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Browse entries in the PDBbind-CN Database

HEADER    TRANSFERASE                             29-AUG-17   6ATH              
TITLE     CDK2/CYCLIN A/P27-KID-DELTAC                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CELL DIVISION PROTEIN KINASE 2,P33 PROTEIN KINASE;          
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: PHOSPHORYLATED;                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CYCLIN-A2;                                                 
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 173-432;                                      
COMPND  12 SYNONYM: CYCLIN-A,CYCLIN A;                                          
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: CYCLIN-DEPENDENT KINASE INHIBITOR 1B;                      
COMPND  16 CHAIN: C;                                                            
COMPND  17 FRAGMENT: UNP RESIDUES 22-85;                                        
COMPND  18 SYNONYM: CYCLIN-DEPENDENT KINASE INHIBITOR P27,P27KIP1;              
COMPND  19 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK2, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX4T1;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: CCNA2, CCN1, CCNA;                                             
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 GENE: CDKN1B, KIP1;                                                  
SOURCE  24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  27 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    INHIBITOR, COMPLEX, IDP, CDK, CYCLIN, KINASE, PHOSPHORTLATION,        
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.W.WHITE,M.YUN                                                       
REVDAT   5   04-DEC-19 6ATH    1       REMARK                                   
REVDAT   4   24-APR-19 6ATH    1       JRNL                                     
REVDAT   3   10-APR-19 6ATH    1       JRNL                                     
REVDAT   2   20-FEB-19 6ATH    1       REMARK                                   
REVDAT   1   12-SEP-18 6ATH    0                                                
JRNL        AUTH   M.TSYTLONOK,H.SANABRIA,Y.WANG,S.FELEKYAN,K.HEMMEN,           
JRNL        AUTH 2 A.H.PHILLIPS,M.K.YUN,M.B.WADDELL,C.G.PARK,S.VAITHIYALINGAM,  
JRNL        AUTH 3 L.ICONARU,S.W.WHITE,P.TOMPA,C.A.M.SEIDEL,R.KRIWACKI          
JRNL        TITL   DYNAMIC ANTICIPATION BY CDK2/CYCLIN A-BOUND P27 MEDIATES     
JRNL        TITL 2 SIGNAL INTEGRATION IN CELL CYCLE REGULATION.                 
JRNL        REF    NAT COMMUN                    V.  10  1676 2019              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   30976006                                                     
JRNL        DOI    10.1038/S41467-019-09446-W                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.82 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.7.3_928                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.63                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 71378                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.187                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3582                            
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 29.6286 -  5.3689    1.00     2848   147  0.2001 0.2011        
REMARK   3     2  5.3689 -  4.2656    1.00     2728   146  0.1581 0.1690        
REMARK   3     3  4.2656 -  3.7275    1.00     2681   148  0.1509 0.1525        
REMARK   3     4  3.7275 -  3.3873    1.00     2681   144  0.1585 0.1766        
REMARK   3     5  3.3873 -  3.1448    1.00     2657   146  0.1772 0.1903        
REMARK   3     6  3.1448 -  2.9595    1.00     2684   131  0.1827 0.2112        
REMARK   3     7  2.9595 -  2.8114    1.00     2670   119  0.1808 0.1770        
REMARK   3     8  2.8114 -  2.6891    1.00     2623   146  0.1698 0.1722        
REMARK   3     9  2.6891 -  2.5857    1.00     2663   145  0.1683 0.1781        
REMARK   3    10  2.5857 -  2.4965    1.00     2638   111  0.1615 0.2378        
REMARK   3    11  2.4965 -  2.4185    1.00     2644   135  0.1610 0.1666        
REMARK   3    12  2.4185 -  2.3494    1.00     2662   128  0.1609 0.1916        
REMARK   3    13  2.3494 -  2.2876    1.00     2610   129  0.1613 0.1938        
REMARK   3    14  2.2876 -  2.2318    1.00     2641   132  0.1586 0.1749        
REMARK   3    15  2.2318 -  2.1810    1.00     2618   124  0.1531 0.1668        
REMARK   3    16  2.1810 -  2.1346    1.00     2629   170  0.1484 0.1679        
REMARK   3    17  2.1346 -  2.0920    1.00     2603   135  0.1531 0.1779        
REMARK   3    18  2.0920 -  2.0525    1.00     2587   139  0.1546 0.1772        
REMARK   3    19  2.0525 -  2.0158    1.00     2652   138  0.1573 0.1836        
REMARK   3    20  2.0158 -  1.9817    1.00     2579   139  0.1621 0.2051        
REMARK   3    21  1.9817 -  1.9497    0.98     2541   139  0.1787 0.2214        
REMARK   3    22  1.9497 -  1.9197    0.97     2533   151  0.1915 0.2581        
REMARK   3    23  1.9197 -  1.8915    0.97     2509   152  0.2170 0.2225        
REMARK   3    24  1.8915 -  1.8649    0.98     2560   121  0.2286 0.2399        
REMARK   3    25  1.8649 -  1.8397    0.96     2484   147  0.2596 0.2892        
REMARK   3    26  1.8397 -  1.8158    0.80     2071   120  0.2914 0.2772        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.86                                          
REMARK   3   K_SOL              : 0.38                                          
REMARK   3   B_SOL              : 42.91                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.440           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.19490                                             
REMARK   3    B22 (A**2) : 1.69790                                              
REMARK   3    B33 (A**2) : -1.50300                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
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      :  0.005           4903                                  
REMARK   3   ANGLE     :  0.940           6661                                  
REMARK   3   CHIRALITY :  0.068            746                                  
REMARK   3   PLANARITY :  0.005            840                                  
REMARK   3   DIHEDRAL  : 14.082           1830                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  17.1938   9.2721  71.8809              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0761 T22:   0.1253                                     
REMARK   3      T33:   0.0963 T12:  -0.0195                                     
REMARK   3      T13:   0.0379 T23:  -0.0349                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2434 L22:   0.9592                                     
REMARK   3      L33:   1.1998 L12:  -0.4186                                     
REMARK   3      L13:  -0.1776 L23:   0.4075                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0896 S12:  -0.1458 S13:   0.0112                       
REMARK   3      S21:   0.1193 S22:   0.0057 S23:   0.0630                       
REMARK   3      S31:   0.2019 S32:  -0.0512 S33:   0.0314                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  31.8965  -5.5514  45.7430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0861 T22:   0.0636                                     
REMARK   3      T33:   0.0708 T12:   0.0018                                     
REMARK   3      T13:   0.0139 T23:  -0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9857 L22:   1.4135                                     
REMARK   3      L33:   1.1638 L12:   0.1627                                     
REMARK   3      L13:  -0.2098 L23:   0.3742                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0401 S12:   0.0205 S13:   0.0272                       
REMARK   3      S21:  -0.0243 S22:  -0.0016 S23:   0.0753                       
REMARK   3      S31:   0.1071 S32:  -0.0280 S33:   0.0254                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  23.0649 -23.9802  67.1630              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9315 T22:   0.2307                                     
REMARK   3      T33:   0.2607 T12:  -0.0711                                     
REMARK   3      T13:   0.1370 T23:   0.1762                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1466 L22:   0.1956                                     
REMARK   3      L33:   1.4249 L12:  -0.1567                                     
REMARK   3      L13:  -0.0979 L23:  -0.0710                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2282 S12:  -0.3142 S13:  -0.5608                       
REMARK   3      S21:   0.7855 S22:   0.0352 S23:   0.1470                       
REMARK   3      S31:   0.4297 S32:  -0.0250 S33:  -0.1744                       
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 6ATH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229789.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71452                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.820                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 10.70                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.89                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP V9.2.10                                        
REMARK 200 STARTING MODEL: 1JSU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, LITHIUM SULFATE, PH 7.2, VAPOR    
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291.15K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       37.09550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.75550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.82250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.75550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.09550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.82250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     PHE A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     VAL A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     ILE A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     GLU A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     THR A    14                                                      
REMARK 465     TYR A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     THR A    41                                                      
REMARK 465     GLY B   170                                                      
REMARK 465     SER B   171                                                      
REMARK 465     MET B   172                                                      
REMARK 465     GLY C    18                                                      
REMARK 465     SER C    19                                                      
REMARK 465     HIS C    20                                                      
REMARK 465     MET C    21                                                      
REMARK 465     GLU C    22                                                      
REMARK 465     HIS C    23                                                      
REMARK 465     PRO C    24                                                      
REMARK 465     CYS C    49                                                      
REMARK 465     ARG C    50                                                      
REMARK 465     ASP C    51                                                      
REMARK 465     MET C    52                                                      
REMARK 465     GLU C    53                                                      
REMARK 465     GLU C    80                                                      
REMARK 465     LYS C    81                                                      
REMARK 465     GLY C    82                                                      
REMARK 465     SER C    83                                                      
REMARK 465     LEU C    84                                                      
REMARK 465     PRO C    85                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  36    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 323    CG   CD   OE1  NE2                                  
REMARK 470     GLU C  54    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  71    CG   CD   OE1  OE2                                  
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  58       62.00   -111.79                                   
REMARK 500    ASP A 127       48.53   -151.02                                   
REMARK 500    ASP A 145       77.46     60.00                                   
REMARK 500    VAL A 164      132.44     76.92                                   
REMARK 500    SER A 181     -137.01   -151.92                                   
REMARK 500    THR A 290     -167.41   -129.71                                   
REMARK 500    PHE B 304       15.71     59.28                                   
REMARK 500    PRO B 324     -166.84   -100.65                                   
REMARK 500    TRP B 372      112.54    -28.70                                   
REMARK 500    ASN C  61       56.58     37.53                                   
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 B 684        DISTANCE =  6.51 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301                 
DBREF  6ATH A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  6ATH B  173   432  UNP    P20248   CCNA2_HUMAN    173    432             
DBREF  6ATH C   22    85  UNP    P46527   CDN1B_HUMAN     22     85             
SEQADV 6ATH GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 6ATH SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 6ATH GLY B  170  UNP  P20248              EXPRESSION TAG                 
SEQADV 6ATH SER B  171  UNP  P20248              EXPRESSION TAG                 
SEQADV 6ATH MET B  172  UNP  P20248              EXPRESSION TAG                 
SEQADV 6ATH GLY C   18  UNP  P46527              EXPRESSION TAG                 
SEQADV 6ATH SER C   19  UNP  P46527              EXPRESSION TAG                 
SEQADV 6ATH HIS C   20  UNP  P46527              EXPRESSION TAG                 
SEQADV 6ATH MET C   21  UNP  P46527              EXPRESSION TAG                 
SEQRES   1 A  300  GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY          
SEQRES   2 A  300  GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS          
SEQRES   3 A  300  LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU          
SEQRES   4 A  300  ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG          
SEQRES   5 A  300  GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE          
SEQRES   6 A  300  VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU          
SEQRES   7 A  300  TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS          
SEQRES   8 A  300  PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO          
SEQRES   9 A  300  LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU          
SEQRES  10 A  300  ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU          
SEQRES  11 A  300  LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE          
SEQRES  12 A  300  LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL          
SEQRES  13 A  300  PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP          
SEQRES  14 A  300  TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR          
SEQRES  15 A  300  SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE          
SEQRES  16 A  300  ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP          
SEQRES  17 A  300  SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU          
SEQRES  18 A  300  GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER          
SEQRES  19 A  300  MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG          
SEQRES  20 A  300  GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP          
SEQRES  21 A  300  GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO          
SEQRES  22 A  300  ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO          
SEQRES  23 A  300  PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG          
SEQRES  24 A  300  LEU                                                          
SEQRES   1 B  263  GLY SER MET ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE          
SEQRES   2 B  263  HIS THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO          
SEQRES   3 B  263  LYS VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN          
SEQRES   4 B  263  SER MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL          
SEQRES   5 B  263  GLY GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU          
SEQRES   6 B  263  ALA VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER          
SEQRES   7 B  263  VAL LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA          
SEQRES   8 B  263  MET LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO          
SEQRES   9 B  263  GLU VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR          
SEQRES  10 B  263  THR LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU          
SEQRES  11 B  263  LYS VAL LEU THR PHE ASP LEU ALA ALA PRO THR VAL ASN          
SEQRES  12 B  263  GLN PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA          
SEQRES  13 B  263  ASN CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU          
SEQRES  14 B  263  LEU SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU          
SEQRES  15 B  263  PRO SER VAL ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU          
SEQRES  16 B  263  TYR THR VAL THR GLY GLN SER TRP PRO GLU SER LEU ILE          
SEQRES  17 B  263  ARG LYS THR GLY TYR THR LEU GLU SER LEU LYS PRO CYS          
SEQRES  18 B  263  LEU MET ASP LEU HIS GLN THR TYR LEU LYS ALA PRO GLN          
SEQRES  19 B  263  HIS ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER          
SEQRES  20 B  263  LYS TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR          
SEQRES  21 B  263  LEU ASN LEU                                                  
SEQRES   1 C   68  GLY SER HIS MET GLU HIS PRO LYS PRO SER ALA CYS ARG          
SEQRES   2 C   68  ASN LEU PHE GLY PRO VAL ASP HIS GLU GLU LEU THR ARG          
SEQRES   3 C   68  ASP LEU GLU LYS HIS CYS ARG ASP MET GLU GLU ALA SER          
SEQRES   4 C   68  GLN ARG LYS TRP ASN PHE ASP PHE GLN ASN HIS LYS PRO          
SEQRES   5 C   68  LEU GLU GLY LYS TYR GLU TRP GLN GLU VAL GLU LYS GLY          
SEQRES   6 C   68  SER LEU PRO                                                  
MODRES 6ATH TPO A  160  THR  MODIFIED RESIDUE                                   
HET    TPO  A 160      11                                                       
HET    SO4  A 301       5                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5  HOH   *399(H2 O)                                                    
HELIX    1 AA1 PRO A   45  LYS A   56  1                                  12    
HELIX    2 AA2 LEU A   87  SER A   94  1                                   8    
HELIX    3 AA3 PRO A  100  HIS A  121  1                                  22    
HELIX    4 AA4 LYS A  129  GLN A  131  5                                   3    
HELIX    5 AA5 THR A  165  ARG A  169  5                                   5    
HELIX    6 AA6 ALA A  170  LEU A  175  1                                   6    
HELIX    7 AA7 THR A  182  ARG A  199  1                                  18    
HELIX    8 AA8 SER A  207  GLY A  220  1                                  14    
HELIX    9 AA9 GLY A  229  MET A  233  5                                   5    
HELIX   10 AB1 ASP A  247  VAL A  252  1                                   6    
HELIX   11 AB2 ASP A  256  LEU A  267  1                                  12    
HELIX   12 AB3 SER A  276  LEU A  281  1                                   6    
HELIX   13 AB4 ALA A  282  GLN A  287  5                                   6    
HELIX   14 AB5 TYR B  178  CYS B  193  1                                  16    
HELIX   15 AB6 GLY B  198  GLN B  203  5                                   6    
HELIX   16 AB7 THR B  207  TYR B  225  1                                  19    
HELIX   17 AB8 GLN B  228  MET B  246  1                                  19    
HELIX   18 AB9 LEU B  249  GLU B  269  1                                  21    
HELIX   19 AC1 GLU B  274  THR B  282  1                                   9    
HELIX   20 AC2 THR B  287  LEU B  302  1                                  16    
HELIX   21 AC3 THR B  310  LEU B  320  1                                  11    
HELIX   22 AC4 ASN B  326  ASP B  343  1                                  18    
HELIX   23 AC5 ASP B  343  LEU B  348  1                                   6    
HELIX   24 AC6 LEU B  351  GLY B  369  1                                  19    
HELIX   25 AC7 PRO B  373  GLY B  381  1                                   9    
HELIX   26 AC8 THR B  383  ALA B  401  1                                  19    
HELIX   27 AC9 PRO B  402  HIS B  404  5                                   3    
HELIX   28 AD1 GLN B  407  TYR B  413  1                                   7    
HELIX   29 AD2 LYS B  414  HIS B  419  5                                   6    
HELIX   30 AD3 GLY B  420  LEU B  424  5                                   5    
HELIX   31 AD4 ASP C   37  HIS C   48  1                                  12    
HELIX   32 AD5 ALA C   55  ASN C   61  1                                   7    
SHEET    1 AA1 5 LEU A  66  HIS A  71  0                                        
SHEET    2 AA1 5 LYS A  75  GLU A  81 -1  O  TYR A  77   N  ILE A  70           
SHEET    3 AA1 5 VAL A  29  ARG A  36 -1  N  LYS A  33   O  LEU A  78           
SHEET    4 AA1 5 TYR A  19  ASN A  23 -1  N  TYR A  19   O  LEU A  32           
SHEET    5 AA1 5 TYR C  74  GLU C  78 -1  O  GLN C  77   N  LYS A  20           
SHEET    1 AA2 3 GLN A  85  ASP A  86  0                                        
SHEET    2 AA2 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3 AA2 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1 AA3 2 VAL A 123  LEU A 124  0                                        
SHEET    2 AA3 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1 AA4 2 PHE C  62  ASP C  63  0                                        
SHEET    2 AA4 2 LYS C  68  PRO C  69 -1  O  LYS C  68   N  ASP C  63           
LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.33  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
CISPEP   1 VAL A  154    PRO A  155          0        -5.67                     
CISPEP   2 GLN B  323    PRO B  324          0        -8.31                     
CISPEP   3 ASP B  345    PRO B  346          0        12.02                     
SITE     1 AC1  7 ARG A 214  ARG A 217  LYS A 278  HOH A 405                    
SITE     2 AC1  7 HOH A 414  HOH A 552  HOH B 531                               
CRYST1   74.191   77.645  137.511  90.00  90.00  90.00 P 21 21 21    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      0.013479  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012879  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007272        0.00000                         
ATOM      1  N   VAL A  17      14.630  -9.610  79.029  1.00 61.84           N  
ANISOU    1  N   VAL A  17     9041   6961   7495   -332   1387    482       N  
ATOM      2  CA  VAL A  17      15.448  -9.949  80.188  1.00 62.37           C  
ANISOU    2  CA  VAL A  17     9214   7029   7457   -205   1394    584       C  
ATOM      3  C   VAL A  17      14.732 -10.966  81.069  1.00 65.50           C  
ANISOU    3  C   VAL A  17     9685   7351   7851   -241   1486    653       C  
ATOM      4  O   VAL A  17      13.639 -10.703  81.572  1.00 69.06           O  
ANISOU    4  O   VAL A  17    10078   7848   8315   -325   1531    644       O  
ATOM      5  CB  VAL A  17      15.784  -8.702  81.020  1.00 59.25           C  
ANISOU    5  CB  VAL A  17     8761   6787   6964   -132   1342    591       C  
ATOM      6  CG1 VAL A  17      16.799  -9.044  82.097  1.00 56.91           C  
ANISOU    6  CG1 VAL A  17     8569   6501   6551     19   1327    683       C  
ATOM      7  CG2 VAL A  17      16.311  -7.595  80.118  1.00 61.26           C  
ANISOU    7  CG2 VAL A  17     8923   7121   7231   -119   1260    514       C  
ATOM      8  N   VAL A  18      15.351 -12.128  81.252  1.00 63.51           N  
ANISOU    8  N   VAL A  18     9561   6985   7584   -174   1514    722       N  
ATOM      9  CA  VAL A  18      14.718 -13.220  81.982  1.00 63.83           C  
ANISOU    9  CA  VAL A  18     9684   6935   7631   -211   1608    791       C  
ATOM     10  C   VAL A  18      15.600 -13.772  83.101  1.00 63.54           C  
ANISOU   10  C   VAL A  18     9776   6882   7486    -67   1616    904       C  
ATOM     11  O   VAL A  18      15.163 -14.610  83.889  1.00 67.87           O  
ANISOU   11  O   VAL A  18    10403   7365   8019    -80   1696    980       O  
ATOM     12  CB  VAL A  18      14.319 -14.368  81.033  1.00 63.89           C  
ANISOU   12  CB  VAL A  18     9727   6793   7754   -301   1655    759       C  
ATOM     13  CG1 VAL A  18      13.250 -13.900  80.055  1.00 63.40           C  
ANISOU   13  CG1 VAL A  18     9534   6759   7797   -449   1652    645       C  
ATOM     14  CG2 VAL A  18      15.541 -14.893  80.290  1.00 59.12           C  
ANISOU   14  CG2 VAL A  18     9196   6113   7153   -205   1605    757       C  
ATOM     15  N   TYR A  19      16.840 -13.299  83.164  1.00 55.61           N  
ANISOU   15  N   TYR A  19     8788   5938   6404     74   1532    915       N  
ATOM     16  CA  TYR A  19      17.777 -13.726  84.200  1.00 51.11           C  
ANISOU   16  CA  TYR A  19     8326   5373   5721    231   1518   1010       C  
ATOM     17  C   TYR A  19      18.821 -12.653  84.475  1.00 48.40           C  
ANISOU   17  C   TYR A  19     7937   5172   5282    361   1413    994       C  
ATOM     18  O   TYR A  19      19.276 -11.973  83.555  1.00 46.68           O  
ANISOU   18  O   TYR A  19     7646   4993   5096    364   1345    922       O  
ATOM     19  CB  TYR A  19      18.488 -15.018  83.790  1.00 52.04           C  
ANISOU   19  CB  TYR A  19     8561   5346   5867    295   1531   1048       C  
ATOM     20  CG  TYR A  19      17.810 -16.284  84.260  1.00 59.16           C  
ANISOU   20  CG  TYR A  19     9562   6117   6799    241   1638   1119       C  
ATOM     21  CD1 TYR A  19      17.893 -16.684  85.587  1.00 61.20           C  
ANISOU   21  CD1 TYR A  19     9910   6385   6960    319   1678   1223       C  
ATOM     22  CD2 TYR A  19      17.100 -17.087  83.375  1.00 61.65           C  
ANISOU   22  CD2 TYR A  19     9883   6303   7238    112   1697   1080       C  
ATOM     23  CE1 TYR A  19      17.280 -17.841  86.022  1.00 64.35           C  
ANISOU   23  CE1 TYR A  19    10404   6660   7386    269   1782   1296       C  
ATOM     24  CE2 TYR A  19      16.483 -18.248  83.802  1.00 65.67           C  
ANISOU   24  CE2 TYR A  19    10482   6690   7781     59   1797   1144       C  
ATOM     25  CZ  TYR A  19      16.575 -18.620  85.128  1.00 67.04           C  
ANISOU   25  CZ  TYR A  19    10747   6867   7858    136   1842   1256       C  
ATOM     26  OH  TYR A  19      15.964 -19.776  85.560  1.00 70.00           O  
ANISOU   26  OH  TYR A  19    11216   7115   8266     81   1948   1328       O  
ATOM     27  N   LYS A  20      19.201 -12.501  85.739  1.00 42.22           N  
ANISOU   27  N   LYS A  20     7193   4468   4380    470   1398   1058       N  
ATOM     28  CA  LYS A  20      20.347 -11.664  86.083  1.00 43.15           C  
ANISOU   28  CA  LYS A  20     7278   4715   4402    615   1290   1042       C  
ATOM     29  C   LYS A  20      21.256 -12.392  87.060  1.00 44.62           C  
ANISOU   29  C   LYS A  20     7576   4894   4484    779   1274   1128       C  
ATOM     30  O   LYS A  20      20.835 -13.349  87.709  1.00 50.10           O  
ANISOU   30  O   LYS A  20     8368   5505   5163    772   1355   1208       O  
ATOM     31  CB  LYS A  20      19.916 -10.302  86.635  1.00 46.94           C  
ANISOU   31  CB  LYS A  20     7647   5357   4832    586   1256    996       C  
ATOM     32  CG  LYS A  20      19.578 -10.271  88.119  1.00 52.75           C  
ANISOU   32  CG  LYS A  20     8418   6163   5462    626   1288   1059       C  
ATOM     33  CD  LYS A  20      19.684  -8.844  88.653  1.00 54.90           C  
ANISOU   33  CD  LYS A  20     8582   6614   5662    657   1214    998       C  
ATOM     34  CE  LYS A  20      19.102  -8.702  90.052  1.00 60.54           C  
ANISOU   34  CE  LYS A  20     9316   7406   6280    667   1256   1044       C  
ATOM     35  NZ  LYS A  20      19.298  -7.319  90.581  1.00 61.98           N  
ANISOU   35  NZ  LYS A  20     9395   7763   6391    707   1175    972       N  
ATOM     36  N   ALA A  21      22.505 -11.950  87.160  1.00 41.89           N  
ANISOU   36  N   ALA A  21     7211   4636   4069    928   1169   1108       N  
ATOM     37  CA  ALA A  21      23.471 -12.649  87.999  1.00 47.28           C  
ANISOU   37  CA  ALA A  21     7990   5318   4655   1097   1141   1177       C  
ATOM     38  C   ALA A  21      24.655 -11.782  88.414  1.00 50.13           C  
ANISOU   38  C   ALA A  21     8287   5838   4922   1249   1015   1135       C  
ATOM     39  O   ALA A  21      25.242 -11.079  87.594  1.00 45.10           O  
ANISOU   39  O   ALA A  21     7562   5256   4320   1261    936   1057       O  
ATOM     40  CB  ALA A  21      23.963 -13.910  87.296  1.00 44.13           C  
ANISOU   40  CB  ALA A  21     7687   4766   4314   1132   1166   1208       C  
ATOM     41  N   ARG A  22      25.004 -11.849  89.696  1.00 55.75           N  
ANISOU   41  N   ARG A  22     9041   6624   5516   1364    995   1184       N  
ATOM     42  CA  ARG A  22      26.188 -11.169  90.206  1.00 62.25           C  
ANISOU   42  CA  ARG A  22     9808   7597   6248   1521    873   1140       C  
ATOM     43  C   ARG A  22      27.375 -12.130  90.259  1.00 66.06           C  
ANISOU   43  C   ARG A  22    10371   8036   6694   1682    834   1177       C  
ATOM     44  O   ARG A  22      27.231 -13.284  90.660  1.00 67.21           O  
ANISOU   44  O   ARG A  22    10643   8073   6820   1712    905   1268       O  
ATOM     45  CB  ARG A  22      25.922 -10.591  91.598  1.00 67.22           C  
ANISOU   45  CB  ARG A  22    10424   8352   6764   1560    862   1155       C  
ATOM     46  CG  ARG A  22      27.141  -9.943  92.236  1.00 71.32           C  
ANISOU   46  CG  ARG A  22    10883   9030   7187   1725    734   1102       C  
ATOM     47  CD  ARG A  22      26.920  -9.648  93.711  1.00 78.22           C  
ANISOU   47  CD  ARG A  22    11775  10008   7936   1783    734   1131       C  
ATOM     48  NE  ARG A  22      28.170  -9.280  94.372  1.00 83.12           N  
ANISOU   48  NE  ARG A  22    12354  10764   8463   1958    614   1085       N  
ATOM     49  CZ  ARG A  22      29.003 -10.150  94.936  1.00 87.04           C  
ANISOU   49  CZ  ARG A  22    12938  11248   8885   2112    595   1141       C  
ATOM     50  NH1 ARG A  22      28.723 -11.447  94.926  1.00 88.27           N  
ANISOU   50  NH1 ARG A  22    13235  11255   9049   2114    689   1250       N  
ATOM     51  NH2 ARG A  22      30.120  -9.723  95.511  1.00 88.04           N  
ANISOU   51  NH2 ARG A  22    13008  11511   8932   2263    481   1082       N  
ATOM     52  N   ASN A  23      28.542 -11.647  89.844  1.00 69.29           N  
ANISOU   52  N   ASN A  23    10701   8532   7095   1783    721   1104       N  
ATOM     53  CA  ASN A  23      29.772 -12.430  89.902  1.00 76.19           C  
ANISOU   53  CA  ASN A  23    11626   9394   7929   1946    669   1121       C  
ATOM     54  C   ASN A  23      30.416 -12.311  91.283  1.00 81.53           C  
ANISOU   54  C   ASN A  23    12314  10194   8469   2100    611   1138       C  
ATOM     55  O   ASN A  23      30.636 -11.210  91.778  1.00 82.60           O  
ANISOU   55  O   ASN A  23    12345  10484   8555   2126    534   1070       O  
ATOM     56  CB  ASN A  23      30.739 -11.960  88.813  1.00 75.71           C  
ANISOU   56  CB  ASN A  23    11461   9380   7925   1981    576   1026       C  
ATOM     57  CG  ASN A  23      31.948 -12.872  88.656  1.00 79.54           C  
ANISOU   57  CG  ASN A  23    11995   9837   8390   2130    533   1037       C  
ATOM     58  OD1 ASN A  23      32.493 -13.385  89.634  1.00 82.10           O  
ANISOU   58  OD1 ASN A  23    12381  10192   8619   2262    515   1081       O  
ATOM     59  ND2 ASN A  23      32.374 -13.073  87.414  1.00 78.80           N  
ANISOU   59  ND2 ASN A  23    11871   9687   8384   2110    517    993       N  
ATOM     60  N   LYS A  24      30.721 -13.449  91.898  1.00 85.36           N  
ANISOU   60  N   LYS A  24    12927  10611   8895   2204    646   1225       N  
ATOM     61  CA  LYS A  24      31.264 -13.471  93.255  1.00 87.69           C  
ANISOU   61  CA  LYS A  24    13253  11012   9052   2355    602   1254       C  
ATOM     62  C   LYS A  24      32.656 -12.844  93.347  1.00 88.34           C  
ANISOU   62  C   LYS A  24    13226  11253   9086   2501    459   1157       C  
ATOM     63  O   LYS A  24      32.927 -12.037  94.237  1.00 88.47           O  
ANISOU   63  O   LYS A  24    13174  11421   9018   2564    391   1111       O  
ATOM     64  CB  LYS A  24      31.302 -14.907  93.782  1.00 89.58           C  
ANISOU   64  CB  LYS A  24    13663  11130   9245   2434    675   1375       C  
ATOM     65  CG  LYS A  24      29.962 -15.621  93.712  1.00 90.45           C  
ANISOU   65  CG  LYS A  24    13880  11077   9410   2287    821   1470       C  
ATOM     66  CD  LYS A  24      30.092 -17.088  94.090  1.00 93.58           C  
ANISOU   66  CD  LYS A  24    14444  11337   9776   2365    892   1585       C  
ATOM     67  CE  LYS A  24      28.764 -17.815  93.941  1.00 93.71           C  
ANISOU   67  CE  LYS A  24    14556  11185   9865   2204   1039   1669       C  
ATOM     68  NZ  LYS A  24      28.878 -19.261  94.280  1.00 95.17           N  
ANISOU   68  NZ  LYS A  24    14907  11225  10028   2274   1112   1783       N  
ATOM     69  N   LEU A  25      33.528 -13.220  92.418  1.00 88.48           N  
ANISOU   69  N   LEU A  25    13221  11236   9160   2548    416   1118       N  
ATOM     70  CA  LEU A  25      34.917 -12.766  92.410  1.00 89.71           C  
ANISOU   70  CA  LEU A  25    13270  11533   9281   2683    287   1023       C  
ATOM     71  C   LEU A  25      35.069 -11.268  92.127  1.00 88.86           C  
ANISOU   71  C   LEU A  25    12985  11572   9206   2626    202    897       C  
ATOM     72  O   LEU A  25      35.987 -10.623  92.636  1.00 88.95           O  
ANISOU   72  O   LEU A  25    12898  11740   9161   2727     97    814       O  
ATOM     73  CB  LEU A  25      35.721 -13.588  91.395  1.00 90.66           C  
ANISOU   73  CB  LEU A  25    13412  11571   9464   2730    274   1014       C  
ATOM     74  CG  LEU A  25      37.013 -13.016  90.803  1.00 91.07           C  
ANISOU   74  CG  LEU A  25    13320  11746   9538   2803    154    893       C  
ATOM     75  CD1 LEU A  25      38.164 -13.060  91.803  1.00 92.98           C  
ANISOU   75  CD1 LEU A  25    13539  12123   9666   2986     63    864       C  
ATOM     76  CD2 LEU A  25      37.374 -13.753  89.519  1.00 90.06           C  
ANISOU   76  CD2 LEU A  25    13212  11504   9504   2783    173    891       C  
ATOM     77  N   THR A  26      34.165 -10.716  91.322  1.00 87.29           N  
ANISOU   77  N   THR A  26    12743  11323   9101   2462    246    879       N  
ATOM     78  CA  THR A  26      34.264  -9.314  90.922  1.00 83.93           C  
ANISOU   78  CA  THR A  26    12152  11020   8718   2397    172    763       C  
ATOM     79  C   THR A  26      33.180  -8.424  91.526  1.00 78.69           C  
ANISOU   79  C   THR A  26    11459  10404   8034   2293    201    760       C  
ATOM     80  O   THR A  26      33.439  -7.273  91.876  1.00 79.81           O  
ANISOU   80  O   THR A  26    11478  10690   8158   2297    121    666       O  
ATOM     81  CB  THR A  26      34.238  -9.160  89.389  1.00 85.56           C  
ANISOU   81  CB  THR A  26    12302  11159   9048   2298    178    721       C  
ATOM     82  OG1 THR A  26      33.198  -9.981  88.846  1.00 87.04           O  
ANISOU   82  OG1 THR A  26    12607  11170   9294   2190    297    810       O  
ATOM     83  CG2 THR A  26      35.571  -9.578  88.788  1.00 86.59           C  
ANISOU   83  CG2 THR A  26    12394  11309   9196   2406    109    675       C  
ATOM     84  N   GLY A  27      31.968  -8.952  91.644  1.00 73.31           N  
ANISOU   84  N   GLY A  27    10886   9605   7365   2194    317    854       N  
ATOM     85  CA  GLY A  27      30.849  -8.162  92.126  1.00 70.25           C  
ANISOU   85  CA  GLY A  27    10470   9255   6967   2080    357    850       C  
ATOM     86  C   GLY A  27      30.095  -7.523  90.977  1.00 66.58           C  
ANISOU   86  C   GLY A  27     9935   8748   6614   1912    387    806       C  
ATOM     87  O   GLY A  27      29.124  -6.793  91.184  1.00 63.14           O  
ANISOU   87  O   GLY A  27     9461   8342   6187   1800    421    789       O  
ATOM     88  N   GLU A  28      30.546  -7.799  89.757  1.00 65.73           N  
ANISOU   88  N   GLU A  28     9811   8573   6591   1899    375    784       N  
ATOM     89  CA  GLU A  28      29.901  -7.265  88.564  1.00 64.66           C  
ANISOU   89  CA  GLU A  28     9615   8392   6560   1750    403    744       C  
ATOM     90  C   GLU A  28      28.631  -8.048  88.241  1.00 59.23           C  
ANISOU   90  C   GLU A  28     9032   7545   5927   1618    538    827       C  
ATOM     91  O   GLU A  28      28.585  -9.267  88.399  1.00 61.71           O  
ANISOU   91  O   GLU A  28     9469   7742   6234   1651    601    910       O  
ATOM     92  CB  GLU A  28      30.868  -7.278  87.379  1.00 71.68           C  
ANISOU   92  CB  GLU A  28    10448   9275   7514   1788    342    690       C  
ATOM     93  CG  GLU A  28      32.187  -6.576  87.671  1.00 79.43           C  
ANISOU   93  CG  GLU A  28    11312  10414   8454   1913    211    599       C  
ATOM     94  CD  GLU A  28      32.801  -5.937  86.441  1.00 83.33           C  
ANISOU   94  CD  GLU A  28    11687  10945   9029   1887    147    513       C  
ATOM     95  OE1 GLU A  28      33.023  -6.652  85.439  1.00 84.33           O  
ANISOU   95  OE1 GLU A  28    11854  10971   9215   1884    174    537       O  
ATOM     96  OE2 GLU A  28      33.057  -4.714  86.476  1.00 84.26           O  
ANISOU   96  OE2 GLU A  28    11670  11193   9153   1867     72    417       O  
ATOM     97  N   VAL A  29      27.601  -7.338  87.793  1.00 51.23           N  
ANISOU   97  N   VAL A  29     7963   6528   4972   1465    581    795       N  
ATOM     98  CA  VAL A  29      26.296  -7.945  87.563  1.00 44.44           C  
ANISOU   98  CA  VAL A  29     7177   5537   4170   1323    706    855       C  
ATOM     99  C   VAL A  29      25.946  -7.971  86.075  1.00 40.52           C  
ANISOU   99  C   VAL A  29     6654   4948   3792   1207    739    822       C  
ATOM    100  O   VAL A  29      26.200  -7.006  85.352  1.00 36.72           O  
ANISOU  100  O   VAL A  29     6067   4541   3345   1179    679    742       O  
ATOM    101  CB  VAL A  29      25.201  -7.189  88.333  1.00 43.17           C  
ANISOU  101  CB  VAL A  29     6974   5446   3981   1228    746    845       C  
ATOM    102  CG1 VAL A  29      23.886  -7.946  88.273  1.00 42.82           C  
ANISOU  102  CG1 VAL A  29     7004   5274   3991   1093    878    909       C  
ATOM    103  CG2 VAL A  29      25.629  -6.979  89.783  1.00 48.36           C  
ANISOU  103  CG2 VAL A  29     7643   6218   4514   1350    699    861       C  
ATOM    104  N   VAL A  30      25.366  -9.078  85.621  1.00 37.96           N  
ANISOU  104  N   VAL A  30     6425   4465   3533   1138    833    878       N  
ATOM    105  CA  VAL A  30      25.011  -9.226  84.213  1.00 35.00           C  
ANISOU  105  CA  VAL A  30     6034   3992   3272   1028    868    844       C  
ATOM    106  C   VAL A  30      23.536  -9.558  84.052  1.00 38.15           C  
ANISOU  106  C   VAL A  30     6455   4296   3746    856    980    861       C  
ATOM    107  O   VAL A  30      22.876  -9.967  85.005  1.00 38.06           O  
ANISOU  107  O   VAL A  30     6497   4266   3700    834   1043    918       O  
ATOM    108  CB  VAL A  30      25.850 -10.316  83.525  1.00 34.74           C  
ANISOU  108  CB  VAL A  30     6080   3847   3273   1107    861    868       C  
ATOM    109  CG1 VAL A  30      27.321  -9.951  83.571  1.00 33.30           C  
ANISOU  109  CG1 VAL A  30     5853   3771   3031   1273    743    836       C  
ATOM    110  CG2 VAL A  30      25.606 -11.665  84.183  1.00 37.21           C  
ANISOU  110  CG2 VAL A  30     6526   4040   3570   1132    938    955       C  
ATOM    111  N   ALA A  31      23.030  -9.374  82.838  1.00 34.18           N  
ANISOU  111  N   ALA A  31     5904   3739   3345    735   1004    807       N  
ATOM    112  CA  ALA A  31      21.642  -9.673  82.519  1.00 32.84           C  
ANISOU  112  CA  ALA A  31     5731   3484   3262    564   1101    800       C  
ATOM    113  C   ALA A  31      21.582 -10.588  81.305  1.00 40.51           C  
ANISOU  113  C   ALA A  31     6746   4306   4338    505   1137    785       C  
ATOM    114  O   ALA A  31      22.340 -10.411  80.348  1.00 40.53           O  
ANISOU  114  O   ALA A  31     6726   4305   4367    544   1083    744       O  
ATOM    115  CB  ALA A  31      20.880  -8.393  82.242  1.00 32.33           C  
ANISOU  115  CB  ALA A  31     5536   3521   3227    455   1090    725       C  
ATOM    116  N   LEU A  32      20.671 -11.555  81.338  1.00 37.01           N  
ANISOU  116  N   LEU A  32     6361   3745   3955    410   1228    811       N  
ATOM    117  CA  LEU A  32      20.531 -12.504  80.243  1.00 41.26           C  
ANISOU  117  CA  LEU A  32     6940   4141   4597    347   1263    785       C  
ATOM    118  C   LEU A  32      19.259 -12.257  79.439  1.00 45.36           C  
ANISOU  118  C   LEU A  32     7375   4636   5222    163   1308    709       C  
ATOM    119  O   LEU A  32      18.156 -12.272  79.980  1.00 49.15           O  
ANISOU  119  O   LEU A  32     7832   5122   5719     66   1369    717       O  
ATOM    120  CB  LEU A  32      20.545 -13.937  80.771  1.00 43.09           C  
ANISOU  120  CB  LEU A  32     7301   4247   4825    382   1326    860       C  
ATOM    121  CG  LEU A  32      20.608 -15.036  79.711  1.00 45.49           C  
ANISOU  121  CG  LEU A  32     7657   4402   5224    344   1352    832       C  
ATOM    122  CD1 LEU A  32      21.939 -14.987  78.977  1.00 45.61           C  
ANISOU  122  CD1 LEU A  32     7679   4425   5225    467   1269    806       C  
ATOM    123  CD2 LEU A  32      20.386 -16.405  80.339  1.00 48.48           C  
ANISOU  123  CD2 LEU A  32     8159   4657   5606    353   1429    909       C  
ATOM    124  N   LYS A  33      19.427 -12.028  78.141  1.00 40.23           N  
ANISOU  124  N   LYS A  33     6675   3968   4643    121   1274    633       N  
ATOM    125  CA  LYS A  33      18.301 -11.808  77.244  1.00 44.80           C  
ANISOU  125  CA  LYS A  33     7165   4532   5324    -42   1300    547       C  
ATOM    126  C   LYS A  33      18.178 -12.992  76.292  1.00 45.84           C  
ANISOU  126  C   LYS A  33     7346   4523   5546    -92   1329    512       C  
ATOM    127  O   LYS A  33      19.180 -13.581  75.891  1.00 44.47           O  
ANISOU  127  O   LYS A  33     7243   4287   5366      3   1301    526       O  
ATOM    128  CB  LYS A  33      18.487 -10.499  76.472  1.00 50.31           C  
ANISOU  128  CB  LYS A  33     7749   5335   6030    -61   1235    475       C  
ATOM    129  CG  LYS A  33      17.432 -10.213  75.413  1.00 56.03           C  
ANISOU  129  CG  LYS A  33     8372   6059   6857   -213   1244    374       C  
ATOM    130  CD  LYS A  33      17.659  -8.846  74.785  1.00 58.13           C  
ANISOU  130  CD  LYS A  33     8528   6441   7119   -220   1180    314       C  
ATOM    131  CE  LYS A  33      17.019  -8.742  73.409  1.00 58.37           C  
ANISOU  131  CE  LYS A  33     8470   6457   7249   -331   1160    207       C  
ATOM    132  NZ  LYS A  33      17.307  -7.420  72.780  1.00 55.42           N  
ANISOU  132  NZ  LYS A  33     7959   6226   6872   -309   1059    133       N  
ATOM    133  N   LYS A  34      16.945 -13.347  75.945  1.00 49.45           N  
ANISOU  133  N   LYS A  34     7761   4940   6089   -236   1381    462       N  
ATOM    134  CA  LYS A  34      16.691 -14.516  75.112  1.00 53.72           C  
ANISOU  134  CA  LYS A  34     8341   5354   6716   -294   1410    422       C  
ATOM    135  C   LYS A  34      15.886 -14.146  73.871  1.00 55.81           C  
ANISOU  135  C   LYS A  34     8490   5643   7071   -420   1388    301       C  
ATOM    136  O   LYS A  34      15.000 -13.291  73.925  1.00 55.59           O  
ANISOU  136  O   LYS A  34     8357   5707   7057   -503   1385    258       O  
ATOM    137  CB  LYS A  34      15.951 -15.582  75.922  1.00 59.99           C  
ANISOU  137  CB  LYS A  34     9207   6059   7528   -342   1499    480       C  
ATOM    138  CG  LYS A  34      15.670 -16.871  75.172  1.00 68.46           C  
ANISOU  138  CG  LYS A  34    10326   6993   8691   -403   1534    445       C  
ATOM    139  CD  LYS A  34      14.897 -17.851  76.042  1.00 78.51           C  
ANISOU  139  CD  LYS A  34    11668   8178   9984   -457   1630    510       C  
ATOM    140  CE  LYS A  34      13.527 -17.302  76.421  1.00 84.15           C  
ANISOU  140  CE  LYS A  34    12284   8964  10727   -585   1672    482       C  
ATOM    141  NZ  LYS A  34      12.630 -17.161  75.240  1.00 86.57           N  
ANISOU  141  NZ  LYS A  34    12475   9283  11134   -715   1654    357       N  
ATOM    142  N   ILE A  35      16.210 -14.783  72.749  1.00 55.64           N  
ANISOU  142  N   ILE A  35     8484   5549   7106   -425   1364    241       N  
ATOM    143  CA  ILE A  35      15.434 -14.634  71.523  1.00 56.59           C  
ANISOU  143  CA  ILE A  35     8503   5688   7310   -537   1339    122       C  
ATOM    144  C   ILE A  35      15.092 -16.004  70.940  1.00 58.60           C  
ANISOU  144  C   ILE A  35     8806   5819   7642   -590   1372     87       C  
ATOM    145  O   ILE A  35      15.984 -16.784  70.600  1.00 59.29           O  
ANISOU  145  O   ILE A  35     8979   5820   7728   -513   1360    102       O  
ATOM    146  CB  ILE A  35      16.195 -13.824  70.455  1.00 59.51           C  
ANISOU  146  CB  ILE A  35     8817   6122   7672   -492   1255     57       C  
ATOM    147  CG1 ILE A  35      16.657 -12.479  71.020  1.00 57.66           C  
ANISOU  147  CG1 ILE A  35     8542   6000   7365   -434   1222     96       C  
ATOM    148  CG2 ILE A  35      15.322 -13.619  69.222  1.00 60.51           C  
ANISOU  148  CG2 ILE A  35     8832   6288   7872   -602   1223    -66       C  
ATOM    149  CD1 ILE A  35      17.416 -11.630  70.024  1.00 56.87           C  
ANISOU  149  CD1 ILE A  35     8388   5958   7260   -391   1147     38       C  
ATOM    150  N   ARG A  36      13.800 -16.296  70.834  1.00 58.83           N  
ANISOU  150  N   ARG A  36     8776   5838   7738   -718   1411     38       N  
ATOM    151  CA  ARG A  36      13.350 -17.535  70.214  1.00 62.62           C  
ANISOU  151  CA  ARG A  36     9286   6204   8301   -785   1439     -9       C  
ATOM    152  C   ARG A  36      13.456 -17.412  68.698  1.00 63.26           C  
ANISOU  152  C   ARG A  36     9298   6311   8427   -804   1364   -128       C  
ATOM    153  O   ARG A  36      13.225 -16.340  68.138  1.00 64.30           O  
ANISOU  153  O   ARG A  36     9320   6562   8548   -826   1308   -192       O  
ATOM    154  CB  ARG A  36      11.911 -17.854  70.623  1.00 64.58           C  
ANISOU  154  CB  ARG A  36     9487   6441   8609   -915   1506    -25       C  
ATOM    155  N   LEU A  37      13.813 -18.508  68.037  1.00 62.45           N  
ANISOU  155  N   LEU A  37     9260   6099   8370   -792   1362   -158       N  
ATOM    156  CA  LEU A  37      13.999 -18.495  66.591  1.00 63.16           C  
ANISOU  156  CA  LEU A  37     9296   6210   8494   -797   1288   -271       C  
ATOM    157  C   LEU A  37      12.855 -19.205  65.871  1.00 67.29           C  
ANISOU  157  C   LEU A  37     9766   6692   9111   -920   1298   -368       C  
ATOM    158  O   LEU A  37      12.664 -20.411  66.029  1.00 70.07           O  
ANISOU  158  O   LEU A  37    10194   6912   9518   -951   1349   -355       O  
ATOM    159  CB  LEU A  37      15.334 -19.141  66.224  1.00 59.53           C  
ANISOU  159  CB  LEU A  37     8937   5670   8014   -677   1261   -251       C  
ATOM    160  CG  LEU A  37      16.578 -18.519  66.856  1.00 54.23           C  
ANISOU  160  CG  LEU A  37     8317   5038   7250   -539   1242   -162       C  
ATOM    161  CD1 LEU A  37      17.787 -19.382  66.568  1.00 53.88           C  
ANISOU  161  CD1 LEU A  37     8374   4903   7196   -420   1223   -143       C  
ATOM    162  CD2 LEU A  37      16.792 -17.101  66.348  1.00 50.36           C  
ANISOU  162  CD2 LEU A  37     7723   4693   6717   -522   1175   -207       C  
ATOM    163  N   GLU A  42      11.524 -17.213  59.405  1.00 46.05           N  
ANISOU  163  N   GLU A  42     6613   4425   6459  -1012    901   -942       N  
ATOM    164  CA  GLU A  42      12.425 -16.443  58.554  1.00 42.26           C  
ANISOU  164  CA  GLU A  42     6114   4035   5909   -919    825   -968       C  
ATOM    165  C   GLU A  42      13.857 -16.457  59.079  1.00 33.95           C  
ANISOU  165  C   GLU A  42     5161   2930   4808   -808    845   -878       C  
ATOM    166  O   GLU A  42      14.714 -15.716  58.592  1.00 33.43           O  
ANISOU  166  O   GLU A  42     5083   2941   4680   -724    796   -880       O  
ATOM    167  CB  GLU A  42      11.931 -15.002  58.411  1.00 46.20           C  
ANISOU  167  CB  GLU A  42     6495   4695   6364   -930    781   -978       C  
ATOM    168  CG  GLU A  42      10.633 -14.867  57.634  1.00 50.66           C  
ANISOU  168  CG  GLU A  42     6950   5338   6962  -1011    739  -1080       C  
ATOM    169  CD  GLU A  42      10.755 -15.365  56.202  1.00 52.34           C  
ANISOU  169  CD  GLU A  42     7159   5556   7172   -990    670  -1189       C  
ATOM    170  OE1 GLU A  42      11.728 -14.984  55.514  1.00 47.69           O  
ANISOU  170  OE1 GLU A  42     6591   5010   6520   -898    621  -1197       O  
ATOM    171  OE2 GLU A  42       9.879 -16.143  55.768  1.00 52.54           O  
ANISOU  171  OE2 GLU A  42     7160   5545   7257  -1063    667  -1269       O  
ATOM    172  N   GLY A  43      14.116 -17.305  60.070  1.00 29.00           N  
ANISOU  172  N   GLY A  43     4634   2176   4208   -803    917   -799       N  
ATOM    173  CA  GLY A  43      15.439 -17.397  60.668  1.00 28.34           C  
ANISOU  173  CA  GLY A  43     4649   2041   4078   -689    937   -708       C  
ATOM    174  C   GLY A  43      15.703 -16.286  61.666  1.00 30.41           C  
ANISOU  174  C   GLY A  43     4896   2377   4282   -658    955   -616       C  
ATOM    175  O   GLY A  43      14.783 -15.786  62.314  1.00 29.19           O  
ANISOU  175  O   GLY A  43     4687   2266   4137   -735    985   -594       O  
ATOM    176  N   VAL A  44      16.964 -15.888  61.797  1.00 25.67           N  
ANISOU  176  N   VAL A  44     4339   1793   3621   -541    936   -566       N  
ATOM    177  CA  VAL A  44      17.313 -14.811  62.719  1.00 25.93           C  
ANISOU  177  CA  VAL A  44     4360   1893   3598   -502    947   -485       C  
ATOM    178  C   VAL A  44      16.704 -13.483  62.281  1.00 27.70           C  
ANISOU  178  C   VAL A  44     4459   2259   3806   -554    902   -536       C  
ATOM    179  O   VAL A  44      16.924 -13.036  61.158  1.00 24.84           O  
ANISOU  179  O   VAL A  44     4038   1971   3427   -532    839   -609       O  
ATOM    180  CB  VAL A  44      18.834 -14.647  62.850  1.00 28.03           C  
ANISOU  180  CB  VAL A  44     4688   2158   3805   -357    926   -433       C  
ATOM    181  CG1 VAL A  44      19.165 -13.557  63.857  1.00 26.29           C  
ANISOU  181  CG1 VAL A  44     4458   2002   3531   -317    935   -354       C  
ATOM    182  CG2 VAL A  44      19.468 -15.970  63.253  1.00 32.89           C  
ANISOU  182  CG2 VAL A  44     5425   2640   4433   -290    962   -383       C  
ATOM    183  N   PRO A  45      15.925 -12.851  63.174  1.00 25.52           N  
ANISOU  183  N   PRO A  45     4141   2025   3531   -617    933   -495       N  
ATOM    184  CA  PRO A  45      15.278 -11.568  62.883  1.00 25.32           C  
ANISOU  184  CA  PRO A  45     3994   2133   3494   -663    892   -537       C  
ATOM    185  C   PRO A  45      16.292 -10.509  62.465  1.00 23.36           C  
ANISOU  185  C   PRO A  45     3722   1966   3188   -576    837   -538       C  
ATOM    186  O   PRO A  45      17.380 -10.440  63.037  1.00 21.25           O  
ANISOU  186  O   PRO A  45     3526   1666   2883   -485    850   -473       O  
ATOM    187  CB  PRO A  45      14.648 -11.188  64.228  1.00 28.21           C  
ANISOU  187  CB  PRO A  45     4353   2509   3858   -708    947   -466       C  
ATOM    188  CG  PRO A  45      14.402 -12.492  64.899  1.00 31.88           C  
ANISOU  188  CG  PRO A  45     4908   2850   4356   -733   1019   -421       C  
ATOM    189  CD  PRO A  45      15.538 -13.380  64.493  1.00 27.80           C  
ANISOU  189  CD  PRO A  45     4492   2238   3832   -646   1012   -410       C  
ATOM    190  N   SER A  46      15.933  -9.694  61.479  1.00 16.98           N  
ANISOU  190  N   SER A  46     2814   1266   2370   -596    775   -612       N  
ATOM    191  CA  SER A  46      16.811  -8.634  61.006  1.00 22.34           C  
ANISOU  191  CA  SER A  46     3461   2034   2995   -519    726   -617       C  
ATOM    192  C   SER A  46      17.138  -7.645  62.118  1.00 22.91           C  
ANISOU  192  C   SER A  46     3508   2166   3031   -481    729   -527       C  
ATOM    193  O   SER A  46      18.237  -7.097  62.163  1.00 17.22           O  
ANISOU  193  O   SER A  46     2780   1500   2261   -382    696   -481       O  
ATOM    194  CB  SER A  46      16.193  -7.911  59.807  1.00 26.31           C  
ANISOU  194  CB  SER A  46     3856   2652   3488   -549    659   -698       C  
ATOM    195  OG  SER A  46      14.977  -7.283  60.159  1.00 33.15           O  
ANISOU  195  OG  SER A  46     4638   3579   4378   -631    656   -707       O  
ATOM    196  N   THR A  47      16.191  -7.430  63.030  1.00 21.41           N  
ANISOU  196  N   THR A  47     3295   1974   2866   -557    765   -502       N  
ATOM    197  CA  THR A  47      16.448  -6.567  64.174  1.00 22.65           C  
ANISOU  197  CA  THR A  47     3429   2193   2985   -517    767   -418       C  
ATOM    198  C   THR A  47      17.548  -7.127  65.074  1.00 20.90           C  
ANISOU  198  C   THR A  47     3307   1906   2727   -425    796   -331       C  
ATOM    199  O   THR A  47      18.347  -6.372  65.622  1.00 24.78           O  
ANISOU  199  O   THR A  47     3778   2468   3170   -344    766   -277       O  
ATOM    200  CB  THR A  47      15.173  -6.326  65.001  1.00 24.80           C  
ANISOU  200  CB  THR A  47     3662   2475   3287   -616    811   -413       C  
ATOM    201  OG1 THR A  47      14.569  -7.586  65.319  1.00 24.84           O  
ANISOU  201  OG1 THR A  47     3744   2353   3343   -691    888   -416       O  
ATOM    202  CG2 THR A  47      14.189  -5.487  64.206  1.00 29.43           C  
ANISOU  202  CG2 THR A  47     4129   3158   3896   -680    765   -493       C  
ATOM    203  N   ALA A  48      17.580  -8.445  65.231  1.00 18.91           N  
ANISOU  203  N   ALA A  48     3163   1519   2504   -436    853   -320       N  
ATOM    204  CA  ALA A  48      18.624  -9.101  66.015  1.00 19.24           C  
ANISOU  204  CA  ALA A  48     3311   1490   2510   -335    878   -237       C  
ATOM    205  C   ALA A  48      19.962  -9.056  65.279  1.00 22.07           C  
ANISOU  205  C   ALA A  48     3671   1880   2835   -218    821   -249       C  
ATOM    206  O   ALA A  48      21.008  -8.828  65.888  1.00 20.46           O  
ANISOU  206  O   ALA A  48     3485   1709   2581   -111    802   -187       O  
ATOM    207  CB  ALA A  48      18.240 -10.541  66.315  1.00 24.05           C  
ANISOU  207  CB  ALA A  48     4043   1931   3165   -379    959   -220       C  
ATOM    208  N   ILE A  49      19.913  -9.300  63.971  1.00 20.00           N  
ANISOU  208  N   ILE A  49     3388   1611   2599   -239    797   -335       N  
ATOM    209  CA  ILE A  49      21.089  -9.204  63.106  1.00 21.45           C  
ANISOU  209  CA  ILE A  49     3560   1839   2751   -138    749   -359       C  
ATOM    210  C   ILE A  49      21.772  -7.847  63.293  1.00 22.14           C  
ANISOU  210  C   ILE A  49     3554   2070   2790    -77    696   -325       C  
ATOM    211  O   ILE A  49      22.970  -7.765  63.596  1.00 19.68           O  
ANISOU  211  O   ILE A  49     3253   1783   2440     30    678   -283       O  
ATOM    212  CB  ILE A  49      20.696  -9.378  61.614  1.00 20.64           C  
ANISOU  212  CB  ILE A  49     3424   1745   2672   -184    726   -466       C  
ATOM    213  CG1 ILE A  49      20.295 -10.822  61.312  1.00 26.54           C  
ANISOU  213  CG1 ILE A  49     4263   2348   3471   -225    768   -511       C  
ATOM    214  CG2 ILE A  49      21.838  -8.953  60.692  1.00 22.71           C  
ANISOU  214  CG2 ILE A  49     3648   2092   2890    -86    677   -487       C  
ATOM    215  CD1 ILE A  49      21.388 -11.820  61.554  1.00 28.68           C  
ANISOU  215  CD1 ILE A  49     4632   2533   3732   -119    784   -468       C  
ATOM    216  N   ARG A  50      21.001  -6.778  63.131  1.00 17.14           N  
ANISOU  216  N   ARG A  50     2826   1528   2160   -146    671   -346       N  
ATOM    217  CA  ARG A  50      21.544  -5.432  63.284  1.00 18.78           C  
ANISOU  217  CA  ARG A  50     2944   1858   2333   -103    625   -319       C  
ATOM    218  C   ARG A  50      21.965  -5.112  64.721  1.00 18.53           C  
ANISOU  218  C   ARG A  50     2924   1841   2274    -56    632   -242       C  
ATOM    219  O   ARG A  50      23.059  -4.601  64.941  1.00 17.40           O  
ANISOU  219  O   ARG A  50     2754   1758   2101     28    600   -214       O  
ATOM    220  CB  ARG A  50      20.541  -4.389  62.792  1.00 19.32           C  
ANISOU  220  CB  ARG A  50     2917   2008   2415   -183    598   -359       C  
ATOM    221  CG  ARG A  50      20.291  -4.448  61.292  1.00 20.79           C  
ANISOU  221  CG  ARG A  50     3075   2217   2607   -206    573   -435       C  
ATOM    222  CD  ARG A  50      19.129  -3.543  60.915  1.00 18.45           C  
ANISOU  222  CD  ARG A  50     2695   1991   2325   -282    547   -472       C  
ATOM    223  NE  ARG A  50      19.048  -3.326  59.470  1.00 19.59           N  
ANISOU  223  NE  ARG A  50     2802   2188   2453   -280    510   -534       N  
ATOM    224  CZ  ARG A  50      18.094  -2.613  58.882  1.00 21.22           C  
ANISOU  224  CZ  ARG A  50     2939   2462   2663   -329    477   -575       C  
ATOM    225  NH1 ARG A  50      17.132  -2.057  59.619  1.00 16.71           N  
ANISOU  225  NH1 ARG A  50     2322   1910   2118   -387    479   -565       N  
ATOM    226  NH2 ARG A  50      18.096  -2.458  57.560  1.00 18.05           N  
ANISOU  226  NH2 ARG A  50     2514   2111   2231   -313    443   -626       N  
ATOM    227  N   GLU A  51      21.099  -5.401  65.689  1.00 17.05           N  
ANISOU  227  N   GLU A  51     2775   1607   2098   -112    674   -212       N  
ATOM    228  CA  GLU A  51      21.409  -5.095  67.086  1.00 18.59           C  
ANISOU  228  CA  GLU A  51     2985   1824   2254    -66    681   -141       C  
ATOM    229  C   GLU A  51      22.741  -5.701  67.511  1.00 16.90           C  
ANISOU  229  C   GLU A  51     2839   1582   2002     56    674    -94       C  
ATOM    230  O   GLU A  51      23.589  -5.014  68.069  1.00 17.95           O  
ANISOU  230  O   GLU A  51     2932   1793   2096    132    635    -68       O  
ATOM    231  CB  GLU A  51      20.293  -5.581  68.024  1.00 21.78           C  
ANISOU  231  CB  GLU A  51     3440   2165   2668   -141    746   -110       C  
ATOM    232  CG  GLU A  51      20.621  -5.380  69.497  1.00 28.45           C  
ANISOU  232  CG  GLU A  51     4317   3034   3458    -83    758    -34       C  
ATOM    233  CD  GLU A  51      19.436  -5.648  70.412  1.00 43.34           C  
ANISOU  233  CD  GLU A  51     6237   4881   5348   -165    828     -3       C  
ATOM    234  OE1 GLU A  51      18.402  -6.161  69.929  1.00 48.67           O  
ANISOU  234  OE1 GLU A  51     6918   5493   6079   -269    874    -39       O  
ATOM    235  OE2 GLU A  51      19.543  -5.342  71.616  1.00 45.73           O  
ANISOU  235  OE2 GLU A  51     6556   5222   5596   -125    839     53       O  
ATOM    236  N   ILE A  52      22.929  -6.985  67.219  1.00 17.03           N  
ANISOU  236  N   ILE A  52     2952   1485   2031     79    709    -92       N  
ATOM    237  CA  ILE A  52      24.125  -7.687  67.663  1.00 15.42           C  
ANISOU  237  CA  ILE A  52     2824   1243   1792    205    705    -45       C  
ATOM    238  C   ILE A  52      25.366  -7.224  66.900  1.00 17.98           C  
ANISOU  238  C   ILE A  52     3081   1649   2102    292    647    -78       C  
ATOM    239  O   ILE A  52      26.384  -6.882  67.503  1.00 15.83           O  
ANISOU  239  O   ILE A  52     2786   1439   1789    391    613    -45       O  
ATOM    240  CB  ILE A  52      23.968  -9.214  67.533  1.00 18.43           C  
ANISOU  240  CB  ILE A  52     3336   1467   2199    208    763    -34       C  
ATOM    241  CG1 ILE A  52      22.798  -9.697  68.403  1.00 19.90           C  
ANISOU  241  CG1 ILE A  52     3592   1568   2401    119    834     10       C  
ATOM    242  CG2 ILE A  52      25.260  -9.918  67.925  1.00 22.69           C  
ANISOU  242  CG2 ILE A  52     3951   1969   2700    357    752     13       C  
ATOM    243  CD1 ILE A  52      22.474 -11.175  68.230  1.00 18.62           C  
ANISOU  243  CD1 ILE A  52     3559   1232   2284     95    901     16       C  
ATOM    244  N   SER A  53      25.282  -7.204  65.573  1.00 19.05           N  
ANISOU  244  N   SER A  53     3179   1791   2269    256    638   -145       N  
ATOM    245  CA  SER A  53      26.441  -6.827  64.769  1.00 13.61           C  
ANISOU  245  CA  SER A  53     2428   1176   1566    334    597   -175       C  
ATOM    246  C   SER A  53      26.890  -5.395  65.055  1.00 19.08           C  
ANISOU  246  C   SER A  53     3006   2003   2241    345    552   -165       C  
ATOM    247  O   SER A  53      28.083  -5.115  65.057  1.00 19.42           O  
ANISOU  247  O   SER A  53     3007   2108   2265    433    522   -161       O  
ATOM    248  CB  SER A  53      26.174  -7.028  63.268  1.00 17.58           C  
ANISOU  248  CB  SER A  53     2914   1670   2094    290    600   -249       C  
ATOM    249  OG  SER A  53      25.164  -6.152  62.801  1.00 19.86           O  
ANISOU  249  OG  SER A  53     3132   2014   2400    186    589   -281       O  
ATOM    250  N   LEU A  54      25.944  -4.494  65.321  1.00 15.80           N  
ANISOU  250  N   LEU A  54     2538   1629   1837    256    547   -166       N  
ATOM    251  CA  LEU A  54      26.305  -3.110  65.627  1.00 16.55           C  
ANISOU  251  CA  LEU A  54     2529   1835   1923    261    506   -160       C  
ATOM    252  C   LEU A  54      26.815  -2.941  67.066  1.00 18.50           C  
ANISOU  252  C   LEU A  54     2784   2108   2136    325    491   -113       C  
ATOM    253  O   LEU A  54      27.814  -2.259  67.298  1.00 17.00           O  
ANISOU  253  O   LEU A  54     2528   1998   1934    385    451   -114       O  
ATOM    254  CB  LEU A  54      25.141  -2.154  65.327  1.00 16.33           C  
ANISOU  254  CB  LEU A  54     2440   1844   1921    155    502   -184       C  
ATOM    255  CG  LEU A  54      24.682  -2.128  63.860  1.00 17.24           C  
ANISOU  255  CG  LEU A  54     2532   1960   2058    104    503   -235       C  
ATOM    256  CD1 LEU A  54      23.544  -1.125  63.652  1.00 19.11           C  
ANISOU  256  CD1 LEU A  54     2705   2241   2315     15    491   -254       C  
ATOM    257  CD2 LEU A  54      25.842  -1.849  62.907  1.00 17.66           C  
ANISOU  257  CD2 LEU A  54     2541   2067   2102    165    484   -251       C  
ATOM    258  N   LEU A  55      26.156  -3.581  68.030  1.00 15.95           N  
ANISOU  258  N   LEU A  55     2543   1721   1794    312    523    -73       N  
ATOM    259  CA  LEU A  55      26.602  -3.486  69.422  1.00 18.94           C  
ANISOU  259  CA  LEU A  55     2942   2130   2124    382    509    -26       C  
ATOM    260  C   LEU A  55      28.016  -4.002  69.655  1.00 21.87           C  
ANISOU  260  C   LEU A  55     3335   2513   2463    516    481     -8       C  
ATOM    261  O   LEU A  55      28.728  -3.484  70.516  1.00 24.77           O  
ANISOU  261  O   LEU A  55     3663   2957   2792    586    439      4       O  
ATOM    262  CB  LEU A  55      25.636  -4.194  70.369  1.00 20.62           C  
ANISOU  262  CB  LEU A  55     3253   2267   2317    349    563     24       C  
ATOM    263  CG  LEU A  55      24.462  -3.335  70.810  1.00 22.81           C  
ANISOU  263  CG  LEU A  55     3481   2583   2602    250    575     16       C  
ATOM    264  CD1 LEU A  55      23.503  -4.169  71.647  1.00 25.78           C  
ANISOU  264  CD1 LEU A  55     3957   2878   2962    210    645     66       C  
ATOM    265  CD2 LEU A  55      24.968  -2.122  71.600  1.00 26.00           C  
ANISOU  265  CD2 LEU A  55     3802   3102   2973    292    521     11       C  
ATOM    266  N   LYS A  56      28.420  -5.019  68.901  1.00 24.67           N  
ANISOU  266  N   LYS A  56     3748   2796   2830    556    500    -15       N  
ATOM    267  CA  LYS A  56      29.778  -5.553  69.009  1.00 32.49           C  
ANISOU  267  CA  LYS A  56     4753   3798   3793    693    473     -6       C  
ATOM    268  C   LYS A  56      30.833  -4.490  68.699  1.00 31.72           C  
ANISOU  268  C   LYS A  56     4521   3829   3701    731    417    -47       C  
ATOM    269  O   LYS A  56      31.951  -4.545  69.212  1.00 34.30           O  
ANISOU  269  O   LYS A  56     4825   4209   3999    843    379    -41       O  
ATOM    270  CB  LYS A  56      29.962  -6.770  68.089  1.00 38.30           C  
ANISOU  270  CB  LYS A  56     5568   4432   4551    722    506    -20       C  
ATOM    271  CG  LYS A  56      29.150  -7.982  68.517  1.00 43.81           C  
ANISOU  271  CG  LYS A  56     6411   4987   5249    703    564     25       C  
ATOM    272  CD  LYS A  56      29.329  -9.161  67.575  1.00 46.34           C  
ANISOU  272  CD  LYS A  56     6808   5198   5600    730    594     -2       C  
ATOM    273  CE  LYS A  56      30.458 -10.079  68.026  1.00 50.92           C  
ANISOU  273  CE  LYS A  56     7464   5737   6146    889    584     35       C  
ATOM    274  NZ  LYS A  56      31.804  -9.460  67.885  1.00 50.29           N  
ANISOU  274  NZ  LYS A  56     7279   5787   6044    994    523      8       N  
ATOM    275  N   GLU A  57      30.469  -3.526  67.861  1.00 21.53           N  
ANISOU  275  N   GLU A  57     3142   2588   2452    639    414    -88       N  
ATOM    276  CA  GLU A  57      31.372  -2.439  67.491  1.00 25.99           C  
ANISOU  276  CA  GLU A  57     3579   3262   3034    653    374   -125       C  
ATOM    277  C   GLU A  57      31.221  -1.186  68.350  1.00 29.67           C  
ANISOU  277  C   GLU A  57     3967   3807   3500    618    339   -127       C  
ATOM    278  O   GLU A  57      31.965  -0.223  68.171  1.00 39.72           O  
ANISOU  278  O   GLU A  57     5132   5165   4797    622    308   -158       O  
ATOM    279  CB  GLU A  57      31.150  -2.042  66.030  1.00 27.12           C  
ANISOU  279  CB  GLU A  57     3672   3413   3217    582    394   -163       C  
ATOM    280  CG  GLU A  57      31.375  -3.170  65.039  1.00 34.20           C  
ANISOU  280  CG  GLU A  57     4632   4247   4115    618    425   -179       C  
ATOM    281  CD  GLU A  57      31.449  -2.678  63.608  1.00 42.92           C  
ANISOU  281  CD  GLU A  57     5675   5392   5243    573    437   -219       C  
ATOM    282  OE1 GLU A  57      31.626  -1.456  63.401  1.00 42.24           O  
ANISOU  282  OE1 GLU A  57     5490   5386   5175    533    422   -226       O  
ATOM    283  OE2 GLU A  57      31.336  -3.516  62.689  1.00 51.32           O  
ANISOU  283  OE2 GLU A  57     6792   6402   6304    580    464   -243       O  
ATOM    284  N   LEU A  58      30.261  -1.184  69.267  1.00 21.24           N  
ANISOU  284  N   LEU A  58     2951   2710   2409    579    349    -98       N  
ATOM    285  CA  LEU A  58      29.962   0.034  70.019  1.00 19.90           C  
ANISOU  285  CA  LEU A  58     2710   2609   2241    538    320   -110       C  
ATOM    286  C   LEU A  58      30.329  -0.058  71.497  1.00 27.61           C  
ANISOU  286  C   LEU A  58     3711   3623   3157    618    289    -87       C  
ATOM    287  O   LEU A  58      29.465   0.058  72.367  1.00 29.94           O  
ANISOU  287  O   LEU A  58     4045   3908   3422    587    302    -65       O  
ATOM    288  CB  LEU A  58      28.489   0.413  69.857  1.00 19.86           C  
ANISOU  288  CB  LEU A  58     2718   2568   2258    423    352   -109       C  
ATOM    289  CG  LEU A  58      28.051   0.786  68.438  1.00 21.09           C  
ANISOU  289  CG  LEU A  58     2834   2712   2466    344    369   -138       C  
ATOM    290  CD1 LEU A  58      26.539   0.917  68.346  1.00 24.14           C  
ANISOU  290  CD1 LEU A  58     3244   3060   2868    245    398   -138       C  
ATOM    291  CD2 LEU A  58      28.733   2.070  67.961  1.00 19.88           C  
ANISOU  291  CD2 LEU A  58     2565   2639   2350    334    335   -171       C  
ATOM    292  N   ASN A  59      31.613  -0.247  71.781  1.00 20.39           N  
ANISOU  292  N   ASN A  59     2768   2760   2220    726    247    -96       N  
ATOM    293  CA  ASN A  59      32.076  -0.246  73.161  1.00 21.73           C  
ANISOU  293  CA  ASN A  59     2948   2985   2324    816    204    -83       C  
ATOM    294  C   ASN A  59      32.352   1.172  73.667  1.00 22.59           C  
ANISOU  294  C   ASN A  59     2936   3199   2450    791    151   -139       C  
ATOM    295  O   ASN A  59      33.311   1.819  73.248  1.00 22.41           O  
ANISOU  295  O   ASN A  59     2803   3241   2469    803    114   -190       O  
ATOM    296  CB  ASN A  59      33.320  -1.124  73.323  1.00 31.02           C  
ANISOU  296  CB  ASN A  59     4147   4176   3464    957    175    -73       C  
ATOM    297  CG  ASN A  59      33.677  -1.354  74.780  1.00 44.45           C  
ANISOU  297  CG  ASN A  59     5887   5925   5076   1066    133    -47       C  
ATOM    298  OD1 ASN A  59      32.798  -1.453  75.637  1.00 47.85           O  
ANISOU  298  OD1 ASN A  59     6393   6331   5457   1046    155     -5       O  
ATOM    299  ND2 ASN A  59      34.971  -1.427  75.069  1.00 49.77           N  
ANISOU  299  ND2 ASN A  59     6505   6677   5727   1186     71    -73       N  
ATOM    300  N   HIS A  60      31.500   1.647  74.570  1.00 21.33           N  
ANISOU  300  N   HIS A  60     2794   3051   2258    752    151   -132       N  
ATOM    301  CA  HIS A  60      31.610   2.996  75.114  1.00 17.67           C  
ANISOU  301  CA  HIS A  60     2228   2675   1812    723    103   -191       C  
ATOM    302  C   HIS A  60      30.946   2.992  76.488  1.00 16.86           C  
ANISOU  302  C   HIS A  60     2184   2592   1628    747     99   -170       C  
ATOM    303  O   HIS A  60      29.979   2.260  76.693  1.00 19.00           O  
ANISOU  303  O   HIS A  60     2560   2795   1863    725    157   -111       O  
ATOM    304  CB  HIS A  60      30.915   3.997  74.181  1.00 17.49           C  
ANISOU  304  CB  HIS A  60     2139   2631   1875    597    127   -221       C  
ATOM    305  CG  HIS A  60      31.095   5.426  74.586  1.00 17.25           C  
ANISOU  305  CG  HIS A  60     2001   2672   1882    562     81   -287       C  
ATOM    306  ND1 HIS A  60      30.262   6.057  75.490  1.00 17.87           N  
ANISOU  306  ND1 HIS A  60     2084   2770   1936    532     74   -302       N  
ATOM    307  CD2 HIS A  60      32.022   6.346  74.228  1.00 19.45           C  
ANISOU  307  CD2 HIS A  60     2164   3004   2224    553     43   -345       C  
ATOM    308  CE1 HIS A  60      30.668   7.300  75.666  1.00 18.32           C  
ANISOU  308  CE1 HIS A  60     2037   2883   2042    508     29   -371       C  
ATOM    309  NE2 HIS A  60      31.737   7.501  74.915  1.00 18.61           N  
ANISOU  309  NE2 HIS A  60     1998   2937   2135    516     11   -396       N  
ATOM    310  N   PRO A  61      31.463   3.796  77.440  1.00 18.78           N  
ANISOU  310  N   PRO A  61     2360   2934   1843    791     35   -223       N  
ATOM    311  CA  PRO A  61      30.910   3.791  78.804  1.00 19.86           C  
ANISOU  311  CA  PRO A  61     2553   3106   1885    829     29   -207       C  
ATOM    312  C   PRO A  61      29.449   4.222  78.870  1.00 17.43           C  
ANISOU  312  C   PRO A  61     2273   2757   1592    722     85   -196       C  
ATOM    313  O   PRO A  61      28.774   3.952  79.873  1.00 17.74           O  
ANISOU  313  O   PRO A  61     2384   2805   1550    743    109   -162       O  
ATOM    314  CB  PRO A  61      31.779   4.816  79.540  1.00 24.57           C  
ANISOU  314  CB  PRO A  61     3041   3821   2474    876    -58   -294       C  
ATOM    315  CG  PRO A  61      33.049   4.860  78.770  1.00 30.07           C  
ANISOU  315  CG  PRO A  61     3649   4542   3232    907    -99   -333       C  
ATOM    316  CD  PRO A  61      32.660   4.651  77.340  1.00 23.98           C  
ANISOU  316  CD  PRO A  61     2886   3677   2547    817    -35   -302       C  
ATOM    317  N   ASN A  62      28.964   4.892  77.832  1.00 15.49           N  
ANISOU  317  N   ASN A  62     1967   2473   1445    614    107   -224       N  
ATOM    318  CA  ASN A  62      27.569   5.337  77.810  1.00 14.90           C  
ANISOU  318  CA  ASN A  62     1905   2365   1391    517    155   -221       C  
ATOM    319  C   ASN A  62      26.713   4.592  76.795  1.00 16.81           C  
ANISOU  319  C   ASN A  62     2206   2509   1672    444    226   -171       C  
ATOM    320  O   ASN A  62      25.694   5.105  76.332  1.00 15.49           O  
ANISOU  320  O   ASN A  62     2015   2316   1554    353    256   -185       O  
ATOM    321  CB  ASN A  62      27.494   6.843  77.559  1.00 16.24           C  
ANISOU  321  CB  ASN A  62     1960   2572   1637    453    119   -299       C  
ATOM    322  CG  ASN A  62      28.151   7.631  78.659  1.00 18.28           C  
ANISOU  322  CG  ASN A  62     2160   2925   1861    512     51   -363       C  
ATOM    323  OD1 ASN A  62      29.139   8.317  78.432  1.00 17.56           O  
ANISOU  323  OD1 ASN A  62     1977   2874   1820    523     -3   -422       O  
ATOM    324  ND2 ASN A  62      27.618   7.515  79.877  1.00 16.79           N  
ANISOU  324  ND2 ASN A  62     2022   2775   1581    549     56   -356       N  
ATOM    325  N   ILE A  63      27.157   3.392  76.443  1.00 15.99           N  
ANISOU  325  N   ILE A  63     2174   2353   1547    491    247   -121       N  
ATOM    326  CA  ILE A  63      26.388   2.484  75.603  1.00 14.61           C  
ANISOU  326  CA  ILE A  63     2070   2080   1400    432    314    -78       C  
ATOM    327  C   ILE A  63      26.379   1.135  76.317  1.00 19.57           C  
ANISOU  327  C   ILE A  63     2824   2658   1952    498    353     -5       C  
ATOM    328  O   ILE A  63      27.438   0.638  76.719  1.00 18.62           O  
ANISOU  328  O   ILE A  63     2732   2558   1784    607    319     13       O  
ATOM    329  CB  ILE A  63      27.015   2.342  74.202  1.00 15.80           C  
ANISOU  329  CB  ILE A  63     2185   2201   1618    420    305    -95       C  
ATOM    330  CG1 ILE A  63      26.955   3.678  73.459  1.00 13.67           C  
ANISOU  330  CG1 ILE A  63     1802   1970   1421    352    278   -152       C  
ATOM    331  CG2 ILE A  63      26.309   1.240  73.393  1.00 20.02           C  
ANISOU  331  CG2 ILE A  63     2802   2634   2171    374    368    -59       C  
ATOM    332  CD1 ILE A  63      27.611   3.655  72.067  1.00 13.61           C  
ANISOU  332  CD1 ILE A  63     1754   1946   1471    342    274   -166       C  
ATOM    333  N   VAL A  64      25.191   0.558  76.501  1.00 18.08           N  
ANISOU  333  N   VAL A  64     2711   2403   1753    435    425     36       N  
ATOM    334  CA  VAL A  64      25.072  -0.720  77.207  1.00 20.08           C  
ANISOU  334  CA  VAL A  64     3097   2593   1940    487    478    116       C  
ATOM    335  C   VAL A  64      25.970  -1.764  76.546  1.00 22.25           C  
ANISOU  335  C   VAL A  64     3428   2800   2225    554    473    142       C  
ATOM    336  O   VAL A  64      25.982  -1.914  75.323  1.00 21.13           O  
ANISOU  336  O   VAL A  64     3261   2612   2156    505    479    113       O  
ATOM    337  CB  VAL A  64      23.609  -1.223  77.275  1.00 23.89           C  
ANISOU  337  CB  VAL A  64     3642   2999   2435    384    569    150       C  
ATOM    338  CG1 VAL A  64      23.040  -1.450  75.870  1.00 30.86           C  
ANISOU  338  CG1 VAL A  64     4503   3809   3415    283    596    119       C  
ATOM    339  CG2 VAL A  64      23.521  -2.497  78.110  1.00 22.87           C  
ANISOU  339  CG2 VAL A  64     3656   2797   2234    437    633    242       C  
ATOM    340  N   LYS A  65      26.758  -2.459  77.355  1.00 20.24           N  
ANISOU  340  N   LYS A  65     3249   2548   1892    676    459    193       N  
ATOM    341  CA  LYS A  65      27.758  -3.363  76.799  1.00 21.40           C  
ANISOU  341  CA  LYS A  65     3440   2645   2047    763    444    209       C  
ATOM    342  C   LYS A  65      27.207  -4.762  76.545  1.00 24.67           C  
ANISOU  342  C   LYS A  65     3991   2912   2470    745    526    275       C  
ATOM    343  O   LYS A  65      26.653  -5.394  77.446  1.00 24.68           O  
ANISOU  343  O   LYS A  65     4100   2862   2414    756    582    348       O  
ATOM    344  CB  LYS A  65      28.978  -3.436  77.723  1.00 28.36           C  
ANISOU  344  CB  LYS A  65     4327   3604   2843    920    377    225       C  
ATOM    345  CG  LYS A  65      30.176  -4.152  77.104  1.00 33.48           C  
ANISOU  345  CG  LYS A  65     4986   4229   3505   1023    345    223       C  
ATOM    346  CD  LYS A  65      31.409  -4.021  77.979  1.00 41.86           C  
ANISOU  346  CD  LYS A  65     6020   5395   4489   1178    263    219       C  
ATOM    347  CE  LYS A  65      32.629  -4.622  77.300  1.00 49.44           C  
ANISOU  347  CE  LYS A  65     6966   6347   5472   1281    228    203       C  
ATOM    348  NZ  LYS A  65      33.875  -4.360  78.074  1.00 55.51           N  
ANISOU  348  NZ  LYS A  65     7676   7239   6175   1428    136    179       N  
ATOM    349  N   LEU A  66      27.363  -5.235  75.310  1.00 21.00           N  
ANISOU  349  N   LEU A  66     3524   2377   2077    715    536    247       N  
ATOM    350  CA  LEU A  66      27.061  -6.617  74.960  1.00 20.99           C  
ANISOU  350  CA  LEU A  66     3652   2228   2095    711    604    294       C  
ATOM    351  C   LEU A  66      28.269  -7.471  75.321  1.00 26.00           C  
ANISOU  351  C   LEU A  66     4362   2840   2677    874    577    339       C  
ATOM    352  O   LEU A  66      29.353  -7.285  74.771  1.00 25.01           O  
ANISOU  352  O   LEU A  66     4170   2769   2564    950    515    294       O  
ATOM    353  CB  LEU A  66      26.767  -6.741  73.462  1.00 22.99           C  
ANISOU  353  CB  LEU A  66     3867   2427   2442    622    618    231       C  
ATOM    354  CG  LEU A  66      26.506  -8.155  72.937  1.00 27.25           C  
ANISOU  354  CG  LEU A  66     4529   2809   3017    612    682    256       C  
ATOM    355  CD1 LEU A  66      25.307  -8.800  73.634  1.00 24.94           C  
ANISOU  355  CD1 LEU A  66     4341   2416   2721    533    770    317       C  
ATOM    356  CD2 LEU A  66      26.301  -8.127  71.424  1.00 26.91           C  
ANISOU  356  CD2 LEU A  66     4429   2740   3053    533    680    176       C  
ATOM    357  N   LEU A  67      28.085  -8.396  76.257  1.00 27.19           N  
ANISOU  357  N   LEU A  67     4651   2913   2767    932    624    429       N  
ATOM    358  CA  LEU A  67      29.202  -9.165  76.792  1.00 32.42           C  
ANISOU  358  CA  LEU A  67     5394   3562   3362   1107    593    482       C  
ATOM    359  C   LEU A  67      29.457 -10.458  76.028  1.00 35.96           C  
ANISOU  359  C   LEU A  67     5945   3859   3858   1143    632    501       C  
ATOM    360  O   LEU A  67      30.605 -10.878  75.875  1.00 38.37           O  
ANISOU  360  O   LEU A  67     6259   4174   4145   1282    584    498       O  
ATOM    361  CB  LEU A  67      28.978  -9.462  78.276  1.00 31.01           C  
ANISOU  361  CB  LEU A  67     5321   3385   3076   1177    619    580       C  
ATOM    362  CG  LEU A  67      28.762  -8.205  79.120  1.00 33.63           C  
ANISOU  362  CG  LEU A  67     5556   3871   3350   1155    578    555       C  
ATOM    363  CD1 LEU A  67      28.553  -8.564  80.579  1.00 36.92           C  
ANISOU  363  CD1 LEU A  67     6087   4295   3646   1234    608    653       C  
ATOM    364  CD2 LEU A  67      29.940  -7.252  78.962  1.00 33.98           C  
ANISOU  364  CD2 LEU A  67     5455   4066   3389   1233    463    471       C  
ATOM    365  N   ASP A  68      28.389 -11.088  75.552  1.00 34.42           N  
ANISOU  365  N   ASP A  68     5823   3528   3727   1020    719    513       N  
ATOM    366  CA  ASP A  68      28.518 -12.363  74.861  1.00 34.20           C  
ANISOU  366  CA  ASP A  68     5904   3339   3750   1044    763    524       C  
ATOM    367  C   ASP A  68      27.251 -12.695  74.078  1.00 28.27           C  
ANISOU  367  C   ASP A  68     5175   2473   3092    867    842    491       C  
ATOM    368  O   ASP A  68      26.169 -12.178  74.371  1.00 26.72           O  
ANISOU  368  O   ASP A  68     4947   2300   2907    739    881    492       O  
ATOM    369  CB  ASP A  68      28.814 -13.480  75.870  1.00 35.82           C  
ANISOU  369  CB  ASP A  68     6243   3477   3891   1144    792    616       C  
ATOM    370  CG  ASP A  68      29.565 -14.652  75.252  1.00 41.13           C  
ANISOU  370  CG  ASP A  68     6963   4068   4595   1213    785    598       C  
ATOM    371  OD1 ASP A  68      29.803 -14.635  74.025  1.00 41.80           O  
ANISOU  371  OD1 ASP A  68     6995   4137   4751   1186    766    520       O  
ATOM    372  OD2 ASP A  68      29.909 -15.595  76.001  1.00 40.24           O  
ANISOU  372  OD2 ASP A  68     6943   3912   4436   1295    799    660       O  
ATOM    373  N   VAL A  69      27.395 -13.566  73.083  1.00 28.82           N  
ANISOU  373  N   VAL A  69     5290   2430   3229    862    862    452       N  
ATOM    374  CA  VAL A  69      26.260 -14.061  72.308  1.00 29.51           C  
ANISOU  374  CA  VAL A  69     5393   2413   3407    698    927    406       C  
ATOM    375  C   VAL A  69      26.319 -15.581  72.241  1.00 33.41           C  
ANISOU  375  C   VAL A  69     5986   2783   3926    711    966    425       C  
ATOM    376  O   VAL A  69      27.355 -16.149  71.908  1.00 36.17           O  
ANISOU  376  O   VAL A  69     6354   3123   4265    826    925    415       O  
ATOM    377  CB  VAL A  69      26.268 -13.503  70.866  1.00 30.97           C  
ANISOU  377  CB  VAL A  69     5470   2639   3657    637    890    290       C  
ATOM    378  CG1 VAL A  69      25.065 -14.020  70.087  1.00 30.26           C  
ANISOU  378  CG1 VAL A  69     5395   2448   3655    475    949    234       C  
ATOM    379  CG2 VAL A  69      26.287 -11.985  70.883  1.00 27.34           C  
ANISOU  379  CG2 VAL A  69     4850   2367   3171    604    826    251       C  
ATOM    380  N   ILE A  70      25.208 -16.238  72.557  1.00 32.75           N  
ANISOU  380  N   ILE A  70     5958   2605   3879    594   1044    450       N  
ATOM    381  CA  ILE A  70      25.164 -17.696  72.530  1.00 38.06           C  
ANISOU  381  CA  ILE A  70     6729   3146   4587    597   1088    471       C  
ATOM    382  C   ILE A  70      24.047 -18.206  71.626  1.00 39.47           C  
ANISOU  382  C   ILE A  70     6892   3235   4871    432   1136    397       C  
ATOM    383  O   ILE A  70      22.867 -17.950  71.875  1.00 37.87           O  
ANISOU  383  O   ILE A  70     6662   3029   4698    297   1187    394       O  
ATOM    384  CB  ILE A  70      24.997 -18.298  73.945  1.00 42.57           C  
ANISOU  384  CB  ILE A  70     7400   3676   5100    638   1141    583       C  
ATOM    385  CG1 ILE A  70      26.207 -17.963  74.826  1.00 43.95           C  
ANISOU  385  CG1 ILE A  70     7591   3943   5163    821   1081    647       C  
ATOM    386  CG2 ILE A  70      24.815 -19.807  73.863  1.00 45.26           C  
ANISOU  386  CG2 ILE A  70     7844   3862   5492    622   1195    603       C  
ATOM    387  CD1 ILE A  70      26.093 -16.647  75.581  1.00 46.88           C  
ANISOU  387  CD1 ILE A  70     7895   4452   5464    830   1054    671       C  
ATOM    388  N   HIS A  71      24.426 -18.922  70.569  1.00 45.77           N  
ANISOU  388  N   HIS A  71     7697   3969   5723    444   1114    331       N  
ATOM    389  CA AHIS A  71      23.446 -19.476  69.634  0.50 52.20           C  
ANISOU  389  CA AHIS A  71     8492   4705   6636    299   1146    248       C  
ATOM    390  CA BHIS A  71      23.463 -19.470  69.627  0.50 52.19           C  
ANISOU  390  CA BHIS A  71     8491   4705   6635    301   1145    248       C  
ATOM    391  C   HIS A  71      23.141 -20.923  69.974  1.00 55.50           C  
ANISOU  391  C   HIS A  71     9020   4973   7097    282   1208    289       C  
ATOM    392  O   HIS A  71      24.045 -21.721  70.231  1.00 61.05           O  
ANISOU  392  O   HIS A  71     9807   5616   7774    405   1199    336       O  
ATOM    393  CB AHIS A  71      23.906 -19.444  68.167  0.50 53.79           C  
ANISOU  393  CB AHIS A  71     8632   4926   6880    310   1087    136       C  
ATOM    394  CB BHIS A  71      24.039 -19.392  68.213  0.50 53.77           C  
ANISOU  394  CB BHIS A  71     8630   4932   6868    326   1082    142       C  
ATOM    395  CG AHIS A  71      25.014 -18.479  67.867  0.50 52.20           C  
ANISOU  395  CG AHIS A  71     8366   4849   6620    425   1013    120       C  
ATOM    396  CG BHIS A  71      23.028 -19.069  67.156  0.50 52.30           C  
ANISOU  396  CG BHIS A  71     8356   4764   6753    177   1079     34       C  
ATOM    397  ND1AHIS A  71      24.892 -17.486  66.921  0.50 49.91           N  
ANISOU  397  ND1AHIS A  71     7966   4656   6343    377    970     33       N  
ATOM    398  ND1BHIS A  71      21.670 -19.092  67.390  0.50 52.50           N  
ANISOU  398  ND1BHIS A  71     8361   4762   6825     27   1133     25       N  
ATOM    399  CD2AHIS A  71      26.279 -18.392  68.344  0.50 52.94           C  
ANISOU  399  CD2AHIS A  71     8481   4990   6644    588    972    173       C  
ATOM    400  CD2BHIS A  71      23.179 -18.716  65.857  0.50 49.60           C  
ANISOU  400  CD2BHIS A  71     7935   4476   6437    162   1026    -73       C  
ATOM    401  CE1AHIS A  71      26.025 -16.807  66.849  0.50 49.53           C  
ANISOU  401  CE1AHIS A  71     7874   4707   6239    501    913     36       C  
ATOM    402  CE1BHIS A  71      21.029 -18.767  66.282  0.50 50.42           C  
ANISOU  402  CE1BHIS A  71     8008   4538   6614    -72   1106    -85       C  
ATOM    403  NE2AHIS A  71      26.881 -17.336  67.703  0.50 52.40           N  
ANISOU  403  NE2AHIS A  71     8310   5046   6554    629    909    117       N  
ATOM    404  NE2BHIS A  71      21.921 -18.535  65.336  0.50 47.22           N  
ANISOU  404  NE2BHIS A  71     7569   4180   6192      8   1042   -144       N  
ATOM    405  N   THR A  72      21.858 -21.256  69.993  1.00 52.52           N  
ANISOU  405  N   THR A  72     8635   4535   6786    130   1270    269       N  
ATOM    406  CA  THR A  72      21.434 -22.644  70.089  1.00 54.50           C  
ANISOU  406  CA  THR A  72     8976   4631   7100     87   1330    286       C  
ATOM    407  C   THR A  72      20.468 -22.845  68.935  1.00 56.05           C  
ANISOU  407  C   THR A  72     9100   4797   7399    -62   1331    165       C  
ATOM    408  O   THR A  72      20.112 -21.879  68.260  1.00 53.72           O  
ANISOU  408  O   THR A  72     8693   4608   7109   -123   1291     87       O  
ATOM    409  CB  THR A  72      20.755 -22.981  71.434  1.00 47.22           C  
ANISOU  409  CB  THR A  72     8122   3662   6159     48   1415    392       C  
ATOM    410  OG1 THR A  72      19.486 -22.322  71.514  1.00 46.58           O  
ANISOU  410  OG1 THR A  72     7952   3637   6108   -103   1449    359       O  
ATOM    411  CG2 THR A  72      21.631 -22.553  72.604  1.00 46.17           C  
ANISOU  411  CG2 THR A  72     8039   3594   5908    195   1402    503       C  
ATOM    412  N   GLU A  73      20.050 -24.086  68.709  1.00 58.16           N  
ANISOU  412  N   GLU A  73     9430   4921   7745   -116   1374    147       N  
ATOM    413  CA  GLU A  73      19.249 -24.436  67.538  1.00 62.42           C  
ANISOU  413  CA  GLU A  73     9908   5424   8383   -240   1363     21       C  
ATOM    414  C   GLU A  73      18.005 -23.567  67.333  1.00 62.04           C  
ANISOU  414  C   GLU A  73     9737   5473   8362   -388   1369    -40       C  
ATOM    415  O   GLU A  73      17.674 -23.206  66.203  1.00 64.75           O  
ANISOU  415  O   GLU A  73     9986   5874   8741   -447   1317   -156       O  
ATOM    416  CB  GLU A  73      18.859 -25.914  67.585  1.00 70.30           C  
ANISOU  416  CB  GLU A  73    11001   6245   9467   -286   1421     27       C  
ATOM    417  CG  GLU A  73      20.049 -26.857  67.563  1.00 76.25           C  
ANISOU  417  CG  GLU A  73    11867   6894  10209   -142   1405     64       C  
ATOM    418  CD  GLU A  73      19.639 -28.315  67.561  1.00 82.46           C  
ANISOU  418  CD  GLU A  73    12749   7492  11088   -193   1462     64       C  
ATOM    419  OE1 GLU A  73      18.635 -28.655  68.226  1.00 83.39           O  
ANISOU  419  OE1 GLU A  73    12889   7549  11247   -303   1541    107       O  
ATOM    420  OE2 GLU A  73      20.317 -29.122  66.890  1.00 84.83           O  
ANISOU  420  OE2 GLU A  73    13102   7705  11426   -123   1430     19       O  
ATOM    421  N   ASN A  74      17.325 -23.225  68.421  1.00 58.34           N  
ANISOU  421  N   ASN A  74     9266   5030   7869   -441   1430     37       N  
ATOM    422  CA  ASN A  74      16.108 -22.424  68.324  1.00 57.73           C  
ANISOU  422  CA  ASN A  74     9069   5049   7818   -576   1439    -18       C  
ATOM    423  C   ASN A  74      16.080 -21.225  69.270  1.00 52.96           C  
ANISOU  423  C   ASN A  74     8424   4567   7130   -552   1445     52       C  
ATOM    424  O   ASN A  74      15.050 -20.564  69.418  1.00 51.83           O  
ANISOU  424  O   ASN A  74     8188   4503   7002   -655   1461     23       O  
ATOM    425  CB  ASN A  74      14.874 -23.306  68.532  1.00 62.87           C  
ANISOU  425  CB  ASN A  74     9728   5603   8558   -713   1515    -31       C  
ATOM    426  CG  ASN A  74      15.067 -24.322  69.636  1.00 68.05           C  
ANISOU  426  CG  ASN A  74    10523   6126   9208   -674   1596     89       C  
ATOM    427  OD1 ASN A  74      15.839 -24.101  70.569  1.00 67.87           O  
ANISOU  427  OD1 ASN A  74    10570   6121   9098   -561   1606    197       O  
ATOM    428  ND2 ASN A  74      14.373 -25.452  69.530  1.00 72.62           N  
ANISOU  428  ND2 ASN A  74    11141   6570   9879   -765   1653     69       N  
ATOM    429  N   LYS A  75      17.213 -20.940  69.904  1.00 52.46           N  
ANISOU  429  N   LYS A  75     8427   4527   6979   -411   1426    138       N  
ATOM    430  CA  LYS A  75      17.306 -19.802  70.815  1.00 51.24           C  
ANISOU  430  CA  LYS A  75     8240   4489   6741   -373   1423    202       C  
ATOM    431  C   LYS A  75      18.620 -19.040  70.670  1.00 45.29           C  
ANISOU  431  C   LYS A  75     7485   3813   5909   -231   1349    218       C  
ATOM    432  O   LYS A  75      19.673 -19.629  70.429  1.00 44.79           O  
ANISOU  432  O   LYS A  75     7493   3695   5829   -118   1321    234       O  
ATOM    433  CB  LYS A  75      17.112 -20.247  72.269  1.00 55.05           C  
ANISOU  433  CB  LYS A  75     8811   4923   7181   -352   1500    324       C  
ATOM    434  CG  LYS A  75      15.677 -20.613  72.621  1.00 61.13           C  
ANISOU  434  CG  LYS A  75     9553   5658   8016   -502   1579    316       C  
ATOM    435  CD  LYS A  75      15.543 -21.019  74.078  1.00 67.97           C  
ANISOU  435  CD  LYS A  75    10510   6483   8831   -472   1656    442       C  
ATOM    436  CE  LYS A  75      14.105 -21.386  74.417  1.00 74.38           C  
ANISOU  436  CE  LYS A  75    11290   7261   9712   -623   1738    433       C  
ATOM    437  NZ  LYS A  75      13.956 -21.800  75.841  1.00 78.70           N  
ANISOU  437  NZ  LYS A  75    11929   7768  10207   -594   1819    560       N  
ATOM    438  N   LEU A  76      18.539 -17.722  70.822  1.00 41.65           N  
ANISOU  438  N   LEU A  76     6940   3481   5404   -237   1317    209       N  
ATOM    439  CA  LEU A  76      19.708 -16.856  70.774  1.00 39.69           C  
ANISOU  439  CA  LEU A  76     6679   3316   5084   -111   1250    225       C  
ATOM    440  C   LEU A  76      19.831 -16.104  72.100  1.00 37.67           C  
ANISOU  440  C   LEU A  76     6436   3136   4743    -57   1263    319       C  
ATOM    441  O   LEU A  76      18.925 -15.367  72.487  1.00 37.30           O  
ANISOU  441  O   LEU A  76     6320   3157   4697   -147   1285    313       O  
ATOM    442  CB  LEU A  76      19.573 -15.874  69.605  1.00 42.84           C  
ANISOU  442  CB  LEU A  76     6960   3804   5513   -163   1190    119       C  
ATOM    443  CG  LEU A  76      20.787 -15.062  69.157  1.00 40.59           C  
ANISOU  443  CG  LEU A  76     6648   3594   5179    -44   1115    104       C  
ATOM    444  CD1 LEU A  76      21.966 -15.968  68.864  1.00 40.82           C  
ANISOU  444  CD1 LEU A  76     6756   3559   5195     85   1090    118       C  
ATOM    445  CD2 LEU A  76      20.429 -14.228  67.930  1.00 37.90           C  
ANISOU  445  CD2 LEU A  76     6192   3331   4878   -118   1067     -8       C  
ATOM    446  N   TYR A  77      20.945 -16.299  72.800  1.00 38.23           N  
ANISOU  446  N   TYR A  77     6586   3204   4736     96   1244    401       N  
ATOM    447  CA  TYR A  77      21.157 -15.658  74.097  1.00 41.69           C  
ANISOU  447  CA  TYR A  77     7039   3722   5080    166   1246    489       C  
ATOM    448  C   TYR A  77      22.113 -14.477  74.011  1.00 38.96           C  
ANISOU  448  C   TYR A  77     6637   3493   4672    269   1166    483       C  
ATOM    449  O   TYR A  77      23.197 -14.589  73.443  1.00 38.01           O  
ANISOU  449  O   TYR A  77     6528   3373   4543    376   1108    464       O  
ATOM    450  CB  TYR A  77      21.703 -16.665  75.113  1.00 44.20           C  
ANISOU  450  CB  TYR A  77     7480   3973   5340    277   1275    589       C  
ATOM    451  CG  TYR A  77      20.687 -17.661  75.621  1.00 47.78           C  
ANISOU  451  CG  TYR A  77     7994   4324   5836    182   1367    626       C  
ATOM    452  CD1 TYR A  77      19.891 -17.368  76.722  1.00 49.77           C  
ANISOU  452  CD1 TYR A  77     8243   4617   6051    133   1420    681       C  
ATOM    453  CD2 TYR A  77      20.531 -18.899  75.011  1.00 50.89           C  
ANISOU  453  CD2 TYR A  77     8446   4582   6307    142   1401    603       C  
ATOM    454  CE1 TYR A  77      18.962 -18.277  77.197  1.00 53.44           C  
ANISOU  454  CE1 TYR A  77     8761   4988   6558     46   1508    717       C  
ATOM    455  CE2 TYR A  77      19.602 -19.816  75.480  1.00 54.99           C  
ANISOU  455  CE2 TYR A  77     9021   5001   6871     53   1489    638       C  
ATOM    456  CZ  TYR A  77      18.822 -19.498  76.573  1.00 56.95           C  
ANISOU  456  CZ  TYR A  77     9264   5291   7083      4   1544    697       C  
ATOM    457  OH  TYR A  77      17.897 -20.403  77.046  1.00 62.77           O  
ANISOU  457  OH  TYR A  77    10053   5930   7867    -86   1635    735       O  
ATOM    458  N   LEU A  78      21.709 -13.349  74.588  1.00 35.71           N  
ANISOU  458  N   LEU A  78     6160   3189   4219    236   1160    496       N  
ATOM    459  CA  LEU A  78      22.584 -12.189  74.699  1.00 31.08           C  
ANISOU  459  CA  LEU A  78     5519   2724   3566    335   1086    501       C  
ATOM    460  C   LEU A  78      22.865 -11.881  76.165  1.00 34.86           C  
ANISOU  460  C   LEU A  78     6027   3283   3933    427   1081    589       C  
ATOM    461  O   LEU A  78      21.939 -11.742  76.964  1.00 34.66           O  
ANISOU  461  O   LEU A  78     5992   3283   3892    352   1131    613       O  
ATOM    462  CB  LEU A  78      21.952 -10.971  74.033  1.00 33.76           C  
ANISOU  462  CB  LEU A  78     5693   3185   3948    222   1044    402       C  
ATOM    463  CG  LEU A  78      21.584 -11.099  72.555  1.00 33.76           C  
ANISOU  463  CG  LEU A  78     5637   3144   4047    127   1034    300       C  
ATOM    464  CD1 LEU A  78      21.201  -9.744  71.997  1.00 26.91           C  
ANISOU  464  CD1 LEU A  78     4607   2420   3197     59    975    218       C  
ATOM    465  CD2 LEU A  78      22.741 -11.698  71.785  1.00 37.76           C  
ANISOU  465  CD2 LEU A  78     6181   3604   4562    235    990    278       C  
ATOM    466  N   VAL A  79      24.142 -11.786  76.520  1.00 32.97           N  
ANISOU  466  N   VAL A  79     5808   3101   3619    594   1011    620       N  
ATOM    467  CA  VAL A  79      24.520 -11.372  77.867  1.00 34.24           C  
ANISOU  467  CA  VAL A  79     5978   3367   3665    695    985    684       C  
ATOM    468  C   VAL A  79      24.954  -9.907  77.848  1.00 33.00           C  
ANISOU  468  C   VAL A  79     5665   3395   3479    715    888    613       C  
ATOM    469  O   VAL A  79      25.876  -9.535  77.121  1.00 32.46           O  
ANISOU  469  O   VAL A  79     5515   3386   3434    772    806    547       O  
ATOM    470  CB  VAL A  79      25.660 -12.235  78.431  1.00 36.84           C  
ANISOU  470  CB  VAL A  79     6390   3677   3932    867    949    736       C  
ATOM    471  CG1 VAL A  79      25.920 -11.879  79.894  1.00 38.43           C  
ANISOU  471  CG1 VAL A  79     6598   3988   4017    962    923    791       C  
ATOM    472  CG2 VAL A  79      25.325 -13.707  78.291  1.00 38.03           C  
ANISOU  472  CG2 VAL A  79     6647   3667   4137    834   1022    764       C  
ATOM    473  N   PHE A  80      24.272  -9.082  78.640  1.00 28.91           N  
ANISOU  473  N   PHE A  80     5100   2969   2918    662    901    618       N  
ATOM    474  CA  PHE A  80      24.572  -7.656  78.740  1.00 27.62           C  
ANISOU  474  CA  PHE A  80     4786   2975   2734    670    813    544       C  
ATOM    475  C   PHE A  80      25.087  -7.290  80.123  1.00 30.74           C  
ANISOU  475  C   PHE A  80     5201   3476   3002    791    777    591       C  
ATOM    476  O   PHE A  80      24.868  -8.022  81.094  1.00 30.77           O  
ANISOU  476  O   PHE A  80     5333   3432   2928    841    837    689       O  
ATOM    477  CB  PHE A  80      23.309  -6.830  78.496  1.00 28.64           C  
ANISOU  477  CB  PHE A  80     4824   3139   2919    510    847    490       C  
ATOM    478  CG  PHE A  80      22.831  -6.840  77.074  1.00 29.43           C  
ANISOU  478  CG  PHE A  80     4864   3182   3136    394    855    417       C  
ATOM    479  CD1 PHE A  80      23.341  -5.939  76.153  1.00 29.85           C  
ANISOU  479  CD1 PHE A  80     4791   3316   3236    390    774    330       C  
ATOM    480  CD2 PHE A  80      21.850  -7.730  76.665  1.00 30.33           C  
ANISOU  480  CD2 PHE A  80     5046   3166   3313    287    946    433       C  
ATOM    481  CE1 PHE A  80      22.891  -5.934  74.844  1.00 29.35           C  
ANISOU  481  CE1 PHE A  80     4676   3209   3265    292    779    265       C  
ATOM    482  CE2 PHE A  80      21.400  -7.733  75.360  1.00 32.78           C  
ANISOU  482  CE2 PHE A  80     5297   3435   3722    186    945    356       C  
ATOM    483  CZ  PHE A  80      21.921  -6.832  74.450  1.00 31.58           C  
ANISOU  483  CZ  PHE A  80     5025   3371   3602    195    859    275       C  
ATOM    484  N   GLU A  81      25.747  -6.141  80.225  1.00 26.79           N  
ANISOU  484  N   GLU A  81     4575   3122   2481    836    679    520       N  
ATOM    485  CA  GLU A  81      26.001  -5.573  81.539  1.00 31.86           C  
ANISOU  485  CA  GLU A  81     5213   3885   3008    923    642    539       C  
ATOM    486  C   GLU A  81      24.634  -5.213  82.107  1.00 30.56           C  
ANISOU  486  C   GLU A  81     5054   3727   2830    810    721    554       C  
ATOM    487  O   GLU A  81      23.711  -4.893  81.357  1.00 26.75           O  
ANISOU  487  O   GLU A  81     4512   3210   2442    667    761    508       O  
ATOM    488  CB  GLU A  81      26.906  -4.340  81.464  1.00 36.76           C  
ANISOU  488  CB  GLU A  81     5683   4654   3631    971    525    441       C  
ATOM    489  CG  GLU A  81      26.245  -3.103  80.889  1.00 38.83           C  
ANISOU  489  CG  GLU A  81     5808   4971   3976    838    512    349       C  
ATOM    490  CD  GLU A  81      27.135  -1.872  80.940  1.00 36.72           C  
ANISOU  490  CD  GLU A  81     5401   4839   3711    882    404    257       C  
ATOM    491  OE1 GLU A  81      27.477  -1.345  79.864  1.00 33.47           O  
ANISOU  491  OE1 GLU A  81     4891   4433   3393    833    368    190       O  
ATOM    492  OE2 GLU A  81      27.478  -1.414  82.053  1.00 34.39           O  
ANISOU  492  OE2 GLU A  81     5095   4646   3324    963    358    249       O  
ATOM    493  N   PHE A  82      24.499  -5.293  83.425  1.00 29.14           N  
ANISOU  493  N   PHE A  82     4923   3593   2554    868    733    605       N  
ATOM    494  CA  PHE A  82      23.224  -5.028  84.078  1.00 32.38           C  
ANISOU  494  CA  PHE A  82     5322   4014   2969    762    800    612       C  
ATOM    495  C   PHE A  82      23.136  -3.577  84.532  1.00 31.80           C  
ANISOU  495  C   PHE A  82     5126   4094   2862    754    739    530       C  
ATOM    496  O   PHE A  82      24.054  -3.066  85.173  1.00 32.53           O  
ANISOU  496  O   PHE A  82     5184   4294   2881    869    650    503       O  
ATOM    497  CB  PHE A  82      23.046  -5.964  85.282  1.00 36.89           C  
ANISOU  497  CB  PHE A  82     6002   4544   3472    816    848    704       C  
ATOM    498  CG  PHE A  82      21.823  -5.670  86.109  1.00 39.87           C  
ANISOU  498  CG  PHE A  82     6363   4954   3834    725    913    714       C  
ATOM    499  CD1 PHE A  82      20.587  -6.185  85.751  1.00 40.66           C  
ANISOU  499  CD1 PHE A  82     6482   4953   4013    582   1016    734       C  
ATOM    500  CD2 PHE A  82      21.910  -4.880  87.246  1.00 43.24           C  
ANISOU  500  CD2 PHE A  82     6747   5514   4168    782    869    694       C  
ATOM    501  CE1 PHE A  82      19.461  -5.914  86.507  1.00 44.89           C  
ANISOU  501  CE1 PHE A  82     6993   5530   4535    501   1076    740       C  
ATOM    502  CE2 PHE A  82      20.786  -4.602  88.006  1.00 45.11           C  
ANISOU  502  CE2 PHE A  82     6967   5786   4385    703    931    701       C  
ATOM    503  CZ  PHE A  82      19.561  -5.122  87.637  1.00 46.41           C  
ANISOU  503  CZ  PHE A  82     7150   5857   4628    563   1036    726       C  
ATOM    504  N   LEU A  83      22.033  -2.917  84.188  1.00 29.72           N  
ANISOU  504  N   LEU A  83     4791   3841   2660    620    782    482       N  
ATOM    505  CA  LEU A  83      21.725  -1.594  84.734  1.00 31.44           C  
ANISOU  505  CA  LEU A  83     4902   4190   2854    602    740    406       C  
ATOM    506  C   LEU A  83      20.373  -1.625  85.438  1.00 32.41           C  
ANISOU  506  C   LEU A  83     5031   4308   2974    509    823    428       C  
ATOM    507  O   LEU A  83      19.475  -2.358  85.025  1.00 30.16           O  
ANISOU  507  O   LEU A  83     4784   3922   2752    410    910    467       O  
ATOM    508  CB  LEU A  83      21.766  -0.515  83.655  1.00 31.37           C  
ANISOU  508  CB  LEU A  83     4773   4221   2925    544    695    305       C  
ATOM    509  CG  LEU A  83      23.182  -0.058  83.302  1.00 32.81           C  
ANISOU  509  CG  LEU A  83     4890   4458   3119    636    576    250       C  
ATOM    510  CD1 LEU A  83      23.685  -0.749  82.041  1.00 34.52           C  
ANISOU  510  CD1 LEU A  83     5117   4576   3424    619    570    259       C  
ATOM    511  CD2 LEU A  83      23.251   1.456  83.165  1.00 31.48           C  
ANISOU  511  CD2 LEU A  83     4575   4388   2996    604    501    137       C  
ATOM    512  N   HIS A  84      20.244  -0.818  86.490  1.00 29.65           N  
ANISOU  512  N   HIS A  84     4638   4073   2556    541    792    395       N  
ATOM    513  CA  HIS A  84      19.149  -0.928  87.453  1.00 35.65           C  
ANISOU  513  CA  HIS A  84     5416   4850   3278    488    866    427       C  
ATOM    514  C   HIS A  84      17.754  -0.683  86.872  1.00 37.69           C  
ANISOU  514  C   HIS A  84     5612   5079   3629    336    940    395       C  
ATOM    515  O   HIS A  84      16.834  -1.465  87.112  1.00 40.17           O  
ANISOU  515  O   HIS A  84     5973   5331   3959    267   1031    453       O  
ATOM    516  CB  HIS A  84      19.409  -0.012  88.658  1.00 37.72           C  
ANISOU  516  CB  HIS A  84     5639   5249   3445    564    806    382       C  
ATOM    517  CG  HIS A  84      20.711  -0.284  89.350  1.00 46.47           C  
ANISOU  517  CG  HIS A  84     6800   6397   4461    718    729    409       C  
ATOM    518  ND1 HIS A  84      20.786  -0.783  90.634  1.00 53.71           N  
ANISOU  518  ND1 HIS A  84     7794   7343   5272    796    745    473       N  
ATOM    519  CD2 HIS A  84      21.992  -0.140  88.930  1.00 44.18           C  
ANISOU  519  CD2 HIS A  84     6489   6128   4171    812    634    378       C  
ATOM    520  CE1 HIS A  84      22.054  -0.928  90.976  1.00 52.68           C  
ANISOU  520  CE1 HIS A  84     7686   7249   5080    935    659    478       C  
ATOM    521  NE2 HIS A  84      22.806  -0.541  89.960  1.00 49.93           N  
ANISOU  521  NE2 HIS A  84     7275   6900   4797    946    589    418       N  
ATOM    522  N   GLN A  85      17.598   0.397  86.112  1.00 29.01           N  
ANISOU  522  N   GLN A  85     4402   4025   2594    288    899    299       N  
ATOM    523  CA  GLN A  85      16.308   0.708  85.501  1.00 29.16           C  
ANISOU  523  CA  GLN A  85     4346   4027   2706    156    954    258       C  
ATOM    524  C   GLN A  85      16.438   1.743  84.398  1.00 26.91           C  
ANISOU  524  C   GLN A  85     3957   3765   2503    124    898    163       C  
ATOM    525  O   GLN A  85      17.544   2.159  84.051  1.00 23.17           O  
ANISOU  525  O   GLN A  85     3471   3313   2018    198    822    132       O  
ATOM    526  CB  GLN A  85      15.304   1.187  86.545  1.00 38.97           C  
ANISOU  526  CB  GLN A  85     5550   5353   3905    125    995    243       C  
ATOM    527  CG  GLN A  85      15.584   2.565  87.103  1.00 36.24           C  
ANISOU  527  CG  GLN A  85     5127   5132   3512    177    924    153       C  
ATOM    528  CD  GLN A  85      14.409   3.095  87.897  1.00 49.91           C  
ANISOU  528  CD  GLN A  85     6805   6939   5220    127    973    120       C  
ATOM    529  OE1 GLN A  85      13.439   2.376  88.142  1.00 58.53           O  
ANISOU  529  OE1 GLN A  85     7918   8002   6319     64   1059    177       O  
ATOM    530  NE2 GLN A  85      14.484   4.358  88.301  1.00 51.77           N  
ANISOU  530  NE2 GLN A  85     6972   7261   5435    154    921     25       N  
ATOM    531  N   ASP A  86      15.305   2.152  83.838  1.00 24.13           N  
ANISOU  531  N   ASP A  86     3523   3409   2236     20    930    116       N  
ATOM    532  CA  ASP A  86      15.328   3.076  82.711  1.00 20.26           C  
ANISOU  532  CA  ASP A  86     2937   2927   1834    -17    880     31       C  
ATOM    533  C   ASP A  86      14.861   4.472  83.108  1.00 20.85           C  
ANISOU  533  C   ASP A  86     2909   3103   1909    -14    846    -54       C  
ATOM    534  O   ASP A  86      14.281   4.668  84.180  1.00 23.55           O  
ANISOU  534  O   ASP A  86     3245   3510   2191      0    874    -49       O  
ATOM    535  CB  ASP A  86      14.522   2.536  81.519  1.00 24.82           C  
ANISOU  535  CB  ASP A  86     3491   3414   2526   -127    914     28       C  
ATOM    536  CG  ASP A  86      13.053   2.337  81.840  1.00 32.16           C  
ANISOU  536  CG  ASP A  86     4386   4343   3490   -208    976     32       C  
ATOM    537  OD1 ASP A  86      12.329   3.344  81.978  1.00 28.39           O  
ANISOU  537  OD1 ASP A  86     3814   3935   3037   -225    957    -28       O  
ATOM    538  OD2 ASP A  86      12.618   1.170  81.935  1.00 39.44           O  
ANISOU  538  OD2 ASP A  86     5375   5190   4422   -253   1043     93       O  
ATOM    539  N   LEU A  87      15.129   5.438  82.236  1.00 19.93           N  
ANISOU  539  N   LEU A  87     2711   2998   1865    -27    783   -132       N  
ATOM    540  CA  LEU A  87      14.863   6.841  82.530  1.00 17.91           C  
ANISOU  540  CA  LEU A  87     2358   2818   1628    -11    727   -216       C  
ATOM    541  C   LEU A  87      13.369   7.149  82.627  1.00 19.49           C  
ANISOU  541  C   LEU A  87     2503   3019   1881    -72    764   -230       C  
ATOM    542  O   LEU A  87      12.961   8.044  83.360  1.00 19.97           O  
ANISOU  542  O   LEU A  87     2524   3137   1928    -45    748   -274       O  
ATOM    543  CB  LEU A  87      15.528   7.730  81.479  1.00 18.39           C  
ANISOU  543  CB  LEU A  87     2342   2871   1775    -12    636   -280       C  
ATOM    544  CG  LEU A  87      15.465   9.236  81.727  1.00 20.56           C  
ANISOU  544  CG  LEU A  87     2528   3199   2085     12    567   -364       C  
ATOM    545  CD1 LEU A  87      16.212   9.589  83.023  1.00 20.84           C  
ANISOU  545  CD1 LEU A  87     2587   3304   2027    101    530   -382       C  
ATOM    546  CD2 LEU A  87      16.026   9.989  80.526  1.00 17.12           C  
ANISOU  546  CD2 LEU A  87     2024   2737   1745     -3    496   -411       C  
ATOM    547  N   LYS A  88      12.544   6.418  81.886  1.00 21.07           N  
ANISOU  547  N   LYS A  88     2700   3157   2147   -154    808   -201       N  
ATOM    548  CA ALYS A  88      11.102   6.634  81.945  0.53 22.22           C  
ANISOU  548  CA ALYS A  88     2787   3312   2344   -213    840   -221       C  
ATOM    549  CA BLYS A  88      11.102   6.646  81.954  0.47 22.39           C  
ANISOU  549  CA BLYS A  88     2809   3334   2365   -212    839   -221       C  
ATOM    550  C   LYS A  88      10.579   6.331  83.350  1.00 24.39           C  
ANISOU  550  C   LYS A  88     3100   3636   2532   -187    909   -181       C  
ATOM    551  O   LYS A  88       9.852   7.128  83.946  1.00 22.51           O  
ANISOU  551  O   LYS A  88     2810   3452   2291   -175    911   -221       O  
ATOM    552  CB ALYS A  88      10.389   5.773  80.902  0.53 25.26           C  
ANISOU  552  CB ALYS A  88     3167   3621   2811   -305    869   -205       C  
ATOM    553  CB BLYS A  88      10.344   5.812  80.925  0.47 26.39           C  
ANISOU  553  CB BLYS A  88     3306   3766   2954   -305    869   -207       C  
ATOM    554  CG ALYS A  88       8.868   5.839  80.954  0.53 30.46           C  
ANISOU  554  CG ALYS A  88     3764   4290   3518   -369    904   -229       C  
ATOM    555  CG BLYS A  88       8.842   6.087  80.927  0.47 31.13           C  
ANISOU  555  CG BLYS A  88     3834   4385   3609   -363    892   -242       C  
ATOM    556  CD ALYS A  88       8.366   7.274  80.894  0.53 31.11           C  
ANISOU  556  CD ALYS A  88     3752   4431   3637   -349    845   -306       C  
ATOM    557  CD BLYS A  88       8.060   4.938  80.324  0.47 31.82           C  
ANISOU  557  CD BLYS A  88     3936   4405   3750   -452    943   -219       C  
ATOM    558  CE ALYS A  88       6.844   7.322  80.840  0.53 34.31           C  
ANISOU  558  CE ALYS A  88     4093   4850   4092   -408    876   -336       C  
ATOM    559  CE BLYS A  88       6.626   5.330  80.017  0.47 34.78           C  
ANISOU  559  CE BLYS A  88     4221   4802   4192   -508    944   -275       C  
ATOM    560  NZ ALYS A  88       6.309   8.677  81.174  0.53 33.67           N  
ANISOU  560  NZ ALYS A  88     3936   4833   4022   -373    835   -402       N  
ATOM    561  NZ BLYS A  88       5.974   4.339  79.117  0.47 32.34           N  
ANISOU  561  NZ BLYS A  88     3912   4426   3949   -592    968   -279       N  
ATOM    562  N   LYS A  89      10.970   5.178  83.885  1.00 21.51           N  
ANISOU  562  N   LYS A  89     2829   3250   2094   -174    964    -99       N  
ATOM    563  CA  LYS A  89      10.531   4.789  85.225  1.00 24.71           C  
ANISOU  563  CA  LYS A  89     3275   3708   2404   -147   1032    -48       C  
ATOM    564  C   LYS A  89      11.064   5.764  86.270  1.00 21.81           C  
ANISOU  564  C   LYS A  89     2906   3441   1942    -41    995    -83       C  
ATOM    565  O   LYS A  89      10.378   6.102  87.232  1.00 21.13           O  
ANISOU  565  O   LYS A  89     2808   3414   1807    -15   1035    -87       O  
ATOM    566  CB  LYS A  89      10.974   3.361  85.555  1.00 32.85           C  
ANISOU  566  CB  LYS A  89     4419   4683   3379   -154   1085     49       C  
ATOM    567  CG  LYS A  89      10.228   2.287  84.785  1.00 42.87           C  
ANISOU  567  CG  LYS A  89     5706   5842   4740   -257   1143     86       C  
ATOM    568  CD  LYS A  89      10.304   0.945  85.504  1.00 52.13           C  
ANISOU  568  CD  LYS A  89     6994   6958   5854   -259   1219    188       C  
ATOM    569  CE  LYS A  89      10.895  -0.133  84.613  1.00 57.49           C  
ANISOU  569  CE  LYS A  89     7753   7505   6585   -283   1223    229       C  
ATOM    570  NZ  LYS A  89      10.154  -0.248  83.327  1.00 60.44           N  
ANISOU  570  NZ  LYS A  89     8062   7814   7090   -384   1223    175       N  
ATOM    571  N   PHE A  90      12.290   6.227  86.062  1.00 23.38           N  
ANISOU  571  N   PHE A  90     3122   3644   2118     25    924   -115       N  
ATOM    572  CA  PHE A  90      12.918   7.178  86.970  1.00 22.63           C  
ANISOU  572  CA  PHE A  90     3058   3577   1964     90    886   -179       C  
ATOM    573  C   PHE A  90      12.152   8.498  86.985  1.00 23.21           C  
ANISOU  573  C   PHE A  90     3020   3692   2105     78    842   -266       C  
ATOM    574  O   PHE A  90      11.859   9.044  88.046  1.00 25.15           O  
ANISOU  574  O   PHE A  90     3266   3992   2296    111    848   -298       O  
ATOM    575  CB  PHE A  90      14.373   7.401  86.554  1.00 18.91           C  
ANISOU  575  CB  PHE A  90     2582   3113   1489    132    784   -211       C  
ATOM    576  CG  PHE A  90      15.138   8.319  87.461  1.00 21.00           C  
ANISOU  576  CG  PHE A  90     2823   3455   1701    216    693   -270       C  
ATOM    577  CD1 PHE A  90      15.483   7.920  88.744  1.00 27.68           C  
ANISOU  577  CD1 PHE A  90     3739   4351   2428    279    699   -236       C  
ATOM    578  CD2 PHE A  90      15.547   9.568  87.018  1.00 23.84           C  
ANISOU  578  CD2 PHE A  90     3088   3836   2136    232    596   -360       C  
ATOM    579  CE1 PHE A  90      16.196   8.761  89.579  1.00 28.33           C  
ANISOU  579  CE1 PHE A  90     3794   4506   2465    362    611   -296       C  
ATOM    580  CE2 PHE A  90      16.264  10.412  87.846  1.00 24.58           C  
ANISOU  580  CE2 PHE A  90     3153   3995   2190    304    512   -422       C  
ATOM    581  CZ  PHE A  90      16.592  10.007  89.127  1.00 27.66           C  
ANISOU  581  CZ  PHE A  90     3610   4439   2460    372    518   -393       C  
ATOM    582  N   MET A  91      11.813   9.009  85.806  1.00 19.96           N  
ANISOU  582  N   MET A  91     2519   3253   1811     23    798   -309       N  
ATOM    583  CA  MET A  91      11.034  10.243  85.738  1.00 22.59           C  
ANISOU  583  CA  MET A  91     2756   3614   2213      6    758   -390       C  
ATOM    584  C   MET A  91       9.628  10.084  86.321  1.00 22.59           C  
ANISOU  584  C   MET A  91     2741   3637   2206    -24    838   -376       C  
ATOM    585  O   MET A  91       9.126  10.992  86.976  1.00 27.00           O  
ANISOU  585  O   MET A  91     3258   4245   2758     -1    826   -432       O  
ATOM    586  CB  MET A  91      10.974  10.775  84.311  1.00 21.11           C  
ANISOU  586  CB  MET A  91     2492   3383   2146    -44    696   -431       C  
ATOM    587  CG  MET A  91      12.323  11.283  83.819  1.00 23.16           C  
ANISOU  587  CG  MET A  91     2743   3633   2422     -7    610   -463       C  
ATOM    588  SD  MET A  91      12.185  12.099  82.223  1.00 30.74           S  
ANISOU  588  SD  MET A  91     3618   4544   3519    -57    544   -511       S  
ATOM    589  CE  MET A  91      11.604  10.741  81.225  1.00 17.48           C  
ANISOU  589  CE  MET A  91     1967   2802   1871   -134    607   -443       C  
ATOM    590  N   ASP A  92       9.000   8.935  86.083  1.00 25.67           N  
ANISOU  590  N   ASP A  92     3157   3994   2601    -79    917   -304       N  
ATOM    591  CA  ASP A  92       7.688   8.655  86.672  1.00 24.59           C  
ANISOU  591  CA  ASP A  92     3001   3884   2457   -112    999   -285       C  
ATOM    592  C   ASP A  92       7.783   8.594  88.193  1.00 24.48           C  
ANISOU  592  C   ASP A  92     3055   3929   2318    -38   1056   -255       C  
ATOM    593  O   ASP A  92       6.895   9.073  88.902  1.00 24.85           O  
ANISOU  593  O   ASP A  92     3068   4023   2351    -33   1093   -283       O  
ATOM    594  CB  ASP A  92       7.108   7.345  86.133  1.00 31.73           C  
ANISOU  594  CB  ASP A  92     3921   4736   3397   -195   1066   -216       C  
ATOM    595  CG  ASP A  92       6.573   7.477  84.716  1.00 39.35           C  
ANISOU  595  CG  ASP A  92     4813   5647   4491   -277   1023   -262       C  
ATOM    596  OD1 ASP A  92       6.441   8.621  84.226  1.00 37.11           O  
ANISOU  596  OD1 ASP A  92     4457   5380   4263   -268    951   -340       O  
ATOM    597  OD2 ASP A  92       6.278   6.433  84.096  1.00 45.14           O  
ANISOU  597  OD2 ASP A  92     5565   6319   5265   -349   1059   -223       O  
ATOM    598  N   ALA A  93       8.866   8.006  88.693  1.00 21.11           N  
ANISOU  598  N   ALA A  93     2729   3497   1795     23   1064   -200       N  
ATOM    599  CA  ALA A  93       9.104   7.949  90.130  1.00 29.08           C  
ANISOU  599  CA  ALA A  93     3833   4538   2677     88   1116   -182       C  
ATOM    600  C   ALA A  93       9.356   9.352  90.674  1.00 28.94           C  
ANISOU  600  C   ALA A  93     3765   4578   2652    122   1032   -295       C  
ATOM    601  O   ALA A  93       9.086   9.644  91.837  1.00 29.15           O  
ANISOU  601  O   ALA A  93     3816   4659   2599    152   1062   -315       O  
ATOM    602  CB  ALA A  93      10.274   7.032  90.443  1.00 34.82           C  
ANISOU  602  CB  ALA A  93     4686   5218   3327     78   1116   -140       C  
ATOM    603  N   SER A  94       9.872  10.222  89.817  1.00 28.62           N  
ANISOU  603  N   SER A  94     3646   4534   2695    123    921   -365       N  
ATOM    604  CA  SER A  94      10.148  11.596  90.206  1.00 27.02           C  
ANISOU  604  CA  SER A  94     3378   4386   2501    167    828   -466       C  
ATOM    605  C   SER A  94       9.104  12.542  89.617  1.00 32.84           C  
ANISOU  605  C   SER A  94     4006   5125   3346    126    808   -530       C  
ATOM    606  O   SER A  94       9.380  13.721  89.410  1.00 31.25           O  
ANISOU  606  O   SER A  94     3737   4937   3197    146    718   -613       O  
ATOM    607  CB  SER A  94      11.544  12.008  89.724  1.00 33.21           C  
ANISOU  607  CB  SER A  94     4149   5163   3305    202    715   -502       C  
ATOM    608  OG  SER A  94      11.859  13.319  90.150  1.00 32.19           O  
ANISOU  608  OG  SER A  94     3957   5083   3190    247    626   -597       O  
ATOM    609  N   ALA A  95       7.908  12.024  89.353  1.00 36.12           N  
ANISOU  609  N   ALA A  95     4403   5525   3797     70    890   -493       N  
ATOM    610  CA  ALA A  95       6.866  12.800  88.679  1.00 38.57           C  
ANISOU  610  CA  ALA A  95     4608   5835   4210     25    867   -551       C  
ATOM    611  C   ALA A  95       6.506  14.097  89.407  1.00 34.99           C  
ANISOU  611  C   ALA A  95     4101   5440   3752     70    828   -640       C  
ATOM    612  O   ALA A  95       6.188  15.102  88.770  1.00 39.55           O  
ANISOU  612  O   ALA A  95     4599   6012   4417     59    762   -709       O  
ATOM    613  CB  ALA A  95       5.614  11.949  88.466  1.00 45.28           C  
ANISOU  613  CB  ALA A  95     5442   6674   5088    -41    961   -500       C  
ATOM    614  N   LEU A  96       6.559  14.071  90.733  1.00 28.79           N  
ANISOU  614  N   LEU A  96     3366   4711   2861    122    869   -638       N  
ATOM    615  CA  LEU A  96       6.171  15.233  91.532  1.00 28.53           C  
ANISOU  615  CA  LEU A  96     3286   4739   2814    166    839   -723       C  
ATOM    616  C   LEU A  96       7.367  15.873  92.228  1.00 29.68           C  
ANISOU  616  C   LEU A  96     3458   4917   2901    237    757   -773       C  
ATOM    617  O   LEU A  96       7.217  16.809  93.005  1.00 32.12           O  
ANISOU  617  O   LEU A  96     3737   5280   3188    282    726   -847       O  
ATOM    618  CB  LEU A  96       5.099  14.852  92.555  1.00 41.10           C  
ANISOU  618  CB  LEU A  96     4896   6383   4336    169    951   -699       C  
ATOM    619  CG  LEU A  96       3.783  14.335  91.966  1.00 44.54           C  
ANISOU  619  CG  LEU A  96     5283   6802   4838     98   1028   -664       C  
ATOM    620  CD1 LEU A  96       2.755  14.097  93.066  1.00 44.55           C  
ANISOU  620  CD1 LEU A  96     5293   6863   4772    107   1139   -648       C  
ATOM    621  CD2 LEU A  96       3.241  15.294  90.910  1.00 45.82           C  
ANISOU  621  CD2 LEU A  96     5337   6946   5125     68    951   -739       C  
ATOM    622  N   THR A  97       8.557  15.367  91.931  1.00 33.40           N  
ANISOU  622  N   THR A  97     3979   5358   3352    248    718   -737       N  
ATOM    623  CA  THR A  97       9.786  15.890  92.513  1.00 34.35           C  
ANISOU  623  CA  THR A  97     4114   5512   3424    314    629   -784       C  
ATOM    624  C   THR A  97      10.711  16.339  91.387  1.00 30.45           C  
ANISOU  624  C   THR A  97     3577   4966   3027    301    533   -813       C  
ATOM    625  O   THR A  97      10.912  15.608  90.429  1.00 29.24           O  
ANISOU  625  O   THR A  97     3441   4757   2913    259    549   -755       O  
ATOM    626  CB  THR A  97      10.511  14.797  93.308  1.00 40.58           C  
ANISOU  626  CB  THR A  97     5007   6326   4086    351    666   -712       C  
ATOM    627  OG1 THR A  97       9.600  14.201  94.240  1.00 42.42           O  
ANISOU  627  OG1 THR A  97     5294   6593   4231    349    777   -666       O  
ATOM    628  CG2 THR A  97      11.715  15.376  94.048  1.00 41.85           C  
ANISOU  628  CG2 THR A  97     5170   6541   4190    429    565   -769       C  
ATOM    629  N   GLY A  98      11.280  17.534  91.490  1.00 27.16           N  
ANISOU  629  N   GLY A  98     3104   4564   2651    335    437   -904       N  
ATOM    630  CA  GLY A  98      12.184  17.987  90.444  1.00 30.45           C  
ANISOU  630  CA  GLY A  98     3481   4928   3162    319    355   -931       C  
ATOM    631  C   GLY A  98      13.434  17.121  90.355  1.00 28.76           C  
ANISOU  631  C   GLY A  98     3321   4708   2897    340    334   -880       C  
ATOM    632  O   GLY A  98      14.020  16.781  91.381  1.00 31.72           O  
ANISOU  632  O   GLY A  98     3743   5140   3169    398    325   -873       O  
ATOM    633  N   ILE A  99      13.831  16.738  89.143  1.00 24.89           N  
ANISOU  633  N   ILE A  99     2827   4156   2476    299    325   -844       N  
ATOM    634  CA  ILE A  99      15.145  16.128  88.955  1.00 21.82           C  
ANISOU  634  CA  ILE A  99     2473   3762   2057    325    286   -814       C  
ATOM    635  C   ILE A  99      16.149  17.263  89.028  1.00 23.40           C  
ANISOU  635  C   ILE A  99     2610   3976   2307    358    182   -906       C  
ATOM    636  O   ILE A  99      16.058  18.215  88.254  1.00 23.34           O  
ANISOU  636  O   ILE A  99     2535   3922   2411    323    144   -959       O  
ATOM    637  CB  ILE A  99      15.267  15.411  87.601  1.00 27.73           C  
ANISOU  637  CB  ILE A  99     3231   4440   2865    271    310   -753       C  
ATOM    638  CG1 ILE A  99      14.183  14.338  87.479  1.00 31.81           C  
ANISOU  638  CG1 ILE A  99     3799   4935   3351    227    417   -671       C  
ATOM    639  CG2 ILE A  99      16.660  14.800  87.436  1.00 26.10           C  
ANISOU  639  CG2 ILE A  99     3057   4234   2625    308    269   -727       C  
ATOM    640  CD1 ILE A  99      14.170  13.638  86.153  1.00 31.95           C  
ANISOU  640  CD1 ILE A  99     3822   4885   3432    170    442   -618       C  
ATOM    641  N   PRO A 100      17.098  17.182  89.972  1.00 20.53           N  
ANISOU  641  N   PRO A 100     2264   3672   1863    426    134   -927       N  
ATOM    642  CA  PRO A 100      18.044  18.285  90.170  1.00 19.78           C  
ANISOU  642  CA  PRO A 100     2098   3596   1820    456     36  -1026       C  
ATOM    643  C   PRO A 100      18.775  18.620  88.876  1.00 20.51           C  
ANISOU  643  C   PRO A 100     2141   3621   2032    413     -6  -1043       C  
ATOM    644  O   PRO A 100      19.155  17.712  88.137  1.00 20.38           O  
ANISOU  644  O   PRO A 100     2158   3574   2010    397     15   -976       O  
ATOM    645  CB  PRO A 100      19.025  17.723  91.207  1.00 25.65           C  
ANISOU  645  CB  PRO A 100     2881   4416   2450    537      0  -1020       C  
ATOM    646  CG  PRO A 100      18.227  16.697  91.953  1.00 30.28           C  
ANISOU  646  CG  PRO A 100     3558   5035   2913    556     86   -936       C  
ATOM    647  CD  PRO A 100      17.344  16.068  90.905  1.00 27.14           C  
ANISOU  647  CD  PRO A 100     3186   4562   2562    480    169   -860       C  
ATOM    648  N   LEU A 101      18.937  19.909  88.597  1.00 21.45           N  
ANISOU  648  N   LEU A 101     2182   3709   2257    394    -59  -1130       N  
ATOM    649  CA  LEU A 101      19.664  20.352  87.400  1.00 20.62           C  
ANISOU  649  CA  LEU A 101     2027   3535   2272    351    -94  -1150       C  
ATOM    650  C   LEU A 101      21.036  19.689  87.187  1.00 19.24           C  
ANISOU  650  C   LEU A 101     1856   3377   2076    376   -130  -1134       C  
ATOM    651  O   LEU A 101      21.358  19.327  86.060  1.00 21.17           O  
ANISOU  651  O   LEU A 101     2100   3568   2374    338   -118  -1096       O  
ATOM    652  CB  LEU A 101      19.784  21.880  87.368  1.00 23.68           C  
ANISOU  652  CB  LEU A 101     2335   3889   2774    338   -144  -1249       C  
ATOM    653  CG  LEU A 101      20.497  22.479  86.154  1.00 23.79           C  
ANISOU  653  CG  LEU A 101     2297   3820   2924    292   -168  -1269       C  
ATOM    654  CD1 LEU A 101      19.773  22.091  84.878  1.00 26.61           C  
ANISOU  654  CD1 LEU A 101     2679   4109   3325    235   -117  -1198       C  
ATOM    655  CD2 LEU A 101      20.582  23.994  86.279  1.00 29.17           C  
ANISOU  655  CD2 LEU A 101     2910   4459   3715    286   -204  -1361       C  
ATOM    656  N   PRO A 102      21.852  19.535  88.253  1.00 20.29           N  
ANISOU  656  N   PRO A 102     1991   3588   2132    446   -176  -1165       N  
ATOM    657  CA  PRO A 102      23.134  18.857  88.003  1.00 17.85           C  
ANISOU  657  CA  PRO A 102     1681   3298   1802    476   -211  -1149       C  
ATOM    658  C   PRO A 102      22.974  17.447  87.435  1.00 22.64           C  
ANISOU  658  C   PRO A 102     2370   3890   2343    473   -154  -1037       C  
ATOM    659  O   PRO A 102      23.813  17.007  86.647  1.00 19.51           O  
ANISOU  659  O   PRO A 102     1965   3472   1975    468   -169  -1019       O  
ATOM    660  CB  PRO A 102      23.773  18.795  89.396  1.00 23.19           C  
ANISOU  660  CB  PRO A 102     2358   4071   2381    565   -261  -1189       C  
ATOM    661  CG  PRO A 102      23.209  19.980  90.106  1.00 28.17           C  
ANISOU  661  CG  PRO A 102     2945   4713   3045    562   -277  -1272       C  
ATOM    662  CD  PRO A 102      21.786  20.082  89.625  1.00 26.81           C  
ANISOU  662  CD  PRO A 102     2803   4485   2898    502   -208  -1230       C  
ATOM    663  N   LEU A 103      21.909  16.749  87.817  1.00 19.77           N  
ANISOU  663  N   LEU A 103     2082   3533   1898    474    -84   -966       N  
ATOM    664  CA  LEU A 103      21.700  15.389  87.325  1.00 16.94           C  
ANISOU  664  CA  LEU A 103     1804   3149   1483    467    -18   -858       C  
ATOM    665  C   LEU A 103      21.192  15.416  85.890  1.00 18.85           C  
ANISOU  665  C   LEU A 103     2029   3305   1828    385     23   -833       C  
ATOM    666  O   LEU A 103      21.625  14.621  85.054  1.00 17.63           O  
ANISOU  666  O   LEU A 103     1900   3119   1681    375     41   -780       O  
ATOM    667  CB  LEU A 103      20.740  14.613  88.237  1.00 19.38           C  
ANISOU  667  CB  LEU A 103     2198   3486   1679    488     54   -790       C  
ATOM    668  CG  LEU A 103      20.560  13.130  87.919  1.00 20.89           C  
ANISOU  668  CG  LEU A 103     2484   3648   1806    487    129   -675       C  
ATOM    669  CD1 LEU A 103      21.875  12.382  88.086  1.00 20.14           C  
ANISOU  669  CD1 LEU A 103     2421   3583   1647    563     82   -646       C  
ATOM    670  CD2 LEU A 103      19.485  12.506  88.800  1.00 23.66           C  
ANISOU  670  CD2 LEU A 103     2911   4015   2065    488    214   -614       C  
ATOM    671  N   ILE A 104      20.281  16.339  85.598  1.00 16.79           N  
ANISOU  671  N   ILE A 104     1724   3009   1645    332     35   -871       N  
ATOM    672  CA  ILE A 104      19.797  16.515  84.229  1.00 15.70           C  
ANISOU  672  CA  ILE A 104     1561   2792   1610    260     64   -853       C  
ATOM    673  C   ILE A 104      20.971  16.835  83.305  1.00 14.91           C  
ANISOU  673  C   ILE A 104     1415   2660   1592    249     15   -883       C  
ATOM    674  O   ILE A 104      21.114  16.258  82.219  1.00 14.80           O  
ANISOU  674  O   ILE A 104     1412   2599   1611    218     43   -833       O  
ATOM    675  CB  ILE A 104      18.761  17.653  84.142  1.00 14.53           C  
ANISOU  675  CB  ILE A 104     1366   2618   1538    222     66   -901       C  
ATOM    676  CG1 ILE A 104      17.507  17.293  84.944  1.00 17.81           C  
ANISOU  676  CG1 ILE A 104     1820   3066   1881    226    126   -871       C  
ATOM    677  CG2 ILE A 104      18.394  17.936  82.691  1.00 17.69           C  
ANISOU  677  CG2 ILE A 104     1736   2939   2046    159     81   -886       C  
ATOM    678  CD1 ILE A 104      16.417  18.351  84.884  1.00 18.17           C  
ANISOU  678  CD1 ILE A 104     1817   3093   1993    198    129   -919       C  
ATOM    679  N   LYS A 105      21.820  17.748  83.761  1.00 15.81           N  
ANISOU  679  N   LYS A 105     1471   2798   1739    273    -56   -966       N  
ATOM    680  CA  LYS A 105      22.994  18.170  82.996  1.00 16.11           C  
ANISOU  680  CA  LYS A 105     1451   2807   1863    259   -102  -1009       C  
ATOM    681  C   LYS A 105      23.967  17.015  82.791  1.00 16.32           C  
ANISOU  681  C   LYS A 105     1510   2863   1827    297   -104   -964       C  
ATOM    682  O   LYS A 105      24.501  16.816  81.692  1.00 16.05           O  
ANISOU  682  O   LYS A 105     1461   2776   1861    263    -98   -929       O  
ATOM    683  CB  LYS A 105      23.681  19.327  83.729  1.00 17.75           C  
ANISOU  683  CB  LYS A 105     1587   3040   2117    280   -170  -1110       C  
ATOM    684  CG  LYS A 105      24.885  19.909  83.020  1.00 21.75           C  
ANISOU  684  CG  LYS A 105     2025   3508   2732    257   -205  -1157       C  
ATOM    685  CD  LYS A 105      25.352  21.177  83.748  1.00 23.90           C  
ANISOU  685  CD  LYS A 105     2236   3776   3067    274   -241  -1248       C  
ATOM    686  CE  LYS A 105      24.236  22.210  83.802  1.00 21.30           C  
ANISOU  686  CE  LYS A 105     1897   3399   2799    245   -221  -1272       C  
ATOM    687  NZ  LYS A 105      24.690  23.522  84.341  1.00 28.34           N  
ANISOU  687  NZ  LYS A 105     2735   4266   3767    255   -250  -1362       N  
ATOM    688  N   SER A 106      24.197  16.245  83.849  1.00 16.00           N  
ANISOU  688  N   SER A 106     1519   2895   1666    367   -114   -939       N  
ATOM    689  CA  SER A 106      25.073  15.080  83.759  1.00 15.25           C  
ANISOU  689  CA  SER A 106     1466   2830   1499    421   -117   -888       C  
ATOM    690  C   SER A 106      24.524  14.038  82.792  1.00 18.59           C  
ANISOU  690  C   SER A 106     1954   3184   1925    383    -42   -776       C  
ATOM    691  O   SER A 106      25.253  13.505  81.955  1.00 13.91           O  
ANISOU  691  O   SER A 106     1361   2554   1370    377    -46   -731       O  
ATOM    692  CB  SER A 106      25.267  14.443  85.138  1.00 19.07           C  
ANISOU  692  CB  SER A 106     2004   3394   1846    510   -136   -866       C  
ATOM    693  OG  SER A 106      26.016  13.252  85.019  1.00 18.28           O  
ANISOU  693  OG  SER A 106     1958   3313   1674    570   -135   -803       O  
ATOM    694  N   TYR A 107      23.240  13.731  82.916  1.00 15.30           N  
ANISOU  694  N   TYR A 107     1589   2750   1475    354     26   -733       N  
ATOM    695  CA  TYR A 107      22.636  12.739  82.031  1.00 14.22           C  
ANISOU  695  CA  TYR A 107     1510   2543   1350    308     96   -634       C  
ATOM    696  C   TYR A 107      22.715  13.181  80.570  1.00 15.16           C  
ANISOU  696  C   TYR A 107     1578   2584   1597    237     93   -630       C  
ATOM    697  O   TYR A 107      23.040  12.383  79.697  1.00 14.80           O  
ANISOU  697  O   TYR A 107     1561   2492   1570    224    112   -567       O  
ATOM    698  CB  TYR A 107      21.175  12.484  82.408  1.00 15.55           C  
ANISOU  698  CB  TYR A 107     1721   2711   1477    277    171   -605       C  
ATOM    699  CG  TYR A 107      20.959  11.552  83.585  1.00 17.38           C  
ANISOU  699  CG  TYR A 107     2038   2991   1573    334    209   -554       C  
ATOM    700  CD1 TYR A 107      22.017  10.867  84.175  1.00 16.96           C  
ANISOU  700  CD1 TYR A 107     2032   2979   1433    419    177   -528       C  
ATOM    701  CD2 TYR A 107      19.684  11.361  84.106  1.00 15.89           C  
ANISOU  701  CD2 TYR A 107     1885   2801   1353    302    278   -524       C  
ATOM    702  CE1 TYR A 107      21.805  10.012  85.249  1.00 17.68           C  
ANISOU  702  CE1 TYR A 107     2212   3099   1406    472    213   -464       C  
ATOM    703  CE2 TYR A 107      19.464  10.517  85.173  1.00 17.54           C  
ANISOU  703  CE2 TYR A 107     2178   3040   1446    345    323   -465       C  
ATOM    704  CZ  TYR A 107      20.523   9.843  85.741  1.00 18.60           C  
ANISOU  704  CZ  TYR A 107     2368   3206   1494    430    291   -431       C  
ATOM    705  OH  TYR A 107      20.287   8.997  86.799  1.00 19.49           O  
ANISOU  705  OH  TYR A 107     2572   3341   1494    474    337   -362       O  
ATOM    706  N   LEU A 108      22.416  14.448  80.298  1.00 12.67           N  
ANISOU  706  N   LEU A 108     1193   2253   1368    198     70   -696       N  
ATOM    707  CA  LEU A 108      22.441  14.921  78.913  1.00 11.99           C  
ANISOU  707  CA  LEU A 108     1067   2094   1396    136     72   -683       C  
ATOM    708  C   LEU A 108      23.847  14.845  78.343  1.00 10.54           C  
ANISOU  708  C   LEU A 108      854   1900   1251    148     34   -679       C  
ATOM    709  O   LEU A 108      24.048  14.424  77.199  1.00 12.10           O  
ANISOU  709  O   LEU A 108     1060   2049   1490    118     56   -625       O  
ATOM    710  CB  LEU A 108      21.914  16.353  78.806  1.00 13.22           C  
ANISOU  710  CB  LEU A 108     1161   2228   1636    103     53   -752       C  
ATOM    711  CG  LEU A 108      21.786  16.883  77.375  1.00 14.94           C  
ANISOU  711  CG  LEU A 108     1349   2368   1961     45     61   -727       C  
ATOM    712  CD1 LEU A 108      20.767  16.070  76.561  1.00 18.03           C  
ANISOU  712  CD1 LEU A 108     1784   2728   2338     12    116   -653       C  
ATOM    713  CD2 LEU A 108      21.400  18.353  77.403  1.00 12.89           C  
ANISOU  713  CD2 LEU A 108     1033   2081   1784     27     38   -796       C  
ATOM    714  N   PHE A 109      24.820  15.243  79.153  1.00 11.98           N  
ANISOU  714  N   PHE A 109      997   2137   1417    194    -22   -743       N  
ATOM    715  CA  PHE A 109      26.225  15.233  78.741  1.00 12.85           C  
ANISOU  715  CA  PHE A 109     1062   2254   1568    209    -61   -755       C  
ATOM    716  C   PHE A 109      26.648  13.812  78.370  1.00 14.08           C  
ANISOU  716  C   PHE A 109     1278   2408   1663    244    -36   -672       C  
ATOM    717  O   PHE A 109      27.300  13.593  77.352  1.00 13.49           O  
ANISOU  717  O   PHE A 109     1184   2300   1641    225    -29   -643       O  
ATOM    718  CB  PHE A 109      27.088  15.764  79.888  1.00 14.88           C  
ANISOU  718  CB  PHE A 109     1267   2588   1799    262   -131   -849       C  
ATOM    719  CG  PHE A 109      28.502  16.112  79.496  1.00 14.40           C  
ANISOU  719  CG  PHE A 109     1126   2537   1808    261   -176   -892       C  
ATOM    720  CD1 PHE A 109      28.758  17.015  78.476  1.00 15.10           C  
ANISOU  720  CD1 PHE A 109     1174   2545   2019    183   -163   -896       C  
ATOM    721  CD2 PHE A 109      29.575  15.563  80.185  1.00 15.70           C  
ANISOU  721  CD2 PHE A 109     1275   2782   1907    338   -227   -918       C  
ATOM    722  CE1 PHE A 109      30.070  17.358  78.132  1.00 15.62           C  
ANISOU  722  CE1 PHE A 109     1207   2589   2137    170   -180   -911       C  
ATOM    723  CE2 PHE A 109      30.887  15.895  79.849  1.00 19.75           C  
ANISOU  723  CE2 PHE A 109     1726   3295   2483    329   -259   -954       C  
ATOM    724  CZ  PHE A 109      31.130  16.793  78.821  1.00 17.97           C  
ANISOU  724  CZ  PHE A 109     1482   2969   2377    238   -226   -944       C  
ATOM    725  N   GLN A 110      26.279  12.852  79.213  1.00 14.20           N  
ANISOU  725  N   GLN A 110     1370   2458   1567    297    -19   -635       N  
ATOM    726  CA  GLN A 110      26.606  11.451  78.977  1.00 12.94           C  
ANISOU  726  CA  GLN A 110     1283   2286   1347    338      8   -555       C  
ATOM    727  C   GLN A 110      25.893  10.898  77.752  1.00 14.79           C  
ANISOU  727  C   GLN A 110     1557   2438   1625    274     71   -486       C  
ATOM    728  O   GLN A 110      26.478  10.135  76.984  1.00 12.89           O  
ANISOU  728  O   GLN A 110     1337   2168   1394    285     82   -443       O  
ATOM    729  CB  GLN A 110      26.232  10.602  80.194  1.00 11.95           C  
ANISOU  729  CB  GLN A 110     1243   2205   1094    405     24   -522       C  
ATOM    730  CG  GLN A 110      27.078  10.858  81.435  1.00 14.14           C  
ANISOU  730  CG  GLN A 110     1496   2578   1298    494    -44   -581       C  
ATOM    731  CD  GLN A 110      26.641   9.970  82.578  1.00 16.76           C  
ANISOU  731  CD  GLN A 110     1927   2950   1490    565    -18   -531       C  
ATOM    732  OE1 GLN A 110      26.851   8.761  82.540  1.00 17.56           O  
ANISOU  732  OE1 GLN A 110     2111   3029   1533    612     11   -449       O  
ATOM    733  NE2 GLN A 110      25.999  10.557  83.584  1.00 15.70           N  
ANISOU  733  NE2 GLN A 110     1793   2871   1302    574    -20   -575       N  
ATOM    734  N   LEU A 111      24.623  11.256  77.580  1.00 13.19           N  
ANISOU  734  N   LEU A 111     1363   2204   1444    213    109   -483       N  
ATOM    735  CA  LEU A 111      23.872  10.796  76.414  1.00 14.56           C  
ANISOU  735  CA  LEU A 111     1565   2309   1659    152    160   -431       C  
ATOM    736  C   LEU A 111      24.489  11.331  75.123  1.00 13.18           C  
ANISOU  736  C   LEU A 111     1334   2101   1574    119    144   -438       C  
ATOM    737  O   LEU A 111      24.552  10.622  74.117  1.00 13.20           O  
ANISOU  737  O   LEU A 111     1365   2062   1589    102    171   -393       O  
ATOM    738  CB  LEU A 111      22.401  11.213  76.507  1.00 14.54           C  
ANISOU  738  CB  LEU A 111     1563   2293   1667     98    196   -440       C  
ATOM    739  CG  LEU A 111      21.565  10.544  77.602  1.00 18.19           C  
ANISOU  739  CG  LEU A 111     2087   2781   2042    114    238   -419       C  
ATOM    740  CD1 LEU A 111      20.219  11.255  77.750  1.00 18.04           C  
ANISOU  740  CD1 LEU A 111     2039   2768   2049     65    263   -451       C  
ATOM    741  CD2 LEU A 111      21.366   9.081  77.274  1.00 16.98           C  
ANISOU  741  CD2 LEU A 111     2018   2582   1851    108    292   -344       C  
ATOM    742  N   LEU A 112      24.951  12.577  75.155  1.00 13.37           N  
ANISOU  742  N   LEU A 112     1281   2141   1660    108    103   -496       N  
ATOM    743  CA  LEU A 112      25.605  13.159  73.986  1.00 12.22           C  
ANISOU  743  CA  LEU A 112     1080   1962   1598     75     96   -497       C  
ATOM    744  C   LEU A 112      26.910  12.425  73.674  1.00 12.57           C  
ANISOU  744  C   LEU A 112     1122   2023   1630    116     86   -478       C  
ATOM    745  O   LEU A 112      27.256  12.225  72.504  1.00 12.01           O  
ANISOU  745  O   LEU A 112     1046   1922   1597     95    108   -445       O  
ATOM    746  CB  LEU A 112      25.855  14.655  74.204  1.00 12.24           C  
ANISOU  746  CB  LEU A 112     1004   1968   1677     52     60   -564       C  
ATOM    747  CG  LEU A 112      24.600  15.530  74.149  1.00 15.48           C  
ANISOU  747  CG  LEU A 112     1411   2348   2125     10     72   -580       C  
ATOM    748  CD1 LEU A 112      24.871  16.911  74.754  1.00 15.37           C  
ANISOU  748  CD1 LEU A 112     1336   2335   2170      3     31   -658       C  
ATOM    749  CD2 LEU A 112      24.122  15.645  72.705  1.00 14.72           C  
ANISOU  749  CD2 LEU A 112     1321   2193   2080    -37    104   -529       C  
ATOM    750  N   GLN A 113      27.643  12.025  74.712  1.00 12.28           N  
ANISOU  750  N   GLN A 113     1088   2043   1536    182     53   -501       N  
ATOM    751  CA  GLN A 113      28.876  11.256  74.486  1.00 13.16           C  
ANISOU  751  CA  GLN A 113     1194   2177   1630    237     40   -486       C  
ATOM    752  C   GLN A 113      28.582   9.914  73.827  1.00 16.66           C  
ANISOU  752  C   GLN A 113     1722   2577   2030    249     87   -412       C  
ATOM    753  O   GLN A 113      29.267   9.515  72.880  1.00 14.43           O  
ANISOU  753  O   GLN A 113     1429   2279   1773    255     99   -392       O  
ATOM    754  CB  GLN A 113      29.641  11.026  75.794  1.00 14.16           C  
ANISOU  754  CB  GLN A 113     1312   2380   1689    321    -12   -524       C  
ATOM    755  CG  GLN A 113      30.183  12.299  76.418  1.00 12.49           C  
ANISOU  755  CG  GLN A 113     1003   2217   1524    313    -69   -616       C  
ATOM    756  CD  GLN A 113      30.935  12.037  77.708  1.00 17.40           C  
ANISOU  756  CD  GLN A 113     1615   2928   2068    406   -130   -662       C  
ATOM    757  OE1 GLN A 113      31.816  11.182  77.762  1.00 19.43           O  
ANISOU  757  OE1 GLN A 113     1881   3220   2282    478   -147   -643       O  
ATOM    758  NE2 GLN A 113      30.579  12.766  78.758  1.00 17.90           N  
ANISOU  758  NE2 GLN A 113     1661   3034   2108    413   -165   -725       N  
ATOM    759  N   GLY A 114      27.568   9.214  74.333  1.00 12.76           N  
ANISOU  759  N   GLY A 114     1311   2062   1474    252    117   -376       N  
ATOM    760  CA  GLY A 114      27.194   7.935  73.750  1.00 14.06           C  
ANISOU  760  CA  GLY A 114     1562   2174   1608    254    165   -314       C  
ATOM    761  C   GLY A 114      26.725   8.089  72.313  1.00 12.99           C  
ANISOU  761  C   GLY A 114     1414   1987   1536    184    197   -300       C  
ATOM    762  O   GLY A 114      27.061   7.285  71.432  1.00 12.75           O  
ANISOU  762  O   GLY A 114     1414   1924   1506    193    218   -271       O  
ATOM    763  N   LEU A 115      25.950   9.136  72.062  1.00 14.89           N  
ANISOU  763  N   LEU A 115     1612   2221   1824    122    197   -323       N  
ATOM    764  CA  LEU A 115      25.394   9.343  70.725  1.00 11.84           C  
ANISOU  764  CA  LEU A 115     1218   1794   1487     63    222   -308       C  
ATOM    765  C   LEU A 115      26.483   9.773  69.753  1.00 13.29           C  
ANISOU  765  C   LEU A 115     1347   1983   1719     66    212   -312       C  
ATOM    766  O   LEU A 115      26.508   9.335  68.606  1.00 12.75           O  
ANISOU  766  O   LEU A 115     1297   1889   1658     53    237   -286       O  
ATOM    767  CB  LEU A 115      24.279  10.390  70.763  1.00 13.32           C  
ANISOU  767  CB  LEU A 115     1374   1976   1710      9    221   -331       C  
ATOM    768  CG  LEU A 115      23.462  10.540  69.478  1.00 14.74           C  
ANISOU  768  CG  LEU A 115     1555   2121   1924    -42    242   -314       C  
ATOM    769  CD1 LEU A 115      22.891   9.189  69.074  1.00 14.16           C  
ANISOU  769  CD1 LEU A 115     1552   2019   1811    -50    278   -284       C  
ATOM    770  CD2 LEU A 115      22.333  11.562  69.683  1.00 13.41           C  
ANISOU  770  CD2 LEU A 115     1355   1953   1787    -78    236   -339       C  
ATOM    771  N   ALA A 116      27.397  10.625  70.205  1.00 11.61           N  
ANISOU  771  N   ALA A 116     1066   1807   1540     82    178   -348       N  
ATOM    772  CA  ALA A 116      28.475  11.072  69.318  1.00 11.34           C  
ANISOU  772  CA  ALA A 116      971   1781   1559     77    179   -351       C  
ATOM    773  C   ALA A 116      29.315   9.870  68.891  1.00 14.74           C  
ANISOU  773  C   ALA A 116     1430   2219   1951    129    193   -327       C  
ATOM    774  O   ALA A 116      29.775   9.785  67.748  1.00 13.33           O  
ANISOU  774  O   ALA A 116     1236   2032   1795    119    219   -308       O  
ATOM    775  CB  ALA A 116      29.353  12.118  70.011  1.00 15.45           C  
ANISOU  775  CB  ALA A 116     1405   2339   2127     80    140   -405       C  
ATOM    776  N   PHE A 117      29.506   8.935  69.817  1.00 11.04           N  
ANISOU  776  N   PHE A 117     1007   1768   1421    190    179   -325       N  
ATOM    777  CA  PHE A 117      30.265   7.725  69.521  1.00 10.98           C  
ANISOU  777  CA  PHE A 117     1036   1760   1375    253    189   -303       C  
ATOM    778  C   PHE A 117      29.534   6.912  68.459  1.00 13.12           C  
ANISOU  778  C   PHE A 117     1378   1973   1633    226    236   -264       C  
ATOM    779  O   PHE A 117      30.148   6.428  67.509  1.00 12.00           O  
ANISOU  779  O   PHE A 117     1236   1826   1497    245    256   -255       O  
ATOM    780  CB  PHE A 117      30.468   6.892  70.790  1.00 11.40           C  
ANISOU  780  CB  PHE A 117     1141   1833   1357    331    166   -299       C  
ATOM    781  CG  PHE A 117      31.439   5.751  70.619  1.00 14.07           C  
ANISOU  781  CG  PHE A 117     1509   2176   1661    415    166   -282       C  
ATOM    782  CD1 PHE A 117      32.791   5.940  70.844  1.00 17.13           C  
ANISOU  782  CD1 PHE A 117     1820   2629   2059    477    128   -316       C  
ATOM    783  CD2 PHE A 117      30.995   4.493  70.250  1.00 18.82           C  
ANISOU  783  CD2 PHE A 117     2211   2715   2225    434    205   -238       C  
ATOM    784  CE1 PHE A 117      33.690   4.889  70.702  1.00 21.21           C  
ANISOU  784  CE1 PHE A 117     2360   3155   2544    567    126   -304       C  
ATOM    785  CE2 PHE A 117      31.884   3.443  70.096  1.00 22.67           C  
ANISOU  785  CE2 PHE A 117     2732   3199   2684    520    205   -225       C  
ATOM    786  CZ  PHE A 117      33.232   3.642  70.322  1.00 21.49           C  
ANISOU  786  CZ  PHE A 117     2505   3121   2541    591    165   -256       C  
ATOM    787  N   CYS A 118      28.220   6.768  68.611  1.00 12.15           N  
ANISOU  787  N   CYS A 118     1310   1811   1494    182    253   -250       N  
ATOM    788  CA  CYS A 118      27.426   6.057  67.610  1.00 11.55           C  
ANISOU  788  CA  CYS A 118     1293   1683   1413    148    291   -228       C  
ATOM    789  C   CYS A 118      27.602   6.687  66.241  1.00 13.23           C  
ANISOU  789  C   CYS A 118     1459   1903   1667    113    302   -231       C  
ATOM    790  O   CYS A 118      27.904   6.001  65.268  1.00 10.72           O  
ANISOU  790  O   CYS A 118     1166   1570   1338    127    324   -222       O  
ATOM    791  CB  CYS A 118      25.936   6.070  67.970  1.00 12.39           C  
ANISOU  791  CB  CYS A 118     1437   1760   1511     92    306   -224       C  
ATOM    792  SG  CYS A 118      25.514   4.983  69.327  1.00 16.55           S  
ANISOU  792  SG  CYS A 118     2050   2263   1978    124    321   -203       S  
ATOM    793  N   HIS A 119      27.396   7.997  66.167  1.00 10.73           N  
ANISOU  793  N   HIS A 119     1079   1603   1393     71    288   -242       N  
ATOM    794  CA  HIS A 119      27.429   8.694  64.877  1.00  7.71           C  
ANISOU  794  CA  HIS A 119      662   1222   1045     37    304   -232       C  
ATOM    795  C   HIS A 119      28.816   8.648  64.246  1.00 10.70           C  
ANISOU  795  C   HIS A 119     1000   1628   1436     70    316   -229       C  
ATOM    796  O   HIS A 119      28.948   8.499  63.029  1.00 11.43           O  
ANISOU  796  O   HIS A 119     1099   1720   1523     65    345   -212       O  
ATOM    797  CB  HIS A 119      26.923  10.124  65.053  1.00 11.62           C  
ANISOU  797  CB  HIS A 119     1107   1719   1590     -8    288   -240       C  
ATOM    798  CG  HIS A 119      25.469  10.184  65.402  1.00 11.94           C  
ANISOU  798  CG  HIS A 119     1179   1739   1619    -41    282   -245       C  
ATOM    799  ND1 HIS A 119      24.829  11.345  65.791  1.00 13.42           N  
ANISOU  799  ND1 HIS A 119     1331   1924   1844    -70    264   -260       N  
ATOM    800  CD2 HIS A 119      24.524   9.216  65.409  1.00 10.75           C  
ANISOU  800  CD2 HIS A 119     1088   1568   1429    -49    295   -243       C  
ATOM    801  CE1 HIS A 119      23.554  11.084  66.021  1.00 15.35           C  
ANISOU  801  CE1 HIS A 119     1606   2157   2069    -91    266   -266       C  
ATOM    802  NE2 HIS A 119      23.342   9.799  65.797  1.00 11.19           N  
ANISOU  802  NE2 HIS A 119     1136   1620   1498    -84    286   -256       N  
ATOM    803  N   SER A 120      29.848   8.746  65.077  1.00  9.69           N  
ANISOU  803  N   SER A 120      827   1533   1320    107    296   -249       N  
ATOM    804  CA  SER A 120      31.215   8.661  64.586  1.00 10.97           C  
ANISOU  804  CA  SER A 120      938   1733   1498    142    308   -254       C  
ATOM    805  C   SER A 120      31.566   7.265  64.096  1.00 14.91           C  
ANISOU  805  C   SER A 120     1493   2226   1947    199    328   -244       C  
ATOM    806  O   SER A 120      32.552   7.092  63.377  1.00 12.05           O  
ANISOU  806  O   SER A 120     1095   1893   1591    228    351   -246       O  
ATOM    807  CB  SER A 120      32.211   9.085  65.669  1.00 15.18           C  
ANISOU  807  CB  SER A 120     1399   2312   2058    172    271   -291       C  
ATOM    808  OG  SER A 120      32.117  10.477  65.897  1.00 18.18           O  
ANISOU  808  OG  SER A 120     1716   2693   2500    115    258   -308       O  
ATOM    809  N   HIS A 121      30.771   6.277  64.503  1.00 11.55           N  
ANISOU  809  N   HIS A 121     1155   1760   1475    216    325   -236       N  
ATOM    810  CA  HIS A 121      30.934   4.905  64.012  1.00 10.87           C  
ANISOU  810  CA  HIS A 121     1137   1646   1346    265    347   -230       C  
ATOM    811  C   HIS A 121      29.801   4.488  63.071  1.00 12.00           C  
ANISOU  811  C   HIS A 121     1345   1742   1473    219    373   -221       C  
ATOM    812  O   HIS A 121      29.469   3.312  62.975  1.00 12.88           O  
ANISOU  812  O   HIS A 121     1534   1807   1552    240    386   -222       O  
ATOM    813  CB  HIS A 121      31.076   3.925  65.179  1.00 13.19           C  
ANISOU  813  CB  HIS A 121     1488   1921   1602    329    328   -227       C  
ATOM    814  CG  HIS A 121      32.317   4.152  65.984  1.00 16.08           C  
ANISOU  814  CG  HIS A 121     1790   2346   1972    394    294   -244       C  
ATOM    815  ND1 HIS A 121      32.456   5.223  66.841  1.00 19.92           N  
ANISOU  815  ND1 HIS A 121     2208   2876   2485    374    259   -263       N  
ATOM    816  CD2 HIS A 121      33.491   3.481  66.022  1.00 21.96           C  
ANISOU  816  CD2 HIS A 121     2522   3120   2703    482    287   -254       C  
ATOM    817  CE1 HIS A 121      33.658   5.189  67.390  1.00 19.54           C  
ANISOU  817  CE1 HIS A 121     2103   2885   2436    444    229   -287       C  
ATOM    818  NE2 HIS A 121      34.308   4.145  66.908  1.00 21.69           N  
ANISOU  818  NE2 HIS A 121     2406   3152   2684    512    245   -280       N  
ATOM    819  N   ARG A 122      29.251   5.468  62.354  1.00  9.93           N  
ANISOU  819  N   ARG A 122     1048   1491   1233    159    379   -216       N  
ATOM    820  CA  ARG A 122      28.239   5.262  61.306  1.00 10.26           C  
ANISOU  820  CA  ARG A 122     1132   1509   1258    119    395   -215       C  
ATOM    821  C   ARG A 122      27.007   4.448  61.713  1.00 12.92           C  
ANISOU  821  C   ARG A 122     1541   1794   1575     93    392   -225       C  
ATOM    822  O   ARG A 122      26.452   3.697  60.911  1.00 11.90           O  
ANISOU  822  O   ARG A 122     1460   1638   1423     82    406   -240       O  
ATOM    823  CB  ARG A 122      28.844   4.802  59.945  1.00 11.07           C  
ANISOU  823  CB  ARG A 122     1243   1630   1336    148    425   -218       C  
ATOM    824  CG  ARG A 122      29.757   3.554  59.940  1.00 14.85           C  
ANISOU  824  CG  ARG A 122     1756   2098   1789    219    439   -234       C  
ATOM    825  CD  ARG A 122      28.955   2.255  59.946  1.00 18.79           C  
ANISOU  825  CD  ARG A 122     2349   2531   2260    222    443   -252       C  
ATOM    826  NE  ARG A 122      29.773   1.049  59.804  1.00 23.71           N  
ANISOU  826  NE  ARG A 122     3016   3132   2861    296    459   -268       N  
ATOM    827  CZ  ARG A 122      30.187   0.285  60.812  1.00 19.61           C  
ANISOU  827  CZ  ARG A 122     2534   2577   2338    349    451   -262       C  
ATOM    828  NH1 ARG A 122      29.886   0.598  62.077  1.00 19.76           N  
ANISOU  828  NH1 ARG A 122     2551   2588   2367    336    429   -240       N  
ATOM    829  NH2 ARG A 122      30.913  -0.794  60.554  1.00 17.20           N  
ANISOU  829  NH2 ARG A 122     2272   2248   2014    424    466   -277       N  
ATOM    830  N   VAL A 123      26.564   4.650  62.951  1.00 12.75           N  
ANISOU  830  N   VAL A 123     1520   1760   1563     79    375   -222       N  
ATOM    831  CA  VAL A 123      25.339   4.026  63.440  1.00 11.74           C  
ANISOU  831  CA  VAL A 123     1450   1588   1424     42    382   -227       C  
ATOM    832  C   VAL A 123      24.297   5.078  63.820  1.00 12.78           C  
ANISOU  832  C   VAL A 123     1541   1735   1579    -14    366   -231       C  
ATOM    833  O   VAL A 123      24.594   6.002  64.575  1.00 11.85           O  
ANISOU  833  O   VAL A 123     1377   1646   1480     -9    347   -227       O  
ATOM    834  CB  VAL A 123      25.621   3.124  64.663  1.00 10.40           C  
ANISOU  834  CB  VAL A 123     1333   1386   1232     83    388   -214       C  
ATOM    835  CG1 VAL A 123      24.313   2.577  65.242  1.00 11.34           C  
ANISOU  835  CG1 VAL A 123     1506   1457   1344     33    407   -214       C  
ATOM    836  CG2 VAL A 123      26.555   1.966  64.273  1.00 11.88           C  
ANISOU  836  CG2 VAL A 123     1570   1546   1397    148    403   -212       C  
ATOM    837  N   LEU A 124      23.086   4.935  63.282  1.00 10.71           N  
ANISOU  837  N   LEU A 124     1295   1456   1318    -65    372   -248       N  
ATOM    838  CA  LEU A 124      21.920   5.702  63.729  1.00 12.98           C  
ANISOU  838  CA  LEU A 124     1551   1755   1625   -113    361   -258       C  
ATOM    839  C   LEU A 124      21.152   4.842  64.714  1.00 10.98           C  
ANISOU  839  C   LEU A 124     1345   1466   1361   -137    383   -263       C  
ATOM    840  O   LEU A 124      20.912   3.680  64.442  1.00 12.78           O  
ANISOU  840  O   LEU A 124     1630   1650   1577   -148    408   -270       O  
ATOM    841  CB  LEU A 124      20.982   6.013  62.552  1.00 13.04           C  
ANISOU  841  CB  LEU A 124     1540   1775   1638   -150    351   -278       C  
ATOM    842  CG  LEU A 124      21.524   6.809  61.367  1.00 16.66           C  
ANISOU  842  CG  LEU A 124     1966   2267   2097   -130    338   -264       C  
ATOM    843  CD1 LEU A 124      20.439   6.968  60.275  1.00 19.96           C  
ANISOU  843  CD1 LEU A 124     2377   2702   2504   -157    323   -286       C  
ATOM    844  CD2 LEU A 124      22.068   8.171  61.817  1.00 15.76           C  
ANISOU  844  CD2 LEU A 124     1797   2176   2016   -119    324   -241       C  
ATOM    845  N   HIS A 125      20.751   5.403  65.854  1.00 10.57           N  
ANISOU  845  N   HIS A 125     1271   1429   1314   -147    380   -260       N  
ATOM    846  CA  HIS A 125      20.019   4.619  66.843  1.00 11.93           C  
ANISOU  846  CA  HIS A 125     1491   1572   1471   -171    413   -256       C  
ATOM    847  C   HIS A 125      18.542   4.488  66.440  1.00 12.30           C  
ANISOU  847  C   HIS A 125     1525   1610   1538   -243    429   -286       C  
ATOM    848  O   HIS A 125      17.983   3.384  66.414  1.00 12.63           O  
ANISOU  848  O   HIS A 125     1617   1606   1578   -278    465   -293       O  
ATOM    849  CB  HIS A 125      20.170   5.247  68.232  1.00  9.57           C  
ANISOU  849  CB  HIS A 125     1174   1305   1158   -148    406   -245       C  
ATOM    850  CG  HIS A 125      19.533   4.449  69.323  1.00 13.66           C  
ANISOU  850  CG  HIS A 125     1746   1798   1646   -163    449   -229       C  
ATOM    851  ND1 HIS A 125      18.168   4.415  69.517  1.00 13.08           N  
ANISOU  851  ND1 HIS A 125     1662   1721   1586   -228    479   -247       N  
ATOM    852  CD2 HIS A 125      20.067   3.638  70.271  1.00 16.69           C  
ANISOU  852  CD2 HIS A 125     2197   2159   1986   -119    471   -193       C  
ATOM    853  CE1 HIS A 125      17.888   3.617  70.530  1.00 14.65           C  
ANISOU  853  CE1 HIS A 125     1920   1893   1752   -232    526   -219       C  
ATOM    854  NE2 HIS A 125      19.024   3.136  71.010  1.00 15.95           N  
ANISOU  854  NE2 HIS A 125     2139   2045   1878   -163    521   -183       N  
ATOM    855  N   ARG A 126      17.928   5.628  66.138  1.00 11.99           N  
ANISOU  855  N   ARG A 126     1418   1616   1524   -262    400   -308       N  
ATOM    856  CA  ARG A 126      16.556   5.702  65.609  1.00 12.83           C  
ANISOU  856  CA  ARG A 126     1490   1733   1651   -319    401   -346       C  
ATOM    857  C   ARG A 126      15.447   5.270  66.563  1.00 12.83           C  
ANISOU  857  C   ARG A 126     1493   1725   1656   -370    441   -361       C  
ATOM    858  O   ARG A 126      14.314   5.074  66.130  1.00 12.49           O  
ANISOU  858  O   ARG A 126     1422   1688   1635   -424    448   -400       O  
ATOM    859  CB  ARG A 126      16.425   4.941  64.280  1.00 11.22           C  
ANISOU  859  CB  ARG A 126     1307   1509   1446   -336    398   -369       C  
ATOM    860  CG  ARG A 126      17.475   5.347  63.257  1.00 13.48           C  
ANISOU  860  CG  ARG A 126     1591   1811   1720   -286    368   -353       C  
ATOM    861  CD  ARG A 126      17.128   4.796  61.875  1.00 12.87           C  
ANISOU  861  CD  ARG A 126     1524   1734   1633   -301    358   -387       C  
ATOM    862  NE  ARG A 126      17.030   3.341  61.887  1.00 13.84           N  
ANISOU  862  NE  ARG A 126     1708   1800   1751   -326    392   -408       N  
ATOM    863  CZ  ARG A 126      16.716   2.609  60.822  1.00 12.46           C  
ANISOU  863  CZ  ARG A 126     1552   1613   1569   -344    388   -452       C  
ATOM    864  NH1 ARG A 126      16.471   3.206  59.665  1.00 11.31           N  
ANISOU  864  NH1 ARG A 126     1368   1522   1409   -333    349   -476       N  
ATOM    865  NH2 ARG A 126      16.640   1.285  60.914  1.00 12.98           N  
ANISOU  865  NH2 ARG A 126     1679   1612   1642   -371    422   -474       N  
ATOM    866  N   ASP A 127      15.753   5.105  67.846  1.00 12.66           N  
ANISOU  866  N   ASP A 127     1503   1695   1612   -353    469   -332       N  
ATOM    867  CA  ASP A 127      14.677   4.927  68.824  1.00 15.23           C  
ANISOU  867  CA  ASP A 127     1822   2028   1938   -399    514   -341       C  
ATOM    868  C   ASP A 127      15.068   5.445  70.208  1.00 15.45           C  
ANISOU  868  C   ASP A 127     1855   2084   1932   -357    520   -316       C  
ATOM    869  O   ASP A 127      14.905   4.758  71.209  1.00 14.11           O  
ANISOU  869  O   ASP A 127     1734   1897   1729   -364    571   -290       O  
ATOM    870  CB  ASP A 127      14.213   3.469  68.889  1.00 15.66           C  
ANISOU  870  CB  ASP A 127     1941   2019   1992   -452    575   -334       C  
ATOM    871  CG  ASP A 127      12.804   3.326  69.460  1.00 22.28           C  
ANISOU  871  CG  ASP A 127     2746   2868   2849   -525    625   -359       C  
ATOM    872  OD1 ASP A 127      12.028   4.302  69.420  1.00 20.73           O  
ANISOU  872  OD1 ASP A 127     2479   2727   2672   -522    580   -392       O  
ATOM    873  OD2 ASP A 127      12.475   2.232  69.938  1.00 24.69           O  
ANISOU  873  OD2 ASP A 127     3111   3118   3151   -565    687   -339       O  
ATOM    874  N   LEU A 128      15.600   6.658  70.249  1.00 11.98           N  
ANISOU  874  N   LEU A 128     1367   1688   1499   -313    469   -326       N  
ATOM    875  CA  LEU A 128      15.958   7.284  71.511  1.00 14.48           C  
ANISOU  875  CA  LEU A 128     1676   2040   1785   -271    464   -321       C  
ATOM    876  C   LEU A 128      14.684   7.777  72.181  1.00 19.88           C  
ANISOU  876  C   LEU A 128     2315   2763   2476   -306    489   -353       C  
ATOM    877  O   LEU A 128      13.977   8.633  71.650  1.00 25.88           O  
ANISOU  877  O   LEU A 128     3016   3540   3279   -319    450   -385       O  
ATOM    878  CB  LEU A 128      16.930   8.438  71.280  1.00  9.81           C  
ANISOU  878  CB  LEU A 128     1041   1473   1213   -222    403   -333       C  
ATOM    879  CG  LEU A 128      18.290   7.994  70.722  1.00 12.54           C  
ANISOU  879  CG  LEU A 128     1420   1793   1551   -183    383   -304       C  
ATOM    880  CD1 LEU A 128      19.152   9.193  70.394  1.00 16.55           C  
ANISOU  880  CD1 LEU A 128     1873   2323   2092   -152    333   -319       C  
ATOM    881  CD2 LEU A 128      19.002   7.073  71.716  1.00 16.41           C  
ANISOU  881  CD2 LEU A 128     1977   2275   1983   -140    404   -271       C  
ATOM    882  N   LYS A 129      14.388   7.187  73.329  1.00 16.66           N  
ANISOU  882  N   LYS A 129     1949   2360   2022   -311    542   -333       N  
ATOM    883  CA  LYS A 129      13.246   7.558  74.157  1.00 16.81           C  
ANISOU  883  CA  LYS A 129     1937   2410   2038   -329    557   -350       C  
ATOM    884  C   LYS A 129      13.620   7.099  75.555  1.00 18.27           C  
ANISOU  884  C   LYS A 129     2182   2614   2147   -296    605   -316       C  
ATOM    885  O   LYS A 129      14.468   6.222  75.696  1.00 17.10           O  
ANISOU  885  O   LYS A 129     2107   2434   1956   -273    631   -273       O  
ATOM    886  CB  LYS A 129      11.973   6.868  73.666  1.00 18.43           C  
ANISOU  886  CB  LYS A 129     2137   2588   2279   -398    585   -357       C  
ATOM    887  CG  LYS A 129      12.029   5.352  73.660  1.00 19.68           C  
ANISOU  887  CG  LYS A 129     2372   2685   2421   -437    651   -316       C  
ATOM    888  CD  LYS A 129      10.719   4.781  73.149  1.00 25.26           C  
ANISOU  888  CD  LYS A 129     3057   3368   3174   -509    671   -343       C  
ATOM    889  CE  LYS A 129      10.761   3.272  73.060  1.00 24.69           C  
ANISOU  889  CE  LYS A 129     3063   3219   3101   -555    736   -309       C  
ATOM    890  NZ  LYS A 129       9.478   2.758  72.494  1.00 30.07           N  
ANISOU  890  NZ  LYS A 129     3712   3881   3833   -627    749   -352       N  
ATOM    891  N   PRO A 130      13.007   7.690  76.595  1.00 17.58           N  
ANISOU  891  N   PRO A 130     2069   2576   2036   -282    612   -332       N  
ATOM    892  CA  PRO A 130      13.409   7.413  77.981  1.00 16.08           C  
ANISOU  892  CA  PRO A 130     1934   2419   1756   -234    649   -302       C  
ATOM    893  C   PRO A 130      13.419   5.932  78.340  1.00 18.62           C  
ANISOU  893  C   PRO A 130     2352   2694   2030   -251    726   -231       C  
ATOM    894  O   PRO A 130      14.275   5.512  79.111  1.00 18.89           O  
ANISOU  894  O   PRO A 130     2458   2737   1982   -193    744   -192       O  
ATOM    895  CB  PRO A 130      12.350   8.151  78.805  1.00 18.60           C  
ANISOU  895  CB  PRO A 130     2204   2789   2073   -236    655   -333       C  
ATOM    896  CG  PRO A 130      11.939   9.283  77.918  1.00 23.52           C  
ANISOU  896  CG  PRO A 130     2741   3417   2779   -252    590   -392       C  
ATOM    897  CD  PRO A 130      11.955   8.722  76.527  1.00 17.41           C  
ANISOU  897  CD  PRO A 130     1968   2586   2061   -298    580   -381       C  
ATOM    898  N   GLN A 131      12.503   5.152  77.775  1.00 16.52           N  
ANISOU  898  N   GLN A 131     2090   2373   1814   -326    766   -216       N  
ATOM    899  CA  GLN A 131      12.466   3.718  78.044  1.00 20.87           C  
ANISOU  899  CA  GLN A 131     2736   2858   2337   -351    839   -149       C  
ATOM    900  C   GLN A 131      13.725   2.995  77.574  1.00 16.49           C  
ANISOU  900  C   GLN A 131     2261   2244   1759   -315    837   -111       C  
ATOM    901  O   GLN A 131      14.031   1.902  78.059  1.00 20.90           O  
ANISOU  901  O   GLN A 131     2920   2748   2272   -299    890    -43       O  
ATOM    902  CB  GLN A 131      11.258   3.067  77.367  1.00 28.19           C  
ANISOU  902  CB  GLN A 131     3640   3732   3340   -445    872   -163       C  
ATOM    903  CG  GLN A 131       9.920   3.619  77.803  1.00 33.88           C  
ANISOU  903  CG  GLN A 131     4285   4504   4084   -481    882   -199       C  
ATOM    904  CD  GLN A 131       9.403   4.728  76.898  1.00 38.38           C  
ANISOU  904  CD  GLN A 131     4752   5112   4719   -493    809   -276       C  
ATOM    905  OE1 GLN A 131      10.064   5.751  76.690  1.00 24.03           O  
ANISOU  905  OE1 GLN A 131     2900   3331   2899   -441    746   -303       O  
ATOM    906  NE2 GLN A 131       8.207   4.526  76.352  1.00 48.86           N  
ANISOU  906  NE2 GLN A 131     6030   6428   6104   -557    816   -313       N  
ATOM    907  N   ASN A 132      14.441   3.594  76.626  1.00 16.35           N  
ANISOU  907  N   ASN A 132     2201   2234   1777   -294    770   -151       N  
ATOM    908  CA  ASN A 132      15.641   2.973  76.057  1.00 18.01           C  
ANISOU  908  CA  ASN A 132     2470   2390   1984   -244    734   -119       C  
ATOM    909  C   ASN A 132      16.956   3.534  76.597  1.00 16.28           C  
ANISOU  909  C   ASN A 132     2253   2219   1713   -140    667   -112       C  
ATOM    910  O   ASN A 132      18.021   3.282  76.035  1.00 17.96           O  
ANISOU  910  O   ASN A 132     2485   2406   1932    -93    624   -102       O  
ATOM    911  CB  ASN A 132      15.633   3.062  74.527  1.00 17.14           C  
ANISOU  911  CB  ASN A 132     2313   2248   1952   -284    695   -158       C  
ATOM    912  CG  ASN A 132      14.628   2.121  73.897  1.00 21.76           C  
ANISOU  912  CG  ASN A 132     2917   2768   2584   -376    755   -163       C  
ATOM    913  OD1 ASN A 132      14.121   1.208  74.552  1.00 20.30           O  
ANISOU  913  OD1 ASN A 132     2796   2539   2379   -411    834   -124       O  
ATOM    914  ND2 ASN A 132      14.343   2.330  72.616  1.00 19.33           N  
ANISOU  914  ND2 ASN A 132     2553   2453   2337   -417    720   -212       N  
ATOM    915  N   LEU A 133      16.865   4.301  77.676  1.00 16.36           N  
ANISOU  915  N   LEU A 133     2238   2305   1674   -105    658   -128       N  
ATOM    916  CA  LEU A 133      18.032   4.873  78.329  1.00 14.95           C  
ANISOU  916  CA  LEU A 133     2053   2183   1444     -9    592   -137       C  
ATOM    917  C   LEU A 133      18.106   4.315  79.743  1.00 20.12           C  
ANISOU  917  C   LEU A 133     2789   2866   1992     49    633    -86       C  
ATOM    918  O   LEU A 133      17.196   4.521  80.541  1.00 19.03           O  
ANISOU  918  O   LEU A 133     2648   2765   1817     25    683    -89       O  
ATOM    919  CB  LEU A 133      17.924   6.400  78.364  1.00 14.48           C  
ANISOU  919  CB  LEU A 133     1889   2192   1419    -10    534   -214       C  
ATOM    920  CG  LEU A 133      17.648   7.051  77.002  1.00 15.69           C  
ANISOU  920  CG  LEU A 133     1966   2320   1673    -68    502   -256       C  
ATOM    921  CD1 LEU A 133      17.495   8.566  77.144  1.00 15.59           C  
ANISOU  921  CD1 LEU A 133     1863   2363   1696    -63    452   -325       C  
ATOM    922  CD2 LEU A 133      18.748   6.704  75.993  1.00 13.17           C  
ANISOU  922  CD2 LEU A 133     1659   1960   1386    -45    463   -240       C  
ATOM    923  N   LEU A 134      19.187   3.603  80.049  1.00 17.93           N  
ANISOU  923  N   LEU A 134     2583   2573   1657    132    614    -38       N  
ATOM    924  CA  LEU A 134      19.290   2.887  81.314  1.00 17.05           C  
ANISOU  924  CA  LEU A 134     2570   2477   1432    198    657     28       C  
ATOM    925  C   LEU A 134      20.220   3.621  82.275  1.00 17.80           C  
ANISOU  925  C   LEU A 134     2641   2675   1449    305    580     -4       C  
ATOM    926  O   LEU A 134      21.242   4.167  81.859  1.00 19.90           O  
ANISOU  926  O   LEU A 134     2848   2968   1747    348    494    -51       O  
ATOM    927  CB  LEU A 134      19.788   1.461  81.073  1.00 20.19           C  
ANISOU  927  CB  LEU A 134     3079   2781   1811    230    692    111       C  
ATOM    928  CG  LEU A 134      18.925   0.644  80.108  1.00 25.98           C  
ANISOU  928  CG  LEU A 134     3841   3406   2627    123    765    133       C  
ATOM    929  CD1 LEU A 134      19.500  -0.750  79.911  1.00 30.14           C  
ANISOU  929  CD1 LEU A 134     4484   3830   3137    163    797    209       C  
ATOM    930  CD2 LEU A 134      17.496   0.574  80.624  1.00 29.14           C  
ANISOU  930  CD2 LEU A 134     4246   3804   3021     35    859    145       C  
ATOM    931  N   ILE A 135      19.859   3.627  83.553  1.00 16.82           N  
ANISOU  931  N   ILE A 135     2559   2610   1221    346    614     17       N  
ATOM    932  CA  ILE A 135      20.635   4.327  84.571  1.00 18.35           C  
ANISOU  932  CA  ILE A 135     2730   2913   1328    449    541    -25       C  
ATOM    933  C   ILE A 135      21.056   3.389  85.694  1.00 22.87           C  
ANISOU  933  C   ILE A 135     3410   3494   1785    539    554     58       C  
ATOM    934  O   ILE A 135      20.418   2.362  85.927  1.00 22.92           O  
ANISOU  934  O   ILE A 135     3507   3431   1771    508    639    145       O  
ATOM    935  CB  ILE A 135      19.845   5.506  85.191  1.00 20.32           C  
ANISOU  935  CB  ILE A 135     2901   3240   1578    413    535   -101       C  
ATOM    936  CG1 ILE A 135      18.558   5.019  85.862  1.00 23.83           C  
ANISOU  936  CG1 ILE A 135     3397   3667   1990    353    636    -50       C  
ATOM    937  CG2 ILE A 135      19.532   6.556  84.148  1.00 18.70           C  
ANISOU  937  CG2 ILE A 135     2581   3025   1497    336    502   -186       C  
ATOM    938  CD1 ILE A 135      17.844   6.112  86.643  1.00 21.90           C  
ANISOU  938  CD1 ILE A 135     3087   3497   1737    334    629   -123       C  
ATOM    939  N   ASN A 136      22.138   3.740  86.386  1.00 23.61           N  
ANISOU  939  N   ASN A 136     3487   3666   1816    648    462     26       N  
ATOM    940  CA  ASN A 136      22.554   2.995  87.571  1.00 23.69           C  
ANISOU  940  CA  ASN A 136     3586   3698   1717    746    458     96       C  
ATOM    941  C   ASN A 136      22.661   3.879  88.817  1.00 25.18           C  
ANISOU  941  C   ASN A 136     3729   3999   1838    799    400     34       C  
ATOM    942  O   ASN A 136      22.413   5.089  88.760  1.00 24.00           O  
ANISOU  942  O   ASN A 136     3480   3904   1736    756    363    -64       O  
ATOM    943  CB  ASN A 136      23.850   2.199  87.315  1.00 27.17           C  
ANISOU  943  CB  ASN A 136     4077   4117   2131    854    407    138       C  
ATOM    944  CG  ASN A 136      25.065   3.088  87.070  1.00 27.66           C  
ANISOU  944  CG  ASN A 136     4034   4264   2210    920    286     39       C  
ATOM    945  OD1 ASN A 136      25.064   4.278  87.382  1.00 25.34           O  
ANISOU  945  OD1 ASN A 136     3641   4051   1935    904    230    -58       O  
ATOM    946  ND2 ASN A 136      26.121   2.497  86.515  1.00 29.60           N  
ANISOU  946  ND2 ASN A 136     4299   4489   2459    993    246     59       N  
ATOM    947  N   THR A 137      23.031   3.273  89.940  1.00 25.41           N  
ANISOU  947  N   THR A 137     3833   4059   1762    895    394     92       N  
ATOM    948  CA  THR A 137      23.084   3.990  91.208  1.00 29.93           C  
ANISOU  948  CA  THR A 137     4375   4737   2260    951    347     41       C  
ATOM    949  C   THR A 137      24.291   4.919  91.303  1.00 29.36           C  
ANISOU  949  C   THR A 137     4203   4756   2197   1029    215    -66       C  
ATOM    950  O   THR A 137      24.357   5.768  92.187  1.00 28.99           O  
ANISOU  950  O   THR A 137     4102   4797   2114   1062    164   -138       O  
ATOM    951  CB  THR A 137      23.107   3.012  92.395  1.00 34.01           C  
ANISOU  951  CB  THR A 137     5006   5261   2656   1035    384    139       C  
ATOM    952  OG1 THR A 137      24.227   2.129  92.259  1.00 32.63           O  
ANISOU  952  OG1 THR A 137     4886   5059   2452   1142    343    194       O  
ATOM    953  CG2 THR A 137      21.826   2.197  92.430  1.00 35.48           C  
ANISOU  953  CG2 THR A 137     5277   5364   2841    942    520    234       C  
ATOM    954  N   GLU A 138      25.240   4.763  90.387  1.00 27.61           N  
ANISOU  954  N   GLU A 138     3951   4513   2028   1057    162    -80       N  
ATOM    955  CA  GLU A 138      26.453   5.577  90.411  1.00 32.59           C  
ANISOU  955  CA  GLU A 138     4477   5228   2679   1124     40   -185       C  
ATOM    956  C   GLU A 138      26.331   6.889  89.629  1.00 29.90           C  
ANISOU  956  C   GLU A 138     4009   4899   2454   1031      3   -301       C  
ATOM    957  O   GLU A 138      27.230   7.727  89.671  1.00 32.74           O  
ANISOU  957  O   GLU A 138     4267   5325   2850   1064    -93   -402       O  
ATOM    958  CB  GLU A 138      27.645   4.766  89.907  1.00 35.44           C  
ANISOU  958  CB  GLU A 138     4860   5573   3034   1212     -4   -150       C  
ATOM    959  CG  GLU A 138      28.019   3.609  90.823  1.00 46.08           C  
ANISOU  959  CG  GLU A 138     6320   6920   4270   1332      8    -53       C  
ATOM    960  CD  GLU A 138      29.138   2.754  90.260  1.00 56.64           C  
ANISOU  960  CD  GLU A 138     7683   8230   5609   1422    -28    -17       C  
ATOM    961  OE1 GLU A 138      29.590   3.035  89.129  1.00 56.36           O  
ANISOU  961  OE1 GLU A 138     7579   8178   5657   1385    -58    -64       O  
ATOM    962  OE2 GLU A 138      29.566   1.803  90.950  1.00 63.13           O  
ANISOU  962  OE2 GLU A 138     8592   9046   6347   1533    -25     58       O  
ATOM    963  N   GLY A 139      25.220   7.065  88.921  1.00 22.27           N  
ANISOU  963  N   GLY A 139     3044   3864   1553    915     80   -289       N  
ATOM    964  CA  GLY A 139      24.993   8.291  88.175  1.00 22.20           C  
ANISOU  964  CA  GLY A 139     2923   3854   1658    828     54   -391       C  
ATOM    965  C   GLY A 139      25.242   8.161  86.682  1.00 23.32           C  
ANISOU  965  C   GLY A 139     3036   3931   1895    773     65   -390       C  
ATOM    966  O   GLY A 139      25.200   9.155  85.956  1.00 21.84           O  
ANISOU  966  O   GLY A 139     2754   3735   1811    706     39   -471       O  
ATOM    967  N   ALA A 140      25.488   6.938  86.218  1.00 19.06           N  
ANISOU  967  N   ALA A 140     2580   3337   1323    802    105   -298       N  
ATOM    968  CA  ALA A 140      25.697   6.696  84.799  1.00 17.98           C  
ANISOU  968  CA  ALA A 140     2420   3119   1292    744    120   -285       C  
ATOM    969  C   ALA A 140      24.353   6.579  84.094  1.00 18.69           C  
ANISOU  969  C   ALA A 140     2531   3121   1451    623    212   -247       C  
ATOM    970  O   ALA A 140      23.361   6.158  84.692  1.00 19.45           O  
ANISOU  970  O   ALA A 140     2697   3210   1483    607    287   -197       O  
ATOM    971  CB  ALA A 140      26.511   5.431  84.574  1.00 22.73           C  
ANISOU  971  CB  ALA A 140     3099   3681   1855    820    121   -204       C  
ATOM    972  N   ILE A 141      24.339   6.969  82.827  1.00 16.26           N  
ANISOU  972  N   ILE A 141     2157   2753   1270    542    206   -273       N  
ATOM    973  CA  ILE A 141      23.208   6.713  81.942  1.00 15.02           C  
ANISOU  973  CA  ILE A 141     2015   2509   1183    436    282   -238       C  
ATOM    974  C   ILE A 141      23.758   6.167  80.625  1.00 17.91           C  
ANISOU  974  C   ILE A 141     2380   2799   1626    412    279   -211       C  
ATOM    975  O   ILE A 141      24.820   6.599  80.167  1.00 18.54           O  
ANISOU  975  O   ILE A 141     2396   2899   1750    440    214   -251       O  
ATOM    976  CB  ILE A 141      22.338   7.973  81.732  1.00 16.20           C  
ANISOU  976  CB  ILE A 141     2077   2674   1405    356    280   -311       C  
ATOM    977  CG1 ILE A 141      21.078   7.634  80.920  1.00 15.36           C  
ANISOU  977  CG1 ILE A 141     1985   2493   1356    257    357   -276       C  
ATOM    978  CG2 ILE A 141      23.124   9.087  81.057  1.00 18.23           C  
ANISOU  978  CG2 ILE A 141     2229   2943   1754    345    204   -388       C  
ATOM    979  CD1 ILE A 141      20.004   8.728  80.992  1.00 15.34           C  
ANISOU  979  CD1 ILE A 141     1914   2516   1398    197    367   -338       C  
ATOM    980  N   LYS A 142      23.061   5.196  80.028  1.00 14.13           N  
ANISOU  980  N   LYS A 142     1969   2236   1165    360    352   -146       N  
ATOM    981  CA  LYS A 142      23.593   4.511  78.841  1.00 15.49           C  
ANISOU  981  CA  LYS A 142     2155   2336   1394    350    353   -120       C  
ATOM    982  C   LYS A 142      22.523   4.250  77.793  1.00 14.68           C  
ANISOU  982  C   LYS A 142     2057   2156   1364    244    411   -109       C  
ATOM    983  O   LYS A 142      21.381   3.955  78.131  1.00 17.00           O  
ANISOU  983  O   LYS A 142     2387   2428   1643    191    475    -86       O  
ATOM    984  CB  LYS A 142      24.245   3.181  79.234  1.00 17.97           C  
ANISOU  984  CB  LYS A 142     2575   2618   1635    436    370    -47       C  
ATOM    985  CG  LYS A 142      25.277   3.311  80.340  1.00 20.60           C  
ANISOU  985  CG  LYS A 142     2912   3037   1879    557    308    -55       C  
ATOM    986  CD  LYS A 142      26.135   2.069  80.485  1.00 22.77           C  
ANISOU  986  CD  LYS A 142     3278   3278   2095    658    308     11       C  
ATOM    987  CE  LYS A 142      26.973   2.169  81.756  1.00 21.44           C  
ANISOU  987  CE  LYS A 142     3121   3209   1818    786    247      7       C  
ATOM    988  NZ  LYS A 142      28.240   1.386  81.650  1.00 25.30           N  
ANISOU  988  NZ  LYS A 142     3640   3696   2278    902    204     33       N  
ATOM    989  N   LEU A 143      22.899   4.376  76.526  1.00 13.58           N  
ANISOU  989  N   LEU A 143     1874   1984   1300    214    389   -129       N  
ATOM    990  CA  LEU A 143      22.004   4.054  75.420  1.00 13.55           C  
ANISOU  990  CA  LEU A 143     1874   1914   1360    125    433   -125       C  
ATOM    991  C   LEU A 143      21.787   2.550  75.356  1.00 17.99           C  
ANISOU  991  C   LEU A 143     2544   2394   1896    125    494    -64       C  
ATOM    992  O   LEU A 143      22.739   1.774  75.463  1.00 17.91           O  
ANISOU  992  O   LEU A 143     2592   2362   1852    200    485    -29       O  
ATOM    993  CB  LEU A 143      22.595   4.513  74.086  1.00 13.59           C  
ANISOU  993  CB  LEU A 143     1816   1912   1436    110    394   -157       C  
ATOM    994  CG  LEU A 143      23.099   5.939  73.913  1.00 22.51           C  
ANISOU  994  CG  LEU A 143     2844   3101   2608    113    335   -210       C  
ATOM    995  CD1 LEU A 143      23.452   6.170  72.435  1.00 20.97           C  
ANISOU  995  CD1 LEU A 143     2608   2882   2479     84    322   -222       C  
ATOM    996  CD2 LEU A 143      22.075   6.930  74.382  1.00 28.01           C  
ANISOU  996  CD2 LEU A 143     3495   3829   3319     66    336   -245       C  
ATOM    997  N   ALA A 144      20.535   2.138  75.171  1.00 14.69           N  
ANISOU  997  N   ALA A 144     2151   1929   1501     41    557    -55       N  
ATOM    998  CA  ALA A 144      20.207   0.719  75.071  1.00 17.14           C  
ANISOU  998  CA  ALA A 144     2563   2145   1803     22    625     -3       C  
ATOM    999  C   ALA A 144      19.236   0.476  73.923  1.00 18.96           C  
ANISOU  999  C   ALA A 144     2771   2322   2109    -82    655    -34       C  
ATOM   1000  O   ALA A 144      18.754   1.425  73.299  1.00 17.19           O  
ANISOU 1000  O   ALA A 144     2458   2142   1933   -131    625    -88       O  
ATOM   1001  CB  ALA A 144      19.606   0.224  76.380  1.00 17.45           C  
ANISOU 1001  CB  ALA A 144     2676   2179   1777     25    690     50       C  
ATOM   1002  N   ASP A 145      18.966  -0.799  73.658  1.00 19.83           N  
ANISOU 1002  N   ASP A 145     2968   2337   2231   -110    713     -3       N  
ATOM   1003  CA  ASP A 145      17.972  -1.223  72.670  1.00 23.76           C  
ANISOU 1003  CA  ASP A 145     3453   2779   2797   -212    747    -39       C  
ATOM   1004  C   ASP A 145      18.295  -0.720  71.271  1.00 16.75           C  
ANISOU 1004  C   ASP A 145     2495   1912   1958   -219    686    -96       C  
ATOM   1005  O   ASP A 145      17.678   0.235  70.777  1.00 19.44           O  
ANISOU 1005  O   ASP A 145     2745   2309   2332   -266    658   -145       O  
ATOM   1006  CB  ASP A 145      16.565  -0.775  73.080  1.00 28.82           C  
ANISOU 1006  CB  ASP A 145     4042   3451   3457   -303    789    -62       C  
ATOM   1007  CG  ASP A 145      15.469  -1.566  72.378  1.00 43.71           C  
ANISOU 1007  CG  ASP A 145     5935   5266   5406   -411    845    -90       C  
ATOM   1008  OD1 ASP A 145      15.731  -2.125  71.290  1.00 44.03           O  
ANISOU 1008  OD1 ASP A 145     5992   5253   5485   -421    828   -116       O  
ATOM   1009  OD2 ASP A 145      14.343  -1.629  72.920  1.00 53.06           O  
ANISOU 1009  OD2 ASP A 145     7104   6453   6602   -485    906    -93       O  
ATOM   1010  N   PHE A 146      19.251  -1.388  70.632  1.00 16.22           N  
ANISOU 1010  N   PHE A 146     2474   1798   1890   -167    670    -88       N  
ATOM   1011  CA  PHE A 146      19.681  -1.041  69.289  1.00 18.21           C  
ANISOU 1011  CA  PHE A 146     2673   2069   2175   -163    621   -135       C  
ATOM   1012  C   PHE A 146      18.963  -1.853  68.215  1.00 17.43           C  
ANISOU 1012  C   PHE A 146     2597   1904   2123   -234    648   -174       C  
ATOM   1013  O   PHE A 146      19.409  -1.918  67.070  1.00 17.35           O  
ANISOU 1013  O   PHE A 146     2572   1894   2127   -219    618   -208       O  
ATOM   1014  CB  PHE A 146      21.203  -1.192  69.167  1.00 19.20           C  
ANISOU 1014  CB  PHE A 146     2820   2201   2272    -59    585   -114       C  
ATOM   1015  CG  PHE A 146      21.962  -0.055  69.790  1.00 18.30           C  
ANISOU 1015  CG  PHE A 146     2642   2179   2132      0    535   -108       C  
ATOM   1016  CD1 PHE A 146      22.025   0.075  71.169  1.00 15.48           C  
ANISOU 1016  CD1 PHE A 146     2307   1847   1729     36    541    -73       C  
ATOM   1017  CD2 PHE A 146      22.578   0.900  69.001  1.00 16.71           C  
ANISOU 1017  CD2 PHE A 146     2358   2037   1954     15    485   -140       C  
ATOM   1018  CE1 PHE A 146      22.701   1.132  71.755  1.00 14.19           C  
ANISOU 1018  CE1 PHE A 146     2078   1767   1544     87    490    -83       C  
ATOM   1019  CE2 PHE A 146      23.263   1.958  69.579  1.00 17.53           C  
ANISOU 1019  CE2 PHE A 146     2399   2216   2047     58    442   -144       C  
ATOM   1020  CZ  PHE A 146      23.327   2.071  70.960  1.00 15.24           C  
ANISOU 1020  CZ  PHE A 146     2126   1951   1714     93    440   -121       C  
ATOM   1021  N   GLY A 147      17.837  -2.456  68.580  1.00 21.49           N  
ANISOU 1021  N   GLY A 147     3140   2366   2658   -314    706   -176       N  
ATOM   1022  CA  GLY A 147      17.087  -3.276  67.643  1.00 25.32           C  
ANISOU 1022  CA  GLY A 147     3642   2785   3194   -392    732   -226       C  
ATOM   1023  C   GLY A 147      16.606  -2.513  66.418  1.00 24.64           C  
ANISOU 1023  C   GLY A 147     3461   2765   3137   -430    680   -299       C  
ATOM   1024  O   GLY A 147      16.406  -3.096  65.356  1.00 24.98           O  
ANISOU 1024  O   GLY A 147     3513   2773   3207   -460    675   -351       O  
ATOM   1025  N   LEU A 148      16.433  -1.202  66.560  1.00 17.81           N  
ANISOU 1025  N   LEU A 148     2509   1996   2263   -422    640   -304       N  
ATOM   1026  CA  LEU A 148      15.946  -0.373  65.458  1.00 15.34           C  
ANISOU 1026  CA  LEU A 148     2110   1749   1970   -447    589   -362       C  
ATOM   1027  C   LEU A 148      17.049   0.455  64.810  1.00 17.82           C  
ANISOU 1027  C   LEU A 148     2394   2117   2261   -370    532   -351       C  
ATOM   1028  O   LEU A 148      16.790   1.285  63.947  1.00 14.55           O  
ANISOU 1028  O   LEU A 148     1914   1760   1852   -374    490   -382       O  
ATOM   1029  CB  LEU A 148      14.798   0.520  65.937  1.00 21.43           C  
ANISOU 1029  CB  LEU A 148     2802   2581   2759   -499    588   -381       C  
ATOM   1030  CG  LEU A 148      13.530  -0.282  66.239  1.00 26.21           C  
ANISOU 1030  CG  LEU A 148     3413   3144   3401   -594    646   -411       C  
ATOM   1031  CD1 LEU A 148      12.508   0.548  67.019  1.00 31.58           C  
ANISOU 1031  CD1 LEU A 148     4019   3887   4092   -633    659   -421       C  
ATOM   1032  CD2 LEU A 148      12.916  -0.823  64.944  1.00 28.04           C  
ANISOU 1032  CD2 LEU A 148     3625   3360   3669   -649    630   -486       C  
ATOM   1033  N   ALA A 149      18.289   0.203  65.217  1.00 14.54           N  
ANISOU 1033  N   ALA A 149     2027   1683   1817   -297    534   -306       N  
ATOM   1034  CA  ALA A 149      19.432   0.929  64.689  1.00 12.18           C  
ANISOU 1034  CA  ALA A 149     1694   1432   1500   -229    491   -295       C  
ATOM   1035  C   ALA A 149      19.778   0.494  63.266  1.00 16.88           C  
ANISOU 1035  C   ALA A 149     2300   2019   2094   -217    478   -328       C  
ATOM   1036  O   ALA A 149      19.317  -0.542  62.784  1.00 17.37           O  
ANISOU 1036  O   ALA A 149     2410   2025   2167   -250    501   -361       O  
ATOM   1037  CB  ALA A 149      20.646   0.732  65.598  1.00 15.44           C  
ANISOU 1037  CB  ALA A 149     2146   1837   1885   -152    494   -247       C  
ATOM   1038  N   ARG A 150      20.600   1.290  62.596  1.00 11.92           N  
ANISOU 1038  N   ARG A 150     1630   1446   1455   -171    446   -322       N  
ATOM   1039  CA  ARG A 150      21.123   0.866  61.305  1.00 17.46           C  
ANISOU 1039  CA  ARG A 150     2345   2148   2140   -144    441   -346       C  
ATOM   1040  C   ARG A 150      22.479   1.498  61.024  1.00 15.96           C  
ANISOU 1040  C   ARG A 150     2125   2005   1935    -75    427   -317       C  
ATOM   1041  O   ARG A 150      22.765   2.621  61.464  1.00 14.58           O  
ANISOU 1041  O   ARG A 150     1894   1876   1769    -67    409   -291       O  
ATOM   1042  CB  ARG A 150      20.096   1.126  60.191  1.00 23.68           C  
ANISOU 1042  CB  ARG A 150     3101   2966   2931   -193    421   -395       C  
ATOM   1043  CG  ARG A 150      20.361   2.297  59.285  1.00 30.08           C  
ANISOU 1043  CG  ARG A 150     3853   3851   3725   -169    389   -386       C  
ATOM   1044  CD  ARG A 150      20.536   1.838  57.829  1.00 31.11           C  
ANISOU 1044  CD  ARG A 150     4001   3998   3821   -150    383   -423       C  
ATOM   1045  NE  ARG A 150      19.318   1.320  57.200  1.00 32.06           N  
ANISOU 1045  NE  ARG A 150     4127   4113   3941   -201    370   -488       N  
ATOM   1046  CZ  ARG A 150      19.319   0.556  56.108  1.00 24.42           C  
ANISOU 1046  CZ  ARG A 150     3190   3144   2945   -191    366   -541       C  
ATOM   1047  NH1 ARG A 150      20.473   0.213  55.547  1.00 17.43           N  
ANISOU 1047  NH1 ARG A 150     2337   2260   2027   -130    381   -532       N  
ATOM   1048  NH2 ARG A 150      18.185   0.121  55.578  1.00 27.01           N  
ANISOU 1048  NH2 ARG A 150     3514   3473   3277   -242    347   -612       N  
ATOM   1049  N   ALA A 151      23.331   0.766  60.314  1.00 11.54           N  
ANISOU 1049  N   ALA A 151     1599   1431   1355    -27    438   -327       N  
ATOM   1050  CA  ALA A 151      24.601   1.333  59.891  1.00 12.79           C  
ANISOU 1050  CA  ALA A 151     1718   1642   1501     32    433   -306       C  
ATOM   1051  C   ALA A 151      24.338   2.192  58.658  1.00 20.58           C  
ANISOU 1051  C   ALA A 151     2657   2686   2475     13    420   -316       C  
ATOM   1052  O   ALA A 151      23.743   1.719  57.688  1.00 22.29           O  
ANISOU 1052  O   ALA A 151     2899   2899   2671     -4    420   -354       O  
ATOM   1053  CB  ALA A 151      25.613   0.216  59.565  1.00 15.05           C  
ANISOU 1053  CB  ALA A 151     2053   1898   1767     99    453   -317       C  
ATOM   1054  N   PHE A 152      24.772   3.449  58.685  1.00 15.64           N  
ANISOU 1054  N   PHE A 152     1968   2112   1862     18    410   -283       N  
ATOM   1055  CA  PHE A 152      24.541   4.322  57.537  1.00 12.44           C  
ANISOU 1055  CA  PHE A 152     1529   1756   1442      7    404   -277       C  
ATOM   1056  C   PHE A 152      25.784   4.527  56.677  1.00 18.63           C  
ANISOU 1056  C   PHE A 152     2293   2582   2205     55    428   -258       C  
ATOM   1057  O   PHE A 152      26.885   4.124  57.042  1.00 15.10           O  
ANISOU 1057  O   PHE A 152     1841   2132   1762     97    445   -253       O  
ATOM   1058  CB  PHE A 152      23.899   5.659  57.940  1.00 14.65           C  
ANISOU 1058  CB  PHE A 152     1757   2055   1752    -30    381   -253       C  
ATOM   1059  CG  PHE A 152      24.760   6.543  58.809  1.00 15.17           C  
ANISOU 1059  CG  PHE A 152     1775   2130   1857    -19    382   -220       C  
ATOM   1060  CD1 PHE A 152      24.725   6.427  60.194  1.00 11.40           C  
ANISOU 1060  CD1 PHE A 152     1298   1630   1405    -24    372   -224       C  
ATOM   1061  CD2 PHE A 152      25.554   7.534  58.244  1.00 12.57           C  
ANISOU 1061  CD2 PHE A 152     1400   1835   1540     -7    394   -188       C  
ATOM   1062  CE1 PHE A 152      25.480   7.278  61.005  1.00 12.76           C  
ANISOU 1062  CE1 PHE A 152     1420   1818   1611    -14    365   -208       C  
ATOM   1063  CE2 PHE A 152      26.326   8.382  59.042  1.00 16.86           C  
ANISOU 1063  CE2 PHE A 152     1891   2385   2131     -7    393   -170       C  
ATOM   1064  CZ  PHE A 152      26.290   8.250  60.429  1.00 12.26           C  
ANISOU 1064  CZ  PHE A 152     1304   1784   1571     -9    373   -186       C  
ATOM   1065  N   GLY A 153      25.586   5.139  55.517  1.00 16.65           N  
ANISOU 1065  N   GLY A 153     2028   2374   1924     53    431   -247       N  
ATOM   1066  CA  GLY A 153      26.682   5.388  54.609  1.00 19.63           C  
ANISOU 1066  CA  GLY A 153     2386   2797   2276     93    465   -224       C  
ATOM   1067  C   GLY A 153      26.840   6.871  54.394  1.00 17.49           C  
ANISOU 1067  C   GLY A 153     2062   2557   2026     75    472   -169       C  
ATOM   1068  O   GLY A 153      25.982   7.663  54.793  1.00 17.26           O  
ANISOU 1068  O   GLY A 153     2019   2514   2025     39    445   -156       O  
ATOM   1069  N   VAL A 154      27.949   7.247  53.770  1.00 14.83           N  
ANISOU 1069  N   VAL A 154     1696   2258   1681    101    515   -138       N  
ATOM   1070  CA  VAL A 154      28.229   8.640  53.471  1.00 15.78           C  
ANISOU 1070  CA  VAL A 154     1771   2397   1827     81    536    -79       C  
ATOM   1071  C   VAL A 154      28.410   8.845  51.969  1.00 13.41           C  
ANISOU 1071  C   VAL A 154     1488   2148   1459    106    576    -48       C  
ATOM   1072  O   VAL A 154      29.335   8.296  51.379  1.00 14.45           O  
ANISOU 1072  O   VAL A 154     1618   2315   1557    142    618    -54       O  
ATOM   1073  CB  VAL A 154      29.510   9.092  54.172  1.00 22.75           C  
ANISOU 1073  CB  VAL A 154     2589   3283   2774     78    564    -63       C  
ATOM   1074  CG1 VAL A 154      29.899  10.481  53.714  1.00 26.76           C  
ANISOU 1074  CG1 VAL A 154     3052   3801   3314     51    601     -2       C  
ATOM   1075  CG2 VAL A 154      29.328   9.037  55.690  1.00 23.60           C  
ANISOU 1075  CG2 VAL A 154     2679   3349   2937     60    521    -91       C  
ATOM   1076  N   PRO A 155      27.515   9.620  51.334  1.00 15.15           N  
ANISOU 1076  N   PRO A 155     1728   2377   1653     96    561    -14       N  
ATOM   1077  CA  PRO A 155      26.299  10.211  51.903  1.00 15.59           C  
ANISOU 1077  CA  PRO A 155     1786   2399   1741     64    508    -14       C  
ATOM   1078  C   PRO A 155      25.225   9.147  52.102  1.00 15.79           C  
ANISOU 1078  C   PRO A 155     1848   2414   1737     62    458    -84       C  
ATOM   1079  O   PRO A 155      25.377   8.035  51.591  1.00 14.52           O  
ANISOU 1079  O   PRO A 155     1720   2270   1525     87    465   -128       O  
ATOM   1080  CB  PRO A 155      25.852  11.198  50.819  1.00 20.75           C  
ANISOU 1080  CB  PRO A 155     2454   3079   2352     77    516     45       C  
ATOM   1081  CG  PRO A 155      26.387  10.649  49.561  1.00 25.05           C  
ANISOU 1081  CG  PRO A 155     3029   3682   2808    121    556     51       C  
ATOM   1082  CD  PRO A 155      27.682   9.958  49.909  1.00 18.42           C  
ANISOU 1082  CD  PRO A 155     2162   2844   1991    127    600     30       C  
ATOM   1083  N   VAL A 156      24.160   9.477  52.823  1.00 13.54           N  
ANISOU 1083  N   VAL A 156     1556   2100   1488     30    413    -99       N  
ATOM   1084  CA  VAL A 156      23.132   8.482  53.127  1.00 16.31           C  
ANISOU 1084  CA  VAL A 156     1933   2437   1827     14    374   -167       C  
ATOM   1085  C   VAL A 156      22.271   8.152  51.913  1.00 15.56           C  
ANISOU 1085  C   VAL A 156     1867   2386   1658     33    349   -197       C  
ATOM   1086  O   VAL A 156      22.181   8.932  50.965  1.00 15.69           O  
ANISOU 1086  O   VAL A 156     1886   2446   1632     60    349   -156       O  
ATOM   1087  CB  VAL A 156      22.209   8.894  54.305  1.00 17.02           C  
ANISOU 1087  CB  VAL A 156     1999   2492   1977    -26    340   -180       C  
ATOM   1088  CG1 VAL A 156      23.005   9.030  55.610  1.00 18.28           C  
ANISOU 1088  CG1 VAL A 156     2133   2614   2198    -40    356   -168       C  
ATOM   1089  CG2 VAL A 156      21.436  10.171  53.981  1.00 16.19           C  
ANISOU 1089  CG2 VAL A 156     1870   2403   1878    -26    314   -146       C  
ATOM   1090  N   ARG A 157      21.652   6.976  51.972  1.00 15.19           N  
ANISOU 1090  N   ARG A 157     1847   2327   1597     18    328   -270       N  
ATOM   1091  CA  ARG A 157      20.690   6.493  50.998  1.00 20.33           C  
ANISOU 1091  CA  ARG A 157     2519   3019   2189     25    292   -327       C  
ATOM   1092  C   ARG A 157      19.323   6.659  51.654  1.00 17.97           C  
ANISOU 1092  C   ARG A 157     2192   2705   1931    -20    247   -362       C  
ATOM   1093  O   ARG A 157      19.243   6.975  52.837  1.00 16.63           O  
ANISOU 1093  O   ARG A 157     1999   2493   1828    -53    252   -344       O  
ATOM   1094  CB  ARG A 157      20.960   4.997  50.789  1.00 26.37           C  
ANISOU 1094  CB  ARG A 157     3325   3762   2932     27    305   -397       C  
ATOM   1095  CG  ARG A 157      20.625   4.432  49.449  1.00 40.73           C  
ANISOU 1095  CG  ARG A 157     5173   5635   4669     57    286   -454       C  
ATOM   1096  CD  ARG A 157      21.198   3.022  49.346  1.00 34.90           C  
ANISOU 1096  CD  ARG A 157     4480   4859   3922     66    311   -516       C  
ATOM   1097  NE  ARG A 157      20.596   2.099  50.307  1.00 31.19           N  
ANISOU 1097  NE  ARG A 157     4022   4311   3517     10    303   -572       N  
ATOM   1098  CZ  ARG A 157      21.286   1.274  51.092  1.00 28.61           C  
ANISOU 1098  CZ  ARG A 157     3725   3911   3232      7    338   -574       C  
ATOM   1099  NH1 ARG A 157      22.614   1.245  51.034  1.00 31.07           N  
ANISOU 1099  NH1 ARG A 157     4048   4226   3531     60    378   -533       N  
ATOM   1100  NH2 ARG A 157      20.645   0.462  51.925  1.00 25.26           N  
ANISOU 1100  NH2 ARG A 157     3322   3413   2864    -46    336   -615       N  
ATOM   1101  N   THR A 158      18.241   6.437  50.915  1.00 13.97           N  
ANISOU 1101  N   THR A 158     1683   2242   1384    -20    202   -419       N  
ATOM   1102  CA  THR A 158      16.943   6.387  51.581  1.00 17.07           C  
ANISOU 1102  CA  THR A 158     2040   2624   1823    -70    164   -468       C  
ATOM   1103  C   THR A 158      16.855   5.131  52.452  1.00 14.65           C  
ANISOU 1103  C   THR A 158     1751   2249   1565   -126    187   -524       C  
ATOM   1104  O   THR A 158      17.168   4.027  51.995  1.00 18.17           O  
ANISOU 1104  O   THR A 158     2238   2679   1986   -126    200   -573       O  
ATOM   1105  CB  THR A 158      15.787   6.420  50.568  1.00 22.11           C  
ANISOU 1105  CB  THR A 158     2660   3333   2409    -56    105   -527       C  
ATOM   1106  OG1 THR A 158      15.822   7.663  49.856  1.00 21.36           O  
ANISOU 1106  OG1 THR A 158     2555   3293   2267      5     85   -460       O  
ATOM   1107  CG2 THR A 158      14.449   6.286  51.276  1.00 23.60           C  
ANISOU 1107  CG2 THR A 158     2798   3515   2653   -113     71   -589       C  
ATOM   1108  N   TYR A 159      16.444   5.308  53.707  1.00 13.48           N  
ANISOU 1108  N   TYR A 159     1578   2060   1484   -171    195   -516       N  
ATOM   1109  CA  TYR A 159      16.299   4.196  54.645  1.00 13.10           C  
ANISOU 1109  CA  TYR A 159     1552   1943   1481   -225    225   -553       C  
ATOM   1110  C   TYR A 159      14.839   4.025  55.013  1.00 16.14           C  
ANISOU 1110  C   TYR A 159     1896   2333   1902   -286    203   -614       C  
ATOM   1111  O   TYR A 159      13.966   4.642  54.396  1.00 17.20           O  
ANISOU 1111  O   TYR A 159     1984   2532   2020   -280    156   -641       O  
ATOM   1112  CB  TYR A 159      17.136   4.422  55.915  1.00 12.43           C  
ANISOU 1112  CB  TYR A 159     1478   1809   1436   -223    263   -490       C  
ATOM   1113  CG  TYR A 159      18.603   4.641  55.622  1.00 13.24           C  
ANISOU 1113  CG  TYR A 159     1603   1913   1513   -166    286   -435       C  
ATOM   1114  CD1 TYR A 159      19.268   3.846  54.701  1.00 15.23           C  
ANISOU 1114  CD1 TYR A 159     1898   2168   1723   -133    299   -456       C  
ATOM   1115  CD2 TYR A 159      19.314   5.652  56.247  1.00 17.09           C  
ANISOU 1115  CD2 TYR A 159     2066   2405   2024   -145    295   -371       C  
ATOM   1116  CE1 TYR A 159      20.608   4.052  54.412  1.00 16.82           C  
ANISOU 1116  CE1 TYR A 159     2109   2380   1902    -81    325   -410       C  
ATOM   1117  CE2 TYR A 159      20.655   5.866  55.963  1.00 17.60           C  
ANISOU 1117  CE2 TYR A 159     2137   2476   2074   -100    319   -328       C  
ATOM   1118  CZ  TYR A 159      21.292   5.062  55.047  1.00 17.74           C  
ANISOU 1118  CZ  TYR A 159     2191   2501   2047    -68    336   -345       C  
ATOM   1119  OH  TYR A 159      22.621   5.274  54.752  1.00 16.97           O  
ANISOU 1119  OH  TYR A 159     2092   2420   1936    -24    365   -306       O  
HETATM 1120  N   TPO A 160      14.586   3.179  56.010  1.00 13.88           N  
ANISOU 1120  N   TPO A 160     1627   1982   1664   -343    239   -635       N  
HETATM 1121  CA  TPO A 160      13.218   2.855  56.422  1.00 16.34           C  
ANISOU 1121  CA  TPO A 160     1898   2292   2018   -416    234   -697       C  
HETATM 1122  CB  TPO A 160      13.234   1.785  57.521  1.00 16.81           C  
ANISOU 1122  CB  TPO A 160     2001   2263   2124   -473    294   -700       C  
HETATM 1123  CG2 TPO A 160      11.805   1.447  57.941  1.00 18.53           C  
ANISOU 1123  CG2 TPO A 160     2169   2480   2392   -559    302   -764       C  
HETATM 1124  OG1 TPO A 160      13.825   0.598  56.965  1.00 17.36           O  
ANISOU 1124  OG1 TPO A 160     2140   2277   2180   -470    313   -729       O  
HETATM 1125  P   TPO A 160      15.253   0.262  57.649  1.00 15.41           P  
ANISOU 1125  P   TPO A 160     1965   1966   1925   -421    357   -654       P  
HETATM 1126  O1P TPO A 160      15.789  -0.943  56.942  1.00 16.82           O  
ANISOU 1126  O1P TPO A 160     2211   2091   2089   -409    372   -694       O  
HETATM 1127  O2P TPO A 160      16.252   1.481  57.416  1.00 15.49           O  
ANISOU 1127  O2P TPO A 160     1953   2036   1896   -343    334   -585       O  
HETATM 1128  O3P TPO A 160      15.071  -0.058  59.200  1.00 16.02           O  
ANISOU 1128  O3P TPO A 160     2063   1978   2045   -462    408   -615       O  
HETATM 1129  C   TPO A 160      12.482   4.121  56.871  1.00 16.50           C  
ANISOU 1129  C   TPO A 160     1845   2367   2056   -412    207   -677       C  
HETATM 1130  O   TPO A 160      13.015   4.921  57.637  1.00 15.11           O  
ANISOU 1130  O   TPO A 160     1666   2183   1890   -386    221   -610       O  
ATOM   1131  N   HIS A 161      11.272   4.319  56.351  1.00 15.71           N  
ANISOU 1131  N   HIS A 161     1682   2325   1960   -433    165   -742       N  
ATOM   1132  CA  HIS A 161      10.487   5.500  56.702  1.00 20.65           C  
ANISOU 1132  CA  HIS A 161     2236   3006   2604   -421    135   -731       C  
ATOM   1133  C   HIS A 161       9.700   5.316  58.006  1.00 22.34           C  
ANISOU 1133  C   HIS A 161     2414   3196   2880   -489    174   -750       C  
ATOM   1134  O   HIS A 161       9.561   4.195  58.506  1.00 19.27           O  
ANISOU 1134  O   HIS A 161     2059   2749   2516   -542    223   -765       O  
ATOM   1135  CB  HIS A 161       9.531   5.862  55.562  1.00 24.48           C  
ANISOU 1135  CB  HIS A 161     2663   3577   3059   -398     65   -792       C  
ATOM   1136  CG  HIS A 161       8.572   4.768  55.208  1.00 39.20           C  
ANISOU 1136  CG  HIS A 161     4504   5446   4942   -454     60   -883       C  
ATOM   1137  ND1 HIS A 161       8.932   3.683  54.437  1.00 49.53           N  
ANISOU 1137  ND1 HIS A 161     5862   6730   6227   -466     63   -923       N  
ATOM   1138  CD2 HIS A 161       7.263   4.597  55.511  1.00 46.88           C  
ANISOU 1138  CD2 HIS A 161     5421   6434   5958   -482     61   -916       C  
ATOM   1139  CE1 HIS A 161       7.887   2.888  54.284  1.00 50.98           C  
ANISOU 1139  CE1 HIS A 161     6015   6910   6445   -506     63   -980       C  
ATOM   1140  NE2 HIS A 161       6.862   3.420  54.927  1.00 51.69           N  
ANISOU 1140  NE2 HIS A 161     6040   7027   6574   -518     64   -977       N  
ATOM   1141  N   GLU A 162       9.198   6.427  58.546  1.00 21.39           N  
ANISOU 1141  N   GLU A 162     2240   3112   2776   -463    159   -726       N  
ATOM   1142  CA  GLU A 162       8.333   6.421  59.738  1.00 29.58           C  
ANISOU 1142  CA  GLU A 162     3261   4131   3848   -484    196   -718       C  
ATOM   1143  C   GLU A 162       9.000   5.793  60.959  1.00 32.26           C  
ANISOU 1143  C   GLU A 162     3659   4399   4201   -517    263   -676       C  
ATOM   1144  O   GLU A 162       8.330   5.230  61.830  1.00 37.55           O  
ANISOU 1144  O   GLU A 162     4334   5042   4890   -554    306   -683       O  
ATOM   1145  CB  GLU A 162       7.001   5.714  59.458  1.00 37.05           C  
ANISOU 1145  CB  GLU A 162     4171   5095   4810   -520    194   -781       C  
ATOM   1146  CG  GLU A 162       6.113   6.399  58.435  1.00 44.51           C  
ANISOU 1146  CG  GLU A 162     5048   6120   5741   -479    125   -825       C  
ATOM   1147  CD  GLU A 162       4.783   5.681  58.253  1.00 52.96           C  
ANISOU 1147  CD  GLU A 162     6075   7211   6835   -518    127   -893       C  
ATOM   1148  OE1 GLU A 162       4.369   4.952  59.179  1.00 55.37           O  
ANISOU 1148  OE1 GLU A 162     6391   7472   7174   -574    187   -897       O  
ATOM   1149  OE2 GLU A 162       4.159   5.840  57.182  1.00 53.29           O  
ANISOU 1149  OE2 GLU A 162     6071   7316   6861   -492     69   -944       O  
ATOM   1150  N   VAL A 163      10.320   5.886  61.016  1.00 21.97           N  
ANISOU 1150  N   VAL A 163     2395   3067   2884   -502    274   -635       N  
ATOM   1151  CA  VAL A 163      11.076   5.348  62.137  1.00 15.96           C  
ANISOU 1151  CA  VAL A 163     1690   2245   2128   -519    333   -593       C  
ATOM   1152  C   VAL A 163      10.974   6.312  63.327  1.00 16.91           C  
ANISOU 1152  C   VAL A 163     1794   2378   2252   -486    336   -553       C  
ATOM   1153  O   VAL A 163      10.507   7.439  63.165  1.00 18.78           O  
ANISOU 1153  O   VAL A 163     1984   2660   2493   -448    293   -555       O  
ATOM   1154  CB  VAL A 163      12.562   5.155  61.745  1.00 17.39           C  
ANISOU 1154  CB  VAL A 163     1940   2391   2277   -467    331   -543       C  
ATOM   1155  CG1 VAL A 163      12.710   3.998  60.746  1.00 18.04           C  
ANISOU 1155  CG1 VAL A 163     2066   2443   2345   -484    333   -578       C  
ATOM   1156  CG2 VAL A 163      13.119   6.435  61.152  1.00 18.39           C  
ANISOU 1156  CG2 VAL A 163     2041   2560   2387   -400    284   -509       C  
ATOM   1157  N   VAL A 164      11.428   5.854  64.497  1.00 17.84           N  
ANISOU 1157  N   VAL A 164     1956   2455   2367   -497    386   -520       N  
ATOM   1158  CA  VAL A 164      11.433   6.600  65.770  1.00 13.47           C  
ANISOU 1158  CA  VAL A 164     1397   1912   1809   -469    391   -490       C  
ATOM   1159  C   VAL A 164      10.038   6.634  66.390  1.00 13.37           C  
ANISOU 1159  C   VAL A 164     1354   1919   1808   -494    401   -518       C  
ATOM   1160  O   VAL A 164       9.049   6.900  65.701  1.00 15.78           O  
ANISOU 1160  O   VAL A 164     1612   2256   2126   -498    371   -558       O  
ATOM   1161  CB  VAL A 164      12.009   8.050  65.664  1.00 13.70           C  
ANISOU 1161  CB  VAL A 164     1394   1972   1839   -407    342   -469       C  
ATOM   1162  CG1 VAL A 164      12.171   8.657  67.052  1.00 13.77           C  
ANISOU 1162  CG1 VAL A 164     1404   1984   1842   -384    351   -450       C  
ATOM   1163  CG2 VAL A 164      13.363   8.064  64.931  1.00 13.23           C  
ANISOU 1163  CG2 VAL A 164     1354   1902   1772   -382    336   -443       C  
ATOM   1164  N   THR A 165       9.967   6.331  67.682  1.00 13.50           N  
ANISOU 1164  N   THR A 165     1396   1920   1815   -509    447   -498       N  
ATOM   1165  CA  THR A 165       8.713   6.390  68.425  1.00 15.61           C  
ANISOU 1165  CA  THR A 165     1631   2208   2090   -533    467   -520       C  
ATOM   1166  C   THR A 165       8.100   7.780  68.251  1.00 12.95           C  
ANISOU 1166  C   THR A 165     1230   1926   1763   -489    411   -545       C  
ATOM   1167  O   THR A 165       8.807   8.778  68.332  1.00 12.06           O  
ANISOU 1167  O   THR A 165     1112   1824   1646   -439    377   -527       O  
ATOM   1168  CB  THR A 165       8.961   6.057  69.904  1.00 22.61           C  
ANISOU 1168  CB  THR A 165     2557   3080   2954   -541    524   -482       C  
ATOM   1169  OG1 THR A 165       9.364   4.680  70.003  1.00 21.50           O  
ANISOU 1169  OG1 THR A 165     2486   2878   2806   -582    583   -455       O  
ATOM   1170  CG2 THR A 165       7.710   6.281  70.730  1.00 21.32           C  
ANISOU 1170  CG2 THR A 165     2355   2950   2796   -561    546   -504       C  
ATOM   1171  N   LEU A 166       6.793   7.829  67.985  1.00 15.07           N  
ANISOU 1171  N   LEU A 166     1450   2226   2051   -509    405   -589       N  
ATOM   1172  CA  LEU A 166       6.140   9.051  67.502  1.00 13.85           C  
ANISOU 1172  CA  LEU A 166     1236   2119   1909   -464    350   -617       C  
ATOM   1173  C   LEU A 166       6.501  10.340  68.251  1.00 11.25           C  
ANISOU 1173  C   LEU A 166      897   1804   1576   -411    329   -600       C  
ATOM   1174  O   LEU A 166       6.855  11.338  67.631  1.00 13.25           O  
ANISOU 1174  O   LEU A 166     1134   2063   1836   -362    280   -594       O  
ATOM   1175  CB  LEU A 166       4.614   8.876  67.498  1.00 19.10           C  
ANISOU 1175  CB  LEU A 166     1846   2820   2592   -494    359   -669       C  
ATOM   1176  CG  LEU A 166       3.820  10.065  66.949  1.00 19.96           C  
ANISOU 1176  CG  LEU A 166     1889   2980   2714   -445    304   -702       C  
ATOM   1177  CD1 LEU A 166       4.115  10.292  65.471  1.00 17.69           C  
ANISOU 1177  CD1 LEU A 166     1592   2704   2427   -415    249   -706       C  
ATOM   1178  CD2 LEU A 166       2.322   9.834  67.168  1.00 21.91           C  
ANISOU 1178  CD2 LEU A 166     2077   3268   2979   -477    322   -756       C  
ATOM   1179  N   TRP A 167       6.396  10.322  69.577  1.00 11.14           N  
ANISOU 1179  N   TRP A 167      890   1792   1551   -421    367   -594       N  
ATOM   1180  CA  TRP A 167       6.641  11.526  70.373  1.00 11.66           C  
ANISOU 1180  CA  TRP A 167      941   1876   1614   -374    348   -593       C  
ATOM   1181  C   TRP A 167       8.047  12.090  70.195  1.00 12.51           C  
ANISOU 1181  C   TRP A 167     1077   1957   1718   -333    319   -560       C  
ATOM   1182  O   TRP A 167       8.289  13.270  70.460  1.00 14.44           O  
ANISOU 1182  O   TRP A 167     1303   2209   1974   -289    289   -568       O  
ATOM   1183  CB  TRP A 167       6.424  11.236  71.850  1.00 13.94           C  
ANISOU 1183  CB  TRP A 167     1237   2178   1881   -394    402   -590       C  
ATOM   1184  CG  TRP A 167       5.003  11.019  72.213  1.00 15.79           C  
ANISOU 1184  CG  TRP A 167     1430   2446   2125   -426    431   -625       C  
ATOM   1185  CD1 TRP A 167       3.919  11.075  71.380  1.00 17.71           C  
ANISOU 1185  CD1 TRP A 167     1625   2710   2394   -436    410   -665       C  
ATOM   1186  CD2 TRP A 167       4.500  10.707  73.510  1.00 15.83           C  
ANISOU 1186  CD2 TRP A 167     1432   2472   2109   -449    490   -623       C  
ATOM   1187  NE1 TRP A 167       2.764  10.826  72.093  1.00 19.12           N  
ANISOU 1187  NE1 TRP A 167     1766   2922   2577   -469    452   -693       N  
ATOM   1188  CE2 TRP A 167       3.097  10.594  73.403  1.00 21.19           C  
ANISOU 1188  CE2 TRP A 167     2057   3183   2810   -479    505   -665       C  
ATOM   1189  CE3 TRP A 167       5.100  10.516  74.759  1.00 19.50           C  
ANISOU 1189  CE3 TRP A 167     1934   2940   2535   -444    534   -590       C  
ATOM   1190  CZ2 TRP A 167       2.284  10.297  74.495  1.00 26.99           C  
ANISOU 1190  CZ2 TRP A 167     2773   3948   3535   -509    566   -671       C  
ATOM   1191  CZ3 TRP A 167       4.284  10.225  75.848  1.00 26.86           C  
ANISOU 1191  CZ3 TRP A 167     2854   3904   3449   -467    596   -592       C  
ATOM   1192  CH2 TRP A 167       2.897  10.117  75.705  1.00 30.72           C  
ANISOU 1192  CH2 TRP A 167     3287   4419   3965   -502    613   -631       C  
ATOM   1193  N   TYR A 168       8.976  11.245  69.755  1.00 12.87           N  
ANISOU 1193  N   TYR A 168     1166   1972   1752   -350    332   -529       N  
ATOM   1194  CA  TYR A 168      10.384  11.633  69.665  1.00 10.63           C  
ANISOU 1194  CA  TYR A 168      907   1667   1465   -317    313   -498       C  
ATOM   1195  C   TYR A 168      10.846  11.741  68.212  1.00 15.10           C  
ANISOU 1195  C   TYR A 168     1474   2218   2046   -305    279   -485       C  
ATOM   1196  O   TYR A 168      12.042  11.884  67.931  1.00 14.53           O  
ANISOU 1196  O   TYR A 168     1421   2126   1974   -286    269   -457       O  
ATOM   1197  CB  TYR A 168      11.258  10.645  70.471  1.00 12.10           C  
ANISOU 1197  CB  TYR A 168     1142   1837   1620   -335    360   -469       C  
ATOM   1198  CG  TYR A 168      10.763  10.538  71.893  1.00 13.73           C  
ANISOU 1198  CG  TYR A 168     1348   2066   1801   -343    400   -475       C  
ATOM   1199  CD1 TYR A 168      11.189  11.435  72.865  1.00 15.36           C  
ANISOU 1199  CD1 TYR A 168     1542   2300   1996   -303    388   -485       C  
ATOM   1200  CD2 TYR A 168       9.835   9.569  72.256  1.00 14.92           C  
ANISOU 1200  CD2 TYR A 168     1511   2216   1942   -391    451   -476       C  
ATOM   1201  CE1 TYR A 168      10.694  11.370  74.165  1.00 18.47           C  
ANISOU 1201  CE1 TYR A 168     1936   2725   2356   -303    426   -493       C  
ATOM   1202  CE2 TYR A 168       9.343   9.495  73.546  1.00 14.95           C  
ANISOU 1202  CE2 TYR A 168     1516   2245   1918   -396    494   -475       C  
ATOM   1203  CZ  TYR A 168       9.780  10.394  74.498  1.00 16.43           C  
ANISOU 1203  CZ  TYR A 168     1692   2466   2083   -349    482   -482       C  
ATOM   1204  OH  TYR A 168       9.284  10.313  75.784  1.00 15.70           O  
ANISOU 1204  OH  TYR A 168     1604   2409   1953   -347    528   -480       O  
ATOM   1205  N   ARG A 169       9.882  11.701  67.296  1.00 11.50           N  
ANISOU 1205  N   ARG A 169      991   1779   1601   -314    261   -508       N  
ATOM   1206  CA  ARG A 169      10.170  11.628  65.865  1.00 12.70           C  
ANISOU 1206  CA  ARG A 169     1138   1930   1756   -308    234   -502       C  
ATOM   1207  C   ARG A 169      10.397  13.003  65.244  1.00 15.03           C  
ANISOU 1207  C   ARG A 169     1404   2233   2074   -257    188   -490       C  
ATOM   1208  O   ARG A 169       9.590  13.913  65.421  1.00 13.48           O  
ANISOU 1208  O   ARG A 169     1170   2056   1896   -232    166   -510       O  
ATOM   1209  CB  ARG A 169       9.028  10.900  65.139  1.00 10.56           C  
ANISOU 1209  CB  ARG A 169      845   1684   1485   -341    233   -541       C  
ATOM   1210  CG  ARG A 169       9.305  10.604  63.666  1.00 10.43           C  
ANISOU 1210  CG  ARG A 169      824   1678   1462   -341    208   -547       C  
ATOM   1211  CD  ARG A 169       8.138   9.819  63.030  1.00 13.84           C  
ANISOU 1211  CD  ARG A 169     1227   2137   1892   -376    204   -600       C  
ATOM   1212  NE  ARG A 169       7.861   8.589  63.773  1.00 16.98           N  
ANISOU 1212  NE  ARG A 169     1656   2505   2292   -434    259   -613       N  
ATOM   1213  CZ  ARG A 169       6.753   7.862  63.656  1.00 21.62           C  
ANISOU 1213  CZ  ARG A 169     2219   3105   2890   -476    274   -659       C  
ATOM   1214  NH1 ARG A 169       5.786   8.229  62.815  1.00 19.51           N  
ANISOU 1214  NH1 ARG A 169     1894   2889   2629   -461    231   -704       N  
ATOM   1215  NH2 ARG A 169       6.609   6.768  64.393  1.00 20.22           N  
ANISOU 1215  NH2 ARG A 169     2075   2890   2719   -531    332   -661       N  
ATOM   1216  N   ALA A 170      11.498  13.145  64.510  1.00 11.06           N  
ANISOU 1216  N   ALA A 170      916   1716   1572   -243    179   -458       N  
ATOM   1217  CA  ALA A 170      11.891  14.432  63.939  1.00 10.45           C  
ANISOU 1217  CA  ALA A 170      812   1636   1523   -201    148   -438       C  
ATOM   1218  C   ALA A 170      10.972  14.852  62.796  1.00 15.06           C  
ANISOU 1218  C   ALA A 170     1349   2262   2112   -180    110   -457       C  
ATOM   1219  O   ALA A 170      10.386  14.007  62.115  1.00 12.42           O  
ANISOU 1219  O   ALA A 170     1006   1959   1752   -202    105   -483       O  
ATOM   1220  CB  ALA A 170      13.357  14.388  63.471  1.00 11.30           C  
ANISOU 1220  CB  ALA A 170      943   1721   1631   -196    160   -397       C  
ATOM   1221  N   PRO A 171      10.836  16.167  62.588  1.00 13.50           N  
ANISOU 1221  N   PRO A 171     1116   2065   1950   -133     80   -449       N  
ATOM   1222  CA  PRO A 171       9.907  16.655  61.563  1.00 14.79           C  
ANISOU 1222  CA  PRO A 171     1243   2269   2109    -91     34   -460       C  
ATOM   1223  C   PRO A 171      10.287  16.219  60.146  1.00 15.57           C  
ANISOU 1223  C   PRO A 171     1380   2379   2158    -76     17   -425       C  
ATOM   1224  O   PRO A 171       9.389  16.042  59.330  1.00 16.40           O  
ANISOU 1224  O   PRO A 171     1458   2537   2236    -57    -20   -453       O  
ATOM   1225  CB  PRO A 171       9.987  18.180  61.711  1.00 15.99           C  
ANISOU 1225  CB  PRO A 171     1386   2385   2304    -32     12   -434       C  
ATOM   1226  CG  PRO A 171      11.283  18.432  62.398  1.00 18.50           C  
ANISOU 1226  CG  PRO A 171     1741   2641   2646    -50     46   -401       C  
ATOM   1227  CD  PRO A 171      11.464  17.273  63.331  1.00 13.69           C  
ANISOU 1227  CD  PRO A 171     1142   2045   2017   -108     83   -431       C  
ATOM   1228  N   GLU A 172      11.571  16.029  59.852  1.00 17.10           N  
ANISOU 1228  N   GLU A 172     1629   2532   2335    -82     43   -371       N  
ATOM   1229  CA  GLU A 172      11.937  15.544  58.517  1.00 17.45           C  
ANISOU 1229  CA  GLU A 172     1711   2595   2324    -66     34   -343       C  
ATOM   1230  C   GLU A 172      11.392  14.143  58.246  1.00 19.92           C  
ANISOU 1230  C   GLU A 172     2020   2950   2601   -108     34   -401       C  
ATOM   1231  O   GLU A 172      11.086  13.810  57.105  1.00 19.44           O  
ANISOU 1231  O   GLU A 172     1965   2931   2491    -88      5   -411       O  
ATOM   1232  CB  GLU A 172      13.452  15.577  58.273  1.00 16.53           C  
ANISOU 1232  CB  GLU A 172     1648   2433   2199    -65     70   -279       C  
ATOM   1233  CG  GLU A 172      14.275  14.731  59.237  1.00 15.88           C  
ANISOU 1233  CG  GLU A 172     1582   2323   2130   -114    112   -291       C  
ATOM   1234  CD  GLU A 172      14.789  15.530  60.423  1.00 15.26           C  
ANISOU 1234  CD  GLU A 172     1488   2202   2108   -119    127   -281       C  
ATOM   1235  OE1 GLU A 172      14.080  16.455  60.881  1.00 15.27           O  
ANISOU 1235  OE1 GLU A 172     1455   2200   2146   -102    107   -297       O  
ATOM   1236  OE2 GLU A 172      15.910  15.232  60.892  1.00 14.88           O  
ANISOU 1236  OE2 GLU A 172     1460   2127   2066   -135    157   -265       O  
ATOM   1237  N   ILE A 173      11.257  13.328  59.287  1.00 12.19           N  
ANISOU 1237  N   ILE A 173     1031   1959   1643   -167     67   -441       N  
ATOM   1238  CA  ILE A 173      10.685  11.996  59.111  1.00 12.45           C  
ANISOU 1238  CA  ILE A 173     1060   2015   1656   -218     75   -499       C  
ATOM   1239  C   ILE A 173       9.180  12.126  58.910  1.00 16.97           C  
ANISOU 1239  C   ILE A 173     1561   2649   2238   -221     37   -565       C  
ATOM   1240  O   ILE A 173       8.603  11.519  58.001  1.00 15.88           O  
ANISOU 1240  O   ILE A 173     1409   2554   2071   -228      8   -611       O  
ATOM   1241  CB  ILE A 173      10.981  11.075  60.307  1.00 11.59           C  
ANISOU 1241  CB  ILE A 173      971   1865   1567   -278    131   -512       C  
ATOM   1242  CG1 ILE A 173      12.500  10.889  60.468  1.00 16.10           C  
ANISOU 1242  CG1 ILE A 173     1605   2386   2125   -266    162   -454       C  
ATOM   1243  CG2 ILE A 173      10.289   9.712  60.128  1.00 16.77           C  
ANISOU 1243  CG2 ILE A 173     1625   2531   2217   -339    146   -573       C  
ATOM   1244  CD1 ILE A 173      12.884  10.249  61.786  1.00 19.38           C  
ANISOU 1244  CD1 ILE A 173     2044   2764   2556   -302    209   -452       C  
ATOM   1245  N   LEU A 174       8.552  12.946  59.747  1.00 14.60           N  
ANISOU 1245  N   LEU A 174     1213   2356   1979   -210     33   -576       N  
ATOM   1246  CA  LEU A 174       7.118  13.208  59.630  1.00 14.23           C  
ANISOU 1246  CA  LEU A 174     1119   2352   1936   -192     -1   -622       C  
ATOM   1247  C   LEU A 174       6.721  13.761  58.261  1.00 17.08           C  
ANISOU 1247  C   LEU A 174     1436   2785   2271   -131    -73   -637       C  
ATOM   1248  O   LEU A 174       5.641  13.460  57.755  1.00 18.84           O  
ANISOU 1248  O   LEU A 174     1625   3056   2477   -126   -105   -690       O  
ATOM   1249  CB  LEU A 174       6.686  14.186  60.721  1.00 12.80           C  
ANISOU 1249  CB  LEU A 174      925   2150   1790   -167      8   -611       C  
ATOM   1250  CG  LEU A 174       6.727  13.600  62.131  1.00 15.17           C  
ANISOU 1250  CG  LEU A 174     1261   2405   2100   -216     68   -609       C  
ATOM   1251  CD1 LEU A 174       6.688  14.709  63.163  1.00 17.23           C  
ANISOU 1251  CD1 LEU A 174     1514   2645   2386   -184     71   -595       C  
ATOM   1252  CD2 LEU A 174       5.548  12.643  62.325  1.00 16.84           C  
ANISOU 1252  CD2 LEU A 174     1452   2639   2306   -261     87   -662       C  
ATOM   1253  N   LEU A 175       7.587  14.580  57.675  1.00 13.81           N  
ANISOU 1253  N   LEU A 175     1068   2344   1834    -69    -88   -563       N  
ATOM   1254  CA  LEU A 175       7.310  15.193  56.369  1.00 14.14           C  
ANISOU 1254  CA  LEU A 175     1113   2431   1829     12   -149   -541       C  
ATOM   1255  C   LEU A 175       7.758  14.327  55.186  1.00 17.71           C  
ANISOU 1255  C   LEU A 175     1611   2908   2210     11   -159   -540       C  
ATOM   1256  O   LEU A 175       7.652  14.735  54.023  1.00 17.54           O  
ANISOU 1256  O   LEU A 175     1605   2930   2130     82   -206   -516       O  
ATOM   1257  CB  LEU A 175       7.930  16.595  56.283  1.00 16.82           C  
ANISOU 1257  CB  LEU A 175     1490   2720   2180     84   -153   -453       C  
ATOM   1258  CG  LEU A 175       7.294  17.635  57.223  1.00 16.52           C  
ANISOU 1258  CG  LEU A 175     1403   2667   2207    110   -162   -466       C  
ATOM   1259  CD1 LEU A 175       8.132  18.904  57.267  1.00 18.25           C  
ANISOU 1259  CD1 LEU A 175     1672   2809   2454    160   -150   -380       C  
ATOM   1260  CD2 LEU A 175       5.849  17.955  56.821  1.00 16.09           C  
ANISOU 1260  CD2 LEU A 175     1274   2693   2146    164   -227   -524       C  
ATOM   1261  N   GLY A 176       8.242  13.128  55.485  1.00 16.62           N  
ANISOU 1261  N   GLY A 176     1499   2744   2073    -64   -114   -566       N  
ATOM   1262  CA  GLY A 176       8.521  12.142  54.454  1.00 18.18           C  
ANISOU 1262  CA  GLY A 176     1732   2967   2209    -72   -123   -589       C  
ATOM   1263  C   GLY A 176       9.782  12.416  53.653  1.00 18.51           C  
ANISOU 1263  C   GLY A 176     1850   2984   2197    -24   -107   -505       C  
ATOM   1264  O   GLY A 176       9.860  12.039  52.488  1.00 20.91           O  
ANISOU 1264  O   GLY A 176     2180   3334   2431      8   -133   -516       O  
ATOM   1265  N   CYS A 177      10.766  13.061  54.281  1.00 19.51           N  
ANISOU 1265  N   CYS A 177     2011   3045   2359    -20    -63   -429       N  
ATOM   1266  CA  CYS A 177      12.057  13.338  53.642  1.00 19.15           C  
ANISOU 1266  CA  CYS A 177     2029   2972   2276     14    -34   -347       C  
ATOM   1267  C   CYS A 177      12.633  12.110  52.943  1.00 21.34           C  
ANISOU 1267  C   CYS A 177     2347   3263   2497     -5    -15   -372       C  
ATOM   1268  O   CYS A 177      12.599  11.008  53.490  1.00 20.62           O  
ANISOU 1268  O   CYS A 177     2255   3152   2427    -65      6   -429       O  
ATOM   1269  CB  CYS A 177      13.074  13.822  54.677  1.00 21.02           C  
ANISOU 1269  CB  CYS A 177     2281   3133   2574    -10     19   -292       C  
ATOM   1270  SG  CYS A 177      13.471  12.586  55.976  1.00 46.56           S  
ANISOU 1270  SG  CYS A 177     5516   6324   5849    -92     66   -339       S  
ATOM   1271  N   LYS A 178      13.166  12.304  51.738  1.00 20.79           N  
ANISOU 1271  N   LYS A 178     2320   3225   2356     51    -20   -328       N  
ATOM   1272  CA  LYS A 178      13.853  11.223  51.041  1.00 23.40           C  
ANISOU 1272  CA  LYS A 178     2695   3569   2630     44      3   -349       C  
ATOM   1273  C   LYS A 178      15.068  10.765  51.847  1.00 22.58           C  
ANISOU 1273  C   LYS A 178     2616   3394   2569      2     69   -322       C  
ATOM   1274  O   LYS A 178      15.374   9.574  51.907  1.00 21.39           O  
ANISOU 1274  O   LYS A 178     2487   3230   2411    -30     89   -370       O  
ATOM   1275  CB  LYS A 178      14.280  11.667  49.637  1.00 26.38           C  
ANISOU 1275  CB  LYS A 178     3113   3997   2914    119     -4   -294       C  
ATOM   1276  CG  LYS A 178      15.019  10.589  48.846  1.00 33.49           C  
ANISOU 1276  CG  LYS A 178     4059   4919   3747    122     21   -321       C  
ATOM   1277  CD  LYS A 178      15.000  10.873  47.350  1.00 40.91           C  
ANISOU 1277  CD  LYS A 178     5032   5940   4573    202     -3   -296       C  
ATOM   1278  CE  LYS A 178      15.866   9.877  46.585  1.00 49.31           C  
ANISOU 1278  CE  LYS A 178     6142   7024   5567    212     31   -320       C  
ATOM   1279  NZ  LYS A 178      15.576   8.456  46.945  1.00 51.68           N  
ANISOU 1279  NZ  LYS A 178     6434   7307   5894    153     22   -434       N  
ATOM   1280  N   TYR A 179      15.743  11.718  52.484  1.00 17.20           N  
ANISOU 1280  N   TYR A 179     1932   2667   1936      6     99   -250       N  
ATOM   1281  CA  TYR A 179      16.952  11.417  53.242  1.00 14.13           C  
ANISOU 1281  CA  TYR A 179     1558   2223   1586    -22    154   -225       C  
ATOM   1282  C   TYR A 179      16.878  11.934  54.668  1.00 18.66           C  
ANISOU 1282  C   TYR A 179     2099   2748   2242    -56    161   -221       C  
ATOM   1283  O   TYR A 179      16.394  13.039  54.912  1.00 21.07           O  
ANISOU 1283  O   TYR A 179     2377   3048   2580    -42    141   -197       O  
ATOM   1284  CB  TYR A 179      18.163  12.052  52.574  1.00 15.89           C  
ANISOU 1284  CB  TYR A 179     1807   2444   1787     14    193   -144       C  
ATOM   1285  CG  TYR A 179      18.358  11.630  51.138  1.00 20.47           C  
ANISOU 1285  CG  TYR A 179     2424   3080   2273     57    195   -140       C  
ATOM   1286  CD1 TYR A 179      18.672  10.316  50.815  1.00 16.87           C  
ANISOU 1286  CD1 TYR A 179     1994   2638   1777     49    207   -195       C  
ATOM   1287  CD2 TYR A 179      18.233  12.550  50.105  1.00 26.24           C  
ANISOU 1287  CD2 TYR A 179     3171   3848   2952    111    186    -80       C  
ATOM   1288  CE1 TYR A 179      18.857   9.930  49.489  1.00 19.50           C  
ANISOU 1288  CE1 TYR A 179     2361   3029   2018     94    208   -200       C  
ATOM   1289  CE2 TYR A 179      18.414  12.176  48.784  1.00 30.21           C  
ANISOU 1289  CE2 TYR A 179     3711   4412   3354    158    189    -75       C  
ATOM   1290  CZ  TYR A 179      18.725  10.868  48.482  1.00 31.56           C  
ANISOU 1290  CZ  TYR A 179     3902   4605   3484    149    198   -140       C  
ATOM   1291  OH  TYR A 179      18.901  10.501  47.166  1.00 37.13           O  
ANISOU 1291  OH  TYR A 179     4645   5378   4084    200    200   -145       O  
ATOM   1292  N   TYR A 180      17.368  11.127  55.602  1.00 16.47           N  
ANISOU 1292  N   TYR A 180     1828   2436   1994    -94    189   -244       N  
ATOM   1293  CA  TYR A 180      17.582  11.568  56.977  1.00 14.68           C  
ANISOU 1293  CA  TYR A 180     1577   2169   1831   -118    202   -237       C  
ATOM   1294  C   TYR A 180      18.866  10.927  57.496  1.00 17.88           C  
ANISOU 1294  C   TYR A 180     2005   2545   2244   -124    242   -224       C  
ATOM   1295  O   TYR A 180      19.325   9.912  56.963  1.00 13.89           O  
ANISOU 1295  O   TYR A 180     1533   2044   1700   -118    258   -237       O  
ATOM   1296  CB  TYR A 180      16.382  11.222  57.881  1.00 11.95           C  
ANISOU 1296  CB  TYR A 180     1205   1823   1511   -155    185   -294       C  
ATOM   1297  CG  TYR A 180      16.120   9.736  58.092  1.00 14.90           C  
ANISOU 1297  CG  TYR A 180     1604   2188   1869   -192    200   -344       C  
ATOM   1298  CD1 TYR A 180      16.885   8.993  58.990  1.00 15.34           C  
ANISOU 1298  CD1 TYR A 180     1688   2204   1937   -208    236   -340       C  
ATOM   1299  CD2 TYR A 180      15.092   9.083  57.412  1.00 14.31           C  
ANISOU 1299  CD2 TYR A 180     1524   2144   1770   -210    178   -400       C  
ATOM   1300  CE1 TYR A 180      16.652   7.638  59.197  1.00 12.69           C  
ANISOU 1300  CE1 TYR A 180     1386   1845   1592   -241    256   -378       C  
ATOM   1301  CE2 TYR A 180      14.844   7.716  57.616  1.00 16.03           C  
ANISOU 1301  CE2 TYR A 180     1767   2339   1986   -253    198   -449       C  
ATOM   1302  CZ  TYR A 180      15.635   7.006  58.512  1.00 15.53           C  
ANISOU 1302  CZ  TYR A 180     1742   2221   1936   -268    241   -433       C  
ATOM   1303  OH  TYR A 180      15.418   5.661  58.731  1.00 15.31           O  
ANISOU 1303  OH  TYR A 180     1751   2156   1911   -308    267   -473       O  
ATOM   1304  N   SER A 181      19.449  11.511  58.535  1.00 14.86           N  
ANISOU 1304  N   SER A 181     1601   2135   1910   -130    253   -207       N  
ATOM   1305  CA  SER A 181      20.655  10.926  59.120  1.00 14.05           C  
ANISOU 1305  CA  SER A 181     1511   2015   1814   -127    281   -201       C  
ATOM   1306  C   SER A 181      20.768  11.269  60.593  1.00 11.20           C  
ANISOU 1306  C   SER A 181     1126   1633   1496   -141    278   -212       C  
ATOM   1307  O   SER A 181      19.779  11.209  61.319  1.00 12.50           O  
ANISOU 1307  O   SER A 181     1284   1795   1669   -161    265   -241       O  
ATOM   1308  CB  SER A 181      21.922  11.349  58.355  1.00 24.00           C  
ANISOU 1308  CB  SER A 181     2767   3281   3070   -102    306   -156       C  
ATOM   1309  OG  SER A 181      22.056  12.757  58.309  1.00 35.70           O  
ANISOU 1309  OG  SER A 181     4216   4754   4594   -102    304   -120       O  
ATOM   1310  N   THR A 182      21.975  11.625  61.028  1.00  9.41           N  
ANISOU 1310  N   THR A 182      881   1399   1294   -128    290   -194       N  
ATOM   1311  CA  THR A 182      22.268  11.745  62.452  1.00 11.11           C  
ANISOU 1311  CA  THR A 182     1078   1606   1536   -130    283   -214       C  
ATOM   1312  C   THR A 182      21.380  12.740  63.188  1.00  9.27           C  
ANISOU 1312  C   THR A 182      815   1367   1339   -147    261   -232       C  
ATOM   1313  O   THR A 182      21.107  12.571  64.377  1.00 10.49           O  
ANISOU 1313  O   THR A 182      967   1524   1494   -151    255   -260       O  
ATOM   1314  CB  THR A 182      23.734  12.125  62.673  1.00 10.51           C  
ANISOU 1314  CB  THR A 182      973   1534   1488   -113    292   -202       C  
ATOM   1315  OG1 THR A 182      24.007  13.366  62.012  1.00 12.80           O  
ANISOU 1315  OG1 THR A 182     1228   1816   1820   -122    297   -175       O  
ATOM   1316  CG2 THR A 182      24.637  11.035  62.095  1.00 12.20           C  
ANISOU 1316  CG2 THR A 182     1213   1758   1663    -87    316   -191       C  
ATOM   1317  N   ALA A 183      20.932  13.776  62.488  1.00  9.79           N  
ANISOU 1317  N   ALA A 183      862   1428   1432   -149    250   -216       N  
ATOM   1318  CA  ALA A 183      20.074  14.792  63.116  1.00 10.89           C  
ANISOU 1318  CA  ALA A 183      971   1557   1609   -155    227   -237       C  
ATOM   1319  C   ALA A 183      18.803  14.216  63.732  1.00 12.40           C  
ANISOU 1319  C   ALA A 183     1166   1766   1777   -169    219   -275       C  
ATOM   1320  O   ALA A 183      18.255  14.803  64.667  1.00 11.15           O  
ANISOU 1320  O   ALA A 183      983   1608   1644   -171    207   -305       O  
ATOM   1321  CB  ALA A 183      19.727  15.895  62.122  1.00 13.01           C  
ANISOU 1321  CB  ALA A 183     1229   1810   1903   -145    218   -205       C  
ATOM   1322  N   VAL A 184      18.306  13.093  63.207  1.00  8.74           N  
ANISOU 1322  N   VAL A 184      732   1317   1270   -180    229   -280       N  
ATOM   1323  CA  VAL A 184      17.083  12.524  63.782  1.00 10.00           C  
ANISOU 1323  CA  VAL A 184      890   1492   1417   -204    230   -319       C  
ATOM   1324  C   VAL A 184      17.282  12.079  65.231  1.00 13.47           C  
ANISOU 1324  C   VAL A 184     1339   1928   1851   -213    249   -335       C  
ATOM   1325  O   VAL A 184      16.359  12.174  66.042  1.00 13.21           O  
ANISOU 1325  O   VAL A 184     1295   1905   1819   -225    249   -360       O  
ATOM   1326  CB  VAL A 184      16.450  11.373  62.938  1.00 16.95           C  
ANISOU 1326  CB  VAL A 184     1796   2382   2261   -225    238   -332       C  
ATOM   1327  CG1 VAL A 184      16.343  11.772  61.466  1.00 14.47           C  
ANISOU 1327  CG1 VAL A 184     1478   2084   1935   -205    215   -316       C  
ATOM   1328  CG2 VAL A 184      17.209  10.064  63.105  1.00 20.66           C  
ANISOU 1328  CG2 VAL A 184     2318   2831   2702   -232    268   -325       C  
ATOM   1329  N   ASP A 185      18.480  11.606  65.567  1.00 12.40           N  
ANISOU 1329  N   ASP A 185     1230   1781   1701   -196    262   -316       N  
ATOM   1330  CA  ASP A 185      18.757  11.210  66.952  1.00  9.41           C  
ANISOU 1330  CA  ASP A 185      866   1406   1304   -189    274   -326       C  
ATOM   1331  C   ASP A 185      18.908  12.422  67.885  1.00 10.23           C  
ANISOU 1331  C   ASP A 185      926   1522   1437   -174    252   -348       C  
ATOM   1332  O   ASP A 185      18.531  12.366  69.055  1.00 12.21           O  
ANISOU 1332  O   ASP A 185     1179   1791   1671   -172    259   -371       O  
ATOM   1333  CB  ASP A 185      20.018  10.340  67.041  1.00  8.81           C  
ANISOU 1333  CB  ASP A 185      829   1318   1199   -162    286   -303       C  
ATOM   1334  CG  ASP A 185      19.811   8.932  66.503  1.00 12.62           C  
ANISOU 1334  CG  ASP A 185     1368   1779   1649   -174    314   -291       C  
ATOM   1335  OD1 ASP A 185      18.676   8.416  66.588  1.00 12.95           O  
ANISOU 1335  OD1 ASP A 185     1424   1813   1683   -210    332   -306       O  
ATOM   1336  OD2 ASP A 185      20.806   8.331  66.031  1.00 12.70           O  
ANISOU 1336  OD2 ASP A 185     1404   1776   1644   -147    319   -273       O  
ATOM   1337  N   ILE A 186      19.482  13.500  67.364  1.00 10.81           N  
ANISOU 1337  N   ILE A 186      968   1585   1554   -163    229   -342       N  
ATOM   1338  CA  ILE A 186      19.651  14.736  68.135  1.00  7.04           C  
ANISOU 1338  CA  ILE A 186      462   1101   1112   -149    200   -365       C  
ATOM   1339  C   ILE A 186      18.267  15.323  68.452  1.00 11.68           C  
ANISOU 1339  C   ILE A 186     1041   1690   1708   -154    190   -389       C  
ATOM   1340  O   ILE A 186      18.023  15.792  69.569  1.00 11.26           O  
ANISOU 1340  O   ILE A 186      974   1649   1655   -145    181   -426       O  
ATOM   1341  CB  ILE A 186      20.517  15.752  67.370  1.00  9.38           C  
ANISOU 1341  CB  ILE A 186      738   1366   1459   -144    186   -343       C  
ATOM   1342  CG1 ILE A 186      21.970  15.261  67.323  1.00 10.65           C  
ANISOU 1342  CG1 ILE A 186      896   1535   1616   -135    194   -331       C  
ATOM   1343  CG2 ILE A 186      20.438  17.153  68.003  1.00 13.23           C  
ANISOU 1343  CG2 ILE A 186     1199   1831   1996   -138    160   -373       C  
ATOM   1344  CD1 ILE A 186      22.635  15.250  68.696  1.00 18.78           C  
ANISOU 1344  CD1 ILE A 186     1907   2589   2638   -117    179   -373       C  
ATOM   1345  N   TRP A 187      17.356  15.273  67.482  1.00 12.09           N  
ANISOU 1345  N   TRP A 187     1096   1738   1761   -165    190   -375       N  
ATOM   1346  CA  TRP A 187      15.979  15.710  67.738  1.00 11.02           C  
ANISOU 1346  CA  TRP A 187      944   1613   1629   -165    180   -402       C  
ATOM   1347  C   TRP A 187      15.381  14.962  68.928  1.00 13.27           C  
ANISOU 1347  C   TRP A 187     1240   1927   1877   -178    203   -430       C  
ATOM   1348  O   TRP A 187      14.825  15.577  69.846  1.00 12.14           O  
ANISOU 1348  O   TRP A 187     1078   1797   1739   -168    198   -464       O  
ATOM   1349  CB  TRP A 187      15.075  15.511  66.513  1.00 10.42           C  
ANISOU 1349  CB  TRP A 187      861   1546   1551   -173    176   -391       C  
ATOM   1350  CG  TRP A 187      13.660  15.972  66.777  1.00 11.02           C  
ANISOU 1350  CG  TRP A 187      911   1642   1635   -167    163   -425       C  
ATOM   1351  CD1 TRP A 187      12.647  15.248  67.333  1.00 11.20           C  
ANISOU 1351  CD1 TRP A 187      935   1690   1629   -188    180   -451       C  
ATOM   1352  CD2 TRP A 187      13.120  17.265  66.488  1.00 10.82           C  
ANISOU 1352  CD2 TRP A 187      848   1610   1652   -137    135   -436       C  
ATOM   1353  NE1 TRP A 187      11.506  16.021  67.430  1.00 10.87           N  
ANISOU 1353  NE1 TRP A 187      857   1665   1606   -171    162   -481       N  
ATOM   1354  CE2 TRP A 187      11.776  17.265  66.916  1.00 10.34           C  
ANISOU 1354  CE2 TRP A 187      767   1579   1583   -136    132   -474       C  
ATOM   1355  CE3 TRP A 187      13.650  18.430  65.914  1.00 13.07           C  
ANISOU 1355  CE3 TRP A 187     1110   1864   1990   -111    117   -419       C  
ATOM   1356  CZ2 TRP A 187      10.944  18.377  66.768  1.00 15.69           C  
ANISOU 1356  CZ2 TRP A 187     1404   2262   2297   -101    105   -497       C  
ATOM   1357  CZ3 TRP A 187      12.827  19.537  65.777  1.00 15.84           C  
ANISOU 1357  CZ3 TRP A 187     1422   2211   2385    -77     92   -441       C  
ATOM   1358  CH2 TRP A 187      11.488  19.500  66.202  1.00 14.58           C  
ANISOU 1358  CH2 TRP A 187     1244   2087   2209    -68     83   -480       C  
ATOM   1359  N   SER A 188      15.484  13.634  68.908  1.00 11.47           N  
ANISOU 1359  N   SER A 188     1040   1708   1612   -202    234   -416       N  
ATOM   1360  CA  SER A 188      14.962  12.810  69.995  1.00 12.03           C  
ANISOU 1360  CA  SER A 188     1125   1800   1644   -220    271   -431       C  
ATOM   1361  C   SER A 188      15.613  13.198  71.317  1.00 11.43           C  
ANISOU 1361  C   SER A 188     1043   1747   1555   -194    273   -449       C  
ATOM   1362  O   SER A 188      14.947  13.274  72.352  1.00 11.04           O  
ANISOU 1362  O   SER A 188      986   1724   1482   -194    289   -474       O  
ATOM   1363  CB  SER A 188      15.194  11.322  69.729  1.00 16.07           C  
ANISOU 1363  CB  SER A 188     1680   2303   2125   -248    313   -407       C  
ATOM   1364  OG  SER A 188      14.577  10.910  68.523  1.00 17.03           O  
ANISOU 1364  OG  SER A 188     1802   2410   2257   -274    308   -405       O  
ATOM   1365  N   LEU A 189      16.919  13.436  71.292  1.00 12.62           N  
ANISOU 1365  N   LEU A 189     1189   1891   1713   -170    258   -443       N  
ATOM   1366  CA  LEU A 189      17.614  13.812  72.523  1.00 12.11           C  
ANISOU 1366  CA  LEU A 189     1113   1857   1631   -137    249   -473       C  
ATOM   1367  C   LEU A 189      17.156  15.172  73.033  1.00 12.75           C  
ANISOU 1367  C   LEU A 189     1154   1942   1747   -125    217   -519       C  
ATOM   1368  O   LEU A 189      17.103  15.398  74.240  1.00 13.00           O  
ANISOU 1368  O   LEU A 189     1177   2012   1750   -104    218   -559       O  
ATOM   1369  CB  LEU A 189      19.135  13.815  72.311  1.00 15.51           C  
ANISOU 1369  CB  LEU A 189     1550   2275   2070   -111    223   -457       C  
ATOM   1370  CG  LEU A 189      19.944  13.074  73.368  1.00 33.07           C  
ANISOU 1370  CG  LEU A 189     3809   4528   4229    -73    225   -453       C  
ATOM   1371  CD1 LEU A 189      19.376  11.668  73.555  1.00 37.20           C  
ANISOU 1371  CD1 LEU A 189     4397   5047   4689    -82    273   -412       C  
ATOM   1372  CD2 LEU A 189      21.421  13.017  72.966  1.00 22.12           C  
ANISOU 1372  CD2 LEU A 189     2413   3134   2857    -48    198   -441       C  
ATOM   1373  N   GLY A 190      16.819  16.076  72.119  1.00 12.94           N  
ANISOU 1373  N   GLY A 190     1164   1926   1826   -131    190   -514       N  
ATOM   1374  CA  GLY A 190      16.293  17.376  72.513  1.00 12.34           C  
ANISOU 1374  CA  GLY A 190     1059   1842   1788   -115    164   -558       C  
ATOM   1375  C   GLY A 190      14.949  17.212  73.214  1.00 11.88           C  
ANISOU 1375  C   GLY A 190      995   1820   1699   -119    184   -585       C  
ATOM   1376  O   GLY A 190      14.681  17.839  74.247  1.00 12.95           O  
ANISOU 1376  O   GLY A 190     1109   1980   1830   -101    177   -636       O  
ATOM   1377  N   CYS A 191      14.102  16.349  72.665  1.00 11.41           N  
ANISOU 1377  N   CYS A 191      952   1766   1618   -146    209   -555       N  
ATOM   1378  CA  CYS A 191      12.824  16.023  73.306  1.00 12.62           C  
ANISOU 1378  CA  CYS A 191     1097   1954   1743   -159    235   -575       C  
ATOM   1379  C   CYS A 191      13.024  15.432  74.708  1.00 13.08           C  
ANISOU 1379  C   CYS A 191     1169   2056   1743   -157    270   -586       C  
ATOM   1380  O   CYS A 191      12.250  15.710  75.620  1.00 13.98           O  
ANISOU 1380  O   CYS A 191     1268   2205   1838   -150    283   -616       O  
ATOM   1381  CB  CYS A 191      12.022  15.039  72.450  1.00 15.55           C  
ANISOU 1381  CB  CYS A 191     1482   2320   2104   -196    257   -546       C  
ATOM   1382  SG  CYS A 191      11.479  15.704  70.861  1.00 15.18           S  
ANISOU 1382  SG  CYS A 191     1416   2247   2105   -186    218   -538       S  
ATOM   1383  N   ILE A 192      14.054  14.606  74.869  1.00 12.50           N  
ANISOU 1383  N   ILE A 192     1129   1984   1635   -154    288   -557       N  
ATOM   1384  CA  ILE A 192      14.322  13.953  76.155  1.00 12.60           C  
ANISOU 1384  CA  ILE A 192     1173   2038   1575   -136    324   -553       C  
ATOM   1385  C   ILE A 192      14.865  14.945  77.184  1.00 12.47           C  
ANISOU 1385  C   ILE A 192     1135   2057   1548    -89    289   -606       C  
ATOM   1386  O   ILE A 192      14.517  14.883  78.368  1.00 13.80           O  
ANISOU 1386  O   ILE A 192     1315   2270   1659    -68    308   -621       O  
ATOM   1387  CB  ILE A 192      15.305  12.773  75.980  1.00 15.93           C  
ANISOU 1387  CB  ILE A 192     1647   2449   1956   -133    350   -507       C  
ATOM   1388  CG1 ILE A 192      14.604  11.625  75.244  1.00 17.21           C  
ANISOU 1388  CG1 ILE A 192     1842   2579   2119   -185    395   -463       C  
ATOM   1389  CG2 ILE A 192      15.842  12.292  77.330  1.00 15.40           C  
ANISOU 1389  CG2 ILE A 192     1623   2426   1801    -90    372   -503       C  
ATOM   1390  CD1 ILE A 192      15.570  10.576  74.727  1.00 17.99           C  
ANISOU 1390  CD1 ILE A 192     1993   2647   2197   -183    412   -420       C  
ATOM   1391  N   PHE A 193      15.714  15.859  76.716  1.00 13.69           N  
ANISOU 1391  N   PHE A 193     1257   2188   1758    -72    238   -635       N  
ATOM   1392  CA  PHE A 193      16.211  16.978  77.518  1.00 12.37           C  
ANISOU 1392  CA  PHE A 193     1058   2039   1604    -36    195   -700       C  
ATOM   1393  C   PHE A 193      15.024  17.740  78.112  1.00 15.03           C  
ANISOU 1393  C   PHE A 193     1371   2393   1947    -33    194   -742       C  
ATOM   1394  O   PHE A 193      14.906  17.874  79.338  1.00 15.48           O  
ANISOU 1394  O   PHE A 193     1431   2500   1951     -4    195   -775       O  
ATOM   1395  CB  PHE A 193      17.063  17.890  76.615  1.00 12.95           C  
ANISOU 1395  CB  PHE A 193     1098   2058   1765    -39    150   -716       C  
ATOM   1396  CG  PHE A 193      17.720  19.054  77.322  1.00 13.03           C  
ANISOU 1396  CG  PHE A 193     1072   2072   1809    -12    103   -792       C  
ATOM   1397  CD1 PHE A 193      17.765  19.140  78.712  1.00 15.94           C  
ANISOU 1397  CD1 PHE A 193     1439   2503   2116     24     92   -844       C  
ATOM   1398  CD2 PHE A 193      18.280  20.080  76.574  1.00 11.41           C  
ANISOU 1398  CD2 PHE A 193      842   1800   1695    -23     70   -807       C  
ATOM   1399  CE1 PHE A 193      18.372  20.223  79.344  1.00 17.81           C  
ANISOU 1399  CE1 PHE A 193     1635   2742   2388     46     41   -926       C  
ATOM   1400  CE2 PHE A 193      18.888  21.167  77.191  1.00 12.93           C  
ANISOU 1400  CE2 PHE A 193      999   1981   1931     -6     31   -885       C  
ATOM   1401  CZ  PHE A 193      18.934  21.238  78.586  1.00 16.81           C  
ANISOU 1401  CZ  PHE A 193     1473   2546   2368     27     11   -957       C  
ATOM   1402  N   ALA A 194      14.126  18.203  77.250  1.00 15.51           N  
ANISOU 1402  N   ALA A 194     1413   2416   2064    -56    191   -737       N  
ATOM   1403  CA  ALA A 194      12.950  18.939  77.711  1.00 16.22           C  
ANISOU 1403  CA  ALA A 194     1476   2523   2164    -48    190   -779       C  
ATOM   1404  C   ALA A 194      12.144  18.117  78.709  1.00 17.00           C  
ANISOU 1404  C   ALA A 194     1592   2682   2187    -52    240   -767       C  
ATOM   1405  O   ALA A 194      11.662  18.636  79.719  1.00 17.51           O  
ANISOU 1405  O   ALA A 194     1639   2786   2227    -28    241   -810       O  
ATOM   1406  CB  ALA A 194      12.073  19.342  76.529  1.00 15.05           C  
ANISOU 1406  CB  ALA A 194     1313   2332   2075    -63    182   -766       C  
ATOM   1407  N   GLU A 195      12.008  16.831  78.424  1.00 15.73           N  
ANISOU 1407  N   GLU A 195     1466   2523   1990    -84    286   -707       N  
ATOM   1408  CA  GLU A 195      11.201  15.959  79.256  1.00 15.69           C  
ANISOU 1408  CA  GLU A 195     1482   2558   1920    -97    347   -684       C  
ATOM   1409  C   GLU A 195      11.813  15.766  80.642  1.00 17.93           C  
ANISOU 1409  C   GLU A 195     1800   2891   2123    -55    362   -688       C  
ATOM   1410  O   GLU A 195      11.088  15.639  81.624  1.00 19.23           O  
ANISOU 1410  O   GLU A 195     1971   3099   2238    -46    401   -693       O  
ATOM   1411  CB  GLU A 195      10.966  14.612  78.561  1.00 17.47           C  
ANISOU 1411  CB  GLU A 195     1743   2759   2138   -146    393   -620       C  
ATOM   1412  CG  GLU A 195       9.902  13.758  79.219  1.00 17.42           C  
ANISOU 1412  CG  GLU A 195     1753   2778   2089   -174    463   -596       C  
ATOM   1413  CD  GLU A 195       9.540  12.540  78.382  1.00 18.87           C  
ANISOU 1413  CD  GLU A 195     1961   2922   2286   -232    502   -547       C  
ATOM   1414  OE1 GLU A 195       9.827  12.547  77.163  1.00 16.84           O  
ANISOU 1414  OE1 GLU A 195     1696   2624   2077   -248    466   -544       O  
ATOM   1415  OE2 GLU A 195       8.976  11.582  78.945  1.00 18.86           O  
ANISOU 1415  OE2 GLU A 195     1989   2929   2247   -260    569   -514       O  
ATOM   1416  N   MET A 196      13.137  15.772  80.740  1.00 17.68           N  
ANISOU 1416  N   MET A 196     1787   2856   2073    -24    328   -690       N  
ATOM   1417  CA  MET A 196      13.765  15.636  82.051  1.00 19.39           C  
ANISOU 1417  CA  MET A 196     2037   3126   2203     29    328   -701       C  
ATOM   1418  C   MET A 196      13.464  16.851  82.916  1.00 18.39           C  
ANISOU 1418  C   MET A 196     1870   3035   2081     62    292   -775       C  
ATOM   1419  O   MET A 196      13.316  16.733  84.129  1.00 18.85           O  
ANISOU 1419  O   MET A 196     1952   3149   2061     98    312   -783       O  
ATOM   1420  CB  MET A 196      15.280  15.432  81.944  1.00 15.46           C  
ANISOU 1420  CB  MET A 196     1560   2625   1689     61    287   -698       C  
ATOM   1421  CG  MET A 196      15.696  14.052  81.411  1.00 16.71           C  
ANISOU 1421  CG  MET A 196     1776   2761   1813     46    329   -622       C  
ATOM   1422  SD  MET A 196      17.466  13.777  81.648  1.00 20.76           S  
ANISOU 1422  SD  MET A 196     2313   3296   2280    108    279   -626       S  
ATOM   1423  CE  MET A 196      18.157  14.738  80.295  1.00 19.55           C  
ANISOU 1423  CE  MET A 196     2087   3089   2252     81    220   -668       C  
ATOM   1424  N   VAL A 197      13.355  18.015  82.284  1.00 14.98           N  
ANISOU 1424  N   VAL A 197     1382   2570   1741     53    243   -828       N  
ATOM   1425  CA  VAL A 197      13.137  19.252  83.026  1.00 18.86           C  
ANISOU 1425  CA  VAL A 197     1833   3083   2250     85    205   -906       C  
ATOM   1426  C   VAL A 197      11.706  19.337  83.563  1.00 21.41           C  
ANISOU 1426  C   VAL A 197     2144   3439   2551     82    248   -914       C  
ATOM   1427  O   VAL A 197      11.465  19.902  84.633  1.00 20.69           O  
ANISOU 1427  O   VAL A 197     2042   3394   2424    118    242   -963       O  
ATOM   1428  CB  VAL A 197      13.477  20.492  82.168  1.00 17.63           C  
ANISOU 1428  CB  VAL A 197     1628   2866   2204     78    145   -957       C  
ATOM   1429  CG1 VAL A 197      13.200  21.778  82.952  1.00 22.81           C  
ANISOU 1429  CG1 VAL A 197     2245   3536   2885    111    108  -1041       C  
ATOM   1430  CG2 VAL A 197      14.953  20.444  81.719  1.00 13.67           C  
ANISOU 1430  CG2 VAL A 197     1129   2336   1729     80    106   -957       C  
ATOM   1431  N   THR A 198      10.762  18.744  82.835  1.00 19.36           N  
ANISOU 1431  N   THR A 198     1884   3160   2310     38    293   -868       N  
ATOM   1432  CA  THR A 198       9.346  18.821  83.212  1.00 27.71           C  
ANISOU 1432  CA  THR A 198     2919   4250   3360     29    335   -879       C  
ATOM   1433  C   THR A 198       8.715  17.495  83.656  1.00 28.31           C  
ANISOU 1433  C   THR A 198     3033   4357   3367      2    420   -816       C  
ATOM   1434  O   THR A 198       7.650  17.489  84.284  1.00 29.95           O  
ANISOU 1434  O   THR A 198     3224   4604   3550      1    465   -826       O  
ATOM   1435  CB  THR A 198       8.505  19.389  82.056  1.00 28.59           C  
ANISOU 1435  CB  THR A 198     2983   4319   3560      3    314   -895       C  
ATOM   1436  OG1 THR A 198       8.524  18.475  80.951  1.00 30.24           O  
ANISOU 1436  OG1 THR A 198     3210   4489   3790    -44    332   -834       O  
ATOM   1437  CG2 THR A 198       9.066  20.727  81.596  1.00 31.10           C  
ANISOU 1437  CG2 THR A 198     3272   4593   3952     30    241   -951       C  
ATOM   1438  N   ARG A 199       9.380  16.387  83.341  1.00 20.56           N  
ANISOU 1438  N   ARG A 199     2103   3353   2356    -18    446   -751       N  
ATOM   1439  CA  ARG A 199       8.831  15.029  83.492  1.00 23.40           C  
ANISOU 1439  CA  ARG A 199     2506   3717   2669    -55    530   -680       C  
ATOM   1440  C   ARG A 199       7.592  14.777  82.633  1.00 29.03           C  
ANISOU 1440  C   ARG A 199     3177   4408   3445   -116    556   -673       C  
ATOM   1441  O   ARG A 199       6.876  13.798  82.852  1.00 29.82           O  
ANISOU 1441  O   ARG A 199     3296   4513   3520   -153    628   -630       O  
ATOM   1442  CB  ARG A 199       8.561  14.655  84.957  1.00 30.98           C  
ANISOU 1442  CB  ARG A 199     3505   4734   3530    -23    592   -665       C  
ATOM   1443  CG  ARG A 199       9.803  14.246  85.733  1.00 29.70           C  
ANISOU 1443  CG  ARG A 199     3415   4590   3279     29    587   -640       C  
ATOM   1444  CD  ARG A 199      10.302  15.394  86.583  1.00 25.86           C  
ANISOU 1444  CD  ARG A 199     2907   4150   2768     93    524   -714       C  
ATOM   1445  NE  ARG A 199       9.262  15.852  87.499  1.00 24.22           N  
ANISOU 1445  NE  ARG A 199     2677   3993   2532    107    560   -747       N  
ATOM   1446  CZ  ARG A 199       9.155  17.096  87.946  1.00 27.42           C  
ANISOU 1446  CZ  ARG A 199     3032   4428   2957    142    507   -830       C  
ATOM   1447  NH1 ARG A 199      10.027  18.019  87.561  1.00 25.80           N  
ANISOU 1447  NH1 ARG A 199     2794   4201   2806    163    417   -887       N  
ATOM   1448  NH2 ARG A 199       8.171  17.419  88.774  1.00 30.40           N  
ANISOU 1448  NH2 ARG A 199     3392   4855   3304    156    548   -858       N  
ATOM   1449  N   ARG A 200       7.349  15.662  81.666  1.00 23.41           N  
ANISOU 1449  N   ARG A 200     2412   3670   2815   -122    495   -716       N  
ATOM   1450  CA  ARG A 200       6.244  15.508  80.713  1.00 25.96           C  
ANISOU 1450  CA  ARG A 200     2694   3975   3196   -169    501   -719       C  
ATOM   1451  C   ARG A 200       6.767  15.588  79.279  1.00 19.72           C  
ANISOU 1451  C   ARG A 200     1903   3126   2464   -183    447   -709       C  
ATOM   1452  O   ARG A 200       7.597  16.439  78.971  1.00 17.51           O  
ANISOU 1452  O   ARG A 200     1619   2824   2210   -149    390   -731       O  
ATOM   1453  CB  ARG A 200       5.186  16.597  80.920  1.00 32.80           C  
ANISOU 1453  CB  ARG A 200     3497   4874   4093   -147    481   -784       C  
ATOM   1454  CG  ARG A 200       4.163  16.316  82.024  1.00 45.33           C  
ANISOU 1454  CG  ARG A 200     5069   6520   5635   -152    550   -790       C  
ATOM   1455  CD  ARG A 200       4.782  16.380  83.413  1.00 50.86           C  
ANISOU 1455  CD  ARG A 200     5808   7260   6256   -107    576   -788       C  
ATOM   1456  NE  ARG A 200       3.810  16.171  84.486  1.00 48.75           N  
ANISOU 1456  NE  ARG A 200     5531   7053   5941   -105    648   -792       N  
ATOM   1457  CZ  ARG A 200       4.138  15.960  85.758  1.00 48.74           C  
ANISOU 1457  CZ  ARG A 200     5573   7092   5852    -69    692   -776       C  
ATOM   1458  NH1 ARG A 200       5.416  15.924  86.117  1.00 42.91           N  
ANISOU 1458  NH1 ARG A 200     4892   6346   5065    -30    664   -762       N  
ATOM   1459  NH2 ARG A 200       3.191  15.780  86.672  1.00 46.31           N  
ANISOU 1459  NH2 ARG A 200     5255   6839   5502    -67    765   -777       N  
ATOM   1460  N   ALA A 201       6.266  14.721  78.402  1.00 17.41           N  
ANISOU 1460  N   ALA A 201     1614   2808   2194   -234    467   -680       N  
ATOM   1461  CA  ALA A 201       6.722  14.711  77.012  1.00 19.17           C  
ANISOU 1461  CA  ALA A 201     1842   2981   2461   -243    421   -667       C  
ATOM   1462  C   ALA A 201       6.501  16.071  76.350  1.00 18.74           C  
ANISOU 1462  C   ALA A 201     1744   2917   2458   -205    356   -712       C  
ATOM   1463  O   ALA A 201       5.445  16.692  76.506  1.00 19.35           O  
ANISOU 1463  O   ALA A 201     1777   3023   2553   -192    351   -753       O  
ATOM   1464  CB  ALA A 201       6.016  13.599  76.220  1.00 20.11           C  
ANISOU 1464  CB  ALA A 201     1965   3082   2594   -301    450   -644       C  
ATOM   1465  N   LEU A 202       7.504  16.531  75.612  1.00 16.94           N  
ANISOU 1465  N   LEU A 202     1533   2648   2256   -183    311   -701       N  
ATOM   1466  CA  LEU A 202       7.448  17.826  74.938  1.00 17.37           C  
ANISOU 1466  CA  LEU A 202     1560   2679   2363   -142    256   -730       C  
ATOM   1467  C   LEU A 202       6.371  17.896  73.847  1.00 21.05           C  
ANISOU 1467  C   LEU A 202     1996   3143   2858   -145    241   -733       C  
ATOM   1468  O   LEU A 202       5.639  18.886  73.749  1.00 17.16           O  
ANISOU 1468  O   LEU A 202     1464   2660   2396   -110    215   -771       O  
ATOM   1469  CB  LEU A 202       8.815  18.144  74.328  1.00 17.40           C  
ANISOU 1469  CB  LEU A 202     1590   2633   2388   -126    224   -705       C  
ATOM   1470  CG  LEU A 202       8.974  19.498  73.637  1.00 18.53           C  
ANISOU 1470  CG  LEU A 202     1713   2735   2591    -85    175   -722       C  
ATOM   1471  CD1 LEU A 202       8.627  20.641  74.591  1.00 23.33           C  
ANISOU 1471  CD1 LEU A 202     2290   3356   3218    -48    160   -785       C  
ATOM   1472  CD2 LEU A 202      10.395  19.638  73.130  1.00 17.26           C  
ANISOU 1472  CD2 LEU A 202     1579   2527   2453    -81    157   -691       C  
ATOM   1473  N   PHE A 203       6.280  16.844  73.035  1.00 14.62           N  
ANISOU 1473  N   PHE A 203     1200   2320   2035   -183    254   -699       N  
ATOM   1474  CA  PHE A 203       5.369  16.814  71.890  1.00 14.40           C  
ANISOU 1474  CA  PHE A 203     1143   2298   2029   -184    234   -706       C  
ATOM   1475  C   PHE A 203       4.562  15.521  71.908  1.00 16.89           C  
ANISOU 1475  C   PHE A 203     1455   2638   2324   -242    276   -707       C  
ATOM   1476  O   PHE A 203       4.881  14.577  71.187  1.00 15.45           O  
ANISOU 1476  O   PHE A 203     1300   2436   2135   -274    284   -679       O  
ATOM   1477  CB  PHE A 203       6.152  16.864  70.570  1.00 14.14           C  
ANISOU 1477  CB  PHE A 203     1132   2228   2013   -171    199   -668       C  
ATOM   1478  CG  PHE A 203       7.047  18.070  70.413  1.00 16.29           C  
ANISOU 1478  CG  PHE A 203     1409   2464   2317   -124    164   -659       C  
ATOM   1479  CD1 PHE A 203       6.531  19.358  70.463  1.00 17.34           C  
ANISOU 1479  CD1 PHE A 203     1504   2598   2487    -75    133   -692       C  
ATOM   1480  CD2 PHE A 203       8.405  17.907  70.170  1.00 17.34           C  
ANISOU 1480  CD2 PHE A 203     1580   2558   2448   -128    161   -620       C  
ATOM   1481  CE1 PHE A 203       7.357  20.458  70.290  1.00 17.49           C  
ANISOU 1481  CE1 PHE A 203     1527   2572   2548    -36    104   -686       C  
ATOM   1482  CE2 PHE A 203       9.236  19.006  69.994  1.00 19.71           C  
ANISOU 1482  CE2 PHE A 203     1880   2820   2788    -92    133   -614       C  
ATOM   1483  CZ  PHE A 203       8.707  20.284  70.049  1.00 18.19           C  
ANISOU 1483  CZ  PHE A 203     1652   2621   2640    -49    106   -647       C  
ATOM   1484  N   PRO A 204       3.519  15.459  72.747  1.00 15.99           N  
ANISOU 1484  N   PRO A 204     1305   2566   2204   -257    308   -741       N  
ATOM   1485  CA  PRO A 204       2.807  14.190  72.924  1.00 15.33           C  
ANISOU 1485  CA  PRO A 204     1218   2498   2107   -320    360   -740       C  
ATOM   1486  C   PRO A 204       1.684  13.987  71.904  1.00 19.73           C  
ANISOU 1486  C   PRO A 204     1728   3077   2690   -334    343   -773       C  
ATOM   1487  O   PRO A 204       0.509  14.040  72.271  1.00 22.34           O  
ANISOU 1487  O   PRO A 204     2006   3451   3030   -346    362   -814       O  
ATOM   1488  CB  PRO A 204       2.225  14.326  74.330  1.00 21.93           C  
ANISOU 1488  CB  PRO A 204     2032   3374   2925   -326    406   -760       C  
ATOM   1489  CG  PRO A 204       1.998  15.789  74.488  1.00 24.05           C  
ANISOU 1489  CG  PRO A 204     2263   3664   3211   -262    362   -800       C  
ATOM   1490  CD  PRO A 204       3.082  16.486  73.707  1.00 19.67           C  
ANISOU 1490  CD  PRO A 204     1738   3064   2674   -220    305   -780       C  
ATOM   1491  N   GLY A 205       2.040  13.759  70.645  1.00 18.21           N  
ANISOU 1491  N   GLY A 205     1550   2862   2507   -330    308   -759       N  
ATOM   1492  CA  GLY A 205       1.047  13.620  69.588  1.00 16.90           C  
ANISOU 1492  CA  GLY A 205     1335   2726   2361   -334    282   -796       C  
ATOM   1493  C   GLY A 205       0.263  12.321  69.630  1.00 25.52           C  
ANISOU 1493  C   GLY A 205     2413   3829   3455   -407    330   -818       C  
ATOM   1494  O   GLY A 205       0.738  11.313  70.154  1.00 23.92           O  
ANISOU 1494  O   GLY A 205     2257   3594   3239   -459    381   -789       O  
ATOM   1495  N   ASP A 206      -0.935  12.349  69.046  1.00 27.93           N  
ANISOU 1495  N   ASP A 206     2651   4180   3780   -411    313   -871       N  
ATOM   1496  CA  ASP A 206      -1.825  11.190  69.016  1.00 36.02           C  
ANISOU 1496  CA  ASP A 206     3648   5220   4819   -483    357   -905       C  
ATOM   1497  C   ASP A 206      -1.810  10.486  67.656  1.00 37.27           C  
ANISOU 1497  C   ASP A 206     3805   5372   4985   -501    328   -922       C  
ATOM   1498  O   ASP A 206      -2.364   9.397  67.502  1.00 40.88           O  
ANISOU 1498  O   ASP A 206     4248   5827   5458   -567    364   -951       O  
ATOM   1499  CB  ASP A 206      -3.255  11.621  69.360  1.00 44.79           C  
ANISOU 1499  CB  ASP A 206     4673   6395   5951   -481    362   -966       C  
ATOM   1500  CG  ASP A 206      -3.340  12.353  70.688  1.00 54.94           C  
ANISOU 1500  CG  ASP A 206     5953   7696   7227   -460    390   -959       C  
ATOM   1501  OD1 ASP A 206      -3.202  11.693  71.739  1.00 55.94           O  
ANISOU 1501  OD1 ASP A 206     6107   7807   7342   -509    458   -934       O  
ATOM   1502  OD2 ASP A 206      -3.546  13.587  70.686  1.00 58.09           O  
ANISOU 1502  OD2 ASP A 206     6319   8122   7629   -391    345   -977       O  
ATOM   1503  N   SER A 207      -1.173  11.122  66.677  1.00 23.52           N  
ANISOU 1503  N   SER A 207     2077   3626   3233   -443    266   -905       N  
ATOM   1504  CA  SER A 207      -1.087  10.608  65.319  1.00 20.24           C  
ANISOU 1504  CA  SER A 207     1658   3216   2817   -447    230   -921       C  
ATOM   1505  C   SER A 207       0.017  11.382  64.626  1.00 19.48           C  
ANISOU 1505  C   SER A 207     1599   3101   2702   -384    179   -875       C  
ATOM   1506  O   SER A 207       0.523  12.353  65.179  1.00 19.87           O  
ANISOU 1506  O   SER A 207     1664   3136   2748   -339    170   -841       O  
ATOM   1507  CB  SER A 207      -2.405  10.848  64.581  1.00 25.73           C  
ANISOU 1507  CB  SER A 207     2266   3981   3529   -431    191   -992       C  
ATOM   1508  OG  SER A 207      -2.640  12.241  64.435  1.00 19.55           O  
ANISOU 1508  OG  SER A 207     1450   3234   2745   -349    136   -994       O  
ATOM   1509  N   GLU A 208       0.391  10.972  63.418  1.00 16.91           N  
ANISOU 1509  N   GLU A 208     1282   2777   2366   -381    146   -878       N  
ATOM   1510  CA  GLU A 208       1.448  11.680  62.706  1.00 17.98           C  
ANISOU 1510  CA  GLU A 208     1448   2899   2483   -325    101   -833       C  
ATOM   1511  C   GLU A 208       1.115  13.155  62.482  1.00 18.35           C  
ANISOU 1511  C   GLU A 208     1455   2982   2537   -245     46   -832       C  
ATOM   1512  O   GLU A 208       1.956  14.020  62.699  1.00 16.91           O  
ANISOU 1512  O   GLU A 208     1300   2769   2354   -204     34   -784       O  
ATOM   1513  CB  GLU A 208       1.787  10.996  61.380  1.00 24.74           C  
ANISOU 1513  CB  GLU A 208     2312   3767   3322   -333     72   -846       C  
ATOM   1514  CG  GLU A 208       2.651   9.754  61.546  1.00 29.23           C  
ANISOU 1514  CG  GLU A 208     2944   4280   3884   -395    122   -826       C  
ATOM   1515  CD  GLU A 208       3.075   9.150  60.220  1.00 40.21           C  
ANISOU 1515  CD  GLU A 208     4343   5681   5253   -399     91   -843       C  
ATOM   1516  OE1 GLU A 208       3.571   9.899  59.351  1.00 37.57           O  
ANISOU 1516  OE1 GLU A 208     4004   5374   4895   -342     36   -826       O  
ATOM   1517  OE2 GLU A 208       2.905   7.926  60.047  1.00 51.18           O  
ANISOU 1517  OE2 GLU A 208     5745   7053   6650   -458    120   -876       O  
ATOM   1518  N   ILE A 209      -0.110  13.448  62.058  1.00 18.05           N  
ANISOU 1518  N   ILE A 209     1349   3004   2506   -220     11   -887       N  
ATOM   1519  CA  ILE A 209      -0.458  14.841  61.802  1.00 17.15           C  
ANISOU 1519  CA  ILE A 209     1197   2920   2398   -135    -45   -885       C  
ATOM   1520  C   ILE A 209      -0.576  15.627  63.109  1.00 18.13           C  
ANISOU 1520  C   ILE A 209     1321   3022   2544   -122    -16   -875       C  
ATOM   1521  O   ILE A 209      -0.170  16.792  63.180  1.00 16.45           O  
ANISOU 1521  O   ILE A 209     1115   2792   2342    -59    -44   -845       O  
ATOM   1522  CB  ILE A 209      -1.739  14.976  60.932  1.00 20.50           C  
ANISOU 1522  CB  ILE A 209     1547   3423   2820   -100    -98   -950       C  
ATOM   1523  CG1 ILE A 209      -1.897  16.419  60.448  1.00 25.86           C  
ANISOU 1523  CG1 ILE A 209     2200   4126   3498      5   -166   -935       C  
ATOM   1524  CG2 ILE A 209      -2.979  14.484  61.682  1.00 25.42           C  
ANISOU 1524  CG2 ILE A 209     2116   4076   3465   -148    -59  -1013       C  
ATOM   1525  CD1 ILE A 209      -0.752  16.876  59.540  1.00 25.00           C  
ANISOU 1525  CD1 ILE A 209     2136   3998   3367     56   -208   -873       C  
ATOM   1526  N   ASP A 210      -1.099  14.993  64.155  1.00 15.77           N  
ANISOU 1526  N   ASP A 210     1016   2722   2254   -181     42   -901       N  
ATOM   1527  CA  ASP A 210      -1.197  15.674  65.445  1.00 15.55           C  
ANISOU 1527  CA  ASP A 210      988   2682   2239   -170     71   -898       C  
ATOM   1528  C   ASP A 210       0.201  15.933  65.995  1.00 16.81           C  
ANISOU 1528  C   ASP A 210     1219   2778   2392   -167     89   -836       C  
ATOM   1529  O   ASP A 210       0.452  16.974  66.592  1.00 14.02           O  
ANISOU 1529  O   ASP A 210      867   2409   2050   -123     80   -826       O  
ATOM   1530  CB  ASP A 210      -2.024  14.877  66.457  1.00 17.21           C  
ANISOU 1530  CB  ASP A 210     1174   2911   2453   -236    133   -935       C  
ATOM   1531  CG  ASP A 210      -2.200  15.620  67.785  1.00 28.50           C  
ANISOU 1531  CG  ASP A 210     2597   4343   3889   -219    159   -939       C  
ATOM   1532  OD1 ASP A 210      -2.571  16.816  67.770  1.00 27.36           O  
ANISOU 1532  OD1 ASP A 210     2418   4219   3760   -151    120   -957       O  
ATOM   1533  OD2 ASP A 210      -1.956  15.009  68.843  1.00 27.23           O  
ANISOU 1533  OD2 ASP A 210     2465   4163   3717   -271    218   -926       O  
ATOM   1534  N   GLN A 211       1.108  14.982  65.778  1.00 14.55           N  
ANISOU 1534  N   GLN A 211      986   2455   2088   -212    112   -801       N  
ATOM   1535  CA  GLN A 211       2.496  15.139  66.202  1.00 13.25           C  
ANISOU 1535  CA  GLN A 211      885   2236   1916   -208    127   -746       C  
ATOM   1536  C   GLN A 211       3.106  16.360  65.528  1.00 13.55           C  
ANISOU 1536  C   GLN A 211      921   2260   1969   -140     74   -719       C  
ATOM   1537  O   GLN A 211       3.714  17.211  66.180  1.00 12.73           O  
ANISOU 1537  O   GLN A 211      834   2124   1878   -111     75   -699       O  
ATOM   1538  CB  GLN A 211       3.316  13.899  65.834  1.00 16.23           C  
ANISOU 1538  CB  GLN A 211     1312   2581   2272   -259    152   -718       C  
ATOM   1539  CG  GLN A 211       4.746  13.928  66.374  1.00 13.01           C  
ANISOU 1539  CG  GLN A 211      966   2122   1854   -259    171   -665       C  
ATOM   1540  CD  GLN A 211       4.777  13.900  67.887  1.00 12.60           C  
ANISOU 1540  CD  GLN A 211      929   2061   1796   -276    215   -665       C  
ATOM   1541  OE1 GLN A 211       3.883  13.355  68.516  1.00 17.18           O  
ANISOU 1541  OE1 GLN A 211     1491   2665   2374   -312    249   -694       O  
ATOM   1542  NE2 GLN A 211       5.825  14.471  68.479  1.00 13.08           N  
ANISOU 1542  NE2 GLN A 211     1021   2093   1855   -251    214   -636       N  
ATOM   1543  N   LEU A 212       2.934  16.438  64.215  1.00 13.85           N  
ANISOU 1543  N   LEU A 212      936   2322   2004   -113     28   -720       N  
ATOM   1544  CA  LEU A 212       3.426  17.564  63.434  1.00 15.87           C  
ANISOU 1544  CA  LEU A 212     1185   2571   2275    -43    -23   -691       C  
ATOM   1545  C   LEU A 212       2.852  18.887  63.943  1.00 15.04           C  
ANISOU 1545  C   LEU A 212     1045   2467   2202     19    -45   -708       C  
ATOM   1546  O   LEU A 212       3.581  19.866  64.100  1.00 14.63           O  
ANISOU 1546  O   LEU A 212     1008   2373   2179     60    -56   -677       O  
ATOM   1547  CB  LEU A 212       3.049  17.359  61.968  1.00 17.37           C  
ANISOU 1547  CB  LEU A 212     1345   2809   2445    -17    -74   -701       C  
ATOM   1548  CG  LEU A 212       3.916  17.882  60.827  1.00 28.16           C  
ANISOU 1548  CG  LEU A 212     2721   4173   3804     36   -118   -656       C  
ATOM   1549  CD1 LEU A 212       5.401  17.660  61.071  1.00 20.80           C  
ANISOU 1549  CD1 LEU A 212     1843   3184   2876      4    -81   -605       C  
ATOM   1550  CD2 LEU A 212       3.485  17.189  59.537  1.00 28.76           C  
ANISOU 1550  CD2 LEU A 212     2777   4312   3838     41   -159   -681       C  
ATOM   1551  N   PHE A 213       1.549  18.918  64.207  1.00 14.52           N  
ANISOU 1551  N   PHE A 213      930   2448   2138     25    -49   -760       N  
ATOM   1552  CA  PHE A 213       0.903  20.150  64.674  1.00 13.50           C  
ANISOU 1552  CA  PHE A 213      765   2326   2040     88    -72   -785       C  
ATOM   1553  C   PHE A 213       1.339  20.562  66.087  1.00 17.52           C  
ANISOU 1553  C   PHE A 213     1299   2794   2564     74    -31   -786       C  
ATOM   1554  O   PHE A 213       1.440  21.754  66.394  1.00 15.35           O  
ANISOU 1554  O   PHE A 213     1018   2493   2323    132    -51   -789       O  
ATOM   1555  CB  PHE A 213      -0.627  20.035  64.584  1.00 14.48           C  
ANISOU 1555  CB  PHE A 213      823   2519   2159     98    -86   -847       C  
ATOM   1556  CG  PHE A 213      -1.165  20.078  63.173  1.00 18.07           C  
ANISOU 1556  CG  PHE A 213     1243   3022   2602    145   -148   -856       C  
ATOM   1557  CD1 PHE A 213      -0.314  20.257  62.087  1.00 18.75           C  
ANISOU 1557  CD1 PHE A 213     1358   3091   2676    181   -187   -806       C  
ATOM   1558  CD2 PHE A 213      -2.526  19.943  62.935  1.00 17.02           C  
ANISOU 1558  CD2 PHE A 213     1044   2958   2465    157   -168   -918       C  
ATOM   1559  CE1 PHE A 213      -0.810  20.294  60.792  1.00 15.69           C  
ANISOU 1559  CE1 PHE A 213      941   2757   2263    234   -249   -814       C  
ATOM   1560  CE2 PHE A 213      -3.030  19.985  61.645  1.00 19.04           C  
ANISOU 1560  CE2 PHE A 213     1268   3267   2701    208   -232   -932       C  
ATOM   1561  CZ  PHE A 213      -2.170  20.158  60.571  1.00 18.51           C  
ANISOU 1561  CZ  PHE A 213     1236   3185   2613    249   -274   -878       C  
ATOM   1562  N   ARG A 214       1.594  19.591  66.957  1.00 13.56           N  
ANISOU 1562  N   ARG A 214      827   2287   2038      3     25   -788       N  
ATOM   1563  CA  ARG A 214       2.138  19.931  68.265  1.00 14.93           C  
ANISOU 1563  CA  ARG A 214     1027   2430   2216     -5     57   -789       C  
ATOM   1564  C   ARG A 214       3.519  20.577  68.134  1.00 14.49           C  
ANISOU 1564  C   ARG A 214     1013   2312   2179     19     43   -745       C  
ATOM   1565  O   ARG A 214       3.839  21.535  68.842  1.00 16.27           O  
ANISOU 1565  O   ARG A 214     1240   2509   2432     51     39   -759       O  
ATOM   1566  CB  ARG A 214       2.186  18.711  69.185  1.00 16.54           C  
ANISOU 1566  CB  ARG A 214     1255   2644   2384    -79    117   -791       C  
ATOM   1567  CG  ARG A 214       0.792  18.305  69.649  1.00 21.01           C  
ANISOU 1567  CG  ARG A 214     1771   3269   2944   -103    141   -841       C  
ATOM   1568  CD  ARG A 214       0.823  17.119  70.583  1.00 30.38           C  
ANISOU 1568  CD  ARG A 214     2981   4461   4102   -174    205   -837       C  
ATOM   1569  NE  ARG A 214      -0.517  16.568  70.789  1.00 30.08           N  
ANISOU 1569  NE  ARG A 214     2888   4475   4064   -208    233   -881       N  
ATOM   1570  CZ  ARG A 214      -1.280  16.804  71.851  1.00 30.67           C  
ANISOU 1570  CZ  ARG A 214     2927   4589   4138   -212    264   -917       C  
ATOM   1571  NH1 ARG A 214      -0.848  17.585  72.832  1.00 32.59           N  
ANISOU 1571  NH1 ARG A 214     3183   4825   4374   -180    269   -918       N  
ATOM   1572  NH2 ARG A 214      -2.474  16.243  71.936  1.00 32.55           N  
ANISOU 1572  NH2 ARG A 214     3111   4874   4382   -249    293   -956       N  
ATOM   1573  N   ILE A 215       4.328  20.066  67.216  1.00 12.02           N  
ANISOU 1573  N   ILE A 215      730   1978   1858      3     36   -699       N  
ATOM   1574  CA  ILE A 215       5.638  20.662  66.988  1.00 15.34           C  
ANISOU 1574  CA  ILE A 215     1182   2343   2305     22     25   -658       C  
ATOM   1575  C   ILE A 215       5.476  22.081  66.438  1.00 14.40           C  
ANISOU 1575  C   ILE A 215     1031   2201   2238     99    -20   -659       C  
ATOM   1576  O   ILE A 215       6.101  23.026  66.932  1.00 15.32           O  
ANISOU 1576  O   ILE A 215     1156   2266   2399    126    -23   -660       O  
ATOM   1577  CB  ILE A 215       6.492  19.801  66.037  1.00 15.05           C  
ANISOU 1577  CB  ILE A 215     1176   2296   2246     -9     29   -611       C  
ATOM   1578  CG1 ILE A 215       6.833  18.460  66.701  1.00 12.41           C  
ANISOU 1578  CG1 ILE A 215      882   1964   1868    -76     76   -606       C  
ATOM   1579  CG2 ILE A 215       7.779  20.529  65.666  1.00 14.54           C  
ANISOU 1579  CG2 ILE A 215     1130   2177   2218     15     18   -569       C  
ATOM   1580  CD1 ILE A 215       7.416  17.431  65.727  1.00 15.93           C  
ANISOU 1580  CD1 ILE A 215     1354   2409   2288   -108     81   -573       C  
ATOM   1581  N   PHE A 216       4.615  22.230  65.434  1.00 13.15           N  
ANISOU 1581  N   PHE A 216      836   2080   2079    141    -59   -662       N  
ATOM   1582  CA  PHE A 216       4.364  23.542  64.831  1.00 15.48           C  
ANISOU 1582  CA  PHE A 216     1106   2354   2421    232   -107   -655       C  
ATOM   1583  C   PHE A 216       3.840  24.573  65.836  1.00 15.30           C  
ANISOU 1583  C   PHE A 216     1066   2310   2435    270   -109   -700       C  
ATOM   1584  O   PHE A 216       4.200  25.745  65.766  1.00 15.24           O  
ANISOU 1584  O   PHE A 216     1064   2240   2485    333   -130   -689       O  
ATOM   1585  CB  PHE A 216       3.343  23.448  63.691  1.00 14.85           C  
ANISOU 1585  CB  PHE A 216      988   2336   2318    278   -155   -659       C  
ATOM   1586  CG  PHE A 216       3.814  22.689  62.476  1.00 16.02           C  
ANISOU 1586  CG  PHE A 216     1148   2509   2431    266   -171   -621       C  
ATOM   1587  CD1 PHE A 216       5.113  22.232  62.365  1.00 18.01           C  
ANISOU 1587  CD1 PHE A 216     1439   2723   2681    223   -142   -579       C  
ATOM   1588  CD2 PHE A 216       2.928  22.447  61.431  1.00 19.11           C  
ANISOU 1588  CD2 PHE A 216     1507   2968   2786    304   -218   -633       C  
ATOM   1589  CE1 PHE A 216       5.527  21.537  61.242  1.00 21.16           C  
ANISOU 1589  CE1 PHE A 216     1844   3152   3043    216   -157   -550       C  
ATOM   1590  CE2 PHE A 216       3.334  21.757  60.301  1.00 17.83           C  
ANISOU 1590  CE2 PHE A 216     1356   2838   2582    299   -238   -606       C  
ATOM   1591  CZ  PHE A 216       4.636  21.305  60.203  1.00 19.02           C  
ANISOU 1591  CZ  PHE A 216     1544   2952   2730    256   -207   -565       C  
ATOM   1592  N   ARG A 217       2.960  24.153  66.743  1.00 13.20           N  
ANISOU 1592  N   ARG A 217      780   2093   2142    237    -85   -752       N  
ATOM   1593  CA  ARG A 217       2.389  25.086  67.712  1.00 13.77           C  
ANISOU 1593  CA  ARG A 217      831   2159   2242    275    -86   -803       C  
ATOM   1594  C   ARG A 217       3.430  25.556  68.712  1.00 18.71           C  
ANISOU 1594  C   ARG A 217     1492   2724   2894    260    -63   -809       C  
ATOM   1595  O   ARG A 217       3.291  26.614  69.323  1.00 18.83           O  
ANISOU 1595  O   ARG A 217     1498   2708   2950    305    -74   -846       O  
ATOM   1596  CB  ARG A 217       1.186  24.471  68.429  1.00 14.18           C  
ANISOU 1596  CB  ARG A 217      846   2286   2257    243    -61   -857       C  
ATOM   1597  CG  ARG A 217      -0.044  24.424  67.543  1.00 14.93           C  
ANISOU 1597  CG  ARG A 217      889   2439   2344    279    -96   -874       C  
ATOM   1598  CD  ARG A 217      -1.321  24.195  68.329  1.00 17.95           C  
ANISOU 1598  CD  ARG A 217     1221   2888   2711    264    -74   -939       C  
ATOM   1599  NE  ARG A 217      -1.414  22.844  68.865  1.00 21.26           N  
ANISOU 1599  NE  ARG A 217     1647   3341   3090    172    -19   -946       N  
ATOM   1600  CZ  ARG A 217      -1.945  21.817  68.211  1.00 23.79           C  
ANISOU 1600  CZ  ARG A 217     1948   3705   3387    130    -15   -950       C  
ATOM   1601  NH1 ARG A 217      -2.428  21.984  66.986  1.00 18.77           N  
ANISOU 1601  NH1 ARG A 217     1281   3094   2755    173    -66   -950       N  
ATOM   1602  NH2 ARG A 217      -2.002  20.625  68.786  1.00 19.42           N  
ANISOU 1602  NH2 ARG A 217     1405   3168   2805     48     40   -954       N  
ATOM   1603  N   THR A 218       4.483  24.767  68.865  1.00 16.67           N  
ANISOU 1603  N   THR A 218     1272   2448   2613    198    -33   -778       N  
ATOM   1604  CA  THR A 218       5.551  25.110  69.799  1.00 16.50           C  
ANISOU 1604  CA  THR A 218     1281   2378   2610    181    -16   -789       C  
ATOM   1605  C   THR A 218       6.678  25.886  69.119  1.00 20.79           C  
ANISOU 1605  C   THR A 218     1843   2838   3219    207    -35   -752       C  
ATOM   1606  O   THR A 218       7.114  26.930  69.611  1.00 25.82           O  
ANISOU 1606  O   THR A 218     2482   3413   3915    236    -45   -779       O  
ATOM   1607  CB  THR A 218       6.110  23.851  70.477  1.00 18.33           C  
ANISOU 1607  CB  THR A 218     1546   2638   2782    107     27   -779       C  
ATOM   1608  OG1 THR A 218       5.075  23.228  71.246  1.00 22.77           O  
ANISOU 1608  OG1 THR A 218     2088   3266   3296     84     53   -815       O  
ATOM   1609  CG2 THR A 218       7.291  24.200  71.398  1.00 22.93           C  
ANISOU 1609  CG2 THR A 218     2155   3180   3379     96     37   -794       C  
ATOM   1610  N   LEU A 219       7.140  25.386  67.981  1.00 15.20           N  
ANISOU 1610  N   LEU A 219     1146   2124   2506    197    -40   -692       N  
ATOM   1611  CA  LEU A 219       8.304  25.960  67.314  1.00 17.88           C  
ANISOU 1611  CA  LEU A 219     1500   2384   2908    213    -47   -648       C  
ATOM   1612  C   LEU A 219       7.935  26.864  66.139  1.00 20.79           C  
ANISOU 1612  C   LEU A 219     1854   2713   3332    297    -85   -614       C  
ATOM   1613  O   LEU A 219       8.812  27.440  65.491  1.00 18.32           O  
ANISOU 1613  O   LEU A 219     1595   2314   3052    303    -85   -547       O  
ATOM   1614  CB  LEU A 219       9.235  24.847  66.839  1.00 20.51           C  
ANISOU 1614  CB  LEU A 219     1858   2733   3201    152    -22   -599       C  
ATOM   1615  CG  LEU A 219       9.706  23.889  67.933  1.00 20.98           C  
ANISOU 1615  CG  LEU A 219     1948   2821   3201     85     13   -618       C  
ATOM   1616  CD1 LEU A 219      10.521  22.760  67.318  1.00 21.96           C  
ANISOU 1616  CD1 LEU A 219     2102   2958   3283     37     33   -565       C  
ATOM   1617  CD2 LEU A 219      10.520  24.639  68.982  1.00 23.02           C  
ANISOU 1617  CD2 LEU A 219     2213   3031   3504     83     17   -655       C  
ATOM   1618  N   GLY A 220       6.639  26.988  65.873  1.00 17.52           N  
ANISOU 1618  N   GLY A 220     1415   2352   2891    344   -113   -632       N  
ATOM   1619  CA  GLY A 220       6.163  27.761  64.743  1.00 15.20           C  
ANISOU 1619  CA  GLY A 220     1115   2033   2628    439   -159   -594       C  
ATOM   1620  C   GLY A 220       6.080  26.876  63.516  1.00 15.98           C  
ANISOU 1620  C   GLY A 220     1222   2190   2659    431   -173   -540       C  
ATOM   1621  O   GLY A 220       6.854  25.930  63.377  1.00 19.68           O  
ANISOU 1621  O   GLY A 220     1718   2673   3088    355   -143   -512       O  
ATOM   1622  N   THR A 221       5.136  27.163  62.629  1.00 18.27           N  
ANISOU 1622  N   THR A 221     1491   2519   2930    511   -222   -530       N  
ATOM   1623  CA  THR A 221       5.082  26.440  61.366  1.00 18.41           C  
ANISOU 1623  CA  THR A 221     1526   2591   2876    513   -244   -479       C  
ATOM   1624  C   THR A 221       6.269  26.880  60.515  1.00 20.79           C  
ANISOU 1624  C   THR A 221     1924   2800   3175    518   -230   -368       C  
ATOM   1625  O   THR A 221       6.451  28.072  60.263  1.00 22.75           O  
ANISOU 1625  O   THR A 221     2217   2958   3470    584   -239   -317       O  
ATOM   1626  CB  THR A 221       3.778  26.704  60.618  1.00 20.66           C  
ANISOU 1626  CB  THR A 221     1762   2951   3136    611   -310   -499       C  
ATOM   1627  OG1 THR A 221       2.677  26.333  61.455  1.00 18.96           O  
ANISOU 1627  OG1 THR A 221     1494   2803   2905    570   -300   -581       O  
ATOM   1628  CG2 THR A 221       3.724  25.889  59.327  1.00 21.57           C  
ANISOU 1628  CG2 THR A 221     1892   3135   3167    612   -338   -460       C  
ATOM   1629  N   PRO A 222       7.093  25.919  60.086  1.00 19.93           N  
ANISOU 1629  N   PRO A 222     1850   2708   3016    447   -200   -331       N  
ATOM   1630  CA  PRO A 222       8.309  26.258  59.341  1.00 20.28           C  
ANISOU 1630  CA  PRO A 222     1978   2672   3057    440   -173   -229       C  
ATOM   1631  C   PRO A 222       7.996  26.750  57.933  1.00 23.54           C  
ANISOU 1631  C   PRO A 222     2434   3087   3423    532   -210   -150       C  
ATOM   1632  O   PRO A 222       7.036  26.287  57.308  1.00 25.38           O  
ANISOU 1632  O   PRO A 222     2632   3417   3593    577   -259   -176       O  
ATOM   1633  CB  PRO A 222       9.064  24.924  59.283  1.00 21.48           C  
ANISOU 1633  CB  PRO A 222     2139   2867   3156    350   -137   -230       C  
ATOM   1634  CG  PRO A 222       8.002  23.895  59.341  1.00 23.82           C  
ANISOU 1634  CG  PRO A 222     2372   3276   3404    337   -164   -306       C  
ATOM   1635  CD  PRO A 222       6.950  24.466  60.277  1.00 17.32           C  
ANISOU 1635  CD  PRO A 222     1482   2467   2631    370   -186   -382       C  
ATOM   1636  N   ASP A 223       8.796  27.699  57.452  1.00 29.82           N  
ANISOU 1636  N   ASP A 223     3302   3778   4249    559   -186    -55       N  
ATOM   1637  CA  ASP A 223       8.688  28.183  56.079  1.00 28.60           C  
ANISOU 1637  CA  ASP A 223     3209   3617   4040    646   -208     42       C  
ATOM   1638  C   ASP A 223      10.036  28.054  55.374  1.00 25.88           C  
ANISOU 1638  C   ASP A 223     2939   3222   3671    599   -148    140       C  
ATOM   1639  O   ASP A 223      11.000  27.566  55.964  1.00 20.82           O  
ANISOU 1639  O   ASP A 223     2294   2559   3060    502    -97    123       O  
ATOM   1640  CB  ASP A 223       8.191  29.636  56.033  1.00 30.32           C  
ANISOU 1640  CB  ASP A 223     3454   3747   4318    748   -232     80       C  
ATOM   1641  CG  ASP A 223       9.031  30.584  56.885  1.00 36.17           C  
ANISOU 1641  CG  ASP A 223     4224   4343   5177    705   -181     93       C  
ATOM   1642  OD1 ASP A 223      10.204  30.277  57.185  1.00 34.33           O  
ANISOU 1642  OD1 ASP A 223     4009   4068   4968    608   -123    107       O  
ATOM   1643  OD2 ASP A 223       8.510  31.655  57.251  1.00 43.90           O  
ANISOU 1643  OD2 ASP A 223     5205   5249   6225    773   -202     82       O  
ATOM   1644  N   GLU A 224      10.094  28.507  54.124  1.00 28.93           N  
ANISOU 1644  N   GLU A 224     3394   3598   4001    673   -152    244       N  
ATOM   1645  CA  GLU A 224      11.307  28.403  53.313  1.00 28.22           C  
ANISOU 1645  CA  GLU A 224     3375   3473   3876    638    -90    344       C  
ATOM   1646  C   GLU A 224      12.487  29.170  53.905  1.00 30.38           C  
ANISOU 1646  C   GLU A 224     3678   3608   4259    570    -16    386       C  
ATOM   1647  O   GLU A 224      13.646  28.811  53.679  1.00 28.16           O  
ANISOU 1647  O   GLU A 224     3420   3309   3971    500     47    428       O  
ATOM   1648  CB  GLU A 224      11.033  28.885  51.886  1.00 31.49           C  
ANISOU 1648  CB  GLU A 224     3861   3900   4203    747   -108    454       C  
ATOM   1649  CG  GLU A 224      10.255  27.888  51.049  1.00 32.97           C  
ANISOU 1649  CG  GLU A 224     4027   4241   4260    795   -169    418       C  
ATOM   1650  CD  GLU A 224      11.023  26.602  50.825  1.00 34.88           C  
ANISOU 1650  CD  GLU A 224     4261   4550   4442    707   -133    394       C  
ATOM   1651  OE1 GLU A 224      12.267  26.667  50.690  1.00 35.01           O  
ANISOU 1651  OE1 GLU A 224     4323   4503   4476    649    -55    462       O  
ATOM   1652  OE2 GLU A 224      10.389  25.524  50.785  1.00 30.99           O  
ANISOU 1652  OE2 GLU A 224     3713   4171   3889    695   -180    304       O  
ATOM   1653  N   VAL A 225      12.192  30.229  54.652  1.00 31.29           N  
ANISOU 1653  N   VAL A 225     3787   3626   4475    593    -24    367       N  
ATOM   1654  CA  VAL A 225      13.239  31.009  55.303  1.00 32.17           C  
ANISOU 1654  CA  VAL A 225     3917   3603   4705    525     38    385       C  
ATOM   1655  C   VAL A 225      13.888  30.204  56.422  1.00 31.32           C  
ANISOU 1655  C   VAL A 225     3744   3525   4632    414     59    288       C  
ATOM   1656  O   VAL A 225      15.109  30.059  56.471  1.00 29.61           O  
ANISOU 1656  O   VAL A 225     3537   3271   4444    335    119    314       O  
ATOM   1657  CB  VAL A 225      12.695  32.331  55.873  1.00 33.81           C  
ANISOU 1657  CB  VAL A 225     4133   3697   5016    581     18    371       C  
ATOM   1658  CG1 VAL A 225      13.812  33.117  56.552  1.00 36.81           C  
ANISOU 1658  CG1 VAL A 225     4527   3934   5525    500     82    376       C  
ATOM   1659  CG2 VAL A 225      12.056  33.153  54.776  1.00 38.11           C  
ANISOU 1659  CG2 VAL A 225     4750   4205   5525    704     -4    476       C  
ATOM   1660  N   VAL A 226      13.058  29.666  57.310  1.00 28.06           N  
ANISOU 1660  N   VAL A 226     3263   3186   4212    413     11    177       N  
ATOM   1661  CA  VAL A 226      13.532  28.881  58.448  1.00 24.32           C  
ANISOU 1661  CA  VAL A 226     2734   2748   3760    323     25     85       C  
ATOM   1662  C   VAL A 226      14.143  27.547  58.014  1.00 26.25           C  
ANISOU 1662  C   VAL A 226     2976   3079   3920    268     48     96       C  
ATOM   1663  O   VAL A 226      15.137  27.089  58.581  1.00 26.88           O  
ANISOU 1663  O   VAL A 226     3040   3152   4023    192     85     73       O  
ATOM   1664  CB  VAL A 226      12.377  28.626  59.450  1.00 40.33           C  
ANISOU 1664  CB  VAL A 226     4694   4839   5791    343    -24    -26       C  
ATOM   1665  CG1 VAL A 226      12.702  27.483  60.394  1.00 39.93           C  
ANISOU 1665  CG1 VAL A 226     4595   4857   5718    262    -11   -105       C  
ATOM   1666  CG2 VAL A 226      12.053  29.901  60.223  1.00 40.00           C  
ANISOU 1666  CG2 VAL A 226     4646   4702   5850    379    -36    -62       C  
ATOM   1667  N   TRP A 227      13.550  26.930  56.997  1.00 22.41           N  
ANISOU 1667  N   TRP A 227     2504   2675   3335    314     23    126       N  
ATOM   1668  CA  TRP A 227      13.947  25.592  56.572  1.00 20.48           C  
ANISOU 1668  CA  TRP A 227     2257   2517   3008    271     36    120       C  
ATOM   1669  C   TRP A 227      13.837  25.487  55.062  1.00 21.99           C  
ANISOU 1669  C   TRP A 227     2500   2748   3108    329     31    202       C  
ATOM   1670  O   TRP A 227      12.800  25.077  54.542  1.00 19.55           O  
ANISOU 1670  O   TRP A 227     2177   2521   2727    383    -22    177       O  
ATOM   1671  CB  TRP A 227      13.033  24.554  57.236  1.00 19.38           C  
ANISOU 1671  CB  TRP A 227     2057   2471   2835    254     -3     17       C  
ATOM   1672  CG  TRP A 227      13.422  23.114  57.034  1.00 19.64           C  
ANISOU 1672  CG  TRP A 227     2086   2577   2799    201     13     -6       C  
ATOM   1673  CD1 TRP A 227      14.470  22.628  56.301  1.00 20.19           C  
ANISOU 1673  CD1 TRP A 227     2196   2649   2827    177     53     49       C  
ATOM   1674  CD2 TRP A 227      12.746  21.972  57.575  1.00 16.47           C  
ANISOU 1674  CD2 TRP A 227     1639   2252   2366    168     -7    -92       C  
ATOM   1675  NE1 TRP A 227      14.484  21.253  56.355  1.00 19.65           N  
ANISOU 1675  NE1 TRP A 227     2114   2650   2705    137     54     -1       N  
ATOM   1676  CE2 TRP A 227      13.438  20.828  57.133  1.00 19.42           C  
ANISOU 1676  CE2 TRP A 227     2035   2660   2683    127     19    -85       C  
ATOM   1677  CE3 TRP A 227      11.619  21.810  58.387  1.00 19.18           C  
ANISOU 1677  CE3 TRP A 227     1926   2635   2727    168    -38   -174       C  
ATOM   1678  CZ2 TRP A 227      13.042  19.537  57.482  1.00 18.65           C  
ANISOU 1678  CZ2 TRP A 227     1911   2623   2551     85     15   -153       C  
ATOM   1679  CZ3 TRP A 227      11.225  20.526  58.731  1.00 19.82           C  
ANISOU 1679  CZ3 TRP A 227     1976   2781   2771    120    -37   -239       C  
ATOM   1680  CH2 TRP A 227      11.937  19.407  58.280  1.00 20.51           C  
ANISOU 1680  CH2 TRP A 227     2095   2890   2808     78    -11   -227       C  
ATOM   1681  N   PRO A 228      14.904  25.872  54.348  1.00 23.90           N  
ANISOU 1681  N   PRO A 228     2796   2936   3348    319     87    297       N  
ATOM   1682  CA  PRO A 228      14.889  25.846  52.880  1.00 24.88           C  
ANISOU 1682  CA  PRO A 228     2979   3099   3374    380     92    386       C  
ATOM   1683  C   PRO A 228      14.505  24.463  52.374  1.00 21.56           C  
ANISOU 1683  C   PRO A 228     2541   2805   2844    381     60    334       C  
ATOM   1684  O   PRO A 228      15.035  23.474  52.868  1.00 21.45           O  
ANISOU 1684  O   PRO A 228     2498   2821   2831    309     81    279       O  
ATOM   1685  CB  PRO A 228      16.342  26.168  52.509  1.00 30.53           C  
ANISOU 1685  CB  PRO A 228     3738   3747   4117    332    178    473       C  
ATOM   1686  CG  PRO A 228      16.843  26.983  53.663  1.00 32.06           C  
ANISOU 1686  CG  PRO A 228     3905   3831   4447    276    205    448       C  
ATOM   1687  CD  PRO A 228      16.171  26.402  54.886  1.00 26.59           C  
ANISOU 1687  CD  PRO A 228     3143   3181   3780    250    153    323       C  
ATOM   1688  N   GLY A 229      13.562  24.401  51.441  1.00 25.38           N  
ANISOU 1688  N   GLY A 229     3041   3361   3240    465      5    346       N  
ATOM   1689  CA  GLY A 229      13.132  23.136  50.876  1.00 26.22           C  
ANISOU 1689  CA  GLY A 229     3131   3587   3246    468    -31    288       C  
ATOM   1690  C   GLY A 229      11.908  22.527  51.541  1.00 29.03           C  
ANISOU 1690  C   GLY A 229     3411   4009   3611    461    -98    169       C  
ATOM   1691  O   GLY A 229      11.310  21.590  51.006  1.00 26.56           O  
ANISOU 1691  O   GLY A 229     3078   3794   3220    472   -139    112       O  
ATOM   1692  N   VAL A 230      11.523  23.050  52.702  1.00 21.64           N  
ANISOU 1692  N   VAL A 230     2431   3022   2770    442   -106    125       N  
ATOM   1693  CA  VAL A 230      10.460  22.412  53.485  1.00 23.25           C  
ANISOU 1693  CA  VAL A 230     2557   3287   2991    418   -151     10       C  
ATOM   1694  C   VAL A 230       9.146  22.304  52.709  1.00 24.39           C  
ANISOU 1694  C   VAL A 230     2670   3528   3067    497   -229    -27       C  
ATOM   1695  O   VAL A 230       8.454  21.289  52.796  1.00 24.77           O  
ANISOU 1695  O   VAL A 230     2663   3660   3087    466   -259   -119       O  
ATOM   1696  CB  VAL A 230      10.233  23.091  54.862  1.00 17.88           C  
ANISOU 1696  CB  VAL A 230     1835   2542   2418    395   -143    -31       C  
ATOM   1697  CG1 VAL A 230       9.680  24.502  54.702  1.00 18.21           C  
ANISOU 1697  CG1 VAL A 230     1889   2534   2496    487   -174     13       C  
ATOM   1698  CG2 VAL A 230       9.297  22.240  55.728  1.00 18.54           C  
ANISOU 1698  CG2 VAL A 230     1839   2694   2513    352   -168   -146       C  
ATOM   1699  N   THR A 231       8.826  23.328  51.922  1.00 22.22           N  
ANISOU 1699  N   THR A 231     2433   3244   2766    600   -261     45       N  
ATOM   1700  CA  THR A 231       7.560  23.347  51.193  1.00 24.28           C  
ANISOU 1700  CA  THR A 231     2660   3603   2960    693   -346      9       C  
ATOM   1701  C   THR A 231       7.559  22.396  49.992  1.00 26.61           C  
ANISOU 1701  C   THR A 231     2975   4001   3135    709   -372      1       C  
ATOM   1702  O   THR A 231       6.526  22.204  49.352  1.00 35.93           O  
ANISOU 1702  O   THR A 231     4117   5284   4251    777   -449    -49       O  
ATOM   1703  CB  THR A 231       7.157  24.775  50.744  1.00 32.77           C  
ANISOU 1703  CB  THR A 231     3775   4636   4041    817   -378     91       C  
ATOM   1704  OG1 THR A 231       8.092  25.268  49.778  1.00 36.40           O  
ANISOU 1704  OG1 THR A 231     4336   5044   4448    855   -338    222       O  
ATOM   1705  CG2 THR A 231       7.118  25.714  51.932  1.00 33.63           C  
ANISOU 1705  CG2 THR A 231     3864   4641   4274    805   -356     84       C  
ATOM   1706  N   SER A 232       8.710  21.795  49.708  1.00 26.55           N  
ANISOU 1706  N   SER A 232     3019   3970   3097    648   -309     40       N  
ATOM   1707  CA  SER A 232       8.841  20.832  48.618  1.00 31.64           C  
ANISOU 1707  CA  SER A 232     3687   4706   3628    656   -325     25       C  
ATOM   1708  C   SER A 232       8.897  19.395  49.128  1.00 31.37           C  
ANISOU 1708  C   SER A 232     3606   4707   3607    550   -311    -84       C  
ATOM   1709  O   SER A 232       9.035  18.456  48.346  1.00 30.10           O  
ANISOU 1709  O   SER A 232     3460   4613   3365    543   -320   -116       O  
ATOM   1710  CB  SER A 232      10.097  21.127  47.786  1.00 30.18           C  
ANISOU 1710  CB  SER A 232     3599   4479   3388    674   -260    147       C  
ATOM   1711  OG  SER A 232       9.985  22.375  47.124  1.00 42.15           O  
ANISOU 1711  OG  SER A 232     5172   5968   4875    780   -272    255       O  
ATOM   1712  N   MET A 233       8.799  19.217  50.440  1.00 26.50           N  
ANISOU 1712  N   MET A 233     2938   4042   3090    471   -287   -139       N  
ATOM   1713  CA  MET A 233       8.891  17.876  51.009  1.00 23.83           C  
ANISOU 1713  CA  MET A 233     2566   3720   2770    371   -264   -228       C  
ATOM   1714  C   MET A 233       7.635  17.064  50.707  1.00 20.37           C  
ANISOU 1714  C   MET A 233     2059   3385   2298    370   -331   -343       C  
ATOM   1715  O   MET A 233       6.546  17.626  50.606  1.00 22.47           O  
ANISOU 1715  O   MET A 233     2272   3701   2565    430   -394   -373       O  
ATOM   1716  CB  MET A 233       9.194  17.960  52.503  1.00 25.37           C  
ANISOU 1716  CB  MET A 233     2734   3835   3070    295   -214   -243       C  
ATOM   1717  CG  MET A 233      10.488  18.715  52.747  1.00 29.46           C  
ANISOU 1717  CG  MET A 233     3312   4258   3624    290   -152   -144       C  
ATOM   1718  SD  MET A 233      11.044  18.693  54.447  1.00 33.87           S  
ANISOU 1718  SD  MET A 233     3845   4735   4288    203    -97   -169       S  
ATOM   1719  CE  MET A 233      11.586  16.994  54.587  1.00 41.78           C  
ANISOU 1719  CE  MET A 233     4855   5761   5259    121    -62   -222       C  
ATOM   1720  N   PRO A 234       7.794  15.740  50.530  1.00 23.83           N  
ANISOU 1720  N   PRO A 234     2495   3852   2708    304   -319   -410       N  
ATOM   1721  CA  PRO A 234       6.730  14.869  50.017  1.00 25.57           C  
ANISOU 1721  CA  PRO A 234     2656   4171   2889    296   -381   -524       C  
ATOM   1722  C   PRO A 234       5.416  14.988  50.778  1.00 23.67           C  
ANISOU 1722  C   PRO A 234     2313   3966   2716    277   -419   -610       C  
ATOM   1723  O   PRO A 234       4.350  14.975  50.158  1.00 25.84           O  
ANISOU 1723  O   PRO A 234     2527   4336   2953    325   -495   -678       O  
ATOM   1724  CB  PRO A 234       7.320  13.466  50.193  1.00 29.74           C  
ANISOU 1724  CB  PRO A 234     3205   4674   3421    200   -332   -575       C  
ATOM   1725  CG  PRO A 234       8.781  13.672  50.068  1.00 31.10           C  
ANISOU 1725  CG  PRO A 234     3466   4777   3575    207   -268   -471       C  
ATOM   1726  CD  PRO A 234       9.041  14.987  50.764  1.00 29.93           C  
ANISOU 1726  CD  PRO A 234     3322   4564   3485    235   -245   -384       C  
ATOM   1727  N   ASP A 235       5.488  15.114  52.100  1.00 19.08           N  
ANISOU 1727  N   ASP A 235     1707   3316   2225    214   -367   -609       N  
ATOM   1728  CA  ASP A 235       4.275  15.167  52.909  1.00 20.18           C  
ANISOU 1728  CA  ASP A 235     1746   3491   2429    189   -388   -693       C  
ATOM   1729  C   ASP A 235       3.980  16.551  53.492  1.00 25.60           C  
ANISOU 1729  C   ASP A 235     2412   4151   3163    255   -398   -646       C  
ATOM   1730  O   ASP A 235       3.154  16.690  54.394  1.00 23.17           O  
ANISOU 1730  O   ASP A 235     2044   3843   2917    228   -388   -696       O  
ATOM   1731  CB  ASP A 235       4.322  14.103  54.009  1.00 23.18           C  
ANISOU 1731  CB  ASP A 235     2106   3830   2873     64   -321   -749       C  
ATOM   1732  CG  ASP A 235       4.293  12.695  53.445  1.00 33.65           C  
ANISOU 1732  CG  ASP A 235     3451   5170   4167      1   -310   -810       C  
ATOM   1733  OD1 ASP A 235       3.504  12.452  52.511  1.00 39.05           O  
ANISOU 1733  OD1 ASP A 235     4111   5917   4808     34   -361   -861       O  
ATOM   1734  OD2 ASP A 235       5.066  11.841  53.917  1.00 34.49           O  
ANISOU 1734  OD2 ASP A 235     3596   5219   4290    -76   -252   -807       O  
ATOM   1735  N   TYR A 236       4.652  17.576  52.973  1.00 22.17           N  
ANISOU 1735  N   TYR A 236     2048   3674   2700    338   -403   -541       N  
ATOM   1736  CA  TYR A 236       4.267  18.947  53.282  1.00 20.30           C  
ANISOU 1736  CA  TYR A 236     1799   3413   2503    420   -427   -500       C  
ATOM   1737  C   TYR A 236       2.954  19.262  52.575  1.00 23.60           C  
ANISOU 1737  C   TYR A 236     2147   3936   2884    512   -519   -554       C  
ATOM   1738  O   TYR A 236       2.750  18.860  51.428  1.00 22.98           O  
ANISOU 1738  O   TYR A 236     2076   3934   2720    554   -570   -568       O  
ATOM   1739  CB  TYR A 236       5.347  19.941  52.832  1.00 23.27           C  
ANISOU 1739  CB  TYR A 236     2275   3705   2862    481   -402   -369       C  
ATOM   1740  CG  TYR A 236       4.952  21.386  53.056  1.00 29.63           C  
ANISOU 1740  CG  TYR A 236     3077   4469   3711    572   -427   -323       C  
ATOM   1741  CD1 TYR A 236       5.246  22.029  54.253  1.00 27.87           C  
ANISOU 1741  CD1 TYR A 236     2851   4158   3582    541   -382   -314       C  
ATOM   1742  CD2 TYR A 236       4.271  22.104  52.074  1.00 32.20           C  
ANISOU 1742  CD2 TYR A 236     3407   4845   3982    696   -498   -294       C  
ATOM   1743  CE1 TYR A 236       4.872  23.350  54.467  1.00 29.88           C  
ANISOU 1743  CE1 TYR A 236     3105   4365   3883    626   -404   -281       C  
ATOM   1744  CE2 TYR A 236       3.895  23.421  52.279  1.00 32.83           C  
ANISOU 1744  CE2 TYR A 236     3491   4877   4106    788   -521   -252       C  
ATOM   1745  CZ  TYR A 236       4.198  24.038  53.474  1.00 33.41           C  
ANISOU 1745  CZ  TYR A 236     3560   4852   4281    750   -472   -247       C  
ATOM   1746  OH  TYR A 236       3.823  25.347  53.672  1.00 40.10           O  
ANISOU 1746  OH  TYR A 236     4415   5643   5178    843   -494   -212       O  
ATOM   1747  N   LYS A 237       2.067  19.985  53.257  1.00 18.83           N  
ANISOU 1747  N   LYS A 237     1483   3334   2340    544   -536   -587       N  
ATOM   1748  CA  LYS A 237       0.807  20.432  52.660  1.00 18.71           C  
ANISOU 1748  CA  LYS A 237     1437   3379   2295    624   -599   -619       C  
ATOM   1749  C   LYS A 237       0.653  21.938  52.841  1.00 20.19           C  
ANISOU 1749  C   LYS A 237     1638   3518   2514    734   -622   -554       C  
ATOM   1750  O   LYS A 237       0.795  22.446  53.954  1.00 22.82           O  
ANISOU 1750  O   LYS A 237     1961   3781   2930    707   -579   -551       O  
ATOM   1751  CB  LYS A 237      -0.393  19.742  53.321  1.00 27.80           C  
ANISOU 1751  CB  LYS A 237     2517   4561   3485    542   -578   -729       C  
ATOM   1752  CG  LYS A 237      -0.281  18.233  53.465  1.00 37.37           C  
ANISOU 1752  CG  LYS A 237     3721   5784   4694    417   -533   -792       C  
ATOM   1753  CD  LYS A 237      -0.529  17.517  52.149  1.00 45.60           C  
ANISOU 1753  CD  LYS A 237     4764   6905   5657    438   -583   -829       C  
ATOM   1754  CE  LYS A 237      -0.676  16.018  52.373  1.00 50.98           C  
ANISOU 1754  CE  LYS A 237     5429   7587   6355    315   -535   -907       C  
ATOM   1755  NZ  LYS A 237      -0.748  15.263  51.089  1.00 53.40           N  
ANISOU 1755  NZ  LYS A 237     5743   7959   6588    330   -579   -947       N  
ATOM   1756  N   PRO A 238       0.338  22.660  51.756  1.00 21.05           N  
ANISOU 1756  N   PRO A 238     1779   3659   2559    860   -687   -504       N  
ATOM   1757  CA  PRO A 238       0.161  24.114  51.865  1.00 24.79           C  
ANISOU 1757  CA  PRO A 238     2281   4072   3067    972   -707   -435       C  
ATOM   1758  C   PRO A 238      -1.000  24.495  52.790  1.00 24.62           C  
ANISOU 1758  C   PRO A 238     2187   4052   3116    960   -706   -514       C  
ATOM   1759  O   PRO A 238      -1.086  25.649  53.216  1.00 25.26           O  
ANISOU 1759  O   PRO A 238     2284   4065   3250   1028   -706   -473       O  
ATOM   1760  CB  PRO A 238      -0.125  24.548  50.419  1.00 32.74           C  
ANISOU 1760  CB  PRO A 238     3339   5130   3972   1098   -775   -376       C  
ATOM   1761  CG  PRO A 238      -0.504  23.298  49.696  1.00 33.35           C  
ANISOU 1761  CG  PRO A 238     3384   5317   3972   1047   -800   -456       C  
ATOM   1762  CD  PRO A 238       0.259  22.197  50.361  1.00 27.15           C  
ANISOU 1762  CD  PRO A 238     2581   4514   3220    909   -739   -496       C  
ATOM   1763  N   SER A 239      -1.870  23.534  53.095  1.00 21.08           N  
ANISOU 1763  N   SER A 239     1666   3675   2669    874   -699   -623       N  
ATOM   1764  CA  SER A 239      -2.984  23.756  54.022  1.00 23.13           C  
ANISOU 1764  CA  SER A 239     1856   3946   2987    853   -686   -701       C  
ATOM   1765  C   SER A 239      -2.586  23.788  55.507  1.00 20.03           C  
ANISOU 1765  C   SER A 239     1456   3477   2678    766   -609   -712       C  
ATOM   1766  O   SER A 239      -3.426  24.108  56.353  1.00 20.04           O  
ANISOU 1766  O   SER A 239     1411   3482   2724    758   -594   -766       O  
ATOM   1767  CB  SER A 239      -4.063  22.685  53.821  1.00 22.76           C  
ANISOU 1767  CB  SER A 239     1737   3996   2914    792   -697   -809       C  
ATOM   1768  OG  SER A 239      -3.569  21.413  54.202  1.00 26.18           O  
ANISOU 1768  OG  SER A 239     2171   4422   3355    660   -638   -843       O  
ATOM   1769  N   PHE A 240      -1.338  23.441  55.823  1.00 19.10           N  
ANISOU 1769  N   PHE A 240     1384   3298   2574    704   -561   -667       N  
ATOM   1770  CA  PHE A 240      -0.857  23.482  57.208  1.00 17.90           C  
ANISOU 1770  CA  PHE A 240     1235   3075   2492    626   -489   -675       C  
ATOM   1771  C   PHE A 240      -1.211  24.827  57.836  1.00 19.22           C  
ANISOU 1771  C   PHE A 240     1398   3190   2714    703   -496   -663       C  
ATOM   1772  O   PHE A 240      -0.975  25.875  57.229  1.00 18.78           O  
ANISOU 1772  O   PHE A 240     1379   3094   2663    813   -537   -597       O  
ATOM   1773  CB  PHE A 240       0.665  23.317  57.270  1.00 19.03           C  
ANISOU 1773  CB  PHE A 240     1435   3150   2645    590   -452   -609       C  
ATOM   1774  CG  PHE A 240       1.153  21.908  57.073  1.00 17.54           C  
ANISOU 1774  CG  PHE A 240     1253   2993   2418    489   -421   -629       C  
ATOM   1775  CD1 PHE A 240       0.294  20.825  57.182  1.00 18.78           C  
ANISOU 1775  CD1 PHE A 240     1373   3209   2554    413   -408   -706       C  
ATOM   1776  CD2 PHE A 240       2.492  21.674  56.792  1.00 18.59           C  
ANISOU 1776  CD2 PHE A 240     1432   3089   2541    471   -401   -571       C  
ATOM   1777  CE1 PHE A 240       0.761  19.532  57.014  1.00 20.21           C  
ANISOU 1777  CE1 PHE A 240     1571   3402   2708    322   -376   -723       C  
ATOM   1778  CE2 PHE A 240       2.963  20.385  56.618  1.00 20.96           C  
ANISOU 1778  CE2 PHE A 240     1742   3414   2807    381   -372   -591       C  
ATOM   1779  CZ  PHE A 240       2.100  19.315  56.734  1.00 19.65           C  
ANISOU 1779  CZ  PHE A 240     1548   3295   2623    307   -359   -666       C  
ATOM   1780  N   PRO A 241      -1.820  24.809  59.032  1.00 19.56           N  
ANISOU 1780  N   PRO A 241     1404   3232   2798    650   -455   -726       N  
ATOM   1781  CA  PRO A 241      -2.034  26.086  59.720  1.00 19.55           C  
ANISOU 1781  CA  PRO A 241     1403   3174   2852    718   -457   -721       C  
ATOM   1782  C   PRO A 241      -0.697  26.761  60.015  1.00 17.77           C  
ANISOU 1782  C   PRO A 241     1241   2839   2673    732   -431   -652       C  
ATOM   1783  O   PRO A 241       0.305  26.075  60.195  1.00 16.77           O  
ANISOU 1783  O   PRO A 241     1141   2687   2544    654   -391   -633       O  
ATOM   1784  CB  PRO A 241      -2.723  25.674  61.028  1.00 21.37           C  
ANISOU 1784  CB  PRO A 241     1588   3429   3101    638   -405   -801       C  
ATOM   1785  CG  PRO A 241      -3.387  24.372  60.705  1.00 20.92           C  
ANISOU 1785  CG  PRO A 241     1492   3459   2999    565   -399   -853       C  
ATOM   1786  CD  PRO A 241      -2.434  23.681  59.752  1.00 17.81           C  
ANISOU 1786  CD  PRO A 241     1140   3058   2567    540   -408   -802       C  
ATOM   1787  N   LYS A 242      -0.685  28.091  60.053  1.00 20.26           N  
ANISOU 1787  N   LYS A 242     1580   3083   3035    830   -453   -619       N  
ATOM   1788  CA  LYS A 242       0.567  28.821  60.235  1.00 26.47           C  
ANISOU 1788  CA  LYS A 242     2430   3749   3877    850   -430   -556       C  
ATOM   1789  C   LYS A 242       0.648  29.415  61.634  1.00 24.24           C  
ANISOU 1789  C   LYS A 242     2145   3405   3661    820   -387   -603       C  
ATOM   1790  O   LYS A 242       0.147  30.506  61.889  1.00 32.89           O  
ANISOU 1790  O   LYS A 242     3242   4457   4797    898   -404   -611       O  
ATOM   1791  CB  LYS A 242       0.720  29.907  59.165  1.00 36.03           C  
ANISOU 1791  CB  LYS A 242     3698   4895   5097    984   -479   -467       C  
ATOM   1792  CG  LYS A 242       1.027  29.343  57.783  1.00 37.54           C  
ANISOU 1792  CG  LYS A 242     3918   5134   5212   1014   -515   -402       C  
ATOM   1793  CD  LYS A 242       1.023  30.420  56.712  1.00 47.98           C  
ANISOU 1793  CD  LYS A 242     5312   6398   6521   1154   -561   -302       C  
ATOM   1794  CE  LYS A 242       1.456  29.852  55.368  1.00 54.04           C  
ANISOU 1794  CE  LYS A 242     6123   7214   7194   1184   -590   -228       C  
ATOM   1795  NZ  LYS A 242       1.278  30.828  54.258  1.00 60.29           N  
ANISOU 1795  NZ  LYS A 242     6995   7967   7947   1321   -632   -123       N  
ATOM   1796  N   TRP A 243       1.274  28.670  62.536  1.00 20.85           N  
ANISOU 1796  N   TRP A 243     1712   2974   3234    710   -331   -634       N  
ATOM   1797  CA  TRP A 243       1.402  29.080  63.922  1.00 22.55           C  
ANISOU 1797  CA  TRP A 243     1927   3147   3492    673   -291   -685       C  
ATOM   1798  C   TRP A 243       2.686  29.874  64.120  1.00 17.15           C  
ANISOU 1798  C   TRP A 243     1300   2337   2879    685   -274   -646       C  
ATOM   1799  O   TRP A 243       3.700  29.589  63.492  1.00 17.48           O  
ANISOU 1799  O   TRP A 243     1374   2338   2928    668   -267   -588       O  
ATOM   1800  CB  TRP A 243       1.419  27.847  64.832  1.00 18.14           C  
ANISOU 1800  CB  TRP A 243     1350   2651   2890    554   -240   -733       C  
ATOM   1801  CG  TRP A 243       0.067  27.200  65.007  1.00 17.81           C  
ANISOU 1801  CG  TRP A 243     1254   2711   2801    532   -242   -790       C  
ATOM   1802  CD1 TRP A 243      -0.979  27.676  65.745  1.00 18.64           C  
ANISOU 1802  CD1 TRP A 243     1319   2848   2916    559   -243   -851       C  
ATOM   1803  CD2 TRP A 243      -0.368  25.950  64.454  1.00 17.23           C  
ANISOU 1803  CD2 TRP A 243     1158   2717   2672    476   -239   -796       C  
ATOM   1804  NE1 TRP A 243      -2.043  26.808  65.676  1.00 21.29           N  
ANISOU 1804  NE1 TRP A 243     1605   3277   3208    523   -239   -893       N  
ATOM   1805  CE2 TRP A 243      -1.691  25.737  64.895  1.00 16.75           C  
ANISOU 1805  CE2 TRP A 243     1042   2728   2595    470   -236   -862       C  
ATOM   1806  CE3 TRP A 243       0.233  24.989  63.634  1.00 17.14           C  
ANISOU 1806  CE3 TRP A 243     1168   2720   2625    431   -238   -758       C  
ATOM   1807  CZ2 TRP A 243      -2.422  24.604  64.546  1.00 17.29           C  
ANISOU 1807  CZ2 TRP A 243     1075   2873   2620    416   -230   -892       C  
ATOM   1808  CZ3 TRP A 243      -0.499  23.862  63.280  1.00 15.59           C  
ANISOU 1808  CZ3 TRP A 243      941   2601   2382    379   -235   -790       C  
ATOM   1809  CH2 TRP A 243      -1.815  23.683  63.736  1.00 16.44           C  
ANISOU 1809  CH2 TRP A 243      994   2771   2482    371   -230   -857       C  
ATOM   1810  N   ALA A 244       2.630  30.871  64.997  1.00 19.82           N  
ANISOU 1810  N   ALA A 244     1648   2611   3273    711   -267   -682       N  
ATOM   1811  CA  ALA A 244       3.806  31.679  65.311  1.00 23.39           C  
ANISOU 1811  CA  ALA A 244     2152   2931   3805    710   -248   -662       C  
ATOM   1812  C   ALA A 244       4.765  30.935  66.230  1.00 25.24           C  
ANISOU 1812  C   ALA A 244     2388   3171   4032    600   -201   -693       C  
ATOM   1813  O   ALA A 244       4.362  30.082  67.018  1.00 23.22           O  
ANISOU 1813  O   ALA A 244     2100   3005   3716    536   -179   -744       O  
ATOM   1814  CB  ALA A 244       3.390  33.002  65.933  1.00 27.19           C  
ANISOU 1814  CB  ALA A 244     2644   3340   4345    774   -259   -699       C  
ATOM   1815  N   ARG A 245       6.044  31.265  66.122  1.00 20.71           N  
ANISOU 1815  N   ARG A 245     1855   2493   3521    580   -183   -657       N  
ATOM   1816  CA  ARG A 245       7.054  30.668  66.977  1.00 22.73           C  
ANISOU 1816  CA  ARG A 245     2113   2749   3773    485   -143   -685       C  
ATOM   1817  C   ARG A 245       7.001  31.329  68.350  1.00 27.32           C  
ANISOU 1817  C   ARG A 245     2691   3308   4380    473   -136   -767       C  
ATOM   1818  O   ARG A 245       6.901  32.552  68.459  1.00 24.13           O  
ANISOU 1818  O   ARG A 245     2307   2816   4047    528   -153   -781       O  
ATOM   1819  CB  ARG A 245       8.440  30.849  66.361  1.00 22.73           C  
ANISOU 1819  CB  ARG A 245     2169   2649   3818    451   -124   -610       C  
ATOM   1820  CG  ARG A 245       9.574  30.312  67.224  1.00 25.53           C  
ANISOU 1820  CG  ARG A 245     2528   3004   4169    357    -88   -639       C  
ATOM   1821  CD  ARG A 245      10.894  30.374  66.482  1.00 33.01           C  
ANISOU 1821  CD  ARG A 245     3533   3872   5136    308    -66   -550       C  
ATOM   1822  NE  ARG A 245      11.977  29.733  67.222  1.00 40.18           N  
ANISOU 1822  NE  ARG A 245     4437   4799   6032    226    -38   -578       N  
ATOM   1823  CZ  ARG A 245      12.283  28.441  67.136  1.00 40.48           C  
ANISOU 1823  CZ  ARG A 245     4469   4920   5991    175    -21   -559       C  
ATOM   1824  NH1 ARG A 245      11.579  27.634  66.346  1.00 25.39           N  
ANISOU 1824  NH1 ARG A 245     2556   3082   4010    188    -27   -520       N  
ATOM   1825  NH2 ARG A 245      13.296  27.957  67.843  1.00 41.25           N  
ANISOU 1825  NH2 ARG A 245     4565   5029   6081    114     -1   -583       N  
ATOM   1826  N   GLN A 246       7.059  30.525  69.405  1.00 33.69           N  
ANISOU 1826  N   GLN A 246     3481   4192   5127    405   -112   -819       N  
ATOM   1827  CA  GLN A 246       7.081  31.099  70.743  1.00 39.74           C  
ANISOU 1827  CA  GLN A 246     4243   4949   5908    396   -109   -898       C  
ATOM   1828  C   GLN A 246       8.478  31.005  71.351  1.00 30.29           C  
ANISOU 1828  C   GLN A 246     3064   3708   4735    335    -91   -915       C  
ATOM   1829  O   GLN A 246       9.302  30.191  70.926  1.00 32.83           O  
ANISOU 1829  O   GLN A 246     3396   4037   5039    288    -72   -870       O  
ATOM   1830  CB  GLN A 246       6.026  30.454  71.647  1.00 42.71           C  
ANISOU 1830  CB  GLN A 246     4588   5441   6199    380    -98   -951       C  
ATOM   1831  CG  GLN A 246       6.220  28.978  71.882  1.00 41.11           C  
ANISOU 1831  CG  GLN A 246     4387   5322   5910    306    -65   -933       C  
ATOM   1832  CD  GLN A 246       5.270  28.428  72.935  1.00 46.35           C  
ANISOU 1832  CD  GLN A 246     5028   6079   6503    288    -44   -983       C  
ATOM   1833  OE1 GLN A 246       4.386  29.135  73.425  1.00 42.24           O  
ANISOU 1833  OE1 GLN A 246     4480   5575   5995    332    -55  -1034       O  
ATOM   1834  NE2 GLN A 246       5.455  27.161  73.292  1.00 46.54           N  
ANISOU 1834  NE2 GLN A 246     5064   6162   6455    225     -9   -966       N  
ATOM   1835  N   ASP A 247       8.742  31.854  72.338  1.00 40.78           N  
ANISOU 1835  N   ASP A 247     4393   4997   6106    339    -99   -983       N  
ATOM   1836  CA  ASP A 247      10.044  31.883  72.991  1.00 38.12           C  
ANISOU 1836  CA  ASP A 247     4064   4625   5796    286    -92  -1014       C  
ATOM   1837  C   ASP A 247      10.279  30.575  73.724  1.00 32.23           C  
ANISOU 1837  C   ASP A 247     3311   3989   4948    231    -71  -1027       C  
ATOM   1838  O   ASP A 247       9.344  29.999  74.282  1.00 28.25           O  
ANISOU 1838  O   ASP A 247     2795   3578   4363    234    -62  -1046       O  
ATOM   1839  CB  ASP A 247      10.105  33.040  73.990  1.00 51.69           C  
ANISOU 1839  CB  ASP A 247     5777   6298   7565    303   -112  -1095       C  
ATOM   1840  CG  ASP A 247       9.603  34.339  73.403  1.00 60.80           C  
ANISOU 1840  CG  ASP A 247     6948   7348   8805    367   -131  -1083       C  
ATOM   1841  OD1 ASP A 247       9.963  34.647  72.246  1.00 63.84           O  
ANISOU 1841  OD1 ASP A 247     7364   7640   9253    380   -127  -1010       O  
ATOM   1842  OD2 ASP A 247       8.841  35.047  74.096  1.00 65.65           O  
ANISOU 1842  OD2 ASP A 247     7550   7972   9422    409   -147  -1144       O  
ATOM   1843  N   PHE A 248      11.529  30.119  73.739  1.00 28.37           N  
ANISOU 1843  N   PHE A 248     2831   3484   4465    183    -59  -1014       N  
ATOM   1844  CA  PHE A 248      11.894  28.903  74.456  1.00 26.94           C  
ANISOU 1844  CA  PHE A 248     2654   3395   4186    139    -41  -1019       C  
ATOM   1845  C   PHE A 248      11.748  29.063  75.954  1.00 28.27           C  
ANISOU 1845  C   PHE A 248     2808   3623   4311    142    -51  -1100       C  
ATOM   1846  O   PHE A 248      11.666  28.076  76.690  1.00 30.41           O  
ANISOU 1846  O   PHE A 248     3085   3983   4486    123    -34  -1103       O  
ATOM   1847  CB  PHE A 248      13.325  28.466  74.097  1.00 34.44           C  
ANISOU 1847  CB  PHE A 248     3614   4314   5157     97    -31   -989       C  
ATOM   1848  CG  PHE A 248      13.373  27.413  73.037  1.00 34.83           C  
ANISOU 1848  CG  PHE A 248     3685   4387   5162     75     -7   -896       C  
ATOM   1849  CD1 PHE A 248      13.342  27.755  71.701  1.00 36.55           C  
ANISOU 1849  CD1 PHE A 248     3900   4544   5442     89     -6   -832       C  
ATOM   1850  CD2 PHE A 248      13.408  26.072  73.379  1.00 39.81           C  
ANISOU 1850  CD2 PHE A 248     4341   5099   5685     46     14   -869       C  
ATOM   1851  CE1 PHE A 248      13.370  26.781  70.726  1.00 37.22           C  
ANISOU 1851  CE1 PHE A 248     4002   4661   5478     67     11   -750       C  
ATOM   1852  CE2 PHE A 248      13.428  25.098  72.406  1.00 37.08           C  
ANISOU 1852  CE2 PHE A 248     4019   4771   5297     24     33   -786       C  
ATOM   1853  CZ  PHE A 248      13.408  25.454  71.078  1.00 36.16           C  
ANISOU 1853  CZ  PHE A 248     3897   4605   5238     32     29   -731       C  
ATOM   1854  N   SER A 249      11.703  30.315  76.407  1.00 21.55           N  
ANISOU 1854  N   SER A 249     1938   2721   3528    171    -78  -1160       N  
ATOM   1855  CA  SER A 249      11.516  30.583  77.822  1.00 22.73           C  
ANISOU 1855  CA  SER A 249     2067   2931   3636    184    -91  -1238       C  
ATOM   1856  C   SER A 249      10.114  30.151  78.212  1.00 25.68           C  
ANISOU 1856  C   SER A 249     2437   3390   3932    208    -73  -1241       C  
ATOM   1857  O   SER A 249       9.824  29.940  79.387  1.00 33.52           O  
ANISOU 1857  O   SER A 249     3417   4461   4856    215    -68  -1286       O  
ATOM   1858  CB  SER A 249      11.737  32.063  78.135  1.00 24.36           C  
ANISOU 1858  CB  SER A 249     2258   3058   3940    211   -122  -1299       C  
ATOM   1859  OG  SER A 249      10.765  32.868  77.501  1.00 28.58           O  
ANISOU 1859  OG  SER A 249     2798   3534   4527    256   -127  -1289       O  
ATOM   1860  N   LYS A 250       9.244  30.023  77.212  1.00 20.48           N  
ANISOU 1860  N   LYS A 250     1783   2717   3282    223    -63  -1191       N  
ATOM   1861  CA  LYS A 250       7.876  29.571  77.441  1.00 24.65           C  
ANISOU 1861  CA  LYS A 250     2297   3325   3745    239    -43  -1192       C  
ATOM   1862  C   LYS A 250       7.729  28.082  77.148  1.00 23.50           C  
ANISOU 1862  C   LYS A 250     2167   3244   3518    195     -6  -1130       C  
ATOM   1863  O   LYS A 250       6.808  27.439  77.637  1.00 30.00           O  
ANISOU 1863  O   LYS A 250     2978   4146   4275    189     21  -1133       O  
ATOM   1864  CB  LYS A 250       6.885  30.382  76.589  1.00 24.37           C  
ANISOU 1864  CB  LYS A 250     2248   3246   3767    292    -60  -1184       C  
ATOM   1865  CG  LYS A 250       6.812  31.842  76.984  1.00 26.31           C  
ANISOU 1865  CG  LYS A 250     2482   3427   4087    343    -91  -1246       C  
ATOM   1866  CD  LYS A 250       6.424  31.977  78.447  1.00 30.04           C  
ANISOU 1866  CD  LYS A 250     2932   3972   4508    352    -87  -1324       C  
ATOM   1867  CE  LYS A 250       6.778  33.349  79.008  1.00 35.37           C  
ANISOU 1867  CE  LYS A 250     3604   4578   5258    388   -119  -1394       C  
ATOM   1868  NZ  LYS A 250       8.246  33.502  79.245  1.00 38.00           N  
ANISOU 1868  NZ  LYS A 250     3951   4861   5627    349   -132  -1405       N  
ATOM   1869  N   VAL A 251       8.646  27.540  76.354  1.00 21.17           N  
ANISOU 1869  N   VAL A 251     1898   2913   3233    163     -2  -1074       N  
ATOM   1870  CA  VAL A 251       8.604  26.125  76.001  1.00 23.15           C  
ANISOU 1870  CA  VAL A 251     2169   3213   3413    121     32  -1012       C  
ATOM   1871  C   VAL A 251       9.009  25.259  77.195  1.00 26.81           C  
ANISOU 1871  C   VAL A 251     2645   3744   3796     93     57  -1025       C  
ATOM   1872  O   VAL A 251       8.332  24.291  77.528  1.00 23.30           O  
ANISOU 1872  O   VAL A 251     2203   3364   3284     72     93  -1004       O  
ATOM   1873  CB  VAL A 251       9.513  25.818  74.798  1.00 23.52           C  
ANISOU 1873  CB  VAL A 251     2242   3204   3493    101     29   -946       C  
ATOM   1874  CG1 VAL A 251       9.546  24.326  74.518  1.00 29.01           C  
ANISOU 1874  CG1 VAL A 251     2962   3946   4113     57     62   -886       C  
ATOM   1875  CG2 VAL A 251       9.025  26.578  73.567  1.00 29.47           C  
ANISOU 1875  CG2 VAL A 251     2980   3901   4314    137      7   -919       C  
ATOM   1876  N   VAL A 252      10.124  25.617  77.828  1.00 22.52           N  
ANISOU 1876  N   VAL A 252     2107   3185   3265     94     38  -1059       N  
ATOM   1877  CA  VAL A 252      10.594  24.941  79.034  1.00 22.00           C  
ANISOU 1877  CA  VAL A 252     2049   3188   3121     85     53  -1074       C  
ATOM   1878  C   VAL A 252      10.951  25.999  80.087  1.00 19.09           C  
ANISOU 1878  C   VAL A 252     1656   2823   2773    117     19  -1156       C  
ATOM   1879  O   VAL A 252      12.111  26.380  80.234  1.00 18.29           O  
ANISOU 1879  O   VAL A 252     1551   2693   2706    116    -11  -1181       O  
ATOM   1880  CB  VAL A 252      11.816  24.037  78.737  1.00 26.75           C  
ANISOU 1880  CB  VAL A 252     2681   3784   3698     56     60  -1027       C  
ATOM   1881  CG1 VAL A 252      12.241  23.305  79.986  1.00 35.45           C  
ANISOU 1881  CG1 VAL A 252     3795   4962   4711     61     75  -1035       C  
ATOM   1882  CG2 VAL A 252      11.488  23.022  77.652  1.00 22.26           C  
ANISOU 1882  CG2 VAL A 252     2138   3206   3114     25     91   -947       C  
ATOM   1883  N   PRO A 253       9.936  26.503  80.812  1.00 18.92           N  
ANISOU 1883  N   PRO A 253     1612   2839   2736    147     22  -1201       N  
ATOM   1884  CA  PRO A 253      10.131  27.645  81.713  1.00 18.33           C  
ANISOU 1884  CA  PRO A 253     1513   2762   2692    183    -13  -1283       C  
ATOM   1885  C   PRO A 253      11.276  27.541  82.742  1.00 19.16           C  
ANISOU 1885  C   PRO A 253     1620   2904   2757    189    -32  -1317       C  
ATOM   1886  O   PRO A 253      11.957  28.547  82.933  1.00 18.72           O  
ANISOU 1886  O   PRO A 253     1541   2803   2768    203    -73  -1374       O  
ATOM   1887  CB  PRO A 253       8.766  27.784  82.406  1.00 17.81           C  
ANISOU 1887  CB  PRO A 253     1429   2756   2583    212     10  -1313       C  
ATOM   1888  CG  PRO A 253       7.800  27.268  81.382  1.00 19.76           C  
ANISOU 1888  CG  PRO A 253     1677   2995   2836    194     38  -1256       C  
ATOM   1889  CD  PRO A 253       8.516  26.116  80.713  1.00 23.12           C  
ANISOU 1889  CD  PRO A 253     2135   3413   3235    149     58  -1182       C  
ATOM   1890  N   PRO A 254      11.491  26.372  83.381  1.00 20.47           N  
ANISOU 1890  N   PRO A 254     1811   3148   2820    182     -1  -1282       N  
ATOM   1891  CA  PRO A 254      12.548  26.362  84.405  1.00 22.28           C  
ANISOU 1891  CA  PRO A 254     2042   3419   3006    203    -27  -1320       C  
ATOM   1892  C   PRO A 254      13.968  26.398  83.847  1.00 21.69           C  
ANISOU 1892  C   PRO A 254     1961   3295   2984    184    -61  -1314       C  
ATOM   1893  O   PRO A 254      14.909  26.564  84.616  1.00 18.20           O  
ANISOU 1893  O   PRO A 254     1509   2883   2525    205    -92  -1357       O  
ATOM   1894  CB  PRO A 254      12.336  25.016  85.116  1.00 27.24           C  
ANISOU 1894  CB  PRO A 254     2709   4134   3506    206     22  -1267       C  
ATOM   1895  CG  PRO A 254      10.967  24.577  84.748  1.00 24.36           C  
ANISOU 1895  CG  PRO A 254     2350   3780   3127    188     75  -1225       C  
ATOM   1896  CD  PRO A 254      10.741  25.103  83.371  1.00 23.67           C  
ANISOU 1896  CD  PRO A 254     2244   3607   3142    162     57  -1214       C  
ATOM   1897  N   LEU A 255      14.127  26.225  82.541  1.00 17.79           N  
ANISOU 1897  N   LEU A 255     1475   2732   2552    148    -53  -1264       N  
ATOM   1898  CA  LEU A 255      15.460  26.131  81.948  1.00 20.70           C  
ANISOU 1898  CA  LEU A 255     1838   3059   2969    127    -73  -1252       C  
ATOM   1899  C   LEU A 255      16.143  27.495  81.852  1.00 23.45           C  
ANISOU 1899  C   LEU A 255     2142   3335   3435    133   -112  -1314       C  
ATOM   1900  O   LEU A 255      15.521  28.478  81.432  1.00 22.11           O  
ANISOU 1900  O   LEU A 255     1958   3098   3344    136   -118  -1333       O  
ATOM   1901  CB  LEU A 255      15.350  25.494  80.559  1.00 23.56           C  
ANISOU 1901  CB  LEU A 255     2226   3369   3356     88    -45  -1176       C  
ATOM   1902  CG  LEU A 255      16.534  24.693  80.038  1.00 31.06           C  
ANISOU 1902  CG  LEU A 255     3190   4313   4298     66    -43  -1136       C  
ATOM   1903  CD1 LEU A 255      17.054  23.750  81.109  1.00 29.94           C  
ANISOU 1903  CD1 LEU A 255     3067   4263   4045     89    -41  -1133       C  
ATOM   1904  CD2 LEU A 255      16.105  23.926  78.788  1.00 29.96           C  
ANISOU 1904  CD2 LEU A 255     3091   4138   4156     36     -5  -1054       C  
ATOM   1905  N   ASP A 256      17.418  27.551  82.242  1.00 22.86           N  
ANISOU 1905  N   ASP A 256     2047   3270   3370    140   -135  -1342       N  
ATOM   1906  CA  ASP A 256      18.187  28.797  82.216  1.00 27.78           C  
ANISOU 1906  CA  ASP A 256     2632   3819   4103    144   -160  -1398       C  
ATOM   1907  C   ASP A 256      18.643  29.159  80.803  1.00 20.53           C  
ANISOU 1907  C   ASP A 256     1718   2787   3294    110   -141  -1350       C  
ATOM   1908  O   ASP A 256      18.397  28.412  79.861  1.00 20.38           O  
ANISOU 1908  O   ASP A 256     1726   2756   3263     89   -112  -1279       O  
ATOM   1909  CB  ASP A 256      19.391  28.735  83.175  1.00 31.27           C  
ANISOU 1909  CB  ASP A 256     3054   4315   4514    166   -189  -1451       C  
ATOM   1910  CG  ASP A 256      20.411  27.653  82.797  1.00 40.48           C  
ANISOU 1910  CG  ASP A 256     4237   5506   5638    155   -177  -1401       C  
ATOM   1911  OD1 ASP A 256      20.869  27.603  81.631  1.00 36.29           O  
ANISOU 1911  OD1 ASP A 256     3721   4898   5171    122   -153  -1351       O  
ATOM   1912  OD2 ASP A 256      20.764  26.847  83.685  1.00 39.67           O  
ANISOU 1912  OD2 ASP A 256     4142   5500   5430    183   -193  -1411       O  
ATOM   1913  N   GLU A 257      19.324  30.295  80.677  1.00 21.63           N  
ANISOU 1913  N   GLU A 257     1837   2843   3537    102   -155  -1387       N  
ATOM   1914  CA  GLU A 257      19.712  30.828  79.371  1.00 22.36           C  
ANISOU 1914  CA  GLU A 257     1943   2814   3736     66   -135  -1335       C  
ATOM   1915  C   GLU A 257      20.564  29.856  78.557  1.00 20.89           C  
ANISOU 1915  C   GLU A 257     1788   2627   3524     38   -109  -1262       C  
ATOM   1916  O   GLU A 257      20.314  29.649  77.368  1.00 18.62           O  
ANISOU 1916  O   GLU A 257     1529   2282   3263     14    -84  -1187       O  
ATOM   1917  CB  GLU A 257      20.461  32.153  79.534  1.00 31.63           C  
ANISOU 1917  CB  GLU A 257     3093   3906   5019     52   -154  -1388       C  
ATOM   1918  CG  GLU A 257      20.734  32.873  78.222  1.00 41.12           C  
ANISOU 1918  CG  GLU A 257     4312   4975   6337     10   -132  -1329       C  
ATOM   1919  CD  GLU A 257      21.263  34.286  78.434  1.00 55.60           C  
ANISOU 1919  CD  GLU A 257     6123   6718   8284     -8   -146  -1385       C  
ATOM   1920  OE1 GLU A 257      22.048  34.494  79.385  1.00 57.83           O  
ANISOU 1920  OE1 GLU A 257     6372   7041   8560     -5   -168  -1461       O  
ATOM   1921  OE2 GLU A 257      20.884  35.188  77.657  1.00 59.11           O  
ANISOU 1921  OE2 GLU A 257     6587   7050   8823    -24   -134  -1354       O  
ATOM   1922  N   ASP A 258      21.577  29.274  79.193  1.00 18.93           N  
ANISOU 1922  N   ASP A 258     1535   2441   3218     42   -120  -1283       N  
ATOM   1923  CA  ASP A 258      22.434  28.302  78.507  1.00 20.00           C  
ANISOU 1923  CA  ASP A 258     1701   2582   3316     16   -102  -1216       C  
ATOM   1924  C   ASP A 258      21.650  27.052  78.114  1.00 16.26           C  
ANISOU 1924  C   ASP A 258     1269   2157   2751     20    -79  -1152       C  
ATOM   1925  O   ASP A 258      21.820  26.521  77.017  1.00 17.47           O  
ANISOU 1925  O   ASP A 258     1456   2276   2905    -12    -57  -1069       O  
ATOM   1926  CB  ASP A 258      23.623  27.903  79.372  1.00 20.74           C  
ANISOU 1926  CB  ASP A 258     1775   2744   3360     29   -128  -1261       C  
ATOM   1927  CG  ASP A 258      24.677  28.996  79.465  1.00 33.36           C  
ANISOU 1927  CG  ASP A 258     3335   4285   5057      7   -144  -1312       C  
ATOM   1928  OD1 ASP A 258      24.703  29.887  78.595  1.00 31.10           O  
ANISOU 1928  OD1 ASP A 258     3047   3895   4876    -32   -126  -1285       O  
ATOM   1929  OD2 ASP A 258      25.485  28.947  80.412  1.00 34.98           O  
ANISOU 1929  OD2 ASP A 258     3508   4551   5232     28   -175  -1380       O  
ATOM   1930  N   GLY A 259      20.787  26.580  79.007  1.00 15.57           N  
ANISOU 1930  N   GLY A 259     1174   2157   2585     55    -83  -1188       N  
ATOM   1931  CA  GLY A 259      19.968  25.416  78.697  1.00 15.75           C  
ANISOU 1931  CA  GLY A 259     1234   2227   2525     51    -57  -1135       C  
ATOM   1932  C   GLY A 259      19.021  25.641  77.529  1.00 16.14           C  
ANISOU 1932  C   GLY A 259     1308   2203   2621     28    -34  -1086       C  
ATOM   1933  O   GLY A 259      18.859  24.763  76.674  1.00 16.26           O  
ANISOU 1933  O   GLY A 259     1362   2217   2600      1    -15  -1001       O  
ATOM   1934  N   ARG A 260      18.395  26.815  77.485  1.00 15.02           N  
ANISOU 1934  N   ARG A 260     1137   2011   2560     38    -46  -1116       N  
ATOM   1935  CA  ARG A 260      17.494  27.160  76.384  1.00 17.02           C  
ANISOU 1935  CA  ARG A 260     1404   2195   2867     27    -34  -1078       C  
ATOM   1936  C   ARG A 260      18.268  27.260  75.076  1.00 15.87           C  
ANISOU 1936  C   ARG A 260     1275   1968   2786     -7    -22   -998       C  
ATOM   1937  O   ARG A 260      17.782  26.849  74.026  1.00 18.05           O  
ANISOU 1937  O   ARG A 260     1572   2231   3055    -22     -6   -920       O  
ATOM   1938  CB  ARG A 260      16.774  28.488  76.657  1.00 21.47           C  
ANISOU 1938  CB  ARG A 260     1919   2721   3515     44    -62  -1131       C  
ATOM   1939  CG  ARG A 260      15.846  28.457  77.863  1.00 25.83           C  
ANISOU 1939  CG  ARG A 260     2460   3359   3993     66    -80  -1187       C  
ATOM   1940  CD  ARG A 260      14.940  29.685  77.908  1.00 22.48           C  
ANISOU 1940  CD  ARG A 260     2027   2882   3632     96    -96  -1223       C  
ATOM   1941  NE  ARG A 260      15.672  30.945  77.908  1.00 27.15           N  
ANISOU 1941  NE  ARG A 260     2598   3385   4334     99   -115  -1259       N  
ATOM   1942  CZ  ARG A 260      16.068  31.582  79.004  1.00 30.58           C  
ANISOU 1942  CZ  ARG A 260     3006   3837   4774    114   -139  -1333       C  
ATOM   1943  NH1 ARG A 260      15.804  31.083  80.204  1.00 28.39           N  
ANISOU 1943  NH1 ARG A 260     2719   3670   4398    135   -148  -1376       N  
ATOM   1944  NH2 ARG A 260      16.733  32.721  78.901  1.00 35.85           N  
ANISOU 1944  NH2 ARG A 260     3663   4412   5547    108   -152  -1361       N  
ATOM   1945  N   SER A 261      19.472  27.815  75.148  1.00 16.11           N  
ANISOU 1945  N   SER A 261     1293   1957   2871    -23    -30  -1007       N  
ATOM   1946  CA  SER A 261      20.310  27.930  73.963  1.00 15.77           C  
ANISOU 1946  CA  SER A 261     1265   1845   2882    -64    -14   -928       C  
ATOM   1947  C   SER A 261      20.591  26.553  73.365  1.00 16.34           C  
ANISOU 1947  C   SER A 261     1373   1973   2864    -80      6   -844       C  
ATOM   1948  O   SER A 261      20.402  26.330  72.165  1.00 15.91           O  
ANISOU 1948  O   SER A 261     1335   1889   2821    -98     26   -763       O  
ATOM   1949  CB  SER A 261      21.626  28.627  74.300  1.00 22.57           C  
ANISOU 1949  CB  SER A 261     2104   2672   3802    -82    -21   -960       C  
ATOM   1950  OG  SER A 261      22.536  28.503  73.221  1.00 22.26           O  
ANISOU 1950  OG  SER A 261     2076   2590   3792   -124      3   -881       O  
ATOM   1951  N   LEU A 262      21.028  25.625  74.207  1.00 16.63           N  
ANISOU 1951  N   LEU A 262     1418   2090   2810    -69     -1   -865       N  
ATOM   1952  CA  LEU A 262      21.326  24.270  73.741  1.00 14.48           C  
ANISOU 1952  CA  LEU A 262     1177   1868   2457    -80     15   -792       C  
ATOM   1953  C   LEU A 262      20.075  23.589  73.211  1.00 12.53           C  
ANISOU 1953  C   LEU A 262      955   1643   2161    -77     33   -743       C  
ATOM   1954  O   LEU A 262      20.089  22.991  72.134  1.00 12.89           O  
ANISOU 1954  O   LEU A 262     1023   1681   2193    -93     53   -664       O  
ATOM   1955  CB  LEU A 262      21.939  23.436  74.866  1.00 15.40           C  
ANISOU 1955  CB  LEU A 262     1290   2066   2494    -62     -1   -834       C  
ATOM   1956  CG  LEU A 262      22.244  21.979  74.541  1.00 14.00           C  
ANISOU 1956  CG  LEU A 262     1140   1942   2240    -66     13   -770       C  
ATOM   1957  CD1 LEU A 262      23.140  21.889  73.298  1.00 16.60           C  
ANISOU 1957  CD1 LEU A 262     1476   2225   2607    -93     28   -698       C  
ATOM   1958  CD2 LEU A 262      22.903  21.306  75.737  1.00 16.29           C  
ANISOU 1958  CD2 LEU A 262     1414   2313   2462    -38    -10   -823       C  
ATOM   1959  N   LEU A 263      18.979  23.685  73.959  1.00 12.25           N  
ANISOU 1959  N   LEU A 263      913   1641   2101    -55     29   -793       N  
ATOM   1960  CA  LEU A 263      17.755  23.017  73.528  1.00 14.00           C  
ANISOU 1960  CA  LEU A 263     1154   1892   2275    -53     48   -751       C  
ATOM   1961  C   LEU A 263      17.288  23.551  72.174  1.00 15.08           C  
ANISOU 1961  C   LEU A 263     1289   1968   2472    -58     53   -698       C  
ATOM   1962  O   LEU A 263      16.859  22.782  71.309  1.00 12.73           O  
ANISOU 1962  O   LEU A 263     1012   1687   2137    -67     69   -635       O  
ATOM   1963  CB  LEU A 263      16.645  23.172  74.581  1.00 12.80           C  
ANISOU 1963  CB  LEU A 263      986   1787   2089    -30     46   -818       C  
ATOM   1964  CG  LEU A 263      15.323  22.497  74.190  1.00 13.13           C  
ANISOU 1964  CG  LEU A 263     1043   1862   2084    -33     69   -777       C  
ATOM   1965  CD1 LEU A 263      15.480  20.987  74.083  1.00 14.92           C  
ANISOU 1965  CD1 LEU A 263     1301   2134   2233    -55     97   -722       C  
ATOM   1966  CD2 LEU A 263      14.209  22.859  75.172  1.00 16.88           C  
ANISOU 1966  CD2 LEU A 263     1498   2378   2538    -12     68   -840       C  
ATOM   1967  N   SER A 264      17.398  24.860  71.975  1.00 15.54           N  
ANISOU 1967  N   SER A 264     1318   1958   2630    -52     38   -727       N  
ATOM   1968  CA  SER A 264      16.968  25.449  70.712  1.00 15.82           C  
ANISOU 1968  CA  SER A 264     1339   1936   2735    -50     42   -679       C  
ATOM   1969  C   SER A 264      17.799  24.937  69.534  1.00 16.89           C  
ANISOU 1969  C   SER A 264     1494   2055   2868    -79     62   -593       C  
ATOM   1970  O   SER A 264      17.299  24.816  68.412  1.00 16.43           O  
ANISOU 1970  O   SER A 264     1443   1990   2811    -72     71   -533       O  
ATOM   1971  CB  SER A 264      16.995  26.978  70.774  1.00 19.72           C  
ANISOU 1971  CB  SER A 264     1801   2341   3351    -37     25   -724       C  
ATOM   1972  OG  SER A 264      18.324  27.468  70.815  1.00 20.42           O  
ANISOU 1972  OG  SER A 264     1881   2372   3505    -75     26   -732       O  
ATOM   1973  N   GLN A 265      19.059  24.613  69.795  1.00 14.20           N  
ANISOU 1973  N   GLN A 265     1167   1717   2511   -104     68   -587       N  
ATOM   1974  CA  GLN A 265      19.953  24.137  68.741  1.00 15.27           C  
ANISOU 1974  CA  GLN A 265     1318   1843   2642   -129     91   -512       C  
ATOM   1975  C   GLN A 265      19.724  22.653  68.417  1.00 14.06           C  
ANISOU 1975  C   GLN A 265     1198   1760   2385   -127    103   -469       C  
ATOM   1976  O   GLN A 265      19.961  22.206  67.288  1.00 15.45           O  
ANISOU 1976  O   GLN A 265     1384   1935   2551   -138    123   -407       O  
ATOM   1977  CB  GLN A 265      21.414  24.407  69.126  1.00 15.01           C  
ANISOU 1977  CB  GLN A 265     1278   1789   2637   -151     91   -528       C  
ATOM   1978  CG  GLN A 265      21.742  25.895  69.215  1.00 16.18           C  
ANISOU 1978  CG  GLN A 265     1396   1850   2903   -165     88   -563       C  
ATOM   1979  CD  GLN A 265      23.177  26.156  69.621  1.00 22.25           C  
ANISOU 1979  CD  GLN A 265     2150   2608   3695   -187     88   -587       C  
ATOM   1980  OE1 GLN A 265      24.109  25.678  68.980  1.00 24.37           O  
ANISOU 1980  OE1 GLN A 265     2424   2889   3947   -208    110   -536       O  
ATOM   1981  NE2 GLN A 265      23.363  26.920  70.690  1.00 24.44           N  
ANISOU 1981  NE2 GLN A 265     2403   2870   4012   -179     64   -672       N  
ATOM   1982  N   MET A 266      19.244  21.898  69.403  1.00 11.45           N  
ANISOU 1982  N   MET A 266      882   1486   1984   -114     95   -505       N  
ATOM   1983  CA  MET A 266      18.900  20.495  69.187  1.00 12.23           C  
ANISOU 1983  CA  MET A 266     1010   1637   2000   -117    110   -472       C  
ATOM   1984  C   MET A 266      17.547  20.352  68.499  1.00 13.47           C  
ANISOU 1984  C   MET A 266     1169   1805   2144   -111    114   -455       C  
ATOM   1985  O   MET A 266      17.250  19.306  67.933  1.00 12.65           O  
ANISOU 1985  O   MET A 266     1086   1731   1991   -120    128   -423       O  
ATOM   1986  CB  MET A 266      18.888  19.728  70.513  1.00 13.59           C  
ANISOU 1986  CB  MET A 266     1191   1862   2112   -110    109   -514       C  
ATOM   1987  CG  MET A 266      20.224  19.780  71.261  1.00 14.88           C  
ANISOU 1987  CG  MET A 266     1341   2032   2279   -106     97   -542       C  
ATOM   1988  SD  MET A 266      20.125  18.998  72.891  1.00 17.14           S  
ANISOU 1988  SD  MET A 266     1623   2396   2494    -86     93   -600       S  
ATOM   1989  CE  MET A 266      20.092  17.263  72.444  1.00 17.81           C  
ANISOU 1989  CE  MET A 266     1740   2516   2509    -94    129   -542       C  
ATOM   1990  N   LEU A 267      16.728  21.403  68.556  1.00 13.52           N  
ANISOU 1990  N   LEU A 267     1148   1790   2200    -93     99   -484       N  
ATOM   1991  CA  LEU A 267      15.395  21.361  67.958  1.00 15.32           C  
ANISOU 1991  CA  LEU A 267     1364   2038   2418    -78     95   -478       C  
ATOM   1992  C   LEU A 267      15.257  22.284  66.748  1.00 18.14           C  
ANISOU 1992  C   LEU A 267     1693   2352   2846    -58     86   -447       C  
ATOM   1993  O   LEU A 267      14.149  22.664  66.364  1.00 18.83           O  
ANISOU 1993  O   LEU A 267     1769   2448   2938    -26     68   -452       O  
ATOM   1994  CB  LEU A 267      14.326  21.688  69.001  1.00 12.97           C  
ANISOU 1994  CB  LEU A 267     1052   1764   2112    -59     86   -539       C  
ATOM   1995  CG  LEU A 267      14.201  20.688  70.153  1.00 11.34           C  
ANISOU 1995  CG  LEU A 267      868   1609   1833    -75    103   -564       C  
ATOM   1996  CD1 LEU A 267      13.130  21.145  71.144  1.00 14.52           C  
ANISOU 1996  CD1 LEU A 267     1248   2040   2231    -56    100   -625       C  
ATOM   1997  CD2 LEU A 267      13.885  19.283  69.635  1.00 13.42           C  
ANISOU 1997  CD2 LEU A 267     1157   1908   2035   -100    125   -525       C  
ATOM   1998  N   HIS A 268      16.385  22.653  66.154  1.00 16.13           N  
ANISOU 1998  N   HIS A 268     1459   2046   2624    -71     96   -400       N  
ATOM   1999  CA  HIS A 268      16.367  23.398  64.903  1.00 16.11           C  
ANISOU 1999  CA  HIS A 268     1478   1993   2651    -49     94   -335       C  
ATOM   2000  C   HIS A 268      15.608  22.584  63.867  1.00 13.77           C  
ANISOU 2000  C   HIS A 268     1198   1749   2284    -33     90   -298       C  
ATOM   2001  O   HIS A 268      15.808  21.372  63.768  1.00 17.22           O  
ANISOU 2001  O   HIS A 268     1644   2236   2661    -59    103   -296       O  
ATOM   2002  CB  HIS A 268      17.798  23.625  64.418  1.00 21.37           C  
ANISOU 2002  CB  HIS A 268     2160   2609   3349    -78    122   -285       C  
ATOM   2003  CG  HIS A 268      17.981  24.887  63.640  1.00 35.03           C  
ANISOU 2003  CG  HIS A 268     3910   4255   5147    -62    130   -231       C  
ATOM   2004  ND1 HIS A 268      17.562  25.025  62.332  1.00 37.67           N  
ANISOU 2004  ND1 HIS A 268     4280   4582   5451    -28    133   -155       N  
ATOM   2005  CD2 HIS A 268      18.536  26.073  63.984  1.00 37.01           C  
ANISOU 2005  CD2 HIS A 268     4152   4419   5492    -73    137   -241       C  
ATOM   2006  CE1 HIS A 268      17.855  26.239  61.905  1.00 37.83           C  
ANISOU 2006  CE1 HIS A 268     4319   4511   5541    -17    147   -109       C  
ATOM   2007  NE2 HIS A 268      18.450  26.895  62.887  1.00 37.22           N  
ANISOU 2007  NE2 HIS A 268     4215   4378   5547    -49    151   -162       N  
ATOM   2008  N   TYR A 269      14.729  23.232  63.105  1.00 15.48           N  
ANISOU 2008  N   TYR A 269     1420   1954   2507     14     67   -273       N  
ATOM   2009  CA  TYR A 269      13.966  22.518  62.072  1.00 16.23           C  
ANISOU 2009  CA  TYR A 269     1525   2110   2533     35     53   -249       C  
ATOM   2010  C   TYR A 269      14.866  21.921  61.007  1.00 17.75           C  
ANISOU 2010  C   TYR A 269     1758   2306   2680     19     77   -184       C  
ATOM   2011  O   TYR A 269      14.725  20.750  60.643  1.00 18.61           O  
ANISOU 2011  O   TYR A 269     1872   2474   2724      2     79   -192       O  
ATOM   2012  CB  TYR A 269      12.963  23.449  61.387  1.00 15.92           C  
ANISOU 2012  CB  TYR A 269     1484   2059   2506    103     17   -230       C  
ATOM   2013  CG  TYR A 269      11.607  23.493  62.051  1.00 16.67           C  
ANISOU 2013  CG  TYR A 269     1527   2201   2605    129    -14   -304       C  
ATOM   2014  CD1 TYR A 269      10.814  22.355  62.132  1.00 16.78           C  
ANISOU 2014  CD1 TYR A 269     1509   2303   2565    107    -21   -351       C  
ATOM   2015  CD2 TYR A 269      11.114  24.675  62.581  1.00 17.39           C  
ANISOU 2015  CD2 TYR A 269     1600   2248   2761    174    -33   -330       C  
ATOM   2016  CE1 TYR A 269       9.559  22.395  62.733  1.00 16.11           C  
ANISOU 2016  CE1 TYR A 269     1366   2268   2488    125    -42   -422       C  
ATOM   2017  CE2 TYR A 269       9.862  24.727  63.191  1.00 17.67           C  
ANISOU 2017  CE2 TYR A 269     1579   2335   2799    202    -58   -403       C  
ATOM   2018  CZ  TYR A 269       9.089  23.582  63.256  1.00 17.82           C  
ANISOU 2018  CZ  TYR A 269     1558   2449   2762    176    -60   -447       C  
ATOM   2019  OH  TYR A 269       7.844  23.625  63.855  1.00 15.47           O  
ANISOU 2019  OH  TYR A 269     1195   2209   2471    198    -76   -521       O  
ATOM   2020  N   ASP A 270      15.771  22.742  60.491  1.00 14.55           N  
ANISOU 2020  N   ASP A 270     1381   1836   2312     24     99   -121       N  
ATOM   2021  CA  ASP A 270      16.652  22.331  59.406  1.00 14.72           C  
ANISOU 2021  CA  ASP A 270     1439   1862   2291     16    130    -52       C  
ATOM   2022  C   ASP A 270      17.693  21.345  59.927  1.00 14.87           C  
ANISOU 2022  C   ASP A 270     1451   1902   2298    -38    160    -75       C  
ATOM   2023  O   ASP A 270      18.534  21.717  60.745  1.00 17.87           O  
ANISOU 2023  O   ASP A 270     1812   2242   2736    -68    177    -93       O  
ATOM   2024  CB  ASP A 270      17.342  23.567  58.831  1.00 18.12           C  
ANISOU 2024  CB  ASP A 270     1898   2210   2776     29    157     23       C  
ATOM   2025  CG  ASP A 270      18.091  23.281  57.542  1.00 21.96           C  
ANISOU 2025  CG  ASP A 270     2427   2709   3209     32    194    104       C  
ATOM   2026  OD1 ASP A 270      18.313  22.096  57.203  1.00 22.87           O  
ANISOU 2026  OD1 ASP A 270     2546   2891   3254     18    201     93       O  
ATOM   2027  OD2 ASP A 270      18.464  24.259  56.867  1.00 25.88           O  
ANISOU 2027  OD2 ASP A 270     2955   3142   3735     50    222    181       O  
ATOM   2028  N   PRO A 271      17.637  20.083  59.458  1.00 15.01           N  
ANISOU 2028  N   PRO A 271     1482   1981   2239    -45    163    -81       N  
ATOM   2029  CA  PRO A 271      18.539  19.032  59.959  1.00 16.83           C  
ANISOU 2029  CA  PRO A 271     1711   2232   2453    -83    188   -104       C  
ATOM   2030  C   PRO A 271      19.999  19.383  59.741  1.00 24.17           C  
ANISOU 2030  C   PRO A 271     2642   3126   3414   -100    228    -61       C  
ATOM   2031  O   PRO A 271      20.856  18.960  60.516  1.00 27.11           O  
ANISOU 2031  O   PRO A 271     2996   3500   3803   -126    242    -89       O  
ATOM   2032  CB  PRO A 271      18.176  17.811  59.106  1.00 19.10           C  
ANISOU 2032  CB  PRO A 271     2024   2576   2657    -76    185   -105       C  
ATOM   2033  CG  PRO A 271      16.793  18.082  58.624  1.00 21.96           C  
ANISOU 2033  CG  PRO A 271     2382   2965   2999    -44    146   -115       C  
ATOM   2034  CD  PRO A 271      16.696  19.568  58.452  1.00 16.83           C  
ANISOU 2034  CD  PRO A 271     1729   2265   2399    -12    138    -74       C  
ATOM   2035  N   ASN A 272      20.274  20.155  58.696  1.00 23.60           N  
ANISOU 2035  N   ASN A 272     2591   3026   3349    -82    248      7       N  
ATOM   2036  CA  ASN A 272      21.642  20.560  58.396  1.00 30.97           C  
ANISOU 2036  CA  ASN A 272     3522   3926   4321   -106    297     52       C  
ATOM   2037  C   ASN A 272      22.160  21.650  59.330  1.00 28.54           C  
ANISOU 2037  C   ASN A 272     3177   3550   4117   -136    303     32       C  
ATOM   2038  O   ASN A 272      23.364  21.882  59.405  1.00 32.63           O  
ANISOU 2038  O   ASN A 272     3671   4046   4681   -169    340     43       O  
ATOM   2039  CB  ASN A 272      21.776  20.992  56.931  1.00 42.40           C  
ANISOU 2039  CB  ASN A 272     5010   5367   5734    -79    329    140       C  
ATOM   2040  CG  ASN A 272      21.700  19.819  55.970  1.00 54.01           C  
ANISOU 2040  CG  ASN A 272     6511   6911   7100    -56    334    151       C  
ATOM   2041  OD1 ASN A 272      22.670  19.079  55.799  1.00 61.34           O  
ANISOU 2041  OD1 ASN A 272     7435   7867   8006    -73    369    151       O  
ATOM   2042  ND2 ASN A 272      20.544  19.641  55.342  1.00 58.96           N  
ANISOU 2042  ND2 ASN A 272     7165   7574   7664    -14    296    153       N  
ATOM   2043  N   LYS A 273      21.253  22.313  60.042  1.00 17.63           N  
ANISOU 2043  N   LYS A 273     1786   2140   2775   -123    265     -6       N  
ATOM   2044  CA  LYS A 273      21.648  23.348  60.997  1.00 18.11           C  
ANISOU 2044  CA  LYS A 273     1812   2134   2934   -149    263    -42       C  
ATOM   2045  C   LYS A 273      21.568  22.856  62.439  1.00 18.55           C  
ANISOU 2045  C   LYS A 273     1830   2224   2993   -162    231   -134       C  
ATOM   2046  O   LYS A 273      22.125  23.479  63.346  1.00 17.56           O  
ANISOU 2046  O   LYS A 273     1669   2064   2938   -186    226   -182       O  
ATOM   2047  CB  LYS A 273      20.780  24.597  60.834  1.00 24.99           C  
ANISOU 2047  CB  LYS A 273     2701   2939   3857   -119    246    -23       C  
ATOM   2048  CG  LYS A 273      20.967  25.307  59.495  1.00 37.26           C  
ANISOU 2048  CG  LYS A 273     4300   4442   5416   -101    283     80       C  
ATOM   2049  CD  LYS A 273      22.433  25.647  59.264  1.00 48.36           C  
ANISOU 2049  CD  LYS A 273     5692   5802   6879   -155    344    117       C  
ATOM   2050  CE  LYS A 273      22.630  26.451  57.986  1.00 60.24           C  
ANISOU 2050  CE  LYS A 273     7248   7248   8394   -141    394    228       C  
ATOM   2051  NZ  LYS A 273      24.056  26.842  57.787  1.00 64.07           N  
ANISOU 2051  NZ  LYS A 273     7711   7685   8947   -204    465    262       N  
ATOM   2052  N   ARG A 274      20.857  21.752  62.643  1.00 14.97           N  
ANISOU 2052  N   ARG A 274     1387   1838   2462   -146    211   -160       N  
ATOM   2053  CA  ARG A 274      20.697  21.165  63.976  1.00 16.15           C  
ANISOU 2053  CA  ARG A 274     1513   2026   2596   -153    188   -235       C  
ATOM   2054  C   ARG A 274      22.070  20.790  64.537  1.00 16.06           C  
ANISOU 2054  C   ARG A 274     1487   2026   2590   -175    200   -252       C  
ATOM   2055  O   ARG A 274      22.908  20.237  63.821  1.00 14.75           O  
ANISOU 2055  O   ARG A 274     1328   1875   2403   -183    227   -213       O  
ATOM   2056  CB  ARG A 274      19.783  19.936  63.890  1.00 16.05           C  
ANISOU 2056  CB  ARG A 274     1522   2075   2500   -141    180   -244       C  
ATOM   2057  CG  ARG A 274      19.075  19.566  65.196  1.00 19.96           C  
ANISOU 2057  CG  ARG A 274     2004   2603   2977   -140    160   -309       C  
ATOM   2058  CD  ARG A 274      18.017  18.474  64.977  1.00 14.86           C  
ANISOU 2058  CD  ARG A 274     1376   2006   2265   -138    160   -315       C  
ATOM   2059  NE  ARG A 274      16.983  18.889  64.026  1.00 16.29           N  
ANISOU 2059  NE  ARG A 274     1556   2187   2445   -118    145   -296       N  
ATOM   2060  CZ  ARG A 274      16.287  18.052  63.260  1.00 14.60           C  
ANISOU 2060  CZ  ARG A 274     1357   2011   2179   -118    143   -288       C  
ATOM   2061  NH1 ARG A 274      16.503  16.738  63.328  1.00 10.80           N  
ANISOU 2061  NH1 ARG A 274      897   1558   1650   -141    161   -295       N  
ATOM   2062  NH2 ARG A 274      15.377  18.531  62.422  1.00 14.88           N  
ANISOU 2062  NH2 ARG A 274     1388   2055   2212    -90    120   -276       N  
ATOM   2063  N   ILE A 275      22.311  21.104  65.806  1.00 14.07           N  
ANISOU 2063  N   ILE A 275     1228   1771   2348   -173    172   -309       N  
ATOM   2064  CA  ILE A 275      23.620  20.843  66.412  1.00 11.82           C  
ANISOU 2064  CA  ILE A 275      936   1501   2055   -179    168   -328       C  
ATOM   2065  C   ILE A 275      23.988  19.354  66.407  1.00 15.54           C  
ANISOU 2065  C   ILE A 275     1428   2030   2447   -166    174   -314       C  
ATOM   2066  O   ILE A 275      23.118  18.488  66.530  1.00 13.41           O  
ANISOU 2066  O   ILE A 275     1182   1791   2121   -154    172   -316       O  
ATOM   2067  CB  ILE A 275      23.702  21.437  67.845  1.00 12.55           C  
ANISOU 2067  CB  ILE A 275     1011   1589   2168   -172    135   -402       C  
ATOM   2068  CG1 ILE A 275      25.154  21.546  68.313  1.00 15.40           C  
ANISOU 2068  CG1 ILE A 275     1347   1956   2548   -180    129   -428       C  
ATOM   2069  CG2 ILE A 275      22.858  20.633  68.822  1.00 12.09           C  
ANISOU 2069  CG2 ILE A 275      971   1583   2041   -148    117   -439       C  
ATOM   2070  CD1 ILE A 275      25.300  22.314  69.613  1.00 18.60           C  
ANISOU 2070  CD1 ILE A 275     1727   2355   2985   -174     97   -510       C  
ATOM   2071  N   SER A 276      25.273  19.052  66.218  1.00 12.11           N  
ANISOU 2071  N   SER A 276      979   1607   2013   -170    185   -302       N  
ATOM   2072  CA  SER A 276      25.726  17.665  66.301  1.00 13.77           C  
ANISOU 2072  CA  SER A 276     1202   1868   2161   -151    191   -298       C  
ATOM   2073  C   SER A 276      26.026  17.305  67.756  1.00 11.04           C  
ANISOU 2073  C   SER A 276      844   1556   1793   -130    160   -356       C  
ATOM   2074  O   SER A 276      26.275  18.188  68.583  1.00 13.18           O  
ANISOU 2074  O   SER A 276     1091   1817   2100   -134    135   -401       O  
ATOM   2075  CB  SER A 276      26.982  17.458  65.452  1.00 14.10           C  
ANISOU 2075  CB  SER A 276     1227   1918   2213   -155    218   -264       C  
ATOM   2076  OG  SER A 276      28.098  18.065  66.066  1.00 16.17           O  
ANISOU 2076  OG  SER A 276     1448   2178   2517   -162    203   -296       O  
ATOM   2077  N   ALA A 277      26.013  16.012  68.069  1.00 10.47           N  
ANISOU 2077  N   ALA A 277      788   1529   1662   -106    166   -359       N  
ATOM   2078  CA  ALA A 277      26.333  15.565  69.425  1.00 12.71           C  
ANISOU 2078  CA  ALA A 277     1057   1858   1915    -76    141   -410       C  
ATOM   2079  C   ALA A 277      27.731  15.990  69.843  1.00 13.51           C  
ANISOU 2079  C   ALA A 277     1112   1975   2045    -66    116   -441       C  
ATOM   2080  O   ALA A 277      27.941  16.438  70.971  1.00 12.90           O  
ANISOU 2080  O   ALA A 277     1011   1920   1970    -53     81   -498       O  
ATOM   2081  CB  ALA A 277      26.176  14.052  69.557  1.00 11.98           C  
ANISOU 2081  CB  ALA A 277      992   1805   1754    -44    163   -398       C  
ATOM   2082  N   LYS A 278      28.708  15.868  68.954  1.00 13.71           N  
ANISOU 2082  N   LYS A 278     1123   1996   2091    -71    134   -409       N  
ATOM   2083  CA  LYS A 278      30.043  16.229  69.403  1.00 15.17           C  
ANISOU 2083  CA  LYS A 278     1257   2202   2304    -63    111   -446       C  
ATOM   2084  C   LYS A 278      30.206  17.738  69.565  1.00 13.42           C  
ANISOU 2084  C   LYS A 278     1009   1936   2153   -103     98   -474       C  
ATOM   2085  O   LYS A 278      30.914  18.185  70.466  1.00 15.84           O  
ANISOU 2085  O   LYS A 278     1277   2262   2478    -96     65   -535       O  
ATOM   2086  CB  LYS A 278      31.157  15.584  68.577  1.00 30.75           C  
ANISOU 2086  CB  LYS A 278     3211   4198   4276    -50    134   -415       C  
ATOM   2087  CG  LYS A 278      31.080  15.764  67.114  1.00 31.46           C  
ANISOU 2087  CG  LYS A 278     3315   4251   4387    -81    181   -352       C  
ATOM   2088  CD  LYS A 278      32.315  15.110  66.488  1.00 29.72           C  
ANISOU 2088  CD  LYS A 278     3066   4067   4161    -60    203   -335       C  
ATOM   2089  CE  LYS A 278      32.322  15.317  65.000  1.00 31.44           C  
ANISOU 2089  CE  LYS A 278     3295   4260   4392    -87    255   -274       C  
ATOM   2090  NZ  LYS A 278      33.483  14.654  64.359  1.00 20.36           N  
ANISOU 2090  NZ  LYS A 278     1862   2896   2978    -63    283   -259       N  
ATOM   2091  N   ALA A 279      29.514  18.531  68.747  1.00 13.48           N  
ANISOU 2091  N   ALA A 279     1037   1885   2200   -139    124   -436       N  
ATOM   2092  CA  ALA A 279      29.571  19.983  68.947  1.00 12.58           C  
ANISOU 2092  CA  ALA A 279      900   1719   2160   -171    117   -466       C  
ATOM   2093  C   ALA A 279      28.876  20.389  70.247  1.00 17.02           C  
ANISOU 2093  C   ALA A 279     1465   2286   2716   -155     79   -535       C  
ATOM   2094  O   ALA A 279      29.304  21.330  70.930  1.00 15.87           O  
ANISOU 2094  O   ALA A 279     1287   2123   2619   -164     57   -596       O  
ATOM   2095  CB  ALA A 279      28.959  20.725  67.771  1.00 19.60           C  
ANISOU 2095  CB  ALA A 279     1809   2545   3092   -203    153   -408       C  
ATOM   2096  N   ALA A 280      27.797  19.682  70.569  1.00 14.35           N  
ANISOU 2096  N   ALA A 280     1163   1972   2317   -131     74   -529       N  
ATOM   2097  CA  ALA A 280      27.012  19.955  71.773  1.00 14.88           C  
ANISOU 2097  CA  ALA A 280     1233   2055   2366   -112     46   -591       C  
ATOM   2098  C   ALA A 280      27.816  19.733  73.059  1.00 13.25           C  
ANISOU 2098  C   ALA A 280      994   1910   2129    -81      6   -665       C  
ATOM   2099  O   ALA A 280      27.562  20.377  74.074  1.00 13.34           O  
ANISOU 2099  O   ALA A 280      991   1931   2146    -69    -21   -735       O  
ATOM   2100  CB  ALA A 280      25.741  19.112  71.782  1.00 11.85           C  
ANISOU 2100  CB  ALA A 280      888   1694   1920    -98     59   -565       C  
ATOM   2101  N   LEU A 281      28.794  18.833  73.013  1.00 13.10           N  
ANISOU 2101  N   LEU A 281      961   1939   2078    -60      1   -654       N  
ATOM   2102  CA  LEU A 281      29.629  18.564  74.194  1.00 14.09           C  
ANISOU 2102  CA  LEU A 281     1052   2136   2167    -18    -44   -724       C  
ATOM   2103  C   LEU A 281      30.369  19.810  74.682  1.00 16.26           C  
ANISOU 2103  C   LEU A 281     1283   2389   2507    -36    -69   -795       C  
ATOM   2104  O   LEU A 281      30.712  19.918  75.864  1.00 14.46           O  
ANISOU 2104  O   LEU A 281     1029   2215   2250      0   -112   -874       O  
ATOM   2105  CB  LEU A 281      30.623  17.431  73.904  1.00 14.20           C  
ANISOU 2105  CB  LEU A 281     1053   2200   2144     15    -45   -696       C  
ATOM   2106  CG  LEU A 281      30.013  16.058  73.605  1.00 15.39           C  
ANISOU 2106  CG  LEU A 281     1242   2380   2225     48    -20   -640       C  
ATOM   2107  CD1 LEU A 281      31.093  15.070  73.168  1.00 14.81           C  
ANISOU 2107  CD1 LEU A 281     1156   2343   2129     86    -16   -613       C  
ATOM   2108  CD2 LEU A 281      29.272  15.525  74.827  1.00 15.09           C  
ANISOU 2108  CD2 LEU A 281     1219   2406   2108    101    -42   -674       C  
ATOM   2109  N   ALA A 282      30.612  20.752  73.773  1.00 14.05           N  
ANISOU 2109  N   ALA A 282      992   2033   2313    -87    -40   -768       N  
ATOM   2110  CA  ALA A 282      31.347  21.975  74.112  1.00 13.17           C  
ANISOU 2110  CA  ALA A 282      834   1890   2279   -112    -54   -833       C  
ATOM   2111  C   ALA A 282      30.432  23.159  74.425  1.00 16.17           C  
ANISOU 2111  C   ALA A 282     1223   2211   2711   -127    -53   -869       C  
ATOM   2112  O   ALA A 282      30.903  24.281  74.576  1.00 15.87           O  
ANISOU 2112  O   ALA A 282     1148   2128   2753   -153    -56   -918       O  
ATOM   2113  CB  ALA A 282      32.312  22.343  72.983  1.00 18.26           C  
ANISOU 2113  CB  ALA A 282     1451   2493   2994   -159    -19   -788       C  
ATOM   2114  N   HIS A 283      29.127  22.919  74.520  1.00 14.65           N  
ANISOU 2114  N   HIS A 283     1073   2015   2478   -111    -47   -849       N  
ATOM   2115  CA  HIS A 283      28.198  24.010  74.805  1.00 12.87           C  
ANISOU 2115  CA  HIS A 283      852   1737   2302   -116    -47   -886       C  
ATOM   2116  C   HIS A 283      28.402  24.519  76.238  1.00 18.14           C  
ANISOU 2116  C   HIS A 283     1484   2443   2963    -84    -88   -997       C  
ATOM   2117  O   HIS A 283      28.655  23.726  77.141  1.00 16.81           O  
ANISOU 2117  O   HIS A 283     1311   2362   2714    -42   -118  -1036       O  
ATOM   2118  CB  HIS A 283      26.747  23.553  74.592  1.00 14.73           C  
ANISOU 2118  CB  HIS A 283     1133   1974   2490   -103    -31   -843       C  
ATOM   2119  CG  HIS A 283      25.761  24.680  74.582  1.00 15.00           C  
ANISOU 2119  CG  HIS A 283     1168   1945   2586   -109    -26   -867       C  
ATOM   2120  ND1 HIS A 283      25.344  25.313  75.733  1.00 15.47           N  
ANISOU 2120  ND1 HIS A 283     1207   2020   2651    -81    -51   -957       N  
ATOM   2121  CD2 HIS A 283      25.146  25.316  73.557  1.00 16.72           C  
ANISOU 2121  CD2 HIS A 283     1399   2087   2867   -133      1   -816       C  
ATOM   2122  CE1 HIS A 283      24.499  26.279  75.420  1.00 19.15           C  
ANISOU 2122  CE1 HIS A 283     1673   2419   3185    -88    -41   -962       C  
ATOM   2123  NE2 HIS A 283      24.352  26.295  74.106  1.00 16.33           N  
ANISOU 2123  NE2 HIS A 283     1336   2004   2864   -119    -11   -876       N  
ATOM   2124  N   PRO A 284      28.299  25.847  76.451  1.00 17.37           N  
ANISOU 2124  N   PRO A 284     1361   2286   2954    -99    -91  -1051       N  
ATOM   2125  CA  PRO A 284      28.461  26.461  77.780  1.00 22.64           C  
ANISOU 2125  CA  PRO A 284     1990   2988   3624    -67   -129  -1163       C  
ATOM   2126  C   PRO A 284      27.549  25.880  78.867  1.00 20.58           C  
ANISOU 2126  C   PRO A 284     1745   2810   3265     -9   -151  -1203       C  
ATOM   2127  O   PRO A 284      27.847  26.030  80.053  1.00 19.58           O  
ANISOU 2127  O   PRO A 284     1586   2747   3106     31   -187  -1290       O  
ATOM   2128  CB  PRO A 284      28.083  27.923  77.532  1.00 28.13           C  
ANISOU 2128  CB  PRO A 284     2668   3586   4435    -96   -116  -1187       C  
ATOM   2129  CG  PRO A 284      28.392  28.157  76.105  1.00 32.56           C  
ANISOU 2129  CG  PRO A 284     3241   4064   5065   -151    -75  -1099       C  
ATOM   2130  CD  PRO A 284      28.096  26.863  75.402  1.00 23.63           C  
ANISOU 2130  CD  PRO A 284     2155   2972   3850   -145    -57  -1007       C  
ATOM   2131  N   PHE A 285      26.459  25.232  78.470  1.00 17.56           N  
ANISOU 2131  N   PHE A 285     1407   2433   2832     -5   -128  -1142       N  
ATOM   2132  CA  PHE A 285      25.549  24.603  79.427  1.00 17.31           C  
ANISOU 2132  CA  PHE A 285     1388   2487   2704     44   -139  -1172       C  
ATOM   2133  C   PHE A 285      26.293  23.581  80.296  1.00 21.32           C  
ANISOU 2133  C   PHE A 285     1887   3102   3111     88   -171  -1198       C  
ATOM   2134  O   PHE A 285      25.958  23.375  81.457  1.00 20.90           O  
ANISOU 2134  O   PHE A 285     1822   3135   2984    140   -194  -1251       O  
ATOM   2135  CB  PHE A 285      24.389  23.940  78.682  1.00 16.41           C  
ANISOU 2135  CB  PHE A 285     1319   2360   2557     29   -105  -1096       C  
ATOM   2136  CG  PHE A 285      23.356  23.319  79.583  1.00 18.75           C  
ANISOU 2136  CG  PHE A 285     1622   2743   2760     68   -106  -1123       C  
ATOM   2137  CD1 PHE A 285      22.609  24.103  80.452  1.00 18.58           C  
ANISOU 2137  CD1 PHE A 285     1570   2743   2748     96   -116  -1190       C  
ATOM   2138  CD2 PHE A 285      23.127  21.952  79.551  1.00 19.49           C  
ANISOU 2138  CD2 PHE A 285     1742   2903   2760     74    -95  -1076       C  
ATOM   2139  CE1 PHE A 285      21.649  23.533  81.270  1.00 16.52           C  
ANISOU 2139  CE1 PHE A 285     1308   2571   2397    121   -118  -1194       C  
ATOM   2140  CE2 PHE A 285      22.171  21.375  80.362  1.00 17.16           C  
ANISOU 2140  CE2 PHE A 285     1449   2694   2378    101    -91  -1091       C  
ATOM   2141  CZ  PHE A 285      21.429  22.170  81.223  1.00 15.30           C  
ANISOU 2141  CZ  PHE A 285     1196   2474   2142    119   -104  -1136       C  
ATOM   2142  N   PHE A 286      27.325  22.963  79.737  1.00 17.37           N  
ANISOU 2142  N   PHE A 286     1388   2605   2608     73   -174  -1157       N  
ATOM   2143  CA  PHE A 286      28.063  21.938  80.466  1.00 13.67           C  
ANISOU 2143  CA  PHE A 286      912   2239   2043    125   -208  -1175       C  
ATOM   2144  C   PHE A 286      29.299  22.453  81.190  1.00 17.99           C  
ANISOU 2144  C   PHE A 286     1407   2817   2610    149   -249  -1256       C  
ATOM   2145  O   PHE A 286      30.123  21.660  81.639  1.00 20.64           O  
ANISOU 2145  O   PHE A 286     1731   3231   2878    194   -281  -1268       O  
ATOM   2146  CB  PHE A 286      28.450  20.793  79.525  1.00 14.62           C  
ANISOU 2146  CB  PHE A 286     1056   2363   2137    111   -190  -1085       C  
ATOM   2147  CG  PHE A 286      27.273  20.148  78.853  1.00 13.02           C  
ANISOU 2147  CG  PHE A 286      898   2142   1909     91   -151  -1008       C  
ATOM   2148  CD1 PHE A 286      26.314  19.487  79.605  1.00 14.82           C  
ANISOU 2148  CD1 PHE A 286     1142   2444   2045    130   -153  -1018       C  
ATOM   2149  CD2 PHE A 286      27.122  20.201  77.475  1.00 14.76           C  
ANISOU 2149  CD2 PHE A 286     1138   2278   2191     37   -109   -926       C  
ATOM   2150  CE1 PHE A 286      25.222  18.890  78.999  1.00 13.13           C  
ANISOU 2150  CE1 PHE A 286      957   2216   1816    108   -108   -950       C  
ATOM   2151  CE2 PHE A 286      26.036  19.599  76.857  1.00 15.42           C  
ANISOU 2151  CE2 PHE A 286     1258   2347   2251     22    -72   -859       C  
ATOM   2152  CZ  PHE A 286      25.083  18.946  77.621  1.00 15.18           C  
ANISOU 2152  CZ  PHE A 286     1239   2385   2142     54    -69   -873       C  
ATOM   2153  N   GLN A 287      29.437  23.768  81.309  1.00 18.72           N  
ANISOU 2153  N   GLN A 287     1466   2850   2797    122   -251  -1315       N  
ATOM   2154  CA  GLN A 287      30.649  24.323  81.912  1.00 23.11           C  
ANISOU 2154  CA  GLN A 287     1964   3429   3387    133   -289  -1399       C  
ATOM   2155  C   GLN A 287      30.867  23.825  83.341  1.00 28.03           C  
ANISOU 2155  C   GLN A 287     2570   4177   3902    219   -340  -1469       C  
ATOM   2156  O   GLN A 287      32.006  23.632  83.775  1.00 29.44           O  
ANISOU 2156  O   GLN A 287     2711   4412   4063    247   -377  -1516       O  
ATOM   2157  CB  GLN A 287      30.629  25.853  81.890  1.00 33.84           C  
ANISOU 2157  CB  GLN A 287     3287   4704   4866     93   -283  -1457       C  
ATOM   2158  CG  GLN A 287      31.987  26.465  82.203  1.00 51.11           C  
ANISOU 2158  CG  GLN A 287     5410   6896   7115     81   -312  -1535       C  
ATOM   2159  CD  GLN A 287      31.893  27.888  82.723  1.00 63.84           C  
ANISOU 2159  CD  GLN A 287     6977   8460   8818     66   -324  -1626       C  
ATOM   2160  OE1 GLN A 287      30.823  28.499  82.712  1.00 67.80           O  
ANISOU 2160  OE1 GLN A 287     7499   8913   9350     62   -307  -1621       O  
ATOM   2161  NE2 GLN A 287      33.019  28.419  83.193  1.00 67.31           N  
ANISOU 2161  NE2 GLN A 287     7354   8917   9305     61   -355  -1713       N  
ATOM   2162  N   ASP A 288      29.779  23.609  84.073  1.00 22.13           N  
ANISOU 2162  N   ASP A 288     1846   3481   3080    263   -342  -1473       N  
ATOM   2163  CA  ASP A 288      29.900  23.185  85.467  1.00 28.71           C  
ANISOU 2163  CA  ASP A 288     2668   4439   3804    351   -389  -1526       C  
ATOM   2164  C   ASP A 288      29.394  21.760  85.698  1.00 29.45           C  
ANISOU 2164  C   ASP A 288     2814   4616   3761    404   -387  -1451       C  
ATOM   2165  O   ASP A 288      29.027  21.397  86.821  1.00 28.99           O  
ANISOU 2165  O   ASP A 288     2768   4650   3596    474   -414  -1462       O  
ATOM   2166  CB  ASP A 288      29.159  24.168  86.381  1.00 31.35           C  
ANISOU 2166  CB  ASP A 288     2979   4782   4151    368   -402  -1596       C  
ATOM   2167  CG  ASP A 288      27.698  24.328  86.001  1.00 36.34           C  
ANISOU 2167  CG  ASP A 288     3646   5367   4794    337   -360  -1544       C  
ATOM   2168  OD1 ASP A 288      27.310  23.870  84.899  1.00 35.21           O  
ANISOU 2168  OD1 ASP A 288     3540   5166   4672    291   -318  -1463       O  
ATOM   2169  OD2 ASP A 288      26.936  24.922  86.795  1.00 37.00           O  
ANISOU 2169  OD2 ASP A 288     3720   5475   4865    358   -371  -1588       O  
ATOM   2170  N   VAL A 289      29.380  20.956  84.640  1.00 24.35           N  
ANISOU 2170  N   VAL A 289     2203   3936   3115    372   -357  -1368       N  
ATOM   2171  CA  VAL A 289      28.852  19.597  84.728  1.00 20.39           C  
ANISOU 2171  CA  VAL A 289     1756   3499   2491    415   -351  -1290       C  
ATOM   2172  C   VAL A 289      29.666  18.723  85.688  1.00 25.88           C  
ANISOU 2172  C   VAL A 289     2460   4306   3068    514   -399  -1295       C  
ATOM   2173  O   VAL A 289      30.896  18.809  85.749  1.00 25.47           O  
ANISOU 2173  O   VAL A 289     2366   4271   3039    535   -432  -1340       O  
ATOM   2174  CB  VAL A 289      28.714  18.930  83.326  1.00 17.19           C  
ANISOU 2174  CB  VAL A 289     1380   3033   2119    358   -311  -1206       C  
ATOM   2175  CG1 VAL A 289      30.083  18.630  82.716  1.00 18.77           C  
ANISOU 2175  CG1 VAL A 289     1557   3220   2356    353   -327  -1196       C  
ATOM   2176  CG2 VAL A 289      27.866  17.661  83.402  1.00 19.71           C  
ANISOU 2176  CG2 VAL A 289     1773   3400   2315    390   -291  -1129       C  
ATOM   2177  N   THR A 290      28.957  17.911  86.464  1.00 20.79           N  
ANISOU 2177  N   THR A 290     1881   3728   2292    573   -398  -1242       N  
ATOM   2178  CA  THR A 290      29.571  16.950  87.369  1.00 26.72           C  
ANISOU 2178  CA  THR A 290     2667   4573   2911    678   -433  -1218       C  
ATOM   2179  C   THR A 290      28.922  15.595  87.124  1.00 28.89           C  
ANISOU 2179  C   THR A 290     3052   4845   3079    699   -386  -1095       C  
ATOM   2180  O   THR A 290      28.223  15.413  86.128  1.00 25.17           O  
ANISOU 2180  O   THR A 290     2613   4302   2649    628   -331  -1044       O  
ATOM   2181  CB  THR A 290      29.363  17.353  88.840  1.00 30.35           C  
ANISOU 2181  CB  THR A 290     3129   5105   3299    742   -463  -1266       C  
ATOM   2182  OG1 THR A 290      27.959  17.424  89.122  1.00 31.16           O  
ANISOU 2182  OG1 THR A 290     3290   5187   3361    712   -415  -1224       O  
ATOM   2183  CG2 THR A 290      29.995  18.709  89.119  1.00 33.21           C  
ANISOU 2183  CG2 THR A 290     3392   5461   3767    722   -501  -1394       C  
ATOM   2184  N   LYS A 291      29.154  14.639  88.017  1.00 27.15           N  
ANISOU 2184  N   LYS A 291     2900   4692   2725    797   -397  -1043       N  
ATOM   2185  CA  LYS A 291      28.480  13.346  87.911  1.00 27.24           C  
ANISOU 2185  CA  LYS A 291     3033   4681   2635    818   -330   -915       C  
ATOM   2186  C   LYS A 291      27.825  12.960  89.238  1.00 27.58           C  
ANISOU 2186  C   LYS A 291     3156   4770   2553    879   -307   -870       C  
ATOM   2187  O   LYS A 291      28.343  12.119  89.976  1.00 27.26           O  
ANISOU 2187  O   LYS A 291     3171   4781   2406    978   -324   -824       O  
ATOM   2188  CB  LYS A 291      29.449  12.251  87.459  1.00 32.04           C  
ANISOU 2188  CB  LYS A 291     3672   5299   3203    882   -345   -861       C  
ATOM   2189  CG  LYS A 291      28.766  10.946  87.073  1.00 30.13           C  
ANISOU 2189  CG  LYS A 291     3558   5002   2890    886   -261   -728       C  
ATOM   2190  CD  LYS A 291      29.780   9.850  86.766  1.00 35.41           C  
ANISOU 2190  CD  LYS A 291     4262   5681   3509    970   -281   -674       C  
ATOM   2191  CE  LYS A 291      29.081   8.542  86.413  1.00 40.51           C  
ANISOU 2191  CE  LYS A 291     5043   6254   4095    971   -188   -539       C  
ATOM   2192  NZ  LYS A 291      30.044   7.427  86.184  1.00 45.20           N  
ANISOU 2192  NZ  LYS A 291     5687   6850   4638   1067   -206   -480       N  
ATOM   2193  N   PRO A 292      26.683  13.589  89.554  1.00 23.31           N  
ANISOU 2193  N   PRO A 292     2621   4210   2025    823   -266   -885       N  
ATOM   2194  CA  PRO A 292      26.005  13.267  90.812  1.00 27.79           C  
ANISOU 2194  CA  PRO A 292     3261   4823   2474    873   -236   -845       C  
ATOM   2195  C   PRO A 292      25.288  11.920  90.738  1.00 29.12           C  
ANISOU 2195  C   PRO A 292     3557   4951   2557    875   -142   -708       C  
ATOM   2196  O   PRO A 292      24.971  11.446  89.649  1.00 24.21           O  
ANISOU 2196  O   PRO A 292     2960   4253   1985    813    -89   -654       O  
ATOM   2197  CB  PRO A 292      24.995  14.407  90.964  1.00 30.19           C  
ANISOU 2197  CB  PRO A 292     3520   5110   2839    802   -216   -909       C  
ATOM   2198  CG  PRO A 292      24.706  14.841  89.585  1.00 27.93           C  
ANISOU 2198  CG  PRO A 292     3189   4739   2684    704   -194   -922       C  
ATOM   2199  CD  PRO A 292      25.978  14.635  88.793  1.00 27.26           C  
ANISOU 2199  CD  PRO A 292     3061   4648   2650    717   -246   -938       C  
ATOM   2200  N   VAL A 293      25.059  11.302  91.892  1.00 27.55           N  
ANISOU 2200  N   VAL A 293     3437   4797   2233    945   -118   -653       N  
ATOM   2201  CA  VAL A 293      24.236  10.100  91.961  1.00 28.60           C  
ANISOU 2201  CA  VAL A 293     3693   4883   2292    934    -15   -525       C  
ATOM   2202  C   VAL A 293      22.764  10.512  91.846  1.00 24.65           C  
ANISOU 2202  C   VAL A 293     3196   4342   1827    834     69   -524       C  
ATOM   2203  O   VAL A 293      22.435  11.683  92.047  1.00 25.86           O  
ANISOU 2203  O   VAL A 293     3272   4522   2032    804     39   -617       O  
ATOM   2204  CB  VAL A 293      24.479   9.337  93.281  1.00 29.51           C  
ANISOU 2204  CB  VAL A 293     3892   5059   2263   1042    -13   -464       C  
ATOM   2205  CG1 VAL A 293      25.941   8.919  93.385  1.00 34.78           C  
ANISOU 2205  CG1 VAL A 293     4549   5768   2898   1153   -100   -469       C  
ATOM   2206  CG2 VAL A 293      24.089  10.196  94.463  1.00 31.73           C  
ANISOU 2206  CG2 VAL A 293     4142   5419   2497   1065    -34   -535       C  
ATOM   2207  N   PRO A 294      21.874   9.564  91.504  1.00 27.14           N  
ANISOU 2207  N   PRO A 294     3595   4591   2125    781    176   -423       N  
ATOM   2208  CA  PRO A 294      20.446   9.908  91.422  1.00 26.01           C  
ANISOU 2208  CA  PRO A 294     3448   4417   2018    689    260   -427       C  
ATOM   2209  C   PRO A 294      19.891  10.431  92.752  1.00 25.86           C  
ANISOU 2209  C   PRO A 294     3431   4470   1924    719    267   -461       C  
ATOM   2210  O   PRO A 294      20.364  10.047  93.822  1.00 25.72           O  
ANISOU 2210  O   PRO A 294     3462   4513   1796    806    247   -436       O  
ATOM   2211  CB  PRO A 294      19.783   8.576  91.058  1.00 26.95           C  
ANISOU 2211  CB  PRO A 294     3665   4464   2110    644    371   -306       C  
ATOM   2212  CG  PRO A 294      20.853   7.804  90.349  1.00 25.03           C  
ANISOU 2212  CG  PRO A 294     3452   4185   1875    685    336   -259       C  
ATOM   2213  CD  PRO A 294      22.145   8.198  91.015  1.00 26.12           C  
ANISOU 2213  CD  PRO A 294     3556   4402   1965    796    222   -312       C  
ATOM   2214  N   HIS A 295      18.897  11.310  92.675  1.00 27.58           N  
ANISOU 2214  N   HIS A 295     3594   4682   2202    654    295   -520       N  
ATOM   2215  CA  HIS A 295      18.318  11.924  93.867  1.00 28.64           C  
ANISOU 2215  CA  HIS A 295     3722   4885   2276    681    303   -565       C  
ATOM   2216  C   HIS A 295      17.293  11.009  94.540  1.00 29.37           C  
ANISOU 2216  C   HIS A 295     3908   4976   2276    661    423   -474       C  
ATOM   2217  O   HIS A 295      16.858  11.271  95.660  1.00 31.92           O  
ANISOU 2217  O   HIS A 295     4246   5363   2521    695    443   -492       O  
ATOM   2218  CB  HIS A 295      17.672  13.264  93.513  1.00 29.78           C  
ANISOU 2218  CB  HIS A 295     3768   5021   2527    627    281   -665       C  
ATOM   2219  CG  HIS A 295      16.483  13.143  92.612  1.00 27.91           C  
ANISOU 2219  CG  HIS A 295     3524   4711   2369    530    368   -635       C  
ATOM   2220  ND1 HIS A 295      16.543  12.538  91.376  1.00 26.97           N  
ANISOU 2220  ND1 HIS A 295     3413   4517   2319    475    393   -584       N  
ATOM   2221  CD2 HIS A 295      15.200  13.551  92.768  1.00 27.03           C  
ANISOU 2221  CD2 HIS A 295     3393   4597   2282    484    432   -653       C  
ATOM   2222  CE1 HIS A 295      15.351  12.582  90.807  1.00 24.92           C  
ANISOU 2222  CE1 HIS A 295     3136   4211   2123    399    466   -573       C  
ATOM   2223  NE2 HIS A 295      14.517  13.188  91.633  1.00 26.65           N  
ANISOU 2223  NE2 HIS A 295     3336   4474   2318    404    490   -613       N  
ATOM   2224  N   LEU A 296      16.905   9.944  93.845  1.00 29.89           N  
ANISOU 2224  N   LEU A 296     4032   4967   2356    603    507   -381       N  
ATOM   2225  CA  LEU A 296      15.994   8.949  94.399  1.00 30.42           C  
ANISOU 2225  CA  LEU A 296     4188   5021   2348    569    629   -288       C  
ATOM   2226  C   LEU A 296      16.697   7.599  94.435  1.00 30.12           C  
ANISOU 2226  C   LEU A 296     4247   4954   2242    610    645   -177       C  
ATOM   2227  O   LEU A 296      17.556   7.323  93.603  1.00 28.54           O  
ANISOU 2227  O   LEU A 296     4042   4713   2088    627    592   -164       O  
ATOM   2228  CB  LEU A 296      14.729   8.839  93.546  1.00 32.95           C  
ANISOU 2228  CB  LEU A 296     4488   5272   2761    450    728   -277       C  
ATOM   2229  CG  LEU A 296      13.897  10.095  93.298  1.00 38.54           C  
ANISOU 2229  CG  LEU A 296     5098   5988   3556    411    720   -374       C  
ATOM   2230  CD1 LEU A 296      12.782   9.783  92.313  1.00 42.06           C  
ANISOU 2230  CD1 LEU A 296     5526   6357   4098    309    811   -348       C  
ATOM   2231  CD2 LEU A 296      13.331  10.654  94.591  1.00 41.65           C  
ANISOU 2231  CD2 LEU A 296     5491   6460   3874    447    740   -413       C  
ATOM   2232  N   ARG A 297      16.330   6.758  95.395  1.00 24.86           N  
ANISOU 2232  N   ARG A 297     3671   4307   1469    628    719    -93       N  
ATOM   2233  CA  ARG A 297      16.897   5.416  95.478  1.00 26.52           C  
ANISOU 2233  CA  ARG A 297     3982   4475   1619    672    741     26       C  
ATOM   2234  C   ARG A 297      16.355   4.582  94.323  1.00 31.20           C  
ANISOU 2234  C   ARG A 297     4593   4961   2300    568    820     90       C  
ATOM   2235  O   ARG A 297      15.165   4.642  94.015  1.00 36.80           O  
ANISOU 2235  O   ARG A 297     5272   5648   3063    457    906     81       O  
ATOM   2236  CB  ARG A 297      16.531   4.772  96.821  1.00 30.37           C  
ANISOU 2236  CB  ARG A 297     4559   5007   1974    714    807    102       C  
ATOM   2237  CG  ARG A 297      17.602   3.857  97.398  1.00 39.76           C  
ANISOU 2237  CG  ARG A 297     5842   6199   3067    838    768    189       C  
ATOM   2238  CD  ARG A 297      17.186   3.331  98.767  1.00 44.94           C  
ANISOU 2238  CD  ARG A 297     6584   6904   3588    882    835    261       C  
ATOM   2239  NE  ARG A 297      16.730   4.405  99.646  1.00 52.53           N  
ANISOU 2239  NE  ARG A 297     7490   7969   4499    893    823    170       N  
ATOM   2240  CZ  ARG A 297      17.382   4.823 100.725  1.00 56.83           C  
ANISOU 2240  CZ  ARG A 297     8041   8614   4939   1014    749    134       C  
ATOM   2241  NH1 ARG A 297      18.525   4.251 101.078  1.00 57.81           N  
ANISOU 2241  NH1 ARG A 297     8220   8753   4994   1138    681    183       N  
ATOM   2242  NH2 ARG A 297      16.883   5.811 101.457  1.00 61.95           N  
ANISOU 2242  NH2 ARG A 297     8638   9349   5553   1015    743     46       N  
ATOM   2243  N   LEU A 298      17.228   3.823  93.668  1.00 34.74           N  
ANISOU 2243  N   LEU A 298     5084   5346   2768    605    788    147       N  
ATOM   2244  CA  LEU A 298      16.807   2.995  92.544  1.00 43.98           C  
ANISOU 2244  CA  LEU A 298     6275   6409   4027    515    854    206       C  
ATOM   2245  C   LEU A 298      16.325   1.626  93.015  1.00 61.77           C  
ANISOU 2245  C   LEU A 298     8638   8602   6232    499    956    334       C  
ATOM   2246  O   LEU A 298      17.115   0.798  93.470  1.00 68.09           O  
ANISOU 2246  O   LEU A 298     9532   9377   6964    594    941    414       O  
ATOM   2247  CB  LEU A 298      17.937   2.847  91.523  1.00 40.53           C  
ANISOU 2247  CB  LEU A 298     5832   5923   3647    560    777    200       C  
ATOM   2248  CG  LEU A 298      18.393   4.142  90.850  1.00 30.45           C  
ANISOU 2248  CG  LEU A 298     4440   4689   2440    560    682     79       C  
ATOM   2249  CD1 LEU A 298      19.310   3.845  89.672  1.00 27.85           C  
ANISOU 2249  CD1 LEU A 298     4105   4301   2177    578    633     84       C  
ATOM   2250  CD2 LEU A 298      17.202   4.971  90.397  1.00 32.30           C  
ANISOU 2250  CD2 LEU A 298     4590   4927   2756    446    728      8       C  
ATOM   2251  OXT LEU A 298      15.133   1.316  92.950  1.00 66.73           O  
ANISOU 2251  OXT LEU A 298     9258   9204   6895    394   1055    359       O  
TER    2252      LEU A 298                                                      
ATOM   2253  N   ASN B 173      21.777  14.611  51.813  1.00 42.59           N  
ANISOU 2253  N   ASN B 173     5005   4766   6413    436    202   -484       N  
ATOM   2254  CA  ASN B 173      22.206  13.298  52.287  1.00 38.80           C  
ANISOU 2254  CA  ASN B 173     4526   4362   5856    376    229   -503       C  
ATOM   2255  C   ASN B 173      23.622  13.300  52.876  1.00 35.98           C  
ANISOU 2255  C   ASN B 173     4239   4003   5427    319    258   -516       C  
ATOM   2256  O   ASN B 173      24.125  12.269  53.335  1.00 25.82           O  
ANISOU 2256  O   ASN B 173     2965   2775   4069    272    279   -530       O  
ATOM   2257  CB  ASN B 173      22.087  12.258  51.167  1.00 40.74           C  
ANISOU 2257  CB  ASN B 173     4749   4642   6089    384    172   -450       C  
ATOM   2258  CG  ASN B 173      22.662  12.745  49.855  1.00 46.46           C  
ANISOU 2258  CG  ASN B 173     5516   5311   6825    416    103   -375       C  
ATOM   2259  OD1 ASN B 173      23.193  13.855  49.771  1.00 46.28           O  
ANISOU 2259  OD1 ASN B 173     5544   5220   6820    427    103   -360       O  
ATOM   2260  ND2 ASN B 173      22.565  11.914  48.821  1.00 45.21           N  
ANISOU 2260  ND2 ASN B 173     5344   5181   6653    426     46   -327       N  
ATOM   2261  N   GLU B 174      24.269  14.459  52.869  1.00 38.07           N  
ANISOU 2261  N   GLU B 174     4551   4202   5712    323    258   -514       N  
ATOM   2262  CA  GLU B 174      25.605  14.549  53.438  1.00 39.24           C  
ANISOU 2262  CA  GLU B 174     4757   4352   5802    266    281   -535       C  
ATOM   2263  C   GLU B 174      25.544  14.628  54.964  1.00 39.33           C  
ANISOU 2263  C   GLU B 174     4769   4397   5779    231    340   -611       C  
ATOM   2264  O   GLU B 174      24.545  15.071  55.536  1.00 42.15           O  
ANISOU 2264  O   GLU B 174     5093   4746   6177    256    371   -649       O  
ATOM   2265  CB  GLU B 174      26.382  15.731  52.848  1.00 49.62           C  
ANISOU 2265  CB  GLU B 174     6122   5581   7149    269    263   -506       C  
ATOM   2266  CG  GLU B 174      26.632  15.612  51.350  1.00 53.97           C  
ANISOU 2266  CG  GLU B 174     6693   6099   7714    292    207   -423       C  
ATOM   2267  CD  GLU B 174      27.701  16.566  50.850  1.00 60.58           C  
ANISOU 2267  CD  GLU B 174     7596   6860   8561    269    202   -393       C  
ATOM   2268  OE1 GLU B 174      28.745  16.705  51.526  1.00 62.20           O  
ANISOU 2268  OE1 GLU B 174     7828   7075   8732    209    234   -434       O  
ATOM   2269  OE2 GLU B 174      27.499  17.176  49.778  1.00 62.81           O  
ANISOU 2269  OE2 GLU B 174     7906   7075   8883    307    166   -328       O  
ATOM   2270  N   VAL B 175      26.616  14.169  55.610  1.00 33.41           N  
ANISOU 2270  N   VAL B 175     4056   3687   4951    176    354   -633       N  
ATOM   2271  CA  VAL B 175      26.742  14.172  57.066  1.00 35.61           C  
ANISOU 2271  CA  VAL B 175     4350   4003   5177    139    400   -699       C  
ATOM   2272  C   VAL B 175      28.067  14.834  57.441  1.00 43.46           C  
ANISOU 2272  C   VAL B 175     5394   4978   6143     98    396   -724       C  
ATOM   2273  O   VAL B 175      28.899  14.216  58.109  1.00 46.88           O  
ANISOU 2273  O   VAL B 175     5851   5465   6495     55    396   -745       O  
ATOM   2274  CB  VAL B 175      26.737  12.727  57.636  1.00 50.43           C  
ANISOU 2274  CB  VAL B 175     6228   5966   6969    110    413   -703       C  
ATOM   2275  CG1 VAL B 175      26.380  12.728  59.118  1.00 53.02           C  
ANISOU 2275  CG1 VAL B 175     6567   6327   7250     85    467   -765       C  
ATOM   2276  CG2 VAL B 175      25.770  11.840  56.860  1.00 52.08           C  
ANISOU 2276  CG2 VAL B 175     6390   6195   7203    139    402   -664       C  
ATOM   2277  N   PRO B 176      28.261  16.101  57.024  1.00 42.07           N  
ANISOU 2277  N   PRO B 176     5232   4721   6032    111    391   -722       N  
ATOM   2278  CA  PRO B 176      29.586  16.744  57.039  1.00 34.78           C  
ANISOU 2278  CA  PRO B 176     4349   3769   5098     66    381   -735       C  
ATOM   2279  C   PRO B 176      30.309  16.652  58.385  1.00 29.14           C  
ANISOU 2279  C   PRO B 176     3656   3106   4309     13    400   -804       C  
ATOM   2280  O   PRO B 176      31.535  16.555  58.411  1.00 30.67           O  
ANISOU 2280  O   PRO B 176     3869   3319   4466    -33    379   -810       O  
ATOM   2281  CB  PRO B 176      29.272  18.204  56.687  1.00 37.93           C  
ANISOU 2281  CB  PRO B 176     4761   4067   5582     93    390   -736       C  
ATOM   2282  CG  PRO B 176      27.827  18.379  57.023  1.00 43.92           C  
ANISOU 2282  CG  PRO B 176     5486   4818   6383    146    415   -754       C  
ATOM   2283  CD  PRO B 176      27.190  17.066  56.718  1.00 43.79           C  
ANISOU 2283  CD  PRO B 176     5430   4871   6339    165    401   -720       C  
ATOM   2284  N   ASP B 177      29.557  16.644  59.480  1.00 22.67           N  
ANISOU 2284  N   ASP B 177     2832   2313   3467     17    438   -854       N  
ATOM   2285  CA  ASP B 177      30.161  16.652  60.809  1.00 24.17           C  
ANISOU 2285  CA  ASP B 177     3052   2549   3582    -29    454   -920       C  
ATOM   2286  C   ASP B 177      30.888  15.352  61.161  1.00 22.64           C  
ANISOU 2286  C   ASP B 177     2872   2444   3287    -59    427   -910       C  
ATOM   2287  O   ASP B 177      31.775  15.351  62.015  1.00 25.94           O  
ANISOU 2287  O   ASP B 177     3318   2899   3638   -100    415   -952       O  
ATOM   2288  CB  ASP B 177      29.106  16.944  61.875  1.00 28.91           C  
ANISOU 2288  CB  ASP B 177     3651   3153   4179    -16    507   -974       C  
ATOM   2289  CG  ASP B 177      28.510  18.329  61.740  1.00 33.77           C  
ANISOU 2289  CG  ASP B 177     4260   3680   4890     12    535  -1000       C  
ATOM   2290  OD1 ASP B 177      29.237  19.257  61.317  1.00 31.84           O  
ANISOU 2290  OD1 ASP B 177     4036   3374   4687      0    518  -1001       O  
ATOM   2291  OD2 ASP B 177      27.314  18.482  62.058  1.00 32.26           O  
ANISOU 2291  OD2 ASP B 177     4044   3479   4735     47    575  -1020       O  
ATOM   2292  N   TYR B 178      30.508  14.251  60.520  1.00 15.98           N  
ANISOU 2292  N   TYR B 178     2008   1632   2431    -36    414   -855       N  
ATOM   2293  CA  TYR B 178      31.083  12.952  60.871  1.00 15.73           C  
ANISOU 2293  CA  TYR B 178     1994   1679   2304    -56    392   -842       C  
ATOM   2294  C   TYR B 178      31.821  12.252  59.743  1.00 14.62           C  
ANISOU 2294  C   TYR B 178     1841   1548   2165    -53    348   -787       C  
ATOM   2295  O   TYR B 178      32.309  11.139  59.935  1.00 14.53           O  
ANISOU 2295  O   TYR B 178     1843   1597   2079    -63    327   -773       O  
ATOM   2296  CB  TYR B 178      30.003  12.014  61.430  1.00 13.73           C  
ANISOU 2296  CB  TYR B 178     1740   1470   2008    -41    427   -836       C  
ATOM   2297  CG  TYR B 178      29.427  12.506  62.740  1.00 13.59           C  
ANISOU 2297  CG  TYR B 178     1742   1458   1963    -53    476   -897       C  
ATOM   2298  CD1 TYR B 178      30.093  12.276  63.941  1.00 14.00           C  
ANISOU 2298  CD1 TYR B 178     1845   1560   1914    -87    473   -937       C  
ATOM   2299  CD2 TYR B 178      28.229  13.217  62.776  1.00 14.80           C  
ANISOU 2299  CD2 TYR B 178     1864   1569   2191    -28    522   -918       C  
ATOM   2300  CE1 TYR B 178      29.578  12.727  65.151  1.00 14.97           C  
ANISOU 2300  CE1 TYR B 178     1993   1689   2004   -100    520   -995       C  
ATOM   2301  CE2 TYR B 178      27.707  13.678  63.981  1.00 18.04           C  
ANISOU 2301  CE2 TYR B 178     2293   1984   2578    -40    574   -980       C  
ATOM   2302  CZ  TYR B 178      28.387  13.427  65.167  1.00 15.57           C  
ANISOU 2302  CZ  TYR B 178     2038   1721   2159    -78    575  -1018       C  
ATOM   2303  OH  TYR B 178      27.884  13.880  66.366  1.00 16.73           O  
ANISOU 2303  OH  TYR B 178     2209   1874   2275    -93    628  -1081       O  
ATOM   2304  N   HIS B 179      31.896  12.883  58.572  1.00 15.11           N  
ANISOU 2304  N   HIS B 179     1884   1548   2309    -39    335   -754       N  
ATOM   2305  CA  HIS B 179      32.520  12.247  57.401  1.00 14.95           C  
ANISOU 2305  CA  HIS B 179     1854   1530   2295    -37    301   -701       C  
ATOM   2306  C   HIS B 179      33.920  11.721  57.688  1.00 11.55           C  
ANISOU 2306  C   HIS B 179     1435   1152   1800    -76    270   -719       C  
ATOM   2307  O   HIS B 179      34.250  10.576  57.350  1.00 14.55           O  
ANISOU 2307  O   HIS B 179     1813   1578   2137    -70    248   -691       O  
ATOM   2308  CB  HIS B 179      32.612  13.239  56.240  1.00 23.52           C  
ANISOU 2308  CB  HIS B 179     2934   2533   3469    -27    294   -668       C  
ATOM   2309  CG  HIS B 179      31.305  13.499  55.562  1.00 31.33           C  
ANISOU 2309  CG  HIS B 179     3905   3475   4522     25    302   -631       C  
ATOM   2310  ND1 HIS B 179      31.176  14.387  54.515  1.00 35.91           N  
ANISOU 2310  ND1 HIS B 179     4491   3975   5177     47    291   -590       N  
ATOM   2311  CD2 HIS B 179      30.073  12.986  55.778  1.00 33.45           C  
ANISOU 2311  CD2 HIS B 179     4150   3769   4793     60    316   -627       C  
ATOM   2312  CE1 HIS B 179      29.917  14.407  54.113  1.00 38.35           C  
ANISOU 2312  CE1 HIS B 179     4776   4265   5530     99    289   -564       C  
ATOM   2313  NE2 HIS B 179      29.227  13.565  54.861  1.00 34.35           N  
ANISOU 2313  NE2 HIS B 179     4244   3823   4985    105    306   -590       N  
ATOM   2314  N   GLU B 180      34.745  12.560  58.301  1.00 14.06           N  
ANISOU 2314  N   GLU B 180     1762   1465   2116   -114    264   -768       N  
ATOM   2315  CA  GLU B 180      36.135  12.184  58.557  1.00 16.02           C  
ANISOU 2315  CA  GLU B 180     2006   1766   2313   -153    225   -792       C  
ATOM   2316  C   GLU B 180      36.256  11.064  59.597  1.00 14.09           C  
ANISOU 2316  C   GLU B 180     1781   1610   1963   -149    204   -809       C  
ATOM   2317  O   GLU B 180      37.030  10.120  59.411  1.00 12.46           O  
ANISOU 2317  O   GLU B 180     1565   1456   1711   -149    166   -796       O  
ATOM   2318  CB  GLU B 180      36.967  13.403  58.981  1.00 21.89           C  
ANISOU 2318  CB  GLU B 180     2749   2485   3084   -201    222   -845       C  
ATOM   2319  CG  GLU B 180      38.441  13.076  59.179  1.00 30.11           C  
ANISOU 2319  CG  GLU B 180     3768   3587   4086   -243    174   -873       C  
ATOM   2320  CD  GLU B 180      39.252  14.260  59.684  1.00 47.73           C  
ANISOU 2320  CD  GLU B 180     5993   5800   6341   -297    170   -931       C  
ATOM   2321  OE1 GLU B 180      38.710  15.386  59.734  1.00 51.22           O  
ANISOU 2321  OE1 GLU B 180     6455   6170   6837   -301    209   -945       O  
ATOM   2322  OE2 GLU B 180      40.435  14.060  60.035  1.00 52.29           O  
ANISOU 2322  OE2 GLU B 180     6544   6439   6886   -333    126   -964       O  
ATOM   2323  N   ASP B 181      35.499  11.172  60.689  1.00 13.03           N  
ANISOU 2323  N   ASP B 181     1676   1487   1787   -143    231   -837       N  
ATOM   2324  CA  ASP B 181      35.485  10.127  61.707  1.00 15.62           C  
ANISOU 2324  CA  ASP B 181     2040   1889   2007   -139    219   -844       C  
ATOM   2325  C   ASP B 181      35.115   8.793  61.080  1.00 14.71           C  
ANISOU 2325  C   ASP B 181     1923   1797   1868   -107    218   -784       C  
ATOM   2326  O   ASP B 181      35.747   7.768  61.337  1.00 11.21           O  
ANISOU 2326  O   ASP B 181     1499   1414   1348   -104    181   -773       O  
ATOM   2327  CB  ASP B 181      34.442  10.423  62.803  1.00 14.03           C  
ANISOU 2327  CB  ASP B 181     1872   1683   1775   -137    268   -873       C  
ATOM   2328  CG  ASP B 181      34.769  11.642  63.643  1.00 22.26           C  
ANISOU 2328  CG  ASP B 181     2928   2709   2822   -168    272   -940       C  
ATOM   2329  OD1 ASP B 181      35.930  12.122  63.637  1.00 20.19           O  
ANISOU 2329  OD1 ASP B 181     2655   2454   2563   -200    229   -969       O  
ATOM   2330  OD2 ASP B 181      33.835  12.112  64.341  1.00 19.97           O  
ANISOU 2330  OD2 ASP B 181     2656   2399   2533   -164    322   -969       O  
ATOM   2331  N   ILE B 182      34.065   8.805  60.264  1.00 10.56           N  
ANISOU 2331  N   ILE B 182     1378   1226   1409    -82    254   -747       N  
ATOM   2332  CA  ILE B 182      33.576   7.576  59.659  1.00  9.92           C  
ANISOU 2332  CA  ILE B 182     1296   1162   1312    -56    259   -694       C  
ATOM   2333  C   ILE B 182      34.595   6.965  58.700  1.00 11.38           C  
ANISOU 2333  C   ILE B 182     1464   1364   1496    -50    210   -650       C  
ATOM   2334  O   ILE B 182      34.829   5.762  58.729  1.00 10.93           O  
ANISOU 2334  O   ILE B 182     1423   1351   1377    -36    189   -606       O  
ATOM   2335  CB  ILE B 182      32.200   7.790  58.973  1.00  9.77           C  
ANISOU 2335  CB  ILE B 182     1248   1095   1369    -31    298   -666       C  
ATOM   2336  CG1 ILE B 182      31.145   8.072  60.061  1.00 12.41           C  
ANISOU 2336  CG1 ILE B 182     1594   1431   1689    -34    347   -698       C  
ATOM   2337  CG2 ILE B 182      31.812   6.569  58.161  1.00 10.17           C  
ANISOU 2337  CG2 ILE B 182     1291   1159   1413    -11    296   -614       C  
ATOM   2338  CD1 ILE B 182      29.813   8.624  59.543  1.00 13.22           C  
ANISOU 2338  CD1 ILE B 182     1653   1488   1883    -10    381   -691       C  
ATOM   2339  N   HIS B 183      35.217   7.801  57.876  1.00 12.12           N  
ANISOU 2339  N   HIS B 183     1526   1421   1657    -61    193   -646       N  
ATOM   2340  CA  HIS B 183      36.239   7.314  56.954  1.00 11.87           C  
ANISOU 2340  CA  HIS B 183     1473   1410   1628    -60    152   -595       C  
ATOM   2341  C   HIS B 183      37.378   6.661  57.716  1.00 10.39           C  
ANISOU 2341  C   HIS B 183     1290   1293   1366    -66    106   -609       C  
ATOM   2342  O   HIS B 183      37.825   5.569  57.359  1.00 11.71           O  
ANISOU 2342  O   HIS B 183     1455   1496   1498    -43     79   -560       O  
ATOM   2343  CB  HIS B 183      36.771   8.451  56.084  1.00 14.55           C  
ANISOU 2343  CB  HIS B 183     1786   1696   2047    -83    153   -597       C  
ATOM   2344  CG  HIS B 183      37.847   8.024  55.137  1.00 12.34           C  
ANISOU 2344  CG  HIS B 183     1481   1438   1771    -89    126   -552       C  
ATOM   2345  ND1 HIS B 183      39.190   8.223  55.393  1.00 14.40           N  
ANISOU 2345  ND1 HIS B 183     1714   1733   2025   -121     98   -585       N  
ATOM   2346  CD2 HIS B 183      37.786   7.381  53.947  1.00 13.71           C  
ANISOU 2346  CD2 HIS B 183     1649   1607   1952    -70    125   -485       C  
ATOM   2347  CE1 HIS B 183      39.903   7.733  54.396  1.00 12.26           C  
ANISOU 2347  CE1 HIS B 183     1417   1477   1764   -118     89   -539       C  
ATOM   2348  NE2 HIS B 183      39.077   7.218  53.502  1.00 13.62           N  
ANISOU 2348  NE2 HIS B 183     1609   1626   1941    -88    107   -478       N  
ATOM   2349  N   THR B 184      37.845   7.330  58.767  1.00 13.08           N  
ANISOU 2349  N   THR B 184     1637   1651   1680    -95     94   -679       N  
ATOM   2350  CA  THR B 184      38.921   6.789  59.592  1.00 13.41           C  
ANISOU 2350  CA  THR B 184     1681   1767   1647    -98     36   -699       C  
ATOM   2351  C   THR B 184      38.513   5.456  60.193  1.00 15.41           C  
ANISOU 2351  C   THR B 184     1983   2063   1809    -62     27   -660       C  
ATOM   2352  O   THR B 184      39.293   4.498  60.209  1.00 14.71           O  
ANISOU 2352  O   THR B 184     1892   2022   1676    -36    -23   -624       O  
ATOM   2353  CB  THR B 184      39.312   7.770  60.706  1.00 15.33           C  
ANISOU 2353  CB  THR B 184     1932   2023   1868   -140     24   -791       C  
ATOM   2354  OG1 THR B 184      39.924   8.923  60.113  1.00 17.36           O  
ANISOU 2354  OG1 THR B 184     2143   2239   2213   -180     28   -825       O  
ATOM   2355  CG2 THR B 184      40.296   7.124  61.686  1.00 20.70           C  
ANISOU 2355  CG2 THR B 184     2621   2791   2454   -136    -50   -810       C  
ATOM   2356  N   TYR B 185      37.281   5.390  60.688  1.00 13.61           N  
ANISOU 2356  N   TYR B 185     1800   1815   1557    -60     80   -667       N  
ATOM   2357  CA  TYR B 185      36.776   4.138  61.246  1.00 12.43           C  
ANISOU 2357  CA  TYR B 185     1706   1694   1322    -36     87   -627       C  
ATOM   2358  C   TYR B 185      36.695   3.004  60.220  1.00 11.10           C  
ANISOU 2358  C   TYR B 185     1528   1516   1172     -3     83   -546       C  
ATOM   2359  O   TYR B 185      37.102   1.874  60.512  1.00 13.98           O  
ANISOU 2359  O   TYR B 185     1928   1915   1471     23     51   -505       O  
ATOM   2360  CB  TYR B 185      35.409   4.340  61.913  1.00 14.22           C  
ANISOU 2360  CB  TYR B 185     1972   1898   1532    -50    162   -657       C  
ATOM   2361  CG  TYR B 185      34.903   3.078  62.577  1.00 17.46           C  
ANISOU 2361  CG  TYR B 185     2450   2336   1849    -38    181   -618       C  
ATOM   2362  CD1 TYR B 185      35.637   2.474  63.591  1.00 23.85           C  
ANISOU 2362  CD1 TYR B 185     3318   3199   2545    -33    133   -614       C  
ATOM   2363  CD2 TYR B 185      33.697   2.497  62.202  1.00 20.16           C  
ANISOU 2363  CD2 TYR B 185     2798   2648   2215    -35    244   -586       C  
ATOM   2364  CE1 TYR B 185      35.197   1.322  64.212  1.00 27.63           C  
ANISOU 2364  CE1 TYR B 185     3874   3692   2932    -24    154   -570       C  
ATOM   2365  CE2 TYR B 185      33.238   1.332  62.829  1.00 21.26           C  
ANISOU 2365  CE2 TYR B 185     3005   2803   2268    -35    271   -550       C  
ATOM   2366  CZ  TYR B 185      34.000   0.757  63.836  1.00 27.02           C  
ANISOU 2366  CZ  TYR B 185     3807   3579   2883    -29    229   -539       C  
ATOM   2367  OH  TYR B 185      33.586  -0.392  64.478  1.00 30.01           O  
ANISOU 2367  OH  TYR B 185     4269   3965   3170    -30    257   -495       O  
ATOM   2368  N   LEU B 186      36.177   3.293  59.027  1.00 10.43           N  
ANISOU 2368  N   LEU B 186     1404   1384   1173     -1    112   -523       N  
ATOM   2369  CA  LEU B 186      36.111   2.283  57.974  1.00 10.01           C  
ANISOU 2369  CA  LEU B 186     1344   1322   1136     24    108   -456       C  
ATOM   2370  C   LEU B 186      37.517   1.812  57.585  1.00 13.08           C  
ANISOU 2370  C   LEU B 186     1710   1743   1516     43     51   -433       C  
ATOM   2371  O   LEU B 186      37.722   0.634  57.288  1.00 11.35           O  
ANISOU 2371  O   LEU B 186     1510   1535   1270     72     38   -385       O  
ATOM   2372  CB  LEU B 186      35.390   2.809  56.728  1.00 11.18           C  
ANISOU 2372  CB  LEU B 186     1456   1421   1372     20    137   -439       C  
ATOM   2373  CG  LEU B 186      33.920   3.195  56.932  1.00 15.70           C  
ANISOU 2373  CG  LEU B 186     2031   1961   1973     12    190   -459       C  
ATOM   2374  CD1 LEU B 186      33.340   3.703  55.624  1.00 20.23           C  
ANISOU 2374  CD1 LEU B 186     2566   2490   2630     19    196   -435       C  
ATOM   2375  CD2 LEU B 186      33.112   2.012  57.463  1.00 15.33           C  
ANISOU 2375  CD2 LEU B 186     2024   1930   1870     15    220   -440       C  
ATOM   2376  N   ARG B 187      38.476   2.731  57.573  1.00 11.03           N  
ANISOU 2376  N   ARG B 187     1409   1496   1287     24     23   -471       N  
ATOM   2377  CA  ARG B 187      39.866   2.348  57.284  1.00 10.24           C  
ANISOU 2377  CA  ARG B 187     1269   1434   1187     40    -28   -461       C  
ATOM   2378  C   ARG B 187      40.434   1.393  58.346  1.00 17.45           C  
ANISOU 2378  C   ARG B 187     2215   2401   2015     74    -80   -455       C  
ATOM   2379  O   ARG B 187      41.248   0.522  58.031  1.00 18.31           O  
ANISOU 2379  O   ARG B 187     2306   2533   2117    112   -116   -423       O  
ATOM   2380  CB  ARG B 187      40.756   3.590  57.113  1.00 11.72           C  
ANISOU 2380  CB  ARG B 187     1399   1624   1431      2    -41   -512       C  
ATOM   2381  CG  ARG B 187      40.529   4.330  55.782  1.00 12.20           C  
ANISOU 2381  CG  ARG B 187     1431   1629   1576    -22      2   -495       C  
ATOM   2382  CD  ARG B 187      41.151   3.581  54.596  1.00 13.08           C  
ANISOU 2382  CD  ARG B 187     1514   1748   1708     -2      1   -447       C  
ATOM   2383  NE  ARG B 187      42.597   3.482  54.767  1.00 13.46           N  
ANISOU 2383  NE  ARG B 187     1507   1847   1761     -2    -39   -473       N  
ATOM   2384  CZ  ARG B 187      43.478   4.370  54.307  1.00 16.16           C  
ANISOU 2384  CZ  ARG B 187     1791   2187   2160    -44    -32   -504       C  
ATOM   2385  NH1 ARG B 187      43.079   5.424  53.598  1.00 12.94           N  
ANISOU 2385  NH1 ARG B 187     1390   1721   1806    -87     14   -504       N  
ATOM   2386  NH2 ARG B 187      44.768   4.199  54.556  1.00 13.99           N  
ANISOU 2386  NH2 ARG B 187     1453   1969   1892    -44    -72   -535       N  
ATOM   2387  N   GLU B 188      40.003   1.556  59.596  1.00 16.21           N  
ANISOU 2387  N   GLU B 188     2108   2261   1790     63    -83   -485       N  
ATOM   2388  CA  GLU B 188      40.377   0.630  60.671  1.00 16.11           C  
ANISOU 2388  CA  GLU B 188     2150   2295   1678     96   -133   -468       C  
ATOM   2389  C   GLU B 188      39.729  -0.720  60.451  1.00 17.27           C  
ANISOU 2389  C   GLU B 188     2354   2415   1791    131   -107   -398       C  
ATOM   2390  O   GLU B 188      40.382  -1.762  60.525  1.00 20.66           O  
ANISOU 2390  O   GLU B 188     2801   2862   2185    179   -152   -355       O  
ATOM   2391  CB  GLU B 188      39.899   1.138  62.030  1.00 17.04           C  
ANISOU 2391  CB  GLU B 188     2325   2431   1718     67   -126   -517       C  
ATOM   2392  CG  GLU B 188      40.694   2.244  62.653  1.00 35.48           C  
ANISOU 2392  CG  GLU B 188     4625   4806   4051     35   -171   -594       C  
ATOM   2393  CD  GLU B 188      40.072   2.701  63.961  1.00 48.20           C  
ANISOU 2393  CD  GLU B 188     6306   6430   5577      4   -151   -646       C  
ATOM   2394  OE1 GLU B 188      39.552   1.835  64.707  1.00 49.56           O  
ANISOU 2394  OE1 GLU B 188     6563   6616   5653     22   -141   -611       O  
ATOM   2395  OE2 GLU B 188      40.083   3.922  64.229  1.00 51.92           O  
ANISOU 2395  OE2 GLU B 188     6754   6895   6077    -42   -138   -723       O  
ATOM   2396  N   MET B 189      38.427  -0.705  60.185  1.00 15.53           N  
ANISOU 2396  N   MET B 189     2163   2151   1589    108    -33   -388       N  
ATOM   2397  CA  MET B 189      37.668  -1.947  60.108  1.00 15.76           C  
ANISOU 2397  CA  MET B 189     2252   2152   1584    125      1   -331       C  
ATOM   2398  C   MET B 189      37.943  -2.793  58.862  1.00 17.48           C  
ANISOU 2398  C   MET B 189     2445   2345   1852    156     -2   -282       C  
ATOM   2399  O   MET B 189      37.811  -4.014  58.916  1.00 19.89           O  
ANISOU 2399  O   MET B 189     2805   2633   2120    182      1   -234       O  
ATOM   2400  CB  MET B 189      36.168  -1.682  60.255  1.00 15.81           C  
ANISOU 2400  CB  MET B 189     2284   2126   1598     86     82   -346       C  
ATOM   2401  CG  MET B 189      35.781  -1.039  61.591  1.00 18.49           C  
ANISOU 2401  CG  MET B 189     2664   2487   1873     57    102   -396       C  
ATOM   2402  SD  MET B 189      36.441  -1.874  63.063  1.00 36.75           S  
ANISOU 2402  SD  MET B 189     5075   4847   4041     78     53   -375       S  
ATOM   2403  CE  MET B 189      35.554  -3.430  63.003  1.00 36.14           C  
ANISOU 2403  CE  MET B 189     5079   4728   3924     86    109   -300       C  
ATOM   2404  N   GLU B 190      38.320  -2.167  57.745  1.00 15.04           N  
ANISOU 2404  N   GLU B 190     2063   2027   1624    149     -4   -295       N  
ATOM   2405  CA  GLU B 190      38.533  -2.939  56.518  1.00 15.19           C  
ANISOU 2405  CA  GLU B 190     2065   2024   1684    172      1   -256       C  
ATOM   2406  C   GLU B 190      39.731  -3.867  56.657  1.00 16.43           C  
ANISOU 2406  C   GLU B 190     2224   2204   1815    226    -51   -232       C  
ATOM   2407  O   GLU B 190      39.822  -4.882  55.974  1.00 17.72           O  
ANISOU 2407  O   GLU B 190     2402   2343   1989    255    -42   -196       O  
ATOM   2408  CB  GLU B 190      38.684  -2.036  55.278  1.00 14.28           C  
ANISOU 2408  CB  GLU B 190     1882   1895   1649    149     16   -272       C  
ATOM   2409  CG  GLU B 190      39.994  -1.252  55.222  1.00 12.43           C  
ANISOU 2409  CG  GLU B 190     1585   1695   1445    148    -23   -304       C  
ATOM   2410  CD  GLU B 190      40.178  -0.527  53.884  1.00 16.52           C  
ANISOU 2410  CD  GLU B 190     2052   2192   2034    122      3   -306       C  
ATOM   2411  OE1 GLU B 190      39.417  -0.820  52.936  1.00 12.20           O  
ANISOU 2411  OE1 GLU B 190     1521   1610   1504    118     36   -277       O  
ATOM   2412  OE2 GLU B 190      41.076   0.328  53.791  1.00 14.02           O  
ANISOU 2412  OE2 GLU B 190     1682   1892   1751    103    -12   -338       O  
ATOM   2413  N   VAL B 191      40.649  -3.522  57.550  1.00 13.90           N  
ANISOU 2413  N   VAL B 191     1887   1930   1463    241   -108   -256       N  
ATOM   2414  CA  VAL B 191      41.783  -4.389  57.808  1.00 19.52           C  
ANISOU 2414  CA  VAL B 191     2595   2670   2153    304   -170   -234       C  
ATOM   2415  C   VAL B 191      41.334  -5.584  58.655  1.00 25.85           C  
ANISOU 2415  C   VAL B 191     3499   3451   2871    339   -176   -184       C  
ATOM   2416  O   VAL B 191      41.794  -6.707  58.460  1.00 32.99           O  
ANISOU 2416  O   VAL B 191     4426   4338   3769    396   -197   -142       O  
ATOM   2417  CB  VAL B 191      42.918  -3.622  58.495  1.00 24.36           C  
ANISOU 2417  CB  VAL B 191     3148   3347   2760    308   -241   -281       C  
ATOM   2418  CG1 VAL B 191      44.060  -4.560  58.857  1.00 29.01           C  
ANISOU 2418  CG1 VAL B 191     3727   3969   3326    384   -318   -257       C  
ATOM   2419  CG2 VAL B 191      43.398  -2.492  57.585  1.00 25.46           C  
ANISOU 2419  CG2 VAL B 191     3191   3494   2988    265   -223   -327       C  
ATOM   2420  N   LYS B 192      40.409  -5.338  59.576  1.00 25.29           N  
ANISOU 2420  N   LYS B 192     3494   3377   2737    302   -150   -189       N  
ATOM   2421  CA  LYS B 192      39.905  -6.387  60.464  1.00 25.84           C  
ANISOU 2421  CA  LYS B 192     3675   3426   2718    321   -143   -140       C  
ATOM   2422  C   LYS B 192      38.920  -7.334  59.773  1.00 26.40           C  
ANISOU 2422  C   LYS B 192     3793   3428   2809    310    -71    -98       C  
ATOM   2423  O   LYS B 192      38.801  -8.499  60.157  1.00 28.31           O  
ANISOU 2423  O   LYS B 192     4121   3636   3000    339    -68    -45       O  
ATOM   2424  CB  LYS B 192      39.249  -5.766  61.702  1.00 27.87           C  
ANISOU 2424  CB  LYS B 192     3987   3706   2896    277   -126   -167       C  
ATOM   2425  CG  LYS B 192      40.239  -5.111  62.652  1.00 35.13           C  
ANISOU 2425  CG  LYS B 192     4890   4694   3764    291   -209   -204       C  
ATOM   2426  CD  LYS B 192      39.536  -4.343  63.759  1.00 43.08           C  
ANISOU 2426  CD  LYS B 192     5948   5723   4698    237   -180   -247       C  
ATOM   2427  CE  LYS B 192      40.542  -3.747  64.734  1.00 49.00           C  
ANISOU 2427  CE  LYS B 192     6690   6545   5385    247   -271   -289       C  
ATOM   2428  NZ  LYS B 192      39.901  -2.792  65.675  1.00 51.54           N  
ANISOU 2428  NZ  LYS B 192     7049   6887   5648    187   -234   -351       N  
ATOM   2429  N   CYS B 193      38.207  -6.831  58.767  1.00 21.52           N  
ANISOU 2429  N   CYS B 193     3123   2787   2265    266    -15   -122       N  
ATOM   2430  CA  CYS B 193      37.176  -7.619  58.084  1.00 29.99           C  
ANISOU 2430  CA  CYS B 193     4231   3804   3361    243     50    -96       C  
ATOM   2431  C   CYS B 193      37.682  -8.229  56.777  1.00 31.03           C  
ANISOU 2431  C   CYS B 193     4326   3909   3554    273     44    -80       C  
ATOM   2432  O   CYS B 193      36.900  -8.749  55.977  1.00 31.08           O  
ANISOU 2432  O   CYS B 193     4346   3873   3591    249     92    -71       O  
ATOM   2433  CB  CYS B 193      35.928  -6.765  57.802  1.00 31.80           C  
ANISOU 2433  CB  CYS B 193     4427   4026   3628    178    110   -132       C  
ATOM   2434  SG  CYS B 193      35.016  -6.214  59.286  1.00 42.75           S  
ANISOU 2434  SG  CYS B 193     5865   5431   4948    134    151   -159       S  
ATOM   2435  N   LYS B 194      38.990  -8.155  56.557  1.00 29.66           N  
ANISOU 2435  N   LYS B 194     4105   3764   3399    323    -13    -84       N  
ATOM   2436  CA  LYS B 194      39.580  -8.649  55.319  1.00 29.12           C  
ANISOU 2436  CA  LYS B 194     3997   3677   3389    353    -11    -79       C  
ATOM   2437  C   LYS B 194      39.652 -10.176  55.292  1.00 31.32           C  
ANISOU 2437  C   LYS B 194     4350   3902   3647    399     -5    -34       C  
ATOM   2438  O   LYS B 194      40.083 -10.797  56.258  1.00 31.68           O  
ANISOU 2438  O   LYS B 194     4451   3944   3640    447    -43     -1       O  
ATOM   2439  CB  LYS B 194      40.983  -8.062  55.128  1.00 36.67           C  
ANISOU 2439  CB  LYS B 194     4868   4684   4380    388    -64   -105       C  
ATOM   2440  CG  LYS B 194      41.576  -8.319  53.752  1.00 43.27           C  
ANISOU 2440  CG  LYS B 194     5651   5509   5281    405    -46   -113       C  
ATOM   2441  CD  LYS B 194      42.920  -7.626  53.577  1.00 48.96           C  
ANISOU 2441  CD  LYS B 194     6275   6285   6044    426    -85   -148       C  
ATOM   2442  CE  LYS B 194      43.382  -7.674  52.123  1.00 53.94           C  
ANISOU 2442  CE  LYS B 194     6852   6906   6736    424    -46   -163       C  
ATOM   2443  NZ  LYS B 194      44.690  -6.982  51.930  1.00 54.65           N  
ANISOU 2443  NZ  LYS B 194     6840   7049   6873    433    -70   -201       N  
ATOM   2444  N   PRO B 195      39.223 -10.789  54.176  1.00 25.57           N  
ANISOU 2444  N   PRO B 195     3629   3127   2957    385     41    -31       N  
ATOM   2445  CA  PRO B 195      39.357 -12.242  54.028  1.00 25.37           C  
ANISOU 2445  CA  PRO B 195     3674   3040   2925    429     53      5       C  
ATOM   2446  C   PRO B 195      40.822 -12.619  53.811  1.00 30.82           C  
ANISOU 2446  C   PRO B 195     4325   3742   3643    514      5      6       C  
ATOM   2447  O   PRO B 195      41.629 -11.752  53.475  1.00 33.03           O  
ANISOU 2447  O   PRO B 195     4512   4080   3958    522    -22    -28       O  
ATOM   2448  CB  PRO B 195      38.549 -12.543  52.758  1.00 25.29           C  
ANISOU 2448  CB  PRO B 195     3664   2990   2954    380    112    -12       C  
ATOM   2449  CG  PRO B 195      37.697 -11.317  52.530  1.00 31.21           C  
ANISOU 2449  CG  PRO B 195     4364   3778   3718    309    129    -43       C  
ATOM   2450  CD  PRO B 195      38.508 -10.180  53.045  1.00 28.20           C  
ANISOU 2450  CD  PRO B 195     3918   3460   3337    327     83    -60       C  
ATOM   2451  N   LYS B 196      41.153 -13.893  53.994  1.00 28.16           N  
ANISOU 2451  N   LYS B 196     4055   3348   3295    577     -1     43       N  
ATOM   2452  CA  LYS B 196      42.519 -14.366  53.793  1.00 31.65           C  
ANISOU 2452  CA  LYS B 196     4455   3796   3774    670    -45     43       C  
ATOM   2453  C   LYS B 196      42.847 -14.494  52.305  1.00 32.44           C  
ANISOU 2453  C   LYS B 196     4497   3884   3944    668      0      3       C  
ATOM   2454  O   LYS B 196      42.182 -15.227  51.577  1.00 30.99           O  
ANISOU 2454  O   LYS B 196     4369   3637   3770    643     57      4       O  
ATOM   2455  CB  LYS B 196      42.725 -15.705  54.505  1.00 36.20           C  
ANISOU 2455  CB  LYS B 196     5133   4304   4319    746    -67    101       C  
ATOM   2456  CG  LYS B 196      42.684 -15.615  56.025  1.00 45.69           C  
ANISOU 2456  CG  LYS B 196     6396   5525   5438    765   -125    145       C  
ATOM   2457  CD  LYS B 196      42.935 -16.979  56.657  1.00 54.95           C  
ANISOU 2457  CD  LYS B 196     7682   6620   6577    847   -149    213       C  
ATOM   2458  CE  LYS B 196      43.389 -16.863  58.107  1.00 62.78           C  
ANISOU 2458  CE  LYS B 196     8716   7651   7486    897   -236    257       C  
ATOM   2459  NZ  LYS B 196      42.326 -16.334  59.007  1.00 65.74           N  
ANISOU 2459  NZ  LYS B 196     9161   8044   7774    810   -209    269       N  
ATOM   2460  N   VAL B 197      43.881 -13.782  51.866  1.00 28.56           N  
ANISOU 2460  N   VAL B 197     3897   3455   3498    690    -23    -35       N  
ATOM   2461  CA  VAL B 197      44.237 -13.693  50.448  1.00 30.65           C  
ANISOU 2461  CA  VAL B 197     4103   3723   3821    676     28    -78       C  
ATOM   2462  C   VAL B 197      44.398 -15.039  49.725  1.00 33.51           C  
ANISOU 2462  C   VAL B 197     4513   4009   4208    726     69    -77       C  
ATOM   2463  O   VAL B 197      43.922 -15.207  48.601  1.00 37.75           O  
ANISOU 2463  O   VAL B 197     5066   4520   4758    679    131   -102       O  
ATOM   2464  CB  VAL B 197      45.520 -12.855  50.253  1.00 39.67           C  
ANISOU 2464  CB  VAL B 197     5121   4942   5012    701      0   -117       C  
ATOM   2465  CG1 VAL B 197      45.904 -12.793  48.783  1.00 43.66           C  
ANISOU 2465  CG1 VAL B 197     5574   5448   5567    682     65   -160       C  
ATOM   2466  CG2 VAL B 197      45.322 -11.456  50.810  1.00 45.29           C  
ANISOU 2466  CG2 VAL B 197     5787   5718   5704    639    -29   -129       C  
ATOM   2467  N   GLY B 198      45.059 -15.996  50.363  1.00 32.59           N  
ANISOU 2467  N   GLY B 198     4428   3857   4099    821     32    -48       N  
ATOM   2468  CA  GLY B 198      45.350 -17.258  49.700  1.00 37.56           C  
ANISOU 2468  CA  GLY B 198     5097   4409   4765    876     70    -53       C  
ATOM   2469  C   GLY B 198      44.421 -18.418  50.018  1.00 35.15           C  
ANISOU 2469  C   GLY B 198     4924   4008   4425    860     94    -10       C  
ATOM   2470  O   GLY B 198      44.757 -19.576  49.747  1.00 35.12           O  
ANISOU 2470  O   GLY B 198     4950   3944   4451    892    110     -5       O  
ATOM   2471  N   TYR B 199      43.244 -18.114  50.558  1.00 31.59           N  
ANISOU 2471  N   TYR B 199     4543   3543   3916    796    103     17       N  
ATOM   2472  CA  TYR B 199      42.356 -19.151  51.087  1.00 23.89           C  
ANISOU 2472  CA  TYR B 199     3698   2477   2904    779    126     63       C  
ATOM   2473  C   TYR B 199      41.950 -20.228  50.075  1.00 22.46           C  
ANISOU 2473  C   TYR B 199     3557   2224   2752    738    192     40       C  
ATOM   2474  O   TYR B 199      41.734 -21.383  50.443  1.00 25.63           O  
ANISOU 2474  O   TYR B 199     4042   2551   3145    747    203     73       O  
ATOM   2475  CB  TYR B 199      41.120 -18.533  51.767  1.00 26.83           C  
ANISOU 2475  CB  TYR B 199     4110   2868   3216    687    136     83       C  
ATOM   2476  CG  TYR B 199      39.967 -18.138  50.856  1.00 21.40           C  
ANISOU 2476  CG  TYR B 199     3411   2185   2536    577    196     42       C  
ATOM   2477  CD1 TYR B 199      39.147 -19.102  50.269  1.00 23.05           C  
ANISOU 2477  CD1 TYR B 199     3696   2311   2752    532    256     34       C  
ATOM   2478  CD2 TYR B 199      39.663 -16.800  50.631  1.00 16.30           C  
ANISOU 2478  CD2 TYR B 199     2681   1624   1888    517    187     12       C  
ATOM   2479  CE1 TYR B 199      38.096 -18.747  49.447  1.00 18.19           C  
ANISOU 2479  CE1 TYR B 199     3062   1708   2141    435    297     -5       C  
ATOM   2480  CE2 TYR B 199      38.604 -16.434  49.823  1.00 16.33           C  
ANISOU 2480  CE2 TYR B 199     2673   1634   1897    428    229    -19       C  
ATOM   2481  CZ  TYR B 199      37.822 -17.414  49.238  1.00 16.77           C  
ANISOU 2481  CZ  TYR B 199     2797   1617   1959    387    279    -29       C  
ATOM   2482  OH  TYR B 199      36.765 -17.056  48.438  1.00 18.76           O  
ANISOU 2482  OH  TYR B 199     3029   1882   2216    301    308    -63       O  
ATOM   2483  N   MET B 200      41.846 -19.850  48.807  1.00 21.91           N  
ANISOU 2483  N   MET B 200     3432   2181   2713    690    232    -18       N  
ATOM   2484  CA  MET B 200      41.361 -20.781  47.791  1.00 25.89           C  
ANISOU 2484  CA  MET B 200     3974   2627   3234    640    289    -48       C  
ATOM   2485  C   MET B 200      42.313 -21.970  47.625  1.00 30.13           C  
ANISOU 2485  C   MET B 200     4519   3113   3815    714    289    -48       C  
ATOM   2486  O   MET B 200      41.896 -23.071  47.254  1.00 30.10           O  
ANISOU 2486  O   MET B 200     4581   3036   3820    690    327    -54       O  
ATOM   2487  CB  MET B 200      41.136 -20.051  46.463  1.00 30.84           C  
ANISOU 2487  CB  MET B 200     4542   3306   3872    577    322   -108       C  
ATOM   2488  CG  MET B 200      40.254 -20.805  45.485  1.00 29.42           C  
ANISOU 2488  CG  MET B 200     4411   3080   3689    500    372   -140       C  
ATOM   2489  SD  MET B 200      38.605 -21.144  46.134  1.00 24.96           S  
ANISOU 2489  SD  MET B 200     3935   2464   3084    414    390   -112       S  
ATOM   2490  CE  MET B 200      37.802 -19.564  45.857  1.00 24.44           C  
ANISOU 2490  CE  MET B 200     3811   2479   2995    342    380   -134       C  
ATOM   2491  N   LYS B 201      43.589 -21.752  47.932  1.00 31.70           N  
ANISOU 2491  N   LYS B 201     4647   3350   4047    803    245    -45       N  
ATOM   2492  CA  LYS B 201      44.586 -22.819  47.855  1.00 35.90           C  
ANISOU 2492  CA  LYS B 201     5172   3835   4633    885    238    -47       C  
ATOM   2493  C   LYS B 201      44.386 -23.870  48.943  1.00 34.46           C  
ANISOU 2493  C   LYS B 201     5090   3574   4430    924    212     20       C  
ATOM   2494  O   LYS B 201      44.887 -24.991  48.837  1.00 41.81           O  
ANISOU 2494  O   LYS B 201     6046   4437   5402    977    218     23       O  
ATOM   2495  CB  LYS B 201      46.000 -22.237  47.935  1.00 41.25           C  
ANISOU 2495  CB  LYS B 201     5731   4584   5360    965    194    -64       C  
ATOM   2496  CG  LYS B 201      46.268 -21.164  46.897  1.00 47.41           C  
ANISOU 2496  CG  LYS B 201     6413   5443   6159    922    226   -127       C  
ATOM   2497  CD  LYS B 201      47.698 -20.657  46.957  1.00 56.60           C  
ANISOU 2497  CD  LYS B 201     7451   6673   7382    992    193   -151       C  
ATOM   2498  CE  LYS B 201      47.843 -19.352  46.183  1.00 61.27           C  
ANISOU 2498  CE  LYS B 201     7954   7351   7975    935    223   -200       C  
ATOM   2499  NZ  LYS B 201      49.126 -19.282  45.426  1.00 65.27           N  
ANISOU 2499  NZ  LYS B 201     8348   7893   8558    969    252   -257       N  
ATOM   2500  N   LYS B 202      43.649 -23.509  49.988  1.00 29.58           N  
ANISOU 2500  N   LYS B 202     4532   2962   3746    896    188     72       N  
ATOM   2501  CA  LYS B 202      43.396 -24.420  51.098  1.00 32.78           C  
ANISOU 2501  CA  LYS B 202     5042   3298   4116    922    168    140       C  
ATOM   2502  C   LYS B 202      42.066 -25.158  50.940  1.00 35.23           C  
ANISOU 2502  C   LYS B 202     5459   3529   4397    830    237    146       C  
ATOM   2503  O   LYS B 202      41.757 -26.072  51.706  1.00 37.50           O  
ANISOU 2503  O   LYS B 202     5843   3746   4659    836    240    197       O  
ATOM   2504  CB  LYS B 202      43.454 -23.662  52.430  1.00 39.49           C  
ANISOU 2504  CB  LYS B 202     5899   4201   4903    947    102    193       C  
ATOM   2505  CG  LYS B 202      44.827 -23.056  52.707  1.00 48.72           C  
ANISOU 2505  CG  LYS B 202     6960   5450   6103   1039     23    187       C  
ATOM   2506  CD  LYS B 202      44.782 -21.937  53.737  1.00 55.68           C  
ANISOU 2506  CD  LYS B 202     7825   6411   6920   1039    -39    212       C  
ATOM   2507  CE  LYS B 202      44.641 -22.467  55.153  1.00 62.01           C  
ANISOU 2507  CE  LYS B 202     8727   7183   7650   1066    -86    287       C  
ATOM   2508  NZ  LYS B 202      44.846 -21.379  56.154  1.00 66.33           N  
ANISOU 2508  NZ  LYS B 202     9245   7821   8138   1076   -160    302       N  
ATOM   2509  N   GLN B 203      41.282 -24.763  49.941  1.00 26.90           N  
ANISOU 2509  N   GLN B 203     4382   2491   3347    741    290     93       N  
ATOM   2510  CA  GLN B 203      40.025 -25.443  49.657  1.00 23.17           C  
ANISOU 2510  CA  GLN B 203     3990   1955   2859    645    354     85       C  
ATOM   2511  C   GLN B 203      40.306 -26.699  48.831  1.00 24.09           C  
ANISOU 2511  C   GLN B 203     4132   1996   3024    660    389     55       C  
ATOM   2512  O   GLN B 203      40.971 -26.629  47.798  1.00 29.91           O  
ANISOU 2512  O   GLN B 203     4802   2756   3807    684    395      1       O  
ATOM   2513  CB  GLN B 203      39.069 -24.515  48.903  1.00 22.76           C  
ANISOU 2513  CB  GLN B 203     3897   1956   2794    545    385     37       C  
ATOM   2514  CG  GLN B 203      38.542 -23.354  49.738  1.00 22.71           C  
ANISOU 2514  CG  GLN B 203     3880   2006   2741    516    363     63       C  
ATOM   2515  CD  GLN B 203      37.424 -23.775  50.665  1.00 24.04           C  
ANISOU 2515  CD  GLN B 203     4142   2126   2866    452    394    103       C  
ATOM   2516  OE1 GLN B 203      36.834 -24.847  50.501  1.00 26.69           O  
ANISOU 2516  OE1 GLN B 203     4542   2393   3208    407    440    101       O  
ATOM   2517  NE2 GLN B 203      37.124 -22.935  51.652  1.00 22.44           N  
ANISOU 2517  NE2 GLN B 203     3947   1961   2618    444    374    135       N  
ATOM   2518  N   PRO B 204      39.802 -27.850  49.286  1.00 27.39           N  
ANISOU 2518  N   PRO B 204     4650   2323   3434    642    417     87       N  
ATOM   2519  CA  PRO B 204      40.030 -29.115  48.583  1.00 34.08           C  
ANISOU 2519  CA  PRO B 204     5534   3085   4330    657    452     59       C  
ATOM   2520  C   PRO B 204      39.271 -29.229  47.260  1.00 35.72           C  
ANISOU 2520  C   PRO B 204     5729   3293   4551    562    508    -16       C  
ATOM   2521  O   PRO B 204      39.766 -29.889  46.348  1.00 36.92           O  
ANISOU 2521  O   PRO B 204     5870   3410   4749    586    528    -63       O  
ATOM   2522  CB  PRO B 204      39.512 -30.161  49.577  1.00 32.13           C  
ANISOU 2522  CB  PRO B 204     5405   2745   4057    648    468    121       C  
ATOM   2523  CG  PRO B 204      38.494 -29.441  50.378  1.00 34.32           C  
ANISOU 2523  CG  PRO B 204     5709   3062   4269    572    475    152       C  
ATOM   2524  CD  PRO B 204      39.016 -28.039  50.517  1.00 29.09           C  
ANISOU 2524  CD  PRO B 204     4955   2507   3592    607    422    150       C  
ATOM   2525  N   ASP B 205      38.099 -28.607  47.147  1.00 27.38           N  
ANISOU 2525  N   ASP B 205     4671   2276   3458    457    530    -30       N  
ATOM   2526  CA  ASP B 205      37.273 -28.819  45.956  1.00 24.53           C  
ANISOU 2526  CA  ASP B 205     4303   1912   3104    362    574    -98       C  
ATOM   2527  C   ASP B 205      37.026 -27.560  45.121  1.00 29.10           C  
ANISOU 2527  C   ASP B 205     4795   2593   3670    315    561   -145       C  
ATOM   2528  O   ASP B 205      37.185 -27.582  43.900  1.00 33.59           O  
ANISOU 2528  O   ASP B 205     5329   3181   4254    297    573   -206       O  
ATOM   2529  CB  ASP B 205      35.936 -29.464  46.326  1.00 27.74           C  
ANISOU 2529  CB  ASP B 205     4786   2265   3490    264    618    -89       C  
ATOM   2530  CG  ASP B 205      35.192 -30.006  45.115  1.00 34.40           C  
ANISOU 2530  CG  ASP B 205     5632   3089   4349    176    659   -161       C  
ATOM   2531  OD1 ASP B 205      35.838 -30.634  44.246  1.00 31.13           O  
ANISOU 2531  OD1 ASP B 205     5218   2643   3967    211    668   -202       O  
ATOM   2532  OD2 ASP B 205      33.959 -29.813  45.031  1.00 33.27           O  
ANISOU 2532  OD2 ASP B 205     5488   2964   4188     71    680   -181       O  
ATOM   2533  N   ILE B 206      36.642 -26.464  45.766  1.00 22.94           N  
ANISOU 2533  N   ILE B 206     3984   1873   2858    295    537   -117       N  
ATOM   2534  CA  ILE B 206      36.254 -25.280  45.012  1.00 22.49           C  
ANISOU 2534  CA  ILE B 206     3853   1904   2790    242    525   -158       C  
ATOM   2535  C   ILE B 206      37.446 -24.469  44.527  1.00 23.44           C  
ANISOU 2535  C   ILE B 206     3895   2089   2923    314    494   -174       C  
ATOM   2536  O   ILE B 206      38.566 -24.623  45.019  1.00 23.49           O  
ANISOU 2536  O   ILE B 206     3890   2085   2948    409    473   -148       O  
ATOM   2537  CB  ILE B 206      35.279 -24.384  45.790  1.00 21.35           C  
ANISOU 2537  CB  ILE B 206     3700   1797   2614    185    517   -133       C  
ATOM   2538  CG1 ILE B 206      35.957 -23.815  47.042  1.00 23.51           C  
ANISOU 2538  CG1 ILE B 206     3974   2087   2872    261    482    -74       C  
ATOM   2539  CG2 ILE B 206      34.012 -25.172  46.139  1.00 21.14           C  
ANISOU 2539  CG2 ILE B 206     3737   1714   2580     97    559   -131       C  
ATOM   2540  CD1 ILE B 206      35.151 -22.743  47.742  1.00 31.44           C  
ANISOU 2540  CD1 ILE B 206     4961   3137   3847    213    474    -58       C  
ATOM   2541  N   THR B 207      37.189 -23.608  43.549  1.00 18.08           N  
ANISOU 2541  N   THR B 207     3158   1478   2234    266    491   -219       N  
ATOM   2542  CA  THR B 207      38.236 -22.839  42.887  1.00 16.61           C  
ANISOU 2542  CA  THR B 207     2897   1356   2057    314    475   -243       C  
ATOM   2543  C   THR B 207      37.792 -21.406  42.633  1.00 15.41           C  
ANISOU 2543  C   THR B 207     2689   1289   1879    269    454   -251       C  
ATOM   2544  O   THR B 207      36.623 -21.066  42.804  1.00 14.77           O  
ANISOU 2544  O   THR B 207     2621   1215   1777    197    451   -248       O  
ATOM   2545  CB  THR B 207      38.555 -23.430  41.509  1.00 18.33           C  
ANISOU 2545  CB  THR B 207     3114   1567   2285    302    506   -303       C  
ATOM   2546  OG1 THR B 207      37.387 -23.333  40.683  1.00 16.30           O  
ANISOU 2546  OG1 THR B 207     2872   1325   1998    203    516   -338       O  
ATOM   2547  CG2 THR B 207      38.991 -24.893  41.611  1.00 23.15           C  
ANISOU 2547  CG2 THR B 207     3779   2087   2928    347    531   -305       C  
ATOM   2548  N   ASN B 208      38.724 -20.566  42.194  1.00 16.78           N  
ANISOU 2548  N   ASN B 208     2795   1524   2058    307    444   -265       N  
ATOM   2549  CA  ASN B 208      38.371 -19.190  41.854  1.00 19.87           C  
ANISOU 2549  CA  ASN B 208     3136   1990   2423    265    426   -272       C  
ATOM   2550  C   ASN B 208      37.337 -19.122  40.731  1.00 17.81           C  
ANISOU 2550  C   ASN B 208     2890   1744   2132    176    435   -310       C  
ATOM   2551  O   ASN B 208      36.506 -18.217  40.700  1.00 13.15           O  
ANISOU 2551  O   ASN B 208     2282   1193   1519    126    414   -308       O  
ATOM   2552  CB  ASN B 208      39.614 -18.375  41.477  1.00 23.47           C  
ANISOU 2552  CB  ASN B 208     3521   2507   2892    315    425   -284       C  
ATOM   2553  CG  ASN B 208      40.471 -18.023  42.682  1.00 22.44           C  
ANISOU 2553  CG  ASN B 208     3354   2387   2787    393    397   -248       C  
ATOM   2554  OD1 ASN B 208      41.693 -17.909  42.577  1.00 33.20           O  
ANISOU 2554  OD1 ASN B 208     4661   3773   4179    453    399   -260       O  
ATOM   2555  ND2 ASN B 208      39.840 -17.867  43.828  1.00 24.84           N  
ANISOU 2555  ND2 ASN B 208     3686   2674   3077    391    372   -209       N  
ATOM   2556  N   SER B 209      37.396 -20.086  39.814  1.00 17.40           N  
ANISOU 2556  N   SER B 209     2871   1661   2080    161    462   -347       N  
ATOM   2557  CA  SER B 209      36.460 -20.144  38.695  1.00 16.83           C  
ANISOU 2557  CA  SER B 209     2818   1604   1973     80    463   -387       C  
ATOM   2558  C   SER B 209      35.042 -20.451  39.176  1.00 14.22           C  
ANISOU 2558  C   SER B 209     2519   1244   1640     13    452   -382       C  
ATOM   2559  O   SER B 209      34.062 -19.925  38.648  1.00 15.34           O  
ANISOU 2559  O   SER B 209     2649   1423   1755    -55    429   -403       O  
ATOM   2560  CB  SER B 209      36.919 -21.169  37.652  1.00 23.11           C  
ANISOU 2560  CB  SER B 209     3645   2369   2768     83    498   -433       C  
ATOM   2561  OG  SER B 209      37.253 -22.409  38.267  1.00 25.83           O  
ANISOU 2561  OG  SER B 209     4029   2634   3151    125    521   -425       O  
ATOM   2562  N   MET B 210      34.935 -21.300  40.189  1.00 11.96           N  
ANISOU 2562  N   MET B 210     2271    892   1382     31    468   -355       N  
ATOM   2563  CA  MET B 210      33.627 -21.588  40.765  1.00 13.07           C  
ANISOU 2563  CA  MET B 210     2437   1005   1524    -37    469   -349       C  
ATOM   2564  C   MET B 210      33.110 -20.401  41.561  1.00 15.77           C  
ANISOU 2564  C   MET B 210     2739   1392   1861    -50    442   -322       C  
ATOM   2565  O   MET B 210      31.918 -20.088  41.532  1.00 13.48           O  
ANISOU 2565  O   MET B 210     2434   1120   1567   -123    431   -339       O  
ATOM   2566  CB  MET B 210      33.694 -22.832  41.644  1.00 13.87           C  
ANISOU 2566  CB  MET B 210     2602   1020   1649    -17    501   -322       C  
ATOM   2567  CG  MET B 210      33.942 -24.091  40.848  1.00 13.30           C  
ANISOU 2567  CG  MET B 210     2575    892   1587    -19    531   -359       C  
ATOM   2568  SD  MET B 210      34.107 -25.501  41.938  1.00 21.49           S  
ANISOU 2568  SD  MET B 210     3693   1820   2651     15    567   -318       S  
ATOM   2569  CE  MET B 210      35.358 -26.459  41.086  1.00 22.85           C  
ANISOU 2569  CE  MET B 210     3886   1949   2848     86    588   -350       C  
ATOM   2570  N   ARG B 211      34.013 -19.733  42.269  1.00 13.60           N  
ANISOU 2570  N   ARG B 211     2441   1137   1589     21    430   -285       N  
ATOM   2571  CA  ARG B 211      33.642 -18.531  43.002  1.00 12.44           C  
ANISOU 2571  CA  ARG B 211     2255   1034   1436     16    407   -263       C  
ATOM   2572  C   ARG B 211      33.129 -17.461  42.036  1.00 13.82           C  
ANISOU 2572  C   ARG B 211     2380   1277   1594    -30    380   -295       C  
ATOM   2573  O   ARG B 211      32.147 -16.779  42.316  1.00 12.37           O  
ANISOU 2573  O   ARG B 211     2156   1130   1413    -77    355   -290       O  
ATOM   2574  CB  ARG B 211      34.843 -18.013  43.808  1.00 14.15           C  
ANISOU 2574  CB  ARG B 211     2452   1265   1657    104    394   -226       C  
ATOM   2575  CG  ARG B 211      34.554 -16.764  44.637  1.00 13.94           C  
ANISOU 2575  CG  ARG B 211     2369   1300   1626     99    361   -196       C  
ATOM   2576  CD  ARG B 211      35.838 -16.180  45.224  1.00 15.34           C  
ANISOU 2576  CD  ARG B 211     2509   1512   1808    179    336   -168       C  
ATOM   2577  NE  ARG B 211      35.595 -14.861  45.820  1.00 12.19           N  
ANISOU 2577  NE  ARG B 211     2047   1179   1406    165    303   -151       N  
ATOM   2578  CZ  ARG B 211      35.408 -13.761  45.103  1.00 13.84           C  
ANISOU 2578  CZ  ARG B 211     2197   1444   1617    135    285   -166       C  
ATOM   2579  NH1 ARG B 211      35.442 -13.825  43.773  1.00 12.03           N  
ANISOU 2579  NH1 ARG B 211     1966   1221   1382    114    294   -195       N  
ATOM   2580  NH2 ARG B 211      35.183 -12.605  45.706  1.00 14.22           N  
ANISOU 2580  NH2 ARG B 211     2195   1537   1668    126    259   -153       N  
ATOM   2581  N   ALA B 212      33.791 -17.320  40.894  1.00 11.35           N  
ANISOU 2581  N   ALA B 212     2055    994   1264    -17    376   -318       N  
ATOM   2582  CA  ALA B 212      33.357 -16.355  39.893  1.00 12.54           C  
ANISOU 2582  CA  ALA B 212     2174   1206   1385    -58    347   -340       C  
ATOM   2583  C   ALA B 212      31.941 -16.665  39.402  1.00 12.57           C  
ANISOU 2583  C   ALA B 212     2188   1209   1380   -142    329   -375       C  
ATOM   2584  O   ALA B 212      31.112 -15.758  39.260  1.00 13.66           O  
ANISOU 2584  O   ALA B 212     2273   1402   1516   -176    282   -368       O  
ATOM   2585  CB  ALA B 212      34.334 -16.333  38.719  1.00 11.79           C  
ANISOU 2585  CB  ALA B 212     2081   1134   1264    -35    360   -359       C  
ATOM   2586  N   ILE B 213      31.665 -17.947  39.157  1.00 13.31           N  
ANISOU 2586  N   ILE B 213     2323   1252   1480   -169    353   -400       N  
ATOM   2587  CA  ILE B 213      30.328 -18.379  38.756  1.00 12.61           C  
ANISOU 2587  CA  ILE B 213     2237   1161   1392   -253    337   -438       C  
ATOM   2588  C   ILE B 213      29.304 -18.000  39.824  1.00 13.88           C  
ANISOU 2588  C   ILE B 213     2367   1322   1586   -290    331   -427       C  
ATOM   2589  O   ILE B 213      28.237 -17.453  39.517  1.00 13.47           O  
ANISOU 2589  O   ILE B 213     2264   1315   1537   -346    290   -449       O  
ATOM   2590  CB  ILE B 213      30.291 -19.906  38.489  1.00 14.76           C  
ANISOU 2590  CB  ILE B 213     2561   1371   1676   -273    374   -462       C  
ATOM   2591  CG1 ILE B 213      31.055 -20.220  37.199  1.00 16.50           C  
ANISOU 2591  CG1 ILE B 213     2806   1603   1862   -255    378   -492       C  
ATOM   2592  CG2 ILE B 213      28.841 -20.412  38.395  1.00 15.77           C  
ANISOU 2592  CG2 ILE B 213     2683   1492   1819   -364    365   -499       C  
ATOM   2593  CD1 ILE B 213      31.305 -21.707  36.991  1.00 22.64           C  
ANISOU 2593  CD1 ILE B 213     3637   2309   2654   -255    422   -515       C  
ATOM   2594  N   LEU B 214      29.649 -18.259  41.081  1.00 10.19           N  
ANISOU 2594  N   LEU B 214     1918    811   1143   -253    366   -386       N  
ATOM   2595  CA  LEU B 214      28.775 -17.912  42.201  1.00 12.74           C  
ANISOU 2595  CA  LEU B 214     2208   1138   1495   -283    371   -367       C  
ATOM   2596  C   LEU B 214      28.487 -16.410  42.301  1.00 14.85           C  
ANISOU 2596  C   LEU B 214     2385   1491   1767   -270    320   -346       C  
ATOM   2597  O   LEU B 214      27.334 -16.000  42.433  1.00 13.23           O  
ANISOU 2597  O   LEU B 214     2122   1318   1586   -320    301   -361       O  
ATOM   2598  CB  LEU B 214      29.367 -18.412  43.521  1.00 12.32           C  
ANISOU 2598  CB  LEU B 214     2207   1026   1448   -237    415   -320       C  
ATOM   2599  CG  LEU B 214      28.551 -18.032  44.766  1.00 14.23           C  
ANISOU 2599  CG  LEU B 214     2420   1279   1708   -265    429   -294       C  
ATOM   2600  CD1 LEU B 214      27.247 -18.829  44.819  1.00 14.88           C  
ANISOU 2600  CD1 LEU B 214     2515   1322   1815   -362    467   -331       C  
ATOM   2601  CD2 LEU B 214      29.375 -18.245  46.028  1.00 14.08           C  
ANISOU 2601  CD2 LEU B 214     2454   1222   1674   -201    454   -237       C  
ATOM   2602  N   VAL B 215      29.530 -15.588  42.263  1.00 12.81           N  
ANISOU 2602  N   VAL B 215     2109   1265   1492   -202    300   -314       N  
ATOM   2603  CA  VAL B 215      29.342 -14.143  42.410  1.00  9.43           C  
ANISOU 2603  CA  VAL B 215     1605    903   1072   -186    256   -291       C  
ATOM   2604  C   VAL B 215      28.527 -13.584  41.244  1.00 12.56           C  
ANISOU 2604  C   VAL B 215     1960   1350   1464   -226    205   -318       C  
ATOM   2605  O   VAL B 215      27.651 -12.742  41.441  1.00 13.57           O  
ANISOU 2605  O   VAL B 215     2022   1515   1617   -242    171   -315       O  
ATOM   2606  CB  VAL B 215      30.697 -13.400  42.540  1.00 14.23           C  
ANISOU 2606  CB  VAL B 215     2207   1532   1667   -115    250   -257       C  
ATOM   2607  CG1 VAL B 215      30.485 -11.878  42.659  1.00 13.89           C  
ANISOU 2607  CG1 VAL B 215     2095   1546   1638   -104    209   -237       C  
ATOM   2608  CG2 VAL B 215      31.453 -13.921  43.765  1.00 16.33           C  
ANISOU 2608  CG2 VAL B 215     2508   1758   1937    -69    284   -230       C  
ATOM   2609  N   ASP B 216      28.803 -14.062  40.034  1.00 11.91           N  
ANISOU 2609  N   ASP B 216     1916   1264   1344   -240    196   -346       N  
ATOM   2610  CA  ASP B 216      28.040 -13.616  38.871  1.00 16.39           C  
ANISOU 2610  CA  ASP B 216     2457   1880   1890   -279    138   -369       C  
ATOM   2611  C   ASP B 216      26.550 -13.928  39.034  1.00 17.62           C  
ANISOU 2611  C   ASP B 216     2570   2043   2083   -344    117   -405       C  
ATOM   2612  O   ASP B 216      25.687 -13.110  38.680  1.00 16.60           O  
ANISOU 2612  O   ASP B 216     2375   1966   1966   -358     55   -407       O  
ATOM   2613  CB  ASP B 216      28.576 -14.254  37.588  1.00 13.73           C  
ANISOU 2613  CB  ASP B 216     2185   1537   1496   -291    142   -402       C  
ATOM   2614  CG  ASP B 216      27.884 -13.729  36.338  1.00 19.78           C  
ANISOU 2614  CG  ASP B 216     2936   2361   2220   -327     71   -420       C  
ATOM   2615  OD1 ASP B 216      28.337 -12.704  35.794  1.00 20.08           O  
ANISOU 2615  OD1 ASP B 216     2966   2438   2225   -295     39   -386       O  
ATOM   2616  OD2 ASP B 216      26.887 -14.336  35.903  1.00 17.53           O  
ANISOU 2616  OD2 ASP B 216     2648   2080   1934   -388     44   -468       O  
ATOM   2617  N   TRP B 217      26.249 -15.105  39.577  1.00 13.27           N  
ANISOU 2617  N   TRP B 217     2053   1437   1553   -384    169   -432       N  
ATOM   2618  CA  TRP B 217      24.867 -15.463  39.884  1.00 14.67           C  
ANISOU 2618  CA  TRP B 217     2183   1616   1775   -455    167   -470       C  
ATOM   2619  C   TRP B 217      24.271 -14.526  40.942  1.00 14.13           C  
ANISOU 2619  C   TRP B 217     2034   1578   1758   -441    165   -442       C  
ATOM   2620  O   TRP B 217      23.117 -14.110  40.831  1.00 14.97           O  
ANISOU 2620  O   TRP B 217     2059   1727   1904   -477    127   -468       O  
ATOM   2621  CB  TRP B 217      24.770 -16.938  40.324  1.00 13.62           C  
ANISOU 2621  CB  TRP B 217     2118   1403   1655   -505    239   -499       C  
ATOM   2622  CG  TRP B 217      23.420 -17.308  40.830  1.00 16.48           C  
ANISOU 2622  CG  TRP B 217     2430   1760   2070   -586    257   -535       C  
ATOM   2623  CD1 TRP B 217      22.272 -17.419  40.099  1.00 18.82           C  
ANISOU 2623  CD1 TRP B 217     2667   2095   2387   -660    213   -595       C  
ATOM   2624  CD2 TRP B 217      23.067 -17.599  42.185  1.00 16.16           C  
ANISOU 2624  CD2 TRP B 217     2391   1680   2069   -605    326   -517       C  
ATOM   2625  NE1 TRP B 217      21.224 -17.761  40.921  1.00 17.48           N  
ANISOU 2625  NE1 TRP B 217     2446   1918   2277   -714    253   -610       N  
ATOM   2626  CE2 TRP B 217      21.689 -17.885  42.204  1.00 16.22           C  
ANISOU 2626  CE2 TRP B 217     2331   1707   2126   -689    330   -565       C  
ATOM   2627  CE3 TRP B 217      23.787 -17.656  43.386  1.00 16.13           C  
ANISOU 2627  CE3 TRP B 217     2438   1633   2058   -556    384   -461       C  
ATOM   2628  CZ2 TRP B 217      21.013 -18.219  43.376  1.00 17.29           C  
ANISOU 2628  CZ2 TRP B 217     2449   1819   2301   -726    400   -556       C  
ATOM   2629  CZ3 TRP B 217      23.114 -17.986  44.546  1.00 15.50           C  
ANISOU 2629  CZ3 TRP B 217     2356   1522   2009   -600    449   -456       C  
ATOM   2630  CH2 TRP B 217      21.740 -18.257  44.533  1.00 17.61           C  
ANISOU 2630  CH2 TRP B 217     2556   1810   2323   -686    462   -503       C  
ATOM   2631  N   LEU B 218      25.046 -14.173  41.963  1.00 10.91           N  
ANISOU 2631  N   LEU B 218     1644   1151   1351   -385    203   -395       N  
ATOM   2632  CA  LEU B 218      24.524 -13.254  42.980  1.00 12.15           C  
ANISOU 2632  CA  LEU B 218     1731   1334   1549   -372    207   -376       C  
ATOM   2633  C   LEU B 218      24.200 -11.879  42.396  1.00 13.91           C  
ANISOU 2633  C   LEU B 218     1877   1621   1786   -342    133   -368       C  
ATOM   2634  O   LEU B 218      23.276 -11.206  42.855  1.00 13.84           O  
ANISOU 2634  O   LEU B 218     1789   1641   1828   -349    122   -378       O  
ATOM   2635  CB  LEU B 218      25.493 -13.109  44.160  1.00 11.96           C  
ANISOU 2635  CB  LEU B 218     1750   1283   1512   -318    253   -330       C  
ATOM   2636  CG  LEU B 218      25.635 -14.390  44.989  1.00 18.02           C  
ANISOU 2636  CG  LEU B 218     2595   1983   2270   -343    324   -327       C  
ATOM   2637  CD1 LEU B 218      26.702 -14.196  46.031  1.00 19.70           C  
ANISOU 2637  CD1 LEU B 218     2851   2177   2457   -279    348   -278       C  
ATOM   2638  CD2 LEU B 218      24.307 -14.745  45.640  1.00 18.87           C  
ANISOU 2638  CD2 LEU B 218     2669   2082   2419   -417    367   -356       C  
ATOM   2639  N   VAL B 219      24.965 -11.455  41.393  1.00 11.16           N  
ANISOU 2639  N   VAL B 219     1554   1290   1394   -306     88   -350       N  
ATOM   2640  CA  VAL B 219      24.655 -10.205  40.694  1.00 13.39           C  
ANISOU 2640  CA  VAL B 219     1782   1623   1682   -280     15   -335       C  
ATOM   2641  C   VAL B 219      23.260 -10.296  40.080  1.00 16.21           C  
ANISOU 2641  C   VAL B 219     2074   2015   2069   -327    -41   -377       C  
ATOM   2642  O   VAL B 219      22.445  -9.373  40.215  1.00 14.23           O  
ANISOU 2642  O   VAL B 219     1741   1799   1868   -312    -83   -375       O  
ATOM   2643  CB  VAL B 219      25.689  -9.886  39.588  1.00 13.50           C  
ANISOU 2643  CB  VAL B 219     1851   1647   1633   -248    -15   -309       C  
ATOM   2644  CG1 VAL B 219      25.247  -8.656  38.773  1.00 14.86           C  
ANISOU 2644  CG1 VAL B 219     1981   1864   1803   -227    -96   -288       C  
ATOM   2645  CG2 VAL B 219      27.063  -9.649  40.200  1.00 13.45           C  
ANISOU 2645  CG2 VAL B 219     1884   1616   1611   -199     33   -273       C  
ATOM   2646  N   GLU B 220      22.983 -11.419  39.422  1.00 12.72           N  
ANISOU 2646  N   GLU B 220     1665   1564   1602   -385    -41   -420       N  
ATOM   2647  CA  GLU B 220      21.668 -11.654  38.821  1.00 15.17           C  
ANISOU 2647  CA  GLU B 220     1911   1913   1941   -441    -97   -471       C  
ATOM   2648  C   GLU B 220      20.560 -11.684  39.861  1.00 17.22           C  
ANISOU 2648  C   GLU B 220     2081   2175   2286   -474    -65   -500       C  
ATOM   2649  O   GLU B 220      19.469 -11.163  39.634  1.00 17.04           O  
ANISOU 2649  O   GLU B 220     1959   2200   2314   -484   -124   -525       O  
ATOM   2650  CB  GLU B 220      21.644 -12.980  38.050  1.00 17.51           C  
ANISOU 2650  CB  GLU B 220     2269   2188   2195   -508    -89   -522       C  
ATOM   2651  CG  GLU B 220      22.477 -12.981  36.801  1.00 22.81           C  
ANISOU 2651  CG  GLU B 220     3018   2870   2779   -489   -127   -513       C  
ATOM   2652  CD  GLU B 220      22.028 -14.067  35.842  1.00 37.50           C  
ANISOU 2652  CD  GLU B 220     4913   4731   4604   -564   -148   -581       C  
ATOM   2653  OE1 GLU B 220      22.414 -15.231  36.053  1.00 37.28           O  
ANISOU 2653  OE1 GLU B 220     4953   4642   4569   -599    -75   -612       O  
ATOM   2654  OE2 GLU B 220      21.272 -13.753  34.900  1.00 48.13           O  
ANISOU 2654  OE2 GLU B 220     6220   6137   5930   -586   -241   -606       O  
ATOM   2655  N   VAL B 221      20.835 -12.322  40.992  1.00 14.79           N  
ANISOU 2655  N   VAL B 221     1810   1817   1994   -491     30   -497       N  
ATOM   2656  CA  VAL B 221      19.852 -12.397  42.065  1.00 14.44           C  
ANISOU 2656  CA  VAL B 221     1694   1771   2022   -530     83   -524       C  
ATOM   2657  C   VAL B 221      19.538 -10.991  42.570  1.00 15.59           C  
ANISOU 2657  C   VAL B 221     1754   1956   2215   -471     57   -501       C  
ATOM   2658  O   VAL B 221      18.374 -10.643  42.786  1.00 17.34           O  
ANISOU 2658  O   VAL B 221     1868   2211   2508   -492     46   -538       O  
ATOM   2659  CB  VAL B 221      20.354 -13.279  43.232  1.00 18.23           C  
ANISOU 2659  CB  VAL B 221     2254   2183   2490   -551    192   -510       C  
ATOM   2660  CG1 VAL B 221      19.420 -13.167  44.428  1.00 19.39           C  
ANISOU 2660  CG1 VAL B 221     2334   2332   2701   -587    257   -529       C  
ATOM   2661  CG2 VAL B 221      20.482 -14.742  42.767  1.00 16.94           C  
ANISOU 2661  CG2 VAL B 221     2171   1967   2298   -615    223   -540       C  
ATOM   2662  N   GLY B 222      20.578 -10.183  42.749  1.00 14.99           N  
ANISOU 2662  N   GLY B 222     1721   1872   2104   -397     52   -446       N  
ATOM   2663  CA  GLY B 222      20.401  -8.807  43.190  1.00 14.68           C  
ANISOU 2663  CA  GLY B 222     1614   1856   2106   -338     30   -425       C  
ATOM   2664  C   GLY B 222      19.557  -8.003  42.214  1.00 17.40           C  
ANISOU 2664  C   GLY B 222     1873   2251   2488   -318    -70   -437       C  
ATOM   2665  O   GLY B 222      18.720  -7.198  42.620  1.00 17.32           O  
ANISOU 2665  O   GLY B 222     1766   2262   2550   -296    -83   -451       O  
ATOM   2666  N   GLU B 223      19.780  -8.220  40.922  1.00 14.98           N  
ANISOU 2666  N   GLU B 223     1603   1960   2128   -322   -142   -430       N  
ATOM   2667  CA  GLU B 223      18.972  -7.568  39.888  1.00 21.88           C  
ANISOU 2667  CA  GLU B 223     2408   2884   3021   -304   -252   -436       C  
ATOM   2668  C   GLU B 223      17.520  -8.026  39.907  1.00 20.14           C  
ANISOU 2668  C   GLU B 223     2077   2700   2874   -359   -273   -504       C  
ATOM   2669  O   GLU B 223      16.604  -7.213  39.759  1.00 23.02           O  
ANISOU 2669  O   GLU B 223     2336   3103   3305   -326   -339   -514       O  
ATOM   2670  CB  GLU B 223      19.568  -7.807  38.501  1.00 21.66           C  
ANISOU 2670  CB  GLU B 223     2462   2868   2901   -305   -318   -417       C  
ATOM   2671  CG  GLU B 223      20.770  -6.933  38.191  1.00 27.15           C  
ANISOU 2671  CG  GLU B 223     3233   3544   3538   -241   -326   -348       C  
ATOM   2672  CD  GLU B 223      20.386  -5.476  38.025  1.00 41.20           C  
ANISOU 2672  CD  GLU B 223     4955   5340   5357   -174   -396   -309       C  
ATOM   2673  OE1 GLU B 223      19.903  -5.108  36.931  1.00 47.34           O  
ANISOU 2673  OE1 GLU B 223     5721   6153   6111   -160   -497   -298       O  
ATOM   2674  OE2 GLU B 223      20.560  -4.702  38.989  1.00 45.85           O  
ANISOU 2674  OE2 GLU B 223     5518   5905   5998   -133   -353   -290       O  
ATOM   2675  N   GLU B 224      17.307  -9.327  40.078  1.00 18.64           N  
ANISOU 2675  N   GLU B 224     1909   2495   2679   -442   -217   -552       N  
ATOM   2676  CA  GLU B 224      15.951  -9.883  40.083  1.00 22.14           C  
ANISOU 2676  CA  GLU B 224     2245   2971   3194   -513   -227   -626       C  
ATOM   2677  C   GLU B 224      15.110  -9.358  41.249  1.00 21.92           C  
ANISOU 2677  C   GLU B 224     2105   2953   3271   -506   -171   -649       C  
ATOM   2678  O   GLU B 224      13.917  -9.095  41.101  1.00 22.88           O  
ANISOU 2678  O   GLU B 224     2094   3124   3475   -519   -219   -698       O  
ATOM   2679  CB  GLU B 224      16.003 -11.417  40.122  1.00 23.16           C  
ANISOU 2679  CB  GLU B 224     2439   3064   3297   -611   -159   -671       C  
ATOM   2680  CG  GLU B 224      14.647 -12.102  40.252  1.00 23.87           C  
ANISOU 2680  CG  GLU B 224     2431   3178   3460   -694   -145   -742       C  
ATOM   2681  CD  GLU B 224      13.782 -11.973  39.006  1.00 31.76           C  
ANISOU 2681  CD  GLU B 224     3363   4243   4462   -695   -272   -767       C  
ATOM   2682  OE1 GLU B 224      14.318 -11.662  37.920  1.00 31.30           O  
ANISOU 2682  OE1 GLU B 224     3351   4208   4335   -666   -368   -750       O  
ATOM   2683  OE2 GLU B 224      12.555 -12.190  39.119  1.00 35.93           O  
ANISOU 2683  OE2 GLU B 224     3795   4799   5056   -727   -275   -802       O  
ATOM   2684  N   TYR B 225      15.728  -9.219  42.413  1.00 20.43           N  
ANISOU 2684  N   TYR B 225     1965   2719   3077   -487    -71   -619       N  
ATOM   2685  CA  TYR B 225      14.997  -8.753  43.584  1.00 23.20           C  
ANISOU 2685  CA  TYR B 225     2225   3076   3514   -485     -1   -646       C  
ATOM   2686  C   TYR B 225      15.228  -7.278  43.867  1.00 22.86           C  
ANISOU 2686  C   TYR B 225     2150   3038   3497   -385    -30   -607       C  
ATOM   2687  O   TYR B 225      14.834  -6.770  44.918  1.00 23.01           O  
ANISOU 2687  O   TYR B 225     2113   3055   3576   -371     37   -625       O  
ATOM   2688  CB  TYR B 225      15.317  -9.630  44.801  1.00 21.05           C  
ANISOU 2688  CB  TYR B 225     2025   2752   3221   -543    137   -650       C  
ATOM   2689  CG  TYR B 225      14.759 -11.023  44.630  1.00 24.85           C  
ANISOU 2689  CG  TYR B 225     2514   3221   3706   -650    176   -700       C  
ATOM   2690  CD1 TYR B 225      13.396 -11.259  44.759  1.00 29.38           C  
ANISOU 2690  CD1 TYR B 225     2994   3826   4342   -683    189   -743       C  
ATOM   2691  CD2 TYR B 225      15.580 -12.092  44.305  1.00 25.47           C  
ANISOU 2691  CD2 TYR B 225     2720   3250   3707   -687    197   -682       C  
ATOM   2692  CE1 TYR B 225      12.867 -12.524  44.585  1.00 32.25           C  
ANISOU 2692  CE1 TYR B 225     3383   4174   4697   -763    223   -773       C  
ATOM   2693  CE2 TYR B 225      15.057 -13.369  44.126  1.00 28.29           C  
ANISOU 2693  CE2 TYR B 225     3105   3586   4058   -765    231   -713       C  
ATOM   2694  CZ  TYR B 225      13.703 -13.575  44.265  1.00 24.07           C  
ANISOU 2694  CZ  TYR B 225     2473   3084   3588   -803    243   -757       C  
ATOM   2695  OH  TYR B 225      13.163 -14.829  44.096  1.00 23.61           O  
ANISOU 2695  OH  TYR B 225     2441   3003   3525   -880    279   -788       O  
ATOM   2696  N   LYS B 226      15.853  -6.596  42.911  1.00 17.28           N  
ANISOU 2696  N   LYS B 226     1484   2337   2744   -320   -126   -556       N  
ATOM   2697  CA  LYS B 226      16.094  -5.154  43.010  1.00 19.99           C  
ANISOU 2697  CA  LYS B 226     1808   2677   3112   -225   -163   -515       C  
ATOM   2698  C   LYS B 226      16.797  -4.766  44.315  1.00 21.65           C  
ANISOU 2698  C   LYS B 226     2066   2845   3316   -204    -62   -497       C  
ATOM   2699  O   LYS B 226      16.384  -3.838  45.017  1.00 20.74           O  
ANISOU 2699  O   LYS B 226     1884   2728   3269   -161    -39   -510       O  
ATOM   2700  CB  LYS B 226      14.786  -4.377  42.837  1.00 26.85           C  
ANISOU 2700  CB  LYS B 226     2527   3587   4090   -190   -227   -551       C  
ATOM   2701  CG  LYS B 226      14.147  -4.580  41.461  1.00 36.26           C  
ANISOU 2701  CG  LYS B 226     3671   4828   5279   -197   -355   -562       C  
ATOM   2702  CD  LYS B 226      12.904  -3.721  41.266  1.00 46.20           C  
ANISOU 2702  CD  LYS B 226     4784   6127   6644   -142   -431   -587       C  
ATOM   2703  CE  LYS B 226      11.655  -4.377  41.845  1.00 57.12           C  
ANISOU 2703  CE  LYS B 226     6082   7534   8087   -200   -364   -649       C  
ATOM   2704  NZ  LYS B 226      11.540  -4.217  43.324  1.00 62.97           N  
ANISOU 2704  NZ  LYS B 226     6804   8243   8877   -206   -227   -674       N  
ATOM   2705  N   LEU B 227      17.855  -5.498  44.633  1.00 16.25           N  
ANISOU 2705  N   LEU B 227     1497   2128   2551   -232     -4   -471       N  
ATOM   2706  CA  LEU B 227      18.633  -5.246  45.841  1.00 15.18           C  
ANISOU 2706  CA  LEU B 227     1419   1958   2391   -215     80   -452       C  
ATOM   2707  C   LEU B 227      19.691  -4.176  45.596  1.00 19.67           C  
ANISOU 2707  C   LEU B 227     2039   2509   2927   -143     40   -398       C  
ATOM   2708  O   LEU B 227      20.084  -3.922  44.453  1.00 16.86           O  
ANISOU 2708  O   LEU B 227     1709   2157   2538   -117    -39   -364       O  
ATOM   2709  CB  LEU B 227      19.278  -6.545  46.326  1.00 15.59           C  
ANISOU 2709  CB  LEU B 227     1568   1981   2375   -271    153   -447       C  
ATOM   2710  CG  LEU B 227      18.275  -7.687  46.528  1.00 17.66           C  
ANISOU 2710  CG  LEU B 227     1795   2248   2668   -356    203   -499       C  
ATOM   2711  CD1 LEU B 227      18.974  -8.954  47.014  1.00 19.13           C  
ANISOU 2711  CD1 LEU B 227     2095   2389   2785   -404    275   -483       C  
ATOM   2712  CD2 LEU B 227      17.165  -7.260  47.480  1.00 19.26           C  
ANISOU 2712  CD2 LEU B 227     1896   2470   2953   -372    263   -547       C  
ATOM   2713  N   GLN B 228      20.142  -3.543  46.674  1.00 13.66           N  
ANISOU 2713  N   GLN B 228     1294   1726   2169   -116     96   -393       N  
ATOM   2714  CA  GLN B 228      21.203  -2.547  46.603  1.00 13.97           C  
ANISOU 2714  CA  GLN B 228     1383   1743   2182    -60     72   -350       C  
ATOM   2715  C   GLN B 228      22.528  -3.160  46.203  1.00 15.09           C  
ANISOU 2715  C   GLN B 228     1627   1872   2235    -69     68   -310       C  
ATOM   2716  O   GLN B 228      22.797  -4.325  46.494  1.00 16.23           O  
ANISOU 2716  O   GLN B 228     1819   2011   2335   -110    111   -315       O  
ATOM   2717  CB  GLN B 228      21.375  -1.872  47.967  1.00 15.57           C  
ANISOU 2717  CB  GLN B 228     1583   1929   2403    -43    140   -368       C  
ATOM   2718  CG  GLN B 228      20.179  -1.058  48.373  1.00 18.97           C  
ANISOU 2718  CG  GLN B 228     1912   2367   2930    -21    151   -413       C  
ATOM   2719  CD  GLN B 228      19.978   0.126  47.454  1.00 23.64           C  
ANISOU 2719  CD  GLN B 228     2461   2949   3573     43     66   -390       C  
ATOM   2720  OE1 GLN B 228      20.931   0.838  47.129  1.00 24.97           O  
ANISOU 2720  OE1 GLN B 228     2687   3091   3711     78     35   -347       O  
ATOM   2721  NE2 GLN B 228      18.746   0.330  47.008  1.00 25.98           N  
ANISOU 2721  NE2 GLN B 228     2656   3266   3948     59     25   -417       N  
ATOM   2722  N   ASN B 229      23.370  -2.357  45.560  1.00 13.55           N  
ANISOU 2722  N   ASN B 229     1465   1665   2017    -28     23   -269       N  
ATOM   2723  CA  ASN B 229      24.728  -2.774  45.273  1.00 13.05           C  
ANISOU 2723  CA  ASN B 229     1486   1590   1880    -30     30   -236       C  
ATOM   2724  C   ASN B 229      25.477  -3.069  46.560  1.00 14.92           C  
ANISOU 2724  C   ASN B 229     1761   1815   2092    -36     96   -243       C  
ATOM   2725  O   ASN B 229      26.295  -3.975  46.602  1.00 12.18           O  
ANISOU 2725  O   ASN B 229     1474   1463   1692    -49    117   -231       O  
ATOM   2726  CB  ASN B 229      25.471  -1.699  44.474  1.00 16.60           C  
ANISOU 2726  CB  ASN B 229     1958   2030   2320      8    -16   -195       C  
ATOM   2727  CG  ASN B 229      24.975  -1.594  43.045  1.00 23.09           C  
ANISOU 2727  CG  ASN B 229     2774   2865   3134     11    -90   -175       C  
ATOM   2728  OD1 ASN B 229      24.230  -2.454  42.576  1.00 21.11           O  
ANISOU 2728  OD1 ASN B 229     2505   2637   2878    -18   -110   -196       O  
ATOM   2729  ND2 ASN B 229      25.396  -0.549  42.342  1.00 28.60           N  
ANISOU 2729  ND2 ASN B 229     3492   3549   3827     44   -130   -134       N  
ATOM   2730  N   GLU B 230      25.190  -2.307  47.614  1.00 12.45           N  
ANISOU 2730  N   GLU B 230     1417   1497   1817    -22    127   -264       N  
ATOM   2731  CA  GLU B 230      25.870  -2.533  48.892  1.00 10.47           C  
ANISOU 2731  CA  GLU B 230     1208   1240   1530    -27    183   -271       C  
ATOM   2732  C   GLU B 230      25.613  -3.940  49.412  1.00 12.98           C  
ANISOU 2732  C   GLU B 230     1560   1560   1813    -68    230   -281       C  
ATOM   2733  O   GLU B 230      26.512  -4.580  49.954  1.00 13.09           O  
ANISOU 2733  O   GLU B 230     1638   1565   1770    -68    252   -264       O  
ATOM   2734  CB  GLU B 230      25.422  -1.502  49.937  1.00 14.93           C  
ANISOU 2734  CB  GLU B 230     1734   1801   2137    -13    214   -304       C  
ATOM   2735  CG  GLU B 230      25.954  -1.781  51.343  1.00 15.89           C  
ANISOU 2735  CG  GLU B 230     1903   1924   2210    -25    271   -318       C  
ATOM   2736  CD  GLU B 230      27.454  -1.595  51.472  1.00 23.63           C  
ANISOU 2736  CD  GLU B 230     2937   2902   3139     -5    249   -293       C  
ATOM   2737  OE1 GLU B 230      28.111  -1.167  50.491  1.00 17.75           O  
ANISOU 2737  OE1 GLU B 230     2190   2151   2401     14    204   -267       O  
ATOM   2738  OE2 GLU B 230      27.979  -1.869  52.577  1.00 19.59           O  
ANISOU 2738  OE2 GLU B 230     2468   2397   2578    -10    279   -300       O  
ATOM   2739  N   THR B 231      24.384  -4.420  49.227  1.00 11.96           N  
ANISOU 2739  N   THR B 231     1386   1437   1720   -102    242   -307       N  
ATOM   2740  CA  THR B 231      23.994  -5.760  49.661  1.00 11.97           C  
ANISOU 2740  CA  THR B 231     1420   1430   1698   -153    294   -318       C  
ATOM   2741  C   THR B 231      24.847  -6.831  48.982  1.00 14.14           C  
ANISOU 2741  C   THR B 231     1768   1687   1917   -159    277   -288       C  
ATOM   2742  O   THR B 231      25.332  -7.777  49.624  1.00 10.72           O  
ANISOU 2742  O   THR B 231     1406   1231   1438   -172    319   -275       O  
ATOM   2743  CB  THR B 231      22.501  -5.992  49.369  1.00 14.08           C  
ANISOU 2743  CB  THR B 231     1609   1713   2029   -194    304   -359       C  
ATOM   2744  OG1 THR B 231      21.740  -4.960  50.022  1.00 15.31           O  
ANISOU 2744  OG1 THR B 231     1690   1883   2245   -179    325   -392       O  
ATOM   2745  CG2 THR B 231      22.052  -7.368  49.874  1.00 12.18           C  
ANISOU 2745  CG2 THR B 231     1405   1455   1768   -261    371   -374       C  
ATOM   2746  N   LEU B 232      25.050  -6.665  47.683  1.00 10.07           N  
ANISOU 2746  N   LEU B 232     1242   1180   1405   -145    217   -277       N  
ATOM   2747  CA  LEU B 232      25.913  -7.570  46.927  1.00 10.21           C  
ANISOU 2747  CA  LEU B 232     1325   1181   1373   -146    203   -257       C  
ATOM   2748  C   LEU B 232      27.345  -7.552  47.464  1.00 11.68           C  
ANISOU 2748  C   LEU B 232     1569   1354   1514   -106    216   -227       C  
ATOM   2749  O   LEU B 232      27.959  -8.606  47.663  1.00 11.10           O  
ANISOU 2749  O   LEU B 232     1558   1255   1403   -107    240   -215       O  
ATOM   2750  CB  LEU B 232      25.902  -7.189  45.437  1.00 12.44           C  
ANISOU 2750  CB  LEU B 232     1588   1482   1658   -137    138   -252       C  
ATOM   2751  CG  LEU B 232      26.920  -7.884  44.531  1.00 14.03           C  
ANISOU 2751  CG  LEU B 232     1855   1671   1805   -131    127   -235       C  
ATOM   2752  CD1 LEU B 232      26.615  -9.372  44.400  1.00 15.87           C  
ANISOU 2752  CD1 LEU B 232     2130   1878   2022   -176    158   -258       C  
ATOM   2753  CD2 LEU B 232      26.954  -7.205  43.161  1.00 17.53           C  
ANISOU 2753  CD2 LEU B 232     2284   2137   2239   -120     66   -225       C  
ATOM   2754  N   HIS B 233      27.884  -6.357  47.701  1.00  9.71           N  
ANISOU 2754  N   HIS B 233     1297   1120   1274    -69    196   -216       N  
ATOM   2755  CA  HIS B 233      29.255  -6.255  48.203  1.00  9.90           C  
ANISOU 2755  CA  HIS B 233     1360   1141   1262    -34    199   -195       C  
ATOM   2756  C   HIS B 233      29.409  -6.898  49.574  1.00  9.75           C  
ANISOU 2756  C   HIS B 233     1382   1109   1211    -36    241   -194       C  
ATOM   2757  O   HIS B 233      30.418  -7.554  49.849  1.00 10.21           O  
ANISOU 2757  O   HIS B 233     1492   1157   1232    -12    243   -175       O  
ATOM   2758  CB  HIS B 233      29.710  -4.789  48.276  1.00 12.25           C  
ANISOU 2758  CB  HIS B 233     1621   1454   1581     -7    175   -193       C  
ATOM   2759  CG  HIS B 233      30.071  -4.203  46.948  1.00  9.42           C  
ANISOU 2759  CG  HIS B 233     1249   1099   1231      3    136   -177       C  
ATOM   2760  ND1 HIS B 233      31.377  -3.995  46.558  1.00 13.53           N  
ANISOU 2760  ND1 HIS B 233     1789   1623   1730     23    128   -160       N  
ATOM   2761  CD2 HIS B 233      29.297  -3.762  45.927  1.00 13.69           C  
ANISOU 2761  CD2 HIS B 233     1763   1643   1796     -5    104   -174       C  
ATOM   2762  CE1 HIS B 233      31.392  -3.455  45.352  1.00 14.58           C  
ANISOU 2762  CE1 HIS B 233     1915   1757   1867     21    102   -146       C  
ATOM   2763  NE2 HIS B 233      30.145  -3.309  44.944  1.00 14.80           N  
ANISOU 2763  NE2 HIS B 233     1919   1785   1918      7     81   -150       N  
ATOM   2764  N   LEU B 234      28.420  -6.689  50.443  1.00 10.03           N  
ANISOU 2764  N   LEU B 234     1399   1149   1264    -61    275   -215       N  
ATOM   2765  CA  LEU B 234      28.439  -7.308  51.757  1.00  9.79           C  
ANISOU 2765  CA  LEU B 234     1421   1106   1191    -71    321   -211       C  
ATOM   2766  C   LEU B 234      28.420  -8.834  51.644  1.00  9.12           C  
ANISOU 2766  C   LEU B 234     1402    985   1077    -92    347   -193       C  
ATOM   2767  O   LEU B 234      29.181  -9.525  52.326  1.00 11.93           O  
ANISOU 2767  O   LEU B 234     1828   1321   1382    -71    357   -166       O  
ATOM   2768  CB  LEU B 234      27.228  -6.848  52.583  1.00 10.72           C  
ANISOU 2768  CB  LEU B 234     1503   1234   1336   -105    368   -244       C  
ATOM   2769  CG  LEU B 234      27.263  -5.421  53.127  1.00 12.36           C  
ANISOU 2769  CG  LEU B 234     1666   1465   1564    -83    361   -267       C  
ATOM   2770  CD1 LEU B 234      25.918  -5.109  53.787  1.00 12.38           C  
ANISOU 2770  CD1 LEU B 234     1625   1475   1604   -117    419   -309       C  
ATOM   2771  CD2 LEU B 234      28.400  -5.276  54.141  1.00 14.33           C  
ANISOU 2771  CD2 LEU B 234     1972   1722   1750    -56    357   -254       C  
ATOM   2772  N   ALA B 235      27.537  -9.355  50.793  1.00  9.66           N  
ANISOU 2772  N   ALA B 235     1449   1043   1179   -132    354   -210       N  
ATOM   2773  CA  ALA B 235      27.407 -10.803  50.619  1.00 11.28           C  
ANISOU 2773  CA  ALA B 235     1717   1203   1365   -163    385   -202       C  
ATOM   2774  C   ALA B 235      28.741 -11.431  50.208  1.00 12.44           C  
ANISOU 2774  C   ALA B 235     1925   1326   1477   -115    359   -171       C  
ATOM   2775  O   ALA B 235      29.138 -12.485  50.726  1.00 11.15           O  
ANISOU 2775  O   ALA B 235     1840   1118   1279   -108    386   -147       O  
ATOM   2776  CB  ALA B 235      26.319 -11.127  49.588  1.00 11.22           C  
ANISOU 2776  CB  ALA B 235     1664   1195   1403   -216    382   -236       C  
ATOM   2777  N   VAL B 236      29.436 -10.776  49.285  1.00 10.55           N  
ANISOU 2777  N   VAL B 236     1648   1112   1247    -80    310   -172       N  
ATOM   2778  CA  VAL B 236      30.725 -11.284  48.812  1.00  8.87           C  
ANISOU 2778  CA  VAL B 236     1476    884   1012    -33    291   -153       C  
ATOM   2779  C   VAL B 236      31.755 -11.263  49.933  1.00 11.72           C  
ANISOU 2779  C   VAL B 236     1869   1244   1339     19    287   -124       C  
ATOM   2780  O   VAL B 236      32.532 -12.214  50.096  1.00 12.88           O  
ANISOU 2780  O   VAL B 236     2074   1357   1463     54    291   -103       O  
ATOM   2781  CB  VAL B 236      31.242 -10.495  47.599  1.00 11.32           C  
ANISOU 2781  CB  VAL B 236     1739   1226   1337    -15    251   -161       C  
ATOM   2782  CG1 VAL B 236      32.628 -10.992  47.190  1.00 12.87           C  
ANISOU 2782  CG1 VAL B 236     1966   1411   1515     34    244   -149       C  
ATOM   2783  CG2 VAL B 236      30.266 -10.647  46.432  1.00 12.39           C  
ANISOU 2783  CG2 VAL B 236     1854   1363   1490    -62    243   -186       C  
ATOM   2784  N   ASN B 237      31.755 -10.186  50.713  1.00  9.47           N  
ANISOU 2784  N   ASN B 237     1549    997   1053     25    276   -127       N  
ATOM   2785  CA  ASN B 237      32.597 -10.145  51.913  1.00 13.17           C  
ANISOU 2785  CA  ASN B 237     2050   1473   1481     66    265   -106       C  
ATOM   2786  C   ASN B 237      32.326 -11.321  52.855  1.00 13.88           C  
ANISOU 2786  C   ASN B 237     2228   1520   1527     59    301    -79       C  
ATOM   2787  O   ASN B 237      33.262 -11.960  53.344  1.00 10.64           O  
ANISOU 2787  O   ASN B 237     1870   1091   1080    109    283    -48       O  
ATOM   2788  CB  ASN B 237      32.428  -8.821  52.662  1.00 14.86           C  
ANISOU 2788  CB  ASN B 237     2219   1731   1697     59    256   -124       C  
ATOM   2789  CG  ASN B 237      33.206  -8.787  53.967  1.00 18.04           C  
ANISOU 2789  CG  ASN B 237     2660   2147   2045     93    241   -109       C  
ATOM   2790  OD1 ASN B 237      32.705  -9.200  55.009  1.00 16.46           O  
ANISOU 2790  OD1 ASN B 237     2517   1936   1802     76    272    -99       O  
ATOM   2791  ND2 ASN B 237      34.450  -8.318  53.907  1.00 19.09           N  
ANISOU 2791  ND2 ASN B 237     2766   2308   2178    137    192   -108       N  
ATOM   2792  N   TYR B 238      31.051 -11.612  53.107  1.00 11.28           N  
ANISOU 2792  N   TYR B 238     1912   1171   1202     -2    352    -90       N  
ATOM   2793  CA  TYR B 238      30.697 -12.701  54.022  1.00 10.29           C  
ANISOU 2793  CA  TYR B 238     1880    998   1033    -22    400    -62       C  
ATOM   2794  C   TYR B 238      31.161 -14.036  53.463  1.00 13.64           C  
ANISOU 2794  C   TYR B 238     2370   1358   1455     -2    403    -37       C  
ATOM   2795  O   TYR B 238      31.652 -14.885  54.197  1.00 14.03           O  
ANISOU 2795  O   TYR B 238     2508   1364   1458     29    410      5       O  
ATOM   2796  CB  TYR B 238      29.188 -12.777  54.241  1.00 10.31           C  
ANISOU 2796  CB  TYR B 238     1871    992   1056   -103    466    -89       C  
ATOM   2797  CG  TYR B 238      28.552 -11.525  54.800  1.00 11.26           C  
ANISOU 2797  CG  TYR B 238     1925   1166   1189   -124    478   -122       C  
ATOM   2798  CD1 TYR B 238      29.314 -10.537  55.414  1.00 13.22           C  
ANISOU 2798  CD1 TYR B 238     2157   1457   1411    -79    440   -121       C  
ATOM   2799  CD2 TYR B 238      27.178 -11.345  54.724  1.00 12.23           C  
ANISOU 2799  CD2 TYR B 238     1995   1295   1356   -190    529   -161       C  
ATOM   2800  CE1 TYR B 238      28.714  -9.383  55.915  1.00 12.86           C  
ANISOU 2800  CE1 TYR B 238     2054   1450   1381    -98    457   -158       C  
ATOM   2801  CE2 TYR B 238      26.569 -10.210  55.233  1.00 15.65           C  
ANISOU 2801  CE2 TYR B 238     2364   1771   1811   -203    545   -196       C  
ATOM   2802  CZ  TYR B 238      27.339  -9.234  55.822  1.00 14.56           C  
ANISOU 2802  CZ  TYR B 238     2221   1666   1644   -156    512   -195       C  
ATOM   2803  OH  TYR B 238      26.724  -8.102  56.311  1.00 14.03           O  
ANISOU 2803  OH  TYR B 238     2094   1634   1603   -167    533   -237       O  
ATOM   2804  N   ILE B 239      30.978 -14.218  52.160  1.00 12.46           N  
ANISOU 2804  N   ILE B 239     2182   1200   1353    -18    398    -64       N  
ATOM   2805  CA  ILE B 239      31.367 -15.467  51.510  1.00 13.67           C  
ANISOU 2805  CA  ILE B 239     2396   1289   1510     -4    407    -54       C  
ATOM   2806  C   ILE B 239      32.867 -15.692  51.603  1.00 13.76           C  
ANISOU 2806  C   ILE B 239     2432   1293   1503     88    365    -24       C  
ATOM   2807  O   ILE B 239      33.317 -16.778  51.972  1.00 14.16           O  
ANISOU 2807  O   ILE B 239     2567   1279   1533    124    376      9       O  
ATOM   2808  CB  ILE B 239      30.954 -15.477  50.027  1.00 15.88           C  
ANISOU 2808  CB  ILE B 239     2626   1573   1834    -39    403    -98       C  
ATOM   2809  CG1 ILE B 239      29.431 -15.560  49.918  1.00 13.61           C  
ANISOU 2809  CG1 ILE B 239     2316   1283   1572   -130    442   -131       C  
ATOM   2810  CG2 ILE B 239      31.605 -16.652  49.296  1.00 15.07           C  
ANISOU 2810  CG2 ILE B 239     2584   1408   1734    -12    410    -97       C  
ATOM   2811  CD1 ILE B 239      28.909 -15.168  48.560  1.00 14.82           C  
ANISOU 2811  CD1 ILE B 239     2400   1470   1763   -164    415   -176       C  
ATOM   2812  N   ASP B 240      33.647 -14.667  51.271  1.00 12.09           N  
ANISOU 2812  N   ASP B 240     2146   1145   1304    128    317    -37       N  
ATOM   2813  CA  ASP B 240      35.104 -14.816  51.296  1.00 11.71           C  
ANISOU 2813  CA  ASP B 240     2098   1101   1251    213    276    -19       C  
ATOM   2814  C   ASP B 240      35.633 -15.063  52.700  1.00 14.09           C  
ANISOU 2814  C   ASP B 240     2454   1395   1503    262    254     26       C  
ATOM   2815  O   ASP B 240      36.542 -15.870  52.882  1.00 15.73           O  
ANISOU 2815  O   ASP B 240     2706   1567   1704    332    234     54       O  
ATOM   2816  CB  ASP B 240      35.791 -13.607  50.666  1.00 11.56           C  
ANISOU 2816  CB  ASP B 240     1982   1152   1258    231    238    -45       C  
ATOM   2817  CG  ASP B 240      35.658 -13.590  49.151  1.00 18.01           C  
ANISOU 2817  CG  ASP B 240     2766   1968   2109    205    252    -79       C  
ATOM   2818  OD1 ASP B 240      35.606 -14.681  48.539  1.00 18.31           O  
ANISOU 2818  OD1 ASP B 240     2851   1951   2153    206    279    -84       O  
ATOM   2819  OD2 ASP B 240      35.597 -12.487  48.587  1.00 13.89           O  
ANISOU 2819  OD2 ASP B 240     2177   1497   1604    184    237    -99       O  
ATOM   2820  N   ARG B 241      35.055 -14.392  53.695  1.00 14.01           N  
ANISOU 2820  N   ARG B 241     2447   1419   1459    228    258     31       N  
ATOM   2821  CA  ARG B 241      35.444 -14.661  55.078  1.00 14.14           C  
ANISOU 2821  CA  ARG B 241     2532   1430   1410    266    238     74       C  
ATOM   2822  C   ARG B 241      35.047 -16.071  55.528  1.00 14.47           C  
ANISOU 2822  C   ARG B 241     2696   1384   1419    262    280    120       C  
ATOM   2823  O   ARG B 241      35.816 -16.739  56.226  1.00 17.01           O  
ANISOU 2823  O   ARG B 241     3089   1675   1699    330    248    169       O  
ATOM   2824  CB  ARG B 241      34.884 -13.601  56.028  1.00 15.31           C  
ANISOU 2824  CB  ARG B 241     2661   1635   1523    224    242     60       C  
ATOM   2825  CG  ARG B 241      35.583 -12.262  55.873  1.00 18.80           C  
ANISOU 2825  CG  ARG B 241     3004   2153   1987    245    189     25       C  
ATOM   2826  CD  ARG B 241      34.708 -11.134  56.365  1.00 25.32           C  
ANISOU 2826  CD  ARG B 241     3793   3020   2806    186    214     -9       C  
ATOM   2827  NE  ARG B 241      34.410 -11.277  57.773  1.00 26.33           N  
ANISOU 2827  NE  ARG B 241     3998   3150   2856    176    229     11       N  
ATOM   2828  CZ  ARG B 241      33.382 -10.699  58.384  1.00 26.54           C  
ANISOU 2828  CZ  ARG B 241     4026   3193   2866    116    280    -14       C  
ATOM   2829  NH1 ARG B 241      32.530  -9.934  57.705  1.00 20.79           N  
ANISOU 2829  NH1 ARG B 241     3219   2477   2203     70    312    -59       N  
ATOM   2830  NH2 ARG B 241      33.203 -10.899  59.679  1.00 21.00           N  
ANISOU 2830  NH2 ARG B 241     3407   2494   2080    107    299      6       N  
ATOM   2831  N   PHE B 242      33.860 -16.526  55.122  1.00 13.42           N  
ANISOU 2831  N   PHE B 242     2586   1206   1306    184    349    105       N  
ATOM   2832  CA  PHE B 242      33.403 -17.879  55.472  1.00 15.49           C  
ANISOU 2832  CA  PHE B 242     2968   1372   1545    164    402    144       C  
ATOM   2833  C   PHE B 242      34.342 -18.928  54.883  1.00 17.82           C  
ANISOU 2833  C   PHE B 242     3308   1599   1864    238    380    166       C  
ATOM   2834  O   PHE B 242      34.761 -19.860  55.575  1.00 19.50           O  
ANISOU 2834  O   PHE B 242     3627   1745   2039    287    377    223       O  
ATOM   2835  CB  PHE B 242      31.965 -18.122  54.990  1.00 14.48           C  
ANISOU 2835  CB  PHE B 242     2834   1216   1451     56    480    108       C  
ATOM   2836  CG  PHE B 242      31.369 -19.420  55.468  1.00 16.07           C  
ANISOU 2836  CG  PHE B 242     3160   1317   1629     13    549    144       C  
ATOM   2837  CD1 PHE B 242      30.763 -19.506  56.714  1.00 18.84           C  
ANISOU 2837  CD1 PHE B 242     3584   1656   1917    -30    597    177       C  
ATOM   2838  CD2 PHE B 242      31.391 -20.550  54.660  1.00 19.08           C  
ANISOU 2838  CD2 PHE B 242     3590   1611   2048      9    573    140       C  
ATOM   2839  CE1 PHE B 242      30.208 -20.700  57.157  1.00 21.74           C  
ANISOU 2839  CE1 PHE B 242     4034   1955   2273    -70    651    193       C  
ATOM   2840  CE2 PHE B 242      30.843 -21.742  55.092  1.00 18.44           C  
ANISOU 2840  CE2 PHE B 242     3588   1467   1953    -31    625    156       C  
ATOM   2841  CZ  PHE B 242      30.248 -21.820  56.345  1.00 22.16           C  
ANISOU 2841  CZ  PHE B 242     4112   1939   2369    -71    664    183       C  
ATOM   2842  N   LEU B 243      34.688 -18.759  53.610  1.00 17.93           N  
ANISOU 2842  N   LEU B 243     3245   1630   1939    250    366    120       N  
ATOM   2843  CA  LEU B 243      35.525 -19.732  52.917  1.00 16.77           C  
ANISOU 2843  CA  LEU B 243     3131   1418   1824    316    358    125       C  
ATOM   2844  C   LEU B 243      36.978 -19.643  53.373  1.00 20.84           C  
ANISOU 2844  C   LEU B 243     3632   1957   2328    433    287    156       C  
ATOM   2845  O   LEU B 243      37.773 -20.544  53.107  1.00 22.14           O  
ANISOU 2845  O   LEU B 243     3835   2061   2516    509    277    172       O  
ATOM   2846  CB  LEU B 243      35.434 -19.549  51.400  1.00 14.87           C  
ANISOU 2846  CB  LEU B 243     2816   1195   1641    287    371     61       C  
ATOM   2847  CG  LEU B 243      34.058 -19.765  50.779  1.00 17.58           C  
ANISOU 2847  CG  LEU B 243     3165   1513   2000    177    429     22       C  
ATOM   2848  CD1 LEU B 243      34.070 -19.407  49.296  1.00 17.45           C  
ANISOU 2848  CD1 LEU B 243     3074   1533   2024    155    423    -38       C  
ATOM   2849  CD2 LEU B 243      33.607 -21.204  50.988  1.00 23.60           C  
ANISOU 2849  CD2 LEU B 243     4038   2169   2760    151    482     42       C  
ATOM   2850  N   SER B 244      37.321 -18.556  54.057  1.00 22.03           N  
ANISOU 2850  N   SER B 244     3723   2196   2449    448    236    160       N  
ATOM   2851  CA  SER B 244      38.652 -18.418  54.634  1.00 26.42           C  
ANISOU 2851  CA  SER B 244     4259   2787   2993    552    159    186       C  
ATOM   2852  C   SER B 244      38.810 -19.333  55.848  1.00 26.46           C  
ANISOU 2852  C   SER B 244     4389   2730   2934    604    141    260       C  
ATOM   2853  O   SER B 244      39.927 -19.653  56.247  1.00 29.12           O  
ANISOU 2853  O   SER B 244     4732   3066   3266    707     73    292       O  
ATOM   2854  CB  SER B 244      38.934 -16.967  55.037  1.00 27.08           C  
ANISOU 2854  CB  SER B 244     4247   2982   3061    540    111    160       C  
ATOM   2855  OG  SER B 244      39.067 -16.123  53.908  1.00 23.91           O  
ANISOU 2855  OG  SER B 244     3734   2632   2718    513    117    102       O  
ATOM   2856  N   SER B 245      37.688 -19.745  56.433  1.00 24.04           N  
ANISOU 2856  N   SER B 245     4182   2373   2581    531    200    289       N  
ATOM   2857  CA  SER B 245      37.709 -20.560  57.647  1.00 29.54           C  
ANISOU 2857  CA  SER B 245     4988   3028   3209    553    190    352       C  
ATOM   2858  C   SER B 245      37.168 -21.974  57.450  1.00 30.19           C  
ANISOU 2858  C   SER B 245     5148   3012   3310    518    254    364       C  
ATOM   2859  O   SER B 245      37.576 -22.896  58.156  1.00 30.47           O  
ANISOU 2859  O   SER B 245     5253   3005   3318    564    233    411       O  
ATOM   2860  CB  SER B 245      36.920 -19.878  58.768  1.00 34.63           C  
ANISOU 2860  CB  SER B 245     5672   3714   3770    486    209    368       C  
ATOM   2861  OG  SER B 245      37.481 -18.620  59.098  1.00 41.07           O  
ANISOU 2861  OG  SER B 245     6412   4633   4561    515    143    350       O  
ATOM   2862  N   MET B 246      36.244 -22.140  56.507  1.00 23.36           N  
ANISOU 2862  N   MET B 246     4270   2113   2492    435    329    321       N  
ATOM   2863  CA  MET B 246      35.531 -23.407  56.347  1.00 23.08           C  
ANISOU 2863  CA  MET B 246     4307   1993   2471    380    396    323       C  
ATOM   2864  C   MET B 246      35.712 -24.022  54.963  1.00 25.41           C  
ANISOU 2864  C   MET B 246     4563   2249   2842    383    415    278       C  
ATOM   2865  O   MET B 246      35.584 -23.332  53.954  1.00 26.27           O  
ANISOU 2865  O   MET B 246     4591   2396   2993    357    420    224       O  
ATOM   2866  CB  MET B 246      34.038 -23.196  56.590  1.00 22.62           C  
ANISOU 2866  CB  MET B 246     4269   1933   2394    254    476    303       C  
ATOM   2867  CG  MET B 246      33.717 -22.586  57.941  1.00 34.07           C  
ANISOU 2867  CG  MET B 246     5753   3425   3767    233    474    336       C  
ATOM   2868  SD  MET B 246      33.650 -23.842  59.228  1.00 50.81           S  
ANISOU 2868  SD  MET B 246     8005   5476   5823    241    491    400       S  
ATOM   2869  CE  MET B 246      32.164 -24.714  58.739  1.00 41.67           C  
ANISOU 2869  CE  MET B 246     6878   4249   4706    113    606    362       C  
ATOM   2870  N   SER B 247      35.992 -25.323  54.918  1.00 27.73           N  
ANISOU 2870  N   SER B 247     4918   2467   3152    412    427    298       N  
ATOM   2871  CA  SER B 247      36.038 -26.045  53.646  1.00 26.31           C  
ANISOU 2871  CA  SER B 247     4715   2243   3038    402    457    251       C  
ATOM   2872  C   SER B 247      34.616 -26.340  53.184  1.00 30.66           C  
ANISOU 2872  C   SER B 247     5284   2766   3599    274    536    210       C  
ATOM   2873  O   SER B 247      33.760 -26.694  53.989  1.00 32.20           O  
ANISOU 2873  O   SER B 247     5546   2931   3758    212    580    235       O  
ATOM   2874  CB  SER B 247      36.828 -27.347  53.780  1.00 38.89           C  
ANISOU 2874  CB  SER B 247     6369   3757   4650    479    443    284       C  
ATOM   2875  OG  SER B 247      38.217 -27.090  53.873  1.00 47.09           O  
ANISOU 2875  OG  SER B 247     7358   4829   5705    598    366    302       O  
ATOM   2876  N   VAL B 248      34.370 -26.185  51.885  1.00 26.32           N  
ANISOU 2876  N   VAL B 248     4668   2234   3098    232    553    145       N  
ATOM   2877  CA  VAL B 248      33.034 -26.344  51.320  1.00 22.23           C  
ANISOU 2877  CA  VAL B 248     4142   1708   2595    110    613     96       C  
ATOM   2878  C   VAL B 248      33.142 -27.103  49.994  1.00 25.36           C  
ANISOU 2878  C   VAL B 248     4523   2072   3041     98    628     43       C  
ATOM   2879  O   VAL B 248      33.940 -26.742  49.129  1.00 27.72           O  
ANISOU 2879  O   VAL B 248     4762   2405   3367    149    593     14       O  
ATOM   2880  CB  VAL B 248      32.367 -24.963  51.062  1.00 30.73           C  
ANISOU 2880  CB  VAL B 248     5134   2869   3671     50    607     59       C  
ATOM   2881  CG1 VAL B 248      31.038 -25.120  50.337  1.00 30.04           C  
ANISOU 2881  CG1 VAL B 248     5018   2786   3611    -69    656      0       C  
ATOM   2882  CG2 VAL B 248      32.172 -24.199  52.368  1.00 34.06           C  
ANISOU 2882  CG2 VAL B 248     5576   3323   4044     52    602    105       C  
ATOM   2883  N   LEU B 249      32.354 -28.162  49.841  1.00 21.64           N  
ANISOU 2883  N   LEU B 249     4105   1535   2581     28    682     27       N  
ATOM   2884  CA  LEU B 249      32.319 -28.899  48.580  1.00 24.33           C  
ANISOU 2884  CA  LEU B 249     4436   1844   2964      3    700    -31       C  
ATOM   2885  C   LEU B 249      31.474 -28.124  47.574  1.00 23.73           C  
ANISOU 2885  C   LEU B 249     4276   1841   2902    -84    700   -100       C  
ATOM   2886  O   LEU B 249      30.601 -27.349  47.968  1.00 21.94           O  
ANISOU 2886  O   LEU B 249     4013   1663   2660   -147    706   -103       O  
ATOM   2887  CB  LEU B 249      31.773 -30.310  48.796  1.00 30.37           C  
ANISOU 2887  CB  LEU B 249     5291   2509   3737    -42    756    -25       C  
ATOM   2888  CG  LEU B 249      32.807 -31.406  49.079  1.00 40.65           C  
ANISOU 2888  CG  LEU B 249     6671   3722   5053     53    751     16       C  
ATOM   2889  CD1 LEU B 249      33.945 -30.901  49.958  1.00 41.82           C  
ANISOU 2889  CD1 LEU B 249     6820   3893   5178    171    693     81       C  
ATOM   2890  CD2 LEU B 249      32.140 -32.624  49.711  1.00 41.14           C  
ANISOU 2890  CD2 LEU B 249     6838   3685   5110      3    809     42       C  
ATOM   2891  N   ARG B 250      31.725 -28.332  46.281  1.00 20.72           N  
ANISOU 2891  N   ARG B 250     3861   1466   2546    -87    691   -156       N  
ATOM   2892  CA  ARG B 250      31.109 -27.489  45.254  1.00 20.90           C  
ANISOU 2892  CA  ARG B 250     3801   1568   2574   -151    673   -217       C  
ATOM   2893  C   ARG B 250      29.580 -27.487  45.303  1.00 20.69           C  
ANISOU 2893  C   ARG B 250     3758   1554   2550   -271    701   -248       C  
ATOM   2894  O   ARG B 250      28.950 -26.473  45.000  1.00 18.62           O  
ANISOU 2894  O   ARG B 250     3421   1368   2287   -318    676   -275       O  
ATOM   2895  CB  ARG B 250      31.598 -27.867  43.850  1.00 21.01           C  
ANISOU 2895  CB  ARG B 250     3797   1580   2604   -140    664   -275       C  
ATOM   2896  CG  ARG B 250      31.091 -29.212  43.349  1.00 21.23           C  
ANISOU 2896  CG  ARG B 250     3883   1534   2651   -195    707   -313       C  
ATOM   2897  CD  ARG B 250      31.735 -29.541  42.010  1.00 22.89           C  
ANISOU 2897  CD  ARG B 250     4082   1744   2872   -172    699   -370       C  
ATOM   2898  NE  ARG B 250      33.175 -29.738  42.144  1.00 24.43           N  
ANISOU 2898  NE  ARG B 250     4291   1912   3079    -55    691   -342       N  
ATOM   2899  CZ  ARG B 250      34.018 -29.806  41.119  1.00 26.22           C  
ANISOU 2899  CZ  ARG B 250     4496   2151   3314    -12    685   -385       C  
ATOM   2900  NH1 ARG B 250      33.564 -29.674  39.879  1.00 21.22           N  
ANISOU 2900  NH1 ARG B 250     3837   1559   2667    -75    684   -453       N  
ATOM   2901  NH2 ARG B 250      35.315 -30.002  41.334  1.00 23.65           N  
ANISOU 2901  NH2 ARG B 250     4173   1802   3011     96    679   -362       N  
ATOM   2902  N   GLY B 251      28.994 -28.613  45.702  1.00 21.26           N  
ANISOU 2902  N   GLY B 251     3896   1552   2630   -320    752   -244       N  
ATOM   2903  CA  GLY B 251      27.546 -28.743  45.763  1.00 22.49           C  
ANISOU 2903  CA  GLY B 251     4031   1717   2796   -436    786   -279       C  
ATOM   2904  C   GLY B 251      26.904 -27.881  46.844  1.00 25.68           C  
ANISOU 2904  C   GLY B 251     4406   2167   3186   -465    796   -249       C  
ATOM   2905  O   GLY B 251      25.684 -27.709  46.871  1.00 23.25           O  
ANISOU 2905  O   GLY B 251     4050   1890   2894   -558    817   -285       O  
ATOM   2906  N   LYS B 252      27.727 -27.344  47.741  1.00 19.84           N  
ANISOU 2906  N   LYS B 252     3689   1432   2418   -383    778   -186       N  
ATOM   2907  CA  LYS B 252      27.238 -26.552  48.870  1.00 22.93           C  
ANISOU 2907  CA  LYS B 252     4066   1859   2787   -402    792   -155       C  
ATOM   2908  C   LYS B 252      27.612 -25.076  48.721  1.00 20.55           C  
ANISOU 2908  C   LYS B 252     3685   1641   2481   -363    737   -156       C  
ATOM   2909  O   LYS B 252      27.209 -24.235  49.532  1.00 20.55           O  
ANISOU 2909  O   LYS B 252     3659   1680   2468   -379    743   -140       O  
ATOM   2910  CB  LYS B 252      27.809 -27.091  50.187  1.00 25.72           C  
ANISOU 2910  CB  LYS B 252     4520   2151   3101   -344    815    -79       C  
ATOM   2911  CG  LYS B 252      27.063 -28.281  50.813  1.00 38.23           C  
ANISOU 2911  CG  LYS B 252     6185   3660   4680   -407    885    -69       C  
ATOM   2912  CD  LYS B 252      26.583 -29.314  49.795  1.00 48.70           C  
ANISOU 2912  CD  LYS B 252     7516   4941   6048   -467    912   -124       C  
ATOM   2913  CE  LYS B 252      26.870 -30.746  50.233  1.00 56.59           C  
ANISOU 2913  CE  LYS B 252     8634   5829   7040   -450    954    -87       C  
ATOM   2914  NZ  LYS B 252      28.127 -31.273  49.626  1.00 58.49           N  
ANISOU 2914  NZ  LYS B 252     8908   6023   7291   -353    916    -75       N  
ATOM   2915  N   LEU B 253      28.396 -24.765  47.692  1.00 17.17           N  
ANISOU 2915  N   LEU B 253     3222   1239   2064   -312    687   -178       N  
ATOM   2916  CA  LEU B 253      28.867 -23.397  47.479  1.00 17.44           C  
ANISOU 2916  CA  LEU B 253     3186   1345   2093   -269    635   -180       C  
ATOM   2917  C   LEU B 253      27.706 -22.426  47.258  1.00 18.42           C  
ANISOU 2917  C   LEU B 253     3224   1538   2237   -350    628   -223       C  
ATOM   2918  O   LEU B 253      27.716 -21.305  47.769  1.00 16.82           O  
ANISOU 2918  O   LEU B 253     2982   1382   2030   -335    610   -210       O  
ATOM   2919  CB  LEU B 253      29.834 -23.342  46.288  1.00 18.02           C  
ANISOU 2919  CB  LEU B 253     3236   1436   2174   -211    594   -205       C  
ATOM   2920  CG  LEU B 253      30.450 -21.976  45.954  1.00 18.84           C  
ANISOU 2920  CG  LEU B 253     3271   1615   2272   -162    542   -209       C  
ATOM   2921  CD1 LEU B 253      31.201 -21.397  47.151  1.00 17.15           C  
ANISOU 2921  CD1 LEU B 253     3075   1404   2039    -88    530   -152       C  
ATOM   2922  CD2 LEU B 253      31.377 -22.084  44.731  1.00 19.96           C  
ANISOU 2922  CD2 LEU B 253     3395   1771   2416   -115    517   -237       C  
ATOM   2923  N   GLN B 254      26.702 -22.857  46.503  1.00 17.34           N  
ANISOU 2923  N   GLN B 254     3053   1408   2126   -433    639   -277       N  
ATOM   2924  CA  GLN B 254      25.554 -21.997  46.243  1.00 17.83           C  
ANISOU 2924  CA  GLN B 254     3020   1539   2214   -506    623   -323       C  
ATOM   2925  C   GLN B 254      24.730 -21.765  47.513  1.00 19.10           C  
ANISOU 2925  C   GLN B 254     3171   1702   2382   -550    673   -305       C  
ATOM   2926  O   GLN B 254      24.110 -20.711  47.678  1.00 18.55           O  
ANISOU 2926  O   GLN B 254     3020   1693   2333   -577    659   -324       O  
ATOM   2927  CB  GLN B 254      24.687 -22.568  45.113  1.00 16.55           C  
ANISOU 2927  CB  GLN B 254     2822   1389   2078   -580    613   -388       C  
ATOM   2928  CG  GLN B 254      23.553 -21.644  44.678  1.00 19.07           C  
ANISOU 2928  CG  GLN B 254     3029   1790   2429   -643    575   -439       C  
ATOM   2929  CD  GLN B 254      22.799 -22.158  43.466  1.00 22.17           C  
ANISOU 2929  CD  GLN B 254     3384   2201   2838   -707    546   -504       C  
ATOM   2930  OE1 GLN B 254      22.928 -23.321  43.085  1.00 20.64           O  
ANISOU 2930  OE1 GLN B 254     3252   1953   2638   -723    572   -516       O  
ATOM   2931  NE2 GLN B 254      22.010 -21.285  42.848  1.00 19.83           N  
ANISOU 2931  NE2 GLN B 254     2987   1983   2563   -740    487   -547       N  
ATOM   2932  N   LEU B 255      24.734 -22.748  48.410  1.00 17.70           N  
ANISOU 2932  N   LEU B 255     3079   1459   2185   -556    733   -268       N  
ATOM   2933  CA  LEU B 255      24.023 -22.621  49.683  1.00 16.01           C  
ANISOU 2933  CA  LEU B 255     2873   1246   1964   -596    790   -249       C  
ATOM   2934  C   LEU B 255      24.708 -21.563  50.537  1.00 15.29           C  
ANISOU 2934  C   LEU B 255     2788   1180   1842   -533    773   -203       C  
ATOM   2935  O   LEU B 255      24.046 -20.737  51.164  1.00 15.78           O  
ANISOU 2935  O   LEU B 255     2795   1288   1912   -567    793   -212       O  
ATOM   2936  CB  LEU B 255      23.995 -23.961  50.422  1.00 17.63           C  
ANISOU 2936  CB  LEU B 255     3187   1369   2144   -609    853   -216       C  
ATOM   2937  CG  LEU B 255      23.281 -23.973  51.775  1.00 19.80           C  
ANISOU 2937  CG  LEU B 255     3487   1638   2397   -651    920   -196       C  
ATOM   2938  CD1 LEU B 255      21.854 -23.481  51.623  1.00 20.65           C  
ANISOU 2938  CD1 LEU B 255     3482   1808   2556   -745    946   -262       C  
ATOM   2939  CD2 LEU B 255      23.300 -25.378  52.380  1.00 23.75           C  
ANISOU 2939  CD2 LEU B 255     4105   2049   2870   -663    977   -164       C  
ATOM   2940  N   VAL B 256      26.039 -21.592  50.561  1.00 15.86           N  
ANISOU 2940  N   VAL B 256     2921   1224   1880   -439    737   -157       N  
ATOM   2941  CA  VAL B 256      26.803 -20.563  51.263  1.00 19.38           C  
ANISOU 2941  CA  VAL B 256     3371   1697   2297   -373    709   -116       C  
ATOM   2942  C   VAL B 256      26.470 -19.179  50.713  1.00 17.25           C  
ANISOU 2942  C   VAL B 256     2973   1523   2058   -379    661   -158       C  
ATOM   2943  O   VAL B 256      26.190 -18.247  51.474  1.00 16.18           O  
ANISOU 2943  O   VAL B 256     2788   1446   1912   -376    661   -151       O  
ATOM   2944  CB  VAL B 256      28.326 -20.806  51.163  1.00 17.85           C  
ANISOU 2944  CB  VAL B 256     3236   1471   2074   -261    662    -72       C  
ATOM   2945  CG1 VAL B 256      29.106 -19.628  51.758  1.00 18.48           C  
ANISOU 2945  CG1 VAL B 256     3275   1623   2124   -185    609    -42       C  
ATOM   2946  CG2 VAL B 256      28.704 -22.118  51.855  1.00 18.14           C  
ANISOU 2946  CG2 VAL B 256     3381   1436   2077   -231    690    -22       C  
ATOM   2947  N   GLY B 257      26.492 -19.054  49.389  1.00 15.85           N  
ANISOU 2947  N   GLY B 257     2739   1370   1911   -381    617   -202       N  
ATOM   2948  CA  GLY B 257      26.217 -17.783  48.742  1.00 16.78           C  
ANISOU 2948  CA  GLY B 257     2738   1583   2053   -375    559   -234       C  
ATOM   2949  C   GLY B 257      24.806 -17.297  49.004  1.00 15.21           C  
ANISOU 2949  C   GLY B 257     2458   1427   1895   -452    583   -272       C  
ATOM   2950  O   GLY B 257      24.570 -16.102  49.188  1.00 15.89           O  
ANISOU 2950  O   GLY B 257     2460   1582   1994   -433    553   -277       O  
ATOM   2951  N   THR B 258      23.862 -18.231  49.037  1.00 15.75           N  
ANISOU 2951  N   THR B 258     2548   1448   1987   -542    641   -302       N  
ATOM   2952  CA  THR B 258      22.466 -17.895  49.288  1.00 15.23           C  
ANISOU 2952  CA  THR B 258     2394   1422   1972   -624    674   -347       C  
ATOM   2953  C   THR B 258      22.246 -17.377  50.707  1.00 19.26           C  
ANISOU 2953  C   THR B 258     2905   1946   2465   -621    729   -319       C  
ATOM   2954  O   THR B 258      21.582 -16.359  50.909  1.00 16.20           O  
ANISOU 2954  O   THR B 258     2416   1628   2113   -626    721   -346       O  
ATOM   2955  CB  THR B 258      21.558 -19.107  49.011  1.00 21.76           C  
ANISOU 2955  CB  THR B 258     3231   2217   2820   -703    716   -382       C  
ATOM   2956  OG1 THR B 258      21.728 -19.505  47.646  1.00 20.57           O  
ANISOU 2956  OG1 THR B 258     3072   2067   2677   -703    658   -413       O  
ATOM   2957  CG2 THR B 258      20.107 -18.756  49.251  1.00 26.12           C  
ANISOU 2957  CG2 THR B 258     3672   2824   3427   -773    742   -432       C  
ATOM   2958  N   ALA B 259      22.808 -18.075  51.690  1.00 17.48           N  
ANISOU 2958  N   ALA B 259     2800   1656   2185   -608    783   -266       N  
ATOM   2959  CA  ALA B 259      22.740 -17.615  53.074  1.00 19.43           C  
ANISOU 2959  CA  ALA B 259     3070   1918   2394   -601    833   -235       C  
ATOM   2960  C   ALA B 259      23.425 -16.260  53.258  1.00 17.28           C  
ANISOU 2960  C   ALA B 259     2742   1720   2104   -513    765   -222       C  
ATOM   2961  O   ALA B 259      22.947 -15.417  54.013  1.00 15.22           O  
ANISOU 2961  O   ALA B 259     2432   1506   1846   -521    791   -236       O  
ATOM   2962  CB  ALA B 259      23.339 -18.651  54.021  1.00 20.39           C  
ANISOU 2962  CB  ALA B 259     3338   1966   2443   -579    873   -173       C  
ATOM   2963  N   ALA B 260      24.549 -16.050  52.582  1.00 14.63           N  
ANISOU 2963  N   ALA B 260     2415   1391   1753   -433    686   -200       N  
ATOM   2964  CA  ALA B 260      25.242 -14.767  52.684  1.00 14.45           C  
ANISOU 2964  CA  ALA B 260     2339   1433   1719   -358    625   -191       C  
ATOM   2965  C   ALA B 260      24.383 -13.632  52.128  1.00 15.00           C  
ANISOU 2965  C   ALA B 260     2277   1569   1852   -376    598   -242       C  
ATOM   2966  O   ALA B 260      24.348 -12.535  52.690  1.00 14.84           O  
ANISOU 2966  O   ALA B 260     2210   1596   1835   -350    591   -248       O  
ATOM   2967  CB  ALA B 260      26.586 -14.814  51.960  1.00 13.70           C  
ANISOU 2967  CB  ALA B 260     2270   1332   1604   -279    555   -164       C  
ATOM   2968  N   MET B 261      23.697 -13.894  51.018  1.00 11.27           N  
ANISOU 2968  N   MET B 261     1751   1101   1431   -418    579   -280       N  
ATOM   2969  CA  MET B 261      22.829 -12.879  50.418  1.00 13.82           C  
ANISOU 2969  CA  MET B 261     1949   1485   1817   -429    542   -325       C  
ATOM   2970  C   MET B 261      21.618 -12.599  51.303  1.00 14.90           C  
ANISOU 2970  C   MET B 261     2026   1641   1993   -483    610   -361       C  
ATOM   2971  O   MET B 261      21.155 -11.460  51.404  1.00 14.11           O  
ANISOU 2971  O   MET B 261     1835   1592   1936   -462    592   -385       O  
ATOM   2972  CB  MET B 261      22.378 -13.306  49.020  1.00 17.12           C  
ANISOU 2972  CB  MET B 261     2328   1907   2270   -462    496   -359       C  
ATOM   2973  CG  MET B 261      21.937 -12.155  48.128  1.00 19.19           C  
ANISOU 2973  CG  MET B 261     2481   2233   2578   -437    419   -384       C  
ATOM   2974  SD  MET B 261      23.315 -11.059  47.698  1.00 25.79           S  
ANISOU 2974  SD  MET B 261     3332   3091   3376   -338    347   -338       S  
ATOM   2975  CE  MET B 261      22.560  -9.993  46.462  1.00 29.78           C  
ANISOU 2975  CE  MET B 261     3729   3653   3933   -326    259   -363       C  
ATOM   2976  N   LEU B 262      21.107 -13.648  51.936  1.00 15.60           N  
ANISOU 2976  N   LEU B 262     2169   1686   2072   -555    694   -365       N  
ATOM   2977  CA  LEU B 262      20.015 -13.505  52.891  1.00 14.63           C  
ANISOU 2977  CA  LEU B 262     2003   1578   1980   -616    781   -399       C  
ATOM   2978  C   LEU B 262      20.446 -12.631  54.062  1.00 16.66           C  
ANISOU 2978  C   LEU B 262     2281   1856   2193   -567    806   -377       C  
ATOM   2979  O   LEU B 262      19.734 -11.700  54.449  1.00 15.07           O  
ANISOU 2979  O   LEU B 262     1990   1700   2036   -570    828   -417       O  
ATOM   2980  CB  LEU B 262      19.550 -14.875  53.391  1.00 15.52           C  
ANISOU 2980  CB  LEU B 262     2195   1626   2075   -704    876   -397       C  
ATOM   2981  CG  LEU B 262      18.467 -14.860  54.472  1.00 20.28           C  
ANISOU 2981  CG  LEU B 262     2772   2247   2689   -744    952   -429       C  
ATOM   2982  CD1 LEU B 262      17.228 -14.097  53.992  1.00 20.06           C  
ANISOU 2982  CD1 LEU B 262     2578   2284   2758   -763    935   -502       C  
ATOM   2983  CD2 LEU B 262      18.109 -16.282  54.893  1.00 23.03           C  
ANISOU 2983  CD2 LEU B 262     3213   2532   3005   -800   1014   -420       C  
ATOM   2984  N   LEU B 263      21.619 -12.928  54.622  1.00 13.14           N  
ANISOU 2984  N   LEU B 263     1954   1379   1662   -521    799   -318       N  
ATOM   2985  CA  LEU B 263      22.141 -12.156  55.754  1.00 16.07           C  
ANISOU 2985  CA  LEU B 263     2358   1772   1977   -477    812   -298       C  
ATOM   2986  C   LEU B 263      22.420 -10.709  55.386  1.00 13.98           C  
ANISOU 2986  C   LEU B 263     2002   1563   1748   -411    740   -319       C  
ATOM   2987  O   LEU B 263      22.090  -9.793  56.134  1.00 14.83           O  
ANISOU 2987  O   LEU B 263     2070   1703   1862   -405    770   -347       O  
ATOM   2988  CB  LEU B 263      23.420 -12.789  56.303  1.00 16.11           C  
ANISOU 2988  CB  LEU B 263     2499   1736   1885   -431    796   -230       C  
ATOM   2989  CG  LEU B 263      23.190 -14.014  57.194  1.00 19.62           C  
ANISOU 2989  CG  LEU B 263     3065   2120   2270   -487    884   -196       C  
ATOM   2990  CD1 LEU B 263      24.517 -14.691  57.496  1.00 19.77           C  
ANISOU 2990  CD1 LEU B 263     3212   2095   2207   -423    843   -124       C  
ATOM   2991  CD2 LEU B 263      22.488 -13.613  58.493  1.00 19.75           C  
ANISOU 2991  CD2 LEU B 263     3080   2158   2267   -516    939   -216       C  
ATOM   2992  N   ALA B 264      23.054 -10.509  54.239  1.00 11.33           N  
ANISOU 2992  N   ALA B 264     1640   1232   1432   -364    652   -307       N  
ATOM   2993  CA  ALA B 264      23.366  -9.159  53.781  1.00 12.93           C  
ANISOU 2993  CA  ALA B 264     1768   1476   1669   -306    584   -319       C  
ATOM   2994  C   ALA B 264      22.077  -8.371  53.535  1.00 11.82           C  
ANISOU 2994  C   ALA B 264     1506   1369   1617   -328    595   -375       C  
ATOM   2995  O   ALA B 264      22.014  -7.167  53.799  1.00 13.19           O  
ANISOU 2995  O   ALA B 264     1625   1569   1819   -292    582   -395       O  
ATOM   2996  CB  ALA B 264      24.225  -9.214  52.519  1.00 10.63           C  
ANISOU 2996  CB  ALA B 264     1480   1181   1379   -264    500   -293       C  
ATOM   2997  N   SER B 265      21.045  -9.056  53.044  1.00 12.01           N  
ANISOU 2997  N   SER B 265     1485   1390   1690   -388    618   -404       N  
ATOM   2998  CA  SER B 265      19.747  -8.417  52.829  1.00 13.33           C  
ANISOU 2998  CA  SER B 265     1524   1593   1950   -409    627   -462       C  
ATOM   2999  C   SER B 265      19.107  -8.000  54.146  1.00 15.83           C  
ANISOU 2999  C   SER B 265     1818   1920   2277   -432    722   -497       C  
ATOM   3000  O   SER B 265      18.587  -6.893  54.265  1.00 15.49           O  
ANISOU 3000  O   SER B 265     1683   1906   2295   -401    718   -535       O  
ATOM   3001  CB  SER B 265      18.800  -9.349  52.074  1.00 15.15           C  
ANISOU 3001  CB  SER B 265     1707   1821   2228   -478    632   -493       C  
ATOM   3002  OG  SER B 265      19.303  -9.611  50.779  1.00 17.47           O  
ANISOU 3002  OG  SER B 265     2014   2111   2512   -456    541   -471       O  
ATOM   3003  N   LYS B 266      19.137  -8.890  55.133  1.00 15.26           N  
ANISOU 3003  N   LYS B 266     1835   1821   2142   -485    812   -485       N  
ATOM   3004  CA  LYS B 266      18.580  -8.560  56.442  1.00 15.94           C  
ANISOU 3004  CA  LYS B 266     1927   1914   2217   -505    891   -511       C  
ATOM   3005  C   LYS B 266      19.292  -7.347  57.052  1.00 14.54           C  
ANISOU 3005  C   LYS B 266     1762   1754   2008   -436    866   -506       C  
ATOM   3006  O   LYS B 266      18.665  -6.484  57.684  1.00 15.65           O  
ANISOU 3006  O   LYS B 266     1851   1911   2185   -426    886   -545       O  
ATOM   3007  CB  LYS B 266      18.661  -9.760  57.387  1.00 15.94           C  
ANISOU 3007  CB  LYS B 266     2053   1870   2134   -558    957   -478       C  
ATOM   3008  CG  LYS B 266      17.632 -10.854  57.090  1.00 17.41           C  
ANISOU 3008  CG  LYS B 266     2221   2034   2361   -635    999   -503       C  
ATOM   3009  CD  LYS B 266      17.824 -12.054  58.008  1.00 21.72           C  
ANISOU 3009  CD  LYS B 266     2907   2524   2822   -679   1061   -462       C  
ATOM   3010  CE  LYS B 266      16.742 -13.099  57.799  1.00 24.41           C  
ANISOU 3010  CE  LYS B 266     3229   2841   3204   -757   1110   -495       C  
ATOM   3011  NZ  LYS B 266      16.891 -14.233  58.746  1.00 23.49           N  
ANISOU 3011  NZ  LYS B 266     3254   2664   3006   -796   1175   -455       N  
ATOM   3012  N   PHE B 267      20.602  -7.282  56.863  1.00 11.39           N  
ANISOU 3012  N   PHE B 267     1436   1348   1545   -388    817   -461       N  
ATOM   3013  CA  PHE B 267      21.399  -6.191  57.420  1.00 14.83           C  
ANISOU 3013  CA  PHE B 267     1890   1798   1946   -329    787   -458       C  
ATOM   3014  C   PHE B 267      21.113  -4.869  56.699  1.00 15.49           C  
ANISOU 3014  C   PHE B 267     1861   1902   2124   -279    732   -494       C  
ATOM   3015  O   PHE B 267      20.899  -3.834  57.330  1.00 15.97           O  
ANISOU 3015  O   PHE B 267     1890   1971   2205   -257    741   -524       O  
ATOM   3016  CB  PHE B 267      22.898  -6.528  57.336  1.00 14.93           C  
ANISOU 3016  CB  PHE B 267     2003   1795   1874   -287    721   -396       C  
ATOM   3017  CG  PHE B 267      23.795  -5.469  57.932  1.00 14.03           C  
ANISOU 3017  CG  PHE B 267     1909   1698   1722   -236    688   -399       C  
ATOM   3018  CD1 PHE B 267      24.089  -5.471  59.288  1.00 14.76           C  
ANISOU 3018  CD1 PHE B 267     2077   1797   1734   -244    720   -392       C  
ATOM   3019  CD2 PHE B 267      24.328  -4.467  57.141  1.00 11.82           C  
ANISOU 3019  CD2 PHE B 267     1574   1427   1490   -183    610   -401       C  
ATOM   3020  CE1 PHE B 267      24.909  -4.492  59.836  1.00 14.85           C  
ANISOU 3020  CE1 PHE B 267     2102   1828   1713   -203    680   -401       C  
ATOM   3021  CE2 PHE B 267      25.142  -3.485  57.683  1.00 15.28           C  
ANISOU 3021  CE2 PHE B 267     2028   1877   1901   -147    584   -411       C  
ATOM   3022  CZ  PHE B 267      25.435  -3.503  59.030  1.00 17.23           C  
ANISOU 3022  CZ  PHE B 267     2346   2135   2067   -159    621   -418       C  
ATOM   3023  N   GLU B 268      21.089  -4.920  55.371  1.00 14.33           N  
ANISOU 3023  N   GLU B 268     1662   1752   2029   -261    654   -478       N  
ATOM   3024  CA  GLU B 268      21.183  -3.705  54.558  1.00 12.05           C  
ANISOU 3024  CA  GLU B 268     1300   1472   1805   -200    577   -484       C  
ATOM   3025  C   GLU B 268      19.870  -3.206  53.965  1.00 15.47           C  
ANISOU 3025  C   GLU B 268     1607   1921   2350   -199    569   -529       C  
ATOM   3026  O   GLU B 268      19.691  -1.997  53.774  1.00 13.86           O  
ANISOU 3026  O   GLU B 268     1340   1718   2208   -147    537   -548       O  
ATOM   3027  CB  GLU B 268      22.201  -3.926  53.430  1.00 10.47           C  
ANISOU 3027  CB  GLU B 268     1140   1261   1576   -170    486   -429       C  
ATOM   3028  CG  GLU B 268      22.592  -2.664  52.666  1.00 14.74           C  
ANISOU 3028  CG  GLU B 268     1640   1802   2160   -110    411   -420       C  
ATOM   3029  CD  GLU B 268      23.260  -1.628  53.559  1.00 20.15           C  
ANISOU 3029  CD  GLU B 268     2349   2480   2826    -78    426   -431       C  
ATOM   3030  OE1 GLU B 268      23.920  -2.024  54.547  1.00 19.18           O  
ANISOU 3030  OE1 GLU B 268     2300   2359   2629    -93    464   -426       O  
ATOM   3031  OE2 GLU B 268      23.128  -0.418  53.275  1.00 18.44           O  
ANISOU 3031  OE2 GLU B 268     2082   2255   2670    -39    396   -445       O  
ATOM   3032  N   GLU B 269      18.958  -4.128  53.662  1.00 13.62           N  
ANISOU 3032  N   GLU B 269     1332   1697   2147   -253    595   -548       N  
ATOM   3033  CA  GLU B 269      17.745  -3.781  52.911  1.00 16.64           C  
ANISOU 3033  CA  GLU B 269     1581   2102   2637   -250    564   -589       C  
ATOM   3034  C   GLU B 269      16.588  -3.306  53.781  1.00 19.35           C  
ANISOU 3034  C   GLU B 269     1851   2457   3044   -261    632   -649       C  
ATOM   3035  O   GLU B 269      16.386  -3.795  54.889  1.00 18.73           O  
ANISOU 3035  O   GLU B 269     1829   2370   2918   -309    716   -660       O  
ATOM   3036  CB  GLU B 269      17.272  -4.971  52.058  1.00 14.77           C  
ANISOU 3036  CB  GLU B 269     1331   1875   2408   -307    541   -587       C  
ATOM   3037  CG  GLU B 269      18.271  -5.405  50.978  1.00 16.41           C  
ANISOU 3037  CG  GLU B 269     1613   2067   2555   -289    453   -529       C  
ATOM   3038  CD  GLU B 269      18.342  -4.433  49.811  1.00 17.88           C  
ANISOU 3038  CD  GLU B 269     1746   2267   2781   -223    342   -512       C  
ATOM   3039  OE1 GLU B 269      17.391  -3.640  49.624  1.00 19.75           O  
ANISOU 3039  OE1 GLU B 269     1872   2525   3107   -196    318   -547       O  
ATOM   3040  OE2 GLU B 269      19.358  -4.462  49.081  1.00 17.41           O  
ANISOU 3040  OE2 GLU B 269     1757   2194   2663   -196    281   -463       O  
ATOM   3041  N   ILE B 270      15.819  -2.354  53.256  1.00 15.34           N  
ANISOU 3041  N   ILE B 270     1241   1960   2628   -210    575   -673       N  
ATOM   3042  CA  ILE B 270      14.553  -1.975  53.876  1.00 15.60           C  
ANISOU 3042  CA  ILE B 270     1206   2000   2723   -216    616   -724       C  
ATOM   3043  C   ILE B 270      13.572  -3.148  53.786  1.00 19.20           C  
ANISOU 3043  C   ILE B 270     1624   2474   3195   -291    652   -752       C  
ATOM   3044  O   ILE B 270      12.882  -3.468  54.755  1.00 18.14           O  
ANISOU 3044  O   ILE B 270     1495   2339   3058   -338    738   -787       O  
ATOM   3045  CB  ILE B 270      13.944  -0.734  53.188  1.00 16.54           C  
ANISOU 3045  CB  ILE B 270     1225   2122   2939   -137    536   -736       C  
ATOM   3046  CG1 ILE B 270      14.898   0.461  53.295  1.00 17.28           C  
ANISOU 3046  CG1 ILE B 270     1364   2184   3017    -68    505   -707       C  
ATOM   3047  CG2 ILE B 270      12.582  -0.397  53.790  1.00 20.80           C  
ANISOU 3047  CG2 ILE B 270     1684   2670   3548   -142    582   -793       C  
ATOM   3048  CD1 ILE B 270      14.459   1.669  52.480  1.00 17.79           C  
ANISOU 3048  CD1 ILE B 270     1354   2238   3168     15    417   -702       C  
ATOM   3049  N   TYR B 271      13.522  -3.799  52.624  1.00 17.77           N  
ANISOU 3049  N   TYR B 271     1412   2311   3030   -307    587   -739       N  
ATOM   3050  CA  TYR B 271      12.655  -4.966  52.448  1.00 20.65           C  
ANISOU 3050  CA  TYR B 271     1749   2690   3407   -384    614   -767       C  
ATOM   3051  C   TYR B 271      13.439  -6.192  51.983  1.00 22.80           C  
ANISOU 3051  C   TYR B 271     2106   2948   3608   -442    613   -732       C  
ATOM   3052  O   TYR B 271      13.521  -6.456  50.785  1.00 23.91           O  
ANISOU 3052  O   TYR B 271     2218   3104   3763   -441    527   -721       O  
ATOM   3053  CB  TYR B 271      11.547  -4.668  51.437  1.00 28.67           C  
ANISOU 3053  CB  TYR B 271     2635   3742   4516   -360    529   -796       C  
ATOM   3054  CG  TYR B 271      10.697  -3.465  51.774  1.00 28.02           C  
ANISOU 3054  CG  TYR B 271     2463   3669   4515   -297    523   -830       C  
ATOM   3055  CD1 TYR B 271       9.750  -3.519  52.789  1.00 30.55           C  
ANISOU 3055  CD1 TYR B 271     2750   3991   4866   -332    617   -882       C  
ATOM   3056  CD2 TYR B 271      10.830  -2.278  51.064  1.00 29.69           C  
ANISOU 3056  CD2 TYR B 271     2627   3881   4771   -205    426   -808       C  
ATOM   3057  CE1 TYR B 271       8.968  -2.421  53.096  1.00 33.94           C  
ANISOU 3057  CE1 TYR B 271     3096   4425   5373   -275    615   -916       C  
ATOM   3058  CE2 TYR B 271      10.054  -1.178  51.363  1.00 33.19           C  
ANISOU 3058  CE2 TYR B 271     2996   4324   5291   -145    421   -836       C  
ATOM   3059  CZ  TYR B 271       9.126  -1.255  52.377  1.00 36.28           C  
ANISOU 3059  CZ  TYR B 271     3349   4719   5715   -180    516   -893       C  
ATOM   3060  OH  TYR B 271       8.356  -0.156  52.673  1.00 41.65           O  
ANISOU 3060  OH  TYR B 271     3952   5396   6475   -121    515   -925       O  
ATOM   3061  N   PRO B 272      14.013  -6.951  52.930  1.00 21.44           N  
ANISOU 3061  N   PRO B 272     2049   2743   3354   -491    704   -712       N  
ATOM   3062  CA  PRO B 272      14.765  -8.156  52.551  1.00 22.70           C  
ANISOU 3062  CA  PRO B 272     2303   2876   3445   -543    709   -675       C  
ATOM   3063  C   PRO B 272      13.808  -9.183  51.950  1.00 19.62           C  
ANISOU 3063  C   PRO B 272     1874   2493   3089   -610    703   -707       C  
ATOM   3064  O   PRO B 272      12.678  -9.301  52.434  1.00 20.22           O  
ANISOU 3064  O   PRO B 272     1893   2581   3209   -641    752   -752       O  
ATOM   3065  CB  PRO B 272      15.296  -8.681  53.891  1.00 28.42           C  
ANISOU 3065  CB  PRO B 272     3156   3562   4082   -574    810   -649       C  
ATOM   3066  CG  PRO B 272      15.095  -7.561  54.884  1.00 33.00           C  
ANISOU 3066  CG  PRO B 272     3713   4155   4673   -530    842   -669       C  
ATOM   3067  CD  PRO B 272      13.925  -6.782  54.392  1.00 26.91           C  
ANISOU 3067  CD  PRO B 272     2796   3418   4009   -503    801   -722       C  
ATOM   3068  N   PRO B 273      14.233  -9.899  50.900  1.00 20.62           N  
ANISOU 3068  N   PRO B 273     2028   2610   3195   -634    645   -689       N  
ATOM   3069  CA  PRO B 273      13.374 -10.969  50.372  1.00 23.55           C  
ANISOU 3069  CA  PRO B 273     2377   2983   3588   -703    644   -721       C  
ATOM   3070  C   PRO B 273      13.190 -12.084  51.398  1.00 23.89           C  
ANISOU 3070  C   PRO B 273     2511   2979   3585   -773    761   -720       C  
ATOM   3071  O   PRO B 273      14.078 -12.317  52.220  1.00 22.70           O  
ANISOU 3071  O   PRO B 273     2479   2786   3361   -771    819   -676       O  
ATOM   3072  CB  PRO B 273      14.157 -11.490  49.155  1.00 21.69           C  
ANISOU 3072  CB  PRO B 273     2191   2735   3317   -709    562   -695       C  
ATOM   3073  CG  PRO B 273      15.092 -10.367  48.793  1.00 20.54           C  
ANISOU 3073  CG  PRO B 273     2037   2602   3163   -633    493   -663       C  
ATOM   3074  CD  PRO B 273      15.460  -9.728  50.108  1.00 17.93           C  
ANISOU 3074  CD  PRO B 273     1738   2259   2816   -601    574   -645       C  
ATOM   3075  N   GLU B 274      12.046 -12.760  51.350  1.00 25.32           N  
ANISOU 3075  N   GLU B 274     2641   3169   3809   -834    791   -767       N  
ATOM   3076  CA  GLU B 274      11.783 -13.878  52.246  1.00 28.13           C  
ANISOU 3076  CA  GLU B 274     3084   3479   4127   -907    901   -769       C  
ATOM   3077  C   GLU B 274      12.690 -15.051  51.906  1.00 26.83           C  
ANISOU 3077  C   GLU B 274     3053   3253   3888   -937    903   -724       C  
ATOM   3078  O   GLU B 274      13.184 -15.157  50.786  1.00 25.21           O  
ANISOU 3078  O   GLU B 274     2848   3051   3680   -921    819   -713       O  
ATOM   3079  CB  GLU B 274      10.324 -14.319  52.134  1.00 32.54           C  
ANISOU 3079  CB  GLU B 274     3544   4063   4758   -970    927   -835       C  
ATOM   3080  CG  GLU B 274       9.320 -13.300  52.638  1.00 48.51           C  
ANISOU 3080  CG  GLU B 274     5442   6135   6856   -945    944   -884       C  
ATOM   3081  CD  GLU B 274       7.892 -13.797  52.512  1.00 65.28           C  
ANISOU 3081  CD  GLU B 274     7465   8285   9055  -1011    973   -952       C  
ATOM   3082  OE1 GLU B 274       7.678 -14.816  51.817  1.00 67.53           O  
ANISOU 3082  OE1 GLU B 274     7760   8559   9340  -1070    956   -963       O  
ATOM   3083  OE2 GLU B 274       6.987 -13.174  53.109  1.00 73.68           O  
ANISOU 3083  OE2 GLU B 274     8438   9378  10178  -1005   1013   -997       O  
ATOM   3084  N   VAL B 275      12.890 -15.935  52.877  1.00 27.81           N  
ANISOU 3084  N   VAL B 275     3297   3317   3952   -978    998   -698       N  
ATOM   3085  CA  VAL B 275      13.706 -17.128  52.684  1.00 29.49           C  
ANISOU 3085  CA  VAL B 275     3647   3460   4098   -999   1009   -653       C  
ATOM   3086  C   VAL B 275      13.183 -17.980  51.529  1.00 28.86           C  
ANISOU 3086  C   VAL B 275     3530   3379   4056  -1050    969   -690       C  
ATOM   3087  O   VAL B 275      13.963 -18.570  50.784  1.00 26.11           O  
ANISOU 3087  O   VAL B 275     3254   2995   3673  -1041    926   -663       O  
ATOM   3088  CB  VAL B 275      13.765 -17.972  53.973  1.00 35.69           C  
ANISOU 3088  CB  VAL B 275     4559   4180   4820  -1036   1118   -624       C  
ATOM   3089  CG1 VAL B 275      14.692 -19.168  53.794  1.00 33.82           C  
ANISOU 3089  CG1 VAL B 275     4471   3865   4516  -1040   1122   -570       C  
ATOM   3090  CG2 VAL B 275      14.233 -17.108  55.138  1.00 40.84           C  
ANISOU 3090  CG2 VAL B 275     5250   4840   5428   -989   1150   -592       C  
ATOM   3091  N   ALA B 276      11.862 -18.030  51.378  1.00 25.92           N  
ANISOU 3091  N   ALA B 276     3045   3047   3756  -1102    982   -755       N  
ATOM   3092  CA  ALA B 276      11.239 -18.782  50.288  1.00 27.58           C  
ANISOU 3092  CA  ALA B 276     3207   3266   4007  -1155    939   -798       C  
ATOM   3093  C   ALA B 276      11.672 -18.276  48.913  1.00 24.45           C  
ANISOU 3093  C   ALA B 276     2759   2909   3621  -1110    809   -799       C  
ATOM   3094  O   ALA B 276      11.785 -19.055  47.960  1.00 21.94           O  
ANISOU 3094  O   ALA B 276     2470   2573   3292  -1140    765   -810       O  
ATOM   3095  CB  ALA B 276       9.720 -18.745  50.413  1.00 31.61           C  
ANISOU 3095  CB  ALA B 276     3586   3823   4599  -1212    968   -871       C  
ATOM   3096  N   GLU B 277      11.912 -16.972  48.809  1.00 22.25           N  
ANISOU 3096  N   GLU B 277     2412   2682   3361  -1038    748   -789       N  
ATOM   3097  CA  GLU B 277      12.364 -16.387  47.548  1.00 24.46           C  
ANISOU 3097  CA  GLU B 277     2652   2999   3643   -991    623   -785       C  
ATOM   3098  C   GLU B 277      13.797 -16.798  47.232  1.00 23.46           C  
ANISOU 3098  C   GLU B 277     2663   2816   3436   -964    608   -731       C  
ATOM   3099  O   GLU B 277      14.147 -17.050  46.075  1.00 22.48           O  
ANISOU 3099  O   GLU B 277     2554   2694   3293   -962    528   -737       O  
ATOM   3100  CB  GLU B 277      12.246 -14.858  47.582  1.00 26.03           C  
ANISOU 3100  CB  GLU B 277     2745   3260   3885   -917    566   -786       C  
ATOM   3101  CG  GLU B 277      10.810 -14.340  47.599  1.00 30.10           C  
ANISOU 3101  CG  GLU B 277     3108   3837   4490   -924    552   -843       C  
ATOM   3102  CD  GLU B 277      10.086 -14.555  46.271  1.00 44.46           C  
ANISOU 3102  CD  GLU B 277     4843   5703   6348   -946    447   -883       C  
ATOM   3103  OE1 GLU B 277      10.747 -14.916  45.269  1.00 47.54           O  
ANISOU 3103  OE1 GLU B 277     5289   6083   6691   -947    375   -867       O  
ATOM   3104  OE2 GLU B 277       8.851 -14.358  46.226  1.00 50.41           O  
ANISOU 3104  OE2 GLU B 277     5474   6504   7176   -963    435   -933       O  
ATOM   3105  N   PHE B 278      14.636 -16.856  48.259  1.00 20.97           N  
ANISOU 3105  N   PHE B 278     2449   2449   3068   -941    681   -681       N  
ATOM   3106  CA  PHE B 278      16.015 -17.287  48.050  1.00 22.07           C  
ANISOU 3106  CA  PHE B 278     2721   2529   3135   -909    671   -628       C  
ATOM   3107  C   PHE B 278      16.074 -18.769  47.669  1.00 26.70           C  
ANISOU 3107  C   PHE B 278     3397   3054   3693   -959    697   -631       C  
ATOM   3108  O   PHE B 278      16.859 -19.158  46.806  1.00 26.97           O  
ANISOU 3108  O   PHE B 278     3493   3061   3692   -938    648   -618       O  
ATOM   3109  CB  PHE B 278      16.870 -16.996  49.283  1.00 20.52           C  
ANISOU 3109  CB  PHE B 278     2612   2296   2889   -869    735   -570       C  
ATOM   3110  CG  PHE B 278      17.269 -15.559  49.406  1.00 18.58           C  
ANISOU 3110  CG  PHE B 278     2307   2098   2657   -807    693   -559       C  
ATOM   3111  CD1 PHE B 278      18.261 -15.033  48.593  1.00 20.86           C  
ANISOU 3111  CD1 PHE B 278     2612   2389   2924   -753    612   -537       C  
ATOM   3112  CD2 PHE B 278      16.649 -14.728  50.327  1.00 21.27           C  
ANISOU 3112  CD2 PHE B 278     2576   2477   3030   -799    735   -573       C  
ATOM   3113  CE1 PHE B 278      18.633 -13.702  48.700  1.00 19.95           C  
ANISOU 3113  CE1 PHE B 278     2448   2324   2808   -667    560   -514       C  
ATOM   3114  CE2 PHE B 278      17.016 -13.402  50.437  1.00 19.80           C  
ANISOU 3114  CE2 PHE B 278     2333   2330   2860   -739    699   -565       C  
ATOM   3115  CZ  PHE B 278      18.009 -12.887  49.623  1.00 20.49           C  
ANISOU 3115  CZ  PHE B 278     2444   2426   2916   -663    604   -530       C  
ATOM   3116  N   VAL B 279      15.237 -19.586  48.306  1.00 21.95           N  
ANISOU 3116  N   VAL B 279     2804   2428   3108  -1023    778   -651       N  
ATOM   3117  CA  VAL B 279      15.123 -21.004  47.942  1.00 19.17           C  
ANISOU 3117  CA  VAL B 279     2525   2017   2742  -1079    808   -663       C  
ATOM   3118  C   VAL B 279      14.718 -21.134  46.482  1.00 22.65           C  
ANISOU 3118  C   VAL B 279     2897   2496   3214  -1103    718   -716       C  
ATOM   3119  O   VAL B 279      15.346 -21.863  45.702  1.00 23.88           O  
ANISOU 3119  O   VAL B 279     3129   2609   3335  -1101    690   -711       O  
ATOM   3120  CB  VAL B 279      14.083 -21.735  48.813  1.00 23.19           C  
ANISOU 3120  CB  VAL B 279     3032   2504   3276  -1155    907   -689       C  
ATOM   3121  CG1 VAL B 279      13.764 -23.117  48.234  1.00 28.35           C  
ANISOU 3121  CG1 VAL B 279     3734   3105   3934  -1223    926   -717       C  
ATOM   3122  CG2 VAL B 279      14.569 -21.844  50.249  1.00 28.85           C  
ANISOU 3122  CG2 VAL B 279     3852   3168   3940  -1135    997   -632       C  
ATOM   3123  N   TYR B 280      13.667 -20.405  46.120  1.00 22.03           N  
ANISOU 3123  N   TYR B 280     2675   2498   3199  -1121    669   -767       N  
ATOM   3124  CA  TYR B 280      13.166 -20.373  44.751  1.00 26.84           C  
ANISOU 3124  CA  TYR B 280     3207   3157   3835  -1141    567   -817       C  
ATOM   3125  C   TYR B 280      14.246 -20.022  43.731  1.00 26.97           C  
ANISOU 3125  C   TYR B 280     3271   3177   3800  -1082    476   -794       C  
ATOM   3126  O   TYR B 280      14.354 -20.665  42.683  1.00 24.26           O  
ANISOU 3126  O   TYR B 280     2960   2823   3434  -1104    428   -819       O  
ATOM   3127  CB  TYR B 280      12.015 -19.367  44.644  1.00 28.28           C  
ANISOU 3127  CB  TYR B 280     3223   3431   4091  -1140    516   -860       C  
ATOM   3128  CG  TYR B 280      11.583 -19.070  43.231  1.00 28.71           C  
ANISOU 3128  CG  TYR B 280     3196   3549   4164  -1140    386   -900       C  
ATOM   3129  CD1 TYR B 280      10.775 -19.961  42.533  1.00 34.29           C  
ANISOU 3129  CD1 TYR B 280     3875   4260   4893  -1214    365   -955       C  
ATOM   3130  CD2 TYR B 280      11.971 -17.898  42.595  1.00 29.69           C  
ANISOU 3130  CD2 TYR B 280     3274   3728   4280  -1067    282   -882       C  
ATOM   3131  CE1 TYR B 280      10.372 -19.698  41.239  1.00 36.29           C  
ANISOU 3131  CE1 TYR B 280     4060   4575   5153  -1214    239   -991       C  
ATOM   3132  CE2 TYR B 280      11.571 -17.625  41.297  1.00 33.51           C  
ANISOU 3132  CE2 TYR B 280     3694   4271   4767  -1064    157   -913       C  
ATOM   3133  CZ  TYR B 280      10.771 -18.530  40.626  1.00 39.10           C  
ANISOU 3133  CZ  TYR B 280     4379   4986   5491  -1138    133   -967       C  
ATOM   3134  OH  TYR B 280      10.365 -18.271  39.338  1.00 42.06           O  
ANISOU 3134  OH  TYR B 280     4698   5421   5860  -1136      2   -996       O  
ATOM   3135  N   ILE B 281      15.049 -19.012  44.041  1.00 22.26           N  
ANISOU 3135  N   ILE B 281     2684   2594   3182  -1009    457   -749       N  
ATOM   3136  CA  ILE B 281      16.000 -18.492  43.063  1.00 20.34           C  
ANISOU 3136  CA  ILE B 281     2471   2364   2892   -953    369   -732       C  
ATOM   3137  C   ILE B 281      17.211 -19.418  42.853  1.00 20.86           C  
ANISOU 3137  C   ILE B 281     2686   2351   2890   -936    400   -700       C  
ATOM   3138  O   ILE B 281      17.986 -19.233  41.917  1.00 22.05           O  
ANISOU 3138  O   ILE B 281     2876   2507   2996   -898    337   -696       O  
ATOM   3139  CB  ILE B 281      16.429 -17.042  43.397  1.00 19.81           C  
ANISOU 3139  CB  ILE B 281     2357   2339   2832   -883    335   -702       C  
ATOM   3140  CG1 ILE B 281      16.814 -16.283  42.121  1.00 24.11           C  
ANISOU 3140  CG1 ILE B 281     2876   2933   3350   -841    216   -708       C  
ATOM   3141  CG2 ILE B 281      17.530 -17.022  44.445  1.00 20.52           C  
ANISOU 3141  CG2 ILE B 281     2547   2368   2882   -842    410   -643       C  
ATOM   3142  CD1 ILE B 281      15.635 -16.010  41.201  1.00 24.57           C  
ANISOU 3142  CD1 ILE B 281     2818   3066   3450   -867    123   -758       C  
ATOM   3143  N   THR B 282      17.352 -20.427  43.707  1.00 20.06           N  
ANISOU 3143  N   THR B 282     2667   2176   2778   -960    497   -679       N  
ATOM   3144  CA  THR B 282      18.346 -21.477  43.481  1.00 21.28           C  
ANISOU 3144  CA  THR B 282     2954   2252   2882   -943    526   -654       C  
ATOM   3145  C   THR B 282      17.772 -22.591  42.605  1.00 25.07           C  
ANISOU 3145  C   THR B 282     3443   2712   3369  -1009    518   -707       C  
ATOM   3146  O   THR B 282      18.412 -23.630  42.409  1.00 23.09           O  
ANISOU 3146  O   THR B 282     3295   2390   3087  -1005    552   -697       O  
ATOM   3147  CB  THR B 282      18.839 -22.105  44.808  1.00 19.19           C  
ANISOU 3147  CB  THR B 282     2787   1909   2596   -930    626   -599       C  
ATOM   3148  OG1 THR B 282      17.795 -22.889  45.395  1.00 21.10           O  
ANISOU 3148  OG1 THR B 282     3018   2129   2870  -1007    696   -623       O  
ATOM   3149  CG2 THR B 282      19.285 -21.027  45.792  1.00 19.88           C  
ANISOU 3149  CG2 THR B 282     2864   2016   2675   -875    638   -551       C  
ATOM   3150  N   ASP B 283      16.567 -22.360  42.083  1.00 24.86           N  
ANISOU 3150  N   ASP B 283     3306   2751   3389  -1066    472   -766       N  
ATOM   3151  CA  ASP B 283      15.809 -23.371  41.333  1.00 27.65           C  
ANISOU 3151  CA  ASP B 283     3652   3095   3759  -1142    464   -826       C  
ATOM   3152  C   ASP B 283      15.517 -24.566  42.235  1.00 30.11           C  
ANISOU 3152  C   ASP B 283     4027   3327   4087  -1196    576   -821       C  
ATOM   3153  O   ASP B 283      15.582 -25.721  41.809  1.00 29.69           O  
ANISOU 3153  O   ASP B 283     4044   3215   4023  -1235    601   -844       O  
ATOM   3154  CB  ASP B 283      16.557 -23.790  40.060  1.00 26.31           C  
ANISOU 3154  CB  ASP B 283     3550   2909   3537  -1122    407   -842       C  
ATOM   3155  CG  ASP B 283      15.643 -24.401  39.012  1.00 37.72           C  
ANISOU 3155  CG  ASP B 283     4953   4379   4999  -1197    357   -917       C  
ATOM   3156  OD1 ASP B 283      14.404 -24.363  39.187  1.00 39.00           O  
ANISOU 3156  OD1 ASP B 283     5017   4582   5219  -1259    351   -957       O  
ATOM   3157  OD2 ASP B 283      16.172 -24.906  37.999  1.00 40.40           O  
ANISOU 3157  OD2 ASP B 283     5356   4699   5293  -1191    323   -939       O  
ATOM   3158  N   ASP B 284      15.190 -24.260  43.490  1.00 27.26           N  
ANISOU 3158  N   ASP B 284     3646   2963   3748  -1199    645   -793       N  
ATOM   3159  CA  ASP B 284      14.886 -25.258  44.517  1.00 28.66           C  
ANISOU 3159  CA  ASP B 284     3889   3069   3932  -1248    758   -780       C  
ATOM   3160  C   ASP B 284      15.975 -26.308  44.733  1.00 26.63           C  
ANISOU 3160  C   ASP B 284     3788   2706   3622  -1219    810   -732       C  
ATOM   3161  O   ASP B 284      15.688 -27.489  44.906  1.00 26.93           O  
ANISOU 3161  O   ASP B 284     3889   2676   3666  -1275    874   -745       O  
ATOM   3162  CB  ASP B 284      13.532 -25.925  44.251  1.00 38.04           C  
ANISOU 3162  CB  ASP B 284     5007   4270   5176  -1351    776   -852       C  
ATOM   3163  CG  ASP B 284      12.376 -24.966  44.432  1.00 48.04           C  
ANISOU 3163  CG  ASP B 284     6118   5630   6503  -1375    750   -891       C  
ATOM   3164  OD1 ASP B 284      12.173 -24.501  45.570  1.00 48.48           O  
ANISOU 3164  OD1 ASP B 284     6157   5693   6570  -1364    814   -866       O  
ATOM   3165  OD2 ASP B 284      11.676 -24.678  43.441  1.00 56.85           O  
ANISOU 3165  OD2 ASP B 284     7131   6813   7655  -1400    665   -948       O  
ATOM   3166  N   THR B 285      17.224 -25.860  44.753  1.00 22.83           N  
ANISOU 3166  N   THR B 285     3369   2212   3094  -1129    782   -677       N  
ATOM   3167  CA  THR B 285      18.352 -26.742  45.011  1.00 26.42           C  
ANISOU 3167  CA  THR B 285     3963   2572   3504  -1081    823   -625       C  
ATOM   3168  C   THR B 285      18.393 -27.160  46.478  1.00 27.30           C  
ANISOU 3168  C   THR B 285     4151   2624   3599  -1081    915   -571       C  
ATOM   3169  O   THR B 285      18.698 -28.313  46.803  1.00 25.63           O  
ANISOU 3169  O   THR B 285     4047   2322   3370  -1087    972   -547       O  
ATOM   3170  CB  THR B 285      19.672 -26.058  44.618  1.00 25.27           C  
ANISOU 3170  CB  THR B 285     3846   2437   3316   -980    763   -585       C  
ATOM   3171  OG1 THR B 285      19.662 -25.799  43.210  1.00 26.87           O  
ANISOU 3171  OG1 THR B 285     3999   2689   3522   -983    683   -636       O  
ATOM   3172  CG2 THR B 285      20.868 -26.933  44.971  1.00 24.61           C  
ANISOU 3172  CG2 THR B 285     3897   2259   3194   -917    801   -529       C  
ATOM   3173  N   TYR B 286      18.068 -26.220  47.364  1.00 26.26           N  
ANISOU 3173  N   TYR B 286     3967   2541   3471  -1073    930   -552       N  
ATOM   3174  CA  TYR B 286      18.080 -26.482  48.797  1.00 22.58           C  
ANISOU 3174  CA  TYR B 286     3574   2028   2978  -1072   1013   -502       C  
ATOM   3175  C   TYR B 286      16.701 -26.224  49.388  1.00 26.33           C  
ANISOU 3175  C   TYR B 286     3962   2547   3494  -1153   1064   -545       C  
ATOM   3176  O   TYR B 286      15.854 -25.607  48.749  1.00 28.81           O  
ANISOU 3176  O   TYR B 286     4146   2939   3862  -1190   1022   -605       O  
ATOM   3177  CB  TYR B 286      19.118 -25.593  49.497  1.00 18.66           C  
ANISOU 3177  CB  TYR B 286     3113   1542   2435   -978    993   -435       C  
ATOM   3178  CG  TYR B 286      20.456 -25.570  48.789  1.00 22.61           C  
ANISOU 3178  CG  TYR B 286     3665   2021   2905   -892    929   -403       C  
ATOM   3179  CD1 TYR B 286      21.361 -26.617  48.933  1.00 20.06           C  
ANISOU 3179  CD1 TYR B 286     3465   1608   2547   -847    950   -359       C  
ATOM   3180  CD2 TYR B 286      20.810 -24.505  47.974  1.00 22.48           C  
ANISOU 3180  CD2 TYR B 286     3570   2072   2898   -852    850   -420       C  
ATOM   3181  CE1 TYR B 286      22.586 -26.599  48.275  1.00 20.09           C  
ANISOU 3181  CE1 TYR B 286     3506   1596   2532   -763    895   -336       C  
ATOM   3182  CE2 TYR B 286      22.026 -24.479  47.311  1.00 23.44           C  
ANISOU 3182  CE2 TYR B 286     3736   2177   2994   -774    798   -397       C  
ATOM   3183  CZ  TYR B 286      22.911 -25.529  47.469  1.00 20.11           C  
ANISOU 3183  CZ  TYR B 286     3428   1670   2542   -729    823   -357       C  
ATOM   3184  OH  TYR B 286      24.124 -25.494  46.811  1.00 22.40           O  
ANISOU 3184  OH  TYR B 286     3750   1948   2813   -647    775   -340       O  
ATOM   3185  N   THR B 287      16.484 -26.692  50.611  1.00 23.38           N  
ANISOU 3185  N   THR B 287     3661   2126   3097  -1176   1152   -514       N  
ATOM   3186  CA  THR B 287      15.220 -26.447  51.297  1.00 24.63           C  
ANISOU 3186  CA  THR B 287     3744   2323   3292  -1249   1214   -554       C  
ATOM   3187  C   THR B 287      15.331 -25.200  52.156  1.00 25.15           C  
ANISOU 3187  C   THR B 287     3769   2445   3341  -1202   1213   -530       C  
ATOM   3188  O   THR B 287      16.433 -24.724  52.430  1.00 23.37           O  
ANISOU 3188  O   THR B 287     3603   2211   3065  -1119   1180   -471       O  
ATOM   3189  CB  THR B 287      14.833 -27.611  52.218  1.00 26.70           C  
ANISOU 3189  CB  THR B 287     4109   2501   3533  -1310   1320   -539       C  
ATOM   3190  OG1 THR B 287      15.751 -27.677  53.317  1.00 26.65           O  
ANISOU 3190  OG1 THR B 287     4233   2441   3452  -1246   1350   -456       O  
ATOM   3191  CG2 THR B 287      14.832 -28.940  51.456  1.00 28.80           C  
ANISOU 3191  CG2 THR B 287     4436   2694   3813  -1354   1330   -557       C  
ATOM   3192  N   LYS B 288      14.185 -24.680  52.585  1.00 24.05           N  
ANISOU 3192  N   LYS B 288     3527   2363   3247  -1254   1251   -579       N  
ATOM   3193  CA  LYS B 288      14.145 -23.556  53.513  1.00 26.86           C  
ANISOU 3193  CA  LYS B 288     3846   2767   3591  -1219   1266   -565       C  
ATOM   3194  C   LYS B 288      14.970 -23.820  54.771  1.00 28.38           C  
ANISOU 3194  C   LYS B 288     4190   2895   3697  -1181   1318   -489       C  
ATOM   3195  O   LYS B 288      15.768 -22.980  55.180  1.00 25.66           O  
ANISOU 3195  O   LYS B 288     3866   2571   3313  -1108   1284   -447       O  
ATOM   3196  CB  LYS B 288      12.699 -23.242  53.912  1.00 33.54           C  
ANISOU 3196  CB  LYS B 288     4577   3666   4502  -1290   1321   -633       C  
ATOM   3197  CG  LYS B 288      11.969 -22.309  52.962  1.00 42.96           C  
ANISOU 3197  CG  LYS B 288     5591   4954   5779  -1289   1246   -699       C  
ATOM   3198  CD  LYS B 288      10.721 -21.727  53.622  1.00 52.52           C  
ANISOU 3198  CD  LYS B 288     6689   6220   7048  -1329   1301   -755       C  
ATOM   3199  CE  LYS B 288       9.511 -22.644  53.472  1.00 59.74           C  
ANISOU 3199  CE  LYS B 288     7556   7125   8017  -1431   1358   -818       C  
ATOM   3200  NZ  LYS B 288       8.844 -22.483  52.145  1.00 60.96           N  
ANISOU 3200  NZ  LYS B 288     7570   7342   8251  -1449   1270   -880       N  
ATOM   3201  N   LYS B 289      14.768 -24.984  55.386  1.00 25.99           N  
ANISOU 3201  N   LYS B 289     3994   2516   3365  -1230   1396   -471       N  
ATOM   3202  CA  LYS B 289      15.484 -25.335  56.611  1.00 30.03           C  
ANISOU 3202  CA  LYS B 289     4656   2963   3790  -1196   1441   -395       C  
ATOM   3203  C   LYS B 289      16.997 -25.377  56.413  1.00 28.09           C  
ANISOU 3203  C   LYS B 289     4507   2681   3486  -1095   1370   -322       C  
ATOM   3204  O   LYS B 289      17.755 -24.992  57.302  1.00 29.11           O  
ANISOU 3204  O   LYS B 289     4710   2801   3549  -1034   1362   -263       O  
ATOM   3205  CB  LYS B 289      14.996 -26.675  57.168  1.00 38.50           C  
ANISOU 3205  CB  LYS B 289     5831   3951   4845  -1268   1533   -387       C  
ATOM   3206  CG  LYS B 289      13.584 -26.641  57.724  1.00 53.17           C  
ANISOU 3206  CG  LYS B 289     7619   5837   6745  -1366   1622   -449       C  
ATOM   3207  CD  LYS B 289      13.521 -27.320  59.084  1.00 63.20           C  
ANISOU 3207  CD  LYS B 289     9029   7036   7948  -1397   1717   -402       C  
ATOM   3208  CE  LYS B 289      12.117 -27.806  59.397  1.00 69.76           C  
ANISOU 3208  CE  LYS B 289     9815   7863   8827  -1515   1821   -466       C  
ATOM   3209  NZ  LYS B 289      11.707 -28.913  58.486  1.00 71.71           N  
ANISOU 3209  NZ  LYS B 289    10057   8063   9124  -1580   1835   -501       N  
ATOM   3210  N   GLN B 290      17.434 -25.852  55.251  1.00 24.71           N  
ANISOU 3210  N   GLN B 290     4075   2232   3083  -1078   1317   -329       N  
ATOM   3211  CA  GLN B 290      18.859 -25.901  54.945  1.00 26.71           C  
ANISOU 3211  CA  GLN B 290     4405   2451   3291   -980   1249   -268       C  
ATOM   3212  C   GLN B 290      19.447 -24.492  54.825  1.00 25.01           C  
ANISOU 3212  C   GLN B 290     4119   2311   3071   -912   1180   -260       C  
ATOM   3213  O   GLN B 290      20.548 -24.218  55.313  1.00 21.84           O  
ANISOU 3213  O   GLN B 290     3790   1894   2613   -829   1147   -197       O  
ATOM   3214  CB  GLN B 290      19.104 -26.698  53.663  1.00 25.02           C  
ANISOU 3214  CB  GLN B 290     4193   2203   3110   -984   1213   -290       C  
ATOM   3215  CG  GLN B 290      18.958 -28.205  53.843  1.00 27.15           C  
ANISOU 3215  CG  GLN B 290     4572   2374   3371  -1026   1275   -277       C  
ATOM   3216  CD  GLN B 290      18.832 -28.938  52.525  1.00 29.05           C  
ANISOU 3216  CD  GLN B 290     4788   2592   3659  -1058   1251   -324       C  
ATOM   3217  OE1 GLN B 290      18.706 -28.318  51.469  1.00 29.46           O  
ANISOU 3217  OE1 GLN B 290     4733   2709   3750  -1059   1188   -373       O  
ATOM   3218  NE2 GLN B 290      18.859 -30.269  52.580  1.00 30.03           N  
ANISOU 3218  NE2 GLN B 290     5013   2621   3777  -1085   1299   -312       N  
ATOM   3219  N   VAL B 291      18.706 -23.599  54.179  1.00 23.25           N  
ANISOU 3219  N   VAL B 291     3754   2170   2911   -944   1155   -323       N  
ATOM   3220  CA  VAL B 291      19.147 -22.211  54.050  1.00 19.90           C  
ANISOU 3220  CA  VAL B 291     3254   1815   2490   -887   1095   -320       C  
ATOM   3221  C   VAL B 291      19.237 -21.548  55.428  1.00 23.40           C  
ANISOU 3221  C   VAL B 291     3730   2274   2886   -865   1131   -288       C  
ATOM   3222  O   VAL B 291      20.194 -20.829  55.723  1.00 27.15           O  
ANISOU 3222  O   VAL B 291     4232   2764   3321   -793   1089   -244       O  
ATOM   3223  CB  VAL B 291      18.227 -21.395  53.117  1.00 23.18           C  
ANISOU 3223  CB  VAL B 291     3506   2314   2987   -925   1058   -395       C  
ATOM   3224  CG1 VAL B 291      18.590 -19.899  53.167  1.00 22.27           C  
ANISOU 3224  CG1 VAL B 291     3315   2267   2879   -870   1009   -391       C  
ATOM   3225  CG2 VAL B 291      18.325 -21.916  51.688  1.00 22.62           C  
ANISOU 3225  CG2 VAL B 291     3410   2235   2948   -935   1000   -423       C  
ATOM   3226  N   LEU B 292      18.250 -21.807  56.278  1.00 23.95           N  
ANISOU 3226  N   LEU B 292     3799   2341   2959   -930   1210   -310       N  
ATOM   3227  CA  LEU B 292      18.251 -21.221  57.616  1.00 25.21           C  
ANISOU 3227  CA  LEU B 292     3993   2515   3070   -917   1248   -286       C  
ATOM   3228  C   LEU B 292      19.370 -21.794  58.482  1.00 26.33           C  
ANISOU 3228  C   LEU B 292     4297   2592   3116   -859   1245   -200       C  
ATOM   3229  O   LEU B 292      19.987 -21.070  59.263  1.00 23.80           O  
ANISOU 3229  O   LEU B 292     4007   2294   2742   -806   1223   -163       O  
ATOM   3230  CB  LEU B 292      16.887 -21.385  58.298  1.00 27.37           C  
ANISOU 3230  CB  LEU B 292     4227   2800   3372  -1003   1338   -336       C  
ATOM   3231  CG  LEU B 292      15.773 -20.609  57.598  1.00 32.15           C  
ANISOU 3231  CG  LEU B 292     4656   3485   4076  -1044   1331   -422       C  
ATOM   3232  CD1 LEU B 292      14.453 -20.734  58.341  1.00 35.27           C  
ANISOU 3232  CD1 LEU B 292     5007   3892   4502  -1124   1423   -474       C  
ATOM   3233  CD2 LEU B 292      16.169 -19.145  57.431  1.00 33.92           C  
ANISOU 3233  CD2 LEU B 292     4793   3780   4316   -979   1267   -427       C  
ATOM   3234  N   ARG B 293      19.635 -23.090  58.343  1.00 28.28           N  
ANISOU 3234  N   ARG B 293     4644   2758   3342   -866   1260   -169       N  
ATOM   3235  CA  ARG B 293      20.749 -23.702  59.063  1.00 27.73           C  
ANISOU 3235  CA  ARG B 293     4724   2624   3189   -798   1243    -85       C  
ATOM   3236  C   ARG B 293      22.080 -23.117  58.602  1.00 25.12           C  
ANISOU 3236  C   ARG B 293     4394   2311   2837   -695   1148    -46       C  
ATOM   3237  O   ARG B 293      22.963 -22.850  59.418  1.00 26.17           O  
ANISOU 3237  O   ARG B 293     4599   2444   2902   -625   1115     13       O  
ATOM   3238  CB  ARG B 293      20.755 -25.225  58.900  1.00 28.77           C  
ANISOU 3238  CB  ARG B 293     4956   2662   3315   -821   1278    -63       C  
ATOM   3239  CG  ARG B 293      19.720 -25.940  59.754  1.00 36.56           C  
ANISOU 3239  CG  ARG B 293     5991   3610   4290   -910   1378    -74       C  
ATOM   3240  CD  ARG B 293      20.091 -27.401  59.941  1.00 46.04           C  
ANISOU 3240  CD  ARG B 293     7333   4704   5457   -906   1405    -22       C  
ATOM   3241  NE  ARG B 293      18.971 -28.182  60.455  1.00 55.76           N  
ANISOU 3241  NE  ARG B 293     8598   5893   6696  -1010   1508    -46       N  
ATOM   3242  CZ  ARG B 293      18.042 -28.739  59.685  1.00 63.72           C  
ANISOU 3242  CZ  ARG B 293     9546   6890   7775  -1095   1552   -111       C  
ATOM   3243  NH1 ARG B 293      18.101 -28.595  58.367  1.00 66.07           N  
ANISOU 3243  NH1 ARG B 293     9749   7218   8137  -1087   1498   -156       N  
ATOM   3244  NH2 ARG B 293      17.054 -29.436  60.229  1.00 65.20           N  
ANISOU 3244  NH2 ARG B 293     9767   7038   7968  -1190   1651   -131       N  
ATOM   3245  N   MET B 294      22.220 -22.916  57.294  1.00 22.29           N  
ANISOU 3245  N   MET B 294     3957   1974   2538   -686   1102    -80       N  
ATOM   3246  CA  MET B 294      23.428 -22.298  56.752  1.00 21.61           C  
ANISOU 3246  CA  MET B 294     3862   1907   2441   -595   1019    -51       C  
ATOM   3247  C   MET B 294      23.578 -20.849  57.234  1.00 20.84           C  
ANISOU 3247  C   MET B 294     3701   1888   2328   -568    993    -52       C  
ATOM   3248  O   MET B 294      24.685 -20.408  57.543  1.00 21.73           O  
ANISOU 3248  O   MET B 294     3853   2010   2393   -486    939     -4       O  
ATOM   3249  CB  MET B 294      23.450 -22.366  55.223  1.00 22.27           C  
ANISOU 3249  CB  MET B 294     3873   1998   2590   -602    980    -94       C  
ATOM   3250  CG  MET B 294      24.732 -21.814  54.595  1.00 23.02           C  
ANISOU 3250  CG  MET B 294     3964   2105   2677   -509    899    -67       C  
ATOM   3251  SD  MET B 294      26.261 -22.634  55.122  1.00 30.73           S  
ANISOU 3251  SD  MET B 294     5077   3010   3587   -397    861     17       S  
ATOM   3252  CE  MET B 294      26.190 -24.146  54.183  1.00 35.11           C  
ANISOU 3252  CE  MET B 294     5675   3489   4178   -418    879     -1       C  
ATOM   3253  N   GLU B 295      22.470 -20.114  57.303  1.00 20.26           N  
ANISOU 3253  N   GLU B 295     3526   1873   2300   -634   1031   -111       N  
ATOM   3254  CA  GLU B 295      22.495 -18.767  57.883  1.00 19.40           C  
ANISOU 3254  CA  GLU B 295     3357   1837   2177   -612   1018   -118       C  
ATOM   3255  C   GLU B 295      23.093 -18.801  59.289  1.00 21.12           C  
ANISOU 3255  C   GLU B 295     3680   2042   2302   -571   1023    -60       C  
ATOM   3256  O   GLU B 295      23.972 -18.000  59.625  1.00 20.52           O  
ANISOU 3256  O   GLU B 295     3610   2004   2183   -503    970    -31       O  
ATOM   3257  CB  GLU B 295      21.093 -18.167  57.947  1.00 22.39           C  
ANISOU 3257  CB  GLU B 295     3618   2270   2620   -687   1070   -192       C  
ATOM   3258  CG  GLU B 295      21.025 -16.892  58.794  1.00 27.32           C  
ANISOU 3258  CG  GLU B 295     4195   2960   3227   -666   1071   -202       C  
ATOM   3259  CD  GLU B 295      19.624 -16.310  58.888  1.00 29.82           C  
ANISOU 3259  CD  GLU B 295     4390   3326   3616   -728   1122   -278       C  
ATOM   3260  OE1 GLU B 295      18.826 -16.794  59.728  1.00 25.69           O  
ANISOU 3260  OE1 GLU B 295     3897   2783   3082   -784   1195   -292       O  
ATOM   3261  OE2 GLU B 295      19.328 -15.362  58.128  1.00 25.04           O  
ANISOU 3261  OE2 GLU B 295     3658   2777   3079   -719   1088   -324       O  
ATOM   3262  N   HIS B 296      22.617 -19.744  60.095  1.00 23.23           N  
ANISOU 3262  N   HIS B 296     4032   2258   2537   -613   1083    -44       N  
ATOM   3263  CA  HIS B 296      23.108 -19.944  61.459  1.00 27.55           C  
ANISOU 3263  CA  HIS B 296     4691   2786   2989   -581   1089     15       C  
ATOM   3264  C   HIS B 296      24.610 -20.199  61.451  1.00 24.56           C  
ANISOU 3264  C   HIS B 296     4396   2383   2554   -478   1006     86       C  
ATOM   3265  O   HIS B 296      25.358 -19.601  62.224  1.00 23.98           O  
ANISOU 3265  O   HIS B 296     4352   2345   2414   -420    960    121       O  
ATOM   3266  CB  HIS B 296      22.356 -21.120  62.104  1.00 37.62           C  
ANISOU 3266  CB  HIS B 296     6052   3996   4245   -648   1171     23       C  
ATOM   3267  CG  HIS B 296      22.833 -21.491  63.478  1.00 50.03           C  
ANISOU 3267  CG  HIS B 296     7755   5540   5715   -621   1178     90       C  
ATOM   3268  ND1 HIS B 296      21.986 -21.542  64.564  1.00 54.01           N  
ANISOU 3268  ND1 HIS B 296     8292   6046   6184   -686   1257     80       N  
ATOM   3269  CD2 HIS B 296      24.050 -21.875  63.932  1.00 53.29           C  
ANISOU 3269  CD2 HIS B 296     8273   5923   6052   -535   1114    167       C  
ATOM   3270  CE1 HIS B 296      22.667 -21.917  65.634  1.00 56.64           C  
ANISOU 3270  CE1 HIS B 296     8751   6351   6417   -645   1241    151       C  
ATOM   3271  NE2 HIS B 296      23.920 -22.124  65.277  1.00 56.20           N  
ANISOU 3271  NE2 HIS B 296     8738   6279   6338   -551   1150    204       N  
ATOM   3272  N   LEU B 297      25.047 -21.087  60.566  1.00 24.65           N  
ANISOU 3272  N   LEU B 297     4438   2336   2592   -454    983    102       N  
ATOM   3273  CA  LEU B 297      26.454 -21.457  60.486  1.00 26.58           C  
ANISOU 3273  CA  LEU B 297     4754   2550   2796   -351    905    165       C  
ATOM   3274  C   LEU B 297      27.330 -20.281  60.054  1.00 23.36           C  
ANISOU 3274  C   LEU B 297     4276   2210   2391   -281    828    163       C  
ATOM   3275  O   LEU B 297      28.422 -20.081  60.590  1.00 21.31           O  
ANISOU 3275  O   LEU B 297     4060   1965   2072   -196    762    211       O  
ATOM   3276  CB  LEU B 297      26.634 -22.637  59.527  1.00 26.31           C  
ANISOU 3276  CB  LEU B 297     4751   2439   2804   -344    906    167       C  
ATOM   3277  CG  LEU B 297      28.051 -23.184  59.378  1.00 28.19           C  
ANISOU 3277  CG  LEU B 297     5056   2637   3016   -233    832    226       C  
ATOM   3278  CD1 LEU B 297      28.680 -23.431  60.741  1.00 32.76           C  
ANISOU 3278  CD1 LEU B 297     5737   3203   3506   -176    805    296       C  
ATOM   3279  CD2 LEU B 297      28.016 -24.471  58.570  1.00 28.90           C  
ANISOU 3279  CD2 LEU B 297     5184   2646   3150   -241    853    221       C  
ATOM   3280  N   VAL B 298      26.851 -19.505  59.087  1.00 20.10           N  
ANISOU 3280  N   VAL B 298     3750   1841   2045   -317    834    106       N  
ATOM   3281  CA  VAL B 298      27.594 -18.335  58.632  1.00 20.02           C  
ANISOU 3281  CA  VAL B 298     3671   1897   2038   -261    770    101       C  
ATOM   3282  C   VAL B 298      27.757 -17.337  59.780  1.00 21.18           C  
ANISOU 3282  C   VAL B 298     3810   2113   2124   -241    755    106       C  
ATOM   3283  O   VAL B 298      28.850 -16.818  60.009  1.00 21.22           O  
ANISOU 3283  O   VAL B 298     3825   2154   2084   -162    684    133       O  
ATOM   3284  CB  VAL B 298      26.945 -17.671  57.394  1.00 18.45           C  
ANISOU 3284  CB  VAL B 298     3352   1734   1922   -310    783     38       C  
ATOM   3285  CG1 VAL B 298      27.681 -16.375  57.022  1.00 17.70           C  
ANISOU 3285  CG1 VAL B 298     3156   1726   1844   -239    695     16       C  
ATOM   3286  CG2 VAL B 298      26.966 -18.634  56.198  1.00 17.77           C  
ANISOU 3286  CG2 VAL B 298     3275   1583   1893   -322    779     29       C  
ATOM   3287  N   LEU B 299      26.676 -17.100  60.520  1.00 19.29           N  
ANISOU 3287  N   LEU B 299     3552   1894   1885   -313    820     74       N  
ATOM   3288  CA  LEU B 299      26.716 -16.175  61.654  1.00 20.34           C  
ANISOU 3288  CA  LEU B 299     3677   2088   1963   -304    813     68       C  
ATOM   3289  C   LEU B 299      27.732 -16.611  62.708  1.00 22.51           C  
ANISOU 3289  C   LEU B 299     4067   2348   2138   -239    764    136       C  
ATOM   3290  O   LEU B 299      28.462 -15.785  63.256  1.00 22.13           O  
ANISOU 3290  O   LEU B 299     4011   2359   2039   -189    707    141       O  
ATOM   3291  CB  LEU B 299      25.331 -16.047  62.298  1.00 19.49           C  
ANISOU 3291  CB  LEU B 299     3540   1989   1875   -393    902     23       C  
ATOM   3292  CG  LEU B 299      24.302 -15.221  61.528  1.00 20.93           C  
ANISOU 3292  CG  LEU B 299     3582   2216   2153   -446    936    -54       C  
ATOM   3293  CD1 LEU B 299      22.917 -15.378  62.129  1.00 22.86           C  
ANISOU 3293  CD1 LEU B 299     3805   2457   2426   -532   1027    -97       C  
ATOM   3294  CD2 LEU B 299      24.719 -13.757  61.532  1.00 19.90           C  
ANISOU 3294  CD2 LEU B 299     3371   2164   2027   -400    888    -83       C  
ATOM   3295  N   LYS B 300      27.770 -17.910  62.988  1.00 24.22           N  
ANISOU 3295  N   LYS B 300     4386   2486   2328   -241    783    183       N  
ATOM   3296  CA  LYS B 300      28.726 -18.460  63.946  1.00 28.39           C  
ANISOU 3296  CA  LYS B 300     5025   2994   2766   -174    731    252       C  
ATOM   3297  C   LYS B 300      30.167 -18.276  63.470  1.00 25.64           C  
ANISOU 3297  C   LYS B 300     4669   2663   2408    -66    624    283       C  
ATOM   3298  O   LYS B 300      31.024 -17.813  64.221  1.00 24.17           O  
ANISOU 3298  O   LYS B 300     4504   2526   2156     -6    554    308       O  
ATOM   3299  CB  LYS B 300      28.432 -19.944  64.204  1.00 38.91           C  
ANISOU 3299  CB  LYS B 300     6466   4232   4086   -196    777    294       C  
ATOM   3300  CG  LYS B 300      29.494 -20.670  65.025  1.00 50.32           C  
ANISOU 3300  CG  LYS B 300     8026   5645   5450   -114    713    373       C  
ATOM   3301  CD  LYS B 300      29.745 -19.982  66.362  1.00 60.06           C  
ANISOU 3301  CD  LYS B 300     9291   6942   6587   -102    685    390       C  
ATOM   3302  CE  LYS B 300      30.627 -20.826  67.278  1.00 65.72           C  
ANISOU 3302  CE  LYS B 300    10129   7624   7217    -32    627    471       C  
ATOM   3303  NZ  LYS B 300      29.824 -21.696  68.187  1.00 68.28           N  
ANISOU 3303  NZ  LYS B 300    10562   7890   7491    -97    709    502       N  
ATOM   3304  N   VAL B 301      30.430 -18.637  62.218  1.00 22.47           N  
ANISOU 3304  N   VAL B 301     4236   2227   2076    -43    611    277       N  
ATOM   3305  CA  VAL B 301      31.774 -18.514  61.654  1.00 22.53           C  
ANISOU 3305  CA  VAL B 301     4227   2246   2087     60    517    301       C  
ATOM   3306  C   VAL B 301      32.239 -17.061  61.580  1.00 23.14           C  
ANISOU 3306  C   VAL B 301     4216   2421   2154     87    465    268       C  
ATOM   3307  O   VAL B 301      33.400 -16.754  61.856  1.00 24.61           O  
ANISOU 3307  O   VAL B 301     4404   2645   2303    172    376    290       O  
ATOM   3308  CB  VAL B 301      31.856 -19.196  60.273  1.00 18.76           C  
ANISOU 3308  CB  VAL B 301     3730   1708   1690     70    526    292       C  
ATOM   3309  CG1 VAL B 301      33.183 -18.904  59.588  1.00 22.08           C  
ANISOU 3309  CG1 VAL B 301     4112   2148   2129    173    437    304       C  
ATOM   3310  CG2 VAL B 301      31.647 -20.699  60.428  1.00 22.86           C  
ANISOU 3310  CG2 VAL B 301     4343   2131   2212     61    562    324       C  
ATOM   3311  N   LEU B 302      31.327 -16.158  61.233  1.00 18.41           N  
ANISOU 3311  N   LEU B 302     3536   1867   1594     15    517    208       N  
ATOM   3312  CA  LEU B 302      31.664 -14.740  61.167  1.00 18.82           C  
ANISOU 3312  CA  LEU B 302     3492   2010   1650     33    473    161       C  
ATOM   3313  C   LEU B 302      31.593 -14.066  62.541  1.00 21.46           C  
ANISOU 3313  C   LEU B 302     3849   2397   1908     20    470    153       C  
ATOM   3314  O   LEU B 302      31.884 -12.874  62.670  1.00 20.13           O  
ANISOU 3314  O   LEU B 302     3614   2301   1733     32    436    110       O  
ATOM   3315  CB  LEU B 302      30.746 -14.015  60.187  1.00 17.74           C  
ANISOU 3315  CB  LEU B 302     3229   1898   1613    -27    512     90       C  
ATOM   3316  CG  LEU B 302      30.760 -14.515  58.741  1.00 21.29           C  
ANISOU 3316  CG  LEU B 302     3626   2310   2152    -22    501     78       C  
ATOM   3317  CD1 LEU B 302      29.978 -13.571  57.836  1.00 21.38           C  
ANISOU 3317  CD1 LEU B 302     3510   2364   2249    -67    514     11       C  
ATOM   3318  CD2 LEU B 302      32.187 -14.690  58.250  1.00 21.82           C  
ANISOU 3318  CD2 LEU B 302     3685   2378   2226     72    413    103       C  
ATOM   3319  N   THR B 303      31.222 -14.842  63.557  1.00 21.28           N  
ANISOU 3319  N   THR B 303     3916   2337   1833     -5    503    190       N  
ATOM   3320  CA  THR B 303      30.958 -14.325  64.904  1.00 25.66           C  
ANISOU 3320  CA  THR B 303     4496   2937   2317    -33    515    180       C  
ATOM   3321  C   THR B 303      30.120 -13.043  64.890  1.00 21.90           C  
ANISOU 3321  C   THR B 303     3920   2521   1880    -91    563    102       C  
ATOM   3322  O   THR B 303      30.446 -12.070  65.567  1.00 24.66           O  
ANISOU 3322  O   THR B 303     4246   2935   2188    -79    531     73       O  
ATOM   3323  CB  THR B 303      32.255 -14.104  65.720  1.00 29.77           C  
ANISOU 3323  CB  THR B 303     5058   3502   2751     46    412    213       C  
ATOM   3324  OG1 THR B 303      33.128 -13.214  65.014  1.00 33.61           O  
ANISOU 3324  OG1 THR B 303     5461   4043   3265    100    337    182       O  
ATOM   3325  CG2 THR B 303      32.967 -15.429  65.961  1.00 35.42           C  
ANISOU 3325  CG2 THR B 303     5875   4154   3427    106    368    293       C  
ATOM   3326  N   PHE B 304      29.053 -13.055  64.097  1.00 18.41           N  
ANISOU 3326  N   PHE B 304     3414   2055   1524   -151    635     64       N  
ATOM   3327  CA  PHE B 304      28.115 -11.942  64.018  1.00 17.91           C  
ANISOU 3327  CA  PHE B 304     3247   2038   1519   -201    684    -10       C  
ATOM   3328  C   PHE B 304      28.736 -10.618  63.584  1.00 20.21           C  
ANISOU 3328  C   PHE B 304     3450   2393   1836   -159    624    -56       C  
ATOM   3329  O   PHE B 304      28.120  -9.568  63.746  1.00 22.31           O  
ANISOU 3329  O   PHE B 304     3639   2698   2140   -186    652   -116       O  
ATOM   3330  CB  PHE B 304      27.379 -11.751  65.353  1.00 21.46           C  
ANISOU 3330  CB  PHE B 304     3730   2504   1919   -251    743    -26       C  
ATOM   3331  CG  PHE B 304      25.972 -12.259  65.344  1.00 25.51           C  
ANISOU 3331  CG  PHE B 304     4229   2980   2485   -332    844    -48       C  
ATOM   3332  CD1 PHE B 304      24.946 -11.479  64.838  1.00 31.69           C  
ANISOU 3332  CD1 PHE B 304     4893   3787   3361   -374    892   -119       C  
ATOM   3333  CD2 PHE B 304      25.671 -13.512  65.842  1.00 26.59           C  
ANISOU 3333  CD2 PHE B 304     4467   3055   2580   -365    889     -2       C  
ATOM   3334  CE1 PHE B 304      23.643 -11.943  64.834  1.00 30.74           C  
ANISOU 3334  CE1 PHE B 304     4749   3638   3293   -450    980   -147       C  
ATOM   3335  CE2 PHE B 304      24.369 -13.984  65.835  1.00 30.48           C  
ANISOU 3335  CE2 PHE B 304     4944   3515   3124   -446    984    -31       C  
ATOM   3336  CZ  PHE B 304      23.357 -13.195  65.331  1.00 31.41           C  
ANISOU 3336  CZ  PHE B 304     4934   3664   3335   -489   1028   -105       C  
ATOM   3337  N   ASP B 305      29.940 -10.657  63.024  1.00 17.54           N  
ANISOU 3337  N   ASP B 305     3121   2061   1484    -91    543    -31       N  
ATOM   3338  CA  ASP B 305      30.599  -9.419  62.612  1.00 17.41           C  
ANISOU 3338  CA  ASP B 305     3025   2099   1492    -54    486    -78       C  
ATOM   3339  C   ASP B 305      30.208  -9.091  61.174  1.00 20.01           C  
ANISOU 3339  C   ASP B 305     3240   2418   1946    -61    485   -109       C  
ATOM   3340  O   ASP B 305      30.939  -9.406  60.235  1.00 19.20           O  
ANISOU 3340  O   ASP B 305     3109   2301   1884    -19    426    -86       O  
ATOM   3341  CB  ASP B 305      32.117  -9.532  62.753  1.00 22.73           C  
ANISOU 3341  CB  ASP B 305     3726   2791   2118     24    379    -42       C  
ATOM   3342  CG  ASP B 305      32.570  -9.571  64.208  1.00 28.36           C  
ANISOU 3342  CG  ASP B 305     4531   3533   2712     37    354    -20       C  
ATOM   3343  OD1 ASP B 305      32.028  -8.799  65.023  1.00 30.17           O  
ANISOU 3343  OD1 ASP B 305     4743   3798   2924     -5    387    -64       O  
ATOM   3344  OD2 ASP B 305      33.462 -10.380  64.537  1.00 28.58           O  
ANISOU 3344  OD2 ASP B 305     4631   3548   2679     92    291     40       O  
ATOM   3345  N   LEU B 306      29.051  -8.448  61.014  1.00 16.15           N  
ANISOU 3345  N   LEU B 306     2683   1938   1516   -113    549   -162       N  
ATOM   3346  CA  LEU B 306      28.449  -8.266  59.693  1.00 15.91           C  
ANISOU 3346  CA  LEU B 306     2554   1895   1596   -126    550   -186       C  
ATOM   3347  C   LEU B 306      28.607  -6.860  59.115  1.00 12.08           C  
ANISOU 3347  C   LEU B 306     1965   1445   1182   -103    506   -231       C  
ATOM   3348  O   LEU B 306      28.401  -6.650  57.922  1.00 14.58           O  
ANISOU 3348  O   LEU B 306     2208   1753   1577    -98    481   -239       O  
ATOM   3349  CB  LEU B 306      26.965  -8.612  59.743  1.00 19.34           C  
ANISOU 3349  CB  LEU B 306     2971   2310   2066   -197    645   -212       C  
ATOM   3350  CG  LEU B 306      26.629 -10.028  60.210  1.00 25.22           C  
ANISOU 3350  CG  LEU B 306     3817   3008   2758   -237    702   -168       C  
ATOM   3351  CD1 LEU B 306      25.129 -10.252  60.150  1.00 32.80           C  
ANISOU 3351  CD1 LEU B 306     4725   3955   3783   -313    782   -203       C  
ATOM   3352  CD2 LEU B 306      27.374 -11.067  59.382  1.00 23.48           C  
ANISOU 3352  CD2 LEU B 306     3640   2744   2538   -205    654   -117       C  
ATOM   3353  N   ALA B 307      28.948  -5.896  59.960  1.00 11.83           N  
ANISOU 3353  N   ALA B 307     1933   1446   1117    -92    497   -262       N  
ATOM   3354  CA  ALA B 307      29.012  -4.502  59.521  1.00 13.38           C  
ANISOU 3354  CA  ALA B 307     2040   1661   1382    -76    468   -308       C  
ATOM   3355  C   ALA B 307      30.338  -4.183  58.826  1.00 17.42           C  
ANISOU 3355  C   ALA B 307     2528   2182   1907    -29    380   -288       C  
ATOM   3356  O   ALA B 307      31.099  -3.317  59.271  1.00 16.60           O  
ANISOU 3356  O   ALA B 307     2417   2104   1788    -11    344   -312       O  
ATOM   3357  CB  ALA B 307      28.776  -3.559  60.713  1.00 16.04           C  
ANISOU 3357  CB  ALA B 307     2386   2023   1685    -91    505   -361       C  
ATOM   3358  N   ALA B 308      30.598  -4.877  57.725  1.00 13.07           N  
ANISOU 3358  N   ALA B 308     1966   1611   1389    -13    351   -252       N  
ATOM   3359  CA  ALA B 308      31.890  -4.789  57.046  1.00 12.62           C  
ANISOU 3359  CA  ALA B 308     1892   1562   1340     29    281   -231       C  
ATOM   3360  C   ALA B 308      31.955  -3.604  56.097  1.00 16.97           C  
ANISOU 3360  C   ALA B 308     2361   2117   1968     32    257   -256       C  
ATOM   3361  O   ALA B 308      30.968  -3.272  55.441  1.00 16.27           O  
ANISOU 3361  O   ALA B 308     2230   2014   1939     13    280   -269       O  
ATOM   3362  CB  ALA B 308      32.167  -6.085  56.278  1.00 16.41           C  
ANISOU 3362  CB  ALA B 308     2403   2016   1817     44    271   -186       C  
ATOM   3363  N   PRO B 309      33.131  -2.969  56.006  1.00 13.90           N  
ANISOU 3363  N   PRO B 309     1952   1747   1581     57    208   -261       N  
ATOM   3364  CA  PRO B 309      33.326  -1.916  55.005  1.00 15.30           C  
ANISOU 3364  CA  PRO B 309     2066   1918   1828     57    189   -274       C  
ATOM   3365  C   PRO B 309      33.404  -2.545  53.623  1.00 18.12           C  
ANISOU 3365  C   PRO B 309     2412   2260   2214     65    177   -240       C  
ATOM   3366  O   PRO B 309      33.918  -3.656  53.491  1.00 20.17           O  
ANISOU 3366  O   PRO B 309     2704   2518   2440     82    169   -212       O  
ATOM   3367  CB  PRO B 309      34.694  -1.320  55.385  1.00 18.97           C  
ANISOU 3367  CB  PRO B 309     2520   2409   2278     72    146   -289       C  
ATOM   3368  CG  PRO B 309      34.926  -1.748  56.808  1.00 19.38           C  
ANISOU 3368  CG  PRO B 309     2624   2487   2253     77    142   -298       C  
ATOM   3369  CD  PRO B 309      34.293  -3.102  56.902  1.00 17.42           C  
ANISOU 3369  CD  PRO B 309     2430   2222   1965     80    169   -259       C  
ATOM   3370  N   THR B 310      32.893  -1.853  52.612  1.00 13.26           N  
ANISOU 3370  N   THR B 310     1755   1628   1655     56    176   -242       N  
ATOM   3371  CA  THR B 310      32.894  -2.374  51.255  1.00 11.35           C  
ANISOU 3371  CA  THR B 310     1508   1375   1429     58    165   -214       C  
ATOM   3372  C   THR B 310      33.529  -1.368  50.311  1.00 10.67           C  
ANISOU 3372  C   THR B 310     1390   1285   1378     61    142   -209       C  
ATOM   3373  O   THR B 310      33.699  -0.201  50.661  1.00 10.95           O  
ANISOU 3373  O   THR B 310     1403   1317   1440     58    139   -229       O  
ATOM   3374  CB  THR B 310      31.459  -2.587  50.756  1.00 10.24           C  
ANISOU 3374  CB  THR B 310     1354   1219   1317     38    181   -216       C  
ATOM   3375  OG1 THR B 310      30.770  -1.337  50.795  1.00 13.46           O  
ANISOU 3375  OG1 THR B 310     1719   1620   1775     36    181   -237       O  
ATOM   3376  CG2 THR B 310      30.716  -3.599  51.652  1.00 13.70           C  
ANISOU 3376  CG2 THR B 310     1824   1656   1726     21    219   -222       C  
ATOM   3377  N   VAL B 311      33.840  -1.811  49.094  1.00  9.15           N  
ANISOU 3377  N   VAL B 311     1203   1090   1185     63    133   -185       N  
ATOM   3378  CA  VAL B 311      34.306  -0.895  48.047  1.00 11.28           C  
ANISOU 3378  CA  VAL B 311     1454   1352   1480     58    121   -173       C  
ATOM   3379  C   VAL B 311      33.274   0.214  47.848  1.00 12.97           C  
ANISOU 3379  C   VAL B 311     1648   1542   1737     51    114   -175       C  
ATOM   3380  O   VAL B 311      33.609   1.389  47.685  1.00 10.96           O  
ANISOU 3380  O   VAL B 311     1380   1271   1513     48    109   -175       O  
ATOM   3381  CB  VAL B 311      34.512  -1.661  46.717  1.00 10.94           C  
ANISOU 3381  CB  VAL B 311     1431   1309   1416     56    119   -149       C  
ATOM   3382  CG1 VAL B 311      34.672  -0.695  45.529  1.00 12.93           C  
ANISOU 3382  CG1 VAL B 311     1679   1550   1684     44    111   -129       C  
ATOM   3383  CG2 VAL B 311      35.711  -2.594  46.837  1.00 11.67           C  
ANISOU 3383  CG2 VAL B 311     1536   1418   1480     73    129   -151       C  
ATOM   3384  N   ASN B 312      32.007  -0.174  47.899  1.00 11.00           N  
ANISOU 3384  N   ASN B 312     1393   1290   1498     49    115   -179       N  
ATOM   3385  CA  ASN B 312      30.911   0.755  47.684  1.00 14.71           C  
ANISOU 3385  CA  ASN B 312     1832   1738   2017     54    103   -183       C  
ATOM   3386  C   ASN B 312      30.881   1.872  48.720  1.00 16.72           C  
ANISOU 3386  C   ASN B 312     2067   1977   2308     60    118   -213       C  
ATOM   3387  O   ASN B 312      30.644   3.029  48.394  1.00 12.80           O  
ANISOU 3387  O   ASN B 312     1555   1450   1858     71    106   -210       O  
ATOM   3388  CB  ASN B 312      29.581  -0.010  47.668  1.00 17.50           C  
ANISOU 3388  CB  ASN B 312     2168   2100   2380     46    105   -193       C  
ATOM   3389  CG  ASN B 312      28.395   0.896  47.478  1.00 29.19           C  
ANISOU 3389  CG  ASN B 312     3603   3566   3924     60     87   -202       C  
ATOM   3390  OD1 ASN B 312      28.202   1.466  46.400  1.00 29.66           O  
ANISOU 3390  OD1 ASN B 312     3656   3611   4001     74     46   -174       O  
ATOM   3391  ND2 ASN B 312      27.576   1.032  48.523  1.00 30.66           N  
ANISOU 3391  ND2 ASN B 312     3755   3751   4141     60    119   -240       N  
ATOM   3392  N   GLN B 313      31.130   1.526  49.975  1.00 11.28           N  
ANISOU 3392  N   GLN B 313     1387   1306   1594     54    145   -243       N  
ATOM   3393  CA  GLN B 313      31.147   2.530  51.024  1.00 11.08           C  
ANISOU 3393  CA  GLN B 313     1350   1268   1591     55    163   -283       C  
ATOM   3394  C   GLN B 313      32.264   3.559  50.837  1.00 14.40           C  
ANISOU 3394  C   GLN B 313     1773   1673   2026     51    149   -284       C  
ATOM   3395  O   GLN B 313      32.094   4.721  51.182  1.00 15.36           O  
ANISOU 3395  O   GLN B 313     1882   1763   2192     52    157   -310       O  
ATOM   3396  CB  GLN B 313      31.286   1.874  52.389  1.00 14.91           C  
ANISOU 3396  CB  GLN B 313     1859   1782   2025     45    189   -311       C  
ATOM   3397  CG  GLN B 313      29.998   1.265  52.905  1.00 16.52           C  
ANISOU 3397  CG  GLN B 313     2057   1991   2228     38    225   -327       C  
ATOM   3398  CD  GLN B 313      30.251   0.451  54.153  1.00 20.42           C  
ANISOU 3398  CD  GLN B 313     2597   2511   2652     25    253   -340       C  
ATOM   3399  OE1 GLN B 313      30.668   0.991  55.176  1.00 22.93           O  
ANISOU 3399  OE1 GLN B 313     2930   2839   2945     22    263   -372       O  
ATOM   3400  NE2 GLN B 313      30.034  -0.857  54.065  1.00 15.24           N  
ANISOU 3400  NE2 GLN B 313     1970   1863   1959     16    263   -314       N  
ATOM   3401  N   PHE B 314      33.412   3.129  50.316  1.00 11.39           N  
ANISOU 3401  N   PHE B 314     1405   1309   1614     45    134   -260       N  
ATOM   3402  CA  PHE B 314      34.484   4.081  50.016  1.00 10.95           C  
ANISOU 3402  CA  PHE B 314     1344   1239   1580     31    129   -262       C  
ATOM   3403  C   PHE B 314      34.178   4.901  48.765  1.00 12.71           C  
ANISOU 3403  C   PHE B 314     1568   1416   1843     31    122   -226       C  
ATOM   3404  O   PHE B 314      34.400   6.111  48.751  1.00 11.97           O  
ANISOU 3404  O   PHE B 314     1474   1283   1793     20    128   -235       O  
ATOM   3405  CB  PHE B 314      35.850   3.379  49.917  1.00 11.34           C  
ANISOU 3405  CB  PHE B 314     1393   1325   1589     25    121   -256       C  
ATOM   3406  CG  PHE B 314      36.402   2.991  51.253  1.00 11.30           C  
ANISOU 3406  CG  PHE B 314     1386   1357   1548     28    115   -292       C  
ATOM   3407  CD1 PHE B 314      36.969   3.955  52.084  1.00 11.53           C  
ANISOU 3407  CD1 PHE B 314     1400   1387   1592      9    112   -337       C  
ATOM   3408  CD2 PHE B 314      36.304   1.684  51.709  1.00 11.25           C  
ANISOU 3408  CD2 PHE B 314     1402   1382   1492     47    110   -282       C  
ATOM   3409  CE1 PHE B 314      37.465   3.614  53.330  1.00 12.64           C  
ANISOU 3409  CE1 PHE B 314     1545   1569   1688     12     96   -371       C  
ATOM   3410  CE2 PHE B 314      36.806   1.332  52.955  1.00 11.53           C  
ANISOU 3410  CE2 PHE B 314     1447   1450   1483     55     97   -307       C  
ATOM   3411  CZ  PHE B 314      37.376   2.299  53.772  1.00 11.85           C  
ANISOU 3411  CZ  PHE B 314     1471   1501   1529     38     86   -352       C  
ATOM   3412  N   LEU B 315      33.660   4.255  47.723  1.00 12.85           N  
ANISOU 3412  N   LEU B 315     1598   1439   1846     40    108   -186       N  
ATOM   3413  CA  LEU B 315      33.330   4.981  46.491  1.00 11.35           C  
ANISOU 3413  CA  LEU B 315     1422   1211   1681     44     92   -144       C  
ATOM   3414  C   LEU B 315      32.381   6.140  46.748  1.00 13.77           C  
ANISOU 3414  C   LEU B 315     1716   1467   2050     63     85   -152       C  
ATOM   3415  O   LEU B 315      32.594   7.228  46.234  1.00 13.05           O  
ANISOU 3415  O   LEU B 315     1642   1326   1991     61     82   -130       O  
ATOM   3416  CB  LEU B 315      32.715   4.056  45.432  1.00 11.49           C  
ANISOU 3416  CB  LEU B 315     1454   1248   1664     52     68   -109       C  
ATOM   3417  CG  LEU B 315      33.701   3.194  44.657  1.00 14.43           C  
ANISOU 3417  CG  LEU B 315     1852   1650   1982     34     78    -90       C  
ATOM   3418  CD1 LEU B 315      32.936   2.293  43.693  1.00 16.62           C  
ANISOU 3418  CD1 LEU B 315     2147   1943   2225     39     54    -68       C  
ATOM   3419  CD2 LEU B 315      34.665   4.107  43.902  1.00 14.93           C  
ANISOU 3419  CD2 LEU B 315     1936   1688   2048     14     92    -65       C  
ATOM   3420  N   THR B 316      31.332   5.925  47.543  1.00 10.76           N  
ANISOU 3420  N   THR B 316     1305   1093   1689     83     88   -185       N  
ATOM   3421  CA  THR B 316      30.359   6.999  47.723  1.00 11.38           C  
ANISOU 3421  CA  THR B 316     1363   1123   1839    111     83   -197       C  
ATOM   3422  C   THR B 316      30.983   8.203  48.431  1.00 14.13           C  
ANISOU 3422  C   THR B 316     1719   1425   2224    101    109   -230       C  
ATOM   3423  O   THR B 316      30.608   9.348  48.180  1.00 13.36           O  
ANISOU 3423  O   THR B 316     1625   1263   2187    121    104   -222       O  
ATOM   3424  CB  THR B 316      29.052   6.526  48.431  1.00 15.55           C  
ANISOU 3424  CB  THR B 316     1846   1671   2390    131     93   -234       C  
ATOM   3425  OG1 THR B 316      29.347   6.093  49.762  1.00 15.45           O  
ANISOU 3425  OG1 THR B 316     1833   1689   2348    110    135   -285       O  
ATOM   3426  CG2 THR B 316      28.424   5.376  47.662  1.00 14.68           C  
ANISOU 3426  CG2 THR B 316     1726   1601   2250    131     65   -206       C  
ATOM   3427  N   GLN B 317      31.960   7.952  49.298  1.00 12.49           N  
ANISOU 3427  N   GLN B 317     1517   1248   1980     69    133   -267       N  
ATOM   3428  CA  GLN B 317      32.660   9.056  49.934  1.00 11.42           C  
ANISOU 3428  CA  GLN B 317     1389   1075   1876     48    154   -306       C  
ATOM   3429  C   GLN B 317      33.553   9.773  48.933  1.00 13.35           C  
ANISOU 3429  C   GLN B 317     1659   1278   2135     25    149   -265       C  
ATOM   3430  O   GLN B 317      33.586  11.004  48.885  1.00 16.88           O  
ANISOU 3430  O   GLN B 317     2121   1654   2638     20    161   -272       O  
ATOM   3431  CB  GLN B 317      33.506   8.559  51.100  1.00 14.70           C  
ANISOU 3431  CB  GLN B 317     1800   1543   2241     20    168   -357       C  
ATOM   3432  CG  GLN B 317      32.707   7.965  52.232  1.00 18.79           C  
ANISOU 3432  CG  GLN B 317     2308   2096   2734     33    185   -399       C  
ATOM   3433  CD  GLN B 317      33.625   7.542  53.346  1.00 32.67           C  
ANISOU 3433  CD  GLN B 317     4076   3905   4431      8    187   -440       C  
ATOM   3434  OE1 GLN B 317      34.271   8.379  53.970  1.00 33.40           O  
ANISOU 3434  OE1 GLN B 317     4170   3985   4534    -16    192   -487       O  
ATOM   3435  NE2 GLN B 317      33.732   6.239  53.566  1.00 38.47           N  
ANISOU 3435  NE2 GLN B 317     4819   4696   5101     13    178   -423       N  
ATOM   3436  N   TYR B 318      34.273   8.999  48.131  1.00 10.20           N  
ANISOU 3436  N   TYR B 318     1270    918   1687      8    140   -225       N  
ATOM   3437  CA  TYR B 318      35.160   9.586  47.123  1.00 11.92           C  
ANISOU 3437  CA  TYR B 318     1516   1103   1910    -22    148   -186       C  
ATOM   3438  C   TYR B 318      34.393  10.451  46.110  1.00 11.86           C  
ANISOU 3438  C   TYR B 318     1544   1022   1939      1    134   -130       C  
ATOM   3439  O   TYR B 318      34.920  11.456  45.624  1.00 15.17           O  
ANISOU 3439  O   TYR B 318     1996   1380   2387    -25    151   -107       O  
ATOM   3440  CB  TYR B 318      35.903   8.492  46.352  1.00 12.97           C  
ANISOU 3440  CB  TYR B 318     1652   1294   1982    -37    147   -155       C  
ATOM   3441  CG  TYR B 318      36.851   7.621  47.163  1.00 11.48           C  
ANISOU 3441  CG  TYR B 318     1430   1173   1757    -52    155   -199       C  
ATOM   3442  CD1 TYR B 318      37.154   7.906  48.491  1.00 10.67           C  
ANISOU 3442  CD1 TYR B 318     1303   1083   1668    -61    157   -260       C  
ATOM   3443  CD2 TYR B 318      37.466   6.520  46.567  1.00  9.70           C  
ANISOU 3443  CD2 TYR B 318     1203    998   1484    -53    156   -179       C  
ATOM   3444  CE1 TYR B 318      38.026   7.090  49.226  1.00 11.62           C  
ANISOU 3444  CE1 TYR B 318     1397   1268   1751    -67    150   -293       C  
ATOM   3445  CE2 TYR B 318      38.337   5.707  47.282  1.00 10.57           C  
ANISOU 3445  CE2 TYR B 318     1282   1165   1568    -54    155   -213       C  
ATOM   3446  CZ  TYR B 318      38.619   5.998  48.605  1.00 12.71           C  
ANISOU 3446  CZ  TYR B 318     1528   1450   1849    -59    147   -266       C  
ATOM   3447  OH  TYR B 318      39.489   5.179  49.303  1.00 12.50           O  
ANISOU 3447  OH  TYR B 318     1475   1483   1793    -53    134   -294       O  
ATOM   3448  N   PHE B 319      33.166  10.045  45.778  1.00 13.22           N  
ANISOU 3448  N   PHE B 319     1710   1201   2112     48    100   -105       N  
ATOM   3449  CA  PHE B 319      32.344  10.781  44.810  1.00 14.30           C  
ANISOU 3449  CA  PHE B 319     1876   1276   2280     83     68    -47       C  
ATOM   3450  C   PHE B 319      32.097  12.232  45.218  1.00 20.31           C  
ANISOU 3450  C   PHE B 319     2650   1945   3123     98     81    -61       C  
ATOM   3451  O   PHE B 319      31.900  13.095  44.365  1.00 19.95           O  
ANISOU 3451  O   PHE B 319     2650   1827   3104    115     64     -4       O  
ATOM   3452  CB  PHE B 319      30.974  10.113  44.621  1.00 13.82           C  
ANISOU 3452  CB  PHE B 319     1785   1246   2220    133     24    -38       C  
ATOM   3453  CG  PHE B 319      31.024   8.781  43.930  1.00 12.70           C  
ANISOU 3453  CG  PHE B 319     1646   1176   2003    121      4    -15       C  
ATOM   3454  CD1 PHE B 319      32.150   8.379  43.233  1.00 12.58           C  
ANISOU 3454  CD1 PHE B 319     1670   1183   1926     80     21     12       C  
ATOM   3455  CD2 PHE B 319      29.921   7.939  43.962  1.00 16.15           C  
ANISOU 3455  CD2 PHE B 319     2044   1655   2436    147    -27    -26       C  
ATOM   3456  CE1 PHE B 319      32.184   7.142  42.597  1.00 14.77           C  
ANISOU 3456  CE1 PHE B 319     1954   1521   2138     71      9     25       C  
ATOM   3457  CE2 PHE B 319      29.942   6.706  43.329  1.00 16.50           C  
ANISOU 3457  CE2 PHE B 319     2097   1758   2415    131    -43    -11       C  
ATOM   3458  CZ  PHE B 319      31.070   6.308  42.645  1.00 12.54           C  
ANISOU 3458  CZ  PHE B 319     1640   1274   1850     96    -25     14       C  
ATOM   3459  N   LEU B 320      32.080  12.493  46.521  1.00 15.53           N  
ANISOU 3459  N   LEU B 320     2010   1336   2554     94    110   -136       N  
ATOM   3460  CA  LEU B 320      31.863  13.853  47.024  1.00 16.03           C  
ANISOU 3460  CA  LEU B 320     2084   1307   2698    106    131   -165       C  
ATOM   3461  C   LEU B 320      32.992  14.810  46.647  1.00 19.48           C  
ANISOU 3461  C   LEU B 320     2573   1677   3150     54    160   -148       C  
ATOM   3462  O   LEU B 320      32.856  16.031  46.778  1.00 20.70           O  
ANISOU 3462  O   LEU B 320     2757   1734   3376     61    176   -155       O  
ATOM   3463  CB  LEU B 320      31.660  13.839  48.543  1.00 18.59           C  
ANISOU 3463  CB  LEU B 320     2367   1653   3044    104    162   -260       C  
ATOM   3464  CG  LEU B 320      30.464  12.999  48.993  1.00 24.14           C  
ANISOU 3464  CG  LEU B 320     3019   2411   3741    149    150   -283       C  
ATOM   3465  CD1 LEU B 320      30.372  12.942  50.516  1.00 28.47           C  
ANISOU 3465  CD1 LEU B 320     3541   2987   4290    136    192   -375       C  
ATOM   3466  CD2 LEU B 320      29.159  13.518  48.381  1.00 28.35           C  
ANISOU 3466  CD2 LEU B 320     3538   2890   4344    219    118   -249       C  
ATOM   3467  N   HIS B 321      34.100  14.248  46.176  1.00 15.13           N  
ANISOU 3467  N   HIS B 321     2033   1176   2538      0    171   -127       N  
ATOM   3468  CA  HIS B 321      35.256  15.030  45.759  1.00 20.28           C  
ANISOU 3468  CA  HIS B 321     2727   1778   3201    -64    209   -113       C  
ATOM   3469  C   HIS B 321      35.271  15.339  44.261  1.00 27.46           C  
ANISOU 3469  C   HIS B 321     3704   2639   4091    -64    201    -14       C  
ATOM   3470  O   HIS B 321      36.278  15.808  43.731  1.00 31.88           O  
ANISOU 3470  O   HIS B 321     4301   3166   4644   -126    241      8       O  
ATOM   3471  CB  HIS B 321      36.541  14.308  46.167  1.00 19.64           C  
ANISOU 3471  CB  HIS B 321     2608   1780   3073   -126    233   -158       C  
ATOM   3472  CG  HIS B 321      36.759  14.284  47.645  1.00 21.79           C  
ANISOU 3472  CG  HIS B 321     2832   2086   3360   -139    241   -253       C  
ATOM   3473  ND1 HIS B 321      37.767  14.995  48.259  1.00 23.86           N  
ANISOU 3473  ND1 HIS B 321     3085   2328   3652   -202    273   -312       N  
ATOM   3474  CD2 HIS B 321      36.071  13.669  48.638  1.00 21.12           C  
ANISOU 3474  CD2 HIS B 321     2712   2053   3261   -101    223   -300       C  
ATOM   3475  CE1 HIS B 321      37.699  14.808  49.566  1.00 24.54           C  
ANISOU 3475  CE1 HIS B 321     3134   2456   3733   -199    266   -392       C  
ATOM   3476  NE2 HIS B 321      36.678  14.010  49.821  1.00 21.56           N  
ANISOU 3476  NE2 HIS B 321     2745   2120   3326   -138    240   -383       N  
ATOM   3477  N   GLN B 322      34.162  15.072  43.578  1.00 20.39           N  
ANISOU 3477  N   GLN B 322     2824   1741   3182      1    149     43       N  
ATOM   3478  CA  GLN B 322      34.069  15.401  42.156  1.00 30.87           C  
ANISOU 3478  CA  GLN B 322     4228   3023   4479      8    130    142       C  
ATOM   3479  C   GLN B 322      33.951  16.901  41.903  1.00 40.30           C  
ANISOU 3479  C   GLN B 322     5489   4081   5741     16    142    181       C  
ATOM   3480  O   GLN B 322      33.226  17.602  42.609  1.00 41.09           O  
ANISOU 3480  O   GLN B 322     5572   4118   5921     62    132    148       O  
ATOM   3481  CB  GLN B 322      32.871  14.713  41.522  1.00 35.24           C  
ANISOU 3481  CB  GLN B 322     4774   3615   4999     78     58    187       C  
ATOM   3482  CG  GLN B 322      32.979  13.224  41.425  1.00 35.65           C  
ANISOU 3482  CG  GLN B 322     4785   3786   4976     66     47    169       C  
ATOM   3483  CD  GLN B 322      31.757  12.638  40.765  1.00 35.33           C  
ANISOU 3483  CD  GLN B 322     4737   3777   4908    126    -26    207       C  
ATOM   3484  OE1 GLN B 322      31.769  12.353  39.564  1.00 30.04           O  
ANISOU 3484  OE1 GLN B 322     4122   3123   4171    122    -55    272       O  
ATOM   3485  NE2 GLN B 322      30.673  12.492  41.538  1.00 27.08           N  
ANISOU 3485  NE2 GLN B 322     3626   2744   3918    179    -56    164       N  
ATOM   3486  N   GLN B 323      34.642  17.384  40.874  1.00 46.84           N  
ANISOU 3486  N   GLN B 323     6401   4860   6537    -30    169    252       N  
ATOM   3487  CA  GLN B 323      34.585  18.797  40.509  1.00 55.42           C  
ANISOU 3487  CA  GLN B 323     7570   5809   7677    -28    182    302       C  
ATOM   3488  C   GLN B 323      34.155  19.005  39.055  1.00 59.80           C  
ANISOU 3488  C   GLN B 323     8220   6328   8174      3    136    423       C  
ATOM   3489  O   GLN B 323      34.998  19.066  38.159  1.00 62.70           O  
ANISOU 3489  O   GLN B 323     8650   6697   8475    -63    172    475       O  
ATOM   3490  CB  GLN B 323      35.939  19.466  40.753  1.00 56.52           C  
ANISOU 3490  CB  GLN B 323     7722   5928   7823   -130    256    265       C  
ATOM   3491  N   PRO B 324      32.835  19.096  38.813  1.00 58.62           N  
ANISOU 3491  N   PRO B 324     8074   6157   8043    103     52    463       N  
ATOM   3492  CA  PRO B 324      31.769  18.844  39.787  1.00 52.99           C  
ANISOU 3492  CA  PRO B 324     7267   5471   7398    180     11    395       C  
ATOM   3493  C   PRO B 324      31.179  17.452  39.576  1.00 41.58           C  
ANISOU 3493  C   PRO B 324     5757   4150   5893    211    -44    390       C  
ATOM   3494  O   PRO B 324      31.770  16.662  38.842  1.00 42.51           O  
ANISOU 3494  O   PRO B 324     5901   4339   5914    163    -37    420       O  
ATOM   3495  CB  PRO B 324      30.734  19.905  39.429  1.00 56.70           C  
ANISOU 3495  CB  PRO B 324     7786   5863   7896    267    -45    440       C  
ATOM   3496  CG  PRO B 324      30.856  20.020  37.940  1.00 60.84           C  
ANISOU 3496  CG  PRO B 324     8419   6361   8335    266    -73    558       C  
ATOM   3497  CD  PRO B 324      32.306  19.723  37.589  1.00 60.80           C  
ANISOU 3497  CD  PRO B 324     8439   6376   8286    143    -14    572       C  
ATOM   3498  N   ALA B 325      30.032  17.170  40.194  1.00 37.39           N  
ANISOU 3498  N   ALA B 325     5145   3648   5415    284    -92    346       N  
ATOM   3499  CA  ALA B 325      29.422  15.838  40.146  1.00 39.90           C  
ANISOU 3499  CA  ALA B 325     5392   4087   5682    303   -138    323       C  
ATOM   3500  C   ALA B 325      29.142  15.375  38.721  1.00 33.71           C  
ANISOU 3500  C   ALA B 325     4663   3338   4808    317   -206    412       C  
ATOM   3501  O   ALA B 325      28.618  16.133  37.908  1.00 30.74           O  
ANISOU 3501  O   ALA B 325     4348   2892   4441    369   -263    492       O  
ATOM   3502  CB  ALA B 325      28.144  15.811  40.968  1.00 40.40           C  
ANISOU 3502  CB  ALA B 325     5361   4158   5829    379   -172    267       C  
ATOM   3503  N   ASN B 326      29.500  14.128  38.433  1.00 26.42           N  
ANISOU 3503  N   ASN B 326     3723   2520   3797    273   -201    397       N  
ATOM   3504  CA  ASN B 326      29.287  13.531  37.120  1.00 26.81           C  
ANISOU 3504  CA  ASN B 326     3823   2616   3746    275   -261    465       C  
ATOM   3505  C   ASN B 326      28.712  12.136  37.301  1.00 24.62           C  
ANISOU 3505  C   ASN B 326     3466   2451   3437    279   -292    411       C  
ATOM   3506  O   ASN B 326      29.401  11.240  37.775  1.00 20.14           O  
ANISOU 3506  O   ASN B 326     2869   1946   2838    225   -236    356       O  
ATOM   3507  CB  ASN B 326      30.613  13.464  36.348  1.00 26.62           C  
ANISOU 3507  CB  ASN B 326     3890   2593   3630    194   -199    505       C  
ATOM   3508  CG  ASN B 326      30.442  13.005  34.907  1.00 25.73           C  
ANISOU 3508  CG  ASN B 326     3855   2519   3403    193   -253    579       C  
ATOM   3509  OD1 ASN B 326      29.803  11.992  34.632  1.00 27.21           O  
ANISOU 3509  OD1 ASN B 326     4004   2789   3546    210   -309    561       O  
ATOM   3510  ND2 ASN B 326      31.028  13.754  33.976  1.00 24.52           N  
ANISOU 3510  ND2 ASN B 326     3817   2303   3196    165   -233    661       N  
ATOM   3511  N   CYS B 327      27.452  11.947  36.926  1.00 26.70           N  
ANISOU 3511  N   CYS B 327     3695   2738   3714    342   -384    427       N  
ATOM   3512  CA  CYS B 327      26.789  10.668  37.171  1.00 29.16           C  
ANISOU 3512  CA  CYS B 327     3923   3147   4010    340   -411    368       C  
ATOM   3513  C   CYS B 327      27.333   9.521  36.319  1.00 23.15           C  
ANISOU 3513  C   CYS B 327     3207   2461   3128    283   -408    378       C  
ATOM   3514  O   CYS B 327      27.254   8.358  36.716  1.00 21.23           O  
ANISOU 3514  O   CYS B 327     2909   2290   2868    255   -391    318       O  
ATOM   3515  CB  CYS B 327      25.271  10.802  37.025  1.00 38.68           C  
ANISOU 3515  CB  CYS B 327     5062   4359   5274    419   -509    372       C  
ATOM   3516  SG  CYS B 327      24.507  11.758  38.361  1.00 75.95           S  
ANISOU 3516  SG  CYS B 327     9690   9014  10154    485   -489    317       S  
ATOM   3517  N   LYS B 328      27.888   9.844  35.155  1.00 20.13           N  
ANISOU 3517  N   LYS B 328     2929   2059   2661    263   -420    452       N  
ATOM   3518  CA  LYS B 328      28.524   8.826  34.325  1.00 19.57           C  
ANISOU 3518  CA  LYS B 328     2910   2053   2472    204   -401    456       C  
ATOM   3519  C   LYS B 328      29.791   8.303  35.003  1.00 18.14           C  
ANISOU 3519  C   LYS B 328     2716   1890   2284    141   -291    402       C  
ATOM   3520  O   LYS B 328      30.043   7.099  35.019  1.00 17.09           O  
ANISOU 3520  O   LYS B 328     2562   1825   2106    109   -268    356       O  
ATOM   3521  CB  LYS B 328      28.843   9.393  32.936  1.00 30.04           C  
ANISOU 3521  CB  LYS B 328     4361   3349   3702    195   -428    550       C  
ATOM   3522  CG  LYS B 328      29.019   8.346  31.856  1.00 35.63           C  
ANISOU 3522  CG  LYS B 328     5124   4133   4280    154   -444    555       C  
ATOM   3523  CD  LYS B 328      29.188   8.986  30.469  1.00 41.62           C  
ANISOU 3523  CD  LYS B 328     6017   4862   4933    149   -479    654       C  
ATOM   3524  CE  LYS B 328      27.888   9.581  29.949  1.00 49.29           C  
ANISOU 3524  CE  LYS B 328     7000   5815   5913    227   -616    714       C  
ATOM   3525  NZ  LYS B 328      28.039  10.143  28.567  1.00 54.24           N  
ANISOU 3525  NZ  LYS B 328     7756   6426   6426    221   -645    807       N  
ATOM   3526  N   VAL B 329      30.585   9.209  35.566  1.00 15.66           N  
ANISOU 3526  N   VAL B 329     2415   1515   2022    126   -226    405       N  
ATOM   3527  CA  VAL B 329      31.766   8.798  36.332  1.00 14.60           C  
ANISOU 3527  CA  VAL B 329     2252   1401   1896     73   -133    348       C  
ATOM   3528  C   VAL B 329      31.371   7.905  37.506  1.00 15.64           C  
ANISOU 3528  C   VAL B 329     2287   1583   2073     86   -130    268       C  
ATOM   3529  O   VAL B 329      32.008   6.877  37.759  1.00 13.61           O  
ANISOU 3529  O   VAL B 329     2009   1380   1782     53    -88    226       O  
ATOM   3530  CB  VAL B 329      32.580  10.013  36.837  1.00 14.50           C  
ANISOU 3530  CB  VAL B 329     2256   1311   1942     51    -73    355       C  
ATOM   3531  CG1 VAL B 329      33.654   9.577  37.834  1.00 14.28           C  
ANISOU 3531  CG1 VAL B 329     2174   1315   1937      7      3    283       C  
ATOM   3532  CG2 VAL B 329      33.208  10.775  35.655  1.00 14.20           C  
ANISOU 3532  CG2 VAL B 329     2326   1222   1846     18    -51    434       C  
ATOM   3533  N   GLU B 330      30.319   8.289  38.225  1.00 17.62           N  
ANISOU 3533  N   GLU B 330     2481   1813   2402    135   -169    249       N  
ATOM   3534  CA  GLU B 330      29.879   7.487  39.368  1.00 13.92           C  
ANISOU 3534  CA  GLU B 330     1929   1389   1973    142   -158    176       C  
ATOM   3535  C   GLU B 330      29.446   6.089  38.936  1.00 12.18           C  
ANISOU 3535  C   GLU B 330     1694   1240   1693    131   -184    159       C  
ATOM   3536  O   GLU B 330      29.848   5.097  39.540  1.00 12.23           O  
ANISOU 3536  O   GLU B 330     1674   1288   1684    105   -143    112       O  
ATOM   3537  CB  GLU B 330      28.757   8.194  40.144  1.00 14.83           C  
ANISOU 3537  CB  GLU B 330     1984   1468   2183    195   -187    154       C  
ATOM   3538  CG  GLU B 330      29.162   9.547  40.706  1.00 18.38           C  
ANISOU 3538  CG  GLU B 330     2448   1837   2698    205   -153    156       C  
ATOM   3539  CD  GLU B 330      28.093  10.159  41.604  1.00 26.57           C  
ANISOU 3539  CD  GLU B 330     3420   2840   3834    259   -166    118       C  
ATOM   3540  OE1 GLU B 330      27.048   9.511  41.827  1.00 26.48           O  
ANISOU 3540  OE1 GLU B 330     3345   2874   3842    285   -198     88       O  
ATOM   3541  OE2 GLU B 330      28.304  11.287  42.086  1.00 26.80           O  
ANISOU 3541  OE2 GLU B 330     3461   2796   3925    271   -140    112       O  
ATOM   3542  N   SER B 331      28.644   6.005  37.880  1.00 13.16           N  
ANISOU 3542  N   SER B 331     1840   1377   1784    151   -256    197       N  
ATOM   3543  CA  SER B 331      28.190   4.703  37.394  1.00 14.27           C  
ANISOU 3543  CA  SER B 331     1970   1583   1869    133   -285    175       C  
ATOM   3544  C   SER B 331      29.331   3.811  36.928  1.00 13.02           C  
ANISOU 3544  C   SER B 331     1866   1457   1626     82   -231    169       C  
ATOM   3545  O   SER B 331      29.334   2.604  37.185  1.00 12.52           O  
ANISOU 3545  O   SER B 331     1780   1435   1542     60   -211    123       O  
ATOM   3546  CB  SER B 331      27.184   4.867  36.252  1.00 15.81           C  
ANISOU 3546  CB  SER B 331     2184   1790   2034    161   -383    218       C  
ATOM   3547  OG  SER B 331      25.961   5.384  36.745  1.00 19.96           O  
ANISOU 3547  OG  SER B 331     2633   2302   2650    214   -437    206       O  
ATOM   3548  N   LEU B 332      30.286   4.404  36.225  1.00 12.86           N  
ANISOU 3548  N   LEU B 332     1917   1411   1559     62   -203    214       N  
ATOM   3549  CA  LEU B 332      31.432   3.647  35.721  1.00  9.70           C  
ANISOU 3549  CA  LEU B 332     1562   1038   1084     16   -143    204       C  
ATOM   3550  C   LEU B 332      32.326   3.187  36.870  1.00 10.19           C  
ANISOU 3550  C   LEU B 332     1576   1108   1186      2    -70    151       C  
ATOM   3551  O   LEU B 332      32.853   2.067  36.842  1.00 10.58           O  
ANISOU 3551  O   LEU B 332     1627   1194   1199    -18    -35    116       O  
ATOM   3552  CB  LEU B 332      32.237   4.482  34.712  1.00 11.37           C  
ANISOU 3552  CB  LEU B 332     1859   1220   1240     -7   -119    265       C  
ATOM   3553  CG  LEU B 332      33.426   3.765  34.069  1.00 12.23           C  
ANISOU 3553  CG  LEU B 332     2014   1359   1272    -55    -47    252       C  
ATOM   3554  CD1 LEU B 332      32.953   2.481  33.396  1.00 13.78           C  
ANISOU 3554  CD1 LEU B 332     2228   1611   1398    -63    -76    226       C  
ATOM   3555  CD2 LEU B 332      34.143   4.656  33.041  1.00 12.23           C  
ANISOU 3555  CD2 LEU B 332     2104   1329   1215    -87    -13    314       C  
ATOM   3556  N   ALA B 333      32.479   4.026  37.895  1.00 12.08           N  
ANISOU 3556  N   ALA B 333     1777   1313   1501     15    -51    141       N  
ATOM   3557  CA  ALA B 333      33.263   3.616  39.059  1.00 10.09           C  
ANISOU 3557  CA  ALA B 333     1479   1074   1281      6      3     90       C  
ATOM   3558  C   ALA B 333      32.595   2.442  39.774  1.00  9.89           C  
ANISOU 3558  C   ALA B 333     1410   1084   1262     18     -9     45       C  
ATOM   3559  O   ALA B 333      33.269   1.501  40.186  1.00  9.82           O  
ANISOU 3559  O   ALA B 333     1393   1102   1237      7     27     13       O  
ATOM   3560  CB  ALA B 333      33.482   4.795  40.031  1.00 11.72           C  
ANISOU 3560  CB  ALA B 333     1656   1236   1559     13     19     82       C  
ATOM   3561  N   MET B 334      31.272   2.502  39.925  1.00  9.87           N  
ANISOU 3561  N   MET B 334     1379   1079   1290     42    -59     43       N  
ATOM   3562  CA AMET B 334      30.535   1.401  40.544  0.51 11.88           C  
ANISOU 3562  CA AMET B 334     1596   1365   1553     43    -63      1       C  
ATOM   3563  CA BMET B 334      30.527   1.405  40.539  0.49 11.90           C  
ANISOU 3563  CA BMET B 334     1599   1368   1556     43    -63      1       C  
ATOM   3564  C   MET B 334      30.667   0.123  39.732  1.00 11.56           C  
ANISOU 3564  C   MET B 334     1589   1356   1446     19    -63     -6       C  
ATOM   3565  O   MET B 334      30.834  -0.965  40.287  1.00 11.86           O  
ANISOU 3565  O   MET B 334     1620   1411   1477      9    -32    -40       O  
ATOM   3566  CB AMET B 334      29.061   1.766  40.721  0.51 14.69           C  
ANISOU 3566  CB AMET B 334     1905   1715   1961     68   -113     -4       C  
ATOM   3567  CB BMET B 334      29.046   1.756  40.674  0.49 13.65           C  
ANISOU 3567  CB BMET B 334     1775   1584   1828     68   -115     -3       C  
ATOM   3568  CG AMET B 334      28.823   2.854  41.758  0.51 18.41           C  
ANISOU 3568  CG AMET B 334     2336   2153   2508     94   -100    -16       C  
ATOM   3569  CG BMET B 334      28.746   2.754  41.781  0.49 18.16           C  
ANISOU 3569  CG BMET B 334     2301   2124   2475     93   -101    -19       C  
ATOM   3570  SD AMET B 334      27.071   3.099  42.109  0.51 31.13           S  
ANISOU 3570  SD AMET B 334     3871   3763   4192    127   -144    -39       S  
ATOM   3571  SD BMET B 334      29.109   2.120  43.432  0.49 23.72           S  
ANISOU 3571  SD BMET B 334     2975   2841   3195     80    -36    -75       S  
ATOM   3572  CE AMET B 334      26.547   3.994  40.648  0.51 37.70           C  
ANISOU 3572  CE AMET B 334     4728   4574   5021    161   -229     23       C  
ATOM   3573  CE BMET B 334      28.364   0.490  43.382  0.49 18.99           C  
ANISOU 3573  CE BMET B 334     2365   2284   2567     57    -38   -102       C  
ATOM   3574  N   PHE B 335      30.591   0.264  38.415  1.00 11.78           N  
ANISOU 3574  N   PHE B 335     1663   1390   1423     11    -95     27       N  
ATOM   3575  CA  PHE B 335      30.761  -0.858  37.500  1.00 10.80           C  
ANISOU 3575  CA  PHE B 335     1582   1295   1227    -15    -93     16       C  
ATOM   3576  C   PHE B 335      32.118  -1.526  37.713  1.00 12.13           C  
ANISOU 3576  C   PHE B 335     1770   1466   1371    -29    -20     -4       C  
ATOM   3577  O   PHE B 335      32.206  -2.744  37.867  1.00 10.92           O  
ANISOU 3577  O   PHE B 335     1620   1325   1202    -38      2    -40       O  
ATOM   3578  CB  PHE B 335      30.625  -0.346  36.064  1.00 12.37           C  
ANISOU 3578  CB  PHE B 335     1840   1498   1363    -22   -136     61       C  
ATOM   3579  CG  PHE B 335      31.048  -1.329  35.011  1.00 14.02           C  
ANISOU 3579  CG  PHE B 335     2109   1734   1483    -54   -121     48       C  
ATOM   3580  CD1 PHE B 335      30.356  -2.518  34.828  1.00 13.51           C  
ANISOU 3580  CD1 PHE B 335     2040   1696   1398    -72   -143      5       C  
ATOM   3581  CD2 PHE B 335      32.126  -1.047  34.180  1.00 17.54           C  
ANISOU 3581  CD2 PHE B 335     2620   2178   1868    -73    -77     73       C  
ATOM   3582  CE1 PHE B 335      30.739  -3.413  33.846  1.00 15.37           C  
ANISOU 3582  CE1 PHE B 335     2337   1951   1552   -103   -125    -15       C  
ATOM   3583  CE2 PHE B 335      32.510  -1.939  33.192  1.00 17.98           C  
ANISOU 3583  CE2 PHE B 335     2734   2259   1839   -103    -54     54       C  
ATOM   3584  CZ  PHE B 335      31.812  -3.121  33.022  1.00 15.18           C  
ANISOU 3584  CZ  PHE B 335     2378   1927   1463   -116    -80      8       C  
ATOM   3585  N   LEU B 336      33.176  -0.721  37.729  1.00 10.99           N  
ANISOU 3585  N   LEU B 336     1637   1308   1232    -29     17     16       N  
ATOM   3586  CA  LEU B 336      34.525  -1.253  37.891  1.00 13.48           C  
ANISOU 3586  CA  LEU B 336     1955   1631   1534    -37     82     -6       C  
ATOM   3587  C   LEU B 336      34.710  -1.893  39.261  1.00 14.96           C  
ANISOU 3587  C   LEU B 336     2096   1820   1767    -18    100    -42       C  
ATOM   3588  O   LEU B 336      35.349  -2.933  39.371  1.00 12.86           O  
ANISOU 3588  O   LEU B 336     1835   1565   1486    -14    133    -69       O  
ATOM   3589  CB  LEU B 336      35.567  -0.158  37.656  1.00 14.74           C  
ANISOU 3589  CB  LEU B 336     2124   1777   1701    -50    118     20       C  
ATOM   3590  CG  LEU B 336      35.559   0.435  36.246  1.00 13.05           C  
ANISOU 3590  CG  LEU B 336     1976   1556   1426    -74    113     64       C  
ATOM   3591  CD1 LEU B 336      36.494   1.640  36.175  1.00 13.12           C  
ANISOU 3591  CD1 LEU B 336     1993   1538   1454    -94    156     91       C  
ATOM   3592  CD2 LEU B 336      35.958  -0.620  35.201  1.00 14.87           C  
ANISOU 3592  CD2 LEU B 336     2255   1816   1578    -95    144     48       C  
ATOM   3593  N   GLY B 337      34.147  -1.277  40.302  1.00 11.12           N  
ANISOU 3593  N   GLY B 337     1570   1322   1334     -4     80    -44       N  
ATOM   3594  CA  GLY B 337      34.197  -1.868  41.634  1.00 13.05           C  
ANISOU 3594  CA  GLY B 337     1783   1570   1607     12     93    -75       C  
ATOM   3595  C   GLY B 337      33.490  -3.212  41.711  1.00 14.30           C  
ANISOU 3595  C   GLY B 337     1954   1734   1747      9     90    -95       C  
ATOM   3596  O   GLY B 337      33.933  -4.136  42.407  1.00 11.72           O  
ANISOU 3596  O   GLY B 337     1630   1408   1417     20    115   -113       O  
ATOM   3597  N   GLU B 338      32.389  -3.334  40.978  1.00 11.49           N  
ANISOU 3597  N   GLU B 338     1606   1380   1379     -5     56    -90       N  
ATOM   3598  CA  GLU B 338      31.659  -4.592  40.946  1.00 12.00           C  
ANISOU 3598  CA  GLU B 338     1682   1447   1430    -20     54   -115       C  
ATOM   3599  C   GLU B 338      32.429  -5.673  40.203  1.00  9.82           C  
ANISOU 3599  C   GLU B 338     1455   1172   1106    -29     83   -128       C  
ATOM   3600  O   GLU B 338      32.459  -6.828  40.635  1.00 10.74           O  
ANISOU 3600  O   GLU B 338     1587   1275   1220    -30    108   -151       O  
ATOM   3601  CB  GLU B 338      30.269  -4.392  40.332  1.00 14.63           C  
ANISOU 3601  CB  GLU B 338     1999   1790   1769    -37      2   -115       C  
ATOM   3602  CG  GLU B 338      29.160  -4.851  41.257  1.00 24.31           C  
ANISOU 3602  CG  GLU B 338     3184   3013   3038    -47      2   -143       C  
ATOM   3603  CD  GLU B 338      27.785  -4.428  40.791  1.00 15.45           C  
ANISOU 3603  CD  GLU B 338     2020   1908   1944    -56    -55   -147       C  
ATOM   3604  OE1 GLU B 338      27.141  -5.222  40.070  1.00 17.57           O  
ANISOU 3604  OE1 GLU B 338     2296   2190   2191    -86    -80   -168       O  
ATOM   3605  OE2 GLU B 338      27.347  -3.311  41.152  1.00 17.64           O  
ANISOU 3605  OE2 GLU B 338     2253   2182   2268    -31    -76   -134       O  
ATOM   3606  N   LEU B 339      33.066  -5.303  39.092  1.00  9.80           N  
ANISOU 3606  N   LEU B 339     1481   1179   1064    -34     86   -113       N  
ATOM   3607  CA  LEU B 339      33.877  -6.260  38.346  1.00 12.14           C  
ANISOU 3607  CA  LEU B 339     1822   1476   1315    -40    124   -133       C  
ATOM   3608  C   LEU B 339      34.935  -6.899  39.242  1.00 12.47           C  
ANISOU 3608  C   LEU B 339     1852   1505   1382    -10    171   -149       C  
ATOM   3609  O   LEU B 339      35.249  -8.071  39.082  1.00 13.40           O  
ANISOU 3609  O   LEU B 339     1999   1608   1484     -5    200   -175       O  
ATOM   3610  CB  LEU B 339      34.566  -5.605  37.150  1.00 11.94           C  
ANISOU 3610  CB  LEU B 339     1828   1464   1243    -53    137   -114       C  
ATOM   3611  CG  LEU B 339      33.715  -5.219  35.935  1.00 13.78           C  
ANISOU 3611  CG  LEU B 339     2100   1712   1423    -80     89    -96       C  
ATOM   3612  CD1 LEU B 339      34.657  -4.713  34.839  1.00 13.99           C  
ANISOU 3612  CD1 LEU B 339     2173   1749   1392    -95    123    -76       C  
ATOM   3613  CD2 LEU B 339      32.877  -6.404  35.432  1.00 12.93           C  
ANISOU 3613  CD2 LEU B 339     2021   1611   1282   -104     67   -133       C  
ATOM   3614  N   SER B 340      35.477  -6.126  40.181  1.00 11.45           N  
ANISOU 3614  N   SER B 340     1680   1378   1290     12    174   -135       N  
ATOM   3615  CA  SER B 340      36.512  -6.643  41.082  1.00 10.42           C  
ANISOU 3615  CA  SER B 340     1533   1243   1182     47    203   -148       C  
ATOM   3616  C   SER B 340      36.020  -7.789  41.981  1.00 12.17           C  
ANISOU 3616  C   SER B 340     1772   1442   1412     61    202   -159       C  
ATOM   3617  O   SER B 340      36.817  -8.616  42.426  1.00 13.56           O  
ANISOU 3617  O   SER B 340     1955   1604   1591     96    224   -169       O  
ATOM   3618  CB  SER B 340      37.111  -5.522  41.944  1.00 12.48           C  
ANISOU 3618  CB  SER B 340     1745   1517   1478     60    196   -137       C  
ATOM   3619  OG  SER B 340      36.284  -5.221  43.063  1.00 13.22           O  
ANISOU 3619  OG  SER B 340     1823   1606   1596     62    169   -133       O  
ATOM   3620  N   LEU B 341      34.717  -7.831  42.248  1.00 10.06           N  
ANISOU 3620  N   LEU B 341     1509   1166   1148     36    180   -158       N  
ATOM   3621  CA  LEU B 341      34.134  -8.871  43.096  1.00 10.74           C  
ANISOU 3621  CA  LEU B 341     1616   1224   1239     36    189   -167       C  
ATOM   3622  C   LEU B 341      34.222 -10.249  42.447  1.00 13.77           C  
ANISOU 3622  C   LEU B 341     2052   1578   1601     31    215   -187       C  
ATOM   3623  O   LEU B 341      34.239 -11.262  43.135  1.00 11.64           O  
ANISOU 3623  O   LEU B 341     1816   1273   1336     44    235   -190       O  
ATOM   3624  CB  LEU B 341      32.656  -8.571  43.370  1.00 12.90           C  
ANISOU 3624  CB  LEU B 341     1872   1501   1529      0    168   -169       C  
ATOM   3625  CG  LEU B 341      32.289  -7.268  44.091  1.00 12.52           C  
ANISOU 3625  CG  LEU B 341     1774   1472   1511      4    148   -158       C  
ATOM   3626  CD1 LEU B 341      30.779  -7.068  44.091  1.00 14.10           C  
ANISOU 3626  CD1 LEU B 341     1947   1675   1735    -28    131   -169       C  
ATOM   3627  CD2 LEU B 341      32.835  -7.266  45.511  1.00 14.80           C  
ANISOU 3627  CD2 LEU B 341     2061   1756   1805     31    165   -153       C  
ATOM   3628  N   ILE B 342      34.236 -10.284  41.116  1.00 11.47           N  
ANISOU 3628  N   ILE B 342     1779   1297   1284     10    215   -202       N  
ATOM   3629  CA  ILE B 342      34.179 -11.553  40.398  1.00 13.93           C  
ANISOU 3629  CA  ILE B 342     2145   1578   1572     -5    240   -232       C  
ATOM   3630  C   ILE B 342      35.474 -12.352  40.509  1.00 14.64           C  
ANISOU 3630  C   ILE B 342     2258   1640   1665     45    282   -242       C  
ATOM   3631  O   ILE B 342      35.445 -13.576  40.597  1.00 14.41           O  
ANISOU 3631  O   ILE B 342     2276   1563   1638     51    308   -261       O  
ATOM   3632  CB  ILE B 342      33.866 -11.334  38.898  1.00 12.35           C  
ANISOU 3632  CB  ILE B 342     1963   1401   1328    -43    226   -250       C  
ATOM   3633  CG1 ILE B 342      32.530 -10.617  38.729  1.00 14.33           C  
ANISOU 3633  CG1 ILE B 342     2187   1679   1581    -83    171   -241       C  
ATOM   3634  CG2 ILE B 342      33.847 -12.658  38.151  1.00 16.38           C  
ANISOU 3634  CG2 ILE B 342     2534   1879   1810    -62    256   -294       C  
ATOM   3635  CD1 ILE B 342      31.314 -11.478  39.124  1.00 15.26           C  
ANISOU 3635  CD1 ILE B 342     2308   1773   1716   -121    163   -267       C  
ATOM   3636  N   ASP B 343      36.607 -11.654  40.502  1.00 13.80           N  
ANISOU 3636  N   ASP B 343     2115   1561   1566     81    290   -231       N  
ATOM   3637  CA  ASP B 343      37.911 -12.298  40.343  1.00 17.11           C  
ANISOU 3637  CA  ASP B 343     2539   1967   1995    130    330   -248       C  
ATOM   3638  C   ASP B 343      38.762 -12.209  41.607  1.00 15.47           C  
ANISOU 3638  C   ASP B 343     2292   1761   1825    189    321   -228       C  
ATOM   3639  O   ASP B 343      39.416 -11.198  41.843  1.00 13.90           O  
ANISOU 3639  O   ASP B 343     2037   1603   1642    200    309   -217       O  
ATOM   3640  CB  ASP B 343      38.651 -11.645  39.165  1.00 16.97           C  
ANISOU 3640  CB  ASP B 343     2505   1986   1955    118    356   -262       C  
ATOM   3641  CG  ASP B 343      37.889 -11.770  37.851  1.00 21.64           C  
ANISOU 3641  CG  ASP B 343     3148   2582   2493     62    359   -281       C  
ATOM   3642  OD1 ASP B 343      37.485 -12.901  37.518  1.00 19.35           O  
ANISOU 3642  OD1 ASP B 343     2909   2255   2188     52    375   -313       O  
ATOM   3643  OD2 ASP B 343      37.695 -10.743  37.156  1.00 22.53           O  
ANISOU 3643  OD2 ASP B 343     3253   2732   2576     28    344   -266       O  
ATOM   3644  N   ALA B 344      38.754 -13.273  42.410  1.00 17.30           N  
ANISOU 3644  N   ALA B 344     2560   1945   2070    226    323   -222       N  
ATOM   3645  CA  ALA B 344      39.482 -13.296  43.680  1.00 18.24           C  
ANISOU 3645  CA  ALA B 344     2653   2065   2212    286    301   -198       C  
ATOM   3646  C   ALA B 344      40.974 -13.100  43.454  1.00 19.12           C  
ANISOU 3646  C   ALA B 344     2707   2205   2351    341    311   -214       C  
ATOM   3647  O   ALA B 344      41.662 -12.449  44.242  1.00 15.35           O  
ANISOU 3647  O   ALA B 344     2173   1765   1893    371    281   -202       O  
ATOM   3648  CB  ALA B 344      39.218 -14.603  44.429  1.00 19.37           C  
ANISOU 3648  CB  ALA B 344     2865   2141   2356    317    306   -184       C  
ATOM   3649  N   ASP B 345      41.467 -13.684  42.372  1.00 15.53           N  
ANISOU 3649  N   ASP B 345     2265   1735   1900    350    357   -248       N  
ATOM   3650  CA  ASP B 345      42.798 -13.385  41.882  1.00 17.37           C  
ANISOU 3650  CA  ASP B 345     2433   2004   2162    385    384   -274       C  
ATOM   3651  C   ASP B 345      42.566 -12.404  40.746  1.00 15.32           C  
ANISOU 3651  C   ASP B 345     2162   1785   1873    314    409   -286       C  
ATOM   3652  O   ASP B 345      42.012 -12.779  39.719  1.00 18.04           O  
ANISOU 3652  O   ASP B 345     2561   2111   2180    275    440   -306       O  
ATOM   3653  CB  ASP B 345      43.464 -14.663  41.373  1.00 22.49           C  
ANISOU 3653  CB  ASP B 345     3102   2611   2833    434    422   -305       C  
ATOM   3654  CG  ASP B 345      44.902 -14.446  40.949  1.00 31.66           C  
ANISOU 3654  CG  ASP B 345     4180   3813   4036    473    451   -338       C  
ATOM   3655  OD1 ASP B 345      45.350 -13.282  40.932  1.00 27.72           O  
ANISOU 3655  OD1 ASP B 345     3618   3370   3544    458    458   -340       O  
ATOM   3656  OD2 ASP B 345      45.581 -15.442  40.617  1.00 37.02           O  
ANISOU 3656  OD2 ASP B 345     4854   4466   4745    515    471   -365       O  
ATOM   3657  N   PRO B 346      43.014 -11.148  40.907  1.00 15.70           N  
ANISOU 3657  N   PRO B 346     2144   1885   1934    296    396   -276       N  
ATOM   3658  CA  PRO B 346      43.921 -10.644  41.949  1.00 16.13           C  
ANISOU 3658  CA  PRO B 346     2123   1973   2034    338    365   -270       C  
ATOM   3659  C   PRO B 346      43.289  -9.841  43.087  1.00 16.02           C  
ANISOU 3659  C   PRO B 346     2099   1973   2016    320    305   -237       C  
ATOM   3660  O   PRO B 346      44.026  -9.418  43.990  1.00 18.02           O  
ANISOU 3660  O   PRO B 346     2293   2256   2299    350    273   -237       O  
ATOM   3661  CB  PRO B 346      44.805  -9.686  41.155  1.00 18.39           C  
ANISOU 3661  CB  PRO B 346     2347   2306   2335    307    407   -292       C  
ATOM   3662  CG  PRO B 346      43.818  -9.051  40.181  1.00 18.41           C  
ANISOU 3662  CG  PRO B 346     2404   2305   2285    231    422   -277       C  
ATOM   3663  CD  PRO B 346      42.824 -10.159  39.829  1.00 19.05           C  
ANISOU 3663  CD  PRO B 346     2569   2340   2327    230    421   -278       C  
ATOM   3664  N   TYR B 347      41.983  -9.609  43.064  1.00 13.22           N  
ANISOU 3664  N   TYR B 347     1795   1600   1627    272    290   -215       N  
ATOM   3665  CA  TYR B 347      41.433  -8.542  43.913  1.00 12.15           C  
ANISOU 3665  CA  TYR B 347     1639   1484   1493    245    249   -195       C  
ATOM   3666  C   TYR B 347      41.422  -8.785  45.422  1.00 15.94           C  
ANISOU 3666  C   TYR B 347     2118   1962   1978    283    206   -180       C  
ATOM   3667  O   TYR B 347      41.342  -7.829  46.189  1.00 14.91           O  
ANISOU 3667  O   TYR B 347     1956   1856   1852    268    177   -176       O  
ATOM   3668  CB  TYR B 347      40.093  -8.002  43.372  1.00 10.23           C  
ANISOU 3668  CB  TYR B 347     1432   1231   1224    186    245   -180       C  
ATOM   3669  CG  TYR B 347      40.348  -7.400  42.020  1.00 10.68           C  
ANISOU 3669  CG  TYR B 347     1486   1303   1270    150    275   -187       C  
ATOM   3670  CD1 TYR B 347      41.082  -6.220  41.900  1.00 14.14           C  
ANISOU 3670  CD1 TYR B 347     1875   1770   1728    133    283   -186       C  
ATOM   3671  CD2 TYR B 347      39.965  -8.058  40.865  1.00 12.42           C  
ANISOU 3671  CD2 TYR B 347     1756   1508   1455    131    301   -196       C  
ATOM   3672  CE1 TYR B 347      41.381  -5.687  40.668  1.00 15.07           C  
ANISOU 3672  CE1 TYR B 347     2001   1897   1828     97    320   -186       C  
ATOM   3673  CE2 TYR B 347      40.256  -7.532  39.617  1.00 12.08           C  
ANISOU 3673  CE2 TYR B 347     1723   1482   1387     97    332   -200       C  
ATOM   3674  CZ  TYR B 347      40.964  -6.343  39.530  1.00 17.23           C  
ANISOU 3674  CZ  TYR B 347     2332   2159   2057     81    344   -191       C  
ATOM   3675  OH  TYR B 347      41.267  -5.821  38.300  1.00 19.53           O  
ANISOU 3675  OH  TYR B 347     2644   2462   2315     42    383   -188       O  
ATOM   3676  N   LEU B 348      41.553 -10.037  45.857  1.00 14.35           N  
ANISOU 3676  N   LEU B 348     1954   1727   1770    332    204   -174       N  
ATOM   3677  CA  LEU B 348      41.679 -10.291  47.293  1.00 18.18           C  
ANISOU 3677  CA  LEU B 348     2448   2212   2247    373    161   -154       C  
ATOM   3678  C   LEU B 348      42.954  -9.678  47.877  1.00 18.53           C  
ANISOU 3678  C   LEU B 348     2414   2308   2318    411    125   -167       C  
ATOM   3679  O   LEU B 348      43.054  -9.481  49.086  1.00 19.87           O  
ANISOU 3679  O   LEU B 348     2582   2495   2473    431     79   -156       O  
ATOM   3680  CB  LEU B 348      41.632 -11.794  47.610  1.00 18.67           C  
ANISOU 3680  CB  LEU B 348     2579   2218   2299    424    165   -137       C  
ATOM   3681  CG  LEU B 348      40.274 -12.480  47.494  1.00 21.57           C  
ANISOU 3681  CG  LEU B 348     3027   2530   2637    381    191   -123       C  
ATOM   3682  CD1 LEU B 348      40.370 -13.923  47.993  1.00 25.69           C  
ANISOU 3682  CD1 LEU B 348     3624   2987   3151    433    196   -101       C  
ATOM   3683  CD2 LEU B 348      39.218 -11.708  48.266  1.00 26.53           C  
ANISOU 3683  CD2 LEU B 348     3662   3175   3242    329    176   -109       C  
ATOM   3684  N   LYS B 349      43.917  -9.365  47.018  1.00 17.23           N  
ANISOU 3684  N   LYS B 349     2186   2170   2191    415    150   -196       N  
ATOM   3685  CA  LYS B 349      45.162  -8.730  47.450  1.00 19.17           C  
ANISOU 3685  CA  LYS B 349     2340   2470   2473    439    121   -219       C  
ATOM   3686  C   LYS B 349      44.974  -7.301  47.945  1.00 19.09           C  
ANISOU 3686  C   LYS B 349     2294   2496   2462    383     98   -226       C  
ATOM   3687  O   LYS B 349      45.828  -6.788  48.665  1.00 19.68           O  
ANISOU 3687  O   LYS B 349     2304   2616   2559    397     58   -246       O  
ATOM   3688  CB  LYS B 349      46.187  -8.700  46.302  1.00 20.68           C  
ANISOU 3688  CB  LYS B 349     2468   2681   2710    443    171   -255       C  
ATOM   3689  CG  LYS B 349      46.842 -10.039  46.001  1.00 32.59           C  
ANISOU 3689  CG  LYS B 349     3979   4164   4240    520    189   -265       C  
ATOM   3690  CD  LYS B 349      48.022  -9.876  45.048  1.00 40.20           C  
ANISOU 3690  CD  LYS B 349     4858   5161   5256    526    242   -311       C  
ATOM   3691  CE  LYS B 349      47.589  -9.879  43.592  1.00 41.58           C  
ANISOU 3691  CE  LYS B 349     5076   5313   5409    470    323   -323       C  
ATOM   3692  NZ  LYS B 349      48.771  -9.881  42.672  1.00 39.06           N  
ANISOU 3692  NZ  LYS B 349     4683   5022   5135    478    390   -371       N  
ATOM   3693  N   TYR B 350      43.885  -6.651  47.533  1.00 13.45           N  
ANISOU 3693  N   TYR B 350     1619   1763   1728    320    121   -215       N  
ATOM   3694  CA  TYR B 350      43.705  -5.220  47.768  1.00 12.28           C  
ANISOU 3694  CA  TYR B 350     1440   1635   1589    265    113   -225       C  
ATOM   3695  C   TYR B 350      42.578  -4.917  48.759  1.00 14.41           C  
ANISOU 3695  C   TYR B 350     1756   1892   1827    248     85   -210       C  
ATOM   3696  O   TYR B 350      41.541  -5.584  48.760  1.00 14.88           O  
ANISOU 3696  O   TYR B 350     1879   1918   1858    248     94   -187       O  
ATOM   3697  CB  TYR B 350      43.403  -4.488  46.455  1.00 12.77           C  
ANISOU 3697  CB  TYR B 350     1505   1685   1662    208    161   -224       C  
ATOM   3698  CG  TYR B 350      44.445  -4.720  45.375  1.00 14.58           C  
ANISOU 3698  CG  TYR B 350     1696   1929   1915    212    207   -242       C  
ATOM   3699  CD1 TYR B 350      45.716  -4.180  45.491  1.00 16.45           C  
ANISOU 3699  CD1 TYR B 350     1849   2206   2197    210    212   -274       C  
ATOM   3700  CD2 TYR B 350      44.146  -5.464  44.244  1.00 15.30           C  
ANISOU 3700  CD2 TYR B 350     1834   1996   1985    211    250   -235       C  
ATOM   3701  CE1 TYR B 350      46.678  -4.388  44.512  1.00 17.45           C  
ANISOU 3701  CE1 TYR B 350     1934   2348   2350    210    267   -297       C  
ATOM   3702  CE2 TYR B 350      45.100  -5.681  43.249  1.00 15.04           C  
ANISOU 3702  CE2 TYR B 350     1769   1976   1968    213    304   -258       C  
ATOM   3703  CZ  TYR B 350      46.367  -5.139  43.394  1.00 18.08           C  
ANISOU 3703  CZ  TYR B 350     2066   2401   2401    213    316   -289       C  
ATOM   3704  OH  TYR B 350      47.330  -5.346  42.420  1.00 17.41           O  
ANISOU 3704  OH  TYR B 350     1943   2334   2339    210    382   -318       O  
ATOM   3705  N   LEU B 351      42.787  -3.891  49.577  1.00 11.08           N  
ANISOU 3705  N   LEU B 351     1300   1496   1414    227     57   -229       N  
ATOM   3706  CA  LEU B 351      41.757  -3.400  50.494  1.00 10.42           C  
ANISOU 3706  CA  LEU B 351     1253   1401   1303    205     43   -226       C  
ATOM   3707  C   LEU B 351      40.661  -2.696  49.713  1.00 12.16           C  
ANISOU 3707  C   LEU B 351     1494   1589   1537    158     77   -217       C  
ATOM   3708  O   LEU B 351      40.930  -2.115  48.669  1.00 12.56           O  
ANISOU 3708  O   LEU B 351     1522   1634   1618    133    101   -217       O  
ATOM   3709  CB  LEU B 351      42.378  -2.417  51.494  1.00 14.28           C  
ANISOU 3709  CB  LEU B 351     1699   1926   1800    192      7   -261       C  
ATOM   3710  CG  LEU B 351      43.305  -3.027  52.541  1.00 18.14           C  
ANISOU 3710  CG  LEU B 351     2172   2457   2264    242    -48   -271       C  
ATOM   3711  CD1 LEU B 351      44.048  -1.934  53.311  1.00 17.22           C  
ANISOU 3711  CD1 LEU B 351     1999   2383   2161    217    -86   -318       C  
ATOM   3712  CD2 LEU B 351      42.511  -3.928  53.489  1.00 21.66           C  
ANISOU 3712  CD2 LEU B 351     2698   2886   2645    271    -64   -241       C  
ATOM   3713  N   PRO B 352      39.414  -2.733  50.224  1.00 10.80           N  
ANISOU 3713  N   PRO B 352     1364   1395   1344    148     80   -208       N  
ATOM   3714  CA  PRO B 352      38.304  -2.029  49.570  1.00 12.51           C  
ANISOU 3714  CA  PRO B 352     1590   1584   1581    113    101   -201       C  
ATOM   3715  C   PRO B 352      38.596  -0.549  49.298  1.00 10.04           C  
ANISOU 3715  C   PRO B 352     1240   1267   1309     82    103   -217       C  
ATOM   3716  O   PRO B 352      38.166  -0.043  48.264  1.00 10.71           O  
ANISOU 3716  O   PRO B 352     1329   1328   1414     63    117   -200       O  
ATOM   3717  CB  PRO B 352      37.157  -2.165  50.587  1.00 12.01           C  
ANISOU 3717  CB  PRO B 352     1557   1511   1497    109    102   -205       C  
ATOM   3718  CG  PRO B 352      37.442  -3.457  51.270  1.00 18.54           C  
ANISOU 3718  CG  PRO B 352     2419   2345   2279    140     95   -193       C  
ATOM   3719  CD  PRO B 352      38.951  -3.561  51.358  1.00 15.98           C  
ANISOU 3719  CD  PRO B 352     2066   2052   1956    170     68   -200       C  
ATOM   3720  N   SER B 353      39.315   0.130  50.190  1.00 10.60           N  
ANISOU 3720  N   SER B 353     1282   1358   1388     76     87   -248       N  
ATOM   3721  CA  SER B 353      39.583   1.558  50.002  1.00 12.83           C  
ANISOU 3721  CA  SER B 353     1536   1625   1714     40     94   -268       C  
ATOM   3722  C   SER B 353      40.500   1.781  48.803  1.00 12.66           C  
ANISOU 3722  C   SER B 353     1489   1603   1717     23    115   -256       C  
ATOM   3723  O   SER B 353      40.447   2.826  48.144  1.00 12.36           O  
ANISOU 3723  O   SER B 353     1451   1534   1713    -11    135   -250       O  
ATOM   3724  CB  SER B 353      40.209   2.175  51.261  1.00 11.51           C  
ANISOU 3724  CB  SER B 353     1342   1482   1547     30     71   -315       C  
ATOM   3725  OG  SER B 353      41.438   1.545  51.593  1.00 12.80           O  
ANISOU 3725  OG  SER B 353     1473   1694   1696     50     44   -328       O  
ATOM   3726  N   VAL B 354      41.339   0.786  48.529  1.00  7.39           N  
ANISOU 3726  N   VAL B 354      806    967   1035     47    114   -253       N  
ATOM   3727  CA  VAL B 354      42.298   0.859  47.440  1.00 10.39           C  
ANISOU 3727  CA  VAL B 354     1157   1355   1436     30    145   -250       C  
ATOM   3728  C   VAL B 354      41.612   0.534  46.122  1.00 10.49           C  
ANISOU 3728  C   VAL B 354     1218   1339   1430     25    174   -211       C  
ATOM   3729  O   VAL B 354      41.788   1.239  45.124  1.00 11.28           O  
ANISOU 3729  O   VAL B 354     1323   1420   1541    -11    206   -197       O  
ATOM   3730  CB  VAL B 354      43.485  -0.099  47.697  1.00 10.77           C  
ANISOU 3730  CB  VAL B 354     1161   1448   1482     67    135   -270       C  
ATOM   3731  CG1 VAL B 354      44.389  -0.208  46.466  1.00 11.79           C  
ANISOU 3731  CG1 VAL B 354     1261   1587   1633     53    182   -272       C  
ATOM   3732  CG2 VAL B 354      44.280   0.391  48.899  1.00 11.64           C  
ANISOU 3732  CG2 VAL B 354     1217   1596   1612     66     95   -313       C  
ATOM   3733  N   ILE B 355      40.818  -0.530  46.122  1.00  9.92           N  
ANISOU 3733  N   ILE B 355     1183   1261   1323     55    163   -194       N  
ATOM   3734  CA  ILE B 355      40.032  -0.858  44.944  1.00  9.33           C  
ANISOU 3734  CA  ILE B 355     1155   1165   1226     47    179   -164       C  
ATOM   3735  C   ILE B 355      39.109   0.310  44.579  1.00 10.76           C  
ANISOU 3735  C   ILE B 355     1356   1313   1420     18    173   -143       C  
ATOM   3736  O   ILE B 355      39.005   0.682  43.406  1.00  9.18           O  
ANISOU 3736  O   ILE B 355     1181   1097   1209     -4    189   -117       O  
ATOM   3737  CB  ILE B 355      39.212  -2.154  45.152  1.00 12.32           C  
ANISOU 3737  CB  ILE B 355     1571   1539   1573     75    167   -157       C  
ATOM   3738  CG1 ILE B 355      40.159  -3.355  45.285  1.00 14.82           C  
ANISOU 3738  CG1 ILE B 355     1879   1873   1878    112    176   -170       C  
ATOM   3739  CG2 ILE B 355      38.262  -2.371  43.993  1.00 13.46           C  
ANISOU 3739  CG2 ILE B 355     1757   1664   1694     58    172   -134       C  
ATOM   3740  CD1 ILE B 355      39.454  -4.655  45.638  1.00 14.01           C  
ANISOU 3740  CD1 ILE B 355     1820   1754   1748    138    168   -163       C  
ATOM   3741  N   ALA B 356      38.460   0.900  45.584  1.00  9.48           N  
ANISOU 3741  N   ALA B 356     1185   1139   1279     20    151   -154       N  
ATOM   3742  CA  ALA B 356      37.617   2.070  45.344  1.00 10.08           C  
ANISOU 3742  CA  ALA B 356     1272   1176   1382      4    144   -139       C  
ATOM   3743  C   ALA B 356      38.411   3.225  44.736  1.00  9.51           C  
ANISOU 3743  C   ALA B 356     1196   1082   1334    -29    166   -130       C  
ATOM   3744  O   ALA B 356      37.901   3.943  43.867  1.00  9.99           O  
ANISOU 3744  O   ALA B 356     1289   1107   1401    -41    166    -95       O  
ATOM   3745  CB  ALA B 356      36.930   2.526  46.634  1.00 11.09           C  
ANISOU 3745  CB  ALA B 356     1386   1295   1533     13    129   -166       C  
ATOM   3746  N   GLY B 357      39.646   3.409  45.198  1.00 10.62           N  
ANISOU 3746  N   GLY B 357     1299   1245   1492    -45    183   -161       N  
ATOM   3747  CA  GLY B 357      40.490   4.481  44.683  1.00 11.91           C  
ANISOU 3747  CA  GLY B 357     1454   1387   1685    -89    215   -160       C  
ATOM   3748  C   GLY B 357      40.828   4.262  43.220  1.00 14.03           C  
ANISOU 3748  C   GLY B 357     1754   1653   1925   -108    250   -123       C  
ATOM   3749  O   GLY B 357      40.712   5.168  42.377  1.00 10.84           O  
ANISOU 3749  O   GLY B 357     1388   1207   1525   -139    270    -88       O  
ATOM   3750  N   ALA B 358      41.252   3.042  42.914  1.00 10.45           N  
ANISOU 3750  N   ALA B 358     1291   1242   1438    -88    259   -130       N  
ATOM   3751  CA  ALA B 358      41.566   2.668  41.540  1.00 11.06           C  
ANISOU 3751  CA  ALA B 358     1402   1323   1477   -104    299   -105       C  
ATOM   3752  C   ALA B 358      40.335   2.797  40.637  1.00 12.46           C  
ANISOU 3752  C   ALA B 358     1651   1469   1614   -102    277    -56       C  
ATOM   3753  O   ALA B 358      40.429   3.295  39.519  1.00 10.83           O  
ANISOU 3753  O   ALA B 358     1492   1243   1380   -133    304    -21       O  
ATOM   3754  CB  ALA B 358      42.128   1.240  41.495  1.00 11.55           C  
ANISOU 3754  CB  ALA B 358     1443   1429   1516    -73    311   -131       C  
ATOM   3755  N   ALA B 359      39.179   2.357  41.127  1.00 11.62           N  
ANISOU 3755  N   ALA B 359     1554   1360   1503    -68    228    -53       N  
ATOM   3756  CA  ALA B 359      37.946   2.428  40.350  1.00 11.99           C  
ANISOU 3756  CA  ALA B 359     1651   1385   1519    -62    194    -14       C  
ATOM   3757  C   ALA B 359      37.548   3.874  40.082  1.00 12.47           C  
ANISOU 3757  C   ALA B 359     1736   1395   1605    -76    183     23       C  
ATOM   3758  O   ALA B 359      37.127   4.216  38.979  1.00 11.41           O  
ANISOU 3758  O   ALA B 359     1657   1241   1435    -84    171     69       O  
ATOM   3759  CB  ALA B 359      36.816   1.691  41.059  1.00 11.41           C  
ANISOU 3759  CB  ALA B 359     1564   1320   1450    -28    151    -29       C  
ATOM   3760  N   PHE B 360      37.659   4.720  41.101  1.00 10.98           N  
ANISOU 3760  N   PHE B 360     1513   1182   1476    -76    182      2       N  
ATOM   3761  CA  PHE B 360      37.299   6.117  40.926  1.00 11.17           C  
ANISOU 3761  CA  PHE B 360     1563   1145   1535    -85    175     34       C  
ATOM   3762  C   PHE B 360      38.232   6.803  39.936  1.00 12.29           C  
ANISOU 3762  C   PHE B 360     1747   1262   1661   -133    222     67       C  
ATOM   3763  O   PHE B 360      37.772   7.496  39.029  1.00 12.82           O  
ANISOU 3763  O   PHE B 360     1877   1284   1711   -137    212    124       O  
ATOM   3764  CB  PHE B 360      37.304   6.867  42.260  1.00 11.42           C  
ANISOU 3764  CB  PHE B 360     1552   1152   1634    -82    173     -8       C  
ATOM   3765  CG  PHE B 360      36.900   8.308  42.134  1.00 13.46           C  
ANISOU 3765  CG  PHE B 360     1841   1335   1940    -86    169     19       C  
ATOM   3766  CD1 PHE B 360      35.628   8.645  41.706  1.00 17.41           C  
ANISOU 3766  CD1 PHE B 360     2370   1798   2447    -47    124     59       C  
ATOM   3767  CD2 PHE B 360      37.800   9.321  42.415  1.00 14.49           C  
ANISOU 3767  CD2 PHE B 360     1968   1424   2111   -129    209      3       C  
ATOM   3768  CE1 PHE B 360      35.252   9.975  41.574  1.00 15.36           C  
ANISOU 3768  CE1 PHE B 360     2143   1457   2238    -39    118     88       C  
ATOM   3769  CE2 PHE B 360      37.430  10.655  42.293  1.00 20.10           C  
ANISOU 3769  CE2 PHE B 360     2717   2049   2870   -132    210     28       C  
ATOM   3770  CZ  PHE B 360      36.156  10.981  41.867  1.00 19.48           C  
ANISOU 3770  CZ  PHE B 360     2673   1928   2799    -83    164     74       C  
ATOM   3771  N   HIS B 361      39.539   6.636  40.109  1.00  9.79           N  
ANISOU 3771  N   HIS B 361     1397    973   1352   -169    276     33       N  
ATOM   3772  CA  HIS B 361      40.457   7.250  39.153  1.00 12.98           C  
ANISOU 3772  CA  HIS B 361     1836   1356   1741   -224    336     59       C  
ATOM   3773  C   HIS B 361      40.218   6.751  37.730  1.00 13.13           C  
ANISOU 3773  C   HIS B 361     1927   1385   1677   -228    345    109       C  
ATOM   3774  O   HIS B 361      40.203   7.540  36.786  1.00 15.42           O  
ANISOU 3774  O   HIS B 361     2289   1631   1939   -258    365    165       O  
ATOM   3775  CB  HIS B 361      41.918   7.009  39.502  1.00 11.86           C  
ANISOU 3775  CB  HIS B 361     1629   1255   1624   -262    395      6       C  
ATOM   3776  CG  HIS B 361      42.849   7.436  38.412  1.00 13.67           C  
ANISOU 3776  CG  HIS B 361     1890   1472   1831   -325    472     28       C  
ATOM   3777  ND1 HIS B 361      43.155   8.756  38.171  1.00 14.87           N  
ANISOU 3777  ND1 HIS B 361     2076   1560   2015   -380    511     54       N  
ATOM   3778  CD2 HIS B 361      43.489   6.722  37.451  1.00 13.46           C  
ANISOU 3778  CD2 HIS B 361     1878   1486   1753   -344    526     31       C  
ATOM   3779  CE1 HIS B 361      43.964   8.839  37.128  1.00 17.54           C  
ANISOU 3779  CE1 HIS B 361     2446   1900   2318   -436    588     73       C  
ATOM   3780  NE2 HIS B 361      44.188   7.616  36.678  1.00 14.78           N  
ANISOU 3780  NE2 HIS B 361     2082   1616   1916   -414    600     56       N  
ATOM   3781  N   LEU B 362      40.069   5.438  37.573  1.00 11.83           N  
ANISOU 3781  N   LEU B 362     1749   1277   1468   -201    332     89       N  
ATOM   3782  CA  LEU B 362      39.933   4.866  36.237  1.00 11.52           C  
ANISOU 3782  CA  LEU B 362     1778   1255   1343   -210    344    121       C  
ATOM   3783  C   LEU B 362      38.649   5.368  35.577  1.00 13.17           C  
ANISOU 3783  C   LEU B 362     2060   1428   1516   -191    279    184       C  
ATOM   3784  O   LEU B 362      38.641   5.684  34.393  1.00 11.70           O  
ANISOU 3784  O   LEU B 362     1956   1228   1263   -216    291    236       O  
ATOM   3785  CB  LEU B 362      39.974   3.334  36.296  1.00 12.65           C  
ANISOU 3785  CB  LEU B 362     1895   1457   1457   -183    341     78       C  
ATOM   3786  CG  LEU B 362      39.943   2.554  34.980  1.00 13.81           C  
ANISOU 3786  CG  LEU B 362     2107   1629   1512   -196    362     90       C  
ATOM   3787  CD1 LEU B 362      41.022   3.044  34.027  1.00 19.96           C  
ANISOU 3787  CD1 LEU B 362     2925   2405   2256   -252    448    106       C  
ATOM   3788  CD2 LEU B 362      40.124   1.057  35.276  1.00 14.41           C  
ANISOU 3788  CD2 LEU B 362     2145   1748   1581   -167    368     35       C  
ATOM   3789  N   ALA B 363      37.576   5.472  36.357  1.00 13.90           N  
ANISOU 3789  N   ALA B 363     2123   1507   1653   -145    209    180       N  
ATOM   3790  CA  ALA B 363      36.305   5.961  35.826  1.00 13.43           C  
ANISOU 3790  CA  ALA B 363     2111   1415   1576   -116    137    234       C  
ATOM   3791  C   ALA B 363      36.399   7.442  35.474  1.00 13.50           C  
ANISOU 3791  C   ALA B 363     2174   1350   1604   -131    145    292       C  
ATOM   3792  O   ALA B 363      35.948   7.869  34.415  1.00 13.06           O  
ANISOU 3792  O   ALA B 363     2200   1270   1494   -128    115    359       O  
ATOM   3793  CB  ALA B 363      35.184   5.727  36.835  1.00 12.65           C  
ANISOU 3793  CB  ALA B 363     1951   1321   1534    -65     74    205       C  
ATOM   3794  N   LEU B 364      36.990   8.215  36.376  1.00 12.34           N  
ANISOU 3794  N   LEU B 364     1988   1167   1534   -147    183    267       N  
ATOM   3795  CA  LEU B 364      37.173   9.648  36.171  1.00 16.08           C  
ANISOU 3795  CA  LEU B 364     2513   1556   2041   -168    203    314       C  
ATOM   3796  C   LEU B 364      37.996   9.889  34.917  1.00 16.61           C  
ANISOU 3796  C   LEU B 364     2664   1611   2034   -226    263    365       C  
ATOM   3797  O   LEU B 364      37.637  10.707  34.068  1.00 16.39           O  
ANISOU 3797  O   LEU B 364     2729   1524   1974   -227    247    442       O  
ATOM   3798  CB  LEU B 364      37.889  10.253  37.376  1.00 13.52           C  
ANISOU 3798  CB  LEU B 364     2125   1206   1806   -192    246    258       C  
ATOM   3799  CG  LEU B 364      38.149  11.755  37.331  1.00 19.01           C  
ANISOU 3799  CG  LEU B 364     2868   1804   2553   -223    277    292       C  
ATOM   3800  CD1 LEU B 364      36.832  12.516  37.332  1.00 19.77           C  
ANISOU 3800  CD1 LEU B 364     3001   1830   2682   -159    205    339       C  
ATOM   3801  CD2 LEU B 364      39.012  12.162  38.511  1.00 25.57           C  
ANISOU 3801  CD2 LEU B 364     3628   2627   3462   -261    323    218       C  
ATOM   3802  N   TYR B 365      39.102   9.162  34.804  1.00 12.16           N  
ANISOU 3802  N   TYR B 365     2071   1104   1444   -271    334    322       N  
ATOM   3803  CA  TYR B 365      39.989   9.321  33.661  1.00 14.75           C  
ANISOU 3803  CA  TYR B 365     2470   1430   1704   -335    412    357       C  
ATOM   3804  C   TYR B 365      39.321   8.904  32.353  1.00 13.46           C  
ANISOU 3804  C   TYR B 365     2406   1284   1426   -322    376    418       C  
ATOM   3805  O   TYR B 365      39.454   9.582  31.333  1.00 16.30           O  
ANISOU 3805  O   TYR B 365     2870   1601   1722   -357    403    488       O  
ATOM   3806  CB  TYR B 365      41.299   8.549  33.862  1.00 13.73           C  
ANISOU 3806  CB  TYR B 365     2270   1365   1582   -378    497    286       C  
ATOM   3807  CG  TYR B 365      42.287   8.824  32.750  1.00 13.79           C  
ANISOU 3807  CG  TYR B 365     2342   1367   1531   -453    598    313       C  
ATOM   3808  CD1 TYR B 365      42.879  10.071  32.621  1.00 16.98           C  
ANISOU 3808  CD1 TYR B 365     2781   1702   1968   -516    660    344       C  
ATOM   3809  CD2 TYR B 365      42.619   7.839  31.828  1.00 14.61           C  
ANISOU 3809  CD2 TYR B 365     2474   1530   1545   -466    638    304       C  
ATOM   3810  CE1 TYR B 365      43.776  10.339  31.594  1.00 20.30           C  
ANISOU 3810  CE1 TYR B 365     3249   2125   2337   -581    748    362       C  
ATOM   3811  CE2 TYR B 365      43.517   8.094  30.801  1.00 16.32           C  
ANISOU 3811  CE2 TYR B 365     2749   1747   1706   -536    739    323       C  
ATOM   3812  CZ  TYR B 365      44.092   9.345  30.694  1.00 19.39           C  
ANISOU 3812  CZ  TYR B 365     3150   2081   2137   -584    780    346       C  
ATOM   3813  OH  TYR B 365      44.976   9.609  29.679  1.00 21.76           O  
ANISOU 3813  OH  TYR B 365     3481   2392   2395   -634    854    351       O  
ATOM   3814  N   THR B 366      38.602   7.786  32.380  1.00 14.02           N  
ANISOU 3814  N   THR B 366     2448   1414   1464   -275    314    390       N  
ATOM   3815  CA  THR B 366      37.932   7.294  31.175  1.00 13.33           C  
ANISOU 3815  CA  THR B 366     2447   1353   1264   -265    269    434       C  
ATOM   3816  C   THR B 366      36.941   8.320  30.620  1.00 16.43           C  
ANISOU 3816  C   THR B 366     2925   1684   1634   -236    191    524       C  
ATOM   3817  O   THR B 366      36.954   8.648  29.424  1.00 17.35           O  
ANISOU 3817  O   THR B 366     3156   1786   1651   -260    194    592       O  
ATOM   3818  CB  THR B 366      37.199   5.961  31.468  1.00 15.36           C  
ANISOU 3818  CB  THR B 366     2648   1676   1511   -221    208    380       C  
ATOM   3819  OG1 THR B 366      38.169   4.948  31.773  1.00 15.65           O  
ANISOU 3819  OG1 THR B 366     2629   1765   1554   -244    282    307       O  
ATOM   3820  CG2 THR B 366      36.370   5.522  30.261  1.00 17.32           C  
ANISOU 3820  CG2 THR B 366     2982   1951   1646   -212    144    419       C  
ATOM   3821  N   VAL B 367      36.107   8.858  31.503  1.00 16.21           N  
ANISOU 3821  N   VAL B 367     2845   1617   1698   -182    122    524       N  
ATOM   3822  CA  VAL B 367      35.023   9.757  31.086  1.00 16.70           C  
ANISOU 3822  CA  VAL B 367     2969   1620   1758   -132     31    603       C  
ATOM   3823  C   VAL B 367      35.470  11.200  30.825  1.00 17.90           C  
ANISOU 3823  C   VAL B 367     3202   1671   1929   -157     72    675       C  
ATOM   3824  O   VAL B 367      35.010  11.841  29.867  1.00 19.55           O  
ANISOU 3824  O   VAL B 367     3519   1835   2075   -142     26    766       O  
ATOM   3825  CB  VAL B 367      33.867   9.742  32.121  1.00 15.88           C  
ANISOU 3825  CB  VAL B 367     2769   1513   1752    -58    -54    569       C  
ATOM   3826  CG1 VAL B 367      32.760  10.715  31.716  1.00 22.85           C  
ANISOU 3826  CG1 VAL B 367     3702   2331   2648      4   -150    646       C  
ATOM   3827  CG2 VAL B 367      33.316   8.332  32.275  1.00 17.18           C  
ANISOU 3827  CG2 VAL B 367     2869   1768   1892    -40    -95    507       C  
ATOM   3828  N   THR B 368      36.369  11.716  31.661  1.00 19.06           N  
ANISOU 3828  N   THR B 368     3301   1780   2160   -197    155    635       N  
ATOM   3829  CA  THR B 368      36.707  13.140  31.605  1.00 18.86           C  
ANISOU 3829  CA  THR B 368     3344   1646   2178   -222    194    692       C  
ATOM   3830  C   THR B 368      38.163  13.459  31.272  1.00 21.18           C  
ANISOU 3830  C   THR B 368     3656   1936   2457   -318    318    681       C  
ATOM   3831  O   THR B 368      38.481  14.591  30.907  1.00 21.44           O  
ANISOU 3831  O   THR B 368     3731   1905   2510   -343    346    723       O  
ATOM   3832  CB  THR B 368      36.390  13.854  32.938  1.00 19.18           C  
ANISOU 3832  CB  THR B 368     3303   1626   2357   -187    177    649       C  
ATOM   3833  OG1 THR B 368      37.364  13.493  33.926  1.00 17.98           O  
ANISOU 3833  OG1 THR B 368     3053   1514   2263   -234    252    554       O  
ATOM   3834  CG2 THR B 368      35.002  13.492  33.424  1.00 20.72           C  
ANISOU 3834  CG2 THR B 368     3438   1846   2589    -92     66    633       C  
ATOM   3835  N   GLY B 369      39.051  12.485  31.439  1.00 18.29           N  
ANISOU 3835  N   GLY B 369     3239   1643   2069   -367    391    615       N  
ATOM   3836  CA  GLY B 369      40.469  12.720  31.223  1.00 16.48           C  
ANISOU 3836  CA  GLY B 369     2988   1427   1845   -450    505    583       C  
ATOM   3837  C   GLY B 369      41.158  13.297  32.450  1.00 19.33           C  
ANISOU 3837  C   GLY B 369     3265   1752   2330   -484    555    520       C  
ATOM   3838  O   GLY B 369      42.356  13.564  32.435  1.00 19.96           O  
ANISOU 3838  O   GLY B 369     3306   1843   2433   -553    642    482       O  
ATOM   3839  N   GLN B 370      40.392  13.498  33.517  1.00 16.55           N  
ANISOU 3839  N   GLN B 370     2866   1365   2057   -430    490    498       N  
ATOM   3840  CA  GLN B 370      40.940  14.053  34.754  1.00 17.75           C  
ANISOU 3840  CA  GLN B 370     2932   1489   2324   -455    522    428       C  
ATOM   3841  C   GLN B 370      41.483  12.929  35.627  1.00 19.98           C  
ANISOU 3841  C   GLN B 370     3086   1877   2629   -450    528    328       C  
ATOM   3842  O   GLN B 370      41.209  11.759  35.369  1.00 17.28           O  
ANISOU 3842  O   GLN B 370     2724   1613   2227   -413    497    317       O  
ATOM   3843  CB  GLN B 370      39.861  14.834  35.506  1.00 21.72           C  
ANISOU 3843  CB  GLN B 370     3435   1916   2901   -390    445    438       C  
ATOM   3844  CG  GLN B 370      39.373  16.073  34.749  1.00 24.91           C  
ANISOU 3844  CG  GLN B 370     3951   2213   3301   -380    427    532       C  
ATOM   3845  CD  GLN B 370      38.096  16.650  35.333  1.00 35.78           C  
ANISOU 3845  CD  GLN B 370     5332   3518   4745   -293    342    548       C  
ATOM   3846  OE1 GLN B 370      37.494  16.068  36.237  1.00 36.01           O  
ANISOU 3846  OE1 GLN B 370     5277   3593   4813   -239    293    488       O  
ATOM   3847  NE2 GLN B 370      37.677  17.798  34.818  1.00 41.17           N  
ANISOU 3847  NE2 GLN B 370     6082   4119   5444   -271    312    617       N  
ATOM   3848  N   SER B 371      42.253  13.282  36.652  1.00 17.25           N  
ANISOU 3848  N   SER B 371     2658   1528   2368   -488    564    255       N  
ATOM   3849  CA  SER B 371      42.889  12.281  37.509  1.00 17.39           C  
ANISOU 3849  CA  SER B 371     2557   1643   2408   -483    566    165       C  
ATOM   3850  C   SER B 371      42.498  12.434  38.976  1.00 22.03           C  
ANISOU 3850  C   SER B 371     3072   2230   3070   -444    511    102       C  
ATOM   3851  O   SER B 371      41.991  13.480  39.380  1.00 18.59           O  
ANISOU 3851  O   SER B 371     2665   1711   2686   -440    493    113       O  
ATOM   3852  CB  SER B 371      44.413  12.365  37.381  1.00 24.33           C  
ANISOU 3852  CB  SER B 371     3386   2549   3309   -570    663    120       C  
ATOM   3853  OG  SER B 371      44.851  11.915  36.110  1.00 24.55           O  
ANISOU 3853  OG  SER B 371     3466   2604   3259   -602    725    159       O  
ATOM   3854  N   TRP B 372      42.737  11.369  39.740  1.00 18.49           N  
ANISOU 3854  N   TRP B 372     2536   1870   2622   -415    486     38       N  
ATOM   3855  CA  TRP B 372      42.668  11.339  41.208  1.00 16.64           C  
ANISOU 3855  CA  TRP B 372     2224   1656   2443   -391    446    -34       C  
ATOM   3856  C   TRP B 372      42.986  12.711  41.812  1.00 14.65           C  
ANISOU 3856  C   TRP B 372     1971   1329   2267   -441    469    -62       C  
ATOM   3857  O   TRP B 372      44.109  13.206  41.690  1.00 18.04           O  
ANISOU 3857  O   TRP B 372     2376   1751   2727   -518    531    -88       O  
ATOM   3858  CB  TRP B 372      43.678  10.292  41.694  1.00 20.02           C  
ANISOU 3858  CB  TRP B 372     2560   2181   2865   -395    456    -98       C  
ATOM   3859  CG  TRP B 372      43.714   9.989  43.170  1.00 17.78           C  
ANISOU 3859  CG  TRP B 372     2202   1939   2613   -366    408   -169       C  
ATOM   3860  CD1 TRP B 372      44.723  10.297  44.046  1.00 20.29           C  
ANISOU 3860  CD1 TRP B 372     2445   2285   2980   -406    417   -240       C  
ATOM   3861  CD2 TRP B 372      42.727   9.277  43.930  1.00 14.99           C  
ANISOU 3861  CD2 TRP B 372     1845   1612   2238   -296    344   -176       C  
ATOM   3862  NE1 TRP B 372      44.416   9.833  45.305  1.00 16.04           N  
ANISOU 3862  NE1 TRP B 372     1866   1787   2440   -361    357   -287       N  
ATOM   3863  CE2 TRP B 372      43.200   9.204  45.260  1.00 13.96           C  
ANISOU 3863  CE2 TRP B 372     1648   1521   2134   -295    319   -247       C  
ATOM   3864  CE3 TRP B 372      41.490   8.703  43.616  1.00 14.92           C  
ANISOU 3864  CE3 TRP B 372     1882   1599   2189   -238    306   -132       C  
ATOM   3865  CZ2 TRP B 372      42.479   8.576  46.274  1.00  9.54           C  
ANISOU 3865  CZ2 TRP B 372     1078    992   1555   -240    266   -269       C  
ATOM   3866  CZ3 TRP B 372      40.767   8.087  44.631  1.00 11.89           C  
ANISOU 3866  CZ3 TRP B 372     1476   1244   1798   -188    259   -159       C  
ATOM   3867  CH2 TRP B 372      41.267   8.027  45.943  1.00 10.79           C  
ANISOU 3867  CH2 TRP B 372     1281   1139   1678   -190    243   -224       C  
ATOM   3868  N   PRO B 373      41.982  13.353  42.428  1.00 19.23           N  
ANISOU 3868  N   PRO B 373     2576   1849   2881   -403    427    -61       N  
ATOM   3869  CA  PRO B 373      42.152  14.739  42.883  1.00 22.20           C  
ANISOU 3869  CA  PRO B 373     2971   2134   3331   -449    453    -84       C  
ATOM   3870  C   PRO B 373      43.018  14.868  44.139  1.00 21.58           C  
ANISOU 3870  C   PRO B 373     2806   2093   3300   -491    459   -186       C  
ATOM   3871  O   PRO B 373      43.058  13.959  44.968  1.00 17.75           O  
ANISOU 3871  O   PRO B 373     2255   1696   2794   -456    419   -236       O  
ATOM   3872  CB  PRO B 373      40.716  15.189  43.177  1.00 21.53           C  
ANISOU 3872  CB  PRO B 373     2930   1983   3266   -377    401    -58       C  
ATOM   3873  CG  PRO B 373      39.988  13.934  43.503  1.00 19.45           C  
ANISOU 3873  CG  PRO B 373     2629   1807   2956   -305    344    -66       C  
ATOM   3874  CD  PRO B 373      40.600  12.877  42.607  1.00 16.90           C  
ANISOU 3874  CD  PRO B 373     2300   1560   2564   -318    360    -36       C  
ATOM   3875  N   GLU B 374      43.686  16.010  44.266  1.00 17.44           N  
ANISOU 3875  N   GLU B 374     2289   1501   2837   -568    508   -215       N  
ATOM   3876  CA  GLU B 374      44.543  16.292  45.412  1.00 18.30           C  
ANISOU 3876  CA  GLU B 374     2319   1648   2986   -613    505   -315       C  
ATOM   3877  C   GLU B 374      43.765  16.211  46.726  1.00 14.45           C  
ANISOU 3877  C   GLU B 374     1811   1170   2511   -562    448   -374       C  
ATOM   3878  O   GLU B 374      44.318  15.819  47.763  1.00 18.00           O  
ANISOU 3878  O   GLU B 374     2186   1696   2958   -573    420   -455       O  
ATOM   3879  CB  GLU B 374      45.186  17.673  45.254  1.00 24.31           C  
ANISOU 3879  CB  GLU B 374     3106   2347   3783   -675    546   -319       C  
ATOM   3880  CG  GLU B 374      46.325  17.943  46.219  1.00 30.38           C  
ANISOU 3880  CG  GLU B 374     3789   3174   4581   -730    546   -416       C  
ATOM   3881  CD  GLU B 374      45.865  18.539  47.538  1.00 32.85           C  
ANISOU 3881  CD  GLU B 374     4096   3467   4919   -711    504   -483       C  
ATOM   3882  OE1 GLU B 374      44.723  19.057  47.611  1.00 28.99           O  
ANISOU 3882  OE1 GLU B 374     3677   2899   4440   -663    490   -451       O  
ATOM   3883  OE2 GLU B 374      46.661  18.497  48.504  1.00 33.42           O  
ANISOU 3883  OE2 GLU B 374     4094   3607   4999   -740    484   -567       O  
ATOM   3884  N   SER B 375      42.485  16.569  46.683  1.00 16.14           N  
ANISOU 3884  N   SER B 375     2089   1311   2731   -502    427   -334       N  
ATOM   3885  CA  SER B 375      41.654  16.514  47.888  1.00 15.61           C  
ANISOU 3885  CA  SER B 375     2006   1254   2670   -449    383   -389       C  
ATOM   3886  C   SER B 375      41.513  15.084  48.407  1.00 15.94           C  
ANISOU 3886  C   SER B 375     1995   1419   2644   -397    335   -405       C  
ATOM   3887  O   SER B 375      41.343  14.859  49.612  1.00 14.95           O  
ANISOU 3887  O   SER B 375     1837   1335   2508   -379    306   -472       O  
ATOM   3888  CB  SER B 375      40.274  17.146  47.652  1.00 18.84           C  
ANISOU 3888  CB  SER B 375     2483   1573   3102   -384    371   -340       C  
ATOM   3889  OG  SER B 375      39.502  16.397  46.732  1.00 18.13           O  
ANISOU 3889  OG  SER B 375     2420   1498   2971   -324    347   -257       O  
ATOM   3890  N   LEU B 376      41.590  14.110  47.506  1.00 14.34           N  
ANISOU 3890  N   LEU B 376     1790   1268   2391   -373    330   -343       N  
ATOM   3891  CA  LEU B 376      41.504  12.718  47.931  1.00 13.64           C  
ANISOU 3891  CA  LEU B 376     1659   1282   2241   -325    290   -353       C  
ATOM   3892  C   LEU B 376      42.855  12.207  48.408  1.00 14.83           C  
ANISOU 3892  C   LEU B 376     1737   1517   2382   -363    288   -409       C  
ATOM   3893  O   LEU B 376      42.930  11.254  49.186  1.00 14.54           O  
ANISOU 3893  O   LEU B 376     1662   1558   2304   -328    248   -439       O  
ATOM   3894  CB  LEU B 376      40.933  11.827  46.817  1.00 12.55           C  
ANISOU 3894  CB  LEU B 376     1552   1162   2054   -279    283   -273       C  
ATOM   3895  CG  LEU B 376      39.407  11.909  46.721  1.00 14.95           C  
ANISOU 3895  CG  LEU B 376     1900   1423   2359   -218    255   -235       C  
ATOM   3896  CD1 LEU B 376      38.879  11.063  45.566  1.00 16.04           C  
ANISOU 3896  CD1 LEU B 376     2067   1581   2446   -182    241   -163       C  
ATOM   3897  CD2 LEU B 376      38.774  11.473  48.042  1.00 15.25           C  
ANISOU 3897  CD2 LEU B 376     1908   1499   2389   -180    225   -291       C  
ATOM   3898  N   ILE B 377      43.928  12.837  47.943  1.00 13.41           N  
ANISOU 3898  N   ILE B 377     1537   1319   2240   -435    330   -423       N  
ATOM   3899  CA  ILE B 377      45.231  12.524  48.506  1.00 12.92           C  
ANISOU 3899  CA  ILE B 377     1388   1336   2186   -474    323   -490       C  
ATOM   3900  C   ILE B 377      45.223  12.966  49.965  1.00 16.49           C  
ANISOU 3900  C   ILE B 377     1815   1799   2651   -484    283   -574       C  
ATOM   3901  O   ILE B 377      45.634  12.216  50.848  1.00 17.89           O  
ANISOU 3901  O   ILE B 377     1938   2063   2794   -460    233   -620       O  
ATOM   3902  CB  ILE B 377      46.373  13.222  47.760  1.00 14.89           C  
ANISOU 3902  CB  ILE B 377     1611   1561   2485   -563    387   -499       C  
ATOM   3903  CG1 ILE B 377      46.451  12.718  46.315  1.00 16.96           C  
ANISOU 3903  CG1 ILE B 377     1903   1822   2719   -557    433   -420       C  
ATOM   3904  CG2 ILE B 377      47.694  12.993  48.499  1.00 17.12           C  
ANISOU 3904  CG2 ILE B 377     1785   1930   2790   -603    369   -585       C  
ATOM   3905  CD1 ILE B 377      47.435  13.503  45.460  1.00 22.38           C  
ANISOU 3905  CD1 ILE B 377     2583   2470   3449   -652    515   -418       C  
ATOM   3906  N   ARG B 378      44.715  14.171  50.214  1.00 14.24           N  
ANISOU 3906  N   ARG B 378     1578   1423   2411   -513    304   -593       N  
ATOM   3907  CA  ARG B 378      44.596  14.688  51.582  1.00 17.86           C  
ANISOU 3907  CA  ARG B 378     2027   1883   2878   -525    274   -679       C  
ATOM   3908  C   ARG B 378      43.714  13.809  52.477  1.00 20.40           C  
ANISOU 3908  C   ARG B 378     2359   2258   3133   -447    223   -685       C  
ATOM   3909  O   ARG B 378      44.047  13.562  53.638  1.00 18.04           O  
ANISOU 3909  O   ARG B 378     2029   2024   2802   -450    181   -754       O  
ATOM   3910  CB  ARG B 378      44.066  16.127  51.580  1.00 17.64           C  
ANISOU 3910  CB  ARG B 378     2063   1749   2890   -538    308   -670       C  
ATOM   3911  CG  ARG B 378      45.066  17.146  51.046  1.00 25.46           C  
ANISOU 3911  CG  ARG B 378     3048   2701   3925   -611    352   -669       C  
ATOM   3912  CD  ARG B 378      44.579  18.582  51.211  1.00 29.66           C  
ANISOU 3912  CD  ARG B 378     3643   3129   4497   -623    378   -671       C  
ATOM   3913  NE  ARG B 378      43.632  19.000  50.177  1.00 30.56           N  
ANISOU 3913  NE  ARG B 378     3837   3143   4632   -590    406   -583       N  
ATOM   3914  CZ  ARG B 378      42.359  19.324  50.403  1.00 37.88           C  
ANISOU 3914  CZ  ARG B 378     4815   4011   5568   -527    394   -565       C  
ATOM   3915  NH1 ARG B 378      41.862  19.278  51.633  1.00 38.27           N  
ANISOU 3915  NH1 ARG B 378     4848   4090   5602   -497    366   -629       N  
ATOM   3916  NH2 ARG B 378      41.581  19.705  49.396  1.00 35.04           N  
ANISOU 3916  NH2 ARG B 378     4522   3566   5227   -493    408   -481       N  
ATOM   3917  N   LYS B 379      42.588  13.344  51.946  1.00 14.06           N  
ANISOU 3917  N   LYS B 379     1604   1431   2308   -383    227   -614       N  
ATOM   3918  CA  LYS B 379      41.669  12.525  52.737  1.00 15.53           C  
ANISOU 3918  CA  LYS B 379     1803   1660   2436   -317    193   -616       C  
ATOM   3919  C   LYS B 379      42.200  11.115  53.012  1.00 14.47           C  
ANISOU 3919  C   LYS B 379     1631   1633   2235   -286    151   -608       C  
ATOM   3920  O   LYS B 379      42.114  10.627  54.138  1.00 14.39           O  
ANISOU 3920  O   LYS B 379     1616   1677   2174   -266    115   -649       O  
ATOM   3921  CB  LYS B 379      40.315  12.410  52.031  1.00 17.71           C  
ANISOU 3921  CB  LYS B 379     2128   1883   2717   -262    207   -546       C  
ATOM   3922  CG  LYS B 379      39.277  11.564  52.788  1.00 17.42           C  
ANISOU 3922  CG  LYS B 379     2103   1887   2630   -203    185   -550       C  
ATOM   3923  CD  LYS B 379      38.068  11.287  51.892  1.00 21.64           C  
ANISOU 3923  CD  LYS B 379     2666   2384   3172   -153    193   -478       C  
ATOM   3924  CE  LYS B 379      36.899  10.680  52.673  1.00 24.46           C  
ANISOU 3924  CE  LYS B 379     3030   2765   3499   -107    187   -492       C  
ATOM   3925  NZ  LYS B 379      36.310  11.676  53.603  1.00 28.24           N  
ANISOU 3925  NZ  LYS B 379     3519   3195   4014   -110    209   -557       N  
ATOM   3926  N   THR B 380      42.722  10.458  51.976  1.00 12.00           N  
ANISOU 3926  N   THR B 380     1298   1345   1918   -280    158   -555       N  
ATOM   3927  CA  THR B 380      43.021   9.023  52.042  1.00 13.51           C  
ANISOU 3927  CA  THR B 380     1465   1617   2051   -234    125   -533       C  
ATOM   3928  C   THR B 380      44.500   8.719  52.263  1.00 16.47           C  
ANISOU 3928  C   THR B 380     1765   2063   2429   -257    102   -573       C  
ATOM   3929  O   THR B 380      44.858   7.625  52.700  1.00 14.38           O  
ANISOU 3929  O   THR B 380     1476   1868   2119   -214     60   -573       O  
ATOM   3930  CB  THR B 380      42.618   8.290  50.742  1.00 13.21           C  
ANISOU 3930  CB  THR B 380     1450   1567   2000   -202    147   -454       C  
ATOM   3931  OG1 THR B 380      43.504   8.683  49.691  1.00 12.06           O  
ANISOU 3931  OG1 THR B 380     1282   1407   1892   -246    185   -439       O  
ATOM   3932  CG2 THR B 380      41.171   8.607  50.347  1.00 11.09           C  
ANISOU 3932  CG2 THR B 380     1243   1234   1738   -178    163   -412       C  
ATOM   3933  N   GLY B 381      45.362   9.664  51.919  1.00 15.16           N  
ANISOU 3933  N   GLY B 381     1562   1875   2322   -325    130   -606       N  
ATOM   3934  CA  GLY B 381      46.791   9.404  51.929  1.00 12.40           C  
ANISOU 3934  CA  GLY B 381     1124   1594   1992   -352    116   -645       C  
ATOM   3935  C   GLY B 381      47.265   8.621  50.715  1.00 18.96           C  
ANISOU 3935  C   GLY B 381     1931   2445   2827   -334    149   -593       C  
ATOM   3936  O   GLY B 381      48.460   8.369  50.573  1.00 20.37           O  
ANISOU 3936  O   GLY B 381     2027   2679   3033   -353    149   -624       O  
ATOM   3937  N   TYR B 382      46.340   8.230  49.838  1.00 14.14           N  
ANISOU 3937  N   TYR B 382     1389   1792   2191   -300    179   -520       N  
ATOM   3938  CA  TYR B 382      46.712   7.481  48.629  1.00 13.25           C  
ANISOU 3938  CA  TYR B 382     1267   1695   2072   -286    217   -475       C  
ATOM   3939  C   TYR B 382      47.072   8.429  47.488  1.00 15.52           C  
ANISOU 3939  C   TYR B 382     1566   1927   2402   -357    291   -456       C  
ATOM   3940  O   TYR B 382      46.455   9.482  47.315  1.00 15.45           O  
ANISOU 3940  O   TYR B 382     1614   1842   2413   -392    314   -439       O  
ATOM   3941  CB  TYR B 382      45.573   6.582  48.151  1.00 13.87           C  
ANISOU 3941  CB  TYR B 382     1417   1758   2096   -223    211   -409       C  
ATOM   3942  CG  TYR B 382      45.113   5.512  49.129  1.00 14.55           C  
ANISOU 3942  CG  TYR B 382     1509   1886   2133   -155    152   -414       C  
ATOM   3943  CD1 TYR B 382      45.991   4.942  50.049  1.00 14.93           C  
ANISOU 3943  CD1 TYR B 382     1497   2003   2174   -132    105   -457       C  
ATOM   3944  CD2 TYR B 382      43.797   5.073  49.122  1.00 12.73           C  
ANISOU 3944  CD2 TYR B 382     1346   1627   1863   -116    143   -372       C  
ATOM   3945  CE1 TYR B 382      45.562   3.953  50.933  1.00 15.55           C  
ANISOU 3945  CE1 TYR B 382     1598   2112   2198    -70     54   -450       C  
ATOM   3946  CE2 TYR B 382      43.359   4.088  49.991  1.00 16.48           C  
ANISOU 3946  CE2 TYR B 382     1836   2134   2291    -63    102   -372       C  
ATOM   3947  CZ  TYR B 382      44.244   3.533  50.897  1.00 16.47           C  
ANISOU 3947  CZ  TYR B 382     1790   2192   2275    -40     59   -407       C  
ATOM   3948  OH  TYR B 382      43.802   2.558  51.765  1.00 15.07           O  
ANISOU 3948  OH  TYR B 382     1643   2039   2043     11     20   -398       O  
ATOM   3949  N   THR B 383      48.061   8.029  46.702  1.00 19.23           N  
ANISOU 3949  N   THR B 383     1986   2434   2886   -376    334   -457       N  
ATOM   3950  CA  THR B 383      48.455   8.768  45.517  1.00 19.56           C  
ANISOU 3950  CA  THR B 383     2047   2429   2955   -447    417   -433       C  
ATOM   3951  C   THR B 383      48.320   7.842  44.319  1.00 18.08           C  
ANISOU 3951  C   THR B 383     1895   2253   2720   -415    455   -378       C  
ATOM   3952  O   THR B 383      48.078   6.647  44.480  1.00 18.56           O  
ANISOU 3952  O   THR B 383     1950   2359   2742   -343    417   -371       O  
ATOM   3953  CB  THR B 383      49.920   9.211  45.609  1.00 21.86           C  
ANISOU 3953  CB  THR B 383     2235   2758   3312   -519    455   -500       C  
ATOM   3954  OG1 THR B 383      50.750   8.055  45.782  1.00 19.34           O  
ANISOU 3954  OG1 THR B 383     1826   2531   2992   -472    433   -533       O  
ATOM   3955  CG2 THR B 383      50.127  10.164  46.786  1.00 21.30           C  
ANISOU 3955  CG2 THR B 383     2128   2677   3287   -563    416   -567       C  
ATOM   3956  N   LEU B 384      48.491   8.382  43.117  1.00 16.55           N  
ANISOU 3956  N   LEU B 384     1745   2016   2525   -471    533   -340       N  
ATOM   3957  CA  LEU B 384      48.474   7.531  41.930  1.00 20.44           C  
ANISOU 3957  CA  LEU B 384     2274   2525   2965   -450    576   -297       C  
ATOM   3958  C   LEU B 384      49.596   6.503  41.996  1.00 22.87           C  
ANISOU 3958  C   LEU B 384     2481   2919   3291   -428    592   -350       C  
ATOM   3959  O   LEU B 384      49.459   5.394  41.479  1.00 24.04           O  
ANISOU 3959  O   LEU B 384     2644   3095   3394   -375    596   -333       O  
ATOM   3960  CB  LEU B 384      48.568   8.365  40.649  1.00 21.00           C  
ANISOU 3960  CB  LEU B 384     2418   2538   3024   -524    663   -249       C  
ATOM   3961  CG  LEU B 384      47.260   9.025  40.207  1.00 22.91           C  
ANISOU 3961  CG  LEU B 384     2783   2696   3225   -515    640   -172       C  
ATOM   3962  CD1 LEU B 384      47.470   9.875  38.952  1.00 27.79           C  
ANISOU 3962  CD1 LEU B 384     3482   3255   3824   -589    725   -117       C  
ATOM   3963  CD2 LEU B 384      46.179   7.971  39.987  1.00 21.40           C  
ANISOU 3963  CD2 LEU B 384     2641   2524   2965   -433    583   -134       C  
ATOM   3964  N   GLU B 385      50.701   6.868  42.643  1.00 18.19           N  
ANISOU 3964  N   GLU B 385     1780   2364   2767   -465    597   -419       N  
ATOM   3965  CA  GLU B 385      51.796   5.926  42.837  1.00 19.25           C  
ANISOU 3965  CA  GLU B 385     1800   2582   2932   -432    598   -475       C  
ATOM   3966  C   GLU B 385      51.371   4.743  43.705  1.00 20.80           C  
ANISOU 3966  C   GLU B 385     1987   2819   3098   -326    504   -478       C  
ATOM   3967  O   GLU B 385      51.633   3.587  43.362  1.00 22.36           O  
ANISOU 3967  O   GLU B 385     2164   3053   3280   -266    511   -478       O  
ATOM   3968  CB  GLU B 385      53.023   6.622  43.437  1.00 28.52           C  
ANISOU 3968  CB  GLU B 385     2869   3788   4178   -483    594   -544       C  
ATOM   3969  CG  GLU B 385      54.219   5.699  43.625  1.00 42.46           C  
ANISOU 3969  CG  GLU B 385     4529   5632   5970   -432    573   -591       C  
ATOM   3970  CD  GLU B 385      55.453   6.422  44.142  1.00 58.20           C  
ANISOU 3970  CD  GLU B 385     6433   7655   8025   -480    561   -653       C  
ATOM   3971  OE1 GLU B 385      55.342   7.609  44.526  1.00 62.92           O  
ANISOU 3971  OE1 GLU B 385     7050   8213   8642   -548    559   -665       O  
ATOM   3972  OE2 GLU B 385      56.538   5.802  44.163  1.00 62.13           O  
ANISOU 3972  OE2 GLU B 385     6840   8211   8553   -448    554   -690       O  
ATOM   3973  N   SER B 386      50.699   5.017  44.820  1.00 17.60           N  
ANISOU 3973  N   SER B 386     1604   2401   2683   -304    423   -479       N  
ATOM   3974  CA  SER B 386      50.308   3.934  45.716  1.00 20.81           C  
ANISOU 3974  CA  SER B 386     2010   2841   3054   -211    340   -478       C  
ATOM   3975  C   SER B 386      49.149   3.119  45.140  1.00 20.74           C  
ANISOU 3975  C   SER B 386     2104   2797   2978   -160    341   -414       C  
ATOM   3976  O   SER B 386      49.024   1.930  45.417  1.00 17.14           O  
ANISOU 3976  O   SER B 386     1651   2367   2495    -87    305   -408       O  
ATOM   3977  CB  SER B 386      49.964   4.459  47.115  1.00 23.21           C  
ANISOU 3977  CB  SER B 386     2310   3148   3359   -209    261   -505       C  
ATOM   3978  OG  SER B 386      48.733   5.152  47.118  1.00 21.53           O  
ANISOU 3978  OG  SER B 386     2195   2867   3118   -229    262   -466       O  
ATOM   3979  N   LEU B 387      48.307   3.764  44.336  1.00 15.44           N  
ANISOU 3979  N   LEU B 387     1519   2065   2282   -200    379   -367       N  
ATOM   3980  CA  LEU B 387      47.190   3.079  43.697  1.00 13.43           C  
ANISOU 3980  CA  LEU B 387     1356   1781   1966   -162    378   -311       C  
ATOM   3981  C   LEU B 387      47.617   2.289  42.458  1.00 16.32           C  
ANISOU 3981  C   LEU B 387     1732   2162   2308   -157    440   -300       C  
ATOM   3982  O   LEU B 387      46.848   1.484  41.948  1.00 15.33           O  
ANISOU 3982  O   LEU B 387     1671   2023   2131   -121    434   -268       O  
ATOM   3983  CB  LEU B 387      46.103   4.082  43.301  1.00 13.12           C  
ANISOU 3983  CB  LEU B 387     1401   1675   1909   -199    382   -265       C  
ATOM   3984  CG  LEU B 387      45.356   4.779  44.445  1.00 13.74           C  
ANISOU 3984  CG  LEU B 387     1490   1727   2003   -194    327   -273       C  
ATOM   3985  CD1 LEU B 387      44.433   5.864  43.910  1.00 18.89           C  
ANISOU 3985  CD1 LEU B 387     2215   2306   2654   -226    340   -229       C  
ATOM   3986  CD2 LEU B 387      44.561   3.766  45.244  1.00 13.22           C  
ANISOU 3986  CD2 LEU B 387     1440   1681   1901   -126    268   -270       C  
ATOM   3987  N   LYS B 388      48.836   2.517  41.979  1.00 16.48           N  
ANISOU 3987  N   LYS B 388     1685   2209   2368   -196    503   -334       N  
ATOM   3988  CA  LYS B 388      49.258   1.971  40.678  1.00 13.02           C  
ANISOU 3988  CA  LYS B 388     1263   1779   1904   -206    583   -328       C  
ATOM   3989  C   LYS B 388      49.080   0.453  40.478  1.00 15.57           C  
ANISOU 3989  C   LYS B 388     1602   2122   2192   -129    571   -330       C  
ATOM   3990  O   LYS B 388      48.502   0.039  39.476  1.00 16.90           O  
ANISOU 3990  O   LYS B 388     1852   2269   2301   -131    603   -299       O  
ATOM   3991  CB  LYS B 388      50.681   2.418  40.306  1.00 18.19           C  
ANISOU 3991  CB  LYS B 388     1827   2467   2618   -263    663   -376       C  
ATOM   3992  CG  LYS B 388      51.099   1.978  38.899  1.00 19.21           C  
ANISOU 3992  CG  LYS B 388     1982   2602   2714   -285    764   -373       C  
ATOM   3993  CD  LYS B 388      52.431   2.579  38.484  1.00 25.78           C  
ANISOU 3993  CD  LYS B 388     2747   3453   3595   -346    829   -407       C  
ATOM   3994  CE  LYS B 388      52.814   2.138  37.079  1.00 30.43           C  
ANISOU 3994  CE  LYS B 388     3386   4041   4135   -360    909   -395       C  
ATOM   3995  NZ  LYS B 388      54.113   2.716  36.643  1.00 34.44           N  
ANISOU 3995  NZ  LYS B 388     3835   4565   4688   -418    972   -427       N  
ATOM   3996  N   PRO B 389      49.549  -0.379  41.430  1.00 17.47           N  
ANISOU 3996  N   PRO B 389     1771   2399   2466    -61    521   -366       N  
ATOM   3997  CA  PRO B 389      49.396  -1.828  41.228  1.00 20.01           C  
ANISOU 3997  CA  PRO B 389     2117   2726   2761     12    515   -367       C  
ATOM   3998  C   PRO B 389      47.944  -2.253  41.018  1.00 17.94           C  
ANISOU 3998  C   PRO B 389     1969   2418   2428     27    484   -317       C  
ATOM   3999  O   PRO B 389      47.635  -3.037  40.110  1.00 16.97           O  
ANISOU 3999  O   PRO B 389     1904   2281   2263     38    519   -308       O  
ATOM   4000  CB  PRO B 389      49.941  -2.420  42.532  1.00 20.44           C  
ANISOU 4000  CB  PRO B 389     2093   2814   2859     84    443   -397       C  
ATOM   4001  CG  PRO B 389      50.924  -1.400  43.016  1.00 21.04           C  
ANISOU 4001  CG  PRO B 389     2067   2928   2998     40    443   -437       C  
ATOM   4002  CD  PRO B 389      50.314  -0.074  42.655  1.00 20.79           C  
ANISOU 4002  CD  PRO B 389     2091   2860   2949    -48    469   -409       C  
ATOM   4003  N   CYS B 390      47.053  -1.732  41.853  1.00 12.72           N  
ANISOU 4003  N   CYS B 390     1338   1737   1758     23    419   -291       N  
ATOM   4004  CA  CYS B 390      45.643  -2.060  41.729  1.00 13.35           C  
ANISOU 4004  CA  CYS B 390     1510   1780   1783     33    388   -250       C  
ATOM   4005  C   CYS B 390      45.082  -1.498  40.426  1.00 14.89           C  
ANISOU 4005  C   CYS B 390     1775   1948   1936    -21    430   -217       C  
ATOM   4006  O   CYS B 390      44.300  -2.163  39.746  1.00 14.66           O  
ANISOU 4006  O   CYS B 390     1813   1902   1855    -13    430   -198       O  
ATOM   4007  CB  CYS B 390      44.863  -1.507  42.920  1.00 15.36           C  
ANISOU 4007  CB  CYS B 390     1771   2022   2045     37    321   -237       C  
ATOM   4008  SG  CYS B 390      43.140  -1.997  42.909  1.00 16.94           S  
ANISOU 4008  SG  CYS B 390     2059   2183   2193     51    284   -198       S  
ATOM   4009  N   LEU B 391      45.487  -0.274  40.083  1.00 12.62           N  
ANISOU 4009  N   LEU B 391     1474   1654   1666    -79    463   -210       N  
ATOM   4010  CA  LEU B 391      45.043   0.372  38.841  1.00 16.20           C  
ANISOU 4010  CA  LEU B 391     2003   2080   2074   -131    501   -170       C  
ATOM   4011  C   LEU B 391      45.445  -0.423  37.596  1.00 17.49           C  
ANISOU 4011  C   LEU B 391     2200   2258   2188   -137    566   -178       C  
ATOM   4012  O   LEU B 391      44.660  -0.569  36.658  1.00 15.89           O  
ANISOU 4012  O   LEU B 391     2082   2038   1917   -150    567   -145       O  
ATOM   4013  CB  LEU B 391      45.631   1.786  38.736  1.00 18.48           C  
ANISOU 4013  CB  LEU B 391     2272   2352   2397   -195    538   -164       C  
ATOM   4014  CG  LEU B 391      44.744   2.962  39.131  1.00 27.07           C  
ANISOU 4014  CG  LEU B 391     3398   3392   3496   -215    494   -126       C  
ATOM   4015  CD1 LEU B 391      45.551   4.265  39.064  1.00 24.88           C  
ANISOU 4015  CD1 LEU B 391     3097   3092   3265   -283    543   -131       C  
ATOM   4016  CD2 LEU B 391      43.536   3.022  38.205  1.00 22.68           C  
ANISOU 4016  CD2 LEU B 391     2943   2801   2875   -214    473    -67       C  
ATOM   4017  N   MET B 392      46.679  -0.913  37.585  1.00 15.55           N  
ANISOU 4017  N   MET B 392     1883   2048   1978   -127    620   -226       N  
ATOM   4018  CA  MET B 392      47.169  -1.726  36.472  1.00 19.02           C  
ANISOU 4018  CA  MET B 392     2345   2503   2379   -129    695   -248       C  
ATOM   4019  C   MET B 392      46.333  -2.991  36.299  1.00 19.06           C  
ANISOU 4019  C   MET B 392     2410   2497   2335    -78    661   -247       C  
ATOM   4020  O   MET B 392      46.021  -3.389  35.173  1.00 16.37           O  
ANISOU 4020  O   MET B 392     2144   2151   1925    -98    698   -242       O  
ATOM   4021  CB  MET B 392      48.646  -2.089  36.671  1.00 19.95           C  
ANISOU 4021  CB  MET B 392     2354   2662   2564   -113    754   -310       C  
ATOM   4022  CG  MET B 392      49.594  -0.899  36.668  1.00 28.50           C  
ANISOU 4022  CG  MET B 392     3370   3760   3698   -178    806   -323       C  
ATOM   4023  SD  MET B 392      49.575   0.028  35.118  1.00 43.52           S  
ANISOU 4023  SD  MET B 392     5368   5637   5530   -275    895   -281       S  
ATOM   4024  CE  MET B 392      48.460   1.367  35.508  1.00 52.66           C  
ANISOU 4024  CE  MET B 392     6594   6741   6673   -314    832   -213       C  
ATOM   4025  N   ASP B 393      45.968  -3.617  37.416  1.00 13.31           N  
ANISOU 4025  N   ASP B 393     1653   1764   1639    -20    591   -254       N  
ATOM   4026  CA  ASP B 393      45.105  -4.801  37.379  1.00 16.00           C  
ANISOU 4026  CA  ASP B 393     2052   2085   1941     20    558   -253       C  
ATOM   4027  C   ASP B 393      43.706  -4.445  36.887  1.00 14.67           C  
ANISOU 4027  C   ASP B 393     1971   1892   1711    -14    518   -209       C  
ATOM   4028  O   ASP B 393      43.150  -5.121  36.013  1.00 13.81           O  
ANISOU 4028  O   ASP B 393     1930   1774   1542    -21    527   -210       O  
ATOM   4029  CB  ASP B 393      45.011  -5.454  38.767  1.00 17.30           C  
ANISOU 4029  CB  ASP B 393     2176   2246   2152     84    496   -262       C  
ATOM   4030  CG  ASP B 393      46.224  -6.305  39.094  1.00 25.69           C  
ANISOU 4030  CG  ASP B 393     3170   3326   3264    142    524   -306       C  
ATOM   4031  OD1 ASP B 393      46.872  -6.793  38.145  1.00 26.72           O  
ANISOU 4031  OD1 ASP B 393     3300   3464   3388    142    594   -338       O  
ATOM   4032  OD2 ASP B 393      46.525  -6.490  40.294  1.00 19.46           O  
ANISOU 4032  OD2 ASP B 393     2329   2546   2520    190    473   -311       O  
ATOM   4033  N   LEU B 394      43.142  -3.381  37.449  1.00 13.53           N  
ANISOU 4033  N   LEU B 394     1820   1737   1583    -32    470   -174       N  
ATOM   4034  CA  LEU B 394      41.765  -3.008  37.145  1.00 14.13           C  
ANISOU 4034  CA  LEU B 394     1960   1790   1617    -51    419   -133       C  
ATOM   4035  C   LEU B 394      41.621  -2.540  35.706  1.00 11.09           C  
ANISOU 4035  C   LEU B 394     1645   1403   1163    -99    450   -106       C  
ATOM   4036  O   LEU B 394      40.587  -2.760  35.073  1.00 13.64           O  
ANISOU 4036  O   LEU B 394     2033   1719   1431   -107    413    -86       O  
ATOM   4037  CB  LEU B 394      41.261  -1.932  38.117  1.00 15.42           C  
ANISOU 4037  CB  LEU B 394     2096   1939   1825    -53    367   -108       C  
ATOM   4038  CG  LEU B 394      39.751  -1.683  38.127  1.00 14.58           C  
ANISOU 4038  CG  LEU B 394     2031   1810   1698    -53    304    -76       C  
ATOM   4039  CD1 LEU B 394      38.995  -2.941  38.551  1.00 15.14           C  
ANISOU 4039  CD1 LEU B 394     2109   1882   1760    -23    273    -95       C  
ATOM   4040  CD2 LEU B 394      39.426  -0.514  39.084  1.00 14.37           C  
ANISOU 4040  CD2 LEU B 394     1970   1764   1724    -54    270    -61       C  
ATOM   4041  N   HIS B 395      42.663  -1.904  35.184  1.00 11.82           N  
ANISOU 4041  N   HIS B 395     1728   1506   1259   -133    517   -108       N  
ATOM   4042  CA  HIS B 395      42.646  -1.483  33.791  1.00 15.08           C  
ANISOU 4042  CA  HIS B 395     2220   1916   1593   -183    559    -79       C  
ATOM   4043  C   HIS B 395      42.611  -2.698  32.859  1.00 14.99           C  
ANISOU 4043  C   HIS B 395     2261   1922   1511   -179    590   -110       C  
ATOM   4044  O   HIS B 395      41.882  -2.717  31.861  1.00 15.01           O  
ANISOU 4044  O   HIS B 395     2351   1923   1428   -204    573    -85       O  
ATOM   4045  CB  HIS B 395      43.865  -0.618  33.475  1.00 16.59           C  
ANISOU 4045  CB  HIS B 395     2387   2113   1805   -229    643    -80       C  
ATOM   4046  CG  HIS B 395      43.823  -0.011  32.109  1.00 19.16           C  
ANISOU 4046  CG  HIS B 395     2807   2428   2043   -287    689    -38       C  
ATOM   4047  ND1 HIS B 395      44.949   0.148  31.330  1.00 22.01           N  
ANISOU 4047  ND1 HIS B 395     3174   2806   2383   -336    798    -55       N  
ATOM   4048  CD2 HIS B 395      42.790   0.475  31.385  1.00 20.46           C  
ANISOU 4048  CD2 HIS B 395     3071   2572   2133   -303    639     23       C  
ATOM   4049  CE1 HIS B 395      44.610   0.709  30.183  1.00 26.19           C  
ANISOU 4049  CE1 HIS B 395     3809   3321   2823   -381    811     -3       C  
ATOM   4050  NE2 HIS B 395      43.305   0.916  30.189  1.00 21.98           N  
ANISOU 4050  NE2 HIS B 395     3337   2764   2249   -361    715     48       N  
ATOM   4051  N   GLN B 396      43.403  -3.715  33.187  1.00 14.82           N  
ANISOU 4051  N   GLN B 396     2188   1917   1528   -145    633   -168       N  
ATOM   4052  CA  GLN B 396      43.373  -4.960  32.431  1.00 15.00           C  
ANISOU 4052  CA  GLN B 396     2257   1947   1497   -135    666   -209       C  
ATOM   4053  C   GLN B 396      42.007  -5.649  32.518  1.00 17.94           C  
ANISOU 4053  C   GLN B 396     2680   2301   1835   -119    584   -201       C  
ATOM   4054  O   GLN B 396      41.493  -6.150  31.521  1.00 17.30           O  
ANISOU 4054  O   GLN B 396     2677   2224   1674   -142    587   -211       O  
ATOM   4055  CB  GLN B 396      44.483  -5.910  32.889  1.00 19.72           C  
ANISOU 4055  CB  GLN B 396     2779   2553   2159    -88    718   -269       C  
ATOM   4056  CG  GLN B 396      45.871  -5.473  32.462  1.00 26.72           C  
ANISOU 4056  CG  GLN B 396     3610   3464   3080   -107    791   -286       C  
ATOM   4057  CD  GLN B 396      45.978  -5.260  30.960  1.00 33.16           C  
ANISOU 4057  CD  GLN B 396     4499   4287   3815   -162    835   -274       C  
ATOM   4058  OE1 GLN B 396      45.593  -6.125  30.167  1.00 29.48           O  
ANISOU 4058  OE1 GLN B 396     4093   3817   3292   -158    831   -291       O  
ATOM   4059  NE2 GLN B 396      46.498  -4.100  30.562  1.00 32.89           N  
ANISOU 4059  NE2 GLN B 396     4463   4259   3774   -215    878   -247       N  
ATOM   4060  N   THR B 397      41.426  -5.677  33.711  1.00 14.96           N  
ANISOU 4060  N   THR B 397     2257   1908   1518    -85    516   -190       N  
ATOM   4061  CA  THR B 397      40.107  -6.273  33.885  1.00 14.11           C  
ANISOU 4061  CA  THR B 397     2184   1786   1391    -77    445   -185       C  
ATOM   4062  C   THR B 397      39.082  -5.532  33.032  1.00 16.10           C  
ANISOU 4062  C   THR B 397     2499   2043   1576   -118    395   -143       C  
ATOM   4063  O   THR B 397      38.261  -6.142  32.350  1.00 15.18           O  
ANISOU 4063  O   THR B 397     2438   1929   1400   -134    365   -154       O  
ATOM   4064  CB  THR B 397      39.697  -6.255  35.368  1.00 15.68           C  
ANISOU 4064  CB  THR B 397     2323   1969   1665    -40    392   -176       C  
ATOM   4065  OG1 THR B 397      40.560  -7.136  36.099  1.00 16.62           O  
ANISOU 4065  OG1 THR B 397     2400   2082   1833      5    425   -213       O  
ATOM   4066  CG2 THR B 397      38.253  -6.704  35.544  1.00 16.28           C  
ANISOU 4066  CG2 THR B 397     2428   2031   1727    -44    326   -171       C  
ATOM   4067  N   TYR B 398      39.157  -4.208  33.061  1.00 12.05           N  
ANISOU 4067  N   TYR B 398     1977   1529   1073   -133    384    -95       N  
ATOM   4068  CA  TYR B 398      38.259  -3.364  32.277  1.00 14.77           C  
ANISOU 4068  CA  TYR B 398     2382   1872   1360   -161    331    -43       C  
ATOM   4069  C   TYR B 398      38.428  -3.651  30.782  1.00 16.34           C  
ANISOU 4069  C   TYR B 398     2669   2089   1448   -199    366    -47       C  
ATOM   4070  O   TYR B 398      37.447  -3.853  30.052  1.00 14.86           O  
ANISOU 4070  O   TYR B 398     2542   1912   1191   -213    306    -36       O  
ATOM   4071  CB  TYR B 398      38.574  -1.902  32.596  1.00 14.15           C  
ANISOU 4071  CB  TYR B 398     2281   1774   1319   -169    333      6       C  
ATOM   4072  CG  TYR B 398      37.605  -0.875  32.043  1.00 16.98           C  
ANISOU 4072  CG  TYR B 398     2694   2117   1641   -181    266     70       C  
ATOM   4073  CD1 TYR B 398      36.388  -1.249  31.476  1.00 17.27           C  
ANISOU 4073  CD1 TYR B 398     2773   2165   1624   -176    188     80       C  
ATOM   4074  CD2 TYR B 398      37.921   0.478  32.082  1.00 14.98           C  
ANISOU 4074  CD2 TYR B 398     2446   1834   1411   -194    277    120       C  
ATOM   4075  CE1 TYR B 398      35.515  -0.294  30.964  1.00 17.32           C  
ANISOU 4075  CE1 TYR B 398     2823   2158   1600   -175    116    142       C  
ATOM   4076  CE2 TYR B 398      37.055   1.437  31.585  1.00 16.10           C  
ANISOU 4076  CE2 TYR B 398     2642   1951   1525   -194    213    185       C  
ATOM   4077  CZ  TYR B 398      35.857   1.048  31.028  1.00 17.83           C  
ANISOU 4077  CZ  TYR B 398     2899   2186   1691   -179    128    197       C  
ATOM   4078  OH  TYR B 398      35.010   2.007  30.526  1.00 18.08           O  
ANISOU 4078  OH  TYR B 398     2979   2193   1697   -168     54    264       O  
ATOM   4079  N   LEU B 399      39.674  -3.675  30.325  1.00 13.12           N  
ANISOU 4079  N   LEU B 399     2269   1691   1023   -219    463    -66       N  
ATOM   4080  CA  LEU B 399      39.957  -3.912  28.908  1.00 15.29           C  
ANISOU 4080  CA  LEU B 399     2636   1987   1187   -261    516    -74       C  
ATOM   4081  C   LEU B 399      39.437  -5.266  28.427  1.00 20.06           C  
ANISOU 4081  C   LEU B 399     3263   2601   1757   -252    489   -127       C  
ATOM   4082  O   LEU B 399      38.955  -5.395  27.298  1.00 19.27           O  
ANISOU 4082  O   LEU B 399     3231   2516   1575   -278    459   -120       O  
ATOM   4083  CB  LEU B 399      41.462  -3.801  28.630  1.00 19.53           C  
ANISOU 4083  CB  LEU B 399     3132   2530   1758   -273    619    -97       C  
ATOM   4084  CG  LEU B 399      42.053  -2.391  28.578  1.00 20.31           C  
ANISOU 4084  CG  LEU B 399     3230   2618   1869   -307    658    -45       C  
ATOM   4085  CD1 LEU B 399      43.572  -2.456  28.630  1.00 23.22           C  
ANISOU 4085  CD1 LEU B 399     3525   2998   2300   -314    757    -88       C  
ATOM   4086  CD2 LEU B 399      41.598  -1.651  27.324  1.00 21.24           C  
ANISOU 4086  CD2 LEU B 399     3448   2733   1889   -347    633     15       C  
ATOM   4087  N   LYS B 400      39.538  -6.275  29.285  1.00 17.80           N  
ANISOU 4087  N   LYS B 400     2923   2304   1538   -215    498   -179       N  
ATOM   4088  CA  LYS B 400      39.151  -7.632  28.910  1.00 20.35           C  
ANISOU 4088  CA  LYS B 400     3264   2624   1846   -209    484   -232       C  
ATOM   4089  C   LYS B 400      37.708  -7.993  29.271  1.00 17.73           C  
ANISOU 4089  C   LYS B 400     2952   2285   1500   -211    394   -234       C  
ATOM   4090  O   LYS B 400      37.259  -9.109  28.995  1.00 18.21           O  
ANISOU 4090  O   LYS B 400     3028   2339   1554   -214    378   -279       O  
ATOM   4091  CB  LYS B 400      40.123  -8.642  29.528  1.00 24.15           C  
ANISOU 4091  CB  LYS B 400     3682   3087   2408   -166    545   -285       C  
ATOM   4092  CG  LYS B 400      41.572  -8.404  29.103  1.00 32.81           C  
ANISOU 4092  CG  LYS B 400     4746   4196   3523   -164    632   -295       C  
ATOM   4093  CD  LYS B 400      42.478  -9.565  29.479  1.00 42.64           C  
ANISOU 4093  CD  LYS B 400     5937   5427   4839   -116    679   -351       C  
ATOM   4094  CE  LYS B 400      42.525  -9.786  30.977  1.00 49.64           C  
ANISOU 4094  CE  LYS B 400     6756   6292   5813    -63    655   -352       C  
ATOM   4095  NZ  LYS B 400      43.542 -10.818  31.347  1.00 55.96           N  
ANISOU 4095  NZ  LYS B 400     7502   7078   6682     -7    696   -397       N  
ATOM   4096  N   ALA B 401      36.984  -7.048  29.866  1.00 12.74           N  
ANISOU 4096  N   ALA B 401     2297   1652    892   -206    325   -182       N  
ATOM   4097  CA  ALA B 401      35.626  -7.322  30.366  1.00 15.85           C  
ANISOU 4097  CA  ALA B 401     2669   2041   1314   -201    233   -181       C  
ATOM   4098  C   ALA B 401      34.648  -7.928  29.340  1.00 17.06           C  
ANISOU 4098  C   ALA B 401     2889   2214   1379   -239    179   -208       C  
ATOM   4099  O   ALA B 401      33.886  -8.832  29.685  1.00 18.33           O  
ANISOU 4099  O   ALA B 401     3033   2365   1566   -244    146   -249       O  
ATOM   4100  CB  ALA B 401      35.019  -6.073  31.018  1.00 13.13           C  
ANISOU 4100  CB  ALA B 401     2276   1692   1019   -184    166   -118       C  
ATOM   4101  N   PRO B 402      34.653  -7.436  28.085  1.00 19.36           N  
ANISOU 4101  N   PRO B 402     3258   2534   1564   -271    168   -186       N  
ATOM   4102  CA  PRO B 402      33.696  -8.037  27.142  1.00 19.04           C  
ANISOU 4102  CA  PRO B 402     3258   2518   1458   -301    101   -212       C  
ATOM   4103  C   PRO B 402      33.988  -9.502  26.808  1.00 23.46           C  
ANISOU 4103  C   PRO B 402     3821   3066   2027   -310    153   -289       C  
ATOM   4104  O   PRO B 402      33.122 -10.181  26.250  1.00 20.71           O  
ANISOU 4104  O   PRO B 402     3492   2732   1644   -337    100   -325       O  
ATOM   4105  CB  PRO B 402      33.852  -7.172  25.882  1.00 21.54           C  
ANISOU 4105  CB  PRO B 402     3638   2864   1684   -319     86   -161       C  
ATOM   4106  CG  PRO B 402      34.381  -5.877  26.372  1.00 24.83           C  
ANISOU 4106  CG  PRO B 402     4046   3265   2122   -302    106    -92       C  
ATOM   4107  CD  PRO B 402      35.306  -6.247  27.503  1.00 20.12           C  
ANISOU 4107  CD  PRO B 402     3389   2640   1616   -278    194   -124       C  
ATOM   4108  N   GLN B 403      35.182  -9.981  27.145  1.00 20.08           N  
ANISOU 4108  N   GLN B 403     3369   2611   1649   -286    251   -313       N  
ATOM   4109  CA  GLN B 403      35.564 -11.356  26.841  1.00 21.61           C  
ANISOU 4109  CA  GLN B 403     3568   2784   1859   -285    303   -379       C  
ATOM   4110  C   GLN B 403      35.473 -12.296  28.049  1.00 20.35           C  
ANISOU 4110  C   GLN B 403     3360   2578   1793   -257    317   -413       C  
ATOM   4111  O   GLN B 403      35.665 -13.508  27.916  1.00 19.74           O  
ANISOU 4111  O   GLN B 403     3290   2471   1738   -253    351   -463       O  
ATOM   4112  CB  GLN B 403      36.976 -11.402  26.244  1.00 22.68           C  
ANISOU 4112  CB  GLN B 403     3711   2921   1987   -274    399   -389       C  
ATOM   4113  CG  GLN B 403      37.078 -10.848  24.823  1.00 33.28           C  
ANISOU 4113  CG  GLN B 403     5118   4301   3225   -310    400   -371       C  
ATOM   4114  CD  GLN B 403      37.138  -9.329  24.775  1.00 38.60           C  
ANISOU 4114  CD  GLN B 403     5801   4996   3868   -317    380   -295       C  
ATOM   4115  OE1 GLN B 403      36.418  -8.694  24.005  1.00 45.10           O  
ANISOU 4115  OE1 GLN B 403     6678   5847   4611   -344    315   -257       O  
ATOM   4116  NE2 GLN B 403      38.006  -8.742  25.591  1.00 36.55           N  
ANISOU 4116  NE2 GLN B 403     5490   4721   3675   -292    433   -271       N  
ATOM   4117  N   HIS B 404      35.176 -11.740  29.218  1.00 18.04           N  
ANISOU 4117  N   HIS B 404     3027   2275   1554   -237    291   -382       N  
ATOM   4118  CA  HIS B 404      35.131 -12.514  30.458  1.00 16.42           C  
ANISOU 4118  CA  HIS B 404     2780   2024   1436   -207    306   -402       C  
ATOM   4119  C   HIS B 404      33.989 -13.535  30.415  1.00 17.98           C  
ANISOU 4119  C   HIS B 404     2994   2202   1636   -241    264   -444       C  
ATOM   4120  O   HIS B 404      32.914 -13.260  29.869  1.00 18.40           O  
ANISOU 4120  O   HIS B 404     3065   2287   1640   -285    193   -447       O  
ATOM   4121  CB  HIS B 404      34.961 -11.563  31.654  1.00 16.74           C  
ANISOU 4121  CB  HIS B 404     2777   2064   1520   -185    282   -360       C  
ATOM   4122  CG  HIS B 404      35.313 -12.166  32.982  1.00 19.46           C  
ANISOU 4122  CG  HIS B 404     3075   2364   1955   -141    312   -365       C  
ATOM   4123  ND1 HIS B 404      34.557 -13.151  33.581  1.00 21.16           N  
ANISOU 4123  ND1 HIS B 404     3294   2541   2205   -149    298   -392       N  
ATOM   4124  CD2 HIS B 404      36.324 -11.895  33.842  1.00 21.73           C  
ANISOU 4124  CD2 HIS B 404     3315   2641   2300    -89    350   -344       C  
ATOM   4125  CE1 HIS B 404      35.095 -13.471  34.745  1.00 18.52           C  
ANISOU 4125  CE1 HIS B 404     2927   2171   1939   -101    327   -380       C  
ATOM   4126  NE2 HIS B 404      36.168 -12.722  34.929  1.00 20.30           N  
ANISOU 4126  NE2 HIS B 404     3117   2416   2178    -62    352   -353       N  
ATOM   4127  N   ALA B 405      34.228 -14.711  30.988  1.00 17.74           N  
ANISOU 4127  N   ALA B 405     2954   2119   1666   -221    304   -474       N  
ATOM   4128  CA  ALA B 405      33.215 -15.767  31.030  1.00 20.75           C  
ANISOU 4128  CA  ALA B 405     3352   2472   2062   -258    279   -515       C  
ATOM   4129  C   ALA B 405      31.943 -15.315  31.746  1.00 19.58           C  
ANISOU 4129  C   ALA B 405     3174   2332   1932   -290    213   -504       C  
ATOM   4130  O   ALA B 405      30.842 -15.751  31.407  1.00 21.14           O  
ANISOU 4130  O   ALA B 405     3377   2536   2118   -342    166   -537       O  
ATOM   4131  CB  ALA B 405      33.775 -17.016  31.695  1.00 22.61           C  
ANISOU 4131  CB  ALA B 405     3587   2638   2364   -224    337   -534       C  
ATOM   4132  N   GLN B 406      32.105 -14.446  32.740  1.00 16.71           N  
ANISOU 4132  N   GLN B 406     2776   1972   1604   -259    210   -463       N  
ATOM   4133  CA  GLN B 406      30.972 -13.925  33.499  1.00 16.27           C  
ANISOU 4133  CA  GLN B 406     2666   1929   1588   -277    149   -441       C  
ATOM   4134  C   GLN B 406      30.577 -12.542  32.976  1.00 17.51           C  
ANISOU 4134  C   GLN B 406     2793   2149   1712   -278     79   -396       C  
ATOM   4135  O   GLN B 406      31.414 -11.647  32.890  1.00 16.28           O  
ANISOU 4135  O   GLN B 406     2633   2009   1543   -243     94   -353       O  
ATOM   4136  CB  GLN B 406      31.302 -13.879  34.991  1.00 17.34           C  
ANISOU 4136  CB  GLN B 406     2756   2029   1802   -231    181   -406       C  
ATOM   4137  CG  GLN B 406      31.197 -15.237  35.690  1.00 16.41           C  
ANISOU 4137  CG  GLN B 406     2667   1842   1724   -238    228   -440       C  
ATOM   4138  CD  GLN B 406      32.246 -16.219  35.231  1.00 20.39           C  
ANISOU 4138  CD  GLN B 406     3217   2309   2220   -209    285   -460       C  
ATOM   4139  OE1 GLN B 406      33.438 -15.930  35.281  1.00 20.16           O  
ANISOU 4139  OE1 GLN B 406     3181   2284   2194   -154    318   -439       O  
ATOM   4140  NE2 GLN B 406      31.808 -17.388  34.775  1.00 20.90           N  
ANISOU 4140  NE2 GLN B 406     3313   2342   2286   -245    295   -499       N  
ATOM   4141  N   GLN B 407      29.302 -12.382  32.622  1.00 17.22           N  
ANISOU 4141  N   GLN B 407     2733   2143   1666   -319      1   -407       N  
ATOM   4142  CA  GLN B 407      28.839 -11.187  31.910  1.00 16.56           C  
ANISOU 4142  CA  GLN B 407     2636   2115   1541   -317    -79   -366       C  
ATOM   4143  C   GLN B 407      27.681 -10.452  32.582  1.00 16.71           C  
ANISOU 4143  C   GLN B 407     2568   2154   1628   -310   -150   -341       C  
ATOM   4144  O   GLN B 407      27.177  -9.463  32.047  1.00 16.07           O  
ANISOU 4144  O   GLN B 407     2470   2112   1525   -300   -226   -305       O  
ATOM   4145  CB  GLN B 407      28.420 -11.562  30.482  1.00 15.41           C  
ANISOU 4145  CB  GLN B 407     2553   2005   1298   -367   -127   -406       C  
ATOM   4146  CG  GLN B 407      29.584 -11.809  29.541  1.00 20.73           C  
ANISOU 4146  CG  GLN B 407     3317   2677   1883   -368    -64   -418       C  
ATOM   4147  CD  GLN B 407      30.360 -10.542  29.256  1.00 20.34           C  
ANISOU 4147  CD  GLN B 407     3280   2648   1800   -332    -57   -347       C  
ATOM   4148  OE1 GLN B 407      29.784  -9.527  28.853  1.00 18.21           O  
ANISOU 4148  OE1 GLN B 407     3003   2415   1503   -328   -136   -298       O  
ATOM   4149  NE2 GLN B 407      31.674 -10.587  29.471  1.00 17.48           N  
ANISOU 4149  NE2 GLN B 407     2936   2260   1447   -304     38   -342       N  
ATOM   4150  N   SER B 408      27.250 -10.921  33.749  1.00 15.70           N  
ANISOU 4150  N   SER B 408     2387   1997   1583   -313   -123   -358       N  
ATOM   4151  CA  SER B 408      26.047 -10.353  34.352  1.00 15.45           C  
ANISOU 4151  CA  SER B 408     2266   1985   1619   -314   -180   -349       C  
ATOM   4152  C   SER B 408      26.222  -8.896  34.775  1.00 15.03           C  
ANISOU 4152  C   SER B 408     2171   1944   1597   -258   -203   -285       C  
ATOM   4153  O   SER B 408      25.276  -8.113  34.723  1.00 14.77           O  
ANISOU 4153  O   SER B 408     2078   1940   1596   -248   -274   -270       O  
ATOM   4154  CB  SER B 408      25.570 -11.207  35.529  1.00 17.04           C  
ANISOU 4154  CB  SER B 408     2431   2150   1894   -338   -130   -383       C  
ATOM   4155  OG  SER B 408      25.203 -12.499  35.067  1.00 17.28           O  
ANISOU 4155  OG  SER B 408     2497   2164   1903   -400   -118   -447       O  
ATOM   4156  N   ILE B 409      27.432  -8.534  35.186  1.00 12.79           N  
ANISOU 4156  N   ILE B 409     1915   1634   1310   -220   -143   -251       N  
ATOM   4157  CA  ILE B 409      27.705  -7.152  35.575  1.00 12.11           C  
ANISOU 4157  CA  ILE B 409     1798   1551   1253   -173   -156   -195       C  
ATOM   4158  C   ILE B 409      27.687  -6.231  34.353  1.00 14.51           C  
ANISOU 4158  C   ILE B 409     2135   1882   1496   -165   -218   -156       C  
ATOM   4159  O   ILE B 409      27.071  -5.161  34.385  1.00 14.85           O  
ANISOU 4159  O   ILE B 409     2138   1934   1570   -139   -277   -120       O  
ATOM   4160  CB  ILE B 409      29.031  -7.028  36.360  1.00 12.04           C  
ANISOU 4160  CB  ILE B 409     1803   1512   1259   -143    -78   -177       C  
ATOM   4161  CG1 ILE B 409      28.937  -7.802  37.671  1.00 16.39           C  
ANISOU 4161  CG1 ILE B 409     2326   2036   1866   -143    -31   -203       C  
ATOM   4162  CG2 ILE B 409      29.360  -5.549  36.648  1.00 11.17           C  
ANISOU 4162  CG2 ILE B 409     1668   1401   1176   -105    -91   -126       C  
ATOM   4163  CD1 ILE B 409      30.268  -7.900  38.417  1.00 12.49           C  
ANISOU 4163  CD1 ILE B 409     1849   1517   1379   -111     34   -191       C  
ATOM   4164  N   ARG B 410      28.328  -6.652  33.265  1.00 13.41           N  
ANISOU 4164  N   ARG B 410     2074   1753   1269   -187   -204   -162       N  
ATOM   4165  CA  ARG B 410      28.276  -5.866  32.034  1.00 12.00           C  
ANISOU 4165  CA  ARG B 410     1946   1602   1013   -187   -263   -121       C  
ATOM   4166  C   ARG B 410      26.841  -5.644  31.581  1.00 15.34           C  
ANISOU 4166  C   ARG B 410     2333   2060   1438   -193   -375   -123       C  
ATOM   4167  O   ARG B 410      26.470  -4.534  31.206  1.00 18.12           O  
ANISOU 4167  O   ARG B 410     2681   2420   1783   -162   -442    -69       O  
ATOM   4168  CB  ARG B 410      29.102  -6.503  30.906  1.00 17.36           C  
ANISOU 4168  CB  ARG B 410     2720   2290   1585   -219   -222   -141       C  
ATOM   4169  CG  ARG B 410      30.596  -6.226  31.011  1.00 19.02           C  
ANISOU 4169  CG  ARG B 410     2965   2477   1784   -204   -127   -119       C  
ATOM   4170  CD  ARG B 410      31.329  -6.652  29.738  1.00 18.97           C  
ANISOU 4170  CD  ARG B 410     3055   2488   1667   -236    -87   -135       C  
ATOM   4171  NE  ARG B 410      31.155  -5.693  28.645  1.00 21.00           N  
ANISOU 4171  NE  ARG B 410     3373   2770   1837   -244   -140    -81       N  
ATOM   4172  CZ  ARG B 410      30.481  -5.936  27.522  1.00 23.99           C  
ANISOU 4172  CZ  ARG B 410     3812   3186   2118   -274   -208    -91       C  
ATOM   4173  NH1 ARG B 410      29.910  -7.116  27.322  1.00 24.06           N  
ANISOU 4173  NH1 ARG B 410     3823   3210   2110   -307   -228   -162       N  
ATOM   4174  NH2 ARG B 410      30.386  -4.994  26.591  1.00 23.03           N  
ANISOU 4174  NH2 ARG B 410     3755   3082   1912   -275   -258    -28       N  
ATOM   4175  N   GLU B 411      26.029  -6.692  31.647  1.00 15.29           N  
ANISOU 4175  N   GLU B 411     2296   2068   1446   -230   -395   -186       N  
ATOM   4176  CA  GLU B 411      24.634  -6.591  31.221  1.00 17.70           C  
ANISOU 4176  CA  GLU B 411     2549   2415   1760   -241   -505   -202       C  
ATOM   4177  C   GLU B 411      23.878  -5.615  32.111  1.00 20.00           C  
ANISOU 4177  C   GLU B 411     2740   2701   2158   -194   -543   -172       C  
ATOM   4178  O   GLU B 411      23.095  -4.790  31.628  1.00 20.06           O  
ANISOU 4178  O   GLU B 411     2717   2735   2169   -164   -642   -141       O  
ATOM   4179  CB  GLU B 411      23.960  -7.964  31.244  1.00 19.33           C  
ANISOU 4179  CB  GLU B 411     2734   2633   1977   -303   -504   -286       C  
ATOM   4180  CG  GLU B 411      24.342  -8.843  30.063  1.00 22.48           C  
ANISOU 4180  CG  GLU B 411     3231   3049   2263   -353   -502   -326       C  
ATOM   4181  CD  GLU B 411      24.068  -8.157  28.737  1.00 26.12           C  
ANISOU 4181  CD  GLU B 411     3741   3560   2623   -348   -604   -292       C  
ATOM   4182  OE1 GLU B 411      22.902  -7.775  28.493  1.00 25.53           O  
ANISOU 4182  OE1 GLU B 411     3604   3528   2569   -343   -717   -291       O  
ATOM   4183  OE2 GLU B 411      25.028  -7.981  27.954  1.00 29.10           O  
ANISOU 4183  OE2 GLU B 411     4220   3937   2902   -346   -571   -264       O  
ATOM   4184  N   LYS B 412      24.129  -5.716  33.413  1.00 16.97           N  
ANISOU 4184  N   LYS B 412     2310   2281   1857   -183   -464   -183       N  
ATOM   4185  CA  LYS B 412      23.495  -4.854  34.402  1.00 18.25           C  
ANISOU 4185  CA  LYS B 412     2380   2433   2122   -141   -476   -167       C  
ATOM   4186  C   LYS B 412      23.801  -3.385  34.128  1.00 17.81           C  
ANISOU 4186  C   LYS B 412     2341   2364   2063    -82   -514    -94       C  
ATOM   4187  O   LYS B 412      22.915  -2.529  34.188  1.00 18.46           O  
ANISOU 4187  O   LYS B 412     2359   2453   2201    -42   -584    -75       O  
ATOM   4188  CB  LYS B 412      23.991  -5.246  35.798  1.00 14.85           C  
ANISOU 4188  CB  LYS B 412     1927   1964   1750   -144   -373   -187       C  
ATOM   4189  CG  LYS B 412      23.583  -4.326  36.940  1.00 17.26           C  
ANISOU 4189  CG  LYS B 412     2154   2253   2151   -103   -361   -174       C  
ATOM   4190  CD  LYS B 412      24.239  -4.839  38.229  1.00 13.49           C  
ANISOU 4190  CD  LYS B 412     1682   1743   1702   -112   -259   -192       C  
ATOM   4191  CE  LYS B 412      23.951  -3.969  39.439  1.00 18.76           C  
ANISOU 4191  CE  LYS B 412     2285   2393   2450    -77   -234   -188       C  
ATOM   4192  NZ  LYS B 412      24.604  -4.560  40.657  1.00 17.41           N  
ANISOU 4192  NZ  LYS B 412     2132   2196   2287    -89   -143   -204       N  
ATOM   4193  N   TYR B 413      25.058  -3.101  33.808  1.00 15.74           N  
ANISOU 4193  N   TYR B 413     2163   2078   1738    -78   -463    -55       N  
ATOM   4194  CA  TYR B 413      25.496  -1.720  33.596  1.00 14.45           C  
ANISOU 4194  CA  TYR B 413     2029   1888   1572    -32   -479     16       C  
ATOM   4195  C   TYR B 413      25.277  -1.185  32.163  1.00 17.30           C  
ANISOU 4195  C   TYR B 413     2458   2270   1846    -24   -567     67       C  
ATOM   4196  O   TYR B 413      25.678  -0.065  31.850  1.00 19.72           O  
ANISOU 4196  O   TYR B 413     2808   2546   2137      8   -578    134       O  
ATOM   4197  CB  TYR B 413      26.943  -1.534  34.093  1.00 13.20           C  
ANISOU 4197  CB  TYR B 413     1914   1693   1407    -34   -377     32       C  
ATOM   4198  CG  TYR B 413      27.005  -1.410  35.604  1.00 14.80           C  
ANISOU 4198  CG  TYR B 413     2048   1870   1707    -17   -321      8       C  
ATOM   4199  CD1 TYR B 413      27.036  -2.541  36.420  1.00 14.00           C  
ANISOU 4199  CD1 TYR B 413     1918   1773   1628    -42   -267    -47       C  
ATOM   4200  CD2 TYR B 413      26.999  -0.165  36.216  1.00 15.68           C  
ANISOU 4200  CD2 TYR B 413     2128   1947   1882     23   -322     40       C  
ATOM   4201  CE1 TYR B 413      27.068  -2.429  37.798  1.00 13.86           C  
ANISOU 4201  CE1 TYR B 413     1849   1736   1683    -29   -219    -65       C  
ATOM   4202  CE2 TYR B 413      27.029  -0.044  37.593  1.00 14.56           C  
ANISOU 4202  CE2 TYR B 413     1929   1785   1817     35   -272     12       C  
ATOM   4203  CZ  TYR B 413      27.068  -1.176  38.377  1.00 15.64           C  
ANISOU 4203  CZ  TYR B 413     2043   1935   1963      9   -222    -39       C  
ATOM   4204  OH  TYR B 413      27.097  -1.054  39.748  1.00 16.56           O  
ANISOU 4204  OH  TYR B 413     2115   2036   2141     19   -174    -63       O  
ATOM   4205  N   LYS B 414      24.624  -1.974  31.310  1.00 15.28           N  
ANISOU 4205  N   LYS B 414     2213   2062   1529    -56   -632     36       N  
ATOM   4206  CA  LYS B 414      24.124  -1.451  30.036  1.00 18.85           C  
ANISOU 4206  CA  LYS B 414     2718   2544   1902    -42   -742     82       C  
ATOM   4207  C   LYS B 414      22.844  -0.638  30.252  1.00 22.60           C  
ANISOU 4207  C   LYS B 414     3101   3026   2462     16   -850    102       C  
ATOM   4208  O   LYS B 414      22.462   0.181  29.410  1.00 20.95           O  
ANISOU 4208  O   LYS B 414     2927   2822   2209     55   -948    163       O  
ATOM   4209  CB  LYS B 414      23.858  -2.582  29.032  1.00 21.70           C  
ANISOU 4209  CB  LYS B 414     3125   2960   2162    -99   -782     32       C  
ATOM   4210  CG  LYS B 414      25.108  -3.266  28.504  1.00 24.37           C  
ANISOU 4210  CG  LYS B 414     3570   3291   2398   -147   -687     18       C  
ATOM   4211  CD  LYS B 414      24.760  -4.356  27.496  1.00 23.93           C  
ANISOU 4211  CD  LYS B 414     3562   3286   2242   -205   -729    -40       C  
ATOM   4212  CE  LYS B 414      26.008  -5.039  26.954  1.00 29.20           C  
ANISOU 4212  CE  LYS B 414     4337   3945   2813   -248   -625    -61       C  
ATOM   4213  NZ  LYS B 414      25.667  -6.214  26.090  1.00 26.76           N  
ANISOU 4213  NZ  LYS B 414     4074   3678   2416   -309   -652   -135       N  
ATOM   4214  N   ASN B 415      22.180  -0.888  31.377  1.00 21.63           N  
ANISOU 4214  N   ASN B 415     2860   2900   2458     23   -830     49       N  
ATOM   4215  CA  ASN B 415      20.942  -0.196  31.748  1.00 21.86           C  
ANISOU 4215  CA  ASN B 415     2778   2936   2591     79   -914     50       C  
ATOM   4216  C   ASN B 415      21.109   1.319  31.729  1.00 20.71           C  
ANISOU 4216  C   ASN B 415     2657   2739   2474    155   -942    134       C  
ATOM   4217  O   ASN B 415      22.135   1.840  32.163  1.00 21.90           O  
ANISOU 4217  O   ASN B 415     2861   2835   2625    160   -855    168       O  
ATOM   4218  CB  ASN B 415      20.510  -0.641  33.149  1.00 25.39           C  
ANISOU 4218  CB  ASN B 415     3113   3376   3159     67   -842    -18       C  
ATOM   4219  CG  ASN B 415      19.055  -0.312  33.463  1.00 33.89           C  
ANISOU 4219  CG  ASN B 415     4053   4479   4345    106   -922    -48       C  
ATOM   4220  OD1 ASN B 415      18.490   0.657  32.953  1.00 33.98           O  
ANISOU 4220  OD1 ASN B 415     4044   4491   4376    172  -1023     -1       O  
ATOM   4221  ND2 ASN B 415      18.446  -1.121  34.324  1.00 35.52           N  
ANISOU 4221  ND2 ASN B 415     4165   4705   4627     65   -873   -126       N  
ATOM   4222  N   SER B 416      20.089   2.027  31.245  1.00 23.65           N  
ANISOU 4222  N   SER B 416     2984   3124   2876    215  -1067    166       N  
ATOM   4223  CA  SER B 416      20.114   3.488  31.231  1.00 28.29           C  
ANISOU 4223  CA  SER B 416     3593   3650   3504    296  -1102    247       C  
ATOM   4224  C   SER B 416      20.182   4.050  32.654  1.00 25.69           C  
ANISOU 4224  C   SER B 416     3188   3265   3310    327  -1012    223       C  
ATOM   4225  O   SER B 416      20.683   5.149  32.876  1.00 25.11           O  
ANISOU 4225  O   SER B 416     3157   3120   3263    370   -984    279       O  
ATOM   4226  CB  SER B 416      18.898   4.047  30.482  1.00 34.53           C  
ANISOU 4226  CB  SER B 416     4338   4468   4312    365  -1260    279       C  
ATOM   4227  OG  SER B 416      17.686   3.662  31.108  1.00 38.08           O  
ANISOU 4227  OG  SER B 416     4629   4963   4878    376  -1285    201       O  
ATOM   4228  N   LYS B 417      19.681   3.274  33.609  1.00 29.15           N  
ANISOU 4228  N   LYS B 417     3517   3732   3825    298   -963    137       N  
ATOM   4229  CA  LYS B 417      19.797   3.587  35.029  1.00 31.55           C  
ANISOU 4229  CA  LYS B 417     3757   3994   4236    310   -863    100       C  
ATOM   4230  C   LYS B 417      21.254   3.843  35.422  1.00 28.86           C  
ANISOU 4230  C   LYS B 417     3514   3600   3853    284   -755    128       C  
ATOM   4231  O   LYS B 417      21.543   4.677  36.286  1.00 28.05           O  
ANISOU 4231  O   LYS B 417     3398   3441   3820    315   -699    134       O  
ATOM   4232  CB  LYS B 417      19.217   2.428  35.844  1.00 36.91           C  
ANISOU 4232  CB  LYS B 417     4339   4720   4965    257   -813      6       C  
ATOM   4233  CG  LYS B 417      19.781   2.254  37.238  1.00 45.53           C  
ANISOU 4233  CG  LYS B 417     5415   5780   6104    232   -681    -34       C  
ATOM   4234  CD  LYS B 417      19.523   0.836  37.732  1.00 52.02           C  
ANISOU 4234  CD  LYS B 417     6196   6645   6922    158   -626   -108       C  
ATOM   4235  CE  LYS B 417      18.514   0.795  38.863  1.00 57.50           C  
ANISOU 4235  CE  LYS B 417     6766   7349   7734    163   -588   -173       C  
ATOM   4236  NZ  LYS B 417      18.016  -0.593  39.089  1.00 62.08           N  
ANISOU 4236  NZ  LYS B 417     7304   7972   8310     86   -555   -240       N  
ATOM   4237  N   TYR B 418      22.170   3.126  34.776  1.00 20.92           N  
ANISOU 4237  N   TYR B 418     2601   2613   2733    227   -725    140       N  
ATOM   4238  CA  TYR B 418      23.602   3.306  35.020  1.00 20.23           C  
ANISOU 4238  CA  TYR B 418     2599   2486   2603    200   -628    164       C  
ATOM   4239  C   TYR B 418      24.272   4.000  33.843  1.00 23.49           C  
ANISOU 4239  C   TYR B 418     3127   2873   2925    206   -658    245       C  
ATOM   4240  O   TYR B 418      25.479   3.864  33.635  1.00 21.35           O  
ANISOU 4240  O   TYR B 418     2935   2589   2587    166   -585    261       O  
ATOM   4241  CB  TYR B 418      24.276   1.962  35.287  1.00 17.87           C  
ANISOU 4241  CB  TYR B 418     2316   2219   2253    132   -549    111       C  
ATOM   4242  CG  TYR B 418      23.806   1.309  36.568  1.00 20.55           C  
ANISOU 4242  CG  TYR B 418     2564   2570   2673    118   -498     40       C  
ATOM   4243  CD1 TYR B 418      24.064   1.892  37.803  1.00 26.26           C  
ANISOU 4243  CD1 TYR B 418     3251   3254   3471    139   -433     27       C  
ATOM   4244  CD2 TYR B 418      23.108   0.111  36.538  1.00 19.55           C  
ANISOU 4244  CD2 TYR B 418     2396   2491   2542     79   -511    -16       C  
ATOM   4245  CE1 TYR B 418      23.633   1.295  38.979  1.00 26.70           C  
ANISOU 4245  CE1 TYR B 418     3236   3322   3586    123   -381    -35       C  
ATOM   4246  CE2 TYR B 418      22.674  -0.493  37.702  1.00 23.92           C  
ANISOU 4246  CE2 TYR B 418     2877   3050   3163     60   -455    -76       C  
ATOM   4247  CZ  TYR B 418      22.938   0.105  38.919  1.00 30.48           C  
ANISOU 4247  CZ  TYR B 418     3679   3845   4058     83   -389    -82       C  
ATOM   4248  OH  TYR B 418      22.505  -0.501  40.076  1.00 37.49           O  
ANISOU 4248  OH  TYR B 418     4507   4739   4999     60   -329   -138       O  
ATOM   4249  N   HIS B 419      23.473   4.738  33.081  1.00 20.25           N  
ANISOU 4249  N   HIS B 419     2724   2456   2514    258   -765    298       N  
ATOM   4250  CA  HIS B 419      23.963   5.527  31.949  1.00 25.31           C  
ANISOU 4250  CA  HIS B 419     3485   3066   3067    271   -803    389       C  
ATOM   4251  C   HIS B 419      24.704   4.696  30.896  1.00 23.78           C  
ANISOU 4251  C   HIS B 419     3393   2915   2726    205   -785    397       C  
ATOM   4252  O   HIS B 419      25.524   5.227  30.147  1.00 23.51           O  
ANISOU 4252  O   HIS B 419     3473   2851   2609    190   -762    462       O  
ATOM   4253  CB  HIS B 419      24.838   6.677  32.453  1.00 27.66           C  
ANISOU 4253  CB  HIS B 419     3826   3276   3407    286   -728    432       C  
ATOM   4254  CG  HIS B 419      24.232   7.425  33.598  1.00 35.44           C  
ANISOU 4254  CG  HIS B 419     4716   4214   4535    343   -723    408       C  
ATOM   4255  ND1 HIS B 419      24.509   7.124  34.915  1.00 36.77           N  
ANISOU 4255  ND1 HIS B 419     4812   4379   4778    322   -632    336       N  
ATOM   4256  CD2 HIS B 419      23.331   8.435  33.625  1.00 41.21           C  
ANISOU 4256  CD2 HIS B 419     5412   4900   5347    423   -799    442       C  
ATOM   4257  CE1 HIS B 419      23.820   7.930  35.703  1.00 39.70           C  
ANISOU 4257  CE1 HIS B 419     5111   4707   5265    380   -644    323       C  
ATOM   4258  NE2 HIS B 419      23.096   8.735  34.945  1.00 42.83           N  
ANISOU 4258  NE2 HIS B 419     5525   5075   5675    446   -743    384       N  
ATOM   4259  N   GLY B 420      24.395   3.401  30.837  1.00 20.83           N  
ANISOU 4259  N   GLY B 420     2981   2609   2323    162   -790    327       N  
ATOM   4260  CA  GLY B 420      25.009   2.492  29.881  1.00 23.94           C  
ANISOU 4260  CA  GLY B 420     3464   3046   2585    100   -769    316       C  
ATOM   4261  C   GLY B 420      26.531   2.458  29.898  1.00 21.18           C  
ANISOU 4261  C   GLY B 420     3195   2668   2185     56   -644    327       C  
ATOM   4262  O   GLY B 420      27.166   2.210  28.872  1.00 19.57           O  
ANISOU 4262  O   GLY B 420     3094   2481   1862     18   -626    349       O  
ATOM   4263  N   VAL B 421      27.126   2.681  31.064  1.00 20.87           N  
ANISOU 4263  N   VAL B 421     3105   2589   2235     60   -555    306       N  
ATOM   4264  CA  VAL B 421      28.577   2.839  31.140  1.00 17.66           C  
ANISOU 4264  CA  VAL B 421     2758   2154   1801     25   -443    317       C  
ATOM   4265  C   VAL B 421      29.378   1.615  30.717  1.00 15.80           C  
ANISOU 4265  C   VAL B 421     2561   1958   1483    -31   -376    270       C  
ATOM   4266  O   VAL B 421      30.522   1.748  30.285  1.00 20.56           O  
ANISOU 4266  O   VAL B 421     3233   2550   2030    -63   -299    289       O  
ATOM   4267  CB  VAL B 421      29.041   3.298  32.545  1.00 16.95           C  
ANISOU 4267  CB  VAL B 421     2597   2020   1823     40   -372    295       C  
ATOM   4268  CG1 VAL B 421      28.606   4.731  32.807  1.00 17.81           C  
ANISOU 4268  CG1 VAL B 421     2697   2069   2002     90   -412    349       C  
ATOM   4269  CG2 VAL B 421      28.516   2.348  33.621  1.00 17.16           C  
ANISOU 4269  CG2 VAL B 421     2525   2075   1919     42   -362    218       C  
ATOM   4270  N   SER B 422      28.802   0.420  30.821  1.00 16.24           N  
ANISOU 4270  N   SER B 422     2576   2059   1536    -46   -397    206       N  
ATOM   4271  CA  SER B 422      29.552  -0.770  30.397  1.00 17.83           C  
ANISOU 4271  CA  SER B 422     2822   2289   1665    -95   -331    157       C  
ATOM   4272  C   SER B 422      29.807  -0.788  28.876  1.00 18.76           C  
ANISOU 4272  C   SER B 422     3053   2431   1644   -125   -348    187       C  
ATOM   4273  O   SER B 422      30.618  -1.577  28.389  1.00 20.59           O  
ANISOU 4273  O   SER B 422     3337   2679   1806   -165   -277    152       O  
ATOM   4274  CB  SER B 422      28.884  -2.067  30.870  1.00 15.86           C  
ANISOU 4274  CB  SER B 422     2512   2067   1448   -110   -342     80       C  
ATOM   4275  OG  SER B 422      27.587  -2.204  30.338  1.00 18.92           O  
ANISOU 4275  OG  SER B 422     2882   2489   1817   -108   -450     74       O  
ATOM   4276  N   LEU B 423      29.125   0.093  28.142  1.00 17.86           N  
ANISOU 4276  N   LEU B 423     2981   2318   1487   -104   -442    252       N  
ATOM   4277  CA  LEU B 423      29.310   0.220  26.697  1.00 21.08           C  
ANISOU 4277  CA  LEU B 423     3512   2749   1749   -131   -467    294       C  
ATOM   4278  C   LEU B 423      30.423   1.201  26.309  1.00 26.55           C  
ANISOU 4278  C   LEU B 423     4291   3399   2397   -143   -390    363       C  
ATOM   4279  O   LEU B 423      30.802   1.288  25.138  1.00 26.44           O  
ANISOU 4279  O   LEU B 423     4381   3400   2264   -173   -376    394       O  
ATOM   4280  CB  LEU B 423      28.003   0.654  26.033  1.00 25.64           C  
ANISOU 4280  CB  LEU B 423     4101   3351   2291    -98   -619    336       C  
ATOM   4281  CG  LEU B 423      26.816  -0.287  26.224  1.00 31.02           C  
ANISOU 4281  CG  LEU B 423     4697   4082   3007    -98   -705    264       C  
ATOM   4282  CD1 LEU B 423      25.543   0.343  25.671  1.00 35.54           C  
ANISOU 4282  CD1 LEU B 423     5259   4678   3567    -53   -864    311       C  
ATOM   4283  CD2 LEU B 423      27.091  -1.624  25.568  1.00 29.05           C  
ANISOU 4283  CD2 LEU B 423     4498   3880   2661   -162   -671    191       C  
ATOM   4284  N   LEU B 424      30.933   1.951  27.282  1.00 22.31           N  
ANISOU 4284  N   LEU B 424     3702   2809   1967   -122   -333    381       N  
ATOM   4285  CA  LEU B 424      32.008   2.904  27.011  1.00 22.38           C  
ANISOU 4285  CA  LEU B 424     3781   2772   1951   -143   -250    440       C  
ATOM   4286  C   LEU B 424      33.294   2.169  26.663  1.00 28.53           C  
ANISOU 4286  C   LEU B 424     4597   3573   2669   -201   -124    395       C  
ATOM   4287  O   LEU B 424      33.551   1.076  27.164  1.00 27.26           O  
ANISOU 4287  O   LEU B 424     4375   3442   2542   -210    -81    315       O  
ATOM   4288  CB  LEU B 424      32.250   3.819  28.214  1.00 23.73           C  
ANISOU 4288  CB  LEU B 424     3877   2883   2258   -114   -219    453       C  
ATOM   4289  CG  LEU B 424      31.142   4.801  28.592  1.00 28.58           C  
ANISOU 4289  CG  LEU B 424     4458   3456   2946    -51   -322    502       C  
ATOM   4290  CD1 LEU B 424      31.540   5.600  29.822  1.00 28.47           C  
ANISOU 4290  CD1 LEU B 424     4375   3381   3060    -33   -269    497       C  
ATOM   4291  CD2 LEU B 424      30.813   5.724  27.429  1.00 35.12           C  
ANISOU 4291  CD2 LEU B 424     5402   4256   3684    -39   -388    601       C  
ATOM   4292  N   ASN B 425      34.100   2.773  25.797  1.00 27.71           N  
ANISOU 4292  N   ASN B 425     4586   3454   2489   -238    -60    443       N  
ATOM   4293  CA  ASN B 425      35.403   2.221  25.472  1.00 29.82           C  
ANISOU 4293  CA  ASN B 425     4858   3741   2732   -287     72    392       C  
ATOM   4294  C   ASN B 425      36.436   2.585  26.536  1.00 24.01           C  
ANISOU 4294  C   ASN B 425     4067   2968   2087   -299    172    379       C  
ATOM   4295  O   ASN B 425      36.604   3.755  26.874  1.00 27.80           O  
ANISOU 4295  O   ASN B 425     4549   3395   2620   -296    179    434       O  
ATOM   4296  CB  ASN B 425      35.866   2.712  24.097  1.00 38.18           C  
ANISOU 4296  CB  ASN B 425     5999   4803   3705   -318    107    431       C  
ATOM   4297  CG  ASN B 425      34.955   2.251  22.976  1.00 46.02           C  
ANISOU 4297  CG  ASN B 425     7047   5841   4598   -311     18    434       C  
ATOM   4298  OD1 ASN B 425      34.562   1.085  22.916  1.00 46.75           O  
ANISOU 4298  OD1 ASN B 425     7116   5979   4668   -311     -8    367       O  
ATOM   4299  ND2 ASN B 425      34.606   3.171  22.083  1.00 52.70           N  
ANISOU 4299  ND2 ASN B 425     7965   6673   5385   -305    -30    511       N  
ATOM   4300  N   PRO B 426      37.120   1.578  27.085  1.00 25.41           N  
ANISOU 4300  N   PRO B 426     4173   3174   2309   -306    243    296       N  
ATOM   4301  CA  PRO B 426      38.201   1.894  28.019  1.00 24.67           C  
ANISOU 4301  CA  PRO B 426     3998   3058   2319   -312    331    270       C  
ATOM   4302  C   PRO B 426      39.342   2.579  27.269  1.00 27.69           C  
ANISOU 4302  C   PRO B 426     4435   3427   2660   -368    436    297       C  
ATOM   4303  O   PRO B 426      39.531   2.318  26.083  1.00 24.71           O  
ANISOU 4303  O   PRO B 426     4111   3074   2203   -389    454    294       O  
ATOM   4304  CB  PRO B 426      38.637   0.517  28.535  1.00 23.40           C  
ANISOU 4304  CB  PRO B 426     3763   2935   2193   -299    372    178       C  
ATOM   4305  CG  PRO B 426      38.159  -0.454  27.519  1.00 31.41           C  
ANISOU 4305  CG  PRO B 426     4850   3987   3098   -311    351    155       C  
ATOM   4306  CD  PRO B 426      36.910   0.129  26.934  1.00 31.23           C  
ANISOU 4306  CD  PRO B 426     4894   3958   3012   -303    238    221       C  
ATOM   4307  N   PRO B 427      40.080   3.467  27.945  1.00 27.66           N  
ANISOU 4307  N   PRO B 427     4391   3384   2736   -387    494    311       N  
ATOM   4308  CA  PRO B 427      41.242   4.069  27.291  1.00 26.14           C  
ANISOU 4308  CA  PRO B 427     4209   3183   2542   -436    589    315       C  
ATOM   4309  C   PRO B 427      42.302   2.997  27.070  1.00 23.45           C  
ANISOU 4309  C   PRO B 427     3813   2894   2203   -451    678    230       C  
ATOM   4310  O   PRO B 427      42.433   2.078  27.880  1.00 20.86           O  
ANISOU 4310  O   PRO B 427     3409   2592   1924   -423    685    168       O  
ATOM   4311  CB  PRO B 427      41.713   5.106  28.314  1.00 29.25           C  
ANISOU 4311  CB  PRO B 427     4548   3526   3040   -451    622    329       C  
ATOM   4312  CG  PRO B 427      41.262   4.566  29.626  1.00 30.88           C  
ANISOU 4312  CG  PRO B 427     4657   3742   3333   -398    565    284       C  
ATOM   4313  CD  PRO B 427      39.955   3.875  29.355  1.00 29.02           C  
ANISOU 4313  CD  PRO B 427     4456   3527   3042   -350    458    294       C  
ATOM   4314  N   GLU B 428      43.037   3.095  25.971  1.00 25.22           N  
ANISOU 4314  N   GLU B 428     4077   3131   2376   -490    744    229       N  
ATOM   4315  CA  GLU B 428      44.042   2.091  25.650  1.00 29.54           C  
ANISOU 4315  CA  GLU B 428     4575   3721   2927   -499    826    150       C  
ATOM   4316  C   GLU B 428      45.172   2.120  26.666  1.00 27.25           C  
ANISOU 4316  C   GLU B 428     4165   3434   2754   -503    898     96       C  
ATOM   4317  O   GLU B 428      45.747   1.086  27.004  1.00 27.40           O  
ANISOU 4317  O   GLU B 428     4108   3487   2815   -477    931     24       O  
ATOM   4318  CB  GLU B 428      44.617   2.343  24.253  1.00 37.74           C  
ANISOU 4318  CB  GLU B 428     5687   4768   3887   -546    889    164       C  
ATOM   4319  CG  GLU B 428      43.599   2.832  23.236  1.00 48.81           C  
ANISOU 4319  CG  GLU B 428     7213   6156   5176   -551    817    240       C  
ATOM   4320  CD  GLU B 428      44.142   2.801  21.818  1.00 60.76           C  
ANISOU 4320  CD  GLU B 428     8802   7687   6596   -595    882    242       C  
ATOM   4321  OE1 GLU B 428      44.563   3.864  21.311  1.00 62.56           O  
ANISOU 4321  OE1 GLU B 428     9080   7886   6804   -637    925    294       O  
ATOM   4322  OE2 GLU B 428      44.152   1.709  21.211  1.00 66.54           O  
ANISOU 4322  OE2 GLU B 428     9547   8460   7275   -588    893    190       O  
ATOM   4323  N   THR B 429      45.496   3.316  27.141  1.00 22.70           N  
ANISOU 4323  N   THR B 429     3570   2821   2235   -533    916    131       N  
ATOM   4324  CA  THR B 429      46.573   3.476  28.103  1.00 21.07           C  
ANISOU 4324  CA  THR B 429     3243   2620   2142   -543    974     79       C  
ATOM   4325  C   THR B 429      46.185   4.490  29.160  1.00 22.04           C  
ANISOU 4325  C   THR B 429     3342   2697   2334   -546    934    114       C  
ATOM   4326  O   THR B 429      45.292   5.314  28.952  1.00 21.48           O  
ANISOU 4326  O   THR B 429     3356   2578   2226   -551    880    189       O  
ATOM   4327  CB  THR B 429      47.870   3.960  27.431  1.00 33.34           C  
ANISOU 4327  CB  THR B 429     4780   4179   3710   -601   1075     61       C  
ATOM   4328  OG1 THR B 429      48.927   3.983  28.399  1.00 39.56           O  
ANISOU 4328  OG1 THR B 429     5435   4983   4614   -605   1118     -2       O  
ATOM   4329  CG2 THR B 429      47.680   5.354  26.875  1.00 30.80           C  
ANISOU 4329  CG2 THR B 429     4547   3802   3353   -652   1080    139       C  
ATOM   4330  N   LEU B 430      46.851   4.417  30.305  1.00 20.56           N  
ANISOU 4330  N   LEU B 430     3035   2523   2252   -539    954     59       N  
ATOM   4331  CA  LEU B 430      46.657   5.397  31.360  1.00 22.02           C  
ANISOU 4331  CA  LEU B 430     3185   2665   2516   -551    927     77       C  
ATOM   4332  C   LEU B 430      47.777   6.420  31.250  1.00 25.44           C  
ANISOU 4332  C   LEU B 430     3582   3078   3004   -615    995     67       C  
ATOM   4333  O   LEU B 430      48.685   6.260  30.435  1.00 27.40           O  
ANISOU 4333  O   LEU B 430     3826   3353   3231   -645   1064     43       O  
ATOM   4334  CB  LEU B 430      46.665   4.720  32.729  1.00 21.20           C  
ANISOU 4334  CB  LEU B 430     2967   2593   2494   -499    885     17       C  
ATOM   4335  CG  LEU B 430      45.583   3.648  32.910  1.00 21.73           C  
ANISOU 4335  CG  LEU B 430     3055   2679   2522   -420    792     17       C  
ATOM   4336  CD1 LEU B 430      45.581   3.117  34.336  1.00 22.46           C  
ANISOU 4336  CD1 LEU B 430     3040   2793   2699   -360    729    -35       C  
ATOM   4337  CD2 LEU B 430      44.211   4.183  32.531  1.00 23.58           C  
ANISOU 4337  CD2 LEU B 430     3393   2867   2698   -408    712     93       C  
ATOM   4338  N   ASN B 431      47.719   7.479  32.046  1.00 23.17           N  
ANISOU 4338  N   ASN B 431     3273   2742   2789   -638    977     80       N  
ATOM   4339  CA  ASN B 431      48.740   8.519  31.933  1.00 27.13           C  
ANISOU 4339  CA  ASN B 431     3749   3219   3341   -704   1039     69       C  
ATOM   4340  C   ASN B 431      49.541   8.704  33.218  1.00 34.90           C  
ANISOU 4340  C   ASN B 431     4594   4222   4444   -715   1041     -6       C  
ATOM   4341  O   ASN B 431      49.895   9.822  33.586  1.00 36.38           O  
ANISOU 4341  O   ASN B 431     4768   4365   4690   -762   1053     -7       O  
ATOM   4342  CB  ASN B 431      48.133   9.847  31.454  1.00 27.18           C  
ANISOU 4342  CB  ASN B 431     3870   3138   3319   -736   1024    155       C  
ATOM   4343  CG  ASN B 431      47.200  10.474  32.475  1.00 25.52           C  
ANISOU 4343  CG  ASN B 431     3665   2869   3163   -710    949    180       C  
ATOM   4344  OD1 ASN B 431      46.740   9.816  33.415  1.00 25.84           O  
ANISOU 4344  OD1 ASN B 431     3647   2933   3237   -665    900    147       O  
ATOM   4345  ND2 ASN B 431      46.909  11.760  32.290  1.00 21.94           N  
ANISOU 4345  ND2 ASN B 431     3284   2333   2720   -735    940    238       N  
ATOM   4346  N   LEU B 432      49.828   7.592  33.887  1.00 34.75           N  
ANISOU 4346  N   LEU B 432     4474   4271   4459   -668   1024    -72       N  
ATOM   4347  CA  LEU B 432      50.554   7.620  35.149  1.00 38.98           C  
ANISOU 4347  CA  LEU B 432     4872   4838   5099   -664   1005   -146       C  
ATOM   4348  C   LEU B 432      52.039   7.863  34.909  1.00 48.85           C  
ANISOU 4348  C   LEU B 432     6044   6121   6398   -711   1071   -201       C  
ATOM   4349  O   LEU B 432      52.727   8.468  35.733  1.00 53.58           O  
ANISOU 4349  O   LEU B 432     6556   6724   7080   -739   1063   -248       O  
ATOM   4350  CB  LEU B 432      50.358   6.306  35.912  1.00 36.71           C  
ANISOU 4350  CB  LEU B 432     4510   4614   4826   -586    956   -191       C  
ATOM   4351  CG  LEU B 432      48.930   5.770  36.036  1.00 37.73           C  
ANISOU 4351  CG  LEU B 432     4716   4725   4896   -522    881   -145       C  
ATOM   4352  CD1 LEU B 432      48.885   4.573  36.972  1.00 40.17           C  
ANISOU 4352  CD1 LEU B 432     4945   5088   5229   -435    810   -194       C  
ATOM   4353  CD2 LEU B 432      47.972   6.846  36.501  1.00 30.48           C  
ANISOU 4353  CD2 LEU B 432     3858   3736   3988   -528    817    -96       C  
ATOM   4354  OXT LEU B 432      52.584   7.460  33.882  1.00 49.03           O  
ANISOU 4354  OXT LEU B 432     6086   6165   6378   -723   1133   -202       O  
TER    4355      LEU B 432                                                      
ATOM   4356  N   LYS C  25      11.791 -19.633  36.044  1.00 51.16           N  
ANISOU 4356  N   LYS C  25     6356   6349   6733   -590    912   -854       N  
ATOM   4357  CA  LYS C  25      11.489 -18.861  34.840  1.00 51.46           C  
ANISOU 4357  CA  LYS C  25     6384   6318   6848   -637    732   -870       C  
ATOM   4358  C   LYS C  25      12.395 -17.641  34.621  1.00 41.93           C  
ANISOU 4358  C   LYS C  25     5046   5199   5685   -734    927  -1029       C  
ATOM   4359  O   LYS C  25      12.883 -17.442  33.508  1.00 41.82           O  
ANISOU 4359  O   LYS C  25     5104   5166   5621   -545    611   -823       O  
ATOM   4360  CB  LYS C  25      10.012 -18.452  34.788  1.00 57.32           C  
ANISOU 4360  CB  LYS C  25     7096   7174   7510   -573    856   -917       C  
ATOM   4361  CG  LYS C  25       9.661 -17.619  33.562  1.00 61.05           C  
ANISOU 4361  CG  LYS C  25     7416   7738   8040   -597    835   -860       C  
ATOM   4362  CD  LYS C  25       8.336 -16.888  33.728  1.00 67.14           C  
ANISOU 4362  CD  LYS C  25     8284   8483   8742   -581    820   -971       C  
ATOM   4363  CE  LYS C  25       7.185 -17.646  33.081  1.00 70.07           C  
ANISOU 4363  CE  LYS C  25     8651   8754   9220   -724    767  -1041       C  
ATOM   4364  NZ  LYS C  25       6.928 -18.964  33.725  1.00 71.80           N  
ANISOU 4364  NZ  LYS C  25     8798   8977   9506   -824    874   -975       N  
ATOM   4365  N   PRO C  26      12.620 -16.813  35.664  1.00 37.70           N  
ANISOU 4365  N   PRO C  26     4566   4682   5077   -741    905   -979       N  
ATOM   4366  CA  PRO C  26      13.585 -15.736  35.418  1.00 32.97           C  
ANISOU 4366  CA  PRO C  26     4033   4155   4338   -464    648   -738       C  
ATOM   4367  C   PRO C  26      14.984 -16.303  35.246  1.00 31.03           C  
ANISOU 4367  C   PRO C  26     3701   3866   4222   -635    776   -883       C  
ATOM   4368  O   PRO C  26      15.264 -17.391  35.747  1.00 34.54           O  
ANISOU 4368  O   PRO C  26     4180   4262   4680   -656    830   -883       O  
ATOM   4369  CB  PRO C  26      13.503 -14.884  36.691  1.00 35.88           C  
ANISOU 4369  CB  PRO C  26     4453   4537   4643   -487    645   -703       C  
ATOM   4370  CG  PRO C  26      12.971 -15.797  37.731  1.00 37.75           C  
ANISOU 4370  CG  PRO C  26     4741   4739   4863   -533    717   -715       C  
ATOM   4371  CD  PRO C  26      12.032 -16.718  37.013  1.00 32.70           C  
ANISOU 4371  CD  PRO C  26     4016   4029   4380   -679    704   -711       C  
ATOM   4372  N   SER C  27      15.844 -15.575  34.542  1.00 29.94           N  
ANISOU 4372  N   SER C  27     3631   3722   4024   -459    486   -681       N  
ATOM   4373  CA  SER C  27      17.192 -16.049  34.253  1.00 35.36           C  
ANISOU 4373  CA  SER C  27     4199   4440   4796   -525    651   -817       C  
ATOM   4374  C   SER C  27      18.024 -16.262  35.515  1.00 31.13           C  
ANISOU 4374  C   SER C  27     3761   3942   4127   -385    555   -588       C  
ATOM   4375  O   SER C  27      18.946 -17.080  35.518  1.00 31.45           O  
ANISOU 4375  O   SER C  27     3793   3947   4209   -408    580   -622       O  
ATOM   4376  CB  SER C  27      17.905 -15.084  33.307  1.00 40.90           C  
ANISOU 4376  CB  SER C  27     4892   5225   5425   -338    468   -580       C  
ATOM   4377  OG  SER C  27      17.972 -13.786  33.863  1.00 50.14           O  
ANISOU 4377  OG  SER C  27     6166   6343   6544   -366    367   -601       O  
ATOM   4378  N   ALA C  28      17.695 -15.535  36.582  1.00 24.46           N  
ANISOU 4378  N   ALA C  28     2965   3106   3223   -424    568   -571       N  
ATOM   4379  CA  ALA C  28      18.442 -15.647  37.835  1.00 22.88           C  
ANISOU 4379  CA  ALA C  28     2837   2875   2982   -503    613   -582       C  
ATOM   4380  C   ALA C  28      18.136 -16.964  38.540  1.00 23.42           C  
ANISOU 4380  C   ALA C  28     2966   2872   3061   -585    721   -637       C  
ATOM   4381  O   ALA C  28      18.911 -17.433  39.371  1.00 22.36           O  
ANISOU 4381  O   ALA C  28     2916   2687   2893   -652    771   -643       O  
ATOM   4382  CB  ALA C  28      18.144 -14.459  38.760  1.00 24.09           C  
ANISOU 4382  CB  ALA C  28     3044   3051   3059   -521    590   -535       C  
ATOM   4383  N   CYS C  29      16.987 -17.551  38.218  1.00 22.30           N  
ANISOU 4383  N   CYS C  29     2800   2717   2955   -584    764   -671       N  
ATOM   4384  CA  CYS C  29      16.571 -18.798  38.836  1.00 23.31           C  
ANISOU 4384  CA  CYS C  29     2990   2765   3102   -663    883   -725       C  
ATOM   4385  C   CYS C  29      17.354 -19.958  38.235  1.00 29.76           C  
ANISOU 4385  C   CYS C  29     3775   3531   4001   -669    926   -764       C  
ATOM   4386  O   CYS C  29      17.013 -20.447  37.157  1.00 26.61           O  
ANISOU 4386  O   CYS C  29     3296   3140   3674   -628    915   -790       O  
ATOM   4387  CB  CYS C  29      15.066 -19.007  38.630  1.00 27.79           C  
ANISOU 4387  CB  CYS C  29     3539   3336   3684   -665    917   -757       C  
ATOM   4388  SG  CYS C  29      14.403 -20.524  39.330  1.00 34.22           S  
ANISOU 4388  SG  CYS C  29     4432   4042   4528   -768   1080   -829       S  
ATOM   4389  N   ARG C  30      18.407 -20.397  38.921  1.00 26.20           N  
ANISOU 4389  N   ARG C  30     3404   3004   3546   -703    887   -717       N  
ATOM   4390  CA  ARG C  30      19.222 -21.494  38.405  1.00 28.91           C  
ANISOU 4390  CA  ARG C  30     3729   3271   3983   -690    827   -695       C  
ATOM   4391  C   ARG C  30      20.060 -22.232  39.446  1.00 24.98           C  
ANISOU 4391  C   ARG C  30     3361   2644   3487   -731    741   -608       C  
ATOM   4392  O   ARG C  30      20.489 -21.661  40.448  1.00 26.12           O  
ANISOU 4392  O   ARG C  30     3598   2767   3558   -744    677   -553       O  
ATOM   4393  CB  ARG C  30      20.106 -21.029  37.236  1.00 35.46           C  
ANISOU 4393  CB  ARG C  30     4447   4173   4853   -609    752   -701       C  
ATOM   4394  CG  ARG C  30      20.913 -19.770  37.478  1.00 35.81           C  
ANISOU 4394  CG  ARG C  30     4503   4274   4828   -577    651   -652       C  
ATOM   4395  CD  ARG C  30      21.621 -19.351  36.186  1.00 37.44           C  
ANISOU 4395  CD  ARG C  30     4589   4553   5084   -489    605   -669       C  
ATOM   4396  NE  ARG C  30      22.307 -18.070  36.295  1.00 35.88           N  
ANISOU 4396  NE  ARG C  30     4395   4414   4824   -456    523   -627       N  
ATOM   4397  CZ  ARG C  30      23.619 -17.943  36.475  1.00 42.60           C  
ANISOU 4397  CZ  ARG C  30     5292   5228   5668   -439    383   -564       C  
ATOM   4398  NH1 ARG C  30      24.379 -19.027  36.561  1.00 45.96           N  
ANISOU 4398  NH1 ARG C  30     5759   5564   6142   -451    309   -537       N  
ATOM   4399  NH2 ARG C  30      24.173 -16.737  36.563  1.00 42.11           N  
ANISOU 4399  NH2 ARG C  30     5238   5215   5548   -412    318   -529       N  
ATOM   4400  N   ASN C  31      20.256 -23.522  39.197  1.00 20.01           N  
ANISOU 4400  N   ASN C  31     2740   1922   2941   -748    746   -599       N  
ATOM   4401  CA  ASN C  31      21.145 -24.355  39.993  1.00 19.91           C  
ANISOU 4401  CA  ASN C  31     2839   1777   2947   -771    665   -518       C  
ATOM   4402  C   ASN C  31      22.538 -24.277  39.386  1.00 24.56           C  
ANISOU 4402  C   ASN C  31     3392   2371   3568   -714    523   -488       C  
ATOM   4403  O   ASN C  31      22.689 -24.404  38.172  1.00 26.97           O  
ANISOU 4403  O   ASN C  31     3589   2731   3929   -673    523   -530       O  
ATOM   4404  CB  ASN C  31      20.650 -25.802  39.981  1.00 25.27           C  
ANISOU 4404  CB  ASN C  31     3552   2352   3699   -817    748   -519       C  
ATOM   4405  CG  ASN C  31      21.698 -26.783  40.461  1.00 29.82           C  
ANISOU 4405  CG  ASN C  31     4223   2792   4315   -819    664   -438       C  
ATOM   4406  OD1 ASN C  31      22.481 -27.310  39.667  1.00 27.80           O  
ANISOU 4406  OD1 ASN C  31     3927   2516   4121   -786    598   -435       O  
ATOM   4407  ND2 ASN C  31      21.717 -27.041  41.765  1.00 24.17           N  
ANISOU 4407  ND2 ASN C  31     3639   1981   3563   -851    673   -371       N  
ATOM   4408  N   LEU C  32      23.552 -24.080  40.222  1.00 15.32           N  
ANISOU 4408  N   LEU C  32     2311   1143   2365   -705    406   -420       N  
ATOM   4409  CA  LEU C  32      24.915 -23.878  39.724  1.00 14.73           C  
ANISOU 4409  CA  LEU C  32     2209   1077   2311   -649    258   -396       C  
ATOM   4410  C   LEU C  32      25.727 -25.161  39.584  1.00 22.07           C  
ANISOU 4410  C   LEU C  32     3180   1890   3316   -644    200   -360       C  
ATOM   4411  O   LEU C  32      26.382 -25.378  38.558  1.00 21.01           O  
ANISOU 4411  O   LEU C  32     2984   1782   3215   -607    144   -373       O  
ATOM   4412  CB  LEU C  32      25.680 -22.899  40.619  1.00 17.51           C  
ANISOU 4412  CB  LEU C  32     2618   1438   2597   -629    156   -356       C  
ATOM   4413  CG  LEU C  32      25.088 -21.497  40.707  1.00 16.97           C  
ANISOU 4413  CG  LEU C  32     2520   1489   2438   -627    192   -383       C  
ATOM   4414  CD1 LEU C  32      25.957 -20.612  41.599  1.00 16.29           C  
ANISOU 4414  CD1 LEU C  32     2496   1409   2283   -608     99   -346       C  
ATOM   4415  CD2 LEU C  32      24.920 -20.909  39.318  1.00 14.69           C  
ANISOU 4415  CD2 LEU C  32     2098   1320   2164   -584    208   -432       C  
ATOM   4416  N   PHE C  33      25.700 -26.002  40.614  1.00 20.87           N  
ANISOU 4416  N   PHE C  33     3139   1610   3182   -675    225   -309       N  
ATOM   4417  CA  PHE C  33      26.590 -27.161  40.659  1.00 22.29           C  
ANISOU 4417  CA  PHE C  33     3376   1664   3431   -656    164   -261       C  
ATOM   4418  C   PHE C  33      25.911 -28.502  40.957  1.00 21.98           C  
ANISOU 4418  C   PHE C  33     3409   1509   3435   -702    277   -239       C  
ATOM   4419  O   PHE C  33      26.475 -29.361  41.640  1.00 22.87           O  
ANISOU 4419  O   PHE C  33     3618   1492   3579   -690    257   -171       O  
ATOM   4420  CB  PHE C  33      27.762 -26.889  41.609  1.00 22.61           C  
ANISOU 4420  CB  PHE C  33     3469   1647   3473   -612     66   -203       C  
ATOM   4421  CG  PHE C  33      28.598 -25.706  41.197  1.00 21.59           C  
ANISOU 4421  CG  PHE C  33     3247   1624   3334   -562    -40   -236       C  
ATOM   4422  CD1 PHE C  33      29.396 -25.776  40.067  1.00 22.64           C  
ANISOU 4422  CD1 PHE C  33     3298   1817   3487   -509   -138   -253       C  
ATOM   4423  CD2 PHE C  33      28.571 -24.520  41.925  1.00 18.42           C  
ANISOU 4423  CD2 PHE C  33     2859   1296   2843   -564    -25   -242       C  
ATOM   4424  CE1 PHE C  33      30.160 -24.694  39.667  1.00 17.49           C  
ANISOU 4424  CE1 PHE C  33     2517   1296   2832   -446   -175   -294       C  
ATOM   4425  CE2 PHE C  33      29.332 -23.429  41.531  1.00 20.60           C  
ANISOU 4425  CE2 PHE C  33     3054   1682   3092   -525    -84   -283       C  
ATOM   4426  CZ  PHE C  33      30.126 -23.516  40.393  1.00 21.04           C  
ANISOU 4426  CZ  PHE C  33     2984   1804   3207   -471   -115   -324       C  
ATOM   4427  N   GLY C  34      24.707 -28.678  40.419  1.00 24.68           N  
ANISOU 4427  N   GLY C  34     3696   1899   3784   -746    403   -297       N  
ATOM   4428  CA  GLY C  34      24.047 -29.973  40.415  1.00 24.31           C  
ANISOU 4428  CA  GLY C  34     3695   1754   3790   -791    510   -293       C  
ATOM   4429  C   GLY C  34      23.164 -30.240  41.620  1.00 25.46           C  
ANISOU 4429  C   GLY C  34     3942   1832   3898   -848    619   -256       C  
ATOM   4430  O   GLY C  34      23.097 -29.429  42.541  1.00 23.18           O  
ANISOU 4430  O   GLY C  34     3700   1569   3540   -849    611   -229       O  
ATOM   4431  N   PRO C  35      22.478 -31.391  41.620  1.00 27.11           N  
ANISOU 4431  N   PRO C  35     4195   1956   4151   -896    724   -254       N  
ATOM   4432  CA  PRO C  35      21.589 -31.769  42.727  1.00 30.77           C  
ANISOU 4432  CA  PRO C  35     4761   2351   4580   -955    837   -217       C  
ATOM   4433  C   PRO C  35      22.387 -32.133  43.974  1.00 31.30           C  
ANISOU 4433  C   PRO C  35     4974   2300   4620   -930    792   -106       C  
ATOM   4434  O   PRO C  35      23.551 -32.514  43.857  1.00 28.71           O  
ANISOU 4434  O   PRO C  35     4673   1911   4325   -873    692    -62       O  
ATOM   4435  CB  PRO C  35      20.882 -33.015  42.190  1.00 32.01           C  
ANISOU 4435  CB  PRO C  35     4919   2439   4804  -1007    940   -243       C  
ATOM   4436  CG  PRO C  35      21.862 -33.607  41.226  1.00 33.95           C  
ANISOU 4436  CG  PRO C  35     5130   2652   5118   -959    852   -246       C  
ATOM   4437  CD  PRO C  35      22.549 -32.436  40.582  1.00 29.40           C  
ANISOU 4437  CD  PRO C  35     4446   2203   4523   -898    740   -283       C  
ATOM   4438  N   VAL C  36      21.777 -32.024  45.150  1.00 30.53           N  
ANISOU 4438  N   VAL C  36     4970   2172   4460   -965    869    -61       N  
ATOM   4439  CA  VAL C  36      22.460 -32.426  46.374  1.00 30.81           C  
ANISOU 4439  CA  VAL C  36     5148   2098   4460   -934    846     51       C  
ATOM   4440  C   VAL C  36      21.723 -33.535  47.120  1.00 37.16           C  
ANISOU 4440  C   VAL C  36     6069   2788   5264   -987    971    104       C  
ATOM   4441  O   VAL C  36      20.513 -33.715  46.967  1.00 37.88           O  
ANISOU 4441  O   VAL C  36     6134   2899   5360  -1060   1084     54       O  
ATOM   4442  CB  VAL C  36      22.703 -31.237  47.331  1.00 37.72           C  
ANISOU 4442  CB  VAL C  36     6059   3033   5239   -907    805     85       C  
ATOM   4443  CG1 VAL C  36      23.530 -30.153  46.640  1.00 32.59           C  
ANISOU 4443  CG1 VAL C  36     5306   2490   4588   -855    677     38       C  
ATOM   4444  CG2 VAL C  36      21.389 -30.680  47.836  1.00 35.66           C  
ANISOU 4444  CG2 VAL C  36     5803   2831   4914   -970    915     53       C  
ATOM   4445  N   ASP C  37      22.479 -34.281  47.918  1.00 38.43           N  
ANISOU 4445  N   ASP C  37     6356   2831   5416   -945    950    206       N  
ATOM   4446  CA  ASP C  37      21.924 -35.303  48.791  1.00 44.47           C  
ANISOU 4446  CA  ASP C  37     7252   3480   6165   -985   1061    274       C  
ATOM   4447  C   ASP C  37      21.399 -34.621  50.052  1.00 42.88           C  
ANISOU 4447  C   ASP C  37     7121   3309   5864  -1001   1112    320       C  
ATOM   4448  O   ASP C  37      22.168 -34.294  50.958  1.00 41.91           O  
ANISOU 4448  O   ASP C  37     7103   3158   5661   -943   1080    394       O  
ATOM   4449  CB  ASP C  37      23.004 -36.329  49.132  1.00 49.69           C  
ANISOU 4449  CB  ASP C  37     8024   4010   6846   -917   1015    368       C  
ATOM   4450  CG  ASP C  37      22.500 -37.441  50.032  1.00 58.30           C  
ANISOU 4450  CG  ASP C  37     9264   4973   7914   -951   1130    444       C  
ATOM   4451  OD1 ASP C  37      21.271 -37.553  50.229  1.00 60.54           O  
ANISOU 4451  OD1 ASP C  37     9549   5265   8187  -1039   1244    415       O  
ATOM   4452  OD2 ASP C  37      23.343 -38.213  50.535  1.00 62.26           O  
ANISOU 4452  OD2 ASP C  37     9897   5361   8399   -888   1121    528       O  
ATOM   4453  N   HIS C  38      20.088 -34.403  50.095  1.00 38.62           N  
ANISOU 4453  N   HIS C  38     6550   2817   5308  -1082   1220    267       N  
ATOM   4454  CA  HIS C  38      19.468 -33.645  51.178  1.00 42.52           C  
ANISOU 4454  CA  HIS C  38     7100   3351   5703  -1103   1278    293       C  
ATOM   4455  C   HIS C  38      19.675 -34.262  52.558  1.00 43.68           C  
ANISOU 4455  C   HIS C  38     7442   3380   5775  -1089   1345    406       C  
ATOM   4456  O   HIS C  38      19.916 -33.544  53.528  1.00 42.43           O  
ANISOU 4456  O   HIS C  38     7369   3241   5513  -1055   1339    453       O  
ATOM   4457  CB  HIS C  38      17.978 -33.424  50.904  1.00 47.66           C  
ANISOU 4457  CB  HIS C  38     7677   4071   6361  -1191   1386    213       C  
ATOM   4458  CG  HIS C  38      17.704 -32.303  49.949  1.00 51.36           C  
ANISOU 4458  CG  HIS C  38     7996   4681   6835  -1190   1347    101       C  
ATOM   4459  ND1 HIS C  38      16.474 -32.106  49.361  1.00 56.68           N  
ANISOU 4459  ND1 HIS C  38     8580   5429   7528  -1255   1435      6       N  
ATOM   4460  CD2 HIS C  38      18.507 -31.318  49.482  1.00 49.45           C  
ANISOU 4460  CD2 HIS C  38     7685   4525   6581  -1129   1231     71       C  
ATOM   4461  CE1 HIS C  38      16.531 -31.049  48.569  1.00 55.05           C  
ANISOU 4461  CE1 HIS C  38     8256   5346   7316  -1226   1377    -77       C  
ATOM   4462  NE2 HIS C  38      17.752 -30.551  48.627  1.00 49.31           N  
ANISOU 4462  NE2 HIS C  38     7538   4626   6569  -1154   1253    -39       N  
ATOM   4463  N   GLU C  39      19.583 -35.586  52.643  1.00 46.29           N  
ANISOU 4463  N   GLU C  39     7848   3590   6151  -1111   1404    451       N  
ATOM   4464  CA  GLU C  39      19.779 -36.279  53.913  1.00 51.39           C  
ANISOU 4464  CA  GLU C  39     8680   4118   6726  -1091   1468    562       C  
ATOM   4465  C   GLU C  39      21.181 -36.011  54.442  1.00 46.13           C  
ANISOU 4465  C   GLU C  39     8102   3428   5997   -979   1368    638       C  
ATOM   4466  O   GLU C  39      21.363 -35.708  55.619  1.00 45.05           O  
ANISOU 4466  O   GLU C  39     8086   3278   5752   -943   1385    712       O  
ATOM   4467  CB  GLU C  39      19.574 -37.788  53.751  1.00 62.79           C  
ANISOU 4467  CB  GLU C  39    10188   5432   8236  -1126   1535    592       C  
ATOM   4468  CG  GLU C  39      18.425 -38.176  52.838  1.00 72.12           C  
ANISOU 4468  CG  GLU C  39    11256   6642   9504  -1228   1600    504       C  
ATOM   4469  CD  GLU C  39      17.117 -37.505  53.212  1.00 78.14           C  
ANISOU 4469  CD  GLU C  39    11977   7489  10224  -1307   1693    462       C  
ATOM   4470  OE1 GLU C  39      16.761 -37.511  54.409  1.00 82.28           O  
ANISOU 4470  OE1 GLU C  39    12623   7975  10666  -1321   1772    528       O  
ATOM   4471  OE2 GLU C  39      16.446 -36.967  52.306  1.00 78.74           O  
ANISOU 4471  OE2 GLU C  39    11901   7672  10344  -1351   1687    362       O  
ATOM   4472  N   GLU C  40      22.168 -36.113  53.557  1.00 43.81           N  
ANISOU 4472  N   GLU C  40     7743   3137   5768   -923   1259    618       N  
ATOM   4473  CA  GLU C  40      23.557 -35.910  53.945  1.00 50.21           C  
ANISOU 4473  CA  GLU C  40     8626   3929   6524   -814   1158    687       C  
ATOM   4474  C   GLU C  40      23.815 -34.446  54.281  1.00 45.12           C  
ANISOU 4474  C   GLU C  40     7951   3403   5791   -787   1091    671       C  
ATOM   4475  O   GLU C  40      24.510 -34.139  55.248  1.00 42.84           O  
ANISOU 4475  O   GLU C  40     7776   3106   5396   -717   1056    749       O  
ATOM   4476  CB  GLU C  40      24.505 -36.364  52.835  1.00 61.69           C  
ANISOU 4476  CB  GLU C  40    10005   5361   8073   -763   1060    663       C  
ATOM   4477  CG  GLU C  40      25.875 -36.787  53.342  1.00 75.70           C  
ANISOU 4477  CG  GLU C  40    11900   7063   9799   -647    991    760       C  
ATOM   4478  CD  GLU C  40      26.978 -36.565  52.325  1.00 84.93           C  
ANISOU 4478  CD  GLU C  40    12970   8270  11031   -580    861    726       C  
ATOM   4479  OE1 GLU C  40      26.669 -36.447  51.120  1.00 87.76           O  
ANISOU 4479  OE1 GLU C  40    13172   8678  11495   -627    832    631       O  
ATOM   4480  OE2 GLU C  40      28.156 -36.498  52.736  1.00 88.46           O  
ANISOU 4480  OE2 GLU C  40    13492   8704  11416   -477    785    796       O  
ATOM   4481  N   LEU C  41      23.252 -33.550  53.474  1.00 40.74           N  
ANISOU 4481  N   LEU C  41     7244   2961   5274   -838   1072    569       N  
ATOM   4482  CA  LEU C  41      23.402 -32.116  53.699  1.00 36.23           C  
ANISOU 4482  CA  LEU C  41     6643   2505   4619   -821   1014    540       C  
ATOM   4483  C   LEU C  41      22.775 -31.700  55.031  1.00 39.96           C  
ANISOU 4483  C   LEU C  41     7236   2980   4966   -837   1093    589       C  
ATOM   4484  O   LEU C  41      23.388 -30.971  55.814  1.00 40.43           O  
ANISOU 4484  O   LEU C  41     7376   3071   4913   -782   1038    636       O  
ATOM   4485  CB  LEU C  41      22.791 -31.321  52.539  1.00 35.92           C  
ANISOU 4485  CB  LEU C  41     6418   2585   4647   -872    990    417       C  
ATOM   4486  CG  LEU C  41      22.813 -29.794  52.676  1.00 35.96           C  
ANISOU 4486  CG  LEU C  41     6387   2711   4563   -864    938    374       C  
ATOM   4487  CD1 LEU C  41      24.199 -29.304  53.071  1.00 39.64           C  
ANISOU 4487  CD1 LEU C  41     6926   3181   4953   -781    822    429       C  
ATOM   4488  CD2 LEU C  41      22.364 -29.126  51.379  1.00 33.87           C  
ANISOU 4488  CD2 LEU C  41     5930   2562   4376   -895    900    255       C  
ATOM   4489  N   THR C  42      21.556 -32.166  55.283  1.00 40.26           N  
ANISOU 4489  N   THR C  42     7286   2989   5020   -912   1219    578       N  
ATOM   4490  CA  THR C  42      20.879 -31.886  56.543  1.00 46.01           C  
ANISOU 4490  CA  THR C  42     8127   3715   5641   -930   1305    627       C  
ATOM   4491  C   THR C  42      21.691 -32.433  57.714  1.00 50.53           C  
ANISOU 4491  C   THR C  42     8871   4197   6130   -855   1293    751       C  
ATOM   4492  O   THR C  42      21.836 -31.769  58.740  1.00 50.33           O  
ANISOU 4492  O   THR C  42     8935   4203   5985   -817   1280    799       O  
ATOM   4493  CB  THR C  42      19.453 -32.468  56.557  1.00 52.21           C  
ANISOU 4493  CB  THR C  42     8894   4475   6469  -1027   1446    598       C  
ATOM   4494  OG1 THR C  42      18.628 -31.715  55.657  1.00 50.76           O  
ANISOU 4494  OG1 THR C  42     8556   4401   6329  -1085   1456    484       O  
ATOM   4495  CG2 THR C  42      18.850 -32.417  57.961  1.00 52.35           C  
ANISOU 4495  CG2 THR C  42     9045   4466   6379  -1037   1537    668       C  
ATOM   4496  N   ARG C  43      22.235 -33.635  57.541  1.00 55.47           N  
ANISOU 4496  N   ARG C  43     9543   4717   6815   -827   1291    800       N  
ATOM   4497  CA  ARG C  43      23.104 -34.246  58.543  1.00 60.99           C  
ANISOU 4497  CA  ARG C  43    10401   5332   7442   -742   1272    917       C  
ATOM   4498  C   ARG C  43      24.308 -33.366  58.870  1.00 58.49           C  
ANISOU 4498  C   ARG C  43    10109   5081   7035   -644   1141    950       C  
ATOM   4499  O   ARG C  43      24.599 -33.110  60.037  1.00 57.06           O  
ANISOU 4499  O   ARG C  43    10041   4903   6736   -591   1131   1025       O  
ATOM   4500  CB  ARG C  43      23.591 -35.621  58.072  1.00 66.71           C  
ANISOU 4500  CB  ARG C  43    11155   5938   8253   -719   1278    950       C  
ATOM   4501  CG  ARG C  43      22.828 -36.798  58.661  1.00 72.16           C  
ANISOU 4501  CG  ARG C  43    11951   6514   8952   -766   1408   1000       C  
ATOM   4502  CD  ARG C  43      23.526 -38.126  58.371  1.00 77.85           C  
ANISOU 4502  CD  ARG C  43    12739   7110   9731   -719   1400   1049       C  
ATOM   4503  NE  ARG C  43      22.881 -38.881  57.297  1.00 82.06           N  
ANISOU 4503  NE  ARG C  43    13188   7601  10390   -802   1452    978       N  
ATOM   4504  CZ  ARG C  43      23.433 -39.132  56.112  1.00 83.50           C  
ANISOU 4504  CZ  ARG C  43    13275   7783  10670   -784   1378    927       C  
ATOM   4505  NH1 ARG C  43      24.654 -38.695  55.835  1.00 81.92           N  
ANISOU 4505  NH1 ARG C  43    13050   7619  10458   -687   1254    940       N  
ATOM   4506  NH2 ARG C  43      22.763 -39.829  55.203  1.00 84.91           N  
ANISOU 4506  NH2 ARG C  43    13382   7927  10954   -863   1427    864       N  
ATOM   4507  N   ASP C  44      25.004 -32.911  57.833  1.00 60.25           N  
ANISOU 4507  N   ASP C  44    10221   5359   7311   -623   1036    892       N  
ATOM   4508  CA  ASP C  44      26.209 -32.105  58.007  1.00 64.73           C  
ANISOU 4508  CA  ASP C  44    10803   5994   7797   -536    902    918       C  
ATOM   4509  C   ASP C  44      25.920 -30.761  58.671  1.00 63.07           C  
ANISOU 4509  C   ASP C  44    10606   5888   7470   -546    881    899       C  
ATOM   4510  O   ASP C  44      26.759 -30.229  59.397  1.00 68.07           O  
ANISOU 4510  O   ASP C  44    11310   6562   7991   -472    796    952       O  
ATOM   4511  CB  ASP C  44      26.911 -31.887  56.663  1.00 71.82           C  
ANISOU 4511  CB  ASP C  44    11569   6932   8786   -523    802    850       C  
ATOM   4512  CG  ASP C  44      27.474 -33.173  56.083  1.00 81.96           C  
ANISOU 4512  CG  ASP C  44    12856   8115  10169   -485    797    880       C  
ATOM   4513  OD1 ASP C  44      27.761 -34.106  56.865  1.00 85.85           O  
ANISOU 4513  OD1 ASP C  44    13480   8513  10625   -434    834    973       O  
ATOM   4514  OD2 ASP C  44      27.633 -33.250  54.844  1.00 83.55           O  
ANISOU 4514  OD2 ASP C  44    12930   8332  10484   -503    755    808       O  
ATOM   4515  N   LEU C  45      24.732 -30.219  58.420  1.00 56.13           N  
ANISOU 4515  N   LEU C  45     9657   5057   6611   -633    955    821       N  
ATOM   4516  CA  LEU C  45      24.336 -28.935  58.993  1.00 51.11           C  
ANISOU 4516  CA  LEU C  45     9035   4518   5867   -646    945    793       C  
ATOM   4517  C   LEU C  45      23.804 -29.087  60.416  1.00 55.52           C  
ANISOU 4517  C   LEU C  45     9725   5043   6327   -638   1025    869       C  
ATOM   4518  O   LEU C  45      23.998 -28.205  61.256  1.00 51.14           O  
ANISOU 4518  O   LEU C  45     9229   4549   5652   -601    980    891       O  
ATOM   4519  CB  LEU C  45      23.285 -28.257  58.111  1.00 43.00           C  
ANISOU 4519  CB  LEU C  45     7876   3564   4897   -733    990    676       C  
ATOM   4520  CG  LEU C  45      23.743 -27.788  56.730  1.00 39.32           C  
ANISOU 4520  CG  LEU C  45     7265   3163   4513   -740    900    586       C  
ATOM   4521  CD1 LEU C  45      22.539 -27.502  55.848  1.00 40.78           C  
ANISOU 4521  CD1 LEU C  45     7314   3404   4777   -825    972    479       C  
ATOM   4522  CD2 LEU C  45      24.634 -26.555  56.850  1.00 35.99           C  
ANISOU 4522  CD2 LEU C  45     6858   2831   3987   -691    770    574       C  
ATOM   4523  N   GLU C  46      23.133 -30.205  60.682  1.00 62.15           N  
ANISOU 4523  N   GLU C  46    10608   5787   7217   -673   1141    908       N  
ATOM   4524  CA  GLU C  46      22.580 -30.467  62.010  1.00 69.95           C  
ANISOU 4524  CA  GLU C  46    11720   6736   8122   -670   1227    983       C  
ATOM   4525  C   GLU C  46      23.678 -30.625  63.054  1.00 72.60           C  
ANISOU 4525  C   GLU C  46    12179   7047   8357   -565   1154   1088       C  
ATOM   4526  O   GLU C  46      23.453 -30.381  64.241  1.00 74.26           O  
ANISOU 4526  O   GLU C  46    12482   7267   8466   -541   1181   1143       O  
ATOM   4527  CB  GLU C  46      21.672 -31.700  61.998  1.00 74.45           C  
ANISOU 4527  CB  GLU C  46    12312   7205   8771   -736   1364   1000       C  
ATOM   4528  CG  GLU C  46      20.251 -31.414  61.537  1.00 79.85           C  
ANISOU 4528  CG  GLU C  46    12904   7930   9504   -843   1466    914       C  
ATOM   4529  CD  GLU C  46      19.374 -32.651  61.541  1.00 87.76           C  
ANISOU 4529  CD  GLU C  46    13929   8837  10580   -915   1596    931       C  
ATOM   4530  OE1 GLU C  46      19.873 -33.734  61.916  1.00 90.96           O  
ANISOU 4530  OE1 GLU C  46    14431   9135  10995   -881   1610   1010       O  
ATOM   4531  OE2 GLU C  46      18.186 -32.541  61.169  1.00 89.47           O  
ANISOU 4531  OE2 GLU C  46    14068   9086  10839  -1005   1685    865       O  
ATOM   4532  N   LYS C  47      24.859 -31.039  62.603  1.00 73.52           N  
ANISOU 4532  N   LYS C  47    12292   7140   8503   -499   1060   1115       N  
ATOM   4533  CA  LYS C  47      26.039 -31.103  63.456  1.00 77.41           C  
ANISOU 4533  CA  LYS C  47    12881   7633   8900   -391    970   1206       C  
ATOM   4534  C   LYS C  47      26.281 -29.762  64.137  1.00 75.23           C  
ANISOU 4534  C   LYS C  47    12613   7472   8500   -360    890   1198       C  
ATOM   4535  O   LYS C  47      26.402 -29.682  65.359  1.00 74.43           O  
ANISOU 4535  O   LYS C  47    12608   7376   8297   -313    891   1268       O  
ATOM   4536  CB  LYS C  47      27.269 -31.466  62.626  1.00 81.09           C  
ANISOU 4536  CB  LYS C  47    13305   8087   9417   -328    864   1212       C  
ATOM   4537  CG  LYS C  47      27.426 -32.943  62.313  1.00 87.26           C  
ANISOU 4537  CG  LYS C  47    14126   8742  10288   -313    918   1256       C  
ATOM   4538  CD  LYS C  47      28.548 -33.171  61.301  1.00 90.42           C  
ANISOU 4538  CD  LYS C  47    14461   9144  10749   -257    812   1243       C  
ATOM   4539  CE  LYS C  47      29.635 -32.101  61.403  1.00 90.38           C  
ANISOU 4539  CE  LYS C  47    14430   9257  10654   -186    663   1245       C  
ATOM   4540  NZ  LYS C  47      30.870 -32.478  60.658  1.00 89.87           N  
ANISOU 4540  NZ  LYS C  47    14329   9190  10629   -108    558   1260       N  
ATOM   4541  N   HIS C  48      26.348 -28.710  63.328  1.00 73.88           N  
ANISOU 4541  N   HIS C  48    12338   7393   8338   -389    820   1108       N  
ATOM   4542  CA  HIS C  48      26.610 -27.368  63.828  1.00 72.32           C  
ANISOU 4542  CA  HIS C  48    12141   7309   8029   -367    733   1084       C  
ATOM   4543  C   HIS C  48      25.368 -26.755  64.472  1.00 70.60           C  
ANISOU 4543  C   HIS C  48    11945   7118   7762   -420    825   1057       C  
ATOM   4544  O   HIS C  48      25.346 -26.488  65.676  1.00 68.59           O  
ANISOU 4544  O   HIS C  48    11773   6880   7407   -383    826   1112       O  
ATOM   4545  CB  HIS C  48      27.114 -26.476  62.691  1.00 71.89           C  
ANISOU 4545  CB  HIS C  48    11976   7338   8001   -382    626    994       C  
ATOM   4546  CG  HIS C  48      28.312 -27.024  61.979  1.00 71.07           C  
ANISOU 4546  CG  HIS C  48    11840   7216   7949   -329    533   1016       C  
ATOM   4547  ND1 HIS C  48      28.220 -27.727  60.797  1.00 70.20           N  
ANISOU 4547  ND1 HIS C  48    11652   7049   7970   -362    562    978       N  
ATOM   4548  CD2 HIS C  48      29.630 -26.976  62.287  1.00 71.55           C  
ANISOU 4548  CD2 HIS C  48    11926   7313   7947   -241    411   1071       C  
ATOM   4549  CE1 HIS C  48      29.430 -28.085  60.404  1.00 69.60           C  
ANISOU 4549  CE1 HIS C  48    11566   6971   7910   -293    462   1011       C  
ATOM   4550  NE2 HIS C  48      30.303 -27.641  61.290  1.00 71.24           N  
ANISOU 4550  NE2 HIS C  48    11834   7237   7997   -219    369   1069       N  
ATOM   4551  N   GLU C  54      29.468 -25.605  74.911  1.00 81.97           N  
ANISOU 4551  N   GLU C  54    14008   8784   8355    123    494   1659       N  
ATOM   4552  CA  GLU C  54      29.857 -25.970  76.267  1.00 84.50           C  
ANISOU 4552  CA  GLU C  54    14422   9097   8588    190    491   1755       C  
ATOM   4553  C   GLU C  54      30.853 -24.968  76.843  1.00 83.93           C  
ANISOU 4553  C   GLU C  54    14307   9152   8429    232    355   1754       C  
ATOM   4554  O   GLU C  54      30.901 -24.754  78.054  1.00 84.93           O  
ANISOU 4554  O   GLU C  54    14518   9290   8460    269    355   1799       O  
ATOM   4555  CB  GLU C  54      30.456 -27.378  76.293  1.00 86.66           C  
ANISOU 4555  CB  GLU C  54    14762   9279   8886    247    513   1844       C  
ATOM   4556  N   ALA C  55      31.644 -24.356  75.967  1.00 81.27           N  
ANISOU 4556  N   ALA C  55    13864   8896   8117    226    245   1696       N  
ATOM   4557  CA  ALA C  55      32.664 -23.399  76.388  1.00 80.38           C  
ANISOU 4557  CA  ALA C  55    13738   8888   7914    260    117   1680       C  
ATOM   4558  C   ALA C  55      32.046 -22.140  76.992  1.00 80.36           C  
ANISOU 4558  C   ALA C  55    13766   8926   7841    227    118   1616       C  
ATOM   4559  O   ALA C  55      32.597 -21.559  77.927  1.00 81.15           O  
ANISOU 4559  O   ALA C  55    13916   9077   7842    262     55   1635       O  
ATOM   4560  CB  ALA C  55      33.575 -23.043  75.223  1.00 79.15           C  
ANISOU 4560  CB  ALA C  55    13461   8805   7807    252      8   1625       C  
ATOM   4561  N   SER C  56      30.906 -21.721  76.451  1.00 79.17           N  
ANISOU 4561  N   SER C  56    13587   8753   7743    160    190   1542       N  
ATOM   4562  CA  SER C  56      30.178 -20.580  76.999  1.00 78.64           C  
ANISOU 4562  CA  SER C  56    13555   8712   7614    131    206   1482       C  
ATOM   4563  C   SER C  56      29.456 -20.970  78.283  1.00 79.80           C  
ANISOU 4563  C   SER C  56    13821   8802   7696    156    302   1553       C  
ATOM   4564  O   SER C  56      29.324 -20.162  79.202  1.00 80.63           O  
ANISOU 4564  O   SER C  56    13988   8935   7712    170    286   1543       O  
ATOM   4565  CB  SER C  56      29.180 -20.023  75.980  1.00 75.79           C  
ANISOU 4565  CB  SER C  56    13121   8349   7327     57    253   1382       C  
ATOM   4566  OG  SER C  56      29.790 -19.065  75.131  1.00 71.85           O  
ANISOU 4566  OG  SER C  56    12535   7921   6846     33    145   1292       O  
ATOM   4567  N   GLN C  57      28.990 -22.214  78.336  1.00 79.73           N  
ANISOU 4567  N   GLN C  57    13847   8712   7736    161    403   1623       N  
ATOM   4568  CA  GLN C  57      28.318 -22.736  79.519  1.00 81.05           C  
ANISOU 4568  CA  GLN C  57    14128   8818   7849    183    502   1697       C  
ATOM   4569  C   GLN C  57      29.263 -22.737  80.715  1.00 78.60           C  
ANISOU 4569  C   GLN C  57    13903   8531   7431    260    434   1769       C  
ATOM   4570  O   GLN C  57      28.841 -22.535  81.852  1.00 77.88           O  
ANISOU 4570  O   GLN C  57    13905   8427   7259    281    476   1802       O  
ATOM   4571  CB  GLN C  57      27.789 -24.147  79.253  1.00 84.70           C  
ANISOU 4571  CB  GLN C  57    14609   9180   8393    169    615   1759       C  
ATOM   4572  CG  GLN C  57      27.063 -24.785  80.426  1.00 88.85           C  
ANISOU 4572  CG  GLN C  57    15253   9635   8870    186    726   1838       C  
ATOM   4573  CD  GLN C  57      26.417 -26.107  80.058  1.00 92.84           C  
ANISOU 4573  CD  GLN C  57    15780  10033   9463    155    847   1882       C  
ATOM   4574  OE1 GLN C  57      26.569 -26.593  78.937  1.00 95.03           O  
ANISOU 4574  OE1 GLN C  57    16009  10271   9826    129    850   1853       O  
ATOM   4575  NE2 GLN C  57      25.689 -26.694  80.999  1.00 94.65           N  
ANISOU 4575  NE2 GLN C  57    16110  10196   9658    159    955   1947       N  
ATOM   4576  N   ARG C  58      30.547 -22.956  80.450  1.00 78.95           N  
ANISOU 4576  N   ARG C  58    13910   8613   7473    302    329   1794       N  
ATOM   4577  CA  ARG C  58      31.558 -22.920  81.498  1.00 82.22           C  
ANISOU 4577  CA  ARG C  58    14389   9066   7784    374    251   1860       C  
ATOM   4578  C   ARG C  58      31.817 -21.486  81.940  1.00 77.84           C  
ANISOU 4578  C   ARG C  58    13832   8597   7146    367    166   1797       C  
ATOM   4579  O   ARG C  58      32.033 -21.218  83.123  1.00 78.35           O  
ANISOU 4579  O   ARG C  58    13983   8677   7111    408    148   1838       O  
ATOM   4580  CB  ARG C  58      32.859 -23.563  81.014  1.00 87.47           C  
ANISOU 4580  CB  ARG C  58    15005   9759   8472    422    163   1904       C  
ATOM   4581  CG  ARG C  58      33.988 -23.515  82.031  1.00 93.20           C  
ANISOU 4581  CG  ARG C  58    15782  10539   9090    497     74   1972       C  
ATOM   4582  CD  ARG C  58      35.020 -24.591  81.750  1.00 96.92           C  
ANISOU 4582  CD  ARG C  58    16235  11005   9585    559     32   2048       C  
ATOM   4583  NE  ARG C  58      34.385 -25.874  81.468  1.00 99.27           N  
ANISOU 4583  NE  ARG C  58    16572  11183   9961    561    145   2097       N  
ATOM   4584  CZ  ARG C  58      33.854 -26.670  82.393  1.00101.77           C  
ANISOU 4584  CZ  ARG C  58    17008  11412  10249    592    242   2172       C  
ATOM   4585  NH1 ARG C  58      33.876 -26.318  83.672  1.00101.51           N  
ANISOU 4585  NH1 ARG C  58    17066  11398  10107    628    239   2209       N  
ATOM   4586  NH2 ARG C  58      33.297 -27.819  82.036  1.00103.07           N  
ANISOU 4586  NH2 ARG C  58    17203  11466  10494    584    344   2208       N  
ATOM   4587  N   LYS C  59      31.785 -20.569  80.980  1.00 73.23           N  
ANISOU 4587  N   LYS C  59    13154   8064   6605    312    114   1695       N  
ATOM   4588  CA  LYS C  59      32.044 -19.161  81.253  1.00 72.12           C  
ANISOU 4588  CA  LYS C  59    13007   7996   6399    296     30   1624       C  
ATOM   4589  C   LYS C  59      30.957 -18.531  82.125  1.00 68.20           C  
ANISOU 4589  C   LYS C  59    12597   7470   5845    284    104   1604       C  
ATOM   4590  O   LYS C  59      31.253 -17.729  83.011  1.00 67.60           O  
ANISOU 4590  O   LYS C  59    12579   7430   5676    303     52   1599       O  
ATOM   4591  CB  LYS C  59      32.188 -18.384  79.941  1.00 76.03           C  
ANISOU 4591  CB  LYS C  59    13385   8538   6965    237    -33   1517       C  
ATOM   4592  CG  LYS C  59      32.542 -16.914  80.117  1.00 78.35           C  
ANISOU 4592  CG  LYS C  59    13671   8898   7201    214   -127   1438       C  
ATOM   4593  CD  LYS C  59      32.792 -16.241  78.776  1.00 78.90           C  
ANISOU 4593  CD  LYS C  59    13625   9008   7346    158   -192   1338       C  
ATOM   4594  CE  LYS C  59      33.249 -14.801  78.958  1.00 81.60           C  
ANISOU 4594  CE  LYS C  59    13964   9405   7634    131   -289   1264       C  
ATOM   4595  NZ  LYS C  59      33.582 -14.153  77.657  1.00 80.83           N  
ANISOU 4595  NZ  LYS C  59    13755   9344   7613     75   -357   1169       N  
ATOM   4596  N   TRP C  60      29.704 -18.907  81.881  1.00 65.74           N  
ANISOU 4596  N   TRP C  60    12294   7096   5587    251    227   1594       N  
ATOM   4597  CA  TRP C  60      28.572 -18.260  82.543  1.00 64.38           C  
ANISOU 4597  CA  TRP C  60    12187   6904   5370    235    302   1566       C  
ATOM   4598  C   TRP C  60      27.834 -19.148  83.548  1.00 65.01           C  
ANISOU 4598  C   TRP C  60    12368   6916   5416    265    421   1657       C  
ATOM   4599  O   TRP C  60      26.845 -18.713  84.138  1.00 65.57           O  
ANISOU 4599  O   TRP C  60    12493   6970   5449    257    494   1643       O  
ATOM   4600  CB  TRP C  60      27.572 -17.741  81.502  1.00 58.21           C  
ANISOU 4600  CB  TRP C  60    11330   6121   4666    168    352   1471       C  
ATOM   4601  CG  TRP C  60      28.140 -16.735  80.541  1.00 53.99           C  
ANISOU 4601  CG  TRP C  60    10705   5646   4162    134    244   1372       C  
ATOM   4602  CD1 TRP C  60      28.394 -16.921  79.211  1.00 51.28           C  
ANISOU 4602  CD1 TRP C  60    10253   5317   3915     97    215   1325       C  
ATOM   4603  CD2 TRP C  60      28.521 -15.385  80.836  1.00 53.02           C  
ANISOU 4603  CD2 TRP C  60    10597   5572   3977    131    153   1307       C  
ATOM   4604  NE1 TRP C  60      28.908 -15.771  78.660  1.00 48.66           N  
ANISOU 4604  NE1 TRP C  60     9865   5040   3583     70    112   1236       N  
ATOM   4605  CE2 TRP C  60      28.998 -14.814  79.637  1.00 54.47           C  
ANISOU 4605  CE2 TRP C  60    10677   5795   4225     88     73   1223       C  
ATOM   4606  CE3 TRP C  60      28.507 -14.606  81.995  1.00 56.41           C  
ANISOU 4606  CE3 TRP C  60    11120   6009   4304    159    133   1312       C  
ATOM   4607  CZ2 TRP C  60      29.455 -13.498  79.568  1.00 54.93           C  
ANISOU 4607  CZ2 TRP C  60    10724   5894   4252     68    -25   1146       C  
ATOM   4608  CZ3 TRP C  60      28.962 -13.300  81.923  1.00 56.76           C  
ANISOU 4608  CZ3 TRP C  60    11156   6095   4317    139     35   1235       C  
ATOM   4609  CH2 TRP C  60      29.429 -12.760  80.719  1.00 56.71           C  
ANISOU 4609  CH2 TRP C  60    11046   6120   4379     92    -41   1153       C  
ATOM   4610  N   ASN C  61      28.327 -20.369  83.749  1.00 66.22           N  
ANISOU 4610  N   ASN C  61    12548   7029   5584    302    439   1749       N  
ATOM   4611  CA  ASN C  61      27.626 -21.402  84.527  1.00 68.31           C  
ANISOU 4611  CA  ASN C  61    12903   7214   5838    322    561   1837       C  
ATOM   4612  C   ASN C  61      26.103 -21.418  84.340  1.00 69.09           C  
ANISOU 4612  C   ASN C  61    13001   7271   5980    266    695   1808       C  
ATOM   4613  O   ASN C  61      25.339 -21.304  85.300  1.00 69.22           O  
ANISOU 4613  O   ASN C  61    13099   7266   5936    277    770   1836       O  
ATOM   4614  CB  ASN C  61      28.028 -21.392  86.015  1.00 70.10           C  
ANISOU 4614  CB  ASN C  61    13248   7440   5945    391    544   1910       C  
ATOM   4615  CG  ASN C  61      27.670 -20.097  86.724  1.00 67.55           C  
ANISOU 4615  CG  ASN C  61    12967   7162   5537    390    522   1858       C  
ATOM   4616  OD1 ASN C  61      28.498 -19.193  86.848  1.00 67.30           O  
ANISOU 4616  OD1 ASN C  61    12922   7196   5453    404    406   1820       O  
ATOM   4617  ND2 ASN C  61      26.437 -20.011  87.212  1.00 62.79           N  
ANISOU 4617  ND2 ASN C  61    12416   6523   4919    374    633   1859       N  
ATOM   4618  N   PHE C  62      25.683 -21.559  83.085  1.00 67.73           N  
ANISOU 4618  N   PHE C  62    12730   7092   5912    207    723   1752       N  
ATOM   4619  CA  PHE C  62      24.272 -21.542  82.716  1.00 67.10           C  
ANISOU 4619  CA  PHE C  62    12625   6987   5883    145    842   1717       C  
ATOM   4620  C   PHE C  62      24.046 -22.485  81.534  1.00 69.40           C  
ANISOU 4620  C   PHE C  62    12837   7233   6299     95    894   1713       C  
ATOM   4621  O   PHE C  62      24.829 -22.495  80.585  1.00 66.56           O  
ANISOU 4621  O   PHE C  62    12398   6896   5995     89    812   1679       O  
ATOM   4622  CB  PHE C  62      23.846 -20.117  82.343  1.00 60.99           C  
ANISOU 4622  CB  PHE C  62    11800   6281   5094    116    804   1610       C  
ATOM   4623  CG  PHE C  62      22.362 -19.947  82.150  1.00 57.02           C  
ANISOU 4623  CG  PHE C  62    11278   5768   4621     64    925   1576       C  
ATOM   4624  CD1 PHE C  62      21.754 -20.302  80.955  1.00 56.32           C  
ANISOU 4624  CD1 PHE C  62    11092   5667   4639      0    981   1534       C  
ATOM   4625  CD2 PHE C  62      21.578 -19.411  83.159  1.00 58.62           C  
ANISOU 4625  CD2 PHE C  62    11555   5977   4742     82    981   1586       C  
ATOM   4626  CE1 PHE C  62      20.393 -20.143  80.775  1.00 55.88           C  
ANISOU 4626  CE1 PHE C  62    11011   5613   4608    -49   1091   1505       C  
ATOM   4627  CE2 PHE C  62      20.215 -19.247  82.986  1.00 57.88           C  
ANISOU 4627  CE2 PHE C  62    11436   5884   4671     38   1092   1559       C  
ATOM   4628  CZ  PHE C  62      19.622 -19.613  81.793  1.00 56.99           C  
ANISOU 4628  CZ  PHE C  62    11223   5766   4664    -29   1147   1519       C  
ATOM   4629  N   ASP C  63      22.973 -23.269  81.590  1.00 73.65           N  
ANISOU 4629  N   ASP C  63    13394   7708   6880     55   1030   1748       N  
ATOM   4630  CA  ASP C  63      22.660 -24.217  80.521  1.00 75.42           C  
ANISOU 4630  CA  ASP C  63    13552   7880   7225      0   1091   1745       C  
ATOM   4631  C   ASP C  63      21.689 -23.602  79.518  1.00 66.12           C  
ANISOU 4631  C   ASP C  63    12276   6736   6111    -75   1135   1650       C  
ATOM   4632  O   ASP C  63      20.485 -23.531  79.770  1.00 62.01           O  
ANISOU 4632  O   ASP C  63    11769   6207   5586   -115   1243   1644       O  
ATOM   4633  CB  ASP C  63      22.065 -25.503  81.101  1.00 85.72           C  
ANISOU 4633  CB  ASP C  63    14947   9081   8542     -9   1222   1834       C  
ATOM   4634  CG  ASP C  63      22.082 -26.653  80.110  1.00 92.24           C  
ANISOU 4634  CG  ASP C  63    15762   9813   9471    -47   1278   1839       C  
ATOM   4635  OD1 ASP C  63      21.346 -26.586  79.101  1.00 93.01           O  
ANISOU 4635  OD1 ASP C  63    15788   9905   9647   -120   1333   1771       O  
ATOM   4636  OD2 ASP C  63      22.827 -27.629  80.345  1.00 94.52           O  
ANISOU 4636  OD2 ASP C  63    16115  10034   9763     -2   1267   1911       O  
ATOM   4637  N   PHE C  64      22.217 -23.177  78.374  1.00 61.66           N  
ANISOU 4637  N   PHE C  64    11619   6208   5602    -92   1053   1575       N  
ATOM   4638  CA  PHE C  64      21.443 -22.418  77.393  1.00 57.79           C  
ANISOU 4638  CA  PHE C  64    11036   5760   5160   -154   1073   1473       C  
ATOM   4639  C   PHE C  64      20.437 -23.255  76.599  1.00 62.74           C  
ANISOU 4639  C   PHE C  64    11644   6316   5879   -228   1206   1458       C  
ATOM   4640  O   PHE C  64      19.308 -22.818  76.365  1.00 58.18           O  
ANISOU 4640  O   PHE C  64    11029   5763   5314   -278   1283   1409       O  
ATOM   4641  CB  PHE C  64      22.385 -21.659  76.452  1.00 46.25           C  
ANISOU 4641  CB  PHE C  64     9485   4364   3725   -148    937   1396       C  
ATOM   4642  CG  PHE C  64      23.332 -20.740  77.170  1.00 47.16           C  
ANISOU 4642  CG  PHE C  64     9636   4540   3744    -87    814   1393       C  
ATOM   4643  CD1 PHE C  64      22.942 -19.456  77.519  1.00 48.53           C  
ANISOU 4643  CD1 PHE C  64     9822   4769   3851    -85    789   1330       C  
ATOM   4644  CD2 PHE C  64      24.604 -21.167  77.517  1.00 46.47           C  
ANISOU 4644  CD2 PHE C  64     9581   4447   3627    -31    727   1451       C  
ATOM   4645  CE1 PHE C  64      23.808 -18.612  78.193  1.00 50.42           C  
ANISOU 4645  CE1 PHE C  64    10107   5049   3999    -36    680   1322       C  
ATOM   4646  CE2 PHE C  64      25.474 -20.329  78.191  1.00 47.20           C  
ANISOU 4646  CE2 PHE C  64     9714   4593   3626     18    618   1446       C  
ATOM   4647  CZ  PHE C  64      25.076 -19.050  78.531  1.00 50.21           C  
ANISOU 4647  CZ  PHE C  64    10109   5023   3946     12    595   1379       C  
ATOM   4648  N   GLN C  65      20.849 -24.449  76.186  1.00 72.08           N  
ANISOU 4648  N   GLN C  65    12848   7414   7127   -235   1232   1501       N  
ATOM   4649  CA  GLN C  65      19.977 -25.344  75.428  1.00 83.55           C  
ANISOU 4649  CA  GLN C  65    14279   8790   8674   -311   1357   1488       C  
ATOM   4650  C   GLN C  65      18.689 -25.650  76.191  1.00 87.41           C  
ANISOU 4650  C   GLN C  65    14821   9252   9141   -350   1501   1527       C  
ATOM   4651  O   GLN C  65      17.608 -25.727  75.604  1.00 87.98           O  
ANISOU 4651  O   GLN C  65    14840   9318   9270   -427   1600   1482       O  
ATOM   4652  CB  GLN C  65      20.714 -26.646  75.096  1.00 90.79           C  
ANISOU 4652  CB  GLN C  65    15232   9611   9654   -299   1359   1543       C  
ATOM   4653  CG  GLN C  65      20.897 -26.909  73.606  1.00 95.08           C  
ANISOU 4653  CG  GLN C  65    15683  10136  10308   -346   1343   1475       C  
ATOM   4654  CD  GLN C  65      19.737 -27.673  72.993  1.00 99.99           C  
ANISOU 4654  CD  GLN C  65    16278  10690  11023   -440   1488   1453       C  
ATOM   4655  OE1 GLN C  65      19.609 -28.884  73.180  1.00103.37           O  
ANISOU 4655  OE1 GLN C  65    16768  11018  11490   -455   1568   1514       O  
ATOM   4656  NE2 GLN C  65      18.887 -26.967  72.254  1.00 99.37           N  
ANISOU 4656  NE2 GLN C  65    16107  10670  10981   -505   1520   1362       N  
ATOM   4657  N   ASN C  66      18.813 -25.807  77.505  1.00 89.17           N  
ANISOU 4657  N   ASN C  66    15142   9461   9277   -297   1509   1610       N  
ATOM   4658  CA  ASN C  66      17.680 -26.160  78.354  1.00 92.64           C  
ANISOU 4658  CA  ASN C  66    15641   9871   9685   -326   1642   1660       C  
ATOM   4659  C   ASN C  66      16.994 -24.964  79.008  1.00 95.43           C  
ANISOU 4659  C   ASN C  66    15983  10320   9957   -314   1642   1633       C  
ATOM   4660  O   ASN C  66      15.887 -25.100  79.531  1.00 99.22           O  
ANISOU 4660  O   ASN C  66    16488  10795  10417   -348   1757   1659       O  
ATOM   4661  CB  ASN C  66      18.120 -27.141  79.442  1.00 93.28           C  
ANISOU 4661  CB  ASN C  66    15848   9873   9722   -277   1668   1772       C  
ATOM   4662  CG  ASN C  66      18.463 -28.508  78.891  1.00 92.90           C  
ANISOU 4662  CG  ASN C  66    15828   9713   9758   -299   1710   1808       C  
ATOM   4663  OD1 ASN C  66      17.755 -29.042  78.038  1.00 91.15           O  
ANISOU 4663  OD1 ASN C  66    15559   9446   9627   -380   1799   1773       O  
ATOM   4664  ND2 ASN C  66      19.556 -29.083  79.378  1.00 94.39           N  
ANISOU 4664  ND2 ASN C  66    16092   9856   9917   -225   1647   1876       N  
ATOM   4665  N   HIS C  67      17.661 -23.810  78.981  1.00 92.21           N  
ANISOU 4665  N   HIS C  67    15535   9998   9502   -265   1513   1584       N  
ATOM   4666  CA  HIS C  67      17.196 -22.598  79.663  1.00 89.48           C  
ANISOU 4666  CA  HIS C  67    15184   9741   9072   -239   1491   1559       C  
ATOM   4667  C   HIS C  67      17.206 -22.810  81.179  1.00 86.91           C  
ANISOU 4667  C   HIS C  67    14973   9398   8651   -185   1516   1651       C  
ATOM   4668  O   HIS C  67      16.206 -22.578  81.859  1.00 85.24           O  
ANISOU 4668  O   HIS C  67    14796   9202   8390   -194   1603   1669       O  
ATOM   4669  CB  HIS C  67      15.803 -22.183  79.168  1.00 91.29           C  
ANISOU 4669  CB  HIS C  67    15347  10008   9331   -304   1591   1500       C  
ATOM   4670  CG  HIS C  67      15.466 -20.746  79.420  1.00 93.80           C  
ANISOU 4670  CG  HIS C  67    15632  10425   9582   -275   1541   1442       C  
ATOM   4671  ND1 HIS C  67      16.426 -19.777  79.620  1.00 94.12           N  
ANISOU 4671  ND1 HIS C  67    15699  10501   9560   -214   1409   1404       N  
ATOM   4672  CD2 HIS C  67      14.271 -20.113  79.495  1.00 95.27           C  
ANISOU 4672  CD2 HIS C  67    15789  10665   9746   -298   1615   1409       C  
ATOM   4673  CE1 HIS C  67      15.836 -18.610  79.811  1.00 94.39           C  
ANISOU 4673  CE1 HIS C  67    15729  10596   9539   -200   1404   1349       C  
ATOM   4674  NE2 HIS C  67      14.529 -18.786  79.739  1.00 95.00           N  
ANISOU 4674  NE2 HIS C  67    15771  10688   9637   -246   1528   1352       N  
ATOM   4675  N   LYS C  68      18.351 -23.252  81.696  1.00 84.26           N  
ANISOU 4675  N   LYS C  68    14707   9025   8282   -126   1444   1709       N  
ATOM   4676  CA  LYS C  68      18.499 -23.572  83.113  1.00 84.35           C  
ANISOU 4676  CA  LYS C  68    14848   9003   8200    -69   1467   1798       C  
ATOM   4677  C   LYS C  68      19.809 -23.041  83.686  1.00 76.79           C  
ANISOU 4677  C   LYS C  68    13943   8072   7162     13   1331   1807       C  
ATOM   4678  O   LYS C  68      20.871 -23.225  83.092  1.00 74.75           O  
ANISOU 4678  O   LYS C  68    13647   7814   6939     30   1237   1796       O  
ATOM   4679  CB  LYS C  68      18.469 -25.087  83.321  1.00 89.93           C  
ANISOU 4679  CB  LYS C  68    15607   9612   8952    -84   1551   1890       C  
ATOM   4680  CG  LYS C  68      17.148 -25.767  83.028  1.00 92.60           C  
ANISOU 4680  CG  LYS C  68    15939   9898   9348   -166   1710   1897       C  
ATOM   4681  CD  LYS C  68      17.352 -27.272  82.990  1.00 95.64           C  
ANISOU 4681  CD  LYS C  68    16393  10161   9785   -181   1780   1968       C  
ATOM   4682  CE  LYS C  68      16.046 -28.033  83.109  1.00 98.32           C  
ANISOU 4682  CE  LYS C  68    16759  10441  10156   -258   1948   1998       C  
ATOM   4683  NZ  LYS C  68      16.278 -29.502  83.015  1.00100.00           N  
ANISOU 4683  NZ  LYS C  68    17043  10528  10426   -276   2014   2062       N  
ATOM   4684  N   PRO C  69      19.739 -22.389  84.856  1.00 72.01           N  
ANISOU 4684  N   PRO C  69    13422   7492   6446     64   1320   1827       N  
ATOM   4685  CA  PRO C  69      20.934 -21.944  85.580  1.00 72.11           C  
ANISOU 4685  CA  PRO C  69    13497   7528   6372    140   1200   1845       C  
ATOM   4686  C   PRO C  69      21.727 -23.117  86.140  1.00 78.11           C  
ANISOU 4686  C   PRO C  69    14332   8224   7122    185   1197   1945       C  
ATOM   4687  O   PRO C  69      21.167 -24.185  86.387  1.00 76.38           O  
ANISOU 4687  O   PRO C  69    14156   7933   6932    167   1307   2012       O  
ATOM   4688  CB  PRO C  69      20.360 -21.126  86.742  1.00 71.87           C  
ANISOU 4688  CB  PRO C  69    13548   7525   6235    174   1226   1850       C  
ATOM   4689  CG  PRO C  69      18.990 -20.763  86.321  1.00 70.27           C  
ANISOU 4689  CG  PRO C  69    13291   7341   6065    116   1324   1802       C  
ATOM   4690  CD  PRO C  69      18.502 -21.893  85.480  1.00 70.04           C  
ANISOU 4690  CD  PRO C  69    13203   7263   6147     50   1414   1823       C  
ATOM   4691  N   LEU C  70      23.023 -22.906  86.338  1.00 81.87           N  
ANISOU 4691  N   LEU C  70    14825   8728   7555    242   1073   1954       N  
ATOM   4692  CA  LEU C  70      23.886 -23.902  86.955  1.00 84.65           C  
ANISOU 4692  CA  LEU C  70    15253   9031   7881    300   1055   2049       C  
ATOM   4693  C   LEU C  70      24.583 -23.284  88.157  1.00 85.85           C  
ANISOU 4693  C   LEU C  70    15490   9221   7909    373    977   2077       C  
ATOM   4694  O   LEU C  70      24.858 -22.084  88.169  1.00 85.49           O  
ANISOU 4694  O   LEU C  70    15418   9248   7818    378    891   2010       O  
ATOM   4695  CB  LEU C  70      24.932 -24.391  85.954  1.00 86.55           C  
ANISOU 4695  CB  LEU C  70    15420   9272   8195    303    972   2042       C  
ATOM   4696  CG  LEU C  70      24.714 -25.713  85.215  1.00 87.85           C  
ANISOU 4696  CG  LEU C  70    15561   9352   8465    269   1049   2080       C  
ATOM   4697  CD1 LEU C  70      23.319 -25.808  84.616  1.00 87.44           C  
ANISOU 4697  CD1 LEU C  70    15461   9272   8488    183   1172   2039       C  
ATOM   4698  CD2 LEU C  70      25.774 -25.859  84.134  1.00 85.86           C  
ANISOU 4698  CD2 LEU C  70    15220   9124   8279    275    946   2052       C  
ATOM   4699  N   GLU C  71      24.858 -24.101  89.168  1.00 87.28           N  
ANISOU 4699  N   GLU C  71    15776   9351   8035    428   1009   2174       N  
ATOM   4700  CA  GLU C  71      25.630 -23.650  90.318  1.00 85.52           C  
ANISOU 4700  CA  GLU C  71    15636   9163   7695    502    932   2210       C  
ATOM   4701  C   GLU C  71      26.999 -23.171  89.843  1.00 81.99           C  
ANISOU 4701  C   GLU C  71    15126   8786   7241    528    777   2177       C  
ATOM   4702  O   GLU C  71      27.677 -23.863  89.085  1.00 79.30           O  
ANISOU 4702  O   GLU C  71    14733   8434   6966    530    741   2193       O  
ATOM   4703  CB  GLU C  71      25.782 -24.777  91.342  1.00 86.75           C  
ANISOU 4703  CB  GLU C  71    15909   9246   7805    560    992   2324       C  
ATOM   4704  N   GLY C  72      27.393 -21.979  90.275  1.00 83.28           N  
ANISOU 4704  N   GLY C  72    15295   9021   7326    545    686   2130       N  
ATOM   4705  CA  GLY C  72      28.647 -21.391  89.837  1.00 83.56           C  
ANISOU 4705  CA  GLY C  72    15266   9134   7351    558    539   2093       C  
ATOM   4706  C   GLY C  72      28.843 -19.986  90.373  1.00 81.89           C  
ANISOU 4706  C   GLY C  72    15072   8990   7053    562    458   2034       C  
ATOM   4707  O   GLY C  72      28.038 -19.505  91.171  1.00 80.94           O  
ANISOU 4707  O   GLY C  72    15024   8854   6874    566    517   2029       O  
ATOM   4708  N   LYS C  73      29.906 -19.320  89.929  1.00 80.08           N  
ANISOU 4708  N   LYS C  73    14777   8834   6815    559    326   1989       N  
ATOM   4709  CA  LYS C  73      30.243 -18.000  90.459  1.00 80.47           C  
ANISOU 4709  CA  LYS C  73    14850   8945   6781    561    239   1935       C  
ATOM   4710  C   LYS C  73      29.289 -16.899  89.995  1.00 76.91           C  
ANISOU 4710  C   LYS C  73    14369   8497   6354    504    265   1831       C  
ATOM   4711  O   LYS C  73      29.340 -15.775  90.494  1.00 75.27           O  
ANISOU 4711  O   LYS C  73    14199   8321   6078    504    214   1784       O  
ATOM   4712  CB  LYS C  73      31.698 -17.623  90.156  1.00 81.57           C  
ANISOU 4712  CB  LYS C  73    14928   9165   6901    569     90   1923       C  
ATOM   4713  CG  LYS C  73      31.991 -17.266  88.711  1.00 81.61           C  
ANISOU 4713  CG  LYS C  73    14802   9208   7000    512     32   1841       C  
ATOM   4714  CD  LYS C  73      33.243 -16.404  88.631  1.00 83.94           C  
ANISOU 4714  CD  LYS C  73    15051   9594   7250    508   -116   1806       C  
ATOM   4715  CE  LYS C  73      33.978 -16.603  87.319  1.00 86.02           C  
ANISOU 4715  CE  LYS C  73    15184   9900   7599    478   -184   1775       C  
ATOM   4716  NZ  LYS C  73      34.536 -17.981  87.219  1.00 87.76           N  
ANISOU 4716  NZ  LYS C  73    15391  10107   7846    528   -171   1870       N  
ATOM   4717  N   TYR C  74      28.425 -17.222  89.038  1.00 74.64           N  
ANISOU 4717  N   TYR C  74    14017   8177   6164    456    345   1796       N  
ATOM   4718  CA  TYR C  74      27.339 -16.322  88.666  1.00 72.07           C  
ANISOU 4718  CA  TYR C  74    13672   7850   5862    410    393   1709       C  
ATOM   4719  C   TYR C  74      26.044 -16.804  89.313  1.00 68.10           C  
ANISOU 4719  C   TYR C  74    13240   7289   5346    418    539   1754       C  
ATOM   4720  O   TYR C  74      25.591 -17.919  89.054  1.00 66.52           O  
ANISOU 4720  O   TYR C  74    13029   7042   5205    408    629   1806       O  
ATOM   4721  CB  TYR C  74      27.185 -16.233  87.143  1.00 70.42           C  
ANISOU 4721  CB  TYR C  74    13337   7653   5765    348    384   1632       C  
ATOM   4722  CG  TYR C  74      28.234 -15.378  86.464  1.00 67.95           C  
ANISOU 4722  CG  TYR C  74    12953   7404   5463    328    244   1561       C  
ATOM   4723  CD1 TYR C  74      28.139 -13.990  86.474  1.00 65.12           C  
ANISOU 4723  CD1 TYR C  74    12598   7074   5070    306    189   1474       C  
ATOM   4724  CD2 TYR C  74      29.317 -15.955  85.810  1.00 65.18           C  
ANISOU 4724  CD2 TYR C  74    12529   7079   5155    330    170   1583       C  
ATOM   4725  CE1 TYR C  74      29.095 -13.203  85.857  1.00 63.96           C  
ANISOU 4725  CE1 TYR C  74    12389   6979   4935    279     65   1410       C  
ATOM   4726  CE2 TYR C  74      30.277 -15.175  85.190  1.00 62.95           C  
ANISOU 4726  CE2 TYR C  74    12177   6859   4882    307     44   1520       C  
ATOM   4727  CZ  TYR C  74      30.161 -13.800  85.215  1.00 61.85           C  
ANISOU 4727  CZ  TYR C  74    12045   6746   4711    278     -7   1433       C  
ATOM   4728  OH  TYR C  74      31.113 -13.016  84.603  1.00 57.91           O  
ANISOU 4728  OH  TYR C  74    11478   6303   4223    248   -128   1372       O  
ATOM   4729  N   GLU C  75      25.460 -15.964  90.162  1.00 65.85           N  
ANISOU 4729  N   GLU C  75    13030   7007   4982    435    561   1735       N  
ATOM   4730  CA  GLU C  75      24.244 -16.324  90.889  1.00 70.30           C  
ANISOU 4730  CA  GLU C  75    13665   7526   5520    447    695   1780       C  
ATOM   4731  C   GLU C  75      22.981 -15.903  90.152  1.00 64.95           C  
ANISOU 4731  C   GLU C  75    12928   6848   4901    396    778   1712       C  
ATOM   4732  O   GLU C  75      22.548 -14.757  90.249  1.00 63.81           O  
ANISOU 4732  O   GLU C  75    12794   6729   4722    393    762   1644       O  
ATOM   4733  CB  GLU C  75      24.249 -15.711  92.289  1.00 78.58           C  
ANISOU 4733  CB  GLU C  75    14834   8578   6446    502    684   1806       C  
ATOM   4734  CG  GLU C  75      24.904 -16.579  93.342  1.00 86.17           C  
ANISOU 4734  CG  GLU C  75    15883   9515   7343    561    682   1912       C  
ATOM   4735  CD  GLU C  75      24.423 -16.245  94.737  1.00 92.10           C  
ANISOU 4735  CD  GLU C  75    16758  10251   7986    611    727   1950       C  
ATOM   4736  OE1 GLU C  75      25.037 -15.372  95.385  1.00 94.37           O  
ANISOU 4736  OE1 GLU C  75    17097  10569   8188    641    638   1930       O  
ATOM   4737  OE2 GLU C  75      23.425 -16.851  95.182  1.00 94.14           O  
ANISOU 4737  OE2 GLU C  75    17062  10466   8242    616    853   2002       O  
ATOM   4738  N   TRP C  76      22.375 -16.853  89.451  1.00 64.70           N  
ANISOU 4738  N   TRP C  76    12838   6786   4958    356    868   1734       N  
ATOM   4739  CA  TRP C  76      21.286 -16.562  88.524  1.00 67.28           C  
ANISOU 4739  CA  TRP C  76    13084   7123   5357    299    938   1668       C  
ATOM   4740  C   TRP C  76      19.912 -16.351  89.153  1.00 79.16           C  
ANISOU 4740  C   TRP C  76    14635   8620   6823    300   1059   1681       C  
ATOM   4741  O   TRP C  76      19.040 -17.218  89.079  1.00 85.59           O  
ANISOU 4741  O   TRP C  76    15438   9404   7679    271   1179   1727       O  
ATOM   4742  CB  TRP C  76      21.220 -17.642  87.446  1.00 64.27           C  
ANISOU 4742  CB  TRP C  76    12614   6715   5090    249    983   1682       C  
ATOM   4743  CG  TRP C  76      22.423 -17.622  86.573  1.00 61.48           C  
ANISOU 4743  CG  TRP C  76    12190   6384   4785    241    863   1647       C  
ATOM   4744  CD1 TRP C  76      23.513 -18.436  86.655  1.00 60.90           C  
ANISOU 4744  CD1 TRP C  76    12129   6293   4718    269    808   1708       C  
ATOM   4745  CD2 TRP C  76      22.676 -16.715  85.497  1.00 57.71           C  
ANISOU 4745  CD2 TRP C  76    11619   5954   4355    206    782   1544       C  
ATOM   4746  NE1 TRP C  76      24.427 -18.100  85.685  1.00 60.15           N  
ANISOU 4746  NE1 TRP C  76    11947   6238   4670    252    697   1650       N  
ATOM   4747  CE2 TRP C  76      23.936 -17.045  84.961  1.00 57.53           C  
ANISOU 4747  CE2 TRP C  76    11550   5943   4364    211    680   1548       C  
ATOM   4748  CE3 TRP C  76      21.955 -15.658  84.930  1.00 55.20           C  
ANISOU 4748  CE3 TRP C  76    11252   5668   4054    173    787   1449       C  
ATOM   4749  CZ2 TRP C  76      24.492 -16.357  83.884  1.00 54.04           C  
ANISOU 4749  CZ2 TRP C  76    11015   5545   3972    179    584   1461       C  
ATOM   4750  CZ3 TRP C  76      22.508 -14.978  83.863  1.00 50.62           C  
ANISOU 4750  CZ3 TRP C  76    10584   5125   3525    143    691   1362       C  
ATOM   4751  CH2 TRP C  76      23.764 -15.330  83.351  1.00 49.90           C  
ANISOU 4751  CH2 TRP C  76    10449   5045   3466    144    592   1368       C  
ATOM   4752  N   GLN C  77      19.725 -15.186  89.761  1.00 83.34           N  
ANISOU 4752  N   GLN C  77    15216   9177   7272    332   1026   1639       N  
ATOM   4753  CA  GLN C  77      18.409 -14.761  90.207  1.00 87.91           C  
ANISOU 4753  CA  GLN C  77    15824   9762   7815    335   1129   1634       C  
ATOM   4754  C   GLN C  77      17.555 -14.535  88.966  1.00 85.43           C  
ANISOU 4754  C   GLN C  77    15394   9475   7591    275   1176   1564       C  
ATOM   4755  O   GLN C  77      17.994 -13.887  88.015  1.00 83.80           O  
ANISOU 4755  O   GLN C  77    15115   9294   7431    251   1092   1481       O  
ATOM   4756  CB  GLN C  77      18.520 -13.457  90.995  1.00 93.17           C  
ANISOU 4756  CB  GLN C  77    16568  10450   8382    385   1066   1594       C  
ATOM   4757  CG  GLN C  77      19.810 -13.320  91.788  1.00 98.09           C  
ANISOU 4757  CG  GLN C  77    17271  11065   8932    433    956   1621       C  
ATOM   4758  CD  GLN C  77      20.233 -11.874  91.958  1.00101.07           C  
ANISOU 4758  CD  GLN C  77    17681  11468   9252    453    852   1542       C  
ATOM   4759  OE1 GLN C  77      19.431 -11.020  92.335  1.00103.44           O  
ANISOU 4759  OE1 GLN C  77    18023  11774   9507    472    888   1509       O  
ATOM   4760  NE2 GLN C  77      21.498 -11.589  91.668  1.00100.02           N  
ANISOU 4760  NE2 GLN C  77    17530  11349   9123    447    723   1514       N  
ATOM   4761  N   GLU C  78      16.340 -15.070  88.966  1.00 85.59           N  
ANISOU 4761  N   GLU C  78    15395   9491   7634    247   1310   1598       N  
ATOM   4762  CA  GLU C  78      15.452 -14.920  87.819  1.00 86.96           C  
ANISOU 4762  CA  GLU C  78    15454   9696   7890    187   1364   1538       C  
ATOM   4763  C   GLU C  78      14.675 -13.613  87.897  1.00 87.57           C  
ANISOU 4763  C   GLU C  78    15531   9821   7920    208   1369   1471       C  
ATOM   4764  O   GLU C  78      14.930 -12.775  88.763  1.00 88.07           O  
ANISOU 4764  O   GLU C  78    15683   9887   7893    266   1318   1463       O  
ATOM   4765  CB  GLU C  78      14.473 -16.089  87.741  1.00 90.57           C  
ANISOU 4765  CB  GLU C  78    15882  10134   8396    139   1509   1604       C  
ATOM   4766  CG  GLU C  78      14.908 -17.314  88.518  1.00 95.86           C  
ANISOU 4766  CG  GLU C  78    16630  10741   9052    153   1544   1710       C  
ATOM   4767  CD  GLU C  78      13.744 -18.220  88.858  1.00 98.88           C  
ANISOU 4767  CD  GLU C  78    17019  11104   9448    115   1700   1782       C  
ATOM   4768  OE1 GLU C  78      13.742 -18.793  89.968  1.00100.44           O  
ANISOU 4768  OE1 GLU C  78    17317  11263   9584    148   1746   1869       O  
ATOM   4769  OE2 GLU C  78      12.829 -18.354  88.017  1.00 98.88           O  
ANISOU 4769  OE2 GLU C  78    16924  11131   9517     50   1775   1752       O  
ATOM   4770  N   VAL C  79      13.721 -13.449  86.987  1.00 87.55           N  
ANISOU 4770  N   VAL C  79    15429   9855   7979    161   1431   1424       N  
ATOM   4771  CA  VAL C  79      12.891 -12.252  86.949  1.00 89.51           C  
ANISOU 4771  CA  VAL C  79    15666  10152   8191    182   1444   1362       C  
ATOM   4772  C   VAL C  79      11.415 -12.602  87.103  1.00 94.86           C  
ANISOU 4772  C   VAL C  79    16313  10866   8865    160   1593   1400       C  
ATOM   4773  O   VAL C  79      10.908 -13.502  86.433  1.00 97.21           O  
ANISOU 4773  O   VAL C  79    16527  11169   9241     95   1672   1420       O  
ATOM   4774  CB  VAL C  79      13.085 -11.478  85.635  1.00 85.79           C  
ANISOU 4774  CB  VAL C  79    15095   9710   7790    152   1370   1256       C  
ATOM   4775  CG1 VAL C  79      12.158 -10.275  85.589  1.00 85.89           C  
ANISOU 4775  CG1 VAL C  79    15098   9769   7766    179   1391   1197       C  
ATOM   4776  CG2 VAL C  79      14.537 -11.051  85.482  1.00 84.39           C  
ANISOU 4776  CG2 VAL C  79    14945   9506   7613    168   1221   1215       C  
TER    4777      VAL C  79                                                      
HETATM 4778  S   SO4 A 301      36.178  17.276  65.257  1.00 28.34           S  
HETATM 4779  O1  SO4 A 301      35.536  16.321  64.350  1.00 29.46           O  
HETATM 4780  O2  SO4 A 301      37.027  18.168  64.480  1.00 35.13           O  
HETATM 4781  O3  SO4 A 301      35.130  18.047  65.921  1.00 29.50           O  
HETATM 4782  O4  SO4 A 301      36.971  16.542  66.234  1.00 26.98           O  
HETATM 4783  O   HOH A 401      20.679  14.343  59.460  1.00 26.25           O  
HETATM 4784  O   HOH A 402      22.837  18.279  61.770  1.00 24.00           O  
HETATM 4785  O   HOH A 403       5.561  11.038  56.172  1.00 30.67           O  
HETATM 4786  O   HOH A 404      12.121   6.703  69.948  1.00 36.69           O  
HETATM 4787  O   HOH A 405      39.419  16.265  66.135  1.00 29.49           O  
HETATM 4788  O   HOH A 406      11.114  24.186  48.378  1.00 36.25           O  
HETATM 4789  O   HOH A 407      33.014  19.767  84.870  1.00 33.18           O  
HETATM 4790  O   HOH A 408      31.934  26.306  73.510  1.00 42.47           O  
HETATM 4791  O   HOH A 409      15.079  26.160  67.619  1.00 32.47           O  
HETATM 4792  O   HOH A 410       0.558  26.805  55.428  1.00 32.94           O  
HETATM 4793  O   HOH A 411      33.837   0.010  69.892  1.00 36.99           O  
HETATM 4794  O   HOH A 412      31.442  21.559  77.692  1.00 30.92           O  
HETATM 4795  O   HOH A 413      33.176  19.081  71.273  1.00 18.97           O  
HETATM 4796  O   HOH A 414      36.573  15.263  62.232  1.00 31.06           O  
HETATM 4797  O   HOH A 415      29.279   0.286  78.974  1.00 24.31           O  
HETATM 4798  O   HOH A 416      33.206  -3.681  60.898  1.00 37.18           O  
HETATM 4799  O   HOH A 417      18.634  25.365  83.640  1.00 48.68           O  
HETATM 4800  O   HOH A 418       8.026  11.164  81.336  1.00 36.99           O  
HETATM 4801  O   HOH A 419      23.017  -0.603  56.744  1.00 21.99           O  
HETATM 4802  O   HOH A 420      -5.000  26.191  56.321  1.00 21.57           O  
HETATM 4803  O   HOH A 421      20.812  27.797  86.124  1.00 47.96           O  
HETATM 4804  O   HOH A 422       7.816   8.314  76.628  1.00 40.89           O  
HETATM 4805  O   HOH A 423      17.570   2.696  49.774  1.00 31.89           O  
HETATM 4806  O   HOH A 424       5.413  19.113  48.769  1.00 42.94           O  
HETATM 4807  O   HOH A 425       4.947  26.398  79.171  1.00 46.33           O  
HETATM 4808  O   HOH A 426      23.726   3.751  52.919  1.00 19.65           O  
HETATM 4809  O   HOH A 427      26.838  -1.490  84.602  1.00 46.18           O  
HETATM 4810  O   HOH A 428      16.907  15.065  56.509  1.00 24.21           O  
HETATM 4811  O   HOH A 429      29.094   7.582  83.254  1.00 36.09           O  
HETATM 4812  O   HOH A 430      10.208   0.975  70.413  1.00 43.07           O  
HETATM 4813  O   HOH A 431      23.228  25.923  83.858  1.00 33.77           O  
HETATM 4814  O   HOH A 432      25.380  11.629  87.022  1.00 20.93           O  
HETATM 4815  O   HOH A 433      22.527   8.527  48.362  1.00 33.22           O  
HETATM 4816  O   HOH A 434       8.574  18.383  94.679  1.00 43.71           O  
HETATM 4817  O   HOH A 435       6.163   9.710  59.974  1.00 23.98           O  
HETATM 4818  O   HOH A 436       3.103  27.056  51.734  1.00 41.07           O  
HETATM 4819  O   HOH A 437      14.872  -4.601  60.121  1.00 28.96           O  
HETATM 4820  O   HOH A 438      22.300   7.164  87.059  1.00 20.04           O  
HETATM 4821  O   HOH A 439      32.876  11.557  68.236  1.00 24.47           O  
HETATM 4822  O   HOH A 440      24.214  24.900  66.406  1.00 33.79           O  
HETATM 4823  O   HOH A 441      11.419  31.068  82.149  1.00 40.96           O  
HETATM 4824  O   HOH A 442      10.463  12.367  96.019  1.00 31.33           O  
HETATM 4825  O   HOH A 443       1.238  15.490  55.870  1.00 35.23           O  
HETATM 4826  O   HOH A 444      28.897  -3.614  73.208  1.00 28.17           O  
HETATM 4827  O   HOH A 445       3.181  16.232  77.906  1.00 36.01           O  
HETATM 4828  O   HOH A 446      15.386   8.189  54.227  1.00 19.32           O  
HETATM 4829  O   HOH A 447      26.185  18.304  86.649  1.00 22.29           O  
HETATM 4830  O   HOH A 448      14.895  -0.276  69.503  1.00 31.46           O  
HETATM 4831  O   HOH A 449       9.924 -17.564  53.468  1.00 27.36           O  
HETATM 4832  O   HOH A 450      30.364  18.690  64.725  1.00 27.58           O  
HETATM 4833  O   HOH A 451      17.103  31.170  55.003  1.00 48.48           O  
HETATM 4834  O   HOH A 452       8.700  18.748  78.052  1.00 32.08           O  
HETATM 4835  O   HOH A 453      14.070  -3.031  57.262  1.00 18.75           O  
HETATM 4836  O   HOH A 454      24.173  15.311  63.920  1.00 13.48           O  
HETATM 4837  O   HOH A 455      28.497  13.612  83.936  1.00 21.35           O  
HETATM 4838  O   HOH A 456      12.674  19.640  49.662  1.00 37.19           O  
HETATM 4839  O   HOH A 457      30.899   9.447  80.192  1.00 31.87           O  
HETATM 4840  O   HOH A 458      12.688   3.332  64.771  1.00 20.81           O  
HETATM 4841  O   HOH A 459       4.613  24.617  73.880  1.00 37.78           O  
HETATM 4842  O   HOH A 460      22.176  17.019  64.411  1.00 16.27           O  
HETATM 4843  O   HOH A 461      28.973   9.321  91.077  1.00 47.43           O  
HETATM 4844  O   HOH A 462       8.635   2.107  60.042  1.00 51.97           O  
HETATM 4845  O   HOH A 463      25.325   5.292  51.348  1.00 23.77           O  
HETATM 4846  O   HOH A 464      13.279  25.264  66.078  1.00 26.18           O  
HETATM 4847  O   HOH A 465      17.887  14.119  59.326  1.00 14.92           O  
HETATM 4848  O   HOH A 466       2.125  28.941  68.158  1.00 35.63           O  
HETATM 4849  O   HOH A 467       9.722  14.654  75.302  1.00 15.53           O  
HETATM 4850  O   HOH A 468       9.649  28.426  63.053  1.00 28.59           O  
HETATM 4851  O   HOH A 469      13.669  11.665  65.652  1.00 12.39           O  
HETATM 4852  O   HOH A 470      31.763  10.646  72.497  1.00 17.60           O  
HETATM 4853  O   HOH A 471      14.613  17.713  93.919  1.00 38.13           O  
HETATM 4854  O   HOH A 472      18.064   8.406  54.896  1.00 17.18           O  
HETATM 4855  O   HOH A 473      25.379  27.184  82.547  1.00 47.48           O  
HETATM 4856  O   HOH A 474      12.723  17.779  86.628  1.00 18.11           O  
HETATM 4857  O   HOH A 475      31.134  23.860  78.385  1.00 42.64           O  
HETATM 4858  O   HOH A 476      33.811   9.250  77.827  1.00 38.73           O  
HETATM 4859  O   HOH A 477      22.904  30.967  71.985  1.00 51.75           O  
HETATM 4860  O   HOH A 478       5.011  27.237  55.654  1.00 43.65           O  
HETATM 4861  O   HOH A 479       9.219   8.022  94.101  1.00 28.97           O  
HETATM 4862  O   HOH A 480      16.878  -1.907  62.788  1.00 18.93           O  
HETATM 4863  O   HOH A 481      -4.520  17.716  69.560  1.00 28.17           O  
HETATM 4864  O   HOH A 482      29.408   4.877  82.434  1.00 32.18           O  
HETATM 4865  O   HOH A 483      29.665  -0.489  75.459  1.00 25.79           O  
HETATM 4866  O   HOH A 484       8.339  31.378  81.271  1.00 25.56           O  
HETATM 4867  O   HOH A 485      24.319  30.026  75.828  1.00 31.20           O  
HETATM 4868  O   HOH A 486       9.363  33.657  69.201  1.00 40.55           O  
HETATM 4869  O   HOH A 487      -4.403  25.970  66.934  1.00 30.50           O  
HETATM 4870  O   HOH A 488       3.589  20.127  72.288  1.00 27.12           O  
HETATM 4871  O   HOH A 489      27.054  18.704  91.455  1.00 46.47           O  
HETATM 4872  O   HOH A 490      19.412  31.350  75.319  1.00 31.04           O  
HETATM 4873  O   HOH A 491       7.046   4.047  73.832  1.00 35.87           O  
HETATM 4874  O   HOH A 492      11.709   4.237  52.758  1.00 31.65           O  
HETATM 4875  O   HOH A 493      17.474   1.157  68.066  1.00 15.21           O  
HETATM 4876  O   HOH A 494      16.155   8.453  67.859  1.00 13.72           O  
HETATM 4877  O   HOH A 495       8.073  14.656  72.913  1.00 15.48           O  
HETATM 4878  O   HOH A 496       5.905   9.656  52.333  1.00 47.59           O  
HETATM 4879  O   HOH A 497      28.989   3.775  86.468  1.00 36.24           O  
HETATM 4880  O   HOH A 498      21.217  14.234  92.329  1.00 39.10           O  
HETATM 4881  O   HOH A 499       4.954  29.611  58.393  1.00 39.73           O  
HETATM 4882  O   HOH A 500      16.182  19.653  54.719  1.00 40.79           O  
HETATM 4883  O   HOH A 501      13.030   0.074  61.193  1.00 31.60           O  
HETATM 4884  O   HOH A 502      29.691  -5.963  62.854  1.00 23.72           O  
HETATM 4885  O   HOH A 503      26.867  25.614  69.750  1.00 41.74           O  
HETATM 4886  O   HOH A 504       8.334  29.904  61.421  1.00 59.54           O  
HETATM 4887  O   HOH A 505       8.377  36.127  80.402  1.00 33.92           O  
HETATM 4888  O   HOH A 506      17.949  26.898  57.890  1.00 34.55           O  
HETATM 4889  O   HOH A 507       5.039  20.495  76.059  1.00 42.83           O  
HETATM 4890  O   HOH A 508      29.907   5.196  53.272  1.00 29.30           O  
HETATM 4891  O   HOH A 509      -3.296  20.480  56.916  1.00 23.60           O  
HETATM 4892  O   HOH A 510      14.172   2.024  62.986  1.00 26.86           O  
HETATM 4893  O   HOH A 511      14.426  26.993  87.428  1.00 41.80           O  
HETATM 4894  O   HOH A 512      24.250  25.307  62.648  1.00 45.04           O  
HETATM 4895  O   HOH A 513       8.916  14.868  68.066  1.00 14.59           O  
HETATM 4896  O   HOH A 514       1.517  28.776  73.547  1.00 48.34           O  
HETATM 4897  O   HOH A 515       9.898   1.765  81.142  1.00 41.58           O  
HETATM 4898  O   HOH A 516      12.806   7.284  54.635  1.00 19.40           O  
HETATM 4899  O   HOH A 517      14.229  20.350  87.552  1.00 42.45           O  
HETATM 4900  O   HOH A 518      -2.871  27.811  56.188  1.00 35.60           O  
HETATM 4901  O   HOH A 519      28.586  24.133  71.178  1.00 37.22           O  
HETATM 4902  O   HOH A 520      25.515  20.705  62.630  1.00 37.69           O  
HETATM 4903  O   HOH A 521       8.234   4.504  88.366  1.00 35.40           O  
HETATM 4904  O   HOH A 522      35.164   7.044  64.660  1.00 27.60           O  
HETATM 4905  O   HOH A 523      15.277  -0.671  77.467  1.00 43.88           O  
HETATM 4906  O   HOH A 524       8.901   8.833  56.890  1.00 38.47           O  
HETATM 4907  O   HOH A 525      22.446  -1.815  59.259  1.00 17.21           O  
HETATM 4908  O   HOH A 526      25.915  28.109  71.504  1.00 31.17           O  
HETATM 4909  O   HOH A 527      33.096  10.103  74.728  1.00 26.54           O  
HETATM 4910  O   HOH A 528       7.732  29.572  52.727  1.00 35.67           O  
HETATM 4911  O   HOH A 529      32.627  -5.907  63.839  1.00 47.99           O  
HETATM 4912  O   HOH A 530      26.242  20.934  87.685  1.00 23.54           O  
HETATM 4913  O   HOH A 531      14.405  28.684  50.304  1.00 48.90           O  
HETATM 4914  O   HOH A 532       5.855  23.511  76.069  1.00 42.76           O  
HETATM 4915  O   HOH A 533      24.772   2.322  49.276  1.00 34.33           O  
HETATM 4916  O   HOH A 534       7.803  12.204  92.938  1.00 38.82           O  
HETATM 4917  O   HOH A 535      11.426   8.376  52.692  1.00 42.47           O  
HETATM 4918  O   HOH A 536      -4.208  17.430  74.067  1.00 50.70           O  
HETATM 4919  O   HOH A 537       5.308   5.248  67.663  1.00 24.25           O  
HETATM 4920  O   HOH A 538      12.885  -8.003  62.182  1.00 39.08           O  
HETATM 4921  O   HOH A 539      13.465 -10.314  59.885  1.00 42.45           O  
HETATM 4922  O   HOH A 540      25.552   0.735  89.947  1.00 45.96           O  
HETATM 4923  O   HOH A 541      27.375  31.259  78.366  1.00 48.31           O  
HETATM 4924  O   HOH A 542       8.374   3.710  64.435  1.00 38.16           O  
HETATM 4925  O   HOH A 543      22.591  30.131  81.903  1.00 35.44           O  
HETATM 4926  O   HOH A 544      26.899  21.266  64.946  1.00 18.55           O  
HETATM 4927  O   HOH A 545      20.774  -4.461  80.711  1.00 50.15           O  
HETATM 4928  O   HOH A 546      -1.869  11.302  60.816  1.00 21.52           O  
HETATM 4929  O   HOH A 547       3.246   6.564  62.974  1.00 40.62           O  
HETATM 4930  O   HOH A 548      12.706  33.650  71.382  1.00 48.04           O  
HETATM 4931  O   HOH A 549      20.258   5.931  93.854  1.00 45.58           O  
HETATM 4932  O   HOH A 550      18.371   6.372  47.868  1.00 31.47           O  
HETATM 4933  O   HOH A 551      35.250   3.971  74.216  1.00 43.89           O  
HETATM 4934  O   HOH A 552      32.490  19.590  65.945  1.00 28.77           O  
HETATM 4935  O   HOH A 553      33.514   1.027  77.283  1.00 41.86           O  
HETATM 4936  O   HOH A 554      11.067  19.283  93.999  1.00 34.82           O  
HETATM 4937  O   HOH A 555      18.210  21.934  90.785  1.00 33.55           O  
HETATM 4938  O   HOH A 556       6.812  33.328  63.976  1.00 40.10           O  
HETATM 4939  O   HOH A 557      13.268  -6.144  57.822  1.00 29.65           O  
HETATM 4940  O   HOH A 558      14.157  26.230  63.722  1.00 21.94           O  
HETATM 4941  O   HOH A 559      10.596  34.377  81.141  1.00 40.95           O  
HETATM 4942  O   HOH A 560      19.445  -3.392  75.371  1.00 49.11           O  
HETATM 4943  O   HOH A 561       4.367  12.410  79.384  1.00 38.38           O  
HETATM 4944  O   HOH A 562      -0.130  31.750  66.293  1.00 29.49           O  
HETATM 4945  O   HOH A 563       0.700  27.986  52.000  1.00 43.53           O  
HETATM 4946  O   HOH A 564      15.605  14.875  52.053  1.00 37.33           O  
HETATM 4947  O   HOH A 565      26.057  13.367  94.123  1.00 40.55           O  
HETATM 4948  O   HOH A 566       4.966   7.956  71.190  1.00 25.78           O  
HETATM 4949  O   HOH A 567      -3.049  21.298  51.045  1.00 35.92           O  
HETATM 4950  O   HOH A 568      24.921   7.149  48.538  1.00 31.79           O  
HETATM 4951  O   HOH A 569       7.091   2.841  68.652  1.00 48.47           O  
HETATM 4952  O   HOH A 570      29.803   2.436  84.272  1.00 47.62           O  
HETATM 4953  O   HOH A 571      23.894  22.493  87.322  1.00 28.82           O  
HETATM 4954  O   HOH A 572      -0.978   8.299  62.143  1.00 42.63           O  
HETATM 4955  O   HOH A 573      12.253  -5.635  60.926  1.00 44.42           O  
HETATM 4956  O   HOH A 574      12.862  15.246  50.289  1.00 38.64           O  
HETATM 4957  O   HOH A 575      -2.140  30.989  64.226  1.00 43.88           O  
HETATM 4958  O   HOH A 576      20.387   7.548  46.962  1.00 42.51           O  
HETATM 4959  O   HOH A 577      13.083  -8.767  57.868  1.00 45.06           O  
HETATM 4960  O   HOH A 578      11.485   9.172  56.071  1.00 30.10           O  
HETATM 4961  O   HOH A 579       2.316  13.819  58.117  1.00 57.36           O  
HETATM 4962  O   HOH A 580      -3.885  29.152  67.252  1.00 31.05           O  
HETATM 4963  O   HOH A 581      14.416  -2.386  61.878  1.00 30.96           O  
HETATM 4964  O   HOH A 582      -4.474  26.141  52.017  1.00 39.14           O  
HETATM 4965  O   HOH A 583      25.974  29.647  73.579  1.00 37.46           O  
HETATM 4966  O   HOH A 584      17.057  30.421  72.962  1.00 43.65           O  
HETATM 4967  O   HOH A 585       8.821   8.426  53.181  1.00 47.40           O  
HETATM 4968  O   HOH A 586      35.614   9.005  66.555  1.00 37.83           O  
HETATM 4969  O   HOH A 587      11.895  -2.234  58.795  1.00 39.90           O  
HETATM 4970  O   HOH A 588      16.274  30.184  84.997  1.00 48.60           O  
HETATM 4971  O   HOH A 589      -5.467  13.292  66.944  1.00 47.83           O  
HETATM 4972  O   HOH A 590      30.740   9.605  82.959  1.00 42.58           O  
HETATM 4973  O   HOH A 591      26.766  21.030  90.338  1.00 43.03           O  
HETATM 4974  O   HOH A 592      -4.659  11.158  61.134  1.00 52.50           O  
HETATM 4975  O   HOH A 593      15.323  16.897  55.268  1.00 40.66           O  
HETATM 4976  O   HOH A 594       5.307  29.083  53.738  1.00 35.64           O  
HETATM 4977  O   HOH A 595      23.251  32.296  75.626  1.00 42.91           O  
HETATM 4978  O   HOH A 596      22.371  16.744  91.955  1.00 32.36           O  
HETATM 4979  O   HOH A 597      33.633   8.562  80.543  1.00 37.84           O  
HETATM 4980  O   HOH A 598      17.793 -19.918  63.068  1.00 49.58           O  
HETATM 4981  O   HOH A 599       3.842  26.285  49.338  1.00 46.70           O  
HETATM 4982  O   HOH A 600      -6.377  26.505  54.084  1.00 25.87           O  
HETATM 4983  O   HOH A 601      28.186  26.486  71.857  1.00 42.08           O  
HETATM 4984  O   HOH A 602      22.832  23.801  89.457  1.00 41.60           O  
HETATM 4985  O   HOH A 603      26.709  23.948  65.657  1.00 38.76           O  
HETATM 4986  O   HOH A 604      24.937  17.498  92.748  1.00 36.45           O  
HETATM 4987  O   HOH A 605      10.422   0.017  61.148  1.00 44.78           O  
HETATM 4988  O   HOH A 606      12.015  -3.452  62.647  1.00 39.43           O  
HETATM 4989  O   HOH B 501      20.490  -2.405  39.766  1.00 43.00           O  
HETATM 4990  O   HOH B 502      36.847 -16.319  58.647  1.00 40.08           O  
HETATM 4991  O   HOH B 503      25.423  16.957  62.100  1.00 25.29           O  
HETATM 4992  O   HOH B 504      33.509  13.402  38.179  1.00 30.62           O  
HETATM 4993  O   HOH B 505      48.292  -8.506  40.659  1.00 27.02           O  
HETATM 4994  O   HOH B 506      35.887 -10.228  49.634  1.00 29.37           O  
HETATM 4995  O   HOH B 507      40.845   9.187  57.775  1.00 29.42           O  
HETATM 4996  O   HOH B 508      46.006  -1.251  26.068  1.00 42.58           O  
HETATM 4997  O   HOH B 509      39.953  -9.607  36.209  1.00 24.22           O  
HETATM 4998  O   HOH B 510      32.796   0.727  29.723  1.00 24.08           O  
HETATM 4999  O   HOH B 511      30.487  -0.332  57.385  1.00 26.05           O  
HETATM 5000  O   HOH B 512      36.499 -26.943  48.805  1.00 25.56           O  
HETATM 5001  O   HOH B 513      39.483  -7.158  48.622  1.00 37.60           O  
HETATM 5002  O   HOH B 514      45.402   7.860  27.808  1.00 20.37           O  
HETATM 5003  O   HOH B 515      26.707 -25.149  44.944  1.00 21.61           O  
HETATM 5004  O   HOH B 516      18.633 -24.662  37.155  1.00 31.36           O  
HETATM 5005  O   HOH B 517      37.787  12.160  55.709  1.00 28.05           O  
HETATM 5006  O   HOH B 518      28.597  16.824  35.383  1.00 44.83           O  
HETATM 5007  O   HOH B 519      49.483  -4.678  39.235  1.00 24.38           O  
HETATM 5008  O   HOH B 520      40.344  10.954  61.718  1.00 38.53           O  
HETATM 5009  O   HOH B 521      39.710   0.523  24.175  1.00 40.68           O  
HETATM 5010  O   HOH B 522      46.803   6.090  53.587  1.00 18.02           O  
HETATM 5011  O   HOH B 523      25.262  13.936  66.128  1.00 13.20           O  
HETATM 5012  O   HOH B 524      42.589  -2.165  61.906  1.00 31.21           O  
HETATM 5013  O   HOH B 525      13.549 -26.561  47.878  1.00 34.22           O  
HETATM 5014  O   HOH B 526      14.778  -3.455  49.973  1.00 23.75           O  
HETATM 5015  O   HOH B 527      20.848  -9.096  29.503  1.00 38.88           O  
HETATM 5016  O   HOH B 528      10.362 -22.589  45.349  1.00 36.19           O  
HETATM 5017  O   HOH B 529      18.993 -19.139  60.940  1.00 27.99           O  
HETATM 5018  O   HOH B 530      44.574  13.552  33.886  1.00 23.81           O  
HETATM 5019  O   HOH B 531      36.764  13.620  65.660  1.00 27.16           O  
HETATM 5020  O   HOH B 532      16.328  -5.444  56.979  1.00 18.88           O  
HETATM 5021  O   HOH B 533      38.228  12.656  62.421  1.00 44.70           O  
HETATM 5022  O   HOH B 534      45.209   7.753  34.082  1.00 19.37           O  
HETATM 5023  O   HOH B 535      35.784 -17.157  35.042  1.00 33.74           O  
HETATM 5024  O   HOH B 536      42.796   0.761  55.777  1.00 13.78           O  
HETATM 5025  O   HOH B 537      48.478  16.552  48.595  1.00 36.42           O  
HETATM 5026  O   HOH B 538      26.649  -1.437  54.847  1.00 14.62           O  
HETATM 5027  O   HOH B 539      36.789 -15.580  41.748  1.00 13.97           O  
HETATM 5028  O   HOH B 540      20.378  -2.989  35.365  1.00 32.16           O  
HETATM 5029  O   HOH B 541      32.475  -3.220  29.409  1.00 20.58           O  
HETATM 5030  O   HOH B 542      49.800  -6.113  43.140  1.00 30.52           O  
HETATM 5031  O   HOH B 543      40.877  11.722  56.256  1.00 27.85           O  
HETATM 5032  O   HOH B 544      46.777  12.858  41.571  1.00 28.37           O  
HETATM 5033  O   HOH B 545      35.035  -1.437  66.512  1.00 41.28           O  
HETATM 5034  O   HOH B 546      22.679  -8.877  34.850  1.00 23.55           O  
HETATM 5035  O   HOH B 547      27.928   4.305  51.224  1.00 17.16           O  
HETATM 5036  O   HOH B 548      41.271 -24.679  44.850  1.00 41.15           O  
HETATM 5037  O   HOH B 549      31.150 -12.047  26.171  1.00 31.50           O  
HETATM 5038  O   HOH B 550      27.032 -17.501  37.081  1.00 23.23           O  
HETATM 5039  O   HOH B 551      40.640   5.719  51.856  1.00 11.30           O  
HETATM 5040  O   HOH B 552      10.323 -21.345  47.802  1.00 27.09           O  
HETATM 5041  O   HOH B 553      10.462 -22.597  49.943  1.00 44.77           O  
HETATM 5042  O   HOH B 554      28.567 -16.871  32.445  1.00 38.08           O  
HETATM 5043  O   HOH B 555      51.089   0.347  46.278  1.00 37.91           O  
HETATM 5044  O   HOH B 556      37.465  -3.588  25.867  1.00 41.47           O  
HETATM 5045  O   HOH B 557      38.002 -15.353  38.653  1.00 30.96           O  
HETATM 5046  O   HOH B 558      37.210 -10.300  44.567  1.00 20.23           O  
HETATM 5047  O   HOH B 559      33.241  10.966  27.948  1.00 35.84           O  
HETATM 5048  O   HOH B 560      37.652  -8.820  32.570  1.00 15.81           O  
HETATM 5049  O   HOH B 561      35.854  -5.165  54.743  1.00 41.23           O  
HETATM 5050  O   HOH B 562      27.188  -9.671  27.667  1.00 26.64           O  
HETATM 5051  O   HOH B 563      47.333  -2.504  32.911  1.00 28.57           O  
HETATM 5052  O   HOH B 564      45.865   1.064  52.831  1.00 19.53           O  
HETATM 5053  O   HOH B 565      10.954  -4.788  56.235  1.00 48.75           O  
HETATM 5054  O   HOH B 566      38.080  17.674  44.729  1.00 31.48           O  
HETATM 5055  O   HOH B 567      29.953 -10.451  35.785  1.00 17.03           O  
HETATM 5056  O   HOH B 568      42.270 -17.136  47.488  1.00 38.91           O  
HETATM 5057  O   HOH B 569      14.072 -12.304  54.997  1.00 31.61           O  
HETATM 5058  O   HOH B 570      24.195   1.744  54.656  1.00 22.77           O  
HETATM 5059  O   HOH B 571      40.114  16.329  51.626  1.00 29.55           O  
HETATM 5060  O   HOH B 572      25.809   7.018  41.773  1.00 44.44           O  
HETATM 5061  O   HOH B 573      42.017   4.214  60.716  1.00 40.61           O  
HETATM 5062  O   HOH B 574      34.437 -19.531  35.915  1.00 29.27           O  
HETATM 5063  O   HOH B 575      33.371  -4.602  48.409  1.00 14.20           O  
HETATM 5064  O   HOH B 576      33.118  -6.867  49.554  1.00 33.60           O  
HETATM 5065  O   HOH B 577      35.342  -9.383  36.473  1.00 17.04           O  
HETATM 5066  O   HOH B 578      31.239  -1.060  43.060  1.00 29.59           O  
HETATM 5067  O   HOH B 579      31.617 -14.328  27.619  1.00 32.76           O  
HETATM 5068  O   HOH B 580      24.706 -25.497  43.212  1.00 20.56           O  
HETATM 5069  O   HOH B 581      19.181 -30.281  44.852  1.00 35.59           O  
HETATM 5070  O   HOH B 582      16.477 -12.755  36.485  1.00 33.86           O  
HETATM 5071  O   HOH B 583      32.838  -8.786  32.305  1.00 21.15           O  
HETATM 5072  O   HOH B 584      36.843 -15.426  31.779  1.00 27.24           O  
HETATM 5073  O   HOH B 585      38.869 -28.925  42.070  1.00 41.06           O  
HETATM 5074  O   HOH B 586      42.386  20.291  46.607  1.00 35.58           O  
HETATM 5075  O   HOH B 587      30.720  13.652  31.166  1.00 45.44           O  
HETATM 5076  O   HOH B 588      36.450  -6.614  45.522  1.00 23.33           O  
HETATM 5077  O   HOH B 589      34.143  -1.614  26.500  1.00 43.77           O  
HETATM 5078  O   HOH B 590      36.027   6.456  26.214  1.00 52.64           O  
HETATM 5079  O   HOH B 591      35.239 -12.339  61.040  1.00 40.49           O  
HETATM 5080  O   HOH B 592      22.563  -6.178  44.349  1.00 32.76           O  
HETATM 5081  O   HOH B 593      37.276   7.587  63.736  1.00 33.97           O  
HETATM 5082  O   HOH B 594      42.932   8.520  55.876  1.00 22.55           O  
HETATM 5083  O   HOH B 595      43.708  -7.912  35.842  1.00 24.16           O  
HETATM 5084  O   HOH B 596      28.581  -2.391  56.729  1.00 17.48           O  
HETATM 5085  O   HOH B 597      38.051  -5.748  53.910  1.00 22.75           O  
HETATM 5086  O   HOH B 598      23.053  -6.828  41.430  1.00 18.61           O  
HETATM 5087  O   HOH B 599      28.263   9.957  46.669  1.00 19.83           O  
HETATM 5088  O   HOH B 600      48.508  11.239  42.923  1.00 25.19           O  
HETATM 5089  O   HOH B 601      29.630 -31.370  46.147  1.00 30.04           O  
HETATM 5090  O   HOH B 602      16.920  -2.084  47.260  1.00 21.67           O  
HETATM 5091  O   HOH B 603      18.451 -11.007  36.951  1.00 27.04           O  
HETATM 5092  O   HOH B 604      46.862   3.028  47.627  1.00 26.07           O  
HETATM 5093  O   HOH B 605      43.766   1.463  59.057  1.00 28.48           O  
HETATM 5094  O   HOH B 606      36.299  14.437  52.646  1.00 39.77           O  
HETATM 5095  O   HOH B 607      35.176  -2.942  28.521  1.00 22.89           O  
HETATM 5096  O   HOH B 608      27.251 -14.379  32.998  1.00 29.33           O  
HETATM 5097  O   HOH B 609      48.807   2.414  31.018  1.00 37.22           O  
HETATM 5098  O   HOH B 610      47.635  11.105  35.842  1.00 39.42           O  
HETATM 5099  O   HOH B 611      25.925  14.090  35.716  1.00 39.54           O  
HETATM 5100  O   HOH B 612      50.257   4.962  32.497  1.00 47.23           O  
HETATM 5101  O   HOH B 613      30.374  -8.695  33.491  1.00 14.38           O  
HETATM 5102  O   HOH B 614      43.146  16.011  37.087  1.00 30.90           O  
HETATM 5103  O   HOH B 615      22.305   0.117  44.461  1.00 24.53           O  
HETATM 5104  O   HOH B 616      27.884  12.234  44.807  1.00 33.75           O  
HETATM 5105  O   HOH B 617      41.483 -21.482  42.032  1.00 24.62           O  
HETATM 5106  O   HOH B 618      34.582  -5.976  51.850  1.00 36.16           O  
HETATM 5107  O   HOH B 619      43.632 -14.159  45.553  1.00 42.06           O  
HETATM 5108  O   HOH B 620      26.710   1.829  51.198  1.00 31.69           O  
HETATM 5109  O   HOH B 621      40.238 -15.159  40.160  1.00 23.34           O  
HETATM 5110  O   HOH B 622      34.448  12.438  51.293  1.00 30.92           O  
HETATM 5111  O   HOH B 623      38.300 -11.753  29.762  1.00 37.08           O  
HETATM 5112  O   HOH B 624      41.661 -12.044  36.888  1.00 32.94           O  
HETATM 5113  O   HOH B 625      34.137  15.418  59.217  1.00 24.48           O  
HETATM 5114  O   HOH B 626      34.271  13.816  61.548  1.00 17.44           O  
HETATM 5115  O   HOH B 627      32.757 -10.526  35.295  1.00 17.26           O  
HETATM 5116  O   HOH B 628      29.276  14.502  44.335  1.00 39.61           O  
HETATM 5117  O   HOH B 629      17.038  -0.902  50.763  1.00 17.60           O  
HETATM 5118  O   HOH B 630      47.545  -0.537  44.607  1.00 16.81           O  
HETATM 5119  O   HOH B 631      41.279  18.546  44.787  1.00 21.50           O  
HETATM 5120  O   HOH B 632      32.623 -20.055  33.677  1.00 27.79           O  
HETATM 5121  O   HOH B 633      12.490 -26.831  54.752  1.00 31.91           O  
HETATM 5122  O   HOH B 634      42.599 -16.707  45.176  1.00 42.13           O  
HETATM 5123  O   HOH B 635      29.758   3.791  55.771  1.00 22.90           O  
HETATM 5124  O   HOH B 636      23.953   0.442  47.458  1.00 15.92           O  
HETATM 5125  O   HOH B 637      18.137   0.770  29.298  1.00 46.09           O  
HETATM 5126  O   HOH B 638      22.978   5.257  38.908  1.00 53.58           O  
HETATM 5127  O   HOH B 639      43.696  17.964  41.929  1.00 32.65           O  
HETATM 5128  O   HOH B 640      28.803 -17.970  34.940  1.00 23.37           O  
HETATM 5129  O   HOH B 641      31.049 -29.227  52.404  1.00 48.11           O  
HETATM 5130  O   HOH B 642      11.616 -25.665  51.218  1.00 38.04           O  
HETATM 5131  O   HOH B 643      40.134 -21.411  38.874  1.00 28.77           O  
HETATM 5132  O   HOH B 644      17.641 -28.021  41.408  1.00 45.56           O  
HETATM 5133  O   HOH B 645      42.468  18.013  54.438  1.00 39.99           O  
HETATM 5134  O   HOH B 646      45.740  -2.806  49.550  1.00 14.26           O  
HETATM 5135  O   HOH B 647      35.600  -8.026  50.970  1.00 37.36           O  
HETATM 5136  O   HOH B 648      44.131   6.058  25.616  1.00 39.39           O  
HETATM 5137  O   HOH B 649      15.667  -1.112  35.874  1.00 54.28           O  
HETATM 5138  O   HOH B 650      24.889 -13.071  31.945  1.00 51.88           O  
HETATM 5139  O   HOH B 651      36.412  -8.891  62.241  1.00 46.76           O  
HETATM 5140  O   HOH B 652      44.372  15.688  39.695  1.00 34.52           O  
HETATM 5141  O   HOH B 653      51.741   9.923  42.601  1.00 28.74           O  
HETATM 5142  O   HOH B 654      46.749 -15.537  53.093  1.00 55.38           O  
HETATM 5143  O   HOH B 655      22.751 -11.403  33.148  1.00 35.85           O  
HETATM 5144  O   HOH B 656      31.951 -32.475  44.927  1.00 45.81           O  
HETATM 5145  O   HOH B 657      13.756  -4.627  47.989  1.00 43.06           O  
HETATM 5146  O   HOH B 658      48.248   0.971  48.748  1.00 34.89           O  
HETATM 5147  O   HOH B 659      15.629   0.504  49.074  1.00 33.45           O  
HETATM 5148  O   HOH B 660      35.670  11.460  67.569  1.00 26.21           O  
HETATM 5149  O   HOH B 661      42.439  -0.573  23.687  1.00 49.88           O  
HETATM 5150  O   HOH B 662      37.544  -5.618  48.575  1.00 37.08           O  
HETATM 5151  O   HOH B 663      52.509  -1.305  39.162  1.00 40.84           O  
HETATM 5152  O   HOH B 664      40.724 -14.476  36.153  1.00 51.67           O  
HETATM 5153  O   HOH B 665      41.822 -17.048  38.790  1.00 33.70           O  
HETATM 5154  O   HOH B 666      48.142   2.404  53.809  1.00 36.96           O  
HETATM 5155  O   HOH B 667      45.578  -5.245  55.321  1.00 36.64           O  
HETATM 5156  O   HOH B 668      49.053   4.851  52.390  1.00 37.85           O  
HETATM 5157  O   HOH B 669      39.985 -10.156  33.516  1.00 26.33           O  
HETATM 5158  O   HOH B 670      46.564   6.289  23.836  1.00 43.70           O  
HETATM 5159  O   HOH B 671      37.774 -17.391  36.771  1.00 36.83           O  
HETATM 5160  O   HOH B 672      35.246  -8.522  33.860  1.00 16.70           O  
HETATM 5161  O   HOH B 673      45.432   0.185  55.552  1.00 19.88           O  
HETATM 5162  O   HOH B 674      37.831  -7.068  51.704  1.00 31.84           O  
HETATM 5163  O   HOH B 675      47.905  -1.868  47.299  1.00 34.26           O  
HETATM 5164  O   HOH B 676      26.335   6.104  44.493  1.00 39.74           O  
HETATM 5165  O   HOH B 677      53.993   0.068  41.156  1.00 40.16           O  
HETATM 5166  O   HOH B 678      22.302   5.101  46.261  1.00 42.75           O  
HETATM 5167  O   HOH B 679      46.977  -0.656  51.125  1.00 22.55           O  
HETATM 5168  O   HOH B 680      50.649  12.381  43.745  1.00 37.91           O  
HETATM 5169  O   HOH B 681      52.195  -3.903  39.479  1.00 47.37           O  
HETATM 5170  O   HOH B 682      24.599   4.674  47.981  1.00 30.63           O  
HETATM 5171  O   HOH B 683      26.308   8.314  46.426  1.00 23.27           O  
HETATM 5172  O   HOH B 684      46.824  -2.270  55.918  1.00 37.64           O  
HETATM 5173  O   HOH C 101      25.954 -20.733  35.776  1.00 42.95           O  
HETATM 5174  O   HOH C 102      24.279 -27.943  44.425  1.00 24.75           O  
HETATM 5175  O   HOH C 103      25.937 -31.014  43.808  1.00 31.41           O  
HETATM 5176  O   HOH C 104      16.106 -19.896  34.553  1.00 57.15           O  
HETATM 5177  O   HOH C 105      17.889 -37.409  49.846  1.00 51.34           O  
HETATM 5178  O   HOH C 106      27.001 -23.346  36.567  1.00 37.84           O  
HETATM 5179  O   HOH C 107      22.433 -27.121  36.762  1.00 39.44           O  
HETATM 5180  O   HOH C 108      15.050 -12.481  33.717  1.00 44.87           O  
HETATM 5181  O   HOH C 109      17.793 -35.699  48.086  1.00 48.03           O  
CONECT 1110 1120                                                                
CONECT 1120 1110 1121                                                           
CONECT 1121 1120 1122 1129                                                      
CONECT 1122 1121 1123 1124                                                      
CONECT 1123 1122                                                                
CONECT 1124 1122 1125                                                           
CONECT 1125 1124 1126 1127 1128                                                 
CONECT 1126 1125                                                                
CONECT 1127 1125                                                                
CONECT 1128 1125                                                                
CONECT 1129 1121 1130 1131                                                      
CONECT 1130 1129                                                                
CONECT 1131 1129                                                                
CONECT 4778 4779 4780 4781 4782                                                 
CONECT 4779 4778                                                                
CONECT 4780 4778                                                                
CONECT 4781 4778                                                                
CONECT 4782 4778                                                                
MASTER      367    0    2   32   12    0    2    6 5160    3   18   51          
END

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Related entries of code: 6ath

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
1h27	RCSB PDB PDBbind	11aa, >1H27_3\|Chain... at 100%
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	6ath
Complex Type	Protein-Protein
PDBbind Subset	general set
Protein Name	Cdk2/cyclin A
Ligand Name	Cyclin-dependent kinase inhibitor 1B, p27-KID-deltaC
EC.Number	E.C.2.7.11.22
Resolution	1.82(Å)
Affinity (Kd/Ki/IC50)	Kd=0.33nM
Release Year	2018
Protein/NA Sequence	Check fasta file
Primary Reference	(2019) Nat Commun Vol. 10: pp. 1676-1676

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): P20248 P24941 P46527
Entrez Gene ID	NCBI Entrez Gene ID: 890 1017 1027
ASD	Information of known allosteric effects of PDB entries

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