965  0.88 29.51           O  
ANISOU 8187  O   HOH D 185     3881   3256   4076   -350   1254   -646       O  
HETATM 8188  O   HOH D 186      53.632  10.247  -3.031  1.00 31.39           O  
ANISOU 8188  O   HOH D 186     3886   3722   4317    -76     61   -105       O  
HETATM 8189  O   HOH D 187      72.975  24.103 -34.434  1.00 41.05           O  
ANISOU 8189  O   HOH D 187     5632   4595   5372   -184   1414   -287       O  
HETATM 8190  O   HOH D 188      66.308   8.417 -23.665  1.00 38.56           O  
ANISOU 8190  O   HOH D 188     4812   4547   5291   -220    555   -456       O  
HETATM 8191  O   HOH D 189      62.155  -2.500 -14.901  1.00 35.72           O  
ANISOU 8191  O   HOH D 189     4185   4169   5220   -197    216   -436       O  
HETATM 8192  O   HOH D 190      58.695   6.912  -7.892  1.00 30.68           O  
ANISOU 8192  O   HOH D 190     3722   3580   4353   -124    136   -226       O  
HETATM 8193  O   HOH D 191      55.740   6.727  -5.537  1.00 44.62           O  
ANISOU 8193  O   HOH D 191     5502   5376   6077    -96     76   -166       O  
HETATM 8194  O   HOH D 192      65.281  -1.148 -11.449  0.78 39.38           O  
ANISOU 8194  O   HOH D 192     4624   4578   5760   -190    181   -405       O  
HETATM 8195  O   HOH D 193      74.640   5.701 -36.763  1.00 33.25           O  
ANISOU 8195  O   HOH D 193     4148   3860   4625   -368    978   -764       O  
HETATM 8196  O   HOH D 194      64.185   9.355 -25.140  1.00 40.19           O  
ANISOU 8196  O   HOH D 194     5080   4814   5378   -181    566   -414       O  
HETATM 8197  O   HOH D 195      53.617  11.981  -5.136  0.89 23.97           O  
ANISOU 8197  O   HOH D 195     2986   2783   3336    -75    114   -111       O  
HETATM 8198  O   HOH D 196      73.008   6.440 -40.681  1.00 33.66           O  
ANISOU 8198  O   HOH D 196     4297   4033   4461   -323   1053   -743       O  
HETATM 8199  O   HOH D 197      49.491   1.340 -21.613  1.00 33.12           O  
ANISOU 8199  O   HOH D 197     4024   4199   4361    -72    192   -415       O  
HETATM 8200  O   HOH D 198      77.314  12.147 -34.207  0.94 32.03           O  
ANISOU 8200  O   HOH D 198     4102   3532   4537   -372   1128   -668       O  
HETATM 8201  O   HOH D 199      70.080   2.755 -35.696  1.00 34.98           O  
ANISOU 8201  O   HOH D 199     4310   4207   4775   -318    798   -747       O  
HETATM 8202  O   HOH D 200      78.040  12.981 -23.813  1.00 35.86           O  
ANISOU 8202  O   HOH D 200     4406   3921   5297   -384    870   -664       O  
HETATM 8203  O   HOH D 201      57.759   5.825 -32.177  1.00 47.76           O  
ANISOU 8203  O   HOH D 201     6048   6089   6010    -87    515   -481       O  
HETATM 8204  O   HOH D 202      71.966  -5.091 -23.634  1.00 33.19           O  
ANISOU 8204  O   HOH D 202     3741   3741   5128   -347    472   -748       O  
HETATM 8205  O   HOH D 203      56.991  -2.377 -25.792  1.00 37.83           O  
ANISOU 8205  O   HOH D 203     4525   4699   5150   -189    333   -595       O  
HETATM 8206  O   HOH D 204      69.049   0.926 -12.493  0.80 31.01           O  
ANISOU 8206  O   HOH D 204     3556   3483   4744   -225    246   -469       O  
HETATM 8207  O   HOH D 206      73.101  28.766 -17.884  1.00 54.70           O  
ANISOU 8207  O   HOH D 206     7076   6155   7552   -300   1131   -406       O  
HETATM 8208  O   HOH D 219      60.080   8.923 -24.400  1.00 38.23           O  
ANISOU 8208  O   HOH D 219     4844   4653   5029   -125    471   -359       O  
HETATM 8209  O   HOH D 225      54.282  -1.792 -16.449  0.81 37.87           O  
ANISOU 8209  O   HOH D 225     4532   4594   5265   -144    174   -399       O  
HETATM 8210  O   HOH D 235      67.397   1.613 -36.049  1.00 54.32           O  
ANISOU 8210  O   HOH D 235     6748   6745   7147   -285    732   -745       O  
HETATM 8211  O   HOH D 260      74.141  24.715 -38.809  1.00 51.06           O  
ANISOU 8211  O   HOH D 260     7005   5869   6527   -162   1596   -264       O  
HETATM 8212  O   HOH D 266      63.599   8.398 -27.870  0.96 31.94           O  
ANISOU 8212  O   HOH D 266     4046   3829   4262   -172    593   -443       O  
HETATM 8213  O   HOH D 267      59.095   0.741 -32.455  1.00 44.45           O  
ANISOU 8213  O   HOH D 267     5477   5647   5764   -173    489   -640       O  
HETATM 8214  O   HOH D 271      69.168   8.827 -22.770  1.00 49.07           O  
ANISOU 8214  O   HOH D 271     6109   5807   6729   -259    591   -497       O  
HETATM 8215  O   HOH D 281      67.455  14.734 -37.460  1.00 43.13           O  
ANISOU 8215  O   HOH D 281     5746   5248   5394   -125   1031   -386       O  
HETATM 8216  O   HOH D 282      47.959  -2.217 -23.085  1.00 35.60           O  
ANISOU 8216  O   HOH D 282     4245   4564   4717    -94    181   -528       O  
HETATM 8217  O   HOH D 286      73.533   2.264 -34.643  1.00 57.69           O  
ANISOU 8217  O   HOH D 286     7127   6969   7826   -378    838   -804       O  
HETATM 8218  O   HOH D 296      62.583  12.636 -16.091  0.89 37.99           O  
ANISOU 8218  O   HOH D 296     4785   4464   5186   -159    418   -293       O  
HETATM 8219  O   HOH D 321      61.859   3.881 -31.201  1.00 40.70           O  
ANISOU 8219  O   HOH D 321     5075   5063   5324   -180    554   -561       O  
HETATM 8220  O   HOH D 323      51.329   1.178 -28.514  0.90 37.00           O  
ANISOU 8220  O   HOH D 323     4531   4813   4713    -72    298   -535       O  
HETATM 8221  O   HOH D 324      56.198  -2.232 -20.021  1.00 45.18           O  
ANISOU 8221  O   HOH D 324     5445   5536   6183   -171    241   -481       O  
HETATM 8222  O   HOH D 327      70.211   4.296 -38.116  1.00 46.29           O  
ANISOU 8222  O   HOH D 327     5817   5679   6093   -300    881   -734       O  
HETATM 8223  O   HOH D 331      39.580   8.156 -25.182  1.00 51.08           O  
ANISOU 8223  O   HOH D 331     6453   6815   6138    175    111   -291       O  
HETATM 8224  O   HOH D 334      68.255  -6.927 -27.202  1.00 44.55           O  
ANISOU 8224  O   HOH D 334     5194   5292   6443   -349    492   -802       O  
HETATM 8225  O   HOH D 339      71.916  29.815 -19.829  1.00 78.30           O  
ANISOU 8225  O   HOH D 339    10152   9137  10460   -261   1203   -330       O  
HETATM 8226  O   HOH D 340      68.270  10.577 -24.353  0.95 27.75           O  
ANISOU 8226  O   HOH D 340     3481   3128   3934   -237    647   -461       O  
HETATM 8227  O   HOH D 355      56.917  23.893 -21.087  1.00 48.10           O  
ANISOU 8227  O   HOH D 355     6421   5769   6085     28    691    -16       O  
HETATM 8228  O   HOH D 359      77.014   5.382 -41.530  1.00 52.71           O  
ANISOU 8228  O   HOH D 359     6649   6343   7035   -413   1154   -858       O  
HETATM 8229  O   HOH D 369      82.682  37.177 -18.019  1.00 46.70           O  
ANISOU 8229  O   HOH D 369     5991   4734   7017   -523   1745   -740       O  
HETATM 8230  O   HOH D 392      61.516  11.860 -22.773  1.00 48.51           O  
ANISOU 8230  O   HOH D 392     6188   5881   6361   -129    518   -313       O  
HETATM 8231  O   HOH D 408      56.369  -1.969  -8.541  1.00 43.52           O  
ANISOU 8231  O   HOH D 408     5219   5192   6126   -123     80   -267       O  
HETATM 8232  O   HOH D 424      80.498  37.785 -16.895  1.00 51.41           O  
ANISOU 8232  O   HOH D 424     6619   5367   7547   -482   1684   -666       O  
HETATM 8233  O   HOH D 428      62.041   6.368 -18.255  1.00 47.67           O  
ANISOU 8233  O   HOH D 428     5908   5739   6464   -175    350   -376       O  
HETATM 8234  O   HOH D 431      69.650  14.264 -10.879  1.00 49.15           O  
ANISOU 8234  O   HOH D 431     6057   5755   6863   -244    430   -423       O  
HETATM 8235  O   HOH D 438      66.740  -6.415 -29.145  0.78 32.09           O  
ANISOU 8235  O   HOH D 438     3651   3785   4756   -341    511   -817       O  
HETATM 8236  O   HOH D 444      73.133   5.673 -12.520  1.00 39.26           O  
ANISOU 8236  O   HOH D 444     4618   4483   5815   -267    342   -536       O  
HETATM 8237  O   HOH D 447      76.049  24.268 -35.292  1.00 63.81           O  
ANISOU 8237  O   HOH D 447     8497   7391   8359   -251   1534   -366       O  
HETATM 8238  O   HOH D 463      79.479  11.387 -18.702  1.00 49.31           O  
ANISOU 8238  O   HOH D 463     5960   5618   7159   -389    705   -712       O  
HETATM 8239  O   HOH D 465      77.377  21.881 -15.509  1.00 54.93           O  
ANISOU 8239  O   HOH D 465     6845   6256   7771   -376    888   -612       O  
HETATM 8240  O   HOH D 495      53.274   9.367 -33.908  0.73 61.68           O  
ANISOU 8240  O   HOH D 495     7934   8012   7491     57    496   -357       O  
HETATM 8241  O   HOH D 496      63.386   1.582  -8.361  1.00 55.48           O  
ANISOU 8241  O   HOH D 496     6720   6651   7710   -157    129   -320       O  
HETATM 8242  O   HOH D 497      70.377  16.643 -37.815  0.74 30.67           O  
ANISOU 8242  O   HOH D 497     4206   3555   3892   -165   1174   -393       O  
HETATM 8243  O   HOH D 498      54.878   1.547 -29.390  1.00 46.46           O  
ANISOU 8243  O   HOH D 498     5744   5940   5967   -112    373   -548       O  
CONECT  493 7735                                                                
CONECT 1989 7735                                                                
CONECT 2462 7735                                                                
CONECT 3065 7736                                                                
CONECT 4531 7736                                                                
CONECT 5007 7736                                                                
CONECT 7735  493 1989 2462 7768                                                 
CONECT 7735 7905 7951                                                           
CONECT 7736 3065 4531 5007 8118                                                 
CONECT 7736 8119 8120                                                           
CONECT 7768 7735                                                                
CONECT 7905 7735                                                                
CONECT 7951 7735                                                                
CONECT 8118 7736                                                                
CONECT 8119 7736                                                                
CONECT 8120 7736                                                                
MASTER      431    0    2   27   50    0    4    6 8101    4   16   84          
END

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Related entries of code: 3rt0

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
6nwc	RCSB PDB PDBbind	155aa, >6NWC_1\|Chain... at 99%
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
No complexes with the same small molecule ligand are found!

Entry Information

PDB ID	3rt0
Complex Type	Protein-Protein
PDBbind Subset	general set
Protein Name	Protein phosphatase 2C 16 (HAB1)
Ligand Name	Abscisic acid receptor PYL10
EC.Number	E.C.3.1.3.16
Resolution	2.11(Å)
Affinity (Kd/Ki/IC50)	Kd=1.2uM
Release Year	2011
Protein/NA Sequence	Check fasta file
Primary Reference	(2011) Mol.Cell Vol. 42: pp. 662-672

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): Q8H1R0 Q9CAJ0
Entrez Gene ID	NCBI Entrez Gene ID: 828905 843609
ASD	Information of known allosteric effects of PDB entries

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