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HEADER    DNA BINDING PROTEIN/DNA                 02-JAN-15   4S0N              
TITLE     CRYSTAL STRUCTURE OF HLTF HIRAN DOMAIN BOUND TO DNA                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HELICASE-LIKE TRANSCRIPTION FACTOR;                        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: HIRAN DOMAIN, UNP RESIDUES 55-180;                         
COMPND   5 SYNONYM: DNA-BINDING PROTEIN/PLASMINOGEN ACTIVATOR INHIBITOR 1       
COMPND   6 REGULATOR, HIP116, RING FINGER PROTEIN 80, SWI/SNF-RELATED MATRIX-   
COMPND   7 ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A MEMBER 
COMPND   8 3, SUCROSE NONFERMENTING PROTEIN 2-LIKE 3;                           
COMPND   9 EC: 3.6.4.-, 6.3.2.-;                                                
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: 5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*T)-3';                    
COMPND  13 CHAIN: E, F, G, H;                                                   
COMPND  14 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: HLTF, HIP116A, RNF80, SMARCA3, SNF2L3, ZBU1;                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630                                                
KEYWDS    ALPHA+BETA, DNA 3'-END BINDING, DNA BINDING PROTEIN-DNA COMPLEX       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.A.CHAVEZ,B.F.EICHMAN                                                
REVDAT   2   01-JUL-15 4S0N    1       JRNL                                     
REVDAT   1   27-MAY-15 4S0N    0                                                
JRNL        AUTH   A.C.KILE,D.A.CHAVEZ,J.BACAL,S.ELDIRANY,D.M.KORZHNEV,         
JRNL        AUTH 2 I.BEZSONOVA,B.F.EICHMAN,K.A.CIMPRICH                         
JRNL        TITL   HLTF'S ANCIENT HIRAN DOMAIN BINDS 3' DNA ENDS TO DRIVE       
JRNL        TITL 2 REPLICATION FORK REVERSAL.                                   
JRNL        REF    MOL.CELL                      V.  58  1090 2015              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   26051180                                                     
JRNL        DOI    10.1016/J.MOLCEL.2015.05.013                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1839)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MLHL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.72                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 86121                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.154                           
REMARK   3   R VALUE            (WORKING SET) : 0.153                           
REMARK   3   FREE R VALUE                     : 0.185                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4317                            
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 34.7304 -  4.0720    0.97     4049   233  0.1661 0.1754        
REMARK   3     2  4.0720 -  3.2328    1.00     4151   202  0.1481 0.1973        
REMARK   3     3  3.2328 -  2.8244    1.00     4128   213  0.1632 0.1702        
REMARK   3     4  2.8244 -  2.5663    1.00     4132   207  0.1659 0.1887        
REMARK   3     5  2.5663 -  2.3824    1.00     4106   214  0.1567 0.1992        
REMARK   3     6  2.3824 -  2.2419    1.00     4106   211  0.1477 0.1717        
REMARK   3     7  2.2419 -  2.1297    1.00     4079   209  0.1473 0.1787        
REMARK   3     8  2.1297 -  2.0370    1.00     4133   201  0.1375 0.1762        
REMARK   3     9  2.0370 -  1.9586    1.00     4082   200  0.1354 0.1874        
REMARK   3    10  1.9586 -  1.8910    1.00     4103   225  0.1415 0.1794        
REMARK   3    11  1.8910 -  1.8319    1.00     4097   214  0.1421 0.1897        
REMARK   3    12  1.8319 -  1.7795    1.00     4062   211  0.1423 0.1892        
REMARK   3    13  1.7795 -  1.7327    1.00     4074   250  0.1426 0.1816        
REMARK   3    14  1.7327 -  1.6904    1.00     4063   193  0.1388 0.1864        
REMARK   3    15  1.6904 -  1.6520    1.00     4085   226  0.1391 0.1927        
REMARK   3    16  1.6520 -  1.6168    1.00     4078   225  0.1390 0.1978        
REMARK   3    17  1.6168 -  1.5845    1.00     4074   232  0.1450 0.1961        
REMARK   3    18  1.5845 -  1.5546    1.00     4084   221  0.1426 0.1986        
REMARK   3    19  1.5546 -  1.5268    1.00     4072   209  0.1595 0.2172        
REMARK   3    20  1.5268 -  1.5010    0.99     4046   221  0.1831 0.2530        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.130            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.900           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.006           4475                                  
REMARK   3   ANGLE     :  0.973           6149                                  
REMARK   3   CHIRALITY :  0.039            671                                  
REMARK   3   PLANARITY :  0.005            753                                  
REMARK   3   DIHEDRAL  : 16.036           1717                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 4S0N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-15.                  
REMARK 100 THE RCSB ID CODE IS RCSB088030.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-OCT-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97872                            
REMARK 200  MONOCHROMATOR                  : C(111)                             
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   : 86121                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.45500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.91                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 4000, 250 MM SODIUM ACETATE      
REMARK 280  TRIHYDRATE, 100 MM TRIS-HCL PH 8.5, VAPOR DIFFUSION, SITTING        
REMARK 280  DROP, TEMPERATURE 289.15K                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       37.10550            
REMARK 290   SMTRY3   2  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: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11010 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 25110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H                
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    51                                                      
REMARK 465     PRO A    52                                                      
REMARK 465     GLY A    53                                                      
REMARK 465     SER A    54                                                      
REMARK 465     VAL A    55                                                      
REMARK 465     LEU A   178                                                      
REMARK 465     GLY A   179                                                      
REMARK 465     PHE A   180                                                      
REMARK 465     GLY B    51                                                      
REMARK 465     PRO B    52                                                      
REMARK 465     GLY B    53                                                      
REMARK 465     SER B    54                                                      
REMARK 465     VAL B    55                                                      
REMARK 465     PRO C   175                                                      
REMARK 465     LYS C   176                                                      
REMARK 465     THR C   177                                                      
REMARK 465     LEU C   178                                                      
REMARK 465     GLY C   179                                                      
REMARK 465     PHE C   180                                                      
REMARK 465     THR D   177                                                      
REMARK 465     LEU D   178                                                      
REMARK 465     GLY D   179                                                      
REMARK 465     PHE D   180                                                      
REMARK 465      DT E    11                                                      
REMARK 465      DT E    12                                                      
REMARK 465      DT E    13                                                      
REMARK 465      DT E    14                                                      
REMARK 465      DT F    11                                                      
REMARK 465      DT F    12                                                      
REMARK 465      DT F    13                                                      
REMARK 465      DT F    14                                                      
REMARK 465      DT F    15                                                      
REMARK 465      DT F    16                                                      
REMARK 465      DT G    11                                                      
REMARK 465      DT G    12                                                      
REMARK 465      DT G    13                                                      
REMARK 465      DT G    14                                                      
REMARK 465      DT G    15                                                      
REMARK 465      DT G    16                                                      
REMARK 465      DT H    11                                                      
REMARK 465      DT H    12                                                      
REMARK 465      DT H    13                                                      
REMARK 465      DT H    14                                                      
REMARK 465      DT H    15                                                      
REMARK 465      DT H    16                                                      
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      DT E   5    O5'  N1   C2   O2   N3   C4   O4                    
REMARK 470      DT E   5    C5   C7   C6                                        
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    ASP B  94      107.20   -162.66                                   
REMARK 500    ASP C  94      111.18   -163.02                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 430        DISTANCE =  7.37 ANGSTROMS                       
REMARK 525    HOH B 428        DISTANCE =  5.59 ANGSTROMS                       
REMARK 525    HOH G 103        DISTANCE =  6.01 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610      DT A  202                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 201  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR D  73   O                                                      
REMARK 620 2 LEU D  70   O    88.9                                              
REMARK 620 3 HOH D 311   O    91.0  92.3                                        
REMARK 620 4 HOH D 368   O    76.0  98.4 162.9                                  
REMARK 620 5 HOH D 317   O   165.5  96.3 102.3  89.9                            
REMARK 620 6 HOH D 319   O    92.9 172.1  79.9  89.5  83.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 201  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU C  70   O                                                      
REMARK 620 2 HOH C 302   O    93.3                                              
REMARK 620 3 HOH C 328   O    90.2 176.4                                        
REMARK 620 4 TYR C  73   O    84.2  94.3  87.2                                  
REMARK 620 5 HOH C 338   O    97.1 100.6  77.8 164.9                            
REMARK 620 6 HOH C 410   O   174.4  81.2  95.3  96.6  83.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 202  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 448   O                                                      
REMARK 620 2 TYR B  73   O    90.7                                              
REMARK 620 3 LEU B  70   O   102.4  82.6                                        
REMARK 620 4 HOH B 464   O   171.8  89.5  85.8                                  
REMARK 620 5 HOH B 367   O    92.5 102.2 164.4  79.4                            
REMARK 620 6 HOH B 403   O    73.3 158.1  86.3 108.5  93.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 204  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A  70   O                                                      
REMARK 620 2 TYR A  73   O    86.9                                              
REMARK 620 3 HOH A 342   O   172.2  96.0                                        
REMARK 620 4 HOH A 301   O    89.2  91.8  83.5                                  
REMARK 620 5 HOH A 366   O    91.4 163.1  87.9 105.1                            
REMARK 620 6 HOH A 377   O    98.1  82.6  89.4 170.5  81.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DT A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DT A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 204                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 201                  
DBREF  4S0N A   55   180  UNP    Q14527   HLTF_HUMAN      55    180             
DBREF  4S0N B   55   180  UNP    Q14527   HLTF_HUMAN      55    180             
DBREF  4S0N C   55   180  UNP    Q14527   HLTF_HUMAN      55    180             
DBREF  4S0N D   55   180  UNP    Q14527   HLTF_HUMAN      55    180             
DBREF  4S0N E    5    14  PDB    4S0N     4S0N             5     14             
DBREF  4S0N F    7    16  PDB    4S0N     4S0N             7     16             
DBREF  4S0N G    7    16  PDB    4S0N     4S0N             7     16             
DBREF  4S0N H    7    16  PDB    4S0N     4S0N             7     16             
SEQADV 4S0N GLY A   51  UNP  Q14527              EXPRESSION TAG                 
SEQADV 4S0N PRO A   52  UNP  Q14527              EXPRESSION TAG                 
SEQADV 4S0N GLY A   53  UNP  Q14527              EXPRESSION TAG                 
SEQADV 4S0N SER A   54  UNP  Q14527              EXPRESSION TAG                 
SEQADV 4S0N GLY B   51  UNP  Q14527              EXPRESSION TAG                 
SEQADV 4S0N PRO B   52  UNP  Q14527              EXPRESSION TAG                 
SEQADV 4S0N GLY B   53  UNP  Q14527              EXPRESSION TAG                 
SEQADV 4S0N SER B   54  UNP  Q14527              EXPRESSION TAG                 
SEQADV 4S0N GLY C   51  UNP  Q14527              EXPRESSION TAG                 
SEQADV 4S0N PRO C   52  UNP  Q14527              EXPRESSION TAG                 
SEQADV 4S0N GLY C   53  UNP  Q14527              EXPRESSION TAG                 
SEQADV 4S0N SER C   54  UNP  Q14527              EXPRESSION TAG                 
SEQADV 4S0N GLY D   51  UNP  Q14527              EXPRESSION TAG                 
SEQADV 4S0N PRO D   52  UNP  Q14527              EXPRESSION TAG                 
SEQADV 4S0N GLY D   53  UNP  Q14527              EXPRESSION TAG                 
SEQADV 4S0N SER D   54  UNP  Q14527              EXPRESSION TAG                 
SEQRES   1 A  130  GLY PRO GLY SER VAL ASP SER VAL LEU PHE GLY SER LEU          
SEQRES   2 A  130  ARG GLY HIS VAL VAL GLY LEU ARG TYR TYR THR GLY VAL          
SEQRES   3 A  130  VAL ASN ASN ASN GLU MET VAL ALA LEU GLN ARG ASP PRO          
SEQRES   4 A  130  ASN ASN PRO TYR ASP LYS ASN ALA ILE LYS VAL ASN ASN          
SEQRES   5 A  130  VAL ASN GLY ASN GLN VAL GLY HIS LEU LYS LYS GLU LEU          
SEQRES   6 A  130  ALA GLY ALA LEU ALA TYR ILE MET ASP ASN LYS LEU ALA          
SEQRES   7 A  130  GLN ILE GLU GLY VAL VAL PRO PHE GLY ALA ASN ASN ALA          
SEQRES   8 A  130  PHE THR MET PRO LEU HIS MET THR PHE TRP GLY LYS GLU          
SEQRES   9 A  130  GLU ASN ARG LYS ALA VAL SER ASP GLN LEU LYS LYS HIS          
SEQRES  10 A  130  GLY PHE LYS LEU GLY PRO ALA PRO LYS THR LEU GLY PHE          
SEQRES   1 B  130  GLY PRO GLY SER VAL ASP SER VAL LEU PHE GLY SER LEU          
SEQRES   2 B  130  ARG GLY HIS VAL VAL GLY LEU ARG TYR TYR THR GLY VAL          
SEQRES   3 B  130  VAL ASN ASN ASN GLU MET VAL ALA LEU GLN ARG ASP PRO          
SEQRES   4 B  130  ASN ASN PRO TYR ASP LYS ASN ALA ILE LYS VAL ASN ASN          
SEQRES   5 B  130  VAL ASN GLY ASN GLN VAL GLY HIS LEU LYS LYS GLU LEU          
SEQRES   6 B  130  ALA GLY ALA LEU ALA TYR ILE MET ASP ASN LYS LEU ALA          
SEQRES   7 B  130  GLN ILE GLU GLY VAL VAL PRO PHE GLY ALA ASN ASN ALA          
SEQRES   8 B  130  PHE THR MET PRO LEU HIS MET THR PHE TRP GLY LYS GLU          
SEQRES   9 B  130  GLU ASN ARG LYS ALA VAL SER ASP GLN LEU LYS LYS HIS          
SEQRES  10 B  130  GLY PHE LYS LEU GLY PRO ALA PRO LYS THR LEU GLY PHE          
SEQRES   1 C  130  GLY PRO GLY SER VAL ASP SER VAL LEU PHE GLY SER LEU          
SEQRES   2 C  130  ARG GLY HIS VAL VAL GLY LEU ARG TYR TYR THR GLY VAL          
SEQRES   3 C  130  VAL ASN ASN ASN GLU MET VAL ALA LEU GLN ARG ASP PRO          
SEQRES   4 C  130  ASN ASN PRO TYR ASP LYS ASN ALA ILE LYS VAL ASN ASN          
SEQRES   5 C  130  VAL ASN GLY ASN GLN VAL GLY HIS LEU LYS LYS GLU LEU          
SEQRES   6 C  130  ALA GLY ALA LEU ALA TYR ILE MET ASP ASN LYS LEU ALA          
SEQRES   7 C  130  GLN ILE GLU GLY VAL VAL PRO PHE GLY ALA ASN ASN ALA          
SEQRES   8 C  130  PHE THR MET PRO LEU HIS MET THR PHE TRP GLY LYS GLU          
SEQRES   9 C  130  GLU ASN ARG LYS ALA VAL SER ASP GLN LEU LYS LYS HIS          
SEQRES  10 C  130  GLY PHE LYS LEU GLY PRO ALA PRO LYS THR LEU GLY PHE          
SEQRES   1 D  130  GLY PRO GLY SER VAL ASP SER VAL LEU PHE GLY SER LEU          
SEQRES   2 D  130  ARG GLY HIS VAL VAL GLY LEU ARG TYR TYR THR GLY VAL          
SEQRES   3 D  130  VAL ASN ASN ASN GLU MET VAL ALA LEU GLN ARG ASP PRO          
SEQRES   4 D  130  ASN ASN PRO TYR ASP LYS ASN ALA ILE LYS VAL ASN ASN          
SEQRES   5 D  130  VAL ASN GLY ASN GLN VAL GLY HIS LEU LYS LYS GLU LEU          
SEQRES   6 D  130  ALA GLY ALA LEU ALA TYR ILE MET ASP ASN LYS LEU ALA          
SEQRES   7 D  130  GLN ILE GLU GLY VAL VAL PRO PHE GLY ALA ASN ASN ALA          
SEQRES   8 D  130  PHE THR MET PRO LEU HIS MET THR PHE TRP GLY LYS GLU          
SEQRES   9 D  130  GLU ASN ARG LYS ALA VAL SER ASP GLN LEU LYS LYS HIS          
SEQRES  10 D  130  GLY PHE LYS LEU GLY PRO ALA PRO LYS THR LEU GLY PHE          
SEQRES   1 E   10   DT  DT  DT  DT  DT  DT  DT  DT  DT  DT                      
SEQRES   1 F   10   DT  DT  DT  DT  DT  DT  DT  DT  DT  DT                      
SEQRES   1 G   10   DT  DT  DT  DT  DT  DT  DT  DT  DT  DT                      
SEQRES   1 H   10   DT  DT  DT  DT  DT  DT  DT  DT  DT  DT                      
HET     DT  A 201      40                                                       
HET     DT  A 202       5                                                       
HET    GOL  A 203       6                                                       
HET     NA  A 204       1                                                       
HET    GOL  B 201       6                                                       
HET     NA  B 202       1                                                       
HET     NA  C 201       1                                                       
HET     NA  D 201       1                                                       
HETNAM      DT THYMIDINE-5'-MONOPHOSPHATE                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM      NA SODIUM ION                                                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   9   DT    2(C10 H15 N2 O8 P)                                           
FORMUL  10  GOL    2(C3 H8 O3)                                                  
FORMUL  11   NA    4(NA 1+)                                                     
FORMUL  16  HOH   *589(H2 O)                                                    
HELIX    1   1 GLY A   69  TYR A   73  5                                   5    
HELIX    2   2 LYS A  112  ASN A  125  1                                  14    
HELIX    3   3 LYS A  153  GLU A  155  5                                   3    
HELIX    4   4 ASN A  156  HIS A  167  1                                  12    
HELIX    5   5 GLY B   69  TYR B   73  5                                   5    
HELIX    6   6 LYS B  112  ASN B  125  1                                  14    
HELIX    7   7 LYS B  153  GLU B  155  5                                   3    
HELIX    8   8 ASN B  156  HIS B  167  1                                  12    
HELIX    9   9 GLY C   69  TYR C   73  5                                   5    
HELIX   10  10 LYS C  112  ASN C  125  1                                  14    
HELIX   11  11 LYS C  153  GLU C  155  5                                   3    
HELIX   12  12 ASN C  156  HIS C  167  1                                  12    
HELIX   13  13 LEU D   70  TYR D   73  5                                   4    
HELIX   14  14 LYS D  112  ASN D  125  1                                  14    
HELIX   15  15 LYS D  153  GLU D  155  5                                   3    
HELIX   16  16 ASN D  156  HIS D  167  1                                  12    
SHEET    1   A 7 VAL A  58  VAL A  68  0                                        
SHEET    2   A 7 GLN A 107  LEU A 111 -1  O  HIS A 110   N  VAL A  68           
SHEET    3   A 7 ILE A  98  ASN A 101 -1  N  VAL A 100   O  VAL A 108           
SHEET    4   A 7 GLU A  81  ARG A  87 -1  N  GLN A  86   O  LYS A  99           
SHEET    5   A 7 GLN A 129  VAL A 134 -1  O  VAL A 134   N  GLU A  81           
SHEET    6   A 7 MET A 144  GLY A 152 -1  O  TRP A 151   N  GLN A 129           
SHEET    7   A 7 VAL A  58  VAL A  68 -1  N  VAL A  58   O  GLY A 152           
SHEET    1   B 7 VAL B  58  VAL B  68  0                                        
SHEET    2   B 7 GLN B 107  LEU B 111 -1  O  HIS B 110   N  VAL B  68           
SHEET    3   B 7 ILE B  98  ASN B 101 -1  N  VAL B 100   O  VAL B 108           
SHEET    4   B 7 MET B  82  ARG B  87 -1  N  ALA B  84   O  ASN B 101           
SHEET    5   B 7 GLN B 129  VAL B 133 -1  O  GLY B 132   N  VAL B  83           
SHEET    6   B 7 MET B 144  GLY B 152 -1  O  TRP B 151   N  GLN B 129           
SHEET    7   B 7 VAL B  58  VAL B  68 -1  N  VAL B  58   O  GLY B 152           
SHEET    1   C 7 VAL C  58  VAL C  68  0                                        
SHEET    2   C 7 GLN C 107  LEU C 111 -1  O  HIS C 110   N  VAL C  68           
SHEET    3   C 7 ILE C  98  ASN C 101 -1  N  VAL C 100   O  VAL C 108           
SHEET    4   C 7 GLU C  81  ARG C  87 -1  N  GLN C  86   O  LYS C  99           
SHEET    5   C 7 GLN C 129  VAL C 134 -1  O  GLY C 132   N  VAL C  83           
SHEET    6   C 7 MET C 144  GLY C 152 -1  O  HIS C 147   N  VAL C 133           
SHEET    7   C 7 VAL C  58  VAL C  68 -1  N  PHE C  60   O  PHE C 150           
SHEET    1   D 7 VAL D  58  VAL D  68  0                                        
SHEET    2   D 7 GLN D 107  LEU D 111 -1  O  HIS D 110   N  VAL D  68           
SHEET    3   D 7 ILE D  98  ASN D 101 -1  N  VAL D 100   O  VAL D 108           
SHEET    4   D 7 GLU D  81  ARG D  87 -1  N  ALA D  84   O  ASN D 101           
SHEET    5   D 7 GLN D 129  VAL D 134 -1  O  VAL D 134   N  GLU D  81           
SHEET    6   D 7 THR D 143  GLY D 152 -1  O  HIS D 147   N  VAL D 133           
SHEET    7   D 7 VAL D  58  VAL D  68 -1  N  PHE D  60   O  PHE D 150           
LINK         O   TYR D  73                NA    NA D 201     1555   1555  2.31  
LINK         O   LEU C  70                NA    NA C 201     1555   1555  2.31  
LINK        NA    NA C 201                 O   HOH C 302     1555   1555  2.34  
LINK        NA    NA B 202                 O   HOH B 448     1555   1555  2.35  
LINK         O   LEU D  70                NA    NA D 201     1555   1555  2.35  
LINK         O   TYR B  73                NA    NA B 202     1555   1555  2.36  
LINK        NA    NA C 201                 O   HOH C 328     1555   1555  2.38  
LINK         O   LEU B  70                NA    NA B 202     1555   1555  2.39  
LINK         O   TYR C  73                NA    NA C 201     1555   1555  2.40  
LINK        NA    NA D 201                 O   HOH D 311     1555   1555  2.43  
LINK        NA    NA D 201                 O   HOH D 368     1555   1555  2.45  
LINK        NA    NA C 201                 O   HOH C 338     1555   1555  2.50  
LINK        NA    NA B 202                 O   HOH B 464     1555   1555  2.50  
LINK        NA    NA B 202                 O   HOH B 367     1555   1555  2.51  
LINK        NA    NA C 201                 O   HOH C 410     1555   1555  2.51  
LINK        NA    NA B 202                 O   HOH B 403     1555   1555  2.51  
LINK        NA    NA D 201                 O   HOH D 317     1555   1555  2.55  
LINK        NA    NA D 201                 O   HOH D 319     1555   1555  2.59  
LINK         O   LEU A  70                NA    NA A 204     1555   1555  2.32  
LINK         O   TYR A  73                NA    NA A 204     1555   1555  2.35  
LINK        NA    NA A 204                 O   HOH A 342     1555   1555  2.39  
LINK        NA    NA A 204                 O   HOH A 301     1555   1555  2.42  
LINK        NA    NA A 204                 O   HOH A 366     1555   1555  2.44  
LINK        NA    NA A 204                 O   HOH A 377     1555   1555  2.45  
LINK         O3'A DT A 201                 P    DT A 202     1555   1555  1.60  
LINK         O3'B DT A 201                 P    DT A 202     1555   1555  1.61  
SITE     1 AC1  7 GLN A  86  ARG A  87  ASP A  88  PRO A  89                    
SITE     2 AC1  7 ASN A  90  LYS A  99   DT A 202                               
SITE     1 AC2  1  DT A 201                                                     
SITE     1 AC3  8 SER A  62  ARG A  64  GLY A 172  PRO A 173                    
SITE     2 AC3  8 ALA A 174  HOH A 313  HOH A 333  HOH A 406                    
SITE     1 AC4  6 LEU A  70  TYR A  73  HOH A 301  HOH A 342                    
SITE     2 AC4  6 HOH A 366  HOH A 377                                          
SITE     1 AC5  8 SER B  62  ARG B  64  GLY B 172  PRO B 173                    
SITE     2 AC5  8 ALA B 174  HOH B 324  HOH B 360  HOH B 439                    
SITE     1 AC6  6 LEU B  70  TYR B  73  HOH B 367  HOH B 403                    
SITE     2 AC6  6 HOH B 448  HOH B 464                                          
SITE     1 AC7  6 LEU C  70  TYR C  73  HOH C 302  HOH C 328                    
SITE     2 AC7  6 HOH C 338  HOH C 410                                          
SITE     1 AC8  6 LEU D  70  TYR D  73  HOH D 311  HOH D 317                    
SITE     2 AC8  6 HOH D 319  HOH D 368                                          
CRYST1   61.026   74.211   66.180  90.00 113.68  90.00 P 1 21 1      8          
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      0.016386  0.000000  0.007186        0.00000                         
SCALE2      0.000000  0.013475  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016499        0.00000                         
ATOM      1  N   ASP A  56       3.973 -44.161 -40.688  1.00 58.44           N  
ANISOU    1  N   ASP A  56     8689   8029   5485    -17  -1013    283       N  
ATOM      2  CA  ASP A  56       4.617 -45.470 -40.687  1.00 57.40           C  
ANISOU    2  CA  ASP A  56     8695   7971   5143    -73   -812    352       C  
ATOM      3  C   ASP A  56       5.490 -45.679 -39.453  1.00 49.77           C  
ANISOU    3  C   ASP A  56     7712   6705   4493   -231   -805    499       C  
ATOM      4  O   ASP A  56       5.987 -46.783 -39.220  1.00 49.71           O  
ANISOU    4  O   ASP A  56     7636   6734   4518   -432   -927    192       O  
ATOM      5  CB  ASP A  56       5.463 -45.652 -41.951  1.00 63.77           C  
ANISOU    5  CB  ASP A  56     9547   9063   5620    -59   -528    336       C  
ATOM      6  CG  ASP A  56       4.620 -45.759 -43.209  1.00 70.24           C  
ANISOU    6  CG  ASP A  56    10329   9914   6445   -156     12    187       C  
ATOM      7  OD1 ASP A  56       3.454 -46.198 -43.108  1.00 71.35           O  
ANISOU    7  OD1 ASP A  56    10525  10070   6514   -278    -71    147       O  
ATOM      8  OD2 ASP A  56       5.124 -45.410 -44.298  1.00 73.14           O  
ANISOU    8  OD2 ASP A  56    10620  10269   6901    -77    480     85       O  
ATOM      9  N   SER A  57       5.675 -44.624 -38.661  1.00 41.67           N  
ANISOU    9  N   SER A  57     6671   5402   3759   -321   -476    904       N  
ATOM     10  CA ASER A  57       6.536 -44.692 -37.487  0.49 36.60           C  
ANISOU   10  CA ASER A  57     5987   4593   3328   -600   -113    898       C  
ATOM     11  CA BSER A  57       6.544 -44.704 -37.492  0.51 36.04           C  
ANISOU   11  CA BSER A  57     5898   4625   3173   -449   -560   1057       C  
ATOM     12  C   SER A  57       5.787 -45.203 -36.265  1.00 31.88           C  
ANISOU   12  C   SER A  57     5056   4019   3036   -486   -384    454       C  
ATOM     13  O   SER A  57       4.649 -44.805 -36.007  1.00 32.38           O  
ANISOU   13  O   SER A  57     4773   4054   3477   -187   -100    732       O  
ATOM     14  CB ASER A  57       7.146 -43.322 -37.188  0.49 38.13           C  
ANISOU   14  CB ASER A  57     6294   4564   3630   -745    827   1017       C  
ATOM     15  CB BSER A  57       7.188 -43.347 -37.193  0.51 36.93           C  
ANISOU   15  CB BSER A  57     6071   4689   3270   -318   -342   1473       C  
ATOM     16  OG ASER A  57       8.064 -42.952 -38.199  0.49 40.02           O  
ANISOU   16  OG ASER A  57     6569   4630   4005   -866   1526   1133       O  
ATOM     17  OG BSER A  57       6.456 -42.632 -36.215  0.51 38.03           O  
ANISOU   17  OG BSER A  57     6158   4819   3473   -226   -273   1742       O  
ATOM     18  N   VAL A  58       6.442 -46.080 -35.517  1.00 22.08           N  
ANISOU   18  N   VAL A  58     4048   2569   1772   -212   -535     57       N  
ATOM     19  CA  VAL A  58       5.869 -46.687 -34.326  1.00 18.77           C  
ANISOU   19  CA  VAL A  58     3242   1897   1994   -431   -371   -588       C  
ATOM     20  C   VAL A  58       6.746 -46.394 -33.113  1.00 14.62           C  
ANISOU   20  C   VAL A  58     2514   1501   1539   -317    -84    -73       C  
ATOM     21  O   VAL A  58       7.932 -46.077 -33.240  1.00 15.22           O  
ANISOU   21  O   VAL A  58     2481   1544   1760   -157     99     98       O  
ATOM     22  CB  VAL A  58       5.704 -48.211 -34.475  1.00 22.95           C  
ANISOU   22  CB  VAL A  58     3888   2350   2481   -402   -808   -564       C  
ATOM     23  CG1 VAL A  58       5.020 -48.546 -35.793  1.00 25.91           C  
ANISOU   23  CG1 VAL A  58     4634   2699   2511   -757   -907   -602       C  
ATOM     24  CG2 VAL A  58       7.034 -48.905 -34.383  1.00 24.22           C  
ANISOU   24  CG2 VAL A  58     3806   2201   3195     59   -288   -744       C  
ATOM     25  N   LEU A  59       6.162 -46.536 -31.930  1.00 15.32           N  
ANISOU   25  N   LEU A  59     2820   1877   1126    184    -13     84       N  
ATOM     26  CA  LEU A  59       6.865 -46.265 -30.687  1.00 14.83           C  
ANISOU   26  CA  LEU A  59     2665   1886   1083    -28    185    453       C  
ATOM     27  C   LEU A  59       7.865 -47.377 -30.353  1.00 14.16           C  
ANISOU   27  C   LEU A  59     2332   1317   1730    -45   -199    462       C  
ATOM     28  O   LEU A  59       7.495 -48.549 -30.282  1.00 16.94           O  
ANISOU   28  O   LEU A  59     2834   1375   2228   -117     41    321       O  
ATOM     29  CB  LEU A  59       5.853 -46.097 -29.553  1.00 15.81           C  
ANISOU   29  CB  LEU A  59     2576   1863   1570   -218    127   -125       C  
ATOM     30  CG  LEU A  59       6.443 -45.877 -28.163  1.00 16.36           C  
ANISOU   30  CG  LEU A  59     2585   1814   1817   -239    342    101       C  
ATOM     31  CD1 LEU A  59       7.254 -44.567 -28.095  1.00 16.24           C  
ANISOU   31  CD1 LEU A  59     2658   1464   2049   -306    229   -101       C  
ATOM     32  CD2 LEU A  59       5.326 -45.886 -27.116  1.00 19.67           C  
ANISOU   32  CD2 LEU A  59     2482   2549   2443   -260    810    -97       C  
ATOM     33  N   PHE A  60       9.132 -47.008 -30.143  1.00 13.72           N  
ANISOU   33  N   PHE A  60     1972   1411   1831    -61   -118      0       N  
ATOM     34  CA  PHE A  60      10.161 -47.975 -29.748  1.00 14.40           C  
ANISOU   34  CA  PHE A  60     2133   1544   1793    -69   -136     65       C  
ATOM     35  C   PHE A  60      10.417 -47.986 -28.242  1.00 14.54           C  
ANISOU   35  C   PHE A  60     2173   1508   1845     90    100   -103       C  
ATOM     36  O   PHE A  60      10.934 -48.966 -27.711  1.00 16.05           O  
ANISOU   36  O   PHE A  60     2274   1773   2053    268    124    101       O  
ATOM     37  CB  PHE A  60      11.495 -47.680 -30.441  1.00 14.43           C  
ANISOU   37  CB  PHE A  60     2006   1689   1788    131     37   -166       C  
ATOM     38  CG  PHE A  60      11.510 -47.909 -31.935  1.00 15.02           C  
ANISOU   38  CG  PHE A  60     2662   1582   1465    133   -220   -347       C  
ATOM     39  CD1 PHE A  60      10.554 -48.695 -32.578  1.00 15.75           C  
ANISOU   39  CD1 PHE A  60     3203   1402   1381    113   -188   -436       C  
ATOM     40  CD2 PHE A  60      12.532 -47.346 -32.698  1.00 18.43           C  
ANISOU   40  CD2 PHE A  60     2980   2168   1854    133    213     59       C  
ATOM     41  CE1 PHE A  60      10.615 -48.901 -33.969  1.00 16.78           C  
ANISOU   41  CE1 PHE A  60     2812   1390   2172    124   -136    -45       C  
ATOM     42  CE2 PHE A  60      12.597 -47.542 -34.076  1.00 18.94           C  
ANISOU   42  CE2 PHE A  60     2868   2358   1971    163     57    -40       C  
ATOM     43  CZ  PHE A  60      11.641 -48.331 -34.710  1.00 18.03           C  
ANISOU   43  CZ  PHE A  60     3021   1849   1981    -85   -362   -432       C  
ATOM     44  N   GLY A  61      10.092 -46.888 -27.560  1.00 14.65           N  
ANISOU   44  N   GLY A  61     2391   1513   1662    -96    261     -3       N  
ATOM     45  CA  GLY A  61      10.403 -46.743 -26.147  1.00 14.89           C  
ANISOU   45  CA  GLY A  61     2286   1549   1823   -267     -1   -254       C  
ATOM     46  C   GLY A  61      11.152 -45.467 -25.838  1.00 13.62           C  
ANISOU   46  C   GLY A  61     2202   1502   1472    -22   -151   -104       C  
ATOM     47  O   GLY A  61      11.278 -44.594 -26.709  1.00 15.47           O  
ANISOU   47  O   GLY A  61     2639   1637   1603     40     85    246       O  
ATOM     48  N   SER A  62      11.656 -45.363 -24.612  1.00 12.83           N  
ANISOU   48  N   SER A  62     1932   1322   1619   -235    -40     62       N  
ATOM     49  CA  SER A  62      12.305 -44.139 -24.158  1.00 12.18           C  
ANISOU   49  CA  SER A  62     1941   1356   1330   -118     26    242       C  
ATOM     50  C   SER A  62      13.639 -44.397 -23.467  1.00 12.76           C  
ANISOU   50  C   SER A  62     1909   1553   1386    -83    219    446       C  
ATOM     51  O   SER A  62      13.912 -45.516 -23.010  1.00 13.76           O  
ANISOU   51  O   SER A  62     2246   1131   1851     -5    168    337       O  
ATOM     52  CB  SER A  62      11.382 -43.367 -23.206  1.00 14.52           C  
ANISOU   52  CB  SER A  62     2393   1393   1729   -191    689    337       C  
ATOM     53  OG  SER A  62      11.133 -44.116 -22.023  1.00 15.14           O  
ANISOU   53  OG  SER A  62     2370   1476   1907   -162    393    325       O  
ATOM     54  N   LEU A  63      14.458 -43.351 -23.408  1.00 14.24           N  
ANISOU   54  N   LEU A  63     2001   1701   1710   -292    145    103       N  
ATOM     55  CA  LEU A  63      15.704 -43.319 -22.654  1.00 14.07           C  
ANISOU   55  CA  LEU A  63     1963   1763   1621   -374    191      2       C  
ATOM     56  C   LEU A  63      15.742 -42.039 -21.851  1.00 12.74           C  
ANISOU   56  C   LEU A  63     2061   1368   1413   -242   -150     17       C  
ATOM     57  O   LEU A  63      15.145 -41.034 -22.255  1.00 15.10           O  
ANISOU   57  O   LEU A  63     2321   1652   1763     46     48    451       O  
ATOM     58  CB  LEU A  63      16.944 -43.326 -23.553  1.00 17.03           C  
ANISOU   58  CB  LEU A  63     2297   2081   2094     58    560    617       C  
ATOM     59  CG  LEU A  63      17.350 -44.529 -24.372  1.00 20.89           C  
ANISOU   59  CG  LEU A  63     2941   2219   2776    386   1122    598       C  
ATOM     60  CD1 LEU A  63      18.651 -44.222 -25.100  1.00 19.84           C  
ANISOU   60  CD1 LEU A  63     2606   2433   2499    385    968    625       C  
ATOM     61  CD2 LEU A  63      17.477 -45.765 -23.480  1.00 21.42           C  
ANISOU   61  CD2 LEU A  63     3352   1935   2851    488    797   1184       C  
ATOM     62  N   ARG A  64      16.502 -42.048 -20.765  1.00 15.39           N  
ANISOU   62  N   ARG A  64     2374   1889   1584   -656   -140    -81       N  
ATOM     63  CA  ARG A  64      16.762 -40.819 -20.025  1.00 16.73           C  
ANISOU   63  CA  ARG A  64     2456   2246   1656   -566   -108    195       C  
ATOM     64  C   ARG A  64      18.246 -40.483 -20.036  1.00 18.62           C  
ANISOU   64  C   ARG A  64     2822   2013   2241   -386   -390    657       C  
ATOM     65  O   ARG A  64      19.098 -41.352 -20.195  1.00 19.88           O  
ANISOU   65  O   ARG A  64     2524   2007   3021   -467   -306    934       O  
ATOM     66  CB  ARG A  64      16.189 -40.931 -18.602  1.00 19.66           C  
ANISOU   66  CB  ARG A  64     3042   2600   1827   -615   -108    271       C  
ATOM     67  CG  ARG A  64      14.665 -40.780 -18.665  1.00 23.27           C  
ANISOU   67  CG  ARG A  64     3004   3194   2645   -669    423   -214       C  
ATOM     68  CD  ARG A  64      13.892 -40.909 -17.345  1.00 25.14           C  
ANISOU   68  CD  ARG A  64     2992   3101   3461    263    721   -114       C  
ATOM     69  NE  ARG A  64      12.476 -40.610 -17.597  1.00 27.89           N  
ANISOU   69  NE  ARG A  64     3697   3186   3716   -212   1117     16       N  
ATOM     70  CZ  ARG A  64      11.475 -40.810 -16.744  1.00 28.23           C  
ANISOU   70  CZ  ARG A  64     4255   3510   2962    212    485    -25       C  
ATOM     71  NH1 ARG A  64      11.696 -41.330 -15.541  1.00 31.36           N  
ANISOU   71  NH1 ARG A  64     4896   4382   2637     91    250    208       N  
ATOM     72  NH2 ARG A  64      10.240 -40.496 -17.105  1.00 29.56           N  
ANISOU   72  NH2 ARG A  64     4661   3423   3149    628   1102   -372       N  
ATOM     73  N   GLY A  65      18.548 -39.196 -19.923  1.00 18.91           N  
ANISOU   73  N   GLY A  65     2613   1688   2882   -356   -597    887       N  
ATOM     74  CA  GLY A  65      19.924 -38.741 -19.887  1.00 20.41           C  
ANISOU   74  CA  GLY A  65     2437   1768   3550   -570  -1018    891       C  
ATOM     75  C   GLY A  65      19.995 -37.325 -19.359  1.00 22.24           C  
ANISOU   75  C   GLY A  65     2866   1945   3637   -735   -883    867       C  
ATOM     76  O   GLY A  65      19.055 -36.844 -18.733  1.00 21.47           O  
ANISOU   76  O   GLY A  65     2912   1951   3293   -827   -922    875       O  
ATOM     77  N   HIS A  66      21.112 -36.658 -19.609  1.00 23.71           N  
ANISOU   77  N   HIS A  66     3247   1793   3969   -731  -1039    987       N  
ATOM     78  CA  HIS A  66      21.285 -35.278 -19.174  1.00 24.23           C  
ANISOU   78  CA  HIS A  66     3627   1915   3664  -1066   -685    939       C  
ATOM     79  C   HIS A  66      21.901 -34.437 -20.272  1.00 23.84           C  
ANISOU   79  C   HIS A  66     3331   1749   3980   -764    215    967       C  
ATOM     80  O   HIS A  66      22.759 -34.908 -21.023  1.00 29.81           O  
ANISOU   80  O   HIS A  66     3707   2015   5606   -348    756   1147       O  
ATOM     81  CB  HIS A  66      22.167 -35.199 -17.921  1.00 28.63           C  
ANISOU   81  CB  HIS A  66     4475   2512   3890  -1115  -1357    989       C  
ATOM     82  CG  HIS A  66      21.546 -35.808 -16.703  1.00 30.69           C  
ANISOU   82  CG  HIS A  66     4999   2957   3705   -931  -1458    435       C  
ATOM     83  ND1 HIS A  66      21.700 -37.138 -16.372  1.00 31.90           N  
ANISOU   83  ND1 HIS A  66     5069   2896   4155  -1037  -1146    317       N  
ATOM     84  CD2 HIS A  66      20.754 -35.270 -15.746  1.00 33.35           C  
ANISOU   84  CD2 HIS A  66     5487   3358   3828   -556  -1590    231       C  
ATOM     85  CE1 HIS A  66      21.038 -37.389 -15.255  1.00 33.12           C  
ANISOU   85  CE1 HIS A  66     5810   2914   3862   -338   -810     96       C  
ATOM     86  NE2 HIS A  66      20.453 -36.273 -14.858  1.00 32.86           N  
ANISOU   86  NE2 HIS A  66     5672   3364   3451    -43  -1612    592       N  
ATOM     87  N   VAL A  67      21.461 -33.189 -20.358  1.00 18.13           N  
ANISOU   87  N   VAL A  67     2712   1574   2602   -690   -550    711       N  
ATOM     88  CA  VAL A  67      22.129 -32.212 -21.209  1.00 17.07           C  
ANISOU   88  CA  VAL A  67     2686   1386   2415   -518   -213    490       C  
ATOM     89  C   VAL A  67      23.286 -31.627 -20.416  1.00 17.67           C  
ANISOU   89  C   VAL A  67     2900   1633   2178   -369   -142    224       C  
ATOM     90  O   VAL A  67      23.115 -31.260 -19.252  1.00 18.99           O  
ANISOU   90  O   VAL A  67     3112   2089   2014   -722    159    294       O  
ATOM     91  CB  VAL A  67      21.174 -31.100 -21.650  1.00 17.27           C  
ANISOU   91  CB  VAL A  67     2726   1673   2164   -342     63    516       C  
ATOM     92  CG1 VAL A  67      21.845 -30.166 -22.685  1.00 17.47           C  
ANISOU   92  CG1 VAL A  67     2792   1738   2106   -292    304    641       C  
ATOM     93  CG2 VAL A  67      19.878 -31.707 -22.185  1.00 20.03           C  
ANISOU   93  CG2 VAL A  67     2652   2296   2664   -556    142    619       C  
ATOM     94  N   VAL A  68      24.462 -31.540 -21.031  1.00 16.65           N  
ANISOU   94  N   VAL A  68     2571   1607   2149   -213   -149    343       N  
ATOM     95  CA  VAL A  68      25.640 -31.041 -20.332  1.00 16.09           C  
ANISOU   95  CA  VAL A  68     2321   1544   2249   -254   -226    374       C  
ATOM     96  C   VAL A  68      26.277 -29.871 -21.074  1.00 15.57           C  
ANISOU   96  C   VAL A  68     2337   1674   1907   -418   -124    228       C  
ATOM     97  O   VAL A  68      25.837 -29.510 -22.171  1.00 16.00           O  
ANISOU   97  O   VAL A  68     2651   1605   1825   -268   -124    330       O  
ATOM     98  CB  VAL A  68      26.687 -32.160 -20.136  1.00 16.81           C  
ANISOU   98  CB  VAL A  68     2616   1639   2132   -167    -68    758       C  
ATOM     99  CG1 VAL A  68      26.097 -33.261 -19.289  1.00 19.38           C  
ANISOU   99  CG1 VAL A  68     3300   1729   2334   -123     47    940       C  
ATOM    100  CG2 VAL A  68      27.149 -32.713 -21.494  1.00 19.55           C  
ANISOU  100  CG2 VAL A  68     2969   1702   2758     18    413    591       C  
ATOM    101  N   GLY A  69      27.296 -29.273 -20.465  1.00 16.69           N  
ANISOU  101  N   GLY A  69     2581   1618   2141   -635   -128    333       N  
ATOM    102  CA  GLY A  69      27.944 -28.100 -21.030  1.00 17.44           C  
ANISOU  102  CA  GLY A  69     2804   1506   2316   -300   -208    746       C  
ATOM    103  C   GLY A  69      27.084 -26.848 -21.011  1.00 16.81           C  
ANISOU  103  C   GLY A  69     2759   1759   1870   -277   -341    548       C  
ATOM    104  O   GLY A  69      27.328 -25.930 -21.793  1.00 17.53           O  
ANISOU  104  O   GLY A  69     2912   1808   1942   -428   -172    518       O  
ATOM    105  N   LEU A  70      26.094 -26.794 -20.118  1.00 17.70           N  
ANISOU  105  N   LEU A  70     2818   1753   2156   -257     51    -92       N  
ATOM    106  CA  LEU A  70      25.169 -25.660 -20.066  1.00 17.30           C  
ANISOU  106  CA  LEU A  70     2572   1921   2081   -633    -73    -76       C  
ATOM    107  C   LEU A  70      25.863 -24.310 -19.931  1.00 17.95           C  
ANISOU  107  C   LEU A  70     2831   2087   1901   -670   -282    -14       C  
ATOM    108  O   LEU A  70      25.409 -23.317 -20.496  1.00 20.22           O  
ANISOU  108  O   LEU A  70     3286   1834   2564   -492   -178    433       O  
ATOM    109  CB  LEU A  70      24.180 -25.822 -18.903  1.00 18.54           C  
ANISOU  109  CB  LEU A  70     2803   1969   2271   -817    348   -157       C  
ATOM    110  CG  LEU A  70      23.358 -27.114 -18.881  1.00 21.18           C  
ANISOU  110  CG  LEU A  70     3309   2373   2364  -1058     55   -246       C  
ATOM    111  CD1 LEU A  70      22.449 -27.105 -17.662  1.00 21.86           C  
ANISOU  111  CD1 LEU A  70     3386   2108   2811   -408    478    184       C  
ATOM    112  CD2 LEU A  70      22.548 -27.306 -20.166  1.00 23.31           C  
ANISOU  112  CD2 LEU A  70     3639   3003   2217  -1315   -227     76       C  
ATOM    113  N   ARG A  71      26.963 -24.268 -19.192  1.00 19.38           N  
ANISOU  113  N   ARG A  71     3062   2343   1959   -955   -435     34       N  
ATOM    114  CA  ARG A  71      27.626 -22.994 -18.926  1.00 21.24           C  
ANISOU  114  CA  ARG A  71     3431   2287   2352  -1052   -348     52       C  
ATOM    115  C   ARG A  71      28.264 -22.388 -20.178  1.00 20.83           C  
ANISOU  115  C   ARG A  71     3323   2125   2467  -1013   -394    -50       C  
ATOM    116  O   ARG A  71      28.622 -21.213 -20.187  1.00 24.36           O  
ANISOU  116  O   ARG A  71     4183   2003   3067  -1093    -18   -218       O  
ATOM    117  CB  ARG A  71      28.689 -23.166 -17.840  1.00 26.99           C  
ANISOU  117  CB  ARG A  71     4305   2935   3016   -866   -945    143       C  
ATOM    118  CG  ARG A  71      29.914 -23.946 -18.292  1.00 30.56           C  
ANISOU  118  CG  ARG A  71     4928   3502   3183   -873  -1292    286       C  
ATOM    119  CD  ARG A  71      30.824 -24.275 -17.111  1.00 38.69           C  
ANISOU  119  CD  ARG A  71     6021   4559   4121  -1050   -901     12       C  
ATOM    120  NE  ARG A  71      31.389 -23.080 -16.500  1.00 48.72           N  
ANISOU  120  NE  ARG A  71     6940   5906   5665  -1033   -304    -35       N  
ATOM    121  CZ  ARG A  71      32.643 -22.674 -16.669  1.00 58.37           C  
ANISOU  121  CZ  ARG A  71     8020   7236   6921   -934    496   -141       C  
ATOM    122  NH1 ARG A  71      33.474 -23.376 -17.429  1.00 60.96           N  
ANISOU  122  NH1 ARG A  71     8330   7610   7222   -920    757   -132       N  
ATOM    123  NH2 ARG A  71      33.072 -21.569 -16.071  1.00 62.23           N  
ANISOU  123  NH2 ARG A  71     8408   7746   7492   -958    826   -205       N  
ATOM    124  N   TYR A  72      28.389 -23.175 -21.239  1.00 19.11           N  
ANISOU  124  N   TYR A  72     2912   2133   2216   -543   -368    476       N  
ATOM    125  CA  TYR A  72      29.040 -22.690 -22.449  1.00 19.63           C  
ANISOU  125  CA  TYR A  72     3013   1878   2566   -554     85    321       C  
ATOM    126  C   TYR A  72      28.065 -22.150 -23.507  1.00 18.17           C  
ANISOU  126  C   TYR A  72     2713   2013   2177   -491   -280    231       C  
ATOM    127  O   TYR A  72      28.510 -21.688 -24.565  1.00 22.18           O  
ANISOU  127  O   TYR A  72     3559   2272   2598   -830    121    572       O  
ATOM    128  CB  TYR A  72      29.909 -23.805 -23.047  1.00 19.27           C  
ANISOU  128  CB  TYR A  72     2835   2048   2439    -83   -334    594       C  
ATOM    129  CG  TYR A  72      30.888 -24.366 -22.041  1.00 19.77           C  
ANISOU  129  CG  TYR A  72     2980   1994   2538   -376   -553    526       C  
ATOM    130  CD1 TYR A  72      31.948 -23.592 -21.585  1.00 23.34           C  
ANISOU  130  CD1 TYR A  72     3023   2407   3437   -606   -455    617       C  
ATOM    131  CD2 TYR A  72      30.753 -25.663 -21.545  1.00 19.97           C  
ANISOU  131  CD2 TYR A  72     3231   1883   2475    292   -433    890       C  
ATOM    132  CE1 TYR A  72      32.837 -24.078 -20.660  1.00 22.89           C  
ANISOU  132  CE1 TYR A  72     3104   2345   3247   -346   -731    867       C  
ATOM    133  CE2 TYR A  72      31.646 -26.167 -20.611  1.00 21.84           C  
ANISOU  133  CE2 TYR A  72     3220   2320   2759   -133   -630    420       C  
ATOM    134  CZ  TYR A  72      32.689 -25.370 -20.177  1.00 23.64           C  
ANISOU  134  CZ  TYR A  72     3210   2490   3283   -380   -839    693       C  
ATOM    135  OH  TYR A  72      33.588 -25.851 -19.254  1.00 26.59           O  
ANISOU  135  OH  TYR A  72     3533   2866   3704   -310   -905    668       O  
ATOM    136  N   TYR A  73      26.760 -22.192 -23.221  1.00 17.58           N  
ANISOU  136  N   TYR A  73     2563   1645   2472   -231   -478    159       N  
ATOM    137  CA  TYR A  73      25.729 -21.760 -24.183  1.00 17.36           C  
ANISOU  137  CA  TYR A  73     2726   1482   2386   -246    -28    253       C  
ATOM    138  C   TYR A  73      24.721 -20.843 -23.501  1.00 18.25           C  
ANISOU  138  C   TYR A  73     2992   1420   2521    -14   -144    137       C  
ATOM    139  O   TYR A  73      24.683 -20.751 -22.274  1.00 20.14           O  
ANISOU  139  O   TYR A  73     3618   1828   2206   -102    122    312       O  
ATOM    140  CB  TYR A  73      25.039 -22.982 -24.835  1.00 17.97           C  
ANISOU  140  CB  TYR A  73     2976   1337   2515   -376     34    175       C  
ATOM    141  CG  TYR A  73      26.102 -23.889 -25.403  1.00 16.95           C  
ANISOU  141  CG  TYR A  73     2689   1503   2249   -258     25    454       C  
ATOM    142  CD1 TYR A  73      26.732 -23.570 -26.605  1.00 18.07           C  
ANISOU  142  CD1 TYR A  73     3018   1699   2147   -391     97    600       C  
ATOM    143  CD2 TYR A  73      26.558 -24.993 -24.684  1.00 16.73           C  
ANISOU  143  CD2 TYR A  73     2741   1326   2288   -374   -134     94       C  
ATOM    144  CE1 TYR A  73      27.749 -24.347 -27.104  1.00 18.81           C  
ANISOU  144  CE1 TYR A  73     3391   1749   2008   -413    217    375       C  
ATOM    145  CE2 TYR A  73      27.591 -25.786 -25.174  1.00 17.29           C  
ANISOU  145  CE2 TYR A  73     2971   1724   1874   -384    -96    119       C  
ATOM    146  CZ  TYR A  73      28.186 -25.447 -26.383  1.00 17.76           C  
ANISOU  146  CZ  TYR A  73     3341   1667   1738   -355    267     94       C  
ATOM    147  OH  TYR A  73      29.222 -26.197 -26.884  1.00 20.38           O  
ANISOU  147  OH  TYR A  73     3366   1858   2518   -182    258    137       O  
ATOM    148  N   THR A  74      23.912 -20.155 -24.291  1.00 18.71           N  
ANISOU  148  N   THR A  74     2866   1482   2763     44   -355    100       N  
ATOM    149  CA  THR A  74      23.002 -19.159 -23.730  1.00 19.29           C  
ANISOU  149  CA  THR A  74     3202   1390   2740   -314   -130    -65       C  
ATOM    150  C   THR A  74      21.534 -19.522 -23.881  1.00 17.66           C  
ANISOU  150  C   THR A  74     3161   1592   1957   -388   -203     34       C  
ATOM    151  O   THR A  74      20.664 -18.795 -23.398  1.00 20.26           O  
ANISOU  151  O   THR A  74     3517   1841   2341     15    595    278       O  
ATOM    152  CB  THR A  74      23.230 -17.780 -24.366  1.00 22.53           C  
ANISOU  152  CB  THR A  74     3500   1717   3344   -401    425    485       C  
ATOM    153  OG1 THR A  74      22.937 -17.840 -25.768  1.00 22.70           O  
ANISOU  153  OG1 THR A  74     3552   1841   3231   -186     90    578       O  
ATOM    154  CG2 THR A  74      24.669 -17.364 -24.168  1.00 23.84           C  
ANISOU  154  CG2 THR A  74     3518   1974   3566   -722    568    319       C  
ATOM    155  N   GLY A  75      21.245 -20.650 -24.528  1.00 16.82           N  
ANISOU  155  N   GLY A  75     2989   1631   1772   -335    120     56       N  
ATOM    156  CA  GLY A  75      19.859 -21.057 -24.689  1.00 18.49           C  
ANISOU  156  CA  GLY A  75     3149   1853   2025   -343    151    731       C  
ATOM    157  C   GLY A  75      19.192 -21.409 -23.367  1.00 18.23           C  
ANISOU  157  C   GLY A  75     3048   2099   1780   -258   -346    450       C  
ATOM    158  O   GLY A  75      19.772 -22.112 -22.542  1.00 20.31           O  
ANISOU  158  O   GLY A  75     3609   2325   1782    294   -209    602       O  
ATOM    159  N   VAL A  76      17.983 -20.901 -23.162  1.00 19.32           N  
ANISOU  159  N   VAL A  76     3241   2131   1971   -577    516    -52       N  
ATOM    160  CA AVAL A  76      17.224 -21.245 -21.962  0.52 18.64           C  
ANISOU  160  CA AVAL A  76     3120   2082   1882   -533    272     -8       C  
ATOM    161  CA BVAL A  76      17.184 -21.179 -21.970  0.48 19.29           C  
ANISOU  161  CA BVAL A  76     3445   2067   1816   -592    450   -160       C  
ATOM    162  C   VAL A  76      16.055 -22.173 -22.288  1.00 18.26           C  
ANISOU  162  C   VAL A  76     3503   1991   1445   -476    395    -19       C  
ATOM    163  O   VAL A  76      15.545 -22.196 -23.413  1.00 18.65           O  
ANISOU  163  O   VAL A  76     3436   2079   1571   -551    264     81       O  
ATOM    164  CB AVAL A  76      16.696 -19.989 -21.243  0.52 21.48           C  
ANISOU  164  CB AVAL A  76     3204   2502   2456   -560    394   -468       C  
ATOM    165  CB BVAL A  76      16.597 -19.858 -21.398  0.48 22.63           C  
ANISOU  165  CB BVAL A  76     4003   2456   2137   -629    721   -672       C  
ATOM    166  CG1AVAL A  76      17.857 -19.098 -20.831  0.52 23.60           C  
ANISOU  166  CG1AVAL A  76     3400   2732   2836   -550    629   -727       C  
ATOM    167  CG1BVAL A  76      15.642 -20.116 -20.243  0.48 23.31           C  
ANISOU  167  CG1BVAL A  76     3990   2426   2439   -517    964  -1162       C  
ATOM    168  CG2AVAL A  76      15.719 -19.237 -22.131  0.52 21.27           C  
ANISOU  168  CG2AVAL A  76     2928   2245   2909   -382    322   -414       C  
ATOM    169  CG2BVAL A  76      17.720 -18.925 -20.975  0.48 24.87           C  
ANISOU  169  CG2BVAL A  76     4362   2720   2368   -653    799   -631       C  
ATOM    170  N   VAL A  77      15.655 -22.970 -21.295  1.00 18.83           N  
ANISOU  170  N   VAL A  77     3444   1585   2125   -272    510    116       N  
ATOM    171  CA  VAL A  77      14.558 -23.924 -21.421  1.00 19.89           C  
ANISOU  171  CA  VAL A  77     3399   1721   2437   -211    892     24       C  
ATOM    172  C   VAL A  77      13.595 -23.738 -20.255  1.00 22.16           C  
ANISOU  172  C   VAL A  77     3753   2127   2541   -318   1192     18       C  
ATOM    173  O   VAL A  77      14.021 -23.399 -19.152  1.00 26.52           O  
ANISOU  173  O   VAL A  77     4217   3164   2695   -217    789    166       O  
ATOM    174  CB  VAL A  77      15.086 -25.391 -21.439  1.00 22.37           C  
ANISOU  174  CB  VAL A  77     3880   1738   2879   -618   1114   -120       C  
ATOM    175  CG1 VAL A  77      13.955 -26.408 -21.605  1.00 24.95           C  
ANISOU  175  CG1 VAL A  77     4333   2214   2931   -808   1435   -416       C  
ATOM    176  CG2 VAL A  77      16.102 -25.575 -22.547  1.00 24.59           C  
ANISOU  176  CG2 VAL A  77     4491   1831   3021   -141   1566    135       C  
ATOM    177  N   ASN A  78      12.304 -23.934 -20.510  1.00 22.81           N  
ANISOU  177  N   ASN A  78     3517   2152   2998   -804   1314    199       N  
ATOM    178  CA  ASN A  78      11.293 -23.994 -19.454  1.00 25.23           C  
ANISOU  178  CA  ASN A  78     3984   2345   3258   -474   1464    453       C  
ATOM    179  C   ASN A  78      11.053 -25.438 -19.032  1.00 24.90           C  
ANISOU  179  C   ASN A  78     3991   2802   2667   -749   1212    200       C  
ATOM    180  O   ASN A  78      11.317 -26.347 -19.798  1.00 24.27           O  
ANISOU  180  O   ASN A  78     4128   2658   2434   -417    966    394       O  
ATOM    181  CB  ASN A  78       9.971 -23.376 -19.933  1.00 31.02           C  
ANISOU  181  CB  ASN A  78     4921   2736   4128    205   1714    839       C  
ATOM    182  CG  ASN A  78      10.078 -21.888 -20.204  1.00 34.94           C  
ANISOU  182  CG  ASN A  78     6050   3033   4191    275   2558    566       C  
ATOM    183  OD1 ASN A  78      10.262 -21.098 -19.282  1.00 36.91           O  
ANISOU  183  OD1 ASN A  78     6810   3175   4039    126   2751   -281       O  
ATOM    184  ND2 ASN A  78       9.938 -21.494 -21.474  1.00 36.84           N  
ANISOU  184  ND2 ASN A  78     6446   3087   4466    495   3003    680       N  
ATOM    185  N   ASN A  79      10.534 -25.666 -17.832  1.00 26.88           N  
ANISOU  185  N   ASN A  79     4500   3040   2672  -1182   1191   -127       N  
ATOM    186  CA  ASN A  79      10.178 -27.037 -17.485  1.00 28.17           C  
ANISOU  186  CA  ASN A  79     4411   3617   2676  -1146   1221    226       C  
ATOM    187  C   ASN A  79       9.058 -27.536 -18.396  1.00 25.69           C  
ANISOU  187  C   ASN A  79     4001   3031   2730   -692   1080    295       C  
ATOM    188  O   ASN A  79       8.197 -26.759 -18.798  1.00 26.64           O  
ANISOU  188  O   ASN A  79     3936   2815   3371   -610    979    -79       O  
ATOM    189  CB  ASN A  79       9.779 -27.138 -16.016  1.00 34.61           C  
ANISOU  189  CB  ASN A  79     5149   5064   2937  -1484   1006    416       C  
ATOM    190  CG  ASN A  79      10.969 -26.997 -15.089  1.00 42.35           C  
ANISOU  190  CG  ASN A  79     6280   6261   3550  -1438   1417    198       C  
ATOM    191  OD1 ASN A  79      12.012 -27.621 -15.301  1.00 43.06           O  
ANISOU  191  OD1 ASN A  79     6662   6471   3229  -1845   1461    385       O  
ATOM    192  ND2 ASN A  79      10.829 -26.164 -14.066  1.00 47.49           N  
ANISOU  192  ND2 ASN A  79     6915   6741   4388  -1142   1381   -139       N  
ATOM    193  N   ASN A  80       9.106 -28.827 -18.735  1.00 24.01           N  
ANISOU  193  N   ASN A  80     3563   2644   2916   -459    998    413       N  
ATOM    194  CA  ASN A  80       8.122 -29.483 -19.600  1.00 24.89           C  
ANISOU  194  CA  ASN A  80     3450   3018   2991   -718    405   -106       C  
ATOM    195  C   ASN A  80       8.127 -28.966 -21.025  1.00 26.46           C  
ANISOU  195  C   ASN A  80     3683   3161   3209   -713    127    202       C  
ATOM    196  O   ASN A  80       7.106 -28.958 -21.705  1.00 30.88           O  
ANISOU  196  O   ASN A  80     4414   3504   3814   -868   -231   1154       O  
ATOM    197  CB  ASN A  80       6.715 -29.346 -19.024  1.00 32.94           C  
ANISOU  197  CB  ASN A  80     4016   3756   4742  -1005    775   -737       C  
ATOM    198  CG  ASN A  80       6.292 -30.567 -18.273  1.00 47.43           C  
ANISOU  198  CG  ASN A  80     6058   5480   6486   -740   1617  -1121       C  
ATOM    199  OD1 ASN A  80       5.873 -31.557 -18.868  1.00 52.01           O  
ANISOU  199  OD1 ASN A  80     6984   5915   6860  -1336   1503  -1764       O  
ATOM    200  ND2 ASN A  80       6.411 -30.518 -16.954  1.00 52.38           N  
ANISOU  200  ND2 ASN A  80     6714   6231   6956    -82   2032  -1145       N  
ATOM    201  N   GLU A  81       9.293 -28.560 -21.482  1.00 23.38           N  
ANISOU  201  N   GLU A  81     3401   2850   2632   -392    647   -162       N  
ATOM    202  CA  GLU A  81       9.427 -28.020 -22.818  1.00 21.12           C  
ANISOU  202  CA  GLU A  81     3512   2209   2304   -225    279     55       C  
ATOM    203  C   GLU A  81      10.167 -28.992 -23.712  1.00 16.93           C  
ANISOU  203  C   GLU A  81     2832   1689   1913    -51     31     18       C  
ATOM    204  O   GLU A  81      11.109 -29.635 -23.277  1.00 18.55           O  
ANISOU  204  O   GLU A  81     3109   1763   2175     82    251    288       O  
ATOM    205  CB  GLU A  81      10.171 -26.700 -22.766  1.00 25.28           C  
ANISOU  205  CB  GLU A  81     4409   2232   2963    -18    513     23       C  
ATOM    206  CG  GLU A  81       9.927 -25.800 -23.927  1.00 27.53           C  
ANISOU  206  CG  GLU A  81     4611   2353   3494   -163    474    379       C  
ATOM    207  CD  GLU A  81      10.373 -24.387 -23.617  1.00 28.35           C  
ANISOU  207  CD  GLU A  81     4506   2410   3854    389    707    390       C  
ATOM    208  OE1 GLU A  81      11.595 -24.170 -23.486  1.00 24.17           O  
ANISOU  208  OE1 GLU A  81     3421   2249   3514    233    -69    294       O  
ATOM    209  OE2 GLU A  81       9.503 -23.504 -23.472  1.00 36.11           O  
ANISOU  209  OE2 GLU A  81     5421   3382   4917    728   1366    992       O  
ATOM    210  N   MET A  82       9.757 -29.061 -24.971  1.00 16.75           N  
ANISOU  210  N   MET A  82     2673   1733   1959     55    411     80       N  
ATOM    211  CA  MET A  82      10.480 -29.828 -25.970  1.00 16.84           C  
ANISOU  211  CA  MET A  82     2457   1984   1956   -189    395    120       C  
ATOM    212  C   MET A  82      11.831 -29.185 -26.242  1.00 16.16           C  
ANISOU  212  C   MET A  82     2445   1598   2097    -30    236    754       C  
ATOM    213  O   MET A  82      11.971 -27.952 -26.182  1.00 16.96           O  
ANISOU  213  O   MET A  82     2697   1519   2229    184    467    481       O  
ATOM    214  CB  MET A  82       9.694 -29.889 -27.277  1.00 20.16           C  
ANISOU  214  CB  MET A  82     2869   2482   2308   -257    -10   -106       C  
ATOM    215  CG  MET A  82       8.334 -30.522 -27.162  1.00 27.01           C  
ANISOU  215  CG  MET A  82     3475   2609   4181    -89    255   -490       C  
ATOM    216  SD  MET A  82       8.504 -32.294 -27.112  1.00 34.05           S  
ANISOU  216  SD  MET A  82     4059   3141   5738   -572    442   -418       S  
ATOM    217  CE  MET A  82       6.785 -32.802 -27.123  1.00 35.28           C  
ANISOU  217  CE  MET A  82     3848   3557   5999   -392   -184   -914       C  
ATOM    218  N   VAL A  83      12.803 -30.024 -26.578  1.00 15.89           N  
ANISOU  218  N   VAL A  83     2270   1787   1982     36    340    295       N  
ATOM    219  CA  VAL A  83      14.075 -29.566 -27.092  1.00 15.79           C  
ANISOU  219  CA  VAL A  83     2521   1461   2018     50    386    291       C  
ATOM    220  C   VAL A  83      14.408 -30.353 -28.351  1.00 17.39           C  
ANISOU  220  C   VAL A  83     2835   1595   2177   -254    464     43       C  
ATOM    221  O   VAL A  83      13.879 -31.444 -28.564  1.00 21.70           O  
ANISOU  221  O   VAL A  83     3122   2126   2996   -540    744   -440       O  
ATOM    222  CB  VAL A  83      15.207 -29.702 -26.056  1.00 16.26           C  
ANISOU  222  CB  VAL A  83     2867   1144   2167    257    196    200       C  
ATOM    223  CG1 VAL A  83      14.975 -28.764 -24.886  1.00 17.48           C  
ANISOU  223  CG1 VAL A  83     3235   1330   2077    -22    670    -14       C  
ATOM    224  CG2 VAL A  83      15.346 -31.154 -25.576  1.00 17.97           C  
ANISOU  224  CG2 VAL A  83     2816   1411   2600    173     20    561       C  
ATOM    225  N   ALA A  84      15.272 -29.787 -29.190  1.00 15.88           N  
ANISOU  225  N   ALA A  84     2365   1956   1711     78    310     16       N  
ATOM    226  CA  ALA A  84      15.677 -30.438 -30.432  1.00 17.78           C  
ANISOU  226  CA  ALA A  84     2732   2171   1852    158    120    131       C  
ATOM    227  C   ALA A  84      17.074 -31.035 -30.321  1.00 16.54           C  
ANISOU  227  C   ALA A  84     2444   1986   1854    -15    -58   -167       C  
ATOM    228  O   ALA A  84      17.999 -30.396 -29.811  1.00 17.37           O  
ANISOU  228  O   ALA A  84     2196   1967   2437     35    -89   -176       O  
ATOM    229  CB  ALA A  84      15.615 -29.457 -31.588  1.00 20.67           C  
ANISOU  229  CB  ALA A  84     2840   2705   2309    329   -160    189       C  
ATOM    230  N   LEU A  85      17.221 -32.267 -30.794  1.00 18.83           N  
ANISOU  230  N   LEU A  85     2815   1738   2601    204    607    -45       N  
ATOM    231  CA  LEU A  85      18.539 -32.890 -30.916  1.00 16.81           C  
ANISOU  231  CA  LEU A  85     2725   1728   1936   -300     89    129       C  
ATOM    232  C   LEU A  85      19.058 -32.648 -32.322  1.00 15.54           C  
ANISOU  232  C   LEU A  85     2490   1861   1554   -230    238    292       C  
ATOM    233  O   LEU A  85      18.335 -32.875 -33.293  1.00 19.25           O  
ANISOU  233  O   LEU A  85     2772   2555   1986     34     15     76       O  
ATOM    234  CB  LEU A  85      18.476 -34.390 -30.641  1.00 18.78           C  
ANISOU  234  CB  LEU A  85     3417   1395   2325   -595   -277    363       C  
ATOM    235  CG  LEU A  85      17.883 -34.831 -29.306  1.00 26.33           C  
ANISOU  235  CG  LEU A  85     5070   2109   2826   -583     -2    603       C  
ATOM    236  CD1 LEU A  85      18.198 -36.305 -29.027  1.00 26.62           C  
ANISOU  236  CD1 LEU A  85     5223   1851   3041   -830    614    492       C  
ATOM    237  CD2 LEU A  85      18.339 -33.938 -28.189  1.00 29.03           C  
ANISOU  237  CD2 LEU A  85     5792   2792   2444   -131   -331    716       C  
ATOM    238  N   GLN A  86      20.297 -32.181 -32.430  1.00 15.86           N  
ANISOU  238  N   GLN A  86     2483   1614   1929   -191    428    301       N  
ATOM    239  CA  GLN A  86      20.866 -31.863 -33.735  1.00 16.37           C  
ANISOU  239  CA  GLN A  86     2692   1534   1993    236    346    630       C  
ATOM    240  C   GLN A  86      22.322 -32.306 -33.825  1.00 16.13           C  
ANISOU  240  C   GLN A  86     2271   1600   2256    -88    495   -108       C  
ATOM    241  O   GLN A  86      23.150 -31.881 -33.022  1.00 16.22           O  
ANISOU  241  O   GLN A  86     2401   1936   1827    -79    381     72       O  
ATOM    242  CB  GLN A  86      20.761 -30.362 -34.008  1.00 18.23           C  
ANISOU  242  CB  GLN A  86     3606   1634   1687    359    345    455       C  
ATOM    243  CG  GLN A  86      21.381 -29.938 -35.343  1.00 20.76           C  
ANISOU  243  CG  GLN A  86     4232   1808   1848    653    549    365       C  
ATOM    244  CD  GLN A  86      21.293 -28.441 -35.574  1.00 26.08           C  
ANISOU  244  CD  GLN A  86     5121   2430   2358   1089    836    781       C  
ATOM    245  OE1 GLN A  86      21.555 -27.652 -34.677  1.00 26.44           O  
ANISOU  245  OE1 GLN A  86     4997   2215   2835    442   1278    829       O  
ATOM    246  NE2 GLN A  86      20.918 -28.049 -36.779  1.00 33.28           N  
ANISOU  246  NE2 GLN A  86     6245   3299   3100   1388    887    896       N  
ATOM    247  N   ARG A  87      22.638 -33.157 -34.800  1.00 16.70           N  
ANISOU  247  N   ARG A  87     2759   1575   2013    269    813    242       N  
ATOM    248  CA  ARG A  87      24.001 -33.641 -34.944  1.00 16.15           C  
ANISOU  248  CA  ARG A  87     2691   1416   2027     43    868    -58       C  
ATOM    249  C   ARG A  87      24.982 -32.544 -35.324  1.00 16.22           C  
ANISOU  249  C   ARG A  87     2549   1635   1978   -252    569    171       C  
ATOM    250  O   ARG A  87      24.653 -31.631 -36.101  1.00 18.62           O  
ANISOU  250  O   ARG A  87     2873   1872   2330    -22    413    694       O  
ATOM    251  CB  ARG A  87      24.066 -34.760 -35.988  1.00 15.84           C  
ANISOU  251  CB  ARG A  87     2706   1468   1843     35    477    154       C  
ATOM    252  CG  ARG A  87      23.561 -36.077 -35.461  1.00 15.56           C  
ANISOU  252  CG  ARG A  87     2401   1361   2149   -139    421    174       C  
ATOM    253  CD  ARG A  87      24.661 -36.806 -34.707  1.00 15.77           C  
ANISOU  253  CD  ARG A  87     2451   1496   2047    547    493    290       C  
ATOM    254  NE  ARG A  87      25.648 -37.391 -35.618  1.00 16.37           N  
ANISOU  254  NE  ARG A  87     2195   1766   2258     79    821    242       N  
ATOM    255  CZ  ARG A  87      26.953 -37.128 -35.615  1.00 17.27           C  
ANISOU  255  CZ  ARG A  87     2774   1930   1859   -190    787    239       C  
ATOM    256  NH1 ARG A  87      27.481 -36.246 -34.762  1.00 17.71           N  
ANISOU  256  NH1 ARG A  87     2857   1829   2044   -206    475    270       N  
ATOM    257  NH2 ARG A  87      27.736 -37.746 -36.488  1.00 18.68           N  
ANISOU  257  NH2 ARG A  87     3043   1849   2206    232    558    159       N  
ATOM    258  N   ASP A  88      26.185 -32.643 -34.764  1.00 16.53           N  
ANISOU  258  N   ASP A  88     2381   1871   2028   -520    672    -15       N  
ATOM    259  CA  ASP A  88      27.301 -31.780 -35.145  1.00 17.22           C  
ANISOU  259  CA  ASP A  88     2333   2183   2025   -314    327    382       C  
ATOM    260  C   ASP A  88      28.484 -32.656 -35.559  1.00 18.15           C  
ANISOU  260  C   ASP A  88     2650   2255   1990   -233    661    440       C  
ATOM    261  O   ASP A  88      29.438 -32.825 -34.801  1.00 18.80           O  
ANISOU  261  O   ASP A  88     2435   2567   2141   -142    724    720       O  
ATOM    262  CB  ASP A  88      27.674 -30.842 -33.985  1.00 17.78           C  
ANISOU  262  CB  ASP A  88     2574   2111   2071   -641    335    483       C  
ATOM    263  CG  ASP A  88      28.864 -29.944 -34.304  1.00 20.66           C  
ANISOU  263  CG  ASP A  88     3141   2247   2461   -386    636    344       C  
ATOM    264  OD1 ASP A  88      29.192 -29.768 -35.501  1.00 22.33           O  
ANISOU  264  OD1 ASP A  88     3520   2529   2434   -326    545    526       O  
ATOM    265  OD2 ASP A  88      29.481 -29.421 -33.343  1.00 21.48           O  
ANISOU  265  OD2 ASP A  88     3191   2227   2742   -453    565    453       O  
ATOM    266  N   PRO A  89      28.416 -33.232 -36.771  1.00 18.69           N  
ANISOU  266  N   PRO A  89     2866   2282   1955   -273    779    532       N  
ATOM    267  CA  PRO A  89      29.416 -34.220 -37.195  1.00 22.15           C  
ANISOU  267  CA  PRO A  89     3181   2723   2513    -92    851    288       C  
ATOM    268  C   PRO A  89      30.819 -33.658 -37.383  1.00 22.91           C  
ANISOU  268  C   PRO A  89     3110   3134   2461     75    880    502       C  
ATOM    269  O   PRO A  89      31.774 -34.427 -37.395  1.00 24.74           O  
ANISOU  269  O   PRO A  89     3353   3334   2712    430    779    622       O  
ATOM    270  CB  PRO A  89      28.860 -34.724 -38.529  1.00 21.75           C  
ANISOU  270  CB  PRO A  89     3686   2620   1957    153    588    211       C  
ATOM    271  CG  PRO A  89      27.995 -33.612 -39.015  1.00 22.37           C  
ANISOU  271  CG  PRO A  89     3704   2630   2167     45    366   -129       C  
ATOM    272  CD  PRO A  89      27.348 -33.079 -37.771  1.00 19.83           C  
ANISOU  272  CD  PRO A  89     3205   2570   1761     26    556    188       C  
ATOM    273  N   ASN A  90      30.942 -32.341 -37.507  1.00 22.63           N  
ANISOU  273  N   ASN A  90     3067   3099   2433   -623   1115    515       N  
ATOM    274  CA  ASN A  90      32.247 -31.730 -37.711  1.00 24.05           C  
ANISOU  274  CA  ASN A  90     3234   3640   2263   -433   1038    746       C  
ATOM    275  C   ASN A  90      32.793 -31.064 -36.451  1.00 23.27           C  
ANISOU  275  C   ASN A  90     3121   3264   2455   -383   1028    759       C  
ATOM    276  O   ASN A  90      33.767 -30.315 -36.500  1.00 25.14           O  
ANISOU  276  O   ASN A  90     3065   3615   2872   -621    827    656       O  
ATOM    277  CB  ASN A  90      32.163 -30.734 -38.861  1.00 26.71           C  
ANISOU  277  CB  ASN A  90     3471   3980   2698   -774    794    813       C  
ATOM    278  CG  ASN A  90      31.877 -31.417 -40.172  1.00 33.07           C  
ANISOU  278  CG  ASN A  90     4540   4611   3415   -244    960    414       C  
ATOM    279  OD1 ASN A  90      32.572 -32.358 -40.549  1.00 37.49           O  
ANISOU  279  OD1 ASN A  90     5040   5350   3855     51   1500    205       O  
ATOM    280  ND2 ASN A  90      30.834 -30.975 -40.861  1.00 37.18           N  
ANISOU  280  ND2 ASN A  90     5269   5043   3816   -293    591    -91       N  
ATOM    281  N   ASN A  91      32.171 -31.382 -35.319  1.00 20.78           N  
ANISOU  281  N   ASN A  91     2787   2764   2346   -226    927    920       N  
ATOM    282  CA  ASN A  91      32.664 -30.954 -34.017  1.00 20.45           C  
ANISOU  282  CA  ASN A  91     2680   2780   2310   -182    670    635       C  
ATOM    283  C   ASN A  91      34.133 -31.333 -33.868  1.00 22.29           C  
ANISOU  283  C   ASN A  91     2719   2713   3038   -290    803    663       C  
ATOM    284  O   ASN A  91      34.486 -32.499 -34.030  1.00 25.87           O  
ANISOU  284  O   ASN A  91     3256   3003   3570     98    683    548       O  
ATOM    285  CB  ASN A  91      31.823 -31.595 -32.908  1.00 21.72           C  
ANISOU  285  CB  ASN A  91     3021   2936   2298   -636    562    741       C  
ATOM    286  CG  ASN A  91      32.169 -31.074 -31.525  1.00 22.21           C  
ANISOU  286  CG  ASN A  91     2848   2914   2677   -497    607    623       C  
ATOM    287  OD1 ASN A  91      33.248 -31.342 -30.992  1.00 24.97           O  
ANISOU  287  OD1 ASN A  91     3259   3252   2975   -300    793    314       O  
ATOM    288  ND2 ASN A  91      31.241 -30.353 -30.926  1.00 21.97           N  
ANISOU  288  ND2 ASN A  91     2628   2510   3210   -348    766    687       N  
ATOM    289  N   PRO A  92      34.998 -30.356 -33.568  1.00 21.66           N  
ANISOU  289  N   PRO A  92     2465   2629   3136   -279    505    844       N  
ATOM    290  CA  PRO A  92      36.432 -30.675 -33.538  1.00 25.05           C  
ANISOU  290  CA  PRO A  92     2391   2957   4170   -261    212    660       C  
ATOM    291  C   PRO A  92      36.858 -31.559 -32.365  1.00 25.95           C  
ANISOU  291  C   PRO A  92     2237   3486   4135   -615    197    630       C  
ATOM    292  O   PRO A  92      37.992 -32.032 -32.368  1.00 30.26           O  
ANISOU  292  O   PRO A  92     2402   4476   4620    -41    239    661       O  
ATOM    293  CB  PRO A  92      37.111 -29.295 -33.452  1.00 28.00           C  
ANISOU  293  CB  PRO A  92     2857   2933   4847   -625    902    447       C  
ATOM    294  CG  PRO A  92      36.055 -28.347 -33.037  1.00 27.89           C  
ANISOU  294  CG  PRO A  92     3135   2764   4698   -346    542    506       C  
ATOM    295  CD  PRO A  92      34.729 -28.913 -33.442  1.00 24.26           C  
ANISOU  295  CD  PRO A  92     2756   2520   3942   -577    589    618       C  
ATOM    296  N   TYR A  93      35.982 -31.794 -31.393  1.00 26.15           N  
ANISOU  296  N   TYR A  93     2927   3104   3906  -1024    379    666       N  
ATOM    297  CA  TYR A  93      36.363 -32.599 -30.233  1.00 29.20           C  
ANISOU  297  CA  TYR A  93     3553   3525   4018  -1074    129    741       C  
ATOM    298  C   TYR A  93      35.715 -33.973 -30.212  1.00 27.15           C  
ANISOU  298  C   TYR A  93     3111   3475   3729  -1140   -248    522       C  
ATOM    299  O   TYR A  93      36.226 -34.895 -29.570  1.00 29.68           O  
ANISOU  299  O   TYR A  93     3369   3691   4218   -779   -366    853       O  
ATOM    300  CB  TYR A  93      36.022 -31.857 -28.947  1.00 33.26           C  
ANISOU  300  CB  TYR A  93     4459   4082   4097  -1882   -121    629       C  
ATOM    301  CG  TYR A  93      36.711 -30.523 -28.867  1.00 38.42           C  
ANISOU  301  CG  TYR A  93     5548   4587   4461  -2615    370    344       C  
ATOM    302  CD1 TYR A  93      38.043 -30.434 -28.486  1.00 43.82           C  
ANISOU  302  CD1 TYR A  93     6417   5055   5178  -2745    695    503       C  
ATOM    303  CD2 TYR A  93      36.043 -29.356 -29.202  1.00 40.13           C  
ANISOU  303  CD2 TYR A  93     6048   4613   4588  -2388   1222    108       C  
ATOM    304  CE1 TYR A  93      38.686 -29.215 -28.424  1.00 45.60           C  
ANISOU  304  CE1 TYR A  93     6739   5051   5534  -2974    647     61       C  
ATOM    305  CE2 TYR A  93      36.680 -28.127 -29.142  1.00 41.83           C  
ANISOU  305  CE2 TYR A  93     6226   4699   4970  -2776   1278    195       C  
ATOM    306  CZ  TYR A  93      37.999 -28.066 -28.751  1.00 45.90           C  
ANISOU  306  CZ  TYR A  93     6765   5014   5661  -2840   1088    126       C  
ATOM    307  OH  TYR A  93      38.642 -26.851 -28.689  1.00 49.61           O  
ANISOU  307  OH  TYR A  93     7088   5312   6451  -2720   1069   -183       O  
ATOM    308  N   ASP A  94      34.596 -34.116 -30.911  1.00 22.47           N  
ANISOU  308  N   ASP A  94     2677   2982   2879  -1025   -144    626       N  
ATOM    309  CA  ASP A  94      33.853 -35.370 -30.899  1.00 20.99           C  
ANISOU  309  CA  ASP A  94     2442   2653   2880   -676    398    477       C  
ATOM    310  C   ASP A  94      32.967 -35.448 -32.134  1.00 20.13           C  
ANISOU  310  C   ASP A  94     2535   2426   2686   -400    255    388       C  
ATOM    311  O   ASP A  94      31.951 -34.758 -32.212  1.00 19.68           O  
ANISOU  311  O   ASP A  94     2529   2073   2877   -158    559    451       O  
ATOM    312  CB  ASP A  94      33.012 -35.479 -29.620  1.00 19.19           C  
ANISOU  312  CB  ASP A  94     2372   2295   2625   -216    154    507       C  
ATOM    313  CG  ASP A  94      32.220 -36.771 -29.540  1.00 20.26           C  
ANISOU  313  CG  ASP A  94     2460   2425   2814    -69    366    466       C  
ATOM    314  OD1 ASP A  94      32.397 -37.658 -30.406  1.00 20.47           O  
ANISOU  314  OD1 ASP A  94     2719   2320   2738   -138    659    419       O  
ATOM    315  OD2 ASP A  94      31.418 -36.905 -28.588  1.00 22.08           O  
ANISOU  315  OD2 ASP A  94     3082   2316   2992   -119   1008    284       O  
ATOM    316  N   LYS A  95      33.345 -36.298 -33.090  1.00 20.66           N  
ANISOU  316  N   LYS A  95     2514   2607   2730   -752    484     72       N  
ATOM    317  CA  LYS A  95      32.564 -36.449 -34.316  1.00 20.94           C  
ANISOU  317  CA  LYS A  95     2475   2741   2739   -408    762   -192       C  
ATOM    318  C   LYS A  95      31.132 -36.932 -34.066  1.00 19.20           C  
ANISOU  318  C   LYS A  95     2220   2491   2586   -462    948    207       C  
ATOM    319  O   LYS A  95      30.272 -36.766 -34.931  1.00 19.56           O  
ANISOU  319  O   LYS A  95     2271   2554   2605   -173    581    360       O  
ATOM    320  CB  LYS A  95      33.255 -37.413 -35.277  1.00 23.10           C  
ANISOU  320  CB  LYS A  95     2550   2925   3303   -372   1082   -309       C  
ATOM    321  CG  LYS A  95      33.290 -38.849 -34.791  1.00 31.44           C  
ANISOU  321  CG  LYS A  95     3836   3579   4531   -314   1458   -594       C  
ATOM    322  CD  LYS A  95      34.071 -39.741 -35.755  1.00 37.54           C  
ANISOU  322  CD  LYS A  95     4381   4220   5663   -349   1259   -347       C  
ATOM    323  CE  LYS A  95      33.962 -41.206 -35.366  1.00 45.48           C  
ANISOU  323  CE  LYS A  95     5720   4969   6592   -378   1336     74       C  
ATOM    324  NZ  LYS A  95      34.446 -41.456 -33.977  1.00 50.01           N  
ANISOU  324  NZ  LYS A  95     6394   5288   7318   -397   1340    372       N  
ATOM    325  N   ASN A  96      30.878 -37.519 -32.891  1.00 18.68           N  
ANISOU  325  N   ASN A  96     2243   2325   2531   -229   1118    380       N  
ATOM    326  CA  ASN A  96      29.548 -38.012 -32.542  1.00 17.89           C  
ANISOU  326  CA  ASN A  96     2429   1730   2637    118    719    577       C  
ATOM    327  C   ASN A  96      28.657 -36.958 -31.892  1.00 16.62           C  
ANISOU  327  C   ASN A  96     2330   1709   2274     37    669    -10       C  
ATOM    328  O   ASN A  96      27.535 -37.273 -31.497  1.00 16.75           O  
ANISOU  328  O   ASN A  96     2285   1934   2146   -149    534    489       O  
ATOM    329  CB  ASN A  96      29.649 -39.203 -31.578  1.00 19.82           C  
ANISOU  329  CB  ASN A  96     2458   1729   3343    534    740   1151       C  
ATOM    330  CG  ASN A  96      30.373 -40.370 -32.185  1.00 24.54           C  
ANISOU  330  CG  ASN A  96     2773   2558   3994    431    507   1458       C  
ATOM    331  OD1 ASN A  96      30.207 -40.665 -33.367  1.00 29.87           O  
ANISOU  331  OD1 ASN A  96     3231   3061   5055     -8   1510   1092       O  
ATOM    332  ND2 ASN A  96      31.183 -41.047 -31.380  1.00 26.75           N  
ANISOU  332  ND2 ASN A  96     3268   2715   4182     46   1063    704       N  
ATOM    333  N   ALA A  97      29.150 -35.723 -31.779  1.00 15.64           N  
ANISOU  333  N   ALA A  97     2345   1528   2069    -30    371    216       N  
ATOM    334  CA  ALA A  97      28.457 -34.703 -30.979  1.00 15.20           C  
ANISOU  334  CA  ALA A  97     2332   1486   1957   -342    352    121       C  
ATOM    335  C   ALA A  97      26.988 -34.521 -31.366  1.00 14.47           C  
ANISOU  335  C   ALA A  97     2169   1545   1784   -380    398    282       C  
ATOM    336  O   ALA A  97      26.633 -34.511 -32.550  1.00 15.69           O  
ANISOU  336  O   ALA A  97     2400   1802   1758     -3    464     98       O  
ATOM    337  CB  ALA A  97      29.173 -33.375 -31.083  1.00 16.71           C  
ANISOU  337  CB  ALA A  97     2813   1411   2125   -537    632    407       C  
ATOM    338  N   ILE A  98      26.138 -34.384 -30.355  1.00 14.61           N  
ANISOU  338  N   ILE A  98     2197   1356   1996   -173    551    215       N  
ATOM    339  CA  ILE A  98      24.738 -34.063 -30.575  1.00 14.13           C  
ANISOU  339  CA  ILE A  98     2134   1306   1930   -324    398     91       C  
ATOM    340  C   ILE A  98      24.398 -32.841 -29.740  1.00 14.26           C  
ANISOU  340  C   ILE A  98     2389   1320   1709   -129    442    358       C  
ATOM    341  O   ILE A  98      24.468 -32.875 -28.505  1.00 15.15           O  
ANISOU  341  O   ILE A  98     2581   1525   1652   -140    236    370       O  
ATOM    342  CB  ILE A  98      23.811 -35.251 -30.222  1.00 13.41           C  
ANISOU  342  CB  ILE A  98     2042   1201   1851    -47     70     45       C  
ATOM    343  CG1 ILE A  98      24.105 -36.421 -31.175  1.00 14.17           C  
ANISOU  343  CG1 ILE A  98     2596    880   1907   -283    499    135       C  
ATOM    344  CG2 ILE A  98      22.331 -34.830 -30.299  1.00 14.50           C  
ANISOU  344  CG2 ILE A  98     2156   1280   2073     28    -13    185       C  
ATOM    345  CD1 ILE A  98      23.450 -37.750 -30.784  1.00 15.66           C  
ANISOU  345  CD1 ILE A  98     2481   1407   2061   -360    321    304       C  
ATOM    346  N   LYS A  99      24.050 -31.757 -30.428  1.00 14.64           N  
ANISOU  346  N   LYS A  99     2451   1159   1954    -15    395    195       N  
ATOM    347  CA  LYS A  99      23.625 -30.523 -29.787  1.00 13.93           C  
ANISOU  347  CA  LYS A  99     2378   1344   1570   -385    259    339       C  
ATOM    348  C   LYS A  99      22.204 -30.656 -29.271  1.00 14.95           C  
ANISOU  348  C   LYS A  99     2324   1631   1725   -379    440    202       C  
ATOM    349  O   LYS A  99      21.382 -31.372 -29.850  1.00 16.35           O  
ANISOU  349  O   LYS A  99     2469   1619   2123   -252    196    115       O  
ATOM    350  CB  LYS A  99      23.712 -29.354 -30.776  1.00 15.54           C  
ANISOU  350  CB  LYS A  99     2830   1342   1734   -458    170    538       C  
ATOM    351  CG  LYS A  99      25.114 -29.207 -31.397  1.00 18.13           C  
ANISOU  351  CG  LYS A  99     3050   2091   1749   -469    375    929       C  
ATOM    352  CD  LYS A  99      25.270 -28.003 -32.317  1.00 23.78           C  
ANISOU  352  CD  LYS A  99     3784   2505   2745    316    496   1052       C  
ATOM    353  CE  LYS A  99      24.193 -27.920 -33.344  1.00 27.06           C  
ANISOU  353  CE  LYS A  99     4150   3110   3022      7    698   1361       C  
ATOM    354  NZ  LYS A  99      24.248 -26.622 -34.149  1.00 26.49           N  
ANISOU  354  NZ  LYS A  99     4153   3132   2780    -18    328   1725       N  
ATOM    355  N   VAL A 100      21.900 -29.938 -28.202  1.00 15.20           N  
ANISOU  355  N   VAL A 100     2356   1702   1718    -27    299    282       N  
ATOM    356  CA  VAL A 100      20.520 -29.805 -27.762  1.00 14.09           C  
ANISOU  356  CA  VAL A 100     2299   1446   1608    254   -157    601       C  
ATOM    357  C   VAL A 100      20.162 -28.335 -27.886  1.00 13.66           C  
ANISOU  357  C   VAL A 100     2200   1309   1682    338     -5    416       C  
ATOM    358  O   VAL A 100      20.832 -27.477 -27.288  1.00 16.36           O  
ANISOU  358  O   VAL A 100     2790   1685   1740    -94   -189    183       O  
ATOM    359  CB  VAL A 100      20.321 -30.287 -26.309  1.00 14.83           C  
ANISOU  359  CB  VAL A 100     2489   1431   1714    130    208    444       C  
ATOM    360  CG1 VAL A 100      18.873 -30.079 -25.860  1.00 16.16           C  
ANISOU  360  CG1 VAL A 100     1939   2128   2074      3    608    387       C  
ATOM    361  CG2 VAL A 100      20.742 -31.757 -26.182  1.00 16.47           C  
ANISOU  361  CG2 VAL A 100     3124   1237   1895    131    -99    687       C  
ATOM    362  N   ASN A 101      19.130 -28.056 -28.672  1.00 13.36           N  
ANISOU  362  N   ASN A 101     2232   1237   1608    538     94    544       N  
ATOM    363  CA  ASN A 101      18.659 -26.693 -28.920  1.00 14.05           C  
ANISOU  363  CA  ASN A 101     2414   1548   1378    207    288    575       C  
ATOM    364  C   ASN A 101      17.279 -26.479 -28.320  1.00 15.18           C  
ANISOU  364  C   ASN A 101     2494   1582   1690    232    434    356       C  
ATOM    365  O   ASN A 101      16.483 -27.418 -28.244  1.00 16.84           O  
ANISOU  365  O   ASN A 101     2723   1518   2159     43    272    159       O  
ATOM    366  CB  ASN A 101      18.571 -26.404 -30.413  1.00 16.75           C  
ANISOU  366  CB  ASN A 101     2703   1895   1766    178    554    368       C  
ATOM    367  CG  ASN A 101      19.891 -26.553 -31.126  1.00 16.18           C  
ANISOU  367  CG  ASN A 101     2773   1733   1644   -127    401    262       C  
ATOM    368  OD1 ASN A 101      20.942 -26.199 -30.600  1.00 17.93           O  
ANISOU  368  OD1 ASN A 101     2947   1910   1954   -222    486    238       O  
ATOM    369  ND2 ASN A 101      19.841 -27.077 -32.349  1.00 19.08           N  
ANISOU  369  ND2 ASN A 101     3660   2084   1504    206    138    105       N  
ATOM    370  N   ASN A 102      16.962 -25.248 -27.937  1.00 15.10           N  
ANISOU  370  N   ASN A 102     2419   1280   2038    288    327     -7       N  
ATOM    371  CA  ASN A 102      15.628 -24.988 -27.424  1.00 16.45           C  
ANISOU  371  CA  ASN A 102     2442   1454   2353    361     66    132       C  
ATOM    372  C   ASN A 102      14.651 -24.737 -28.583  1.00 18.59           C  
ANISOU  372  C   ASN A 102     2673   1799   2593     11    -67     52       C  
ATOM    373  O   ASN A 102      15.030 -24.819 -29.759  1.00 20.23           O  
ANISOU  373  O   ASN A 102     3322   1700   2665    276   -122     67       O  
ATOM    374  CB  ASN A 102      15.630 -23.827 -26.406  1.00 16.84           C  
ANISOU  374  CB  ASN A 102     2821   1107   2472     96    249    125       C  
ATOM    375  CG  ASN A 102      16.054 -22.477 -27.000  1.00 16.83           C  
ANISOU  375  CG  ASN A 102     2871   1404   2119    145    210    214       C  
ATOM    376  OD1 ASN A 102      16.000 -22.246 -28.213  1.00 16.87           O  
ANISOU  376  OD1 ASN A 102     3003   1585   1820    -61    285    476       O  
ATOM    377  ND2 ASN A 102      16.468 -21.571 -26.121  1.00 17.59           N  
ANISOU  377  ND2 ASN A 102     2966   1808   1910   -315    393     81       N  
ATOM    378  N   VAL A 103      13.395 -24.456 -28.252  1.00 19.35           N  
ANISOU  378  N   VAL A 103     2798   1997   2559    171    101     30       N  
ATOM    379  CA AVAL A 103      12.375 -24.324 -29.283  0.36 21.04           C  
ANISOU  379  CA AVAL A 103     2980   2318   2696    125     48    -76       C  
ATOM    380  CA BVAL A 103      12.341 -24.275 -29.241  0.64 21.36           C  
ANISOU  380  CA BVAL A 103     2884   2377   2856     70     26    142       C  
ATOM    381  C   VAL A 103      12.676 -23.142 -30.214  1.00 20.97           C  
ANISOU  381  C   VAL A 103     3039   2601   2328     68    -94   -316       C  
ATOM    382  O   VAL A 103      12.300 -23.173 -31.398  1.00 26.00           O  
ANISOU  382  O   VAL A 103     3870   3241   2767    331   -265   -479       O  
ATOM    383  CB AVAL A 103      10.961 -24.194 -28.657  0.36 23.14           C  
ANISOU  383  CB AVAL A 103     3296   2500   2996     26     10    186       C  
ATOM    384  CB BVAL A 103      10.988 -24.002 -28.540  0.64 23.98           C  
ANISOU  384  CB BVAL A 103     3130   2841   3140   -190   -237    891       C  
ATOM    385  CG1AVAL A 103      10.946 -23.145 -27.577  0.36 23.51           C  
ANISOU  385  CG1AVAL A 103     3371   2472   3089     45     73    236       C  
ATOM    386  CG1BVAL A 103       9.883 -23.751 -29.558  0.64 28.24           C  
ANISOU  386  CG1BVAL A 103     3532   3515   3684   -469    198    536       C  
ATOM    387  CG2AVAL A 103       9.899 -23.918 -29.720  0.36 25.35           C  
ANISOU  387  CG2AVAL A 103     3556   2808   3270    -79    159   -107       C  
ATOM    388  CG2BVAL A 103      10.628 -25.174 -27.611  0.64 24.43           C  
ANISOU  388  CG2BVAL A 103     3029   3134   3118   -172   -527   1183       C  
ATOM    389  N   ASN A 104      13.397 -22.133 -29.722  1.00 20.47           N  
ANISOU  389  N   ASN A 104     3167   2161   2451    411    -93    -41       N  
ATOM    390  CA AASN A 104      13.764 -21.003 -30.576  0.52 20.84           C  
ANISOU  390  CA AASN A 104     3561   2180   2178    647    118    264       C  
ATOM    391  CA BASN A 104      13.790 -20.993 -30.554  0.48 21.86           C  
ANISOU  391  CA BASN A 104     3601   2205   2500    721    255     79       C  
ATOM    392  C   ASN A 104      15.075 -21.195 -31.346  1.00 21.34           C  
ANISOU  392  C   ASN A 104     3643   2237   2227    780   -292     28       C  
ATOM    393  O   ASN A 104      15.509 -20.301 -32.077  1.00 23.33           O  
ANISOU  393  O   ASN A 104     4435   1810   2619    649    270    397       O  
ATOM    394  CB AASN A 104      13.843 -19.718 -29.750  0.52 22.15           C  
ANISOU  394  CB AASN A 104     3871   2475   2071   1032   -191    362       C  
ATOM    395  CB BASN A 104      13.950 -19.738 -29.700  0.48 24.74           C  
ANISOU  395  CB BASN A 104     3973   2446   2981   1156    487    -58       C  
ATOM    396  CG AASN A 104      12.475 -19.180 -29.383  0.52 25.05           C  
ANISOU  396  CG AASN A 104     4226   2789   2504   1454   -240    837       C  
ATOM    397  CG BASN A 104      12.648 -19.262 -29.123  0.48 28.62           C  
ANISOU  397  CG BASN A 104     4400   2789   3684   1362    975    107       C  
ATOM    398  OD1AASN A 104      11.723 -19.819 -28.636  0.52 26.36           O  
ANISOU  398  OD1AASN A 104     4333   2896   2787   1211    303    365       O  
ATOM    399  OD1BASN A 104      12.543 -19.029 -27.919  0.48 30.90           O  
ANISOU  399  OD1BASN A 104     4422   3222   4098   1471   1680   -291       O  
ATOM    400  ND2AASN A 104      12.142 -17.998 -29.900  0.52 28.55           N  
ANISOU  400  ND2AASN A 104     4687   3249   2910   1829    -70    937       N  
ATOM    401  ND2BASN A 104      11.635 -19.127 -29.975  0.48 28.54           N  
ANISOU  401  ND2BASN A 104     4718   2504   3623   1352    993    779       N  
ATOM    402  N   GLY A 105      15.699 -22.355 -31.199  1.00 19.61           N  
ANISOU  402  N   GLY A 105     3179   2280   1992    697   -189   -134       N  
ATOM    403  CA  GLY A 105      16.880 -22.657 -31.992  1.00 21.06           C  
ANISOU  403  CA  GLY A 105     3346   2444   2211    169    528    -18       C  
ATOM    404  C   GLY A 105      18.208 -22.286 -31.358  1.00 20.13           C  
ANISOU  404  C   GLY A 105     3120   2254   2274    216    399     29       C  
ATOM    405  O   GLY A 105      19.261 -22.500 -31.954  1.00 22.05           O  
ANISOU  405  O   GLY A 105     2976   2973   2430   -224    336   -340       O  
ATOM    406  N   ASN A 106      18.166 -21.701 -30.166  1.00 17.62           N  
ANISOU  406  N   ASN A 106     3149   1796   1751    -43     81    318       N  
ATOM    407  CA  ASN A 106      19.393 -21.368 -29.464  1.00 15.93           C  
ANISOU  407  CA  ASN A 106     2958   1205   1887   -217    -47     90       C  
ATOM    408  C   ASN A 106      19.926 -22.619 -28.749  1.00 16.12           C  
ANISOU  408  C   ASN A 106     2741   1248   2134    -82    127    531       C  
ATOM    409  O   ASN A 106      19.168 -23.353 -28.106  1.00 17.02           O  
ANISOU  409  O   ASN A 106     2687   1719   2061   -215    246    423       O  
ATOM    410  CB  ASN A 106      19.153 -20.224 -28.476  1.00 18.40           C  
ANISOU  410  CB  ASN A 106     3222   1562   2207      5    150    -79       C  
ATOM    411  CG  ASN A 106      20.449 -19.570 -28.004  1.00 19.62           C  
ANISOU  411  CG  ASN A 106     3552   1443   2460     65    152    485       C  
ATOM    412  OD1 ASN A 106      21.542 -19.941 -28.442  1.00 19.79           O  
ANISOU  412  OD1 ASN A 106     3635   1431   2451   -304    387    268       O  
ATOM    413  ND2 ASN A 106      20.328 -18.576 -27.121  1.00 19.49           N  
ANISOU  413  ND2 ASN A 106     3600   1462   2342    154    318    543       N  
ATOM    414  N   GLN A 107      21.224 -22.870 -28.866  1.00 16.40           N  
ANISOU  414  N   GLN A 107     2758   1483   1991    553    128    607       N  
ATOM    415  CA  GLN A 107      21.798 -24.059 -28.246  1.00 14.96           C  
ANISOU  415  CA  GLN A 107     2419   1661   1605    388    -20    500       C  
ATOM    416  C   GLN A 107      21.756 -23.976 -26.727  1.00 14.86           C  
ANISOU  416  C   GLN A 107     2825   1458   1363   -337     45    200       C  
ATOM    417  O   GLN A 107      22.039 -22.928 -26.142  1.00 16.35           O  
ANISOU  417  O   GLN A 107     2931   1329   1952   -174    -88    199       O  
ATOM    418  CB  GLN A 107      23.240 -24.285 -28.708  1.00 16.04           C  
ANISOU  418  CB  GLN A 107     1949   1749   2395    362    264    379       C  
ATOM    419  CG  GLN A 107      23.838 -25.570 -28.139  1.00 16.68           C  
ANISOU  419  CG  GLN A 107     2212   1723   2402    358    490    509       C  
ATOM    420  CD  GLN A 107      25.130 -25.979 -28.816  1.00 16.43           C  
ANISOU  420  CD  GLN A 107     2642   1621   1980     19    227    698       C  
ATOM    421  OE1 GLN A 107      25.655 -25.257 -29.667  1.00 19.04           O  
ANISOU  421  OE1 GLN A 107     3055   2031   2149    184    440    551       O  
ATOM    422  NE2 GLN A 107      25.645 -27.164 -28.447  1.00 17.05           N  
ANISOU  422  NE2 GLN A 107     2909   1441   2127   -225    129    600       N  
ATOM    423  N   VAL A 108      21.383 -25.091 -26.108  1.00 15.38           N  
ANISOU  423  N   VAL A 108     2926   1515   1402    -10    209    583       N  
ATOM    424  CA  VAL A 108      21.324 -25.230 -24.661  1.00 15.60           C  
ANISOU  424  CA  VAL A 108     2934   1577   1417   -112    360    649       C  
ATOM    425  C   VAL A 108      22.565 -25.948 -24.129  1.00 13.87           C  
ANISOU  425  C   VAL A 108     2515   1283   1473   -206    -80    144       C  
ATOM    426  O   VAL A 108      23.147 -25.558 -23.104  1.00 15.73           O  
ANISOU  426  O   VAL A 108     2789   1373   1814   -270   -112    237       O  
ATOM    427  CB  VAL A 108      20.058 -26.008 -24.255  1.00 16.57           C  
ANISOU  427  CB  VAL A 108     2973   1849   1474    -14    241    697       C  
ATOM    428  CG1 VAL A 108      20.021 -26.284 -22.749  1.00 17.00           C  
ANISOU  428  CG1 VAL A 108     3084   2100   1273   -116    -69    296       C  
ATOM    429  CG2 VAL A 108      18.805 -25.268 -24.753  1.00 18.45           C  
ANISOU  429  CG2 VAL A 108     2910   2319   1781    298   -348    332       C  
ATOM    430  N   GLY A 109      22.981 -26.991 -24.848  1.00 14.84           N  
ANISOU  430  N   GLY A 109     2866   1118   1654    146      9    277       N  
ATOM    431  CA  GLY A 109      24.137 -27.780 -24.464  1.00 14.78           C  
ANISOU  431  CA  GLY A 109     2627   1007   1982   -309     50    231       C  
ATOM    432  C   GLY A 109      24.373 -28.924 -25.427  1.00 14.61           C  
ANISOU  432  C   GLY A 109     2348   1291   1914   -105    128    219       C  
ATOM    433  O   GLY A 109      24.030 -28.824 -26.614  1.00 16.47           O  
ANISOU  433  O   GLY A 109     2788   1586   1883    -76     97    403       O  
ATOM    434  N   HIS A 110      24.986 -29.994 -24.920  1.00 14.42           N  
ANISOU  434  N   HIS A 110     2187   1116   2176   -221    155    247       N  
ATOM    435  CA  HIS A 110      25.246 -31.210 -25.687  1.00 14.75           C  
ANISOU  435  CA  HIS A 110     2410   1178   2016   -237    217    294       C  
ATOM    436  C   HIS A 110      24.735 -32.423 -24.935  1.00 15.85           C  
ANISOU  436  C   HIS A 110     2664   1172   2185   -197    326    527       C  
ATOM    437  O   HIS A 110      24.632 -32.390 -23.709  1.00 16.06           O  
ANISOU  437  O   HIS A 110     2823   1360   1920   -184    186    572       O  
ATOM    438  CB  HIS A 110      26.749 -31.410 -25.932  1.00 16.87           C  
ANISOU  438  CB  HIS A 110     2625   1632   2153   -172    551    488       C  
ATOM    439  CG  HIS A 110      27.321 -30.548 -27.013  1.00 16.00           C  
ANISOU  439  CG  HIS A 110     2703   1394   1980   -439    357    495       C  
ATOM    440  ND1 HIS A 110      28.096 -29.440 -26.750  1.00 18.63           N  
ANISOU  440  ND1 HIS A 110     2908   1616   2556   -770    545    455       N  
ATOM    441  CD2 HIS A 110      27.253 -30.647 -28.363  1.00 18.16           C  
ANISOU  441  CD2 HIS A 110     2771   2137   1993   -523    241    406       C  
ATOM    442  CE1 HIS A 110      28.476 -28.889 -27.892  1.00 17.91           C  
ANISOU  442  CE1 HIS A 110     2386   1943   2478   -406    383    336       C  
ATOM    443  NE2 HIS A 110      27.975 -29.601 -28.886  1.00 18.35           N  
ANISOU  443  NE2 HIS A 110     2193   2217   2562   -392    226    502       N  
ATOM    444  N   LEU A 111      24.445 -33.499 -25.656  1.00 14.39           N  
ANISOU  444  N   LEU A 111     2304   1060   2103    -95    -79    433       N  
ATOM    445  CA  LEU A 111      24.329 -34.785 -24.975  1.00 14.52           C  
ANISOU  445  CA  LEU A 111     2541   1148   1829     61    -72    506       C  
ATOM    446  C   LEU A 111      25.699 -35.216 -24.431  1.00 15.07           C  
ANISOU  446  C   LEU A 111     2422   1446   1856   -200    -43    501       C  
ATOM    447  O   LEU A 111      26.742 -34.887 -25.021  1.00 16.37           O  
ANISOU  447  O   LEU A 111     2490   1467   2264   -256    179    451       O  
ATOM    448  CB  LEU A 111      23.774 -35.864 -25.902  1.00 15.50           C  
ANISOU  448  CB  LEU A 111     2404   1590   1894   -108    112    213       C  
ATOM    449  CG  LEU A 111      22.375 -35.620 -26.465  1.00 14.59           C  
ANISOU  449  CG  LEU A 111     2015   1770   1760     -8    237    300       C  
ATOM    450  CD1 LEU A 111      21.892 -36.850 -27.217  1.00 15.81           C  
ANISOU  450  CD1 LEU A 111     2502   1408   2098   -375    266    -39       C  
ATOM    451  CD2 LEU A 111      21.401 -35.204 -25.366  1.00 16.52           C  
ANISOU  451  CD2 LEU A 111     2425   2212   1642    179    285    173       C  
ATOM    452  N   LYS A 112      25.705 -35.927 -23.303  1.00 15.68           N  
ANISOU  452  N   LYS A 112     2510   1720   1729   -263   -179    658       N  
ATOM    453  CA  LYS A 112      26.956 -36.493 -22.793  1.00 17.94           C  
ANISOU  453  CA  LYS A 112     2895   2282   1640   -119     19    849       C  
ATOM    454  C   LYS A 112      27.601 -37.336 -23.867  1.00 17.44           C  
ANISOU  454  C   LYS A 112     2415   2094   2117     68    -46    792       C  
ATOM    455  O   LYS A 112      26.899 -38.001 -24.631  1.00 17.58           O  
ANISOU  455  O   LYS A 112     2455   2058   2167     36   -129    563       O  
ATOM    456  CB  LYS A 112      26.719 -37.350 -21.553  1.00 22.28           C  
ANISOU  456  CB  LYS A 112     3812   2839   1814   -342    583    681       C  
ATOM    457  CG  LYS A 112      26.502 -36.548 -20.311  1.00 24.46           C  
ANISOU  457  CG  LYS A 112     4022   3424   1848   -376    703    465       C  
ATOM    458  CD  LYS A 112      26.403 -37.435 -19.103  1.00 25.43           C  
ANISOU  458  CD  LYS A 112     4273   3710   1682   -181    765    758       C  
ATOM    459  CE  LYS A 112      26.149 -36.612 -17.850  1.00 28.73           C  
ANISOU  459  CE  LYS A 112     4683   4146   2087   -236    269    761       C  
ATOM    460  NZ  LYS A 112      25.884 -37.487 -16.676  1.00 31.79           N  
ANISOU  460  NZ  LYS A 112     4813   4456   2809   -874     26    993       N  
ATOM    461  N   LYS A 113      28.929 -37.322 -23.922  1.00 17.59           N  
ANISOU  461  N   LYS A 113     2324   2030   2329    -73    227    794       N  
ATOM    462  CA  LYS A 113      29.625 -38.003 -25.007  1.00 17.08           C  
ANISOU  462  CA  LYS A 113     1976   2053   2462    -52    206    648       C  
ATOM    463  C   LYS A 113      29.281 -39.498 -25.074  1.00 16.35           C  
ANISOU  463  C   LYS A 113     2315   1826   2070   -173    515    780       C  
ATOM    464  O   LYS A 113      29.231 -40.067 -26.168  1.00 18.48           O  
ANISOU  464  O   LYS A 113     2537   2169   2316   -174    255    655       O  
ATOM    465  CB  LYS A 113      31.140 -37.806 -24.883  1.00 21.74           C  
ANISOU  465  CB  LYS A 113     2390   2879   2989   -466   -169    292       C  
ATOM    466  CG  LYS A 113      31.738 -38.197 -23.559  1.00 25.54           C  
ANISOU  466  CG  LYS A 113     2380   3612   3711   -645   -699    118       C  
ATOM    467  CD  LYS A 113      33.249 -38.004 -23.604  1.00 30.98           C  
ANISOU  467  CD  LYS A 113     2950   4477   4344   -594   -937   -211       C  
ATOM    468  CE  LYS A 113      33.906 -38.392 -22.288  1.00 35.07           C  
ANISOU  468  CE  LYS A 113     3689   5178   4457   -273   -937   -100       C  
ATOM    469  NZ  LYS A 113      33.628 -37.388 -21.218  1.00 38.22           N  
ANISOU  469  NZ  LYS A 113     4274   5278   4969    -14   -288    115       N  
ATOM    470  N   GLU A 114      29.034 -40.137 -23.927  1.00 15.89           N  
ANISOU  470  N   GLU A 114     1930   1883   2225    -40    382    467       N  
ATOM    471  CA  GLU A 114      28.734 -41.570 -23.937  1.00 15.85           C  
ANISOU  471  CA  GLU A 114     2290   1957   1775     78    220    566       C  
ATOM    472  C   GLU A 114      27.373 -41.835 -24.574  1.00 16.24           C  
ANISOU  472  C   GLU A 114     2170   1933   2066    223    372    241       C  
ATOM    473  O   GLU A 114      27.176 -42.849 -25.252  1.00 18.23           O  
ANISOU  473  O   GLU A 114     2307   2090   2528   -102    281    -21       O  
ATOM    474  CB  GLU A 114      28.765 -42.159 -22.521  1.00 16.53           C  
ANISOU  474  CB  GLU A 114     2356   2112   1812      5    -72    753       C  
ATOM    475  CG  GLU A 114      30.134 -42.117 -21.842  1.00 19.49           C  
ANISOU  475  CG  GLU A 114     2909   2199   2299     83   -323    603       C  
ATOM    476  CD  GLU A 114      30.349 -40.881 -20.981  1.00 22.62           C  
ANISOU  476  CD  GLU A 114     3352   2767   2476    332   -641    908       C  
ATOM    477  OE1 GLU A 114      29.756 -39.820 -21.274  1.00 21.87           O  
ANISOU  477  OE1 GLU A 114     3217   2591   2501     58   -194    876       O  
ATOM    478  OE2 GLU A 114      31.119 -40.973 -19.998  1.00 27.93           O  
ANISOU  478  OE2 GLU A 114     4006   3202   3404    144  -1127    703       O  
ATOM    479  N   LEU A 115      26.425 -40.937 -24.329  1.00 15.26           N  
ANISOU  479  N   LEU A 115     2016   1847   1934    180    324    556       N  
ATOM    480  CA  LEU A 115      25.113 -41.047 -24.941  1.00 14.85           C  
ANISOU  480  CA  LEU A 115     1789   1938   1915    268     30    603       C  
ATOM    481  C   LEU A 115      25.198 -40.722 -26.437  1.00 15.68           C  
ANISOU  481  C   LEU A 115     2347   1834   1775   -165    253    541       C  
ATOM    482  O   LEU A 115      24.644 -41.444 -27.264  1.00 15.10           O  
ANISOU  482  O   LEU A 115     1990   1960   1787   -173    283    308       O  
ATOM    483  CB  LEU A 115      24.113 -40.122 -24.243  1.00 15.35           C  
ANISOU  483  CB  LEU A 115     1633   1889   2309    479    301    496       C  
ATOM    484  CG  LEU A 115      22.690 -40.129 -24.806  1.00 15.89           C  
ANISOU  484  CG  LEU A 115     1869   1881   2288     87    357    522       C  
ATOM    485  CD1 LEU A 115      22.102 -41.548 -24.846  1.00 17.49           C  
ANISOU  485  CD1 LEU A 115     2110   2197   2340   -535    115    678       C  
ATOM    486  CD2 LEU A 115      21.781 -39.158 -24.029  1.00 18.45           C  
ANISOU  486  CD2 LEU A 115     2192   2549   2270    706    851    606       C  
ATOM    487  N   ALA A 116      25.903 -39.645 -26.787  1.00 14.90           N  
ANISOU  487  N   ALA A 116     2150   1762   1748    -36    413    966       N  
ATOM    488  CA  ALA A 116      26.076 -39.295 -28.199  1.00 16.10           C  
ANISOU  488  CA  ALA A 116     2564   1599   1955   -245    496    574       C  
ATOM    489  C   ALA A 116      26.773 -40.424 -28.963  1.00 14.79           C  
ANISOU  489  C   ALA A 116     2215   1662   1742   -129    194    541       C  
ATOM    490  O   ALA A 116      26.468 -40.687 -30.139  1.00 16.06           O  
ANISOU  490  O   ALA A 116     2339   1944   1818   -323    391    411       O  
ATOM    491  CB  ALA A 116      26.863 -37.992 -28.338  1.00 17.54           C  
ANISOU  491  CB  ALA A 116     2776   1518   2371   -188    750    601       C  
ATOM    492  N   GLY A 117      27.702 -41.095 -28.291  1.00 16.25           N  
ANISOU  492  N   GLY A 117     2082   1661   2432    233    735    560       N  
ATOM    493  CA  GLY A 117      28.410 -42.215 -28.886  1.00 16.51           C  
ANISOU  493  CA  GLY A 117     2057   1839   2378     85    372    231       C  
ATOM    494  C   GLY A 117      27.481 -43.328 -29.314  1.00 16.27           C  
ANISOU  494  C   GLY A 117     2305   1870   2008   -176    571    485       C  
ATOM    495  O   GLY A 117      27.763 -44.038 -30.287  1.00 19.83           O  
ANISOU  495  O   GLY A 117     2984   2406   2143    -33    723    379       O  
ATOM    496  N   ALA A 118      26.379 -43.492 -28.586  1.00 16.19           N  
ANISOU  496  N   ALA A 118     2244   1565   2344   -252    409    822       N  
ATOM    497  CA  ALA A 118      25.371 -44.486 -28.940  1.00 16.69           C  
ANISOU  497  CA  ALA A 118     2316   1628   2397   -115    419    422       C  
ATOM    498  C   ALA A 118      24.392 -43.965 -29.992  1.00 14.78           C  
ANISOU  498  C   ALA A 118     2204   1421   1992     63     15    282       C  
ATOM    499  O   ALA A 118      24.009 -44.703 -30.908  1.00 17.16           O  
ANISOU  499  O   ALA A 118     2562   1663   2297    165    439     75       O  
ATOM    500  CB  ALA A 118      24.610 -44.928 -27.703  1.00 19.00           C  
ANISOU  500  CB  ALA A 118     2214   2393   2614   -347    581    557       C  
ATOM    501  N   LEU A 119      23.979 -42.700 -29.876  1.00 14.63           N  
ANISOU  501  N   LEU A 119     2321   1248   1990     33    527    267       N  
ATOM    502  CA  LEU A 119      22.871 -42.216 -30.699  1.00 14.85           C  
ANISOU  502  CA  LEU A 119     2330   1670   1644     93    653    104       C  
ATOM    503  C   LEU A 119      23.267 -41.709 -32.085  1.00 14.36           C  
ANISOU  503  C   LEU A 119     1981   1639   1834     18    788    209       C  
ATOM    504  O   LEU A 119      22.417 -41.646 -32.975  1.00 15.85           O  
ANISOU  504  O   LEU A 119     2411   1774   1838    -62    277    -35       O  
ATOM    505  CB  LEU A 119      22.113 -41.095 -29.976  1.00 15.46           C  
ANISOU  505  CB  LEU A 119     2280   1727   1868     77    903     53       C  
ATOM    506  CG  LEU A 119      21.488 -41.455 -28.617  1.00 17.33           C  
ANISOU  506  CG  LEU A 119     2483   1796   2306    -74   1107     74       C  
ATOM    507  CD1 LEU A 119      20.560 -40.337 -28.163  1.00 16.90           C  
ANISOU  507  CD1 LEU A 119     2574   1633   2212    729    602   -169       C  
ATOM    508  CD2 LEU A 119      20.764 -42.802 -28.617  1.00 20.15           C  
ANISOU  508  CD2 LEU A 119     2809   2153   2694   -524   1327     43       C  
ATOM    509  N   ALA A 120      24.523 -41.322 -32.269  1.00 15.34           N  
ANISOU  509  N   ALA A 120     2274   1561   1993     -3    904    233       N  
ATOM    510  CA  ALA A 120      24.917 -40.685 -33.531  1.00 16.28           C  
ANISOU  510  CA  ALA A 120     2367   2030   1788   -437    621    248       C  
ATOM    511  C   ALA A 120      24.621 -41.588 -34.723  1.00 17.10           C  
ANISOU  511  C   ALA A 120     2585   1860   2050   -303    707    258       C  
ATOM    512  O   ALA A 120      24.113 -41.129 -35.746  1.00 18.41           O  
ANISOU  512  O   ALA A 120     2788   2179   2027    -37    645    406       O  
ATOM    513  CB  ALA A 120      26.402 -40.293 -33.506  1.00 17.48           C  
ANISOU  513  CB  ALA A 120     2363   2145   2136   -538    463    524       C  
ATOM    514  N   TYR A 121      24.911 -42.876 -34.578  1.00 16.86           N  
ANISOU  514  N   TYR A 121     2539   1766   2100   -213    752    -51       N  
ATOM    515  CA  TYR A 121      24.683 -43.829 -35.660  1.00 17.56           C  
ANISOU  515  CA  TYR A 121     2687   1615   2369    -74    711      6       C  
ATOM    516  C   TYR A 121      23.204 -43.901 -36.015  1.00 16.55           C  
ANISOU  516  C   TYR A 121     2705   1765   1817     11    719    235       C  
ATOM    517  O   TYR A 121      22.830 -44.002 -37.188  1.00 17.13           O  
ANISOU  517  O   TYR A 121     2549   2055   1905     49    750    106       O  
ATOM    518  CB  TYR A 121      25.202 -45.210 -35.255  1.00 18.89           C  
ANISOU  518  CB  TYR A 121     3104   1655   2420    375    804   -145       C  
ATOM    519  CG  TYR A 121      24.967 -46.301 -36.270  1.00 21.81           C  
ANISOU  519  CG  TYR A 121     3398   2103   2783    409    736   -404       C  
ATOM    520  CD1 TYR A 121      25.881 -46.530 -37.296  1.00 25.95           C  
ANISOU  520  CD1 TYR A 121     3956   2417   3488    426   1245   -949       C  
ATOM    521  CD2 TYR A 121      23.853 -47.123 -36.188  1.00 21.11           C  
ANISOU  521  CD2 TYR A 121     3320   2091   2608     71    148   -402       C  
ATOM    522  CE1 TYR A 121      25.676 -47.541 -38.220  1.00 27.61           C  
ANISOU  522  CE1 TYR A 121     4134   2628   3729    755   1343  -1022       C  
ATOM    523  CE2 TYR A 121      23.646 -48.144 -37.104  1.00 24.01           C  
ANISOU  523  CE2 TYR A 121     3803   2356   2964    488    564   -620       C  
ATOM    524  CZ  TYR A 121      24.554 -48.340 -38.121  1.00 27.74           C  
ANISOU  524  CZ  TYR A 121     4375   2654   3511    416   1150  -1028       C  
ATOM    525  OH  TYR A 121      24.353 -49.356 -39.038  1.00 31.37           O  
ANISOU  525  OH  TYR A 121     4981   3208   3729     94   1316   -985       O  
ATOM    526  N   ILE A 122      22.365 -43.860 -34.987  1.00 15.96           N  
ANISOU  526  N   ILE A 122     2555   1787   1721    212    516    169       N  
ATOM    527  CA  ILE A 122      20.928 -43.949 -35.163  1.00 16.09           C  
ANISOU  527  CA  ILE A 122     2575   1666   1873    120    830    299       C  
ATOM    528  C   ILE A 122      20.405 -42.723 -35.918  1.00 16.71           C  
ANISOU  528  C   ILE A 122     2756   1768   1823     21    631    -76       C  
ATOM    529  O   ILE A 122      19.606 -42.844 -36.851  1.00 17.52           O  
ANISOU  529  O   ILE A 122     2981   1851   1825   -174    334     29       O  
ATOM    530  CB  ILE A 122      20.238 -44.123 -33.798  1.00 14.65           C  
ANISOU  530  CB  ILE A 122     2162   1469   1936    212    638    298       C  
ATOM    531  CG1 ILE A 122      20.484 -45.558 -33.295  1.00 15.31           C  
ANISOU  531  CG1 ILE A 122     2631   1514   1673    153    278    235       C  
ATOM    532  CG2 ILE A 122      18.753 -43.841 -33.902  1.00 16.13           C  
ANISOU  532  CG2 ILE A 122     2377   1992   1759    108    566     98       C  
ATOM    533  CD1 ILE A 122      20.288 -45.744 -31.793  1.00 17.64           C  
ANISOU  533  CD1 ILE A 122     3101   1997   1604    203    559    146       C  
ATOM    534  N   MET A 123      20.881 -41.544 -35.536  1.00 16.55           N  
ANISOU  534  N   MET A 123     2835   1618   1837     19    678    174       N  
ATOM    535  CA  MET A 123      20.476 -40.318 -36.207  1.00 16.40           C  
ANISOU  535  CA  MET A 123     2924   1975   1330     37    370    122       C  
ATOM    536  C   MET A 123      21.022 -40.249 -37.635  1.00 16.80           C  
ANISOU  536  C   MET A 123     2692   2173   1518   -136    232     60       C  
ATOM    537  O   MET A 123      20.293 -39.919 -38.570  1.00 18.83           O  
ANISOU  537  O   MET A 123     3201   2206   1749    -81    478    152       O  
ATOM    538  CB  MET A 123      20.945 -39.110 -35.405  1.00 16.55           C  
ANISOU  538  CB  MET A 123     3080   1739   1467    185    566    -19       C  
ATOM    539  CG  MET A 123      20.232 -38.989 -34.054  1.00 18.32           C  
ANISOU  539  CG  MET A 123     3198   2191   1571    -86    497   -255       C  
ATOM    540  SD  MET A 123      20.699 -37.495 -33.161  1.00 17.79           S  
ANISOU  540  SD  MET A 123     2759   1998   2004   -198    403    -98       S  
ATOM    541  CE  MET A 123      19.746 -36.281 -34.073  1.00 19.12           C  
ANISOU  541  CE  MET A 123     3039   1821   2404    280    240    284       C  
ATOM    542  N   ASP A 124      22.305 -40.562 -37.798  1.00 17.57           N  
ANISOU  542  N   ASP A 124     2639   2220   1818    -58    708    233       N  
ATOM    543  CA  ASP A 124      22.946 -40.461 -39.107  1.00 18.65           C  
ANISOU  543  CA  ASP A 124     2919   2635   1531   -148    699     66       C  
ATOM    544  C   ASP A 124      22.328 -41.392 -40.145  1.00 18.92           C  
ANISOU  544  C   ASP A 124     3349   2279   1561   -243    806    346       C  
ATOM    545  O   ASP A 124      22.286 -41.076 -41.343  1.00 23.13           O  
ANISOU  545  O   ASP A 124     4312   2612   1865   -514    859    175       O  
ATOM    546  CB  ASP A 124      24.441 -40.751 -38.993  1.00 20.14           C  
ANISOU  546  CB  ASP A 124     3022   2719   1912   -138    612   -133       C  
ATOM    547  CG  ASP A 124      25.195 -39.664 -38.245  1.00 19.69           C  
ANISOU  547  CG  ASP A 124     3115   2385   1983    -29    805    100       C  
ATOM    548  OD1 ASP A 124      24.608 -38.591 -37.966  1.00 20.97           O  
ANISOU  548  OD1 ASP A 124     3555   2458   1956     59    794    -38       O  
ATOM    549  OD2 ASP A 124      26.390 -39.881 -37.949  1.00 22.38           O  
ANISOU  549  OD2 ASP A 124     3293   2562   2647    -65    710   -272       O  
ATOM    550  N   ASN A 125      21.865 -42.551 -39.697  1.00 18.12           N  
ANISOU  550  N   ASN A 125     3031   2244   1610   -269    552    160       N  
ATOM    551  CA  ASN A 125      21.262 -43.498 -40.623  1.00 20.13           C  
ANISOU  551  CA  ASN A 125     3428   2504   1716    -38    636   -216       C  
ATOM    552  C   ASN A 125      19.736 -43.471 -40.603  1.00 19.75           C  
ANISOU  552  C   ASN A 125     3600   2418   1487    -76    897   -197       C  
ATOM    553  O   ASN A 125      19.083 -44.341 -41.177  1.00 22.20           O  
ANISOU  553  O   ASN A 125     3791   2707   1936   -372    471   -132       O  
ATOM    554  CB  ASN A 125      21.797 -44.895 -40.336  1.00 22.23           C  
ANISOU  554  CB  ASN A 125     3462   2921   2063   -148    835   -635       C  
ATOM    555  CG  ASN A 125      23.265 -45.025 -40.701  1.00 24.95           C  
ANISOU  555  CG  ASN A 125     3889   3238   2353    209   1053   -265       C  
ATOM    556  OD1 ASN A 125      23.602 -45.127 -41.873  1.00 27.79           O  
ANISOU  556  OD1 ASN A 125     4299   3805   2455    404   1206   -105       O  
ATOM    557  ND2 ASN A 125      24.144 -44.975 -39.705  1.00 25.17           N  
ANISOU  557  ND2 ASN A 125     4030   2901   2632    370   1082   -251       N  
ATOM    558  N   LYS A 126      19.181 -42.451 -39.950  1.00 18.47           N  
ANISOU  558  N   LYS A 126     3365   2127   1524    170    569    157       N  
ATOM    559  CA  LYS A 126      17.737 -42.215 -39.921  1.00 20.73           C  
ANISOU  559  CA  LYS A 126     3570   2320   1987   -120    273    822       C  
ATOM    560  C   LYS A 126      16.960 -43.455 -39.462  1.00 19.98           C  
ANISOU  560  C   LYS A 126     3512   2237   1841   -155    547    345       C  
ATOM    561  O   LYS A 126      15.901 -43.780 -40.007  1.00 22.10           O  
ANISOU  561  O   LYS A 126     3401   2687   2308    125    -54    432       O  
ATOM    562  CB  LYS A 126      17.254 -41.754 -41.296  1.00 23.12           C  
ANISOU  562  CB  LYS A 126     3632   2829   2325   -161    -55   1060       C  
ATOM    563  CG  LYS A 126      17.904 -40.438 -41.728  1.00 28.38           C  
ANISOU  563  CG  LYS A 126     4212   3568   3004    116   -162   1611       C  
ATOM    564  CD  LYS A 126      17.460 -40.000 -43.112  1.00 35.44           C  
ANISOU  564  CD  LYS A 126     5285   4160   4019     19    497   1600       C  
ATOM    565  CE  LYS A 126      18.172 -38.724 -43.519  1.00 41.76           C  
ANISOU  565  CE  LYS A 126     6390   4611   4867    -18   1108   1396       C  
ATOM    566  NZ  LYS A 126      19.647 -38.922 -43.604  1.00 45.87           N  
ANISOU  566  NZ  LYS A 126     7100   4815   5515   -119   1602   1394       N  
ATOM    567  N   LEU A 127      17.485 -44.130 -38.446  1.00 17.76           N  
ANISOU  567  N   LEU A 127     3270   1915   1563    132    688    284       N  
ATOM    568  CA  LEU A 127      16.866 -45.361 -37.953  1.00 16.93           C  
ANISOU  568  CA  LEU A 127     2654   2021   1756    -52    454    191       C  
ATOM    569  C   LEU A 127      15.738 -45.070 -36.972  1.00 17.90           C  
ANISOU  569  C   LEU A 127     2889   1857   2054     49    410     44       C  
ATOM    570  O   LEU A 127      14.847 -45.898 -36.778  1.00 19.21           O  
ANISOU  570  O   LEU A 127     3152   2089   2058   -110    369   -151       O  
ATOM    571  CB  LEU A 127      17.919 -46.248 -37.292  1.00 18.31           C  
ANISOU  571  CB  LEU A 127     2535   1955   2466    450    590    146       C  
ATOM    572  CG  LEU A 127      18.980 -46.767 -38.270  1.00 19.90           C  
ANISOU  572  CG  LEU A 127     2624   2305   2632    -82    364   -550       C  
ATOM    573  CD1 LEU A 127      20.052 -47.582 -37.551  1.00 21.25           C  
ANISOU  573  CD1 LEU A 127     2621   2363   3089     35    286   -481       C  
ATOM    574  CD2 LEU A 127      18.326 -47.604 -39.358  1.00 24.50           C  
ANISOU  574  CD2 LEU A 127     3560   2936   2812    140    954   -503       C  
ATOM    575  N   ALA A 128      15.801 -43.910 -36.327  1.00 17.21           N  
ANISOU  575  N   ALA A 128     3036   1516   1986     91    381    -44       N  
ATOM    576  CA  ALA A 128      14.737 -43.481 -35.426  1.00 17.32           C  
ANISOU  576  CA  ALA A 128     3259   1385   1937    292    590    303       C  
ATOM    577  C   ALA A 128      14.673 -41.972 -35.395  1.00 16.31           C  
ANISOU  577  C   ALA A 128     3123   1195   1878    -58    702    195       C  
ATOM    578  O   ALA A 128      15.681 -41.282 -35.619  1.00 20.02           O  
ANISOU  578  O   ALA A 128     3289   1680   2639   -198    936     40       O  
ATOM    579  CB  ALA A 128      14.949 -44.008 -34.011  1.00 18.16           C  
ANISOU  579  CB  ALA A 128     3402   1784   1714    328    127    353       C  
ATOM    580  N   GLN A 129      13.482 -41.472 -35.098  1.00 16.59           N  
ANISOU  580  N   GLN A 129     3212   1351   1739    253    342   -230       N  
ATOM    581  CA  GLN A 129      13.283 -40.071 -34.771  1.00 15.95           C  
ANISOU  581  CA  GLN A 129     3047   1742   1273     17   -262     77       C  
ATOM    582  C   GLN A 129      13.256 -39.993 -33.252  1.00 15.65           C  
ANISOU  582  C   GLN A 129     2816   1808   1321    -92   -159    303       C  
ATOM    583  O   GLN A 129      12.600 -40.809 -32.592  1.00 17.51           O  
ANISOU  583  O   GLN A 129     3200   1834   1621   -225    348     85       O  
ATOM    584  CB  GLN A 129      11.992 -39.541 -35.386  1.00 20.66           C  
ANISOU  584  CB  GLN A 129     3921   2294   1634    298   -407    163       C  
ATOM    585  CG  GLN A 129      11.993 -39.534 -36.919  1.00 26.75           C  
ANISOU  585  CG  GLN A 129     5177   2852   2136     57   -212    -33       C  
ATOM    586  CD  GLN A 129      11.864 -40.939 -37.529  1.00 37.41           C  
ANISOU  586  CD  GLN A 129     6428   4275   3510   -214    202    690       C  
ATOM    587  OE1 GLN A 129      10.890 -41.655 -37.274  1.00 40.56           O  
ANISOU  587  OE1 GLN A 129     6800   4615   3996   -502    -27   1131       O  
ATOM    588  NE2 GLN A 129      12.854 -41.335 -38.330  1.00 41.65           N  
ANISOU  588  NE2 GLN A 129     7004   4755   4066    -56    475    915       N  
ATOM    589  N   ILE A 130      13.982 -39.025 -32.703  1.00 16.87           N  
ANISOU  589  N   ILE A 130     3123   1539   1746    -11      1      8       N  
ATOM    590  CA  ILE A 130      14.138 -38.920 -31.266  1.00 17.85           C  
ANISOU  590  CA  ILE A 130     3235   1514   2035   -307    217    -41       C  
ATOM    591  C   ILE A 130      13.554 -37.605 -30.790  1.00 18.75           C  
ANISOU  591  C   ILE A 130     3809   1327   1987   -237    440     96       C  
ATOM    592  O   ILE A 130      14.007 -36.534 -31.199  1.00 24.32           O  
ANISOU  592  O   ILE A 130     4733   1625   2881   -411   1069   -138       O  
ATOM    593  CB  ILE A 130      15.614 -39.019 -30.846  1.00 18.30           C  
ANISOU  593  CB  ILE A 130     3379   1759   1816   -358     31     61       C  
ATOM    594  CG1 ILE A 130      16.250 -40.273 -31.453  1.00 19.85           C  
ANISOU  594  CG1 ILE A 130     3135   2284   2121   -432   -615   -218       C  
ATOM    595  CG2 ILE A 130      15.727 -39.004 -29.323  1.00 18.61           C  
ANISOU  595  CG2 ILE A 130     3315   1969   1787   -572    190    279       C  
ATOM    596  CD1 ILE A 130      17.763 -40.331 -31.278  1.00 21.92           C  
ANISOU  596  CD1 ILE A 130     3226   2667   2434   -622   -418    175       C  
ATOM    597  N   GLU A 131      12.528 -37.702 -29.949  1.00 17.64           N  
ANISOU  597  N   GLU A 131     3397   1603   1700      0    108     45       N  
ATOM    598  CA  GLU A 131      11.857 -36.539 -29.373  1.00 17.82           C  
ANISOU  598  CA  GLU A 131     3189   1970   1613    398   -455     75       C  
ATOM    599  C   GLU A 131      12.415 -36.269 -27.976  1.00 16.64           C  
ANISOU  599  C   GLU A 131     3146   1715   1462    258   -265    457       C  
ATOM    600  O   GLU A 131      12.436 -37.154 -27.133  1.00 19.90           O  
ANISOU  600  O   GLU A 131     3999   1547   2016     66   -640    356       O  
ATOM    601  CB  GLU A 131      10.344 -36.773 -29.302  1.00 21.71           C  
ANISOU  601  CB  GLU A 131     3528   2539   2181    971   -264   -278       C  
ATOM    602  CG  GLU A 131       9.566 -35.652 -28.608  1.00 28.56           C  
ANISOU  602  CG  GLU A 131     4300   3558   2991    265    229     26       C  
ATOM    603  CD  GLU A 131       8.155 -36.064 -28.227  1.00 34.47           C  
ANISOU  603  CD  GLU A 131     5103   4243   3752     -1    141    -49       C  
ATOM    604  OE1 GLU A 131       7.955 -36.522 -27.080  1.00 36.72           O  
ANISOU  604  OE1 GLU A 131     5318   4467   4166   -360    682   -256       O  
ATOM    605  OE2 GLU A 131       7.244 -35.925 -29.064  1.00 37.27           O  
ANISOU  605  OE2 GLU A 131     5502   4442   4218    178    -72     96       O  
ATOM    606  N   GLY A 132      12.865 -35.047 -27.727  1.00 15.83           N  
ANISOU  606  N   GLY A 132     2635   1681   1699   -120     51   -139       N  
ATOM    607  CA  GLY A 132      13.411 -34.706 -26.432  1.00 15.50           C  
ANISOU  607  CA  GLY A 132     2638   1653   1599    269    304     47       C  
ATOM    608  C   GLY A 132      12.524 -33.751 -25.654  1.00 15.16           C  
ANISOU  608  C   GLY A 132     2645   1561   1555    188    -64    -37       C  
ATOM    609  O   GLY A 132      11.970 -32.810 -26.215  1.00 17.02           O  
ANISOU  609  O   GLY A 132     2645   1582   2239    277    109    388       O  
ATOM    610  N  AVAL A 133      12.382 -33.991 -24.358  0.65 15.20           N  
ANISOU  610  N  AVAL A 133     2534   1425   1817    201     22    -73       N  
ATOM    611  N  BVAL A 133      12.398 -34.009 -24.355  0.35 16.53           N  
ANISOU  611  N  BVAL A 133     2618   1626   2038     14    216     24       N  
ATOM    612  CA AVAL A 133      11.687 -33.046 -23.494  0.65 14.11           C  
ANISOU  612  CA AVAL A 133     2284   1440   1637    105   -247     23       C  
ATOM    613  CA BVAL A 133      11.670 -33.136 -23.435  0.35 17.26           C  
ANISOU  613  CA BVAL A 133     2584   1750   2224   -226    415    150       C  
ATOM    614  C  AVAL A 133      12.435 -32.938 -22.172  0.65 14.87           C  
ANISOU  614  C  AVAL A 133     2491   1564   1594    -64   -120   -174       C  
ATOM    615  C  BVAL A 133      12.479 -32.944 -22.159  0.35 16.87           C  
ANISOU  615  C  BVAL A 133     2610   1654   2145   -337    522     22       C  
ATOM    616  O  AVAL A 133      13.021 -33.907 -21.698  0.65 16.42           O  
ANISOU  616  O  AVAL A 133     2875   1526   1840    252   -333    -36       O  
ATOM    617  O  BVAL A 133      13.134 -33.873 -21.689  0.35 18.28           O  
ANISOU  617  O  BVAL A 133     2790   1560   2595   -311    825    232       O  
ATOM    618  CB AVAL A 133      10.213 -33.459 -23.259  0.65 14.49           C  
ANISOU  618  CB AVAL A 133     2037   1364   2104    133      2     -5       C  
ATOM    619  CB BVAL A 133      10.283 -33.713 -23.072  0.35 19.32           C  
ANISOU  619  CB BVAL A 133     2648   2031   2664   -302    669     45       C  
ATOM    620  CG1AVAL A 133      10.130 -34.741 -22.450  0.65 13.76           C  
ANISOU  620  CG1AVAL A 133     2040    932   2255   -103     57   -221       C  
ATOM    621  CG1BVAL A 133       9.557 -32.812 -22.076  0.35 22.41           C  
ANISOU  621  CG1BVAL A 133     2929   2565   3019   -278   1277    191       C  
ATOM    622  CG2AVAL A 133       9.422 -32.320 -22.587  0.65 17.76           C  
ANISOU  622  CG2AVAL A 133     2537   1720   2491    235    388    469       C  
ATOM    623  CG2BVAL A 133       9.451 -33.887 -24.311  0.35 19.86           C  
ANISOU  623  CG2BVAL A 133     2933   1747   2866   -571    775   -127       C  
ATOM    624  N   VAL A 134      12.449 -31.737 -21.606  1.00 15.71           N  
ANISOU  624  N   VAL A 134     2612   1650   1707   -240    366   -182       N  
ATOM    625  CA  VAL A 134      13.083 -31.490 -20.326  1.00 17.33           C  
ANISOU  625  CA  VAL A 134     2819   2125   1641   -729    306   -495       C  
ATOM    626  C   VAL A 134      11.966 -31.448 -19.283  1.00 21.72           C  
ANISOU  626  C   VAL A 134     3350   2898   2006   -205    276   -261       C  
ATOM    627  O   VAL A 134      11.160 -30.513 -19.264  1.00 24.09           O  
ANISOU  627  O   VAL A 134     3489   3193   2471    100    741    -14       O  
ATOM    628  CB  VAL A 134      13.902 -30.191 -20.345  1.00 18.05           C  
ANISOU  628  CB  VAL A 134     2872   2053   1934   -611    364   -478       C  
ATOM    629  CG1 VAL A 134      14.381 -29.851 -18.955  1.00 22.47           C  
ANISOU  629  CG1 VAL A 134     3415   2790   2331   -890    -23   -559       C  
ATOM    630  CG2 VAL A 134      15.073 -30.336 -21.301  1.00 17.21           C  
ANISOU  630  CG2 VAL A 134     2496   1847   2197   -471    435    119       C  
ATOM    631  N   PRO A 135      11.878 -32.497 -18.451  1.00 26.07           N  
ANISOU  631  N   PRO A 135     3944   3985   1974   -762    325    253       N  
ATOM    632  CA  PRO A 135      10.716 -32.646 -17.574  1.00 31.79           C  
ANISOU  632  CA  PRO A 135     4608   4844   2629  -1121    822     -5       C  
ATOM    633  C   PRO A 135      10.832 -31.820 -16.308  1.00 36.52           C  
ANISOU  633  C   PRO A 135     5282   5953   2640  -1128    847   -816       C  
ATOM    634  O   PRO A 135       9.818 -31.493 -15.694  1.00 41.08           O  
ANISOU  634  O   PRO A 135     5781   6618   3211  -1150   1627  -1348       O  
ATOM    635  CB  PRO A 135      10.713 -34.148 -17.249  1.00 33.51           C  
ANISOU  635  CB  PRO A 135     4827   4581   3322  -1130    778    719       C  
ATOM    636  CG  PRO A 135      12.148 -34.543 -17.319  1.00 34.00           C  
ANISOU  636  CG  PRO A 135     5199   4364   3356   -860   1204    801       C  
ATOM    637  CD  PRO A 135      12.774 -33.668 -18.392  1.00 27.73           C  
ANISOU  637  CD  PRO A 135     4367   3715   2452  -1062   1006    705       C  
ATOM    638  N   PHE A 136      12.062 -31.505 -15.927  1.00 36.49           N  
ANISOU  638  N   PHE A 136     5780   5933   2150  -1332    720   -727       N  
ATOM    639  CA  PHE A 136      12.338 -30.742 -14.715  1.00 37.12           C  
ANISOU  639  CA  PHE A 136     6131   5798   2177   -890    589   -308       C  
ATOM    640  C   PHE A 136      13.807 -30.364 -14.725  1.00 35.19           C  
ANISOU  640  C   PHE A 136     6003   5010   2356   -753    204    -20       C  
ATOM    641  O   PHE A 136      14.565 -30.837 -15.573  1.00 34.30           O  
ANISOU  641  O   PHE A 136     5722   4623   2687   -838    145   -130       O  
ATOM    642  CB  PHE A 136      11.992 -31.540 -13.447  1.00 42.99           C  
ANISOU  642  CB  PHE A 136     6856   6694   2782   -816    561    333       C  
ATOM    643  CG  PHE A 136      12.935 -32.678 -13.162  1.00 46.46           C  
ANISOU  643  CG  PHE A 136     7571   7264   2818  -1130    717   1010       C  
ATOM    644  CD1 PHE A 136      12.736 -33.922 -13.738  1.00 48.18           C  
ANISOU  644  CD1 PHE A 136     7754   7694   2858  -1168    752   1049       C  
ATOM    645  CD2 PHE A 136      14.015 -32.506 -12.307  1.00 51.19           C  
ANISOU  645  CD2 PHE A 136     8126   7575   3746  -1247    972    685       C  
ATOM    646  CE1 PHE A 136      13.601 -34.975 -13.474  1.00 50.56           C  
ANISOU  646  CE1 PHE A 136     8167   7832   3212  -1255   1043    987       C  
ATOM    647  CE2 PHE A 136      14.885 -33.553 -12.036  1.00 53.34           C  
ANISOU  647  CE2 PHE A 136     8331   7839   4097  -1294    967    529       C  
ATOM    648  CZ  PHE A 136      14.679 -34.789 -12.623  1.00 52.76           C  
ANISOU  648  CZ  PHE A 136     8397   7810   3840  -1296   1118    719       C  
ATOM    649  N   GLY A 137      14.207 -29.519 -13.782  1.00 34.50           N  
ANISOU  649  N   GLY A 137     6324   4587   2199   -584     16   -267       N  
ATOM    650  CA  GLY A 137      15.600 -29.139 -13.643  1.00 34.78           C  
ANISOU  650  CA  GLY A 137     6322   4374   2521   -463    278   -342       C  
ATOM    651  C   GLY A 137      16.077 -28.240 -14.764  1.00 35.74           C  
ANISOU  651  C   GLY A 137     6241   4128   3210   -342    633   -381       C  
ATOM    652  O   GLY A 137      17.271 -28.173 -15.059  1.00 36.01           O  
ANISOU  652  O   GLY A 137     6295   3983   3404     34    311   -352       O  
ATOM    653  N   ALA A 138      15.139 -27.544 -15.396  1.00 36.24           N  
ANISOU  653  N   ALA A 138     6081   4246   3443   -585   1256    125       N  
ATOM    654  CA  ALA A 138      15.477 -26.677 -16.514  1.00 34.42           C  
ANISOU  654  CA  ALA A 138     5746   3991   3341   -729   1279    538       C  
ATOM    655  C   ALA A 138      16.388 -25.529 -16.085  1.00 36.55           C  
ANISOU  655  C   ALA A 138     6462   4280   3147   -950   1040    -79       C  
ATOM    656  O   ALA A 138      17.106 -24.972 -16.906  1.00 34.74           O  
ANISOU  656  O   ALA A 138     6245   3765   3188   -985    589    291       O  
ATOM    657  CB  ALA A 138      14.216 -26.138 -17.168  1.00 32.22           C  
ANISOU  657  CB  ALA A 138     4897   3952   3393   -648    726    924       C  
ATOM    658  N   ASN A 139      16.381 -25.191 -14.799  1.00 41.01           N  
ANISOU  658  N   ASN A 139     7123   5123   3338  -1456    860   -616       N  
ATOM    659  CA  ASN A 139      17.193 -24.080 -14.315  1.00 48.25           C  
ANISOU  659  CA  ASN A 139     7896   6011   4426  -1431   1300   -993       C  
ATOM    660  C   ASN A 139      18.497 -24.523 -13.649  1.00 48.61           C  
ANISOU  660  C   ASN A 139     7841   6072   4558  -1563   1057  -1370       C  
ATOM    661  O   ASN A 139      19.145 -23.744 -12.948  1.00 50.17           O  
ANISOU  661  O   ASN A 139     8052   6179   4832  -1688    796  -1180       O  
ATOM    662  CB  ASN A 139      16.373 -23.226 -13.353  1.00 53.87           C  
ANISOU  662  CB  ASN A 139     8464   6731   5274  -1399   2180  -1328       C  
ATOM    663  CG  ASN A 139      15.229 -22.514 -14.049  1.00 60.34           C  
ANISOU  663  CG  ASN A 139     9155   7620   6152  -1337   2755  -1480       C  
ATOM    664  OD1 ASN A 139      15.390 -21.996 -15.156  1.00 62.71           O  
ANISOU  664  OD1 ASN A 139     9332   7945   6551  -1205   2869  -1534       O  
ATOM    665  ND2 ASN A 139      14.065 -22.497 -13.415  1.00 62.64           N  
ANISOU  665  ND2 ASN A 139     9399   7918   6482  -1222   2997  -1556       N  
ATOM    666  N   ASN A 140      18.873 -25.777 -13.879  1.00 46.69           N  
ANISOU  666  N   ASN A 140     7462   5915   4364  -1496   1204  -1790       N  
ATOM    667  CA  ASN A 140      20.134 -26.315 -13.381  1.00 46.35           C  
ANISOU  667  CA  ASN A 140     7278   5895   4436  -1647    986  -2090       C  
ATOM    668  C   ASN A 140      21.355 -25.627 -13.994  1.00 48.56           C  
ANISOU  668  C   ASN A 140     7248   6040   5164  -1724   1117  -2040       C  
ATOM    669  O   ASN A 140      21.321 -25.187 -15.144  1.00 48.99           O  
ANISOU  669  O   ASN A 140     7102   5890   5625  -1684   1835  -1778       O  
ATOM    670  CB  ASN A 140      20.209 -27.813 -13.656  1.00 45.05           C  
ANISOU  670  CB  ASN A 140     7160   6027   3930  -1354    691  -1886       C  
ATOM    671  CG  ASN A 140      19.307 -28.624 -12.750  1.00 44.93           C  
ANISOU  671  CG  ASN A 140     7317   6187   3566   -979    429  -1445       C  
ATOM    672  OD1 ASN A 140      18.611 -28.076 -11.898  1.00 45.42           O  
ANISOU  672  OD1 ASN A 140     7392   6494   3370   -407    515  -1093       O  
ATOM    673  ND2 ASN A 140      19.312 -29.941 -12.934  1.00 44.05           N  
ANISOU  673  ND2 ASN A 140     7396   5892   3449  -1096    308  -1579       N  
ATOM    674  N   ALA A 141      22.439 -25.563 -13.227  1.00 49.62           N  
ANISOU  674  N   ALA A 141     7214   6316   5324  -1684    537  -2170       N  
ATOM    675  CA  ALA A 141      23.626 -24.819 -13.636  1.00 51.59           C  
ANISOU  675  CA  ALA A 141     7300   6850   5453  -1353     61  -2196       C  
ATOM    676  C   ALA A 141      24.554 -25.618 -14.548  1.00 51.68           C  
ANISOU  676  C   ALA A 141     7020   7164   5451  -1056   -466  -1998       C  
ATOM    677  O   ALA A 141      25.180 -25.055 -15.446  1.00 50.68           O  
ANISOU  677  O   ALA A 141     7101   7374   4780   -956   -378  -2019       O  
ATOM    678  CB  ALA A 141      24.393 -24.345 -12.407  1.00 52.35           C  
ANISOU  678  CB  ALA A 141     7406   6990   5495  -1553   -333  -2087       C  
ATOM    679  N   PHE A 142      24.655 -26.922 -14.319  1.00 50.49           N  
ANISOU  679  N   PHE A 142     6539   7042   5604   -914  -1312  -2075       N  
ATOM    680  CA  PHE A 142      25.656 -27.709 -15.024  1.00 51.36           C  
ANISOU  680  CA  PHE A 142     6426   7156   5932   -843  -1593  -1610       C  
ATOM    681  C   PHE A 142      25.062 -28.790 -15.904  1.00 45.01           C  
ANISOU  681  C   PHE A 142     5309   6400   5394   -473  -1422  -1079       C  
ATOM    682  O   PHE A 142      25.525 -28.981 -17.031  1.00 44.08           O  
ANISOU  682  O   PHE A 142     4502   6536   5709   -139  -1801   -933       O  
ATOM    683  CB  PHE A 142      26.639 -28.326 -14.028  1.00 58.65           C  
ANISOU  683  CB  PHE A 142     7400   7985   6897  -1077  -1803  -1725       C  
ATOM    684  CG  PHE A 142      27.444 -27.310 -13.277  1.00 65.74           C  
ANISOU  684  CG  PHE A 142     8300   8743   7935  -1538  -1933  -1958       C  
ATOM    685  CD1 PHE A 142      28.267 -26.422 -13.956  1.00 69.11           C  
ANISOU  685  CD1 PHE A 142     8793   9073   8392  -1718  -1911  -2074       C  
ATOM    686  CD2 PHE A 142      27.379 -27.235 -11.896  1.00 69.70           C  
ANISOU  686  CD2 PHE A 142     8836   9124   8524  -1691  -1513  -1945       C  
ATOM    687  CE1 PHE A 142      29.012 -25.476 -13.269  1.00 71.74           C  
ANISOU  687  CE1 PHE A 142     9032   9318   8908  -1922  -1775  -2057       C  
ATOM    688  CE2 PHE A 142      28.123 -26.292 -11.203  1.00 72.03           C  
ANISOU  688  CE2 PHE A 142     9131   9306   8933  -1860  -1343  -2080       C  
ATOM    689  CZ  PHE A 142      28.940 -25.412 -11.892  1.00 72.59           C  
ANISOU  689  CZ  PHE A 142     9159   9395   9026  -1978  -1616  -2157       C  
ATOM    690  N   THR A 143      24.057 -29.507 -15.399  1.00 39.06           N  
ANISOU  690  N   THR A 143     4819   5582   4440   -490  -1059   -613       N  
ATOM    691  CA  THR A 143      23.369 -30.513 -16.210  1.00 33.28           C  
ANISOU  691  CA  THR A 143     4199   4935   3511   -619   -761    -39       C  
ATOM    692  C   THR A 143      21.853 -30.478 -16.045  1.00 28.52           C  
ANISOU  692  C   THR A 143     4055   4085   2696   -480   -373    152       C  
ATOM    693  O   THR A 143      21.335 -30.130 -14.993  1.00 31.94           O  
ANISOU  693  O   THR A 143     4925   4567   2645   -575    -56   -265       O  
ATOM    694  CB  THR A 143      23.847 -31.946 -15.903  1.00 32.95           C  
ANISOU  694  CB  THR A 143     4323   5050   3147   -636   -657    809       C  
ATOM    695  OG1 THR A 143      23.241 -32.421 -14.692  1.00 34.54           O  
ANISOU  695  OG1 THR A 143     4754   4846   3524   -927    156   1298       O  
ATOM    696  CG2 THR A 143      25.366 -32.009 -15.798  1.00 34.97           C  
ANISOU  696  CG2 THR A 143     4336   5168   3781   -536   -494    540       C  
ATOM    697  N   MET A 144      21.162 -30.885 -17.100  1.00 22.39           N  
ANISOU  697  N   MET A 144     3471   2816   2220   -733   -409    109       N  
ATOM    698  CA  MET A 144      19.718 -30.756 -17.234  1.00 21.90           C  
ANISOU  698  CA  MET A 144     3619   2253   2448   -959   -130    205       C  
ATOM    699  C   MET A 144      19.122 -32.122 -17.589  1.00 20.77           C  
ANISOU  699  C   MET A 144     3444   2119   2329   -966    111    344       C  
ATOM    700  O   MET A 144      19.541 -32.724 -18.572  1.00 23.10           O  
ANISOU  700  O   MET A 144     4297   2200   2279   -973    413    347       O  
ATOM    701  CB  MET A 144      19.405 -29.717 -18.327  1.00 23.01           C  
ANISOU  701  CB  MET A 144     3445   2198   3098   -353   -365    252       C  
ATOM    702  CG  MET A 144      17.951 -29.404 -18.543  1.00 24.25           C  
ANISOU  702  CG  MET A 144     4022   2553   2640   -264    -97    539       C  
ATOM    703  SD  MET A 144      17.744 -28.196 -19.852  1.00 24.47           S  
ANISOU  703  SD  MET A 144     4098   2278   2924   -730    341    302       S  
ATOM    704  CE  MET A 144      18.587 -26.760 -19.202  1.00 26.39           C  
ANISOU  704  CE  MET A 144     4528   2436   3063  -1403    453    126       C  
ATOM    705  N   PRO A 145      18.152 -32.618 -16.798  1.00 21.06           N  
ANISOU  705  N   PRO A 145     3255   2611   2134  -1017   -382    -31       N  
ATOM    706  CA  PRO A 145      17.487 -33.884 -17.136  1.00 20.22           C  
ANISOU  706  CA  PRO A 145     3190   2693   1799  -1133   -298    219       C  
ATOM    707  C   PRO A 145      16.823 -33.853 -18.515  1.00 19.88           C  
ANISOU  707  C   PRO A 145     3198   2274   2081   -925   -516    278       C  
ATOM    708  O   PRO A 145      16.218 -32.851 -18.890  1.00 20.45           O  
ANISOU  708  O   PRO A 145     3563   1969   2237   -762   -505    497       O  
ATOM    709  CB  PRO A 145      16.426 -34.027 -16.036  1.00 21.86           C  
ANISOU  709  CB  PRO A 145     3315   3147   1846  -1590    231    131       C  
ATOM    710  CG  PRO A 145      16.919 -33.193 -14.918  1.00 26.87           C  
ANISOU  710  CG  PRO A 145     3792   3690   2726  -1204    305     33       C  
ATOM    711  CD  PRO A 145      17.607 -32.032 -15.561  1.00 23.92           C  
ANISOU  711  CD  PRO A 145     3571   3157   2362  -1283    256     80       C  
ATOM    712  N   LEU A 146      16.928 -34.956 -19.244  1.00 17.91           N  
ANISOU  712  N   LEU A 146     2927   2167   1712   -770   -363    257       N  
ATOM    713  CA  LEU A 146      16.356 -35.087 -20.576  1.00 16.55           C  
ANISOU  713  CA  LEU A 146     2572   1651   2066   -767    113    178       C  
ATOM    714  C   LEU A 146      15.638 -36.431 -20.724  1.00 13.88           C  
ANISOU  714  C   LEU A 146     2130   1351   1791   -195     38    264       C  
ATOM    715  O   LEU A 146      16.190 -37.470 -20.378  1.00 16.34           O  
ANISOU  715  O   LEU A 146     2630   1597   1980    -50   -121    418       O  
ATOM    716  CB  LEU A 146      17.461 -34.963 -21.623  1.00 19.44           C  
ANISOU  716  CB  LEU A 146     2881   2108   2398   -668    594    226       C  
ATOM    717  CG  LEU A 146      17.036 -35.077 -23.078  1.00 17.70           C  
ANISOU  717  CG  LEU A 146     2258   2529   1936   -285    176    -90       C  
ATOM    718  CD1 LEU A 146      16.221 -33.854 -23.458  1.00 19.21           C  
ANISOU  718  CD1 LEU A 146     2660   2451   2189    163    238     15       C  
ATOM    719  CD2 LEU A 146      18.254 -35.175 -23.967  1.00 20.70           C  
ANISOU  719  CD2 LEU A 146     2313   2877   2674   -207    773   -190       C  
ATOM    720  N   HIS A 147      14.415 -36.396 -21.245  1.00 13.82           N  
ANISOU  720  N   HIS A 147     2094   1377   1779   -443     80     90       N  
ATOM    721  CA  HIS A 147      13.649 -37.595 -21.565  1.00 14.00           C  
ANISOU  721  CA  HIS A 147     1917   1761   1643   -301    185    239       C  
ATOM    722  C   HIS A 147      13.563 -37.704 -23.079  1.00 14.05           C  
ANISOU  722  C   HIS A 147     2444   1526   1370    -82    112    334       C  
ATOM    723  O   HIS A 147      13.178 -36.741 -23.749  1.00 15.50           O  
ANISOU  723  O   HIS A 147     2756   1444   1688    -75   -117    264       O  
ATOM    724  CB  HIS A 147      12.254 -37.531 -20.933  1.00 14.61           C  
ANISOU  724  CB  HIS A 147     1886   1768   1896   -213    208    188       C  
ATOM    725  CG  HIS A 147      11.393 -38.705 -21.254  1.00 15.14           C  
ANISOU  725  CG  HIS A 147     2029   1345   2380   -265    506     17       C  
ATOM    726  ND1 HIS A 147      11.254 -39.788 -20.408  1.00 18.28           N  
ANISOU  726  ND1 HIS A 147     2334   1591   3020   -289    793     21       N  
ATOM    727  CD2 HIS A 147      10.627 -38.972 -22.338  1.00 14.87           C  
ANISOU  727  CD2 HIS A 147     2095   1387   2169   -223   -172   -240       C  
ATOM    728  CE1 HIS A 147      10.444 -40.674 -20.965  1.00 17.24           C  
ANISOU  728  CE1 HIS A 147     2287   1479   2784    -95    801    356       C  
ATOM    729  NE2 HIS A 147      10.050 -40.203 -22.133  1.00 18.30           N  
ANISOU  729  NE2 HIS A 147     2374   1474   3104   -376    420   -370       N  
ATOM    730  N   MET A 148      13.941 -38.863 -23.614  1.00 12.73           N  
ANISOU  730  N   MET A 148     2049   1328   1462    -81     20      2       N  
ATOM    731  CA  MET A 148      13.944 -39.080 -25.059  1.00 12.96           C  
ANISOU  731  CA  MET A 148     1958   1348   1618   -104     66    173       C  
ATOM    732  C   MET A 148      12.997 -40.186 -25.455  1.00 13.31           C  
ANISOU  732  C   MET A 148     1919   1361   1776   -213    -52    354       C  
ATOM    733  O   MET A 148      13.076 -41.286 -24.912  1.00 15.52           O  
ANISOU  733  O   MET A 148     2646   1184   2068   -211    -50    523       O  
ATOM    734  CB  MET A 148      15.347 -39.440 -25.547  1.00 13.78           C  
ANISOU  734  CB  MET A 148     1669   1660   1909    -75    452    379       C  
ATOM    735  CG  MET A 148      16.343 -38.321 -25.399  1.00 16.48           C  
ANISOU  735  CG  MET A 148     1526   2154   2582   -600    675    332       C  
ATOM    736  SD  MET A 148      18.064 -38.891 -25.241  1.00 19.18           S  
ANISOU  736  SD  MET A 148     2214   2557   2517    -65    545    422       S  
ATOM    737  CE  MET A 148      18.080 -39.350 -23.497  1.00 19.13           C  
ANISOU  737  CE  MET A 148     2287   3144   1839   -119    364    914       C  
ATOM    738  N   THR A 149      12.121 -39.909 -26.410  1.00 13.25           N  
ANISOU  738  N   THR A 149     2086   1485   1463     53     29     61       N  
ATOM    739  CA  THR A 149      11.209 -40.919 -26.919  1.00 14.05           C  
ANISOU  739  CA  THR A 149     2054   1438   1844   -118    -45    -50       C  
ATOM    740  C   THR A 149      11.586 -41.256 -28.355  1.00 13.66           C  
ANISOU  740  C   THR A 149     2230   1448   1512    191   -288    153       C  
ATOM    741  O   THR A 149      11.790 -40.353 -29.174  1.00 15.93           O  
ANISOU  741  O   THR A 149     3098   1375   1581    193    136     59       O  
ATOM    742  CB  THR A 149       9.732 -40.445 -26.863  1.00 14.93           C  
ANISOU  742  CB  THR A 149     2153   1856   1662   -183     22   -441       C  
ATOM    743  OG1 THR A 149       9.431 -39.957 -25.549  1.00 18.20           O  
ANISOU  743  OG1 THR A 149     2831   2164   1921     26    447   -380       O  
ATOM    744  CG2 THR A 149       8.795 -41.601 -27.204  1.00 17.52           C  
ANISOU  744  CG2 THR A 149     2647   2013   1997   -127    179   -207       C  
ATOM    745  N   PHE A 150      11.686 -42.549 -28.650  1.00 13.07           N  
ANISOU  745  N   PHE A 150     2195   1232   1540     83    220   -147       N  
ATOM    746  CA  PHE A 150      12.169 -43.032 -29.947  1.00 12.82           C  
ANISOU  746  CA  PHE A 150     2262   1186   1422     -4     18    131       C  
ATOM    747  C   PHE A 150      11.021 -43.566 -30.782  1.00 13.96           C  
ANISOU  747  C   PHE A 150     2118   1506   1681     13   -176     -7       C  
ATOM    748  O   PHE A 150      10.234 -44.390 -30.308  1.00 14.92           O  
ANISOU  748  O   PHE A 150     2386   1515   1769   -225     51     18       O  
ATOM    749  CB  PHE A 150      13.213 -44.154 -29.775  1.00 14.39           C  
ANISOU  749  CB  PHE A 150     2038   1482   1947    185    -91    496       C  
ATOM    750  CG  PHE A 150      14.544 -43.693 -29.242  1.00 13.79           C  
ANISOU  750  CG  PHE A 150     2102   1587   1548    -39   -113    508       C  
ATOM    751  CD1 PHE A 150      14.661 -43.135 -27.971  1.00 15.15           C  
ANISOU  751  CD1 PHE A 150     2431   1558   1767    -43   -236    384       C  
ATOM    752  CD2 PHE A 150      15.697 -43.850 -30.009  1.00 16.96           C  
ANISOU  752  CD2 PHE A 150     2147   2052   2244    157    390    276       C  
ATOM    753  CE1 PHE A 150      15.900 -42.717 -27.486  1.00 15.96           C  
ANISOU  753  CE1 PHE A 150     2527   1592   1943    345    150    126       C  
ATOM    754  CE2 PHE A 150      16.936 -43.440 -29.535  1.00 18.89           C  
ANISOU  754  CE2 PHE A 150     2711   2200   2266    269    559    152       C  
ATOM    755  CZ  PHE A 150      17.042 -42.855 -28.277  1.00 16.50           C  
ANISOU  755  CZ  PHE A 150     2763   1725   1782     91    433    146       C  
ATOM    756  N   TRP A 151      10.985 -43.143 -32.039  1.00 14.91           N  
ANISOU  756  N   TRP A 151     2434   1685   1544    184   -275    -45       N  
ATOM    757  CA  TRP A 151       9.971 -43.547 -33.010  1.00 15.94           C  
ANISOU  757  CA  TRP A 151     2670   1700   1686     99   -143   -351       C  
ATOM    758  C   TRP A 151      10.650 -44.021 -34.280  1.00 15.69           C  
ANISOU  758  C   TRP A 151     2910   1458   1594   -225    145   -536       C  
ATOM    759  O   TRP A 151      11.667 -43.451 -34.677  1.00 18.00           O  
ANISOU  759  O   TRP A 151     2974   1637   2228   -197    278     11       O  
ATOM    760  CB  TRP A 151       9.051 -42.380 -33.364  1.00 18.52           C  
ANISOU  760  CB  TRP A 151     2632   2368   2037   1002   -186   -153       C  
ATOM    761  CG  TRP A 151       8.297 -41.848 -32.214  1.00 21.70           C  
ANISOU  761  CG  TRP A 151     3296   2840   2107   1080     76    -94       C  
ATOM    762  CD1 TRP A 151       8.718 -40.912 -31.310  1.00 24.04           C  
ANISOU  762  CD1 TRP A 151     3989   3364   1779   1124    -56   -157       C  
ATOM    763  CD2 TRP A 151       6.978 -42.219 -31.828  1.00 24.80           C  
ANISOU  763  CD2 TRP A 151     3359   3198   2866   1298    -12    708       C  
ATOM    764  NE1 TRP A 151       7.734 -40.683 -30.382  1.00 27.10           N  
ANISOU  764  NE1 TRP A 151     4253   3908   2136   1228   -119    146       N  
ATOM    765  CE2 TRP A 151       6.654 -41.474 -30.676  1.00 27.34           C  
ANISOU  765  CE2 TRP A 151     3758   3573   3056   1472    132    337       C  
ATOM    766  CE3 TRP A 151       6.035 -43.110 -32.344  1.00 25.02           C  
ANISOU  766  CE3 TRP A 151     2882   2593   4033    781    344   1015       C  
ATOM    767  CZ2 TRP A 151       5.430 -41.598 -30.028  1.00 31.54           C  
ANISOU  767  CZ2 TRP A 151     3964   3806   4215   1569    486    670       C  
ATOM    768  CZ3 TRP A 151       4.810 -43.231 -31.694  1.00 29.36           C  
ANISOU  768  CZ3 TRP A 151     3340   3236   4580   1234    574   1094       C  
ATOM    769  CH2 TRP A 151       4.524 -42.478 -30.552  1.00 30.53           C  
ANISOU  769  CH2 TRP A 151     3737   3343   4521   1301    643    843       C  
ATOM    770  N   GLY A 152      10.101 -45.041 -34.931  1.00 15.92           N  
ANISOU  770  N   GLY A 152     2937   1638   1475     30     26   -427       N  
ATOM    771  CA  GLY A 152      10.637 -45.434 -36.218  1.00 17.54           C  
ANISOU  771  CA  GLY A 152     3224   1979   1460   -242    252   -408       C  
ATOM    772  C   GLY A 152       9.824 -46.509 -36.901  1.00 18.82           C  
ANISOU  772  C   GLY A 152     3363   2206   1581   -205     17   -420       C  
ATOM    773  O   GLY A 152       8.754 -46.878 -36.426  1.00 24.48           O  
ANISOU  773  O   GLY A 152     3740   2950   2612   -712    506   -829       O  
ATOM    774  N   LYS A 153      10.341 -47.026 -38.008  1.00 19.19           N  
ANISOU  774  N   LYS A 153     3558   1877   1856    164    161   -109       N  
ATOM    775  CA  LYS A 153       9.683 -48.099 -38.744  1.00 19.54           C  
ANISOU  775  CA  LYS A 153     3697   1581   2147   -178   -148   -205       C  
ATOM    776  C   LYS A 153       9.941 -49.439 -38.058  1.00 18.67           C  
ANISOU  776  C   LYS A 153     3414   1681   1997     -4    -14   -224       C  
ATOM    777  O   LYS A 153      11.037 -49.649 -37.530  1.00 18.61           O  
ANISOU  777  O   LYS A 153     3130   1927   2013    117   -110   -180       O  
ATOM    778  CB  LYS A 153      10.203 -48.150 -40.173  1.00 22.39           C  
ANISOU  778  CB  LYS A 153     4587   2425   1496   -698    169    300       C  
ATOM    779  CG  LYS A 153      10.003 -46.882 -40.993  1.00 27.98           C  
ANISOU  779  CG  LYS A 153     5196   3739   1696   -965    235    615       C  
ATOM    780  CD  LYS A 153      10.784 -46.988 -42.303  1.00 36.19           C  
ANISOU  780  CD  LYS A 153     5933   5517   2298  -1033    377   1294       C  
ATOM    781  CE  LYS A 153      10.553 -45.788 -43.217  1.00 44.46           C  
ANISOU  781  CE  LYS A 153     6452   6988   3451  -1276    958   1147       C  
ATOM    782  NZ  LYS A 153      11.329 -45.889 -44.491  1.00 48.59           N  
ANISOU  782  NZ  LYS A 153     6692   7649   4119  -1351   1031    749       N  
ATOM    783  N   GLU A 154       8.954 -50.338 -38.061  1.00 19.40           N  
ANISOU  783  N   GLU A 154     3460   1707   2206    -52    206   -534       N  
ATOM    784  CA  GLU A 154       9.175 -51.659 -37.470  1.00 19.91           C  
ANISOU  784  CA  GLU A 154     3192   1923   2450   -448   -225   -671       C  
ATOM    785  C   GLU A 154      10.403 -52.332 -38.078  1.00 18.19           C  
ANISOU  785  C   GLU A 154     3122   1772   2017    -97   -191   -355       C  
ATOM    786  O   GLU A 154      11.137 -53.012 -37.370  1.00 19.59           O  
ANISOU  786  O   GLU A 154     3412   1957   2076   -143   -278    172       O  
ATOM    787  CB  GLU A 154       7.960 -52.589 -37.638  1.00 23.99           C  
ANISOU  787  CB  GLU A 154     3275   2906   2933   -553   -269   -998       C  
ATOM    788  CG  GLU A 154       6.843 -52.392 -36.625  1.00 26.22           C  
ANISOU  788  CG  GLU A 154     3734   3282   2948   -189    -84   -554       C  
ATOM    789  CD  GLU A 154       7.188 -52.824 -35.191  1.00 24.51           C  
ANISOU  789  CD  GLU A 154     3663   2780   2871   -103    185   -412       C  
ATOM    790  OE1 GLU A 154       8.176 -53.558 -34.951  1.00 22.17           O  
ANISOU  790  OE1 GLU A 154     3263   2572   2591    -55    418   -714       O  
ATOM    791  OE2 GLU A 154       6.437 -52.434 -34.289  1.00 25.18           O  
ANISOU  791  OE2 GLU A 154     4097   2221   3251    258    239   -138       O  
ATOM    792  N   GLU A 155      10.634 -52.145 -39.379  1.00 19.26           N  
ANISOU  792  N   GLU A 155     3313   1894   2110    -50    116   -431       N  
ATOM    793  CA  GLU A 155      11.796 -52.772 -40.015  1.00 20.10           C  
ANISOU  793  CA  GLU A 155     3443   2390   1803    -76     46   -413       C  
ATOM    794  C   GLU A 155      13.133 -52.329 -39.400  1.00 19.80           C  
ANISOU  794  C   GLU A 155     3316   2135   2072     49    -51   -242       C  
ATOM    795  O   GLU A 155      14.143 -53.028 -39.532  1.00 21.52           O  
ANISOU  795  O   GLU A 155     3522   2311   2343     47    260   -338       O  
ATOM    796  CB  GLU A 155      11.808 -52.505 -41.526  1.00 24.14           C  
ANISOU  796  CB  GLU A 155     3899   3507   1767   -110   -207   -627       C  
ATOM    797  CG  GLU A 155      11.840 -51.051 -41.909  1.00 35.13           C  
ANISOU  797  CG  GLU A 155     5970   4474   2905   -353    652   -334       C  
ATOM    798  CD  GLU A 155      12.048 -50.847 -43.403  1.00 48.55           C  
ANISOU  798  CD  GLU A 155     8182   5561   4703   -177   1047   -599       C  
ATOM    799  OE1 GLU A 155      12.670 -51.719 -44.046  1.00 55.57           O  
ANISOU  799  OE1 GLU A 155     9095   6172   5847   -202   1734   -724       O  
ATOM    800  OE2 GLU A 155      11.590 -49.817 -43.936  1.00 52.27           O  
ANISOU  800  OE2 GLU A 155     8846   5895   5121   -268    621   -454       O  
ATOM    801  N   ASN A 156      13.142 -51.184 -38.720  1.00 17.33           N  
ANISOU  801  N   ASN A 156     2943   1901   1741    -83     77   -100       N  
ATOM    802  CA  ASN A 156      14.364 -50.668 -38.112  1.00 17.31           C  
ANISOU  802  CA  ASN A 156     2999   1908   1668     60    320    107       C  
ATOM    803  C   ASN A 156      14.443 -50.852 -36.600  1.00 16.21           C  
ANISOU  803  C   ASN A 156     2526   1763   1870     91     57     92       C  
ATOM    804  O   ASN A 156      15.433 -50.456 -35.985  1.00 17.03           O  
ANISOU  804  O   ASN A 156     2553   2030   1888     11     34     43       O  
ATOM    805  CB  ASN A 156      14.536 -49.174 -38.456  1.00 18.11           C  
ANISOU  805  CB  ASN A 156     3388   1921   1572    123    460    214       C  
ATOM    806  CG  ASN A 156      14.876 -48.958 -39.916  1.00 18.74           C  
ANISOU  806  CG  ASN A 156     3600   1646   1875    122    525    179       C  
ATOM    807  OD1 ASN A 156      15.511 -49.811 -40.539  1.00 22.13           O  
ANISOU  807  OD1 ASN A 156     3671   2044   2695    330    605     14       O  
ATOM    808  ND2 ASN A 156      14.452 -47.819 -40.473  1.00 22.18           N  
ANISOU  808  ND2 ASN A 156     4006   1996   2427    125    297    269       N  
ATOM    809  N   ARG A 157      13.408 -51.440 -36.002  1.00 15.80           N  
ANISOU  809  N   ARG A 157     2935   1615   1452     62    525     43       N  
ATOM    810  CA  ARG A 157      13.373 -51.601 -34.549  1.00 15.17           C  
ANISOU  810  CA  ARG A 157     2657   1407   1699    -46    461    120       C  
ATOM    811  C   ARG A 157      14.596 -52.378 -34.047  1.00 15.04           C  
ANISOU  811  C   ARG A 157     2592   1247   1877    141    -74      4       C  
ATOM    812  O   ARG A 157      15.243 -51.981 -33.072  1.00 15.92           O  
ANISOU  812  O   ARG A 157     2575   1653   1823     98    -83   -228       O  
ATOM    813  CB  ARG A 157      12.082 -52.298 -34.104  1.00 14.69           C  
ANISOU  813  CB  ARG A 157     2425   1831   1325   -158    207    149       C  
ATOM    814  CG  ARG A 157      11.971 -52.448 -32.601  1.00 16.53           C  
ANISOU  814  CG  ARG A 157     2338   2210   1731   -271    305    450       C  
ATOM    815  CD  ARG A 157      10.809 -53.328 -32.199  1.00 17.18           C  
ANISOU  815  CD  ARG A 157     2244   2073   2213    -76    359     57       C  
ATOM    816  NE  ARG A 157       9.477 -52.786 -32.482  1.00 17.10           N  
ANISOU  816  NE  ARG A 157     2389   1676   2432    -27    450    186       N  
ATOM    817  CZ  ARG A 157       8.773 -52.047 -31.622  1.00 17.98           C  
ANISOU  817  CZ  ARG A 157     2923   1655   2252    439    423    375       C  
ATOM    818  NH1 ARG A 157       9.303 -51.687 -30.454  1.00 18.10           N  
ANISOU  818  NH1 ARG A 157     3216   1758   1903   -108    720    125       N  
ATOM    819  NH2 ARG A 157       7.550 -51.649 -31.932  1.00 18.47           N  
ANISOU  819  NH2 ARG A 157     2868   1702   2447    267    478    168       N  
ATOM    820  N   LYS A 158      14.909 -53.497 -34.698  1.00 15.98           N  
ANISOU  820  N   LYS A 158     2639   1155   2278    106    523    -79       N  
ATOM    821  CA  LYS A 158      16.044 -54.304 -34.271  1.00 17.51           C  
ANISOU  821  CA  LYS A 158     2681   1373   2600    445    752   -194       C  
ATOM    822  C   LYS A 158      17.377 -53.562 -34.393  1.00 16.95           C  
ANISOU  822  C   LYS A 158     2700   1525   2216    183    602    205       C  
ATOM    823  O   LYS A 158      18.203 -53.616 -33.476  1.00 17.54           O  
ANISOU  823  O   LYS A 158     2639   1889   2137    117    424      8       O  
ATOM    824  CB  LYS A 158      16.108 -55.610 -35.071  1.00 18.61           C  
ANISOU  824  CB  LYS A 158     2847   1423   2800    589    676   -416       C  
ATOM    825  CG  LYS A 158      17.211 -56.546 -34.599  1.00 20.90           C  
ANISOU  825  CG  LYS A 158     3034   1420   3488    686    221   -432       C  
ATOM    826  CD  LYS A 158      17.199 -57.864 -35.339  1.00 26.59           C  
ANISOU  826  CD  LYS A 158     3637   1741   4724    818    115   -228       C  
ATOM    827  CE  LYS A 158      18.284 -58.790 -34.810  1.00 34.77           C  
ANISOU  827  CE  LYS A 158     4280   2490   6440    562    346   -398       C  
ATOM    828  NZ  LYS A 158      19.654 -58.222 -34.965  1.00 37.81           N  
ANISOU  828  NZ  LYS A 158     4098   3006   7262    677    131   -553       N  
ATOM    829  N   ALA A 159      17.588 -52.865 -35.512  1.00 16.39           N  
ANISOU  829  N   ALA A 159     2558   1907   1763    -56    671   -150       N  
ATOM    830  CA  ALA A 159      18.846 -52.138 -35.702  1.00 17.86           C  
ANISOU  830  CA  ALA A 159     2803   2022   1961   -130    977   -342       C  
ATOM    831  C   ALA A 159      19.042 -51.084 -34.606  1.00 16.10           C  
ANISOU  831  C   ALA A 159     2390   1782   1945    133    768   -327       C  
ATOM    832  O   ALA A 159      20.160 -50.879 -34.116  1.00 18.14           O  
ANISOU  832  O   ALA A 159     2647   1968   2277     69    493    -44       O  
ATOM    833  CB  ALA A 159      18.891 -51.481 -37.071  1.00 19.87           C  
ANISOU  833  CB  ALA A 159     3444   2255   1849    -83    805    -29       C  
ATOM    834  N   VAL A 160      17.955 -50.419 -34.227  1.00 14.35           N  
ANISOU  834  N   VAL A 160     2325   1445   1683    -21    321     49       N  
ATOM    835  CA  VAL A 160      18.030 -49.436 -33.164  1.00 15.99           C  
ANISOU  835  CA  VAL A 160     2755   1434   1885    304    487    -27       C  
ATOM    836  C   VAL A 160      18.394 -50.103 -31.834  1.00 15.12           C  
ANISOU  836  C   VAL A 160     2445   1394   1907    -22    532   -111       C  
ATOM    837  O   VAL A 160      19.314 -49.664 -31.139  1.00 15.10           O  
ANISOU  837  O   VAL A 160     2436   1539   1763    -53    294   -150       O  
ATOM    838  CB  VAL A 160      16.701 -48.661 -33.030  1.00 15.16           C  
ANISOU  838  CB  VAL A 160     2546   1494   1719    439    289   -205       C  
ATOM    839  CG1 VAL A 160      16.686 -47.806 -31.757  1.00 17.17           C  
ANISOU  839  CG1 VAL A 160     2756   1528   2241     37    260   -339       C  
ATOM    840  CG2 VAL A 160      16.475 -47.796 -34.282  1.00 17.07           C  
ANISOU  840  CG2 VAL A 160     2799   1698   1988   -203   -313    290       C  
ATOM    841  N   SER A 161      17.701 -51.181 -31.478  1.00 14.42           N  
ANISOU  841  N   SER A 161     2213   1456   1811    183    484    125       N  
ATOM    842  CA ASER A 161      17.996 -51.836 -30.210  0.29 14.21           C  
ANISOU  842  CA ASER A 161     2139   1696   1564     18    222    107       C  
ATOM    843  CA BSER A 161      17.992 -51.863 -30.223  0.38 14.76           C  
ANISOU  843  CA BSER A 161     1969   1859   1778     37    234    342       C  
ATOM    844  CA CSER A 161      17.972 -51.895 -30.238  0.32 14.73           C  
ANISOU  844  CA CSER A 161     2056   1609   1930     39    133    312       C  
ATOM    845  C   SER A 161      19.392 -52.466 -30.220  1.00 13.44           C  
ANISOU  845  C   SER A 161     1862   1614   1631     73    113    134       C  
ATOM    846  O   SER A 161      20.069 -52.459 -29.193  1.00 14.42           O  
ANISOU  846  O   SER A 161     2129   1637   1715    156    132     54       O  
ATOM    847  CB ASER A 161      16.933 -52.883 -29.867  0.29 15.45           C  
ANISOU  847  CB ASER A 161     2380   2057   1434     12    482      0       C  
ATOM    848  CB BSER A 161      16.954 -52.944 -29.940  0.38 17.10           C  
ANISOU  848  CB BSER A 161     1878   2584   2034     63    508    588       C  
ATOM    849  CB CSER A 161      16.946 -53.011 -30.045  0.32 17.18           C  
ANISOU  849  CB CSER A 161     2188   1844   2495      8    166    526       C  
ATOM    850  OG ASER A 161      16.835 -53.874 -30.867  0.29 16.36           O  
ANISOU  850  OG ASER A 161     2744   2074   1399    -33    654   -365       O  
ATOM    851  OG BSER A 161      15.785 -52.362 -29.400  0.38 18.72           O  
ANISOU  851  OG BSER A 161     1853   2932   2329      4    616    732       O  
ATOM    852  OG CSER A 161      17.139 -53.677 -28.814  0.32 18.22           O  
ANISOU  852  OG CSER A 161     2356   1749   2818   -127      4    709       O  
ATOM    853  N   ASP A 162      19.842 -52.973 -31.373  1.00 15.72           N  
ANISOU  853  N   ASP A 162     2386   1408   2179    167    739     74       N  
ATOM    854  CA  ASP A 162      21.199 -53.530 -31.467  1.00 16.84           C  
ANISOU  854  CA  ASP A 162     2675   1418   2305     68    642     93       C  
ATOM    855  C   ASP A 162      22.274 -52.465 -31.240  1.00 16.40           C  
ANISOU  855  C   ASP A 162     2313   1382   2537    504    514   -154       C  
ATOM    856  O   ASP A 162      23.251 -52.689 -30.536  1.00 17.04           O  
ANISOU  856  O   ASP A 162     2255   1869   2352    254    474    205       O  
ATOM    857  CB  ASP A 162      21.451 -54.180 -32.831  1.00 17.80           C  
ANISOU  857  CB  ASP A 162     2990   1451   2323    274    701   -441       C  
ATOM    858  CG  ASP A 162      20.733 -55.507 -33.008  1.00 21.75           C  
ANISOU  858  CG  ASP A 162     3332   2185   2747    325    663   -507       C  
ATOM    859  OD1 ASP A 162      20.266 -56.102 -32.010  1.00 23.88           O  
ANISOU  859  OD1 ASP A 162     3713   2311   3048    303    389   -286       O  
ATOM    860  OD2 ASP A 162      20.648 -55.955 -34.171  1.00 23.55           O  
ANISOU  860  OD2 ASP A 162     3440   2540   2969    484    363   -489       O  
ATOM    861  N   GLN A 163      22.085 -51.299 -31.843  1.00 15.35           N  
ANISOU  861  N   GLN A 163     2142   1488   2201    177    602   -330       N  
ATOM    862  CA  GLN A 163      23.041 -50.221 -31.685  1.00 15.48           C  
ANISOU  862  CA  GLN A 163     2087   1760   2034    220    468    -83       C  
ATOM    863  C   GLN A 163      23.066 -49.751 -30.232  1.00 13.49           C  
ANISOU  863  C   GLN A 163     1723   1616   1786     13    359    -44       C  
ATOM    864  O   GLN A 163      24.131 -49.526 -29.654  1.00 15.16           O  
ANISOU  864  O   GLN A 163     1851   2037   1874     70    407     93       O  
ATOM    865  CB  GLN A 163      22.698 -49.072 -32.635  1.00 16.30           C  
ANISOU  865  CB  GLN A 163     2245   1722   2227    107    293    308       C  
ATOM    866  CG  GLN A 163      23.472 -47.768 -32.383  1.00 16.32           C  
ANISOU  866  CG  GLN A 163     2185   1639   2376   -194    623    107       C  
ATOM    867  CD  GLN A 163      24.977 -47.889 -32.601  1.00 18.23           C  
ANISOU  867  CD  GLN A 163     2529   1759   2641   -117    825    437       C  
ATOM    868  OE1 GLN A 163      25.475 -48.859 -33.194  1.00 20.25           O  
ANISOU  868  OE1 GLN A 163     2691   2256   2747     89    978    167       O  
ATOM    869  NE2 GLN A 163      25.713 -46.886 -32.128  1.00 17.87           N  
ANISOU  869  NE2 GLN A 163     2357   1815   2620   -147    561    319       N  
ATOM    870  N   LEU A 164      21.889 -49.599 -29.644  1.00 14.28           N  
ANISOU  870  N   LEU A 164     1949   1695   1781    200    659   -118       N  
ATOM    871  CA  LEU A 164      21.816 -49.184 -28.246  1.00 14.39           C  
ANISOU  871  CA  LEU A 164     1862   1471   2135    290    693    -67       C  
ATOM    872  C   LEU A 164      22.495 -50.221 -27.343  1.00 14.61           C  
ANISOU  872  C   LEU A 164     1835   1649   2069    302    147     11       C  
ATOM    873  O   LEU A 164      23.225 -49.858 -26.420  1.00 15.07           O  
ANISOU  873  O   LEU A 164     1839   1878   2007    270    371    152       O  
ATOM    874  CB  LEU A 164      20.362 -48.957 -27.832  1.00 13.32           C  
ANISOU  874  CB  LEU A 164     1410   1505   2147    299    524    154       C  
ATOM    875  CG  LEU A 164      19.716 -47.713 -28.464  1.00 13.86           C  
ANISOU  875  CG  LEU A 164     1811   1446   2009    200    275     62       C  
ATOM    876  CD1 LEU A 164      18.258 -47.600 -28.062  1.00 14.32           C  
ANISOU  876  CD1 LEU A 164     1720   1748   1975    187    416     35       C  
ATOM    877  CD2 LEU A 164      20.475 -46.425 -28.100  1.00 15.44           C  
ANISOU  877  CD2 LEU A 164     2172   1245   2451     61    368    103       C  
ATOM    878  N   LYS A 165      22.263 -51.506 -27.624  1.00 14.65           N  
ANISOU  878  N   LYS A 165     1862   1655   2051    417    315     30       N  
ATOM    879  CA  LYS A 165      22.789 -52.579 -26.783  1.00 14.99           C  
ANISOU  879  CA  LYS A 165     1928   1382   2385    526     43    100       C  
ATOM    880  C   LYS A 165      24.326 -52.594 -26.758  1.00 16.19           C  
ANISOU  880  C   LYS A 165     1837   1874   2441    581    222     56       C  
ATOM    881  O   LYS A 165      24.922 -52.865 -25.720  1.00 16.77           O  
ANISOU  881  O   LYS A 165     2093   1931   2349    520    160    223       O  
ATOM    882  CB  LYS A 165      22.257 -53.942 -27.262  1.00 15.97           C  
ANISOU  882  CB  LYS A 165     2447   1341   2280    271    -57    302       C  
ATOM    883  CG  LYS A 165      22.795 -55.150 -26.504  1.00 19.03           C  
ANISOU  883  CG  LYS A 165     2728   1884   2619    510    124    790       C  
ATOM    884  CD  LYS A 165      22.446 -55.126 -25.020  1.00 21.23           C  
ANISOU  884  CD  LYS A 165     3026   2271   2770    607    341   1279       C  
ATOM    885  CE  LYS A 165      22.759 -56.483 -24.371  1.00 22.72           C  
ANISOU  885  CE  LYS A 165     2992   2834   2805    926    430   1136       C  
ATOM    886  NZ  LYS A 165      22.534 -56.527 -22.897  1.00 24.22           N  
ANISOU  886  NZ  LYS A 165     3151   3011   3041    728    590   1135       N  
ATOM    887  N   LYS A 166      24.960 -52.298 -27.894  1.00 16.68           N  
ANISOU  887  N   LYS A 166     1666   2155   2517    348    621     12       N  
ATOM    888  CA  LYS A 166      26.419 -52.211 -27.945  1.00 18.01           C  
ANISOU  888  CA  LYS A 166     2105   2418   2319    442    374     29       C  
ATOM    889  C   LYS A 166      26.923 -51.277 -26.857  1.00 17.36           C  
ANISOU  889  C   LYS A 166     2006   2105   2484    410     64     89       C  
ATOM    890  O   LYS A 166      27.971 -51.512 -26.254  1.00 21.18           O  
ANISOU  890  O   LYS A 166     2503   2479   3066    495     71     70       O  
ATOM    891  CB  LYS A 166      26.905 -51.706 -29.310  1.00 20.42           C  
ANISOU  891  CB  LYS A 166     2893   2615   2250    548    687    521       C  
ATOM    892  CG  LYS A 166      26.703 -52.659 -30.462  1.00 29.71           C  
ANISOU  892  CG  LYS A 166     3869   4056   3365    683   1232    439       C  
ATOM    893  CD  LYS A 166      27.227 -52.063 -31.768  1.00 36.53           C  
ANISOU  893  CD  LYS A 166     4931   4906   4043   1244   1964    695       C  
ATOM    894  CE  LYS A 166      27.075 -53.050 -32.915  1.00 43.30           C  
ANISOU  894  CE  LYS A 166     5871   5694   4888   1028   2353    881       C  
ATOM    895  NZ  LYS A 166      27.541 -52.488 -34.210  1.00 45.66           N  
ANISOU  895  NZ  LYS A 166     6364   5919   5065   1059   2506   1141       N  
ATOM    896  N   HIS A 167      26.152 -50.224 -26.602  1.00 16.68           N  
ANISOU  896  N   HIS A 167     2152   1930   2254    269    606     95       N  
ATOM    897  CA  HIS A 167      26.550 -49.217 -25.633  1.00 15.48           C  
ANISOU  897  CA  HIS A 167     1927   1694   2260    214    353    378       C  
ATOM    898  C   HIS A 167      25.926 -49.376 -24.257  1.00 15.57           C  
ANISOU  898  C   HIS A 167     1925   1873   2119    -30    338    224       C  
ATOM    899  O   HIS A 167      26.114 -48.518 -23.390  1.00 17.61           O  
ANISOU  899  O   HIS A 167     2302   2128   2261    187    514    170       O  
ATOM    900  CB  HIS A 167      26.236 -47.838 -26.200  1.00 15.46           C  
ANISOU  900  CB  HIS A 167     1894   1791   2191    397    561    665       C  
ATOM    901  CG  HIS A 167      27.070 -47.503 -27.394  1.00 16.56           C  
ANISOU  901  CG  HIS A 167     2002   2103   2189     67    690    720       C  
ATOM    902  ND1 HIS A 167      28.220 -46.748 -27.305  1.00 20.57           N  
ANISOU  902  ND1 HIS A 167     2186   2416   3215   -361    741    499       N  
ATOM    903  CD2 HIS A 167      26.952 -47.863 -28.696  1.00 17.62           C  
ANISOU  903  CD2 HIS A 167     2124   2324   2246    128    607    817       C  
ATOM    904  CE1 HIS A 167      28.760 -46.635 -28.505  1.00 19.72           C  
ANISOU  904  CE1 HIS A 167     2043   2414   3035   -337    594    722       C  
ATOM    905  NE2 HIS A 167      28.014 -47.308 -29.366  1.00 19.65           N  
ANISOU  905  NE2 HIS A 167     2180   2379   2907   -138    339    632       N  
ATOM    906  N   GLY A 168      25.194 -50.467 -24.054  1.00 15.42           N  
ANISOU  906  N   GLY A 168     2071   1825   1964    265    560    493       N  
ATOM    907  CA  GLY A 168      24.596 -50.752 -22.762  1.00 15.32           C  
ANISOU  907  CA  GLY A 168     1693   1867   2261    197    167    157       C  
ATOM    908  C   GLY A 168      23.209 -50.170 -22.556  1.00 14.46           C  
ANISOU  908  C   GLY A 168     1565   1624   2305    187    125    366       C  
ATOM    909  O   GLY A 168      22.627 -50.340 -21.474  1.00 14.91           O  
ANISOU  909  O   GLY A 168     1840   1699   2127    222    284    305       O  
ATOM    910  N   PHE A 169      22.667 -49.488 -23.571  1.00 13.99           N  
ANISOU  910  N   PHE A 169     1591   1333   2392    476    100    459       N  
ATOM    911  CA  PHE A 169      21.333 -48.903 -23.453  1.00 13.51           C  
ANISOU  911  CA  PHE A 169     1643   1525   1965    266    133    418       C  
ATOM    912  C   PHE A 169      20.237 -49.859 -23.868  1.00 13.45           C  
ANISOU  912  C   PHE A 169     1739   1728   1645    384    494    184       C  
ATOM    913  O   PHE A 169      20.411 -50.647 -24.805  1.00 14.66           O  
ANISOU  913  O   PHE A 169     2052   1697   1820    245    433     20       O  
ATOM    914  CB  PHE A 169      21.201 -47.640 -24.309  1.00 14.94           C  
ANISOU  914  CB  PHE A 169     1826   1643   2206    361    -39    611       C  
ATOM    915  CG  PHE A 169      22.009 -46.483 -23.819  1.00 16.47           C  
ANISOU  915  CG  PHE A 169     2090   1520   2649    254   -316    107       C  
ATOM    916  CD1 PHE A 169      21.574 -45.715 -22.750  1.00 18.63           C  
ANISOU  916  CD1 PHE A 169     2826   1711   2542    703   -512    -91       C  
ATOM    917  CD2 PHE A 169      23.213 -46.162 -24.427  1.00 17.40           C  
ANISOU  917  CD2 PHE A 169     2371   1686   2556   -183   -495    622       C  
ATOM    918  CE1 PHE A 169      22.320 -44.628 -22.307  1.00 19.93           C  
ANISOU  918  CE1 PHE A 169     3450   1741   2381    500   -439    243       C  
ATOM    919  CE2 PHE A 169      23.965 -45.076 -23.982  1.00 20.18           C  
ANISOU  919  CE2 PHE A 169     3264   1787   2614    154   -490    682       C  
ATOM    920  CZ  PHE A 169      23.518 -44.325 -22.908  1.00 21.56           C  
ANISOU  920  CZ  PHE A 169     3788   1558   2845    211   -536    490       C  
ATOM    921  N   LYS A 170      19.098 -49.760 -23.178  1.00 14.19           N  
ANISOU  921  N   LYS A 170     1539   2026   1826     84    479    181       N  
ATOM    922  CA  LYS A 170      17.900 -50.509 -23.549  1.00 15.04           C  
ANISOU  922  CA  LYS A 170     1506   1808   2399    -24    241    313       C  
ATOM    923  C   LYS A 170      16.687 -49.605 -23.409  1.00 13.65           C  
ANISOU  923  C   LYS A 170     1553   1761   1873    202   -138    269       C  
ATOM    924  O   LYS A 170      16.435 -49.052 -22.339  1.00 16.01           O  
ANISOU  924  O   LYS A 170     2061   2217   1803    295    179     65       O  
ATOM    925  CB  LYS A 170      17.728 -51.765 -22.688  1.00 17.25           C  
ANISOU  925  CB  LYS A 170     2135   1695   2724    113    626    133       C  
ATOM    926  CG  LYS A 170      16.517 -52.608 -23.078  1.00 18.99           C  
ANISOU  926  CG  LYS A 170     2374   1377   3462   -194    343    525       C  
ATOM    927  CD  LYS A 170      16.389 -53.829 -22.193  1.00 22.69           C  
ANISOU  927  CD  LYS A 170     2675   1717   4230   -416    259    495       C  
ATOM    928  CE  LYS A 170      15.147 -54.627 -22.530  1.00 28.33           C  
ANISOU  928  CE  LYS A 170     4019   1950   4796   -710    580    659       C  
ATOM    929  NZ  LYS A 170      15.086 -55.833 -21.667  1.00 35.09           N  
ANISOU  929  NZ  LYS A 170     4908   2852   5573   -725    660    548       N  
ATOM    930  N   LEU A 171      15.950 -49.430 -24.493  1.00 13.41           N  
ANISOU  930  N   LEU A 171     1560   1731   1806    123   -108    354       N  
ATOM    931  CA  LEU A 171      14.742 -48.613 -24.447  1.00 13.39           C  
ANISOU  931  CA  LEU A 171     1695   1812   1580    -17     35    232       C  
ATOM    932  C   LEU A 171      13.753 -49.207 -23.464  1.00 14.51           C  
ANISOU  932  C   LEU A 171     1940   1750   1824    254    317    424       C  
ATOM    933  O   LEU A 171      13.613 -50.438 -23.363  1.00 16.17           O  
ANISOU  933  O   LEU A 171     2176   1503   2465     50    443    396       O  
ATOM    934  CB  LEU A 171      14.104 -48.511 -25.830  1.00 14.73           C  
ANISOU  934  CB  LEU A 171     2041   1965   1589   -164    358    404       C  
ATOM    935  CG  LEU A 171      14.963 -47.749 -26.845  1.00 13.67           C  
ANISOU  935  CG  LEU A 171     2052   1592   1548    -82    457     96       C  
ATOM    936  CD1 LEU A 171      14.399 -47.913 -28.253  1.00 20.04           C  
ANISOU  936  CD1 LEU A 171     2810   2920   1886   -259    433    -56       C  
ATOM    937  CD2 LEU A 171      15.073 -46.269 -26.480  1.00 17.00           C  
ANISOU  937  CD2 LEU A 171     2737   1517   2207     34    458     86       C  
ATOM    938  N   GLY A 172      13.072 -48.332 -22.737  1.00 14.06           N  
ANISOU  938  N   GLY A 172     1761   1700   1879    201    684    436       N  
ATOM    939  CA  GLY A 172      12.088 -48.771 -21.773  1.00 14.50           C  
ANISOU  939  CA  GLY A 172     1693   1741   2074     25    587    324       C  
ATOM    940  C   GLY A 172      10.755 -48.083 -21.967  1.00 13.94           C  
ANISOU  940  C   GLY A 172     2054   1504   1739    -70    451    329       C  
ATOM    941  O   GLY A 172      10.555 -47.330 -22.922  1.00 14.63           O  
ANISOU  941  O   GLY A 172     2016   1670   1872   -218    444    283       O  
ATOM    942  N   PRO A 173       9.832 -48.330 -21.038  1.00 13.00           N  
ANISOU  942  N   PRO A 173     1961   1414   1563    -69     90    299       N  
ATOM    943  CA  PRO A 173       8.457 -47.867 -21.174  1.00 14.09           C  
ANISOU  943  CA  PRO A 173     1831   1508   2015   -310     17    247       C  
ATOM    944  C   PRO A 173       8.124 -46.618 -20.365  1.00 13.26           C  
ANISOU  944  C   PRO A 173     1877   1659   1503   -169    -88     97       C  
ATOM    945  O   PRO A 173       6.946 -46.305 -20.234  1.00 14.93           O  
ANISOU  945  O   PRO A 173     1856   1961   1856   -199    156     36       O  
ATOM    946  CB  PRO A 173       7.661 -49.059 -20.653  1.00 14.77           C  
ANISOU  946  CB  PRO A 173     2010   1709   1892   -291    265    268       C  
ATOM    947  CG  PRO A 173       8.535 -49.549 -19.495  1.00 15.74           C  
ANISOU  947  CG  PRO A 173     1971   1879   2130     45    454    624       C  
ATOM    948  CD  PRO A 173       9.967 -49.367 -19.997  1.00 15.17           C  
ANISOU  948  CD  PRO A 173     1906   1770   2086    103    448   1037       C  
ATOM    949  N   ALA A 174       9.120 -45.904 -19.846  1.00 13.61           N  
ANISOU  949  N   ALA A 174     2287   1294   1592    -77   -131    142       N  
ATOM    950  CA  ALA A 174       8.818 -44.728 -19.020  1.00 14.54           C  
ANISOU  950  CA  ALA A 174     2116   1492   1916     66    -73   -330       C  
ATOM    951  C   ALA A 174       8.259 -43.610 -19.878  1.00 14.81           C  
ANISOU  951  C   ALA A 174     2029   1512   2086   -108    369    188       C  
ATOM    952  O   ALA A 174       8.848 -43.262 -20.900  1.00 14.76           O  
ANISOU  952  O   ALA A 174     2385   1469   1755    -89    417     97       O  
ATOM    953  CB  ALA A 174      10.047 -44.248 -18.287  1.00 16.85           C  
ANISOU  953  CB  ALA A 174     2418   1756   2230    -38   -617   -166       C  
ATOM    954  N   PRO A 175       7.118 -43.038 -19.461  1.00 14.43           N  
ANISOU  954  N   PRO A 175     1970   1679   1833    -47    441   -115       N  
ATOM    955  CA  PRO A 175       6.540 -41.901 -20.190  1.00 15.46           C  
ANISOU  955  CA  PRO A 175     2037   1549   2289    153    301    327       C  
ATOM    956  C   PRO A 175       7.208 -40.572 -19.885  1.00 17.88           C  
ANISOU  956  C   PRO A 175     2359   1807   2629   -221    334     27       C  
ATOM    957  O   PRO A 175       8.019 -40.490 -18.957  1.00 18.57           O  
ANISOU  957  O   PRO A 175     2739   1781   2536    -23    477   -279       O  
ATOM    958  CB  PRO A 175       5.095 -41.882 -19.707  1.00 17.62           C  
ANISOU  958  CB  PRO A 175     2200   2185   2310   -290    505     15       C  
ATOM    959  CG  PRO A 175       5.161 -42.452 -18.337  1.00 19.00           C  
ANISOU  959  CG  PRO A 175     2435   2698   2087    202    646     12       C  
ATOM    960  CD  PRO A 175       6.261 -43.475 -18.344  1.00 16.78           C  
ANISOU  960  CD  PRO A 175     2147   2024   2203    224    620   -139       C  
ATOM    961  N   LYS A 176       6.851 -39.545 -20.656  1.00 19.57           N  
ANISOU  961  N   LYS A 176     2686   1906   2843   -205    330    -47       N  
ATOM    962  CA  LYS A 176       7.315 -38.185 -20.391  1.00 25.11           C  
ANISOU  962  CA  LYS A 176     3795   2021   3722   -432    431   -274       C  
ATOM    963  C   LYS A 176       6.898 -37.702 -19.012  1.00 33.11           C  
ANISOU  963  C   LYS A 176     4746   2571   5265   -199   1534  -1079       C  
ATOM    964  O   LYS A 176       7.596 -36.905 -18.388  1.00 37.46           O  
ANISOU  964  O   LYS A 176     5176   3096   5959   -973   1921  -1568       O  
ATOM    965  CB  LYS A 176       6.777 -37.212 -21.438  1.00 28.58           C  
ANISOU  965  CB  LYS A 176     4284   2161   4413   -551    427    277       C  
ATOM    966  CG  LYS A 176       7.384 -37.348 -22.796  1.00 29.60           C  
ANISOU  966  CG  LYS A 176     4474   2607   4168   -146     33    721       C  
ATOM    967  CD  LYS A 176       6.921 -36.190 -23.689  1.00 32.98           C  
ANISOU  967  CD  LYS A 176     5081   3123   4326    372   -469    874       C  
ATOM    968  CE  LYS A 176       5.702 -36.554 -24.508  1.00 37.83           C  
ANISOU  968  CE  LYS A 176     5955   3579   4840    150    366    294       C  
ATOM    969  NZ  LYS A 176       6.062 -37.547 -25.558  1.00 40.97           N  
ANISOU  969  NZ  LYS A 176     6583   3830   5154    328    778    122       N  
ATOM    970  N   THR A 177       5.742 -38.164 -18.551  1.00 37.30           N  
ANISOU  970  N   THR A 177     5091   3067   6013     99   2125  -1111       N  
ATOM    971  CA  THR A 177       5.240 -37.766 -17.239  1.00 43.01           C  
ANISOU  971  CA  THR A 177     5885   3913   6544    547   2123   -720       C  
ATOM    972  C   THR A 177       4.589 -38.926 -16.495  1.00 45.33           C  
ANISOU  972  C   THR A 177     6156   3942   7127   1277   2062   -345       C  
ATOM    973  O   THR A 177       3.754 -39.645 -17.047  1.00 48.07           O  
ANISOU  973  O   THR A 177     6193   4380   7693   1823   2340    111       O  
ATOM    974  CB  THR A 177       4.227 -36.611 -17.350  1.00 47.29           C  
ANISOU  974  CB  THR A 177     6809   4633   6527    506   2262    -50       C  
ATOM    975  OG1 THR A 177       3.576 -36.427 -16.088  1.00 48.87           O  
ANISOU  975  OG1 THR A 177     7505   4760   6302    797   2162    652       O  
ATOM    976  CG2 THR A 177       3.175 -36.908 -18.417  1.00 49.09           C  
ANISOU  976  CG2 THR A 177     7039   4861   6751    330   2052    -47       C  
TER     977      THR A 177                                                      
ATOM    978  N   ASP B  56      20.675 -58.961   5.533  1.00 63.74           N  
ANISOU  978  N   ASP B  56     8162   9243   6814   1361    -94   1688       N  
ATOM    979  CA  ASP B  56      20.206 -60.228   4.982  1.00 61.63           C  
ANISOU  979  CA  ASP B  56     7913   8936   6567   1622     11   1991       C  
ATOM    980  C   ASP B  56      19.167 -60.006   3.882  1.00 53.60           C  
ANISOU  980  C   ASP B  56     7030   7868   5466   1657     54   2186       C  
ATOM    981  O   ASP B  56      18.968 -60.862   3.015  1.00 54.29           O  
ANISOU  981  O   ASP B  56     7403   7889   5334   2050    263   2416       O  
ATOM    982  CB  ASP B  56      19.622 -61.108   6.085  1.00 66.04           C  
ANISOU  982  CB  ASP B  56     8336   9467   7290   1762    138   2053       C  
ATOM    983  CG  ASP B  56      19.338 -62.521   5.612  1.00 70.56           C  
ANISOU  983  CG  ASP B  56     8609  10006   8196   1769    375   1785       C  
ATOM    984  OD1 ASP B  56      20.243 -63.377   5.716  1.00 72.14           O  
ANISOU  984  OD1 ASP B  56     8764  10135   8512   1882    383   1757       O  
ATOM    985  OD2 ASP B  56      18.212 -62.774   5.134  1.00 72.06           O  
ANISOU  985  OD2 ASP B  56     8635  10214   8530   1715    582   1710       O  
ATOM    986  N   SER B  57      18.495 -58.859   3.929  1.00 42.21           N  
ANISOU  986  N   SER B  57     5409   6477   4153   1184   -261   2147       N  
ATOM    987  CA ASER B  57      17.526 -58.505   2.900  0.55 36.26           C  
ANISOU  987  CA ASER B  57     4581   5669   3527    892   -265   2218       C  
ATOM    988  CA BSER B  57      17.525 -58.505   2.900  0.45 35.85           C  
ANISOU  988  CA BSER B  57     4415   5612   3595    897   -516   2187       C  
ATOM    989  C   SER B  57      18.239 -58.106   1.613  1.00 32.01           C  
ANISOU  989  C   SER B  57     3728   4945   3491    301   -512   1701       C  
ATOM    990  O   SER B  57      19.312 -57.501   1.648  1.00 33.65           O  
ANISOU  990  O   SER B  57     4125   5281   3380   -456   -625    896       O  
ATOM    991  CB ASER B  57      16.617 -57.370   3.378  0.55 37.87           C  
ANISOU  991  CB ASER B  57     4990   5841   3559    753    546   2077       C  
ATOM    992  CB BSER B  57      16.616 -57.367   3.375  0.45 36.80           C  
ANISOU  992  CB BSER B  57     4497   5672   3813    764   -162   1959       C  
ATOM    993  OG ASER B  57      15.749 -57.803   4.411  0.55 38.98           O  
ANISOU  993  OG ASER B  57     5388   6047   3374    920   1039   1906       O  
ATOM    994  OG BSER B  57      17.233 -56.103   3.194  0.45 36.76           O  
ANISOU  994  OG BSER B  57     4522   5740   3707    939   -207   1807       O  
ATOM    995  N   VAL B  58      17.643 -58.455   0.480  1.00 23.02           N  
ANISOU  995  N   VAL B  58     2570   3270   2905    175   -319   1609       N  
ATOM    996  CA  VAL B  58      18.193 -58.097  -0.823  1.00 20.43           C  
ANISOU  996  CA  VAL B  58     2144   2512   3106    241   -193    820       C  
ATOM    997  C   VAL B  58      17.242 -57.166  -1.585  1.00 17.94           C  
ANISOU  997  C   VAL B  58     2076   2033   2708    202   -176    651       C  
ATOM    998  O   VAL B  58      16.035 -57.089  -1.309  1.00 18.27           O  
ANISOU  998  O   VAL B  58     2245   2025   2670    243    232    894       O  
ATOM    999  CB  VAL B  58      18.481 -59.345  -1.701  1.00 24.02           C  
ANISOU  999  CB  VAL B  58     2625   2794   3709    525   -329   1110       C  
ATOM   1000  CG1 VAL B  58      19.473 -60.275  -1.012  1.00 25.52           C  
ANISOU 1000  CG1 VAL B  58     3031   2846   3819    398   -120   1209       C  
ATOM   1001  CG2 VAL B  58      17.194 -60.076  -2.046  1.00 25.29           C  
ANISOU 1001  CG2 VAL B  58     3065   2610   3935    285   -213    555       C  
ATOM   1002  N   LEU B  59      17.796 -56.462  -2.557  1.00 17.41           N  
ANISOU 1002  N   LEU B  59     2407   2016   2191     57    -69    693       N  
ATOM   1003  CA  LEU B  59      17.029 -55.533  -3.376  1.00 16.53           C  
ANISOU 1003  CA  LEU B  59     2125   1920   2237     68     17    893       C  
ATOM   1004  C   LEU B  59      16.088 -56.242  -4.349  1.00 15.97           C  
ANISOU 1004  C   LEU B  59     1848   1768   2453     -9   -179    850       C  
ATOM   1005  O   LEU B  59      16.519 -57.123  -5.097  1.00 17.64           O  
ANISOU 1005  O   LEU B  59     2459   1798   2447    187    106    538       O  
ATOM   1006  CB  LEU B  59      18.000 -54.638  -4.146  1.00 16.61           C  
ANISOU 1006  CB  LEU B  59     2175   1830   2305   -268    446   1059       C  
ATOM   1007  CG  LEU B  59      17.398 -53.624  -5.115  1.00 17.30           C  
ANISOU 1007  CG  LEU B  59     2267   1615   2691     72    452   1079       C  
ATOM   1008  CD1 LEU B  59      16.552 -52.585  -4.366  1.00 18.27           C  
ANISOU 1008  CD1 LEU B  59     2437   1710   2794    297    262     98       C  
ATOM   1009  CD2 LEU B  59      18.501 -52.945  -5.923  1.00 20.58           C  
ANISOU 1009  CD2 LEU B  59     2586   2214   3019   -183    812   1193       C  
ATOM   1010  N   PHE B  60      14.809 -55.863  -4.336  1.00 15.30           N  
ANISOU 1010  N   PHE B  60     1570   1821   2422     95    -29    648       N  
ATOM   1011  CA  PHE B  60      13.822 -56.425  -5.267  1.00 14.33           C  
ANISOU 1011  CA  PHE B  60     1629   1749   2065    -34    143    759       C  
ATOM   1012  C   PHE B  60      13.534 -55.488  -6.441  1.00 15.26           C  
ANISOU 1012  C   PHE B  60     1839   1636   2322    -45    254    542       C  
ATOM   1013  O   PHE B  60      13.109 -55.938  -7.509  1.00 16.66           O  
ANISOU 1013  O   PHE B  60     2128   1923   2279    126    360    559       O  
ATOM   1014  CB  PHE B  60      12.488 -56.722  -4.566  1.00 14.85           C  
ANISOU 1014  CB  PHE B  60     1837   1667   2137   -109    412    793       C  
ATOM   1015  CG  PHE B  60      12.527 -57.856  -3.581  1.00 15.25           C  
ANISOU 1015  CG  PHE B  60     2203   1514   2080    115    154    485       C  
ATOM   1016  CD1 PHE B  60      13.553 -58.792  -3.575  1.00 16.27           C  
ANISOU 1016  CD1 PHE B  60     2630   1395   2156    -54    -83    506       C  
ATOM   1017  CD2 PHE B  60      11.467 -58.015  -2.699  1.00 16.91           C  
ANISOU 1017  CD2 PHE B  60     2198   1718   2509    253    481    714       C  
ATOM   1018  CE1 PHE B  60      13.533 -59.852  -2.657  1.00 16.93           C  
ANISOU 1018  CE1 PHE B  60     2266   1759   2410    203    178    213       C  
ATOM   1019  CE2 PHE B  60      11.440 -59.055  -1.794  1.00 16.98           C  
ANISOU 1019  CE2 PHE B  60     2154   1700   2597   -168    129    554       C  
ATOM   1020  CZ  PHE B  60      12.469 -59.982  -1.774  1.00 18.04           C  
ANISOU 1020  CZ  PHE B  60     2286   1811   2758    537     66    396       C  
ATOM   1021  N   GLY B  61      13.742 -54.187  -6.240  1.00 14.94           N  
ANISOU 1021  N   GLY B  61     2098   1391   2188    266    128    621       N  
ATOM   1022  CA  GLY B  61      13.416 -53.202  -7.261  1.00 15.57           C  
ANISOU 1022  CA  GLY B  61     1877   1746   2292    551    317    603       C  
ATOM   1023  C   GLY B  61      12.604 -52.048  -6.722  1.00 15.87           C  
ANISOU 1023  C   GLY B  61     2361   1308   2361    413    499    509       C  
ATOM   1024  O   GLY B  61      12.395 -51.950  -5.510  1.00 16.14           O  
ANISOU 1024  O   GLY B  61     2683   1494   1954    315    382    237       O  
ATOM   1025  N   SER B  62      12.111 -51.205  -7.622  1.00 14.32           N  
ANISOU 1025  N   SER B  62     2222   1254   1965    494    414    179       N  
ATOM   1026  CA  SER B  62      11.376 -50.006  -7.233  1.00 13.38           C  
ANISOU 1026  CA  SER B  62     2204    991   1887    217     73    144       C  
ATOM   1027  C   SER B  62      10.029 -49.869  -7.944  1.00 13.47           C  
ANISOU 1027  C   SER B  62     2201   1360   1555    294    160    142       C  
ATOM   1028  O   SER B  62       9.792 -50.484  -8.980  1.00 14.63           O  
ANISOU 1028  O   SER B  62     2506   1395   1656    306    267   -181       O  
ATOM   1029  CB  SER B  62      12.212 -48.760  -7.503  1.00 15.31           C  
ANISOU 1029  CB  SER B  62     2609   1296   1913    -28    364    129       C  
ATOM   1030  OG  SER B  62      12.422 -48.627  -8.896  1.00 16.17           O  
ANISOU 1030  OG  SER B  62     2558   1790   1796    176    294    175       O  
ATOM   1031  N   LEU B  63       9.166 -49.042  -7.356  1.00 14.27           N  
ANISOU 1031  N   LEU B  63     1941   1598   1881    393    287     32       N  
ATOM   1032  CA  LEU B  63       7.884 -48.656  -7.918  1.00 14.89           C  
ANISOU 1032  CA  LEU B  63     2148   1721   1790    359    395    200       C  
ATOM   1033  C   LEU B  63       7.710 -47.164  -7.735  1.00 14.91           C  
ANISOU 1033  C   LEU B  63     2569   1345   1749    515    545   -296       C  
ATOM   1034  O   LEU B  63       8.205 -46.611  -6.755  1.00 16.26           O  
ANISOU 1034  O   LEU B  63     2855   1266   2057     63    255   -150       O  
ATOM   1035  CB  LEU B  63       6.718 -49.337  -7.204  1.00 19.94           C  
ANISOU 1035  CB  LEU B  63     3167   2037   2371   -287   1536    127       C  
ATOM   1036  CG  LEU B  63       6.192 -50.731  -7.479  1.00 23.27           C  
ANISOU 1036  CG  LEU B  63     3363   3087   2392   -892   1147     70       C  
ATOM   1037  CD1 LEU B  63       4.866 -50.867  -6.740  1.00 20.89           C  
ANISOU 1037  CD1 LEU B  63     2328   3240   2369  -1077    583    325       C  
ATOM   1038  CD2 LEU B  63       6.024 -50.961  -8.971  1.00 22.78           C  
ANISOU 1038  CD2 LEU B  63     3532   3481   1644   -427    744   -178       C  
ATOM   1039  N   ARG B  64       6.962 -46.527  -8.626  1.00 16.15           N  
ANISOU 1039  N   ARG B  64     2890   1313   1931    587    322     17       N  
ATOM   1040  CA  ARG B  64       6.583 -45.131  -8.423  1.00 17.35           C  
ANISOU 1040  CA  ARG B  64     3075   1742   1776    994    630    111       C  
ATOM   1041  C   ARG B  64       5.071 -45.003  -8.217  1.00 18.31           C  
ANISOU 1041  C   ARG B  64     3013   2135   1808    838    417   -459       C  
ATOM   1042  O   ARG B  64       4.278 -45.808  -8.709  1.00 19.06           O  
ANISOU 1042  O   ARG B  64     3068   2102   2072    761    -59   -570       O  
ATOM   1043  CB  ARG B  64       7.075 -44.275  -9.602  1.00 21.32           C  
ANISOU 1043  CB  ARG B  64     4124   1884   2094    903   1102    450       C  
ATOM   1044  CG  ARG B  64       8.602 -44.212  -9.605  1.00 26.89           C  
ANISOU 1044  CG  ARG B  64     4966   2158   3093    498   2007    405       C  
ATOM   1045  CD  ARG B  64       9.277 -43.353 -10.682  1.00 33.63           C  
ANISOU 1045  CD  ARG B  64     6323   2769   3686    -64   2059   -492       C  
ATOM   1046  NE  ARG B  64      10.703 -43.268 -10.350  1.00 39.59           N  
ANISOU 1046  NE  ARG B  64     6632   3725   4685    188   2557    287       N  
ATOM   1047  CZ  ARG B  64      11.661 -42.733 -11.101  1.00 45.23           C  
ANISOU 1047  CZ  ARG B  64     7290   4311   5584    559   2534   1035       C  
ATOM   1048  NH1 ARG B  64      11.392 -42.205 -12.291  1.00 48.41           N  
ANISOU 1048  NH1 ARG B  64     7539   4804   6051    245   2940   1330       N  
ATOM   1049  NH2 ARG B  64      12.909 -42.732 -10.648  1.00 43.12           N  
ANISOU 1049  NH2 ARG B  64     7445   3901   5036    619   1930   1608       N  
ATOM   1050  N   GLY B  65       4.674 -44.003  -7.447  1.00 18.54           N  
ANISOU 1050  N   GLY B  65     2538   2448   2058   1036    227   -742       N  
ATOM   1051  CA  GLY B  65       3.264 -43.749  -7.233  1.00 20.23           C  
ANISOU 1051  CA  GLY B  65     2611   2513   2564    653   -267  -1180       C  
ATOM   1052  C   GLY B  65       3.092 -42.358  -6.675  1.00 23.50           C  
ANISOU 1052  C   GLY B  65     3367   2833   2731   1076   -532   -962       C  
ATOM   1053  O   GLY B  65       3.979 -41.519  -6.833  1.00 22.68           O  
ANISOU 1053  O   GLY B  65     3438   2310   2869    955   -547   -933       O  
ATOM   1054  N   HIS B  66       1.957 -42.122  -6.027  1.00 24.09           N  
ANISOU 1054  N   HIS B  66     3178   2964   3010   1335   -725  -1251       N  
ATOM   1055  CA  HIS B  66       1.664 -40.823  -5.440  1.00 26.56           C  
ANISOU 1055  CA  HIS B  66     4098   3035   2957   1646   -329  -1087       C  
ATOM   1056  C   HIS B  66       1.102 -40.930  -4.040  1.00 26.89           C  
ANISOU 1056  C   HIS B  66     4250   2708   3261   1018    408  -1366       C  
ATOM   1057  O   HIS B  66       0.382 -41.874  -3.697  1.00 27.83           O  
ANISOU 1057  O   HIS B  66     4617   2862   3095    820    366  -1398       O  
ATOM   1058  CB  HIS B  66       0.680 -40.049  -6.312  1.00 30.88           C  
ANISOU 1058  CB  HIS B  66     4998   3235   3498   1983   -343   -788       C  
ATOM   1059  CG  HIS B  66       1.252 -39.617  -7.623  1.00 33.75           C  
ANISOU 1059  CG  HIS B  66     5370   3209   4244   1693   -421   -323       C  
ATOM   1060  ND1 HIS B  66       1.223 -40.416  -8.746  1.00 33.57           N  
ANISOU 1060  ND1 HIS B  66     5602   3039   4115   1156   -792   -850       N  
ATOM   1061  CD2 HIS B  66       1.880 -38.474  -7.988  1.00 35.35           C  
ANISOU 1061  CD2 HIS B  66     5881   3200   4349   1214   -441   -577       C  
ATOM   1062  CE1 HIS B  66       1.806 -39.783  -9.748  1.00 34.74           C  
ANISOU 1062  CE1 HIS B  66     6067   2974   4159   1206   -676   -443       C  
ATOM   1063  NE2 HIS B  66       2.212 -38.602  -9.314  1.00 35.77           N  
ANISOU 1063  NE2 HIS B  66     6242   3219   4131   1053   -521   -522       N  
ATOM   1064  N   VAL B  67       1.446 -39.940  -3.231  1.00 21.54           N  
ANISOU 1064  N   VAL B  67     3345   2218   2621    926     68  -1111       N  
ATOM   1065  CA  VAL B  67       0.778 -39.730  -1.972  1.00 19.01           C  
ANISOU 1065  CA  VAL B  67     2866   2243   2115    644      2   -656       C  
ATOM   1066  C   VAL B  67      -0.399 -38.830  -2.288  1.00 18.07           C  
ANISOU 1066  C   VAL B  67     2744   1836   2284    590   -329   -626       C  
ATOM   1067  O   VAL B  67      -0.233 -37.807  -2.969  1.00 20.35           O  
ANISOU 1067  O   VAL B  67     3196   1875   2663    600    222   -175       O  
ATOM   1068  CB  VAL B  67       1.693 -39.073  -0.950  1.00 17.90           C  
ANISOU 1068  CB  VAL B  67     2431   2242   2127    521   -163   -273       C  
ATOM   1069  CG1 VAL B  67       1.024 -39.040   0.430  1.00 17.91           C  
ANISOU 1069  CG1 VAL B  67     2811   2029   1964    408    392    -95       C  
ATOM   1070  CG2 VAL B  67       3.037 -39.805  -0.917  1.00 22.27           C  
ANISOU 1070  CG2 VAL B  67     2569   3018   2875    809    273     -3       C  
ATOM   1071  N   VAL B  68      -1.582 -39.212  -1.828  1.00 17.65           N  
ANISOU 1071  N   VAL B  68     2571   1930   2205    469   -144   -758       N  
ATOM   1072  CA  VAL B  68      -2.784 -38.440  -2.125  1.00 17.91           C  
ANISOU 1072  CA  VAL B  68     2613   1976   2216     55    -92   -712       C  
ATOM   1073  C   VAL B  68      -3.458 -37.983  -0.842  1.00 18.13           C  
ANISOU 1073  C   VAL B  68     2682   1942   2263    169     -6   -781       C  
ATOM   1074  O   VAL B  68      -3.057 -38.386   0.246  1.00 18.45           O  
ANISOU 1074  O   VAL B  68     2945   1894   2173    331    -14   -603       O  
ATOM   1075  CB  VAL B  68      -3.775 -39.237  -2.989  1.00 19.23           C  
ANISOU 1075  CB  VAL B  68     2995   2269   2043     16    236   -936       C  
ATOM   1076  CG1 VAL B  68      -3.143 -39.549  -4.339  1.00 21.30           C  
ANISOU 1076  CG1 VAL B  68     3317   2743   2033    264    500   -998       C  
ATOM   1077  CG2 VAL B  68      -4.226 -40.516  -2.281  1.00 20.28           C  
ANISOU 1077  CG2 VAL B  68     3061   2390   2252   -100    115   -740       C  
ATOM   1078  N   GLY B  69      -4.448 -37.104  -0.978  1.00 19.26           N  
ANISOU 1078  N   GLY B  69     3028   1580   2709    219    222   -976       N  
ATOM   1079  CA  GLY B  69      -5.196 -36.604   0.160  1.00 19.47           C  
ANISOU 1079  CA  GLY B  69     2996   1765   2636    277    185  -1071       C  
ATOM   1080  C   GLY B  69      -4.422 -35.627   1.023  1.00 19.44           C  
ANISOU 1080  C   GLY B  69     2862   2022   2501    354   -110   -610       C  
ATOM   1081  O   GLY B  69      -4.785 -35.398   2.176  1.00 20.76           O  
ANISOU 1081  O   GLY B  69     3199   2189   2500    213    296   -924       O  
ATOM   1082  N   LEU B  70      -3.355 -35.050   0.469  1.00 18.34           N  
ANISOU 1082  N   LEU B  70     2753   1731   2483    392   -105   -691       N  
ATOM   1083  CA  LEU B  70      -2.518 -34.106   1.207  1.00 19.09           C  
ANISOU 1083  CA  LEU B  70     2678   2013   2564    351    130  -1070       C  
ATOM   1084  C   LEU B  70      -3.325 -32.995   1.864  1.00 18.19           C  
ANISOU 1084  C   LEU B  70     2610   2036   2265    747    -85   -650       C  
ATOM   1085  O   LEU B  70      -3.014 -32.570   2.979  1.00 19.93           O  
ANISOU 1085  O   LEU B  70     3132   2315   2124    656   -197   -909       O  
ATOM   1086  CB  LEU B  70      -1.477 -33.474   0.284  1.00 19.42           C  
ANISOU 1086  CB  LEU B  70     2739   1925   2715    166    120  -1049       C  
ATOM   1087  CG  LEU B  70      -0.532 -34.404  -0.475  1.00 23.11           C  
ANISOU 1087  CG  LEU B  70     3223   2458   3101    501    508   -167       C  
ATOM   1088  CD1 LEU B  70       0.511 -33.584  -1.229  1.00 24.82           C  
ANISOU 1088  CD1 LEU B  70     3731   2305   3393    -80   1103   -244       C  
ATOM   1089  CD2 LEU B  70       0.128 -35.415   0.451  1.00 25.48           C  
ANISOU 1089  CD2 LEU B  70     3731   2497   3455    531    759    318       C  
ATOM   1090  N   ARG B  71      -4.364 -32.517   1.186  1.00 18.36           N  
ANISOU 1090  N   ARG B  71     2605   2006   2365    698   -157   -682       N  
ATOM   1091  CA  ARG B  71      -5.074 -31.355   1.698  1.00 19.60           C  
ANISOU 1091  CA  ARG B  71     3024   2170   2254    844   -407  -1117       C  
ATOM   1092  C   ARG B  71      -5.865 -31.675   2.973  1.00 19.33           C  
ANISOU 1092  C   ARG B  71     2843   2322   2181    776   -415   -904       C  
ATOM   1093  O   ARG B  71      -6.381 -30.772   3.640  1.00 21.51           O  
ANISOU 1093  O   ARG B  71     3175   2332   2666    878   -256  -1196       O  
ATOM   1094  CB  ARG B  71      -5.986 -30.767   0.619  1.00 19.09           C  
ANISOU 1094  CB  ARG B  71     2901   1914   2437    554   -526  -1151       C  
ATOM   1095  CG  ARG B  71      -7.225 -31.573   0.282  1.00 19.66           C  
ANISOU 1095  CG  ARG B  71     2709   2102   2660    525   -788  -1272       C  
ATOM   1096  CD  ARG B  71      -8.017 -30.836  -0.769  1.00 21.18           C  
ANISOU 1096  CD  ARG B  71     2795   2410   2843    546   -678  -1397       C  
ATOM   1097  NE  ARG B  71      -8.949 -31.705  -1.468  1.00 23.65           N  
ANISOU 1097  NE  ARG B  71     3406   2331   3251    802   -625  -1327       N  
ATOM   1098  CZ  ARG B  71      -9.808 -31.290  -2.390  1.00 23.76           C  
ANISOU 1098  CZ  ARG B  71     3621   2264   3141    846  -1025   -872       C  
ATOM   1099  NH1 ARG B  71      -9.878 -30.001  -2.693  1.00 24.65           N  
ANISOU 1099  NH1 ARG B  71     4060   2334   2970    432  -1058   -506       N  
ATOM   1100  NH2 ARG B  71     -10.604 -32.162  -2.996  1.00 24.36           N  
ANISOU 1100  NH2 ARG B  71     3572   2593   3088    553  -1062  -1033       N  
ATOM   1101  N   TYR B  72      -5.916 -32.951   3.343  1.00 20.45           N  
ANISOU 1101  N   TYR B  72     2845   2631   2294    477    -91   -617       N  
ATOM   1102  CA  TYR B  72      -6.642 -33.353   4.549  1.00 21.19           C  
ANISOU 1102  CA  TYR B  72     2793   2744   2513    230   -213   -870       C  
ATOM   1103  C   TYR B  72      -5.742 -33.539   5.778  1.00 24.11           C  
ANISOU 1103  C   TYR B  72     3572   2768   2823    783     69   -675       C  
ATOM   1104  O   TYR B  72      -6.248 -33.841   6.863  1.00 25.37           O  
ANISOU 1104  O   TYR B  72     3465   3322   2854    706   -105   -857       O  
ATOM   1105  CB  TYR B  72      -7.432 -34.641   4.273  1.00 20.83           C  
ANISOU 1105  CB  TYR B  72     2404   2967   2544    197    -80  -1062       C  
ATOM   1106  CG  TYR B  72      -8.390 -34.500   3.114  1.00 21.73           C  
ANISOU 1106  CG  TYR B  72     2498   2938   2821    134   -148  -1005       C  
ATOM   1107  CD1 TYR B  72      -9.467 -33.629   3.179  1.00 23.24           C  
ANISOU 1107  CD1 TYR B  72     2964   2957   2910    114    -31  -1187       C  
ATOM   1108  CD2 TYR B  72      -8.203 -35.218   1.947  1.00 21.85           C  
ANISOU 1108  CD2 TYR B  72     2787   3037   2476    107   -347  -1053       C  
ATOM   1109  CE1 TYR B  72     -10.337 -33.485   2.119  1.00 23.85           C  
ANISOU 1109  CE1 TYR B  72     3072   2930   3061    100   -246   -848       C  
ATOM   1110  CE2 TYR B  72      -9.066 -35.082   0.878  1.00 24.04           C  
ANISOU 1110  CE2 TYR B  72     2923   3151   3058    192   -367   -700       C  
ATOM   1111  CZ  TYR B  72     -10.129 -34.212   0.971  1.00 25.24           C  
ANISOU 1111  CZ  TYR B  72     3180   3135   3276    220   -599   -670       C  
ATOM   1112  OH  TYR B  72     -10.996 -34.081  -0.080  1.00 26.54           O  
ANISOU 1112  OH  TYR B  72     3740   3008   3336    271   -738   -751       O  
ATOM   1113  N   TYR B  73      -4.430 -33.342   5.611  1.00 21.56           N  
ANISOU 1113  N   TYR B  73     3585   2100   2509    895   -205   -843       N  
ATOM   1114  CA  TYR B  73      -3.440 -33.590   6.673  1.00 21.07           C  
ANISOU 1114  CA  TYR B  73     3483   2096   2427    565   -267   -980       C  
ATOM   1115  C   TYR B  73      -2.463 -32.436   6.797  1.00 22.57           C  
ANISOU 1115  C   TYR B  73     3831   2224   2520    477   -555  -1238       C  
ATOM   1116  O   TYR B  73      -2.355 -31.629   5.892  1.00 24.30           O  
ANISOU 1116  O   TYR B  73     3849   2732   2650    486   -776  -1033       O  
ATOM   1117  CB  TYR B  73      -2.681 -34.901   6.399  1.00 20.28           C  
ANISOU 1117  CB  TYR B  73     3550   1887   2268    241   -198  -1067       C  
ATOM   1118  CG  TYR B  73      -3.644 -36.039   6.237  1.00 19.86           C  
ANISOU 1118  CG  TYR B  73     3211   1903   2430    101   -423   -895       C  
ATOM   1119  CD1 TYR B  73      -4.216 -36.639   7.355  1.00 21.81           C  
ANISOU 1119  CD1 TYR B  73     3348   2554   2386   -103    146   -765       C  
ATOM   1120  CD2 TYR B  73      -4.043 -36.471   4.980  1.00 19.89           C  
ANISOU 1120  CD2 TYR B  73     3009   1989   2559    240    -16   -797       C  
ATOM   1121  CE1 TYR B  73      -5.137 -37.655   7.230  1.00 22.34           C  
ANISOU 1121  CE1 TYR B  73     3223   2565   2700   -119    102   -859       C  
ATOM   1122  CE2 TYR B  73      -4.970 -37.501   4.840  1.00 21.27           C  
ANISOU 1122  CE2 TYR B  73     3097   2187   2799   -239    -57   -475       C  
ATOM   1123  CZ  TYR B  73      -5.512 -38.083   5.975  1.00 21.45           C  
ANISOU 1123  CZ  TYR B  73     3175   2407   2569   -227     98   -753       C  
ATOM   1124  OH  TYR B  73      -6.440 -39.091   5.870  1.00 24.14           O  
ANISOU 1124  OH  TYR B  73     3487   2771   2913    -36    285   -877       O  
ATOM   1125  N   THR B  74      -1.729 -32.368   7.905  1.00 24.80           N  
ANISOU 1125  N   THR B  74     4335   2181   2906    255   -550  -1223       N  
ATOM   1126  CA  THR B  74      -0.855 -31.216   8.136  1.00 26.46           C  
ANISOU 1126  CA  THR B  74     4561   2732   2758    -45   -890   -910       C  
ATOM   1127  C   THR B  74       0.636 -31.523   8.013  1.00 26.98           C  
ANISOU 1127  C   THR B  74     4621   2777   2853    -96   -620   -804       C  
ATOM   1128  O   THR B  74       1.457 -30.606   8.040  1.00 28.97           O  
ANISOU 1128  O   THR B  74     5009   2951   3049   -375   -287  -1150       O  
ATOM   1129  CB  THR B  74      -1.080 -30.604   9.532  1.00 31.54           C  
ANISOU 1129  CB  THR B  74     5146   3162   3676    481    194   -593       C  
ATOM   1130  OG1 THR B  74      -0.688 -31.544  10.531  1.00 31.69           O  
ANISOU 1130  OG1 THR B  74     6006   2825   3212   -115    577   -168       O  
ATOM   1131  CG2 THR B  74      -2.534 -30.237   9.742  1.00 33.30           C  
ANISOU 1131  CG2 THR B  74     4782   3583   4288    616   -170  -1121       C  
ATOM   1132  N   GLY B  75       0.989 -32.799   7.891  1.00 26.01           N  
ANISOU 1132  N   GLY B  75     3945   2500   3439     26   -654   -505       N  
ATOM   1133  CA  GLY B  75       2.385 -33.188   7.805  1.00 26.48           C  
ANISOU 1133  CA  GLY B  75     3832   2784   3445    -69   -503   -380       C  
ATOM   1134  C   GLY B  75       3.095 -32.621   6.589  1.00 27.49           C  
ANISOU 1134  C   GLY B  75     3939   3256   3251   -167   -420   -703       C  
ATOM   1135  O   GLY B  75       2.576 -32.660   5.473  1.00 30.81           O  
ANISOU 1135  O   GLY B  75     4504   3947   3257   -239      8   -706       O  
ATOM   1136  N   VAL B  76       4.294 -32.096   6.811  1.00 26.53           N  
ANISOU 1136  N   VAL B  76     3757   2776   3548   -196   -103   -653       N  
ATOM   1137  CA  VAL B  76       5.100 -31.527   5.738  1.00 29.65           C  
ANISOU 1137  CA  VAL B  76     4377   2745   4142     86    399   -558       C  
ATOM   1138  C   VAL B  76       6.255 -32.457   5.381  1.00 30.63           C  
ANISOU 1138  C   VAL B  76     4966   2844   3826   -115    936   -937       C  
ATOM   1139  O   VAL B  76       6.814 -33.123   6.249  1.00 30.81           O  
ANISOU 1139  O   VAL B  76     5232   2805   3670   -208    862   -829       O  
ATOM   1140  CB  VAL B  76       5.644 -30.134   6.140  1.00 33.57           C  
ANISOU 1140  CB  VAL B  76     4569   2986   5200   -127    928   -420       C  
ATOM   1141  CG1 VAL B  76       6.609 -29.595   5.104  1.00 35.64           C  
ANISOU 1141  CG1 VAL B  76     4715   3311   5514     75    729   -368       C  
ATOM   1142  CG2 VAL B  76       4.493 -29.167   6.347  1.00 36.17           C  
ANISOU 1142  CG2 VAL B  76     4453   3495   5796   -231   1073   -216       C  
ATOM   1143  N   VAL B  77       6.578 -32.518   4.092  1.00 31.85           N  
ANISOU 1143  N   VAL B  77     5100   3175   3826   -187   1280   -735       N  
ATOM   1144  CA  VAL B  77       7.743 -33.232   3.589  1.00 33.81           C  
ANISOU 1144  CA  VAL B  77     5124   3458   4263   -134   1245   -795       C  
ATOM   1145  C   VAL B  77       8.598 -32.248   2.801  1.00 35.00           C  
ANISOU 1145  C   VAL B  77     4967   3566   4765   -216   1275   -187       C  
ATOM   1146  O   VAL B  77       8.058 -31.387   2.113  1.00 36.20           O  
ANISOU 1146  O   VAL B  77     4923   3717   5113    -52   1551   -232       O  
ATOM   1147  CB  VAL B  77       7.344 -34.417   2.669  1.00 35.13           C  
ANISOU 1147  CB  VAL B  77     5313   3902   4132    160   1244  -1099       C  
ATOM   1148  CG1 VAL B  77       8.573 -35.119   2.125  1.00 35.34           C  
ANISOU 1148  CG1 VAL B  77     5510   4106   3811    602    674  -1013       C  
ATOM   1149  CG2 VAL B  77       6.460 -35.402   3.400  1.00 35.05           C  
ANISOU 1149  CG2 VAL B  77     5196   3993   4128    109   1602  -1165       C  
ATOM   1150  N   ASN B  78       9.920 -32.361   2.912  1.00 36.35           N  
ANISOU 1150  N   ASN B  78     4992   3552   5269   -536    769    -53       N  
ATOM   1151  CA  ASN B  78      10.830 -31.625   2.037  1.00 41.07           C  
ANISOU 1151  CA  ASN B  78     5720   3982   5902   -457    867    -28       C  
ATOM   1152  C   ASN B  78      11.316 -32.516   0.901  1.00 40.16           C  
ANISOU 1152  C   ASN B  78     5602   4058   5598   -142   1239    606       C  
ATOM   1153  O   ASN B  78      11.272 -33.738   1.014  1.00 37.67           O  
ANISOU 1153  O   ASN B  78     5432   3803   5075    107   1497    243       O  
ATOM   1154  CB  ASN B  78      12.027 -31.082   2.820  1.00 46.97           C  
ANISOU 1154  CB  ASN B  78     6537   4246   7064  -1031    984   -543       C  
ATOM   1155  CG  ASN B  78      11.615 -30.140   3.931  1.00 52.25           C  
ANISOU 1155  CG  ASN B  78     7227   4547   8078  -1473   1168   -848       C  
ATOM   1156  OD1 ASN B  78      11.256 -28.989   3.682  1.00 55.56           O  
ANISOU 1156  OD1 ASN B  78     7545   4950   8615  -1354   1415   -634       O  
ATOM   1157  ND2 ASN B  78      11.668 -30.622   5.168  1.00 52.85           N  
ANISOU 1157  ND2 ASN B  78     7476   4358   8248  -2053   1139  -1310       N  
ATOM   1158  N   ASN B  79      11.775 -31.914  -0.192  1.00 40.67           N  
ANISOU 1158  N   ASN B  79     5456   4220   5777     61   1376   1403       N  
ATOM   1159  CA  ASN B  79      12.297 -32.698  -1.306  1.00 40.37           C  
ANISOU 1159  CA  ASN B  79     5272   4414   5652     40   1007   1526       C  
ATOM   1160  C   ASN B  79      13.471 -33.570  -0.865  1.00 37.83           C  
ANISOU 1160  C   ASN B  79     4795   4384   5194   -321    743   1018       C  
ATOM   1161  O   ASN B  79      14.307 -33.142  -0.064  1.00 37.22           O  
ANISOU 1161  O   ASN B  79     4574   4192   5377   -724    612    882       O  
ATOM   1162  CB  ASN B  79      12.713 -31.794  -2.469  1.00 43.48           C  
ANISOU 1162  CB  ASN B  79     5570   4794   6156     78   1066   1621       C  
ATOM   1163  CG  ASN B  79      11.539 -31.412  -3.363  1.00 45.80           C  
ANISOU 1163  CG  ASN B  79     5868   4956   6576   -208   1398   1747       C  
ATOM   1164  OD1 ASN B  79      10.564 -32.157  -3.485  1.00 44.12           O  
ANISOU 1164  OD1 ASN B  79     5206   5302   6255    204   1384   1498       O  
ATOM   1165  ND2 ASN B  79      11.636 -30.250  -3.999  1.00 47.53           N  
ANISOU 1165  ND2 ASN B  79     6311   4609   7139   -839   1533   1798       N  
ATOM   1166  N   ASN B  80      13.479 -34.794  -1.394  1.00 35.99           N  
ANISOU 1166  N   ASN B  80     4651   4367   4655   -787    421    560       N  
ATOM   1167  CA AASN B  80      14.507 -35.793  -1.096  0.49 34.53           C  
ANISOU 1167  CA AASN B  80     4351   4206   4563  -1076    232    142       C  
ATOM   1168  CA BASN B  80      14.467 -35.832  -1.104  0.51 36.75           C  
ANISOU 1168  CA BASN B  80     4746   4495   4724   -776    501    351       C  
ATOM   1169  C   ASN B  80      14.424 -36.337   0.333  1.00 33.71           C  
ANISOU 1169  C   ASN B  80     4579   4195   4033   -952    304    -25       C  
ATOM   1170  O   ASN B  80      15.347 -37.002   0.791  1.00 34.48           O  
ANISOU 1170  O   ASN B  80     4938   4577   3585   -460    372   -251       O  
ATOM   1171  CB AASN B  80      15.917 -35.230  -1.340  0.49 34.40           C  
ANISOU 1171  CB AASN B  80     3922   4020   5127  -1409    -28   -202       C  
ATOM   1172  CB BASN B  80      15.877 -35.352  -1.446  0.51 41.10           C  
ANISOU 1172  CB BASN B  80     5062   4864   5689   -586    747    415       C  
ATOM   1173  CG AASN B  80      16.027 -34.456  -2.643  0.49 35.21           C  
ANISOU 1173  CG AASN B  80     3748   3871   5759  -1513     35   -291       C  
ATOM   1174  CG BASN B  80      16.235 -35.610  -2.895  0.51 45.45           C  
ANISOU 1174  CG BASN B  80     5473   5145   6649   -352   1196    470       C  
ATOM   1175  OD1AASN B  80      15.239 -34.657  -3.567  0.49 34.34           O  
ANISOU 1175  OD1AASN B  80     3669   3756   5622  -1145   -210   -119       O  
ATOM   1176  OD1BASN B  80      16.336 -36.761  -3.323  0.51 46.45           O  
ANISOU 1176  OD1BASN B  80     5578   5063   7009   -280   1395    534       O  
ATOM   1177  ND2AASN B  80      17.012 -33.564  -2.720  0.49 37.45           N  
ANISOU 1177  ND2AASN B  80     3936   4109   6183  -1499    231   -336       N  
ATOM   1178  ND2BASN B  80      16.427 -34.542  -3.660  0.51 46.83           N  
ANISOU 1178  ND2BASN B  80     5689   5194   6909   -355   1187    441       N  
ATOM   1179  N   GLU B  81      13.333 -36.047   1.036  1.00 30.66           N  
ANISOU 1179  N   GLU B  81     4657   3524   3468  -1158    578   -370       N  
ATOM   1180  CA  GLU B  81      13.141 -36.609   2.371  1.00 28.49           C  
ANISOU 1180  CA  GLU B  81     4365   3004   3456   -903    159   -938       C  
ATOM   1181  C   GLU B  81      12.533 -38.002   2.285  1.00 24.93           C  
ANISOU 1181  C   GLU B  81     4010   2819   2642   -726     47   -845       C  
ATOM   1182  O   GLU B  81      11.714 -38.287   1.414  1.00 25.76           O  
ANISOU 1182  O   GLU B  81     4007   2904   2878   -620    605   -668       O  
ATOM   1183  CB  GLU B  81      12.240 -35.720   3.233  1.00 33.62           C  
ANISOU 1183  CB  GLU B  81     4668   3661   4445   -571    213  -1286       C  
ATOM   1184  CG  GLU B  81      12.958 -34.583   3.929  1.00 39.00           C  
ANISOU 1184  CG  GLU B  81     5199   4366   5256   -477    473  -1417       C  
ATOM   1185  CD  GLU B  81      12.099 -33.914   4.988  1.00 43.48           C  
ANISOU 1185  CD  GLU B  81     5607   4957   5955   -782    631  -1964       C  
ATOM   1186  OE1 GLU B  81      10.919 -34.292   5.135  1.00 41.11           O  
ANISOU 1186  OE1 GLU B  81     5116   4953   5552   -973    545  -2337       O  
ATOM   1187  OE2 GLU B  81      12.611 -33.012   5.681  1.00 48.87           O  
ANISOU 1187  OE2 GLU B  81     6117   5529   6922  -1009    795  -2174       O  
ATOM   1188  N   MET B  82      12.936 -38.867   3.204  1.00 25.05           N  
ANISOU 1188  N   MET B  82     4077   2972   2467   -629    438    -24       N  
ATOM   1189  CA  MET B  82      12.267 -40.144   3.371  1.00 25.05           C  
ANISOU 1189  CA  MET B  82     3677   3218   2624   -299     75   -313       C  
ATOM   1190  C   MET B  82      10.899 -39.925   3.998  1.00 24.06           C  
ANISOU 1190  C   MET B  82     3528   2976   2637   -442    286   -341       C  
ATOM   1191  O   MET B  82      10.676 -38.936   4.701  1.00 23.61           O  
ANISOU 1191  O   MET B  82     3625   2835   2512   -750    289   -397       O  
ATOM   1192  CB  MET B  82      13.094 -41.077   4.250  1.00 29.40           C  
ANISOU 1192  CB  MET B  82     4126   3972   3074    -93   -246   -273       C  
ATOM   1193  CG  MET B  82      14.480 -41.344   3.739  1.00 38.59           C  
ANISOU 1193  CG  MET B  82     5208   4633   4821    152    883   -750       C  
ATOM   1194  SD  MET B  82      14.473 -42.755   2.638  1.00 46.43           S  
ANISOU 1194  SD  MET B  82     5854   5458   6329    412   1833  -1137       S  
ATOM   1195  CE  MET B  82      16.197 -42.836   2.176  1.00 45.39           C  
ANISOU 1195  CE  MET B  82     5460   5356   6432    693   1491   -845       C  
ATOM   1196  N   VAL B  83       9.988 -40.856   3.739  1.00 20.30           N  
ANISOU 1196  N   VAL B  83     2865   2535   2315    -46     -5   -253       N  
ATOM   1197  CA  VAL B  83       8.709 -40.884   4.417  1.00 20.93           C  
ANISOU 1197  CA  VAL B  83     2834   2212   2906    -58     -4   -775       C  
ATOM   1198  C   VAL B  83       8.508 -42.288   4.951  1.00 23.25           C  
ANISOU 1198  C   VAL B  83     2934   2044   3855     70    294   -756       C  
ATOM   1199  O   VAL B  83       9.181 -43.233   4.512  1.00 29.25           O  
ANISOU 1199  O   VAL B  83     3644   2302   5168     35    749   -516       O  
ATOM   1200  CB  VAL B  83       7.554 -40.488   3.481  1.00 22.23           C  
ANISOU 1200  CB  VAL B  83     3488   2282   2676   -272   -112  -1342       C  
ATOM   1201  CG1 VAL B  83       7.683 -39.006   3.091  1.00 23.84           C  
ANISOU 1201  CG1 VAL B  83     3936   2534   2588   -208    133   -759       C  
ATOM   1202  CG2 VAL B  83       7.537 -41.380   2.252  1.00 26.41           C  
ANISOU 1202  CG2 VAL B  83     3873   3142   3017    125   -375   -782       C  
ATOM   1203  N   ALA B  84       7.582 -42.437   5.886  1.00 22.13           N  
ANISOU 1203  N   ALA B  84     2809   2057   3541    -98   -384    -63       N  
ATOM   1204  CA  ALA B  84       7.268 -43.759   6.412  1.00 22.71           C  
ANISOU 1204  CA  ALA B  84     2910   2157   3560   -326   -539    -12       C  
ATOM   1205  C   ALA B  84       5.901 -44.235   5.938  1.00 20.84           C  
ANISOU 1205  C   ALA B  84     2709   1886   3323     20   -520     82       C  
ATOM   1206  O   ALA B  84       4.933 -43.477   5.951  1.00 22.51           O  
ANISOU 1206  O   ALA B  84     2809   2094   3648      2   -288   -169       O  
ATOM   1207  CB  ALA B  84       7.325 -43.748   7.918  1.00 24.75           C  
ANISOU 1207  CB  ALA B  84     3368   2901   3134   -498   -831    528       C  
ATOM   1208  N   LEU B  85       5.834 -45.490   5.516  1.00 21.03           N  
ANISOU 1208  N   LEU B  85     3116   1893   2982   -332    -70   -231       N  
ATOM   1209  CA  LEU B  85       4.566 -46.124   5.192  1.00 19.31           C  
ANISOU 1209  CA  LEU B  85     2766   1943   2628   -525    107     18       C  
ATOM   1210  C   LEU B  85       4.071 -46.880   6.409  1.00 20.93           C  
ANISOU 1210  C   LEU B  85     2993   2503   2456   -371     22    -13       C  
ATOM   1211  O   LEU B  85       4.809 -47.677   6.995  1.00 25.55           O  
ANISOU 1211  O   LEU B  85     3255   3285   3166     95    -51     40       O  
ATOM   1212  CB  LEU B  85       4.703 -47.091   4.023  1.00 20.32           C  
ANISOU 1212  CB  LEU B  85     2774   2275   2672    249     78   -462       C  
ATOM   1213  CG  LEU B  85       5.291 -46.536   2.737  1.00 25.40           C  
ANISOU 1213  CG  LEU B  85     3797   2850   3005    682    693   -301       C  
ATOM   1214  CD1 LEU B  85       5.169 -47.572   1.607  1.00 27.68           C  
ANISOU 1214  CD1 LEU B  85     4493   2659   3366   1242   1415   -238       C  
ATOM   1215  CD2 LEU B  85       4.650 -45.211   2.385  1.00 27.79           C  
ANISOU 1215  CD2 LEU B  85     3884   3676   2998    210   -237     55       C  
ATOM   1216  N   GLN B  86       2.825 -46.632   6.784  1.00 20.11           N  
ANISOU 1216  N   GLN B  86     2882   2217   2541    -32    141    -84       N  
ATOM   1217  CA  GLN B  86       2.252 -47.256   7.967  1.00 19.82           C  
ANISOU 1217  CA  GLN B  86     3111   2473   1949   -241     37   -277       C  
ATOM   1218  C   GLN B  86       0.862 -47.791   7.680  1.00 20.94           C  
ANISOU 1218  C   GLN B  86     3301   2420   2236   -279     89   -196       C  
ATOM   1219  O   GLN B  86      -0.039 -47.029   7.335  1.00 20.55           O  
ANISOU 1219  O   GLN B  86     3432   2423   1952   -148    235    -31       O  
ATOM   1220  CB  GLN B  86       2.197 -46.255   9.112  1.00 21.11           C  
ANISOU 1220  CB  GLN B  86     3460   2817   1743   -310    -96   -121       C  
ATOM   1221  CG  GLN B  86       1.648 -46.827  10.397  1.00 22.90           C  
ANISOU 1221  CG  GLN B  86     3886   3171   1643   -415    -71    -74       C  
ATOM   1222  CD  GLN B  86       1.691 -45.809  11.518  1.00 29.50           C  
ANISOU 1222  CD  GLN B  86     5272   3644   2292   -231    124   -174       C  
ATOM   1223  OE1 GLN B  86       1.236 -44.676  11.357  1.00 30.32           O  
ANISOU 1223  OE1 GLN B  86     5388   3291   2843   -259    455   -465       O  
ATOM   1224  NE2 GLN B  86       2.248 -46.202  12.657  1.00 35.48           N  
ANISOU 1224  NE2 GLN B  86     6233   4369   2879   -220      8   -114       N  
ATOM   1225  N   ARG B  87       0.683 -49.101   7.815  1.00 19.87           N  
ANISOU 1225  N   ARG B  87     3090   2509   1950    -89    281    -27       N  
ATOM   1226  CA  ARG B  87      -0.631 -49.685   7.596  1.00 19.10           C  
ANISOU 1226  CA  ARG B  87     3098   2158   2000   -119    505   -312       C  
ATOM   1227  C   ARG B  87      -1.660 -49.162   8.603  1.00 19.99           C  
ANISOU 1227  C   ARG B  87     3169   2759   1669    -36    592     32       C  
ATOM   1228  O   ARG B  87      -1.351 -48.955   9.779  1.00 22.65           O  
ANISOU 1228  O   ARG B  87     3624   3136   1844    -89     -6     -8       O  
ATOM   1229  CB  ARG B  87      -0.553 -51.206   7.661  1.00 19.39           C  
ANISOU 1229  CB  ARG B  87     3422   2033   1913    -71    401    -13       C  
ATOM   1230  CG  ARG B  87      -0.020 -51.805   6.379  1.00 19.86           C  
ANISOU 1230  CG  ARG B  87     3238   2395   1915   -157    911    -72       C  
ATOM   1231  CD  ARG B  87      -1.139 -51.930   5.356  1.00 18.93           C  
ANISOU 1231  CD  ARG B  87     2907   2509   1777   -653    514    -39       C  
ATOM   1232  NE  ARG B  87      -2.037 -53.040   5.684  1.00 19.53           N  
ANISOU 1232  NE  ARG B  87     2682   2511   2227   -583    933    191       N  
ATOM   1233  CZ  ARG B  87      -3.351 -52.934   5.865  1.00 20.04           C  
ANISOU 1233  CZ  ARG B  87     3158   2383   2073   -136   1177    511       C  
ATOM   1234  NH1 ARG B  87      -3.963 -51.751   5.760  1.00 18.92           N  
ANISOU 1234  NH1 ARG B  87     3051   2132   2006     67    597    271       N  
ATOM   1235  NH2 ARG B  87      -4.057 -54.022   6.143  1.00 22.53           N  
ANISOU 1235  NH2 ARG B  87     3443   2668   2449   -589   1014    276       N  
ATOM   1236  N   ASP B  88      -2.878 -48.938   8.120  1.00 21.15           N  
ANISOU 1236  N   ASP B  88     2904   2773   2359    -24    717   -132       N  
ATOM   1237  CA  ASP B  88      -3.997 -48.600   8.988  1.00 23.61           C  
ANISOU 1237  CA  ASP B  88     3314   3191   2466   -161    894   -116       C  
ATOM   1238  C   ASP B  88      -5.170 -49.527   8.676  1.00 24.59           C  
ANISOU 1238  C   ASP B  88     3381   3540   2421   -232   1157   -182       C  
ATOM   1239  O   ASP B  88      -6.115 -49.138   7.985  1.00 23.68           O  
ANISOU 1239  O   ASP B  88     3193   3473   2331   -380    933   -357       O  
ATOM   1240  CB  ASP B  88      -4.401 -47.134   8.821  1.00 25.60           C  
ANISOU 1240  CB  ASP B  88     3747   3245   2735   -192    897   -368       C  
ATOM   1241  CG  ASP B  88      -5.470 -46.705   9.826  1.00 30.87           C  
ANISOU 1241  CG  ASP B  88     4664   3712   3352     97   1349      0       C  
ATOM   1242  OD1 ASP B  88      -5.739 -47.466  10.788  1.00 33.28           O  
ANISOU 1242  OD1 ASP B  88     5056   4355   3234    384    904   -366       O  
ATOM   1243  OD2 ASP B  88      -6.044 -45.605   9.662  1.00 34.39           O  
ANISOU 1243  OD2 ASP B  88     4973   3952   4143    321   1456   -186       O  
ATOM   1244  N   PRO B  89      -5.113 -50.766   9.187  1.00 24.98           N  
ANISOU 1244  N   PRO B  89     3498   3546   2449   -352    942    111       N  
ATOM   1245  CA  PRO B  89      -6.158 -51.752   8.879  1.00 26.84           C  
ANISOU 1245  CA  PRO B  89     3614   3809   2776   -402    874    339       C  
ATOM   1246  C   PRO B  89      -7.523 -51.384   9.465  1.00 28.49           C  
ANISOU 1246  C   PRO B  89     3512   4173   3139   -483    965    648       C  
ATOM   1247  O   PRO B  89      -8.523 -51.973   9.065  1.00 29.70           O  
ANISOU 1247  O   PRO B  89     3279   4206   3798   -595   1127    787       O  
ATOM   1248  CB  PRO B  89      -5.619 -53.047   9.501  1.00 27.08           C  
ANISOU 1248  CB  PRO B  89     3994   3719   2575   -517    781      5       C  
ATOM   1249  CG  PRO B  89      -4.654 -52.600  10.557  1.00 28.72           C  
ANISOU 1249  CG  PRO B  89     4035   3847   3028   -474    841    411       C  
ATOM   1250  CD  PRO B  89      -4.058 -51.316  10.060  1.00 26.73           C  
ANISOU 1250  CD  PRO B  89     3717   3707   2733   -629   1088    408       C  
ATOM   1251  N   ASN B  90      -7.563 -50.419  10.382  1.00 29.09           N  
ANISOU 1251  N   ASN B  90     3519   4863   2672   -266   1224    424       N  
ATOM   1252  CA  ASN B  90      -8.826 -49.991  10.977  1.00 30.96           C  
ANISOU 1252  CA  ASN B  90     4074   5404   2284    310    939    411       C  
ATOM   1253  C   ASN B  90      -9.442 -48.771  10.299  1.00 29.63           C  
ANISOU 1253  C   ASN B  90     3919   5073   2266    270   1249    146       C  
ATOM   1254  O   ASN B  90     -10.452 -48.246  10.771  1.00 32.45           O  
ANISOU 1254  O   ASN B  90     4171   5522   2637    482   1343     25       O  
ATOM   1255  CB  ASN B  90      -8.637 -49.701  12.464  1.00 35.37           C  
ANISOU 1255  CB  ASN B  90     4779   6004   2655    258    985    629       C  
ATOM   1256  CG  ASN B  90      -8.199 -50.923  13.239  1.00 40.53           C  
ANISOU 1256  CG  ASN B  90     5529   6565   3305     47    781    916       C  
ATOM   1257  OD1 ASN B  90      -7.285 -50.856  14.060  1.00 43.91           O  
ANISOU 1257  OD1 ASN B  90     6208   6882   3592    522    515   1097       O  
ATOM   1258  ND2 ASN B  90      -8.841 -52.055  12.970  1.00 40.64           N  
ANISOU 1258  ND2 ASN B  90     5244   6632   3566   -634    845   1234       N  
ATOM   1259  N   ASN B  91      -8.841 -48.319   9.200  1.00 26.42           N  
ANISOU 1259  N   ASN B  91     3505   4560   1972     39    793     65       N  
ATOM   1260  CA  ASN B  91      -9.428 -47.230   8.425  1.00 24.86           C  
ANISOU 1260  CA  ASN B  91     3085   4367   1993     30    833    189       C  
ATOM   1261  C   ASN B  91     -10.823 -47.634   7.950  1.00 26.52           C  
ANISOU 1261  C   ASN B  91     3058   4420   2597    -10   1052    -94       C  
ATOM   1262  O   ASN B  91     -10.981 -48.644   7.272  1.00 26.00           O  
ANISOU 1262  O   ASN B  91     2708   4366   2807   -135    681   -407       O  
ATOM   1263  CB  ASN B  91      -8.528 -46.870   7.236  1.00 23.41           C  
ANISOU 1263  CB  ASN B  91     2941   4113   1841     48    776     55       C  
ATOM   1264  CG  ASN B  91      -9.044 -45.673   6.450  1.00 24.39           C  
ANISOU 1264  CG  ASN B  91     2846   4210   2209   -145    532   -186       C  
ATOM   1265  OD1 ASN B  91     -10.098 -45.739   5.807  1.00 24.86           O  
ANISOU 1265  OD1 ASN B  91     2616   4161   2669   -139    418   -215       O  
ATOM   1266  ND2 ASN B  91      -8.292 -44.580   6.479  1.00 25.26           N  
ANISOU 1266  ND2 ASN B  91     2756   4306   2537   -264    713   -550       N  
ATOM   1267  N   PRO B  92     -11.849 -46.855   8.316  1.00 26.84           N  
ANISOU 1267  N   PRO B  92     2881   4534   2784     40    839   -416       N  
ATOM   1268  CA  PRO B  92     -13.210 -47.304   8.010  1.00 28.99           C  
ANISOU 1268  CA  PRO B  92     2941   4958   3117    179   1085   -249       C  
ATOM   1269  C   PRO B  92     -13.601 -47.146   6.543  1.00 26.33           C  
ANISOU 1269  C   PRO B  92     2349   4766   2890   -184    617   -325       C  
ATOM   1270  O   PRO B  92     -14.662 -47.640   6.158  1.00 31.56           O  
ANISOU 1270  O   PRO B  92     3201   5243   3547   -704    692   -354       O  
ATOM   1271  CB  PRO B  92     -14.081 -46.415   8.908  1.00 31.02           C  
ANISOU 1271  CB  PRO B  92     3195   5085   3506    305   1434   -343       C  
ATOM   1272  CG  PRO B  92     -13.282 -45.176   9.097  1.00 31.48           C  
ANISOU 1272  CG  PRO B  92     3571   4802   3589    255   1461   -377       C  
ATOM   1273  CD  PRO B  92     -11.828 -45.581   9.057  1.00 30.34           C  
ANISOU 1273  CD  PRO B  92     3411   4770   3346    421   1489   -650       C  
ATOM   1274  N   TYR B  93     -12.770 -46.480   5.744  1.00 24.28           N  
ANISOU 1274  N   TYR B  93     2415   4003   2807    -37   1405   -316       N  
ATOM   1275  CA  TYR B  93     -13.037 -46.340   4.310  1.00 22.66           C  
ANISOU 1275  CA  TYR B  93     2658   3418   2536    128    753   -343       C  
ATOM   1276  C   TYR B  93     -12.343 -47.412   3.480  1.00 24.13           C  
ANISOU 1276  C   TYR B  93     2527   3501   3141    203    576   -372       C  
ATOM   1277  O   TYR B  93     -12.788 -47.731   2.382  1.00 26.03           O  
ANISOU 1277  O   TYR B  93     2607   3778   3504     78    350   -829       O  
ATOM   1278  CB  TYR B  93     -12.605 -44.952   3.820  1.00 22.36           C  
ANISOU 1278  CB  TYR B  93     2598   3169   2728     26    719   -726       C  
ATOM   1279  CG  TYR B  93     -13.346 -43.833   4.525  1.00 23.39           C  
ANISOU 1279  CG  TYR B  93     2278   3314   3294    271    559   -914       C  
ATOM   1280  CD1 TYR B  93     -14.565 -43.371   4.044  1.00 26.42           C  
ANISOU 1280  CD1 TYR B  93     2671   3443   3924    402    723   -912       C  
ATOM   1281  CD2 TYR B  93     -12.831 -43.251   5.676  1.00 25.03           C  
ANISOU 1281  CD2 TYR B  93     2498   3639   3374   -119    763  -1128       C  
ATOM   1282  CE1 TYR B  93     -15.257 -42.364   4.691  1.00 28.56           C  
ANISOU 1282  CE1 TYR B  93     2948   3870   4036    379    425  -1245       C  
ATOM   1283  CE2 TYR B  93     -13.514 -42.232   6.333  1.00 28.54           C  
ANISOU 1283  CE2 TYR B  93     2883   3794   4167    -46    701  -1385       C  
ATOM   1284  CZ  TYR B  93     -14.727 -41.792   5.832  1.00 29.33           C  
ANISOU 1284  CZ  TYR B  93     2939   3900   4304    456    529  -1560       C  
ATOM   1285  OH  TYR B  93     -15.426 -40.788   6.465  1.00 33.19           O  
ANISOU 1285  OH  TYR B  93     3443   4251   4918    618    743  -1417       O  
ATOM   1286  N   ASP B  94     -11.258 -47.968   4.008  1.00 22.33           N  
ANISOU 1286  N   ASP B  94     2249   3301   2935    242   1039   -362       N  
ATOM   1287  CA  ASP B  94     -10.435 -48.906   3.252  1.00 21.12           C  
ANISOU 1287  CA  ASP B  94     2384   2870   2772     -8   1152   -199       C  
ATOM   1288  C   ASP B  94      -9.544 -49.694   4.198  1.00 21.66           C  
ANISOU 1288  C   ASP B  94     2678   2816   2735    232   1069    -74       C  
ATOM   1289  O   ASP B  94      -8.579 -49.152   4.723  1.00 21.91           O  
ANISOU 1289  O   ASP B  94     2878   2855   2594   -140    826   -121       O  
ATOM   1290  CB  ASP B  94      -9.590 -48.145   2.224  1.00 20.05           C  
ANISOU 1290  CB  ASP B  94     2445   2689   2484   -176    996   -336       C  
ATOM   1291  CG  ASP B  94      -8.767 -49.059   1.322  1.00 20.96           C  
ANISOU 1291  CG  ASP B  94     2728   2737   2498   -408    738   -524       C  
ATOM   1292  OD1 ASP B  94      -8.913 -50.305   1.388  1.00 20.48           O  
ANISOU 1292  OD1 ASP B  94     2552   2757   2471   -312    525   -335       O  
ATOM   1293  OD2 ASP B  94      -7.979 -48.516   0.512  1.00 22.36           O  
ANISOU 1293  OD2 ASP B  94     3159   2581   2756   -421    897   -292       O  
ATOM   1294  N   LYS B  95      -9.858 -50.971   4.405  1.00 22.32           N  
ANISOU 1294  N   LYS B  95     2934   2668   2879     90   1135     28       N  
ATOM   1295  CA  LYS B  95      -9.046 -51.825   5.272  1.00 23.65           C  
ANISOU 1295  CA  LYS B  95     3015   2744   3228    -86   1344     93       C  
ATOM   1296  C   LYS B  95      -7.608 -51.984   4.780  1.00 21.65           C  
ANISOU 1296  C   LYS B  95     2631   2606   2990   -204   1248     77       C  
ATOM   1297  O   LYS B  95      -6.740 -52.377   5.548  1.00 23.38           O  
ANISOU 1297  O   LYS B  95     2856   3029   2997   -158   1101    159       O  
ATOM   1298  CB  LYS B  95      -9.680 -53.207   5.412  1.00 27.04           C  
ANISOU 1298  CB  LYS B  95     3446   2781   4045   -137   1343    448       C  
ATOM   1299  CG  LYS B  95      -9.621 -54.048   4.150  1.00 31.81           C  
ANISOU 1299  CG  LYS B  95     3943   2998   5146   -724   1048    256       C  
ATOM   1300  CD  LYS B  95     -10.305 -55.392   4.363  1.00 36.48           C  
ANISOU 1300  CD  LYS B  95     4343   3689   5829   -882    721    185       C  
ATOM   1301  CE  LYS B  95     -10.041 -56.323   3.194  1.00 42.18           C  
ANISOU 1301  CE  LYS B  95     5230   4548   6249   -921    811    170       C  
ATOM   1302  NZ  LYS B  95     -10.416 -55.683   1.902  1.00 45.45           N  
ANISOU 1302  NZ  LYS B  95     5756   5075   6439   -998    790    143       N  
ATOM   1303  N   ASN B  96      -7.357 -51.678   3.508  1.00 20.40           N  
ANISOU 1303  N   ASN B  96     2542   2522   2687   -177   1186   -211       N  
ATOM   1304  CA  ASN B  96      -6.009 -51.755   2.943  1.00 19.08           C  
ANISOU 1304  CA  ASN B  96     2561   2437   2252   -414    419   -401       C  
ATOM   1305  C   ASN B  96      -5.189 -50.481   3.112  1.00 19.06           C  
ANISOU 1305  C   ASN B  96     2763   2247   2231   -122    432   -119       C  
ATOM   1306  O   ASN B  96      -4.068 -50.403   2.607  1.00 18.00           O  
ANISOU 1306  O   ASN B  96     2588   2293   1959   -255    486   -168       O  
ATOM   1307  CB  ASN B  96      -6.084 -52.072   1.451  1.00 20.67           C  
ANISOU 1307  CB  ASN B  96     2765   2533   2555   -298    542   -853       C  
ATOM   1308  CG  ASN B  96      -6.732 -53.386   1.175  1.00 26.09           C  
ANISOU 1308  CG  ASN B  96     3201   3164   3547   -675    949  -1089       C  
ATOM   1309  OD1 ASN B  96      -6.522 -54.352   1.904  1.00 28.11           O  
ANISOU 1309  OD1 ASN B  96     3950   2620   4110   -692   1596   -452       O  
ATOM   1310  ND2 ASN B  96      -7.527 -53.445   0.108  1.00 30.00           N  
ANISOU 1310  ND2 ASN B  96     3384   3964   4050   -749   1029  -1391       N  
ATOM   1311  N   ALA B  97      -5.747 -49.486   3.798  1.00 19.63           N  
ANISOU 1311  N   ALA B  97     2949   2226   2283   -193    788    -29       N  
ATOM   1312  CA  ALA B  97      -5.142 -48.151   3.841  1.00 18.62           C  
ANISOU 1312  CA  ALA B  97     2581   2257   2237   -106    832   -280       C  
ATOM   1313  C   ALA B  97      -3.684 -48.181   4.271  1.00 17.63           C  
ANISOU 1313  C   ALA B  97     2477   2339   1883   -396    769   -282       C  
ATOM   1314  O   ALA B  97      -3.305 -48.924   5.186  1.00 18.47           O  
ANISOU 1314  O   ALA B  97     3012   2037   1968   -202    831    -76       O  
ATOM   1315  CB  ALA B  97      -5.928 -47.246   4.777  1.00 18.20           C  
ANISOU 1315  CB  ALA B  97     2502   2008   2404    248    975   -436       C  
ATOM   1316  N   ILE B  98      -2.868 -47.373   3.599  1.00 17.28           N  
ANISOU 1316  N   ILE B  98     2089   2488   1989   -427    623   -490       N  
ATOM   1317  CA  ILE B  98      -1.489 -47.187   3.998  1.00 15.59           C  
ANISOU 1317  CA  ILE B  98     2126   1824   1973   -206    720   -467       C  
ATOM   1318  C   ILE B  98      -1.249 -45.697   4.146  1.00 17.88           C  
ANISOU 1318  C   ILE B  98     2661   1930   2204    -32    616   -405       C  
ATOM   1319  O   ILE B  98      -1.310 -44.944   3.167  1.00 17.44           O  
ANISOU 1319  O   ILE B  98     2807   1851   1968     69    416   -489       O  
ATOM   1320  CB  ILE B  98      -0.495 -47.816   2.985  1.00 15.15           C  
ANISOU 1320  CB  ILE B  98     2200   1662   1892    -78    116   -284       C  
ATOM   1321  CG1 ILE B  98      -0.694 -49.332   2.947  1.00 15.79           C  
ANISOU 1321  CG1 ILE B  98     2566   1427   2008     18    575   -391       C  
ATOM   1322  CG2 ILE B  98       0.958 -47.503   3.375  1.00 16.51           C  
ANISOU 1322  CG2 ILE B  98     2267   2003   2003   -385    -79   -345       C  
ATOM   1323  CD1 ILE B  98       0.016 -49.989   1.777  1.00 16.25           C  
ANISOU 1323  CD1 ILE B  98     2494   1516   2164     90    512   -432       C  
ATOM   1324  N   LYS B  99      -1.038 -45.280   5.389  1.00 17.73           N  
ANISOU 1324  N   LYS B  99     2704   1889   2144   -162    258   -726       N  
ATOM   1325  CA  LYS B  99      -0.698 -43.902   5.701  1.00 18.11           C  
ANISOU 1325  CA  LYS B  99     2913   1996   1971   -142    325   -656       C  
ATOM   1326  C   LYS B  99       0.714 -43.609   5.236  1.00 16.91           C  
ANISOU 1326  C   LYS B  99     2281   1818   2325   -125    -19   -587       C  
ATOM   1327  O   LYS B  99       1.577 -44.495   5.216  1.00 18.95           O  
ANISOU 1327  O   LYS B  99     2467   2085   2648    136    247   -324       O  
ATOM   1328  CB  LYS B  99      -0.811 -43.630   7.208  1.00 19.57           C  
ANISOU 1328  CB  LYS B  99     3443   2525   1466    129    455   -526       C  
ATOM   1329  CG  LYS B  99      -2.177 -43.930   7.792  1.00 22.27           C  
ANISOU 1329  CG  LYS B  99     3625   3032   1806     45    497   -656       C  
ATOM   1330  CD  LYS B  99      -2.131 -44.005   9.320  1.00 27.34           C  
ANISOU 1330  CD  LYS B  99     4226   3676   2486   -445    549  -1311       C  
ATOM   1331  CE  LYS B  99      -1.619 -42.749   9.942  1.00 30.75           C  
ANISOU 1331  CE  LYS B  99     4686   4456   2540   -157    342   -826       C  
ATOM   1332  NZ  LYS B  99      -1.535 -42.935  11.428  1.00 33.40           N  
ANISOU 1332  NZ  LYS B  99     5174   5038   2478    187     75  -1045       N  
ATOM   1333  N   VAL B 100       0.944 -42.355   4.859  1.00 18.19           N  
ANISOU 1333  N   VAL B 100     2665   1943   2303   -390     43   -481       N  
ATOM   1334  CA  VAL B 100       2.292 -41.883   4.616  1.00 16.01           C  
ANISOU 1334  CA  VAL B 100     2503   1891   1689   -111   -249   -475       C  
ATOM   1335  C   VAL B 100       2.587 -40.822   5.663  1.00 17.36           C  
ANISOU 1335  C   VAL B 100     2799   1910   1885    -76   -315   -341       C  
ATOM   1336  O   VAL B 100       1.892 -39.812   5.724  1.00 19.67           O  
ANISOU 1336  O   VAL B 100     3214   2000   2259     32   -515   -552       O  
ATOM   1337  CB  VAL B 100       2.464 -41.322   3.201  1.00 18.35           C  
ANISOU 1337  CB  VAL B 100     2777   2149   2047   -178   -317   -715       C  
ATOM   1338  CG1 VAL B 100       3.888 -40.808   3.005  1.00 20.77           C  
ANISOU 1338  CG1 VAL B 100     2940   2296   2654   -134    -96   -452       C  
ATOM   1339  CG2 VAL B 100       2.143 -42.407   2.180  1.00 18.48           C  
ANISOU 1339  CG2 VAL B 100     3081   2171   1770    164    -67   -316       C  
ATOM   1340  N   ASN B 101       3.576 -41.092   6.512  1.00 18.81           N  
ANISOU 1340  N   ASN B 101     3077   2167   1904   -423   -395   -392       N  
ATOM   1341  CA  ASN B 101       3.987 -40.175   7.566  1.00 19.76           C  
ANISOU 1341  CA  ASN B 101     2939   2282   2287   -357   -488   -225       C  
ATOM   1342  C   ASN B 101       5.327 -39.541   7.262  1.00 20.88           C  
ANISOU 1342  C   ASN B 101     2856   2386   2692   -527   -721   -276       C  
ATOM   1343  O   ASN B 101       6.162 -40.134   6.569  1.00 22.65           O  
ANISOU 1343  O   ASN B 101     3165   2626   2815   -178   -436   -362       O  
ATOM   1344  CB  ASN B 101       4.090 -40.893   8.912  1.00 21.02           C  
ANISOU 1344  CB  ASN B 101     3373   2554   2058    -74   -433    101       C  
ATOM   1345  CG  ASN B 101       2.786 -41.516   9.343  1.00 21.65           C  
ANISOU 1345  CG  ASN B 101     3446   2616   2163    202   -285   -127       C  
ATOM   1346  OD1 ASN B 101       1.713 -40.991   9.064  1.00 22.48           O  
ANISOU 1346  OD1 ASN B 101     3469   2499   2573    232   -284   -386       O  
ATOM   1347  ND2 ASN B 101       2.872 -42.641  10.040  1.00 23.96           N  
ANISOU 1347  ND2 ASN B 101     3888   2820   2396    189    102    -71       N  
ATOM   1348  N   ASN B 102       5.562 -38.353   7.806  1.00 21.57           N  
ANISOU 1348  N   ASN B 102     3062   2199   2934   -457   -850  -1066       N  
ATOM   1349  CA  ASN B 102       6.854 -37.722   7.580  1.00 25.17           C  
ANISOU 1349  CA  ASN B 102     3564   2620   3378   -650   -771  -1199       C  
ATOM   1350  C   ASN B 102       7.872 -38.163   8.627  1.00 28.41           C  
ANISOU 1350  C   ASN B 102     3818   3232   3745   -400   -899  -1276       C  
ATOM   1351  O   ASN B 102       7.568 -39.007   9.471  1.00 28.13           O  
ANISOU 1351  O   ASN B 102     3840   3211   3637    191  -1098   -982       O  
ATOM   1352  CB  ASN B 102       6.723 -36.189   7.535  1.00 25.15           C  
ANISOU 1352  CB  ASN B 102     4044   2282   3231   -531    -48  -1226       C  
ATOM   1353  CG  ASN B 102       6.290 -35.559   8.864  1.00 25.98           C  
ANISOU 1353  CG  ASN B 102     4226   2485   3159   -765    149  -1117       C  
ATOM   1354  OD1 ASN B 102       6.331 -36.175   9.925  1.00 24.58           O  
ANISOU 1354  OD1 ASN B 102     3509   2960   2871   -737   -451   -826       O  
ATOM   1355  ND2 ASN B 102       5.890 -34.292   8.792  1.00 27.34           N  
ANISOU 1355  ND2 ASN B 102     4537   2464   3386   -697    673  -1328       N  
ATOM   1356  N   VAL B 103       9.074 -37.593   8.559  1.00 30.70           N  
ANISOU 1356  N   VAL B 103     3775   3960   3932   -776  -1116  -1429       N  
ATOM   1357  CA  VAL B 103      10.162 -37.944   9.469  1.00 36.49           C  
ANISOU 1357  CA  VAL B 103     4489   4873   4502   -686   -363  -1518       C  
ATOM   1358  C   VAL B 103       9.802 -37.768  10.941  1.00 39.44           C  
ANISOU 1358  C   VAL B 103     4799   5836   4351   -174   -817  -1366       C  
ATOM   1359  O   VAL B 103      10.389 -38.415  11.804  1.00 43.14           O  
ANISOU 1359  O   VAL B 103     5121   6690   4579    112   -518  -1262       O  
ATOM   1360  CB  VAL B 103      11.428 -37.110   9.176  1.00 38.63           C  
ANISOU 1360  CB  VAL B 103     4733   4767   5178  -1076    238  -1672       C  
ATOM   1361  CG1 VAL B 103      12.041 -37.524   7.849  1.00 40.51           C  
ANISOU 1361  CG1 VAL B 103     4996   4768   5628   -964    499  -1372       C  
ATOM   1362  CG2 VAL B 103      11.100 -35.623   9.180  1.00 40.63           C  
ANISOU 1362  CG2 VAL B 103     4735   4871   5833  -1577    525  -1678       C  
ATOM   1363  N   ASN B 104       8.834 -36.903  11.224  1.00 37.43           N  
ANISOU 1363  N   ASN B 104     4878   5665   3678   -100  -1557  -1992       N  
ATOM   1364  CA  ASN B 104       8.428 -36.638  12.601  1.00 40.86           C  
ANISOU 1364  CA  ASN B 104     5536   6003   3985   -308  -1589  -1930       C  
ATOM   1365  C   ASN B 104       7.249 -37.497  13.058  1.00 38.70           C  
ANISOU 1365  C   ASN B 104     5871   5762   3071    -77  -1536  -1282       C  
ATOM   1366  O   ASN B 104       6.811 -37.391  14.199  1.00 39.81           O  
ANISOU 1366  O   ASN B 104     6191   6302   2634    197  -1523  -1014       O  
ATOM   1367  CB  ASN B 104       8.075 -35.159  12.774  1.00 45.54           C  
ANISOU 1367  CB  ASN B 104     5881   6260   5161   -777  -1583  -2355       C  
ATOM   1368  CG  ASN B 104       9.276 -34.246  12.615  1.00 51.69           C  
ANISOU 1368  CG  ASN B 104     6943   6472   6224   -766   -562  -2180       C  
ATOM   1369  OD1 ASN B 104      10.351 -34.513  13.155  1.00 52.35           O  
ANISOU 1369  OD1 ASN B 104     6868   6525   6499   -861  -1164  -2229       O  
ATOM   1370  ND2 ASN B 104       9.097 -33.159  11.870  1.00 54.18           N  
ANISOU 1370  ND2 ASN B 104     7542   6534   6511   -710    484  -1976       N  
ATOM   1371  N   GLY B 105       6.727 -38.333  12.166  1.00 36.99           N  
ANISOU 1371  N   GLY B 105     5723   5065   3267    143  -1327   -697       N  
ATOM   1372  CA  GLY B 105       5.619 -39.212  12.507  1.00 34.52           C  
ANISOU 1372  CA  GLY B 105     5221   4678   3219     14  -1180   -253       C  
ATOM   1373  C   GLY B 105       4.243 -38.630  12.225  1.00 32.13           C  
ANISOU 1373  C   GLY B 105     4717   4326   3165   -361  -1051   -412       C  
ATOM   1374  O   GLY B 105       3.219 -39.245  12.528  1.00 33.37           O  
ANISOU 1374  O   GLY B 105     4764   4548   3369   -710   -542   -167       O  
ATOM   1375  N   ASN B 106       4.221 -37.442  11.636  1.00 28.38           N  
ANISOU 1375  N   ASN B 106     4300   3630   2853     -4  -1228   -430       N  
ATOM   1376  CA  ASN B 106       2.980 -36.750  11.318  1.00 28.45           C  
ANISOU 1376  CA  ASN B 106     4500   3705   2606   -641   -974   -958       C  
ATOM   1377  C   ASN B 106       2.456 -37.199   9.957  1.00 24.23           C  
ANISOU 1377  C   ASN B 106     3934   2975   2296   -390   -790   -804       C  
ATOM   1378  O   ASN B 106       3.224 -37.270   8.992  1.00 24.30           O  
ANISOU 1378  O   ASN B 106     4065   2950   2216   -446   -226   -845       O  
ATOM   1379  CB  ASN B 106       3.222 -35.239  11.327  1.00 34.60           C  
ANISOU 1379  CB  ASN B 106     5491   4206   3451   -815   -843  -1962       C  
ATOM   1380  CG  ASN B 106       1.938 -34.427  11.353  1.00 48.54           C  
ANISOU 1380  CG  ASN B 106     7191   5467   5784  -1362    495  -1930       C  
ATOM   1381  OD1 ASN B 106       0.838 -34.968  11.453  1.00 51.37           O  
ANISOU 1381  OD1 ASN B 106     7308   5782   6428  -1785    436  -1670       O  
ATOM   1382  ND2 ASN B 106       2.080 -33.107  11.277  1.00 55.96           N  
ANISOU 1382  ND2 ASN B 106     8035   6212   7015  -1356   1405  -2034       N  
ATOM   1383  N   GLN B 107       1.163 -37.505   9.873  1.00 23.16           N  
ANISOU 1383  N   GLN B 107     3877   2537   2384    -56   -539   -468       N  
ATOM   1384  CA  GLN B 107       0.604 -37.976   8.616  1.00 20.47           C  
ANISOU 1384  CA  GLN B 107     3086   2638   2053      6   -795   -698       C  
ATOM   1385  C   GLN B 107       0.629 -36.886   7.552  1.00 20.23           C  
ANISOU 1385  C   GLN B 107     3351   2366   1969    295   -267   -694       C  
ATOM   1386  O   GLN B 107       0.274 -35.724   7.804  1.00 22.09           O  
ANISOU 1386  O   GLN B 107     3757   2331   2305    275   -426   -779       O  
ATOM   1387  CB  GLN B 107      -0.829 -38.495   8.785  1.00 22.06           C  
ANISOU 1387  CB  GLN B 107     3048   2906   2427   -329   -571   -897       C  
ATOM   1388  CG  GLN B 107      -1.335 -39.162   7.503  1.00 20.91           C  
ANISOU 1388  CG  GLN B 107     2593   2881   2470   -356   -470   -914       C  
ATOM   1389  CD  GLN B 107      -2.591 -39.980   7.692  1.00 21.99           C  
ANISOU 1389  CD  GLN B 107     2935   2762   2657   -209    -94   -386       C  
ATOM   1390  OE1 GLN B 107      -3.181 -40.010   8.777  1.00 24.74           O  
ANISOU 1390  OE1 GLN B 107     3416   3019   2964     -4   -142    -31       O  
ATOM   1391  NE2 GLN B 107      -3.016 -40.647   6.624  1.00 19.45           N  
ANISOU 1391  NE2 GLN B 107     2562   2383   2445    -49   -225   -351       N  
ATOM   1392  N   VAL B 108       1.069 -37.285   6.363  1.00 20.45           N  
ANISOU 1392  N   VAL B 108     3135   2518   2116    156   -379   -706       N  
ATOM   1393  CA  VAL B 108       1.146 -36.430   5.186  1.00 21.51           C  
ANISOU 1393  CA  VAL B 108     3294   2471   2407      8   -377   -584       C  
ATOM   1394  C   VAL B 108      -0.031 -36.694   4.239  1.00 18.96           C  
ANISOU 1394  C   VAL B 108     3203   1719   2280    129   -427   -629       C  
ATOM   1395  O   VAL B 108      -0.614 -35.780   3.665  1.00 19.34           O  
ANISOU 1395  O   VAL B 108     3482   1899   1969    327   -468   -618       O  
ATOM   1396  CB  VAL B 108       2.492 -36.676   4.449  1.00 22.20           C  
ANISOU 1396  CB  VAL B 108     2814   3131   2491   -290   -524   -134       C  
ATOM   1397  CG1 VAL B 108       2.565 -35.926   3.124  1.00 23.38           C  
ANISOU 1397  CG1 VAL B 108     3205   3270   2408    118     -6   -199       C  
ATOM   1398  CG2 VAL B 108       3.650 -36.300   5.356  1.00 24.64           C  
ANISOU 1398  CG2 VAL B 108     3127   3530   2705   -839   -489   -417       C  
ATOM   1399  N   GLY B 109      -0.365 -37.968   4.073  1.00 19.65           N  
ANISOU 1399  N   GLY B 109     3442   1436   2589   -154   -172   -769       N  
ATOM   1400  CA  GLY B 109      -1.452 -38.380   3.196  1.00 18.48           C  
ANISOU 1400  CA  GLY B 109     3245   1459   2316   -137   -311   -753       C  
ATOM   1401  C   GLY B 109      -1.603 -39.890   3.238  1.00 17.81           C  
ANISOU 1401  C   GLY B 109     2836   1672   2261    246   -239   -698       C  
ATOM   1402  O   GLY B 109      -1.214 -40.532   4.221  1.00 19.77           O  
ANISOU 1402  O   GLY B 109     3243   2059   2209    186   -200   -646       O  
ATOM   1403  N   HIS B 110      -2.190 -40.441   2.180  1.00 17.63           N  
ANISOU 1403  N   HIS B 110     2707   1740   2253    -24    -58   -609       N  
ATOM   1404  CA  HIS B 110      -2.332 -41.886   2.001  1.00 16.67           C  
ANISOU 1404  CA  HIS B 110     2402   1620   2311    -59    107   -703       C  
ATOM   1405  C   HIS B 110      -1.750 -42.314   0.670  1.00 15.53           C  
ANISOU 1405  C   HIS B 110     2617   1407   1875     31    -66   -647       C  
ATOM   1406  O   HIS B 110      -1.666 -41.512  -0.258  1.00 17.63           O  
ANISOU 1406  O   HIS B 110     3023   1537   2138    115     19   -382       O  
ATOM   1407  CB  HIS B 110      -3.806 -42.308   2.035  1.00 18.35           C  
ANISOU 1407  CB  HIS B 110     2333   2292   2347   -161    155   -852       C  
ATOM   1408  CG  HIS B 110      -4.382 -42.445   3.408  1.00 18.36           C  
ANISOU 1408  CG  HIS B 110     2450   2415   2110    106    475   -692       C  
ATOM   1409  ND1 HIS B 110      -5.295 -41.547   3.921  1.00 19.59           N  
ANISOU 1409  ND1 HIS B 110     2742   2419   2281    111    481  -1067       N  
ATOM   1410  CD2 HIS B 110      -4.205 -43.390   4.363  1.00 20.15           C  
ANISOU 1410  CD2 HIS B 110     2662   2717   2276     14    434   -789       C  
ATOM   1411  CE1 HIS B 110      -5.643 -41.925   5.140  1.00 20.60           C  
ANISOU 1411  CE1 HIS B 110     2766   2888   2174     96    221   -769       C  
ATOM   1412  NE2 HIS B 110      -4.996 -43.039   5.432  1.00 21.73           N  
ANISOU 1412  NE2 HIS B 110     2747   3035   2475   -113    330   -433       N  
ATOM   1413  N   LEU B 111      -1.376 -43.583   0.550  1.00 15.00           N  
ANISOU 1413  N   LEU B 111     2249   1423   2027    108    369   -566       N  
ATOM   1414  CA  LEU B 111      -1.132 -44.131  -0.781  1.00 14.35           C  
ANISOU 1414  CA  LEU B 111     2482   1397   1575    155    292   -534       C  
ATOM   1415  C   LEU B 111      -2.455 -44.211  -1.540  1.00 16.13           C  
ANISOU 1415  C   LEU B 111     2489   1758   1880   -138    532   -630       C  
ATOM   1416  O   LEU B 111      -3.503 -44.419  -0.925  1.00 16.14           O  
ANISOU 1416  O   LEU B 111     2451   1955   1727   -177    394   -518       O  
ATOM   1417  CB  LEU B 111      -0.483 -45.512  -0.707  1.00 14.94           C  
ANISOU 1417  CB  LEU B 111     2667   1288   1723    195     -6   -152       C  
ATOM   1418  CG  LEU B 111       0.924 -45.599  -0.103  1.00 15.86           C  
ANISOU 1418  CG  LEU B 111     2536   1547   1943    181    147      4       C  
ATOM   1419  CD1 LEU B 111       1.504 -47.006  -0.291  1.00 16.91           C  
ANISOU 1419  CD1 LEU B 111     2581   1523   2321    247    345   -203       C  
ATOM   1420  CD2 LEU B 111       1.835 -44.552  -0.728  1.00 17.57           C  
ANISOU 1420  CD2 LEU B 111     2663   1703   2308   -131    335     91       C  
ATOM   1421  N   LYS B 112      -2.418 -44.026  -2.864  1.00 16.27           N  
ANISOU 1421  N   LYS B 112     2720   1722   1738    148    386   -187       N  
ATOM   1422  CA ALYS B 112      -3.619 -44.205  -3.683  0.44 17.06           C  
ANISOU 1422  CA ALYS B 112     2680   1801   2001     96    453    -13       C  
ATOM   1423  CA BLYS B 112      -3.615 -44.183  -3.680  0.56 17.55           C  
ANISOU 1423  CA BLYS B 112     2729   2018   1921    137    302    105       C  
ATOM   1424  C   LYS B 112      -4.220 -45.563  -3.403  1.00 15.91           C  
ANISOU 1424  C   LYS B 112     2387   1836   1823      3     91   -251       C  
ATOM   1425  O   LYS B 112      -3.490 -46.530  -3.216  1.00 16.74           O  
ANISOU 1425  O   LYS B 112     2573   1794   1994    209     72   -636       O  
ATOM   1426  CB ALYS B 112      -3.318 -44.087  -5.176  0.44 20.71           C  
ANISOU 1426  CB ALYS B 112     3178   2270   2422    -29   1071     68       C  
ATOM   1427  CB BLYS B 112      -3.281 -44.006  -5.166  0.56 22.90           C  
ANISOU 1427  CB BLYS B 112     3387   3002   2312    120    745    268       C  
ATOM   1428  CG ALYS B 112      -3.151 -42.677  -5.666  0.44 21.48           C  
ANISOU 1428  CG ALYS B 112     3270   2480   2413   -564   1198   -161       C  
ATOM   1429  CG BLYS B 112      -4.327 -43.245  -5.972  0.56 26.14           C  
ANISOU 1429  CG BLYS B 112     3611   3669   2651   -498    679    145       C  
ATOM   1430  CD ALYS B 112      -3.175 -42.607  -7.189  0.44 24.09           C  
ANISOU 1430  CD ALYS B 112     3855   2885   2413   -568    891    114       C  
ATOM   1431  CD BLYS B 112      -3.806 -42.826  -7.348  0.56 29.03           C  
ANISOU 1431  CD BLYS B 112     4161   3576   3293   -783    755    101       C  
ATOM   1432  CE ALYS B 112      -4.593 -42.761  -7.741  0.44 28.70           C  
ANISOU 1432  CE ALYS B 112     4314   3329   3262    -14   1175     19       C  
ATOM   1433  CE BLYS B 112      -3.137 -41.452  -7.323  0.56 29.51           C  
ANISOU 1433  CE BLYS B 112     4267   3534   3411   -735    539   -147       C  
ATOM   1434  NZ ALYS B 112      -5.540 -41.731  -7.220  0.44 32.19           N  
ANISOU 1434  NZ ALYS B 112     4788   3830   3614    483   1271   -199       N  
ATOM   1435  NZ BLYS B 112      -2.774 -40.963  -8.690  0.56 32.56           N  
ANISOU 1435  NZ BLYS B 112     4432   3731   4208   -745    654    185       N  
ATOM   1436  N   LYS B 113      -5.548 -45.640  -3.383  1.00 16.67           N  
ANISOU 1436  N   LYS B 113     2263   2182   1891   -230    235   -537       N  
ATOM   1437  CA  LYS B 113      -6.213 -46.886  -3.004  1.00 16.76           C  
ANISOU 1437  CA  LYS B 113     2222   2162   1985    121    211   -470       C  
ATOM   1438  C   LYS B 113      -5.831 -48.066  -3.908  1.00 16.22           C  
ANISOU 1438  C   LYS B 113     2380   2119   1662    183    415   -303       C  
ATOM   1439  O   LYS B 113      -5.715 -49.188  -3.420  1.00 16.97           O  
ANISOU 1439  O   LYS B 113     2502   2084   1861    196    457   -188       O  
ATOM   1440  CB  LYS B 113      -7.734 -46.706  -2.965  1.00 21.50           C  
ANISOU 1440  CB  LYS B 113     2590   2776   2804    832    323   -376       C  
ATOM   1441  CG  LYS B 113      -8.411 -46.379  -4.276  1.00 23.57           C  
ANISOU 1441  CG  LYS B 113     2318   3105   3532    731     22   -641       C  
ATOM   1442  CD  LYS B 113      -9.930 -46.259  -4.081  1.00 29.89           C  
ANISOU 1442  CD  LYS B 113     3248   3392   4719    760    120   -446       C  
ATOM   1443  CE  LYS B 113     -10.608 -45.748  -5.335  1.00 35.02           C  
ANISOU 1443  CE  LYS B 113     4109   4019   5176    352   -273   -295       C  
ATOM   1444  NZ  LYS B 113     -10.277 -44.303  -5.559  1.00 38.12           N  
ANISOU 1444  NZ  LYS B 113     4793   4383   5309    512   -303   -252       N  
ATOM   1445  N   GLU B 114      -5.593 -47.829  -5.200  1.00 14.34           N  
ANISOU 1445  N   GLU B 114     2137   1736   1576    -96    272   -572       N  
ATOM   1446  CA  GLU B 114      -5.210 -48.944  -6.074  1.00 13.93           C  
ANISOU 1446  CA  GLU B 114     2409   1582   1301   -101     -8   -432       C  
ATOM   1447  C   GLU B 114      -3.822 -49.490  -5.714  1.00 15.02           C  
ANISOU 1447  C   GLU B 114     2294   1499   1912   -335    -14   -423       C  
ATOM   1448  O   GLU B 114      -3.582 -50.700  -5.815  1.00 16.78           O  
ANISOU 1448  O   GLU B 114     2391   1841   2143    -46    451   -314       O  
ATOM   1449  CB  GLU B 114      -5.240 -48.531  -7.544  1.00 16.18           C  
ANISOU 1449  CB  GLU B 114     2771   1989   1390   -203   -113   -229       C  
ATOM   1450  CG  GLU B 114      -6.614 -48.135  -8.069  1.00 18.39           C  
ANISOU 1450  CG  GLU B 114     2757   2305   1926    340   -684   -373       C  
ATOM   1451  CD  GLU B 114      -6.992 -46.664  -7.844  1.00 23.62           C  
ANISOU 1451  CD  GLU B 114     3550   2800   2626    567   -812   -336       C  
ATOM   1452  OE1 GLU B 114      -6.354 -45.948  -7.029  1.00 22.81           O  
ANISOU 1452  OE1 GLU B 114     3506   2728   2434    232    -76   -131       O  
ATOM   1453  OE2 GLU B 114      -7.959 -46.222  -8.501  1.00 28.78           O  
ANISOU 1453  OE2 GLU B 114     4173   3093   3670    957  -1170   -589       O  
ATOM   1454  N   LEU B 115      -2.914 -48.606  -5.303  1.00 15.12           N  
ANISOU 1454  N   LEU B 115     2331   1679   1733   -174    216   -275       N  
ATOM   1455  CA  LEU B 115      -1.581 -49.023  -4.880  1.00 14.67           C  
ANISOU 1455  CA  LEU B 115     1838   1746   1989   -232     17     64       C  
ATOM   1456  C   LEU B 115      -1.634 -49.696  -3.506  1.00 14.86           C  
ANISOU 1456  C   LEU B 115     1904   2122   1618    227    164    139       C  
ATOM   1457  O   LEU B 115      -1.013 -50.749  -3.302  1.00 14.84           O  
ANISOU 1457  O   LEU B 115     2055   1750   1834    103    229    -52       O  
ATOM   1458  CB  LEU B 115      -0.615 -47.835  -4.863  1.00 14.81           C  
ANISOU 1458  CB  LEU B 115     1782   2025   1819   -354    222    -37       C  
ATOM   1459  CG  LEU B 115       0.811 -48.110  -4.386  1.00 17.68           C  
ANISOU 1459  CG  LEU B 115     1821   2889   2010   -287    407    162       C  
ATOM   1460  CD1 LEU B 115       1.499 -49.139  -5.304  1.00 20.66           C  
ANISOU 1460  CD1 LEU B 115     2504   3588   1759    281   1008   -362       C  
ATOM   1461  CD2 LEU B 115       1.637 -46.819  -4.290  1.00 20.35           C  
ANISOU 1461  CD2 LEU B 115     2105   3247   2380   -944    422    289       C  
ATOM   1462  N   ALA B 116      -2.386 -49.113  -2.570  1.00 14.88           N  
ANISOU 1462  N   ALA B 116     2227   1961   1466     16    473   -141       N  
ATOM   1463  CA  ALA B 116      -2.580 -49.743  -1.260  1.00 15.41           C  
ANISOU 1463  CA  ALA B 116     2234   2014   1606    -29    528   -268       C  
ATOM   1464  C   ALA B 116      -3.194 -51.138  -1.393  1.00 15.51           C  
ANISOU 1464  C   ALA B 116     2223   1917   1753   -126    174   -167       C  
ATOM   1465  O   ALA B 116      -2.877 -52.047  -0.616  1.00 17.43           O  
ANISOU 1465  O   ALA B 116     2592   2042   1988   -160    458    -64       O  
ATOM   1466  CB  ALA B 116      -3.455 -48.865  -0.369  1.00 17.04           C  
ANISOU 1466  CB  ALA B 116     2526   2190   1756    170    788   -256       C  
ATOM   1467  N   GLY B 117      -4.089 -51.295  -2.365  1.00 15.99           N  
ANISOU 1467  N   GLY B 117     2246   1852   1979   -244    478   -434       N  
ATOM   1468  CA  GLY B 117      -4.729 -52.574  -2.619  1.00 16.13           C  
ANISOU 1468  CA  GLY B 117     2107   1768   2254   -174    659   -235       C  
ATOM   1469  C   GLY B 117      -3.743 -53.669  -2.967  1.00 16.89           C  
ANISOU 1469  C   GLY B 117     2274   2089   2055   -301    361    128       C  
ATOM   1470  O   GLY B 117      -3.984 -54.855  -2.697  1.00 18.47           O  
ANISOU 1470  O   GLY B 117     2872   1944   2202    -85    641    159       O  
ATOM   1471  N   ALA B 118      -2.636 -53.274  -3.584  1.00 15.63           N  
ANISOU 1471  N   ALA B 118     1794   2142   2005   -391    455   -464       N  
ATOM   1472  CA  ALA B 118      -1.573 -54.208  -3.916  1.00 15.93           C  
ANISOU 1472  CA  ALA B 118     2213   1988   1852   -403    730   -387       C  
ATOM   1473  C   ALA B 118      -0.604 -54.409  -2.753  1.00 15.36           C  
ANISOU 1473  C   ALA B 118     2410   1749   1678   -298    366    -29       C  
ATOM   1474  O   ALA B 118      -0.173 -55.535  -2.479  1.00 17.55           O  
ANISOU 1474  O   ALA B 118     2538   1757   2374   -231    437     55       O  
ATOM   1475  CB  ALA B 118      -0.817 -53.718  -5.150  1.00 15.46           C  
ANISOU 1475  CB  ALA B 118     2095   1890   1888   -144    626   -430       C  
ATOM   1476  N   LEU B 119      -0.246 -53.324  -2.072  1.00 14.57           N  
ANISOU 1476  N   LEU B 119     2240   1554   1741   -244    494   -325       N  
ATOM   1477  CA  LEU B 119       0.842 -53.379  -1.091  1.00 14.49           C  
ANISOU 1477  CA  LEU B 119     2064   1506   1936   -260    465    115       C  
ATOM   1478  C   LEU B 119       0.431 -53.870   0.291  1.00 15.09           C  
ANISOU 1478  C   LEU B 119     2048   1770   1914   -255    588    357       C  
ATOM   1479  O   LEU B 119       1.278 -54.348   1.032  1.00 17.13           O  
ANISOU 1479  O   LEU B 119     2587   1926   1998     80    575    287       O  
ATOM   1480  CB  LEU B 119       1.508 -52.008  -0.929  1.00 14.37           C  
ANISOU 1480  CB  LEU B 119     2111   1334   2013   -258    518    185       C  
ATOM   1481  CG  LEU B 119       2.137 -51.402  -2.185  1.00 17.73           C  
ANISOU 1481  CG  LEU B 119     2640   1736   2362   -552   1227     45       C  
ATOM   1482  CD1 LEU B 119       2.970 -50.172  -1.825  1.00 16.28           C  
ANISOU 1482  CD1 LEU B 119     2346   1407   2432   -588    206    197       C  
ATOM   1483  CD2 LEU B 119       2.963 -52.412  -2.970  1.00 21.69           C  
ANISOU 1483  CD2 LEU B 119     3327   2208   2707   -501   1047   -135       C  
ATOM   1484  N   ALA B 120      -0.843 -53.748   0.655  1.00 15.92           N  
ANISOU 1484  N   ALA B 120     1994   2156   1901   -367    776    189       N  
ATOM   1485  CA  ALA B 120      -1.240 -54.098   2.019  1.00 18.16           C  
ANISOU 1485  CA  ALA B 120     2341   2409   2151     95    872    490       C  
ATOM   1486  C   ALA B 120      -0.863 -55.552   2.342  1.00 17.85           C  
ANISOU 1486  C   ALA B 120     2433   2120   2229    134    739    307       C  
ATOM   1487  O   ALA B 120      -0.360 -55.855   3.424  1.00 18.77           O  
ANISOU 1487  O   ALA B 120     2743   2227   2163   -216    432    458       O  
ATOM   1488  CB  ALA B 120      -2.734 -53.868   2.225  1.00 20.14           C  
ANISOU 1488  CB  ALA B 120     2497   2687   2470    177    917    313       C  
ATOM   1489  N   TYR B 121      -1.081 -56.443   1.385  1.00 17.46           N  
ANISOU 1489  N   TYR B 121     2237   2168   2228   -100    386    405       N  
ATOM   1490  CA  TYR B 121      -0.755 -57.856   1.564  1.00 18.85           C  
ANISOU 1490  CA  TYR B 121     2670   2157   2335     37    321    605       C  
ATOM   1491  C   TYR B 121       0.741 -58.065   1.800  1.00 17.62           C  
ANISOU 1491  C   TYR B 121     2365   2210   2119   -107    733    491       C  
ATOM   1492  O   TYR B 121       1.159 -58.900   2.615  1.00 19.00           O  
ANISOU 1492  O   TYR B 121     2822   2005   2392   -174    416    401       O  
ATOM   1493  CB  TYR B 121      -1.223 -58.631   0.339  1.00 19.69           C  
ANISOU 1493  CB  TYR B 121     3109   1855   2516   -257   -114    296       C  
ATOM   1494  CG  TYR B 121      -0.943 -60.115   0.300  1.00 23.84           C  
ANISOU 1494  CG  TYR B 121     3743   2132   3182   -815   -433    441       C  
ATOM   1495  CD1 TYR B 121       0.262 -60.609  -0.197  1.00 22.27           C  
ANISOU 1495  CD1 TYR B 121     3917   1583   2960   -354   -734    648       C  
ATOM   1496  CD2 TYR B 121      -1.912 -61.023   0.691  1.00 28.38           C  
ANISOU 1496  CD2 TYR B 121     4589   2307   3887  -1014   -687    505       C  
ATOM   1497  CE1 TYR B 121       0.496 -61.971  -0.275  1.00 27.73           C  
ANISOU 1497  CE1 TYR B 121     4570   2181   3784   -436  -1289    677       C  
ATOM   1498  CE2 TYR B 121      -1.684 -62.374   0.620  1.00 30.56           C  
ANISOU 1498  CE2 TYR B 121     5006   1947   4657  -1165   -917    513       C  
ATOM   1499  CZ  TYR B 121      -0.478 -62.845   0.139  1.00 29.31           C  
ANISOU 1499  CZ  TYR B 121     4944   1856   4338   -845  -1602    547       C  
ATOM   1500  OH  TYR B 121      -0.268 -64.206   0.059  1.00 34.98           O  
ANISOU 1500  OH  TYR B 121     5902   2041   5348   -726  -1419    329       O  
ATOM   1501  N   ILE B 122       1.547 -57.310   1.067  1.00 15.49           N  
ANISOU 1501  N   ILE B 122     1964   1978   1944   -166    602    413       N  
ATOM   1502  CA  ILE B 122       2.987 -57.413   1.171  1.00 15.31           C  
ANISOU 1502  CA  ILE B 122     2337   1752   1729   -178    425     88       C  
ATOM   1503  C   ILE B 122       3.451 -56.932   2.545  1.00 16.55           C  
ANISOU 1503  C   ILE B 122     2519   1807   1961    -43    316    245       C  
ATOM   1504  O   ILE B 122       4.284 -57.566   3.174  1.00 17.37           O  
ANISOU 1504  O   ILE B 122     2748   1999   1854    -53    114    300       O  
ATOM   1505  CB  ILE B 122       3.661 -56.618   0.029  1.00 15.82           C  
ANISOU 1505  CB  ILE B 122     2074   2142   1794   -368    456    200       C  
ATOM   1506  CG1 ILE B 122       3.479 -57.383  -1.297  1.00 17.38           C  
ANISOU 1506  CG1 ILE B 122     2390   2372   1844    -33    294    474       C  
ATOM   1507  CG2 ILE B 122       5.141 -56.369   0.311  1.00 17.97           C  
ANISOU 1507  CG2 ILE B 122     2585   2139   2102    -55    456    602       C  
ATOM   1508  CD1 ILE B 122       3.723 -56.530  -2.549  1.00 17.26           C  
ANISOU 1508  CD1 ILE B 122     2444   2123   1993    161    493    688       C  
ATOM   1509  N   MET B 123       2.911 -55.806   3.010  1.00 17.13           N  
ANISOU 1509  N   MET B 123     3027   1581   1902   -206    568     52       N  
ATOM   1510  CA  MET B 123       3.268 -55.302   4.331  1.00 17.80           C  
ANISOU 1510  CA  MET B 123     3189   1442   2130   -358    792    325       C  
ATOM   1511  C   MET B 123       2.770 -56.218   5.455  1.00 18.77           C  
ANISOU 1511  C   MET B 123     3220   1814   2098   -355    464    336       C  
ATOM   1512  O   MET B 123       3.515 -56.524   6.390  1.00 19.69           O  
ANISOU 1512  O   MET B 123     3333   2162   1986   -236    226    461       O  
ATOM   1513  CB  MET B 123       2.723 -53.891   4.519  1.00 18.11           C  
ANISOU 1513  CB  MET B 123     3034   1506   2342   -320    641    305       C  
ATOM   1514  CG  MET B 123       3.335 -52.901   3.519  1.00 18.69           C  
ANISOU 1514  CG  MET B 123     2853   1608   2641   -432    456    604       C  
ATOM   1515  SD  MET B 123       2.852 -51.192   3.803  1.00 19.72           S  
ANISOU 1515  SD  MET B 123     3236   1948   2310   -281    350    335       S  
ATOM   1516  CE  MET B 123       3.723 -50.811   5.332  1.00 23.08           C  
ANISOU 1516  CE  MET B 123     3722   2527   2521    232    195    360       C  
ATOM   1517  N   ASP B 124       1.519 -56.658   5.356  1.00 18.41           N  
ANISOU 1517  N   ASP B 124     3170   1876   1948   -326    549    370       N  
ATOM   1518  CA  ASP B 124       0.921 -57.459   6.410  1.00 20.11           C  
ANISOU 1518  CA  ASP B 124     3193   2124   2325   -183    797    695       C  
ATOM   1519  C   ASP B 124       1.640 -58.802   6.598  1.00 21.46           C  
ANISOU 1519  C   ASP B 124     3700   2109   2344   -139    903    552       C  
ATOM   1520  O   ASP B 124       1.739 -59.298   7.721  1.00 25.11           O  
ANISOU 1520  O   ASP B 124     4396   2820   2322   -100    903    844       O  
ATOM   1521  CB  ASP B 124      -0.560 -57.702   6.124  1.00 21.11           C  
ANISOU 1521  CB  ASP B 124     2833   2699   2487   -342    719    498       C  
ATOM   1522  CG  ASP B 124      -1.405 -56.438   6.260  1.00 22.31           C  
ANISOU 1522  CG  ASP B 124     3058   2735   2686   -305    831    339       C  
ATOM   1523  OD1 ASP B 124      -0.895 -55.413   6.765  1.00 22.85           O  
ANISOU 1523  OD1 ASP B 124     3430   2915   2338   -241    490    466       O  
ATOM   1524  OD2 ASP B 124      -2.592 -56.477   5.860  1.00 23.35           O  
ANISOU 1524  OD2 ASP B 124     3287   2672   2912     11    792    400       O  
ATOM   1525  N   ASN B 125       2.142 -59.381   5.508  1.00 18.76           N  
ANISOU 1525  N   ASN B 125     3049   1852   2227   -132    367    532       N  
ATOM   1526  CA  ASN B 125       2.838 -60.660   5.591  1.00 19.24           C  
ANISOU 1526  CA  ASN B 125     2991   2070   2250   -330    362    349       C  
ATOM   1527  C   ASN B 125       4.349 -60.510   5.656  1.00 20.01           C  
ANISOU 1527  C   ASN B 125     3327   2065   2213   -399    392    708       C  
ATOM   1528  O   ASN B 125       5.078 -61.503   5.599  1.00 22.46           O  
ANISOU 1528  O   ASN B 125     3603   2162   2770   -106    310    868       O  
ATOM   1529  CB  ASN B 125       2.453 -61.547   4.408  1.00 19.01           C  
ANISOU 1529  CB  ASN B 125     2559   2272   2394   -675    113    665       C  
ATOM   1530  CG  ASN B 125       1.036 -62.045   4.511  1.00 23.00           C  
ANISOU 1530  CG  ASN B 125     2948   2639   3151   -560    199   1074       C  
ATOM   1531  OD1 ASN B 125       0.726 -62.882   5.359  1.00 28.04           O  
ANISOU 1531  OD1 ASN B 125     3651   3078   3924   -562    371   1600       O  
ATOM   1532  ND2 ASN B 125       0.159 -61.525   3.664  1.00 23.69           N  
ANISOU 1532  ND2 ASN B 125     3181   2537   3282   -456    105   1045       N  
ATOM   1533  N   LYS B 126       4.805 -59.263   5.782  1.00 19.32           N  
ANISOU 1533  N   LYS B 126     3185   2099   2058   -344    595    453       N  
ATOM   1534  CA  LYS B 126       6.227 -58.933   5.891  1.00 20.69           C  
ANISOU 1534  CA  LYS B 126     3042   2867   1951     16    267    484       C  
ATOM   1535  C   LYS B 126       7.031 -59.557   4.752  1.00 19.62           C  
ANISOU 1535  C   LYS B 126     3007   2412   2035     57    300    475       C  
ATOM   1536  O   LYS B 126       8.139 -60.057   4.949  1.00 22.54           O  
ANISOU 1536  O   LYS B 126     3155   2629   2781    148     79    519       O  
ATOM   1537  CB  LYS B 126       6.785 -59.369   7.251  1.00 22.68           C  
ANISOU 1537  CB  LYS B 126     3250   3654   1711   -138     96    669       C  
ATOM   1538  CG  LYS B 126       6.096 -58.673   8.415  1.00 28.07           C  
ANISOU 1538  CG  LYS B 126     4103   4675   1889    125    -46    739       C  
ATOM   1539  CD  LYS B 126       6.669 -59.081   9.756  1.00 34.32           C  
ANISOU 1539  CD  LYS B 126     5077   5487   2476    687    152    422       C  
ATOM   1540  CE  LYS B 126       5.949 -58.361  10.885  1.00 40.35           C  
ANISOU 1540  CE  LYS B 126     5963   6283   3085    515    156    533       C  
ATOM   1541  NZ  LYS B 126       6.428 -58.802  12.218  1.00 44.36           N  
ANISOU 1541  NZ  LYS B 126     6571   6674   3610    461   -152    394       N  
ATOM   1542  N   LEU B 127       6.472 -59.496   3.550  1.00 17.63           N  
ANISOU 1542  N   LEU B 127     2851   1909   1938   -186    238    300       N  
ATOM   1543  CA  LEU B 127       7.146 -60.062   2.386  1.00 17.17           C  
ANISOU 1543  CA  LEU B 127     2501   2017   2005   -467    288    218       C  
ATOM   1544  C   LEU B 127       8.235 -59.132   1.867  1.00 18.44           C  
ANISOU 1544  C   LEU B 127     2721   1895   2391   -229    234    502       C  
ATOM   1545  O   LEU B 127       9.175 -59.578   1.211  1.00 18.54           O  
ANISOU 1545  O   LEU B 127     2627   1974   2445   -292    274    618       O  
ATOM   1546  CB  LEU B 127       6.139 -60.365   1.280  1.00 17.56           C  
ANISOU 1546  CB  LEU B 127     2305   1838   2530   -765   -254    248       C  
ATOM   1547  CG  LEU B 127       5.162 -61.498   1.591  1.00 20.38           C  
ANISOU 1547  CG  LEU B 127     2870   1693   3181   -533   -213     15       C  
ATOM   1548  CD1 LEU B 127       4.126 -61.611   0.488  1.00 21.59           C  
ANISOU 1548  CD1 LEU B 127     3232   2006   2966   -373   -123    -20       C  
ATOM   1549  CD2 LEU B 127       5.905 -62.811   1.771  1.00 23.69           C  
ANISOU 1549  CD2 LEU B 127     3597   1434   3971   -391     56    391       C  
ATOM   1550  N   ALA B 128       8.103 -57.836   2.152  1.00 16.48           N  
ANISOU 1550  N   ALA B 128     2402   1634   2227   -208    192    540       N  
ATOM   1551  CA  ALA B 128       9.125 -56.870   1.775  1.00 15.88           C  
ANISOU 1551  CA  ALA B 128     2717   1715   1600    -33    333    326       C  
ATOM   1552  C   ALA B 128       9.085 -55.695   2.720  1.00 16.54           C  
ANISOU 1552  C   ALA B 128     2687   1649   1950    -67    267    193       C  
ATOM   1553  O   ALA B 128       8.041 -55.378   3.290  1.00 20.14           O  
ANISOU 1553  O   ALA B 128     2988   2130   2533   -107    532    -30       O  
ATOM   1554  CB  ALA B 128       8.935 -56.382   0.333  1.00 17.52           C  
ANISOU 1554  CB  ALA B 128     2767   2250   1641    -15    169    302       C  
ATOM   1555  N   GLN B 129      10.243 -55.068   2.871  1.00 17.38           N  
ANISOU 1555  N   GLN B 129     2985   1691   1927   -491     54    316       N  
ATOM   1556  CA  GLN B 129      10.362 -53.773   3.504  1.00 18.59           C  
ANISOU 1556  CA  GLN B 129     3130   2099   1835   -531   -394    544       C  
ATOM   1557  C   GLN B 129      10.356 -52.715   2.410  1.00 17.91           C  
ANISOU 1557  C   GLN B 129     2799   2147   1860   -123     17    734       C  
ATOM   1558  O   GLN B 129      11.051 -52.841   1.396  1.00 18.89           O  
ANISOU 1558  O   GLN B 129     2982   2058   2138    325    612    585       O  
ATOM   1559  CB  GLN B 129      11.636 -53.694   4.348  1.00 22.66           C  
ANISOU 1559  CB  GLN B 129     3852   2652   2107   -505   -471    483       C  
ATOM   1560  CG  GLN B 129      11.631 -54.635   5.547  1.00 28.15           C  
ANISOU 1560  CG  GLN B 129     4873   3006   2815   -435   -368    249       C  
ATOM   1561  CD  GLN B 129      11.903 -56.086   5.170  1.00 37.17           C  
ANISOU 1561  CD  GLN B 129     5898   4447   3777   -332   -159    205       C  
ATOM   1562  OE1 GLN B 129      12.950 -56.409   4.598  1.00 39.62           O  
ANISOU 1562  OE1 GLN B 129     6141   4989   3924    -49    138     79       O  
ATOM   1563  NE2 GLN B 129      10.958 -56.968   5.489  1.00 40.68           N  
ANISOU 1563  NE2 GLN B 129     6439   4856   4160   -225   -276    616       N  
ATOM   1564  N   ILE B 130       9.551 -51.680   2.606  1.00 17.60           N  
ANISOU 1564  N   ILE B 130     2771   1812   2104     65    133    475       N  
ATOM   1565  CA  ILE B 130       9.362 -50.673   1.567  1.00 17.57           C  
ANISOU 1565  CA  ILE B 130     3097   1607   1971    -37    331    114       C  
ATOM   1566  C   ILE B 130       9.846 -49.324   2.048  1.00 19.40           C  
ANISOU 1566  C   ILE B 130     3575   1708   2088    -78    872    321       C  
ATOM   1567  O   ILE B 130       9.377 -48.811   3.057  1.00 24.41           O  
ANISOU 1567  O   ILE B 130     4471   2303   2502   -251   1467   -202       O  
ATOM   1568  CB  ILE B 130       7.892 -50.569   1.140  1.00 18.68           C  
ANISOU 1568  CB  ILE B 130     3006   2137   1955    250    168    383       C  
ATOM   1569  CG1 ILE B 130       7.344 -51.958   0.795  1.00 19.87           C  
ANISOU 1569  CG1 ILE B 130     2728   2388   2435    241   -361    203       C  
ATOM   1570  CG2 ILE B 130       7.746 -49.602  -0.043  1.00 20.19           C  
ANISOU 1570  CG2 ILE B 130     3434   2336   1900    791    532    384       C  
ATOM   1571  CD1 ILE B 130       5.838 -51.970   0.539  1.00 21.30           C  
ANISOU 1571  CD1 ILE B 130     2918   2651   2524    217     24    172       C  
ATOM   1572  N   GLU B 131      10.811 -48.774   1.321  1.00 17.80           N  
ANISOU 1572  N   GLU B 131     2984   1967   1814   -318    -16    363       N  
ATOM   1573  CA  GLU B 131      11.423 -47.494   1.642  1.00 20.40           C  
ANISOU 1573  CA  GLU B 131     3040   2413   2296      0   -138    216       C  
ATOM   1574  C   GLU B 131      10.859 -46.438   0.713  1.00 18.17           C  
ANISOU 1574  C   GLU B 131     3143   2074   1687    134   -396      9       C  
ATOM   1575  O   GLU B 131      10.917 -46.594  -0.498  1.00 20.27           O  
ANISOU 1575  O   GLU B 131     4029   1991   1681    415   -116   -113       O  
ATOM   1576  CB  GLU B 131      12.940 -47.597   1.481  1.00 25.22           C  
ANISOU 1576  CB  GLU B 131     2921   3246   3413   -312   -753   -102       C  
ATOM   1577  CG  GLU B 131      13.744 -46.347   1.732  1.00 35.10           C  
ANISOU 1577  CG  GLU B 131     4039   4732   4564    -28    340    -92       C  
ATOM   1578  CD  GLU B 131      15.221 -46.597   1.453  1.00 47.12           C  
ANISOU 1578  CD  GLU B 131     5456   6092   6354   -264   1516   -317       C  
ATOM   1579  OE1 GLU B 131      15.525 -47.438   0.575  1.00 51.25           O  
ANISOU 1579  OE1 GLU B 131     5709   6784   6980   -457   1598   -180       O  
ATOM   1580  OE2 GLU B 131      16.075 -45.983   2.121  1.00 51.71           O  
ANISOU 1580  OE2 GLU B 131     6177   6424   7048   -348   2239   -231       O  
ATOM   1581  N   GLY B 132      10.301 -45.375   1.274  1.00 19.23           N  
ANISOU 1581  N   GLY B 132     3022   2106   2181     67     50    -48       N  
ATOM   1582  CA  GLY B 132       9.726 -44.328   0.457  1.00 18.25           C  
ANISOU 1582  CA  GLY B 132     2861   1929   2146    -36   -127   -178       C  
ATOM   1583  C   GLY B 132      10.532 -43.049   0.511  1.00 18.01           C  
ANISOU 1583  C   GLY B 132     3079   2100   1664   -192   -131   -414       C  
ATOM   1584  O   GLY B 132      10.984 -42.632   1.580  1.00 20.49           O  
ANISOU 1584  O   GLY B 132     3627   2138   2022   -224   -170   -490       O  
ATOM   1585  N   VAL B 133      10.699 -42.412  -0.643  1.00 18.26           N  
ANISOU 1585  N   VAL B 133     3105   1915   1918   -129    412      5       N  
ATOM   1586  CA  VAL B 133      11.331 -41.105  -0.698  1.00 20.35           C  
ANISOU 1586  CA  VAL B 133     3244   1831   2658   -150    481     67       C  
ATOM   1587  C   VAL B 133      10.543 -40.222  -1.656  1.00 19.74           C  
ANISOU 1587  C   VAL B 133     3442   1538   2520   -394    550   -165       C  
ATOM   1588  O   VAL B 133       9.939 -40.712  -2.618  1.00 17.68           O  
ANISOU 1588  O   VAL B 133     2825   1694   2199    -59    298   -212       O  
ATOM   1589  CB  VAL B 133      12.826 -41.209  -1.125  1.00 21.66           C  
ANISOU 1589  CB  VAL B 133     3373   2022   2835   -467    439   -499       C  
ATOM   1590  CG1 VAL B 133      12.955 -41.664  -2.571  1.00 21.74           C  
ANISOU 1590  CG1 VAL B 133     3321   2452   2489   -491    133   -513       C  
ATOM   1591  CG2 VAL B 133      13.548 -39.884  -0.899  1.00 23.57           C  
ANISOU 1591  CG2 VAL B 133     3567   2222   3166   -565    214   -515       C  
ATOM   1592  N   VAL B 134      10.505 -38.919  -1.370  1.00 20.15           N  
ANISOU 1592  N   VAL B 134     3547   1572   2538   -402    680     95       N  
ATOM   1593  CA  VAL B 134       9.803 -37.995  -2.240  1.00 20.94           C  
ANISOU 1593  CA  VAL B 134     3530   1825   2602    -24    880    186       C  
ATOM   1594  C   VAL B 134      10.847 -37.283  -3.073  1.00 24.48           C  
ANISOU 1594  C   VAL B 134     3714   2431   3156    -31    593    760       C  
ATOM   1595  O   VAL B 134      11.586 -36.452  -2.565  1.00 26.91           O  
ANISOU 1595  O   VAL B 134     3623   3091   3512   -732    -21    787       O  
ATOM   1596  CB  VAL B 134       8.945 -36.994  -1.436  1.00 20.09           C  
ANISOU 1596  CB  VAL B 134     3499   1755   2379   -163    415    -13       C  
ATOM   1597  CG1 VAL B 134       8.404 -35.899  -2.352  1.00 23.98           C  
ANISOU 1597  CG1 VAL B 134     3859   2812   2439     68    743    379       C  
ATOM   1598  CG2 VAL B 134       7.823 -37.742  -0.727  1.00 22.62           C  
ANISOU 1598  CG2 VAL B 134     3928   1817   2848   -151   1035   -298       C  
ATOM   1599  N   PRO B 135      10.927 -37.630  -4.361  1.00 28.26           N  
ANISOU 1599  N   PRO B 135     4116   3048   3575     99   1118   1085       N  
ATOM   1600  CA  PRO B 135      12.038 -37.172  -5.198  1.00 33.00           C  
ANISOU 1600  CA  PRO B 135     4364   3622   4553    252   1801   1254       C  
ATOM   1601  C   PRO B 135      11.877 -35.741  -5.713  1.00 35.58           C  
ANISOU 1601  C   PRO B 135     4343   3809   5367    140   1612   1878       C  
ATOM   1602  O   PRO B 135      12.875 -35.106  -6.054  1.00 39.44           O  
ANISOU 1602  O   PRO B 135     4426   4154   6406    181   1712   2065       O  
ATOM   1603  CB  PRO B 135      12.023 -38.179  -6.350  1.00 32.97           C  
ANISOU 1603  CB  PRO B 135     4467   3859   4203    248   2219    470       C  
ATOM   1604  CG  PRO B 135      10.587 -38.542  -6.486  1.00 32.27           C  
ANISOU 1604  CG  PRO B 135     4721   3745   3797     82   2356    599       C  
ATOM   1605  CD  PRO B 135      10.034 -38.554  -5.083  1.00 30.56           C  
ANISOU 1605  CD  PRO B 135     4569   3386   3658     65   1906    697       C  
ATOM   1606  N   PHE B 136      10.641 -35.253  -5.761  1.00 32.00           N  
ANISOU 1606  N   PHE B 136     3959   3433   4768    254   1121   1872       N  
ATOM   1607  CA  PHE B 136      10.337 -33.890  -6.198  1.00 33.60           C  
ANISOU 1607  CA  PHE B 136     4320   3727   4720    253   1144   1551       C  
ATOM   1608  C   PHE B 136       8.869 -33.615  -5.893  1.00 32.68           C  
ANISOU 1608  C   PHE B 136     4266   3389   4762    -43    697   1084       C  
ATOM   1609  O   PHE B 136       8.116 -34.536  -5.576  1.00 30.20           O  
ANISOU 1609  O   PHE B 136     4099   3037   4340   -463    348    901       O  
ATOM   1610  CB  PHE B 136      10.634 -33.694  -7.694  1.00 36.36           C  
ANISOU 1610  CB  PHE B 136     4600   4326   4889    193    825   1688       C  
ATOM   1611  CG  PHE B 136       9.852 -34.608  -8.597  1.00 41.50           C  
ANISOU 1611  CG  PHE B 136     5603   5175   4990    529   1258   1902       C  
ATOM   1612  CD1 PHE B 136      10.336 -35.863  -8.924  1.00 44.45           C  
ANISOU 1612  CD1 PHE B 136     6210   5629   5050    471   1135   2173       C  
ATOM   1613  CD2 PHE B 136       8.633 -34.209  -9.123  1.00 45.99           C  
ANISOU 1613  CD2 PHE B 136     6301   5637   5535    492   1526   1566       C  
ATOM   1614  CE1 PHE B 136       9.614 -36.709  -9.754  1.00 47.01           C  
ANISOU 1614  CE1 PHE B 136     6541   5908   5412    434   1364   2104       C  
ATOM   1615  CE2 PHE B 136       7.907 -35.047  -9.954  1.00 47.47           C  
ANISOU 1615  CE2 PHE B 136     6500   5856   5681    478   1454   1553       C  
ATOM   1616  CZ  PHE B 136       8.396 -36.296 -10.270  1.00 47.44           C  
ANISOU 1616  CZ  PHE B 136     6590   5844   5593    404   1249   1863       C  
ATOM   1617  N   GLY B 137       8.464 -32.353  -5.974  1.00 34.01           N  
ANISOU 1617  N   GLY B 137     4219   3350   5352    286    833   1137       N  
ATOM   1618  CA  GLY B 137       7.081 -31.982  -5.738  1.00 33.61           C  
ANISOU 1618  CA  GLY B 137     3940   3283   5547    327   1050    999       C  
ATOM   1619  C   GLY B 137       6.627 -32.126  -4.294  1.00 34.39           C  
ANISOU 1619  C   GLY B 137     3892   3158   6018    -51   1298    594       C  
ATOM   1620  O   GLY B 137       5.432 -32.255  -4.022  1.00 35.22           O  
ANISOU 1620  O   GLY B 137     4076   2808   6497   -179   1259    290       O  
ATOM   1621  N   ALA B 138       7.571 -32.087  -3.359  1.00 35.58           N  
ANISOU 1621  N   ALA B 138     4131   3490   5898     15   1499    459       N  
ATOM   1622  CA  ALA B 138       7.227 -32.190  -1.943  1.00 36.88           C  
ANISOU 1622  CA  ALA B 138     4323   3468   6222    -67   1317    144       C  
ATOM   1623  C   ALA B 138       6.362 -31.022  -1.466  1.00 39.46           C  
ANISOU 1623  C   ALA B 138     4657   3502   6832    117   1641   -373       C  
ATOM   1624  O   ALA B 138       5.673 -31.137  -0.454  1.00 42.38           O  
ANISOU 1624  O   ALA B 138     5550   3566   6985    329   2605   -757       O  
ATOM   1625  CB  ALA B 138       8.484 -32.285  -1.101  1.00 37.69           C  
ANISOU 1625  CB  ALA B 138     4612   3342   6367   -290   1283    172       C  
ATOM   1626  N   ASN B 139       6.382 -29.907  -2.190  1.00 38.64           N  
ANISOU 1626  N   ASN B 139     4267   3043   7372    337   1402   -535       N  
ATOM   1627  CA  ASN B 139       5.594 -28.749  -1.781  1.00 42.06           C  
ANISOU 1627  CA  ASN B 139     4906   3115   7961   -186   1244   -671       C  
ATOM   1628  C   ASN B 139       4.217 -28.690  -2.446  1.00 39.55           C  
ANISOU 1628  C   ASN B 139     4903   2784   7343   -537   1462   -651       C  
ATOM   1629  O   ASN B 139       3.503 -27.697  -2.313  1.00 40.87           O  
ANISOU 1629  O   ASN B 139     4733   3205   7591    105   1594   -223       O  
ATOM   1630  CB  ASN B 139       6.357 -27.450  -2.067  1.00 49.48           C  
ANISOU 1630  CB  ASN B 139     5785   3788   9226   -205   1483   -759       C  
ATOM   1631  CG  ASN B 139       5.846 -26.280  -1.239  1.00 58.60           C  
ANISOU 1631  CG  ASN B 139     6791   4995  10480   -217   1805   -327       C  
ATOM   1632  OD1 ASN B 139       5.333 -26.468  -0.134  1.00 61.61           O  
ANISOU 1632  OD1 ASN B 139     7157   5555  10697    -19   1919   -324       O  
ATOM   1633  ND2 ASN B 139       5.972 -25.069  -1.775  1.00 61.18           N  
ANISOU 1633  ND2 ASN B 139     7048   5269  10927   -489   1884   -242       N  
ATOM   1634  N   ASN B 140       3.837 -29.749  -3.157  1.00 36.41           N  
ANISOU 1634  N   ASN B 140     4895   2641   6297   -933   1323   -728       N  
ATOM   1635  CA  ASN B 140       2.534 -29.774  -3.809  1.00 34.83           C  
ANISOU 1635  CA  ASN B 140     4684   2896   5652   -447   1370   -317       C  
ATOM   1636  C   ASN B 140       1.400 -29.746  -2.785  1.00 31.15           C  
ANISOU 1636  C   ASN B 140     4310   2846   4680   -161    890   -533       C  
ATOM   1637  O   ASN B 140       1.538 -30.286  -1.689  1.00 34.01           O  
ANISOU 1637  O   ASN B 140     4747   3639   4538    142    831   -363       O  
ATOM   1638  CB  ASN B 140       2.397 -31.010  -4.697  1.00 37.11           C  
ANISOU 1638  CB  ASN B 140     4995   3130   5975   -164   1624   -324       C  
ATOM   1639  CG  ASN B 140       3.439 -31.067  -5.802  1.00 42.13           C  
ANISOU 1639  CG  ASN B 140     5884   3528   6594    696   2036     45       C  
ATOM   1640  OD1 ASN B 140       4.137 -30.088  -6.070  1.00 43.93           O  
ANISOU 1640  OD1 ASN B 140     6148   3491   7052    512   2047     90       O  
ATOM   1641  ND2 ASN B 140       3.553 -32.228  -6.448  1.00 42.55           N  
ANISOU 1641  ND2 ASN B 140     5826   3733   6609   1520   1813    435       N  
ATOM   1642  N   ALA B 141       0.274 -29.140  -3.141  1.00 30.28           N  
ANISOU 1642  N   ALA B 141     4463   2470   4570   -503    619   -589       N  
ATOM   1643  CA  ALA B 141      -0.852 -29.043  -2.202  1.00 25.86           C  
ANISOU 1643  CA  ALA B 141     4037   1825   3963     18   -513   -688       C  
ATOM   1644  C   ALA B 141      -1.769 -30.272  -2.179  1.00 23.39           C  
ANISOU 1644  C   ALA B 141     3731   1790   3367    126   -184   -340       C  
ATOM   1645  O   ALA B 141      -2.473 -30.498  -1.191  1.00 22.48           O  
ANISOU 1645  O   ALA B 141     3381   1786   3373    407    261   -568       O  
ATOM   1646  CB  ALA B 141      -1.679 -27.813  -2.511  1.00 28.81           C  
ANISOU 1646  CB  ALA B 141     4794   1843   4309    -57  -1155   -236       C  
ATOM   1647  N   PHE B 142      -1.781 -31.054  -3.255  1.00 19.50           N  
ANISOU 1647  N   PHE B 142     3161   1791   2456     82   -330   -518       N  
ATOM   1648  CA  PHE B 142      -2.802 -32.096  -3.398  1.00 20.76           C  
ANISOU 1648  CA  PHE B 142     3064   1904   2919    424   -321   -398       C  
ATOM   1649  C   PHE B 142      -2.264 -33.507  -3.500  1.00 20.80           C  
ANISOU 1649  C   PHE B 142     3150   1990   2763    650    192   -551       C  
ATOM   1650  O   PHE B 142      -2.819 -34.429  -2.908  1.00 21.32           O  
ANISOU 1650  O   PHE B 142     3266   2199   2635    514     35   -969       O  
ATOM   1651  CB  PHE B 142      -3.670 -31.811  -4.628  1.00 21.39           C  
ANISOU 1651  CB  PHE B 142     3424   2211   2492    516   -315   -718       C  
ATOM   1652  CG  PHE B 142      -4.276 -30.432  -4.626  1.00 21.82           C  
ANISOU 1652  CG  PHE B 142     3561   2011   2719    889   -155   -589       C  
ATOM   1653  CD1 PHE B 142      -5.362 -30.140  -3.820  1.00 23.71           C  
ANISOU 1653  CD1 PHE B 142     3756   2319   2933   1026   -300   -340       C  
ATOM   1654  CD2 PHE B 142      -3.744 -29.424  -5.415  1.00 22.17           C  
ANISOU 1654  CD2 PHE B 142     4067   1802   2552    579   -213   -413       C  
ATOM   1655  CE1 PHE B 142      -5.921 -28.862  -3.811  1.00 25.46           C  
ANISOU 1655  CE1 PHE B 142     4143   2000   3529   1048    279   -138       C  
ATOM   1656  CE2 PHE B 142      -4.290 -28.139  -5.407  1.00 23.17           C  
ANISOU 1656  CE2 PHE B 142     3937   2244   2623    817    -94   -375       C  
ATOM   1657  CZ  PHE B 142      -5.384 -27.863  -4.609  1.00 24.78           C  
ANISOU 1657  CZ  PHE B 142     4036   2156   3224   1017     33   -343       C  
ATOM   1658  N   THR B 143      -1.226 -33.680  -4.309  1.00 19.53           N  
ANISOU 1658  N   THR B 143     2931   1580   2909    832    302   -285       N  
ATOM   1659  CA  THR B 143      -0.610 -34.984  -4.497  1.00 20.43           C  
ANISOU 1659  CA  THR B 143     3450   1726   2589    642    512   -356       C  
ATOM   1660  C   THR B 143       0.888 -34.819  -4.614  1.00 20.88           C  
ANISOU 1660  C   THR B 143     3309   1897   2729    589   -150   -261       C  
ATOM   1661  O   THR B 143       1.375 -33.788  -5.078  1.00 24.83           O  
ANISOU 1661  O   THR B 143     3665   2308   3463    507    323    226       O  
ATOM   1662  CB  THR B 143      -1.123 -35.719  -5.759  1.00 26.01           C  
ANISOU 1662  CB  THR B 143     4014   3079   2791    484    230   -595       C  
ATOM   1663  OG1 THR B 143      -0.634 -35.066  -6.939  1.00 31.86           O  
ANISOU 1663  OG1 THR B 143     4731   4010   3366    561    244   -695       O  
ATOM   1664  CG2 THR B 143      -2.647 -35.793  -5.779  1.00 23.73           C  
ANISOU 1664  CG2 THR B 143     3484   3062   2469    741    -17  -1067       C  
ATOM   1665  N   MET B 144       1.612 -35.857  -4.222  1.00 20.53           N  
ANISOU 1665  N   MET B 144     3223   2174   2402    933   -323   -450       N  
ATOM   1666  CA  MET B 144       3.055 -35.815  -4.126  1.00 22.06           C  
ANISOU 1666  CA  MET B 144     3434   2519   2428   1095   -174   -814       C  
ATOM   1667  C   MET B 144       3.651 -37.088  -4.741  1.00 21.75           C  
ANISOU 1667  C   MET B 144     3408   2295   2559    711    332   -858       C  
ATOM   1668  O   MET B 144       3.190 -38.186  -4.435  1.00 22.53           O  
ANISOU 1668  O   MET B 144     3510   2135   2914    443    528   -650       O  
ATOM   1669  CB  MET B 144       3.436 -35.679  -2.652  1.00 28.24           C  
ANISOU 1669  CB  MET B 144     3849   3400   3480    664   -527  -1736       C  
ATOM   1670  CG  MET B 144       4.881 -35.667  -2.342  1.00 30.14           C  
ANISOU 1670  CG  MET B 144     4240   3706   3507    675   -437  -1378       C  
ATOM   1671  SD  MET B 144       5.072 -35.443  -0.567  1.00 29.72           S  
ANISOU 1671  SD  MET B 144     4393   3561   3338    412    -86  -1288       S  
ATOM   1672  CE  MET B 144       4.123 -33.953  -0.270  1.00 31.55           C  
ANISOU 1672  CE  MET B 144     4473   4058   3457    789   -534   -688       C  
ATOM   1673  N   PRO B 145       4.657 -36.950  -5.622  1.00 22.90           N  
ANISOU 1673  N   PRO B 145     3789   2510   2404   1037    317     23       N  
ATOM   1674  CA  PRO B 145       5.331 -38.133  -6.170  1.00 23.88           C  
ANISOU 1674  CA  PRO B 145     3662   2904   2509    903    336    273       C  
ATOM   1675  C   PRO B 145       6.036 -38.930  -5.088  1.00 20.93           C  
ANISOU 1675  C   PRO B 145     3368   2254   2330   1137    570    -18       C  
ATOM   1676  O   PRO B 145       6.572 -38.362  -4.124  1.00 21.31           O  
ANISOU 1676  O   PRO B 145     3828   1858   2413    790    348   -330       O  
ATOM   1677  CB  PRO B 145       6.355 -37.544  -7.151  1.00 25.88           C  
ANISOU 1677  CB  PRO B 145     3517   3593   2722   1321    696    440       C  
ATOM   1678  CG  PRO B 145       5.855 -36.174  -7.452  1.00 28.21           C  
ANISOU 1678  CG  PRO B 145     3949   3446   3324    988    655    152       C  
ATOM   1679  CD  PRO B 145       5.168 -35.701  -6.210  1.00 26.82           C  
ANISOU 1679  CD  PRO B 145     4042   3160   2987   1006    570      5       C  
ATOM   1680  N   LEU B 146       6.042 -40.246  -5.255  1.00 17.86           N  
ANISOU 1680  N   LEU B 146     2712   1967   2108    733    371    -11       N  
ATOM   1681  CA  LEU B 146       6.680 -41.134  -4.299  1.00 16.74           C  
ANISOU 1681  CA  LEU B 146     2522   2022   1816    728    369   -210       C  
ATOM   1682  C   LEU B 146       7.488 -42.187  -5.051  1.00 15.90           C  
ANISOU 1682  C   LEU B 146     2464   1809   1767    689    511   -267       C  
ATOM   1683  O   LEU B 146       6.984 -42.811  -5.992  1.00 17.35           O  
ANISOU 1683  O   LEU B 146     2660   1948   1983    356    138   -506       O  
ATOM   1684  CB  LEU B 146       5.639 -41.802  -3.392  1.00 20.74           C  
ANISOU 1684  CB  LEU B 146     2901   2862   2116    612    696   -278       C  
ATOM   1685  CG  LEU B 146       6.191 -42.685  -2.268  1.00 21.63           C  
ANISOU 1685  CG  LEU B 146     2818   2829   2573    367    892    -72       C  
ATOM   1686  CD1 LEU B 146       6.936 -41.841  -1.243  1.00 22.27           C  
ANISOU 1686  CD1 LEU B 146     2815   3277   2368    651    361     86       C  
ATOM   1687  CD2 LEU B 146       5.097 -43.477  -1.589  1.00 25.29           C  
ANISOU 1687  CD2 LEU B 146     3502   2928   3179    -52   1630     52       C  
ATOM   1688  N   HIS B 147       8.728 -42.387  -4.609  1.00 15.20           N  
ANISOU 1688  N   HIS B 147     2184   1422   2169    460    430   -140       N  
ATOM   1689  CA  HIS B 147       9.573 -43.458  -5.119  1.00 15.09           C  
ANISOU 1689  CA  HIS B 147     1913   1670   2152    235    174    293       C  
ATOM   1690  C   HIS B 147       9.737 -44.499  -4.019  1.00 15.24           C  
ANISOU 1690  C   HIS B 147     2274   1617   1899     89    286    181       C  
ATOM   1691  O   HIS B 147      10.145 -44.177  -2.900  1.00 17.04           O  
ANISOU 1691  O   HIS B 147     2804   1758   1913    -47     68   -104       O  
ATOM   1692  CB  HIS B 147      10.934 -42.917  -5.572  1.00 16.48           C  
ANISOU 1692  CB  HIS B 147     2253   1676   2334    149    493    246       C  
ATOM   1693  CG  HIS B 147      11.885 -43.980  -6.025  1.00 17.01           C  
ANISOU 1693  CG  HIS B 147     2198   1771   2492    200    551    -39       C  
ATOM   1694  ND1 HIS B 147      12.100 -44.270  -7.356  1.00 19.74           N  
ANISOU 1694  ND1 HIS B 147     2489   1880   3131   -295    885   -136       N  
ATOM   1695  CD2 HIS B 147      12.664 -44.837  -5.324  1.00 17.49           C  
ANISOU 1695  CD2 HIS B 147     2190   1715   2742    529    -33   -291       C  
ATOM   1696  CE1 HIS B 147      12.983 -45.248  -7.455  1.00 17.34           C  
ANISOU 1696  CE1 HIS B 147     1785   1961   2842    117    410      5       C  
ATOM   1697  NE2 HIS B 147      13.338 -45.611  -6.236  1.00 20.31           N  
ANISOU 1697  NE2 HIS B 147     2462   1971   3284    416    426    -20       N  
ATOM   1698  N   MET B 148       9.394 -45.743  -4.330  1.00 14.29           N  
ANISOU 1698  N   MET B 148     2627   1237   1565     93    470     66       N  
ATOM   1699  CA  MET B 148       9.429 -46.836  -3.354  1.00 15.19           C  
ANISOU 1699  CA  MET B 148     2325   1522   1925    365    470    250       C  
ATOM   1700  C   MET B 148      10.467 -47.881  -3.726  1.00 14.47           C  
ANISOU 1700  C   MET B 148     2371   1659   1468    232     53    -80       C  
ATOM   1701  O   MET B 148      10.452 -48.379  -4.839  1.00 16.68           O  
ANISOU 1701  O   MET B 148     3000   1916   1424    552    149    -54       O  
ATOM   1702  CB  MET B 148       8.057 -47.499  -3.259  1.00 15.39           C  
ANISOU 1702  CB  MET B 148     2179   1740   1928    216    475    195       C  
ATOM   1703  CG  MET B 148       7.002 -46.626  -2.616  1.00 17.11           C  
ANISOU 1703  CG  MET B 148     1958   2308   2235    220    309    -53       C  
ATOM   1704  SD  MET B 148       5.314 -47.077  -3.117  1.00 19.73           S  
ANISOU 1704  SD  MET B 148     2318   2625   2553    -90    571    228       S  
ATOM   1705  CE  MET B 148       5.252 -46.297  -4.743  1.00 19.45           C  
ANISOU 1705  CE  MET B 148     2475   2984   1930    247    445    395       C  
ATOM   1706  N   THR B 149      11.344 -48.226  -2.790  1.00 13.90           N  
ANISOU 1706  N   THR B 149     1864   1528   1891     19    -92    119       N  
ATOM   1707  CA  THR B 149      12.319 -49.275  -3.016  1.00 15.21           C  
ANISOU 1707  CA  THR B 149     1862   1676   2243     -4    194    596       C  
ATOM   1708  C   THR B 149      11.977 -50.465  -2.128  1.00 14.63           C  
ANISOU 1708  C   THR B 149     2097   1574   1888    -66    168    440       C  
ATOM   1709  O   THR B 149      11.705 -50.306  -0.934  1.00 16.23           O  
ANISOU 1709  O   THR B 149     2548   1853   1767   -161    151    201       O  
ATOM   1710  CB  THR B 149      13.757 -48.797  -2.730  1.00 16.52           C  
ANISOU 1710  CB  THR B 149     2128   1772   2379     29    292    381       C  
ATOM   1711  OG1 THR B 149      14.010 -47.578  -3.446  1.00 18.37           O  
ANISOU 1711  OG1 THR B 149     2480   1892   2609   -150    500    515       O  
ATOM   1712  CG2 THR B 149      14.764 -49.839  -3.174  1.00 16.86           C  
ANISOU 1712  CG2 THR B 149     2164   1916   2327    127    273    446       C  
ATOM   1713  N   PHE B 150      11.965 -51.650  -2.730  1.00 14.29           N  
ANISOU 1713  N   PHE B 150     2064   1291   2072   -114    298    107       N  
ATOM   1714  CA  PHE B 150      11.532 -52.875  -2.073  1.00 14.23           C  
ANISOU 1714  CA  PHE B 150     1983   1528   1895    -25    125    245       C  
ATOM   1715  C   PHE B 150      12.728 -53.762  -1.735  1.00 15.06           C  
ANISOU 1715  C   PHE B 150     1986   1659   2076   -100    -19    498       C  
ATOM   1716  O   PHE B 150      13.572 -54.024  -2.599  1.00 16.16           O  
ANISOU 1716  O   PHE B 150     2088   1988   2062     31    230    331       O  
ATOM   1717  CB  PHE B 150      10.586 -53.654  -2.976  1.00 15.40           C  
ANISOU 1717  CB  PHE B 150     1902   1880   2069   -360     52    151       C  
ATOM   1718  CG  PHE B 150       9.216 -53.061  -3.098  1.00 14.36           C  
ANISOU 1718  CG  PHE B 150     1875   1783   1796    -48    102    370       C  
ATOM   1719  CD1 PHE B 150       9.024 -51.827  -3.707  1.00 14.76           C  
ANISOU 1719  CD1 PHE B 150     2087   1609   1912    -11    105    117       C  
ATOM   1720  CD2 PHE B 150       8.106 -53.765  -2.635  1.00 15.71           C  
ANISOU 1720  CD2 PHE B 150     1793   2194   1982    -11    262     77       C  
ATOM   1721  CE1 PHE B 150       7.750 -51.294  -3.838  1.00 15.67           C  
ANISOU 1721  CE1 PHE B 150     1971   1771   2212   -140    229    -21       C  
ATOM   1722  CE2 PHE B 150       6.834 -53.239  -2.761  1.00 17.24           C  
ANISOU 1722  CE2 PHE B 150     2081   2197   2273    -61    400    455       C  
ATOM   1723  CZ  PHE B 150       6.655 -51.991  -3.362  1.00 16.57           C  
ANISOU 1723  CZ  PHE B 150     2364   1704   2228     37    542    288       C  
ATOM   1724  N   TRP B 151      12.782 -54.213  -0.486  1.00 16.00           N  
ANISOU 1724  N   TRP B 151     2307   1766   2004     13   -306    573       N  
ATOM   1725  CA  TRP B 151      13.823 -55.109   0.008  1.00 17.71           C  
ANISOU 1725  CA  TRP B 151     2404   1753   2571   -399   -100    684       C  
ATOM   1726  C   TRP B 151      13.194 -56.328   0.659  1.00 17.73           C  
ANISOU 1726  C   TRP B 151     2411   1686   2638   -103     23    646       C  
ATOM   1727  O   TRP B 151      12.159 -56.211   1.308  1.00 18.40           O  
ANISOU 1727  O   TRP B 151     2471   2081   2441    -33    203    369       O  
ATOM   1728  CB  TRP B 151      14.690 -54.404   1.041  1.00 20.46           C  
ANISOU 1728  CB  TRP B 151     2578   2210   2986  -1079   -523    475       C  
ATOM   1729  CG  TRP B 151      15.370 -53.191   0.531  1.00 21.91           C  
ANISOU 1729  CG  TRP B 151     3293   2136   2895   -932   -516    687       C  
ATOM   1730  CD1 TRP B 151      14.857 -51.918   0.465  1.00 23.73           C  
ANISOU 1730  CD1 TRP B 151     3898   2420   2698   -796   -672    834       C  
ATOM   1731  CD2 TRP B 151      16.696 -53.118   0.017  1.00 24.97           C  
ANISOU 1731  CD2 TRP B 151     3289   3148   3049   -785   -604    479       C  
ATOM   1732  NE1 TRP B 151      15.791 -51.064  -0.070  1.00 27.53           N  
ANISOU 1732  NE1 TRP B 151     4347   3324   2789   -802   -893    655       N  
ATOM   1733  CE2 TRP B 151      16.929 -51.773  -0.352  1.00 26.43           C  
ANISOU 1733  CE2 TRP B 151     3539   3532   2972  -1078   -846    215       C  
ATOM   1734  CE3 TRP B 151      17.712 -54.056  -0.173  1.00 26.65           C  
ANISOU 1734  CE3 TRP B 151     3017   3661   3449  -1061      2    156       C  
ATOM   1735  CZ2 TRP B 151      18.137 -51.347  -0.895  1.00 29.45           C  
ANISOU 1735  CZ2 TRP B 151     3839   4200   3151   -899   -366     99       C  
ATOM   1736  CZ3 TRP B 151      18.915 -53.626  -0.714  1.00 29.08           C  
ANISOU 1736  CZ3 TRP B 151     3036   4083   3929  -1264    366   -103       C  
ATOM   1737  CH2 TRP B 151      19.114 -52.287  -1.070  1.00 28.79           C  
ANISOU 1737  CH2 TRP B 151     3350   4038   3549   -640   -183     66       C  
ATOM   1738  N   GLY B 152      13.821 -57.488   0.529  1.00 18.44           N  
ANISOU 1738  N   GLY B 152     2786   1739   2483   -198    -73    877       N  
ATOM   1739  CA  GLY B 152      13.307 -58.647   1.236  1.00 19.30           C  
ANISOU 1739  CA  GLY B 152     2480   1732   3120     82    190   1126       C  
ATOM   1740  C   GLY B 152      14.208 -59.859   1.147  1.00 20.72           C  
ANISOU 1740  C   GLY B 152     2755   2037   3081    -54    -94    883       C  
ATOM   1741  O   GLY B 152      15.276 -59.801   0.555  1.00 25.51           O  
ANISOU 1741  O   GLY B 152     2923   2510   4260    117    452   1133       O  
ATOM   1742  N   LYS B 153      13.770 -60.962   1.739  1.00 20.99           N  
ANISOU 1742  N   LYS B 153     2812   2121   3040   -119   -238   1079       N  
ATOM   1743  CA  LYS B 153      14.512 -62.206   1.644  1.00 21.02           C  
ANISOU 1743  CA  LYS B 153     2921   1966   3099   -139   -153    955       C  
ATOM   1744  C   LYS B 153      14.320 -62.799   0.261  1.00 20.01           C  
ANISOU 1744  C   LYS B 153     2385   1893   3324    300   -159    933       C  
ATOM   1745  O   LYS B 153      13.219 -62.734  -0.304  1.00 19.86           O  
ANISOU 1745  O   LYS B 153     2390   1667   3489    116    -34    925       O  
ATOM   1746  CB  LYS B 153      14.052 -63.188   2.719  1.00 24.94           C  
ANISOU 1746  CB  LYS B 153     4014   2114   3349   -117    346   1408       C  
ATOM   1747  CG  LYS B 153      14.142 -62.618   4.124  1.00 32.15           C  
ANISOU 1747  CG  LYS B 153     5442   3079   3696    237    750   1404       C  
ATOM   1748  CD  LYS B 153      13.491 -63.549   5.127  1.00 40.18           C  
ANISOU 1748  CD  LYS B 153     6850   4131   4286    482   1388    978       C  
ATOM   1749  CE  LYS B 153      13.180 -62.828   6.430  1.00 46.26           C  
ANISOU 1749  CE  LYS B 153     7752   4884   4941    346   1865    769       C  
ATOM   1750  NZ  LYS B 153      12.423 -63.707   7.361  1.00 49.03           N  
ANISOU 1750  NZ  LYS B 153     8154   5136   5338   -157   2200    658       N  
ATOM   1751  N   GLU B 154      15.382 -63.389  -0.276  1.00 22.56           N  
ANISOU 1751  N   GLU B 154     2736   2033   3801    258    459   1123       N  
ATOM   1752  CA  GLU B 154      15.347 -63.913  -1.636  1.00 23.10           C  
ANISOU 1752  CA  GLU B 154     2545   2460   3772    532    287    824       C  
ATOM   1753  C   GLU B 154      14.174 -64.882  -1.830  1.00 20.77           C  
ANISOU 1753  C   GLU B 154     2154   2433   3304    144    270    855       C  
ATOM   1754  O   GLU B 154      13.544 -64.891  -2.885  1.00 21.25           O  
ANISOU 1754  O   GLU B 154     2479   2716   2879    452    147    673       O  
ATOM   1755  CB  GLU B 154      16.682 -64.585  -1.976  1.00 27.03           C  
ANISOU 1755  CB  GLU B 154     2962   3166   4141   1115    307    848       C  
ATOM   1756  CG  GLU B 154      16.858 -64.961  -3.436  1.00 31.87           C  
ANISOU 1756  CG  GLU B 154     3866   3676   4565   1375    226    882       C  
ATOM   1757  CD  GLU B 154      16.657 -63.796  -4.410  1.00 33.22           C  
ANISOU 1757  CD  GLU B 154     4040   3753   4828   1356    117    489       C  
ATOM   1758  OE1 GLU B 154      17.347 -62.757  -4.305  1.00 34.08           O  
ANISOU 1758  OE1 GLU B 154     4524   3562   4864   1437   -389   -109       O  
ATOM   1759  OE2 GLU B 154      15.810 -63.939  -5.306  1.00 34.11           O  
ANISOU 1759  OE2 GLU B 154     4032   4011   4916   1157    154    876       O  
ATOM   1760  N   GLU B 155      13.848 -65.658  -0.797  1.00 20.83           N  
ANISOU 1760  N   GLU B 155     2479   1793   3642     23    382   1025       N  
ATOM   1761  CA  GLU B 155      12.757 -66.623  -0.891  1.00 22.12           C  
ANISOU 1761  CA  GLU B 155     2821   1819   3766    188     54   1275       C  
ATOM   1762  C   GLU B 155      11.378 -65.992  -1.059  1.00 19.97           C  
ANISOU 1762  C   GLU B 155     2672   1715   3200     -4    137    936       C  
ATOM   1763  O   GLU B 155      10.427 -66.678  -1.443  1.00 21.20           O  
ANISOU 1763  O   GLU B 155     2959   1571   3526    -40      0    689       O  
ATOM   1764  CB  GLU B 155      12.735 -67.516   0.347  1.00 25.10           C  
ANISOU 1764  CB  GLU B 155     3197   1820   4522      6    -68   1328       C  
ATOM   1765  CG  GLU B 155      13.897 -68.473   0.446  1.00 30.38           C  
ANISOU 1765  CG  GLU B 155     3859   2269   5417    476   -474   1363       C  
ATOM   1766  CD  GLU B 155      15.087 -67.889   1.189  1.00 33.95           C  
ANISOU 1766  CD  GLU B 155     4385   2633   5881    842   -795   1179       C  
ATOM   1767  OE1 GLU B 155      15.105 -66.663   1.461  1.00 32.53           O  
ANISOU 1767  OE1 GLU B 155     4440   2650   5271    899   -917   1348       O  
ATOM   1768  OE2 GLU B 155      16.006 -68.671   1.506  1.00 38.81           O  
ANISOU 1768  OE2 GLU B 155     4864   3236   6647    983   -605    946       O  
ATOM   1769  N   ASN B 156      11.268 -64.698  -0.761  1.00 17.78           N  
ANISOU 1769  N   ASN B 156     2507   1658   2591    119     83   1046       N  
ATOM   1770  CA  ASN B 156      10.005 -63.977  -0.898  1.00 17.23           C  
ANISOU 1770  CA  ASN B 156     2666   1998   1881    140    276    531       C  
ATOM   1771  C   ASN B 156       9.887 -63.166  -2.187  1.00 16.37           C  
ANISOU 1771  C   ASN B 156     2428   1687   2103     72    475    727       C  
ATOM   1772  O   ASN B 156       8.851 -62.528  -2.433  1.00 16.52           O  
ANISOU 1772  O   ASN B 156     2261   1737   2278    109    309    655       O  
ATOM   1773  CB  ASN B 156       9.804 -63.059   0.318  1.00 16.26           C  
ANISOU 1773  CB  ASN B 156     2207   2133   1838    -64    241    649       C  
ATOM   1774  CG  ASN B 156       9.372 -63.836   1.548  1.00 19.03           C  
ANISOU 1774  CG  ASN B 156     2681   2111   2437   -406   -158    878       C  
ATOM   1775  OD1 ASN B 156       8.751 -64.890   1.425  1.00 19.91           O  
ANISOU 1775  OD1 ASN B 156     3228   1891   2444   -467    157    645       O  
ATOM   1776  ND2 ASN B 156       9.711 -63.337   2.732  1.00 20.93           N  
ANISOU 1776  ND2 ASN B 156     2963   2503   2487   -307   -281    510       N  
ATOM   1777  N   ARG B 157      10.926 -63.196  -3.016  1.00 15.76           N  
ANISOU 1777  N   ARG B 157     2451   1599   1939    -42    374    742       N  
ATOM   1778  CA  ARG B 157      10.933 -62.364  -4.224  1.00 15.96           C  
ANISOU 1778  CA  ARG B 157     2300   1747   2016     25    481    581       C  
ATOM   1779  C   ARG B 157       9.761 -62.700  -5.150  1.00 14.77           C  
ANISOU 1779  C   ARG B 157     2180   1474   1959    228    168    691       C  
ATOM   1780  O   ARG B 157       9.063 -61.800  -5.624  1.00 15.60           O  
ANISOU 1780  O   ARG B 157     2131   1563   2234    428    307    668       O  
ATOM   1781  CB  ARG B 157      12.266 -62.511  -4.980  1.00 17.73           C  
ANISOU 1781  CB  ARG B 157     2473   2027   2235    -87    998    709       C  
ATOM   1782  CG  ARG B 157      12.328 -61.679  -6.240  1.00 18.93           C  
ANISOU 1782  CG  ARG B 157     2175   2248   2767   -227    884    722       C  
ATOM   1783  CD  ARG B 157      13.583 -61.950  -7.035  1.00 18.11           C  
ANISOU 1783  CD  ARG B 157     2147   1849   2886   -375    819    329       C  
ATOM   1784  NE  ARG B 157      14.817 -61.597  -6.339  1.00 19.08           N  
ANISOU 1784  NE  ARG B 157     2082   2227   2939   -465   1108    384       N  
ATOM   1785  CZ  ARG B 157      15.410 -60.406  -6.406  1.00 17.30           C  
ANISOU 1785  CZ  ARG B 157     2062   2163   2348    -36    221    508       C  
ATOM   1786  NH1 ARG B 157      14.844 -59.415  -7.087  1.00 17.91           N  
ANISOU 1786  NH1 ARG B 157     2240   2007   2560    294    704    566       N  
ATOM   1787  NH2 ARG B 157      16.552 -60.202  -5.759  1.00 20.69           N  
ANISOU 1787  NH2 ARG B 157     2594   2529   2739   -130     98    415       N  
ATOM   1788  N   LYS B 158       9.512 -63.989  -5.384  1.00 16.20           N  
ANISOU 1788  N   LYS B 158     2433   1631   2091   -303    431     55       N  
ATOM   1789  CA  LYS B 158       8.424 -64.362  -6.281  1.00 16.10           C  
ANISOU 1789  CA  LYS B 158     2283   1337   2495   -236    246    255       C  
ATOM   1790  C   LYS B 158       7.060 -63.974  -5.703  1.00 15.44           C  
ANISOU 1790  C   LYS B 158     2417   1400   2051     78    -17    490       C  
ATOM   1791  O   LYS B 158       6.177 -63.506  -6.430  1.00 16.37           O  
ANISOU 1791  O   LYS B 158     2575   1341   2303     79   -250    431       O  
ATOM   1792  CB  LYS B 158       8.448 -65.871  -6.585  1.00 18.93           C  
ANISOU 1792  CB  LYS B 158     2754   1478   2960   -198    -93     95       C  
ATOM   1793  CG  LYS B 158       7.316 -66.296  -7.520  1.00 24.26           C  
ANISOU 1793  CG  LYS B 158     3563   1988   3666    -35   -291    387       C  
ATOM   1794  CD  LYS B 158       7.352 -67.769  -7.884  1.00 29.11           C  
ANISOU 1794  CD  LYS B 158     4442   2691   3928    -73   -499    267       C  
ATOM   1795  CE  LYS B 158       6.042 -68.193  -8.548  1.00 31.65           C  
ANISOU 1795  CE  LYS B 158     5148   3099   3779    339   -612    963       C  
ATOM   1796  NZ  LYS B 158       5.762 -67.366  -9.745  1.00 34.89           N  
ANISOU 1796  NZ  LYS B 158     5435   3639   4181    238   -551    777       N  
ATOM   1797  N   ALA B 159       6.875 -64.181  -4.403  1.00 16.33           N  
ANISOU 1797  N   ALA B 159     2672   1490   2041   -213    390    319       N  
ATOM   1798  CA  ALA B 159       5.598 -63.836  -3.780  1.00 16.94           C  
ANISOU 1798  CA  ALA B 159     2428   1663   2345   -139    390    472       C  
ATOM   1799  C   ALA B 159       5.287 -62.335  -3.929  1.00 16.64           C  
ANISOU 1799  C   ALA B 159     2457   1735   2130     -9    215    439       C  
ATOM   1800  O   ALA B 159       4.142 -61.937  -4.173  1.00 16.54           O  
ANISOU 1800  O   ALA B 159     2287   1719   2277     84     82    386       O  
ATOM   1801  CB  ALA B 159       5.603 -64.234  -2.311  1.00 19.38           C  
ANISOU 1801  CB  ALA B 159     2713   2008   2642   -203    836    555       C  
ATOM   1802  N   VAL B 160       6.309 -61.508  -3.778  1.00 15.29           N  
ANISOU 1802  N   VAL B 160     2358   1464   1989     34    268    507       N  
ATOM   1803  CA  VAL B 160       6.130 -60.069  -3.928  1.00 14.61           C  
ANISOU 1803  CA  VAL B 160     2122   1345   2082    -68    -53    384       C  
ATOM   1804  C   VAL B 160       5.742 -59.747  -5.364  1.00 15.10           C  
ANISOU 1804  C   VAL B 160     2380   1503   1854    127    445    524       C  
ATOM   1805  O   VAL B 160       4.787 -59.011  -5.612  1.00 15.35           O  
ANISOU 1805  O   VAL B 160     2262   1574   1996    150     76    560       O  
ATOM   1806  CB  VAL B 160       7.414 -59.303  -3.529  1.00 13.34           C  
ANISOU 1806  CB  VAL B 160     1850   1177   2040   -376   -177    420       C  
ATOM   1807  CG1 VAL B 160       7.358 -57.849  -3.978  1.00 15.85           C  
ANISOU 1807  CG1 VAL B 160     2253   1152   2619    -12    375    439       C  
ATOM   1808  CG2 VAL B 160       7.624 -59.381  -2.020  1.00 16.41           C  
ANISOU 1808  CG2 VAL B 160     2528   1793   1915     71    -43    366       C  
ATOM   1809  N  ASER B 161       6.472 -60.300  -6.323  0.55 13.79           N  
ANISOU 1809  N  ASER B 161     2078   1504   1658     29    536    486       N  
ATOM   1810  N  BSER B 161       6.506 -60.292  -6.307  0.45 14.93           N  
ANISOU 1810  N  BSER B 161     2429   1771   1474    -50    378    197       N  
ATOM   1811  CA ASER B 161       6.157 -60.032  -7.722  0.55 14.35           C  
ANISOU 1811  CA ASER B 161     1869   1810   1772     88    540    561       C  
ATOM   1812  CA BSER B 161       6.262 -60.058  -7.727  0.45 16.99           C  
ANISOU 1812  CA BSER B 161     2539   2246   1670     12    380    119       C  
ATOM   1813  C  ASER B 161       4.787 -60.571  -8.126  0.55 13.13           C  
ANISOU 1813  C  ASER B 161     1899   1250   1840     24    294    481       C  
ATOM   1814  C  BSER B 161       4.863 -60.498  -8.139  0.45 16.80           C  
ANISOU 1814  C  BSER B 161     2319   2161   1903      6    121    245       C  
ATOM   1815  O  ASER B 161       4.067 -59.929  -8.900  0.55 14.08           O  
ANISOU 1815  O  ASER B 161     2009   1399   1941    445    176    430       O  
ATOM   1816  O  BSER B 161       4.186 -59.810  -8.910  0.45 17.78           O  
ANISOU 1816  O  BSER B 161     2319   2430   2009    129      1    253       O  
ATOM   1817  CB ASER B 161       7.234 -60.612  -8.627  0.55 17.52           C  
ANISOU 1817  CB ASER B 161     2120   2620   1917    -30   1032    626       C  
ATOM   1818  CB BSER B 161       7.304 -60.789  -8.574  0.45 19.89           C  
ANISOU 1818  CB BSER B 161     3068   2753   1735     15    722    -21       C  
ATOM   1819  OG ASER B 161       8.371 -59.773  -8.607  0.55 20.33           O  
ANISOU 1819  OG ASER B 161     2091   3283   2350   -355    817    405       O  
ATOM   1820  OG BSER B 161       7.004 -60.671  -9.954  0.45 21.88           O  
ANISOU 1820  OG BSER B 161     3293   2882   2136    305    608   -139       O  
ATOM   1821  N  AASP B 162       4.419 -61.739  -7.603  0.55 14.37           N  
ANISOU 1821  N  AASP B 162     2358   1013   2090     24    647    239       N  
ATOM   1822  N  BASP B 162       4.431 -61.643  -7.621  0.45 17.76           N  
ANISOU 1822  N  BASP B 162     2463   2071   2215     31    407    282       N  
ATOM   1823  CA AASP B 162       3.103 -62.293  -7.892  0.55 16.95           C  
ANISOU 1823  CA AASP B 162     2540   1375   2527     72    405    305       C  
ATOM   1824  CA BASP B 162       3.125 -62.187  -7.967  0.45 18.16           C  
ANISOU 1824  CA BASP B 162     2381   2085   2435    -63    116    367       C  
ATOM   1825  C  AASP B 162       1.992 -61.377  -7.386  0.55 15.98           C  
ANISOU 1825  C  AASP B 162     2463   1417   2191   -163    592    127       C  
ATOM   1826  C  BASP B 162       1.985 -61.353  -7.393  0.45 16.66           C  
ANISOU 1826  C  BASP B 162     2373   1842   2114   -155    361     27       C  
ATOM   1827  O  AASP B 162       1.015 -61.130  -8.087  0.55 16.07           O  
ANISOU 1827  O  AASP B 162     2313   1455   2337    -69    558    363       O  
ATOM   1828  O  BASP B 162       0.970 -61.149  -8.052  0.45 16.88           O  
ANISOU 1828  O  BASP B 162     2252   2113   2048     21     51     20       O  
ATOM   1829  CB AASP B 162       2.936 -63.681  -7.266  0.55 17.60           C  
ANISOU 1829  CB AASP B 162     2815    885   2988    122      2    154       C  
ATOM   1830  CB BASP B 162       3.002 -63.633  -7.484  0.45 19.98           C  
ANISOU 1830  CB BASP B 162     2566   2142   2883   -113   -279    238       C  
ATOM   1831  CG AASP B 162       3.759 -64.755  -7.957  0.55 21.73           C  
ANISOU 1831  CG AASP B 162     3501   1586   3168    312   -296    608       C  
ATOM   1832  CG BASP B 162       1.610 -64.201  -7.689  0.45 25.50           C  
ANISOU 1832  CG BASP B 162     3167   3000   3522     69   -166    271       C  
ATOM   1833  OD1AASP B 162       4.251 -64.534  -9.081  0.55 24.14           O  
ANISOU 1833  OD1AASP B 162     3445   2049   3679     94   -336    387       O  
ATOM   1834  OD1BASP B 162       1.114 -64.175  -8.836  0.45 27.85           O  
ANISOU 1834  OD1BASP B 162     3691   3275   3614   -384     84    178       O  
ATOM   1835  OD2AASP B 162       3.901 -65.845  -7.360  0.55 23.66           O  
ANISOU 1835  OD2AASP B 162     4055   1588   3345     69   -189    140       O  
ATOM   1836  OD2BASP B 162       1.011 -64.674  -6.700  0.45 26.50           O  
ANISOU 1836  OD2BASP B 162     2815   3590   3664    305   -633     12       O  
ATOM   1837  N   GLN B 163       2.146 -60.880  -6.162  1.00 14.50           N  
ANISOU 1837  N   GLN B 163     2266   1295   1948   -229    514    165       N  
ATOM   1838  CA  GLN B 163       1.128 -60.037  -5.554  1.00 14.68           C  
ANISOU 1838  CA  GLN B 163     2224   1538   1816    -21    646    155       C  
ATOM   1839  C   GLN B 163       1.012 -58.730  -6.330  1.00 14.74           C  
ANISOU 1839  C   GLN B 163     1994   1474   2133    -74    634    460       C  
ATOM   1840  O   GLN B 163      -0.095 -58.251  -6.604  1.00 16.06           O  
ANISOU 1840  O   GLN B 163     2029   1584   2488   -149    494    460       O  
ATOM   1841  CB  GLN B 163       1.451 -59.763  -4.084  1.00 14.53           C  
ANISOU 1841  CB  GLN B 163     2293   1534   1695     76    685    145       C  
ATOM   1842  CG  GLN B 163       0.578 -58.697  -3.440  1.00 15.17           C  
ANISOU 1842  CG  GLN B 163     1911   1835   2017     38    602    -95       C  
ATOM   1843  CD  GLN B 163      -0.903 -59.053  -3.369  1.00 16.55           C  
ANISOU 1843  CD  GLN B 163     2267   1787   2236    -21    842    159       C  
ATOM   1844  OE1 GLN B 163      -1.301 -60.210  -3.549  1.00 19.11           O  
ANISOU 1844  OE1 GLN B 163     2719   2035   2507   -454    767    275       O  
ATOM   1845  NE2 GLN B 163      -1.731 -58.044  -3.101  1.00 17.74           N  
ANISOU 1845  NE2 GLN B 163     2787   1689   2263    168    589    134       N  
ATOM   1846  N   LEU B 164       2.151 -58.151  -6.691  1.00 13.17           N  
ANISOU 1846  N   LEU B 164     2035   1400   1568   -125    395    236       N  
ATOM   1847  CA  LEU B 164       2.124 -56.920  -7.480  1.00 12.60           C  
ANISOU 1847  CA  LEU B 164     1802   1577   1410   -238    206    340       C  
ATOM   1848  C   LEU B 164       1.472 -57.167  -8.841  1.00 13.57           C  
ANISOU 1848  C   LEU B 164     1834   1622   1701    189    426    260       C  
ATOM   1849  O   LEU B 164       0.661 -56.366  -9.300  1.00 14.10           O  
ANISOU 1849  O   LEU B 164     1796   1433   2129    -35    190    277       O  
ATOM   1850  CB  LEU B 164       3.534 -56.375  -7.657  1.00 13.18           C  
ANISOU 1850  CB  LEU B 164     1674   1722   1612   -440    293    242       C  
ATOM   1851  CG  LEU B 164       4.148 -55.832  -6.367  1.00 13.34           C  
ANISOU 1851  CG  LEU B 164     1654   1552   1864    132    392    282       C  
ATOM   1852  CD1 LEU B 164       5.593 -55.459  -6.607  1.00 14.89           C  
ANISOU 1852  CD1 LEU B 164     1657   1657   2344      1    339    215       C  
ATOM   1853  CD2 LEU B 164       3.347 -54.651  -5.827  1.00 15.73           C  
ANISOU 1853  CD2 LEU B 164     1966   1992   2019    405    197     31       C  
ATOM   1854  N   LYS B 165       1.817 -58.285  -9.473  1.00 13.54           N  
ANISOU 1854  N   LYS B 165     2237   1568   1340    188    365     54       N  
ATOM   1855  CA  LYS B 165       1.318 -58.595 -10.821  1.00 14.34           C  
ANISOU 1855  CA  LYS B 165     2151   1692   1606    253    310   -130       C  
ATOM   1856  C   LYS B 165      -0.207 -58.708 -10.838  1.00 15.14           C  
ANISOU 1856  C   LYS B 165     2364   1566   1821    -52    142    109       C  
ATOM   1857  O   LYS B 165      -0.852 -58.276 -11.794  1.00 15.11           O  
ANISOU 1857  O   LYS B 165     2224   1591   1925     39   -159     18       O  
ATOM   1858  CB  LYS B 165       1.952 -59.891 -11.341  1.00 15.69           C  
ANISOU 1858  CB  LYS B 165     2655   1895   1413    441     11   -265       C  
ATOM   1859  CG  LYS B 165       1.315 -60.447 -12.615  1.00 19.57           C  
ANISOU 1859  CG  LYS B 165     2877   2386   2172     66     81   -144       C  
ATOM   1860  CD  LYS B 165       1.622 -59.583 -13.817  1.00 23.79           C  
ANISOU 1860  CD  LYS B 165     3151   3455   2433   -186    274   -123       C  
ATOM   1861  CE  LYS B 165       1.381 -60.357 -15.112  1.00 28.45           C  
ANISOU 1861  CE  LYS B 165     3719   4755   2334   -411   -262    189       C  
ATOM   1862  NZ  LYS B 165       1.669 -59.539 -16.321  1.00 30.54           N  
ANISOU 1862  NZ  LYS B 165     3767   5065   2770   -309   -388     36       N  
ATOM   1863  N   LYS B 166      -0.788 -59.280  -9.782  1.00 15.85           N  
ANISOU 1863  N   LYS B 166     2438   1571   2012   -378    307   -100       N  
ATOM   1864  CA  LYS B 166      -2.245 -59.397  -9.704  1.00 17.69           C  
ANISOU 1864  CA  LYS B 166     2355   1736   2628   -304     89    219       C  
ATOM   1865  C   LYS B 166      -2.928 -58.043  -9.850  1.00 16.19           C  
ANISOU 1865  C   LYS B 166     1726   1807   2617   -443   -168     61       C  
ATOM   1866  O   LYS B 166      -4.052 -57.964 -10.343  1.00 20.12           O  
ANISOU 1866  O   LYS B 166     2228   2084   3334   -301   -257   -108       O  
ATOM   1867  CB  LYS B 166      -2.670 -60.027  -8.381  1.00 23.47           C  
ANISOU 1867  CB  LYS B 166     2993   2104   3820   -735   -122    458       C  
ATOM   1868  CG  LYS B 166      -2.367 -61.488  -8.258  1.00 31.50           C  
ANISOU 1868  CG  LYS B 166     4322   2874   4771   -549     46    770       C  
ATOM   1869  CD  LYS B 166      -2.850 -61.987  -6.914  1.00 37.78           C  
ANISOU 1869  CD  LYS B 166     5564   3112   5678   -970    499   1587       C  
ATOM   1870  CE  LYS B 166      -2.303 -63.355  -6.598  1.00 43.65           C  
ANISOU 1870  CE  LYS B 166     6293   3841   6452   -578    589   1294       C  
ATOM   1871  NZ  LYS B 166      -2.601 -63.713  -5.194  1.00 46.21           N  
ANISOU 1871  NZ  LYS B 166     6512   4256   6791   -594    608   1134       N  
ATOM   1872  N   HIS B 167      -2.237 -56.990  -9.420  1.00 14.86           N  
ANISOU 1872  N   HIS B 167     1921   1560   2164   -487    222    289       N  
ATOM   1873  CA  HIS B 167      -2.760 -55.633  -9.487  1.00 14.48           C  
ANISOU 1873  CA  HIS B 167     1986   1569   1947   -232    146     30       C  
ATOM   1874  C   HIS B 167      -2.166 -54.794 -10.624  1.00 14.06           C  
ANISOU 1874  C   HIS B 167     1888   1537   1917   -236    196    -94       C  
ATOM   1875  O   HIS B 167      -2.411 -53.581 -10.710  1.00 15.08           O  
ANISOU 1875  O   HIS B 167     2279   1423   2026   -127    324    -13       O  
ATOM   1876  CB  HIS B 167      -2.530 -54.951  -8.144  1.00 13.81           C  
ANISOU 1876  CB  HIS B 167     2076   1572   1598   -232    240    -71       C  
ATOM   1877  CG  HIS B 167      -3.310 -55.578  -7.038  1.00 16.39           C  
ANISOU 1877  CG  HIS B 167     2349   1718   2162   -359    417      4       C  
ATOM   1878  ND1 HIS B 167      -4.527 -55.089  -6.618  1.00 19.19           N  
ANISOU 1878  ND1 HIS B 167     2546   2333   2411   -170    327   -232       N  
ATOM   1879  CD2 HIS B 167      -3.070 -56.687  -6.293  1.00 15.96           C  
ANISOU 1879  CD2 HIS B 167     2525   1764   1776   -555    495     36       C  
ATOM   1880  CE1 HIS B 167      -4.998 -55.863  -5.656  1.00 19.38           C  
ANISOU 1880  CE1 HIS B 167     2671   2722   1971    -14    627     23       C  
ATOM   1881  NE2 HIS B 167      -4.138 -56.844  -5.447  1.00 18.33           N  
ANISOU 1881  NE2 HIS B 167     2496   2277   2193   -229    812   -108       N  
ATOM   1882  N   GLY B 168      -1.389 -55.428 -11.494  1.00 13.83           N  
ANISOU 1882  N   GLY B 168     1911   1602   1742   -207    138    182       N  
ATOM   1883  CA  GLY B 168      -0.839 -54.741 -12.652  1.00 14.90           C  
ANISOU 1883  CA  GLY B 168     2017   1753   1891   -305    299    126       C  
ATOM   1884  C   GLY B 168       0.518 -54.098 -12.430  1.00 12.81           C  
ANISOU 1884  C   GLY B 168     1803   1389   1676   -156    408    -49       C  
ATOM   1885  O   GLY B 168       1.062 -53.490 -13.348  1.00 14.60           O  
ANISOU 1885  O   GLY B 168     2007   1690   1850   -197    209    211       O  
ATOM   1886  N   PHE B 169       1.068 -54.226 -11.221  1.00 13.22           N  
ANISOU 1886  N   PHE B 169     1775   1405   1842     -2    -18     39       N  
ATOM   1887  CA  PHE B 169       2.362 -53.618 -10.912  1.00 14.85           C  
ANISOU 1887  CA  PHE B 169     1927   1872   1842    -21    192    168       C  
ATOM   1888  C   PHE B 169       3.517 -54.550 -11.196  1.00 12.85           C  
ANISOU 1888  C   PHE B 169     1506   1628   1749   -187    141    298       C  
ATOM   1889  O   PHE B 169       3.394 -55.762 -11.037  1.00 14.35           O  
ANISOU 1889  O   PHE B 169     2059   1460   1934    -93    285    303       O  
ATOM   1890  CB  PHE B 169       2.445 -53.176  -9.447  1.00 14.04           C  
ANISOU 1890  CB  PHE B 169     2162   1647   1527     36    200     18       C  
ATOM   1891  CG  PHE B 169       1.505 -52.061  -9.096  1.00 14.37           C  
ANISOU 1891  CG  PHE B 169     2184   1511   1764    -38   -144   -110       C  
ATOM   1892  CD1 PHE B 169       1.810 -50.748  -9.425  1.00 16.20           C  
ANISOU 1892  CD1 PHE B 169     2896   1667   1591   -229   -212    149       C  
ATOM   1893  CD2 PHE B 169       0.314 -52.328  -8.426  1.00 15.10           C  
ANISOU 1893  CD2 PHE B 169     2225   1986   1526    391    -25     -6       C  
ATOM   1894  CE1 PHE B 169       0.933 -49.723  -9.095  1.00 17.64           C  
ANISOU 1894  CE1 PHE B 169     3144   1600   1956   -316   -113    -60       C  
ATOM   1895  CE2 PHE B 169      -0.562 -51.313  -8.093  1.00 15.99           C  
ANISOU 1895  CE2 PHE B 169     2650   1717   1710     92     91    152       C  
ATOM   1896  CZ  PHE B 169      -0.254 -50.003  -8.426  1.00 16.92           C  
ANISOU 1896  CZ  PHE B 169     3268   1540   1622    153   -211    117       C  
ATOM   1897  N   LYS B 170       4.648 -53.965 -11.579  1.00 15.62           N  
ANISOU 1897  N   LYS B 170     1492   2502   1939    208    368    337       N  
ATOM   1898  CA  LYS B 170       5.883 -54.712 -11.740  1.00 15.71           C  
ANISOU 1898  CA  LYS B 170     1655   2479   1835    137    207    170       C  
ATOM   1899  C   LYS B 170       7.064 -53.873 -11.265  1.00 15.74           C  
ANISOU 1899  C   LYS B 170     1774   2215   1990    -90    -93    343       C  
ATOM   1900  O   LYS B 170       7.267 -52.756 -11.749  1.00 18.18           O  
ANISOU 1900  O   LYS B 170     2101   2498   2308   -260   -119    799       O  
ATOM   1901  CB  LYS B 170       6.081 -55.132 -13.198  1.00 16.84           C  
ANISOU 1901  CB  LYS B 170     2016   2399   1983    385    244    380       C  
ATOM   1902  CG  LYS B 170       7.325 -55.972 -13.413  1.00 17.61           C  
ANISOU 1902  CG  LYS B 170     2215   2383   2094    474    249    156       C  
ATOM   1903  CD  LYS B 170       7.501 -56.363 -14.876  1.00 21.98           C  
ANISOU 1903  CD  LYS B 170     2787   3016   2547    372    634   -303       C  
ATOM   1904  CE  LYS B 170       8.708 -57.260 -15.048  1.00 25.70           C  
ANISOU 1904  CE  LYS B 170     3402   3471   2890    553   1265   -538       C  
ATOM   1905  NZ  LYS B 170       8.951 -57.574 -16.485  1.00 33.61           N  
ANISOU 1905  NZ  LYS B 170     4367   4492   3909    626   1424   -218       N  
ATOM   1906  N   LEU B 171       7.824 -54.393 -10.303  1.00 14.30           N  
ANISOU 1906  N   LEU B 171     1668   2132   1634    -19    -35    106       N  
ATOM   1907  CA  LEU B 171       9.041 -53.717  -9.859  1.00 13.36           C  
ANISOU 1907  CA  LEU B 171     1762   1790   1524     88     25    118       C  
ATOM   1908  C   LEU B 171      10.020 -53.517 -11.015  1.00 14.51           C  
ANISOU 1908  C   LEU B 171     1932   1834   1749     31    564    244       C  
ATOM   1909  O   LEU B 171      10.165 -54.378 -11.893  1.00 16.76           O  
ANISOU 1909  O   LEU B 171     2210   1963   2196   -211    568   -249       O  
ATOM   1910  CB  LEU B 171       9.738 -54.507  -8.753  1.00 15.19           C  
ANISOU 1910  CB  LEU B 171     2039   2100   1632    523    142    366       C  
ATOM   1911  CG  LEU B 171       8.911 -54.647  -7.473  1.00 16.13           C  
ANISOU 1911  CG  LEU B 171     2337   2133   1659    283    624    461       C  
ATOM   1912  CD1 LEU B 171       9.668 -55.502  -6.471  1.00 18.53           C  
ANISOU 1912  CD1 LEU B 171     2300   2755   1987    320    403    836       C  
ATOM   1913  CD2 LEU B 171       8.575 -53.272  -6.866  1.00 18.38           C  
ANISOU 1913  CD2 LEU B 171     2756   2316   1913   -186    688   -128       C  
ATOM   1914  N   GLY B 172      10.685 -52.372 -11.021  1.00 14.99           N  
ANISOU 1914  N   GLY B 172     1948   1939   1809    -60    685    208       N  
ATOM   1915  CA  GLY B 172      11.657 -52.081 -12.053  1.00 16.10           C  
ANISOU 1915  CA  GLY B 172     1820   2134   2164   -365    823    131       C  
ATOM   1916  C   GLY B 172      12.976 -51.633 -11.460  1.00 13.95           C  
ANISOU 1916  C   GLY B 172     1951   1527   1823    254    609    294       C  
ATOM   1917  O   GLY B 172      13.161 -51.653 -10.248  1.00 14.95           O  
ANISOU 1917  O   GLY B 172     2196   1787   1696    367    587    354       O  
ATOM   1918  N   PRO B 173      13.913 -51.240 -12.320  1.00 13.73           N  
ANISOU 1918  N   PRO B 173     1855   1649   1713      0    370    181       N  
ATOM   1919  CA  PRO B 173      15.271 -50.915 -11.902  1.00 14.47           C  
ANISOU 1919  CA  PRO B 173     1908   1612   1977    198    579    364       C  
ATOM   1920  C   PRO B 173      15.520 -49.425 -11.708  1.00 13.89           C  
ANISOU 1920  C   PRO B 173     2046   1316   1916    234    357    197       C  
ATOM   1921  O   PRO B 173      16.682 -49.045 -11.575  1.00 15.57           O  
ANISOU 1921  O   PRO B 173     2027   1946   1944    -34    340     64       O  
ATOM   1922  CB  PRO B 173      16.107 -51.442 -13.059  1.00 15.73           C  
ANISOU 1922  CB  PRO B 173     2237   2014   1727    204    421    415       C  
ATOM   1923  CG  PRO B 173      15.236 -51.192 -14.264  1.00 14.93           C  
ANISOU 1923  CG  PRO B 173     1713   2200   1760    -64    349    252       C  
ATOM   1924  CD  PRO B 173      13.809 -51.399 -13.781  1.00 13.76           C  
ANISOU 1924  CD  PRO B 173     1768   2016   1445    -92    528    112       C  
ATOM   1925  N   ALA B 174      14.477 -48.594 -11.676  1.00 13.80           N  
ANISOU 1925  N   ALA B 174     2581   1135   1527    179    265    106       N  
ATOM   1926  CA  ALA B 174      14.704 -47.150 -11.566  1.00 15.39           C  
ANISOU 1926  CA  ALA B 174     2618   1254   1974    344     11     39       C  
ATOM   1927  C   ALA B 174      15.241 -46.785 -10.183  1.00 14.87           C  
ANISOU 1927  C   ALA B 174     2555   1353   1744     29    -66    164       C  
ATOM   1928  O   ALA B 174      14.673 -47.165  -9.157  1.00 16.65           O  
ANISOU 1928  O   ALA B 174     2763   1800   1765    -44     98    285       O  
ATOM   1929  CB  ALA B 174      13.429 -46.387 -11.855  1.00 18.48           C  
ANISOU 1929  CB  ALA B 174     2523   1520   2978    575   -217    294       C  
ATOM   1930  N   PRO B 175      16.343 -46.042 -10.146  1.00 15.02           N  
ANISOU 1930  N   PRO B 175     2160   1606   1941   -136     61    164       N  
ATOM   1931  CA  PRO B 175      16.896 -45.621  -8.853  1.00 16.35           C  
ANISOU 1931  CA  PRO B 175     2425   1776   2013   -127     41    175       C  
ATOM   1932  C   PRO B 175      16.163 -44.425  -8.255  1.00 17.66           C  
ANISOU 1932  C   PRO B 175     2732   1864   2114    173    100    118       C  
ATOM   1933  O   PRO B 175      15.358 -43.794  -8.936  1.00 18.15           O  
ANISOU 1933  O   PRO B 175     2619   1585   2692    -70     70     57       O  
ATOM   1934  CB  PRO B 175      18.329 -45.241  -9.202  1.00 19.58           C  
ANISOU 1934  CB  PRO B 175     2768   2143   2530   -352    463    288       C  
ATOM   1935  CG  PRO B 175      18.223 -44.721 -10.616  1.00 19.60           C  
ANISOU 1935  CG  PRO B 175     2802   2289   2356   -607    466    466       C  
ATOM   1936  CD  PRO B 175      17.186 -45.610 -11.277  1.00 17.32           C  
ANISOU 1936  CD  PRO B 175     2312   2068   2202   -791    565    214       C  
ATOM   1937  N   LYS B 176      16.465 -44.121  -6.997  1.00 19.58           N  
ANISOU 1937  N   LYS B 176     3228   2002   2211   -233    322   -282       N  
ATOM   1938  CA  LYS B 176      15.953 -42.923  -6.350  1.00 21.91           C  
ANISOU 1938  CA  LYS B 176     3372   2398   2556     17    311   -408       C  
ATOM   1939  C   LYS B 176      16.368 -41.686  -7.130  1.00 26.20           C  
ANISOU 1939  C   LYS B 176     4202   2550   3202   -218    768   -131       C  
ATOM   1940  O   LYS B 176      15.613 -40.719  -7.224  1.00 27.96           O  
ANISOU 1940  O   LYS B 176     4458   2343   3824     94   1159    113       O  
ATOM   1941  CB  LYS B 176      16.468 -42.813  -4.920  1.00 23.78           C  
ANISOU 1941  CB  LYS B 176     3517   3022   2496    111    -36   -704       C  
ATOM   1942  CG  LYS B 176      15.922 -43.833  -3.965  1.00 27.78           C  
ANISOU 1942  CG  LYS B 176     4046   3543   2967   -203   -212   -278       C  
ATOM   1943  CD  LYS B 176      16.433 -43.565  -2.557  1.00 31.86           C  
ANISOU 1943  CD  LYS B 176     4805   4284   3015   -726   -371     73       C  
ATOM   1944  CE  LYS B 176      17.237 -44.739  -2.016  1.00 39.65           C  
ANISOU 1944  CE  LYS B 176     5795   5118   4152   -849    -69    240       C  
ATOM   1945  NZ  LYS B 176      16.429 -45.992  -1.945  1.00 43.40           N  
ANISOU 1945  NZ  LYS B 176     6150   5690   4648   -919   -415    562       N  
ATOM   1946  N   THR B 177      17.585 -41.716  -7.668  1.00 25.97           N  
ANISOU 1946  N   THR B 177     4083   2583   3201   -890    709   -252       N  
ATOM   1947  CA  THR B 177      18.071 -40.637  -8.521  1.00 28.89           C  
ANISOU 1947  CA  THR B 177     4594   2607   3775   -626    752   -149       C  
ATOM   1948  C   THR B 177      18.994 -41.160  -9.618  1.00 29.61           C  
ANISOU 1948  C   THR B 177     4525   2847   3877   -726    735    242       C  
ATOM   1949  O   THR B 177      19.739 -42.125  -9.420  1.00 30.46           O  
ANISOU 1949  O   THR B 177     4563   3090   3921   -442    491    305       O  
ATOM   1950  CB  THR B 177      18.821 -39.571  -7.708  1.00 31.14           C  
ANISOU 1950  CB  THR B 177     4920   2953   3960   -801    310    140       C  
ATOM   1951  OG1 THR B 177      19.270 -38.539  -8.591  1.00 31.37           O  
ANISOU 1951  OG1 THR B 177     5224   2912   3781   -916    164    174       O  
ATOM   1952  CG2 THR B 177      20.029 -40.177  -7.009  1.00 31.67           C  
ANISOU 1952  CG2 THR B 177     5072   3172   3790   -690   -361     53       C  
ATOM   1953  N   LEU B 178      18.931 -40.534 -10.785  1.00 29.25           N  
ANISOU 1953  N   LEU B 178     4484   2980   3651   -677    301    418       N  
ATOM   1954  CA  LEU B 178      19.833 -40.878 -11.882  1.00 33.56           C  
ANISOU 1954  CA  LEU B 178     4876   3746   4128   -661    699    157       C  
ATOM   1955  C   LEU B 178      21.144 -40.117 -11.763  1.00 40.05           C  
ANISOU 1955  C   LEU B 178     5767   4543   4909   -979   1068    -82       C  
ATOM   1956  O   LEU B 178      22.032 -40.244 -12.612  1.00 43.05           O  
ANISOU 1956  O   LEU B 178     6009   5014   5333   -779   1437   -573       O  
ATOM   1957  CB  LEU B 178      19.181 -40.585 -13.235  1.00 33.08           C  
ANISOU 1957  CB  LEU B 178     4946   3877   3747   -526    256    423       C  
ATOM   1958  CG  LEU B 178      18.117 -41.572 -13.705  1.00 35.69           C  
ANISOU 1958  CG  LEU B 178     5455   4321   3786   -277   -131    756       C  
ATOM   1959  CD1 LEU B 178      17.619 -41.184 -15.095  1.00 36.81           C  
ANISOU 1959  CD1 LEU B 178     5487   4838   3660   -257  -1381    636       C  
ATOM   1960  CD2 LEU B 178      18.677 -42.995 -13.692  1.00 34.60           C  
ANISOU 1960  CD2 LEU B 178     5723   4137   3285    -86    581    981       C  
ATOM   1961  N   GLY B 179      21.258 -39.319 -10.707  1.00 41.22           N  
ANISOU 1961  N   GLY B 179     6143   4554   4963  -1422    773    597       N  
ATOM   1962  CA  GLY B 179      22.436 -38.498 -10.504  1.00 43.41           C  
ANISOU 1962  CA  GLY B 179     6175   4694   5626  -1759    762   1491       C  
ATOM   1963  C   GLY B 179      22.370 -37.240 -11.345  1.00 47.71           C  
ANISOU 1963  C   GLY B 179     6478   5219   6431  -1550    703   1744       C  
ATOM   1964  O   GLY B 179      21.287 -36.726 -11.628  1.00 50.24           O  
ANISOU 1964  O   GLY B 179     6603   5556   6929  -1468    538   1641       O  
ATOM   1965  N   PHE B 180      23.532 -36.743 -11.745  1.00 47.12           N  
ANISOU 1965  N   PHE B 180     6171   5312   6420  -1825    823   2033       N  
ATOM   1966  CA  PHE B 180      23.597 -35.549 -12.579  1.00 49.22           C  
ANISOU 1966  CA  PHE B 180     6150   5619   6932  -1948    724   1682       C  
ATOM   1967  C   PHE B 180      24.417 -35.808 -13.841  1.00 46.58           C  
ANISOU 1967  C   PHE B 180     5644   5681   6374  -1858   -176   1668       C  
ATOM   1968  O   PHE B 180      24.544 -34.939 -14.706  1.00 45.71           O  
ANISOU 1968  O   PHE B 180     5879   5369   6120  -1924    -99   2443       O  
ATOM   1969  CB  PHE B 180      24.179 -34.369 -11.790  1.00 53.48           C  
ANISOU 1969  CB  PHE B 180     6588   6072   7661  -2082    813   1102       C  
ATOM   1970  CG  PHE B 180      25.464 -34.687 -11.071  1.00 57.16           C  
ANISOU 1970  CG  PHE B 180     6958   6388   8371  -2299    656    503       C  
ATOM   1971  CD1 PHE B 180      26.684 -34.585 -11.721  1.00 58.42           C  
ANISOU 1971  CD1 PHE B 180     7083   6474   8640  -2335    737    249       C  
ATOM   1972  CD2 PHE B 180      25.451 -35.078  -9.740  1.00 59.01           C  
ANISOU 1972  CD2 PHE B 180     7183   6516   8721  -2249    592    513       C  
ATOM   1973  CE1 PHE B 180      27.866 -34.872 -11.059  1.00 59.06           C  
ANISOU 1973  CE1 PHE B 180     7113   6477   8849  -2207    585    319       C  
ATOM   1974  CE2 PHE B 180      26.629 -35.367  -9.072  1.00 58.92           C  
ANISOU 1974  CE2 PHE B 180     7190   6453   8744  -2234    349    486       C  
ATOM   1975  CZ  PHE B 180      27.838 -35.264  -9.733  1.00 58.94           C  
ANISOU 1975  CZ  PHE B 180     7155   6467   8771  -2144    251    334       C  
ATOM   1976  OXT PHE B 180      24.962 -36.896 -14.028  1.00 43.88           O  
ANISOU 1976  OXT PHE B 180     4813   6018   5843  -1566   -956    986       O  
TER    1977      PHE B 180                                                      
ATOM   1978  N   GLY C  51       2.867 -40.175 -32.329  1.00 46.30           N  
ANISOU 1978  N   GLY C  51     7476   3783   6334    420  -1066   1140       N  
ATOM   1979  CA  GLY C  51       4.097 -39.984 -33.074  1.00 43.76           C  
ANISOU 1979  CA  GLY C  51     7220   3745   5663    548   -946   1190       C  
ATOM   1980  C   GLY C  51       4.948 -38.886 -32.468  1.00 42.96           C  
ANISOU 1980  C   GLY C  51     7060   4132   5131    599   -521   1493       C  
ATOM   1981  O   GLY C  51       4.545 -38.254 -31.490  1.00 42.88           O  
ANISOU 1981  O   GLY C  51     6738   4003   5552    235   -412   1146       O  
ATOM   1982  N   PRO C  52       6.135 -38.651 -33.047  1.00 41.80           N  
ANISOU 1982  N   PRO C  52     7089   4371   4423   1004    143   1899       N  
ATOM   1983  CA  PRO C  52       7.019 -37.581 -32.574  1.00 43.34           C  
ANISOU 1983  CA  PRO C  52     7185   4568   4715    686    834   1610       C  
ATOM   1984  C   PRO C  52       6.404 -36.207 -32.808  1.00 42.66           C  
ANISOU 1984  C   PRO C  52     6996   4258   4955    131   1148   1285       C  
ATOM   1985  O   PRO C  52       5.872 -35.950 -33.884  1.00 42.44           O  
ANISOU 1985  O   PRO C  52     7095   4371   4658    438    714   1429       O  
ATOM   1986  CB  PRO C  52       8.288 -37.777 -33.410  1.00 44.93           C  
ANISOU 1986  CB  PRO C  52     7404   4859   4807    771    871   1529       C  
ATOM   1987  CG  PRO C  52       7.823 -38.480 -34.642  1.00 44.30           C  
ANISOU 1987  CG  PRO C  52     7455   4661   4716   1211    939   1550       C  
ATOM   1988  CD  PRO C  52       6.701 -39.374 -34.198  1.00 43.39           C  
ANISOU 1988  CD  PRO C  52     7469   4527   4489   1357    581   1920       C  
ATOM   1989  N   GLY C  53       6.462 -35.339 -31.804  1.00 41.58           N  
ANISOU 1989  N   GLY C  53     6779   3726   5294    -95   1331    994       N  
ATOM   1990  CA  GLY C  53       5.885 -34.014 -31.927  1.00 42.90           C  
ANISOU 1990  CA  GLY C  53     6914   3965   5420   -341   1276    785       C  
ATOM   1991  C   GLY C  53       6.918 -32.992 -32.360  1.00 43.32           C  
ANISOU 1991  C   GLY C  53     6958   4222   5280   -497   1098    441       C  
ATOM   1992  O   GLY C  53       8.114 -33.185 -32.153  1.00 46.07           O  
ANISOU 1992  O   GLY C  53     7194   4627   5684   -564   1502     30       O  
ATOM   1993  N   SER C  54       6.459 -31.906 -32.969  1.00 40.28           N  
ANISOU 1993  N   SER C  54     6752   4205   4347   -688    527    488       N  
ATOM   1994  CA  SER C  54       7.355 -30.820 -33.343  1.00 38.95           C  
ANISOU 1994  CA  SER C  54     6363   4245   4189   -358    229    568       C  
ATOM   1995  C   SER C  54       7.943 -30.173 -32.094  1.00 33.68           C  
ANISOU 1995  C   SER C  54     5380   3808   3609   -487     60    623       C  
ATOM   1996  O   SER C  54       7.368 -30.261 -31.011  1.00 30.24           O  
ANISOU 1996  O   SER C  54     4758   3647   3085   -332   -117    854       O  
ATOM   1997  CB  SER C  54       6.621 -29.774 -34.180  1.00 41.15           C  
ANISOU 1997  CB  SER C  54     6722   4632   4282    277     -8    612       C  
ATOM   1998  OG  SER C  54       5.630 -29.120 -33.405  1.00 43.58           O  
ANISOU 1998  OG  SER C  54     7108   4788   4663    694   -531    487       O  
ATOM   1999  N   VAL C  55       9.085 -29.513 -32.244  1.00 32.91           N  
ANISOU 1999  N   VAL C  55     5080   3610   3816   -504    215    534       N  
ATOM   2000  CA  VAL C  55       9.734 -28.880 -31.102  1.00 29.96           C  
ANISOU 2000  CA  VAL C  55     4522   3384   3476      9     84    857       C  
ATOM   2001  C   VAL C  55       8.868 -27.737 -30.542  1.00 30.05           C  
ANISOU 2001  C   VAL C  55     4208   2939   4272    260     85   1462       C  
ATOM   2002  O   VAL C  55       9.014 -27.363 -29.377  1.00 30.24           O  
ANISOU 2002  O   VAL C  55     4030   2731   4730    187    667   1252       O  
ATOM   2003  CB  VAL C  55      11.146 -28.357 -31.471  1.00 31.87           C  
ANISOU 2003  CB  VAL C  55     4675   3495   3942    259    428    963       C  
ATOM   2004  CG1 VAL C  55      11.052 -27.146 -32.377  1.00 32.63           C  
ANISOU 2004  CG1 VAL C  55     4554   3706   4137   -158    832   1293       C  
ATOM   2005  CG2 VAL C  55      11.950 -28.028 -30.220  1.00 34.10           C  
ANISOU 2005  CG2 VAL C  55     5122   3368   4468    605    921    689       C  
ATOM   2006  N   ASP C  56       7.940 -27.204 -31.339  1.00 32.00           N  
ANISOU 2006  N   ASP C  56     3922   3225   5010    197    -17   1655       N  
ATOM   2007  CA  ASP C  56       7.076 -26.147 -30.813  1.00 35.76           C  
ANISOU 2007  CA  ASP C  56     4190   3354   6042    671   -201   2058       C  
ATOM   2008  C   ASP C  56       5.754 -26.710 -30.277  1.00 35.40           C  
ANISOU 2008  C   ASP C  56     3837   3229   6383    424    -28   1854       C  
ATOM   2009  O   ASP C  56       4.834 -25.960 -29.954  1.00 39.33           O  
ANISOU 2009  O   ASP C  56     4201   3216   7527    652    639   2045       O  
ATOM   2010  CB  ASP C  56       6.815 -25.058 -31.863  1.00 41.77           C  
ANISOU 2010  CB  ASP C  56     5067   4019   6786   1121   -552   2425       C  
ATOM   2011  CG  ASP C  56       6.090 -25.572 -33.079  1.00 47.22           C  
ANISOU 2011  CG  ASP C  56     6297   4638   7005   1241     20   2888       C  
ATOM   2012  OD1 ASP C  56       6.287 -26.747 -33.438  1.00 48.79           O  
ANISOU 2012  OD1 ASP C  56     6474   5133   6933    834    326   2531       O  
ATOM   2013  OD2 ASP C  56       5.328 -24.788 -33.685  1.00 54.28           O  
ANISOU 2013  OD2 ASP C  56     7135   5377   8110   1225    512   2413       O  
ATOM   2014  N   SER C  57       5.671 -28.029 -30.152  1.00 31.43           N  
ANISOU 2014  N   SER C  57     3497   3041   5403    -99   -119   1506       N  
ATOM   2015  CA  SER C  57       4.511 -28.649 -29.516  1.00 32.47           C  
ANISOU 2015  CA  SER C  57     3624   3254   5459   -445     70   1080       C  
ATOM   2016  C   SER C  57       4.425 -28.245 -28.055  1.00 30.54           C  
ANISOU 2016  C   SER C  57     3238   2753   5612   -294    203    834       C  
ATOM   2017  O   SER C  57       5.440 -28.186 -27.355  1.00 30.37           O  
ANISOU 2017  O   SER C  57     3030   3103   5406   -429     21    284       O  
ATOM   2018  CB  SER C  57       4.568 -30.174 -29.615  1.00 36.54           C  
ANISOU 2018  CB  SER C  57     4395   3643   5845  -1006    639    707       C  
ATOM   2019  OG  SER C  57       4.243 -30.618 -30.920  1.00 42.25           O  
ANISOU 2019  OG  SER C  57     5232   4229   6592  -1050    926    497       O  
ATOM   2020  N   VAL C  58       3.210 -27.969 -27.600  1.00 31.58           N  
ANISOU 2020  N   VAL C  58     3744   2342   5913   -173    908    977       N  
ATOM   2021  CA  VAL C  58       2.971 -27.652 -26.206  1.00 32.43           C  
ANISOU 2021  CA  VAL C  58     4202   2037   6084   -123   1129    248       C  
ATOM   2022  C   VAL C  58       1.871 -28.544 -25.645  1.00 33.09           C  
ANISOU 2022  C   VAL C  58     4557   2035   5979     52   1623    503       C  
ATOM   2023  O   VAL C  58       1.158 -29.220 -26.386  1.00 32.37           O  
ANISOU 2023  O   VAL C  58     4456   2148   5696    193   1519    716       O  
ATOM   2024  CB  VAL C  58       2.581 -26.175 -26.023  1.00 36.79           C  
ANISOU 2024  CB  VAL C  58     4834   2447   6698    -12   1609    466       C  
ATOM   2025  CG1 VAL C  58       3.739 -25.271 -26.426  1.00 37.12           C  
ANISOU 2025  CG1 VAL C  58     5079   2332   6694   -311   1555    533       C  
ATOM   2026  CG2 VAL C  58       1.345 -25.859 -26.843  1.00 38.09           C  
ANISOU 2026  CG2 VAL C  58     4676   2697   7101    419   1680    612       C  
ATOM   2027  N   LEU C  59       1.742 -28.532 -24.326  1.00 34.26           N  
ANISOU 2027  N   LEU C  59     4544   2223   6251   -411   1806    232       N  
ATOM   2028  CA  LEU C  59       0.756 -29.339 -23.622  1.00 36.40           C  
ANISOU 2028  CA  LEU C  59     4594   2773   6462   -699   1396    221       C  
ATOM   2029  C   LEU C  59      -0.664 -28.797 -23.815  1.00 35.74           C  
ANISOU 2029  C   LEU C  59     4528   2401   6650    138   1324    359       C  
ATOM   2030  O   LEU C  59      -0.923 -27.621 -23.550  1.00 38.81           O  
ANISOU 2030  O   LEU C  59     5162   2556   7026    284   1706     18       O  
ATOM   2031  CB  LEU C  59       1.115 -29.368 -22.140  1.00 40.36           C  
ANISOU 2031  CB  LEU C  59     5134   3601   6599  -1385   1345    163       C  
ATOM   2032  CG  LEU C  59       0.538 -30.444 -21.237  1.00 45.11           C  
ANISOU 2032  CG  LEU C  59     6460   3884   6797  -1342   1406     30       C  
ATOM   2033  CD1 LEU C  59       1.079 -31.787 -21.664  1.00 44.45           C  
ANISOU 2033  CD1 LEU C  59     6947   3232   6709  -1004   1726    616       C  
ATOM   2034  CD2 LEU C  59       0.914 -30.145 -19.798  1.00 47.55           C  
ANISOU 2034  CD2 LEU C  59     6827   4194   7047  -1444   1544   -306       C  
ATOM   2035  N   PHE C  60      -1.581 -29.644 -24.276  1.00 32.86           N  
ANISOU 2035  N   PHE C  60     3946   2074   6467    481   1140    634       N  
ATOM   2036  CA  PHE C  60      -2.987 -29.255 -24.409  1.00 33.14           C  
ANISOU 2036  CA  PHE C  60     3836   2200   6556    774   1224    982       C  
ATOM   2037  C   PHE C  60      -3.807 -29.640 -23.184  1.00 33.91           C  
ANISOU 2037  C   PHE C  60     3928   2176   6781    695   1464    831       C  
ATOM   2038  O   PHE C  60      -4.733 -28.932 -22.792  1.00 37.99           O  
ANISOU 2038  O   PHE C  60     4452   2420   7562    591   2189    918       O  
ATOM   2039  CB  PHE C  60      -3.631 -29.910 -25.631  1.00 35.27           C  
ANISOU 2039  CB  PHE C  60     3737   2735   6929    685   1090   1494       C  
ATOM   2040  CG  PHE C  60      -3.186 -29.342 -26.937  1.00 36.09           C  
ANISOU 2040  CG  PHE C  60     3926   2862   6924    928    810   1797       C  
ATOM   2041  CD1 PHE C  60      -2.448 -28.171 -26.995  1.00 36.97           C  
ANISOU 2041  CD1 PHE C  60     3726   3070   7249    875    821   1791       C  
ATOM   2042  CD2 PHE C  60      -3.533 -29.973 -28.118  1.00 36.04           C  
ANISOU 2042  CD2 PHE C  60     3758   2876   7061    868    252   1732       C  
ATOM   2043  CE1 PHE C  60      -2.052 -27.653 -28.209  1.00 37.49           C  
ANISOU 2043  CE1 PHE C  60     3600   3141   7505    808    698   1819       C  
ATOM   2044  CE2 PHE C  60      -3.144 -29.462 -29.333  1.00 36.72           C  
ANISOU 2044  CE2 PHE C  60     3707   3000   7246    328    154   1828       C  
ATOM   2045  CZ  PHE C  60      -2.404 -28.299 -29.381  1.00 36.72           C  
ANISOU 2045  CZ  PHE C  60     3558   2922   7471    462    234   2014       C  
ATOM   2046  N   GLY C  61      -3.493 -30.792 -22.601  1.00 29.93           N  
ANISOU 2046  N   GLY C  61     3461   1808   6104    411    861    758       N  
ATOM   2047  CA  GLY C  61      -4.280 -31.291 -21.491  1.00 27.23           C  
ANISOU 2047  CA  GLY C  61     3380   1588   5379    451    970    426       C  
ATOM   2048  C   GLY C  61      -4.303 -32.802 -21.454  1.00 27.16           C  
ANISOU 2048  C   GLY C  61     3254   1895   5173    911    946    438       C  
ATOM   2049  O   GLY C  61      -3.565 -33.455 -22.185  1.00 29.13           O  
ANISOU 2049  O   GLY C  61     3499   1987   5580    815   1442    476       O  
ATOM   2050  N   SER C  62      -5.170 -33.338 -20.602  1.00 28.24           N  
ANISOU 2050  N   SER C  62     3700   1564   5465    276   1062    380       N  
ATOM   2051  CA ASER C  62      -5.250 -34.776 -20.395  0.37 29.39           C  
ANISOU 2051  CA ASER C  62     3576   1944   5644    421    836    545       C  
ATOM   2052  CA BSER C  62      -5.254 -34.772 -20.364  0.63 29.15           C  
ANISOU 2052  CA BSER C  62     3666   1929   5480    374    967    584       C  
ATOM   2053  C   SER C  62      -6.673 -35.295 -20.531  1.00 29.76           C  
ANISOU 2053  C   SER C  62     3765   1936   5607    734    879    499       C  
ATOM   2054  O   SER C  62      -7.638 -34.552 -20.415  1.00 31.84           O  
ANISOU 2054  O   SER C  62     4152   1965   5982    946    827    372       O  
ATOM   2055  CB ASER C  62      -4.693 -35.152 -19.021  0.37 31.23           C  
ANISOU 2055  CB ASER C  62     3568   2428   5872    382    782    623       C  
ATOM   2056  CB BSER C  62      -4.751 -35.104 -18.960  0.63 31.62           C  
ANISOU 2056  CB BSER C  62     4070   2435   5509    319   1369    696       C  
ATOM   2057  OG ASER C  62      -3.302 -34.893 -18.944  0.37 32.57           O  
ANISOU 2057  OG ASER C  62     3636   2684   6056    283    582    713       O  
ATOM   2058  OG BSER C  62      -5.519 -34.427 -17.978  0.63 34.16           O  
ANISOU 2058  OG BSER C  62     4807   2607   5566    171   1720    823       O  
ATOM   2059  N   LEU C  63      -6.789 -36.588 -20.778  1.00 27.54           N  
ANISOU 2059  N   LEU C  63     3438   1818   5209    961    428    390       N  
ATOM   2060  CA  LEU C  63      -8.083 -37.223 -20.911  1.00 29.73           C  
ANISOU 2060  CA  LEU C  63     3507   2172   5618    979    831    497       C  
ATOM   2061  C   LEU C  63      -7.983 -38.637 -20.362  1.00 26.56           C  
ANISOU 2061  C   LEU C  63     3320   1869   4903    991    760    494       C  
ATOM   2062  O   LEU C  63      -6.995 -39.323 -20.600  1.00 26.67           O  
ANISOU 2062  O   LEU C  63     2814   2165   5154    814    900    567       O  
ATOM   2063  CB  LEU C  63      -8.520 -37.234 -22.374  1.00 34.61           C  
ANISOU 2063  CB  LEU C  63     3917   3183   6052    820   1024    501       C  
ATOM   2064  CG  LEU C  63      -9.915 -37.740 -22.710  1.00 38.23           C  
ANISOU 2064  CG  LEU C  63     4082   3980   6462   1006    932    354       C  
ATOM   2065  CD1 LEU C  63     -10.961 -36.742 -22.242  1.00 40.07           C  
ANISOU 2065  CD1 LEU C  63     4017   4709   6500   1113    550    387       C  
ATOM   2066  CD2 LEU C  63     -10.024 -37.978 -24.202  1.00 40.11           C  
ANISOU 2066  CD2 LEU C  63     4326   4147   6765    872   1388    243       C  
ATOM   2067  N   ARG C  64      -8.988 -39.054 -19.604  1.00 25.22           N  
ANISOU 2067  N   ARG C  64     3225   1475   4885    593    373    410       N  
ATOM   2068  CA  ARG C  64      -9.050 -40.426 -19.110  1.00 26.21           C  
ANISOU 2068  CA  ARG C  64     3226   2012   4720    688    -10    -72       C  
ATOM   2069  C   ARG C  64      -9.955 -41.259 -20.001  1.00 27.61           C  
ANISOU 2069  C   ARG C  64     3199   2203   5090    735      4     61       C  
ATOM   2070  O   ARG C  64     -11.036 -40.818 -20.398  1.00 30.50           O  
ANISOU 2070  O   ARG C  64     2949   2565   6076    682   -455     63       O  
ATOM   2071  CB  ARG C  64      -9.549 -40.467 -17.662  1.00 34.93           C  
ANISOU 2071  CB  ARG C  64     4429   3075   5768    196    539   -190       C  
ATOM   2072  CG  ARG C  64      -8.541 -39.957 -16.641  1.00 45.57           C  
ANISOU 2072  CG  ARG C  64     6238   4204   6871   -105   1314   -597       C  
ATOM   2073  CD  ARG C  64      -9.012 -38.676 -15.970  1.00 56.11           C  
ANISOU 2073  CD  ARG C  64     7817   5500   8002   -673   1960   -924       C  
ATOM   2074  NE  ARG C  64      -7.980 -38.091 -15.117  1.00 63.23           N  
ANISOU 2074  NE  ARG C  64     8979   6313   8734  -1130   2280  -1220       N  
ATOM   2075  CZ  ARG C  64      -8.154 -37.010 -14.361  1.00 68.65           C  
ANISOU 2075  CZ  ARG C  64     9916   6861   9307  -1314   2566  -1137       C  
ATOM   2076  NH1 ARG C  64      -9.328 -36.389 -14.341  1.00 70.25           N  
ANISOU 2076  NH1 ARG C  64    10147   6982   9561  -1376   2580   -884       N  
ATOM   2077  NH2 ARG C  64      -7.154 -36.551 -13.620  1.00 70.58           N  
ANISOU 2077  NH2 ARG C  64    10248   7154   9416  -1412   2611  -1277       N  
ATOM   2078  N   GLY C  65      -9.517 -42.469 -20.311  1.00 25.36           N  
ANISOU 2078  N   GLY C  65     3347   2012   4276    607    -56    -19       N  
ATOM   2079  CA  GLY C  65     -10.332 -43.377 -21.089  1.00 25.56           C  
ANISOU 2079  CA  GLY C  65     3046   2113   4553    620    -89    109       C  
ATOM   2080  C   GLY C  65     -10.004 -44.814 -20.731  1.00 23.55           C  
ANISOU 2080  C   GLY C  65     2924   2029   3994    497   -342    100       C  
ATOM   2081  O   GLY C  65      -9.511 -45.106 -19.633  1.00 22.92           O  
ANISOU 2081  O   GLY C  65     2573   2058   4078    402    -50    163       O  
ATOM   2082  N   HIS C  66     -10.270 -45.716 -21.667  1.00 25.30           N  
ANISOU 2082  N   HIS C  66     3082   2229   4302    530    -22     -7       N  
ATOM   2083  CA  HIS C  66     -10.123 -47.135 -21.402  1.00 25.32           C  
ANISOU 2083  CA  HIS C  66     3054   2670   3897    511    413    -60       C  
ATOM   2084  C   HIS C  66      -9.596 -47.879 -22.613  1.00 23.48           C  
ANISOU 2084  C   HIS C  66     3309   2494   3117    697    195    316       C  
ATOM   2085  O   HIS C  66      -9.937 -47.553 -23.761  1.00 26.65           O  
ANISOU 2085  O   HIS C  66     3855   2929   3341    895    -75    857       O  
ATOM   2086  CB  HIS C  66     -11.459 -47.736 -20.978  1.00 27.22           C  
ANISOU 2086  CB  HIS C  66     2730   3253   4358   -239    496   -221       C  
ATOM   2087  CG  HIS C  66     -11.947 -47.246 -19.652  1.00 32.60           C  
ANISOU 2087  CG  HIS C  66     3258   4016   5113   -132    404   -633       C  
ATOM   2088  ND1 HIS C  66     -12.797 -46.169 -19.520  1.00 38.81           N  
ANISOU 2088  ND1 HIS C  66     4285   4718   5745   -182    843   -695       N  
ATOM   2089  CD2 HIS C  66     -11.701 -47.687 -18.396  1.00 35.54           C  
ANISOU 2089  CD2 HIS C  66     3663   4491   5350   -292    880   -806       C  
ATOM   2090  CE1 HIS C  66     -13.056 -45.970 -18.240  1.00 40.47           C  
ANISOU 2090  CE1 HIS C  66     4629   4915   5835    286   1417   -453       C  
ATOM   2091  NE2 HIS C  66     -12.403 -46.878 -17.537  1.00 40.16           N  
ANISOU 2091  NE2 HIS C  66     4469   4868   5920     21   1627   -606       N  
ATOM   2092  N   VAL C  67      -8.757 -48.873 -22.342  1.00 21.77           N  
ANISOU 2092  N   VAL C  67     3065   2117   3090    240   -144     71       N  
ATOM   2093  CA  VAL C  67      -8.375 -49.857 -23.336  1.00 19.48           C  
ANISOU 2093  CA  VAL C  67     2661   2113   2627    121   -140    189       C  
ATOM   2094  C   VAL C  67      -9.323 -51.046 -23.202  1.00 19.90           C  
ANISOU 2094  C   VAL C  67     2479   2308   2774     63     18    400       C  
ATOM   2095  O   VAL C  67      -9.516 -51.570 -22.107  1.00 20.46           O  
ANISOU 2095  O   VAL C  67     2823   2252   2698   -178   -139    244       O  
ATOM   2096  CB  VAL C  67      -6.926 -50.324 -23.156  1.00 18.05           C  
ANISOU 2096  CB  VAL C  67     2423   1962   2472   -136    -99   -251       C  
ATOM   2097  CG1 VAL C  67      -6.497 -51.165 -24.348  1.00 19.03           C  
ANISOU 2097  CG1 VAL C  67     2797   2143   2290    173   -109    -70       C  
ATOM   2098  CG2 VAL C  67      -6.000 -49.123 -22.949  1.00 19.93           C  
ANISOU 2098  CG2 VAL C  67     2808   2465   2298   -368     40   -184       C  
ATOM   2099  N   VAL C  68      -9.925 -51.453 -24.313  1.00 19.69           N  
ANISOU 2099  N   VAL C  68     1898   2557   3028    171   -453     33       N  
ATOM   2100  CA  VAL C  68     -10.882 -52.552 -24.307  1.00 20.82           C  
ANISOU 2100  CA  VAL C  68     1925   2605   3381     83   -177   -244       C  
ATOM   2101  C   VAL C  68     -10.429 -53.691 -25.223  1.00 19.92           C  
ANISOU 2101  C   VAL C  68     2138   2647   2786    202   -254   -140       C  
ATOM   2102  O   VAL C  68      -9.411 -53.577 -25.911  1.00 20.91           O  
ANISOU 2102  O   VAL C  68     2233   2969   2743    151   -202   -252       O  
ATOM   2103  CB  VAL C  68     -12.283 -52.069 -24.727  1.00 23.96           C  
ANISOU 2103  CB  VAL C  68     2318   2904   3884    410     72    -19       C  
ATOM   2104  CG1 VAL C  68     -12.757 -50.970 -23.787  1.00 25.35           C  
ANISOU 2104  CG1 VAL C  68     2249   2950   4430    689    354    -79       C  
ATOM   2105  CG2 VAL C  68     -12.271 -51.564 -26.172  1.00 21.81           C  
ANISOU 2105  CG2 VAL C  68     2339   2967   2982    522   -604     11       C  
ATOM   2106  N   GLY C  69     -11.171 -54.795 -25.200  1.00 19.35           N  
ANISOU 2106  N   GLY C  69     2193   2303   2858    -29   -148   -305       N  
ATOM   2107  CA  GLY C  69     -10.837 -55.968 -25.998  1.00 19.87           C  
ANISOU 2107  CA  GLY C  69     2196   2539   2814   -208   -187   -220       C  
ATOM   2108  C   GLY C  69      -9.651 -56.773 -25.505  1.00 18.09           C  
ANISOU 2108  C   GLY C  69     1930   2500   2442      0     32   -377       C  
ATOM   2109  O   GLY C  69      -9.093 -57.584 -26.256  1.00 19.65           O  
ANISOU 2109  O   GLY C  69     2230   2612   2623     99     93   -383       O  
ATOM   2110  N   LEU C  70      -9.265 -56.570 -24.246  1.00 17.92           N  
ANISOU 2110  N   LEU C  70     2150   2455   2206    133   -211   -201       N  
ATOM   2111  CA  LEU C  70      -8.055 -57.208 -23.707  1.00 16.97           C  
ANISOU 2111  CA  LEU C  70     2073   2054   2320    100   -291   -526       C  
ATOM   2112  C   LEU C  70      -8.052 -58.725 -23.853  1.00 16.75           C  
ANISOU 2112  C   LEU C  70     1941   1975   2450   -222    -48   -566       C  
ATOM   2113  O   LEU C  70      -6.987 -59.316 -24.031  1.00 19.42           O  
ANISOU 2113  O   LEU C  70     2259   2282   2837    189    203   -678       O  
ATOM   2114  CB  LEU C  70      -7.855 -56.857 -22.231  1.00 16.86           C  
ANISOU 2114  CB  LEU C  70     2377   1875   2155     -1   -153   -594       C  
ATOM   2115  CG  LEU C  70      -7.802 -55.375 -21.852  1.00 15.56           C  
ANISOU 2115  CG  LEU C  70     2037   1890   1984     14    134   -321       C  
ATOM   2116  CD1 LEU C  70      -7.549 -55.237 -20.353  1.00 16.35           C  
ANISOU 2116  CD1 LEU C  70     2281   2231   1702     45     84   -243       C  
ATOM   2117  CD2 LEU C  70      -6.750 -54.617 -22.657  1.00 17.31           C  
ANISOU 2117  CD2 LEU C  70     2084   2221   2273   -323    334    -83       C  
ATOM   2118  N   ARG C  71      -9.222 -59.359 -23.789  1.00 18.56           N  
ANISOU 2118  N   ARG C  71     2638   2062   2353   -620    109   -540       N  
ATOM   2119  CA  ARG C  71      -9.244 -60.828 -23.796  1.00 19.34           C  
ANISOU 2119  CA  ARG C  71     2611   2256   2480   -609    427   -598       C  
ATOM   2120  C   ARG C  71      -8.787 -61.406 -25.141  1.00 19.51           C  
ANISOU 2120  C   ARG C  71     2698   2203   2513   -370    492   -566       C  
ATOM   2121  O   ARG C  71      -8.401 -62.577 -25.219  1.00 21.88           O  
ANISOU 2121  O   ARG C  71     3103   2153   3057   -390    729   -640       O  
ATOM   2122  CB  ARG C  71     -10.629 -61.360 -23.425  1.00 24.49           C  
ANISOU 2122  CB  ARG C  71     3043   3074   3189   -513    587    207       C  
ATOM   2123  CG  ARG C  71     -11.668 -61.279 -24.517  1.00 32.00           C  
ANISOU 2123  CG  ARG C  71     3645   4145   4368  -1024   1234     67       C  
ATOM   2124  CD  ARG C  71     -12.977 -61.935 -24.065  1.00 39.49           C  
ANISOU 2124  CD  ARG C  71     4711   4762   5533  -1244   1653    -66       C  
ATOM   2125  NE  ARG C  71     -12.817 -63.371 -23.857  1.00 45.54           N  
ANISOU 2125  NE  ARG C  71     5646   5396   6259  -1564   1633   -685       N  
ATOM   2126  CZ  ARG C  71     -13.254 -64.300 -24.701  1.00 48.03           C  
ANISOU 2126  CZ  ARG C  71     6372   5489   6389  -1815   1254  -1271       C  
ATOM   2127  NH1 ARG C  71     -13.898 -63.945 -25.805  1.00 50.13           N  
ANISOU 2127  NH1 ARG C  71     7200   5500   6348  -1690   1895  -1365       N  
ATOM   2128  NH2 ARG C  71     -13.059 -65.584 -24.434  1.00 49.47           N  
ANISOU 2128  NH2 ARG C  71     6388   5735   6673  -1713    964  -1185       N  
ATOM   2129  N   TYR C  72      -8.779 -60.572 -26.177  1.00 19.28           N  
ANISOU 2129  N   TYR C  72     2419   2598   2307   -447    415   -364       N  
ATOM   2130  CA  TYR C  72      -8.446 -61.015 -27.532  1.00 19.39           C  
ANISOU 2130  CA  TYR C  72     2090   2700   2579   -144    -38   -524       C  
ATOM   2131  C   TYR C  72      -6.983 -60.803 -27.941  1.00 18.65           C  
ANISOU 2131  C   TYR C  72     2008   2301   2777   -199    671   -806       C  
ATOM   2132  O   TYR C  72      -6.576 -61.222 -29.045  1.00 20.29           O  
ANISOU 2132  O   TYR C  72     2502   2713   2496   -162    662   -968       O  
ATOM   2133  CB  TYR C  72      -9.361 -60.306 -28.533  1.00 20.95           C  
ANISOU 2133  CB  TYR C  72     2258   3079   2622   -325    -10   -541       C  
ATOM   2134  CG  TYR C  72     -10.813 -60.534 -28.204  1.00 23.65           C  
ANISOU 2134  CG  TYR C  72     2361   3623   3003   -638   -194   -988       C  
ATOM   2135  CD1 TYR C  72     -11.401 -61.780 -28.408  1.00 24.94           C  
ANISOU 2135  CD1 TYR C  72     2374   3814   3287   -768   -436  -1121       C  
ATOM   2136  CD2 TYR C  72     -11.591 -59.520 -27.661  1.00 24.62           C  
ANISOU 2136  CD2 TYR C  72     2330   3783   3242   -350   -128   -864       C  
ATOM   2137  CE1 TYR C  72     -12.721 -62.005 -28.093  1.00 26.69           C  
ANISOU 2137  CE1 TYR C  72     2185   4145   3813   -165   -280   -730       C  
ATOM   2138  CE2 TYR C  72     -12.918 -59.735 -27.342  1.00 26.76           C  
ANISOU 2138  CE2 TYR C  72     2412   4110   3647   -444   -299   -956       C  
ATOM   2139  CZ  TYR C  72     -13.475 -60.981 -27.562  1.00 27.43           C  
ANISOU 2139  CZ  TYR C  72     2329   3997   4098   -237   -185  -1097       C  
ATOM   2140  OH  TYR C  72     -14.789 -61.212 -27.245  1.00 31.77           O  
ANISOU 2140  OH  TYR C  72     2600   4366   5105    162     73   -775       O  
ATOM   2141  N   TYR C  73      -6.199 -60.163 -27.069  1.00 18.66           N  
ANISOU 2141  N   TYR C  73     2279   2028   2782   -512    460   -611       N  
ATOM   2142  CA  TYR C  73      -4.799 -59.860 -27.373  1.00 16.75           C  
ANISOU 2142  CA  TYR C  73     2284   1758   2321   -189    244   -684       C  
ATOM   2143  C   TYR C  73      -3.901 -60.339 -26.246  1.00 17.01           C  
ANISOU 2143  C   TYR C  73     2335   2174   1955    -16    467   -578       C  
ATOM   2144  O   TYR C  73      -4.388 -60.715 -25.171  1.00 20.37           O  
ANISOU 2144  O   TYR C  73     2959   2300   2480    -57    824   -647       O  
ATOM   2145  CB  TYR C  73      -4.618 -58.354 -27.638  1.00 17.47           C  
ANISOU 2145  CB  TYR C  73     2351   1706   2581    -11    213   -170       C  
ATOM   2146  CG  TYR C  73      -5.594 -57.889 -28.686  1.00 19.62           C  
ANISOU 2146  CG  TYR C  73     2526   2309   2619   -230    162   -297       C  
ATOM   2147  CD1 TYR C  73      -5.358 -58.136 -30.034  1.00 21.14           C  
ANISOU 2147  CD1 TYR C  73     2931   2608   2493   -542    139   -410       C  
ATOM   2148  CD2 TYR C  73      -6.791 -57.281 -28.325  1.00 19.15           C  
ANISOU 2148  CD2 TYR C  73     2752   2296   2226    -31   -128     92       C  
ATOM   2149  CE1 TYR C  73      -6.259 -57.756 -30.990  1.00 22.95           C  
ANISOU 2149  CE1 TYR C  73     3309   2897   2513   -278    111   -271       C  
ATOM   2150  CE2 TYR C  73      -7.700 -56.889 -29.274  1.00 20.78           C  
ANISOU 2150  CE2 TYR C  73     2858   2845   2191   -440   -285    102       C  
ATOM   2151  CZ  TYR C  73      -7.435 -57.134 -30.607  1.00 22.44           C  
ANISOU 2151  CZ  TYR C  73     3083   3025   2419   -173     10     84       C  
ATOM   2152  OH  TYR C  73      -8.353 -56.759 -31.558  1.00 26.69           O  
ANISOU 2152  OH  TYR C  73     3423   3891   2826   -668   -246    303       O  
ATOM   2153  N   THR C  74      -2.594 -60.362 -26.482  1.00 16.91           N  
ANISOU 2153  N   THR C  74     2274   1992   2160    -84    236   -628       N  
ATOM   2154  CA  THR C  74      -1.689 -60.866 -25.455  1.00 18.41           C  
ANISOU 2154  CA  THR C  74     2416   2147   2431    101    154   -470       C  
ATOM   2155  C   THR C  74      -0.582 -59.902 -25.093  1.00 17.64           C  
ANISOU 2155  C   THR C  74     2551   1930   2222    219    626   -572       C  
ATOM   2156  O   THR C  74       0.310 -60.252 -24.330  1.00 18.86           O  
ANISOU 2156  O   THR C  74     2779   2137   2252     -1    169   -731       O  
ATOM   2157  CB  THR C  74      -1.024 -62.201 -25.877  1.00 19.96           C  
ANISOU 2157  CB  THR C  74     2784   2061   2739    -57    537  -1004       C  
ATOM   2158  OG1 THR C  74      -0.206 -61.991 -27.038  1.00 21.54           O  
ANISOU 2158  OG1 THR C  74     3192   2263   2732    -36    979   -994       O  
ATOM   2159  CG2 THR C  74      -2.074 -63.260 -26.181  1.00 21.56           C  
ANISOU 2159  CG2 THR C  74     2988   2269   2935   -292    341   -988       C  
ATOM   2160  N   GLY C  75      -0.621 -58.698 -25.651  1.00 18.04           N  
ANISOU 2160  N   GLY C  75     2422   2287   2145    -28    605   -517       N  
ATOM   2161  CA  GLY C  75       0.384 -57.703 -25.326  1.00 18.49           C  
ANISOU 2161  CA  GLY C  75     2614   2370   2041     95    490   -714       C  
ATOM   2162  C   GLY C  75       0.319 -57.386 -23.850  1.00 19.04           C  
ANISOU 2162  C   GLY C  75     2658   2696   1880    403    208   -440       C  
ATOM   2163  O   GLY C  75      -0.750 -57.076 -23.339  1.00 25.76           O  
ANISOU 2163  O   GLY C  75     3378   4219   2191   1567    328   -644       O  
ATOM   2164  N   VAL C  76       1.449 -57.490 -23.161  1.00 16.76           N  
ANISOU 2164  N   VAL C  76     2895   1589   1882   -311    -37   -592       N  
ATOM   2165  CA  VAL C  76       1.496 -57.240 -21.726  1.00 17.46           C  
ANISOU 2165  CA  VAL C  76     3165   1484   1984     91   -312   -448       C  
ATOM   2166  C   VAL C  76       1.888 -55.800 -21.455  1.00 15.28           C  
ANISOU 2166  C   VAL C  76     2531   1560   1715     35     89   -618       C  
ATOM   2167  O   VAL C  76       2.767 -55.246 -22.113  1.00 17.29           O  
ANISOU 2167  O   VAL C  76     2805   1949   1816   -124    525   -443       O  
ATOM   2168  CB  VAL C  76       2.479 -58.188 -21.022  1.00 21.95           C  
ANISOU 2168  CB  VAL C  76     4414   1702   2224      7   -389   -341       C  
ATOM   2169  CG1 VAL C  76       2.597 -57.859 -19.532  1.00 23.01           C  
ANISOU 2169  CG1 VAL C  76     4596   1843   2303    -66   -869   -360       C  
ATOM   2170  CG2 VAL C  76       2.035 -59.628 -21.220  1.00 25.41           C  
ANISOU 2170  CG2 VAL C  76     5384   1805   2464   -517   -100   -360       C  
ATOM   2171  N   VAL C  77       1.219 -55.192 -20.490  1.00 15.21           N  
ANISOU 2171  N   VAL C  77     2841   1379   1560     42    206   -441       N  
ATOM   2172  CA  VAL C  77       1.597 -53.869 -20.046  1.00 14.38           C  
ANISOU 2172  CA  VAL C  77     2426   1434   1604    120    205   -308       C  
ATOM   2173  C   VAL C  77       1.559 -53.897 -18.519  1.00 13.54           C  
ANISOU 2173  C   VAL C  77     2069   1683   1394    -96    197   -155       C  
ATOM   2174  O   VAL C  77       0.851 -54.728 -17.922  1.00 15.37           O  
ANISOU 2174  O   VAL C  77     2217   2087   1536   -363    414   -383       O  
ATOM   2175  CB  VAL C  77       0.659 -52.804 -20.640  1.00 19.39           C  
ANISOU 2175  CB  VAL C  77     3041   1896   2431    721    -51   -503       C  
ATOM   2176  CG1 VAL C  77      -0.760 -53.075 -20.226  1.00 23.14           C  
ANISOU 2176  CG1 VAL C  77     3098   2895   2800    518    -73   -494       C  
ATOM   2177  CG2 VAL C  77       1.089 -51.384 -20.256  1.00 21.88           C  
ANISOU 2177  CG2 VAL C  77     4005   2215   2092    758   -610   -394       C  
ATOM   2178  N   ASN C  78       2.372 -53.050 -17.899  1.00 13.58           N  
ANISOU 2178  N   ASN C  78     2229   1657   1275     17    -53   -130       N  
ATOM   2179  CA  ASN C  78       2.365 -52.881 -16.449  1.00 13.94           C  
ANISOU 2179  CA  ASN C  78     2085   1689   1523    -32   -113   -158       C  
ATOM   2180  C   ASN C  78       1.989 -51.454 -16.102  1.00 12.94           C  
ANISOU 2180  C   ASN C  78     1954   1459   1504    -23    226    -49       C  
ATOM   2181  O   ASN C  78       2.157 -50.538 -16.927  1.00 14.19           O  
ANISOU 2181  O   ASN C  78     2306   1384   1700    -64    246    116       O  
ATOM   2182  CB  ASN C  78       3.733 -53.229 -15.848  1.00 14.52           C  
ANISOU 2182  CB  ASN C  78     2009   1418   2090    138   -242    -46       C  
ATOM   2183  CG  ASN C  78       4.199 -54.622 -16.248  1.00 16.33           C  
ANISOU 2183  CG  ASN C  78     2475   1548   2183    101    133    381       C  
ATOM   2184  OD1 ASN C  78       3.669 -55.615 -15.762  1.00 18.34           O  
ANISOU 2184  OD1 ASN C  78     3033   1681   2256   -213   -141    363       O  
ATOM   2185  ND2 ASN C  78       5.176 -54.697 -17.142  1.00 19.24           N  
ANISOU 2185  ND2 ASN C  78     3013   2008   2290   -289    356    357       N  
ATOM   2186  N   ASN C  79       1.499 -51.260 -14.883  1.00 12.29           N  
ANISOU 2186  N   ASN C  79     1898   1330   1443    149    264   -173       N  
ATOM   2187  CA  ASN C  79       1.143 -49.927 -14.429  1.00 12.26           C  
ANISOU 2187  CA  ASN C  79     1749   1360   1548    145    411   -227       C  
ATOM   2188  C   ASN C  79       2.335 -48.970 -14.552  1.00 13.87           C  
ANISOU 2188  C   ASN C  79     2077   1477   1717   -460    246   -160       C  
ATOM   2189  O   ASN C  79       3.492 -49.364 -14.319  1.00 15.65           O  
ANISOU 2189  O   ASN C  79     2220   1741   1987   -435    102    -55       O  
ATOM   2190  CB  ASN C  79       0.642 -49.957 -12.985  1.00 13.26           C  
ANISOU 2190  CB  ASN C  79     1890   1574   1573   -416    401    -54       C  
ATOM   2191  CG  ASN C  79      -0.599 -50.810 -12.821  1.00 12.45           C  
ANISOU 2191  CG  ASN C  79     1915   1342   1473     14   -128    -67       C  
ATOM   2192  OD1 ASN C  79      -1.344 -51.043 -13.778  1.00 13.26           O  
ANISOU 2192  OD1 ASN C  79     2032   1581   1424    -85     95    -92       O  
ATOM   2193  ND2 ASN C  79      -0.839 -51.273 -11.587  1.00 14.23           N  
ANISOU 2193  ND2 ASN C  79     2183   1719   1503    107    242    -73       N  
ATOM   2194  N   ASN C  80       2.021 -47.727 -14.909  1.00 14.06           N  
ANISOU 2194  N   ASN C  80     2457   1283   1603   -209    552    132       N  
ATOM   2195  CA  ASN C  80       2.978 -46.630 -15.140  1.00 13.82           C  
ANISOU 2195  CA  ASN C  80     2064   1579   1607   -466    -92    258       C  
ATOM   2196  C   ASN C  80       3.766 -46.727 -16.440  1.00 14.25           C  
ANISOU 2196  C   ASN C  80     2213   1432   1770   -137    171     91       C  
ATOM   2197  O   ASN C  80       4.677 -45.931 -16.663  1.00 16.21           O  
ANISOU 2197  O   ASN C  80     2525   1566   2067   -538    214     38       O  
ATOM   2198  CB  ASN C  80       3.989 -46.506 -13.985  1.00 16.03           C  
ANISOU 2198  CB  ASN C  80     2477   2101   1512    -83    218     -5       C  
ATOM   2199  CG  ASN C  80       3.356 -46.071 -12.702  1.00 15.88           C  
ANISOU 2199  CG  ASN C  80     2442   2002   1589   -130   -391   -216       C  
ATOM   2200  OD1 ASN C  80       2.363 -45.342 -12.701  1.00 21.05           O  
ANISOU 2200  OD1 ASN C  80     2970   2110   2917    -49    185   -204       O  
ATOM   2201  ND2 ASN C  80       3.937 -46.503 -11.585  1.00 19.12           N  
ANISOU 2201  ND2 ASN C  80     2903   2674   1686    178    -94   -436       N  
ATOM   2202  N   GLU C  81       3.426 -47.679 -17.304  1.00 13.13           N  
ANISOU 2202  N   GLU C  81     1915   1716   1356     73    265   -167       N  
ATOM   2203  CA  GLU C  81       4.108 -47.782 -18.593  1.00 12.13           C  
ANISOU 2203  CA  GLU C  81     1982   1407   1219    204    175    -85       C  
ATOM   2204  C   GLU C  81       3.392 -46.991 -19.683  1.00 11.82           C  
ANISOU 2204  C   GLU C  81     1764   1228   1498    273   -425    -20       C  
ATOM   2205  O   GLU C  81       2.148 -46.943 -19.725  1.00 14.50           O  
ANISOU 2205  O   GLU C  81     1884   1544   2082    228    -64     19       O  
ATOM   2206  CB  GLU C  81       4.204 -49.248 -19.049  1.00 15.62           C  
ANISOU 2206  CB  GLU C  81     2118   1397   2421    188    286     26       C  
ATOM   2207  CG  GLU C  81       5.145 -50.123 -18.238  1.00 17.56           C  
ANISOU 2207  CG  GLU C  81     1975   1924   2773    372    290    272       C  
ATOM   2208  CD  GLU C  81       5.307 -51.526 -18.824  1.00 18.68           C  
ANISOU 2208  CD  GLU C  81     2231   2085   2783    113   -306    339       C  
ATOM   2209  OE1 GLU C  81       4.573 -51.889 -19.768  1.00 22.39           O  
ANISOU 2209  OE1 GLU C  81     2342   2182   3981    -19    -79    645       O  
ATOM   2210  OE2 GLU C  81       6.207 -52.252 -18.364  1.00 22.00           O  
ANISOU 2210  OE2 GLU C  81     3471   2026   2861   -219    584    678       O  
ATOM   2211  N   MET C  82       4.184 -46.402 -20.575  1.00 14.39           N  
ANISOU 2211  N   MET C  82     2618   1376   1475     99    292    166       N  
ATOM   2212  CA  MET C  82       3.706 -45.916 -21.867  1.00 14.81           C  
ANISOU 2212  CA  MET C  82     2517   1479   1631    137   -135    372       C  
ATOM   2213  C   MET C  82       3.046 -46.997 -22.686  1.00 15.58           C  
ANISOU 2213  C   MET C  82     2522   1804   1593     82   -330   -157       C  
ATOM   2214  O   MET C  82       3.509 -48.150 -22.693  1.00 16.68           O  
ANISOU 2214  O   MET C  82     2786   1738   1813    332     73    104       O  
ATOM   2215  CB  MET C  82       4.867 -45.404 -22.722  1.00 21.02           C  
ANISOU 2215  CB  MET C  82     3168   2299   2522   -668    -31   1078       C  
ATOM   2216  CG  MET C  82       5.418 -44.113 -22.396  1.00 29.58           C  
ANISOU 2216  CG  MET C  82     4260   3096   3884   -312    931    748       C  
ATOM   2217  SD  MET C  82       6.356 -43.580 -23.833  1.00 25.15           S  
ANISOU 2217  SD  MET C  82     4239   2367   2949   -690    872    -91       S  
ATOM   2218  CE  MET C  82       7.625 -44.836 -23.902  1.00 21.34           C  
ANISOU 2218  CE  MET C  82     4039   1569   2499   -283    962    -27       C  
ATOM   2219  N   VAL C  83       2.010 -46.613 -23.419  1.00 14.51           N  
ANISOU 2219  N   VAL C  83     2359   1717   1439     52   -230   -114       N  
ATOM   2220  CA  VAL C  83       1.511 -47.431 -24.512  1.00 16.04           C  
ANISOU 2220  CA  VAL C  83     2438   1974   1682    180   -425    -59       C  
ATOM   2221  C   VAL C  83       1.421 -46.562 -25.758  1.00 17.46           C  
ANISOU 2221  C   VAL C  83     2979   2040   1615    319   -254     44       C  
ATOM   2222  O   VAL C  83       1.385 -45.323 -25.667  1.00 19.67           O  
ANISOU 2222  O   VAL C  83     3579   1994   1900     22   -481     57       O  
ATOM   2223  CB  VAL C  83       0.130 -48.062 -24.205  1.00 17.60           C  
ANISOU 2223  CB  VAL C  83     2519   1936   2231    445   -414     26       C  
ATOM   2224  CG1 VAL C  83       0.252 -49.097 -23.086  1.00 18.27           C  
ANISOU 2224  CG1 VAL C  83     2822   1903   2217    313   -324      4       C  
ATOM   2225  CG2 VAL C  83      -0.889 -46.982 -23.840  1.00 18.57           C  
ANISOU 2225  CG2 VAL C  83     2537   1968   2552    657   -244   -215       C  
ATOM   2226  N   ALA C  84       1.385 -47.207 -26.920  1.00 18.59           N  
ANISOU 2226  N   ALA C  84     2990   2529   1543    349    -81    226       N  
ATOM   2227  CA  ALA C  84       1.271 -46.492 -28.179  1.00 19.10           C  
ANISOU 2227  CA  ALA C  84     2701   2755   1799   -157      4     11       C  
ATOM   2228  C   ALA C  84      -0.147 -46.536 -28.706  1.00 18.64           C  
ANISOU 2228  C   ALA C  84     2449   2702   1930   -379   -231    241       C  
ATOM   2229  O   ALA C  84      -0.778 -47.590 -28.701  1.00 20.06           O  
ANISOU 2229  O   ALA C  84     2606   2703   2314   -341   -152    278       O  
ATOM   2230  CB  ALA C  84       2.214 -47.079 -29.206  1.00 22.67           C  
ANISOU 2230  CB  ALA C  84     2875   3609   2131   -170    317   -467       C  
ATOM   2231  N   LEU C  85      -0.631 -45.398 -29.190  1.00 20.21           N  
ANISOU 2231  N   LEU C  85     2819   2861   1999     38   -367    215       N  
ATOM   2232  CA  LEU C  85      -1.898 -45.343 -29.906  1.00 21.71           C  
ANISOU 2232  CA  LEU C  85     3079   3061   2109   -193   -351    412       C  
ATOM   2233  C   LEU C  85      -1.600 -45.376 -31.397  1.00 23.53           C  
ANISOU 2233  C   LEU C  85     3155   3549   2237   -721   -767    631       C  
ATOM   2234  O   LEU C  85      -0.782 -44.594 -31.896  1.00 26.96           O  
ANISOU 2234  O   LEU C  85     3445   4026   2774  -1161   -365    924       O  
ATOM   2235  CB  LEU C  85      -2.697 -44.088 -29.543  1.00 25.73           C  
ANISOU 2235  CB  LEU C  85     3395   3273   3107    143     -1    375       C  
ATOM   2236  CG  LEU C  85      -3.539 -44.066 -28.266  1.00 30.48           C  
ANISOU 2236  CG  LEU C  85     4065   3747   3770    722    249      8       C  
ATOM   2237  CD1 LEU C  85      -2.700 -44.256 -27.025  1.00 31.21           C  
ANISOU 2237  CD1 LEU C  85     4080   4317   3463    901     94    110       C  
ATOM   2238  CD2 LEU C  85      -4.317 -42.759 -28.180  1.00 32.47           C  
ANISOU 2238  CD2 LEU C  85     4540   3372   4426    403    382   -471       C  
ATOM   2239  N   GLN C  86      -2.251 -46.292 -32.102  1.00 27.20           N  
ANISOU 2239  N   GLN C  86     3526   4391   2419  -1012   -748    747       N  
ATOM   2240  CA  GLN C  86      -1.964 -46.503 -33.511  1.00 29.70           C  
ANISOU 2240  CA  GLN C  86     4088   4893   2303  -1343   -763    565       C  
ATOM   2241  C   GLN C  86      -3.245 -46.699 -34.296  1.00 31.41           C  
ANISOU 2241  C   GLN C  86     4576   5179   2179  -1415   -965    997       C  
ATOM   2242  O   GLN C  86      -3.996 -47.644 -34.048  1.00 32.36           O  
ANISOU 2242  O   GLN C  86     4350   5433   2511  -1625  -1203   1312       O  
ATOM   2243  CB  GLN C  86      -1.047 -47.712 -33.688  1.00 31.43           C  
ANISOU 2243  CB  GLN C  86     4356   5349   2237  -1244   -418    202       C  
ATOM   2244  CG  GLN C  86      -0.676 -48.012 -35.132  1.00 34.70           C  
ANISOU 2244  CG  GLN C  86     5009   5771   2405  -1290    -35    153       C  
ATOM   2245  CD  GLN C  86       0.308 -49.160 -35.239  1.00 39.39           C  
ANISOU 2245  CD  GLN C  86     5621   6161   3185   -841    635    209       C  
ATOM   2246  OE1 GLN C  86       0.020 -50.283 -34.824  1.00 40.09           O  
ANISOU 2246  OE1 GLN C  86     5761   6368   3103   -927    339   -332       O  
ATOM   2247  NE2 GLN C  86       1.487 -48.879 -35.770  1.00 41.95           N  
ANISOU 2247  NE2 GLN C  86     5725   6403   3813   -517   1045    534       N  
ATOM   2248  N   ARG C  87      -3.480 -45.813 -35.256  1.00 32.65           N  
ANISOU 2248  N   ARG C  87     4745   5029   2633  -1276  -1378   1378       N  
ATOM   2249  CA  ARG C  87      -4.681 -45.893 -36.080  1.00 36.63           C  
ANISOU 2249  CA  ARG C  87     5273   5426   3219  -1500  -1671   1730       C  
ATOM   2250  C   ARG C  87      -4.719 -47.170 -36.912  1.00 39.79           C  
ANISOU 2250  C   ARG C  87     5637   6151   3329  -2149  -1773   1526       C  
ATOM   2251  O   ARG C  87      -3.687 -47.652 -37.378  1.00 41.47           O  
ANISOU 2251  O   ARG C  87     5902   6660   3193  -2532  -1626   1354       O  
ATOM   2252  CB  ARG C  87      -4.777 -44.665 -36.990  1.00 37.50           C  
ANISOU 2252  CB  ARG C  87     5329   5374   3544  -1574  -1800   1927       C  
ATOM   2253  CG  ARG C  87      -5.333 -43.452 -36.284  1.00 38.21           C  
ANISOU 2253  CG  ARG C  87     5214   5347   3958  -1648  -2052   2049       C  
ATOM   2254  CD  ARG C  87      -6.841 -43.553 -36.142  1.00 39.91           C  
ANISOU 2254  CD  ARG C  87     5396   5537   4230  -1738  -2239   2109       C  
ATOM   2255  NE  ARG C  87      -7.511 -43.175 -37.384  1.00 40.67           N  
ANISOU 2255  NE  ARG C  87     5390   5615   4446  -1817  -2301   2238       N  
ATOM   2256  CZ  ARG C  87      -8.401 -43.927 -38.025  1.00 41.61           C  
ANISOU 2256  CZ  ARG C  87     5368   5719   4724  -1690  -2468   2226       C  
ATOM   2257  NH1 ARG C  87      -8.746 -45.117 -37.547  1.00 41.63           N  
ANISOU 2257  NH1 ARG C  87     5306   5757   4756  -1490  -2487   2164       N  
ATOM   2258  NH2 ARG C  87      -8.953 -43.483 -39.150  1.00 42.64           N  
ANISOU 2258  NH2 ARG C  87     5568   5772   4859  -1736  -2281   2578       N  
ATOM   2259  N   ASP C  88      -5.917 -47.722 -37.072  1.00 40.09           N  
ANISOU 2259  N   ASP C  88     5633   6085   3514  -2407  -1883   1681       N  
ATOM   2260  CA  ASP C  88      -6.130 -48.879 -37.934  1.00 41.00           C  
ANISOU 2260  CA  ASP C  88     5832   6302   3443  -2383  -1928   1463       C  
ATOM   2261  C   ASP C  88      -7.334 -48.620 -38.832  1.00 43.35           C  
ANISOU 2261  C   ASP C  88     5954   6818   3699  -2525  -2030   1590       C  
ATOM   2262  O   ASP C  88      -8.418 -49.154 -38.602  1.00 43.66           O  
ANISOU 2262  O   ASP C  88     6148   6820   3622  -2822  -1954   1385       O  
ATOM   2263  CB  ASP C  88      -6.336 -50.152 -37.106  1.00 43.87           C  
ANISOU 2263  CB  ASP C  88     6144   6597   3928  -2558  -1526   1130       C  
ATOM   2264  CG  ASP C  88      -6.438 -51.399 -37.966  1.00 47.21           C  
ANISOU 2264  CG  ASP C  88     6568   6860   4512  -2299  -1063    821       C  
ATOM   2265  OD1 ASP C  88      -6.046 -51.345 -39.150  1.00 50.13           O  
ANISOU 2265  OD1 ASP C  88     6792   7204   5052  -1953   -689    260       O  
ATOM   2266  OD2 ASP C  88      -6.911 -52.436 -37.458  1.00 49.01           O  
ANISOU 2266  OD2 ASP C  88     6899   6876   4845  -2086  -1291    788       O  
ATOM   2267  N   PRO C  89      -7.143 -47.789 -39.861  1.00 46.09           N  
ANISOU 2267  N   PRO C  89     6406   7554   3553  -2185  -1945   1489       N  
ATOM   2268  CA  PRO C  89      -8.254 -47.390 -40.731  1.00 49.10           C  
ANISOU 2268  CA  PRO C  89     6915   8071   3669  -2006  -1829   1862       C  
ATOM   2269  C   PRO C  89      -8.865 -48.559 -41.502  1.00 51.75           C  
ANISOU 2269  C   PRO C  89     7185   8406   4072  -2143  -1933   1712       C  
ATOM   2270  O   PRO C  89      -9.998 -48.452 -41.963  1.00 52.89           O  
ANISOU 2270  O   PRO C  89     7150   8822   4125  -1872  -2221   1933       O  
ATOM   2271  CB  PRO C  89      -7.604 -46.389 -41.691  1.00 49.06           C  
ANISOU 2271  CB  PRO C  89     7008   7927   3705  -1880  -1353   2039       C  
ATOM   2272  CG  PRO C  89      -6.161 -46.753 -41.697  1.00 46.45           C  
ANISOU 2272  CG  PRO C  89     6578   7680   3393  -1696  -1672   1754       C  
ATOM   2273  CD  PRO C  89      -5.862 -47.211 -40.298  1.00 45.45           C  
ANISOU 2273  CD  PRO C  89     6376   7518   3374  -1907  -1758   1590       C  
ATOM   2274  N   ASN C  90      -8.127 -49.656 -41.636  1.00 52.45           N  
ANISOU 2274  N   ASN C  90     7470   8336   4121  -2480  -1933   1557       N  
ATOM   2275  CA  ASN C  90      -8.615 -50.808 -42.388  1.00 54.56           C  
ANISOU 2275  CA  ASN C  90     7830   8341   4559  -2692  -1767   1061       C  
ATOM   2276  C   ASN C  90      -9.358 -51.822 -41.518  1.00 53.36           C  
ANISOU 2276  C   ASN C  90     7843   8194   4240  -2898  -1958    580       C  
ATOM   2277  O   ASN C  90      -9.707 -52.910 -41.985  1.00 54.13           O  
ANISOU 2277  O   ASN C  90     8158   8204   4206  -3118  -1988    458       O  
ATOM   2278  CB  ASN C  90      -7.455 -51.499 -43.107  1.00 57.55           C  
ANISOU 2278  CB  ASN C  90     8137   8498   5232  -2487  -1512   1326       C  
ATOM   2279  CG  ASN C  90      -6.928 -50.688 -44.276  1.00 60.68           C  
ANISOU 2279  CG  ASN C  90     8373   8673   6009  -2010  -1598   1697       C  
ATOM   2280  OD1 ASN C  90      -7.688 -49.998 -44.958  1.00 61.84           O  
ANISOU 2280  OD1 ASN C  90     8468   8870   6158  -1660  -1822   1797       O  
ATOM   2281  ND2 ASN C  90      -5.621 -50.766 -44.513  1.00 60.72           N  
ANISOU 2281  ND2 ASN C  90     8207   8600   6262  -1950  -1659   1907       N  
ATOM   2282  N   ASN C  91      -9.593 -51.474 -40.255  1.00 51.67           N  
ANISOU 2282  N   ASN C  91     7378   7999   4256  -2689  -2201    651       N  
ATOM   2283  CA  ASN C  91     -10.390 -52.330 -39.381  1.00 49.22           C  
ANISOU 2283  CA  ASN C  91     6726   7657   4318  -2411  -2432    540       C  
ATOM   2284  C   ASN C  91     -11.807 -52.471 -39.926  1.00 51.72           C  
ANISOU 2284  C   ASN C  91     6602   7969   5082  -2268  -2395    761       C  
ATOM   2285  O   ASN C  91     -12.537 -51.483 -40.038  1.00 51.58           O  
ANISOU 2285  O   ASN C  91     6516   8127   4956  -2314  -2748    798       O  
ATOM   2286  CB  ASN C  91     -10.423 -51.778 -37.957  1.00 46.46           C  
ANISOU 2286  CB  ASN C  91     6214   7103   4338  -1984  -2576    465       C  
ATOM   2287  CG  ASN C  91     -11.051 -52.744 -36.973  1.00 45.36           C  
ANISOU 2287  CG  ASN C  91     6026   6601   4609  -2107  -2529    101       C  
ATOM   2288  OD1 ASN C  91     -12.238 -53.065 -37.068  1.00 46.38           O  
ANISOU 2288  OD1 ASN C  91     6166   6455   5001  -2037  -2415    -20       O  
ATOM   2289  ND2 ASN C  91     -10.258 -53.207 -36.009  1.00 44.65           N  
ANISOU 2289  ND2 ASN C  91     6209   6405   4352  -2335  -1973    106       N  
ATOM   2290  N   PRO C  92     -12.203 -53.706 -40.265  1.00 52.25           N  
ANISOU 2290  N   PRO C  92     6471   7944   5437  -2166  -2490    634       N  
ATOM   2291  CA  PRO C  92     -13.494 -53.947 -40.920  1.00 53.69           C  
ANISOU 2291  CA  PRO C  92     6560   7981   5858  -2122  -2305    652       C  
ATOM   2292  C   PRO C  92     -14.693 -53.726 -39.998  1.00 53.57           C  
ANISOU 2292  C   PRO C  92     6565   8036   5754  -2169  -2793    622       C  
ATOM   2293  O   PRO C  92     -15.821 -53.678 -40.481  1.00 54.77           O  
ANISOU 2293  O   PRO C  92     6636   8134   6039  -2262  -2899    222       O  
ATOM   2294  CB  PRO C  92     -13.400 -55.414 -41.349  1.00 53.36           C  
ANISOU 2294  CB  PRO C  92     6410   7966   5899  -2151  -2296    534       C  
ATOM   2295  CG  PRO C  92     -12.443 -56.026 -40.392  1.00 52.30           C  
ANISOU 2295  CG  PRO C  92     6277   7949   5646  -2105  -2628    592       C  
ATOM   2296  CD  PRO C  92     -11.445 -54.952 -40.052  1.00 51.14           C  
ANISOU 2296  CD  PRO C  92     6190   7951   5290  -2105  -2891    558       C  
ATOM   2297  N   TYR C  93     -14.453 -53.581 -38.698  1.00 52.07           N  
ANISOU 2297  N   TYR C  93     6407   8040   5339  -1933  -3083   1038       N  
ATOM   2298  CA  TYR C  93     -15.543 -53.374 -37.749  1.00 51.86           C  
ANISOU 2298  CA  TYR C  93     6079   7962   5663  -1934  -3091   1308       C  
ATOM   2299  C   TYR C  93     -15.730 -51.893 -37.422  1.00 51.38           C  
ANISOU 2299  C   TYR C  93     5893   7788   5840  -1945  -3085   1765       C  
ATOM   2300  O   TYR C  93     -16.811 -51.471 -37.010  1.00 53.34           O  
ANISOU 2300  O   TYR C  93     6077   7899   6293  -1850  -2873   1918       O  
ATOM   2301  CB  TYR C  93     -15.293 -54.170 -36.463  1.00 52.68           C  
ANISOU 2301  CB  TYR C  93     5969   7928   6119  -2114  -2900   1213       C  
ATOM   2302  CG  TYR C  93     -15.219 -55.666 -36.675  1.00 52.49           C  
ANISOU 2302  CG  TYR C  93     6007   7851   6086  -2299  -3003   1078       C  
ATOM   2303  CD1 TYR C  93     -16.372 -56.442 -36.704  1.00 53.04           C  
ANISOU 2303  CD1 TYR C  93     6222   7793   6136  -2316  -2958    803       C  
ATOM   2304  CD2 TYR C  93     -13.997 -56.302 -36.854  1.00 52.83           C  
ANISOU 2304  CD2 TYR C  93     6343   7857   5871  -2197  -2993   1144       C  
ATOM   2305  CE1 TYR C  93     -16.308 -57.811 -36.901  1.00 53.32           C  
ANISOU 2305  CE1 TYR C  93     6460   7793   6006  -2175  -2987    739       C  
ATOM   2306  CE2 TYR C  93     -13.923 -57.667 -37.052  1.00 53.60           C  
ANISOU 2306  CE2 TYR C  93     6547   7933   5886  -2065  -2920   1083       C  
ATOM   2307  CZ  TYR C  93     -15.080 -58.417 -37.075  1.00 54.29           C  
ANISOU 2307  CZ  TYR C  93     6844   7869   5914  -1929  -2799    847       C  
ATOM   2308  OH  TYR C  93     -15.008 -59.778 -37.270  1.00 55.66           O  
ANISOU 2308  OH  TYR C  93     7303   7914   5931  -1495  -2558    807       O  
ATOM   2309  N   ASP C  94     -14.673 -51.110 -37.613  1.00 49.54           N  
ANISOU 2309  N   ASP C  94     5715   7474   5634  -2138  -2908   1986       N  
ATOM   2310  CA  ASP C  94     -14.684 -49.694 -37.260  1.00 48.44           C  
ANISOU 2310  CA  ASP C  94     5610   7176   5619  -1796  -2616   2194       C  
ATOM   2311  C   ASP C  94     -13.534 -48.971 -37.957  1.00 46.81           C  
ANISOU 2311  C   ASP C  94     5444   6986   5356  -1710  -2747   2197       C  
ATOM   2312  O   ASP C  94     -12.367 -49.195 -37.633  1.00 46.95           O  
ANISOU 2312  O   ASP C  94     5439   6910   5492  -1731  -2815   2173       O  
ATOM   2313  CB  ASP C  94     -14.582 -49.520 -35.737  1.00 47.84           C  
ANISOU 2313  CB  ASP C  94     5227   7056   5895  -1542  -2914   2039       C  
ATOM   2314  CG  ASP C  94     -14.739 -48.074 -35.294  1.00 47.33           C  
ANISOU 2314  CG  ASP C  94     4997   6870   6116  -1262  -2917   2002       C  
ATOM   2315  OD1 ASP C  94     -15.018 -47.205 -36.147  1.00 47.57           O  
ANISOU 2315  OD1 ASP C  94     5304   6742   6028  -1055  -2983   2091       O  
ATOM   2316  OD2 ASP C  94     -14.600 -47.810 -34.082  1.00 47.18           O  
ANISOU 2316  OD2 ASP C  94     4683   6696   6547  -1115  -2539   2309       O  
ATOM   2317  N   LYS C  95     -13.866 -48.108 -38.914  1.00 46.41           N  
ANISOU 2317  N   LYS C  95     5823   7005   4806  -1590  -2625   2051       N  
ATOM   2318  CA  LYS C  95     -12.851 -47.363 -39.648  1.00 46.43           C  
ANISOU 2318  CA  LYS C  95     5882   7018   4742  -1083  -2662   1901       C  
ATOM   2319  C   LYS C  95     -12.075 -46.405 -38.743  1.00 46.55           C  
ANISOU 2319  C   LYS C  95     5918   6920   4848  -1118  -2701   1893       C  
ATOM   2320  O   LYS C  95     -10.974 -45.982 -39.086  1.00 46.52           O  
ANISOU 2320  O   LYS C  95     5934   6751   4990  -1397  -2830   1898       O  
ATOM   2321  CB  LYS C  95     -13.487 -46.587 -40.806  1.00 48.70           C  
ANISOU 2321  CB  LYS C  95     6153   7373   4976   -508  -2742   1986       C  
ATOM   2322  CG  LYS C  95     -14.492 -45.534 -40.375  1.00 51.43           C  
ANISOU 2322  CG  LYS C  95     6507   7754   5278   -155  -2924   1988       C  
ATOM   2323  CD  LYS C  95     -15.130 -44.866 -41.585  1.00 55.57           C  
ANISOU 2323  CD  LYS C  95     7027   8326   5759   -323  -2827   1672       C  
ATOM   2324  CE  LYS C  95     -16.263 -43.939 -41.178  1.00 59.44           C  
ANISOU 2324  CE  LYS C  95     7414   8699   6472   -450  -2485   1166       C  
ATOM   2325  NZ  LYS C  95     -15.781 -42.779 -40.383  1.00 60.91           N  
ANISOU 2325  NZ  LYS C  95     7568   8886   6690   -580  -2479    830       N  
ATOM   2326  N   ASN C  96     -12.649 -46.071 -37.591  1.00 45.45           N  
ANISOU 2326  N   ASN C  96     5729   6824   4714   -669  -2701   1682       N  
ATOM   2327  CA  ASN C  96     -12.007 -45.153 -36.654  1.00 44.34           C  
ANISOU 2327  CA  ASN C  96     5291   6642   4915   -511  -2667   1676       C  
ATOM   2328  C   ASN C  96     -11.141 -45.852 -35.618  1.00 42.56           C  
ANISOU 2328  C   ASN C  96     5005   6280   4888   -774  -2503   1566       C  
ATOM   2329  O   ASN C  96     -10.640 -45.205 -34.700  1.00 42.84           O  
ANISOU 2329  O   ASN C  96     4863   6438   4976   -804  -2712   1325       O  
ATOM   2330  CB  ASN C  96     -13.057 -44.309 -35.937  1.00 45.72           C  
ANISOU 2330  CB  ASN C  96     5167   6953   5253    206  -2663   1666       C  
ATOM   2331  CG  ASN C  96     -13.784 -43.377 -36.877  1.00 50.25           C  
ANISOU 2331  CG  ASN C  96     5705   7798   5589    553  -2314   1420       C  
ATOM   2332  OD1 ASN C  96     -13.524 -43.371 -38.079  1.00 52.57           O  
ANISOU 2332  OD1 ASN C  96     6105   8010   5859    399  -1838   1302       O  
ATOM   2333  ND2 ASN C  96     -14.702 -42.585 -36.338  1.00 52.70           N  
ANISOU 2333  ND2 ASN C  96     5861   8091   6071    765  -1850   1020       N  
ATOM   2334  N   ALA C  97     -10.960 -47.163 -35.773  1.00 40.33           N  
ANISOU 2334  N   ALA C  97     4759   5755   4809  -1242  -2235   1348       N  
ATOM   2335  CA  ALA C  97     -10.258 -47.976 -34.777  1.00 36.74           C  
ANISOU 2335  CA  ALA C  97     4463   5060   4437  -1136  -2180   1420       C  
ATOM   2336  C   ALA C  97      -8.863 -47.454 -34.436  1.00 33.91           C  
ANISOU 2336  C   ALA C  97     4178   4732   3976  -1108  -1973   1295       C  
ATOM   2337  O   ALA C  97      -8.100 -47.035 -35.313  1.00 34.75           O  
ANISOU 2337  O   ALA C  97     4338   4958   3906  -1216  -2052   1380       O  
ATOM   2338  CB  ALA C  97     -10.164 -49.419 -35.251  1.00 38.11           C  
ANISOU 2338  CB  ALA C  97     4676   5076   4727  -1118  -2164   1403       C  
ATOM   2339  N   ILE C  98      -8.548 -47.475 -33.144  1.00 29.81           N  
ANISOU 2339  N   ILE C  98     3553   4230   3544   -842  -1925   1126       N  
ATOM   2340  CA  ILE C  98      -7.228 -47.107 -32.659  1.00 28.39           C  
ANISOU 2340  CA  ILE C  98     3599   3752   3436   -586  -1512   1064       C  
ATOM   2341  C   ILE C  98      -6.701 -48.248 -31.800  1.00 25.72           C  
ANISOU 2341  C   ILE C  98     3342   3668   2764   -540  -1253    692       C  
ATOM   2342  O   ILE C  98      -7.250 -48.561 -30.735  1.00 25.38           O  
ANISOU 2342  O   ILE C  98     3352   3196   3094   -385   -938    753       O  
ATOM   2343  CB  ILE C  98      -7.257 -45.778 -31.865  1.00 28.54           C  
ANISOU 2343  CB  ILE C  98     3515   3391   3937   -266  -1399   1425       C  
ATOM   2344  CG1 ILE C  98      -7.715 -44.633 -32.775  1.00 31.29           C  
ANISOU 2344  CG1 ILE C  98     3868   3526   4497   -168  -1067   1455       C  
ATOM   2345  CG2 ILE C  98      -5.892 -45.453 -31.280  1.00 26.19           C  
ANISOU 2345  CG2 ILE C  98     3123   2869   3957   -696  -1432   1105       C  
ATOM   2346  CD1 ILE C  98      -7.962 -43.339 -32.055  1.00 32.37           C  
ANISOU 2346  CD1 ILE C  98     3932   3449   4916   -449  -1161   1222       C  
ATOM   2347  N   LYS C  99      -5.656 -48.898 -32.295  1.00 24.42           N  
ANISOU 2347  N   LYS C  99     3254   3493   2530   -465   -753    680       N  
ATOM   2348  CA  LYS C  99      -4.987 -49.944 -31.542  1.00 23.18           C  
ANISOU 2348  CA  LYS C  99     3194   3312   2303   -771   -325    114       C  
ATOM   2349  C   LYS C  99      -4.217 -49.348 -30.382  1.00 21.02           C  
ANISOU 2349  C   LYS C  99     2691   2995   2301   -819   -494    -20       C  
ATOM   2350  O   LYS C  99      -3.702 -48.229 -30.466  1.00 22.22           O  
ANISOU 2350  O   LYS C  99     3107   2799   2537   -854   -564    225       O  
ATOM   2351  CB  LYS C  99      -4.034 -50.738 -32.440  1.00 23.96           C  
ANISOU 2351  CB  LYS C  99     3381   3470   2251  -1099    -76   -519       C  
ATOM   2352  CG  LYS C  99      -4.715 -51.424 -33.606  1.00 26.23           C  
ANISOU 2352  CG  LYS C  99     3844   3853   2270  -1390   -376   -625       C  
ATOM   2353  CD  LYS C  99      -3.758 -52.324 -34.357  1.00 30.55           C  
ANISOU 2353  CD  LYS C  99     5011   4318   2279  -1384    505   -603       C  
ATOM   2354  CE  LYS C  99      -2.698 -51.532 -35.053  1.00 36.34           C  
ANISOU 2354  CE  LYS C  99     5793   4919   3097   -620    773   -843       C  
ATOM   2355  NZ  LYS C  99      -1.715 -52.426 -35.734  1.00 39.89           N  
ANISOU 2355  NZ  LYS C  99     6211   5366   3577   -130   1421  -1270       N  
ATOM   2356  N   VAL C 100      -4.128 -50.103 -29.296  1.00 18.50           N  
ANISOU 2356  N   VAL C 100     2531   2679   1819   -116   -143      2       N  
ATOM   2357  CA  VAL C 100      -3.224 -49.759 -28.220  1.00 16.82           C  
ANISOU 2357  CA  VAL C 100     2042   2563   1786    263   -215     -8       C  
ATOM   2358  C   VAL C 100      -2.169 -50.854 -28.154  1.00 16.92           C  
ANISOU 2358  C   VAL C 100     2427   2378   1625    218     83    -39       C  
ATOM   2359  O   VAL C 100      -2.504 -52.032 -27.956  1.00 17.86           O  
ANISOU 2359  O   VAL C 100     2545   2143   2096     49     91     53       O  
ATOM   2360  CB  VAL C 100      -3.965 -49.616 -26.872  1.00 16.57           C  
ANISOU 2360  CB  VAL C 100     2121   2426   1750    631    -86    -48       C  
ATOM   2361  CG1 VAL C 100      -2.972 -49.320 -25.738  1.00 18.15           C  
ANISOU 2361  CG1 VAL C 100     2190   2915   1791    483   -647   -238       C  
ATOM   2362  CG2 VAL C 100      -5.036 -48.526 -26.958  1.00 18.38           C  
ANISOU 2362  CG2 VAL C 100     2229   2408   2348    471     -4    -94       C  
ATOM   2363  N   ASN C 101      -0.909 -50.471 -28.365  1.00 17.26           N  
ANISOU 2363  N   ASN C 101     2261   2536   1761    272   -137   -194       N  
ATOM   2364  CA  ASN C 101       0.220 -51.410 -28.368  1.00 16.45           C  
ANISOU 2364  CA  ASN C 101     2186   2350   1713    158    122    -92       C  
ATOM   2365  C   ASN C 101       1.165 -51.136 -27.216  1.00 16.11           C  
ANISOU 2365  C   ASN C 101     2207   2158   1756    149    142   -367       C  
ATOM   2366  O   ASN C 101       1.270 -49.995 -26.753  1.00 17.25           O  
ANISOU 2366  O   ASN C 101     2571   2155   1826    242     55   -521       O  
ATOM   2367  CB  ASN C 101       1.028 -51.324 -29.670  1.00 17.26           C  
ANISOU 2367  CB  ASN C 101     2558   2501   1499   -109    218   -120       C  
ATOM   2368  CG  ASN C 101       0.183 -51.525 -30.908  1.00 19.51           C  
ANISOU 2368  CG  ASN C 101     2741   2746   1927   -512     39   -320       C  
ATOM   2369  OD1 ASN C 101      -0.756 -52.320 -30.917  1.00 19.93           O  
ANISOU 2369  OD1 ASN C 101     3109   2431   2030   -757    193   -204       O  
ATOM   2370  ND2 ASN C 101       0.533 -50.817 -31.978  1.00 23.09           N  
ANISOU 2370  ND2 ASN C 101     3477   2857   2437   -828    440   -269       N  
ATOM   2371  N   ASN C 102       1.891 -52.149 -26.766  1.00 15.60           N  
ANISOU 2371  N   ASN C 102     2202   1797   1927    266    142   -219       N  
ATOM   2372  CA  ASN C 102       2.936 -51.861 -25.790  1.00 15.76           C  
ANISOU 2372  CA  ASN C 102     2166   1629   2194    117     49   -267       C  
ATOM   2373  C   ASN C 102       4.203 -51.387 -26.506  1.00 16.50           C  
ANISOU 2373  C   ASN C 102     2473   1447   2351    105    284   -422       C  
ATOM   2374  O   ASN C 102       4.239 -51.310 -27.737  1.00 16.49           O  
ANISOU 2374  O   ASN C 102     2502   1579   2182     46     90   -401       O  
ATOM   2375  CB  ASN C 102       3.199 -53.060 -24.850  1.00 15.98           C  
ANISOU 2375  CB  ASN C 102     2464   1335   2272    317    740   -111       C  
ATOM   2376  CG  ASN C 102       3.778 -54.295 -25.544  1.00 16.02           C  
ANISOU 2376  CG  ASN C 102     2509   1529   2048    184    650    271       C  
ATOM   2377  OD1 ASN C 102       4.355 -54.222 -26.620  1.00 16.42           O  
ANISOU 2377  OD1 ASN C 102     2908   1476   1855     15    572   -142       O  
ATOM   2378  ND2 ASN C 102       3.643 -55.448 -24.881  1.00 15.67           N  
ANISOU 2378  ND2 ASN C 102     2411   1716   1827    -72    372   -140       N  
ATOM   2379  N   VAL C 103       5.229 -51.031 -25.746  1.00 15.83           N  
ANISOU 2379  N   VAL C 103     2249   1571   2194     49    -32    -82       N  
ATOM   2380  CA AVAL C 103       6.406 -50.436 -26.394  0.82 16.27           C  
ANISOU 2380  CA AVAL C 103     2498   1708   1975   -179   -430   -443       C  
ATOM   2381  CA BVAL C 103       6.466 -50.476 -26.273  0.18 17.47           C  
ANISOU 2381  CA BVAL C 103     2592   1758   2290   -184      0   -358       C  
ATOM   2382  C   VAL C 103       7.181 -51.431 -27.246  1.00 16.99           C  
ANISOU 2382  C   VAL C 103     2599   1600   2257    -48    278   -265       C  
ATOM   2383  O   VAL C 103       7.981 -51.013 -28.089  1.00 18.08           O  
ANISOU 2383  O   VAL C 103     3099   1725   2046    -81    448   -360       O  
ATOM   2384  CB AVAL C 103       7.396 -49.797 -25.393  0.82 18.75           C  
ANISOU 2384  CB AVAL C 103     3299   1936   1890    589   -448   -367       C  
ATOM   2385  CB BVAL C 103       7.392 -50.105 -25.090  0.18 19.80           C  
ANISOU 2385  CB BVAL C 103     3072   2035   2414   -321     45   -672       C  
ATOM   2386  CG1AVAL C 103       6.798 -48.531 -24.785  0.82 19.26           C  
ANISOU 2386  CG1AVAL C 103     3666   1605   2046    752   -252   -440       C  
ATOM   2387  CG1BVAL C 103       8.723 -49.628 -25.559  0.18 19.37           C  
ANISOU 2387  CG1BVAL C 103     2915   2035   2411   -503    -34   -699       C  
ATOM   2388  CG2AVAL C 103       7.833 -50.811 -24.342  0.82 20.89           C  
ANISOU 2388  CG2AVAL C 103     3386   2564   1989    346   -378     58       C  
ATOM   2389  CG2BVAL C 103       6.734 -49.039 -24.229  0.18 21.50           C  
ANISOU 2389  CG2BVAL C 103     3429   2171   2570   -360    124   -968       C  
ATOM   2390  N   ASN C 104       6.929 -52.733 -27.089  1.00 15.61           N  
ANISOU 2390  N   ASN C 104     2365   1529   2039    175    342   -268       N  
ATOM   2391  CA  ASN C 104       7.577 -53.719 -27.951  1.00 15.32           C  
ANISOU 2391  CA  ASN C 104     2070   1664   2088    337   -247    128       C  
ATOM   2392  C   ASN C 104       6.804 -54.006 -29.227  1.00 17.01           C  
ANISOU 2392  C   ASN C 104     2362   1816   2285    135    363     44       C  
ATOM   2393  O   ASN C 104       7.260 -54.788 -30.073  1.00 18.95           O  
ANISOU 2393  O   ASN C 104     2796   1736   2670    191    775   -237       O  
ATOM   2394  CB  ASN C 104       7.791 -55.029 -27.201  1.00 20.03           C  
ANISOU 2394  CB  ASN C 104     2825   1973   2813    604   -301    177       C  
ATOM   2395  CG  ASN C 104       8.719 -54.870 -26.033  1.00 30.12           C  
ANISOU 2395  CG  ASN C 104     3907   3437   4100     54   -486    617       C  
ATOM   2396  OD1 ASN C 104       8.461 -55.391 -24.948  1.00 38.20           O  
ANISOU 2396  OD1 ASN C 104     5083   4562   4871   -354   -231    613       O  
ATOM   2397  ND2 ASN C 104       9.804 -54.131 -26.237  1.00 31.17           N  
ANISOU 2397  ND2 ASN C 104     3301   3731   4809    283   -802    827       N  
ATOM   2398  N   GLY C 105       5.638 -53.382 -29.370  1.00 16.17           N  
ANISOU 2398  N   GLY C 105     2437   1562   2146    -88   -111   -261       N  
ATOM   2399  CA  GLY C 105       4.863 -53.528 -30.589  1.00 17.15           C  
ANISOU 2399  CA  GLY C 105     2644   1797   2075   -154    156   -367       C  
ATOM   2400  C   GLY C 105       3.666 -54.449 -30.499  1.00 16.48           C  
ANISOU 2400  C   GLY C 105     2430   1899   1935    102    227   -151       C  
ATOM   2401  O   GLY C 105       2.851 -54.501 -31.423  1.00 18.91           O  
ANISOU 2401  O   GLY C 105     2769   2222   2195     53    157   -334       O  
ATOM   2402  N   ASN C 106       3.541 -55.171 -29.390  1.00 17.38           N  
ANISOU 2402  N   ASN C 106     2815   1605   2183   -393    814   -610       N  
ATOM   2403  CA  ASN C 106       2.453 -56.136 -29.248  1.00 17.03           C  
ANISOU 2403  CA  ASN C 106     2619   1713   2140   -115    548   -309       C  
ATOM   2404  C   ASN C 106       1.154 -55.456 -28.877  1.00 15.77           C  
ANISOU 2404  C   ASN C 106     2167   1933   1892   -227    144   -677       C  
ATOM   2405  O   ASN C 106       1.120 -54.636 -27.957  1.00 17.27           O  
ANISOU 2405  O   ASN C 106     2422   2062   2078   -316    251  -1062       O  
ATOM   2406  CB  ASN C 106       2.805 -57.188 -28.205  1.00 18.18           C  
ANISOU 2406  CB  ASN C 106     2806   1870   2233    -45    710   -549       C  
ATOM   2407  CG  ASN C 106       3.887 -58.125 -28.698  1.00 19.89           C  
ANISOU 2407  CG  ASN C 106     2859   2106   2593    282    649   -350       C  
ATOM   2408  OD1 ASN C 106       3.692 -58.820 -29.684  1.00 22.29           O  
ANISOU 2408  OD1 ASN C 106     3173   2331   2964    -26    608  -1053       O  
ATOM   2409  ND2 ASN C 106       5.034 -58.123 -28.039  1.00 23.42           N  
ANISOU 2409  ND2 ASN C 106     3244   2573   3081    107    950    158       N  
ATOM   2410  N   GLN C 107       0.085 -55.798 -29.589  1.00 16.99           N  
ANISOU 2410  N   GLN C 107     1949   2378   2128   -410    223    -83       N  
ATOM   2411  CA  GLN C 107      -1.210 -55.190 -29.314  1.00 15.49           C  
ANISOU 2411  CA  GLN C 107     1681   2297   1906   -220   -128   -173       C  
ATOM   2412  C   GLN C 107      -1.752 -55.593 -27.937  1.00 17.28           C  
ANISOU 2412  C   GLN C 107     2666   2242   1656    -89    254   -267       C  
ATOM   2413  O   GLN C 107      -1.718 -56.765 -27.555  1.00 17.16           O  
ANISOU 2413  O   GLN C 107     2444   2172   1904   -112    263   -186       O  
ATOM   2414  CB  GLN C 107      -2.218 -55.541 -30.400  1.00 18.30           C  
ANISOU 2414  CB  GLN C 107     2116   2839   1998   -232    -14   -127       C  
ATOM   2415  CG  GLN C 107      -3.537 -54.823 -30.215  1.00 19.56           C  
ANISOU 2415  CG  GLN C 107     2358   3018   2057    -51   -213   -404       C  
ATOM   2416  CD  GLN C 107      -4.408 -54.830 -31.458  1.00 22.06           C  
ANISOU 2416  CD  GLN C 107     2908   3235   2239   -549      0   -397       C  
ATOM   2417  OE1 GLN C 107      -4.100 -55.497 -32.454  1.00 24.11           O  
ANISOU 2417  OE1 GLN C 107     3332   3609   2221   -821    232   -538       O  
ATOM   2418  NE2 GLN C 107      -5.511 -54.089 -31.404  1.00 22.92           N  
ANISOU 2418  NE2 GLN C 107     3104   3165   2441   -402      2   -175       N  
ATOM   2419  N   VAL C 108      -2.229 -54.594 -27.194  1.00 17.04           N  
ANISOU 2419  N   VAL C 108     2672   2154   1649    -28    459   -558       N  
ATOM   2420  CA  VAL C 108      -2.846 -54.790 -25.891  1.00 15.54           C  
ANISOU 2420  CA  VAL C 108     2085   1974   1847   -303    130   -498       C  
ATOM   2421  C   VAL C 108      -4.371 -54.853 -26.038  1.00 15.34           C  
ANISOU 2421  C   VAL C 108     2087   1792   1948    -73   -287   -313       C  
ATOM   2422  O   VAL C 108      -5.039 -55.679 -25.420  1.00 17.44           O  
ANISOU 2422  O   VAL C 108     2351   1886   2390   -209    242   -260       O  
ATOM   2423  CB  VAL C 108      -2.452 -53.645 -24.925  1.00 16.01           C  
ANISOU 2423  CB  VAL C 108     2114   2326   1643   -334    -13   -702       C  
ATOM   2424  CG1 VAL C 108      -3.193 -53.756 -23.594  1.00 16.65           C  
ANISOU 2424  CG1 VAL C 108     2826   1896   1604   -336    443   -359       C  
ATOM   2425  CG2 VAL C 108      -0.941 -53.642 -24.703  1.00 19.15           C  
ANISOU 2425  CG2 VAL C 108     2252   2530   2494   -136     19   -473       C  
ATOM   2426  N   GLY C 109      -4.912 -53.962 -26.860  1.00 17.42           N  
ANISOU 2426  N   GLY C 109     2064   2221   2335    120   -267     50       N  
ATOM   2427  CA  GLY C 109      -6.337 -53.906 -27.105  1.00 18.01           C  
ANISOU 2427  CA  GLY C 109     2317   2302   2224     47   -170    104       C  
ATOM   2428  C   GLY C 109      -6.656 -52.764 -28.043  1.00 18.56           C  
ANISOU 2428  C   GLY C 109     2406   2320   2325    -94     10    -80       C  
ATOM   2429  O   GLY C 109      -5.833 -52.411 -28.893  1.00 18.75           O  
ANISOU 2429  O   GLY C 109     2277   2499   2347    -90    -95     51       O  
ATOM   2430  N   HIS C 110      -7.858 -52.210 -27.904  1.00 19.93           N  
ANISOU 2430  N   HIS C 110     2597   2549   2426    123   -369   -121       N  
ATOM   2431  CA  HIS C 110      -8.309 -51.071 -28.700  1.00 21.14           C  
ANISOU 2431  CA  HIS C 110     2512   2869   2650    250   -595    115       C  
ATOM   2432  C   HIS C 110      -8.806 -49.978 -27.781  1.00 21.04           C  
ANISOU 2432  C   HIS C 110     2462   2700   2834    162   -742    395       C  
ATOM   2433  O   HIS C 110      -9.241 -50.261 -26.668  1.00 22.09           O  
ANISOU 2433  O   HIS C 110     2766   2909   2720    -55   -186    498       O  
ATOM   2434  CB  HIS C 110      -9.446 -51.458 -29.655  1.00 22.30           C  
ANISOU 2434  CB  HIS C 110     2757   3135   2580    -99   -852   -109       C  
ATOM   2435  CG  HIS C 110      -8.997 -52.142 -30.909  1.00 23.70           C  
ANISOU 2435  CG  HIS C 110     3114   3436   2456   -251   -757    146       C  
ATOM   2436  ND1 HIS C 110      -9.160 -53.495 -31.119  1.00 25.00           N  
ANISOU 2436  ND1 HIS C 110     3168   3638   2692   -659   -966   -132       N  
ATOM   2437  CD2 HIS C 110      -8.408 -51.656 -32.029  1.00 25.97           C  
ANISOU 2437  CD2 HIS C 110     3358   3865   2643   -321   -566    141       C  
ATOM   2438  CE1 HIS C 110      -8.682 -53.814 -32.309  1.00 25.27           C  
ANISOU 2438  CE1 HIS C 110     3359   3736   2505   -722   -918   -104       C  
ATOM   2439  NE2 HIS C 110      -8.215 -52.718 -32.881  1.00 26.62           N  
ANISOU 2439  NE2 HIS C 110     3522   4006   2587   -507   -809     69       N  
ATOM   2440  N   LEU C 111      -8.771 -48.734 -28.246  1.00 23.00           N  
ANISOU 2440  N   LEU C 111     2558   2751   3430      3   -850    653       N  
ATOM   2441  CA  LEU C 111      -9.538 -47.688 -27.588  1.00 24.35           C  
ANISOU 2441  CA  LEU C 111     2685   2616   3950     31   -732    862       C  
ATOM   2442  C   LEU C 111     -11.022 -47.999 -27.727  1.00 28.27           C  
ANISOU 2442  C   LEU C 111     3035   3126   4579     16   -597    728       C  
ATOM   2443  O   LEU C 111     -11.464 -48.485 -28.772  1.00 27.55           O  
ANISOU 2443  O   LEU C 111     3106   2999   4364   -147   -823    891       O  
ATOM   2444  CB  LEU C 111      -9.240 -46.315 -28.186  1.00 25.89           C  
ANISOU 2444  CB  LEU C 111     3059   2661   4118   -399   -572    774       C  
ATOM   2445  CG  LEU C 111      -7.870 -45.717 -27.885  1.00 26.21           C  
ANISOU 2445  CG  LEU C 111     3453   2666   3838   -243   -554    972       C  
ATOM   2446  CD1 LEU C 111      -7.833 -44.271 -28.349  1.00 27.80           C  
ANISOU 2446  CD1 LEU C 111     3909   2583   4071    -40   -184   1170       C  
ATOM   2447  CD2 LEU C 111      -7.547 -45.808 -26.408  1.00 27.46           C  
ANISOU 2447  CD2 LEU C 111     3666   3146   3620    -96   -996    743       C  
ATOM   2448  N   LYS C 112     -11.783 -47.718 -26.674  1.00 32.46           N  
ANISOU 2448  N   LYS C 112     3131   3608   5596    436   -377    470       N  
ATOM   2449  CA  LYS C 112     -13.237 -47.843 -26.701  1.00 37.21           C  
ANISOU 2449  CA  LYS C 112     3016   4258   6864    557   -513    402       C  
ATOM   2450  C   LYS C 112     -13.783 -47.094 -27.914  1.00 37.49           C  
ANISOU 2450  C   LYS C 112     2508   4342   7394    315  -1519    489       C  
ATOM   2451  O   LYS C 112     -13.366 -45.967 -28.177  1.00 40.45           O  
ANISOU 2451  O   LYS C 112     2900   4225   8246    413  -1100    554       O  
ATOM   2452  CB  LYS C 112     -13.842 -47.294 -25.406  1.00 42.37           C  
ANISOU 2452  CB  LYS C 112     3476   5101   7522    695    191    175       C  
ATOM   2453  CG  LYS C 112     -15.135 -47.963 -24.990  1.00 46.06           C  
ANISOU 2453  CG  LYS C 112     3966   5702   7834    763    383    115       C  
ATOM   2454  CD  LYS C 112     -15.698 -47.361 -23.716  1.00 49.07           C  
ANISOU 2454  CD  LYS C 112     4365   6153   8126    972    785     84       C  
ATOM   2455  CE  LYS C 112     -16.443 -46.068 -24.005  1.00 53.03           C  
ANISOU 2455  CE  LYS C 112     5005   6742   8403    983   1210    160       C  
ATOM   2456  NZ  LYS C 112     -17.309 -45.647 -22.868  1.00 54.55           N  
ANISOU 2456  NZ  LYS C 112     5216   7051   8458   1010   1502    202       N  
ATOM   2457  N   LYS C 113     -14.693 -47.717 -28.660  1.00 38.63           N  
ANISOU 2457  N   LYS C 113     2805   4284   7590    131  -1335    576       N  
ATOM   2458  CA  LYS C 113     -15.102 -47.177 -29.958  1.00 40.52           C  
ANISOU 2458  CA  LYS C 113     3154   4407   7836   -265  -1577    666       C  
ATOM   2459  C   LYS C 113     -15.639 -45.743 -29.886  1.00 41.33           C  
ANISOU 2459  C   LYS C 113     3398   4197   8109     46  -1556   1007       C  
ATOM   2460  O   LYS C 113     -15.443 -44.962 -30.819  1.00 43.05           O  
ANISOU 2460  O   LYS C 113     3809   4429   8120   -178  -1411    820       O  
ATOM   2461  CB  LYS C 113     -16.145 -48.087 -30.617  1.00 43.94           C  
ANISOU 2461  CB  LYS C 113     3670   4712   8313   -553  -1243    507       C  
ATOM   2462  CG  LYS C 113     -17.423 -48.269 -29.828  1.00 44.02           C  
ANISOU 2462  CG  LYS C 113     3435   4837   8454   -920  -1740    414       C  
ATOM   2463  CD  LYS C 113     -18.459 -49.051 -30.627  1.00 47.34           C  
ANISOU 2463  CD  LYS C 113     4183   4861   8942   -939  -1149    748       C  
ATOM   2464  CE  LYS C 113     -19.680 -49.354 -29.780  1.00 48.51           C  
ANISOU 2464  CE  LYS C 113     4554   4910   8968   -676  -1025   1063       C  
ATOM   2465  NZ  LYS C 113     -19.313 -50.170 -28.586  1.00 47.80           N  
ANISOU 2465  NZ  LYS C 113     4795   4638   8727   -388   -873   1739       N  
ATOM   2466  N   GLU C 114     -16.289 -45.390 -28.781  1.00 41.30           N  
ANISOU 2466  N   GLU C 114     3310   3974   8409     68  -1606   1475       N  
ATOM   2467  CA  GLU C 114     -16.825 -44.034 -28.622  1.00 42.49           C  
ANISOU 2467  CA  GLU C 114     3454   3996   8693    128  -1608   1284       C  
ATOM   2468  C   GLU C 114     -15.717 -42.985 -28.578  1.00 41.97           C  
ANISOU 2468  C   GLU C 114     3503   3887   8558    303  -1755   1627       C  
ATOM   2469  O   GLU C 114     -15.856 -41.894 -29.129  1.00 43.33           O  
ANISOU 2469  O   GLU C 114     3751   3667   9045    269  -1396   1560       O  
ATOM   2470  CB  GLU C 114     -17.679 -43.931 -27.356  1.00 47.17           C  
ANISOU 2470  CB  GLU C 114     3896   4686   9339    125  -1038    939       C  
ATOM   2471  CG  GLU C 114     -19.035 -44.613 -27.447  1.00 50.93           C  
ANISOU 2471  CG  GLU C 114     4158   5280   9914    207   -687    941       C  
ATOM   2472  CD  GLU C 114     -18.970 -46.100 -27.155  1.00 53.14           C  
ANISOU 2472  CD  GLU C 114     4062   5857  10271    127   -527   1026       C  
ATOM   2473  OE1 GLU C 114     -17.862 -46.603 -26.872  1.00 52.45           O  
ANISOU 2473  OE1 GLU C 114     3572   5947  10411    240   -712   1127       O  
ATOM   2474  OE2 GLU C 114     -20.031 -46.763 -27.204  1.00 53.98           O  
ANISOU 2474  OE2 GLU C 114     4055   6199  10256     67   -543    950       O  
ATOM   2475  N   LEU C 115     -14.621 -43.318 -27.909  1.00 40.80           N  
ANISOU 2475  N   LEU C 115     3479   3880   8143    232  -1754   1715       N  
ATOM   2476  CA  LEU C 115     -13.465 -42.434 -27.836  1.00 42.07           C  
ANISOU 2476  CA  LEU C 115     3701   4271   8011   -487  -1785   1121       C  
ATOM   2477  C   LEU C 115     -12.712 -42.422 -29.160  1.00 41.65           C  
ANISOU 2477  C   LEU C 115     3433   4364   8028   -874  -2089   1392       C  
ATOM   2478  O   LEU C 115     -12.266 -41.374 -29.621  1.00 42.54           O  
ANISOU 2478  O   LEU C 115     3390   4618   8155   -681  -2180   1895       O  
ATOM   2479  CB  LEU C 115     -12.535 -42.865 -26.706  1.00 42.56           C  
ANISOU 2479  CB  LEU C 115     3716   4597   7859   -493  -1473    614       C  
ATOM   2480  CG  LEU C 115     -11.273 -42.028 -26.539  1.00 44.80           C  
ANISOU 2480  CG  LEU C 115     3890   5259   7873   -349  -1119    510       C  
ATOM   2481  CD1 LEU C 115     -11.637 -40.566 -26.314  1.00 44.77           C  
ANISOU 2481  CD1 LEU C 115     3861   5359   7792   -611  -1144     78       C  
ATOM   2482  CD2 LEU C 115     -10.455 -42.569 -25.392  1.00 45.79           C  
ANISOU 2482  CD2 LEU C 115     3873   5703   7824     52   -889    540       C  
ATOM   2483  N   ALA C 116     -12.568 -43.600 -29.762  1.00 42.14           N  
ANISOU 2483  N   ALA C 116     3626   4405   7982   -869  -2046   1611       N  
ATOM   2484  CA  ALA C 116     -11.952 -43.720 -31.078  1.00 43.01           C  
ANISOU 2484  CA  ALA C 116     3957   4397   7986   -429  -2017   2140       C  
ATOM   2485  C   ALA C 116     -12.675 -42.844 -32.096  1.00 43.25           C  
ANISOU 2485  C   ALA C 116     3897   4538   7999   -289  -2250   2175       C  
ATOM   2486  O   ALA C 116     -12.047 -42.237 -32.961  1.00 43.20           O  
ANISOU 2486  O   ALA C 116     4013   4450   7952   -489  -2215   2086       O  
ATOM   2487  CB  ALA C 116     -11.951 -45.168 -31.533  1.00 44.86           C  
ANISOU 2487  CB  ALA C 116     4253   4604   8187   -197  -1676   2375       C  
ATOM   2488  N   GLY C 117     -13.999 -42.783 -31.980  1.00 44.72           N  
ANISOU 2488  N   GLY C 117     4018   4804   8171     56  -2191   2274       N  
ATOM   2489  CA  GLY C 117     -14.818 -41.984 -32.873  1.00 46.03           C  
ANISOU 2489  CA  GLY C 117     4384   5017   8086    -16  -2114   2391       C  
ATOM   2490  C   GLY C 117     -14.514 -40.499 -32.789  1.00 47.26           C  
ANISOU 2490  C   GLY C 117     4680   5440   7835   -236  -2284   2115       C  
ATOM   2491  O   GLY C 117     -14.813 -39.742 -33.712  1.00 49.06           O  
ANISOU 2491  O   GLY C 117     5016   5847   7777   -249  -2302   2003       O  
ATOM   2492  N   ALA C 118     -13.918 -40.078 -31.680  1.00 46.57           N  
ANISOU 2492  N   ALA C 118     4607   5452   7637   -191  -2495   2333       N  
ATOM   2493  CA  ALA C 118     -13.550 -38.677 -31.508  1.00 47.08           C  
ANISOU 2493  CA  ALA C 118     4927   5266   7694    -41  -2113   2540       C  
ATOM   2494  C   ALA C 118     -12.091 -38.442 -31.883  1.00 45.38           C  
ANISOU 2494  C   ALA C 118     4878   5014   7348   -221  -2366   2644       C  
ATOM   2495  O   ALA C 118     -11.759 -37.471 -32.567  1.00 44.93           O  
ANISOU 2495  O   ALA C 118     5007   4793   7270   -248  -2471   2561       O  
ATOM   2496  CB  ALA C 118     -13.802 -38.236 -30.076  1.00 48.34           C  
ANISOU 2496  CB  ALA C 118     5062   5387   7920    223  -1963   2543       C  
ATOM   2497  N   LEU C 119     -11.219 -39.341 -31.438  1.00 44.43           N  
ANISOU 2497  N   LEU C 119     4787   4926   7166   -229  -2246   2713       N  
ATOM   2498  CA  LEU C 119      -9.783 -39.145 -31.591  1.00 43.08           C  
ANISOU 2498  CA  LEU C 119     4811   4846   6712   -194  -2103   2683       C  
ATOM   2499  C   LEU C 119      -9.288 -39.401 -33.007  1.00 43.63           C  
ANISOU 2499  C   LEU C 119     5042   5275   6261   -445  -2351   2646       C  
ATOM   2500  O   LEU C 119      -8.225 -38.916 -33.384  1.00 44.09           O  
ANISOU 2500  O   LEU C 119     5131   5550   6071   -606  -2370   2712       O  
ATOM   2501  CB  LEU C 119      -9.014 -40.049 -30.627  1.00 40.86           C  
ANISOU 2501  CB  LEU C 119     4590   4529   6405      4  -1940   2475       C  
ATOM   2502  CG  LEU C 119      -9.278 -39.890 -29.132  1.00 40.44           C  
ANISOU 2502  CG  LEU C 119     4619   4302   6443     79  -1448   2603       C  
ATOM   2503  CD1 LEU C 119      -8.182 -40.585 -28.352  1.00 39.36           C  
ANISOU 2503  CD1 LEU C 119     4608   4238   6109    202  -1267   2620       C  
ATOM   2504  CD2 LEU C 119      -9.360 -38.435 -28.741  1.00 40.33           C  
ANISOU 2504  CD2 LEU C 119     4508   4207   6607    310  -1548   2333       C  
ATOM   2505  N   ALA C 120     -10.042 -40.182 -33.775  1.00 44.59           N  
ANISOU 2505  N   ALA C 120     5299   5581   6063   -473  -2370   2694       N  
ATOM   2506  CA  ALA C 120      -9.601 -40.592 -35.103  1.00 46.00           C  
ANISOU 2506  CA  ALA C 120     5518   5923   6036   -953  -2553   2740       C  
ATOM   2507  C   ALA C 120      -9.279 -39.380 -35.971  1.00 47.05           C  
ANISOU 2507  C   ALA C 120     5800   6090   5987  -1013  -2539   2891       C  
ATOM   2508  O   ALA C 120      -8.242 -39.343 -36.628  1.00 47.75           O  
ANISOU 2508  O   ALA C 120     5904   6287   5950   -992  -2395   3035       O  
ATOM   2509  CB  ALA C 120     -10.652 -41.462 -35.769  1.00 47.53           C  
ANISOU 2509  CB  ALA C 120     5812   6110   6139  -1038  -2188   2580       C  
ATOM   2510  N   TYR C 121     -10.163 -38.388 -35.942  1.00 48.44           N  
ANISOU 2510  N   TYR C 121     6116   5912   6378  -1125  -2297   3055       N  
ATOM   2511  CA  TYR C 121      -9.982 -37.150 -36.697  1.00 49.61           C  
ANISOU 2511  CA  TYR C 121     6118   5983   6748   -946  -2604   2951       C  
ATOM   2512  C   TYR C 121      -8.704 -36.419 -36.284  1.00 48.22           C  
ANISOU 2512  C   TYR C 121     5898   5838   6586   -952  -2643   2794       C  
ATOM   2513  O   TYR C 121      -7.956 -35.916 -37.126  1.00 48.20           O  
ANISOU 2513  O   TYR C 121     5865   5829   6622   -903  -2881   2781       O  
ATOM   2514  CB  TYR C 121     -11.194 -36.239 -36.501  1.00 51.55           C  
ANISOU 2514  CB  TYR C 121     6372   6227   6987   -650  -2782   3102       C  
ATOM   2515  CG  TYR C 121     -11.090 -34.902 -37.201  1.00 54.18           C  
ANISOU 2515  CG  TYR C 121     6761   6506   7320   -206  -2746   3199       C  
ATOM   2516  CD1 TYR C 121     -11.387 -34.781 -38.552  1.00 55.38           C  
ANISOU 2516  CD1 TYR C 121     7073   6622   7347   -188  -2519   3354       C  
ATOM   2517  CD2 TYR C 121     -10.704 -33.759 -36.509  1.00 54.48           C  
ANISOU 2517  CD2 TYR C 121     6804   6593   7304     54  -2765   3107       C  
ATOM   2518  CE1 TYR C 121     -11.296 -33.561 -39.197  1.00 55.39           C  
ANISOU 2518  CE1 TYR C 121     7174   6562   7311     19  -2421   3421       C  
ATOM   2519  CE2 TYR C 121     -10.610 -32.535 -37.145  1.00 54.58           C  
ANISOU 2519  CE2 TYR C 121     6996   6610   7133    210  -2567   3180       C  
ATOM   2520  CZ  TYR C 121     -10.908 -32.441 -38.489  1.00 55.77           C  
ANISOU 2520  CZ  TYR C 121     7257   6633   7298     87  -2386   3374       C  
ATOM   2521  OH  TYR C 121     -10.817 -31.221 -39.127  1.00 56.73           O  
ANISOU 2521  OH  TYR C 121     7454   6657   7445    198  -2153   3617       O  
ATOM   2522  N   ILE C 122      -8.463 -36.375 -34.978  1.00 44.85           N  
ANISOU 2522  N   ILE C 122     5423   5546   6073   -674  -2526   2652       N  
ATOM   2523  CA  ILE C 122      -7.321 -35.663 -34.426  1.00 43.37           C  
ANISOU 2523  CA  ILE C 122     5331   5293   5854   -943  -2142   2881       C  
ATOM   2524  C   ILE C 122      -6.000 -36.313 -34.833  1.00 43.28           C  
ANISOU 2524  C   ILE C 122     5587   5417   5441   -982  -2057   2818       C  
ATOM   2525  O   ILE C 122      -5.046 -35.620 -35.192  1.00 43.60           O  
ANISOU 2525  O   ILE C 122     5734   5603   5228   -762  -2126   2681       O  
ATOM   2526  CB  ILE C 122      -7.429 -35.587 -32.891  1.00 43.95           C  
ANISOU 2526  CB  ILE C 122     4971   5165   6563   -791  -1960   2901       C  
ATOM   2527  CG1 ILE C 122      -8.537 -34.600 -32.508  1.00 44.01           C  
ANISOU 2527  CG1 ILE C 122     4816   5085   6822   -454  -1881   3059       C  
ATOM   2528  CG2 ILE C 122      -6.095 -35.195 -32.261  1.00 41.29           C  
ANISOU 2528  CG2 ILE C 122     4354   4669   6664  -1243  -1971   3013       C  
ATOM   2529  CD1 ILE C 122      -9.008 -34.726 -31.077  1.00 42.55           C  
ANISOU 2529  CD1 ILE C 122     4483   5061   6624   -765  -1804   3119       C  
ATOM   2530  N   MET C 123      -5.945 -37.641 -34.782  1.00 42.64           N  
ANISOU 2530  N   MET C 123     5657   5492   5052  -1002  -1926   2742       N  
ATOM   2531  CA  MET C 123      -4.747 -38.360 -35.206  1.00 41.17           C  
ANISOU 2531  CA  MET C 123     5424   5333   4888  -1230  -1644   2777       C  
ATOM   2532  C   MET C 123      -4.551 -38.256 -36.719  1.00 43.96           C  
ANISOU 2532  C   MET C 123     5779   5991   4934  -1470  -2048   2667       C  
ATOM   2533  O   MET C 123      -3.461 -37.927 -37.183  1.00 44.00           O  
ANISOU 2533  O   MET C 123     5849   6096   4772  -1457  -1744   2851       O  
ATOM   2534  CB  MET C 123      -4.814 -39.830 -34.776  1.00 38.55           C  
ANISOU 2534  CB  MET C 123     5021   5026   4601   -813  -1753   2483       C  
ATOM   2535  CG  MET C 123      -4.870 -40.017 -33.273  1.00 37.61           C  
ANISOU 2535  CG  MET C 123     4928   4761   4601  -1153  -1577   2442       C  
ATOM   2536  SD  MET C 123      -4.779 -41.758 -32.828  1.00 37.07           S  
ANISOU 2536  SD  MET C 123     4841   4804   4440  -1346  -1809   2228       S  
ATOM   2537  CE  MET C 123      -3.038 -42.099 -33.084  1.00 36.68           C  
ANISOU 2537  CE  MET C 123     4635   4976   4325  -1365  -2118   1997       C  
ATOM   2538  N   ASP C 124      -5.613 -38.523 -37.479  1.00 44.94           N  
ANISOU 2538  N   ASP C 124     6061   6059   4955  -1483  -2309   2635       N  
ATOM   2539  CA  ASP C 124      -5.527 -38.533 -38.937  1.00 48.45           C  
ANISOU 2539  CA  ASP C 124     6587   6557   5263  -1802  -2208   2689       C  
ATOM   2540  C   ASP C 124      -5.058 -37.189 -39.500  1.00 51.28           C  
ANISOU 2540  C   ASP C 124     7059   6797   5629  -1548  -2085   2883       C  
ATOM   2541  O   ASP C 124      -4.335 -37.148 -40.496  1.00 53.78           O  
ANISOU 2541  O   ASP C 124     7358   7146   5928  -1617  -2024   2804       O  
ATOM   2542  CB  ASP C 124      -6.877 -38.915 -39.556  1.00 48.99           C  
ANISOU 2542  CB  ASP C 124     6618   6727   5270  -2031  -2439   2913       C  
ATOM   2543  CG  ASP C 124      -7.249 -40.372 -39.308  1.00 51.08           C  
ANISOU 2543  CG  ASP C 124     6759   6954   5696  -2227  -2287   2967       C  
ATOM   2544  OD1 ASP C 124      -6.423 -41.117 -38.736  1.00 50.25           O  
ANISOU 2544  OD1 ASP C 124     6540   6835   5716  -2264  -2620   3116       O  
ATOM   2545  OD2 ASP C 124      -8.367 -40.778 -39.697  1.00 51.06           O  
ANISOU 2545  OD2 ASP C 124     6860   6811   5730  -2634  -2100   2942       O  
ATOM   2546  N   ASN C 125      -5.459 -36.096 -38.858  1.00 49.56           N  
ANISOU 2546  N   ASN C 125     6894   6505   5432  -1514  -2448   2910       N  
ATOM   2547  CA  ASN C 125      -5.099 -34.763 -39.337  1.00 49.56           C  
ANISOU 2547  CA  ASN C 125     6878   6474   5480  -1436  -2619   2804       C  
ATOM   2548  C   ASN C 125      -3.958 -34.137 -38.542  1.00 50.57           C  
ANISOU 2548  C   ASN C 125     7126   6597   5494  -1389  -2184   2853       C  
ATOM   2549  O   ASN C 125      -3.678 -32.945 -38.681  1.00 51.50           O  
ANISOU 2549  O   ASN C 125     7360   6562   5646  -1373  -2059   3109       O  
ATOM   2550  CB  ASN C 125      -6.317 -33.846 -39.307  1.00 51.17           C  
ANISOU 2550  CB  ASN C 125     7223   6411   5807  -1187  -2342   3110       C  
ATOM   2551  CG  ASN C 125      -7.412 -34.310 -40.247  1.00 54.11           C  
ANISOU 2551  CG  ASN C 125     7689   6678   6191  -1060  -2359   3198       C  
ATOM   2552  OD1 ASN C 125      -8.402 -34.907 -39.821  1.00 55.90           O  
ANISOU 2552  OD1 ASN C 125     7915   6821   6503   -990  -2601   2972       O  
ATOM   2553  ND2 ASN C 125      -7.231 -34.053 -41.536  1.00 55.12           N  
ANISOU 2553  ND2 ASN C 125     7980   6782   6181   -964  -2168   3179       N  
ATOM   2554  N   LYS C 126      -3.313 -34.949 -37.709  1.00 48.79           N  
ANISOU 2554  N   LYS C 126     6905   6745   4886  -1217  -2204   2734       N  
ATOM   2555  CA  LYS C 126      -2.111 -34.538 -36.986  1.00 50.53           C  
ANISOU 2555  CA  LYS C 126     7066   6793   5341  -1024  -1358   2580       C  
ATOM   2556  C   LYS C 126      -2.306 -33.249 -36.192  1.00 48.58           C  
ANISOU 2556  C   LYS C 126     6567   6428   5462   -829  -1606   2948       C  
ATOM   2557  O   LYS C 126      -1.436 -32.379 -36.178  1.00 50.81           O  
ANISOU 2557  O   LYS C 126     6858   6554   5894   -987  -1254   2950       O  
ATOM   2558  CB  LYS C 126      -0.946 -34.378 -37.966  1.00 53.75           C  
ANISOU 2558  CB  LYS C 126     7730   7049   5645   -854   -255   2504       C  
ATOM   2559  CG  LYS C 126      -0.612 -35.660 -38.713  1.00 57.12           C  
ANISOU 2559  CG  LYS C 126     8285   7455   5962   -495    393   2356       C  
ATOM   2560  CD  LYS C 126       0.011 -35.374 -40.068  1.00 59.77           C  
ANISOU 2560  CD  LYS C 126     8764   7704   6240    -88    653   2257       C  
ATOM   2561  CE  LYS C 126       0.172 -36.654 -40.875  1.00 61.34           C  
ANISOU 2561  CE  LYS C 126     9095   7789   6423    181   1002   2290       C  
ATOM   2562  NZ  LYS C 126       0.734 -36.389 -42.229  1.00 62.51           N  
ANISOU 2562  NZ  LYS C 126     9213   8002   6535    340   1195   2125       N  
ATOM   2563  N   LEU C 127      -3.452 -33.132 -35.533  1.00 45.31           N  
ANISOU 2563  N   LEU C 127     5828   5979   5411   -684  -1960   2887       N  
ATOM   2564  CA  LEU C 127      -3.749 -31.949 -34.737  1.00 43.82           C  
ANISOU 2564  CA  LEU C 127     5313   5522   5815   -335  -1651   2910       C  
ATOM   2565  C   LEU C 127      -3.089 -32.024 -33.367  1.00 40.00           C  
ANISOU 2565  C   LEU C 127     4679   4767   5754    -80  -1556   2714       C  
ATOM   2566  O   LEU C 127      -2.836 -31.001 -32.734  1.00 39.97           O  
ANISOU 2566  O   LEU C 127     4571   4619   5999   -209  -1792   2621       O  
ATOM   2567  CB  LEU C 127      -5.258 -31.773 -34.581  1.00 44.66           C  
ANISOU 2567  CB  LEU C 127     5164   5765   6039   -122  -1903   2939       C  
ATOM   2568  CG  LEU C 127      -6.035 -31.543 -35.875  1.00 46.88           C  
ANISOU 2568  CG  LEU C 127     5616   5852   6346     -9  -1552   3225       C  
ATOM   2569  CD1 LEU C 127      -7.512 -31.348 -35.579  1.00 48.85           C  
ANISOU 2569  CD1 LEU C 127     5881   6052   6629     51  -1218   3124       C  
ATOM   2570  CD2 LEU C 127      -5.464 -30.346 -36.614  1.00 47.68           C  
ANISOU 2570  CD2 LEU C 127     5819   5804   6491    193  -1509   3282       C  
ATOM   2571  N   ALA C 128      -2.823 -33.245 -32.909  1.00 35.77           N  
ANISOU 2571  N   ALA C 128     4151   4274   5165    146  -1289   2403       N  
ATOM   2572  CA  ALA C 128      -2.137 -33.456 -31.646  1.00 34.19           C  
ANISOU 2572  CA  ALA C 128     3896   4040   5055    501   -752   2243       C  
ATOM   2573  C   ALA C 128      -1.479 -34.811 -31.635  1.00 30.87           C  
ANISOU 2573  C   ALA C 128     3869   3486   4374     52   -885   2002       C  
ATOM   2574  O   ALA C 128      -1.935 -35.738 -32.303  1.00 33.49           O  
ANISOU 2574  O   ALA C 128     4226   3963   4536     59   -784   1768       O  
ATOM   2575  CB  ALA C 128      -3.104 -33.347 -30.470  1.00 33.23           C  
ANISOU 2575  CB  ALA C 128     3783   4156   4685    623   -543   2367       C  
ATOM   2576  N   GLN C 129      -0.393 -34.910 -30.878  1.00 26.77           N  
ANISOU 2576  N   GLN C 129     3468   2841   3861    228   -958   1655       N  
ATOM   2577  CA AGLN C 129       0.191 -36.204 -30.578  0.56 26.97           C  
ANISOU 2577  CA AGLN C 129     3645   2910   3693     41   -698   1496       C  
ATOM   2578  CA BGLN C 129       0.223 -36.186 -30.562  0.44 27.69           C  
ANISOU 2578  CA BGLN C 129     3719   2920   3880    -11   -405   1422       C  
ATOM   2579  C   GLN C 129      -0.317 -36.614 -29.207  1.00 25.94           C  
ANISOU 2579  C   GLN C 129     3675   2737   3444     13   -397   1295       C  
ATOM   2580  O   GLN C 129      -0.424 -35.788 -28.297  1.00 26.63           O  
ANISOU 2580  O   GLN C 129     4157   2802   3160    111   -283   1222       O  
ATOM   2581  CB AGLN C 129       1.717 -36.157 -30.624  0.56 26.16           C  
ANISOU 2581  CB AGLN C 129     3455   2925   3561     -1  -1135   1600       C  
ATOM   2582  CB BGLN C 129       1.749 -36.077 -30.544  0.44 29.07           C  
ANISOU 2582  CB BGLN C 129     3787   3025   4232   -226    -98   1304       C  
ATOM   2583  CG AGLN C 129       2.286 -35.708 -31.968  0.56 29.43           C  
ANISOU 2583  CG AGLN C 129     4038   3151   3993   -186   -609   1515       C  
ATOM   2584  CG BGLN C 129       2.373 -35.725 -31.894  0.44 32.46           C  
ANISOU 2584  CG BGLN C 129     4226   3312   4795   -362    504   1137       C  
ATOM   2585  CD AGLN C 129       1.691 -36.447 -33.159  0.56 32.76           C  
ANISOU 2585  CD AGLN C 129     4631   3353   4462    -86     19   1511       C  
ATOM   2586  CD BGLN C 129       2.195 -34.262 -32.275  0.44 35.81           C  
ANISOU 2586  CD BGLN C 129     4585   3560   5462   -321   1142   1015       C  
ATOM   2587  OE1AGLN C 129       1.665 -37.681 -33.198  0.56 33.20           O  
ANISOU 2587  OE1AGLN C 129     4434   3530   4650   -167   -185   1050       O  
ATOM   2588  OE1BGLN C 129       2.535 -33.359 -31.506  0.44 37.44           O  
ANISOU 2588  OE1BGLN C 129     4706   3488   6031   -256   1671    973       O  
ATOM   2589  NE2AGLN C 129       1.212 -35.689 -34.142  0.56 34.19           N  
ANISOU 2589  NE2AGLN C 129     4896   3469   4628    180    341   1582       N  
ATOM   2590  NE2BGLN C 129       1.658 -34.023 -33.466  0.44 37.61           N  
ANISOU 2590  NE2BGLN C 129     4737   3807   5746   -428   1400    863       N  
ATOM   2591  N   ILE C 130      -0.656 -37.888 -29.074  1.00 22.45           N  
ANISOU 2591  N   ILE C 130     3323   2152   3056    206   -257   1097       N  
ATOM   2592  CA  ILE C 130      -1.314 -38.367 -27.873  1.00 21.65           C  
ANISOU 2592  CA  ILE C 130     3111   2065   3052    -64   -226    953       C  
ATOM   2593  C   ILE C 130      -0.477 -39.446 -27.202  1.00 21.57           C  
ANISOU 2593  C   ILE C 130     3581   1621   2994     57   -305    672       C  
ATOM   2594  O   ILE C 130      -0.244 -40.500 -27.793  1.00 26.75           O  
ANISOU 2594  O   ILE C 130     4548   2160   3454     95   -257    594       O  
ATOM   2595  CB  ILE C 130      -2.712 -38.931 -28.203  1.00 23.99           C  
ANISOU 2595  CB  ILE C 130     3102   2394   3617    229    -35   1040       C  
ATOM   2596  CG1 ILE C 130      -3.513 -37.920 -29.031  1.00 26.56           C  
ANISOU 2596  CG1 ILE C 130     3044   3142   3907    -18   -347    910       C  
ATOM   2597  CG2 ILE C 130      -3.446 -39.312 -26.927  1.00 24.68           C  
ANISOU 2597  CG2 ILE C 130     3192   2278   3907    -24    453    610       C  
ATOM   2598  CD1 ILE C 130      -4.817 -38.470 -29.568  1.00 29.14           C  
ANISOU 2598  CD1 ILE C 130     3409   3524   4138    129   -292   1089       C  
ATOM   2599  N   GLU C 131      -0.022 -39.185 -25.976  1.00 22.16           N  
ANISOU 2599  N   GLU C 131     3198   2035   3187    347    130    701       N  
ATOM   2600  CA  GLU C 131       0.752 -40.170 -25.225  1.00 21.33           C  
ANISOU 2600  CA  GLU C 131     3112   1932   3059    686    125    720       C  
ATOM   2601  C   GLU C 131      -0.168 -40.911 -24.272  1.00 19.37           C  
ANISOU 2601  C   GLU C 131     2654   1808   2898    533    472    903       C  
ATOM   2602  O   GLU C 131      -0.916 -40.292 -23.523  1.00 24.68           O  
ANISOU 2602  O   GLU C 131     3318   2042   4018    604   1371    894       O  
ATOM   2603  CB  GLU C 131       1.899 -39.528 -24.428  1.00 24.84           C  
ANISOU 2603  CB  GLU C 131     3304   2254   3879    544    -74    577       C  
ATOM   2604  CG  GLU C 131       2.652 -40.545 -23.542  1.00 29.53           C  
ANISOU 2604  CG  GLU C 131     4114   2661   4447    392   -750    268       C  
ATOM   2605  CD  GLU C 131       3.681 -39.919 -22.591  1.00 34.85           C  
ANISOU 2605  CD  GLU C 131     5048   2786   5407    581   -544    617       C  
ATOM   2606  OE1 GLU C 131       3.278 -39.203 -21.642  1.00 41.01           O  
ANISOU 2606  OE1 GLU C 131     6331   3352   5898    833   -727    453       O  
ATOM   2607  OE2 GLU C 131       4.892 -40.162 -22.780  1.00 31.76           O  
ANISOU 2607  OE2 GLU C 131     4362   2406   5299   -206   -600    554       O  
ATOM   2608  N   GLY C 132      -0.112 -42.239 -24.298  1.00 17.03           N  
ANISOU 2608  N   GLY C 132     2429   1443   2597    320   -195    596       N  
ATOM   2609  CA  GLY C 132      -0.914 -43.039 -23.396  1.00 17.59           C  
ANISOU 2609  CA  GLY C 132     2739   1802   2142    400   -102    577       C  
ATOM   2610  C   GLY C 132      -0.077 -43.635 -22.277  1.00 16.16           C  
ANISOU 2610  C   GLY C 132     2682   1584   1876    104   -193    330       C  
ATOM   2611  O   GLY C 132       1.072 -44.028 -22.498  1.00 16.70           O  
ANISOU 2611  O   GLY C 132     2834   1657   1854    666    172     75       O  
ATOM   2612  N   VAL C 133      -0.641 -43.669 -21.070  1.00 15.39           N  
ANISOU 2612  N   VAL C 133     2491   1305   2052    172   -160    432       N  
ATOM   2613  CA  VAL C 133      -0.026 -44.353 -19.934  1.00 15.04           C  
ANISOU 2613  CA  VAL C 133     2418   1214   2082   -155     65     98       C  
ATOM   2614  C   VAL C 133      -1.111 -45.155 -19.222  1.00 13.23           C  
ANISOU 2614  C   VAL C 133     2089   1033   1903    283     31    136       C  
ATOM   2615  O   VAL C 133      -2.236 -44.675 -19.075  1.00 17.99           O  
ANISOU 2615  O   VAL C 133     2443   1648   2744    680    496    273       O  
ATOM   2616  CB  VAL C 133       0.622 -43.361 -18.942  1.00 16.88           C  
ANISOU 2616  CB  VAL C 133     2664   1894   1855    -93    228    228       C  
ATOM   2617  CG1 VAL C 133       1.158 -44.077 -17.714  1.00 18.68           C  
ANISOU 2617  CG1 VAL C 133     2992   1921   2185    155    169    230       C  
ATOM   2618  CG2 VAL C 133       1.697 -42.529 -19.624  1.00 18.81           C  
ANISOU 2618  CG2 VAL C 133     2915   1904   2329     41    480     52       C  
ATOM   2619  N   VAL C 134      -0.796 -46.379 -18.806  1.00 13.80           N  
ANISOU 2619  N   VAL C 134     2264   1192   1789     87    148    253       N  
ATOM   2620  CA  VAL C 134      -1.738 -47.162 -18.011  1.00 15.08           C  
ANISOU 2620  CA  VAL C 134     2514   1300   1914     48    148    -62       C  
ATOM   2621  C   VAL C 134      -1.388 -46.958 -16.548  1.00 16.62           C  
ANISOU 2621  C   VAL C 134     2613   1515   2188    -92    212    125       C  
ATOM   2622  O   VAL C 134      -0.317 -47.359 -16.111  1.00 18.63           O  
ANISOU 2622  O   VAL C 134     2685   1919   2475    176     27    115       O  
ATOM   2623  CB  VAL C 134      -1.691 -48.662 -18.363  1.00 15.74           C  
ANISOU 2623  CB  VAL C 134     2353   1500   2127    -43    -72     74       C  
ATOM   2624  CG1 VAL C 134      -2.543 -49.448 -17.388  1.00 16.06           C  
ANISOU 2624  CG1 VAL C 134     2254   1572   2275   -105    441    157       C  
ATOM   2625  CG2 VAL C 134      -2.175 -48.872 -19.788  1.00 17.98           C  
ANISOU 2625  CG2 VAL C 134     2947   1714   2169   -232     47   -156       C  
ATOM   2626  N   PRO C 135      -2.278 -46.314 -15.787  1.00 16.36           N  
ANISOU 2626  N   PRO C 135     2791   1586   1840    -37    -77     44       N  
ATOM   2627  CA  PRO C 135      -1.913 -45.996 -14.405  1.00 18.75           C  
ANISOU 2627  CA  PRO C 135     3499   1886   1741   -147    190   -174       C  
ATOM   2628  C   PRO C 135      -2.121 -47.161 -13.449  1.00 17.47           C  
ANISOU 2628  C   PRO C 135     3041   2210   1387   -357   -301     31       C  
ATOM   2629  O   PRO C 135      -1.308 -47.369 -12.531  1.00 20.33           O  
ANISOU 2629  O   PRO C 135     2847   2878   2001   -458   -184    109       O  
ATOM   2630  CB  PRO C 135      -2.850 -44.838 -14.058  1.00 20.56           C  
ANISOU 2630  CB  PRO C 135     3805   1886   2121    -63    405   -472       C  
ATOM   2631  CG  PRO C 135      -4.071 -45.071 -14.917  1.00 20.98           C  
ANISOU 2631  CG  PRO C 135     3447   2095   2430    312    187   -262       C  
ATOM   2632  CD  PRO C 135      -3.504 -45.618 -16.219  1.00 18.19           C  
ANISOU 2632  CD  PRO C 135     2733   1876   2301    159    220   -401       C  
ATOM   2633  N   PHE C 136      -3.206 -47.901 -13.661  1.00 16.58           N  
ANISOU 2633  N   PHE C 136     2548   1672   2081   -213     -6   -149       N  
ATOM   2634  CA  PHE C 136      -3.598 -49.004 -12.793  1.00 15.54           C  
ANISOU 2634  CA  PHE C 136     2390   1625   1888    -35    369   -224       C  
ATOM   2635  C   PHE C 136      -4.326 -50.039 -13.617  1.00 16.21           C  
ANISOU 2635  C   PHE C 136     2332   1861   1964   -194    259   -288       C  
ATOM   2636  O   PHE C 136      -4.648 -49.790 -14.776  1.00 18.12           O  
ANISOU 2636  O   PHE C 136     2455   2191   2240   -383    194     34       O  
ATOM   2637  CB  PHE C 136      -4.505 -48.528 -11.661  1.00 16.89           C  
ANISOU 2637  CB  PHE C 136     2347   1949   2123    152    142   -438       C  
ATOM   2638  CG  PHE C 136      -3.860 -47.537 -10.749  1.00 19.75           C  
ANISOU 2638  CG  PHE C 136     2623   2430   2452    184    433   -494       C  
ATOM   2639  CD1 PHE C 136      -2.787 -47.910  -9.949  1.00 21.60           C  
ANISOU 2639  CD1 PHE C 136     2606   2858   2744     27    233   -256       C  
ATOM   2640  CD2 PHE C 136      -4.324 -46.237 -10.681  1.00 22.66           C  
ANISOU 2640  CD2 PHE C 136     3370   2190   3049    125   1010   -990       C  
ATOM   2641  CE1 PHE C 136      -2.180 -46.999  -9.103  1.00 23.80           C  
ANISOU 2641  CE1 PHE C 136     3398   2609   3036    -13    750   -670       C  
ATOM   2642  CE2 PHE C 136      -3.727 -45.319  -9.824  1.00 25.00           C  
ANISOU 2642  CE2 PHE C 136     3782   2489   3227    303    394   -893       C  
ATOM   2643  CZ  PHE C 136      -2.653 -45.702  -9.038  1.00 24.36           C  
ANISOU 2643  CZ  PHE C 136     3604   2441   3212    393    384   -523       C  
ATOM   2644  N   GLY C 137      -4.600 -51.196 -13.023  1.00 16.93           N  
ANISOU 2644  N   GLY C 137     2197   1700   2537   -428    609   -193       N  
ATOM   2645  CA  GLY C 137      -5.429 -52.191 -13.683  1.00 17.55           C  
ANISOU 2645  CA  GLY C 137     2277   1725   2666   -356    410    -76       C  
ATOM   2646  C   GLY C 137      -4.790 -52.881 -14.878  1.00 16.66           C  
ANISOU 2646  C   GLY C 137     2180   1896   2253   -152     72    -20       C  
ATOM   2647  O   GLY C 137      -5.496 -53.469 -15.706  1.00 16.56           O  
ANISOU 2647  O   GLY C 137     2133   1965   2193    -90   -176    -56       O  
ATOM   2648  N   ALA C 138      -3.463 -52.832 -14.980  1.00 14.98           N  
ANISOU 2648  N   ALA C 138     1975   1776   1938     48     52     70       N  
ATOM   2649  CA  ALA C 138      -2.806 -53.389 -16.163  1.00 14.72           C  
ANISOU 2649  CA  ALA C 138     1937   1659   1997    -28    153   -535       C  
ATOM   2650  C   ALA C 138      -2.971 -54.905 -16.278  1.00 15.79           C  
ANISOU 2650  C   ALA C 138     2165   1488   2348   -337   -158   -215       C  
ATOM   2651  O   ALA C 138      -2.712 -55.460 -17.340  1.00 17.43           O  
ANISOU 2651  O   ALA C 138     2582   1663   2377    -13    -61   -278       O  
ATOM   2652  CB  ALA C 138      -1.326 -53.033 -16.184  1.00 14.64           C  
ANISOU 2652  CB  ALA C 138     1885   1964   1712   -253    268   -135       C  
ATOM   2653  N   ASN C 139      -3.372 -55.569 -15.196  1.00 16.40           N  
ANISOU 2653  N   ASN C 139     2298   1425   2506   -366   -541    205       N  
ATOM   2654  CA  ASN C 139      -3.621 -57.017 -15.235  1.00 18.48           C  
ANISOU 2654  CA  ASN C 139     2376   1619   3026   -522   -873    660       C  
ATOM   2655  C   ASN C 139      -5.106 -57.362 -15.389  1.00 19.24           C  
ANISOU 2655  C   ASN C 139     2383   2022   2906   -607   -391    345       C  
ATOM   2656  O   ASN C 139      -5.500 -58.532 -15.281  1.00 20.69           O  
ANISOU 2656  O   ASN C 139     2781   1950   3129   -459   -623    540       O  
ATOM   2657  CB  ASN C 139      -3.070 -57.695 -13.972  1.00 22.08           C  
ANISOU 2657  CB  ASN C 139     3245   1681   3463   -579  -1561    720       C  
ATOM   2658  CG  ASN C 139      -3.026 -59.204 -14.097  1.00 25.89           C  
ANISOU 2658  CG  ASN C 139     3745   2317   3774   -632  -1567    899       C  
ATOM   2659  OD1 ASN C 139      -2.541 -59.730 -15.092  1.00 27.41           O  
ANISOU 2659  OD1 ASN C 139     3420   2030   4966   -175   -872    149       O  
ATOM   2660  ND2 ASN C 139      -3.574 -59.906 -13.102  1.00 30.27           N  
ANISOU 2660  ND2 ASN C 139     4713   2828   3960  -1011  -1456   1177       N  
ATOM   2661  N   ASN C 140      -5.933 -56.355 -15.652  1.00 18.87           N  
ANISOU 2661  N   ASN C 140     2148   2379   2642   -416      2     61       N  
ATOM   2662  CA  ASN C 140      -7.369 -56.585 -15.792  1.00 18.42           C  
ANISOU 2662  CA  ASN C 140     2025   2409   2566   -531   -147    219       C  
ATOM   2663  C   ASN C 140      -7.705 -57.507 -16.955  1.00 16.95           C  
ANISOU 2663  C   ASN C 140     1639   2057   2746   -405   -160    113       C  
ATOM   2664  O   ASN C 140      -7.008 -57.525 -17.962  1.00 18.84           O  
ANISOU 2664  O   ASN C 140     2068   2262   2828   -513    -20    -38       O  
ATOM   2665  CB  ASN C 140      -8.112 -55.274 -15.972  1.00 16.87           C  
ANISOU 2665  CB  ASN C 140     1869   2195   2347     16    -90   -255       C  
ATOM   2666  CG  ASN C 140      -8.188 -54.452 -14.696  1.00 20.74           C  
ANISOU 2666  CG  ASN C 140     2472   2855   2552   -439    356    146       C  
ATOM   2667  OD1 ASN C 140      -7.733 -54.873 -13.628  1.00 23.59           O  
ANISOU 2667  OD1 ASN C 140     3139   3306   2516   -603    349    130       O  
ATOM   2668  ND2 ASN C 140      -8.758 -53.264 -14.807  1.00 21.99           N  
ANISOU 2668  ND2 ASN C 140     2041   3014   3300   -362    389    271       N  
ATOM   2669  N   ALA C 141      -8.785 -58.267 -16.820  1.00 18.93           N  
ANISOU 2669  N   ALA C 141     1816   2229   3145   -653   -265    189       N  
ATOM   2670  CA  ALA C 141      -9.128 -59.251 -17.833  1.00 17.86           C  
ANISOU 2670  CA  ALA C 141     1731   1759   3297   -513   -514     61       C  
ATOM   2671  C   ALA C 141      -9.767 -58.650 -19.089  1.00 16.77           C  
ANISOU 2671  C   ALA C 141     1992   1611   2770   -291   -349    150       C  
ATOM   2672  O   ALA C 141      -9.574 -59.182 -20.186  1.00 20.67           O  
ANISOU 2672  O   ALA C 141     2565   2264   3023    -42   -208    -71       O  
ATOM   2673  CB  ALA C 141     -10.059 -60.314 -17.240  1.00 20.82           C  
ANISOU 2673  CB  ALA C 141     2218   2205   3488   -669   -241    475       C  
ATOM   2674  N   PHE C 142     -10.514 -57.551 -18.953  1.00 17.98           N  
ANISOU 2674  N   PHE C 142     1712   1910   3209   -160   -167    180       N  
ATOM   2675  CA  PHE C 142     -11.365 -57.113 -20.070  1.00 18.23           C  
ANISOU 2675  CA  PHE C 142     1472   2191   3262   -227    -80    459       C  
ATOM   2676  C   PHE C 142     -11.153 -55.675 -20.489  1.00 20.02           C  
ANISOU 2676  C   PHE C 142     2054   2454   3100   -170     24    170       C  
ATOM   2677  O   PHE C 142     -11.175 -55.381 -21.677  1.00 19.80           O  
ANISOU 2677  O   PHE C 142     2175   2658   2690   -193    -45    290       O  
ATOM   2678  CB  PHE C 142     -12.850 -57.332 -19.731  1.00 18.47           C  
ANISOU 2678  CB  PHE C 142     1354   2332   3330   -317   -125    267       C  
ATOM   2679  CG  PHE C 142     -13.161 -58.741 -19.379  1.00 20.08           C  
ANISOU 2679  CG  PHE C 142     1295   2576   3757   -174    206    393       C  
ATOM   2680  CD1 PHE C 142     -12.987 -59.744 -20.318  1.00 21.87           C  
ANISOU 2680  CD1 PHE C 142     1748   2228   4332    -56    262    485       C  
ATOM   2681  CD2 PHE C 142     -13.575 -59.080 -18.109  1.00 21.96           C  
ANISOU 2681  CD2 PHE C 142     1225   2975   4146   -222    177    405       C  
ATOM   2682  CE1 PHE C 142     -13.240 -61.059 -19.999  1.00 23.84           C  
ANISOU 2682  CE1 PHE C 142     1795   2258   5004   -230    542    263       C  
ATOM   2683  CE2 PHE C 142     -13.844 -60.395 -17.793  1.00 23.81           C  
ANISOU 2683  CE2 PHE C 142     1941   2972   4133   -239    253    222       C  
ATOM   2684  CZ  PHE C 142     -13.667 -61.381 -18.738  1.00 23.72           C  
ANISOU 2684  CZ  PHE C 142     1659   2691   4662   -407     32    288       C  
ATOM   2685  N   THR C 143     -10.975 -54.780 -19.518  1.00 20.17           N  
ANISOU 2685  N   THR C 143     2045   2244   3375   -103    -42    238       N  
ATOM   2686  CA  THR C 143     -10.712 -53.374 -19.805  1.00 19.90           C  
ANISOU 2686  CA  THR C 143     1976   2312   3273   -107   -171     49       C  
ATOM   2687  C   THR C 143      -9.719 -52.832 -18.791  1.00 20.30           C  
ANISOU 2687  C   THR C 143     2195   2327   3190      7    476    -31       C  
ATOM   2688  O   THR C 143      -9.659 -53.331 -17.669  1.00 20.89           O  
ANISOU 2688  O   THR C 143     2450   2376   3113    -32    269    121       O  
ATOM   2689  CB  THR C 143     -11.986 -52.508 -19.752  1.00 24.02           C  
ANISOU 2689  CB  THR C 143     1941   3383   3805     92    204    271       C  
ATOM   2690  OG1 THR C 143     -12.403 -52.342 -18.389  1.00 29.39           O  
ANISOU 2690  OG1 THR C 143     2775   3863   4528    395    504     82       O  
ATOM   2691  CG2 THR C 143     -13.122 -53.113 -20.573  1.00 23.90           C  
ANISOU 2691  CG2 THR C 143     1969   3240   3871    408     76    336       C  
ATOM   2692  N   MET C 144      -8.941 -51.821 -19.180  1.00 18.49           N  
ANISOU 2692  N   MET C 144     2491   1791   2744    -58    305   -215       N  
ATOM   2693  CA  MET C 144      -8.047 -51.160 -18.235  1.00 18.14           C  
ANISOU 2693  CA  MET C 144     2261   1817   2814    117     89    158       C  
ATOM   2694  C   MET C 144      -8.067 -49.657 -18.466  1.00 19.23           C  
ANISOU 2694  C   MET C 144     2374   2092   2840    197    236    195       C  
ATOM   2695  O   MET C 144      -8.306 -49.191 -19.591  1.00 19.58           O  
ANISOU 2695  O   MET C 144     2512   2047   2882    238    105     30       O  
ATOM   2696  CB  MET C 144      -6.609 -51.698 -18.339  1.00 19.46           C  
ANISOU 2696  CB  MET C 144     2325   2373   2694    354    157     -5       C  
ATOM   2697  CG  MET C 144      -5.909 -51.415 -19.658  1.00 20.04           C  
ANISOU 2697  CG  MET C 144     2421   2515   2678    271    469    272       C  
ATOM   2698  SD  MET C 144      -4.181 -51.985 -19.700  1.00 19.17           S  
ANISOU 2698  SD  MET C 144     2523   2071   2688     65   -169   -148       S  
ATOM   2699  CE  MET C 144      -4.362 -53.761 -19.680  1.00 20.17           C  
ANISOU 2699  CE  MET C 144     2526   1954   3186   -486   -265    251       C  
ATOM   2700  N   PRO C 145      -7.831 -48.888 -17.397  1.00 18.29           N  
ANISOU 2700  N   PRO C 145     2411   2200   2337    -32    360    112       N  
ATOM   2701  CA  PRO C 145      -7.837 -47.433 -17.568  1.00 19.53           C  
ANISOU 2701  CA  PRO C 145     2521   2220   2678    102    678    -69       C  
ATOM   2702  C   PRO C 145      -6.633 -46.953 -18.365  1.00 18.03           C  
ANISOU 2702  C   PRO C 145     2140   2085   2626    269    104     12       C  
ATOM   2703  O   PRO C 145      -5.569 -47.580 -18.395  1.00 19.04           O  
ANISOU 2703  O   PRO C 145     2443   2155   2634    204    325    198       O  
ATOM   2704  CB  PRO C 145      -7.795 -46.898 -16.133  1.00 22.39           C  
ANISOU 2704  CB  PRO C 145     3137   2512   2858     80    636   -179       C  
ATOM   2705  CG  PRO C 145      -7.165 -48.003 -15.344  1.00 23.16           C  
ANISOU 2705  CG  PRO C 145     3811   2296   2693    676    688   -120       C  
ATOM   2706  CD  PRO C 145      -7.585 -49.296 -16.003  1.00 19.94           C  
ANISOU 2706  CD  PRO C 145     3056   2371   2149   -188    567   -323       C  
ATOM   2707  N   LEU C 146      -6.829 -45.822 -19.016  1.00 17.82           N  
ANISOU 2707  N   LEU C 146     2323   1820   2627    310    518    259       N  
ATOM   2708  CA  LEU C 146      -5.799 -45.186 -19.807  1.00 17.89           C  
ANISOU 2708  CA  LEU C 146     2366   1584   2848    452    323    -23       C  
ATOM   2709  C   LEU C 146      -5.775 -43.693 -19.540  1.00 19.56           C  
ANISOU 2709  C   LEU C 146     2515   1620   3298    488    415     21       C  
ATOM   2710  O   LEU C 146      -6.810 -43.040 -19.581  1.00 23.61           O  
ANISOU 2710  O   LEU C 146     2657   2048   4264    644    568     72       O  
ATOM   2711  CB  LEU C 146      -6.042 -45.435 -21.292  1.00 19.95           C  
ANISOU 2711  CB  LEU C 146     2744   2249   2589    415   -133     17       C  
ATOM   2712  CG  LEU C 146      -4.920 -44.953 -22.200  1.00 23.78           C  
ANISOU 2712  CG  LEU C 146     3209   2691   3133    189    529   -121       C  
ATOM   2713  CD1 LEU C 146      -3.651 -45.788 -21.973  1.00 24.16           C  
ANISOU 2713  CD1 LEU C 146     2778   2827   3575    144   1082   -778       C  
ATOM   2714  CD2 LEU C 146      -5.358 -45.011 -23.650  1.00 25.50           C  
ANISOU 2714  CD2 LEU C 146     4089   2859   2742     73    296   -277       C  
ATOM   2715  N   HIS C 147      -4.592 -43.171 -19.255  1.00 17.80           N  
ANISOU 2715  N   HIS C 147     2356   1356   3052    331    118     52       N  
ATOM   2716  CA AHIS C 147      -4.401 -41.735 -19.127  0.60 19.41           C  
ANISOU 2716  CA AHIS C 147     2449   1632   3293    244    204    -27       C  
ATOM   2717  CA BHIS C 147      -4.392 -41.730 -19.122  0.40 19.92           C  
ANISOU 2717  CA BHIS C 147     2443   1858   3269    480    282    109       C  
ATOM   2718  C   HIS C 147      -3.735 -41.203 -20.390  1.00 20.61           C  
ANISOU 2718  C   HIS C 147     2599   1910   3320    682    403    396       C  
ATOM   2719  O   HIS C 147      -2.668 -41.671 -20.776  1.00 22.06           O  
ANISOU 2719  O   HIS C 147     2540   2300   3541    993    636    741       O  
ATOM   2720  CB AHIS C 147      -3.558 -41.422 -17.897  0.60 22.56           C  
ANISOU 2720  CB AHIS C 147     3348   1670   3555     65     75   -490       C  
ATOM   2721  CB BHIS C 147      -3.528 -41.401 -17.902  0.40 22.97           C  
ANISOU 2721  CB BHIS C 147     2994   2296   3438    584    299    -83       C  
ATOM   2722  CG AHIS C 147      -3.374 -39.961 -17.653  0.60 27.01           C  
ANISOU 2722  CG AHIS C 147     4231   1883   4150     20    106   -555       C  
ATOM   2723  CG BHIS C 147      -4.257 -41.481 -16.597  0.40 26.55           C  
ANISOU 2723  CG BHIS C 147     3531   2791   3767    729    484    -52       C  
ATOM   2724  ND1AHIS C 147      -2.364 -39.228 -18.239  0.60 29.30           N  
ANISOU 2724  ND1AHIS C 147     4595   2045   4492    201    209   -457       N  
ATOM   2725  ND1BHIS C 147      -5.591 -41.816 -16.505  0.40 28.71           N  
ANISOU 2725  ND1BHIS C 147     3741   3129   4041    921    790    134       N  
ATOM   2726  CD2AHIS C 147      -4.079 -39.093 -16.891  0.60 29.20           C  
ANISOU 2726  CD2AHIS C 147     4570   2098   4426    327    243   -527       C  
ATOM   2727  CD2BHIS C 147      -3.835 -41.266 -15.328  0.40 27.70           C  
ANISOU 2727  CD2BHIS C 147     3870   3006   3648    667    658   -124       C  
ATOM   2728  CE1AHIS C 147      -2.453 -37.970 -17.843  0.60 30.18           C  
ANISOU 2728  CE1AHIS C 147     4843   1825   4798    274    582   -585       C  
ATOM   2729  CE1BHIS C 147      -5.959 -41.804 -15.236  0.40 27.42           C  
ANISOU 2729  CE1BHIS C 147     3722   3138   3559   1095    749    160       C  
ATOM   2730  NE2AHIS C 147      -3.485 -37.862 -17.026  0.60 31.23           N  
ANISOU 2730  NE2AHIS C 147     5079   2033   4753    -47    563   -483       N  
ATOM   2731  NE2BHIS C 147      -4.913 -41.471 -14.501  0.40 28.03           N  
ANISOU 2731  NE2BHIS C 147     3940   3155   3553    933    946   -125       N  
ATOM   2732  N   MET C 148      -4.377 -40.236 -21.037  1.00 20.25           N  
ANISOU 2732  N   MET C 148     2735   1520   3439    402    526    545       N  
ATOM   2733  CA  MET C 148      -3.896 -39.704 -22.304  1.00 21.50           C  
ANISOU 2733  CA  MET C 148     2675   1624   3869    138     29    365       C  
ATOM   2734  C   MET C 148      -3.494 -38.256 -22.159  1.00 23.72           C  
ANISOU 2734  C   MET C 148     2892   1582   4537    588    538    652       C  
ATOM   2735  O   MET C 148      -4.228 -37.459 -21.594  1.00 29.23           O  
ANISOU 2735  O   MET C 148     3603   1928   5574    407   1125    546       O  
ATOM   2736  CB  MET C 148      -4.970 -39.836 -23.387  1.00 21.45           C  
ANISOU 2736  CB  MET C 148     2573   1810   3769    135    -97    213       C  
ATOM   2737  CG  MET C 148      -5.172 -41.277 -23.856  1.00 22.46           C  
ANISOU 2737  CG  MET C 148     2570   2189   3776    241   -768    587       C  
ATOM   2738  SD  MET C 148      -6.766 -41.516 -24.652  1.00 28.98           S  
ANISOU 2738  SD  MET C 148     3250   3374   4387    236   -397    826       S  
ATOM   2739  CE  MET C 148      -7.789 -41.637 -23.188  1.00 30.42           C  
ANISOU 2739  CE  MET C 148     2738   3847   4974   -509   -332    601       C  
ATOM   2740  N   THR C 149      -2.319 -37.924 -22.670  1.00 21.75           N  
ANISOU 2740  N   THR C 149     2742   1457   4065    453    -99    359       N  
ATOM   2741  CA ATHR C 149      -1.835 -36.559 -22.656  0.70 23.27           C  
ANISOU 2741  CA ATHR C 149     3216   1704   3922    392    254    414       C  
ATOM   2742  CA BTHR C 149      -1.865 -36.541 -22.665  0.30 22.50           C  
ANISOU 2742  CA BTHR C 149     2960   1724   3865    584      4    580       C  
ATOM   2743  C   THR C 149      -1.699 -36.053 -24.091  1.00 23.18           C  
ANISOU 2743  C   THR C 149     2990   2031   3788    637     16    719       C  
ATOM   2744  O   THR C 149      -1.116 -36.734 -24.933  1.00 24.47           O  
ANISOU 2744  O   THR C 149     3596   1889   3812    621    468    740       O  
ATOM   2745  CB ATHR C 149      -0.492 -36.463 -21.922  0.70 24.61           C  
ANISOU 2745  CB ATHR C 149     3822   1774   3756    494    438    440       C  
ATOM   2746  CB BTHR C 149      -0.542 -36.358 -21.900  0.30 22.46           C  
ANISOU 2746  CB BTHR C 149     3113   1712   3709    863   -108    834       C  
ATOM   2747  OG1ATHR C 149      -0.611 -37.092 -20.638  0.70 26.84           O  
ANISOU 2747  OG1ATHR C 149     3943   2422   3832    405     73    394       O  
ATOM   2748  OG1BTHR C 149       0.409 -37.337 -22.331  0.30 24.69           O  
ANISOU 2748  OG1BTHR C 149     3253   2262   3864   1022   -427    827       O  
ATOM   2749  CG2ATHR C 149      -0.106 -35.019 -21.728  0.70 25.39           C  
ANISOU 2749  CG2ATHR C 149     4093   1856   3699    259    778    -25       C  
ATOM   2750  CG2BTHR C 149      -0.774 -36.490 -20.401  0.30 21.28           C  
ANISOU 2750  CG2BTHR C 149     3030   1507   3548    784    133    727       C  
ATOM   2751  N   PHE C 150      -2.232 -34.865 -24.349  1.00 22.34           N  
ANISOU 2751  N   PHE C 150     2596   2106   3785    747   -279   1148       N  
ATOM   2752  CA  PHE C 150      -2.269 -34.293 -25.690  1.00 24.79           C  
ANISOU 2752  CA  PHE C 150     2728   2381   4309    602   -562    853       C  
ATOM   2753  C   PHE C 150      -1.241 -33.184 -25.836  1.00 26.19           C  
ANISOU 2753  C   PHE C 150     2930   2327   4694    398    104    837       C  
ATOM   2754  O   PHE C 150      -1.230 -32.246 -25.042  1.00 28.19           O  
ANISOU 2754  O   PHE C 150     3527   2197   4985    690    652    492       O  
ATOM   2755  CB  PHE C 150      -3.665 -33.731 -25.997  1.00 27.19           C  
ANISOU 2755  CB  PHE C 150     2675   2731   4927    646   -642    663       C  
ATOM   2756  CG  PHE C 150      -4.730 -34.780 -26.163  1.00 27.99           C  
ANISOU 2756  CG  PHE C 150     2726   2597   5310    713   -495   1004       C  
ATOM   2757  CD1 PHE C 150      -5.106 -35.590 -25.103  1.00 30.41           C  
ANISOU 2757  CD1 PHE C 150     2971   2842   5741    767   -236   1020       C  
ATOM   2758  CD2 PHE C 150      -5.382 -34.935 -27.376  1.00 28.82           C  
ANISOU 2758  CD2 PHE C 150     3155   2522   5273    175   -434    954       C  
ATOM   2759  CE1 PHE C 150      -6.088 -36.546 -25.259  1.00 30.66           C  
ANISOU 2759  CE1 PHE C 150     2930   2822   5898    426   -367    998       C  
ATOM   2760  CE2 PHE C 150      -6.367 -35.899 -27.534  1.00 30.50           C  
ANISOU 2760  CE2 PHE C 150     3275   2893   5419    -43   -471    876       C  
ATOM   2761  CZ  PHE C 150      -6.717 -36.697 -26.474  1.00 29.99           C  
ANISOU 2761  CZ  PHE C 150     3061   2717   5616   -115   -401    594       C  
ATOM   2762  N   TRP C 151      -0.381 -33.302 -26.847  1.00 26.56           N  
ANISOU 2762  N   TRP C 151     2995   2400   4695    309    614   1157       N  
ATOM   2763  CA  TRP C 151       0.583 -32.259 -27.200  1.00 26.85           C  
ANISOU 2763  CA  TRP C 151     3201   2668   4331    507   -253   1501       C  
ATOM   2764  C   TRP C 151       0.338 -31.794 -28.624  1.00 29.07           C  
ANISOU 2764  C   TRP C 151     3853   2520   4673    192   -443   1687       C  
ATOM   2765  O   TRP C 151      -0.007 -32.597 -29.482  1.00 31.98           O  
ANISOU 2765  O   TRP C 151     4438   3066   4646     96   -698   1853       O  
ATOM   2766  CB  TRP C 151       2.020 -32.772 -27.104  1.00 28.00           C  
ANISOU 2766  CB  TRP C 151     2976   3360   4302    459   -387   1328       C  
ATOM   2767  CG  TRP C 151       2.538 -33.084 -25.748  1.00 28.83           C  
ANISOU 2767  CG  TRP C 151     2991   3853   4109    150   -467   1326       C  
ATOM   2768  CD1 TRP C 151       2.217 -34.159 -24.971  1.00 27.79           C  
ANISOU 2768  CD1 TRP C 151     2978   3705   3874     83   -464   1572       C  
ATOM   2769  CD2 TRP C 151       3.534 -32.349 -25.029  1.00 30.33           C  
ANISOU 2769  CD2 TRP C 151     3183   4116   4225   -232   -183   1032       C  
ATOM   2770  NE1 TRP C 151       2.934 -34.122 -23.796  1.00 28.90           N  
ANISOU 2770  NE1 TRP C 151     2706   4023   4252   -133   -404    950       N  
ATOM   2771  CE2 TRP C 151       3.749 -33.020 -23.809  1.00 30.40           C  
ANISOU 2771  CE2 TRP C 151     3195   4325   4028   -262   -149    664       C  
ATOM   2772  CE3 TRP C 151       4.254 -31.181 -25.294  1.00 31.83           C  
ANISOU 2772  CE3 TRP C 151     3445   4319   4329   -235   -112   1068       C  
ATOM   2773  CZ2 TRP C 151       4.658 -32.565 -22.858  1.00 32.82           C  
ANISOU 2773  CZ2 TRP C 151     3579   4598   4294   -365    192    399       C  
ATOM   2774  CZ3 TRP C 151       5.154 -30.729 -24.349  1.00 33.29           C  
ANISOU 2774  CZ3 TRP C 151     3934   4537   4177   -473    278    790       C  
ATOM   2775  CH2 TRP C 151       5.348 -31.420 -23.144  1.00 33.08           C  
ANISOU 2775  CH2 TRP C 151     3791   4749   4029   -376    207    634       C  
ATOM   2776  N   GLY C 152       0.539 -30.510 -28.891  1.00 29.70           N  
ANISOU 2776  N   GLY C 152     3789   2545   4950    -45   -286   1854       N  
ATOM   2777  CA  GLY C 152       0.413 -30.021 -30.252  1.00 31.75           C  
ANISOU 2777  CA  GLY C 152     4072   2771   5222     -3    118   2051       C  
ATOM   2778  C   GLY C 152       0.806 -28.566 -30.410  1.00 33.37           C  
ANISOU 2778  C   GLY C 152     3906   3004   5767    -71    153   2191       C  
ATOM   2779  O   GLY C 152       1.179 -27.905 -29.441  1.00 32.08           O  
ANISOU 2779  O   GLY C 152     3684   2830   5674    387     42   2055       O  
ATOM   2780  N   LYS C 153       0.723 -28.074 -31.642  1.00 36.23           N  
ANISOU 2780  N   LYS C 153     4262   3506   5998    418   -189   2479       N  
ATOM   2781  CA  LYS C 153       1.014 -26.676 -31.920  1.00 41.15           C  
ANISOU 2781  CA  LYS C 153     4849   3783   7003    452     95   2646       C  
ATOM   2782  C   LYS C 153      -0.101 -25.799 -31.369  1.00 43.70           C  
ANISOU 2782  C   LYS C 153     5127   4012   7464    304    211   2938       C  
ATOM   2783  O   LYS C 153      -1.274 -26.162 -31.440  1.00 44.26           O  
ANISOU 2783  O   LYS C 153     5223   4070   7524     65    104   3010       O  
ATOM   2784  CB  LYS C 153       1.172 -26.435 -33.421  1.00 43.63           C  
ANISOU 2784  CB  LYS C 153     5333   4156   7089    616    120   2592       C  
ATOM   2785  CG  LYS C 153       2.340 -27.150 -34.069  1.00 47.56           C  
ANISOU 2785  CG  LYS C 153     6140   4699   7230    311    333   2308       C  
ATOM   2786  CD  LYS C 153       2.622 -26.554 -35.440  1.00 50.90           C  
ANISOU 2786  CD  LYS C 153     6904   5181   7253    330    554   2505       C  
ATOM   2787  CE  LYS C 153       3.779 -27.246 -36.142  1.00 54.43           C  
ANISOU 2787  CE  LYS C 153     7647   5501   7532    224    724   2302       C  
ATOM   2788  NZ  LYS C 153       3.362 -28.511 -36.803  1.00 56.36           N  
ANISOU 2788  NZ  LYS C 153     7983   5731   7699    -15    802   2094       N  
ATOM   2789  N   GLU C 154       0.275 -24.646 -30.827  1.00 44.81           N  
ANISOU 2789  N   GLU C 154     5296   4120   7611    260    388   3035       N  
ATOM   2790  CA  GLU C 154      -0.681 -23.703 -30.252  1.00 49.03           C  
ANISOU 2790  CA  GLU C 154     5348   4429   8851    603    493   3176       C  
ATOM   2791  C   GLU C 154      -1.875 -23.437 -31.166  1.00 50.23           C  
ANISOU 2791  C   GLU C 154     5410   4669   9009    670    498   3405       C  
ATOM   2792  O   GLU C 154      -3.016 -23.355 -30.709  1.00 46.91           O  
ANISOU 2792  O   GLU C 154     4451   4444   8929    379    445   3296       O  
ATOM   2793  CB  GLU C 154       0.012 -22.377 -29.935  1.00 50.74           C  
ANISOU 2793  CB  GLU C 154     5309   4304   9664    727    711   2763       C  
ATOM   2794  CG  GLU C 154      -0.877 -21.395 -29.198  1.00 52.46           C  
ANISOU 2794  CG  GLU C 154     5474   4316  10145    503   1035   2575       C  
ATOM   2795  CD  GLU C 154      -1.398 -21.980 -27.901  1.00 52.66           C  
ANISOU 2795  CD  GLU C 154     5632   4015  10360    602   1325   2346       C  
ATOM   2796  OE1 GLU C 154      -0.571 -22.499 -27.121  1.00 51.41           O  
ANISOU 2796  OE1 GLU C 154     5784   3585  10162   1119   1363   2039       O  
ATOM   2797  OE2 GLU C 154      -2.627 -21.931 -27.671  1.00 51.76           O  
ANISOU 2797  OE2 GLU C 154     5315   3953  10398    563   1151   2424       O  
ATOM   2798  N   GLU C 155      -1.603 -23.320 -32.461  1.00 51.56           N  
ANISOU 2798  N   GLU C 155     5771   5110   8709    823    130   3595       N  
ATOM   2799  CA  GLU C 155      -2.630 -22.947 -33.426  1.00 53.40           C  
ANISOU 2799  CA  GLU C 155     5606   5406   9278    889   -532   3584       C  
ATOM   2800  C   GLU C 155      -3.673 -24.049 -33.609  1.00 51.98           C  
ANISOU 2800  C   GLU C 155     5224   5442   9084    522   -841   3611       C  
ATOM   2801  O   GLU C 155      -4.773 -23.791 -34.093  1.00 52.24           O  
ANISOU 2801  O   GLU C 155     5233   5599   9017    550   -940   3671       O  
ATOM   2802  CB  GLU C 155      -1.989 -22.593 -34.772  1.00 56.58           C  
ANISOU 2802  CB  GLU C 155     5751   5576  10170    823   -571   3454       C  
ATOM   2803  CG  GLU C 155      -1.253 -23.736 -35.443  1.00 60.68           C  
ANISOU 2803  CG  GLU C 155     6018   6010  11028    602   -316   2808       C  
ATOM   2804  CD  GLU C 155       0.208 -23.420 -35.700  1.00 65.82           C  
ANISOU 2804  CD  GLU C 155     6673   6342  11994    626    447   2214       C  
ATOM   2805  OE1 GLU C 155       0.796 -22.636 -34.921  1.00 64.95           O  
ANISOU 2805  OE1 GLU C 155     6429   6025  12225    892    302   1921       O  
ATOM   2806  OE2 GLU C 155       0.769 -23.954 -36.682  1.00 69.04           O  
ANISOU 2806  OE2 GLU C 155     7275   6691  12267    290    996   1934       O  
ATOM   2807  N   ASN C 156      -3.328 -25.271 -33.208  1.00 50.15           N  
ANISOU 2807  N   ASN C 156     4912   5341   8800    362  -1091   3512       N  
ATOM   2808  CA  ASN C 156      -4.232 -26.409 -33.345  1.00 48.86           C  
ANISOU 2808  CA  ASN C 156     4871   5092   8604    357  -1196   3312       C  
ATOM   2809  C   ASN C 156      -5.002 -26.723 -32.069  1.00 46.49           C  
ANISOU 2809  C   ASN C 156     4590   4611   8463    332  -1188   3014       C  
ATOM   2810  O   ASN C 156      -5.798 -27.662 -32.039  1.00 46.44           O  
ANISOU 2810  O   ASN C 156     4786   4525   8333    142  -1322   3031       O  
ATOM   2811  CB  ASN C 156      -3.460 -27.656 -33.780  1.00 48.94           C  
ANISOU 2811  CB  ASN C 156     4942   5354   8301    356  -1368   3341       C  
ATOM   2812  CG  ASN C 156      -3.056 -27.613 -35.236  1.00 49.10           C  
ANISOU 2812  CG  ASN C 156     5220   5590   7844    389  -1400   3395       C  
ATOM   2813  OD1 ASN C 156      -3.790 -27.093 -36.080  1.00 49.51           O  
ANISOU 2813  OD1 ASN C 156     5578   5859   7375    551  -1409   3386       O  
ATOM   2814  ND2 ASN C 156      -1.885 -28.160 -35.542  1.00 49.82           N  
ANISOU 2814  ND2 ASN C 156     5330   5489   8110    156  -1024   3322       N  
ATOM   2815  N   ARG C 157      -4.767 -25.940 -31.022  1.00 44.68           N  
ANISOU 2815  N   ARG C 157     4294   4310   8371    717   -733   2706       N  
ATOM   2816  CA  ARG C 157      -5.357 -26.220 -29.718  1.00 44.87           C  
ANISOU 2816  CA  ARG C 157     3947   4005   9098    571   -436   2606       C  
ATOM   2817  C   ARG C 157      -6.880 -26.208 -29.746  1.00 46.27           C  
ANISOU 2817  C   ARG C 157     4068   4178   9334    507   -496   2785       C  
ATOM   2818  O   ARG C 157      -7.524 -27.138 -29.255  1.00 44.52           O  
ANISOU 2818  O   ARG C 157     3574   3974   9368    189   -747   2669       O  
ATOM   2819  CB  ARG C 157      -4.855 -25.220 -28.679  1.00 44.25           C  
ANISOU 2819  CB  ARG C 157     3766   3675   9373    568   -385   2229       C  
ATOM   2820  CG  ARG C 157      -5.354 -25.503 -27.273  1.00 44.28           C  
ANISOU 2820  CG  ARG C 157     3611   3579   9635    521   -438   1599       C  
ATOM   2821  CD  ARG C 157      -5.118 -24.315 -26.353  1.00 44.03           C  
ANISOU 2821  CD  ARG C 157     3741   3238   9750    594   -186   1374       C  
ATOM   2822  NE  ARG C 157      -3.698 -24.013 -26.197  1.00 44.93           N  
ANISOU 2822  NE  ARG C 157     4129   3066   9876    709    564   1334       N  
ATOM   2823  CZ  ARG C 157      -2.908 -24.610 -25.312  1.00 44.42           C  
ANISOU 2823  CZ  ARG C 157     4312   3068   9497    599   1146   1486       C  
ATOM   2824  NH1 ARG C 157      -3.401 -25.549 -24.512  1.00 43.72           N  
ANISOU 2824  NH1 ARG C 157     4608   3173   8830    634   1951   1962       N  
ATOM   2825  NH2 ARG C 157      -1.628 -24.282 -25.231  1.00 45.38           N  
ANISOU 2825  NH2 ARG C 157     4417   3177   9650    264   1024   1021       N  
ATOM   2826  N   LYS C 158      -7.452 -25.158 -30.326  1.00 49.06           N  
ANISOU 2826  N   LYS C 158     4531   4464   9645    789   -470   2853       N  
ATOM   2827  CA  LYS C 158      -8.900 -25.024 -30.389  1.00 51.37           C  
ANISOU 2827  CA  LYS C 158     4904   4664   9950    942   -519   2916       C  
ATOM   2828  C   LYS C 158      -9.538 -26.132 -31.218  1.00 51.43           C  
ANISOU 2828  C   LYS C 158     4804   4774   9964   1138   -584   2729       C  
ATOM   2829  O   LYS C 158     -10.578 -26.670 -30.844  1.00 51.05           O  
ANISOU 2829  O   LYS C 158     4253   4883  10261   1030   -935   2366       O  
ATOM   2830  CB  LYS C 158      -9.288 -23.657 -30.960  1.00 55.18           C  
ANISOU 2830  CB  LYS C 158     5622   4872  10473   1052   -261   3193       C  
ATOM   2831  CG  LYS C 158      -9.054 -22.499 -30.005  1.00 58.25           C  
ANISOU 2831  CG  LYS C 158     6053   5216  10864   1205   -300   3267       C  
ATOM   2832  CD  LYS C 158      -9.802 -21.248 -30.456  1.00 61.50           C  
ANISOU 2832  CD  LYS C 158     6320   5654  11394   1220   -231   2917       C  
ATOM   2833  CE  LYS C 158      -8.850 -20.181 -30.981  1.00 64.26           C  
ANISOU 2833  CE  LYS C 158     6528   6126  11763    816     22   2535       C  
ATOM   2834  NZ  LYS C 158      -8.062 -20.649 -32.156  1.00 66.71           N  
ANISOU 2834  NZ  LYS C 158     6841   6422  12085    507    404   2262       N  
ATOM   2835  N   ALA C 159      -8.912 -26.469 -32.342  1.00 50.28           N  
ANISOU 2835  N   ALA C 159     4937   4820   9346   1157   -719   2790       N  
ATOM   2836  CA  ALA C 159      -9.430 -27.510 -33.226  1.00 50.43           C  
ANISOU 2836  CA  ALA C 159     4899   4990   9273    928  -1131   2885       C  
ATOM   2837  C   ALA C 159      -9.519 -28.866 -32.517  1.00 50.07           C  
ANISOU 2837  C   ALA C 159     4764   4655   9607    389  -1469   2874       C  
ATOM   2838  O   ALA C 159     -10.429 -29.652 -32.774  1.00 50.40           O  
ANISOU 2838  O   ALA C 159     4917   4628   9605    389  -1557   2866       O  
ATOM   2839  CB  ALA C 159      -8.567 -27.619 -34.472  1.00 49.81           C  
ANISOU 2839  CB  ALA C 159     4861   5198   8867   1021  -1177   2887       C  
ATOM   2840  N   VAL C 160      -8.571 -29.135 -31.625  1.00 48.01           N  
ANISOU 2840  N   VAL C 160     4503   4346   9392    142  -1288   2850       N  
ATOM   2841  CA  VAL C 160      -8.589 -30.367 -30.849  1.00 47.31           C  
ANISOU 2841  CA  VAL C 160     4323   4603   9048    220  -1661   2709       C  
ATOM   2842  C   VAL C 160      -9.722 -30.351 -29.831  1.00 49.03           C  
ANISOU 2842  C   VAL C 160     4399   4659   9573    347  -1864   2524       C  
ATOM   2843  O   VAL C 160     -10.493 -31.305 -29.729  1.00 49.19           O  
ANISOU 2843  O   VAL C 160     4547   4137  10005    168  -1711   2448       O  
ATOM   2844  CB  VAL C 160      -7.251 -30.589 -30.120  1.00 44.75           C  
ANISOU 2844  CB  VAL C 160     4187   4538   8278    290  -1680   2581       C  
ATOM   2845  CG1 VAL C 160      -7.376 -31.704 -29.089  1.00 42.79           C  
ANISOU 2845  CG1 VAL C 160     4035   4221   8001   -111  -1824   2577       C  
ATOM   2846  CG2 VAL C 160      -6.149 -30.890 -31.122  1.00 46.95           C  
ANISOU 2846  CG2 VAL C 160     4401   4654   8785    260  -1581   2831       C  
ATOM   2847  N   SER C 161      -9.817 -29.256 -29.085  1.00 52.29           N  
ANISOU 2847  N   SER C 161     4559   4966  10343    596  -1520   2429       N  
ATOM   2848  CA  SER C 161     -10.834 -29.112 -28.051  1.00 55.92           C  
ANISOU 2848  CA  SER C 161     4567   5562  11119    476  -1134   2096       C  
ATOM   2849  C   SER C 161     -12.246 -29.135 -28.636  1.00 56.41           C  
ANISOU 2849  C   SER C 161     4416   5691  11328    708  -1329   2066       C  
ATOM   2850  O   SER C 161     -13.172 -29.675 -28.029  1.00 54.35           O  
ANISOU 2850  O   SER C 161     3667   5627  11359    534  -1752   1418       O  
ATOM   2851  CB  SER C 161     -10.606 -27.817 -27.268  1.00 60.10           C  
ANISOU 2851  CB  SER C 161     5058   6152  11625     31   -193   1706       C  
ATOM   2852  OG  SER C 161     -11.606 -27.630 -26.283  1.00 63.16           O  
ANISOU 2852  OG  SER C 161     5525   6579  11895   -206    312   1483       O  
ATOM   2853  N   ASP C 162     -12.400 -28.552 -29.821  1.00 57.37           N  
ANISOU 2853  N   ASP C 162     4716   5912  11168   1056  -1579   2596       N  
ATOM   2854  CA  ASP C 162     -13.692 -28.509 -30.496  1.00 57.83           C  
ANISOU 2854  CA  ASP C 162     5106   5858  11009   1082  -1528   2927       C  
ATOM   2855  C   ASP C 162     -14.126 -29.891 -30.979  1.00 56.37           C  
ANISOU 2855  C   ASP C 162     5126   5728  10563    823  -1654   3037       C  
ATOM   2856  O   ASP C 162     -15.309 -30.227 -30.932  1.00 54.69           O  
ANISOU 2856  O   ASP C 162     5060   5848   9870    855  -2033   2798       O  
ATOM   2857  CB  ASP C 162     -13.647 -27.533 -31.675  1.00 60.58           C  
ANISOU 2857  CB  ASP C 162     5648   6014  11356   1165   -982   3114       C  
ATOM   2858  CG  ASP C 162     -13.748 -26.080 -31.238  1.00 63.14           C  
ANISOU 2858  CG  ASP C 162     6110   6191  11688   1253   -571   3176       C  
ATOM   2859  OD1 ASP C 162     -14.298 -25.825 -30.145  1.00 64.38           O  
ANISOU 2859  OD1 ASP C 162     6338   6222  11900   1286   -100   3104       O  
ATOM   2860  OD2 ASP C 162     -13.286 -25.194 -31.990  1.00 63.28           O  
ANISOU 2860  OD2 ASP C 162     6130   6286  11630   1347   -936   3400       O  
ATOM   2861  N   GLN C 163     -13.167 -30.689 -31.443  1.00 54.83           N  
ANISOU 2861  N   GLN C 163     4988   5488  10357    641  -1776   3016       N  
ATOM   2862  CA  GLN C 163     -13.465 -32.043 -31.904  1.00 54.76           C  
ANISOU 2862  CA  GLN C 163     4995   5535  10277    474  -2142   2751       C  
ATOM   2863  C   GLN C 163     -13.907 -32.926 -30.743  1.00 54.49           C  
ANISOU 2863  C   GLN C 163     5007   5493  10203    329  -2256   2690       C  
ATOM   2864  O   GLN C 163     -14.839 -33.720 -30.872  1.00 54.50           O  
ANISOU 2864  O   GLN C 163     5015   5607  10084    323  -2524   2686       O  
ATOM   2865  CB  GLN C 163     -12.250 -32.661 -32.602  1.00 53.82           C  
ANISOU 2865  CB  GLN C 163     4953   5484  10013    465  -2410   2600       C  
ATOM   2866  CG  GLN C 163     -12.387 -34.148 -32.914  1.00 53.32           C  
ANISOU 2866  CG  GLN C 163     4976   5642   9642    280  -2734   2463       C  
ATOM   2867  CD  GLN C 163     -13.403 -34.441 -34.007  1.00 52.87           C  
ANISOU 2867  CD  GLN C 163     4997   5629   9464    470  -2635   2340       C  
ATOM   2868  OE1 GLN C 163     -13.920 -33.531 -34.654  1.00 51.16           O  
ANISOU 2868  OE1 GLN C 163     5061   5509   8868    769  -2411   2328       O  
ATOM   2869  NE2 GLN C 163     -13.688 -35.719 -34.219  1.00 54.07           N  
ANISOU 2869  NE2 GLN C 163     5121   5798   9624    588  -2744   2220       N  
ATOM   2870  N   LEU C 164     -13.235 -32.782 -29.607  1.00 54.09           N  
ANISOU 2870  N   LEU C 164     4847   5298  10407    547  -1917   2819       N  
ATOM   2871  CA  LEU C 164     -13.603 -33.535 -28.416  1.00 52.77           C  
ANISOU 2871  CA  LEU C 164     4496   5077  10476    303  -1731   2671       C  
ATOM   2872  C   LEU C 164     -14.992 -33.143 -27.911  1.00 54.57           C  
ANISOU 2872  C   LEU C 164     4537   5275  10923    336  -1696   2621       C  
ATOM   2873  O   LEU C 164     -15.786 -34.004 -27.530  1.00 54.68           O  
ANISOU 2873  O   LEU C 164     4483   5184  11109    127  -1681   2474       O  
ATOM   2874  CB  LEU C 164     -12.560 -33.332 -27.318  1.00 49.25           C  
ANISOU 2874  CB  LEU C 164     3915   4834   9963    -38  -1922   2463       C  
ATOM   2875  CG  LEU C 164     -11.160 -33.862 -27.645  1.00 46.97           C  
ANISOU 2875  CG  LEU C 164     4063   4534   9250    183  -1738   2579       C  
ATOM   2876  CD1 LEU C 164     -10.176 -33.475 -26.562  1.00 46.69           C  
ANISOU 2876  CD1 LEU C 164     3870   4505   9367    178  -1800   2322       C  
ATOM   2877  CD2 LEU C 164     -11.177 -35.371 -27.837  1.00 46.77           C  
ANISOU 2877  CD2 LEU C 164     4295   4558   8918    160  -1673   2711       C  
ATOM   2878  N   LYS C 165     -15.288 -31.846 -27.916  1.00 55.88           N  
ANISOU 2878  N   LYS C 165     4491   5610  11130    503  -1672   2508       N  
ATOM   2879  CA  LYS C 165     -16.583 -31.360 -27.448  1.00 56.99           C  
ANISOU 2879  CA  LYS C 165     4516   5945  11194    601  -1585   2603       C  
ATOM   2880  C   LYS C 165     -17.718 -31.877 -28.326  1.00 58.01           C  
ANISOU 2880  C   LYS C 165     4676   6085  11281    377  -1471   2599       C  
ATOM   2881  O   LYS C 165     -18.828 -32.114 -27.849  1.00 57.74           O  
ANISOU 2881  O   LYS C 165     4518   6181  11239    135  -1391   2433       O  
ATOM   2882  CB  LYS C 165     -16.604 -29.830 -27.413  1.00 57.86           C  
ANISOU 2882  CB  LYS C 165     4434   6067  11484    901  -1236   2520       C  
ATOM   2883  CG  LYS C 165     -17.948 -29.240 -27.010  1.00 59.78           C  
ANISOU 2883  CG  LYS C 165     4671   6222  11819   1127   -617   2479       C  
ATOM   2884  CD  LYS C 165     -17.902 -27.727 -26.925  1.00 60.55           C  
ANISOU 2884  CD  LYS C 165     4752   6265  11988   1506   -449   2568       C  
ATOM   2885  CE  LYS C 165     -19.273 -27.167 -26.584  1.00 60.35           C  
ANISOU 2885  CE  LYS C 165     4729   6314  11886   1617   -541   2654       C  
ATOM   2886  NZ  LYS C 165     -19.214 -25.720 -26.259  1.00 59.77           N  
ANISOU 2886  NZ  LYS C 165     4660   6296  11756   1618   -711   2495       N  
ATOM   2887  N   LYS C 166     -17.428 -32.050 -29.610  1.00 57.95           N  
ANISOU 2887  N   LYS C 166     4812   6034  11171    486  -1789   2869       N  
ATOM   2888  CA  LYS C 166     -18.406 -32.559 -30.563  1.00 59.21           C  
ANISOU 2888  CA  LYS C 166     5106   6140  11250    453  -1689   2978       C  
ATOM   2889  C   LYS C 166     -18.901 -33.943 -30.147  1.00 58.19           C  
ANISOU 2889  C   LYS C 166     4818   6244  11048    306  -1760   3045       C  
ATOM   2890  O   LYS C 166     -20.092 -34.250 -30.243  1.00 58.66           O  
ANISOU 2890  O   LYS C 166     4846   6423  11021    569  -1624   3247       O  
ATOM   2891  CB  LYS C 166     -17.794 -32.607 -31.965  1.00 61.26           C  
ANISOU 2891  CB  LYS C 166     5586   6264  11425    641  -1525   3106       C  
ATOM   2892  CG  LYS C 166     -18.728 -33.105 -33.050  1.00 64.47           C  
ANISOU 2892  CG  LYS C 166     6156   6597  11743    606  -1134   3068       C  
ATOM   2893  CD  LYS C 166     -18.044 -33.065 -34.410  1.00 67.22           C  
ANISOU 2893  CD  LYS C 166     6566   6988  11987    486   -895   2939       C  
ATOM   2894  CE  LYS C 166     -18.982 -33.514 -35.519  1.00 69.15           C  
ANISOU 2894  CE  LYS C 166     6883   7304  12088    318   -768   2807       C  
ATOM   2895  NZ  LYS C 166     -18.322 -33.470 -36.854  1.00 69.92           N  
ANISOU 2895  NZ  LYS C 166     7056   7444  12066    224   -637   2784       N  
ATOM   2896  N   HIS C 167     -17.974 -34.766 -29.668  1.00 56.18           N  
ANISOU 2896  N   HIS C 167     4525   6015  10807    136  -1987   3061       N  
ATOM   2897  CA  HIS C 167     -18.285 -36.131 -29.262  1.00 55.35           C  
ANISOU 2897  CA  HIS C 167     4376   5857  10796   -379  -1976   2786       C  
ATOM   2898  C   HIS C 167     -18.526 -36.251 -27.761  1.00 55.98           C  
ANISOU 2898  C   HIS C 167     4215   6093  10961   -539  -1549   2341       C  
ATOM   2899  O   HIS C 167     -18.599 -37.357 -27.224  1.00 57.80           O  
ANISOU 2899  O   HIS C 167     4637   6321  11004   -536  -1146   2372       O  
ATOM   2900  CB  HIS C 167     -17.157 -37.074 -29.674  1.00 54.82           C  
ANISOU 2900  CB  HIS C 167     4516   5636  10678   -288  -2088   3027       C  
ATOM   2901  CG  HIS C 167     -17.081 -37.320 -31.148  1.00 55.37           C  
ANISOU 2901  CG  HIS C 167     4909   5599  10532   -248  -2063   3267       C  
ATOM   2902  ND1 HIS C 167     -16.570 -36.396 -32.033  1.00 56.40           N  
ANISOU 2902  ND1 HIS C 167     5089   5595  10747    -18  -2073   3268       N  
ATOM   2903  CD2 HIS C 167     -17.452 -38.389 -31.892  1.00 55.72           C  
ANISOU 2903  CD2 HIS C 167     5100   5715  10355   -177  -2207   3307       C  
ATOM   2904  CE1 HIS C 167     -16.629 -36.885 -33.259  1.00 56.19           C  
ANISOU 2904  CE1 HIS C 167     5055   5648  10646    -87  -2278   3171       C  
ATOM   2905  NE2 HIS C 167     -17.159 -38.094 -33.200  1.00 57.39           N  
ANISOU 2905  NE2 HIS C 167     5238   5931  10635   -152  -2169   2983       N  
ATOM   2906  N   GLY C 168     -18.637 -35.113 -27.087  1.00 54.40           N  
ANISOU 2906  N   GLY C 168     3739   6043  10886   -407  -1596   2124       N  
ATOM   2907  CA  GLY C 168     -18.935 -35.101 -25.668  1.00 54.26           C  
ANISOU 2907  CA  GLY C 168     3847   5986  10783   -377  -1225   1796       C  
ATOM   2908  C   GLY C 168     -17.742 -35.360 -24.768  1.00 54.37           C  
ANISOU 2908  C   GLY C 168     4034   5880  10745    -88   -804   1659       C  
ATOM   2909  O   GLY C 168     -17.899 -35.869 -23.660  1.00 57.32           O  
ANISOU 2909  O   GLY C 168     4561   6199  11019   -331   -285   1158       O  
ATOM   2910  N   PHE C 169     -16.549 -35.014 -25.242  1.00 52.63           N  
ANISOU 2910  N   PHE C 169     3882   5570  10544    548   -840   1671       N  
ATOM   2911  CA  PHE C 169     -15.344 -35.112 -24.421  1.00 50.70           C  
ANISOU 2911  CA  PHE C 169     3706   5226  10331    745   -913   1603       C  
ATOM   2912  C   PHE C 169     -14.759 -33.726 -24.155  1.00 50.86           C  
ANISOU 2912  C   PHE C 169     3901   5007  10417   1103   -433   1308       C  
ATOM   2913  O   PHE C 169     -15.034 -32.774 -24.887  1.00 51.67           O  
ANISOU 2913  O   PHE C 169     3959   5115  10558   1223   -435   1378       O  
ATOM   2914  CB  PHE C 169     -14.290 -36.001 -25.093  1.00 49.12           C  
ANISOU 2914  CB  PHE C 169     3389   5172  10100    589  -1249   1847       C  
ATOM   2915  CG  PHE C 169     -14.712 -37.435 -25.256  1.00 50.05           C  
ANISOU 2915  CG  PHE C 169     3542   5363  10110    333  -1066   1951       C  
ATOM   2916  CD1 PHE C 169     -14.512 -38.349 -24.236  1.00 51.03           C  
ANISOU 2916  CD1 PHE C 169     3863   5415  10111    118   -685   1993       C  
ATOM   2917  CD2 PHE C 169     -15.291 -37.872 -26.436  1.00 50.62           C  
ANISOU 2917  CD2 PHE C 169     3706   5388  10138    110   -942   1883       C  
ATOM   2918  CE1 PHE C 169     -14.894 -39.672 -24.384  1.00 51.60           C  
ANISOU 2918  CE1 PHE C 169     4007   5550  10050    153   -645   1995       C  
ATOM   2919  CE2 PHE C 169     -15.678 -39.194 -26.590  1.00 50.71           C  
ANISOU 2919  CE2 PHE C 169     3811   5445  10010    281   -993   2043       C  
ATOM   2920  CZ  PHE C 169     -15.478 -40.095 -25.564  1.00 50.61           C  
ANISOU 2920  CZ  PHE C 169     3870   5485   9876    152   -965   1972       C  
ATOM   2921  N   LYS C 170     -13.953 -33.617 -23.104  1.00 49.97           N  
ANISOU 2921  N   LYS C 170     3946   4771  10270   1200   -118    991       N  
ATOM   2922  CA  LYS C 170     -13.239 -32.378 -22.806  1.00 50.42           C  
ANISOU 2922  CA  LYS C 170     4327   4642  10187   1334    540    884       C  
ATOM   2923  C   LYS C 170     -11.917 -32.677 -22.111  1.00 45.94           C  
ANISOU 2923  C   LYS C 170     4144   3869   9441   1001    535   1008       C  
ATOM   2924  O   LYS C 170     -11.864 -33.507 -21.201  1.00 46.93           O  
ANISOU 2924  O   LYS C 170     4457   4009   9367    754    388   1235       O  
ATOM   2925  CB  LYS C 170     -14.096 -31.452 -21.936  1.00 53.90           C  
ANISOU 2925  CB  LYS C 170     4431   5365  10683   1687    619    588       C  
ATOM   2926  CG  LYS C 170     -13.361 -30.212 -21.438  1.00 57.87           C  
ANISOU 2926  CG  LYS C 170     4879   6063  11047   1849    939    549       C  
ATOM   2927  CD  LYS C 170     -14.259 -29.310 -20.600  1.00 61.64           C  
ANISOU 2927  CD  LYS C 170     5237   6699  11484   1854   1378    313       C  
ATOM   2928  CE  LYS C 170     -15.291 -28.592 -21.459  1.00 64.89           C  
ANISOU 2928  CE  LYS C 170     5552   7200  11902   1834   1679    130       C  
ATOM   2929  NZ  LYS C 170     -16.091 -27.602 -20.677  1.00 67.16           N  
ANISOU 2929  NZ  LYS C 170     5988   7397  12131   1571   2004     46       N  
ATOM   2930  N   LEU C 171     -10.844 -32.025 -22.545  1.00 41.38           N  
ANISOU 2930  N   LEU C 171     4042   3047   8632   1192    718    828       N  
ATOM   2931  CA  LEU C 171      -9.560 -32.207 -21.885  1.00 39.14           C  
ANISOU 2931  CA  LEU C 171     3743   2737   8393    822    926    563       C  
ATOM   2932  C   LEU C 171      -9.606 -31.675 -20.464  1.00 40.26           C  
ANISOU 2932  C   LEU C 171     3650   2922   8726    890    914    136       C  
ATOM   2933  O   LEU C 171     -10.278 -30.674 -20.172  1.00 40.69           O  
ANISOU 2933  O   LEU C 171     3452   3210   8798    930    647   -584       O  
ATOM   2934  CB  LEU C 171      -8.429 -31.517 -22.653  1.00 38.27           C  
ANISOU 2934  CB  LEU C 171     3864   2677   8001    551   1161    670       C  
ATOM   2935  CG  LEU C 171      -8.011 -32.132 -23.985  1.00 37.96           C  
ANISOU 2935  CG  LEU C 171     3991   2883   7549    743   1174    955       C  
ATOM   2936  CD1 LEU C 171      -6.799 -31.403 -24.549  1.00 39.38           C  
ANISOU 2936  CD1 LEU C 171     4329   3303   7330    360   1006    569       C  
ATOM   2937  CD2 LEU C 171      -7.725 -33.610 -23.821  1.00 37.16           C  
ANISOU 2937  CD2 LEU C 171     3555   3171   7391   1369    918    843       C  
ATOM   2938  N   GLY C 172      -8.892 -32.362 -19.584  1.00 41.63           N  
ANISOU 2938  N   GLY C 172     4127   3100   8589    846   1153    293       N  
ATOM   2939  CA  GLY C 172      -8.692 -31.902 -18.231  1.00 44.10           C  
ANISOU 2939  CA  GLY C 172     4771   3657   8328    885   1142    -61       C  
ATOM   2940  C   GLY C 172      -7.363 -31.187 -18.153  1.00 49.94           C  
ANISOU 2940  C   GLY C 172     5612   4903   8460    691   1353   -789       C  
ATOM   2941  O   GLY C 172      -6.623 -31.136 -19.139  1.00 49.51           O  
ANISOU 2941  O   GLY C 172     5889   4731   8191    513   1551  -1414       O  
ATOM   2942  N   PRO C 173      -7.044 -30.647 -16.973  1.00 57.42           N  
ANISOU 2942  N   PRO C 173     6354   6541   8921    278   1366  -1125       N  
ATOM   2943  CA  PRO C 173      -5.874 -29.796 -16.730  1.00 62.20           C  
ANISOU 2943  CA  PRO C 173     6850   7446   9336    -57   1412  -1402       C  
ATOM   2944  C   PRO C 173      -4.546 -30.464 -17.064  1.00 66.50           C  
ANISOU 2944  C   PRO C 173     7295   8145   9829    -92   1505  -1451       C  
ATOM   2945  O   PRO C 173      -4.492 -31.671 -17.313  1.00 66.56           O  
ANISOU 2945  O   PRO C 173     7317   8108   9864    122   1838  -1680       O  
ATOM   2946  CB  PRO C 173      -5.965 -29.505 -15.229  1.00 62.26           C  
ANISOU 2946  CB  PRO C 173     6947   7522   9187   -239   1374  -1483       C  
ATOM   2947  CG  PRO C 173      -6.788 -30.622 -14.680  1.00 61.33           C  
ANISOU 2947  CG  PRO C 173     6853   7369   9083   -222   1321  -1383       C  
ATOM   2948  CD  PRO C 173      -7.792 -30.915 -15.735  1.00 59.79           C  
ANISOU 2948  CD  PRO C 173     6622   7060   9036      7   1273  -1167       C  
ATOM   2949  N   ALA C 174      -3.487 -29.659 -17.060  1.00 70.01           N  
ANISOU 2949  N   ALA C 174     7605   8723  10274   -268   1328  -1257       N  
ATOM   2950  CA  ALA C 174      -2.137 -30.113 -17.368  1.00 72.33           C  
ANISOU 2950  CA  ALA C 174     7812   9135  10533   -353   1146  -1087       C  
ATOM   2951  C   ALA C 174      -1.719 -31.306 -16.511  1.00 73.42           C  
ANISOU 2951  C   ALA C 174     7943   9386  10566   -349   1124   -867       C  
ATOM   2952  O   ALA C 174      -0.994 -31.152 -15.528  1.00 74.20           O  
ANISOU 2952  O   ALA C 174     8073   9574  10546   -270   1144   -634       O  
ATOM   2953  CB  ALA C 174      -1.155 -28.967 -17.188  1.00 72.93           C  
ANISOU 2953  CB  ALA C 174     7875   9177  10660   -450   1083  -1045       C  
TER    2954      ALA C 174                                                      
ATOM   2955  N   GLY D  51      20.529 -51.955   1.895  1.00 56.23           N  
ANISOU 2955  N   GLY D  51     8717   8997   3653    353   -576  -1790       N  
ATOM   2956  CA  GLY D  51      19.253 -52.215   2.537  1.00 55.89           C  
ANISOU 2956  CA  GLY D  51     8419   9011   3806    305   -507  -1385       C  
ATOM   2957  C   GLY D  51      18.474 -50.944   2.827  1.00 56.18           C  
ANISOU 2957  C   GLY D  51     8224   9059   4062     63   -569   -764       C  
ATOM   2958  O   GLY D  51      18.949 -49.842   2.545  1.00 57.63           O  
ANISOU 2958  O   GLY D  51     8252   9135   4509     40   -490  -1081       O  
ATOM   2959  N   PRO D  52      17.267 -51.091   3.394  1.00 53.25           N  
ANISOU 2959  N   PRO D  52     7890   8934   3411   -231   -859   -203       N  
ATOM   2960  CA  PRO D  52      16.397 -49.951   3.706  1.00 52.63           C  
ANISOU 2960  CA  PRO D  52     7830   8809   3357   -606   -522   -383       C  
ATOM   2961  C   PRO D  52      16.981 -49.047   4.787  1.00 53.85           C  
ANISOU 2961  C   PRO D  52     7789   8620   4053  -1105     54   -699       C  
ATOM   2962  O   PRO D  52      17.488 -49.532   5.801  1.00 53.85           O  
ANISOU 2962  O   PRO D  52     7955   8551   3954  -1372   -285   -937       O  
ATOM   2963  CB  PRO D  52      15.103 -50.616   4.185  1.00 52.20           C  
ANISOU 2963  CB  PRO D  52     7790   8905   3138   -320   -657    -29       C  
ATOM   2964  CG  PRO D  52      15.517 -51.970   4.647  1.00 52.02           C  
ANISOU 2964  CG  PRO D  52     7814   8846   3104   -245   -885    -16       C  
ATOM   2965  CD  PRO D  52      16.644 -52.377   3.750  1.00 51.77           C  
ANISOU 2965  CD  PRO D  52     7833   8835   3002   -304  -1067     26       C  
ATOM   2966  N   GLY D  53      16.906 -47.740   4.565  1.00 53.46           N  
ANISOU 2966  N   GLY D  53     7418   8453   4441  -1234    603   -838       N  
ATOM   2967  CA  GLY D  53      17.445 -46.783   5.512  1.00 53.01           C  
ANISOU 2967  CA  GLY D  53     7204   8271   4667  -1182   1101   -956       C  
ATOM   2968  C   GLY D  53      16.405 -46.285   6.493  1.00 53.36           C  
ANISOU 2968  C   GLY D  53     7226   8137   4912   -978   1466   -641       C  
ATOM   2969  O   GLY D  53      15.205 -46.466   6.290  1.00 55.21           O  
ANISOU 2969  O   GLY D  53     7294   8102   5580   -710   1926   -565       O  
ATOM   2970  N   SER D  54      16.867 -45.656   7.566  1.00 51.12           N  
ANISOU 2970  N   SER D  54     7027   8092   4303   -889   1343   -144       N  
ATOM   2971  CA  SER D  54      15.958 -45.082   8.548  1.00 49.65           C  
ANISOU 2971  CA  SER D  54     6909   7962   3993   -884   1046    -98       C  
ATOM   2972  C   SER D  54      15.251 -43.868   7.956  1.00 45.60           C  
ANISOU 2972  C   SER D  54     6482   7559   3285  -1145    831    109       C  
ATOM   2973  O   SER D  54      15.768 -43.226   7.039  1.00 42.87           O  
ANISOU 2973  O   SER D  54     6481   7128   2680  -1412    317    386       O  
ATOM   2974  CB  SER D  54      16.709 -44.691   9.818  1.00 51.06           C  
ANISOU 2974  CB  SER D  54     6954   8194   4252   -872    454   -138       C  
ATOM   2975  OG  SER D  54      17.615 -43.636   9.553  1.00 53.09           O  
ANISOU 2975  OG  SER D  54     7097   8441   4633   -815    300   -287       O  
ATOM   2976  N   VAL D  55      14.074 -43.556   8.489  1.00 45.00           N  
ANISOU 2976  N   VAL D  55     6020   7548   3530  -1515    693   -223       N  
ATOM   2977  CA  VAL D  55      13.256 -42.466   7.970  1.00 43.96           C  
ANISOU 2977  CA  VAL D  55     5703   7450   3551  -1765    748   -849       C  
ATOM   2978  C   VAL D  55      13.973 -41.118   8.098  1.00 43.93           C  
ANISOU 2978  C   VAL D  55     5816   7534   3341  -1558    672  -1459       C  
ATOM   2979  O   VAL D  55      13.687 -40.182   7.352  1.00 42.59           O  
ANISOU 2979  O   VAL D  55     5569   7420   3192  -1721    514  -1612       O  
ATOM   2980  CB  VAL D  55      11.879 -42.411   8.690  1.00 45.86           C  
ANISOU 2980  CB  VAL D  55     6044   7465   3916  -1594   1284   -826       C  
ATOM   2981  CG1 VAL D  55      12.035 -41.931  10.126  1.00 45.49           C  
ANISOU 2981  CG1 VAL D  55     6116   7305   3861  -1764   1571   -837       C  
ATOM   2982  CG2 VAL D  55      10.897 -41.534   7.921  1.00 46.20           C  
ANISOU 2982  CG2 VAL D  55     6033   7472   4050  -1596   1043  -1074       C  
ATOM   2983  N   ASP D  56      14.924 -41.023   9.022  1.00 43.10           N  
ANISOU 2983  N   ASP D  56     5729   7646   3000  -1568    -76  -1837       N  
ATOM   2984  CA  ASP D  56      15.658 -39.774   9.194  1.00 46.25           C  
ANISOU 2984  CA  ASP D  56     6214   7866   3493  -1706   -216  -2187       C  
ATOM   2985  C   ASP D  56      16.978 -39.784   8.422  1.00 48.01           C  
ANISOU 2985  C   ASP D  56     6315   8085   3839  -2009    292  -2512       C  
ATOM   2986  O   ASP D  56      17.855 -38.969   8.681  1.00 52.03           O  
ANISOU 2986  O   ASP D  56     6729   8407   4633  -2247    876  -2739       O  
ATOM   2987  CB  ASP D  56      15.904 -39.490  10.682  1.00 52.02           C  
ANISOU 2987  CB  ASP D  56     7175   8533   4058  -1818     44  -2497       C  
ATOM   2988  CG  ASP D  56      16.726 -40.568  11.360  1.00 56.83           C  
ANISOU 2988  CG  ASP D  56     7991   8999   4603  -1798    220  -2627       C  
ATOM   2989  OD1 ASP D  56      16.817 -41.687  10.813  1.00 59.78           O  
ANISOU 2989  OD1 ASP D  56     8409   9200   5106  -1593    508  -2387       O  
ATOM   2990  OD2 ASP D  56      17.277 -40.297  12.448  1.00 58.05           O  
ANISOU 2990  OD2 ASP D  56     8185   9166   4704  -1809    242  -2767       O  
ATOM   2991  N   SER D  57      17.108 -40.699   7.463  1.00 47.64           N  
ANISOU 2991  N   SER D  57     6406   8082   3614  -1780    936  -2406       N  
ATOM   2992  CA  SER D  57      18.300 -40.745   6.614  1.00 51.17           C  
ANISOU 2992  CA  SER D  57     6969   8256   4217  -1861   1663  -2141       C  
ATOM   2993  C   SER D  57      18.336 -39.562   5.658  1.00 53.62           C  
ANISOU 2993  C   SER D  57     7492   8380   4502  -1785   2120  -2026       C  
ATOM   2994  O   SER D  57      17.301 -39.137   5.145  1.00 55.26           O  
ANISOU 2994  O   SER D  57     7531   8623   4842  -1696   2426  -1909       O  
ATOM   2995  CB  SER D  57      18.362 -42.050   5.813  1.00 53.03           C  
ANISOU 2995  CB  SER D  57     7196   8245   4707  -2001   1671  -2088       C  
ATOM   2996  OG  SER D  57      18.656 -43.157   6.646  1.00 54.99           O  
ANISOU 2996  OG  SER D  57     7495   8223   5178  -2013   1567  -2049       O  
ATOM   2997  N   VAL D  58      19.533 -39.043   5.409  1.00 53.32           N  
ANISOU 2997  N   VAL D  58     7801   8135   4323  -2205   2090  -2065       N  
ATOM   2998  CA  VAL D  58      19.702 -37.919   4.500  1.00 56.46           C  
ANISOU 2998  CA  VAL D  58     8408   8115   4928  -2482   2206  -1982       C  
ATOM   2999  C   VAL D  58      20.784 -38.249   3.467  1.00 53.81           C  
ANISOU 2999  C   VAL D  58     8257   7681   4506  -2826   1928  -2000       C  
ATOM   3000  O   VAL D  58      21.583 -39.162   3.670  1.00 50.60           O  
ANISOU 3000  O   VAL D  58     7994   7177   4053  -2865   1910  -2153       O  
ATOM   3001  CB  VAL D  58      20.061 -36.623   5.277  1.00 61.63           C  
ANISOU 3001  CB  VAL D  58     9097   8399   5920  -2503   2741  -1816       C  
ATOM   3002  CG1 VAL D  58      21.510 -36.654   5.747  1.00 62.52           C  
ANISOU 3002  CG1 VAL D  58     9333   8416   6004  -2656   2644  -1995       C  
ATOM   3003  CG2 VAL D  58      19.783 -35.382   4.436  1.00 64.43           C  
ANISOU 3003  CG2 VAL D  58     9401   8596   6484  -2477   3003  -1770       C  
ATOM   3004  N   LEU D  59      20.783 -37.530   2.347  1.00 54.56           N  
ANISOU 3004  N   LEU D  59     8389   7666   4676  -2851   1771  -1992       N  
ATOM   3005  CA  LEU D  59      21.852 -37.638   1.359  1.00 55.76           C  
ANISOU 3005  CA  LEU D  59     8556   7554   5075  -2685   1487  -1970       C  
ATOM   3006  C   LEU D  59      23.185 -37.189   1.937  1.00 53.97           C  
ANISOU 3006  C   LEU D  59     8100   7307   5098  -3240   1209  -1873       C  
ATOM   3007  O   LEU D  59      23.287 -36.099   2.502  1.00 56.31           O  
ANISOU 3007  O   LEU D  59     8418   7339   5638  -3153   1517  -1526       O  
ATOM   3008  CB  LEU D  59      21.528 -36.800   0.121  1.00 57.65           C  
ANISOU 3008  CB  LEU D  59     8853   7526   5525  -2384   1518  -1950       C  
ATOM   3009  CG  LEU D  59      20.594 -37.409  -0.922  1.00 58.41           C  
ANISOU 3009  CG  LEU D  59     9055   7549   5588  -2284   1098  -2236       C  
ATOM   3010  CD1 LEU D  59      20.110 -36.336  -1.881  1.00 59.66           C  
ANISOU 3010  CD1 LEU D  59     9183   7540   5946  -2392   1043  -2088       C  
ATOM   3011  CD2 LEU D  59      21.312 -38.516  -1.679  1.00 57.32           C  
ANISOU 3011  CD2 LEU D  59     9058   7433   5290  -1986   1232  -2726       C  
ATOM   3012  N   PHE D  60      24.206 -38.029   1.805  1.00 49.96           N  
ANISOU 3012  N   PHE D  60     7540   6999   4445  -3693   1168  -2030       N  
ATOM   3013  CA  PHE D  60      25.555 -37.635   2.207  1.00 48.43           C  
ANISOU 3013  CA  PHE D  60     7185   6989   4228  -3780    770  -1691       C  
ATOM   3014  C   PHE D  60      26.281 -37.035   1.015  1.00 46.65           C  
ANISOU 3014  C   PHE D  60     7264   6563   3900  -3457   1123  -1782       C  
ATOM   3015  O   PHE D  60      26.947 -36.011   1.121  1.00 47.83           O  
ANISOU 3015  O   PHE D  60     7446   6739   3988  -3337   1545  -1628       O  
ATOM   3016  CB  PHE D  60      26.352 -38.824   2.745  1.00 48.97           C  
ANISOU 3016  CB  PHE D  60     7193   7420   3993  -3770    263  -1413       C  
ATOM   3017  CG  PHE D  60      25.967 -39.245   4.131  1.00 49.71           C  
ANISOU 3017  CG  PHE D  60     7424   7641   3821  -3437   -120  -1456       C  
ATOM   3018  CD1 PHE D  60      25.111 -38.472   4.898  1.00 50.01           C  
ANISOU 3018  CD1 PHE D  60     7549   7773   3681  -3354   -321  -1295       C  
ATOM   3019  CD2 PHE D  60      26.476 -40.414   4.672  1.00 50.15           C  
ANISOU 3019  CD2 PHE D  60     7782   7704   3570  -3326     17  -1435       C  
ATOM   3020  CE1 PHE D  60      24.762 -38.866   6.176  1.00 51.63           C  
ANISOU 3020  CE1 PHE D  60     7986   7922   3708  -3422    -47  -1359       C  
ATOM   3021  CE2 PHE D  60      26.133 -40.809   5.949  1.00 51.57           C  
ANISOU 3021  CE2 PHE D  60     8106   7887   3602  -3246    364  -1313       C  
ATOM   3022  CZ  PHE D  60      25.277 -40.034   6.701  1.00 51.52           C  
ANISOU 3022  CZ  PHE D  60     8153   7880   3541  -3400    121  -1403       C  
ATOM   3023  N   GLY D  61      26.140 -37.691  -0.128  1.00 43.71           N  
ANISOU 3023  N   GLY D  61     6888   6035   3684  -3079   1004  -1797       N  
ATOM   3024  CA  GLY D  61      26.837 -37.276  -1.325  1.00 41.76           C  
ANISOU 3024  CA  GLY D  61     6579   5764   3525  -3141   1039  -1625       C  
ATOM   3025  C   GLY D  61      26.999 -38.431  -2.287  1.00 41.00           C  
ANISOU 3025  C   GLY D  61     6510   5874   3194  -3351    792  -1243       C  
ATOM   3026  O   GLY D  61      26.402 -39.494  -2.104  1.00 39.16           O  
ANISOU 3026  O   GLY D  61     6574   5661   2643  -3376    460   -676       O  
ATOM   3027  N   SER D  62      27.819 -38.225  -3.310  1.00 41.60           N  
ANISOU 3027  N   SER D  62     6370   6096   3342  -3339    973  -1312       N  
ATOM   3028  CA  SER D  62      27.964 -39.201  -4.378  1.00 40.48           C  
ANISOU 3028  CA  SER D  62     5912   6259   3211  -3341    283   -968       C  
ATOM   3029  C   SER D  62      29.411 -39.646  -4.543  1.00 39.61           C  
ANISOU 3029  C   SER D  62     5242   6469   3339  -3302     50   -663       C  
ATOM   3030  O   SER D  62      30.332 -39.011  -4.023  1.00 41.51           O  
ANISOU 3030  O   SER D  62     5664   6527   3579  -3494     67   -689       O  
ATOM   3031  CB  SER D  62      27.444 -38.616  -5.692  1.00 43.25           C  
ANISOU 3031  CB  SER D  62     6289   6419   3724  -2970    370   -656       C  
ATOM   3032  OG  SER D  62      28.132 -37.412  -6.003  1.00 46.59           O  
ANISOU 3032  OG  SER D  62     6637   6640   4425  -2316    569   -138       O  
ATOM   3033  N   LEU D  63      29.597 -40.732  -5.284  1.00 39.03           N  
ANISOU 3033  N   LEU D  63     4701   6493   3636  -3197     97   -464       N  
ATOM   3034  CA  LEU D  63      30.921 -41.277  -5.591  1.00 36.50           C  
ANISOU 3034  CA  LEU D  63     4125   6554   3190  -2745   -551    -92       C  
ATOM   3035  C   LEU D  63      30.893 -42.085  -6.889  1.00 36.78           C  
ANISOU 3035  C   LEU D  63     4345   6599   3032  -2989     77    310       C  
ATOM   3036  O   LEU D  63      29.959 -42.848  -7.114  1.00 37.56           O  
ANISOU 3036  O   LEU D  63     4452   6210   3608  -3067    -93    111       O  
ATOM   3037  CB  LEU D  63      31.399 -42.170  -4.459  1.00 37.87           C  
ANISOU 3037  CB  LEU D  63     4121   6964   3303  -2554   -478    573       C  
ATOM   3038  CG  LEU D  63      32.747 -42.858  -4.672  1.00 39.45           C  
ANISOU 3038  CG  LEU D  63     4016   7184   3789  -2532   -213    624       C  
ATOM   3039  CD1 LEU D  63      33.883 -41.841  -4.663  1.00 42.16           C  
ANISOU 3039  CD1 LEU D  63     4559   7322   4137  -2385    387    678       C  
ATOM   3040  CD2 LEU D  63      32.963 -43.910  -3.599  1.00 40.30           C  
ANISOU 3040  CD2 LEU D  63     4278   7160   3876  -2398   -129    800       C  
ATOM   3041  N   ARG D  64      31.913 -41.936  -7.730  1.00 37.59           N  
ANISOU 3041  N   ARG D  64     4248   6804   3231  -2777    192    425       N  
ATOM   3042  CA  ARG D  64      32.025 -42.752  -8.938  1.00 36.43           C  
ANISOU 3042  CA  ARG D  64     4162   6629   3050  -2864   -222    601       C  
ATOM   3043  C   ARG D  64      33.064 -43.868  -8.742  1.00 36.30           C  
ANISOU 3043  C   ARG D  64     3670   6674   3449  -2515   -849    588       C  
ATOM   3044  O   ARG D  64      34.089 -43.659  -8.104  1.00 41.41           O  
ANISOU 3044  O   ARG D  64     4330   7383   4022  -2343  -1090    429       O  
ATOM   3045  CB  ARG D  64      32.380 -41.872 -10.147  1.00 37.46           C  
ANISOU 3045  CB  ARG D  64     4545   6623   3068  -2633   -404    701       C  
ATOM   3046  CG  ARG D  64      32.395 -42.611 -11.484  1.00 41.05           C  
ANISOU 3046  CG  ARG D  64     5220   6729   3651  -1902   -488   1601       C  
ATOM   3047  CD  ARG D  64      32.547 -41.648 -12.653  1.00 45.72           C  
ANISOU 3047  CD  ARG D  64     6096   6896   4380  -1306      6   1938       C  
ATOM   3048  NE  ARG D  64      32.942 -42.321 -13.890  1.00 49.29           N  
ANISOU 3048  NE  ARG D  64     6819   6863   5046  -1184    304   1725       N  
ATOM   3049  CZ  ARG D  64      32.166 -42.440 -14.964  1.00 52.57           C  
ANISOU 3049  CZ  ARG D  64     7289   6800   5886  -1679   1154   1215       C  
ATOM   3050  NH1 ARG D  64      30.938 -41.936 -14.960  1.00 51.63           N  
ANISOU 3050  NH1 ARG D  64     6782   6851   5984  -2419   1256    802       N  
ATOM   3051  NH2 ARG D  64      32.620 -43.060 -16.048  1.00 54.79           N  
ANISOU 3051  NH2 ARG D  64     7905   6666   6246  -1539   1769   1430       N  
ATOM   3052  N   GLY D  65      32.777 -45.055  -9.275  1.00 36.84           N  
ANISOU 3052  N   GLY D  65     3698   6909   3392  -2484   -416    963       N  
ATOM   3053  CA  GLY D  65      33.666 -46.207  -9.178  1.00 35.20           C  
ANISOU 3053  CA  GLY D  65     3076   6936   3363  -2151   -730   1129       C  
ATOM   3054  C   GLY D  65      33.482 -47.168 -10.351  1.00 36.40           C  
ANISOU 3054  C   GLY D  65     2916   7440   3475  -1940   -621   1668       C  
ATOM   3055  O   GLY D  65      33.000 -46.761 -11.407  1.00 37.21           O  
ANISOU 3055  O   GLY D  65     3059   7752   3326  -2018   -747   1817       O  
ATOM   3056  N   HIS D  66      33.851 -48.438 -10.169  1.00 36.93           N  
ANISOU 3056  N   HIS D  66     2763   7293   3977  -1585   -256   1953       N  
ATOM   3057  CA  HIS D  66      33.774 -49.444 -11.240  1.00 37.88           C  
ANISOU 3057  CA  HIS D  66     2776   7461   4155  -1295    145   1959       C  
ATOM   3058  C   HIS D  66      33.344 -50.854 -10.793  1.00 37.32           C  
ANISOU 3058  C   HIS D  66     2901   7536   3743   -829    264   2019       C  
ATOM   3059  O   HIS D  66      33.751 -51.334  -9.728  1.00 39.77           O  
ANISOU 3059  O   HIS D  66     3316   8021   3773   -719    176   1853       O  
ATOM   3060  CB  HIS D  66      35.129 -49.564 -11.940  1.00 40.80           C  
ANISOU 3060  CB  HIS D  66     3093   7522   4889  -1258    477   2174       C  
ATOM   3061  CG  HIS D  66      35.595 -48.296 -12.577  1.00 46.19           C  
ANISOU 3061  CG  HIS D  66     3814   7817   5920  -1330   1056   2035       C  
ATOM   3062  ND1 HIS D  66      35.217 -47.922 -13.848  1.00 48.77           N  
ANISOU 3062  ND1 HIS D  66     4299   7948   6284  -1532   1404   1852       N  
ATOM   3063  CD2 HIS D  66      36.399 -47.311 -12.117  1.00 49.07           C  
ANISOU 3063  CD2 HIS D  66     4287   7970   6388  -1368   1193   1893       C  
ATOM   3064  CE1 HIS D  66      35.773 -46.762 -14.146  1.00 51.13           C  
ANISOU 3064  CE1 HIS D  66     4750   8052   6625  -1742   1284   1514       C  
ATOM   3065  NE2 HIS D  66      36.498 -46.371 -13.113  1.00 52.48           N  
ANISOU 3065  NE2 HIS D  66     5118   8117   6706  -1467   1533   1648       N  
ATOM   3066  N   VAL D  67      32.537 -51.511 -11.627  1.00 35.15           N  
ANISOU 3066  N   VAL D  67     2251   7161   3944   -623    213   1831       N  
ATOM   3067  CA  VAL D  67      32.207 -52.931 -11.464  1.00 31.76           C  
ANISOU 3067  CA  VAL D  67     1931   6754   3380    -90     58   1930       C  
ATOM   3068  C   VAL D  67      33.158 -53.782 -12.305  1.00 33.44           C  
ANISOU 3068  C   VAL D  67     2074   7174   3457    405    166   1764       C  
ATOM   3069  O   VAL D  67      33.326 -53.528 -13.499  1.00 33.26           O  
ANISOU 3069  O   VAL D  67     2263   7080   3295    649    510   1695       O  
ATOM   3070  CB  VAL D  67      30.753 -53.254 -11.896  1.00 31.69           C  
ANISOU 3070  CB  VAL D  67     2120   6439   3483   -276    346   1874       C  
ATOM   3071  CG1 VAL D  67      30.406 -54.705 -11.550  1.00 30.06           C  
ANISOU 3071  CG1 VAL D  67     1867   6074   3483    -53     53   2242       C  
ATOM   3072  CG2 VAL D  67      29.765 -52.300 -11.246  1.00 31.80           C  
ANISOU 3072  CG2 VAL D  67     2248   6442   3394   -380     -6   1576       C  
ATOM   3073  N   VAL D  68      33.770 -54.791 -11.692  1.00 36.44           N  
ANISOU 3073  N   VAL D  68     2433   7257   4156    900    760   2103       N  
ATOM   3074  CA  VAL D  68      34.738 -55.633 -12.397  1.00 38.03           C  
ANISOU 3074  CA  VAL D  68     2421   7470   4557    889    611   2276       C  
ATOM   3075  C   VAL D  68      34.333 -57.104 -12.398  1.00 37.50           C  
ANISOU 3075  C   VAL D  68     2716   7195   4338   1380    670   2716       C  
ATOM   3076  O   VAL D  68      33.331 -57.489 -11.785  1.00 37.42           O  
ANISOU 3076  O   VAL D  68     3000   6955   4262   1595   1145   2721       O  
ATOM   3077  CB  VAL D  68      36.156 -55.504 -11.790  1.00 39.83           C  
ANISOU 3077  CB  VAL D  68     2524   7896   4713    327    567   2302       C  
ATOM   3078  CG1 VAL D  68      36.623 -54.057 -11.844  1.00 40.30           C  
ANISOU 3078  CG1 VAL D  68     2296   8008   5008    117    290   2000       C  
ATOM   3079  CG2 VAL D  68      36.182 -56.035 -10.358  1.00 39.12           C  
ANISOU 3079  CG2 VAL D  68     2457   8042   4363    328    525   2277       C  
ATOM   3080  N   GLY D  69      35.110 -57.920 -13.103  1.00 39.96           N  
ANISOU 3080  N   GLY D  69     3284   7232   4666   1524    915   2555       N  
ATOM   3081  CA  GLY D  69      34.871 -59.352 -13.173  1.00 37.95           C  
ANISOU 3081  CA  GLY D  69     3251   6406   4763   1926   1081   2636       C  
ATOM   3082  C   GLY D  69      33.678 -59.740 -14.028  1.00 37.16           C  
ANISOU 3082  C   GLY D  69     3528   5862   4728   2079   1593   2617       C  
ATOM   3083  O   GLY D  69      33.141 -60.834 -13.898  1.00 38.30           O  
ANISOU 3083  O   GLY D  69     3841   5770   4943   2234   1719   2649       O  
ATOM   3084  N   LEU D  70      33.260 -58.840 -14.911  1.00 33.80           N  
ANISOU 3084  N   LEU D  70     3157   5462   4224   1798   1321   2595       N  
ATOM   3085  CA  LEU D  70      32.058 -59.058 -15.714  1.00 33.25           C  
ANISOU 3085  CA  LEU D  70     2925   5175   4533   1671   1314   2332       C  
ATOM   3086  C   LEU D  70      32.070 -60.343 -16.538  1.00 35.39           C  
ANISOU 3086  C   LEU D  70     3292   5048   5107   1829   1547   2345       C  
ATOM   3087  O   LEU D  70      31.025 -60.940 -16.766  1.00 36.75           O  
ANISOU 3087  O   LEU D  70     3641   4869   5455   2037   1461   2038       O  
ATOM   3088  CB  LEU D  70      31.825 -57.872 -16.650  1.00 31.04           C  
ANISOU 3088  CB  LEU D  70     2592   4860   4342   1366   1261   2161       C  
ATOM   3089  CG  LEU D  70      31.734 -56.496 -16.000  1.00 29.52           C  
ANISOU 3089  CG  LEU D  70     2258   4954   4003   1198    640   1965       C  
ATOM   3090  CD1 LEU D  70      31.502 -55.446 -17.067  1.00 27.55           C  
ANISOU 3090  CD1 LEU D  70     2131   4534   3803   1099    365   1886       C  
ATOM   3091  CD2 LEU D  70      30.620 -56.466 -14.960  1.00 29.28           C  
ANISOU 3091  CD2 LEU D  70     2305   5059   3760   1137    985   2230       C  
ATOM   3092  N   ARG D  71      33.243 -60.780 -16.983  1.00 38.59           N  
ANISOU 3092  N   ARG D  71     3557   5328   5777   1830   1909   2578       N  
ATOM   3093  CA  ARG D  71      33.293 -61.941 -17.865  1.00 40.51           C  
ANISOU 3093  CA  ARG D  71     3710   5445   6237   1862   2030   2614       C  
ATOM   3094  C   ARG D  71      32.972 -63.254 -17.138  1.00 40.52           C  
ANISOU 3094  C   ARG D  71     4034   5152   6210   1992   2235   2486       C  
ATOM   3095  O   ARG D  71      32.729 -64.267 -17.784  1.00 42.75           O  
ANISOU 3095  O   ARG D  71     4910   4931   6401   1803   2628   2270       O  
ATOM   3096  CB  ARG D  71      34.663 -62.036 -18.547  1.00 45.35           C  
ANISOU 3096  CB  ARG D  71     4017   6228   6984   1621   2196   2793       C  
ATOM   3097  CG  ARG D  71      35.810 -62.431 -17.643  1.00 50.02           C  
ANISOU 3097  CG  ARG D  71     4499   6981   7524   1297   2504   2630       C  
ATOM   3098  CD  ARG D  71      37.139 -62.181 -18.353  1.00 55.13           C  
ANISOU 3098  CD  ARG D  71     5243   7620   8084   1637   2574   2384       C  
ATOM   3099  NE  ARG D  71      38.172 -63.127 -17.954  1.00 59.89           N  
ANISOU 3099  NE  ARG D  71     6041   8137   8577   1615   2528   2136       N  
ATOM   3100  CZ  ARG D  71      38.588 -64.141 -18.706  1.00 62.08           C  
ANISOU 3100  CZ  ARG D  71     6502   8276   8809   1837   2181   1926       C  
ATOM   3101  NH1 ARG D  71      38.060 -64.343 -19.906  1.00 62.66           N  
ANISOU 3101  NH1 ARG D  71     6615   8383   8810   1815   1823   1836       N  
ATOM   3102  NH2 ARG D  71      39.537 -64.951 -18.261  1.00 62.77           N  
ANISOU 3102  NH2 ARG D  71     6549   8330   8969   1936   2068   1890       N  
ATOM   3103  N   TYR D  72      32.939 -63.225 -15.806  1.00 38.77           N  
ANISOU 3103  N   TYR D  72     3795   5150   5788   1972   1864   2722       N  
ATOM   3104  CA  TYR D  72      32.741 -64.437 -15.014  1.00 40.12           C  
ANISOU 3104  CA  TYR D  72     3782   5446   6017   2005   1861   2738       C  
ATOM   3105  C   TYR D  72      31.294 -64.640 -14.544  1.00 41.67           C  
ANISOU 3105  C   TYR D  72     4371   5237   6223   2187   2195   2787       C  
ATOM   3106  O   TYR D  72      30.998 -65.588 -13.813  1.00 44.37           O  
ANISOU 3106  O   TYR D  72     4826   5349   6683   2399   2325   2669       O  
ATOM   3107  CB  TYR D  72      33.687 -64.420 -13.805  1.00 40.41           C  
ANISOU 3107  CB  TYR D  72     3763   5691   5899   2005   1785   2983       C  
ATOM   3108  CG  TYR D  72      35.142 -64.228 -14.188  1.00 42.98           C  
ANISOU 3108  CG  TYR D  72     3808   6231   6292   2065   1788   3085       C  
ATOM   3109  CD1 TYR D  72      35.858 -65.251 -14.789  1.00 46.52           C  
ANISOU 3109  CD1 TYR D  72     4281   6729   6666   2260   1944   2945       C  
ATOM   3110  CD2 TYR D  72      35.796 -63.024 -13.950  1.00 44.58           C  
ANISOU 3110  CD2 TYR D  72     3970   6578   6391   2247   1758   2974       C  
ATOM   3111  CE1 TYR D  72      37.189 -65.080 -15.148  1.00 47.58           C  
ANISOU 3111  CE1 TYR D  72     4182   7031   6866   2231   2167   2666       C  
ATOM   3112  CE2 TYR D  72      37.131 -62.842 -14.308  1.00 47.07           C  
ANISOU 3112  CE2 TYR D  72     4194   6984   6707   2332   1784   2981       C  
ATOM   3113  CZ  TYR D  72      37.823 -63.874 -14.907  1.00 49.50           C  
ANISOU 3113  CZ  TYR D  72     4508   7324   6975   2431   2307   2641       C  
ATOM   3114  OH  TYR D  72      39.154 -63.705 -15.271  1.00 53.39           O  
ANISOU 3114  OH  TYR D  72     5409   7623   7254   2691   2937   2759       O  
ATOM   3115  N   TYR D  73      30.393 -63.757 -14.970  1.00 39.73           N  
ANISOU 3115  N   TYR D  73     4250   4847   5998   2151   1701   2376       N  
ATOM   3116  CA  TYR D  73      28.999 -63.821 -14.526  1.00 40.78           C  
ANISOU 3116  CA  TYR D  73     4332   4728   6434   1912   2338   2301       C  
ATOM   3117  C   TYR D  73      28.048 -63.552 -15.687  1.00 39.92           C  
ANISOU 3117  C   TYR D  73     4392   4155   6621   1920   2229   1797       C  
ATOM   3118  O   TYR D  73      28.426 -62.908 -16.660  1.00 41.26           O  
ANISOU 3118  O   TYR D  73     4452   4454   6771   1768   2189   1932       O  
ATOM   3119  CB  TYR D  73      28.761 -62.830 -13.382  1.00 42.10           C  
ANISOU 3119  CB  TYR D  73     4281   5458   6256   1999   2197   2820       C  
ATOM   3120  CG  TYR D  73      29.770 -63.005 -12.272  1.00 42.85           C  
ANISOU 3120  CG  TYR D  73     4103   6055   6122   2066   1726   3246       C  
ATOM   3121  CD1 TYR D  73      29.606 -63.992 -11.308  1.00 42.62           C  
ANISOU 3121  CD1 TYR D  73     4156   6245   5795   1895   1642   3385       C  
ATOM   3122  CD2 TYR D  73      30.903 -62.207 -12.207  1.00 42.79           C  
ANISOU 3122  CD2 TYR D  73     3869   6469   5919   2026   1665   3364       C  
ATOM   3123  CE1 TYR D  73      30.545 -64.173 -10.300  1.00 43.56           C  
ANISOU 3123  CE1 TYR D  73     3986   6681   5885   1889   1443   3369       C  
ATOM   3124  CE2 TYR D  73      31.845 -62.378 -11.207  1.00 42.06           C  
ANISOU 3124  CE2 TYR D  73     3678   6735   5569   1958   1555   3421       C  
ATOM   3125  CZ  TYR D  73      31.659 -63.362 -10.255  1.00 44.41           C  
ANISOU 3125  CZ  TYR D  73     3940   6959   5976   1839   1550   3555       C  
ATOM   3126  OH  TYR D  73      32.595 -63.528  -9.261  1.00 45.54           O  
ANISOU 3126  OH  TYR D  73     3669   7263   6372   1816   1325   3742       O  
ATOM   3127  N   THR D  74      26.823 -64.058 -15.597  1.00 39.33           N  
ANISOU 3127  N   THR D  74     4465   3658   6820   1708   2283   1436       N  
ATOM   3128  CA  THR D  74      25.881 -63.930 -16.705  1.00 39.10           C  
ANISOU 3128  CA  THR D  74     4507   3358   6990   1467   2239   1333       C  
ATOM   3129  C   THR D  74      24.758 -62.916 -16.446  1.00 34.51           C  
ANISOU 3129  C   THR D  74     4123   2637   6351   1145   1944   1233       C  
ATOM   3130  O   THR D  74      23.903 -62.708 -17.305  1.00 33.80           O  
ANISOU 3130  O   THR D  74     4007   2613   6221   1166   1913   1071       O  
ATOM   3131  CB  THR D  74      25.236 -65.286 -17.056  1.00 43.12           C  
ANISOU 3131  CB  THR D  74     5377   3397   7608   1672   2379   1243       C  
ATOM   3132  OG1 THR D  74      24.385 -65.713 -15.986  1.00 45.23           O  
ANISOU 3132  OG1 THR D  74     5932   3059   8197   1048   2436   1553       O  
ATOM   3133  CG2 THR D  74      26.307 -66.341 -17.304  1.00 44.39           C  
ANISOU 3133  CG2 THR D  74     5725   3489   7654   1872   2156   1007       C  
ATOM   3134  N   GLY D  75      24.750 -62.298 -15.268  1.00 29.55           N  
ANISOU 3134  N   GLY D  75     3329   2321   5576    984   1260   1182       N  
ATOM   3135  CA  GLY D  75      23.750 -61.284 -14.962  1.00 26.25           C  
ANISOU 3135  CA  GLY D  75     3076   2116   4779    808    669   1292       C  
ATOM   3136  C   GLY D  75      23.848 -60.123 -15.934  1.00 24.49           C  
ANISOU 3136  C   GLY D  75     2593   2014   4700    474    809   1347       C  
ATOM   3137  O   GLY D  75      24.954 -59.707 -16.312  1.00 27.50           O  
ANISOU 3137  O   GLY D  75     2757   2559   5133    574    853   1609       O  
ATOM   3138  N   VAL D  76      22.690 -59.607 -16.339  1.00 20.95           N  
ANISOU 3138  N   VAL D  76     2963   1308   3687    360    807    691       N  
ATOM   3139  CA  VAL D  76      22.620 -58.504 -17.286  1.00 18.76           C  
ANISOU 3139  CA  VAL D  76     2647   1365   3117    388    610    388       C  
ATOM   3140  C   VAL D  76      22.169 -57.227 -16.589  1.00 17.57           C  
ANISOU 3140  C   VAL D  76     2284   1602   2788    280    409    231       C  
ATOM   3141  O   VAL D  76      21.253 -57.253 -15.772  1.00 18.65           O  
ANISOU 3141  O   VAL D  76     2549   1632   2904    197    946    393       O  
ATOM   3142  CB  VAL D  76      21.667 -58.838 -18.443  1.00 21.62           C  
ANISOU 3142  CB  VAL D  76     3456   1595   3163    386    531     36       C  
ATOM   3143  CG1 VAL D  76      21.500 -57.643 -19.376  1.00 21.55           C  
ANISOU 3143  CG1 VAL D  76     3590   1743   2853    330    -24    244       C  
ATOM   3144  CG2 VAL D  76      22.188 -60.057 -19.215  1.00 25.40           C  
ANISOU 3144  CG2 VAL D  76     4278   1934   3438    234    852   -425       C  
ATOM   3145  N   VAL D  77      22.822 -56.116 -16.913  1.00 17.00           N  
ANISOU 3145  N   VAL D  77     2385   1350   2723    381    339    183       N  
ATOM   3146  CA  VAL D  77      22.380 -54.803 -16.453  1.00 15.92           C  
ANISOU 3146  CA  VAL D  77     1992   1545   2511    198     92    688       C  
ATOM   3147  C   VAL D  77      22.327 -53.880 -17.670  1.00 15.56           C  
ANISOU 3147  C   VAL D  77     1809   1607   2497    457    -59    755       C  
ATOM   3148  O   VAL D  77      23.016 -54.130 -18.673  1.00 17.30           O  
ANISOU 3148  O   VAL D  77     2092   1821   2661    136    395    485       O  
ATOM   3149  CB  VAL D  77      23.309 -54.248 -15.331  1.00 18.57           C  
ANISOU 3149  CB  VAL D  77     2288   1994   2773    234     63    200       C  
ATOM   3150  CG1 VAL D  77      24.749 -54.134 -15.805  1.00 20.11           C  
ANISOU 3150  CG1 VAL D  77     2085   2431   3126    213     83     56       C  
ATOM   3151  CG2 VAL D  77      22.810 -52.914 -14.777  1.00 20.67           C  
ANISOU 3151  CG2 VAL D  77     3014   1987   2855    408    -56    369       C  
ATOM   3152  N   ASN D  78      21.482 -52.852 -17.600  1.00 14.71           N  
ANISOU 3152  N   ASN D  78     1723   1583   2282    429    -23    566       N  
ATOM   3153  CA  ASN D  78      21.408 -51.827 -18.633  1.00 14.52           C  
ANISOU 3153  CA  ASN D  78     1907   1657   1953     81   -309    279       C  
ATOM   3154  C   ASN D  78      21.700 -50.476 -18.014  1.00 13.78           C  
ANISOU 3154  C   ASN D  78     2046   1451   1739    168    323    314       C  
ATOM   3155  O   ASN D  78      21.553 -50.302 -16.799  1.00 14.10           O  
ANISOU 3155  O   ASN D  78     2320   1453   1585     88    236    355       O  
ATOM   3156  CB  ASN D  78      20.034 -51.830 -19.311  1.00 14.46           C  
ANISOU 3156  CB  ASN D  78     2294   1442   1757    228    -58    -38       C  
ATOM   3157  CG  ASN D  78      19.686 -53.190 -19.888  1.00 15.31           C  
ANISOU 3157  CG  ASN D  78     2656   1562   1601      6    340    -18       C  
ATOM   3158  OD1 ASN D  78      20.248 -53.602 -20.901  1.00 16.80           O  
ANISOU 3158  OD1 ASN D  78     2867   1666   1851    222    294    108       O  
ATOM   3159  ND2 ASN D  78      18.769 -53.900 -19.234  1.00 18.08           N  
ANISOU 3159  ND2 ASN D  78     2480   2354   2034    -24    227    312       N  
ATOM   3160  N   ASN D  79      22.119 -49.525 -18.843  1.00 14.17           N  
ANISOU 3160  N   ASN D  79     2062   1393   1930    -61   -268    150       N  
ATOM   3161  CA  ASN D  79      22.402 -48.181 -18.360  1.00 12.30           C  
ANISOU 3161  CA  ASN D  79     2040   1010   1622     49    125    267       C  
ATOM   3162  C   ASN D  79      21.184 -47.566 -17.671  1.00 14.97           C  
ANISOU 3162  C   ASN D  79     2257   1604   1826    255    492    451       C  
ATOM   3163  O   ASN D  79      20.037 -47.807 -18.081  1.00 15.80           O  
ANISOU 3163  O   ASN D  79     2275   1548   2182    224    286    239       O  
ATOM   3164  CB  ASN D  79      22.847 -47.267 -19.510  1.00 14.57           C  
ANISOU 3164  CB  ASN D  79     2103   1676   1757    144    438    430       C  
ATOM   3165  CG  ASN D  79      24.128 -47.738 -20.171  1.00 15.03           C  
ANISOU 3165  CG  ASN D  79     1987   1716   2008    182    117    211       C  
ATOM   3166  OD1 ASN D  79      24.929 -48.466 -19.567  1.00 15.95           O  
ANISOU 3166  OD1 ASN D  79     2019   1873   2168     39    275    539       O  
ATOM   3167  ND2 ASN D  79      24.334 -47.320 -21.425  1.00 15.64           N  
ANISOU 3167  ND2 ASN D  79     2316   1731   1895     10    242    123       N  
ATOM   3168  N   ASN D  80      21.461 -46.779 -16.633  1.00 15.19           N  
ANISOU 3168  N   ASN D  80     2577   1597   1599    -63    333    454       N  
ATOM   3169  CA  ASN D  80      20.456 -46.103 -15.787  1.00 14.87           C  
ANISOU 3169  CA  ASN D  80     2542   1769   1337    171    477    716       C  
ATOM   3170  C   ASN D  80      19.712 -47.046 -14.843  1.00 13.77           C  
ANISOU 3170  C   ASN D  80     2049   1478   1705    118    442    225       C  
ATOM   3171  O   ASN D  80      18.789 -46.613 -14.157  1.00 16.56           O  
ANISOU 3171  O   ASN D  80     2610   1758   1925    198    571    163       O  
ATOM   3172  CB  ASN D  80      19.435 -45.323 -16.633  1.00 14.04           C  
ANISOU 3172  CB  ASN D  80     2117   1389   1828    -47    192    522       C  
ATOM   3173  CG  ASN D  80      20.047 -44.100 -17.289  1.00 16.84           C  
ANISOU 3173  CG  ASN D  80     2561   1535   2302    -38     -3    663       C  
ATOM   3174  OD1 ASN D  80      21.027 -43.532 -16.788  1.00 18.60           O  
ANISOU 3174  OD1 ASN D  80     2637   1755   2674   -163    -27    349       O  
ATOM   3175  ND2 ASN D  80      19.487 -43.698 -18.426  1.00 19.48           N  
ANISOU 3175  ND2 ASN D  80     3106   1905   2392    -38    178    769       N  
ATOM   3176  N   GLU D  81      20.114 -48.321 -14.788  1.00 12.98           N  
ANISOU 3176  N   GLU D  81     2065   1057   1809    -51    141    311       N  
ATOM   3177  CA  GLU D  81      19.528 -49.241 -13.816  1.00 13.20           C  
ANISOU 3177  CA  GLU D  81     2306   1134   1575    -55     75    417       C  
ATOM   3178  C   GLU D  81      20.253 -49.205 -12.470  1.00 15.40           C  
ANISOU 3178  C   GLU D  81     2569   1543   1738     31     67    345       C  
ATOM   3179  O   GLU D  81      21.483 -49.082 -12.408  1.00 16.32           O  
ANISOU 3179  O   GLU D  81     2523   1697   1980   -259    114    388       O  
ATOM   3180  CB  GLU D  81      19.535 -50.684 -14.331  1.00 13.60           C  
ANISOU 3180  CB  GLU D  81     2402   1023   1741     17    344    585       C  
ATOM   3181  CG  GLU D  81      18.623 -50.899 -15.531  1.00 14.74           C  
ANISOU 3181  CG  GLU D  81     2535   1435   1628   -271     17      2       C  
ATOM   3182  CD  GLU D  81      18.484 -52.361 -15.926  1.00 15.31           C  
ANISOU 3182  CD  GLU D  81     2396   1576   1847     37     99     91       C  
ATOM   3183  OE1 GLU D  81      19.206 -53.221 -15.355  1.00 16.63           O  
ANISOU 3183  OE1 GLU D  81     2014   2085   2221    124    168    174       O  
ATOM   3184  OE2 GLU D  81      17.629 -52.643 -16.808  1.00 17.84           O  
ANISOU 3184  OE2 GLU D  81     2697   1967   2117     76    227   -171       O  
ATOM   3185  N   MET D  82      19.470 -49.317 -11.402  1.00 14.53           N  
ANISOU 3185  N   MET D  82     2396   1657   1469     31     18    284       N  
ATOM   3186  CA  MET D  82      19.990 -49.702 -10.095  1.00 16.59           C  
ANISOU 3186  CA  MET D  82     2330   2196   1776   -187    -74    441       C  
ATOM   3187  C   MET D  82      20.723 -51.013 -10.160  1.00 17.74           C  
ANISOU 3187  C   MET D  82     2435   2123   2182   -179    -73    795       C  
ATOM   3188  O   MET D  82      20.323 -51.917 -10.896  1.00 18.10           O  
ANISOU 3188  O   MET D  82     2589   1978   2311   -268   -395    544       O  
ATOM   3189  CB  MET D  82      18.863 -49.904  -9.086  1.00 21.67           C  
ANISOU 3189  CB  MET D  82     2775   3320   2136   -105    434    160       C  
ATOM   3190  CG  MET D  82      18.319 -48.692  -8.478  1.00 26.78           C  
ANISOU 3190  CG  MET D  82     3624   3315   3236   -223    628    -91       C  
ATOM   3191  SD  MET D  82      17.300 -49.150  -7.071  1.00 26.57           S  
ANISOU 3191  SD  MET D  82     4470   2645   2981    188   1031    148       S  
ATOM   3192  CE  MET D  82      16.043 -50.126  -7.886  1.00 21.20           C  
ANISOU 3192  CE  MET D  82     3394   2059   2602   -256    832   -119       C  
ATOM   3193  N   VAL D  83      21.745 -51.140  -9.328  1.00 17.99           N  
ANISOU 3193  N   VAL D  83     2380   2229   2228   -201   -160    809       N  
ATOM   3194  CA  VAL D  83      22.318 -52.438  -9.038  1.00 19.01           C  
ANISOU 3194  CA  VAL D  83     2320   2748   2155   -414   -491    843       C  
ATOM   3195  C   VAL D  83      22.366 -52.585  -7.528  1.00 21.79           C  
ANISOU 3195  C   VAL D  83     2766   3300   2214     -3   -382   1016       C  
ATOM   3196  O   VAL D  83      22.326 -51.587  -6.798  1.00 23.57           O  
ANISOU 3196  O   VAL D  83     3558   3478   1918     69   -230    666       O  
ATOM   3197  CB  VAL D  83      23.723 -52.612  -9.651  1.00 20.51           C  
ANISOU 3197  CB  VAL D  83     2498   2890   2405   -532   -532    242       C  
ATOM   3198  CG1 VAL D  83      23.635 -52.679 -11.181  1.00 20.72           C  
ANISOU 3198  CG1 VAL D  83     3081   2355   2435   -374    -54    397       C  
ATOM   3199  CG2 VAL D  83      24.649 -51.499  -9.191  1.00 22.83           C  
ANISOU 3199  CG2 VAL D  83     2402   3007   3268   -557   -396    362       C  
ATOM   3200  N   ALA D  84      22.443 -53.824  -7.056  1.00 22.12           N  
ANISOU 3200  N   ALA D  84     2401   3635   2371    -93   -243   1660       N  
ATOM   3201  CA  ALA D  84      22.536 -54.077  -5.629  1.00 25.20           C  
ANISOU 3201  CA  ALA D  84     2289   4484   2801    162     72   1832       C  
ATOM   3202  C   ALA D  84      23.988 -54.281  -5.227  1.00 25.79           C  
ANISOU 3202  C   ALA D  84     1828   5087   2883     45   -163   2012       C  
ATOM   3203  O   ALA D  84      24.718 -55.017  -5.894  1.00 27.52           O  
ANISOU 3203  O   ALA D  84     2010   5140   3307    304    -46   1851       O  
ATOM   3204  CB  ALA D  84      21.719 -55.289  -5.255  1.00 26.26           C  
ANISOU 3204  CB  ALA D  84     2136   4566   3277     88    305   2069       C  
ATOM   3205  N   LEU D  85      24.407 -53.629  -4.142  1.00 28.08           N  
ANISOU 3205  N   LEU D  85     1959   5719   2991   -367   -224   1921       N  
ATOM   3206  CA  LEU D  85      25.706 -53.897  -3.539  1.00 31.12           C  
ANISOU 3206  CA  LEU D  85     2523   6187   3115   -363    -26   2193       C  
ATOM   3207  C   LEU D  85      25.515 -54.839  -2.369  1.00 32.60           C  
ANISOU 3207  C   LEU D  85     2587   6546   3254     87   -196   2339       C  
ATOM   3208  O   LEU D  85      24.774 -54.541  -1.431  1.00 34.55           O  
ANISOU 3208  O   LEU D  85     2990   6683   3455    334    232   2265       O  
ATOM   3209  CB  LEU D  85      26.384 -52.610  -3.074  1.00 33.62           C  
ANISOU 3209  CB  LEU D  85     2750   6599   3426  -1183    103   1805       C  
ATOM   3210  CG  LEU D  85      26.632 -51.513  -4.112  1.00 39.73           C  
ANISOU 3210  CG  LEU D  85     3830   6967   4299  -1470   1233   1208       C  
ATOM   3211  CD1 LEU D  85      27.669 -50.545  -3.583  1.00 41.75           C  
ANISOU 3211  CD1 LEU D  85     4244   7109   4509  -1190   1038   1191       C  
ATOM   3212  CD2 LEU D  85      27.056 -52.096  -5.445  1.00 41.52           C  
ANISOU 3212  CD2 LEU D  85     4274   7047   4455  -1942   1469    953       C  
ATOM   3213  N   GLN D  86      26.173 -55.987  -2.432  1.00 34.28           N  
ANISOU 3213  N   GLN D  86     2685   6727   3613    278     55   2659       N  
ATOM   3214  CA  GLN D  86      25.957 -57.032  -1.444  1.00 37.64           C  
ANISOU 3214  CA  GLN D  86     3023   7014   4264    302    363   2960       C  
ATOM   3215  C   GLN D  86      27.293 -57.518  -0.905  1.00 37.92           C  
ANISOU 3215  C   GLN D  86     2936   7298   4174    263    -86   2996       C  
ATOM   3216  O   GLN D  86      28.101 -58.051  -1.661  1.00 36.89           O  
ANISOU 3216  O   GLN D  86     2782   6979   4256    481     99   3013       O  
ATOM   3217  CB  GLN D  86      25.176 -58.195  -2.062  1.00 36.86           C  
ANISOU 3217  CB  GLN D  86     3159   6573   4272    480    461   3008       C  
ATOM   3218  CG  GLN D  86      24.819 -59.297  -1.068  1.00 36.63           C  
ANISOU 3218  CG  GLN D  86     3405   6269   4243    681    571   2943       C  
ATOM   3219  CD  GLN D  86      24.080 -60.457  -1.711  1.00 38.23           C  
ANISOU 3219  CD  GLN D  86     3602   6385   4540    887    670   3089       C  
ATOM   3220  OE1 GLN D  86      24.390 -60.868  -2.828  1.00 40.29           O  
ANISOU 3220  OE1 GLN D  86     4083   6243   4981   1002    597   3231       O  
ATOM   3221  NE2 GLN D  86      23.096 -60.996  -1.000  1.00 39.91           N  
ANISOU 3221  NE2 GLN D  86     3710   6617   4839    847   1014   2750       N  
ATOM   3222  N   ARG D  87      27.522 -57.340   0.398  1.00 39.87           N  
ANISOU 3222  N   ARG D  87     2974   7947   4226   -222     18   3106       N  
ATOM   3223  CA  ARG D  87      28.761 -57.807   1.015  1.00 42.79           C  
ANISOU 3223  CA  ARG D  87     3337   8527   4393    -57    -85   3187       C  
ATOM   3224  C   ARG D  87      28.852 -59.322   0.930  1.00 46.94           C  
ANISOU 3224  C   ARG D  87     3896   8804   5133    590     15   3668       C  
ATOM   3225  O   ARG D  87      27.853 -60.022   1.088  1.00 45.57           O  
ANISOU 3225  O   ARG D  87     3827   8248   5239    540     95   3701       O  
ATOM   3226  CB  ARG D  87      28.858 -57.364   2.481  1.00 42.40           C  
ANISOU 3226  CB  ARG D  87     3476   8708   3926   -322   -587   2738       C  
ATOM   3227  CG  ARG D  87      29.259 -55.909   2.670  1.00 43.61           C  
ANISOU 3227  CG  ARG D  87     3851   8853   3867   -600   -488   2349       C  
ATOM   3228  CD  ARG D  87      30.770 -55.714   2.540  1.00 44.36           C  
ANISOU 3228  CD  ARG D  87     4270   8800   3784   -348   -689   2530       C  
ATOM   3229  NE  ARG D  87      31.481 -56.139   3.742  1.00 45.39           N  
ANISOU 3229  NE  ARG D  87     4813   8714   3718   -160   -791   2537       N  
ATOM   3230  CZ  ARG D  87      32.289 -57.193   3.807  1.00 47.52           C  
ANISOU 3230  CZ  ARG D  87     5175   9033   3850    222  -1018   2388       C  
ATOM   3231  NH1 ARG D  87      32.501 -57.938   2.732  1.00 47.37           N  
ANISOU 3231  NH1 ARG D  87     5167   9126   3703    173  -1083   2200       N  
ATOM   3232  NH2 ARG D  87      32.888 -57.502   4.953  1.00 48.65           N  
ANISOU 3232  NH2 ARG D  87     5229   9158   4097    389  -1292   2317       N  
ATOM   3233  N   ASP D  88      30.052 -59.818   0.653  1.00 51.63           N  
ANISOU 3233  N   ASP D  88     4444   9549   5623   1038    -36   3859       N  
ATOM   3234  CA  ASP D  88      30.300 -61.252   0.649  1.00 56.35           C  
ANISOU 3234  CA  ASP D  88     4981  10224   6207   1439     91   4178       C  
ATOM   3235  C   ASP D  88      31.545 -61.553   1.477  1.00 57.78           C  
ANISOU 3235  C   ASP D  88     5105  10614   6234   1587     49   4088       C  
ATOM   3236  O   ASP D  88      32.621 -61.802   0.935  1.00 55.99           O  
ANISOU 3236  O   ASP D  88     4885  10390   5997   1678   -204   3715       O  
ATOM   3237  CB  ASP D  88      30.449 -61.774  -0.781  1.00 59.56           C  
ANISOU 3237  CB  ASP D  88     5518  10523   6591   1536    153   4454       C  
ATOM   3238  CG  ASP D  88      30.547 -63.288  -0.844  1.00 63.95           C  
ANISOU 3238  CG  ASP D  88     6165  10979   7152   1420    528   4801       C  
ATOM   3239  OD1 ASP D  88      30.357 -63.946   0.201  1.00 67.02           O  
ANISOU 3239  OD1 ASP D  88     6473  11289   7703   1250    876   4746       O  
ATOM   3240  OD2 ASP D  88      30.810 -63.822  -1.943  1.00 64.38           O  
ANISOU 3240  OD2 ASP D  88     6405  10823   7233   1567    463   4950       O  
ATOM   3241  N   PRO D  89      31.394 -61.529   2.807  1.00 58.66           N  
ANISOU 3241  N   PRO D  89     5369  10571   6347   1524    -87   4199       N  
ATOM   3242  CA  PRO D  89      32.526 -61.738   3.714  1.00 62.41           C  
ANISOU 3242  CA  PRO D  89     5688  11288   6735   1781    -35   4409       C  
ATOM   3243  C   PRO D  89      33.100 -63.149   3.605  1.00 66.94           C  
ANISOU 3243  C   PRO D  89     6057  12086   7291   2110    103   4525       C  
ATOM   3244  O   PRO D  89      34.253 -63.371   3.976  1.00 66.74           O  
ANISOU 3244  O   PRO D  89     5992  12117   7249   2214   -296   4320       O  
ATOM   3245  CB  PRO D  89      31.914 -61.494   5.096  1.00 61.21           C  
ANISOU 3245  CB  PRO D  89     5691  11005   6563   1516    -21   4438       C  
ATOM   3246  CG  PRO D  89      30.466 -61.802   4.925  1.00 59.86           C  
ANISOU 3246  CG  PRO D  89     5620  10706   6418   1284      9   4434       C  
ATOM   3247  CD  PRO D  89      30.123 -61.358   3.533  1.00 58.52           C  
ANISOU 3247  CD  PRO D  89     5473  10430   6333   1326   -155   4252       C  
ATOM   3248  N   ASN D  90      32.307 -64.084   3.088  1.00 69.90           N  
ANISOU 3248  N   ASN D  90     6294  12524   7741   2262    402   4735       N  
ATOM   3249  CA  ASN D  90      32.752 -65.467   2.935  1.00 72.44           C  
ANISOU 3249  CA  ASN D  90     6544  12825   8156   2431    706   4886       C  
ATOM   3250  C   ASN D  90      33.583 -65.696   1.673  1.00 72.88           C  
ANISOU 3250  C   ASN D  90     6665  12780   8248   2766    535   4917       C  
ATOM   3251  O   ASN D  90      33.983 -66.824   1.386  1.00 74.75           O  
ANISOU 3251  O   ASN D  90     7017  12963   8421   2824    755   4961       O  
ATOM   3252  CB  ASN D  90      31.548 -66.411   2.933  1.00 74.23           C  
ANISOU 3252  CB  ASN D  90     6666  13099   8438   2217   1031   4914       C  
ATOM   3253  CG  ASN D  90      30.903 -66.537   4.301  1.00 75.69           C  
ANISOU 3253  CG  ASN D  90     6855  13307   8598   2269   1183   4993       C  
ATOM   3254  OD1 ASN D  90      31.584 -66.489   5.326  1.00 75.88           O  
ANISOU 3254  OD1 ASN D  90     6940  13268   8623   2331   1320   5155       O  
ATOM   3255  ND2 ASN D  90      29.583 -66.700   4.323  1.00 76.49           N  
ANISOU 3255  ND2 ASN D  90     6917  13455   8691   2127   1267   4859       N  
ATOM   3256  N   ASN D  91      33.836 -64.626   0.922  1.00 70.66           N  
ANISOU 3256  N   ASN D  91     6334  12476   8039   2815    104   4631       N  
ATOM   3257  CA  ASN D  91      34.648 -64.715  -0.287  1.00 68.17           C  
ANISOU 3257  CA  ASN D  91     6139  12077   7685   2763    -66   4280       C  
ATOM   3258  C   ASN D  91      36.079 -65.126   0.043  1.00 69.06           C  
ANISOU 3258  C   ASN D  91     6288  12151   7802   2942     46   4301       C  
ATOM   3259  O   ASN D  91      36.778 -64.428   0.781  1.00 66.77           O  
ANISOU 3259  O   ASN D  91     6328  11590   7454   2741   -361   4003       O  
ATOM   3260  CB  ASN D  91      34.642 -63.382  -1.037  1.00 66.45           C  
ANISOU 3260  CB  ASN D  91     5874  11877   7498   2676     -3   4152       C  
ATOM   3261  CG  ASN D  91      35.293 -63.476  -2.405  1.00 63.99           C  
ANISOU 3261  CG  ASN D  91     5744  11431   7138   2622     37   3999       C  
ATOM   3262  OD1 ASN D  91      36.505 -63.659  -2.517  1.00 62.68           O  
ANISOU 3262  OD1 ASN D  91     5844  11033   6938   2625   -124   3840       O  
ATOM   3263  ND2 ASN D  91      34.489 -63.327  -3.456  1.00 61.73           N  
ANISOU 3263  ND2 ASN D  91     5544  10973   6937   2456    -58   3908       N  
ATOM   3264  N   PRO D  92      36.519 -66.264  -0.516  1.00 69.93           N  
ANISOU 3264  N   PRO D  92     6386  12287   7898   3073    184   4403       N  
ATOM   3265  CA  PRO D  92      37.838 -66.847  -0.244  1.00 71.40           C  
ANISOU 3265  CA  PRO D  92     6367  12470   8292   3129    396   4327       C  
ATOM   3266  C   PRO D  92      39.014 -66.044  -0.807  1.00 70.99           C  
ANISOU 3266  C   PRO D  92     6215  12460   8299   3045    100   4065       C  
ATOM   3267  O   PRO D  92      40.159 -66.438  -0.588  1.00 70.10           O  
ANISOU 3267  O   PRO D  92     6196  12155   8285   3164   -172   3976       O  
ATOM   3268  CB  PRO D  92      37.754 -68.220  -0.921  1.00 71.53           C  
ANISOU 3268  CB  PRO D  92     6473  12463   8241   3200    549   4482       C  
ATOM   3269  CG  PRO D  92      36.737 -68.052  -1.989  1.00 71.45           C  
ANISOU 3269  CG  PRO D  92     6529  12509   8110   3089    559   4393       C  
ATOM   3270  CD  PRO D  92      35.723 -67.103  -1.428  1.00 70.20           C  
ANISOU 3270  CD  PRO D  92     6385  12397   7892   3107    344   4504       C  
ATOM   3271  N   TYR D  93      38.744 -64.945  -1.508  1.00 69.77           N  
ANISOU 3271  N   TYR D  93     6121  12522   7867   2873   -215   4093       N  
ATOM   3272  CA  TYR D  93      39.813 -64.141  -2.096  1.00 68.76           C  
ANISOU 3272  CA  TYR D  93     5889  12551   7685   2764   -384   3865       C  
ATOM   3273  C   TYR D  93      39.937 -62.758  -1.451  1.00 67.39           C  
ANISOU 3273  C   TYR D  93     5606  12503   7496   2610   -357   3763       C  
ATOM   3274  O   TYR D  93      41.013 -62.159  -1.456  1.00 68.93           O  
ANISOU 3274  O   TYR D  93     5625  12659   7907   2699    -65   3832       O  
ATOM   3275  CB  TYR D  93      39.597 -63.987  -3.606  1.00 71.04           C  
ANISOU 3275  CB  TYR D  93     5952  12922   8116   3007   -337   3810       C  
ATOM   3276  CG  TYR D  93      39.651 -65.290  -4.372  1.00 73.39           C  
ANISOU 3276  CG  TYR D  93     6150  13212   8524   3298   -139   3902       C  
ATOM   3277  CD1 TYR D  93      40.851 -65.770  -4.881  1.00 75.78           C  
ANISOU 3277  CD1 TYR D  93     6559  13413   8821   3264    230   3814       C  
ATOM   3278  CD2 TYR D  93      38.503 -66.039  -4.588  1.00 73.91           C  
ANISOU 3278  CD2 TYR D  93     6310  13268   8505   3353    -66   4082       C  
ATOM   3279  CE1 TYR D  93      40.904 -66.964  -5.583  1.00 76.54           C  
ANISOU 3279  CE1 TYR D  93     6657  13514   8909   3331    303   3893       C  
ATOM   3280  CE2 TYR D  93      38.544 -67.230  -5.288  1.00 74.65           C  
ANISOU 3280  CE2 TYR D  93     6361  13361   8640   3400     17   4137       C  
ATOM   3281  CZ  TYR D  93      39.745 -67.689  -5.782  1.00 76.36           C  
ANISOU 3281  CZ  TYR D  93     6660  13496   8857   3295    325   4002       C  
ATOM   3282  OH  TYR D  93      39.783 -68.877  -6.478  1.00 76.69           O  
ANISOU 3282  OH  TYR D  93     6789  13472   8879   3312    428   4129       O  
ATOM   3283  N   ASP D  94      38.837 -62.254  -0.902  1.00 64.43           N  
ANISOU 3283  N   ASP D  94     5305  12078   7098   2371   -500   3510       N  
ATOM   3284  CA  ASP D  94      38.817 -60.920  -0.309  1.00 63.52           C  
ANISOU 3284  CA  ASP D  94     5176  11990   6967   2184   -458   3612       C  
ATOM   3285  C   ASP D  94      37.702 -60.836   0.728  1.00 63.44           C  
ANISOU 3285  C   ASP D  94     5402  11847   6854   2158   -516   3592       C  
ATOM   3286  O   ASP D  94      36.530 -61.000   0.396  1.00 62.25           O  
ANISOU 3286  O   ASP D  94     5456  11371   6824   2224   -867   3269       O  
ATOM   3287  CB  ASP D  94      38.625 -59.854  -1.396  1.00 65.44           C  
ANISOU 3287  CB  ASP D  94     5002  12570   7293   2008    -64   3718       C  
ATOM   3288  CG  ASP D  94      38.799 -58.429  -0.876  1.00 67.23           C  
ANISOU 3288  CG  ASP D  94     4952  12985   7608   1889    262   3761       C  
ATOM   3289  OD1 ASP D  94      38.903 -58.232   0.354  1.00 67.31           O  
ANISOU 3289  OD1 ASP D  94     4689  13217   7670   1674    152   3462       O  
ATOM   3290  OD2 ASP D  94      38.823 -57.497  -1.710  1.00 67.50           O  
ANISOU 3290  OD2 ASP D  94     5038  13029   7580   2001    443   3885       O  
ATOM   3291  N   LYS D  95      38.065 -60.580   1.982  1.00 62.91           N  
ANISOU 3291  N   LYS D  95     5555  11788   6560   1931   -631   3715       N  
ATOM   3292  CA  LYS D  95      37.072 -60.514   3.049  1.00 63.77           C  
ANISOU 3292  CA  LYS D  95     5769  11987   6473   1743   -559   3958       C  
ATOM   3293  C   LYS D  95      36.216 -59.252   2.944  1.00 62.44           C  
ANISOU 3293  C   LYS D  95     5668  11922   6136   1376   -402   4040       C  
ATOM   3294  O   LYS D  95      35.148 -59.165   3.553  1.00 61.86           O  
ANISOU 3294  O   LYS D  95     5865  11927   5710   1231   -413   3886       O  
ATOM   3295  CB  LYS D  95      37.748 -60.589   4.426  1.00 65.41           C  
ANISOU 3295  CB  LYS D  95     5862  12206   6784   1838   -909   3761       C  
ATOM   3296  CG  LYS D  95      38.604 -59.384   4.784  1.00 67.53           C  
ANISOU 3296  CG  LYS D  95     6016  12550   7091   1979  -1010   3773       C  
ATOM   3297  CD  LYS D  95      39.133 -59.486   6.213  1.00 69.38           C  
ANISOU 3297  CD  LYS D  95     6086  12948   7326   2103   -968   3793       C  
ATOM   3298  CE  LYS D  95      39.945 -58.254   6.597  1.00 70.45           C  
ANISOU 3298  CE  LYS D  95     6117  13131   7519   2191   -952   3858       C  
ATOM   3299  NZ  LYS D  95      40.414 -58.307   8.014  1.00 71.21           N  
ANISOU 3299  NZ  LYS D  95     6235  13177   7647   2168   -753   3860       N  
ATOM   3300  N   ASN D  96      36.680 -58.283   2.160  1.00 60.56           N  
ANISOU 3300  N   ASN D  96     5282  11486   6244   1237   -438   4087       N  
ATOM   3301  CA  ASN D  96      35.946 -57.036   1.968  1.00 58.95           C  
ANISOU 3301  CA  ASN D  96     4807  11355   6237    993   -592   3895       C  
ATOM   3302  C   ASN D  96      35.086 -57.062   0.711  1.00 53.35           C  
ANISOU 3302  C   ASN D  96     4055  10433   5783    567   -407   3845       C  
ATOM   3303  O   ASN D  96      34.534 -56.034   0.318  1.00 53.59           O  
ANISOU 3303  O   ASN D  96     3563  10640   6161    234   -425   3808       O  
ATOM   3304  CB  ASN D  96      36.910 -55.849   1.894  1.00 61.16           C  
ANISOU 3304  CB  ASN D  96     4931  11749   6560    986   -971   3726       C  
ATOM   3305  CG  ASN D  96      37.788 -55.729   3.125  1.00 65.27           C  
ANISOU 3305  CG  ASN D  96     5272  12467   7059   1009   -874   3721       C  
ATOM   3306  OD1 ASN D  96      37.344 -55.972   4.247  1.00 68.03           O  
ANISOU 3306  OD1 ASN D  96     5677  12740   7431    939   -659   3539       O  
ATOM   3307  ND2 ASN D  96      39.043 -55.352   2.919  1.00 66.96           N  
ANISOU 3307  ND2 ASN D  96     5338  12740   7365   1264   -950   3696       N  
ATOM   3308  N   ALA D  97      34.982 -58.236   0.090  1.00 50.17           N  
ANISOU 3308  N   ALA D  97     3765   9960   5339    513   -244   3685       N  
ATOM   3309  CA  ALA D  97      34.316 -58.383  -1.205  1.00 49.21           C  
ANISOU 3309  CA  ALA D  97     3423   9722   5552    914    269   3872       C  
ATOM   3310  C   ALA D  97      32.897 -57.847  -1.206  1.00 46.87           C  
ANISOU 3310  C   ALA D  97     3244   9455   5108    623     98   3616       C  
ATOM   3311  O   ALA D  97      32.120 -58.083  -0.280  1.00 47.84           O  
ANISOU 3311  O   ALA D  97     3451   9490   5234    665   -128   3522       O  
ATOM   3312  CB  ALA D  97      34.309 -59.840  -1.636  1.00 50.83           C  
ANISOU 3312  CB  ALA D  97     3381   9973   5960   1000    751   3954       C  
ATOM   3313  N   ILE D  98      32.571 -57.116  -2.264  1.00 42.87           N  
ANISOU 3313  N   ILE D  98     3128   8718   4442    399   -140   3128       N  
ATOM   3314  CA  ILE D  98      31.220 -56.622  -2.461  1.00 40.52           C  
ANISOU 3314  CA  ILE D  98     2827   8306   4263    247   -118   2870       C  
ATOM   3315  C   ILE D  98      30.723 -57.043  -3.838  1.00 38.10           C  
ANISOU 3315  C   ILE D  98     2500   7973   4004    125     24   2949       C  
ATOM   3316  O   ILE D  98      31.227 -56.577  -4.860  1.00 38.51           O  
ANISOU 3316  O   ILE D  98     2427   8095   4112     21    -10   2837       O  
ATOM   3317  CB  ILE D  98      31.156 -55.091  -2.292  1.00 38.80           C  
ANISOU 3317  CB  ILE D  98     2884   8192   3664    -67   -302   2611       C  
ATOM   3318  CG1 ILE D  98      31.627 -54.720  -0.876  1.00 39.87           C  
ANISOU 3318  CG1 ILE D  98     3314   8274   3559    -30    -63   2642       C  
ATOM   3319  CG2 ILE D  98      29.750 -54.577  -2.559  1.00 39.68           C  
ANISOU 3319  CG2 ILE D  98     2844   8539   3694    -91   -231   2594       C  
ATOM   3320  CD1 ILE D  98      31.659 -53.235  -0.592  1.00 41.30           C  
ANISOU 3320  CD1 ILE D  98     3169   8441   4081    305     88   2752       C  
ATOM   3321  N   LYS D  99      29.751 -57.953  -3.851  1.00 37.58           N  
ANISOU 3321  N   LYS D  99     2464   7710   4105    310   -111   2678       N  
ATOM   3322  CA  LYS D  99      29.093 -58.381  -5.083  1.00 36.73           C  
ANISOU 3322  CA  LYS D  99     2660   6959   4338    703    247   2931       C  
ATOM   3323  C   LYS D  99      28.231 -57.268  -5.649  1.00 33.55           C  
ANISOU 3323  C   LYS D  99     2364   6307   4074    545    -32   2596       C  
ATOM   3324  O   LYS D  99      27.671 -56.470  -4.899  1.00 34.13           O  
ANISOU 3324  O   LYS D  99     2602   6379   3988    211     92   2859       O  
ATOM   3325  CB  LYS D  99      28.212 -59.612  -4.843  1.00 38.09           C  
ANISOU 3325  CB  LYS D  99     3106   6581   4785   1094    621   3188       C  
ATOM   3326  CG  LYS D  99      28.960 -60.834  -4.342  1.00 39.18           C  
ANISOU 3326  CG  LYS D  99     3391   6442   5054   1250    502   3159       C  
ATOM   3327  CD  LYS D  99      28.008 -61.871  -3.766  1.00 44.76           C  
ANISOU 3327  CD  LYS D  99     4365   6846   5795   1093    779   3110       C  
ATOM   3328  CE  LYS D  99      26.985 -62.345  -4.786  1.00 47.85           C  
ANISOU 3328  CE  LYS D  99     5098   6986   6096    933   1391   3171       C  
ATOM   3329  NZ  LYS D  99      26.055 -63.346  -4.179  1.00 49.34           N  
ANISOU 3329  NZ  LYS D  99     5488   7004   6255    952   1744   3522       N  
ATOM   3330  N   VAL D 100      28.130 -57.229  -6.972  1.00 30.77           N  
ANISOU 3330  N   VAL D 100     2100   5762   3829    489     86   2493       N  
ATOM   3331  CA  VAL D 100      27.178 -56.356  -7.647  1.00 29.02           C  
ANISOU 3331  CA  VAL D 100     1985   5482   3558    286    109   2496       C  
ATOM   3332  C   VAL D 100      26.167 -57.219  -8.384  1.00 27.90           C  
ANISOU 3332  C   VAL D 100     1854   5229   3518    396    324   2275       C  
ATOM   3333  O   VAL D 100      26.541 -58.001  -9.259  1.00 28.93           O  
ANISOU 3333  O   VAL D 100     2068   5441   3483    687    566   2076       O  
ATOM   3334  CB  VAL D 100      27.862 -55.414  -8.640  1.00 29.11           C  
ANISOU 3334  CB  VAL D 100     2050   5752   3257     11   -154   2312       C  
ATOM   3335  CG1 VAL D 100      26.815 -54.579  -9.360  1.00 28.43           C  
ANISOU 3335  CG1 VAL D 100     2150   5150   3504    118    -53   2429       C  
ATOM   3336  CG2 VAL D 100      28.876 -54.534  -7.920  1.00 30.66           C  
ANISOU 3336  CG2 VAL D 100     2307   6144   3198    277   -211   2157       C  
ATOM   3337  N   ASN D 101      24.895 -57.094  -8.008  1.00 24.94           N  
ANISOU 3337  N   ASN D 101     1664   4393   3421    254    359   2130       N  
ATOM   3338  CA  ASN D 101      23.827 -57.855  -8.638  1.00 23.38           C  
ANISOU 3338  CA  ASN D 101     1826   3820   3239    300    530   1971       C  
ATOM   3339  C   ASN D 101      22.890 -56.930  -9.368  1.00 20.73           C  
ANISOU 3339  C   ASN D 101     1821   2821   3234    -66    130   1737       C  
ATOM   3340  O   ASN D 101      22.774 -55.764  -8.997  1.00 23.35           O  
ANISOU 3340  O   ASN D 101     2268   2776   3827    -41    244   1552       O  
ATOM   3341  CB  ASN D 101      23.021 -58.645  -7.597  1.00 24.44           C  
ANISOU 3341  CB  ASN D 101     1995   3792   3498    617    630   2132       C  
ATOM   3342  CG  ASN D 101      23.899 -59.493  -6.683  1.00 27.81           C  
ANISOU 3342  CG  ASN D 101     2491   4130   3944   1150   1050   2297       C  
ATOM   3343  OD1 ASN D 101      24.863 -60.129  -7.126  1.00 31.30           O  
ANISOU 3343  OD1 ASN D 101     2884   4506   4502   1487   1489   2519       O  
ATOM   3344  ND2 ASN D 101      23.562 -59.507  -5.398  1.00 30.03           N  
ANISOU 3344  ND2 ASN D 101     3209   4338   3863   1425   1423   2070       N  
ATOM   3345  N   ASN D 102      22.194 -57.436 -10.384  1.00 19.80           N  
ANISOU 3345  N   ASN D 102     1870   2602   3053    -29    348   1187       N  
ATOM   3346  CA  ASN D 102      21.137 -56.635 -10.981  1.00 18.03           C  
ANISOU 3346  CA  ASN D 102     2062   2114   2672    122    205    843       C  
ATOM   3347  C   ASN D 102      19.911 -56.652 -10.063  1.00 16.58           C  
ANISOU 3347  C   ASN D 102     2109   1647   2542    189    320   1085       C  
ATOM   3348  O   ASN D 102      19.913 -57.311  -9.011  1.00 18.30           O  
ANISOU 3348  O   ASN D 102     2068   2086   2798     73    341    919       O  
ATOM   3349  CB  ASN D 102      20.797 -57.101 -12.412  1.00 19.56           C  
ANISOU 3349  CB  ASN D 102     2688   1816   2926     40    769    464       C  
ATOM   3350  CG  ASN D 102      20.215 -58.509 -12.479  1.00 21.40           C  
ANISOU 3350  CG  ASN D 102     2927   1741   3461   -159   1298    522       C  
ATOM   3351  OD1 ASN D 102      19.714 -59.044 -11.498  1.00 20.96           O  
ANISOU 3351  OD1 ASN D 102     2750   1493   3721    -28   1246    680       O  
ATOM   3352  ND2 ASN D 102      20.259 -59.099 -13.672  1.00 20.47           N  
ANISOU 3352  ND2 ASN D 102     2838   1615   3326    141   1274    272       N  
ATOM   3353  N   VAL D 103      18.869 -55.923 -10.435  1.00 16.37           N  
ANISOU 3353  N   VAL D 103     2062   1589   2570    380    126    248       N  
ATOM   3354  CA AVAL D 103      17.728 -55.802  -9.521  0.64 17.17           C  
ANISOU 3354  CA AVAL D 103     2330   1472   2719    406   -384    758       C  
ATOM   3355  CA BVAL D 103      17.687 -55.775  -9.603  0.36 17.17           C  
ANISOU 3355  CA BVAL D 103     2209   1514   2802    410    195    561       C  
ATOM   3356  C   VAL D 103      16.976 -57.121  -9.378  1.00 16.97           C  
ANISOU 3356  C   VAL D 103     2347   1443   2657    109     87    653       C  
ATOM   3357  O   VAL D 103      16.315 -57.331  -8.362  1.00 18.49           O  
ANISOU 3357  O   VAL D 103     2719   1719   2587    160    602    699       O  
ATOM   3358  CB AVAL D 103      16.732 -54.697  -9.934  0.64 18.76           C  
ANISOU 3358  CB AVAL D 103     2790   1597   2743      6  -1110    541       C  
ATOM   3359  CB BVAL D 103      16.742 -54.747 -10.242  0.36 18.77           C  
ANISOU 3359  CB BVAL D 103     2492   1634   3006    324    638    331       C  
ATOM   3360  CG1AVAL D 103      17.365 -53.327  -9.729  0.64 21.46           C  
ANISOU 3360  CG1AVAL D 103     3016   1709   3429     34   -852    448       C  
ATOM   3361  CG1BVAL D 103      15.474 -54.637  -9.474  0.36 16.33           C  
ANISOU 3361  CG1BVAL D 103     1989   1354   2861    505    815    441       C  
ATOM   3362  CG2AVAL D 103      16.221 -54.903 -11.360  0.64 20.25           C  
ANISOU 3362  CG2AVAL D 103     2838   1847   3007    182   -822    569       C  
ATOM   3363  CG2BVAL D 103      17.429 -53.394 -10.302  0.36 21.33           C  
ANISOU 3363  CG2BVAL D 103     2612   2041   3450    219    598     42       C  
ATOM   3364  N   ASN D 104      17.110 -58.027 -10.352  1.00 16.99           N  
ANISOU 3364  N   ASN D 104     2253   1368   2835    182    255    473       N  
ATOM   3365  CA  ASN D 104      16.509 -59.363 -10.240  1.00 19.18           C  
ANISOU 3365  CA  ASN D 104     2750   1749   2788     77    426    468       C  
ATOM   3366  C   ASN D 104      17.304 -60.324  -9.345  1.00 19.11           C  
ANISOU 3366  C   ASN D 104     2533   1828   2899    253    864    411       C  
ATOM   3367  O   ASN D 104      16.852 -61.441  -9.051  1.00 21.42           O  
ANISOU 3367  O   ASN D 104     2832   2110   3196   -166    924    666       O  
ATOM   3368  CB  ASN D 104      16.338 -59.985 -11.624  1.00 21.08           C  
ANISOU 3368  CB  ASN D 104     3002   2025   2984   -189   -161    466       C  
ATOM   3369  CG  ASN D 104      15.215 -59.324 -12.427  1.00 33.53           C  
ANISOU 3369  CG  ASN D 104     4535   3461   4742   -366    669    463       C  
ATOM   3370  OD1 ASN D 104      14.281 -58.752 -11.859  1.00 37.57           O  
ANISOU 3370  OD1 ASN D 104     4637   3860   5776   -734    138    584       O  
ATOM   3371  ND2 ASN D 104      15.307 -59.401 -13.749  1.00 39.82           N  
ANISOU 3371  ND2 ASN D 104     5692   4277   5160   -128    724    284       N  
ATOM   3372  N   GLY D 105      18.480 -59.881  -8.913  1.00 19.92           N  
ANISOU 3372  N   GLY D 105     2272   1965   3333    651    657    894       N  
ATOM   3373  CA  GLY D 105      19.313 -60.640  -7.999  1.00 21.18           C  
ANISOU 3373  CA  GLY D 105     2177   2084   3786    479    892   1282       C  
ATOM   3374  C   GLY D 105      20.414 -61.457  -8.648  1.00 25.38           C  
ANISOU 3374  C   GLY D 105     2540   2493   4610    676   1317   1694       C  
ATOM   3375  O   GLY D 105      21.155 -62.149  -7.948  1.00 29.26           O  
ANISOU 3375  O   GLY D 105     3201   2976   4939    901   1213   2002       O  
ATOM   3376  N   ASN D 106      20.529 -61.383  -9.974  1.00 26.51           N  
ANISOU 3376  N   ASN D 106     2572   2364   5136    675   1771   1396       N  
ATOM   3377  CA  ASN D 106      21.598 -62.082 -10.693  1.00 26.02           C  
ANISOU 3377  CA  ASN D 106     2365   2235   5288    667   1508   1383       C  
ATOM   3378  C   ASN D 106      22.927 -61.353 -10.554  1.00 26.54           C  
ANISOU 3378  C   ASN D 106     2348   2712   5025    823   1485   1849       C  
ATOM   3379  O   ASN D 106      22.988 -60.149 -10.785  1.00 27.21           O  
ANISOU 3379  O   ASN D 106     2911   2742   4687    833   1087   1853       O  
ATOM   3380  CB  ASN D 106      21.272 -62.219 -12.185  1.00 30.34           C  
ANISOU 3380  CB  ASN D 106     3569   2271   5687    180   1964    776       C  
ATOM   3381  CG  ASN D 106      19.863 -62.700 -12.444  1.00 36.39           C  
ANISOU 3381  CG  ASN D 106     4736   2987   6105   -250   1937     37       C  
ATOM   3382  OD1 ASN D 106      19.100 -62.058 -13.172  1.00 37.92           O  
ANISOU 3382  OD1 ASN D 106     5222   2929   6258   -797   1680   -607       O  
ATOM   3383  ND2 ASN D 106      19.509 -63.834 -11.859  1.00 37.08           N  
ANISOU 3383  ND2 ASN D 106     4828   3012   6251   -903   1869   -119       N  
ATOM   3384  N   GLN D 107      23.997 -62.066 -10.209  1.00 30.57           N  
ANISOU 3384  N   GLN D 107     2890   3616   5110   1301   1662   2109       N  
ATOM   3385  CA  GLN D 107      25.289 -61.389 -10.070  1.00 30.38           C  
ANISOU 3385  CA  GLN D 107     2717   3991   4834   1284   1298   2349       C  
ATOM   3386  C   GLN D 107      25.821 -60.882 -11.416  1.00 31.62           C  
ANISOU 3386  C   GLN D 107     2896   3982   5137   1313   1581   2473       C  
ATOM   3387  O   GLN D 107      25.802 -61.593 -12.425  1.00 31.23           O  
ANISOU 3387  O   GLN D 107     2969   3689   5210   1282   1752   2349       O  
ATOM   3388  CB  GLN D 107      26.340 -62.295  -9.410  1.00 34.45           C  
ANISOU 3388  CB  GLN D 107     2995   4627   5469   1437   1218   2597       C  
ATOM   3389  CG  GLN D 107      27.604 -61.514  -9.071  1.00 35.23           C  
ANISOU 3389  CG  GLN D 107     2971   5332   5084   1434    804   2709       C  
ATOM   3390  CD  GLN D 107      28.577 -62.274  -8.199  1.00 40.11           C  
ANISOU 3390  CD  GLN D 107     3443   6129   5670   1837   1382   3105       C  
ATOM   3391  OE1 GLN D 107      28.336 -63.421  -7.827  1.00 43.48           O  
ANISOU 3391  OE1 GLN D 107     3959   6425   6137   2081   2032   3423       O  
ATOM   3392  NE2 GLN D 107      29.686 -61.627  -7.860  1.00 39.93           N  
ANISOU 3392  NE2 GLN D 107     3431   6401   5340   1735   1077   3152       N  
ATOM   3393  N   VAL D 108      26.274 -59.631 -11.416  1.00 29.80           N  
ANISOU 3393  N   VAL D 108     2630   4129   4566   1005   1087   2498       N  
ATOM   3394  CA  VAL D 108      26.872 -59.003 -12.588  1.00 28.44           C  
ANISOU 3394  CA  VAL D 108     2308   4004   4496   1052   1064   2377       C  
ATOM   3395  C   VAL D 108      28.401 -58.990 -12.472  1.00 29.80           C  
ANISOU 3395  C   VAL D 108     2562   4406   4355   1315   1226   2419       C  
ATOM   3396  O   VAL D 108      29.113 -59.217 -13.456  1.00 32.53           O  
ANISOU 3396  O   VAL D 108     2916   4550   4896   1448   1333   2526       O  
ATOM   3397  CB  VAL D 108      26.337 -57.573 -12.763  1.00 26.84           C  
ANISOU 3397  CB  VAL D 108     2013   3893   4293    879    972   1987       C  
ATOM   3398  CG1 VAL D 108      27.091 -56.836 -13.845  1.00 26.76           C  
ANISOU 3398  CG1 VAL D 108     2129   3858   4179    738    982   2100       C  
ATOM   3399  CG2 VAL D 108      24.840 -57.614 -13.077  1.00 27.03           C  
ANISOU 3399  CG2 VAL D 108     1738   4050   4482    592    677   1731       C  
ATOM   3400  N   GLY D 109      28.901 -58.749 -11.261  1.00 31.16           N  
ANISOU 3400  N   GLY D 109     2635   5065   4140   1347    840   2465       N  
ATOM   3401  CA  GLY D 109      30.335 -58.727 -11.012  1.00 34.16           C  
ANISOU 3401  CA  GLY D 109     2596   6098   4286   1268    835   2803       C  
ATOM   3402  C   GLY D 109      30.662 -58.387  -9.566  1.00 36.14           C  
ANISOU 3402  C   GLY D 109     2681   6922   4128   1228    692   2892       C  
ATOM   3403  O   GLY D 109      29.884 -58.705  -8.659  1.00 35.89           O  
ANISOU 3403  O   GLY D 109     2616   6752   4268   1224    833   2935       O  
ATOM   3404  N   HIS D 110      31.817 -57.754  -9.352  1.00 37.20           N  
ANISOU 3404  N   HIS D 110     2609   7374   4150   1184    621   2806       N  
ATOM   3405  CA  HIS D 110      32.246 -57.279  -8.033  1.00 36.91           C  
ANISOU 3405  CA  HIS D 110     2522   7471   4032   1019    352   2598       C  
ATOM   3406  C   HIS D 110      32.674 -55.816  -8.090  1.00 38.88           C  
ANISOU 3406  C   HIS D 110     2566   8030   4177    720    293   2944       C  
ATOM   3407  O   HIS D 110      33.047 -55.312  -9.152  1.00 38.48           O  
ANISOU 3407  O   HIS D 110     2452   8177   3989    202    102   2977       O  
ATOM   3408  CB  HIS D 110      33.435 -58.096  -7.498  1.00 37.58           C  
ANISOU 3408  CB  HIS D 110     2761   7428   4091   1338    424   2577       C  
ATOM   3409  CG  HIS D 110      33.080 -59.465  -7.009  1.00 39.40           C  
ANISOU 3409  CG  HIS D 110     3086   7574   4308   1461    555   2892       C  
ATOM   3410  ND1 HIS D 110      32.576 -59.697  -5.746  1.00 42.62           N  
ANISOU 3410  ND1 HIS D 110     3724   7882   4588   1886    538   2827       N  
ATOM   3411  CD2 HIS D 110      33.175 -60.677  -7.605  1.00 39.85           C  
ANISOU 3411  CD2 HIS D 110     3204   7485   4452   1730    658   2799       C  
ATOM   3412  CE1 HIS D 110      32.364 -60.992  -5.591  1.00 42.01           C  
ANISOU 3412  CE1 HIS D 110     3875   7583   4502   1960    722   2932       C  
ATOM   3413  NE2 HIS D 110      32.727 -61.610  -6.701  1.00 43.10           N  
ANISOU 3413  NE2 HIS D 110     4073   7589   4714   1998    568   2942       N  
ATOM   3414  N   LEU D 111      32.676 -55.143  -6.944  1.00 39.49           N  
ANISOU 3414  N   LEU D 111     2565   8207   4232    643    392   2970       N  
ATOM   3415  CA  LEU D 111      33.328 -53.841  -6.854  1.00 41.73           C  
ANISOU 3415  CA  LEU D 111     2586   8820   4449    320     44   2781       C  
ATOM   3416  C   LEU D 111      34.835 -54.017  -6.960  1.00 44.50           C  
ANISOU 3416  C   LEU D 111     2714   9267   4928   -119    195   2497       C  
ATOM   3417  O   LEU D 111      35.375 -55.026  -6.513  1.00 43.50           O  
ANISOU 3417  O   LEU D 111     2660   9073   4793    186   -198   2624       O  
ATOM   3418  CB  LEU D 111      32.980 -53.128  -5.549  1.00 42.50           C  
ANISOU 3418  CB  LEU D 111     2803   8855   4490    -57    -70   2718       C  
ATOM   3419  CG  LEU D 111      31.548 -52.621  -5.402  1.00 42.43           C  
ANISOU 3419  CG  LEU D 111     3053   8758   4310   -447    -25   2679       C  
ATOM   3420  CD1 LEU D 111      31.429 -51.729  -4.181  1.00 43.69           C  
ANISOU 3420  CD1 LEU D 111     3047   8833   4719   -595    317   2464       C  
ATOM   3421  CD2 LEU D 111      31.127 -51.879  -6.660  1.00 41.43           C  
ANISOU 3421  CD2 LEU D 111     3174   8649   3916   -316   -476   2771       C  
ATOM   3422  N   LYS D 112      35.496 -53.038  -7.570  1.00 47.40           N  
ANISOU 3422  N   LYS D 112     2908   9700   5400   -533    457   2226       N  
ATOM   3423  CA  LYS D 112      36.952 -52.973  -7.586  1.00 51.44           C  
ANISOU 3423  CA  LYS D 112     3092  10474   5979   -758    231   2207       C  
ATOM   3424  C   LYS D 112      37.471 -53.077  -6.151  1.00 51.68           C  
ANISOU 3424  C   LYS D 112     3015  10704   5918   -611   -158   2517       C  
ATOM   3425  O   LYS D 112      36.903 -52.470  -5.242  1.00 51.11           O  
ANISOU 3425  O   LYS D 112     3003  10589   5826   -923   -354   2127       O  
ATOM   3426  CB  LYS D 112      37.408 -51.673  -8.254  1.00 54.16           C  
ANISOU 3426  CB  LYS D 112     3570  10751   6259   -854    378   2222       C  
ATOM   3427  CG  LYS D 112      38.860 -51.636  -8.691  1.00 56.21           C  
ANISOU 3427  CG  LYS D 112     3776  10874   6707   -920    590   2223       C  
ATOM   3428  CD  LYS D 112      39.107 -50.440  -9.603  1.00 56.97           C  
ANISOU 3428  CD  LYS D 112     3652  10956   7038  -1059    559   2146       C  
ATOM   3429  CE  LYS D 112      40.579 -50.293  -9.946  1.00 58.54           C  
ANISOU 3429  CE  LYS D 112     3842  11096   7304   -897    229   2114       C  
ATOM   3430  NZ  LYS D 112      41.392 -49.982  -8.737  1.00 60.96           N  
ANISOU 3430  NZ  LYS D 112     4321  11193   7649   -807    466   2083       N  
ATOM   3431  N   LYS D 113      38.540 -53.845  -5.946  1.00 53.89           N  
ANISOU 3431  N   LYS D 113     3140  11027   6308   -215   -112   2956       N  
ATOM   3432  CA  LYS D 113      38.974 -54.205  -4.594  1.00 56.19           C  
ANISOU 3432  CA  LYS D 113     3219  11417   6716   -370    -69   2840       C  
ATOM   3433  C   LYS D 113      39.394 -53.009  -3.734  1.00 56.74           C  
ANISOU 3433  C   LYS D 113     3267  11540   6751   -337   -241   2889       C  
ATOM   3434  O   LYS D 113      39.163 -53.005  -2.526  1.00 56.41           O  
ANISOU 3434  O   LYS D 113     3350  11418   6664     24   -496   3057       O  
ATOM   3435  CB  LYS D 113      40.117 -55.226  -4.653  1.00 58.35           C  
ANISOU 3435  CB  LYS D 113     3319  11812   7040   -445    -90   2651       C  
ATOM   3436  CG  LYS D 113      41.326 -54.812  -5.482  1.00 61.38           C  
ANISOU 3436  CG  LYS D 113     3765  12182   7374   -351    -33   2544       C  
ATOM   3437  CD  LYS D 113      42.424 -55.871  -5.392  1.00 63.86           C  
ANISOU 3437  CD  LYS D 113     4064  12406   7794    -79    372   2658       C  
ATOM   3438  CE  LYS D 113      43.648 -55.508  -6.226  1.00 65.65           C  
ANISOU 3438  CE  LYS D 113     4362  12472   8112     33    838   2739       C  
ATOM   3439  NZ  LYS D 113      43.380 -55.581  -7.691  1.00 66.96           N  
ANISOU 3439  NZ  LYS D 113     4500  12530   8411     88   1134   2711       N  
ATOM   3440  N   GLU D 114      40.000 -51.998  -4.346  1.00 57.86           N  
ANISOU 3440  N   GLU D 114     3327  11769   6886   -695   -310   2580       N  
ATOM   3441  CA  GLU D 114      40.413 -50.811  -3.599  1.00 57.99           C  
ANISOU 3441  CA  GLU D 114     3361  11942   6729   -779   -381   2266       C  
ATOM   3442  C   GLU D 114      39.195 -50.038  -3.104  1.00 56.15           C  
ANISOU 3442  C   GLU D 114     3395  11719   6221  -1107   -678   2053       C  
ATOM   3443  O   GLU D 114      39.229 -49.410  -2.042  1.00 55.08           O  
ANISOU 3443  O   GLU D 114     3347  11473   6106  -1041   -899   1692       O  
ATOM   3444  CB  GLU D 114      41.298 -49.904  -4.454  1.00 59.65           C  
ANISOU 3444  CB  GLU D 114     3339  12196   7130   -838   -305   1898       C  
ATOM   3445  CG  GLU D 114      42.669 -50.484  -4.780  1.00 62.28           C  
ANISOU 3445  CG  GLU D 114     3544  12400   7720   -672    125   1640       C  
ATOM   3446  CD  GLU D 114      42.623 -51.546  -5.864  1.00 63.16           C  
ANISOU 3446  CD  GLU D 114     3452  12462   8084   -390     91   1528       C  
ATOM   3447  OE1 GLU D 114      41.558 -51.710  -6.502  1.00 61.72           O  
ANISOU 3447  OE1 GLU D 114     3232  12309   7909   -107   -217   1634       O  
ATOM   3448  OE2 GLU D 114      43.657 -52.217  -6.077  1.00 62.87           O  
ANISOU 3448  OE2 GLU D 114     3242  12350   8294   -304   -358   1417       O  
ATOM   3449  N   LEU D 115      38.120 -50.092  -3.884  1.00 54.18           N  
ANISOU 3449  N   LEU D 115     3489  11453   5643  -1278   -581   2345       N  
ATOM   3450  CA  LEU D 115      36.870 -49.463  -3.499  1.00 52.40           C  
ANISOU 3450  CA  LEU D 115     3426  11147   5338  -1427   -616   2466       C  
ATOM   3451  C   LEU D 115      36.225 -50.264  -2.378  1.00 50.73           C  
ANISOU 3451  C   LEU D 115     3305  10881   5089  -1390   -496   2661       C  
ATOM   3452  O   LEU D 115      35.761 -49.702  -1.384  1.00 51.39           O  
ANISOU 3452  O   LEU D 115     3562  10822   5141  -1326   -966   2761       O  
ATOM   3453  CB  LEU D 115      35.921 -49.361  -4.694  1.00 52.81           C  
ANISOU 3453  CB  LEU D 115     3325  11016   5724  -1370   -697   2304       C  
ATOM   3454  CG  LEU D 115      34.557 -48.737  -4.414  1.00 54.09           C  
ANISOU 3454  CG  LEU D 115     3391  10940   6222  -1413   -410   2115       C  
ATOM   3455  CD1 LEU D 115      34.720 -47.362  -3.785  1.00 54.02           C  
ANISOU 3455  CD1 LEU D 115     3331  10672   6521  -1664   -171   1974       C  
ATOM   3456  CD2 LEU D 115      33.749 -48.659  -5.701  1.00 54.12           C  
ANISOU 3456  CD2 LEU D 115     3245  10988   6329  -1324   -570   2038       C  
ATOM   3457  N   ALA D 116      36.209 -51.584  -2.551  1.00 48.86           N  
ANISOU 3457  N   ALA D 116     3162  10632   4769  -1173   -444   2734       N  
ATOM   3458  CA  ALA D 116      35.629 -52.485  -1.567  1.00 49.30           C  
ANISOU 3458  CA  ALA D 116     3185  10802   4743   -842   -528   2871       C  
ATOM   3459  C   ALA D 116      36.329 -52.313  -0.230  1.00 51.16           C  
ANISOU 3459  C   ALA D 116     3223  11233   4984  -1001   -425   2552       C  
ATOM   3460  O   ALA D 116      35.692 -52.338   0.821  1.00 51.76           O  
ANISOU 3460  O   ALA D 116     3407  11362   4898   -851     86   2778       O  
ATOM   3461  CB  ALA D 116      35.722 -53.928  -2.041  1.00 48.55           C  
ANISOU 3461  CB  ALA D 116     3151  10603   4693   -644   -552   2794       C  
ATOM   3462  N   GLY D 117      37.644 -52.118  -0.284  1.00 53.32           N  
ANISOU 3462  N   GLY D 117     3340  11438   5479  -1124   -721   2124       N  
ATOM   3463  CA  GLY D 117      38.444 -51.938   0.913  1.00 54.31           C  
ANISOU 3463  CA  GLY D 117     3675  11696   5263  -1414  -1051   1692       C  
ATOM   3464  C   GLY D 117      38.052 -50.711   1.712  1.00 56.47           C  
ANISOU 3464  C   GLY D 117     3895  12085   5477  -1457  -1168   1711       C  
ATOM   3465  O   GLY D 117      38.295 -50.642   2.916  1.00 59.07           O  
ANISOU 3465  O   GLY D 117     4325  12355   5764  -1514  -1010   1759       O  
ATOM   3466  N   ALA D 118      37.448 -49.737   1.042  1.00 55.81           N  
ANISOU 3466  N   ALA D 118     4000  11894   5310  -1666  -1271   1400       N  
ATOM   3467  CA  ALA D 118      36.966 -48.534   1.709  1.00 56.26           C  
ANISOU 3467  CA  ALA D 118     4002  11917   5456  -1926  -1133   1449       C  
ATOM   3468  C   ALA D 118      35.511 -48.675   2.162  1.00 55.06           C  
ANISOU 3468  C   ALA D 118     3825  11639   5458  -1950   -853   1361       C  
ATOM   3469  O   ALA D 118      35.129 -48.176   3.221  1.00 54.70           O  
ANISOU 3469  O   ALA D 118     3583  11648   5551  -1784   -794   1255       O  
ATOM   3470  CB  ALA D 118      37.111 -47.333   0.791  1.00 57.90           C  
ANISOU 3470  CB  ALA D 118     4270  12099   5630  -2063   -727   1518       C  
ATOM   3471  N   LEU D 119      34.705 -49.355   1.354  1.00 51.99           N  
ANISOU 3471  N   LEU D 119     3781  10950   5023  -1727  -1222   1454       N  
ATOM   3472  CA  LEU D 119      33.264 -49.413   1.587  1.00 51.86           C  
ANISOU 3472  CA  LEU D 119     3800  10950   4953  -1735  -1215   1546       C  
ATOM   3473  C   LEU D 119      32.821 -50.516   2.545  1.00 53.35           C  
ANISOU 3473  C   LEU D 119     3927  11201   5144  -1512  -1354   1763       C  
ATOM   3474  O   LEU D 119      31.774 -50.397   3.187  1.00 53.40           O  
ANISOU 3474  O   LEU D 119     3995  11191   5102  -1585  -1387   1782       O  
ATOM   3475  CB  LEU D 119      32.535 -49.585   0.258  1.00 50.11           C  
ANISOU 3475  CB  LEU D 119     4051  10506   4484  -1835  -1344   1514       C  
ATOM   3476  CG  LEU D 119      32.655 -48.420  -0.721  1.00 50.49           C  
ANISOU 3476  CG  LEU D 119     4211  10543   4428  -2106  -1083   1659       C  
ATOM   3477  CD1 LEU D 119      31.648 -48.587  -1.845  1.00 49.35           C  
ANISOU 3477  CD1 LEU D 119     4193  10274   4282  -2258  -1287   1665       C  
ATOM   3478  CD2 LEU D 119      32.454 -47.094  -0.007  1.00 51.40           C  
ANISOU 3478  CD2 LEU D 119     4506  10701   4322  -2004   -724   1825       C  
ATOM   3479  N   ALA D 120      33.601 -51.588   2.630  1.00 54.51           N  
ANISOU 3479  N   ALA D 120     3996  11345   5371  -1155  -1466   1958       N  
ATOM   3480  CA  ALA D 120      33.238 -52.733   3.463  1.00 57.18           C  
ANISOU 3480  CA  ALA D 120     4023  12133   5570  -1137  -1305   2204       C  
ATOM   3481  C   ALA D 120      32.980 -52.331   4.915  1.00 58.41           C  
ANISOU 3481  C   ALA D 120     4271  12619   5302  -1228  -1311   2124       C  
ATOM   3482  O   ALA D 120      32.016 -52.788   5.532  1.00 56.59           O  
ANISOU 3482  O   ALA D 120     4185  12387   4929  -1146  -1136   2345       O  
ATOM   3483  CB  ALA D 120      34.323 -53.793   3.398  1.00 58.44           C  
ANISOU 3483  CB  ALA D 120     4093  12282   5829   -875  -1295   2443       C  
ATOM   3484  N   TYR D 121      33.840 -51.469   5.449  1.00 60.51           N  
ANISOU 3484  N   TYR D 121     4609  13134   5249  -1382  -1420   1863       N  
ATOM   3485  CA  TYR D 121      33.697 -50.975   6.815  1.00 62.90           C  
ANISOU 3485  CA  TYR D 121     4848  13768   5283  -1492  -1414   1856       C  
ATOM   3486  C   TYR D 121      32.400 -50.185   6.979  1.00 60.78           C  
ANISOU 3486  C   TYR D 121     4871  13381   4841  -1685  -1127   1817       C  
ATOM   3487  O   TYR D 121      31.677 -50.354   7.961  1.00 59.61           O  
ANISOU 3487  O   TYR D 121     5056  13179   4413  -1616  -1228   1504       O  
ATOM   3488  CB  TYR D 121      34.906 -50.110   7.192  1.00 67.47           C  
ANISOU 3488  CB  TYR D 121     5264  14701   5672  -1569  -1433   1828       C  
ATOM   3489  CG  TYR D 121      34.808 -49.432   8.541  1.00 71.95           C  
ANISOU 3489  CG  TYR D 121     5690  15503   6146  -1515  -1414   1955       C  
ATOM   3490  CD1 TYR D 121      35.182 -50.094   9.704  1.00 75.50           C  
ANISOU 3490  CD1 TYR D 121     6120  15891   6675  -1416   -885   2003       C  
ATOM   3491  CD2 TYR D 121      34.357 -48.122   8.649  1.00 72.83           C  
ANISOU 3491  CD2 TYR D 121     5678  15789   6207  -1540  -1759   2042       C  
ATOM   3492  CE1 TYR D 121      35.099 -49.473  10.939  1.00 77.02           C  
ANISOU 3492  CE1 TYR D 121     6328  16153   6781  -1429   -791   2025       C  
ATOM   3493  CE2 TYR D 121      34.269 -47.493   9.876  1.00 75.23           C  
ANISOU 3493  CE2 TYR D 121     5972  16091   6521  -1516  -1441   2063       C  
ATOM   3494  CZ  TYR D 121      34.641 -48.172  11.018  1.00 76.95           C  
ANISOU 3494  CZ  TYR D 121     6367  16280   6592  -1441  -1070   2122       C  
ATOM   3495  OH  TYR D 121      34.554 -47.544  12.241  1.00 77.14           O  
ANISOU 3495  OH  TYR D 121     6602  16430   6276  -1403  -1075   2217       O  
ATOM   3496  N   ILE D 122      32.109 -49.333   6.002  1.00 57.86           N  
ANISOU 3496  N   ILE D 122     4541  12848   4595  -1910  -1105   2052       N  
ATOM   3497  CA  ILE D 122      30.913 -48.504   6.027  1.00 55.58           C  
ANISOU 3497  CA  ILE D 122     4275  12501   4343  -2319   -809   2294       C  
ATOM   3498  C   ILE D 122      29.644 -49.360   5.973  1.00 52.44           C  
ANISOU 3498  C   ILE D 122     4070  11872   3982  -2456   -720   2117       C  
ATOM   3499  O   ILE D 122      28.657 -49.066   6.652  1.00 51.55           O  
ANISOU 3499  O   ILE D 122     4388  11466   3734  -2489   -554   2078       O  
ATOM   3500  CB  ILE D 122      30.923 -47.492   4.857  1.00 57.37           C  
ANISOU 3500  CB  ILE D 122     4267  12612   4917  -2607   -572   2314       C  
ATOM   3501  CG1 ILE D 122      32.039 -46.464   5.067  1.00 59.29           C  
ANISOU 3501  CG1 ILE D 122     4471  12778   5277  -2790   -543   2311       C  
ATOM   3502  CG2 ILE D 122      29.574 -46.793   4.717  1.00 57.67           C  
ANISOU 3502  CG2 ILE D 122     4358  12596   4957  -2709   -428   2190       C  
ATOM   3503  CD1 ILE D 122      32.276 -45.555   3.872  1.00 59.24           C  
ANISOU 3503  CD1 ILE D 122     4525  12722   5263  -2850   -549   2453       C  
ATOM   3504  N   MET D 123      29.676 -50.426   5.178  1.00 52.16           N  
ANISOU 3504  N   MET D 123     3868  11790   4159  -2264   -620   2180       N  
ATOM   3505  CA  MET D 123      28.523 -51.316   5.062  1.00 52.21           C  
ANISOU 3505  CA  MET D 123     4083  11647   4106  -1824   -607   2638       C  
ATOM   3506  C   MET D 123      28.355 -52.181   6.309  1.00 52.69           C  
ANISOU 3506  C   MET D 123     4249  11609   4162  -1511   -674   2732       C  
ATOM   3507  O   MET D 123      27.240 -52.361   6.798  1.00 51.90           O  
ANISOU 3507  O   MET D 123     4186  11223   4312  -1410   -770   2935       O  
ATOM   3508  CB  MET D 123      28.643 -52.211   3.825  1.00 51.56           C  
ANISOU 3508  CB  MET D 123     4001  11409   4179  -1654   -779   2687       C  
ATOM   3509  CG  MET D 123      28.629 -51.459   2.499  1.00 50.37           C  
ANISOU 3509  CG  MET D 123     3967  11111   4062  -1403   -556   2773       C  
ATOM   3510  SD  MET D 123      28.581 -52.552   1.059  1.00 49.08           S  
ANISOU 3510  SD  MET D 123     3733  10759   4158  -1303   -348   2903       S  
ATOM   3511  CE  MET D 123      26.898 -53.169   1.131  1.00 46.70           C  
ANISOU 3511  CE  MET D 123     3319  10379   4046  -1603   -626   2808       C  
ATOM   3512  N   ASP D 124      29.464 -52.714   6.817  1.00 53.29           N  
ANISOU 3512  N   ASP D 124     4483  11666   4101  -1276   -892   2408       N  
ATOM   3513  CA  ASP D 124      29.416 -53.614   7.968  1.00 56.57           C  
ANISOU 3513  CA  ASP D 124     5071  12209   4214  -1105   -921   2417       C  
ATOM   3514  C   ASP D 124      28.964 -52.905   9.238  1.00 60.00           C  
ANISOU 3514  C   ASP D 124     5916  12508   4372  -1088   -507   2489       C  
ATOM   3515  O   ASP D 124      28.264 -53.486  10.069  1.00 60.59           O  
ANISOU 3515  O   ASP D 124     5906  12677   4441  -1070    196   2864       O  
ATOM   3516  CB  ASP D 124      30.781 -54.260   8.206  1.00 56.99           C  
ANISOU 3516  CB  ASP D 124     4916  12245   4494   -814  -1190   2347       C  
ATOM   3517  CG  ASP D 124      31.164 -55.234   7.113  1.00 57.75           C  
ANISOU 3517  CG  ASP D 124     4815  12359   4769   -613  -1128   2268       C  
ATOM   3518  OD1 ASP D 124      30.302 -55.547   6.267  1.00 56.71           O  
ANISOU 3518  OD1 ASP D 124     4504  12281   4761   -667  -1295   2020       O  
ATOM   3519  OD2 ASP D 124      32.327 -55.692   7.105  1.00 57.06           O  
ANISOU 3519  OD2 ASP D 124     4913  11983   4783   -309  -1347   2384       O  
ATOM   3520  N   ASN D 125      29.377 -51.653   9.394  1.00 59.67           N  
ANISOU 3520  N   ASN D 125     6529  12167   3978  -1070  -1039   2177       N  
ATOM   3521  CA  ASN D 125      28.998 -50.885  10.570  1.00 61.00           C  
ANISOU 3521  CA  ASN D 125     7419  11898   3860  -1004  -1104   1677       C  
ATOM   3522  C   ASN D 125      27.722 -50.098  10.329  1.00 59.29           C  
ANISOU 3522  C   ASN D 125     7794  11311   3423  -1208   -908   1389       C  
ATOM   3523  O   ASN D 125      27.260 -49.367  11.206  1.00 58.58           O  
ANISOU 3523  O   ASN D 125     7790  11156   3310  -1197  -1037   1255       O  
ATOM   3524  CB  ASN D 125      30.129 -49.947  10.983  1.00 64.52           C  
ANISOU 3524  CB  ASN D 125     8109  12059   4347   -591   -965   1726       C  
ATOM   3525  CG  ASN D 125      31.321 -50.693  11.540  1.00 66.84           C  
ANISOU 3525  CG  ASN D 125     8730  12082   4586   -268   -888   1831       C  
ATOM   3526  OD1 ASN D 125      31.399 -50.946  12.739  1.00 66.92           O  
ANISOU 3526  OD1 ASN D 125     8982  12038   4407    -63  -1102   2156       O  
ATOM   3527  ND2 ASN D 125      32.253 -51.059  10.669  1.00 68.35           N  
ANISOU 3527  ND2 ASN D 125     8919  12129   4922   -242   -870   1618       N  
ATOM   3528  N   LYS D 126      27.162 -50.261   9.132  1.00 57.73           N  
ANISOU 3528  N   LYS D 126     7993  10780   3163  -1360   -794   1202       N  
ATOM   3529  CA  LYS D 126      25.901 -49.630   8.761  1.00 58.33           C  
ANISOU 3529  CA  LYS D 126     8294  10408   3462  -1448   -412   1169       C  
ATOM   3530  C   LYS D 126      25.959 -48.113   8.939  1.00 56.53           C  
ANISOU 3530  C   LYS D 126     8074   9983   3424  -1767   -391    855       C  
ATOM   3531  O   LYS D 126      25.005 -47.492   9.405  1.00 56.41           O  
ANISOU 3531  O   LYS D 126     8010   9959   3463  -1975    289    923       O  
ATOM   3532  CB  LYS D 126      24.751 -50.233   9.575  1.00 62.14           C  
ANISOU 3532  CB  LYS D 126     8815  10589   4207  -1187    -65   1142       C  
ATOM   3533  CG  LYS D 126      24.530 -51.714   9.288  1.00 65.69           C  
ANISOU 3533  CG  LYS D 126     9376  10703   4878  -1011    460   1216       C  
ATOM   3534  CD  LYS D 126      23.486 -52.332  10.203  1.00 68.83           C  
ANISOU 3534  CD  LYS D 126     9984  10802   5367   -752    757   1244       C  
ATOM   3535  CE  LYS D 126      24.036 -52.559  11.602  1.00 70.79           C  
ANISOU 3535  CE  LYS D 126    10345  10841   5710   -669    977   1264       C  
ATOM   3536  NZ  LYS D 126      23.074 -53.307  12.459  1.00 72.08           N  
ANISOU 3536  NZ  LYS D 126    10525  10829   6032   -679    939   1229       N  
ATOM   3537  N   LEU D 127      27.089 -47.525   8.558  1.00 54.45           N  
ANISOU 3537  N   LEU D 127     7770   9491   3427  -1947  -1059    614       N  
ATOM   3538  CA  LEU D 127      27.275 -46.083   8.663  1.00 53.14           C  
ANISOU 3538  CA  LEU D 127     7468   9074   3647  -1964  -1357    539       C  
ATOM   3539  C   LEU D 127      26.504 -45.357   7.571  1.00 48.31           C  
ANISOU 3539  C   LEU D 127     6718   8288   3351  -2276  -1466    212       C  
ATOM   3540  O   LEU D 127      26.135 -44.192   7.722  1.00 48.35           O  
ANISOU 3540  O   LEU D 127     6805   8050   3515  -2576  -1677    -33       O  
ATOM   3541  CB  LEU D 127      28.759 -45.723   8.588  1.00 55.17           C  
ANISOU 3541  CB  LEU D 127     7913   9361   3690  -1773  -1597    431       C  
ATOM   3542  CG  LEU D 127      29.594 -46.073   9.818  1.00 58.83           C  
ANISOU 3542  CG  LEU D 127     8412   9634   4306  -1454  -1233    566       C  
ATOM   3543  CD1 LEU D 127      31.043 -45.669   9.606  1.00 61.20           C  
ANISOU 3543  CD1 LEU D 127     8667   9785   4800  -1262   -802    596       C  
ATOM   3544  CD2 LEU D 127      29.015 -45.392  11.045  1.00 59.29           C  
ANISOU 3544  CD2 LEU D 127     8524   9640   4365  -1478  -1173    608       C  
ATOM   3545  N   ALA D 128      26.261 -46.057   6.468  1.00 42.63           N  
ANISOU 3545  N   ALA D 128     5453   7478   3265  -2108  -1653    404       N  
ATOM   3546  CA  ALA D 128      25.497 -45.499   5.366  1.00 40.69           C  
ANISOU 3546  CA  ALA D 128     5114   7218   3127  -2268   -833    466       C  
ATOM   3547  C   ALA D 128      24.905 -46.601   4.515  1.00 38.25           C  
ANISOU 3547  C   ALA D 128     4625   7028   2882  -1845   -495    571       C  
ATOM   3548  O   ALA D 128      25.397 -47.732   4.499  1.00 37.69           O  
ANISOU 3548  O   ALA D 128     4670   6844   2805  -1437   -578    969       O  
ATOM   3549  CB  ALA D 128      26.370 -44.589   4.506  1.00 40.80           C  
ANISOU 3549  CB  ALA D 128     5337   7028   3139  -2285   -889    703       C  
ATOM   3550  N   GLN D 129      23.827 -46.262   3.822  1.00 35.14           N  
ANISOU 3550  N   GLN D 129     4175   6809   2368  -1780   -351    164       N  
ATOM   3551  CA AGLN D 129      23.267 -47.145   2.815  0.48 35.61           C  
ANISOU 3551  CA AGLN D 129     4247   6735   2547  -1616    -32    169       C  
ATOM   3552  CA BGLN D 129      23.251 -47.134   2.818  0.52 36.23           C  
ANISOU 3552  CA BGLN D 129     4385   6747   2633  -1682      1    219       C  
ATOM   3553  C   GLN D 129      23.722 -46.628   1.464  1.00 34.15           C  
ANISOU 3553  C   GLN D 129     4326   6415   2235  -1505   -139    295       C  
ATOM   3554  O   GLN D 129      23.707 -45.424   1.216  1.00 36.01           O  
ANISOU 3554  O   GLN D 129     4805   6271   2605  -1189     80     12       O  
ATOM   3555  CB AGLN D 129      21.740 -47.203   2.900  0.48 37.40           C  
ANISOU 3555  CB AGLN D 129     4430   7013   2769  -1399    241      9       C  
ATOM   3556  CB BGLN D 129      21.721 -47.147   2.908  0.52 39.25           C  
ANISOU 3556  CB BGLN D 129     4865   7036   3013  -1587    287    166       C  
ATOM   3557  CG AGLN D 129      21.207 -47.640   4.257  0.48 39.78           C  
ANISOU 3557  CG AGLN D 129     4973   7211   2930  -1209    515     61       C  
ATOM   3558  CG BGLN D 129      21.169 -47.725   4.213  0.52 42.71           C  
ANISOU 3558  CG BGLN D 129     5698   7200   3329  -1572    684    362       C  
ATOM   3559  CD AGLN D 129      21.697 -49.016   4.679  0.48 41.47           C  
ANISOU 3559  CD AGLN D 129     5205   7430   3122  -1059    609    112       C  
ATOM   3560  CD BGLN D 129      21.417 -46.831   5.421  0.52 45.51           C  
ANISOU 3560  CD BGLN D 129     6220   7353   3720  -1673    907    573       C  
ATOM   3561  OE1AGLN D 129      21.892 -49.905   3.849  0.48 41.69           O  
ANISOU 3561  OE1AGLN D 129     4882   7492   3467  -1033    276     65       O  
ATOM   3562  OE1BGLN D 129      21.994 -47.263   6.419  0.52 47.35           O  
ANISOU 3562  OE1BGLN D 129     6420   7509   4060  -1726   1393    821       O  
ATOM   3563  NE2AGLN D 129      21.900 -49.195   5.979  0.48 42.45           N  
ANISOU 3563  NE2AGLN D 129     5585   7487   3059   -978   1003    114       N  
ATOM   3564  NE2BGLN D 129      20.977 -45.581   5.335  0.52 45.93           N  
ANISOU 3564  NE2BGLN D 129     6309   7266   3876  -1857    748    379       N  
ATOM   3565  N   ILE D 130      24.151 -47.537   0.600  1.00 31.39           N  
ANISOU 3565  N   ILE D 130     3847   5932   2149  -1643   -534    768       N  
ATOM   3566  CA  ILE D 130      24.719 -47.142  -0.681  1.00 29.39           C  
ANISOU 3566  CA  ILE D 130     3754   5608   1807  -1663   -437    266       C  
ATOM   3567  C   ILE D 130      23.854 -47.631  -1.830  1.00 28.89           C  
ANISOU 3567  C   ILE D 130     3816   5248   1912  -1521   -756    355       C  
ATOM   3568  O   ILE D 130      23.549 -48.823  -1.920  1.00 32.42           O  
ANISOU 3568  O   ILE D 130     4508   5383   2427  -1296   -482    514       O  
ATOM   3569  CB  ILE D 130      26.143 -47.690  -0.837  1.00 31.36           C  
ANISOU 3569  CB  ILE D 130     3643   5923   2348  -1818   -468    144       C  
ATOM   3570  CG1 ILE D 130      26.957 -47.415   0.434  1.00 35.08           C  
ANISOU 3570  CG1 ILE D 130     3857   6144   3327  -1655    191    266       C  
ATOM   3571  CG2 ILE D 130      26.818 -47.087  -2.062  1.00 33.23           C  
ANISOU 3571  CG2 ILE D 130     4049   5821   2754  -1902    500    540       C  
ATOM   3572  CD1 ILE D 130      28.344 -48.033   0.426  1.00 37.29           C  
ANISOU 3572  CD1 ILE D 130     3984   6209   3975  -1825    601    420       C  
ATOM   3573  N   GLU D 131      23.436 -46.708  -2.692  1.00 27.71           N  
ANISOU 3573  N   GLU D 131     3561   5097   1871  -1638    -16    172       N  
ATOM   3574  CA  GLU D 131      22.669 -47.080  -3.870  1.00 26.18           C  
ANISOU 3574  CA  GLU D 131     3338   4802   1808  -1499   -106    349       C  
ATOM   3575  C   GLU D 131      23.591 -46.989  -5.075  1.00 24.77           C  
ANISOU 3575  C   GLU D 131     2937   4278   2197  -1819   -208    235       C  
ATOM   3576  O   GLU D 131      24.241 -45.970  -5.281  1.00 28.84           O  
ANISOU 3576  O   GLU D 131     3631   4478   2850  -2157    255     67       O  
ATOM   3577  CB  GLU D 131      21.435 -46.180  -4.063  1.00 31.30           C  
ANISOU 3577  CB  GLU D 131     4026   5163   2704  -1029    -22    303       C  
ATOM   3578  CG  GLU D 131      20.643 -46.487  -5.351  1.00 33.95           C  
ANISOU 3578  CG  GLU D 131     4244   5294   3363   -804   -312     48       C  
ATOM   3579  CD  GLU D 131      19.567 -45.443  -5.701  1.00 36.46           C  
ANISOU 3579  CD  GLU D 131     4652   5505   3694   -391   -139   -330       C  
ATOM   3580  OE1 GLU D 131      19.916 -44.311  -6.134  1.00 38.78           O  
ANISOU 3580  OE1 GLU D 131     5471   5844   3420      8   -531   -217       O  
ATOM   3581  OE2 GLU D 131      18.369 -45.768  -5.575  1.00 32.92           O  
ANISOU 3581  OE2 GLU D 131     3748   5274   3487    131   -353   -293       O  
ATOM   3582  N   GLY D 132      23.653 -48.057  -5.858  1.00 23.72           N  
ANISOU 3582  N   GLY D 132     3177   4047   1787   -938   -455    178       N  
ATOM   3583  CA  GLY D 132      24.475 -48.079  -7.053  1.00 22.47           C  
ANISOU 3583  CA  GLY D 132     3025   3658   1854   -933   -474    514       C  
ATOM   3584  C   GLY D 132      23.624 -47.953  -8.308  1.00 20.28           C  
ANISOU 3584  C   GLY D 132     2773   3256   1676   -802   -473    509       C  
ATOM   3585  O   GLY D 132      22.489 -48.431  -8.353  1.00 20.14           O  
ANISOU 3585  O   GLY D 132     2623   2899   2129   -873   -462    330       O  
ATOM   3586  N   VAL D 133      24.171 -47.281  -9.316  1.00 19.78           N  
ANISOU 3586  N   VAL D 133     2846   2911   1758  -1035   -121    230       N  
ATOM   3587  CA  VAL D 133      23.532 -47.127 -10.615  1.00 18.30           C  
ANISOU 3587  CA  VAL D 133     2696   2353   1903   -586    147    244       C  
ATOM   3588  C   VAL D 133      24.603 -47.225 -11.679  1.00 18.18           C  
ANISOU 3588  C   VAL D 133     2613   2344   1949   -754   -138    100       C  
ATOM   3589  O   VAL D 133      25.660 -46.612 -11.545  1.00 21.29           O  
ANISOU 3589  O   VAL D 133     3132   2936   2021   -835   -182    257       O  
ATOM   3590  CB  VAL D 133      22.807 -45.762 -10.761  1.00 18.51           C  
ANISOU 3590  CB  VAL D 133     2743   2389   1901    -51   -137    124       C  
ATOM   3591  CG1 VAL D 133      22.271 -45.574 -12.187  1.00 20.67           C  
ANISOU 3591  CG1 VAL D 133     3446   2375   2035     69   -100     11       C  
ATOM   3592  CG2 VAL D 133      21.703 -45.626  -9.735  1.00 21.38           C  
ANISOU 3592  CG2 VAL D 133     2753   2879   2492   -104    326     57       C  
ATOM   3593  N   VAL D 134      24.346 -47.995 -12.732  1.00 15.71           N  
ANISOU 3593  N   VAL D 134     2280   1939   1750   -225   -160    169       N  
ATOM   3594  CA  VAL D 134      25.289 -48.046 -13.841  1.00 15.63           C  
ANISOU 3594  CA  VAL D 134     2300   1670   1966   -152    320    264       C  
ATOM   3595  C   VAL D 134      24.876 -47.019 -14.892  1.00 16.72           C  
ANISOU 3595  C   VAL D 134     2264   1925   2162   -289     59    489       C  
ATOM   3596  O   VAL D 134      23.819 -47.151 -15.490  1.00 17.94           O  
ANISOU 3596  O   VAL D 134     2133   2332   2350    -48     33    605       O  
ATOM   3597  CB  VAL D 134      25.350 -49.454 -14.460  1.00 15.69           C  
ANISOU 3597  CB  VAL D 134     2174   1764   2023   -263      3    436       C  
ATOM   3598  CG1 VAL D 134      26.210 -49.443 -15.720  1.00 16.23           C  
ANISOU 3598  CG1 VAL D 134     2077   2020   2070   -232    306    527       C  
ATOM   3599  CG2 VAL D 134      25.891 -50.445 -13.434  1.00 18.72           C  
ANISOU 3599  CG2 VAL D 134     2695   2244   2175    144    -63    660       C  
ATOM   3600  N   PRO D 135      25.691 -45.965 -15.100  1.00 16.53           N  
ANISOU 3600  N   PRO D 135     2252   2138   1891   -630     82    498       N  
ATOM   3601  CA  PRO D 135      25.235 -44.897 -16.006  1.00 16.59           C  
ANISOU 3601  CA  PRO D 135     2734   1895   1674   -395    327    231       C  
ATOM   3602  C   PRO D 135      25.500 -45.198 -17.477  1.00 17.44           C  
ANISOU 3602  C   PRO D 135     2579   2011   2036   -175    331    576       C  
ATOM   3603  O   PRO D 135      24.699 -44.820 -18.338  1.00 18.06           O  
ANISOU 3603  O   PRO D 135     2516   2042   2304   -173     77    606       O  
ATOM   3604  CB  PRO D 135      26.050 -43.680 -15.552  1.00 19.29           C  
ANISOU 3604  CB  PRO D 135     2887   1987   2455   -327   -293    222       C  
ATOM   3605  CG  PRO D 135      27.325 -44.257 -15.012  1.00 20.42           C  
ANISOU 3605  CG  PRO D 135     2913   2182   2663   -508    -59    374       C  
ATOM   3606  CD  PRO D 135      26.912 -45.590 -14.365  1.00 17.84           C  
ANISOU 3606  CD  PRO D 135     2378   2007   2395  -1236    -31    336       C  
ATOM   3607  N   PHE D 136      26.620 -45.860 -17.751  1.00 16.54           N  
ANISOU 3607  N   PHE D 136     2359   1928   1996    134    211    594       N  
ATOM   3608  CA  PHE D 136      27.058 -46.145 -19.114  1.00 15.63           C  
ANISOU 3608  CA  PHE D 136     2357   1533   2047   -114    503    564       C  
ATOM   3609  C   PHE D 136      27.836 -47.449 -19.106  1.00 17.18           C  
ANISOU 3609  C   PHE D 136     2310   1743   2473    142    309    385       C  
ATOM   3610  O   PHE D 136      28.179 -47.956 -18.037  1.00 18.19           O  
ANISOU 3610  O   PHE D 136     2435   2158   2319    -84    104    511       O  
ATOM   3611  CB  PHE D 136      27.947 -45.026 -19.669  1.00 16.42           C  
ANISOU 3611  CB  PHE D 136     1950   1905   2386     15     87   1010       C  
ATOM   3612  CG  PHE D 136      27.271 -43.693 -19.766  1.00 19.26           C  
ANISOU 3612  CG  PHE D 136     2114   2143   3060   -300    131    921       C  
ATOM   3613  CD1 PHE D 136      26.203 -43.499 -20.626  1.00 19.53           C  
ANISOU 3613  CD1 PHE D 136     2111   2173   3135    -96    157    942       C  
ATOM   3614  CD2 PHE D 136      27.706 -42.629 -18.990  1.00 21.22           C  
ANISOU 3614  CD2 PHE D 136     2876   2142   3044   -338    366    544       C  
ATOM   3615  CE1 PHE D 136      25.582 -42.264 -20.714  1.00 20.06           C  
ANISOU 3615  CE1 PHE D 136     2554   1987   3082   -356    323    572       C  
ATOM   3616  CE2 PHE D 136      27.084 -41.389 -19.076  1.00 22.37           C  
ANISOU 3616  CE2 PHE D 136     3070   2292   3140   -307    317    140       C  
ATOM   3617  CZ  PHE D 136      26.023 -41.211 -19.945  1.00 21.71           C  
ANISOU 3617  CZ  PHE D 136     2855   2077   3317   -628    533    310       C  
ATOM   3618  N   GLY D 137      28.123 -47.984 -20.290  1.00 16.40           N  
ANISOU 3618  N   GLY D 137     1940   1572   2720     58    582    -33       N  
ATOM   3619  CA  GLY D 137      28.987 -49.147 -20.408  1.00 17.55           C  
ANISOU 3619  CA  GLY D 137     2337   1641   2690      5    657    416       C  
ATOM   3620  C   GLY D 137      28.409 -50.452 -19.897  1.00 17.27           C  
ANISOU 3620  C   GLY D 137     2150   1992   2421   -115     68    289       C  
ATOM   3621  O   GLY D 137      29.165 -51.370 -19.598  1.00 17.87           O  
ANISOU 3621  O   GLY D 137     2042   2335   2411    299     44    263       O  
ATOM   3622  N   ALA D 138      27.084 -50.547 -19.782  1.00 15.64           N  
ANISOU 3622  N   ALA D 138     1819   1784   2342    -68    233    380       N  
ATOM   3623  CA  ALA D 138      26.485 -51.732 -19.154  1.00 15.79           C  
ANISOU 3623  CA  ALA D 138     1836   1791   2372   -259    118    289       C  
ATOM   3624  C   ALA D 138      26.690 -53.003 -19.969  1.00 17.59           C  
ANISOU 3624  C   ALA D 138     2231   2055   2398    167   -123    476       C  
ATOM   3625  O   ALA D 138      26.513 -54.109 -19.444  1.00 19.95           O  
ANISOU 3625  O   ALA D 138     2646   2098   2835    144    159    552       O  
ATOM   3626  CB  ALA D 138      24.983 -51.510 -18.884  1.00 16.16           C  
ANISOU 3626  CB  ALA D 138     1597   1919   2623    -99    300    551       C  
ATOM   3627  N   ASN D 139      27.070 -52.880 -21.238  1.00 16.85           N  
ANISOU 3627  N   ASN D 139     1974   2140   2287    436   -365     99       N  
ATOM   3628  CA  ASN D 139      27.358 -54.092 -22.005  1.00 19.27           C  
ANISOU 3628  CA  ASN D 139     2391   2418   2514    501   -494   -149       C  
ATOM   3629  C   ASN D 139      28.861 -54.252 -22.263  1.00 18.64           C  
ANISOU 3629  C   ASN D 139     2094   2304   2683    203   -162    -89       C  
ATOM   3630  O   ASN D 139      29.273 -54.942 -23.194  1.00 22.98           O  
ANISOU 3630  O   ASN D 139     2706   3053   2973    475    147     67       O  
ATOM   3631  CB  ASN D 139      26.577 -54.112 -23.320  1.00 21.44           C  
ANISOU 3631  CB  ASN D 139     2735   2430   2982    764   -454   -418       C  
ATOM   3632  CG  ASN D 139      26.429 -55.526 -23.891  1.00 24.52           C  
ANISOU 3632  CG  ASN D 139     3112   2784   3420    977   -204    -49       C  
ATOM   3633  OD1 ASN D 139      26.382 -56.509 -23.146  1.00 26.11           O  
ANISOU 3633  OD1 ASN D 139     3342   2926   3654    762    -59   -647       O  
ATOM   3634  ND2 ASN D 139      26.366 -55.630 -25.210  1.00 27.74           N  
ANISOU 3634  ND2 ASN D 139     3705   3163   3673   1408    642    -44       N  
ATOM   3635  N   ASN D 140      29.683 -53.628 -21.423  1.00 18.35           N  
ANISOU 3635  N   ASN D 140     1846   2361   2764    420    -55    329       N  
ATOM   3636  CA  ASN D 140      31.136 -53.746 -21.571  1.00 20.15           C  
ANISOU 3636  CA  ASN D 140     1875   2566   3214    533    395    148       C  
ATOM   3637  C   ASN D 140      31.625 -55.169 -21.295  1.00 21.92           C  
ANISOU 3637  C   ASN D 140     1830   2910   3588    708    335    139       C  
ATOM   3638  O   ASN D 140      30.977 -55.933 -20.586  1.00 22.00           O  
ANISOU 3638  O   ASN D 140     1953   2979   3427    596    185    512       O  
ATOM   3639  CB  ASN D 140      31.857 -52.783 -20.635  1.00 21.40           C  
ANISOU 3639  CB  ASN D 140     2030   2612   3491     50    558    140       C  
ATOM   3640  CG  ASN D 140      31.796 -51.345 -21.103  1.00 22.02           C  
ANISOU 3640  CG  ASN D 140     2305   2700   3363     38    902    214       C  
ATOM   3641  OD1 ASN D 140      31.251 -51.036 -22.166  1.00 23.17           O  
ANISOU 3641  OD1 ASN D 140     2896   2591   3316     99    811    443       O  
ATOM   3642  ND2 ASN D 140      32.348 -50.447 -20.294  1.00 22.22           N  
ANISOU 3642  ND2 ASN D 140     2478   2916   3050   -388    667     31       N  
ATOM   3643  N   ALA D 141      32.787 -55.509 -21.830  1.00 20.98           N  
ANISOU 3643  N   ALA D 141     1579   2802   3590    911    312   -122       N  
ATOM   3644  CA  ALA D 141      33.284 -56.868 -21.706  1.00 21.32           C  
ANISOU 3644  CA  ALA D 141     1488   3031   3583    858    210    -43       C  
ATOM   3645  C   ALA D 141      33.848 -57.161 -20.317  1.00 23.15           C  
ANISOU 3645  C   ALA D 141     1705   3443   3646    422     34    388       C  
ATOM   3646  O   ALA D 141      33.669 -58.264 -19.797  1.00 25.37           O  
ANISOU 3646  O   ALA D 141     1886   3306   4447    525    616    554       O  
ATOM   3647  CB  ALA D 141      34.361 -57.138 -22.771  1.00 23.98           C  
ANISOU 3647  CB  ALA D 141     2033   3699   3379    758      5   -825       C  
ATOM   3648  N   PHE D 142      34.541 -56.197 -19.714  1.00 23.63           N  
ANISOU 3648  N   PHE D 142     1435   3859   3684    512     85    373       N  
ATOM   3649  CA  PHE D 142      35.345 -56.520 -18.526  1.00 24.27           C  
ANISOU 3649  CA  PHE D 142     1294   4441   3486    258    -60    313       C  
ATOM   3650  C   PHE D 142      35.086 -55.632 -17.318  1.00 26.11           C  
ANISOU 3650  C   PHE D 142     1675   4712   3532     71    106    422       C  
ATOM   3651  O   PHE D 142      35.143 -56.106 -16.183  1.00 27.28           O  
ANISOU 3651  O   PHE D 142     2116   4904   3347    229    258    573       O  
ATOM   3652  CB  PHE D 142      36.842 -56.471 -18.870  1.00 25.66           C  
ANISOU 3652  CB  PHE D 142     1319   4592   3837    485      0    339       C  
ATOM   3653  CG  PHE D 142      37.218 -57.353 -20.020  1.00 27.38           C  
ANISOU 3653  CG  PHE D 142     1397   4660   4347    637    101    384       C  
ATOM   3654  CD1 PHE D 142      37.059 -58.728 -19.936  1.00 30.19           C  
ANISOU 3654  CD1 PHE D 142     1859   4944   4668    819    230    673       C  
ATOM   3655  CD2 PHE D 142      37.704 -56.809 -21.193  1.00 27.82           C  
ANISOU 3655  CD2 PHE D 142     1566   4690   4314    429    536    556       C  
ATOM   3656  CE1 PHE D 142      37.389 -59.543 -21.003  1.00 31.74           C  
ANISOU 3656  CE1 PHE D 142     1904   5142   5012    816    298    649       C  
ATOM   3657  CE2 PHE D 142      38.042 -57.617 -22.262  1.00 29.23           C  
ANISOU 3657  CE2 PHE D 142     1723   4766   4619    987    -39    770       C  
ATOM   3658  CZ  PHE D 142      37.874 -58.983 -22.172  1.00 30.71           C  
ANISOU 3658  CZ  PHE D 142     1729   5095   4843    935    -34    676       C  
ATOM   3659  N   THR D 143      34.835 -54.348 -17.550  1.00 27.32           N  
ANISOU 3659  N   THR D 143     1881   4803   3698    -98     51    546       N  
ATOM   3660  CA ATHR D 143      34.557 -53.404 -16.464  0.73 27.21           C  
ANISOU 3660  CA ATHR D 143     1764   4820   3754    -16      4    690       C  
ATOM   3661  CA BTHR D 143      34.551 -53.422 -16.464  0.27 26.56           C  
ANISOU 3661  CA BTHR D 143     1981   4588   3523    -10   -129    731       C  
ATOM   3662  C   THR D 143      33.506 -52.399 -16.894  1.00 24.60           C  
ANISOU 3662  C   THR D 143     1723   4401   3221   -116   -325    671       C  
ATOM   3663  O   THR D 143      33.400 -52.079 -18.068  1.00 25.27           O  
ANISOU 3663  O   THR D 143     2372   3933   3298    321    -54    436       O  
ATOM   3664  CB ATHR D 143      35.802 -52.603 -16.019  0.73 30.46           C  
ANISOU 3664  CB ATHR D 143     1999   5331   4243   -303     54    744       C  
ATOM   3665  CB BTHR D 143      35.830 -52.697 -15.995  0.27 28.14           C  
ANISOU 3665  CB BTHR D 143     2481   4544   3667     55   -104    932       C  
ATOM   3666  OG1ATHR D 143      36.156 -51.670 -17.046  0.73 31.52           O  
ANISOU 3666  OG1ATHR D 143     2384   5229   4365   -776   -254    741       O  
ATOM   3667  OG1BTHR D 143      35.508 -51.778 -14.944  0.27 26.84           O  
ANISOU 3667  OG1BTHR D 143     2656   4205   3336    178   -405   1022       O  
ATOM   3668  CG2ATHR D 143      36.985 -53.509 -15.709  0.73 28.92           C  
ANISOU 3668  CG2ATHR D 143     1670   5530   3791   -419   -689    460       C  
ATOM   3669  CG2BTHR D 143      36.471 -51.940 -17.149  0.27 29.30           C  
ANISOU 3669  CG2BTHR D 143     2671   4595   3866    -37   -171    927       C  
ATOM   3670  N   MET D 144      32.730 -51.896 -15.939  1.00 24.30           N  
ANISOU 3670  N   MET D 144     1995   4439   2798   -118    -57    426       N  
ATOM   3671  CA  MET D 144      31.779 -50.837 -16.252  1.00 25.39           C  
ANISOU 3671  CA  MET D 144     2157   4503   2986   -635    399    514       C  
ATOM   3672  C   MET D 144      31.762 -49.826 -15.118  1.00 25.53           C  
ANISOU 3672  C   MET D 144     2279   4786   2635   -704    459    709       C  
ATOM   3673  O   MET D 144      32.042 -50.169 -13.967  1.00 27.42           O  
ANISOU 3673  O   MET D 144     2220   5430   2769   -189    124    526       O  
ATOM   3674  CB  MET D 144      30.373 -51.392 -16.514  1.00 24.42           C  
ANISOU 3674  CB  MET D 144     2015   4177   3089   -746     89    720       C  
ATOM   3675  CG  MET D 144      29.744 -52.071 -15.317  1.00 24.11           C  
ANISOU 3675  CG  MET D 144     1904   4005   3253   -598     15    838       C  
ATOM   3676  SD  MET D 144      28.062 -52.693 -15.609  1.00 23.50           S  
ANISOU 3676  SD  MET D 144     2286   3332   3311    444    147   1052       S  
ATOM   3677  CE  MET D 144      28.360 -54.049 -16.735  1.00 24.53           C  
ANISOU 3677  CE  MET D 144     2508   3258   3554    888    671    594       C  
ATOM   3678  N   PRO D 145      31.448 -48.569 -15.437  1.00 24.46           N  
ANISOU 3678  N   PRO D 145     2544   4345   2404  -1094     21    639       N  
ATOM   3679  CA  PRO D 145      31.388 -47.556 -14.385  1.00 23.24           C  
ANISOU 3679  CA  PRO D 145     2428   4082   2322  -1171     33    872       C  
ATOM   3680  C   PRO D 145      30.162 -47.728 -13.503  1.00 22.87           C  
ANISOU 3680  C   PRO D 145     2460   4231   2000   -992   -307    616       C  
ATOM   3681  O   PRO D 145      29.157 -48.334 -13.901  1.00 21.24           O  
ANISOU 3681  O   PRO D 145     2530   3439   2103   -378   -149    363       O  
ATOM   3682  CB  PRO D 145      31.321 -46.242 -15.171  1.00 24.97           C  
ANISOU 3682  CB  PRO D 145     2811   3910   2765  -1272     24    646       C  
ATOM   3683  CG  PRO D 145      30.682 -46.610 -16.445  1.00 24.84           C  
ANISOU 3683  CG  PRO D 145     2851   3941   2645  -1212   -374    764       C  
ATOM   3684  CD  PRO D 145      31.187 -47.992 -16.767  1.00 25.38           C  
ANISOU 3684  CD  PRO D 145     3061   4103   2480   -667    -28    901       C  
ATOM   3685  N   LEU D 146      30.267 -47.175 -12.301  1.00 25.29           N  
ANISOU 3685  N   LEU D 146     2524   4847   2238  -1374     83    357       N  
ATOM   3686  CA  LEU D 146      29.222 -47.246 -11.306  1.00 26.11           C  
ANISOU 3686  CA  LEU D 146     2982   4943   1998  -1768    166    574       C  
ATOM   3687  C   LEU D 146      29.114 -45.911 -10.581  1.00 26.37           C  
ANISOU 3687  C   LEU D 146     2900   4901   2217  -2046   -182    188       C  
ATOM   3688  O   LEU D 146      30.128 -45.332 -10.170  1.00 30.79           O  
ANISOU 3688  O   LEU D 146     3203   5737   2760  -2124   -240    398       O  
ATOM   3689  CB  LEU D 146      29.521 -48.371 -10.311  1.00 27.83           C  
ANISOU 3689  CB  LEU D 146     3008   5148   2419  -1423   -313    930       C  
ATOM   3690  CG  LEU D 146      28.466 -48.563  -9.236  1.00 30.13           C  
ANISOU 3690  CG  LEU D 146     3371   5204   2874  -1056    290   1107       C  
ATOM   3691  CD1 LEU D 146      27.232 -49.153  -9.881  1.00 30.80           C  
ANISOU 3691  CD1 LEU D 146     3090   5424   3188  -1250    423    675       C  
ATOM   3692  CD2 LEU D 146      28.970 -49.450  -8.117  1.00 32.39           C  
ANISOU 3692  CD2 LEU D 146     3998   5093   3217   -416    336   1389       C  
ATOM   3693  N   HIS D 147      27.891 -45.413 -10.443  1.00 26.61           N  
ANISOU 3693  N   HIS D 147     3503   4534   2074  -1869    290    191       N  
ATOM   3694  CA  HIS D 147      27.645 -44.201  -9.665  1.00 27.10           C  
ANISOU 3694  CA  HIS D 147     3694   4440   2164  -2171     94   -198       C  
ATOM   3695  C   HIS D 147      27.008 -44.606  -8.347  1.00 29.23           C  
ANISOU 3695  C   HIS D 147     3934   4948   2223  -2361   -192   -179       C  
ATOM   3696  O   HIS D 147      26.039 -45.354  -8.339  1.00 29.47           O  
ANISOU 3696  O   HIS D 147     4042   4612   2543  -2542    111   -361       O  
ATOM   3697  CB  HIS D 147      26.727 -43.228 -10.421  1.00 32.26           C  
ANISOU 3697  CB  HIS D 147     4686   4617   2954  -1679    386    246       C  
ATOM   3698  CG  HIS D 147      27.404 -42.469 -11.522  1.00 34.30           C  
ANISOU 3698  CG  HIS D 147     5022   4584   3425  -1441    232    349       C  
ATOM   3699  ND1 HIS D 147      26.707 -41.699 -12.430  1.00 36.02           N  
ANISOU 3699  ND1 HIS D 147     5407   4359   3919  -1445    838    225       N  
ATOM   3700  CD2 HIS D 147      28.710 -42.363 -11.866  1.00 33.37           C  
ANISOU 3700  CD2 HIS D 147     4762   4556   3361  -1725    -32    295       C  
ATOM   3701  CE1 HIS D 147      27.555 -41.144 -13.279  1.00 34.63           C  
ANISOU 3701  CE1 HIS D 147     5217   4272   3669  -1782    330    112       C  
ATOM   3702  NE2 HIS D 147      28.777 -41.531 -12.959  1.00 33.15           N  
ANISOU 3702  NE2 HIS D 147     4687   4259   3648  -2003     15    163       N  
ATOM   3703  N   MET D 148      27.546 -44.119  -7.237  1.00 29.87           N  
ANISOU 3703  N   MET D 148     4079   5227   2044  -2711    129   -156       N  
ATOM   3704  CA  MET D 148      27.012 -44.460  -5.931  1.00 33.62           C  
ANISOU 3704  CA  MET D 148     4145   6035   2593  -2853   -266     87       C  
ATOM   3705  C   MET D 148      26.507 -43.230  -5.187  1.00 36.41           C  
ANISOU 3705  C   MET D 148     4752   5997   3086  -3056    -10   -231       C  
ATOM   3706  O   MET D 148      27.158 -42.190  -5.193  1.00 38.49           O  
ANISOU 3706  O   MET D 148     5128   5929   3566  -3265    489   -403       O  
ATOM   3707  CB  MET D 148      28.081 -45.165  -5.102  1.00 35.64           C  
ANISOU 3707  CB  MET D 148     3729   6968   2844  -2394   -758    791       C  
ATOM   3708  CG  MET D 148      28.466 -46.522  -5.645  1.00 39.62           C  
ANISOU 3708  CG  MET D 148     4111   7738   3204  -2605   -823    787       C  
ATOM   3709  SD  MET D 148      30.104 -47.022  -5.099  1.00 42.07           S  
ANISOU 3709  SD  MET D 148     4710   8246   3029  -2609   -510   1216       S  
ATOM   3710  CE  MET D 148      31.134 -46.109  -6.251  1.00 40.53           C  
ANISOU 3710  CE  MET D 148     4343   8054   3004  -2681   -191   1284       C  
ATOM   3711  N   THR D 149      25.347 -43.347  -4.553  1.00 34.94           N  
ANISOU 3711  N   THR D 149     4874   5834   2566  -3030   -303    -71       N  
ATOM   3712  CA  THR D 149      24.871 -42.295  -3.667  1.00 35.96           C  
ANISOU 3712  CA  THR D 149     5278   5779   2605  -2992   -495    104       C  
ATOM   3713  C   THR D 149      24.798 -42.834  -2.245  1.00 36.84           C  
ANISOU 3713  C   THR D 149     5470   5599   2929  -3059   -600    -69       C  
ATOM   3714  O   THR D 149      24.402 -43.980  -2.016  1.00 35.68           O  
ANISOU 3714  O   THR D 149     5784   5126   2645  -2478   -338    304       O  
ATOM   3715  CB  THR D 149      23.498 -41.740  -4.100  1.00 42.26           C  
ANISOU 3715  CB  THR D 149     6187   6279   3592  -2646    192    675       C  
ATOM   3716  OG1 THR D 149      22.548 -42.805  -4.176  1.00 45.73           O  
ANISOU 3716  OG1 THR D 149     6615   6504   4257  -2284    -82    604       O  
ATOM   3717  CG2 THR D 149      23.598 -41.075  -5.463  1.00 42.79           C  
ANISOU 3717  CG2 THR D 149     6371   6632   3256  -2358    732   1038       C  
ATOM   3718  N   PHE D 150      25.201 -42.002  -1.293  1.00 38.21           N  
ANISOU 3718  N   PHE D 150     5698   5997   2821  -3012   -327   -450       N  
ATOM   3719  CA  PHE D 150      25.282 -42.402   0.104  1.00 40.34           C  
ANISOU 3719  CA  PHE D 150     5697   6659   2971  -2898   -282   -103       C  
ATOM   3720  C   PHE D 150      24.174 -41.756   0.926  1.00 41.63           C  
ANISOU 3720  C   PHE D 150     5768   6796   3254  -2771   -253   -123       C  
ATOM   3721  O   PHE D 150      23.994 -40.536   0.896  1.00 40.88           O  
ANISOU 3721  O   PHE D 150     5606   6753   3172  -2750   -490   -496       O  
ATOM   3722  CB  PHE D 150      26.652 -42.031   0.689  1.00 40.81           C  
ANISOU 3722  CB  PHE D 150     5673   6950   2882  -3112   -566   -274       C  
ATOM   3723  CG  PHE D 150      27.787 -42.882   0.178  1.00 41.94           C  
ANISOU 3723  CG  PHE D 150     5554   7447   2935  -2969   -262    -80       C  
ATOM   3724  CD1 PHE D 150      28.201 -42.801  -1.146  1.00 44.03           C  
ANISOU 3724  CD1 PHE D 150     5710   7786   3235  -2812   -298     46       C  
ATOM   3725  CD2 PHE D 150      28.445 -43.760   1.024  1.00 43.39           C  
ANISOU 3725  CD2 PHE D 150     5608   7626   3252  -2920   -278    -74       C  
ATOM   3726  CE1 PHE D 150      29.245 -43.584  -1.612  1.00 43.27           C  
ANISOU 3726  CE1 PHE D 150     5478   7799   3163  -2995   -293     73       C  
ATOM   3727  CE2 PHE D 150      29.490 -44.544   0.563  1.00 43.95           C  
ANISOU 3727  CE2 PHE D 150     5605   7653   3441  -2908    -43     73       C  
ATOM   3728  CZ  PHE D 150      29.889 -44.457  -0.754  1.00 44.07           C  
ANISOU 3728  CZ  PHE D 150     5449   7694   3600  -3105    -85    147       C  
ATOM   3729  N   TRP D 151      23.433 -42.589   1.650  1.00 40.63           N  
ANISOU 3729  N   TRP D 151     5800   6874   2762  -2637   -486    160       N  
ATOM   3730  CA  TRP D 151      22.386 -42.125   2.552  1.00 41.01           C  
ANISOU 3730  CA  TRP D 151     6275   6807   2502  -2383   -756   -141       C  
ATOM   3731  C   TRP D 151      22.693 -42.533   3.982  1.00 43.26           C  
ANISOU 3731  C   TRP D 151     6808   7108   2521  -2292   -584   -215       C  
ATOM   3732  O   TRP D 151      23.229 -43.613   4.224  1.00 44.73           O  
ANISOU 3732  O   TRP D 151     7311   7245   2441  -1738   -345   -315       O  
ATOM   3733  CB  TRP D 151      21.028 -42.701   2.154  1.00 41.73           C  
ANISOU 3733  CB  TRP D 151     6451   6423   2982  -2479  -1012   -565       C  
ATOM   3734  CG  TRP D 151      20.450 -42.166   0.885  1.00 44.24           C  
ANISOU 3734  CG  TRP D 151     7281   6209   3317  -2353   -289   -937       C  
ATOM   3735  CD1 TRP D 151      20.790 -42.524  -0.389  1.00 43.39           C  
ANISOU 3735  CD1 TRP D 151     7359   6019   3108  -2297   -325  -1167       C  
ATOM   3736  CD2 TRP D 151      19.397 -41.202   0.765  1.00 45.94           C  
ANISOU 3736  CD2 TRP D 151     7721   6003   3732  -2227     55  -1122       C  
ATOM   3737  NE1 TRP D 151      20.024 -41.829  -1.295  1.00 46.78           N  
ANISOU 3737  NE1 TRP D 151     7690   6031   4052  -2161    -24  -1240       N  
ATOM   3738  CE2 TRP D 151      19.161 -41.011  -0.610  1.00 47.50           C  
ANISOU 3738  CE2 TRP D 151     7939   6055   4053  -2129    121  -1163       C  
ATOM   3739  CE3 TRP D 151      18.638 -40.473   1.689  1.00 47.29           C  
ANISOU 3739  CE3 TRP D 151     8043   5969   3957  -2294    136   -929       C  
ATOM   3740  CZ2 TRP D 151      18.195 -40.124  -1.086  1.00 48.94           C  
ANISOU 3740  CZ2 TRP D 151     8104   6024   4468  -2015    287  -1195       C  
ATOM   3741  CZ3 TRP D 151      17.678 -39.598   1.217  1.00 48.77           C  
ANISOU 3741  CZ3 TRP D 151     8230   6064   4236  -2139    364  -1086       C  
ATOM   3742  CH2 TRP D 151      17.467 -39.428  -0.161  1.00 48.76           C  
ANISOU 3742  CH2 TRP D 151     8158   6129   4241  -2085    327  -1093       C  
ATOM   3743  N   GLY D 152      22.332 -41.684   4.935  1.00 43.26           N  
ANISOU 3743  N   GLY D 152     6661   7120   2654  -2669   -558   -390       N  
ATOM   3744  CA  GLY D 152      22.500 -42.048   6.328  1.00 44.52           C  
ANISOU 3744  CA  GLY D 152     6848   7195   2873  -2817   -414   -759       C  
ATOM   3745  C   GLY D 152      22.081 -40.967   7.296  1.00 47.95           C  
ANISOU 3745  C   GLY D 152     7257   7664   3296  -2993   -235  -1229       C  
ATOM   3746  O   GLY D 152      21.594 -39.910   6.894  1.00 45.16           O  
ANISOU 3746  O   GLY D 152     6710   7317   3131  -3009   -227  -1074       O  
ATOM   3747  N   LYS D 153      22.272 -41.239   8.582  1.00 52.39           N  
ANISOU 3747  N   LYS D 153     7883   8379   3645  -3000   -546  -1394       N  
ATOM   3748  CA  LYS D 153      21.962 -40.268   9.618  1.00 59.52           C  
ANISOU 3748  CA  LYS D 153     8883   9308   4423  -3427   -154  -1796       C  
ATOM   3749  C   LYS D 153      23.079 -39.242   9.713  1.00 63.02           C  
ANISOU 3749  C   LYS D 153     8948   9921   5077  -3669   -728  -2138       C  
ATOM   3750  O   LYS D 153      24.255 -39.588   9.598  1.00 61.75           O  
ANISOU 3750  O   LYS D 153     8549   9679   5233  -3541  -1078  -2014       O  
ATOM   3751  CB  LYS D 153      21.760 -40.956  10.968  1.00 62.34           C  
ANISOU 3751  CB  LYS D 153     9477   9649   4560  -3336    551  -1566       C  
ATOM   3752  CG  LYS D 153      20.620 -41.958  11.000  1.00 65.10           C  
ANISOU 3752  CG  LYS D 153    10029   9922   4785  -3211    875  -1433       C  
ATOM   3753  CD  LYS D 153      20.376 -42.450  12.419  1.00 67.18           C  
ANISOU 3753  CD  LYS D 153    10387  10134   5007  -3138    954  -1243       C  
ATOM   3754  CE  LYS D 153      19.208 -43.420  12.485  1.00 68.44           C  
ANISOU 3754  CE  LYS D 153    10572  10286   5148  -3127    824  -1205       C  
ATOM   3755  NZ  LYS D 153      19.485 -44.673  11.730  1.00 70.17           N  
ANISOU 3755  NZ  LYS D 153    10673  10377   5610  -3029    977  -1041       N  
ATOM   3756  N   GLU D 154      22.702 -37.985   9.926  1.00 67.37           N  
ANISOU 3756  N   GLU D 154     9283  10580   5734  -3779  -1110  -2306       N  
ATOM   3757  CA  GLU D 154      23.657 -36.886  10.031  1.00 71.88           C  
ANISOU 3757  CA  GLU D 154     9654  11136   6521  -3529  -1288  -2234       C  
ATOM   3758  C   GLU D 154      24.753 -37.162  11.055  1.00 70.76           C  
ANISOU 3758  C   GLU D 154     9447  11186   6251  -3331  -1863  -2493       C  
ATOM   3759  O   GLU D 154      25.878 -36.687  10.912  1.00 69.27           O  
ANISOU 3759  O   GLU D 154     9191  10767   6359  -3235  -1995  -2499       O  
ATOM   3760  CB  GLU D 154      22.930 -35.589  10.390  1.00 76.01           C  
ANISOU 3760  CB  GLU D 154    10046  11564   7270  -3552  -1136  -1944       C  
ATOM   3761  CG  GLU D 154      22.886 -34.588   9.255  1.00 79.67           C  
ANISOU 3761  CG  GLU D 154    10398  11979   7893  -3506  -1099  -1670       C  
ATOM   3762  CD  GLU D 154      24.273 -34.179   8.805  1.00 82.05           C  
ANISOU 3762  CD  GLU D 154    10693  12296   8187  -3499  -1043  -1449       C  
ATOM   3763  OE1 GLU D 154      24.656 -34.532   7.672  1.00 82.49           O  
ANISOU 3763  OE1 GLU D 154    10807  12339   8197  -3538  -1018  -1351       O  
ATOM   3764  OE2 GLU D 154      24.981 -33.509   9.586  1.00 83.16           O  
ANISOU 3764  OE2 GLU D 154    10830  12448   8320  -3473   -978  -1315       O  
ATOM   3765  N   GLU D 155      24.420 -37.955  12.069  1.00 72.23           N  
ANISOU 3765  N   GLU D 155     9409  11680   6354  -3191  -2017  -2390       N  
ATOM   3766  CA AGLU D 155      25.357 -38.284  13.139  0.54 72.90           C  
ANISOU 3766  CA AGLU D 155     9322  11914   6462  -3107  -2079  -2178       C  
ATOM   3767  CA BGLU D 155      25.358 -38.281  13.138  0.46 72.61           C  
ANISOU 3767  CA BGLU D 155     9298  11915   6374  -3089  -2051  -2207       C  
ATOM   3768  C   GLU D 155      26.515 -39.150  12.646  1.00 72.03           C  
ANISOU 3768  C   GLU D 155     9125  11893   6349  -3105  -2192  -2039       C  
ATOM   3769  O   GLU D 155      27.503 -39.339  13.356  1.00 70.65           O  
ANISOU 3769  O   GLU D 155     9040  11867   5938  -3009  -2355  -1902       O  
ATOM   3770  CB AGLU D 155      24.629 -38.996  14.284  0.54 73.88           C  
ANISOU 3770  CB AGLU D 155     9343  12112   6616  -3034  -2063  -2090       C  
ATOM   3771  CB BGLU D 155      24.628 -38.989  14.282  0.46 73.21           C  
ANISOU 3771  CB BGLU D 155     9295  12122   6398  -2974  -1944  -2175       C  
ATOM   3772  CG AGLU D 155      23.706 -38.103  15.106  0.54 74.51           C  
ANISOU 3772  CG AGLU D 155     9307  12237   6765  -3005  -2106  -2018       C  
ATOM   3773  CG BGLU D 155      24.114 -40.374  13.925  0.46 73.55           C  
ANISOU 3773  CG BGLU D 155     9269  12271   6404  -2878  -1865  -2147       C  
ATOM   3774  CD AGLU D 155      22.418 -37.750  14.384  0.54 74.79           C  
ANISOU 3774  CD AGLU D 155     9241  12266   6910  -2994  -2127  -1993       C  
ATOM   3775  CD BGLU D 155      23.192 -40.946  14.983  0.46 73.78           C  
ANISOU 3775  CD BGLU D 155     9296  12399   6339  -2730  -1793  -2127       C  
ATOM   3776  OE1AGLU D 155      21.755 -36.775  14.799  0.54 75.74           O  
ANISOU 3776  OE1AGLU D 155     9277  12361   7140  -2921  -1842  -1789       O  
ATOM   3777  OE1BGLU D 155      22.235 -40.248  15.378  0.46 74.28           O  
ANISOU 3777  OE1BGLU D 155     9323  12482   6417  -2759  -1655  -2098       O  
ATOM   3778  OE2AGLU D 155      22.065 -38.446  13.409  0.54 73.56           O  
ANISOU 3778  OE2AGLU D 155     9104  12178   6668  -3089  -2496  -2253       O  
ATOM   3779  OE2BGLU D 155      23.425 -42.093  15.421  0.46 73.19           O  
ANISOU 3779  OE2BGLU D 155     9275  12390   6143  -2598  -1893  -2106       O  
ATOM   3780  N   ASN D 156      26.391 -39.674  11.430  1.00 71.42           N  
ANISOU 3780  N   ASN D 156     8886  11817   6433  -3140  -2234  -1809       N  
ATOM   3781  CA  ASN D 156      27.411 -40.559  10.874  1.00 70.18           C  
ANISOU 3781  CA  ASN D 156     8691  11534   6441  -3218  -2446  -1658       C  
ATOM   3782  C   ASN D 156      28.108 -40.004   9.634  1.00 69.18           C  
ANISOU 3782  C   ASN D 156     8550  11223   6510  -3213  -2652  -1623       C  
ATOM   3783  O   ASN D 156      29.039 -40.623   9.119  1.00 67.82           O  
ANISOU 3783  O   ASN D 156     8490  10905   6373  -3156  -2553  -1700       O  
ATOM   3784  CB  ASN D 156      26.796 -41.919  10.536  1.00 68.30           C  
ANISOU 3784  CB  ASN D 156     8541  11287   6125  -3014  -2658  -1477       C  
ATOM   3785  CG  ASN D 156      26.325 -42.666  11.766  1.00 67.19           C  
ANISOU 3785  CG  ASN D 156     8549  11227   5754  -2726  -2786  -1180       C  
ATOM   3786  OD1 ASN D 156      26.944 -42.588  12.828  1.00 66.57           O  
ANISOU 3786  OD1 ASN D 156     8657  11260   5375  -2456  -2823   -932       O  
ATOM   3787  ND2 ASN D 156      25.222 -43.393  11.630  1.00 66.88           N  
ANISOU 3787  ND2 ASN D 156     8603  11231   5577  -2770  -2644  -1158       N  
ATOM   3788  N   ARG D 157      27.664 -38.840   9.165  1.00 70.99           N  
ANISOU 3788  N   ARG D 157     8546  11515   6913  -3416  -2776  -1493       N  
ATOM   3789  CA  ARG D 157      28.197 -38.253   7.937  1.00 73.87           C  
ANISOU 3789  CA  ARG D 157     8659  11994   7415  -3800  -2753  -1426       C  
ATOM   3790  C   ARG D 157      29.706 -38.044   8.010  1.00 73.81           C  
ANISOU 3790  C   ARG D 157     8452  11928   7663  -3878  -2758  -1358       C  
ATOM   3791  O   ARG D 157      30.418 -38.249   7.029  1.00 73.22           O  
ANISOU 3791  O   ARG D 157     8173  11689   7958  -4028  -2597  -1342       O  
ATOM   3792  CB  ARG D 157      27.511 -36.918   7.628  1.00 76.09           C  
ANISOU 3792  CB  ARG D 157     8970  12371   7571  -3899  -2737  -1391       C  
ATOM   3793  CG  ARG D 157      28.040 -36.240   6.367  1.00 78.95           C  
ANISOU 3793  CG  ARG D 157     9441  12711   7846  -3713  -2389  -1115       C  
ATOM   3794  CD  ARG D 157      27.632 -34.778   6.285  1.00 80.75           C  
ANISOU 3794  CD  ARG D 157     9780  12936   7964  -3607  -2271  -1056       C  
ATOM   3795  NE  ARG D 157      26.209 -34.619   6.009  1.00 82.48           N  
ANISOU 3795  NE  ARG D 157    10095  13049   8197  -3632  -2119  -1070       N  
ATOM   3796  CZ  ARG D 157      25.694 -34.472   4.793  1.00 83.96           C  
ANISOU 3796  CZ  ARG D 157    10315  13091   8495  -3768  -1985  -1192       C  
ATOM   3797  NH1 ARG D 157      26.487 -34.464   3.729  1.00 85.21           N  
ANISOU 3797  NH1 ARG D 157    10500  13116   8761  -3795  -1727  -1235       N  
ATOM   3798  NH2 ARG D 157      24.385 -34.332   4.640  1.00 84.06           N  
ANISOU 3798  NH2 ARG D 157    10275  13121   8542  -3794  -2131  -1124       N  
ATOM   3799  N   LYS D 158      30.187 -37.644   9.182  1.00 74.60           N  
ANISOU 3799  N   LYS D 158     8656  12123   7564  -3759  -2920  -1343       N  
ATOM   3800  CA  LYS D 158      31.605 -37.366   9.370  1.00 76.96           C  
ANISOU 3800  CA  LYS D 158     9167  12534   7540  -3685  -2723  -1418       C  
ATOM   3801  C   LYS D 158      32.436 -38.644   9.291  1.00 74.53           C  
ANISOU 3801  C   LYS D 158     8975  12178   7165  -3584  -2783  -1689       C  
ATOM   3802  O   LYS D 158      33.501 -38.666   8.674  1.00 75.19           O  
ANISOU 3802  O   LYS D 158     9031  12267   7269  -3707  -2671  -1829       O  
ATOM   3803  CB  LYS D 158      31.838 -36.669  10.711  1.00 81.55           C  
ANISOU 3803  CB  LYS D 158     9857  13083   8043  -3778  -2328  -1360       C  
ATOM   3804  CG  LYS D 158      33.237 -36.107  10.880  1.00 86.11           C  
ANISOU 3804  CG  LYS D 158    10409  13564   8746  -3714  -1920  -1044       C  
ATOM   3805  CD  LYS D 158      33.459 -34.902   9.979  1.00 89.85           C  
ANISOU 3805  CD  LYS D 158    10863  13924   9352  -3668  -1566   -834       C  
ATOM   3806  CE  LYS D 158      32.526 -33.759  10.349  1.00 92.43           C  
ANISOU 3806  CE  LYS D 158    11199  14153   9768  -3667  -1342   -696       C  
ATOM   3807  NZ  LYS D 158      32.750 -32.558   9.498  1.00 93.68           N  
ANISOU 3807  NZ  LYS D 158    11361  14264   9970  -3675  -1253   -641       N  
ATOM   3808  N   ALA D 159      31.940 -39.705   9.919  1.00 71.58           N  
ANISOU 3808  N   ALA D 159     8613  11616   6966  -3312  -2847  -1605       N  
ATOM   3809  CA  ALA D 159      32.650 -40.978   9.950  1.00 71.47           C  
ANISOU 3809  CA  ALA D 159     8496  11839   6821  -3541  -2697  -1319       C  
ATOM   3810  C   ALA D 159      32.765 -41.588   8.553  1.00 72.31           C  
ANISOU 3810  C   ALA D 159     8346  12281   6847  -3966  -2443   -939       C  
ATOM   3811  O   ALA D 159      33.746 -42.263   8.237  1.00 72.35           O  
ANISOU 3811  O   ALA D 159     8167  12301   7020  -4036  -2463   -869       O  
ATOM   3812  CB  ALA D 159      31.954 -41.947  10.898  1.00 70.99           C  
ANISOU 3812  CB  ALA D 159     8418  11820   6735  -3402  -2803  -1190       C  
ATOM   3813  N   VAL D 160      31.759 -41.351   7.719  1.00 72.36           N  
ANISOU 3813  N   VAL D 160     8271  12492   6730  -4176  -2207   -637       N  
ATOM   3814  CA  VAL D 160      31.788 -41.847   6.350  1.00 71.97           C  
ANISOU 3814  CA  VAL D 160     8104  12546   6695  -4444  -2036   -620       C  
ATOM   3815  C   VAL D 160      32.870 -41.135   5.542  1.00 71.57           C  
ANISOU 3815  C   VAL D 160     7889  12476   6827  -4750  -1678   -434       C  
ATOM   3816  O   VAL D 160      33.696 -41.780   4.894  1.00 69.82           O  
ANISOU 3816  O   VAL D 160     7485  12114   6929  -5034  -1135   -311       O  
ATOM   3817  CB  VAL D 160      30.425 -41.672   5.654  1.00 72.02           C  
ANISOU 3817  CB  VAL D 160     8255  12598   6513  -4238  -2137   -777       C  
ATOM   3818  CG1 VAL D 160      30.533 -42.015   4.174  1.00 72.11           C  
ANISOU 3818  CG1 VAL D 160     8332  12533   6533  -4087  -2233   -917       C  
ATOM   3819  CG2 VAL D 160      29.371 -42.531   6.334  1.00 71.93           C  
ANISOU 3819  CG2 VAL D 160     8307  12710   6314  -4206  -2075   -758       C  
ATOM   3820  N   SER D 161      32.865 -39.805   5.596  1.00 71.93           N  
ANISOU 3820  N   SER D 161     7969  12543   6818  -4643  -1950   -391       N  
ATOM   3821  CA  SER D 161      33.824 -38.996   4.850  1.00 73.60           C  
ANISOU 3821  CA  SER D 161     8145  12905   6915  -4644  -2008   -521       C  
ATOM   3822  C   SER D 161      35.256 -39.292   5.277  1.00 75.88           C  
ANISOU 3822  C   SER D 161     8140  13218   7472  -4673  -2033   -422       C  
ATOM   3823  O   SER D 161      36.160 -39.355   4.445  1.00 76.91           O  
ANISOU 3823  O   SER D 161     8089  13358   7777  -4894  -1747   -353       O  
ATOM   3824  CB  SER D 161      33.525 -37.504   5.027  1.00 74.99           C  
ANISOU 3824  CB  SER D 161     8412  13004   7077  -4653  -1367   -613       C  
ATOM   3825  OG  SER D 161      32.322 -37.137   4.373  1.00 76.83           O  
ANISOU 3825  OG  SER D 161     8716  13046   7430  -4666   -495   -675       O  
ATOM   3826  N   ASP D 162      35.456 -39.480   6.577  1.00 76.31           N  
ANISOU 3826  N   ASP D 162     8120  13196   7679  -4502  -2414   -510       N  
ATOM   3827  CA  ASP D 162      36.784 -39.765   7.110  1.00 77.18           C  
ANISOU 3827  CA  ASP D 162     8173  13398   7752  -4368  -2478   -446       C  
ATOM   3828  C   ASP D 162      37.255 -41.154   6.688  1.00 75.29           C  
ANISOU 3828  C   ASP D 162     7763  13232   7611  -4269  -2437   -211       C  
ATOM   3829  O   ASP D 162      38.450 -41.389   6.519  1.00 75.58           O  
ANISOU 3829  O   ASP D 162     7682  13428   7607  -4157  -2613    -50       O  
ATOM   3830  CB  ASP D 162      36.790 -39.639   8.634  1.00 79.61           C  
ANISOU 3830  CB  ASP D 162     8607  13559   8080  -4380  -2335   -700       C  
ATOM   3831  CG  ASP D 162      36.574 -38.211   9.100  1.00 81.17           C  
ANISOU 3831  CG  ASP D 162     8896  13569   8377  -4310  -2257   -834       C  
ATOM   3832  OD1 ASP D 162      36.778 -37.285   8.286  1.00 82.97           O  
ANISOU 3832  OD1 ASP D 162     9006  13661   8858  -4521  -1810   -828       O  
ATOM   3833  OD2 ASP D 162      36.205 -38.015  10.278  1.00 79.00           O  
ANISOU 3833  OD2 ASP D 162     8790  13339   7888  -4138  -2894  -1085       O  
ATOM   3834  N   GLN D 163      36.311 -42.071   6.509  1.00 71.70           N  
ANISOU 3834  N   GLN D 163     7326  12582   7334  -4177  -2283   -205       N  
ATOM   3835  CA  GLN D 163      36.639 -43.417   6.059  1.00 70.52           C  
ANISOU 3835  CA  GLN D 163     7055  12703   7035  -4439  -1832     76       C  
ATOM   3836  C   GLN D 163      37.064 -43.423   4.596  1.00 71.26           C  
ANISOU 3836  C   GLN D 163     7174  12872   7032  -4506  -1558    529       C  
ATOM   3837  O   GLN D 163      38.036 -44.081   4.227  1.00 71.30           O  
ANISOU 3837  O   GLN D 163     7171  13134   6787  -4326  -1609    899       O  
ATOM   3838  CB  GLN D 163      35.449 -44.360   6.258  1.00 68.79           C  
ANISOU 3838  CB  GLN D 163     6813  12536   6789  -4466  -1536     33       C  
ATOM   3839  CG  GLN D 163      35.608 -45.719   5.585  1.00 67.16           C  
ANISOU 3839  CG  GLN D 163     6633  12612   6274  -4213  -1566    107       C  
ATOM   3840  CD  GLN D 163      36.720 -46.565   6.186  1.00 65.64           C  
ANISOU 3840  CD  GLN D 163     6478  12660   5802  -3824  -1764    446       C  
ATOM   3841  OE1 GLN D 163      37.331 -46.194   7.186  1.00 65.33           O  
ANISOU 3841  OE1 GLN D 163     6440  12551   5832  -3485  -2020    532       O  
ATOM   3842  NE2 GLN D 163      36.981 -47.714   5.576  1.00 65.32           N  
ANISOU 3842  NE2 GLN D 163     6323  12765   5729  -3751  -1778    814       N  
ATOM   3843  N   LEU D 164      36.322 -42.696   3.767  1.00 70.69           N  
ANISOU 3843  N   LEU D 164     7102  12614   7142  -4719  -1688    405       N  
ATOM   3844  CA  LEU D 164      36.651 -42.569   2.352  1.00 69.92           C  
ANISOU 3844  CA  LEU D 164     7130  12364   7074  -4725  -1680    376       C  
ATOM   3845  C   LEU D 164      37.978 -41.845   2.144  1.00 71.18           C  
ANISOU 3845  C   LEU D 164     7194  12448   7406  -4723  -1808    367       C  
ATOM   3846  O   LEU D 164      38.799 -42.264   1.328  1.00 70.19           O  
ANISOU 3846  O   LEU D 164     7025  12147   7498  -4492  -2000    399       O  
ATOM   3847  CB  LEU D 164      35.537 -41.834   1.608  1.00 68.44           C  
ANISOU 3847  CB  LEU D 164     7091  12134   6781  -4775  -1517    434       C  
ATOM   3848  CG  LEU D 164      34.208 -42.585   1.521  1.00 66.23           C  
ANISOU 3848  CG  LEU D 164     6931  11806   6427  -4680  -1488    565       C  
ATOM   3849  CD1 LEU D 164      33.203 -41.798   0.698  1.00 67.34           C  
ANISOU 3849  CD1 LEU D 164     7057  11891   6637  -4940  -1148    461       C  
ATOM   3850  CD2 LEU D 164      34.432 -43.967   0.934  1.00 64.98           C  
ANISOU 3850  CD2 LEU D 164     6819  11659   6212  -4496  -1641    677       C  
ATOM   3851  N   LYS D 165      38.177 -40.759   2.887  1.00 73.00           N  
ANISOU 3851  N   LYS D 165     7434  12587   7717  -4830  -1802     32       N  
ATOM   3852  CA  LYS D 165      39.394 -39.952   2.783  1.00 76.07           C  
ANISOU 3852  CA  LYS D 165     7736  13061   8107  -5197  -1538   -102       C  
ATOM   3853  C   LYS D 165      40.620 -40.746   3.230  1.00 76.25           C  
ANISOU 3853  C   LYS D 165     7565  13295   8113  -5223  -1347    -50       C  
ATOM   3854  O   LYS D 165      41.739 -40.486   2.788  1.00 77.28           O  
ANISOU 3854  O   LYS D 165     7548  13328   8486  -5374   -975    -71       O  
ATOM   3855  CB  LYS D 165      39.255 -38.670   3.608  1.00 78.07           C  
ANISOU 3855  CB  LYS D 165     8163  13223   8277  -5343  -1700   -249       C  
ATOM   3856  CG  LYS D 165      40.361 -37.650   3.378  1.00 80.88           C  
ANISOU 3856  CG  LYS D 165     8667  13596   8468  -5569  -1568   -314       C  
ATOM   3857  CD  LYS D 165      40.057 -36.339   4.083  1.00 82.37           C  
ANISOU 3857  CD  LYS D 165     8973  13867   8456  -5687  -1807   -379       C  
ATOM   3858  CE  LYS D 165      39.925 -36.534   5.585  1.00 84.01           C  
ANISOU 3858  CE  LYS D 165     9275  14099   8545  -5488  -1822   -205       C  
ATOM   3859  NZ  LYS D 165      39.759 -35.237   6.301  1.00 85.70           N  
ANISOU 3859  NZ  LYS D 165     9583  14288   8692  -5174  -1634    -39       N  
ATOM   3860  N   LYS D 166      40.395 -41.714   4.110  1.00 75.37           N  
ANISOU 3860  N   LYS D 166     7480  13502   7655  -5086  -1494     93       N  
ATOM   3861  CA  LYS D 166      41.428 -42.651   4.532  1.00 75.24           C  
ANISOU 3861  CA  LYS D 166     7554  13703   7332  -4943  -1587    140       C  
ATOM   3862  C   LYS D 166      41.915 -43.494   3.352  1.00 72.46           C  
ANISOU 3862  C   LYS D 166     7231  13215   7087  -4674  -1710     96       C  
ATOM   3863  O   LYS D 166      43.073 -43.905   3.298  1.00 72.67           O  
ANISOU 3863  O   LYS D 166     7070  13229   7313  -4494  -1851    105       O  
ATOM   3864  CB  LYS D 166      40.889 -43.542   5.657  1.00 78.85           C  
ANISOU 3864  CB  LYS D 166     8141  14187   7631  -4876  -1177    235       C  
ATOM   3865  CG  LYS D 166      41.472 -44.945   5.727  1.00 81.53           C  
ANISOU 3865  CG  LYS D 166     8548  14563   7866  -4830   -902    327       C  
ATOM   3866  CD  LYS D 166      42.862 -44.961   6.333  1.00 83.15           C  
ANISOU 3866  CD  LYS D 166     8712  14804   8076  -4737   -788    428       C  
ATOM   3867  CE  LYS D 166      43.380 -46.385   6.445  1.00 83.94           C  
ANISOU 3867  CE  LYS D 166     8758  14943   8192  -4728   -767    411       C  
ATOM   3868  NZ  LYS D 166      42.493 -47.231   7.292  1.00 83.94           N  
ANISOU 3868  NZ  LYS D 166     8723  14997   8174  -4756   -900    348       N  
ATOM   3869  N   HIS D 167      41.029 -43.733   2.394  1.00 69.16           N  
ANISOU 3869  N   HIS D 167     6954  12685   6640  -4309  -1862    242       N  
ATOM   3870  CA  HIS D 167      41.372 -44.549   1.234  1.00 68.35           C  
ANISOU 3870  CA  HIS D 167     6736  12555   6678  -4415  -1545    296       C  
ATOM   3871  C   HIS D 167      41.545 -43.715  -0.037  1.00 66.61           C  
ANISOU 3871  C   HIS D 167     6343  12250   6717  -4309  -1349    196       C  
ATOM   3872  O   HIS D 167      41.597 -44.256  -1.140  1.00 65.69           O  
ANISOU 3872  O   HIS D 167     6346  11847   6766  -4383  -1121   -112       O  
ATOM   3873  CB  HIS D 167      40.305 -45.624   1.013  1.00 67.64           C  
ANISOU 3873  CB  HIS D 167     6669  12489   6542  -4362  -1671    509       C  
ATOM   3874  CG  HIS D 167      40.358 -46.744   2.006  1.00 68.76           C  
ANISOU 3874  CG  HIS D 167     6679  12772   6674  -4412  -1670    608       C  
ATOM   3875  ND1 HIS D 167      39.983 -46.592   3.324  1.00 69.55           N  
ANISOU 3875  ND1 HIS D 167     6748  12911   6766  -4458  -1665    537       N  
ATOM   3876  CD2 HIS D 167      40.741 -48.037   1.871  1.00 69.34           C  
ANISOU 3876  CD2 HIS D 167     6620  12892   6834  -4393  -1706    729       C  
ATOM   3877  CE1 HIS D 167      40.134 -47.741   3.959  1.00 69.36           C  
ANISOU 3877  CE1 HIS D 167     6703  12961   6692  -4464  -1638    656       C  
ATOM   3878  NE2 HIS D 167      40.593 -48.634   3.100  1.00 69.79           N  
ANISOU 3878  NE2 HIS D 167     6648  12983   6884  -4412  -1714    733       N  
ATOM   3879  N   GLY D 168      41.641 -42.399   0.121  1.00 65.25           N  
ANISOU 3879  N   GLY D 168     6038  12255   6499  -3934  -1573    462       N  
ATOM   3880  CA  GLY D 168      41.853 -41.513  -1.010  1.00 63.94           C  
ANISOU 3880  CA  GLY D 168     5820  12093   6381  -3734  -1601    461       C  
ATOM   3881  C   GLY D 168      40.591 -41.212  -1.800  1.00 63.88           C  
ANISOU 3881  C   GLY D 168     5858  12043   6372  -3789  -1262    463       C  
ATOM   3882  O   GLY D 168      40.656 -40.660  -2.899  1.00 64.37           O  
ANISOU 3882  O   GLY D 168     5899  12238   6319  -3843  -1167    517       O  
ATOM   3883  N   PHE D 169      39.440 -41.582  -1.246  1.00 62.03           N  
ANISOU 3883  N   PHE D 169     5690  11522   6355  -3829  -1078    394       N  
ATOM   3884  CA  PHE D 169      38.161 -41.253  -1.863  1.00 59.82           C  
ANISOU 3884  CA  PHE D 169     5710  10839   6181  -3858  -1248     86       C  
ATOM   3885  C   PHE D 169      37.531 -40.050  -1.165  1.00 62.06           C  
ANISOU 3885  C   PHE D 169     6066  10945   6569  -4033  -1367    -46       C  
ATOM   3886  O   PHE D 169      37.953 -39.668  -0.075  1.00 62.89           O  
ANISOU 3886  O   PHE D 169     6188  11148   6561  -3741  -1611     10       O  
ATOM   3887  CB  PHE D 169      37.207 -42.449  -1.810  1.00 59.44           C  
ANISOU 3887  CB  PHE D 169     5554  11023   6009  -3829  -1018    136       C  
ATOM   3888  CG  PHE D 169      37.727 -43.681  -2.503  1.00 58.44           C  
ANISOU 3888  CG  PHE D 169     5353  11108   5744  -3539   -614    397       C  
ATOM   3889  CD1 PHE D 169      37.631 -43.814  -3.880  1.00 60.01           C  
ANISOU 3889  CD1 PHE D 169     5665  11240   5895  -3237    142    599       C  
ATOM   3890  CD2 PHE D 169      38.293 -44.714  -1.774  1.00 55.53           C  
ANISOU 3890  CD2 PHE D 169     5015  10877   5208  -3569   -915    724       C  
ATOM   3891  CE1 PHE D 169      38.104 -44.952  -4.516  1.00 59.32           C  
ANISOU 3891  CE1 PHE D 169     5632  11251   5656  -3124    216    677       C  
ATOM   3892  CE2 PHE D 169      38.768 -45.851  -2.403  1.00 54.78           C  
ANISOU 3892  CE2 PHE D 169     4903  10784   5127  -3558   -744    713       C  
ATOM   3893  CZ  PHE D 169      38.672 -45.971  -3.775  1.00 56.73           C  
ANISOU 3893  CZ  PHE D 169     5157  11039   5358  -3263   -289    871       C  
ATOM   3894  N   LYS D 170      36.527 -39.449  -1.796  1.00 65.67           N  
ANISOU 3894  N   LYS D 170     6726  10897   7328  -4297   -631   -229       N  
ATOM   3895  CA  LYS D 170      35.763 -38.383  -1.155  1.00 67.70           C  
ANISOU 3895  CA  LYS D 170     7251  10777   7696  -4440   -284   -329       C  
ATOM   3896  C   LYS D 170      34.372 -38.279  -1.771  1.00 64.47           C  
ANISOU 3896  C   LYS D 170     7232  10184   7081  -4238   -357   -546       C  
ATOM   3897  O   LYS D 170      34.177 -38.604  -2.940  1.00 64.70           O  
ANISOU 3897  O   LYS D 170     7402  10121   7058  -4434   -272   -945       O  
ATOM   3898  CB  LYS D 170      36.496 -37.040  -1.257  1.00 72.99           C  
ANISOU 3898  CB  LYS D 170     7870  11223   8640  -4574    178   -140       C  
ATOM   3899  CG  LYS D 170      36.477 -36.393  -2.635  1.00 77.73           C  
ANISOU 3899  CG  LYS D 170     8386  11579   9570  -4645    620    -18       C  
ATOM   3900  CD  LYS D 170      37.164 -35.031  -2.598  1.00 81.99           C  
ANISOU 3900  CD  LYS D 170     8964  11902  10287  -4444   1021    149       C  
ATOM   3901  CE  LYS D 170      37.002 -34.276  -3.910  1.00 84.82           C  
ANISOU 3901  CE  LYS D 170     9309  12109  10811  -4322   1266    215       C  
ATOM   3902  NZ  LYS D 170      37.650 -34.975  -5.053  1.00 86.03           N  
ANISOU 3902  NZ  LYS D 170     9420  12199  11069  -4287   1348    212       N  
ATOM   3903  N   LEU D 171      33.404 -37.839  -0.975  1.00 61.14           N  
ANISOU 3903  N   LEU D 171     7149   9436   6644  -4113   -133   -555       N  
ATOM   3904  CA  LEU D 171      32.044 -37.668  -1.469  1.00 58.85           C  
ANISOU 3904  CA  LEU D 171     7126   8743   6490  -4122    215   -666       C  
ATOM   3905  C   LEU D 171      31.892 -36.364  -2.233  1.00 54.68           C  
ANISOU 3905  C   LEU D 171     6818   7887   6071  -4154     50   -964       C  
ATOM   3906  O   LEU D 171      32.388 -35.320  -1.808  1.00 54.16           O  
ANISOU 3906  O   LEU D 171     6971   7687   5922  -4176     -7  -1166       O  
ATOM   3907  CB  LEU D 171      31.037 -37.706  -0.319  1.00 61.17           C  
ANISOU 3907  CB  LEU D 171     7397   9010   6835  -4124    588   -540       C  
ATOM   3908  CG  LEU D 171      30.792 -39.057   0.342  1.00 62.44           C  
ANISOU 3908  CG  LEU D 171     7466   9307   6950  -4194    618   -584       C  
ATOM   3909  CD1 LEU D 171      29.802 -38.903   1.478  1.00 63.57           C  
ANISOU 3909  CD1 LEU D 171     7560   9509   7086  -3934   1022   -210       C  
ATOM   3910  CD2 LEU D 171      30.282 -40.054  -0.683  1.00 63.47           C  
ANISOU 3910  CD2 LEU D 171     7503   9464   7149  -4274    519   -629       C  
ATOM   3911  N   GLY D 172      31.207 -36.432  -3.365  1.00 50.74           N  
ANISOU 3911  N   GLY D 172     6667   7130   5480  -3877   -126  -1138       N  
ATOM   3912  CA  GLY D 172      30.867 -35.246  -4.125  1.00 49.16           C  
ANISOU 3912  CA  GLY D 172     6491   6713   5474  -3764   -204   -925       C  
ATOM   3913  C   GLY D 172      29.427 -34.876  -3.840  1.00 49.92           C  
ANISOU 3913  C   GLY D 172     6706   6746   5514  -3767     78   -386       C  
ATOM   3914  O   GLY D 172      28.787 -35.485  -2.981  1.00 47.41           O  
ANISOU 3914  O   GLY D 172     6979   6584   4450  -3592    302    -20       O  
ATOM   3915  N   PRO D 173      28.897 -33.890  -4.572  1.00 53.16           N  
ANISOU 3915  N   PRO D 173     6777   6813   6611  -4027    591    -80       N  
ATOM   3916  CA  PRO D 173      27.517 -33.447  -4.355  1.00 56.15           C  
ANISOU 3916  CA  PRO D 173     7094   7042   7199  -3939    627    -31       C  
ATOM   3917  C   PRO D 173      26.484 -34.480  -4.800  1.00 58.56           C  
ANISOU 3917  C   PRO D 173     7360   7310   7578  -3887    477    -77       C  
ATOM   3918  O   PRO D 173      26.698 -35.203  -5.772  1.00 58.46           O  
ANISOU 3918  O   PRO D 173     7349   7181   7682  -3952    653     48       O  
ATOM   3919  CB  PRO D 173      27.420 -32.188  -5.218  1.00 55.67           C  
ANISOU 3919  CB  PRO D 173     6937   6939   7277  -3996    843    125       C  
ATOM   3920  CG  PRO D 173      28.377 -32.445  -6.331  1.00 55.26           C  
ANISOU 3920  CG  PRO D 173     6855   6941   7201  -3978    986    238       C  
ATOM   3921  CD  PRO D 173      29.526 -33.196  -5.707  1.00 54.57           C  
ANISOU 3921  CD  PRO D 173     6778   6899   7058  -3943    982    183       C  
ATOM   3922  N   ALA D 174      25.375 -34.553  -4.078  1.00 62.00           N  
ANISOU 3922  N   ALA D 174     7897   7739   7920  -3437    334   -196       N  
ATOM   3923  CA  ALA D 174      24.221 -35.300  -4.552  1.00 65.13           C  
ANISOU 3923  CA  ALA D 174     8499   7973   8275  -3314    222   -557       C  
ATOM   3924  C   ALA D 174      23.315 -34.327  -5.300  1.00 67.51           C  
ANISOU 3924  C   ALA D 174     9007   8139   8505  -3209   -158  -1086       C  
ATOM   3925  O   ALA D 174      23.363 -33.125  -5.047  1.00 65.71           O  
ANISOU 3925  O   ALA D 174     8771   7957   8240  -3453   -714  -1472       O  
ATOM   3926  CB  ALA D 174      23.486 -35.963  -3.392  1.00 65.71           C  
ANISOU 3926  CB  ALA D 174     8677   8054   8235  -3167    372   -359       C  
ATOM   3927  N   PRO D 175      22.503 -34.833  -6.242  1.00 71.58           N  
ANISOU 3927  N   PRO D 175     9835   8444   8918  -2896     -6  -1409       N  
ATOM   3928  CA  PRO D 175      21.572 -33.964  -6.974  1.00 75.04           C  
ANISOU 3928  CA  PRO D 175    10369   8724   9419  -2631     82  -1440       C  
ATOM   3929  C   PRO D 175      20.665 -33.145  -6.053  1.00 79.01           C  
ANISOU 3929  C   PRO D 175    10950   9061  10008  -2231    167  -1291       C  
ATOM   3930  O   PRO D 175      20.354 -33.583  -4.944  1.00 79.11           O  
ANISOU 3930  O   PRO D 175    10862   9082  10115  -2166      8  -1354       O  
ATOM   3931  CB  PRO D 175      20.751 -34.957  -7.800  1.00 74.61           C  
ANISOU 3931  CB  PRO D 175    10239   8667   9444  -2793     29  -1476       C  
ATOM   3932  CG  PRO D 175      21.672 -36.104  -8.009  1.00 73.91           C  
ANISOU 3932  CG  PRO D 175    10150   8600   9331  -2800     57  -1467       C  
ATOM   3933  CD  PRO D 175      22.478 -36.218  -6.749  1.00 73.10           C  
ANISOU 3933  CD  PRO D 175    10105   8548   9122  -2744    137  -1386       C  
ATOM   3934  N   LYS D 176      20.258 -31.965  -6.514  1.00 82.59           N  
ANISOU 3934  N   LYS D 176    11621   9316  10444  -1996    482  -1178       N  
ATOM   3935  CA  LYS D 176      19.406 -31.077  -5.727  1.00 85.83           C  
ANISOU 3935  CA  LYS D 176    12245   9584  10784  -1833    745  -1119       C  
ATOM   3936  C   LYS D 176      18.048 -31.711  -5.438  1.00 86.39           C  
ANISOU 3936  C   LYS D 176    12238   9670  10915  -1821    871  -1010       C  
ATOM   3937  O   LYS D 176      17.491 -31.540  -4.353  1.00 86.41           O  
ANISOU 3937  O   LYS D 176    12196   9695  10943  -1846    883  -1057       O  
ATOM   3938  CB  LYS D 176      19.214 -29.741  -6.452  1.00 87.68           C  
ANISOU 3938  CB  LYS D 176    12715   9670  10929  -1679    817  -1162       C  
ATOM   3939  CG  LYS D 176      18.337 -28.745  -5.709  1.00 89.10           C  
ANISOU 3939  CG  LYS D 176    13024   9768  11061  -1557    851  -1175       C  
ATOM   3940  CD  LYS D 176      19.046 -28.176  -4.491  1.00 90.40           C  
ANISOU 3940  CD  LYS D 176    13266   9856  11228  -1473    955  -1156       C  
ATOM   3941  CE  LYS D 176      18.118 -27.290  -3.676  1.00 91.35           C  
ANISOU 3941  CE  LYS D 176    13436   9928  11343  -1436   1053  -1182       C  
ATOM   3942  NZ  LYS D 176      17.500 -26.219  -4.504  1.00 91.89           N  
ANISOU 3942  NZ  LYS D 176    13515  10003  11394  -1460   1077  -1239       N  
TER    3943      LYS D 176                                                      
ATOM   3944  C5'  DT E   5      29.280 -27.308  -7.797  1.00100.52           C  
ANISOU 3944  C5'  DT E   5    17305  12600   8289   -676   -486     83       C  
ATOM   3945  C4'  DT E   5      30.596 -27.030  -8.501  1.00 99.83           C  
ANISOU 3945  C4'  DT E   5    17228  12498   8203   -699   -589    211       C  
ATOM   3946  O4'  DT E   5      30.744 -25.605  -8.700  1.00100.38           O  
ANISOU 3946  O4'  DT E   5    17346  12564   8230   -646   -659    159       O  
ATOM   3947  C3'  DT E   5      31.850 -27.495  -7.745  1.00 97.36           C  
ANISOU 3947  C3'  DT E   5    16870  12206   7916   -776   -682    286       C  
ATOM   3948  O3'  DT E   5      32.594 -28.417  -8.545  1.00 91.56           O  
ANISOU 3948  O3'  DT E   5    16084  11594   7112   -876  -1027    598       O  
ATOM   3949  C2'  DT E   5      32.639 -26.204  -7.483  1.00 99.33           C  
ANISOU 3949  C2'  DT E   5    17145  12411   8185   -743   -700    104       C  
ATOM   3950  C1'  DT E   5      32.096 -25.262  -8.547  1.00100.14           C  
ANISOU 3950  C1'  DT E   5    17311  12533   8206   -688   -720     79       C  
ATOM   3951  P    DT E   6      33.451 -29.593  -7.855  1.00 83.08           P  
ANISOU 3951  P    DT E   6    15063  10829   5677  -1011  -1856    854       P  
ATOM   3952  OP1  DT E   6      33.123 -29.616  -6.411  1.00 83.77           O  
ANISOU 3952  OP1  DT E   6    15173  10970   5687  -1243  -1568    657       O  
ATOM   3953  OP2  DT E   6      34.857 -29.436  -8.286  1.00 82.63           O  
ANISOU 3953  OP2  DT E   6    15078  10868   5450   -953  -2264    853       O  
ATOM   3954  O5'  DT E   6      32.884 -30.931  -8.532  1.00 76.61           O  
ANISOU 3954  O5'  DT E   6    13942   9976   5188   -786  -1765   1349       O  
ATOM   3955  C5'  DT E   6      31.823 -31.637  -7.909  1.00 69.23           C  
ANISOU 3955  C5'  DT E   6    12678   9078   4546   -682  -1891   1423       C  
ATOM   3956  C4'  DT E   6      31.227 -32.677  -8.839  1.00 62.04           C  
ANISOU 3956  C4'  DT E   6    11353   8099   4118   -591  -1781   1508       C  
ATOM   3957  O4'  DT E   6      30.502 -32.020  -9.910  1.00 58.12           O  
ANISOU 3957  O4'  DT E   6    10692   7642   3748   -441  -1726   1178       O  
ATOM   3958  C3'  DT E   6      32.236 -33.617  -9.515  1.00 59.03           C  
ANISOU 3958  C3'  DT E   6    10694   7677   4057   -679  -1553   1905       C  
ATOM   3959  O3'  DT E   6      31.811 -34.968  -9.358  1.00 57.80           O  
ANISOU 3959  O3'  DT E   6    10246   7466   4249   -844  -1310   2383       O  
ATOM   3960  C2'  DT E   6      32.194 -33.186 -10.982  1.00 57.62           C  
ANISOU 3960  C2'  DT E   6    10420   7498   3974   -592  -1497   1508       C  
ATOM   3961  C1'  DT E   6      30.759 -32.709 -11.106  1.00 55.82           C  
ANISOU 3961  C1'  DT E   6    10126   7291   3791   -484  -1404   1195       C  
ATOM   3962  N1   DT E   6      30.532 -31.797 -12.254  1.00 52.56           N  
ANISOU 3962  N1   DT E   6     9279   6654   4038   -551   -774    767       N  
ATOM   3963  C2   DT E   6      29.911 -32.285 -13.375  1.00 49.15           C  
ANISOU 3963  C2   DT E   6     8752   6273   3648   -394   -382    963       C  
ATOM   3964  O2   DT E   6      29.523 -33.435 -13.475  1.00 48.17           O  
ANISOU 3964  O2   DT E   6     8640   6159   3503   -419    485   1073       O  
ATOM   3965  N3   DT E   6      29.752 -31.377 -14.383  1.00 46.65           N  
ANISOU 3965  N3   DT E   6     8524   5740   3460    -42   -908   1301       N  
ATOM   3966  C4   DT E   6      30.152 -30.057 -14.386  1.00 48.68           C  
ANISOU 3966  C4   DT E   6     8698   5753   4047    -97   -848    953       C  
ATOM   3967  O4   DT E   6      29.966 -29.318 -15.352  1.00 48.40           O  
ANISOU 3967  O4   DT E   6     8717   5568   4107     24   -953   1254       O  
ATOM   3968  C5   DT E   6      30.805 -29.607 -13.177  1.00 50.60           C  
ANISOU 3968  C5   DT E   6     8800   6014   4413   -330   -770    676       C  
ATOM   3969  C7   DT E   6      31.284 -28.190 -13.058  1.00 50.96           C  
ANISOU 3969  C7   DT E   6     8756   5804   4804   -775   -633     -1       C  
ATOM   3970  C6   DT E   6      30.962 -30.490 -12.181  1.00 52.07           C  
ANISOU 3970  C6   DT E   6     9042   6313   4430   -373   -696    864       C  
ATOM   3971  P    DT E   7      32.860 -36.183  -9.486  1.00 57.28           P  
ANISOU 3971  P    DT E   7     9928   7421   4413  -1071   -613   2471       P  
ATOM   3972  OP1  DT E   7      32.130 -37.435  -9.159  1.00 56.74           O  
ANISOU 3972  OP1  DT E   7     9799   7225   4534  -1029   -519   2911       O  
ATOM   3973  OP2  DT E   7      34.058 -35.832  -8.686  1.00 59.93           O  
ANISOU 3973  OP2  DT E   7    10364   7626   4782  -1166   -438   2212       O  
ATOM   3974  O5'  DT E   7      33.240 -36.184 -11.043  1.00 55.98           O  
ANISOU 3974  O5'  DT E   7     9451   7408   4409   -967     58   2184       O  
ATOM   3975  C5'  DT E   7      33.753 -37.356 -11.661  1.00 53.59           C  
ANISOU 3975  C5'  DT E   7     8781   7091   4491   -797    203   2161       C  
ATOM   3976  C4'  DT E   7      33.056 -37.602 -12.988  1.00 50.19           C  
ANISOU 3976  C4'  DT E   7     7944   6554   4572   -518    447   2488       C  
ATOM   3977  O4'  DT E   7      31.811 -38.322 -12.753  1.00 49.34           O  
ANISOU 3977  O4'  DT E   7     7633   6439   4674   -600    249   2495       O  
ATOM   3978  C3'  DT E   7      32.673 -36.334 -13.763  1.00 46.20           C  
ANISOU 3978  C3'  DT E   7     7225   6121   4206   -419    780   2758       C  
ATOM   3979  O3'  DT E   7      32.880 -36.529 -15.160  1.00 41.05           O  
ANISOU 3979  O3'  DT E   7     5879   5388   4331   -653    700   2321       O  
ATOM   3980  C2'  DT E   7      31.186 -36.189 -13.453  1.00 47.99           C  
ANISOU 3980  C2'  DT E   7     7584   6254   4398   -430    822   2671       C  
ATOM   3981  C1'  DT E   7      30.760 -37.646 -13.407  1.00 48.95           C  
ANISOU 3981  C1'  DT E   7     7625   6484   4491   -687    849   2256       C  
ATOM   3982  N1   DT E   7      29.486 -37.877 -12.658  1.00 48.19           N  
ANISOU 3982  N1   DT E   7     7598   6592   4120   -791   1273   1626       N  
ATOM   3983  C2   DT E   7      28.293 -37.626 -13.293  1.00 47.97           C  
ANISOU 3983  C2   DT E   7     7794   6630   3801   -725   1167   1148       C  
ATOM   3984  O2   DT E   7      28.223 -37.223 -14.439  1.00 47.55           O  
ANISOU 3984  O2   DT E   7     7983   6625   3457   -398    931    975       O  
ATOM   3985  N3   DT E   7      27.179 -37.860 -12.536  1.00 47.28           N  
ANISOU 3985  N3   DT E   7     7785   6727   3452   -983    911    966       N  
ATOM   3986  C4   DT E   7      27.135 -38.314 -11.235  1.00 48.20           C  
ANISOU 3986  C4   DT E   7     7928   6963   3423  -1061    940    925       C  
ATOM   3987  O4   DT E   7      26.074 -38.495 -10.643  1.00 47.44           O  
ANISOU 3987  O4   DT E   7     7655   7041   3329  -1538    394    416       O  
ATOM   3988  C5   DT E   7      28.424 -38.562 -10.621  1.00 48.61           C  
ANISOU 3988  C5   DT E   7     8001   6961   3506   -832   1271   1354       C  
ATOM   3989  C7   DT E   7      28.504 -39.059  -9.205  1.00 48.74           C  
ANISOU 3989  C7   DT E   7     8158   6997   3362   -707   1495   1419       C  
ATOM   3990  C6   DT E   7      29.529 -38.330 -11.357  1.00 49.23           C  
ANISOU 3990  C6   DT E   7     7955   6770   3979   -803   1201   1486       C  
ATOM   3991  P    DT E   8      34.056 -35.754 -15.938  1.00 37.74           P  
ANISOU 3991  P    DT E   8     4997   4756   4588   -199    218   1972       P  
ATOM   3992  OP1  DT E   8      33.824 -36.005 -17.384  1.00 38.93           O  
ANISOU 3992  OP1  DT E   8     5029   4931   4831     32    751   1457       O  
ATOM   3993  OP2  DT E   8      35.338 -36.129 -15.301  1.00 39.37           O  
ANISOU 3993  OP2  DT E   8     4579   5184   5198    240   -965   1912       O  
ATOM   3994  O5'  DT E   8      33.791 -34.200 -15.637  1.00 36.03           O  
ANISOU 3994  O5'  DT E   8     4981   4276   4432     -1   -146   1605       O  
ATOM   3995  C5'  DT E   8      32.581 -33.589 -16.057  1.00 35.46           C  
ANISOU 3995  C5'  DT E   8     5225   4307   3942   -456   -278   1197       C  
ATOM   3996  C4'  DT E   8      32.625 -32.084 -15.844  1.00 34.17           C  
ANISOU 3996  C4'  DT E   8     5082   4450   3451   -884   -324    858       C  
ATOM   3997  O4'  DT E   8      32.826 -31.787 -14.436  1.00 34.59           O  
ANISOU 3997  O4'  DT E   8     4997   4903   3242   -923  -1021    604       O  
ATOM   3998  C3'  DT E   8      33.739 -31.344 -16.578  1.00 33.80           C  
ANISOU 3998  C3'  DT E   8     5020   4453   3371   -811   -438    864       C  
ATOM   3999  O3'  DT E   8      33.285 -30.058 -16.883  1.00 30.47           O  
ANISOU 3999  O3'  DT E   8     4678   3761   3138   -402   -378    917       O  
ATOM   4000  C2'  DT E   8      34.833 -31.279 -15.522  1.00 35.05           C  
ANISOU 4000  C2'  DT E   8     5126   4933   3257   -921  -1205   1069       C  
ATOM   4001  C1'  DT E   8      33.997 -31.009 -14.283  1.00 36.14           C  
ANISOU 4001  C1'  DT E   8     5475   5174   3081  -1079  -1555    885       C  
ATOM   4002  N1   DT E   8      34.658 -31.404 -13.026  1.00 43.50           N  
ANISOU 4002  N1   DT E   8     6544   6178   3807  -1288  -1740    923       N  
ATOM   4003  C2   DT E   8      34.700 -30.510 -11.986  1.00 47.07           C  
ANISOU 4003  C2   DT E   8     7352   6577   3956  -1650  -1589    808       C  
ATOM   4004  O2   DT E   8      34.220 -29.391 -12.050  1.00 47.67           O  
ANISOU 4004  O2   DT E   8     7468   6577   4067  -1893  -1195    675       O  
ATOM   4005  N3   DT E   8      35.330 -30.972 -10.860  1.00 50.19           N  
ANISOU 4005  N3   DT E   8     7931   7064   4075  -1462  -1802   1147       N  
ATOM   4006  C4   DT E   8      35.906 -32.217 -10.679  1.00 52.42           C  
ANISOU 4006  C4   DT E   8     8357   7317   4244  -1190  -1548   1543       C  
ATOM   4007  O4   DT E   8      36.451 -32.543  -9.631  1.00 53.29           O  
ANISOU 4007  O4   DT E   8     8609   7685   3956  -1032  -1754   1832       O  
ATOM   4008  C5   DT E   8      35.821 -33.110 -11.812  1.00 51.63           C  
ANISOU 4008  C5   DT E   8     8150   7011   4457  -1046  -1225   1647       C  
ATOM   4009  C7   DT E   8      36.409 -34.488 -11.734  1.00 53.71           C  
ANISOU 4009  C7   DT E   8     8373   6964   5073   -943   -595   1845       C  
ATOM   4010  C6   DT E   8      35.206 -32.666 -12.918  1.00 47.67           C  
ANISOU 4010  C6   DT E   8     7370   6602   4142  -1188  -1605   1264       C  
ATOM   4011  P    DT E   9      33.556 -29.393 -18.318  1.00 26.36           P  
ANISOU 4011  P    DT E   9     3614   3265   3135   -651   -823    309       P  
ATOM   4012  OP1  DT E   9      35.003 -29.466 -18.623  1.00 29.80           O  
ANISOU 4012  OP1  DT E   9     3314   3863   4145   -728   -832    212       O  
ATOM   4013  OP2  DT E   9      32.873 -28.080 -18.256  1.00 25.85           O  
ANISOU 4013  OP2  DT E   9     3956   2589   3275   -125   -746     60       O  
ATOM   4014  O5'  DT E   9      32.779 -30.340 -19.339  1.00 23.91           O  
ANISOU 4014  O5'  DT E   9     2960   3161   2964   -749   -861     33       O  
ATOM   4015  C5'  DT E   9      31.414 -30.599 -19.151  1.00 22.46           C  
ANISOU 4015  C5'  DT E   9     2873   2917   2742   -810   -823    130       C  
ATOM   4016  C4'  DT E   9      30.786 -31.000 -20.462  1.00 20.80           C  
ANISOU 4016  C4'  DT E   9     3031   2249   2623   -222   -177    417       C  
ATOM   4017  O4'  DT E   9      30.670 -29.835 -21.303  1.00 20.19           O  
ANISOU 4017  O4'  DT E   9     3137   2067   2467    -99    186    353       O  
ATOM   4018  C3'  DT E   9      31.568 -32.045 -21.277  1.00 19.58           C  
ANISOU 4018  C3'  DT E   9     2805   2203   2433   -586    -53    329       C  
ATOM   4019  O3'  DT E   9      30.665 -33.081 -21.659  1.00 18.48           O  
ANISOU 4019  O3'  DT E   9     2665   1964   2394   -511   -207    133       O  
ATOM   4020  C2'  DT E   9      32.080 -31.247 -22.488  1.00 20.40           C  
ANISOU 4020  C2'  DT E   9     2879   2539   2334   -624   -152    605       C  
ATOM   4021  C1'  DT E   9      30.994 -30.192 -22.619  1.00 20.24           C  
ANISOU 4021  C1'  DT E   9     3018   2154   2518   -388     67    713       C  
ATOM   4022  N1   DT E   9      31.397 -28.950 -23.337  1.00 19.30           N  
ANISOU 4022  N1   DT E   9     2862   2259   2212   -616   -118    478       N  
ATOM   4023  C2   DT E   9      30.516 -28.401 -24.236  1.00 18.28           C  
ANISOU 4023  C2   DT E   9     2854   1955   2136   -409   -301    425       C  
ATOM   4024  O2   DT E   9      29.433 -28.885 -24.467  1.00 18.62           O  
ANISOU 4024  O2   DT E   9     3005   1895   2175   -259   -235    234       O  
ATOM   4025  N3   DT E   9      30.950 -27.252 -24.850  1.00 20.30           N  
ANISOU 4025  N3   DT E   9     2956   2104   2653   -828    368    405       N  
ATOM   4026  C4   DT E   9      32.156 -26.602 -24.637  1.00 22.72           C  
ANISOU 4026  C4   DT E   9     2969   2497   3168  -1142     62    882       C  
ATOM   4027  O4   DT E   9      32.458 -25.571 -25.236  1.00 26.43           O  
ANISOU 4027  O4   DT E   9     3591   2587   3864   -971    254    906       O  
ATOM   4028  C5   DT E   9      33.038 -27.232 -23.665  1.00 23.37           C  
ANISOU 4028  C5   DT E   9     2915   2793   3173  -1230    -82    534       C  
ATOM   4029  C7   DT E   9      34.380 -26.627 -23.348  1.00 24.31           C  
ANISOU 4029  C7   DT E   9     2960   3141   3137  -1271   -117    627       C  
ATOM   4030  C6   DT E   9      32.615 -28.364 -23.071  1.00 21.14           C  
ANISOU 4030  C6   DT E   9     2513   2639   2879  -1036   -376    534       C  
ATOM   4031  P    DT E  10      31.152 -34.404 -22.422  1.00 18.29           P  
ANISOU 4031  P    DT E  10     2379   2031   2538   -255   -265    444       P  
ATOM   4032  OP1  DT E  10      30.119 -35.427 -22.147  1.00 19.69           O  
ANISOU 4032  OP1  DT E  10     2035   2411   3034   -387   -113    208       O  
ATOM   4033  OP2  DT E  10      32.557 -34.716 -22.069  1.00 21.00           O  
ANISOU 4033  OP2  DT E  10     2616   2493   2871   -407   -408    273       O  
ATOM   4034  O5'  DT E  10      31.105 -34.020 -23.964  1.00 18.26           O  
ANISOU 4034  O5'  DT E  10     2439   2298   2201    -81   -173    484       O  
ATOM   4035  C5'  DT E  10      29.869 -33.653 -24.569  1.00 17.94           C  
ANISOU 4035  C5'  DT E  10     2329   2232   2255    -26   -139    514       C  
ATOM   4036  C4'  DT E  10      30.107 -33.026 -25.923  1.00 18.24           C  
ANISOU 4036  C4'  DT E  10     2574   1838   2518   -436    649    314       C  
ATOM   4037  O4'  DT E  10      30.809 -31.791 -25.765  1.00 19.03           O  
ANISOU 4037  O4'  DT E  10     2499   2176   2556   -430    295    606       O  
ATOM   4038  C3'  DT E  10      31.005 -33.838 -26.849  1.00 18.58           C  
ANISOU 4038  C3'  DT E  10     2323   2052   2686   -594    605    281       C  
ATOM   4039  O3'  DT E  10      30.205 -34.702 -27.651  1.00 20.32           O  
ANISOU 4039  O3'  DT E  10     2457   2476   2787   -579    236     21       O  
ATOM   4040  C2'  DT E  10      31.742 -32.775 -27.695  1.00 19.39           C  
ANISOU 4040  C2'  DT E  10     2636   1927   2802   -307    319    325       C  
ATOM   4041  C1'  DT E  10      31.349 -31.457 -27.022  1.00 19.29           C  
ANISOU 4041  C1'  DT E  10     2688   2265   2377   -546    413    444       C  
ATOM   4042  N1   DT E  10      32.473 -30.522 -26.801  1.00 21.75           N  
ANISOU 4042  N1   DT E  10     2779   2760   2726   -789    385    345       N  
ATOM   4043  C2   DT E  10      32.453 -29.300 -27.431  1.00 23.74           C  
ANISOU 4043  C2   DT E  10     2884   2947   3190   -975    637    650       C  
ATOM   4044  O2   DT E  10      31.569 -28.963 -28.196  1.00 24.22           O  
ANISOU 4044  O2   DT E  10     3423   2739   3042   -755    729    459       O  
ATOM   4045  N3   DT E  10      33.518 -28.489 -27.146  1.00 24.84           N  
ANISOU 4045  N3   DT E  10     3185   3303   2948  -1389    208    120       N  
ATOM   4046  C4   DT E  10      34.574 -28.767 -26.299  1.00 25.87           C  
ANISOU 4046  C4   DT E  10     3101   3727   3000  -1505   -193    389       C  
ATOM   4047  O4   DT E  10      35.488 -27.969 -26.106  1.00 28.79           O  
ANISOU 4047  O4   DT E  10     3541   4232   3165  -1971    375   -220       O  
ATOM   4048  C5   DT E  10      34.532 -30.067 -25.665  1.00 26.02           C  
ANISOU 4048  C5   DT E  10     2828   3865   3193  -1245   -516    602       C  
ATOM   4049  C7   DT E  10      35.627 -30.480 -24.726  1.00 29.20           C  
ANISOU 4049  C7   DT E  10     2792   4506   3795  -1103   -688    641       C  
ATOM   4050  C6   DT E  10      33.492 -30.869 -25.937  1.00 24.53           C  
ANISOU 4050  C6   DT E  10     2894   3383   3046   -716   -259    430       C  
TER    4051       DT E  10                                                      
ATOM   4052  O5'  DT F   7     -11.778 -28.989 -11.489  1.00104.39           O  
ANISOU 4052  O5'  DT F   7    16869  11150  11644   1041  -1233   1575       O  
ATOM   4053  C5'  DT F   7     -10.648 -29.769 -11.858  1.00 98.84           C  
ANISOU 4053  C5'  DT F   7    16045  10718  10792   1009  -1591   1487       C  
ATOM   4054  C4'  DT F   7     -10.798 -31.204 -11.383  1.00 92.38           C  
ANISOU 4054  C4'  DT F   7    15066  10211   9823    884  -1825   1240       C  
ATOM   4055  O4'  DT F   7      -9.639 -31.963 -11.803  1.00 91.41           O  
ANISOU 4055  O4'  DT F   7    15107  10134   9490    697  -1785   1094       O  
ATOM   4056  C3'  DT F   7     -10.842 -31.377  -9.874  1.00 86.90           C  
ANISOU 4056  C3'  DT F   7    14001   9727   9289    786  -1895    947       C  
ATOM   4057  O3'  DT F   7     -11.449 -32.621  -9.535  1.00 78.47           O  
ANISOU 4057  O3'  DT F   7    12253   8992   8571    792  -2169    750       O  
ATOM   4058  C2'  DT F   7      -9.365 -31.378  -9.524  1.00 89.06           C  
ANISOU 4058  C2'  DT F   7    14610   9909   9319    604  -1740    860       C  
ATOM   4059  C1'  DT F   7      -8.762 -32.143 -10.703  1.00 90.81           C  
ANISOU 4059  C1'  DT F   7    15154  10023   9327    478  -1563    809       C  
ATOM   4060  N1   DT F   7      -7.418 -31.646 -11.087  1.00 91.84           N  
ANISOU 4060  N1   DT F   7    15757   9997   9141    199  -1124    565       N  
ATOM   4061  C2   DT F   7      -6.395 -32.546 -11.288  1.00 91.87           C  
ANISOU 4061  C2   DT F   7    16088   9926   8893    101   -986    390       C  
ATOM   4062  O2   DT F   7      -6.532 -33.752 -11.175  1.00 90.87           O  
ANISOU 4062  O2   DT F   7    16101   9852   8573     59  -1185    138       O  
ATOM   4063  N3   DT F   7      -5.196 -31.978 -11.633  1.00 93.37           N  
ANISOU 4063  N3   DT F   7    16333   9972   9169     94   -605    515       N  
ATOM   4064  C4   DT F   7      -4.923 -30.629 -11.788  1.00 94.69           C  
ANISOU 4064  C4   DT F   7    16432  10056   9490     90   -412    591       C  
ATOM   4065  O4   DT F   7      -3.810 -30.216 -12.102  1.00 95.55           O  
ANISOU 4065  O4   DT F   7    16485  10164   9657    108   -331    566       O  
ATOM   4066  C5   DT F   7      -6.042 -29.740 -11.557  1.00 94.12           C  
ANISOU 4066  C5   DT F   7    16336   9974   9451    129   -468    644       C  
ATOM   4067  C7   DT F   7      -5.875 -28.255 -11.699  1.00 93.74           C  
ANISOU 4067  C7   DT F   7    16404   9844   9369    224   -512    689       C  
ATOM   4068  C6   DT F   7      -7.219 -30.287 -11.220  1.00 93.00           C  
ANISOU 4068  C6   DT F   7    16053   9997   9288    123   -735    598       C  
ATOM   4069  P    DT F   8     -11.890 -32.920  -8.018  1.00 70.14           P  
ANISOU 4069  P    DT F   8    10609   8306   7735    728  -2434    479       P  
ATOM   4070  OP1  DT F   8     -12.743 -34.129  -8.042  1.00 69.55           O  
ANISOU 4070  OP1  DT F   8    10637   8318   7470    608  -2533    253       O  
ATOM   4071  OP2  DT F   8     -12.386 -31.654  -7.434  1.00 70.66           O  
ANISOU 4071  OP2  DT F   8    10534   8319   7994    753  -2368    362       O  
ATOM   4072  O5'  DT F   8     -10.529 -33.312  -7.270  1.00 61.50           O  
ANISOU 4072  O5'  DT F   8     9536   7361   6469    545  -2419    145       O  
ATOM   4073  C5'  DT F   8     -10.035 -34.642  -7.340  1.00 52.20           C  
ANISOU 4073  C5'  DT F   8     8592   6151   5090    391  -2230    -58       C  
ATOM   4074  C4'  DT F   8      -8.604 -34.705  -6.842  1.00 45.20           C  
ANISOU 4074  C4'  DT F   8     7884   5035   4254    393  -1540   -365       C  
ATOM   4075  O4'  DT F   8      -7.779 -33.853  -7.650  1.00 46.87           O  
ANISOU 4075  O4'  DT F   8     8168   5096   4543    118  -1193   -644       O  
ATOM   4076  C3'  DT F   8      -8.400 -34.207  -5.415  1.00 39.28           C  
ANISOU 4076  C3'  DT F   8     6923   4011   3990    479  -1264   -420       C  
ATOM   4077  O3'  DT F   8      -8.389 -35.318  -4.522  1.00 30.95           O  
ANISOU 4077  O3'  DT F   8     5243   2944   3572    480   -939   -953       O  
ATOM   4078  C2'  DT F   8      -7.033 -33.489  -5.450  1.00 42.29           C  
ANISOU 4078  C2'  DT F   8     7558   4061   4449    -32  -1148   -879       C  
ATOM   4079  C1'  DT F   8      -6.621 -33.542  -6.921  1.00 46.40           C  
ANISOU 4079  C1'  DT F   8     8344   4838   4449   -137  -1230   -879       C  
ATOM   4080  N1   DT F   8      -6.064 -32.255  -7.441  1.00 51.81           N  
ANISOU 4080  N1   DT F   8     9457   5565   4664   -214  -1107  -1070       N  
ATOM   4081  C2   DT F   8      -4.822 -32.253  -8.039  1.00 55.66           C  
ANISOU 4081  C2   DT F   8    10082   5974   5091   -144   -797  -1258       C  
ATOM   4082  O2   DT F   8      -4.140 -33.254  -8.164  1.00 57.97           O  
ANISOU 4082  O2   DT F   8    10213   6327   5488    297   -481  -1320       O  
ATOM   4083  N3   DT F   8      -4.406 -31.030  -8.492  1.00 55.90           N  
ANISOU 4083  N3   DT F   8    10396   5815   5029   -545   -797  -1331       N  
ATOM   4084  C4   DT F   8      -5.091 -29.830  -8.407  1.00 58.53           C  
ANISOU 4084  C4   DT F   8    10630   6120   5487   -566   -482   -594       C  
ATOM   4085  O4   DT F   8      -4.628 -28.776  -8.838  1.00 62.44           O  
ANISOU 4085  O4   DT F   8    11208   6464   6052   -504    154   -305       O  
ATOM   4086  C5   DT F   8      -6.386 -29.902  -7.770  1.00 55.07           C  
ANISOU 4086  C5   DT F   8     9974   5856   5094   -466  -1096   -468       C  
ATOM   4087  C7   DT F   8      -7.221 -28.663  -7.619  1.00 54.45           C  
ANISOU 4087  C7   DT F   8     9822   5878   4989   -494  -1424    -60       C  
ATOM   4088  C6   DT F   8      -6.805 -31.098  -7.323  1.00 51.40           C  
ANISOU 4088  C6   DT F   8     9617   5399   4514   -287  -1384   -879       C  
ATOM   4089  P    DT F   9      -8.551 -35.105  -2.935  1.00 26.65           P  
ANISOU 4089  P    DT F   9     3399   3027   3700    262   -865   -750       P  
ATOM   4090  OP1  DT F   9      -9.997 -35.025  -2.589  1.00 26.29           O  
ANISOU 4090  OP1  DT F   9     2843   3270   3878    745   -740   -489       O  
ATOM   4091  OP2  DT F   9      -7.606 -34.058  -2.497  1.00 22.66           O  
ANISOU 4091  OP2  DT F   9     2632   2619   3360   -188   -637   -840       O  
ATOM   4092  O5'  DT F   9      -8.039 -36.483  -2.368  1.00 25.98           O  
ANISOU 4092  O5'  DT F   9     3290   3008   3574    504   -372   -698       O  
ATOM   4093  C5'  DT F   9      -8.708 -37.663  -2.703  1.00 21.29           C  
ANISOU 4093  C5'  DT F   9     3255   2132   2703    480   -404   -830       C  
ATOM   4094  C4'  DT F   9      -7.965 -38.802  -2.072  1.00 19.02           C  
ANISOU 4094  C4'  DT F   9     2861   2059   2307    150   -270   -814       C  
ATOM   4095  O4'  DT F   9      -7.740 -38.486  -0.673  1.00 20.12           O  
ANISOU 4095  O4'  DT F   9     2811   2220   2613    -97    170   -502       O  
ATOM   4096  C3'  DT F   9      -8.650 -40.159  -2.116  1.00 19.64           C  
ANISOU 4096  C3'  DT F   9     2639   1945   2880    291    403   -586       C  
ATOM   4097  O3'  DT F   9      -7.658 -41.143  -2.432  1.00 17.97           O  
ANISOU 4097  O3'  DT F   9     2581   1623   2623    129     67   -515       O  
ATOM   4098  C2'  DT F   9      -9.199 -40.309  -0.689  1.00 20.06           C  
ANISOU 4098  C2'  DT F   9     2756   2346   2520    -39    429   -797       C  
ATOM   4099  C1'  DT F   9      -8.124 -39.583   0.115  1.00 20.13           C  
ANISOU 4099  C1'  DT F   9     2718   2559   2372   -316    -20   -567       C  
ATOM   4100  N1   DT F   9      -8.566 -39.042   1.433  1.00 20.71           N  
ANISOU 4100  N1   DT F   9     2540   2716   2611    292    190   -530       N  
ATOM   4101  C2   DT F   9      -7.707 -39.136   2.510  1.00 20.07           C  
ANISOU 4101  C2   DT F   9     2654   2223   2751    427    303   -575       C  
ATOM   4102  O2   DT F   9      -6.616 -39.664   2.446  1.00 20.03           O  
ANISOU 4102  O2   DT F   9     2915   2129   2567    352     72   -676       O  
ATOM   4103  N3   DT F   9      -8.180 -38.592   3.672  1.00 21.64           N  
ANISOU 4103  N3   DT F   9     2973   2797   2452     62    594   -820       N  
ATOM   4104  C4   DT F   9      -9.391 -37.944   3.858  1.00 23.90           C  
ANISOU 4104  C4   DT F   9     3274   3114   2692    314    594   -852       C  
ATOM   4105  O4   DT F   9      -9.726 -37.478   4.947  1.00 27.08           O  
ANISOU 4105  O4   DT F   9     4004   3556   2727     72    934   -856       O  
ATOM   4106  C5   DT F   9     -10.237 -37.854   2.684  1.00 22.12           C  
ANISOU 4106  C5   DT F   9     2764   2936   2705    350    220   -707       C  
ATOM   4107  C7   DT F   9     -11.570 -37.171   2.767  1.00 23.40           C  
ANISOU 4107  C7   DT F   9     2532   3094   3264    592    369   -610       C  
ATOM   4108  C6   DT F   9      -9.787 -38.399   1.537  1.00 21.59           C  
ANISOU 4108  C6   DT F   9     2685   2834   2683    -83     66   -729       C  
ATOM   4109  P    DT F  10      -8.046 -42.669  -2.727  1.00 17.71           P  
ANISOU 4109  P    DT F  10     2377   2014   2339    124     32   -554       P  
ATOM   4110  OP1  DT F  10      -6.955 -43.194  -3.578  1.00 18.93           O  
ANISOU 4110  OP1  DT F  10     2615   2273   2304    269    327   -401       O  
ATOM   4111  OP2  DT F  10      -9.446 -42.737  -3.223  1.00 20.22           O  
ANISOU 4111  OP2  DT F  10     2369   2223   3089    318   -312   -719       O  
ATOM   4112  O5'  DT F  10      -7.996 -43.348  -1.280  1.00 17.85           O  
ANISOU 4112  O5'  DT F  10     2617   2065   2099    196    100   -316       O  
ATOM   4113  C5'  DT F  10      -6.781 -43.407  -0.587  1.00 17.57           C  
ANISOU 4113  C5'  DT F  10     2438   2405   1834    140    133   -499       C  
ATOM   4114  C4'  DT F  10      -7.016 -43.783   0.861  1.00 17.09           C  
ANISOU 4114  C4'  DT F  10     2562   2122   1808   -115    486   -856       C  
ATOM   4115  O4'  DT F  10      -7.788 -42.759   1.502  1.00 19.10           O  
ANISOU 4115  O4'  DT F  10     2643   2488   2127   -246    770   -738       O  
ATOM   4116  C3'  DT F  10      -7.828 -45.051   1.068  1.00 18.30           C  
ANISOU 4116  C3'  DT F  10     2362   2136   2457    177    467   -239       C  
ATOM   4117  O3'  DT F  10      -6.943 -46.150   1.217  1.00 19.40           O  
ANISOU 4117  O3'  DT F  10     2376   2409   2584     47    381   -225       O  
ATOM   4118  C2'  DT F  10      -8.634 -44.778   2.359  1.00 18.84           C  
ANISOU 4118  C2'  DT F  10     2481   2279   2396   -176    586   -431       C  
ATOM   4119  C1'  DT F  10      -8.332 -43.303   2.676  1.00 18.88           C  
ANISOU 4119  C1'  DT F  10     2181   2516   2476    -67    589   -415       C  
ATOM   4120  N1   DT F  10      -9.516 -42.475   3.032  1.00 20.67           N  
ANISOU 4120  N1   DT F  10     2556   2733   2565    -41    662   -639       N  
ATOM   4121  C2   DT F  10      -9.559 -41.861   4.262  1.00 22.08           C  
ANISOU 4121  C2   DT F  10     2441   3074   2874    107    573   -800       C  
ATOM   4122  O2   DT F  10      -8.695 -42.009   5.115  1.00 23.03           O  
ANISOU 4122  O2   DT F  10     2669   3445   2637    136    362   -886       O  
ATOM   4123  N3   DT F  10     -10.660 -41.077   4.469  1.00 22.87           N  
ANISOU 4123  N3   DT F  10     2411   2857   3421     53    734   -766       N  
ATOM   4124  C4   DT F  10     -11.697 -40.847   3.587  1.00 23.39           C  
ANISOU 4124  C4   DT F  10     2536   2906   3446    262    626   -568       C  
ATOM   4125  O4   DT F  10     -12.646 -40.129   3.870  1.00 27.17           O  
ANISOU 4125  O4   DT F  10     2782   3241   4300    276    790   -468       O  
ATOM   4126  C5   DT F  10     -11.581 -41.511   2.304  1.00 21.29           C  
ANISOU 4126  C5   DT F  10     2217   2977   2897    -18     58   -605       C  
ATOM   4127  C7   DT F  10     -12.648 -41.339   1.263  1.00 22.81           C  
ANISOU 4127  C7   DT F  10     2369   3145   3153     -4     -3   -458       C  
ATOM   4128  C6   DT F  10     -10.506 -42.278   2.092  1.00 21.51           C  
ANISOU 4128  C6   DT F  10     2441   2788   2944    -31    323   -615       C  
TER    4129       DT F  10                                                      
ATOM   4130  P    DT G   7     -19.871 -50.410 -23.449  1.00 86.44           P  
ANISOU 4130  P    DT G   7     7600  12494  12751   1100   1122     85       P  
ATOM   4131  OP1  DT G   7     -19.198 -50.444 -24.767  1.00 86.96           O  
ANISOU 4131  OP1  DT G   7     7697  12571  12774   1267   1118    221       O  
ATOM   4132  OP2  DT G   7     -20.706 -49.248 -23.070  1.00 86.93           O  
ANISOU 4132  OP2  DT G   7     7672  12514  12843   1191   1155     88       O  
ATOM   4133  O5'  DT G   7     -20.755 -51.735 -23.292  1.00 84.27           O  
ANISOU 4133  O5'  DT G   7     7305  12296  12419    896    929    -17       O  
ATOM   4134  C5'  DT G   7     -21.280 -52.382 -24.447  1.00 81.69           C  
ANISOU 4134  C5'  DT G   7     6963  12050  12024    876    714      8       C  
ATOM   4135  C4'  DT G   7     -21.812 -53.759 -24.094  1.00 78.59           C  
ANISOU 4135  C4'  DT G   7     6496  11745  11622   1048    440     78       C  
ATOM   4136  O4'  DT G   7     -22.416 -53.717 -22.777  1.00 77.21           O  
ANISOU 4136  O4'  DT G   7     6062  11583  11690   1195    453     79       O  
ATOM   4137  C3'  DT G   7     -22.899 -54.284 -25.015  1.00 76.13           C  
ANISOU 4137  C3'  DT G   7     6385  11521  11020   1216    147    200       C  
ATOM   4138  O3'  DT G   7     -22.904 -55.719 -24.997  1.00 73.90           O  
ANISOU 4138  O3'  DT G   7     6496  11280  10303   1240   -234    319       O  
ATOM   4139  C2'  DT G   7     -24.166 -53.695 -24.386  1.00 76.02           C  
ANISOU 4139  C2'  DT G   7     6137  11415  11331   1448    433    209       C  
ATOM   4140  C1'  DT G   7     -23.830 -53.703 -22.888  1.00 75.51           C  
ANISOU 4140  C1'  DT G   7     5669  11366  11654   1518    711     62       C  
ATOM   4141  N1   DT G   7     -24.346 -52.507 -22.135  1.00 72.17           N  
ANISOU 4141  N1   DT G   7     4631  11088  11703   1904    825    -17       N  
ATOM   4142  C2   DT G   7     -25.207 -52.689 -21.070  1.00 68.30           C  
ANISOU 4142  C2   DT G   7     3915  10593  11444   2181    969   -138       C  
ATOM   4143  O2   DT G   7     -25.593 -53.780 -20.695  1.00 61.09           O  
ANISOU 4143  O2   DT G   7     3418   9627  10166   2229    826   -180       O  
ATOM   4144  N3   DT G   7     -25.603 -51.531 -20.453  1.00 71.46           N  
ANISOU 4144  N3   DT G   7     4125  11002  12026   1873   1217   -196       N  
ATOM   4145  C4   DT G   7     -25.239 -50.238 -20.782  1.00 73.81           C  
ANISOU 4145  C4   DT G   7     4544  11225  12277   1771   1263   -262       C  
ATOM   4146  O4   DT G   7     -25.656 -49.260 -20.164  1.00 73.74           O  
ANISOU 4146  O4   DT G   7     4515  11205  12297   1784   1196   -380       O  
ATOM   4147  C5   DT G   7     -24.334 -50.119 -21.902  1.00 74.73           C  
ANISOU 4147  C5   DT G   7     4795  11316  12284   1739   1129   -165       C  
ATOM   4148  C7   DT G   7     -23.865 -48.767 -22.354  1.00 76.65           C  
ANISOU 4148  C7   DT G   7     5225  11453  12445   1596   1203   -154       C  
ATOM   4149  C6   DT G   7     -23.936 -51.245 -22.515  1.00 73.24           C  
ANISOU 4149  C6   DT G   7     4646  11244  11938   1896    891    -81       C  
ATOM   4150  P    DT G   8     -23.483 -56.555 -26.244  1.00 71.60           P  
ANISOU 4150  P    DT G   8     6581  10946   9679   1122   -238    391       P  
ATOM   4151  OP1  DT G   8     -24.041 -55.580 -27.208  1.00 74.63           O  
ANISOU 4151  OP1  DT G   8     6973  11040  10343   1108    166    259       O  
ATOM   4152  OP2  DT G   8     -24.352 -57.627 -25.708  1.00 73.14           O  
ANISOU 4152  OP2  DT G   8     6715  11129   9947   1126    -45    399       O  
ATOM   4153  O5'  DT G   8     -22.195 -57.235 -26.911  1.00 64.98           O  
ANISOU 4153  O5'  DT G   8     5893  10170   8626   1098    -75    302       O  
ATOM   4154  C5'  DT G   8     -21.436 -58.228 -26.196  1.00 56.14           C  
ANISOU 4154  C5'  DT G   8     4894   9203   7234    992    -46    333       C  
ATOM   4155  C4'  DT G   8     -20.221 -57.600 -25.532  1.00 46.90           C  
ANISOU 4155  C4'  DT G   8     3545   8196   6079    779    314    366       C  
ATOM   4156  O4'  DT G   8     -20.461 -57.447 -24.123  1.00 41.73           O  
ANISOU 4156  O4'  DT G   8     2732   8087   5035    134   -311    462       O  
ATOM   4157  C3'  DT G   8     -18.909 -58.380 -25.664  1.00 41.58           C  
ANISOU 4157  C3'  DT G   8     3062   7189   5548    668    733    311       C  
ATOM   4158  O3'  DT G   8     -17.994 -57.577 -26.337  1.00 34.82           O  
ANISOU 4158  O3'  DT G   8     2518   5810   4902    585    329     52       O  
ATOM   4159  C2'  DT G   8     -18.458 -58.640 -24.213  1.00 40.78           C  
ANISOU 4159  C2'  DT G   8     2595   7541   5358    704    515    705       C  
ATOM   4160  C1'  DT G   8     -19.257 -57.606 -23.427  1.00 40.99           C  
ANISOU 4160  C1'  DT G   8     2570   7819   5186    624    145    894       C  
ATOM   4161  N1   DT G   8     -19.612 -58.025 -22.058  1.00 39.90           N  
ANISOU 4161  N1   DT G   8     2132   7715   5312    528   -121   1173       N  
ATOM   4162  C2   DT G   8     -19.756 -57.063 -21.090  1.00 41.56           C  
ANISOU 4162  C2   DT G   8     2441   7804   5545    182   -273    894       C  
ATOM   4163  O2   DT G   8     -19.561 -55.882 -21.296  1.00 44.03           O  
ANISOU 4163  O2   DT G   8     3081   7703   5945    125     88    579       O  
ATOM   4164  N3   DT G   8     -20.125 -57.538 -19.859  1.00 40.44           N  
ANISOU 4164  N3   DT G   8     2087   7800   5479    242   -387    811       N  
ATOM   4165  C4   DT G   8     -20.368 -58.851 -19.515  1.00 41.68           C  
ANISOU 4165  C4   DT G   8     2205   8114   5518    169   -176   1371       C  
ATOM   4166  O4   DT G   8     -20.695 -59.180 -18.381  1.00 45.14           O  
ANISOU 4166  O4   DT G   8     2420   8845   5888    -16    184   1670       O  
ATOM   4167  C5   DT G   8     -20.218 -59.811 -20.583  1.00 42.15           C  
ANISOU 4167  C5   DT G   8     2252   8004   5758    276   -226   1560       C  
ATOM   4168  C7   DT G   8     -20.463 -61.269 -20.323  1.00 44.52           C  
ANISOU 4168  C7   DT G   8     2490   8130   6297    168    104   1648       C  
ATOM   4169  C6   DT G   8     -19.855 -59.356 -21.793  1.00 41.11           C  
ANISOU 4169  C6   DT G   8     2163   7814   5642    442   -242   1176       C  
ATOM   4170  P    DT G   9     -16.745 -58.214 -27.109  1.00 30.16           P  
ANISOU 4170  P    DT G   9     2281   4967   4212   -179     87   -108       P  
ATOM   4171  OP1  DT G   9     -17.192 -58.757 -28.402  1.00 32.67           O  
ANISOU 4171  OP1  DT G   9     3233   5242   3939   -444   -194   -289       O  
ATOM   4172  OP2  DT G   9     -15.980 -59.061 -26.171  1.00 30.95           O  
ANISOU 4172  OP2  DT G   9     2050   5187   4524   -604     97    169       O  
ATOM   4173  O5'  DT G   9     -15.885 -56.934 -27.428  1.00 27.84           O  
ANISOU 4173  O5'  DT G   9     2467   4234   3876     12    -90   -275       O  
ATOM   4174  C5'  DT G   9     -15.490 -56.098 -26.364  1.00 27.86           C  
ANISOU 4174  C5'  DT G   9     2398   3977   4212   -208   -173   -567       C  
ATOM   4175  C4'  DT G   9     -14.679 -54.953 -26.897  1.00 27.70           C  
ANISOU 4175  C4'  DT G   9     2429   3968   4126    -10   -666    -39       C  
ATOM   4176  O4'  DT G   9     -13.482 -55.483 -27.515  1.00 28.45           O  
ANISOU 4176  O4'  DT G   9     2465   4201   4145     -5   -532   -200       O  
ATOM   4177  C3'  DT G   9     -15.378 -54.130 -27.969  1.00 28.76           C  
ANISOU 4177  C3'  DT G   9     2720   3771   4438    -50   -964    137       C  
ATOM   4178  O3'  DT G   9     -15.009 -52.781 -27.804  1.00 31.61           O  
ANISOU 4178  O3'  DT G   9     2972   3911   5129     13   -685    -63       O  
ATOM   4179  C2'  DT G   9     -14.827 -54.718 -29.272  1.00 27.84           C  
ANISOU 4179  C2'  DT G   9     2783   3626   4167   -527   -837      0       C  
ATOM   4180  C1'  DT G   9     -13.410 -55.084 -28.861  1.00 26.70           C  
ANISOU 4180  C1'  DT G   9     2433   3701   4010   -228   -912     37       C  
ATOM   4181  N1   DT G   9     -12.800 -56.210 -29.631  1.00 26.57           N  
ANISOU 4181  N1   DT G   9     2580   3653   3863   -273   -968    -95       N  
ATOM   4182  C2   DT G   9     -11.484 -56.113 -29.998  1.00 26.35           C  
ANISOU 4182  C2   DT G   9     2780   3473   3760    470   -380    282       C  
ATOM   4183  O2   DT G   9     -10.799 -55.144 -29.743  1.00 26.83           O  
ANISOU 4183  O2   DT G   9     3186   3769   3238    284   -116    385       O  
ATOM   4184  N3   DT G   9     -10.993 -57.189 -30.685  1.00 28.17           N  
ANISOU 4184  N3   DT G   9     3347   3668   3689    -18   -441   -483       N  
ATOM   4185  C4   DT G   9     -11.671 -58.339 -31.021  1.00 28.84           C  
ANISOU 4185  C4   DT G   9     3373   3804   3780    -87   -524   -736       C  
ATOM   4186  O4   DT G   9     -11.132 -59.257 -31.636  1.00 30.88           O  
ANISOU 4186  O4   DT G   9     3690   4306   3735    -82   -642   -531       O  
ATOM   4187  C5   DT G   9     -13.052 -58.390 -30.591  1.00 29.29           C  
ANISOU 4187  C5   DT G   9     3312   3705   4113   -256   -305  -1018       C  
ATOM   4188  C7   DT G   9     -13.890 -59.596 -30.894  1.00 32.23           C  
ANISOU 4188  C7   DT G   9     3555   4100   4589   -486    -56  -1229       C  
ATOM   4189  C6   DT G   9     -13.544 -57.334 -29.916  1.00 26.69           C  
ANISOU 4189  C6   DT G   9     2695   3375   4071   -219   -853   -715       C  
ATOM   4190  P    DT G  10     -15.724 -51.625 -28.649  1.00 34.09           P  
ANISOU 4190  P    DT G  10     3052   4149   5752    266   -954    306       P  
ATOM   4191  OP1  DT G  10     -15.571 -50.388 -27.865  1.00 32.64           O  
ANISOU 4191  OP1  DT G  10     3325   3725   5351     49    -44   -238       O  
ATOM   4192  OP2  DT G  10     -17.076 -52.067 -29.046  1.00 33.10           O  
ANISOU 4192  OP2  DT G  10     3044   3912   5621    290  -1630    305       O  
ATOM   4193  O5'  DT G  10     -14.851 -51.515 -29.982  1.00 31.62           O  
ANISOU 4193  O5'  DT G  10     2827   4247   4941   -172  -1756    578       O  
ATOM   4194  C5'  DT G  10     -13.471 -51.191 -29.906  1.00 31.09           C  
ANISOU 4194  C5'  DT G  10     2806   4199   4806   -105  -1771    877       C  
ATOM   4195  C4'  DT G  10     -12.790 -51.494 -31.220  1.00 31.22           C  
ANISOU 4195  C4'  DT G  10     3363   4169   4331   -328  -1391   1015       C  
ATOM   4196  O4'  DT G  10     -12.748 -52.913 -31.420  1.00 31.07           O  
ANISOU 4196  O4'  DT G  10     3477   4274   4053   -698  -1191    687       O  
ATOM   4197  C3'  DT G  10     -13.503 -50.953 -32.452  1.00 33.13           C  
ANISOU 4197  C3'  DT G  10     3884   4446   4258   -589  -1426   1043       C  
ATOM   4198  O3'  DT G  10     -12.938 -49.710 -32.825  1.00 34.62           O  
ANISOU 4198  O3'  DT G  10     4309   4464   4379   -451  -1591   1310       O  
ATOM   4199  C2'  DT G  10     -13.269 -52.034 -33.532  1.00 33.34           C  
ANISOU 4199  C2'  DT G  10     4080   4542   4046   -417  -1423    759       C  
ATOM   4200  C1'  DT G  10     -12.534 -53.150 -32.784  1.00 32.17           C  
ANISOU 4200  C1'  DT G  10     3840   4464   3921   -669  -1489    635       C  
ATOM   4201  N1   DT G  10     -13.021 -54.526 -33.088  1.00 32.73           N  
ANISOU 4201  N1   DT G  10     3615   4730   4092   -960  -2099    347       N  
ATOM   4202  C2   DT G  10     -12.142 -55.459 -33.603  1.00 33.43           C  
ANISOU 4202  C2   DT G  10     3929   4731   4041  -1008  -1879   -177       C  
ATOM   4203  O2   DT G  10     -10.976 -55.217 -33.857  1.00 32.65           O  
ANISOU 4203  O2   DT G  10     3918   4771   3715   -610  -1540   -148       O  
ATOM   4204  N3   DT G  10     -12.685 -56.695 -33.819  1.00 35.20           N  
ANISOU 4204  N3   DT G  10     4292   4738   4345   -949  -2095    -48       N  
ATOM   4205  C4   DT G  10     -13.983 -57.091 -33.570  1.00 37.89           C  
ANISOU 4205  C4   DT G  10     4656   4974   4767  -1004  -1641    -74       C  
ATOM   4206  O4   DT G  10     -14.374 -58.227 -33.802  1.00 39.12           O  
ANISOU 4206  O4   DT G  10     5200   4793   4872  -1153  -1125   -378       O  
ATOM   4207  C5   DT G  10     -14.850 -56.070 -33.025  1.00 36.51           C  
ANISOU 4207  C5   DT G  10     4096   5075   4703   -794  -1956    -22       C  
ATOM   4208  C7   DT G  10     -16.282 -56.384 -32.715  1.00 38.34           C  
ANISOU 4208  C7   DT G  10     4140   5346   5083   -756  -1845    151       C  
ATOM   4209  C6   DT G  10     -14.331 -54.853 -32.808  1.00 35.35           C  
ANISOU 4209  C6   DT G  10     3793   5067   4573   -755  -2185    414       C  
TER    4210       DT G  10                                                      
ATOM   4211  P    DT H   7      52.819 -64.797 -12.358  1.00 92.55           P  
ANISOU 4211  P    DT H   7     8231  13829  13105   2195  -1236   2477       P  
ATOM   4212  OP1  DT H   7      52.660 -65.961 -11.456  1.00 93.74           O  
ANISOU 4212  OP1  DT H   7     8452  13946  13218   2016   -865   2342       O  
ATOM   4213  OP2  DT H   7      53.602 -64.928 -13.609  1.00 92.21           O  
ANISOU 4213  OP2  DT H   7     8087  13798  13150   2281  -1548   2555       O  
ATOM   4214  O5'  DT H   7      51.374 -64.217 -12.732  1.00 91.74           O  
ANISOU 4214  O5'  DT H   7     8009  13780  13066   2160   -909   2338       O  
ATOM   4215  C5'  DT H   7      51.106 -62.829 -12.575  1.00 89.07           C  
ANISOU 4215  C5'  DT H   7     7515  13653  12674   2221  -1087   2435       C  
ATOM   4216  C4'  DT H   7      50.237 -62.310 -13.707  1.00 86.12           C  
ANISOU 4216  C4'  DT H   7     7007  13427  12286   2215  -1221   2575       C  
ATOM   4217  O4'  DT H   7      50.589 -62.985 -14.942  1.00 87.80           O  
ANISOU 4217  O4'  DT H   7     7265  13570  12527   2194  -1155   2538       O  
ATOM   4218  C3'  DT H   7      48.739 -62.519 -13.522  1.00 81.63           C  
ANISOU 4218  C3'  DT H   7     6312  13015  11691   2271  -1369   2704       C  
ATOM   4219  O3'  DT H   7      48.038 -61.405 -14.035  1.00 73.81           O  
ANISOU 4219  O3'  DT H   7     5222  12362  10460   1922  -1557   2641       O  
ATOM   4220  C2'  DT H   7      48.458 -63.780 -14.333  1.00 85.48           C  
ANISOU 4220  C2'  DT H   7     6854  13342  12283   2343  -1264   2562       C  
ATOM   4221  C1'  DT H   7      49.464 -63.659 -15.469  1.00 89.82           C  
ANISOU 4221  C1'  DT H   7     7551  13724  12853   2217  -1002   2336       C  
ATOM   4222  N1   DT H   7      49.924 -64.973 -15.990  1.00 95.80           N  
ANISOU 4222  N1   DT H   7     8435  14292  13672   2148   -744   1901       N  
ATOM   4223  C2   DT H   7      50.020 -65.164 -17.348  1.00 98.54           C  
ANISOU 4223  C2   DT H   7     8952  14503  13987   2152   -530   1861       C  
ATOM   4224  O2   DT H   7      49.739 -64.304 -18.164  1.00 98.60           O  
ANISOU 4224  O2   DT H   7     9100  14443  13919   2192   -561   1958       O  
ATOM   4225  N3   DT H   7      50.458 -66.408 -17.721  1.00100.38           N  
ANISOU 4225  N3   DT H   7     9144  14709  14287   2139   -437   1743       N  
ATOM   4226  C4   DT H   7      50.804 -67.458 -16.887  1.00100.83           C  
ANISOU 4226  C4   DT H   7     9163  14776  14370   2149   -600   1724       C  
ATOM   4227  O4   DT H   7      51.188 -68.541 -17.318  1.00101.60           O  
ANISOU 4227  O4   DT H   7     9307  14815  14482   2165   -501   1757       O  
ATOM   4228  C5   DT H   7      50.680 -67.189 -15.474  1.00 99.46           C  
ANISOU 4228  C5   DT H   7     8913  14725  14152   2124   -924   1693       C  
ATOM   4229  C7   DT H   7      51.026 -68.250 -14.471  1.00 99.73           C  
ANISOU 4229  C7   DT H   7     8916  14791  14187   2078  -1027   1594       C  
ATOM   4230  C6   DT H   7      50.252 -65.975 -15.098  1.00 97.60           C  
ANISOU 4230  C6   DT H   7     8624  14552  13908   2150   -981   1784       C  
ATOM   4231  P    DT H   8      47.812 -60.108 -13.117  0.62 67.22           P  
ANISOU 4231  P    DT H   8     4486  11609   9445   1720  -1495   2535       P  
ATOM   4232  OP1  DT H   8      49.007 -59.241 -13.248  0.82 66.83           O  
ANISOU 4232  OP1  DT H   8     4493  11454   9446   1377  -1338   2307       O  
ATOM   4233  OP2  DT H   8      47.383 -60.571 -11.779  0.42 67.60           O  
ANISOU 4233  OP2  DT H   8     4545  11612   9527   1877  -1249   2534       O  
ATOM   4234  O5'  DT H   8      46.558 -59.404 -13.791  1.00 65.06           O  
ANISOU 4234  O5'  DT H   8     4481  11286   8953   1370   -556   2326       O  
ATOM   4235  C5'  DT H   8      45.422 -60.179 -14.098  1.00 61.03           C  
ANISOU 4235  C5'  DT H   8     3900  10869   8417   1190   -214   2190       C  
ATOM   4236  C4'  DT H   8      44.346 -59.305 -14.685  1.00 55.89           C  
ANISOU 4236  C4'  DT H   8     3162  10292   7780   1041   -532   1944       C  
ATOM   4237  O4'  DT H   8      44.805 -58.758 -15.928  1.00 53.17           O  
ANISOU 4237  O4'  DT H   8     2896   9853   7452    915   -430   1611       O  
ATOM   4238  C3'  DT H   8      43.056 -60.013 -15.034  1.00 54.97           C  
ANISOU 4238  C3'  DT H   8     3183  10069   7635   1345   -180   2043       C  
ATOM   4239  O3'  DT H   8      42.267 -60.117 -13.858  1.00 54.90           O  
ANISOU 4239  O3'  DT H   8     3349  10050   7460   1667    -29   2143       O  
ATOM   4240  C2'  DT H   8      42.445 -59.056 -16.072  1.00 52.95           C  
ANISOU 4240  C2'  DT H   8     2999   9795   7323   1073   -310   1838       C  
ATOM   4241  C1'  DT H   8      43.687 -58.375 -16.694  1.00 50.72           C  
ANISOU 4241  C1'  DT H   8     2917   9297   7056    942   -772   1586       C  
ATOM   4242  N1   DT H   8      43.972 -58.711 -18.139  1.00 47.76           N  
ANISOU 4242  N1   DT H   8     2897   8567   6683    969  -1058   1397       N  
ATOM   4243  C2   DT H   8      43.969 -60.027 -18.573  1.00 48.97           C  
ANISOU 4243  C2   DT H   8     2781   8846   6982    740   -942   1402       C  
ATOM   4244  O2   DT H   8      43.724 -60.977 -17.860  1.00 53.37           O  
ANISOU 4244  O2   DT H   8     3136   9364   7777    489    -64   1135       O  
ATOM   4245  N3   DT H   8      44.266 -60.190 -19.896  1.00 48.21           N  
ANISOU 4245  N3   DT H   8     2922   8701   6697    810  -1282   1189       N  
ATOM   4246  C4   DT H   8      44.575 -59.207 -20.809  1.00 48.39           C  
ANISOU 4246  C4   DT H   8     2935   8804   6648    551  -1481    981       C  
ATOM   4247  O4   DT H   8      44.828 -59.460 -21.979  1.00 51.26           O  
ANISOU 4247  O4   DT H   8     3058   9492   6925     -2  -1151    562       O  
ATOM   4248  C5   DT H   8      44.575 -57.864 -20.298  1.00 47.93           C  
ANISOU 4248  C5   DT H   8     3223   8347   6641    917  -1653   1253       C  
ATOM   4249  C7   DT H   8      44.890 -56.712 -21.210  1.00 51.05           C  
ANISOU 4249  C7   DT H   8     3388   8923   7084    917  -1761   1263       C  
ATOM   4250  C6   DT H   8      44.286 -57.682 -19.002  1.00 47.01           C  
ANISOU 4250  C6   DT H   8     3305   8127   6429   1204  -1355   1605       C  
ATOM   4251  P    DT H   9      40.974 -61.072 -13.775  1.00 54.48           P  
ANISOU 4251  P    DT H   9     3822   9717   7161   2284    178   2399       P  
ATOM   4252  OP1  DT H   9      41.381 -62.392 -13.256  1.00 57.17           O  
ANISOU 4252  OP1  DT H   9     4615   9418   7689   3043   1053   2567       O  
ATOM   4253  OP2  DT H   9      40.224 -60.992 -15.049  1.00 54.38           O  
ANISOU 4253  OP2  DT H   9     3898   9600   7165   2335     -8   2319       O  
ATOM   4254  O5'  DT H   9      40.122 -60.372 -12.637  1.00 54.70           O  
ANISOU 4254  O5'  DT H   9     4012   9592   7179   2388    684   2607       O  
ATOM   4255  C5'  DT H   9      39.815 -58.994 -12.765  1.00 53.45           C  
ANISOU 4255  C5'  DT H   9     3944   9330   7032   2161   1317   2543       C  
ATOM   4256  C4'  DT H   9      38.873 -58.568 -11.673  1.00 49.71           C  
ANISOU 4256  C4'  DT H   9     3689   8844   6354   2150   1017   3047       C  
ATOM   4257  O4'  DT H   9      37.774 -59.506 -11.620  1.00 47.74           O  
ANISOU 4257  O4'  DT H   9     3619   8655   5865   1968    988   3449       O  
ATOM   4258  C3'  DT H   9      39.485 -58.534 -10.273  1.00 47.59           C  
ANISOU 4258  C3'  DT H   9     3478   8551   6052   1961    777   2972       C  
ATOM   4259  O3'  DT H   9      39.038 -57.368  -9.601  1.00 46.73           O  
ANISOU 4259  O3'  DT H   9     2967   8808   5980   1217    580   2912       O  
ATOM   4260  C2'  DT H   9      38.961 -59.816  -9.625  1.00 47.43           C  
ANISOU 4260  C2'  DT H   9     3679   8281   6062   2059    785   3166       C  
ATOM   4261  C1'  DT H   9      37.606 -59.968 -10.304  1.00 48.17           C  
ANISOU 4261  C1'  DT H   9     3883   8380   6041   2164    946   3396       C  
ATOM   4262  N1   DT H   9      37.086 -61.372 -10.368  1.00 48.45           N  
ANISOU 4262  N1   DT H   9     4063   8271   6076   2262   1153   3556       N  
ATOM   4263  C2   DT H   9      35.772 -61.600 -10.053  1.00 48.94           C  
ANISOU 4263  C2   DT H   9     4268   8290   6038   2277   1340   3598       C  
ATOM   4264  O2   DT H   9      35.018 -60.715  -9.719  1.00 45.70           O  
ANISOU 4264  O2   DT H   9     3806   7876   5680   2114   1197   3457       O  
ATOM   4265  N3   DT H   9      35.370 -62.905 -10.145  1.00 50.57           N  
ANISOU 4265  N3   DT H   9     4622   8309   6283   2547   1084   3534       N  
ATOM   4266  C4   DT H   9      36.141 -63.988 -10.518  1.00 53.38           C  
ANISOU 4266  C4   DT H   9     5012   8365   6905   2831   1466   3465       C  
ATOM   4267  O4   DT H   9      35.688 -65.128 -10.570  1.00 53.47           O  
ANISOU 4267  O4   DT H   9     5352   7929   7034   3005   1501   3483       O  
ATOM   4268  C5   DT H   9      37.515 -63.680 -10.846  1.00 51.92           C  
ANISOU 4268  C5   DT H   9     4463   8390   6873   2709   1328   3242       C  
ATOM   4269  C7   DT H   9      38.449 -64.771 -11.269  1.00 51.84           C  
ANISOU 4269  C7   DT H   9     4442   8430   6823   2764    975   2920       C  
ATOM   4270  C6   DT H   9      37.917 -62.400 -10.759  1.00 49.98           C  
ANISOU 4270  C6   DT H   9     4376   8202   6413   2612   1437   3401       C  
ATOM   4271  P    DT H  10      39.730 -56.879  -8.240  1.00 48.05           P  
ANISOU 4271  P    DT H  10     3022   9031   6205   1171    253   2911       P  
ATOM   4272  OP1  DT H  10      39.473 -55.429  -8.100  1.00 51.15           O  
ANISOU 4272  OP1  DT H  10     3191   9697   6545    849    364   2955       O  
ATOM   4273  OP2  DT H  10      41.124 -57.389  -8.221  1.00 48.23           O  
ANISOU 4273  OP2  DT H  10     3013   9035   6278   1193    -15   2585       O  
ATOM   4274  O5'  DT H  10      38.914 -57.647  -7.112  1.00 47.63           O  
ANISOU 4274  O5'  DT H  10     2904   9174   6018    769    -40   2869       O  
ATOM   4275  C5'  DT H  10      37.510 -57.445  -7.016  1.00 47.35           C  
ANISOU 4275  C5'  DT H  10     3119   9039   5833   1002    -70   3080       C  
ATOM   4276  C4'  DT H  10      36.860 -58.537  -6.188  1.00 48.63           C  
ANISOU 4276  C4'  DT H  10     3533   9199   5745   1251    -78   3299       C  
ATOM   4277  O4'  DT H  10      36.875 -59.772  -6.913  1.00 49.06           O  
ANISOU 4277  O4'  DT H  10     3607   9043   5991   1575     56   3192       O  
ATOM   4278  C3'  DT H  10      37.559 -58.860  -4.880  1.00 49.11           C  
ANISOU 4278  C3'  DT H  10     3686   9427   5545   1348   -192   3131       C  
ATOM   4279  O3'  DT H  10      37.040 -58.036  -3.845  1.00 49.13           O  
ANISOU 4279  O3'  DT H  10     3944   9695   5028   1182   -300   3096       O  
ATOM   4280  C2'  DT H  10      37.224 -60.347  -4.649  1.00 48.83           C  
ANISOU 4280  C2'  DT H  10     3642   9108   5803   1465    -38   3223       C  
ATOM   4281  C1'  DT H  10      36.649 -60.810  -5.995  1.00 51.01           C  
ANISOU 4281  C1'  DT H  10     3688   9077   6616   1713    231   3203       C  
ATOM   4282  N1   DT H  10      37.274 -62.045  -6.536  1.00 52.29           N  
ANISOU 4282  N1   DT H  10     3886   9044   6937   1933     97   3171       N  
ATOM   4283  C2   DT H  10      36.504 -63.172  -6.701  1.00 52.82           C  
ANISOU 4283  C2   DT H  10     4196   8975   6898   2010    168   3469       C  
ATOM   4284  O2   DT H  10      35.328 -63.228  -6.404  1.00 54.18           O  
ANISOU 4284  O2   DT H  10     4326   9211   7049   2114    366   3675       O  
ATOM   4285  N3   DT H  10      37.164 -64.243  -7.227  1.00 53.64           N  
ANISOU 4285  N3   DT H  10     4237   9087   7058   2151    228   3394       N  
ATOM   4286  C4   DT H  10      38.490 -64.304  -7.599  1.00 56.43           C  
ANISOU 4286  C4   DT H  10     4584   9248   7610   2259    586   3286       C  
ATOM   4287  O4   DT H  10      38.990 -65.321  -8.061  1.00 60.68           O  
ANISOU 4287  O4   DT H  10     5576   9148   8330   2545   1412   3242       O  
ATOM   4288  C5   DT H  10      39.244 -63.086  -7.409  1.00 54.73           C  
ANISOU 4288  C5   DT H  10     4124   9190   7482   2171    345   3214       C  
ATOM   4289  C7   DT H  10      40.699 -63.032  -7.777  1.00 53.68           C  
ANISOU 4289  C7   DT H  10     3859   9056   7480   2171    262   2818       C  
ATOM   4290  C6   DT H  10      38.606 -62.026  -6.895  1.00 53.36           C  
ANISOU 4290  C6   DT H  10     4025   9131   7117   1973     74   3287       C  
TER    4291       DT H  10                                                      
HETATM 4292  P  A DT A 201      22.410 -29.139 -42.403  0.52 56.21           P  
ANISOU 4292  P  A DT A 201     7684   7497   6178    849   -418  -1502       P  
HETATM 4293  P  B DT A 201      24.141 -26.208 -42.402  0.48 42.78           P  
ANISOU 4293  P  B DT A 201     6427   7033   2795    633   -920   1189       P  
HETATM 4294  OP1A DT A 201      22.204 -28.462 -41.103  0.52 55.11           O  
ANISOU 4294  OP1A DT A 201     7385   7458   6096    880   -419  -1532       O  
HETATM 4295  OP1B DT A 201      24.985 -25.000 -42.558  0.48 40.49           O  
ANISOU 4295  OP1B DT A 201     6492   6503   2391    718  -1256    842       O  
HETATM 4296  OP2A DT A 201      21.554 -30.281 -42.794  0.52 56.86           O  
ANISOU 4296  OP2A DT A 201     7743   7454   6407    647   -320  -1438       O  
HETATM 4297  OP2B DT A 201      23.227 -26.307 -41.239  0.48 42.08           O  
ANISOU 4297  OP2B DT A 201     6280   7159   2548    509   -865   1248       O  
HETATM 4298  O5'A DT A 201      23.937 -29.604 -42.509  0.52 54.69           O  
ANISOU 4298  O5'A DT A 201     7735   7457   5588    993   -622  -1282       O  
HETATM 4299  O5'B DT A 201      25.062 -27.525 -42.427  0.48 45.26           O  
ANISOU 4299  O5'B DT A 201     6850   6887   3458   1002   -974   1321       O  
HETATM 4300  C5'A DT A 201      24.799 -28.992 -43.459  0.52 54.44           C  
ANISOU 4300  C5'A DT A 201     7906   7471   5307   1115   -417   -852       C  
HETATM 4301  C5'B DT A 201      25.788 -27.885 -43.609  0.48 46.26           C  
ANISOU 4301  C5'B DT A 201     7252   6972   3352   1049  -1178    887       C  
HETATM 4302  C4'A DT A 201      26.257 -29.280 -43.145  0.52 54.50           C  
ANISOU 4302  C4'A DT A 201     8079   7455   5172   1219    -75   -484       C  
HETATM 4303  C4'B DT A 201      27.013 -28.730 -43.270  0.48 49.78           C  
ANISOU 4303  C4'B DT A 201     7755   7094   4065    962   -496    484       C  
HETATM 4304  O4'A DT A 201      26.617 -28.673 -41.875  0.52 49.87           O  
ANISOU 4304  O4'A DT A 201     7623   6916   4411   1363   -179   -162       O  
HETATM 4305  O4'B DT A 201      27.504 -28.365 -41.949  0.48 46.18           O  
ANISOU 4305  O4'B DT A 201     7443   6536   3567    905   -614    501       O  
HETATM 4306  C3'A DT A 201      26.619 -30.759 -43.015  0.52 58.73           C  
ANISOU 4306  C3'A DT A 201     8594   7912   5811   1152    460   -428       C  
HETATM 4307  C3'B DT A 201      26.780 -30.242 -43.216  0.48 55.98           C  
ANISOU 4307  C3'B DT A 201     8416   7676   5179    919    217    213       C  
HETATM 4308  O3'A DT A 201      27.901 -30.983 -43.573  0.52 68.85           O  
ANISOU 4308  O3'A DT A 201     9667   9138   7354   1092   1290   -406       O  
HETATM 4309  O3'B DT A 201      27.979 -30.934 -43.590  0.48 67.50           O  
ANISOU 4309  O3'B DT A 201     9580   9015   7052    989   1168   -100       O  
HETATM 4310  C2'A DT A 201      26.632 -30.971 -41.507  0.52 52.30           C  
ANISOU 4310  C2'A DT A 201     7953   7126   4791   1103    264   -308       C  
HETATM 4311  C2'B DT A 201      26.473 -30.455 -41.738  0.48 50.09           C  
ANISOU 4311  C2'B DT A 201     7790   6913   4329    773     96    324       C  
HETATM 4312  C1'A DT A 201      27.214 -29.648 -41.052  0.52 46.76           C  
ANISOU 4312  C1'A DT A 201     7308   6361   4098   1077    175   -235       C  
HETATM 4313  C1'B DT A 201      27.478 -29.500 -41.107  0.48 44.62           C  
ANISOU 4313  C1'B DT A 201     7186   6122   3644    695     14    466       C  
HETATM 4314  N1 A DT A 201      26.915 -29.310 -39.644  0.52 37.77           N  
ANISOU 4314  N1 A DT A 201     6157   5106   3089    747    125   -343       N  
HETATM 4315  N1 B DT A 201      27.112 -29.056 -39.731  0.48 37.00           N  
ANISOU 4315  N1 B DT A 201     6163   4993   2901    421    209    681       N  
HETATM 4316  C2 A DT A 201      27.851 -29.585 -38.675  0.52 32.73           C  
ANISOU 4316  C2 A DT A 201     5239   3935   3262    -33    357   -494       C  
HETATM 4317  C2 B DT A 201      27.843 -29.514 -38.656  0.48 32.00           C  
ANISOU 4317  C2 B DT A 201     5199   3835   3124   -299    732    913       C  
HETATM 4318  O2 A DT A 201      28.920 -30.120 -38.909  0.52 29.28           O  
ANISOU 4318  O2 A DT A 201     4519   3086   3522   -541    267   -919       O  
HETATM 4319  O2 B DT A 201      28.783 -30.284 -38.762  0.48 28.33           O  
ANISOU 4319  O2 B DT A 201     4373   2957   3433   -853   1483    908       O  
HETATM 4320  N3 A DT A 201      27.484 -29.220 -37.411  0.52 29.53           N  
ANISOU 4320  N3 A DT A 201     4959   3672   2589   -174    412   -600       N  
HETATM 4321  N3 B DT A 201      27.430 -29.039 -37.442  0.48 29.51           N  
ANISOU 4321  N3 B DT A 201     4978   3630   2604   -487    504    945       N  
HETATM 4322  C4 A DT A 201      26.300 -28.618 -37.025  0.52 33.25           C  
ANISOU 4322  C4 A DT A 201     5408   4336   2889    420    195   -218       C  
HETATM 4323  C4 B DT A 201      26.383 -28.168 -37.196  0.48 32.81           C  
ANISOU 4323  C4 B DT A 201     5408   4356   2703    144    -12    819       C  
HETATM 4324  O4 A DT A 201      26.063 -28.327 -35.858  0.52 32.14           O  
ANISOU 4324  O4 A DT A 201     5085   4360   2767    361    443   -355       O  
HETATM 4325  O4 B DT A 201      26.089 -27.798 -36.063  0.48 31.87           O  
ANISOU 4325  O4 B DT A 201     5074   4404   2630    216    115    543       O  
HETATM 4326  C5 A DT A 201      25.366 -28.352 -38.091  0.52 37.36           C  
ANISOU 4326  C5 A DT A 201     5880   5150   3164    931    -19   -213       C  
HETATM 4327  C5 B DT A 201      25.663 -27.722 -38.366  0.48 36.38           C  
ANISOU 4327  C5 B DT A 201     5877   4983   2962    474   -209    545       C  
HETATM 4328  C7 A DT A 201      24.050 -27.699 -37.792  0.52 40.17           C  
ANISOU 4328  C7 A DT A 201     6050   5596   3619   1088   -116   -215       C  
HETATM 4329  C7 B DT A 201      24.509 -26.774 -38.225  0.48 38.14           C  
ANISOU 4329  C7 B DT A 201     6093   5151   3247    473   -478    618       C  
HETATM 4330  C6 A DT A 201      25.716 -28.704 -39.336  0.52 38.25           C  
ANISOU 4330  C6 A DT A 201     6084   5258   3192    883   -121   -344       C  
HETATM 4331  C6 B DT A 201      26.060 -28.180 -39.563  0.48 37.31           C  
ANISOU 4331  C6 B DT A 201     6111   5149   2915    430     18    514       C  
HETATM 4332  P    DT A 202      28.042 -31.846 -44.916  1.00 78.43           P  
ANISOU 4332  P    DT A 202    10631  10100   9070   1111   1953   -388       P  
HETATM 4333  OP1  DT A 202      28.524 -30.969 -46.008  1.00 80.03           O  
ANISOU 4333  OP1  DT A 202    10599  10387   9422    983   2612   -380       O  
HETATM 4334  OP2  DT A 202      26.764 -32.578 -45.070  1.00 80.68           O  
ANISOU 4334  OP2  DT A 202    10597  10371   9686   1031   2163   -520       O  
HETATM 4335  O5'  DT A 202      29.190 -32.913 -44.583  1.00 89.45           O  
ANISOU 4335  O5'  DT A 202    11880  11379  10729   1215   2097   -279       O  
HETATM 4336  C5'  DT A 202      30.522 -32.474 -44.331  1.00 97.08           C  
ANISOU 4336  C5'  DT A 202    12681  12339  11866   1159   2418   -299       C  
HETATM 4337  C1  GOL A 203      13.492 -46.752 -18.459  1.00 25.11           C  
ANISOU 4337  C1  GOL A 203     3582   3177   2783    527   -165    875       C  
HETATM 4338  O1  GOL A 203      13.754 -48.054 -18.932  1.00 26.87           O  
ANISOU 4338  O1  GOL A 203     4011   3356   2841    881   -123    218       O  
HETATM 4339  C2  GOL A 203      13.393 -45.778 -19.618  1.00 22.65           C  
ANISOU 4339  C2  GOL A 203     2863   3042   2703    212   -574    474       C  
HETATM 4340  O2  GOL A 203      12.149 -45.963 -20.261  1.00 18.56           O  
ANISOU 4340  O2  GOL A 203     2343   2252   2457     65    -60    466       O  
HETATM 4341  C3  GOL A 203      13.437 -44.391 -19.010  1.00 27.83           C  
ANISOU 4341  C3  GOL A 203     2986   3793   3795    -99   -512   -283       C  
HETATM 4342  O3  GOL A 203      14.680 -44.175 -18.379  1.00 30.35           O  
ANISOU 4342  O3  GOL A 203     3479   4226   3827    255   -386    106       O  
HETATM 4343 NA    NA A 204      23.686 -21.773 -20.412  1.00 21.28          NA  
ANISOU 4343 NA    NA A 204     3796   1976   2313   -209    -54    -60      NA  
HETATM 4344  C1  GOL B 201       9.926 -48.691 -13.244  1.00 29.66           C  
ANISOU 4344  C1  GOL B 201     4314   3768   3186    492    338     56       C  
HETATM 4345  O1  GOL B 201       9.991 -49.987 -13.818  1.00 32.05           O  
ANISOU 4345  O1  GOL B 201     4936   3817   3423    180   -393    445       O  
HETATM 4346  C2  GOL B 201      10.112 -48.783 -11.736  1.00 27.17           C  
ANISOU 4346  C2  GOL B 201     3587   3598   3139    243    -62    138       C  
HETATM 4347  O2  GOL B 201      11.452 -49.044 -11.389  1.00 20.18           O  
ANISOU 4347  O2  GOL B 201     2570   2390   2708    148    -14    363       O  
HETATM 4348  C3  GOL B 201       9.656 -47.513 -11.062  1.00 35.58           C  
ANISOU 4348  C3  GOL B 201     5139   4233   4146     73    592    149       C  
HETATM 4349  O3  GOL B 201       9.827 -46.434 -11.950  1.00 41.02           O  
ANISOU 4349  O3  GOL B 201     6294   4500   4793   -315   1225    466       O  
HETATM 4350 NA    NA B 202      -1.392 -31.034   3.824  1.00 25.94          NA  
ANISOU 4350 NA    NA B 202     5240   1951   2663   -275   -992   -610      NA  
HETATM 4351 NA    NA C 201      -4.925 -59.706 -23.057  1.00 19.19          NA  
ANISOU 4351 NA    NA C 201     2827   2075   2389    -65    123   -430      NA  
HETATM 4352 NA    NA D 201      28.902 -60.938 -17.769  1.00 38.50          NA  
ANISOU 4352 NA    NA D 201     4803   4291   5535   2208   2287   2012      NA  
HETATM 4353  O   HOH A 301      22.364 -23.222 -21.821  1.00 21.68           O  
HETATM 4354  O   HOH A 302      27.816 -25.720 -31.177  1.00 22.27           O  
HETATM 4355  O   HOH A 303      13.070 -25.498 -25.397  1.00 20.70           O  
HETATM 4356  O   HOH A 304      16.507 -51.041 -26.836  1.00 18.41           O  
HETATM 4357  O   HOH A 305       8.634 -51.280 -41.277  1.00 26.30           O  
HETATM 4358  O   HOH A 306      16.561 -47.289 -20.278  1.00 21.17           O  
HETATM 4359  O   HOH A 307      28.436 -28.265 -31.237  1.00 23.66           O  
HETATM 4360  O   HOH A 308      24.242 -55.349 -30.343  1.00 21.99           O  
HETATM 4361  O   HOH A 309      15.435 -37.286 -34.487  1.00 24.92           O  
HETATM 4362  O   HOH A 310      10.286 -37.423 -25.111  1.00 20.90           O  
HETATM 4363  O   HOH A 311      17.355 -23.013 -18.924  1.00 28.08           O  
HETATM 4364  O   HOH A 312      14.267 -50.526 -30.798  1.00 23.83           O  
HETATM 4365  O   HOH A 313      17.096 -44.759 -19.644  1.00 21.52           O  
HETATM 4366  O   HOH A 314       5.307 -50.062 -30.203  1.00 16.71           O  
HETATM 4367  O   HOH A 315      27.401 -34.563 -27.706  1.00 16.55           O  
HETATM 4368  O   HOH A 316      16.410 -53.529 -38.133  1.00 20.58           O  
HETATM 4369  O   HOH A 317      12.928 -46.043 -38.755  1.00 19.99           O  
HETATM 4370  O   HOH A 318      27.007 -43.836 -32.907  1.00 22.73           O  
HETATM 4371  O   HOH A 319      19.046 -52.275 -26.528  1.00 16.35           O  
HETATM 4372  O   HOH A 320      22.016 -41.419 -20.686  1.00 20.19           O  
HETATM 4373  O   HOH A 321      13.245 -54.707 -36.745  1.00 20.31           O  
HETATM 4374  O   HOH A 322      30.906 -39.544 -28.311  1.00 21.19           O  
HETATM 4375  O   HOH A 323      25.592 -22.703 -30.492  1.00 19.38           O  
HETATM 4376  O   HOH A 324      28.083 -29.953 -17.762  1.00 22.97           O  
HETATM 4377  O   HOH A 325      12.880 -21.755 -24.118  1.00 22.98           O  
HETATM 4378  O   HOH A 326      17.341 -51.816 -40.154  1.00 27.24           O  
HETATM 4379  O   HOH A 327      21.211 -17.387 -21.150  1.00 29.49           O  
HETATM 4380  O   HOH A 328      30.998 -28.091 -36.651  1.00 26.20           O  
HETATM 4381  O   HOH A 329      13.168 -21.201 -26.785  1.00 22.80           O  
HETATM 4382  O   HOH A 330      22.389 -51.170 -38.384  1.00 31.20           O  
HETATM 4383  O   HOH A 331      24.813 -51.171 -34.646  1.00 27.53           O  
HETATM 4384  O   HOH A 332       6.417 -49.652 -39.386  1.00 26.99           O  
HETATM 4385  O   HOH A 333      13.633 -49.843 -17.024  1.00 25.47           O  
HETATM 4386  O   HOH A 334      27.837 -46.570 -22.794  1.00 26.79           O  
HETATM 4387  O   HOH A 335      17.139 -39.063 -35.624  1.00 24.54           O  
HETATM 4388  O   HOH A 336      13.544 -52.321 -25.282  1.00 30.67           O  
HETATM 4389  O   HOH A 337      15.109 -25.856 -32.327  1.00 26.68           O  
HETATM 4390  O   HOH A 338      17.234 -27.253 -33.706  1.00 27.45           O  
HETATM 4391  O   HOH A 339      27.364 -42.324 -37.259  1.00 32.55           O  
HETATM 4392  O   HOH A 340      31.596 -27.680 -33.133  1.00 24.56           O  
HETATM 4393  O   HOH A 341      12.854 -52.270 -20.520  1.00 33.19           O  
HETATM 4394  O   HOH A 342      21.716 -20.426 -20.411  1.00 27.99           O  
HETATM 4395  O   HOH A 343      12.104 -19.479 -22.496  1.00 26.65           O  
HETATM 4396  O   HOH A 344      14.860 -33.843 -31.685  1.00 26.15           O  
HETATM 4397  O   HOH A 345      34.482 -39.314 -30.496  1.00 32.28           O  
HETATM 4398  O   HOH A 346       8.138 -41.156 -23.551  1.00 32.62           O  
HETATM 4399  O   HOH A 347      20.090 -51.109 -40.442  1.00 34.27           O  
HETATM 4400  O   HOH A 348      18.035 -38.480 -38.109  1.00 35.53           O  
HETATM 4401  O   HOH A 349      30.357 -44.747 -31.266  1.00 35.94           O  
HETATM 4402  O   HOH A 350      27.033 -44.226 -39.781  1.00 39.26           O  
HETATM 4403  O   HOH A 351      22.353 -24.669 -32.516  1.00 28.39           O  
HETATM 4404  O   HOH A 352      21.917 -54.483 -36.221  1.00 35.11           O  
HETATM 4405  O   HOH A 353       9.892 -47.423 -16.869  1.00 26.50           O  
HETATM 4406  O   HOH A 354      14.800 -46.970 -43.219  1.00 36.47           O  
HETATM 4407  O   HOH A 355      15.216 -37.474 -17.015  1.00 40.04           O  
HETATM 4408  O   HOH A 356      17.846 -37.913 -16.703  1.00 41.26           O  
HETATM 4409  O   HOH A 357      27.974 -26.664 -17.629  1.00 32.51           O  
HETATM 4410  O   HOH A 358      19.638 -16.613 -19.039  1.00 31.36           O  
HETATM 4411  O   HOH A 359      36.006 -37.460 -32.914  1.00 35.88           O  
HETATM 4412  O   HOH A 360      24.198 -40.662 -16.649  1.00 32.70           O  
HETATM 4413  O   HOH A 361      30.486 -22.179 -26.428  1.00 32.14           O  
HETATM 4414  O   HOH A 362      18.377 -55.878 -30.134  1.00 42.98           O  
HETATM 4415  O   HOH A 363      15.032 -50.707 -20.386  1.00 24.22           O  
HETATM 4416  O   HOH A 364      18.725 -54.777 -25.234  1.00 25.71           O  
HETATM 4417  O   HOH A 365      17.825 -25.359 -35.532  1.00 45.91           O  
HETATM 4418  O   HOH A 366      23.130 -22.428 -18.132  1.00 32.24           O  
HETATM 4419  O   HOH A 367      15.099 -53.801 -26.511  1.00 53.27           O  
HETATM 4420  O   HOH A 368       6.333 -39.881 -25.017  1.00 41.85           O  
HETATM 4421  O   HOH A 369       9.488 -18.847 -19.213  1.00 34.57           O  
HETATM 4422  O   HOH A 370      20.193 -23.799 -19.561  1.00 34.49           O  
HETATM 4423  O   HOH A 371      16.568 -18.162 -30.892  1.00 31.72           O  
HETATM 4424  O   HOH A 372      21.852 -45.087 -43.973  1.00 45.83           O  
HETATM 4425  O   HOH A 373      30.995 -24.217 -27.786  1.00 33.55           O  
HETATM 4426  O   HOH A 374      31.384 -44.069 -28.540  1.00 41.38           O  
HETATM 4427  O   HOH A 375      16.231 -34.609 -34.036  1.00 35.05           O  
HETATM 4428  O   HOH A 376      10.971 -52.023 -22.806  1.00 49.27           O  
HETATM 4429  O   HOH A 377      24.866 -20.004 -19.206  1.00 34.89           O  
HETATM 4430  O   HOH A 378       9.952 -37.710 -17.495  1.00 43.03           O  
HETATM 4431  O   HOH A 379      13.574 -21.927 -17.096  1.00 51.43           O  
HETATM 4432  O   HOH A 380      27.357 -19.205 -21.653  1.00 40.25           O  
HETATM 4433  O   HOH A 381      28.724 -47.158 -32.080  1.00 25.60           O  
HETATM 4434  O   HOH A 382      11.072 -51.458 -26.346  1.00 33.07           O  
HETATM 4435  O   HOH A 383       3.940 -51.838 -34.160  1.00 32.50           O  
HETATM 4436  O   HOH A 384      12.094 -43.794 -39.897  1.00 34.98           O  
HETATM 4437  O   HOH A 385      20.167 -23.872 -34.221  1.00 38.87           O  
HETATM 4438  O   HOH A 386       9.568 -16.721 -18.497  1.00 49.79           O  
HETATM 4439  O   HOH A 387      28.759 -43.370 -34.815  1.00 51.70           O  
HETATM 4440  O   HOH A 388      19.053 -58.335 -31.553  1.00 50.35           O  
HETATM 4441  O   HOH A 389       9.016 -18.716 -21.754  1.00 33.98           O  
HETATM 4442  O   HOH A 390      36.264 -37.575 -28.837  1.00 43.51           O  
HETATM 4443  O   HOH A 391      23.553 -28.984 -12.383  1.00 47.81           O  
HETATM 4444  O   HOH A 392      34.678 -37.145 -26.726  1.00 58.75           O  
HETATM 4445  O   HOH A 393      24.750 -56.137 -32.890  1.00 39.39           O  
HETATM 4446  O   HOH A 394      18.330 -36.398 -39.398  1.00 46.85           O  
HETATM 4447  O   HOH A 395      27.899 -49.008 -34.631  1.00 42.84           O  
HETATM 4448  O   HOH A 396      23.558 -59.149 -22.317  1.00 46.27           O  
HETATM 4449  O   HOH A 397      17.320 -20.976 -17.294  1.00 47.19           O  
HETATM 4450  O   HOH A 398      13.910 -55.191 -28.103  1.00 61.98           O  
HETATM 4451  O   HOH A 399      26.616 -51.262 -36.675  1.00 52.86           O  
HETATM 4452  O   HOH A 400      20.866 -23.004 -17.416  1.00 63.66           O  
HETATM 4453  O   HOH A 401      33.111 -39.717 -19.338  1.00 60.07           O  
HETATM 4454  O   HOH A 402      32.368 -26.622 -31.071  1.00 42.51           O  
HETATM 4455  O   HOH A 403       6.508 -19.001 -22.475  1.00 58.56           O  
HETATM 4456  O   HOH A 404      35.295 -32.131 -40.096  1.00 58.70           O  
HETATM 4457  O   HOH A 405      24.092 -17.524 -20.258  1.00 46.04           O  
HETATM 4458  O   HOH A 406      15.801 -44.589 -16.302  1.00 53.28           O  
HETATM 4459  O   HOH A 407      20.398 -38.060 -40.988  1.00 44.11           O  
HETATM 4460  O   HOH A 408       2.155 -45.819 -34.772  1.00 46.04           O  
HETATM 4461  O   HOH A 409       7.642 -40.432 -15.873  1.00 33.78           O  
HETATM 4462  O   HOH A 410      25.143 -22.645 -16.243  1.00 48.82           O  
HETATM 4463  O   HOH A 411       6.751 -24.217 -22.827  1.00 41.38           O  
HETATM 4464  O   HOH A 412       5.855 -26.738 -23.328  1.00 49.99           O  
HETATM 4465  O   HOH A 413      20.682 -33.662 -36.866  1.00 23.56           O  
HETATM 4466  O   HOH A 414      20.553 -36.250 -37.752  1.00 27.46           O  
HETATM 4467  O   HOH A 415      22.750 -36.831 -39.151  1.00 33.05           O  
HETATM 4468  O   HOH A 416      24.178 -34.263 -39.802  1.00 43.33           O  
HETATM 4469  O   HOH A 417      23.226 -32.192 -38.542  1.00 42.59           O  
HETATM 4470  O   HOH A 418      18.147 -33.689 -39.620  1.00 63.24           O  
HETATM 4471  O   HOH A 419      14.088 -36.600 -36.596  1.00 45.90           O  
HETATM 4472  O   HOH A 420      16.565 -34.501 -36.957  1.00 79.21           O  
HETATM 4473  O   HOH A 421      17.220 -31.149 -35.230  1.00 45.99           O  
HETATM 4474  O   HOH A 422      18.238 -30.129 -37.713  1.00 63.54           O  
HETATM 4475  O   HOH A 423      20.415 -29.775 -38.812  1.00 50.34           O  
HETATM 4476  O   HOH A 424      34.784 -27.873 -37.204  1.00 38.07           O  
HETATM 4477  O   HOH A 425      12.040 -35.598 -33.576  1.00 51.10           O  
HETATM 4478  O   HOH A 426      12.427 -33.419 -32.616  1.00 65.35           O  
HETATM 4479  O   HOH A 427      25.693 -35.969 -38.961  1.00 37.45           O  
HETATM 4480  O   HOH A 428      32.339 -41.864 -24.851  1.00 32.64           O  
HETATM 4481  O   HOH A 429      32.707 -41.421 -27.072  1.00 55.17           O  
HETATM 4482  O   HOH A 430      35.400 -44.051 -25.546  1.00 66.43           O  
HETATM 4483  O   HOH A 431      33.045 -43.344 -31.580  1.00 52.68           O  
HETATM 4484  O   HOH A 432      33.669 -42.143 -21.147  1.00 62.00           O  
HETATM 4485  O   HOH A 433      34.918 -40.432 -17.315  1.00 69.41           O  
HETATM 4486  O   HOH A 434      36.226 -40.849 -19.881  1.00 76.73           O  
HETATM 4487  O   HOH A 435      17.269 -43.557 -45.097  1.00 47.80           O  
HETATM 4488  O   HOH A 436      19.269 -46.684 -42.945  1.00 40.60           O  
HETATM 4489  O   HOH A 437      16.141 -50.194 -43.222  1.00 58.32           O  
HETATM 4490  O   HOH A 438      25.818 -46.542 -42.703  1.00 50.70           O  
HETATM 4491  O   HOH A 439      29.066 -47.687 -36.143  1.00 55.45           O  
HETATM 4492  O   HOH A 440      28.531 -50.012 -38.098  1.00 68.09           O  
HETATM 4493  O   HOH A 441      30.279 -51.431 -37.590  1.00 72.54           O  
HETATM 4494  O   HOH A 442      22.573 -36.951 -41.646  1.00 66.93           O  
HETATM 4495  O   HOH A 443      22.774 -59.444 -31.514  1.00 36.16           O  
HETATM 4496  O   HOH A 444      23.473 -61.292 -29.743  1.00 37.40           O  
HETATM 4497  O   HOH A 445      18.715 -58.717 -29.141  1.00 54.58           O  
HETATM 4498  O   HOH A 446      17.936 -57.517 -22.064  1.00 42.19           O  
HETATM 4499  O   HOH A 447      19.400 -56.985 -26.709  1.00 41.87           O  
HETATM 4500  O   HOH A 448      34.498 -34.102 -36.161  1.00 42.03           O  
HETATM 4501  O   HOH A 449      12.708 -28.150 -11.570  1.00 42.80           O  
HETATM 4502  O   HOH A 450      37.944 -33.860 -26.233  1.00 47.11           O  
HETATM 4503  O   HOH A 451      38.882 -35.117 -28.408  1.00 42.58           O  
HETATM 4504  O   HOH A 452      18.300 -32.380 -37.076  1.00 57.98           O  
HETATM 4505  O   HOH A 453      23.312 -36.893 -22.212  1.00 24.86           O  
HETATM 4506  O   HOH A 454      23.574 -24.398 -36.262  1.00 78.72           O  
HETATM 4507  O   HOH A 455      23.167 -38.943 -42.566  1.00 57.95           O  
HETATM 4508  O   HOH A 456      20.622 -32.578 -13.175  1.00 48.01           O  
HETATM 4509  O   HOH A 457      21.068 -48.698 -41.923  1.00 53.09           O  
HETATM 4510  O   HOH A 458      31.322 -44.348 -24.897  1.00 40.51           O  
HETATM 4511  O   HOH A 459       4.562 -35.405 -28.637  1.00 43.13           O  
HETATM 4512  O   HOH A 460       3.177 -37.154 -27.213  1.00 48.18           O  
HETATM 4513  O   HOH A 461      14.167 -54.690 -19.090  1.00 46.05           O  
HETATM 4514  O   HOH A 462      17.757 -18.263 -17.413  1.00 49.51           O  
HETATM 4515  O   HOH A 463      13.970 -19.095 -17.664  1.00 58.78           O  
HETATM 4516  O   HOH A 464      23.240 -38.484 -17.587  1.00 36.05           O  
HETATM 4517  O   HOH A 465      12.084 -18.579 -19.900  1.00 44.39           O  
HETATM 4518  O   HOH A 466      30.468 -37.709 -37.633  1.00 36.83           O  
HETATM 4519  O   HOH A 467      32.231 -41.303 -29.378  1.00 61.11           O  
HETATM 4520  O   HOH A 468      16.936 -28.917 -35.308  1.00 52.56           O  
HETATM 4521  O   HOH A 469      14.223 -19.563 -34.415  1.00 49.59           O  
HETATM 4522  O   HOH A 470      14.542 -44.302 -42.225  1.00 46.03           O  
HETATM 4523  O   HOH A 471       6.507 -39.047 -28.049  1.00 54.69           O  
HETATM 4524  O   HOH A 472      21.473 -58.512 -28.041  1.00 70.25           O  
HETATM 4525  O   HOH A 473       6.762 -32.347 -15.753  1.00 46.21           O  
HETATM 4526  O   HOH A 474       4.395 -40.859 -13.456  1.00 39.29           O  
HETATM 4527  O   HOH A 475       5.756 -42.637 -13.476  1.00 52.19           O  
HETATM 4528  O   HOH A 476       4.930 -37.738 -13.630  1.00 51.13           O  
HETATM 4529  O   HOH A 477      28.688 -45.095 -25.036  1.00 22.99           O  
HETATM 4530  O   HOH A 478      23.183 -38.857 -20.395  1.00 20.43           O  
HETATM 4531  O   HOH A 479      14.483 -18.876 -26.049  1.00 21.97           O  
HETATM 4532  O   HOH A 480      23.982 -20.262 -27.202  1.00 23.75           O  
HETATM 4533  O   HOH A 481       9.472 -55.960 -35.433  1.00 20.41           O  
HETATM 4534  O   HOH A 482      22.339 -51.657 -35.645  1.00 24.29           O  
HETATM 4535  O   HOH A 483      11.821 -51.194 -29.370  1.00 22.60           O  
HETATM 4536  O   HOH A 484      22.241 -57.093 -30.061  1.00 31.71           O  
HETATM 4537  O   HOH A 485      12.468 -33.188 -29.884  1.00 24.56           O  
HETATM 4538  O   HOH A 486       3.319 -47.006 -32.297  1.00 23.02           O  
HETATM 4539  O   HOH A 487      29.502 -26.681 -38.633  1.00 28.12           O  
HETATM 4540  O   HOH B 301      -7.320 -50.281  -1.393  1.00 20.74           O  
HETATM 4541  O   HOH B 302      -3.214 -56.177  -0.465  1.00 23.01           O  
HETATM 4542  O   HOH B 303      12.242 -58.564  -7.756  1.00 24.83           O  
HETATM 4543  O   HOH B 304       1.270 -46.318  -8.436  1.00 19.85           O  
HETATM 4544  O   HOH B 305       5.040 -58.024 -10.819  1.00 16.03           O  
HETATM 4545  O   HOH B 306       8.364 -66.108  -2.997  1.00 19.50           O  
HETATM 4546  O   HOH B 307      19.007 -57.637  -6.283  1.00 20.38           O  
HETATM 4547  O   HOH B 308       7.478 -57.176  -9.674  1.00 19.06           O  
HETATM 4548  O   HOH B 309      12.961 -45.364  -2.227  1.00 21.03           O  
HETATM 4549  O   HOH B 310       0.094 -44.327  -6.927  1.00 21.03           O  
HETATM 4550  O   HOH B 311      11.129 -60.786   2.772  1.00 21.26           O  
HETATM 4551  O   HOH B 312      -0.523 -62.848  -3.793  1.00 26.32           O  
HETATM 4552  O   HOH B 313      -4.267 -51.686 -10.201  1.00 23.93           O  
HETATM 4553  O   HOH B 314       2.701 -50.708   9.088  1.00 25.36           O  
HETATM 4554  O   HOH B 315      -5.189 -52.348  -7.193  1.00 28.13           O  
HETATM 4555  O   HOH B 316      11.470 -66.150  -4.749  1.00 23.56           O  
HETATM 4556  O   HOH B 317       7.019 -50.165 -12.374  1.00 26.92           O  
HETATM 4557  O   HOH B 318      17.910 -63.452   1.087  1.00 27.95           O  
HETATM 4558  O   HOH B 319       9.414 -36.570   5.710  1.00 30.02           O  
HETATM 4559  O   HOH B 320      -5.851 -43.785   7.981  1.00 27.39           O  
HETATM 4560  O   HOH B 321      -0.016 -44.007  -4.300  1.00 30.25           O  
HETATM 4561  O   HOH B 322       6.488 -53.690   4.765  1.00 26.85           O  
HETATM 4562  O   HOH B 323       5.553 -54.746   7.152  1.00 37.69           O  
HETATM 4563  O   HOH B 324       9.960 -50.055 -16.489  1.00 26.97           O  
HETATM 4564  O   HOH B 325      10.324 -57.187 -11.702  1.00 31.91           O  
HETATM 4565  O   HOH B 326      11.793 -46.017 -15.291  1.00 27.31           O  
HETATM 4566  O   HOH B 327       7.616 -41.581  10.758  1.00 38.20           O  
HETATM 4567  O   HOH B 328      -3.845 -61.252  -2.845  1.00 33.06           O  
HETATM 4568  O   HOH B 329     -13.637 -34.835   0.625  1.00 36.19           O  
HETATM 4569  O   HOH B 330       1.911 -63.683  -3.826  1.00 26.62           O  
HETATM 4570  O   HOH B 331       2.989 -53.211   8.187  1.00 33.58           O  
HETATM 4571  O   HOH B 332       4.487 -66.736  -5.308  1.00 28.16           O  
HETATM 4572  O   HOH B 333      -6.685 -55.534   6.783  1.00 34.29           O  
HETATM 4573  O   HOH B 334      -3.538 -38.477  11.012  1.00 35.71           O  
HETATM 4574  O   HOH B 335     -12.726 -49.654   0.288  1.00 38.00           O  
HETATM 4575  O   HOH B 336      -5.509 -41.327   9.302  1.00 35.14           O  
HETATM 4576  O   HOH B 337      -3.698 -57.595   3.701  1.00 34.78           O  
HETATM 4577  O   HOH B 338      -8.151 -44.934  10.852  1.00 44.11           O  
HETATM 4578  O   HOH B 339      -5.984 -37.743  -5.769  1.00 33.86           O  
HETATM 4579  O   HOH B 340       8.323 -47.078   5.235  1.00 32.51           O  
HETATM 4580  O   HOH B 341       8.801 -52.799 -14.391  1.00 29.91           O  
HETATM 4581  O   HOH B 342     -11.591 -45.229   0.041  1.00 35.50           O  
HETATM 4582  O   HOH B 343      -7.943 -39.640   7.987  1.00 35.68           O  
HETATM 4583  O   HOH B 344       0.304 -40.977  11.473  1.00 42.80           O  
HETATM 4584  O   HOH B 345      15.475 -42.176 -11.426  1.00 34.45           O  
HETATM 4585  O   HOH B 346      -0.673 -37.323  12.088  1.00 38.34           O  
HETATM 4586  O   HOH B 347       5.557 -43.353  11.133  1.00 35.98           O  
HETATM 4587  O   HOH B 348      -0.599 -65.132   5.792  1.00 37.52           O  
HETATM 4588  O   HOH B 349     -11.211 -51.172   8.172  1.00 37.25           O  
HETATM 4589  O   HOH B 350       1.072 -54.752   8.721  1.00 34.07           O  
HETATM 4590  O   HOH B 351      10.950 -54.080 -15.107  1.00 36.80           O  
HETATM 4591  O   HOH B 352      -6.441 -56.241  -2.331  1.00 35.64           O  
HETATM 4592  O   HOH B 353      14.833 -37.882 -14.642  1.00 39.49           O  
HETATM 4593  O   HOH B 354      -5.614 -37.140  10.959  1.00 55.24           O  
HETATM 4594  O   HOH B 355      15.462 -47.206  -5.730  1.00 32.69           O  
HETATM 4595  O   HOH B 356     -10.979 -51.622   0.362  1.00 38.06           O  
HETATM 4596  O   HOH B 357       5.905 -47.055   9.322  1.00 49.65           O  
HETATM 4597  O   HOH B 358      -8.555 -54.772   8.400  1.00 42.74           O  
HETATM 4598  O   HOH B 359      13.952 -42.802 -13.795  1.00 39.54           O  
HETATM 4599  O   HOH B 360      10.354 -44.820 -13.720  1.00 47.87           O  
HETATM 4600  O   HOH B 361      -6.279 -55.758   3.849  1.00 46.67           O  
HETATM 4601  O   HOH B 362       9.278 -59.214 -11.468  1.00 45.29           O  
HETATM 4602  O   HOH B 363      -4.791 -58.453  -3.233  1.00 26.09           O  
HETATM 4603  O   HOH B 364      -7.866 -46.923 -11.683  1.00 38.75           O  
HETATM 4604  O   HOH B 365       7.334 -49.341   6.235  1.00 44.50           O  
HETATM 4605  O   HOH B 366       2.156 -35.056  -7.976  1.00 45.64           O  
HETATM 4606  O   HOH B 367       0.738 -29.922   4.533  1.00 34.35           O  
HETATM 4607  O   HOH B 368       2.021 -63.765   7.783  1.00 43.49           O  
HETATM 4608  O   HOH B 369     -14.741 -46.160   0.700  1.00 49.80           O  
HETATM 4609  O   HOH B 370      -7.532 -56.548   0.048  1.00 51.73           O  
HETATM 4610  O   HOH B 371     -12.377 -51.835   3.263  1.00 37.84           O  
HETATM 4611  O   HOH B 372       0.399 -50.488  11.227  1.00 44.21           O  
HETATM 4612  O   HOH B 373      14.510 -65.890  -5.866  1.00 48.43           O  
HETATM 4613  O   HOH B 374      -6.179 -54.738 -10.038  1.00 47.72           O  
HETATM 4614  O   HOH B 375     -10.635 -47.402  -1.133  1.00 49.81           O  
HETATM 4615  O   HOH B 376      17.393 -65.615   2.444  1.00 41.01           O  
HETATM 4616  O   HOH B 377      -4.892 -57.357   1.370  1.00 54.62           O  
HETATM 4617  O   HOH B 378      13.190 -37.444 -16.051  1.00 55.31           O  
HETATM 4618  O   HOH B 379      21.572 -57.675   0.262  1.00 41.19           O  
HETATM 4619  O   HOH B 380      -0.819 -53.138  11.031  1.00 45.18           O  
HETATM 4620  O   HOH B 381      -1.023 -59.306 -18.365  1.00 38.52           O  
HETATM 4621  O   HOH B 382       9.316 -33.362   7.216  1.00 34.41           O  
HETATM 4622  O   HOH B 383      12.889 -56.636 -10.229  1.00 42.41           O  
HETATM 4623  O   HOH B 384      -3.660 -34.111  10.352  1.00 44.77           O  
HETATM 4624  O   HOH B 385      -6.901 -56.590  -9.031  1.00 56.57           O  
HETATM 4625  O   HOH B 386       5.521 -23.079   0.494  1.00 61.38           O  
HETATM 4626  O   HOH B 387      12.852 -55.291 -13.234  1.00 42.44           O  
HETATM 4627  O   HOH B 388      14.448 -39.825 -12.353  1.00 46.93           O  
HETATM 4628  O   HOH B 389      -9.142 -33.699   7.605  1.00 49.30           O  
HETATM 4629  O   HOH B 390      13.201 -40.831  -8.596  1.00 42.81           O  
HETATM 4630  O   HOH B 391      22.894 -42.191  -9.732  1.00 42.18           O  
HETATM 4631  O   HOH B 392      -2.164 -54.298   9.201  1.00 47.76           O  
HETATM 4632  O   HOH B 393      18.636 -45.801   1.775  1.00 46.34           O  
HETATM 4633  O   HOH B 394      15.003 -55.544 -14.379  1.00 47.42           O  
HETATM 4634  O   HOH B 395      27.352 -34.597 -15.501  1.00 41.08           O  
HETATM 4635  O   HOH B 396     -11.515 -46.219 -10.839  1.00 56.72           O  
HETATM 4636  O   HOH B 397      -8.819 -49.903  -5.570  1.00 31.41           O  
HETATM 4637  O   HOH B 398     -11.664 -51.856  -2.553  1.00 61.83           O  
HETATM 4638  O   HOH B 399      -7.719 -53.494  -4.345  1.00 44.03           O  
HETATM 4639  O   HOH B 400       7.957 -40.914  -8.354  1.00 38.80           O  
HETATM 4640  O   HOH B 401       8.370 -39.692 -10.742  1.00 46.91           O  
HETATM 4641  O   HOH B 402      -0.255 -42.327  -8.836  1.00 38.08           O  
HETATM 4642  O   HOH B 403      -1.270 -30.127   1.486  1.00 39.86           O  
HETATM 4643  O   HOH B 404       0.765 -28.918   6.498  1.00 60.59           O  
HETATM 4644  O   HOH B 405       2.747 -32.057   2.103  1.00 49.88           O  
HETATM 4645  O   HOH B 406       4.933 -31.082   2.206  1.00 44.95           O  
HETATM 4646  O   HOH B 407      -1.204 -34.659   9.863  1.00 34.11           O  
HETATM 4647  O   HOH B 408      -4.198 -31.831  11.986  1.00 56.82           O  
HETATM 4648  O   HOH B 409      16.127 -33.949   4.319  1.00 82.99           O  
HETATM 4649  O   HOH B 410      10.720 -45.167   4.224  1.00 32.69           O  
HETATM 4650  O   HOH B 411       9.182 -40.997  12.907  1.00 56.52           O  
HETATM 4651  O   HOH B 412       7.129 -41.808  14.694  1.00 52.13           O  
HETATM 4652  O   HOH B 413      -5.484 -49.261  12.168  1.00 55.31           O  
HETATM 4653  O   HOH B 414     -17.678 -39.351   5.187  1.00 68.66           O  
HETATM 4654  O   HOH B 415       0.218 -39.201  12.810  1.00 76.43           O  
HETATM 4655  O   HOH B 416      -2.708 -40.266  12.862  1.00 61.88           O  
HETATM 4656  O   HOH B 417      -6.890 -40.230  -5.293  1.00 36.84           O  
HETATM 4657  O   HOH B 418      -0.799 -43.389 -11.274  1.00 36.55           O  
HETATM 4658  O   HOH B 419      -2.972 -41.986 -11.497  1.00 41.16           O  
HETATM 4659  O   HOH B 420      -3.787 -56.073   9.874  1.00 48.92           O  
HETATM 4660  O   HOH B 421       3.326 -56.760   9.469  1.00 46.90           O  
HETATM 4661  O   HOH B 422       0.953 -57.116  10.434  1.00 53.47           O  
HETATM 4662  O   HOH B 423       8.546 -56.120   6.643  1.00 46.69           O  
HETATM 4663  O   HOH B 424      -1.057 -32.368  -8.395  1.00 50.75           O  
HETATM 4664  O   HOH B 425      -0.599 -61.808 -19.519  1.00 40.60           O  
HETATM 4665  O   HOH B 426       9.241 -64.439   5.464  1.00 43.20           O  
HETATM 4666  O   HOH B 427       4.809 -62.821 -11.347  1.00 46.13           O  
HETATM 4667  O   HOH B 428     -10.998 -39.742  -8.712  1.00 46.38           O  
HETATM 4668  O   HOH B 429      -9.204 -51.004  -2.961  1.00 60.65           O  
HETATM 4669  O   HOH B 430      -8.868 -50.798  -9.850  1.00 52.88           O  
HETATM 4670  O   HOH B 431      -7.759 -51.714  -6.965  1.00 38.02           O  
HETATM 4671  O   HOH B 432      -2.559 -62.662   4.096  1.00 36.98           O  
HETATM 4672  O   HOH B 433      -4.508 -57.560   7.408  1.00 43.87           O  
HETATM 4673  O   HOH B 434       8.493 -28.993  -4.522  1.00 51.26           O  
HETATM 4674  O   HOH B 435      14.098 -65.660  -8.191  1.00 53.65           O  
HETATM 4675  O   HOH B 436       6.204 -63.700  -9.764  1.00 50.84           O  
HETATM 4676  O   HOH B 437       2.725 -63.783 -11.229  1.00 38.29           O  
HETATM 4677  O   HOH B 438       1.682 -64.781  -1.269  1.00 46.03           O  
HETATM 4678  O   HOH B 439       7.656 -45.928 -13.202  1.00 37.41           O  
HETATM 4679  O   HOH B 440      20.191 -64.030  -0.591  1.00 42.05           O  
HETATM 4680  O   HOH B 441      -6.567 -52.033  -8.922  1.00 47.32           O  
HETATM 4681  O   HOH B 442      -1.355 -37.421  -9.495  1.00 51.56           O  
HETATM 4682  O   HOH B 443      23.683 -41.955 -12.247  1.00 48.45           O  
HETATM 4683  O   HOH B 444      24.319 -39.690 -13.843  1.00 49.09           O  
HETATM 4684  O   HOH B 445       9.303 -42.614 -14.275  1.00 38.78           O  
HETATM 4685  O   HOH B 446       5.396 -40.918  -8.798  1.00 42.97           O  
HETATM 4686  O   HOH B 447      20.195 -34.840 -12.693  1.00 66.06           O  
HETATM 4687  O   HOH B 448      -2.573 -29.005   3.827  1.00 37.10           O  
HETATM 4688  O   HOH B 449      10.448 -63.198  -8.980  1.00 40.99           O  
HETATM 4689  O   HOH B 450       9.657 -55.040 -17.819  1.00 46.06           O  
HETATM 4690  O   HOH B 451     -16.265 -48.965   8.003  1.00 51.05           O  
HETATM 4691  O   HOH B 452     -12.994 -51.218  10.348  1.00 59.05           O  
HETATM 4692  O   HOH B 453     -12.733 -49.002  11.824  1.00 56.40           O  
HETATM 4693  O   HOH B 454      13.269 -38.067  -9.673  1.00 40.28           O  
HETATM 4694  O   HOH B 455      16.873 -38.596 -11.213  1.00 34.80           O  
HETATM 4695  O   HOH B 456      -0.442 -30.963  -5.801  1.00 27.55           O  
HETATM 4696  O   HOH B 457      15.151 -36.250  -8.424  1.00 44.07           O  
HETATM 4697  O   HOH B 458       9.927 -40.452 -12.984  1.00 64.12           O  
HETATM 4698  O   HOH B 459       4.958 -31.312   9.431  1.00 31.76           O  
HETATM 4699  O   HOH B 460       6.584 -32.205  12.801  1.00 39.39           O  
HETATM 4700  O   HOH B 461      23.272 -57.578   5.612  1.00 70.58           O  
HETATM 4701  O   HOH B 462       9.924 -59.140  -6.442  1.00 22.94           O  
HETATM 4702  O   HOH B 463       8.043 -51.487   5.091  1.00 24.99           O  
HETATM 4703  O   HOH B 464       0.128 -33.017   3.988  1.00 24.11           O  
HETATM 4704  O   HOH B 465      13.606 -48.037 -14.944  1.00 23.25           O  
HETATM 4705  O   HOH B 466      20.768 -56.763  -2.399  1.00 23.97           O  
HETATM 4706  O   HOH B 467      -5.193 -36.144  -3.633  1.00 22.30           O  
HETATM 4707  O   HOH B 468      15.922 -35.462  -6.145  1.00 45.32           O  
HETATM 4708  O   HOH C 301      -4.902 -55.416 -12.730  1.00 23.03           O  
HETATM 4709  O   HOH C 302      -4.094 -57.597 -23.655  1.00 22.42           O  
HETATM 4710  O   HOH C 303       5.998 -57.554 -25.240  1.00 23.15           O  
HETATM 4711  O   HOH C 304     -11.590 -55.937 -16.665  1.00 23.78           O  
HETATM 4712  O   HOH C 305       4.414 -50.734 -22.964  1.00 17.93           O  
HETATM 4713  O   HOH C 306       4.347 -51.175 -12.319  1.00 18.01           O  
HETATM 4714  O   HOH C 307      -1.429 -59.176 -28.872  1.00 19.94           O  
HETATM 4715  O   HOH C 308       0.280 -57.652 -31.797  1.00 21.14           O  
HETATM 4716  O   HOH C 309      -4.403 -57.340 -18.726  1.00 20.87           O  
HETATM 4717  O   HOH C 310       5.321 -59.220 -13.402  1.00 24.17           O  
HETATM 4718  O   HOH C 311       3.244 -49.911 -32.115  1.00 22.01           O  
HETATM 4719  O   HOH C 312      -0.300 -39.659 -20.456  1.00 30.86           O  
HETATM 4720  O   HOH C 313      -5.735 -63.264 -25.290  1.00 24.30           O  
HETATM 4721  O   HOH C 314       0.470 -56.353 -15.622  1.00 22.19           O  
HETATM 4722  O   HOH C 315     -13.377 -55.387 -23.409  1.00 27.49           O  
HETATM 4723  O   HOH C 316       6.277 -49.258 -14.902  1.00 22.01           O  
HETATM 4724  O   HOH C 317       5.079 -54.230 -21.503  1.00 25.91           O  
HETATM 4725  O   HOH C 318       7.315 -46.966 -16.096  1.00 28.36           O  
HETATM 4726  O   HOH C 319       8.467 -53.434 -19.378  1.00 34.13           O  
HETATM 4727  O   HOH C 320       2.234 -43.042 -26.465  1.00 27.40           O  
HETATM 4728  O   HOH C 321      -2.342 -57.595 -33.032  1.00 31.09           O  
HETATM 4729  O   HOH C 322      11.805 -53.655 -28.439  1.00 33.68           O  
HETATM 4730  O   HOH C 323       7.608 -27.336 -25.891  1.00 33.19           O  
HETATM 4731  O   HOH C 324      -1.527 -43.967 -35.941  1.00 34.73           O  
HETATM 4732  O   HOH C 325      -9.816 -58.569 -14.134  1.00 38.70           O  
HETATM 4733  O   HOH C 326      -0.519 -29.813 -33.691  1.00 35.11           O  
HETATM 4734  O   HOH C 327       6.493 -53.742 -23.814  1.00 32.55           O  
HETATM 4735  O   HOH C 328      -5.657 -61.858 -22.348  1.00 29.42           O  
HETATM 4736  O   HOH C 329      -7.134 -53.744 -35.259  1.00 36.23           O  
HETATM 4737  O   HOH C 330       2.380 -56.494 -13.751  1.00 30.44           O  
HETATM 4738  O   HOH C 331       4.542 -41.449 -26.599  1.00 41.76           O  
HETATM 4739  O   HOH C 332       2.233 -60.441 -27.094  1.00 26.53           O  
HETATM 4740  O   HOH C 333      -0.482 -39.613 -31.357  1.00 31.63           O  
HETATM 4741  O   HOH C 334      -2.156 -41.381 -36.533  1.00 47.66           O  
HETATM 4742  O   HOH C 335      -9.342 -51.147 -12.719  1.00 39.42           O  
HETATM 4743  O   HOH C 336      -3.095 -61.003 -30.129  1.00 30.76           O  
HETATM 4744  O   HOH C 337     -11.183 -37.428 -18.739  1.00 39.46           O  
HETATM 4745  O   HOH C 338      -5.612 -59.278 -20.694  1.00 31.62           O  
HETATM 4746  O   HOH C 339       0.464 -42.212 -31.445  1.00 33.85           O  
HETATM 4747  O   HOH C 340       6.114 -59.403 -17.538  1.00 37.21           O  
HETATM 4748  O   HOH C 341       6.556 -56.938 -18.385  1.00 36.84           O  
HETATM 4749  O   HOH C 342      -7.705 -60.879 -31.766  1.00 41.09           O  
HETATM 4750  O   HOH C 343      -7.947 -61.386 -20.617  1.00 30.89           O  
HETATM 4751  O   HOH C 344     -17.833 -41.214 -31.059  1.00 56.60           O  
HETATM 4752  O   HOH C 345      -3.778 -59.764 -18.359  1.00 40.38           O  
HETATM 4753  O   HOH C 346      -8.735 -56.970 -11.643  1.00 71.70           O  
HETATM 4754  O   HOH C 347      -5.452 -55.874 -34.673  1.00 39.93           O  
HETATM 4755  O   HOH C 348       3.001 -39.385 -28.353  1.00 41.44           O  
HETATM 4756  O   HOH C 349      -3.793 -61.517 -19.977  1.00 47.08           O  
HETATM 4757  O   HOH C 350      -1.647 -38.416 -33.298  1.00 35.56           O  
HETATM 4758  O   HOH C 351       6.202 -23.417 -28.300  1.00 37.98           O  
HETATM 4759  O   HOH C 352      -0.757 -56.113 -34.484  1.00 36.44           O  
HETATM 4760  O   HOH C 353       8.709 -52.709 -21.750  1.00 42.61           O  
HETATM 4761  O   HOH C 354       6.793 -55.894 -20.640  1.00 54.53           O  
HETATM 4762  O   HOH C 355      -0.182 -51.655 -37.933  1.00 46.12           O  
HETATM 4763  O   HOH C 356      -3.290 -62.829 -16.544  1.00 87.08           O  
HETATM 4764  O   HOH C 357       0.263 -54.239 -32.817  1.00 34.18           O  
HETATM 4765  O   HOH C 358      -6.006 -60.612 -16.570  1.00 47.42           O  
HETATM 4766  O   HOH C 359       4.298 -51.391 -38.869  1.00 39.04           O  
HETATM 4767  O   HOH C 360     -14.355 -35.946 -21.325  1.00 49.38           O  
HETATM 4768  O   HOH C 361       7.110 -25.762 -27.688  1.00 52.09           O  
HETATM 4769  O   HOH C 362       3.036 -36.118 -21.636  1.00 56.40           O  
HETATM 4770  O   HOH C 363     -10.146 -44.144 -17.121  1.00 43.27           O  
HETATM 4771  O   HOH C 364     -12.174 -53.095 -15.284  1.00 51.69           O  
HETATM 4772  O   HOH C 365      -0.793 -58.468 -16.250  1.00 61.26           O  
HETATM 4773  O   HOH C 366       3.027 -51.188 -36.903  1.00 44.52           O  
HETATM 4774  O   HOH C 367      -1.246 -46.093 -38.544  1.00 56.16           O  
HETATM 4775  O   HOH C 368     -12.925 -44.362 -23.003  1.00 35.90           O  
HETATM 4776  O   HOH C 369      -5.768 -22.708 -31.063  1.00 46.75           O  
HETATM 4777  O   HOH C 370       2.510 -53.349 -33.419  1.00 53.82           O  
HETATM 4778  O   HOH C 371      -0.587 -41.679 -15.372  1.00 48.54           O  
HETATM 4779  O   HOH C 372     -14.691 -49.745 -17.365  1.00 59.66           O  
HETATM 4780  O   HOH C 373     -15.358 -49.569 -19.532  1.00 62.21           O  
HETATM 4781  O   HOH C 374     -11.841 -29.359 -35.012  1.00 50.83           O  
HETATM 4782  O   HOH C 375       4.224 -58.337 -15.838  1.00 24.08           O  
HETATM 4783  O   HOH C 376       3.336 -26.789 -22.831  1.00 37.99           O  
HETATM 4784  O   HOH C 377       1.980 -21.716 -27.151  1.00 37.69           O  
HETATM 4785  O   HOH C 378      -8.376 -43.342 -14.496  1.00 53.28           O  
HETATM 4786  O   HOH C 379      12.125 -55.245 -24.215  1.00 42.55           O  
HETATM 4787  O   HOH C 380       1.111 -42.804 -14.159  1.00 47.17           O  
HETATM 4788  O   HOH C 381       4.291 -37.107 -35.495  1.00 47.66           O  
HETATM 4789  O   HOH C 382      10.275 -29.691 -34.849  1.00 43.28           O  
HETATM 4790  O   HOH C 383       2.990 -22.100 -24.519  1.00 50.12           O  
HETATM 4791  O   HOH C 384       2.204 -24.115 -22.978  1.00 53.09           O  
HETATM 4792  O   HOH C 385       0.125 -25.238 -23.072  1.00 44.36           O  
HETATM 4793  O   HOH C 386      -5.945 -27.000 -24.469  1.00 43.74           O  
HETATM 4794  O   HOH C 387      -8.174 -35.561 -17.478  1.00 48.55           O  
HETATM 4795  O   HOH C 388     -11.297 -34.950 -19.245  1.00 53.31           O  
HETATM 4796  O   HOH C 389      -3.425 -62.772 -13.226  1.00 43.35           O  
HETATM 4797  O   HOH C 390      -2.190 -50.375 -38.161  1.00 54.68           O  
HETATM 4798  O   HOH C 391     -15.525 -45.589 -33.554  1.00 41.59           O  
HETATM 4799  O   HOH C 392      -7.077 -24.281 -33.550  1.00 48.76           O  
HETATM 4800  O   HOH C 393       7.875 -60.899 -17.355  1.00 59.72           O  
HETATM 4801  O   HOH C 394     -13.131 -22.311 -30.901  1.00 56.35           O  
HETATM 4802  O   HOH C 395     -10.616 -65.240 -23.293  1.00 51.43           O  
HETATM 4803  O   HOH C 396      -2.285 -57.163 -21.661  1.00 30.72           O  
HETATM 4804  O   HOH C 397     -16.669 -48.864 -40.222  1.00 55.21           O  
HETATM 4805  O   HOH C 398     -17.206 -61.625 -36.677  1.00 55.76           O  
HETATM 4806  O   HOH C 399     -11.472 -43.056 -40.864  1.00 47.50           O  
HETATM 4807  O   HOH C 400       0.724 -20.580 -33.993  1.00 38.45           O  
HETATM 4808  O   HOH C 401       0.535 -18.848 -32.218  1.00 27.37           O  
HETATM 4809  O   HOH C 402     -15.772 -36.754 -36.185  1.00 61.37           O  
HETATM 4810  O   HOH C 403      -7.083 -28.346 -26.710  1.00 40.56           O  
HETATM 4811  O   HOH C 404      -5.653 -21.777 -35.752  1.00 55.19           O  
HETATM 4812  O   HOH C 405       6.408 -47.896 -11.209  1.00 21.55           O  
HETATM 4813  O   HOH C 406      -1.173 -56.618 -19.367  1.00 19.71           O  
HETATM 4814  O   HOH C 407     -10.674 -48.537 -31.396  1.00 29.14           O  
HETATM 4815  O   HOH C 408       7.535 -51.342 -16.244  1.00 25.85           O  
HETATM 4816  O   HOH C 409     -11.977 -58.092 -23.480  1.00 24.50           O  
HETATM 4817  O   HOH C 410      -2.636 -59.897 -22.055  1.00 25.26           O  
HETATM 4818  O   HOH C 411       0.781 -42.922 -28.780  1.00 26.97           O  
HETATM 4819  O   HOH C 412       0.370 -45.848 -11.006  1.00 23.17           O  
HETATM 4820  O   HOH C 413       3.664 -58.836 -24.638  1.00 29.20           O  
HETATM 4821  O   HOH C 414       2.626 -43.283 -10.625  1.00 36.00           O  
HETATM 4822  O   HOH D 301      16.225 -50.654 -17.967  1.00 20.26           O  
HETATM 4823  O   HOH D 302      19.602 -54.018 -12.498  1.00 18.26           O  
HETATM 4824  O   HOH D 303      19.309 -48.070 -20.822  1.00 17.82           O  
HETATM 4825  O   HOH D 304      28.496 -51.216 -23.187  1.00 21.66           O  
HETATM 4826  O   HOH D 305      25.190 -56.462 -18.620  1.00 19.32           O  
HETATM 4827  O   HOH D 306      17.282 -48.108 -17.534  1.00 18.07           O  
HETATM 4828  O   HOH D 307      20.863 -58.708  -4.587  1.00 22.25           O  
HETATM 4829  O   HOH D 308      20.314 -61.302 -16.110  1.00 29.11           O  
HETATM 4830  O   HOH D 309      16.221 -46.951 -15.203  1.00 27.94           O  
HETATM 4831  O   HOH D 310      17.400 -57.092 -13.367  1.00 23.74           O  
HETATM 4832  O   HOH D 311      27.939 -59.638 -15.959  1.00 28.20           O  
HETATM 4833  O   HOH D 312      22.692 -51.520  -2.796  1.00 38.02           O  
HETATM 4834  O   HOH D 313      28.533 -56.303 -19.567  1.00 28.52           O  
HETATM 4835  O   HOH D 314      21.467 -50.118  -4.844  1.00 32.43           O  
HETATM 4836  O   HOH D 315      23.689 -64.940  -9.664  1.00 40.79           O  
HETATM 4837  O   HOH D 316      20.678 -61.456  -4.568  1.00 35.32           O  
HETATM 4838  O   HOH D 317      29.417 -59.149 -19.505  1.00 46.26           O  
HETATM 4839  O   HOH D 318      12.434 -59.613 -10.111  1.00 48.26           O  
HETATM 4840  O   HOH D 319      26.473 -60.683 -18.636  1.00 32.96           O  
HETATM 4841  O   HOH D 320      17.330 -63.655  -7.637  1.00 38.49           O  
HETATM 4842  O   HOH D 321      32.373 -47.498 -20.740  1.00 39.32           O  
HETATM 4843  O   HOH D 322      22.404 -42.508 -14.490  1.00 39.58           O  
HETATM 4844  O   HOH D 323      30.113 -64.688  -5.828  1.00 42.87           O  
HETATM 4845  O   HOH D 324      25.402 -56.241   2.206  1.00 37.89           O  
HETATM 4846  O   HOH D 325      23.314 -52.118   0.021  1.00 60.98           O  
HETATM 4847  O   HOH D 326      14.692 -38.247   5.413  1.00 34.63           O  
HETATM 4848  O   HOH D 327      23.905 -50.146   1.367  1.00 37.02           O  
HETATM 4849  O   HOH D 328      17.316 -47.223  -3.965  1.00 46.53           O  
HETATM 4850  O   HOH D 329      21.864 -62.959  -2.863  1.00 49.63           O  
HETATM 4851  O   HOH D 330      31.391 -43.574 -18.613  1.00 40.13           O  
HETATM 4852  O   HOH D 331      26.988 -65.478  -8.575  1.00 48.57           O  
HETATM 4853  O   HOH D 332      24.218 -63.068  -6.572  1.00 40.11           O  
HETATM 4854  O   HOH D 333      16.888 -64.970 -12.360  1.00 55.06           O  
HETATM 4855  O   HOH D 334      11.794 -51.568 -17.382  1.00 43.74           O  
HETATM 4856  O   HOH D 335      12.086 -58.007 -14.160  1.00 48.25           O  
HETATM 4857  O   HOH D 336      24.832 -57.520 -21.242  1.00 37.91           O  
HETATM 4858  O   HOH D 337      14.713 -62.888 -10.143  1.00 49.28           O  
HETATM 4859  O   HOH D 338      21.406 -52.861 -23.013  1.00 39.94           O  
HETATM 4860  O   HOH D 339      23.301 -43.988  -7.123  1.00 44.51           O  
HETATM 4861  O   HOH D 340      17.682 -56.524 -19.828  1.00 31.00           O  
HETATM 4862  O   HOH D 341      17.418 -57.386 -17.356  1.00 33.67           O  
HETATM 4863  O   HOH D 342      18.866 -55.961 -15.548  1.00 20.11           O  
HETATM 4864  O   HOH D 343      15.509 -54.404 -16.550  1.00 27.52           O  
HETATM 4865  O   HOH D 344      20.638 -48.934  -0.898  1.00 41.84           O  
HETATM 4866  O   HOH D 345      36.538 -47.707  -8.139  1.00 38.19           O  
HETATM 4867  O   HOH D 346      31.447 -63.298  -4.052  1.00 48.68           O  
HETATM 4868  O   HOH D 347      34.362 -46.696 -18.906  1.00 55.36           O  
HETATM 4869  O   HOH D 348      27.501 -57.266 -17.368  1.00 31.68           O  
HETATM 4870  O   HOH D 349      23.917 -43.477   9.032  1.00 38.52           O  
HETATM 4871  O   HOH D 350      20.948 -64.119 -16.023  1.00 60.74           O  
HETATM 4872  O   HOH D 351      22.976 -64.854 -13.845  1.00 50.08           O  
HETATM 4873  O   HOH D 352      19.084 -49.511  -4.121  1.00 45.61           O  
HETATM 4874  O   HOH D 353      26.073 -54.768   4.267  1.00 45.03           O  
HETATM 4875  O   HOH D 354      14.731 -57.708 -16.503  1.00 52.14           O  
HETATM 4876  O   HOH D 355      34.621 -56.229  -4.142  1.00 32.79           O  
HETATM 4877  O   HOH D 356      30.024 -38.972  12.340  1.00 48.76           O  
HETATM 4878  O   HOH D 357      34.963 -43.215  10.246  1.00 53.29           O  
HETATM 4879  O   HOH D 358      27.227 -65.591  -4.188  1.00 71.84           O  
HETATM 4880  O   HOH D 359      17.287 -60.455 -15.117  1.00 64.05           O  
HETATM 4881  O   HOH D 360      39.011 -54.660  -0.658  1.00 59.71           O  
HETATM 4882  O   HOH D 361      33.856 -44.587  12.135  1.00 64.38           O  
HETATM 4883  O   HOH D 362      39.906 -55.453 -13.873  1.00 53.74           O  
HETATM 4884  O   HOH D 363      30.381 -54.582  12.684  1.00 63.14           O  
HETATM 4885  O   HOH D 364      44.161 -46.659   3.069  1.00 48.70           O  
HETATM 4886  O   HOH D 365      31.857 -45.471 -19.914  1.00 59.70           O  
HETATM 4887  O   HOH D 366      28.711 -55.751 -28.604  1.00 45.42           O  
HETATM 4888  O   HOH D 367      19.285 -44.717   3.911  1.00 63.92           O  
HETATM 4889  O   HOH D 368      29.299 -62.677 -19.451  1.00 61.76           O  
HETATM 4890  O   HOH D 369      28.364 -56.857  12.545  1.00 57.91           O  
HETATM 4891  O   HOH D 370      30.426 -48.424 -24.188  1.00 56.94           O  
HETATM 4892  O   HOH D 371      28.472 -36.106  11.375  1.00 49.46           O  
HETATM 4893  O   HOH D 372      28.861 -35.372   2.857  1.00 66.52           O  
HETATM 4894  O   HOH D 373      42.519 -46.747  -1.312  1.00 46.84           O  
HETATM 4895  O   HOH D 374      13.412 -53.506 -17.156  1.00 73.21           O  
HETATM 4896  O   HOH D 375      29.992 -57.526 -23.687  1.00 47.47           O  
HETATM 4897  O   HOH D 376      37.317 -57.062 -14.695  1.00 40.93           O  
HETATM 4898  O   HOH D 377      36.192 -58.983 -16.203  1.00 33.71           O  
HETATM 4899  O   HOH D 378      23.047 -42.648 -18.374  1.00 20.84           O  
HETATM 4900  O   HOH D 379      19.775 -55.624 -22.621  1.00 23.54           O  
HETATM 4901  O   HOH D 380      23.246 -53.968 -21.530  1.00 21.44           O  
HETATM 4902  O   HOH E 101      30.664 -37.384 -20.300  1.00 27.09           O  
HETATM 4903  O   HOH E 102      33.387 -26.106 -28.446  1.00 36.35           O  
HETATM 4904  O   HOH E 103      35.401 -29.635 -21.399  1.00 28.30           O  
HETATM 4905  O   HOH E 104      34.629 -33.959 -23.549  1.00 31.50           O  
HETATM 4906  O   HOH E 105      28.800 -32.514 -16.814  1.00 32.18           O  
HETATM 4907  O   HOH E 106      29.931 -34.147 -18.827  1.00 31.83           O  
HETATM 4908  O   HOH E 107      30.510 -27.498 -17.047  1.00 39.03           O  
HETATM 4909  O   HOH E 108      34.959 -34.414 -26.233  1.00 33.95           O  
HETATM 4910  O   HOH E 109      36.124 -32.244 -21.780  1.00 34.09           O  
HETATM 4911  O   HOH E 110      33.611 -34.457 -19.363  1.00 38.04           O  
HETATM 4912  O   HOH E 111      36.090 -33.557 -19.570  1.00 48.19           O  
HETATM 4913  O   HOH E 112      33.376 -39.331  -7.818  1.00 41.09           O  
HETATM 4914  O   HOH E 113      37.404 -28.121 -22.046  1.00 43.04           O  
HETATM 4915  O   HOH E 114      35.784 -25.130 -26.715  1.00 46.23           O  
HETATM 4916  O   HOH E 115      37.769 -27.525 -24.729  1.00 36.98           O  
HETATM 4917  O   HOH E 116      38.810 -32.795 -23.244  1.00 48.96           O  
HETATM 4918  O   HOH E 117      31.006 -37.464  -6.715  1.00 43.75           O  
HETATM 4919  O   HOH F 101     -14.971 -39.140   2.727  1.00 35.33           O  
HETATM 4920  O   HOH F 102     -14.354 -37.694   0.506  1.00 33.56           O  
HETATM 4921  O   HOH F 103     -16.493 -41.249   1.061  1.00 43.68           O  
HETATM 4922  O   HOH F 104      -4.128 -45.919   1.426  1.00 16.21           O  
HETATM 4923  O   HOH F 105      -5.108 -33.529  -1.543  1.00 19.92           O  
HETATM 4924  O   HOH F 106     -11.591 -43.272  -1.752  1.00 30.18           O  
HETATM 4925  O   HOH F 107     -10.673 -39.947   7.087  1.00 33.12           O  
HETATM 4926  O   HOH F 108     -13.054 -40.833  -2.189  1.00 31.96           O  
HETATM 4927  O   HOH F 109     -12.242 -38.344  -0.975  1.00 28.31           O  
HETATM 4928  O   HOH F 110     -10.993 -35.520   6.085  1.00 39.68           O  
HETATM 4929  O   HOH F 111     -15.559 -41.584  -1.183  1.00 42.31           O  
HETATM 4930  O   HOH F 112      -7.469 -43.529  -6.247  1.00 27.20           O  
HETATM 4931  O   HOH F 113     -11.704 -36.476  -3.025  1.00 34.14           O  
HETATM 4932  O   HOH G 101     -10.855 -58.358 -34.927  1.00 40.44           O  
HETATM 4933  O   HOH G 102     -14.558 -59.175 -23.886  1.00 33.88           O  
HETATM 4934  O   HOH G 103     -20.235 -51.126 -17.331  1.00 54.51           O  
HETATM 4935  O   HOH G 104     -27.130 -53.372 -23.440  1.00 36.64           O  
HETATM 4936  O   HOH G 105     -16.540 -50.848 -24.913  1.00 63.39           O  
HETATM 4937  O   HOH H 101      38.914 -59.294 -16.527  1.00 41.81           O  
HETATM 4938  O   HOH H 102      35.668 -65.994  -7.445  1.00 52.18           O  
HETATM 4939  O   HOH H 103      49.634 -65.788 -11.112  1.00 47.77           O  
HETATM 4940  O   HOH H 104      45.145 -63.338 -16.222  1.00 43.86           O  
HETATM 4941  O   HOH H 105      45.731 -64.941 -18.083  1.00 48.66           O  
CONECT  108 4343                                                                
CONECT  139 4343                                                                
CONECT 1085 4350                                                                
CONECT 1116 4350                                                                
CONECT 2113 4351                                                                
CONECT 2144 4351                                                                
CONECT 3087 4352                                                                
CONECT 3118 4352                                                                
CONECT 4308 4332                                                                
CONECT 4309 4332                                                                
CONECT 4332 4308 4309                                                           
CONECT 4337 4338 4339                                                           
CONECT 4338 4337                                                                
CONECT 4339 4337 4340 4341                                                      
CONECT 4340 4339                                                                
CONECT 4341 4339 4342                                                           
CONECT 4342 4341                                                                
CONECT 4343  108  139 4353 4394                                                 
CONECT 4343 4418 4429                                                           
CONECT 4344 4345 4346                                                           
CONECT 4345 4344                                                                
CONECT 4346 4344 4347 4348                                                      
CONECT 4347 4346                                                                
CONECT 4348 4346 4349                                                           
CONECT 4349 4348                                                                
CONECT 4350 1085 1116 4606 4642                                                 
CONECT 4350 4687 4703                                                           
CONECT 4351 2113 2144 4709 4735                                                 
CONECT 4351 4745 4817                                                           
CONECT 4352 3087 3118 4832 4838                                                 
CONECT 4352 4840 4889                                                           
CONECT 4353 4343                                                                
CONECT 4394 4343                                                                
CONECT 4418 4343                                                                
CONECT 4429 4343                                                                
CONECT 4606 4350                                                                
CONECT 4642 4350                                                                
CONECT 4687 4350                                                                
CONECT 4703 4350                                                                
CONECT 4709 4351                                                                
CONECT 4735 4351                                                                
CONECT 4745 4351                                                                
CONECT 4817 4351                                                                
CONECT 4832 4352                                                                
CONECT 4838 4352                                                                
CONECT 4840 4352                                                                
CONECT 4889 4352                                                                
MASTER      387    0    8   16   28    0   15    6 4812    8   47   44          
END

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Related entries of code: 4s0n

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
No similar entries are found!
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
1zzi	RCSB PDB PDBbind	ssDNA
2ccz	RCSB PDB PDBbind	SSDNA
2vye	RCSB PDB PDBbind	ssDNA
3r8f	RCSB PDB PDBbind	ssDNA
4tmu	RCSB PDB PDBbind	ssDNA
5xs0	RCSB PDB PDBbind	ssDNA
6fwr	RCSB PDB PDBbind	ssDNA

Entry Information

PDB ID	4s0n
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	Helicase-like transcription factor, HLTF HIRAN Domain
Ligand Name	ssDNA
EC.Number	E.C.3.6.4.-
Resolution	1.5(Å)
Affinity (Kd/Ki/IC50)	Kd=13nM
Release Year	2015
Protein/NA Sequence	Check fasta file
Primary Reference	(2015) Mol.Cell Vol. 58: pp. 1090-1100

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): Q14527
Entrez Gene ID	NCBI Entrez Gene ID: 6596
ASD	Information of known allosteric effects of PDB entries

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