CNRS Nantes University UFIP UFIP
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***  3CLpro  ***

elNémo ID: 220302184528127212

Job options:

ID        	=	 220302184528127212
JOBID     	=	 3CLpro
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 3CLpro

HEADER    VIRAL PROTEIN                           15-SEP-20   7D1O              
TITLE     CRYSTAL STRUCTURE OF SARS-COV-2 MAIN PROTEASE WITH NARLAPREVIR        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3C-LIKE PROTEINASE;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MAIN PROTEASE,3CL-PRO,3CLP,MPRO,NON-STRUCTURAL PROTEIN 5,   
COMPND   5 NSP5,SARS CORONAVIRUS MAIN PROTEINASE;                               
COMPND   6 EC: 3.4.22.69;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: K-12                                       
KEYWDS    SARS-COV-2, MAIN PROTEASE, NARLAPREVIR, VIRAL PROTEIN                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.F.FU,Y.FENG,J.X.QI                                                  
REVDAT   4   14-APR-21 7D1O    1       COMPND HETNAM HETSYN                     
REVDAT   3   10-MAR-21 7D1O    1       COMPND                                   
REVDAT   2   24-FEB-21 7D1O    1       JRNL                                     
REVDAT   1   23-SEP-20 7D1O    0                                                
JRNL        AUTH   Y.BAI,F.YE,Y.FENG,H.LIAO,H.SONG,J.QI,G.F.GAO,W.TAN,L.FU,     
JRNL        AUTH 2 Y.SHI                                                        
JRNL        TITL   STRUCTURAL BASIS FOR THE INHIBITION OF THE SARS-COV-2 MAIN   
JRNL        TITL 2 PROTEASE BY THE ANTI-HCV DRUG NARLAPREVIR.                   
JRNL        REF    SIGNAL TRANSDUCT TARGET THER  V.   6    51 2021              
JRNL        REFN                   ESSN 2059-3635                               
JRNL        PMID   33542181                                                     
JRNL        DOI    10.1038/S41392-021-00468-9                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.78 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.16_3549                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.78                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.44                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 25933                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1294                            
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 55.4400 -  3.7000    0.98     2796   140  0.1659 0.1833        
REMARK   3     2  3.7000 -  2.9400    0.99     2751   162  0.2144 0.2381        
REMARK   3     3  2.9400 -  2.5700    0.99     2724   143  0.2581 0.2996        
REMARK   3     4  2.5700 -  2.3300    0.99     2753   142  0.2644 0.3200        
REMARK   3     5  2.3300 -  2.1700    0.99     2719   137  0.2720 0.2798        
REMARK   3     6  2.1700 -  2.0400    0.99     2739   144  0.2797 0.3074        
REMARK   3     7  2.0400 -  1.9400    0.99     2717   152  0.2906 0.3404        
REMARK   3     8  1.9400 -  1.8500    0.99     2734   115  0.3083 0.3107        
REMARK   3     9  1.8500 -  1.7800    0.99     2706   159  0.3485 0.3912        
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)     : 0.281            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.252           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.93                          
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      :  0.005           2421                                  
REMARK   3   ANGLE     :  0.759           3304                                  
REMARK   3   CHIRALITY :  0.051            377                                  
REMARK   3   PLANARITY :  0.005            424                                  
REMARK   3   DIHEDRAL  : 17.723            878                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -16.9000  -0.3778  16.8962              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2108 T22:   0.2242                                     
REMARK   3      T33:   0.2379 T12:  -0.0056                                     
REMARK   3      T13:   0.0346 T23:   0.0027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4670 L22:   1.3524                                     
REMARK   3      L33:   1.6433 L12:   0.2032                                     
REMARK   3      L13:   0.7279 L23:   0.6231                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0624 S12:   0.0286 S13:   0.1573                       
REMARK   3      S21:   0.0232 S22:   0.0227 S23:   0.0029                       
REMARK   3      S31:   0.1287 S32:   0.0459 S33:  -0.0953                       
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 7D1O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-SEP-20.                  
REMARK 100 THE DEPOSITION ID IS D_1300018611.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26120                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.780                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.440                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 7BRO                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG5000, 0.1M BIS-TRIS (PH=6.5),     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       56.60000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       27.02500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       56.60000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       27.02500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       -9.24748            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       45.03027            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 642  LIES ON A SPECIAL POSITION.                          
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   302                                                      
REMARK 465     VAL A   303                                                      
REMARK 465     THR A   304                                                      
REMARK 465     PHE A   305                                                      
REMARK 465     GLN A   306                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  76    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 298    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 240   C     PRO A 241   N       0.164                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 241   C   -  N   -  CA  ANGL. DEV. =  12.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  33     -106.39     52.08                                   
REMARK 500    ASN A  51       74.14   -155.77                                   
REMARK 500    ASN A  84      -39.80     68.54                                   
REMARK 500    CYS A  85       -0.63   -159.17                                   
REMARK 500    TYR A 154      -94.04     52.23                                   
REMARK 500    ARG A 222       54.12    -98.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7D1O A    1   306  UNP    P0DTC1   R1A_SARS2     3264   3569             
SEQRES   1 A  306  SER GLY PHE ARG LYS MET ALA PHE PRO SER GLY LYS VAL          
SEQRES   2 A  306  GLU GLY CYS MET VAL GLN VAL THR CYS GLY THR THR THR          
SEQRES   3 A  306  LEU ASN GLY LEU TRP LEU ASP ASP VAL VAL TYR CYS PRO          
SEQRES   4 A  306  ARG HIS VAL ILE CYS THR SER GLU ASP MET LEU ASN PRO          
SEQRES   5 A  306  ASN TYR GLU ASP LEU LEU ILE ARG LYS SER ASN HIS ASN          
SEQRES   6 A  306  PHE LEU VAL GLN ALA GLY ASN VAL GLN LEU ARG VAL ILE          
SEQRES   7 A  306  GLY HIS SER MET GLN ASN CYS VAL LEU LYS LEU LYS VAL          
SEQRES   8 A  306  ASP THR ALA ASN PRO LYS THR PRO LYS TYR LYS PHE VAL          
SEQRES   9 A  306  ARG ILE GLN PRO GLY GLN THR PHE SER VAL LEU ALA CYS          
SEQRES  10 A  306  TYR ASN GLY SER PRO SER GLY VAL TYR GLN CYS ALA MET          
SEQRES  11 A  306  ARG PRO ASN PHE THR ILE LYS GLY SER PHE LEU ASN GLY          
SEQRES  12 A  306  SER CYS GLY SER VAL GLY PHE ASN ILE ASP TYR ASP CYS          
SEQRES  13 A  306  VAL SER PHE CYS TYR MET HIS HIS MET GLU LEU PRO THR          
SEQRES  14 A  306  GLY VAL HIS ALA GLY THR ASP LEU GLU GLY ASN PHE TYR          
SEQRES  15 A  306  GLY PRO PHE VAL ASP ARG GLN THR ALA GLN ALA ALA GLY          
SEQRES  16 A  306  THR ASP THR THR ILE THR VAL ASN VAL LEU ALA TRP LEU          
SEQRES  17 A  306  TYR ALA ALA VAL ILE ASN GLY ASP ARG TRP PHE LEU ASN          
SEQRES  18 A  306  ARG PHE THR THR THR LEU ASN ASP PHE ASN LEU VAL ALA          
SEQRES  19 A  306  MET LYS TYR ASN TYR GLU PRO LEU THR GLN ASP HIS VAL          
SEQRES  20 A  306  ASP ILE LEU GLY PRO LEU SER ALA GLN THR GLY ILE ALA          
SEQRES  21 A  306  VAL LEU ASP MET CYS ALA SER LEU LYS GLU LEU LEU GLN          
SEQRES  22 A  306  ASN GLY MET ASN GLY ARG THR ILE LEU GLY SER ALA LEU          
SEQRES  23 A  306  LEU GLU ASP GLU PHE THR PRO PHE ASP VAL VAL ARG GLN          
SEQRES  24 A  306  CYS SER GLY VAL THR PHE GLN                                  
HET    NNA  A 401      49                                                       
HETNAM     NNA (1R,2S,5S)-3-[N-({1-[(TERT-BUTYLSULFONYL)                        
HETNAM   2 NNA  METHYL]CYCLOHEXYL}CARBAMOYL)-3-METHYL-L-VALYL]-N-               
HETNAM   3 NNA  {(1S)-1-[(1R)-2-(CYCLOPROPYLAMINO)-1-HYDROXY-2-                 
HETNAM   4 NNA  OXOETHYL]PENTYL}-6,6-DIMETHYL-3-                                
HETNAM   5 NNA  AZABICYCLO[3.1.0]HEXANE-2-CARBOXAMIDE                           
HETSYN     NNA NARLAPREVIR, BOUND FORM                                          
FORMUL   2  NNA    C36 H63 N5 O7 S                                              
FORMUL   3  HOH   *146(H2 O)                                                    
HELIX    1 AA1 SER A   10  GLY A   15  1                                   6    
HELIX    2 AA2 HIS A   41  CYS A   44  5                                   4    
HELIX    3 AA3 GLU A   47  ASN A   51  5                                   5    
HELIX    4 AA4 ASN A   53  ARG A   60  1                                   8    
HELIX    5 AA5 SER A   62  HIS A   64  5                                   3    
HELIX    6 AA6 ILE A  200  ASN A  214  1                                  15    
HELIX    7 AA7 THR A  226  TYR A  237  1                                  12    
HELIX    8 AA8 THR A  243  LEU A  250  1                                   8    
HELIX    9 AA9 LEU A  250  GLY A  258  1                                   9    
HELIX   10 AB1 ALA A  260  GLY A  275  1                                  16    
HELIX   11 AB2 THR A  292  SER A  301  1                                  10    
SHEET    1 AA1 7 VAL A  73  LEU A  75  0                                        
SHEET    2 AA1 7 PHE A  66  ALA A  70 -1  N  ALA A  70   O  VAL A  73           
SHEET    3 AA1 7 MET A  17  CYS A  22 -1  N  GLN A  19   O  GLN A  69           
SHEET    4 AA1 7 THR A  25  LEU A  32 -1  O  LEU A  27   N  VAL A  20           
SHEET    5 AA1 7 VAL A  35  PRO A  39 -1  O  TYR A  37   N  LEU A  30           
SHEET    6 AA1 7 VAL A  86  VAL A  91 -1  O  LEU A  87   N  CYS A  38           
SHEET    7 AA1 7 VAL A  77  GLN A  83 -1  N  SER A  81   O  LYS A  88           
SHEET    1 AA2 5 TYR A 101  PHE A 103  0                                        
SHEET    2 AA2 5 CYS A 156  GLU A 166  1  O  VAL A 157   N  LYS A 102           
SHEET    3 AA2 5 VAL A 148  ASP A 153 -1  N  ASN A 151   O  SER A 158           
SHEET    4 AA2 5 THR A 111  TYR A 118 -1  N  SER A 113   O  PHE A 150           
SHEET    5 AA2 5 SER A 121  ALA A 129 -1  O  SER A 123   N  ALA A 116           
SHEET    1 AA3 3 TYR A 101  PHE A 103  0                                        
SHEET    2 AA3 3 CYS A 156  GLU A 166  1  O  VAL A 157   N  LYS A 102           
SHEET    3 AA3 3 HIS A 172  THR A 175 -1  O  ALA A 173   N  MET A 165           
LINK         SG  CYS A 145                 C43 NNA A 401     1555   1555  1.77  
CRYST1  113.200   54.050   45.970  90.00 101.61  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008834  0.000000  0.001814        0.00000                         
SCALE2      0.000000  0.018501  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022207        0.00000                         
ATOM      1  N   SER A   1      -1.680   3.040  39.350  1.00 58.90           N  
ANISOU    1  N   SER A   1     7563   7742   7076    349   -904  -1315       N  
ATOM      2  CA  SER A   1      -2.665   3.914  38.728  1.00 58.69           C  
ANISOU    2  CA  SER A   1     7474   7701   7124    275   -737  -1294       C  
ATOM      3  C   SER A   1      -2.343   4.159  37.258  1.00 56.89           C  
ANISOU    3  C   SER A   1     7102   7444   7069    274   -670  -1268       C  
ATOM      4  O   SER A   1      -1.788   3.293  36.581  1.00 55.30           O  
ANISOU    4  O   SER A   1     6885   7236   6890    325   -716  -1229       O  
ATOM      5  CB  SER A   1      -2.748   5.244  39.476  1.00 61.14           C  
ANISOU    5  CB  SER A   1     7738   8030   7464    234   -712  -1404       C  
ATOM      6  OG  SER A   1      -1.481   5.876  39.534  1.00 64.26           O  
ANISOU    6  OG  SER A   1     8012   8428   7974    260   -798  -1508       O  
ATOM      7  N   GLY A   2      -2.687   5.342  36.775  1.00 43.03           N  
ANISOU    7  N   GLY A   2     5247   5671   5431    216   -566  -1294       N  
ATOM      8  CA  GLY A   2      -2.562   5.628  35.355  1.00 39.57           C  
ANISOU    8  CA  GLY A   2     4692   5207   5137    196   -486  -1250       C  
ATOM      9  C   GLY A   2      -3.792   5.197  34.583  1.00 37.26           C  
ANISOU    9  C   GLY A   2     4455   4890   4813    170   -379  -1139       C  
ATOM     10  O   GLY A   2      -4.484   4.241  34.932  1.00 42.73           O  
ANISOU   10  O   GLY A   2     5272   5588   5374    182   -386  -1078       O  
ATOM     11  N   PHE A   3      -4.073   5.928  33.506  1.00 41.82           N  
ANISOU   11  N   PHE A   3     4941   5437   5511    127   -283  -1108       N  
ATOM     12  CA  PHE A   3      -5.259   5.688  32.693  1.00 41.56           C  
ANISOU   12  CA  PHE A   3     4943   5380   5467    101   -183  -1011       C  
ATOM     13  C   PHE A   3      -4.858   5.650  31.227  1.00 40.32           C  
ANISOU   13  C   PHE A   3     4696   5214   5411     95   -140   -957       C  
ATOM     14  O   PHE A   3      -4.308   6.625  30.705  1.00 38.46           O  
ANISOU   14  O   PHE A   3     4352   4964   5297     60   -116   -984       O  
ATOM     15  CB  PHE A   3      -6.321   6.763  32.934  1.00 40.30           C  
ANISOU   15  CB  PHE A   3     4780   5192   5339     52   -102  -1028       C  
ATOM     16  CG  PHE A   3      -7.702   6.348  32.524  1.00 39.62           C  
ANISOU   16  CG  PHE A   3     4753   5099   5201     33    -20   -946       C  
ATOM     17  CD1 PHE A   3      -8.445   5.491  33.318  1.00 41.03           C  
ANISOU   17  CD1 PHE A   3     5046   5312   5231     35    -23   -924       C  
ATOM     18  CD2 PHE A   3      -8.256   6.808  31.341  1.00 39.88           C  
ANISOU   18  CD2 PHE A   3     4730   5093   5330      7     57   -887       C  
ATOM     19  CE1 PHE A   3      -9.717   5.104  32.943  1.00 41.00           C  
ANISOU   19  CE1 PHE A   3     5083   5310   5185      7     54   -854       C  
ATOM     20  CE2 PHE A   3      -9.527   6.425  30.960  1.00 40.92           C  
ANISOU   20  CE2 PHE A   3     4905   5222   5420     -7    123   -819       C  
ATOM     21  CZ  PHE A   3     -10.258   5.571  31.762  1.00 39.81           C  
ANISOU   21  CZ  PHE A   3     4864   5122   5141     -9    124   -807       C  
ATOM     22  N   ARG A   4      -5.141   4.530  30.566  1.00 37.73           N  
ANISOU   22  N   ARG A   4     4417   4892   5025    123   -133   -880       N  
ATOM     23  CA  ARG A   4      -4.778   4.333  29.172  1.00 33.77           C  
ANISOU   23  CA  ARG A   4     3841   4396   4593    125    -94   -833       C  
ATOM     24  C   ARG A   4      -5.952   3.726  28.420  1.00 33.12           C  
ANISOU   24  C   ARG A   4     3826   4294   4464    114    -29   -736       C  
ATOM     25  O   ARG A   4      -6.765   2.995  28.993  1.00 34.13           O  
ANISOU   25  O   ARG A   4     4064   4413   4490    122    -42   -705       O  
ATOM     26  CB  ARG A   4      -3.551   3.419  29.035  1.00 34.31           C  
ANISOU   26  CB  ARG A   4     3880   4507   4649    194   -179   -870       C  
ATOM     27  CG  ARG A   4      -2.277   3.994  29.624  1.00 36.40           C  
ANISOU   27  CG  ARG A   4     4051   4803   4976    206   -248   -974       C  
ATOM     28  CD  ARG A   4      -1.730   5.106  28.748  1.00 35.35           C  
ANISOU   28  CD  ARG A   4     3773   4683   4977    141   -177   -988       C  
ATOM     29  NE  ARG A   4      -1.757   4.738  27.335  1.00 35.73           N  
ANISOU   29  NE  ARG A   4     3776   4751   5047    134   -107   -923       N  
ATOM     30  CZ  ARG A   4      -0.852   3.961  26.748  1.00 37.24           C  
ANISOU   30  CZ  ARG A   4     3905   5004   5241    188   -137   -952       C  
ATOM     31  NH1 ARG A   4       0.159   3.468  27.449  1.00 37.21           N  
ANISOU   31  NH1 ARG A   4     3871   5038   5228    258   -243  -1042       N  
ATOM     32  NH2 ARG A   4      -0.958   3.679  25.457  1.00 37.26           N  
ANISOU   32  NH2 ARG A   4     3873   5032   5251    177    -64   -898       N  
ATOM     33  N   LYS A   5      -6.034   4.035  27.128  1.00 34.57           N  
ANISOU   33  N   LYS A   5     3943   4474   4718     88     39   -687       N  
ATOM     34  CA  LYS A   5      -7.007   3.375  26.268  1.00 34.77           C  
ANISOU   34  CA  LYS A   5     4021   4486   4702     85     86   -601       C  
ATOM     35  C   LYS A   5      -6.616   1.911  26.118  1.00 34.68           C  
ANISOU   35  C   LYS A   5     4067   4495   4615    149     23   -593       C  
ATOM     36  O   LYS A   5      -5.546   1.597  25.584  1.00 32.87           O  
ANISOU   36  O   LYS A   5     3772   4300   4414    189     -7   -626       O  
ATOM     37  CB  LYS A   5      -7.079   4.063  24.908  1.00 34.94           C  
ANISOU   37  CB  LYS A   5     3964   4503   4807     44    162   -552       C  
ATOM     38  CG  LYS A   5      -8.298   3.668  24.090  1.00 38.03           C  
ANISOU   38  CG  LYS A   5     4409   4875   5167     31    212   -467       C  
ATOM     39  CD  LYS A   5      -8.419   4.506  22.830  1.00 36.98           C  
ANISOU   39  CD  LYS A   5     4210   4732   5109    -15    277   -414       C  
ATOM     40  CE  LYS A   5      -8.813   5.937  23.151  1.00 36.94           C  
ANISOU   40  CE  LYS A   5     4172   4674   5188    -65    304   -422       C  
ATOM     41  NZ  LYS A   5      -9.023   6.742  21.916  1.00 42.08           N  
ANISOU   41  NZ  LYS A   5     4783   5299   5908   -113    353   -352       N  
ATOM     42  N   MET A   6      -7.478   1.019  26.593  1.00 32.60           N  
ANISOU   42  N   MET A   6     3922   4208   4257    156      1   -553       N  
ATOM     43  CA  MET A   6      -7.139  -0.385  26.753  1.00 36.22           C  
ANISOU   43  CA  MET A   6     4464   4660   4637    218    -85   -549       C  
ATOM     44  C   MET A   6      -8.123  -1.252  25.985  1.00 35.76           C  
ANISOU   44  C   MET A   6     4477   4575   4534    206    -57   -470       C  
ATOM     45  O   MET A   6      -9.333  -1.009  26.012  1.00 35.53           O  
ANISOU   45  O   MET A   6     4483   4531   4487    146      6   -420       O  
ATOM     46  CB  MET A   6      -7.145  -0.776  28.233  1.00 36.20           C  
ANISOU   46  CB  MET A   6     4565   4646   4545    227   -164   -570       C  
ATOM     47  CG  MET A   6      -6.291  -1.979  28.569  1.00 38.22           C  
ANISOU   47  CG  MET A   6     4889   4888   4746    308   -292   -592       C  
ATOM     48  SD  MET A   6      -6.202  -2.244  30.349  1.00 41.49           S  
ANISOU   48  SD  MET A   6     5427   5291   5046    311   -393   -613       S  
ATOM     49  CE  MET A   6      -5.628  -0.638  30.894  1.00 40.56           C  
ANISOU   49  CE  MET A   6     5181   5222   5008    287   -357   -704       C  
ATOM     50  N   ALA A   7      -7.595  -2.262  25.303  1.00 28.57           N  
ANISOU   50  N   ALA A   7     3581   3661   3612    267   -109   -472       N  
ATOM     51  CA  ALA A   7      -8.404  -3.216  24.567  1.00 27.17           C  
ANISOU   51  CA  ALA A   7     3478   3452   3393    264   -103   -411       C  
ATOM     52  C   ALA A   7      -8.372  -4.572  25.261  1.00 29.55           C  
ANISOU   52  C   ALA A   7     3918   3701   3608    304   -215   -401       C  
ATOM     53  O   ALA A   7      -7.421  -4.901  25.975  1.00 26.06           O  
ANISOU   53  O   ALA A   7     3497   3254   3150    366   -311   -452       O  
ATOM     54  CB  ALA A   7      -7.915  -3.349  23.125  1.00 29.33           C  
ANISOU   54  CB  ALA A   7     3671   3758   3717    301    -76   -423       C  
ATOM     55  N   PHE A   8      -9.426  -5.354  25.045  1.00 29.72           N  
ANISOU   55  N   PHE A   8     4040   3678   3576    266   -210   -332       N  
ATOM     56  CA  PHE A   8      -9.527  -6.660  25.671  1.00 29.62           C  
ANISOU   56  CA  PHE A   8     4179   3596   3478    284   -317   -304       C  
ATOM     57  C   PHE A   8      -8.439  -7.594  25.144  1.00 28.73           C  
ANISOU   57  C   PHE A   8     4074   3457   3386    399   -426   -357       C  
ATOM     58  O   PHE A   8      -7.930  -7.405  24.036  1.00 28.29           O  
ANISOU   58  O   PHE A   8     3910   3442   3395    446   -392   -402       O  
ATOM     59  CB  PHE A   8     -10.900  -7.273  25.407  1.00 30.86           C  
ANISOU   59  CB  PHE A   8     4427   3712   3587    204   -282   -220       C  
ATOM     60  CG  PHE A   8     -12.003  -6.667  26.224  1.00 30.31           C  
ANISOU   60  CG  PHE A   8     4377   3666   3475     96   -202   -176       C  
ATOM     61  CD1 PHE A   8     -12.184  -7.033  27.547  1.00 31.90           C  
ANISOU   61  CD1 PHE A   8     4693   3848   3579     54   -248   -152       C  
ATOM     62  CD2 PHE A   8     -12.861  -5.734  25.668  1.00 32.01           C  
ANISOU   62  CD2 PHE A   8     4497   3926   3741     40    -84   -164       C  
ATOM     63  CE1 PHE A   8     -13.199  -6.477  28.302  1.00 34.91           C  
ANISOU   63  CE1 PHE A   8     5081   4271   3911    -45   -162   -125       C  
ATOM     64  CE2 PHE A   8     -13.878  -5.174  26.417  1.00 33.60           C  
ANISOU   64  CE2 PHE A   8     4700   4156   3909    -46    -10   -143       C  
ATOM     65  CZ  PHE A   8     -14.047  -5.547  27.736  1.00 33.83           C  
ANISOU   65  CZ  PHE A   8     4833   4183   3838    -90    -42   -129       C  
ATOM     66  N   PRO A   9      -8.053  -8.602  25.927  1.00 30.79           N  
ANISOU   66  N   PRO A   9     4462   3650   3588    447   -560   -357       N  
ATOM     67  CA  PRO A   9      -7.152  -9.633  25.402  1.00 31.75           C  
ANISOU   67  CA  PRO A   9     4603   3730   3732    568   -679   -414       C  
ATOM     68  C   PRO A   9      -7.771 -10.319  24.193  1.00 31.94           C  
ANISOU   68  C   PRO A   9     4648   3721   3767    565   -654   -389       C  
ATOM     69  O   PRO A   9      -8.957 -10.654  24.185  1.00 32.31           O  
ANISOU   69  O   PRO A   9     4788   3721   3767    474   -621   -304       O  
ATOM     70  CB  PRO A   9      -6.989 -10.597  26.582  1.00 33.86           C  
ANISOU   70  CB  PRO A   9     5044   3903   3918    593   -833   -386       C  
ATOM     71  CG  PRO A   9      -7.285  -9.769  27.788  1.00 32.44           C  
ANISOU   71  CG  PRO A   9     4881   3760   3685    510   -791   -354       C  
ATOM     72  CD  PRO A   9      -8.341  -8.794  27.359  1.00 29.46           C  
ANISOU   72  CD  PRO A   9     4422   3445   3327    399   -617   -313       C  
ATOM     73  N   SER A  10      -6.955 -10.520  23.161  1.00 27.64           N  
ANISOU   73  N   SER A  10     4010   3211   3282    663   -668   -472       N  
ATOM     74  CA  SER A  10      -7.441 -10.973  21.865  1.00 29.85           C  
ANISOU   74  CA  SER A  10     4280   3486   3574    666   -628   -468       C  
ATOM     75  C   SER A  10      -7.226 -12.461  21.620  1.00 30.90           C  
ANISOU   75  C   SER A  10     4532   3519   3692    757   -771   -499       C  
ATOM     76  O   SER A  10      -7.518 -12.935  20.519  1.00 31.33           O  
ANISOU   76  O   SER A  10     4580   3568   3756    775   -755   -516       O  
ATOM     77  CB  SER A  10      -6.766 -10.173  20.747  1.00 28.40           C  
ANISOU   77  CB  SER A  10     3913   3422   3454    702   -531   -541       C  
ATOM     78  OG  SER A  10      -5.355 -10.266  20.836  1.00 27.11           O  
ANISOU   78  OG  SER A  10     3665   3303   3332    817   -598   -652       O  
ATOM     79  N   GLY A  11      -6.742 -13.206  22.617  1.00 35.91           N  
ANISOU   79  N   GLY A  11     5280   4065   4298    815   -920   -506       N  
ATOM     80  CA  GLY A  11      -6.382 -14.597  22.385  1.00 37.97           C  
ANISOU   80  CA  GLY A  11     5652   4216   4560    923  -1078   -550       C  
ATOM     81  C   GLY A  11      -7.538 -15.447  21.893  1.00 37.40           C  
ANISOU   81  C   GLY A  11     5712   4046   4454    853  -1088   -475       C  
ATOM     82  O   GLY A  11      -7.379 -16.255  20.975  1.00 38.82           O  
ANISOU   82  O   GLY A  11     5906   4185   4660    933  -1145   -537       O  
ATOM     83  N   LYS A  12      -8.717 -15.277  22.496  1.00 39.37           N  
ANISOU   83  N   LYS A  12     6052   4262   4644    701  -1032   -352       N  
ATOM     84  CA  LYS A  12      -9.871 -16.077  22.097  1.00 39.83           C  
ANISOU   84  CA  LYS A  12     6232   4230   4673    616  -1041   -278       C  
ATOM     85  C   LYS A  12     -10.297 -15.780  20.665  1.00 40.63           C  
ANISOU   85  C   LYS A  12     6220   4404   4815    608   -933   -311       C  
ATOM     86  O   LYS A  12     -10.840 -16.658  19.984  1.00 39.51           O  
ANISOU   86  O   LYS A  12     6156   4186   4671    601   -979   -306       O  
ATOM     87  CB  LYS A  12     -11.034 -15.833  23.059  1.00 41.91           C  
ANISOU   87  CB  LYS A  12     6584   4474   4864    445   -982   -148       C  
ATOM     88  CG  LYS A  12     -10.836 -16.443  24.438  1.00 46.20           C  
ANISOU   88  CG  LYS A  12     7297   4920   5337    427  -1109    -91       C  
ATOM     89  CD  LYS A  12     -11.966 -16.058  25.379  1.00 45.74           C  
ANISOU   89  CD  LYS A  12     7301   4882   5196    249  -1020     25       C  
ATOM     90  CE  LYS A  12     -11.894 -16.840  26.680  1.00 51.83           C  
ANISOU   90  CE  LYS A  12     8275   5547   5872    210  -1152    102       C  
ATOM     91  NZ  LYS A  12     -10.556 -16.728  27.323  1.00 50.73           N  
ANISOU   91  NZ  LYS A  12     8132   5406   5736    345  -1263     36       N  
ATOM     92  N   VAL A  13     -10.058 -14.560  20.189  1.00 26.70           N  
ANISOU   92  N   VAL A  13     4280   2782   3085    607   -797   -344       N  
ATOM     93  CA  VAL A  13     -10.472 -14.183  18.843  1.00 29.13           C  
ANISOU   93  CA  VAL A  13     4486   3164   3417    591   -694   -364       C  
ATOM     94  C   VAL A  13      -9.428 -14.558  17.792  1.00 29.40           C  
ANISOU   94  C   VAL A  13     4444   3240   3486    734   -731   -489       C  
ATOM     95  O   VAL A  13      -9.789 -14.879  16.655  1.00 30.25           O  
ANISOU   95  O   VAL A  13     4538   3361   3593    742   -709   -514       O  
ATOM     96  CB  VAL A  13     -10.791 -12.678  18.794  1.00 26.15           C  
ANISOU   96  CB  VAL A  13     3972   2908   3056    511   -535   -328       C  
ATOM     97  CG1 VAL A  13     -11.340 -12.286  17.429  1.00 26.78           C  
ANISOU   97  CG1 VAL A  13     3969   3056   3150    483   -439   -327       C  
ATOM     98  CG2 VAL A  13     -11.776 -12.312  19.892  1.00 26.27           C  
ANISOU   98  CG2 VAL A  13     4051   2895   3036    384   -498   -228       C  
ATOM     99  N   GLU A  14      -8.140 -14.531  18.149  1.00 31.28           N  
ANISOU   99  N   GLU A  14     4625   3507   3753    847   -789   -578       N  
ATOM    100  CA  GLU A  14      -7.091 -14.840  17.180  1.00 33.34           C  
ANISOU  100  CA  GLU A  14     4788   3832   4047    984   -813   -715       C  
ATOM    101  C   GLU A  14      -7.272 -16.231  16.586  1.00 33.38           C  
ANISOU  101  C   GLU A  14     4910   3729   4045   1059   -933   -763       C  
ATOM    102  O   GLU A  14      -7.056 -16.435  15.386  1.00 36.65           O  
ANISOU  102  O   GLU A  14     5255   4206   4464   1120   -904   -849       O  
ATOM    103  CB  GLU A  14      -5.715 -14.717  17.833  1.00 34.72           C  
ANISOU  103  CB  GLU A  14     4890   4042   4260   1096   -880   -808       C  
ATOM    104  CG  GLU A  14      -5.368 -13.320  18.310  1.00 35.05           C  
ANISOU  104  CG  GLU A  14     4800   4198   4321   1033   -766   -785       C  
ATOM    105  CD  GLU A  14      -4.125 -13.299  19.174  1.00 34.18           C  
ANISOU  105  CD  GLU A  14     4641   4100   4244   1132   -859   -867       C  
ATOM    106  OE1 GLU A  14      -3.113 -13.913  18.775  1.00 36.95           O  
ANISOU  106  OE1 GLU A  14     4936   4473   4631   1274   -940   -997       O  
ATOM    107  OE2 GLU A  14      -4.158 -12.671  20.253  1.00 33.17           O  
ANISOU  107  OE2 GLU A  14     4528   3967   4110   1072   -855   -811       O  
ATOM    108  N   GLY A  15      -7.670 -17.201  17.408  1.00 32.53           N  
ANISOU  108  N   GLY A  15     4984   3457   3920   1050  -1071   -710       N  
ATOM    109  CA  GLY A  15      -7.889 -18.557  16.940  1.00 33.95           C  
ANISOU  109  CA  GLY A  15     5296   3504   4099   1111  -1204   -748       C  
ATOM    110  C   GLY A  15      -9.097 -18.750  16.050  1.00 34.25           C  
ANISOU  110  C   GLY A  15     5374   3526   4113   1011  -1143   -696       C  
ATOM    111  O   GLY A  15      -9.394 -19.889  15.677  1.00 34.81           O  
ANISOU  111  O   GLY A  15     5566   3474   4185   1045  -1257   -722       O  
ATOM    112  N   CYS A  16      -9.806 -17.673  15.705  1.00 33.59           N  
ANISOU  112  N   CYS A  16     5194   3557   4012    893   -977   -625       N  
ATOM    113  CA  CYS A  16     -10.967 -17.740  14.830  1.00 33.58           C  
ANISOU  113  CA  CYS A  16     5212   3557   3989    800   -917   -578       C  
ATOM    114  C   CYS A  16     -10.788 -16.983  13.522  1.00 31.24           C  
ANISOU  114  C   CYS A  16     4758   3420   3690    824   -792   -638       C  
ATOM    115  O   CYS A  16     -11.668 -17.058  12.659  1.00 32.96           O  
ANISOU  115  O   CYS A  16     4987   3649   3887    765   -754   -614       O  
ATOM    116  CB  CYS A  16     -12.210 -17.196  15.548  1.00 29.80           C  
ANISOU  116  CB  CYS A  16     4774   3062   3488    625   -844   -430       C  
ATOM    117  SG  CYS A  16     -12.431 -17.810  17.230  1.00 34.76           S  
ANISOU  117  SG  CYS A  16     5574   3541   4091    561   -952   -337       S  
ATOM    118  N   MET A  17      -9.689 -16.255  13.353  1.00 30.94           N  
ANISOU  118  N   MET A  17     4578   3508   3668    899   -730   -711       N  
ATOM    119  CA  MET A  17      -9.470 -15.444  12.162  1.00 32.22           C  
ANISOU  119  CA  MET A  17     4595   3831   3815    902   -601   -752       C  
ATOM    120  C   MET A  17      -8.856 -16.292  11.055  1.00 34.79           C  
ANISOU  120  C   MET A  17     4905   4188   4128   1029   -653   -895       C  
ATOM    121  O   MET A  17      -7.813 -16.923  11.252  1.00 35.73           O  
ANISOU  121  O   MET A  17     5014   4289   4273   1162   -743  -1011       O  
ATOM    122  CB  MET A  17      -8.566 -14.251  12.478  1.00 32.49           C  
ANISOU  122  CB  MET A  17     4481   3992   3873    906   -504   -763       C  
ATOM    123  CG  MET A  17      -9.124 -13.320  13.541  1.00 28.52           C  
ANISOU  123  CG  MET A  17     3984   3470   3384    789   -448   -640       C  
ATOM    124  SD  MET A  17     -10.831 -12.839  13.215  1.00 29.38           S  
ANISOU  124  SD  MET A  17     4136   3559   3467    635   -369   -505       S  
ATOM    125  CE  MET A  17     -10.677 -12.081  11.597  1.00 28.32           C  
ANISOU  125  CE  MET A  17     3873   3577   3308    636   -251   -536       C  
ATOM    126  N   VAL A  18      -9.506 -16.299   9.892  1.00 32.28           N  
ANISOU  126  N   VAL A  18     4579   3918   3766    994   -601   -895       N  
ATOM    127  CA  VAL A  18      -9.058 -17.068   8.741  1.00 34.43           C  
ANISOU  127  CA  VAL A  18     4838   4232   4009   1105   -638  -1035       C  
ATOM    128  C   VAL A  18      -8.948 -16.139   7.539  1.00 35.62           C  
ANISOU  128  C   VAL A  18     4857   4573   4104   1073   -488  -1048       C  
ATOM    129  O   VAL A  18      -9.378 -14.985   7.568  1.00 32.21           O  
ANISOU  129  O   VAL A  18     4368   4209   3662    960   -374   -935       O  
ATOM    130  CB  VAL A  18      -9.999 -18.247   8.417  1.00 33.24           C  
ANISOU  130  CB  VAL A  18     4843   3938   3848   1098   -754  -1037       C  
ATOM    131  CG1 VAL A  18     -10.153 -19.153   9.624  1.00 33.36           C  
ANISOU  131  CG1 VAL A  18     5007   3755   3911   1107   -904  -1002       C  
ATOM    132  CG2 VAL A  18     -11.351 -17.732   7.949  1.00 32.32           C  
ANISOU  132  CG2 VAL A  18     4747   3836   3696    952   -678   -915       C  
ATOM    133  N   GLN A  19      -8.361 -16.669   6.472  1.00 39.43           N  
ANISOU  133  N   GLN A  19     5298   5139   4545   1175   -494  -1190       N  
ATOM    134  CA  GLN A  19      -8.229 -15.968   5.204  1.00 41.93           C  
ANISOU  134  CA  GLN A  19     5508   5641   4784   1148   -362  -1213       C  
ATOM    135  C   GLN A  19      -9.318 -16.437   4.249  1.00 41.30           C  
ANISOU  135  C   GLN A  19     5519   5530   4642   1109   -387  -1195       C  
ATOM    136  O   GLN A  19      -9.582 -17.637   4.136  1.00 41.67           O  
ANISOU  136  O   GLN A  19     5672   5463   4698   1178   -514  -1270       O  
ATOM    137  CB  GLN A  19      -6.849 -16.218   4.592  1.00 42.98           C  
ANISOU  137  CB  GLN A  19     5520   5917   4894   1282   -337  -1396       C  
ATOM    138  CG  GLN A  19      -6.534 -15.380   3.367  1.00 46.50           C  
ANISOU  138  CG  GLN A  19     5843   6581   5246   1240   -180  -1414       C  
ATOM    139  CD  GLN A  19      -5.198 -15.743   2.748  1.00 51.20           C  
ANISOU  139  CD  GLN A  19     6311   7331   5811   1372   -152  -1614       C  
ATOM    140  OE1 GLN A  19      -4.353 -14.879   2.513  1.00 53.22           O  
ANISOU  140  OE1 GLN A  19     6417   7760   6044   1344    -25  -1633       O  
ATOM    141  NE2 GLN A  19      -4.999 -17.030   2.484  1.00 51.01           N  
ANISOU  141  NE2 GLN A  19     6344   7246   5792   1515   -274  -1772       N  
ATOM    142  N   VAL A  20      -9.956 -15.486   3.571  1.00 33.83           N  
ANISOU  142  N   VAL A  20     4537   4680   3639    999   -277  -1095       N  
ATOM    143  CA  VAL A  20     -11.023 -15.778   2.620  1.00 32.14           C  
ANISOU  143  CA  VAL A  20     4396   4454   3362    953   -298  -1069       C  
ATOM    144  C   VAL A  20     -10.667 -15.121   1.295  1.00 37.09           C  
ANISOU  144  C   VAL A  20     4932   5281   3878    945   -180  -1101       C  
ATOM    145  O   VAL A  20     -10.575 -13.890   1.214  1.00 35.91           O  
ANISOU  145  O   VAL A  20     4704   5232   3710    860    -63  -1003       O  
ATOM    146  CB  VAL A  20     -12.394 -15.285   3.114  1.00 32.78           C  
ANISOU  146  CB  VAL A  20     4541   4437   3476    816   -300   -898       C  
ATOM    147  CG1 VAL A  20     -13.459 -15.539   2.057  1.00 33.28           C  
ANISOU  147  CG1 VAL A  20     4664   4506   3475    772   -325   -881       C  
ATOM    148  CG2 VAL A  20     -12.764 -15.962   4.424  1.00 33.01           C  
ANISOU  148  CG2 VAL A  20     4666   4283   3595    808   -406   -862       C  
ATOM    149  N   THR A  21     -10.469 -15.935   0.262  1.00 37.18           N  
ANISOU  149  N   THR A  21     4963   5350   3815   1028   -215  -1238       N  
ATOM    150  CA  THR A  21     -10.156 -15.447  -1.074  1.00 36.89           C  
ANISOU  150  CA  THR A  21     4855   5514   3649   1020   -108  -1279       C  
ATOM    151  C   THR A  21     -11.234 -15.923  -2.035  1.00 40.52           C  
ANISOU  151  C   THR A  21     5413   5950   4032    995   -166  -1276       C  
ATOM    152  O   THR A  21     -11.468 -17.129  -2.165  1.00 40.87           O  
ANISOU  152  O   THR A  21     5543   5897   4089   1074   -288  -1384       O  
ATOM    153  CB  THR A  21      -8.777 -15.924  -1.534  1.00 37.94           C  
ANISOU  153  CB  THR A  21     4893   5783   3740   1152    -78  -1476       C  
ATOM    154  OG1 THR A  21      -7.778 -15.463  -0.616  1.00 38.78           O  
ANISOU  154  OG1 THR A  21     4898   5912   3925   1172    -32  -1482       O  
ATOM    155  CG2 THR A  21      -8.467 -15.387  -2.924  1.00 41.05           C  
ANISOU  155  CG2 THR A  21     5215   6404   3979   1124     48  -1511       C  
ATOM    156  N   CYS A  22     -11.889 -14.975  -2.699  1.00 42.63           N  
ANISOU  156  N   CYS A  22     5673   6300   4223    886    -90  -1151       N  
ATOM    157  CA  CYS A  22     -12.887 -15.259  -3.725  1.00 46.52           C  
ANISOU  157  CA  CYS A  22     6246   6800   4628    855   -138  -1142       C  
ATOM    158  C   CYS A  22     -12.419 -14.602  -5.015  1.00 48.06           C  
ANISOU  158  C   CYS A  22     6381   7217   4663    837    -22  -1160       C  
ATOM    159  O   CYS A  22     -12.438 -13.373  -5.134  1.00 47.74           O  
ANISOU  159  O   CYS A  22     6292   7258   4590    739     80  -1024       O  
ATOM    160  CB  CYS A  22     -14.266 -14.746  -3.315  1.00 42.90           C  
ANISOU  160  CB  CYS A  22     5847   6226   4229    738   -176   -968       C  
ATOM    161  SG  CYS A  22     -15.591 -15.185  -4.462  1.00 48.20           S  
ANISOU  161  SG  CYS A  22     6615   6885   4814    703   -264   -962       S  
ATOM    162  N   GLY A  23     -11.997 -15.417  -5.976  1.00 58.84           N  
ANISOU  162  N   GLY A  23     7755   8679   5924    928    -39  -1328       N  
ATOM    163  CA  GLY A  23     -11.462 -14.892  -7.214  1.00 58.67           C  
ANISOU  163  CA  GLY A  23     7676   8887   5728    912     78  -1362       C  
ATOM    164  C   GLY A  23     -10.228 -14.045  -6.988  1.00 60.07           C  
ANISOU  164  C   GLY A  23     7718   9209   5896    893    226  -1355       C  
ATOM    165  O   GLY A  23      -9.156 -14.563  -6.661  1.00 62.79           O  
ANISOU  165  O   GLY A  23     7984   9595   6279    996    241  -1507       O  
ATOM    166  N   THR A  24     -10.377 -12.733  -7.143  1.00 55.76           N  
ANISOU  166  N   THR A  24     7144   8735   5309    763    328  -1182       N  
ATOM    167  CA  THR A  24      -9.265 -11.799  -7.057  1.00 56.53           C  
ANISOU  167  CA  THR A  24     7114   8979   5384    714    477  -1156       C  
ATOM    168  C   THR A  24      -9.200 -11.051  -5.731  1.00 56.65           C  
ANISOU  168  C   THR A  24     7090   8872   5564    658    487  -1032       C  
ATOM    169  O   THR A  24      -8.245 -10.302  -5.508  1.00 55.16           O  
ANISOU  169  O   THR A  24     6792   8785   5383    617    599  -1017       O  
ATOM    170  CB  THR A  24      -9.347 -10.789  -8.206  1.00 61.55           C  
ANISOU  170  CB  THR A  24     7750   9787   5848    594    588  -1046       C  
ATOM    171  OG1 THR A  24      -8.169  -9.973  -8.213  1.00 60.33           O  
ANISOU  171  OG1 THR A  24     7468   9792   5661    538    740  -1039       O  
ATOM    172  CG2 THR A  24     -10.575  -9.903  -8.045  1.00 59.48           C  
ANISOU  172  CG2 THR A  24     7577   9399   5622    479    544   -824       C  
ATOM    173  N   THR A  25     -10.178 -11.236  -4.848  1.00 49.98           N  
ANISOU  173  N   THR A  25     6327   7819   4844    651    376   -950       N  
ATOM    174  CA  THR A  25     -10.275 -10.474  -3.609  1.00 44.97           C  
ANISOU  174  CA  THR A  25     5666   7068   4351    591    384   -826       C  
ATOM    175  C   THR A  25      -9.887 -11.350  -2.424  1.00 41.43           C  
ANISOU  175  C   THR A  25     5211   6493   4036    690    302   -925       C  
ATOM    176  O   THR A  25     -10.331 -12.498  -2.324  1.00 41.21           O  
ANISOU  176  O   THR A  25     5264   6360   4033    768    185  -1007       O  
ATOM    177  CB  THR A  25     -11.691  -9.924  -3.418  1.00 43.43           C  
ANISOU  177  CB  THR A  25     5560   6744   4197    501    328   -655       C  
ATOM    178  OG1 THR A  25     -12.008  -9.034  -4.496  1.00 49.57           O  
ANISOU  178  OG1 THR A  25     6350   7631   4853    412    392   -553       O  
ATOM    179  CG2 THR A  25     -11.805  -9.171  -2.099  1.00 40.68           C  
ANISOU  179  CG2 THR A  25     5184   6280   3994    448    335   -546       C  
ATOM    180  N   THR A  26      -9.063 -10.802  -1.532  1.00 36.26           N  
ANISOU  180  N   THR A  26     4468   5844   3466    682    354   -912       N  
ATOM    181  CA  THR A  26      -8.633 -11.487  -0.320  1.00 34.11           C  
ANISOU  181  CA  THR A  26     4190   5453   3316    768    274   -988       C  
ATOM    182  C   THR A  26      -8.954 -10.615   0.885  1.00 30.54           C  
ANISOU  182  C   THR A  26     3734   4892   2975    686    281   -846       C  
ATOM    183  O   THR A  26      -8.564  -9.443   0.926  1.00 31.38           O  
ANISOU  183  O   THR A  26     3762   5077   3084    603    383   -766       O  
ATOM    184  CB  THR A  26      -7.131 -11.799  -0.357  1.00 37.76           C  
ANISOU  184  CB  THR A  26     4530   6043   3773    866    319  -1154       C  
ATOM    185  OG1 THR A  26      -6.843 -12.650  -1.473  1.00 41.67           O  
ANISOU  185  OG1 THR A  26     5024   6645   4163    954    312  -1307       O  
ATOM    186  CG2 THR A  26      -6.694 -12.486   0.928  1.00 33.08           C  
ANISOU  186  CG2 THR A  26     3942   5318   3310    961    216  -1224       C  
ATOM    187  N   LEU A  27      -9.661 -11.182   1.858  1.00 33.12           N  
ANISOU  187  N   LEU A  27     4150   5043   3392    702    173   -817       N  
ATOM    188  CA  LEU A  27      -9.977 -10.476   3.095  1.00 33.36           C  
ANISOU  188  CA  LEU A  27     4182   4971   3523    636    172   -703       C  
ATOM    189  C   LEU A  27     -10.047 -11.494   4.229  1.00 30.33           C  
ANISOU  189  C   LEU A  27     3870   4435   3221    704     52   -751       C  
ATOM    190  O   LEU A  27      -9.611 -12.641   4.086  1.00 32.82           O  
ANISOU  190  O   LEU A  27     4215   4727   3527    812    -27   -879       O  
ATOM    191  CB  LEU A  27     -11.271  -9.663   2.949  1.00 32.38           C  
ANISOU  191  CB  LEU A  27     4106   4800   3397    521    190   -546       C  
ATOM    192  CG  LEU A  27     -12.554 -10.360   2.492  1.00 31.54           C  
ANISOU  192  CG  LEU A  27     4107   4614   3262    510    107   -523       C  
ATOM    193  CD1 LEU A  27     -13.118 -11.262   3.581  1.00 32.33           C  
ANISOU  193  CD1 LEU A  27     4290   4551   3445    530      0   -530       C  
ATOM    194  CD2 LEU A  27     -13.585  -9.325   2.068  1.00 29.83           C  
ANISOU  194  CD2 LEU A  27     3899   4405   3031    406    145   -383       C  
ATOM    195  N   ASN A  28     -10.601 -11.073   5.362  1.00 30.68           N  
ANISOU  195  N   ASN A  28     3945   4371   3341    642     33   -649       N  
ATOM    196  CA  ASN A  28     -10.621 -11.879   6.573  1.00 28.74           C  
ANISOU  196  CA  ASN A  28     3770   3986   3163    684    -71   -671       C  
ATOM    197  C   ASN A  28     -12.003 -12.471   6.822  1.00 28.22           C  
ANISOU  197  C   ASN A  28     3829   3785   3107    631   -148   -601       C  
ATOM    198  O   ASN A  28     -13.022 -11.929   6.388  1.00 30.00           O  
ANISOU  198  O   ASN A  28     4064   4019   3315    544   -110   -511       O  
ATOM    199  CB  ASN A  28     -10.196 -11.046   7.786  1.00 29.10           C  
ANISOU  199  CB  ASN A  28     3764   4015   3276    649    -37   -618       C  
ATOM    200  CG  ASN A  28      -8.900 -10.298   7.553  1.00 29.47           C  
ANISOU  200  CG  ASN A  28     3674   4201   3323    675     50   -675       C  
ATOM    201  OD1 ASN A  28      -7.813 -10.857   7.697  1.00 33.83           O  
ANISOU  201  OD1 ASN A  28     4181   4786   3887    775     14   -794       O  
ATOM    202  ND2 ASN A  28      -9.008  -9.025   7.192  1.00 30.39           N  
ANISOU  202  ND2 ASN A  28     3721   4397   3431    582    158   -590       N  
ATOM    203  N   GLY A  29     -12.020 -13.598   7.533  1.00 29.35           N  
ANISOU  203  N   GLY A  29     4068   3803   3283    681   -264   -644       N  
ATOM    204  CA  GLY A  29     -13.263 -14.225   7.931  1.00 28.48           C  
ANISOU  204  CA  GLY A  29     4076   3559   3188    614   -340   -576       C  
ATOM    205  C   GLY A  29     -13.202 -14.658   9.380  1.00 26.91           C  
ANISOU  205  C   GLY A  29     3950   3236   3040    608   -412   -548       C  
ATOM    206  O   GLY A  29     -12.128 -14.765   9.978  1.00 26.65           O  
ANISOU  206  O   GLY A  29     3895   3203   3029    686   -439   -606       O  
ATOM    207  N   LEU A  30     -14.381 -14.907   9.945  1.00 28.26           N  
ANISOU  207  N   LEU A  30     4207   3307   3224    509   -445   -458       N  
ATOM    208  CA  LEU A  30     -14.522 -15.328  11.334  1.00 29.57           C  
ANISOU  208  CA  LEU A  30     4461   3357   3418    474   -509   -409       C  
ATOM    209  C   LEU A  30     -14.986 -16.778  11.365  1.00 30.07           C  
ANISOU  209  C   LEU A  30     4673   3274   3477    476   -643   -428       C  
ATOM    210  O   LEU A  30     -16.069 -17.098  10.865  1.00 29.96           O  
ANISOU  210  O   LEU A  30     4701   3228   3454    399   -654   -393       O  
ATOM    211  CB  LEU A  30     -15.503 -14.430  12.087  1.00 28.56           C  
ANISOU  211  CB  LEU A  30     4310   3237   3303    342   -430   -291       C  
ATOM    212  CG  LEU A  30     -15.642 -14.716  13.584  1.00 29.22           C  
ANISOU  212  CG  LEU A  30     4478   3229   3397    291   -474   -235       C  
ATOM    213  CD1 LEU A  30     -14.351 -14.382  14.315  1.00 26.88           C  
ANISOU  213  CD1 LEU A  30     4145   2957   3111    373   -479   -277       C  
ATOM    214  CD2 LEU A  30     -16.809 -13.940  14.174  1.00 26.62           C  
ANISOU  214  CD2 LEU A  30     4122   2920   3073    156   -391   -136       C  
ATOM    215  N   TRP A  31     -14.173 -17.644  11.964  1.00 30.43           N  
ANISOU  215  N   TRP A  31     4799   3227   3536    562   -754   -483       N  
ATOM    216  CA  TRP A  31     -14.391 -19.091  11.935  1.00 33.10           C  
ANISOU  216  CA  TRP A  31     5290   3408   3878    586   -905   -516       C  
ATOM    217  C   TRP A  31     -14.947 -19.537  13.284  1.00 32.13           C  
ANISOU  217  C   TRP A  31     5300   3150   3759    486   -970   -410       C  
ATOM    218  O   TRP A  31     -14.204 -19.885  14.202  1.00 35.30           O  
ANISOU  218  O   TRP A  31     5765   3480   4168    541  -1050   -417       O  
ATOM    219  CB  TRP A  31     -13.090 -19.810  11.590  1.00 33.09           C  
ANISOU  219  CB  TRP A  31     5296   3388   3891    765  -1003   -661       C  
ATOM    220  CG  TRP A  31     -13.192 -21.306  11.478  1.00 35.69           C  
ANISOU  220  CG  TRP A  31     5784   3542   4233    816  -1176   -716       C  
ATOM    221  CD1 TRP A  31     -14.328 -22.049  11.330  1.00 36.15           C  
ANISOU  221  CD1 TRP A  31     5964   3481   4289    714  -1239   -661       C  
ATOM    222  CD2 TRP A  31     -12.104 -22.237  11.498  1.00 35.12           C  
ANISOU  222  CD2 TRP A  31     5766   3389   4190    983  -1318   -844       C  
ATOM    223  NE1 TRP A  31     -14.013 -23.386  11.261  1.00 38.59           N  
ANISOU  223  NE1 TRP A  31     6412   3627   4622    802  -1414   -740       N  
ATOM    224  CE2 TRP A  31     -12.653 -23.527  11.361  1.00 38.39           C  
ANISOU  224  CE2 TRP A  31     6349   3620   4618    976  -1469   -856       C  
ATOM    225  CE3 TRP A  31     -10.717 -22.104  11.621  1.00 36.26           C  
ANISOU  225  CE3 TRP A  31     5826   3597   4356   1141  -1337   -956       C  
ATOM    226  CZ2 TRP A  31     -11.864 -24.677  11.344  1.00 37.90           C  
ANISOU  226  CZ2 TRP A  31     6383   3424   4592   1130  -1646   -976       C  
ATOM    227  CZ3 TRP A  31      -9.936 -23.246  11.604  1.00 40.74           C  
ANISOU  227  CZ3 TRP A  31     6475   4047   4959   1298  -1509  -1082       C  
ATOM    228  CH2 TRP A  31     -10.512 -24.515  11.467  1.00 39.73           C  
ANISOU  228  CH2 TRP A  31     6525   3724   4846   1297  -1665  -1091       C  
ATOM    229  N   LEU A  32     -16.275 -19.635  13.355  1.00 33.48           N  
ANISOU  229  N   LEU A  32     5520   3281   3921    336   -948   -317       N  
ATOM    230  CA  LEU A  32     -16.956 -20.110  14.587  1.00 33.01           C  
ANISOU  230  CA  LEU A  32     5590   3103   3850    209   -997   -208       C  
ATOM    231  C   LEU A  32     -17.624 -21.452  14.277  1.00 36.67           C  
ANISOU  231  C   LEU A  32     6204   3410   4320    160  -1124   -206       C  
ATOM    232  O   LEU A  32     -18.325 -21.538  13.259  1.00 39.14           O  
ANISOU  232  O   LEU A  32     6482   3751   4640    128  -1104   -230       O  
ATOM    233  CB  LEU A  32     -17.977 -19.066  15.040  1.00 34.79           C  
ANISOU  233  CB  LEU A  32     5732   3424   4063     60   -855   -107       C  
ATOM    234  CG  LEU A  32     -17.379 -17.722  15.449  1.00 34.04           C  
ANISOU  234  CG  LEU A  32     5501   3463   3969     96   -738   -105       C  
ATOM    235  CD1 LEU A  32     -18.468 -16.737  15.833  1.00 31.44           C  
ANISOU  235  CD1 LEU A  32     5092   3217   3637    -40   -610    -21       C  
ATOM    236  CD2 LEU A  32     -16.386 -17.899  16.586  1.00 34.95           C  
ANISOU  236  CD2 LEU A  32     5681   3527   4072    155   -801   -107       C  
ATOM    237  N   ASP A  33     -17.399 -22.448  15.134  1.00 42.73           N  
ANISOU  237  N   ASP A  33     7140   4014   5083    152  -1260   -175       N  
ATOM    238  CA  ASP A  33     -17.962 -23.805  14.921  1.00 42.64           C  
ANISOU  238  CA  ASP A  33     7295   3822   5083    101  -1404   -168       C  
ATOM    239  C   ASP A  33     -17.596 -24.265  13.507  1.00 40.78           C  
ANISOU  239  C   ASP A  33     7029   3587   4879    237  -1461   -311       C  
ATOM    240  O   ASP A  33     -16.408 -24.517  13.261  1.00 43.18           O  
ANISOU  240  O   ASP A  33     7327   3880   5199    416  -1532   -423       O  
ATOM    241  CB  ASP A  33     -19.467 -23.847  15.188  1.00 43.75           C  
ANISOU  241  CB  ASP A  33     7468   3947   5210   -120  -1349    -50       C  
ATOM    242  CG  ASP A  33     -19.824 -23.598  16.642  1.00 44.20           C  
ANISOU  242  CG  ASP A  33     7580   3991   5222   -260  -1306     81       C  
ATOM    243  OD1 ASP A  33     -19.094 -24.094  17.514  1.00 47.15           O  
ANISOU  243  OD1 ASP A  33     8079   4260   5576   -216  -1407    104       O  
ATOM    244  OD2 ASP A  33     -20.829 -22.913  16.886  1.00 47.18           O  
ANISOU  244  OD2 ASP A  33     7874   4469   5582   -406  -1176    155       O  
ATOM    245  N   ASP A  34     -18.563 -24.280  12.590  1.00 40.06           N  
ANISOU  245  N   ASP A  34     6899   3530   4791    159  -1422   -316       N  
ATOM    246  CA  ASP A  34     -18.255 -24.790  11.257  1.00 42.11           C  
ANISOU  246  CA  ASP A  34     7146   3790   5066    282  -1485   -455       C  
ATOM    247  C   ASP A  34     -18.737 -23.830  10.175  1.00 42.22           C  
ANISOU  247  C   ASP A  34     6995   3990   5058    266  -1345   -479       C  
ATOM    248  O   ASP A  34     -19.082 -24.248   9.066  1.00 40.40           O  
ANISOU  248  O   ASP A  34     6765   3760   4825    288  -1383   -555       O  
ATOM    249  CB  ASP A  34     -18.822 -26.200  11.054  1.00 45.27           C  
ANISOU  249  CB  ASP A  34     7722   3986   5492    234  -1651   -470       C  
ATOM    250  CG  ASP A  34     -20.326 -26.218  10.841  1.00 48.94           C  
ANISOU  250  CG  ASP A  34     8189   4448   5956     36  -1610   -384       C  
ATOM    251  OD1 ASP A  34     -21.020 -25.295  11.313  1.00 47.04           O  
ANISOU  251  OD1 ASP A  34     7856   4320   5698    -92  -1472   -279       O  
ATOM    252  OD2 ASP A  34     -20.814 -27.173  10.199  1.00 51.59           O  
ANISOU  252  OD2 ASP A  34     8617   4669   6315     12  -1721   -432       O  
ATOM    253  N   VAL A  35     -18.744 -22.536  10.485  1.00 35.13           N  
ANISOU  253  N   VAL A  35     5960   3246   4143    232  -1192   -416       N  
ATOM    254  CA  VAL A  35     -19.158 -21.489   9.560  1.00 34.48           C  
ANISOU  254  CA  VAL A  35     5725   3335   4039    216  -1062   -420       C  
ATOM    255  C   VAL A  35     -18.091 -20.404   9.558  1.00 35.43           C  
ANISOU  255  C   VAL A  35     5716   3602   4146    318   -958   -450       C  
ATOM    256  O   VAL A  35     -17.544 -20.057  10.610  1.00 33.31           O  
ANISOU  256  O   VAL A  35     5444   3326   3886    325   -936   -410       O  
ATOM    257  CB  VAL A  35     -20.532 -20.900   9.950  1.00 34.75           C  
ANISOU  257  CB  VAL A  35     5720   3404   4081     36   -979   -298       C  
ATOM    258  CG1 VAL A  35     -20.930 -19.779   9.000  1.00 33.16           C  
ANISOU  258  CG1 VAL A  35     5368   3368   3863     34   -864   -300       C  
ATOM    259  CG2 VAL A  35     -21.596 -21.988   9.974  1.00 35.49           C  
ANISOU  259  CG2 VAL A  35     5933   3359   4193    -85  -1079   -268       C  
ATOM    260  N   VAL A  36     -17.786 -19.875   8.377  1.00 32.86           N  
ANISOU  260  N   VAL A  36     5287   3409   3791    390   -895   -521       N  
ATOM    261  CA  VAL A  36     -16.882 -18.740   8.233  1.00 32.54           C  
ANISOU  261  CA  VAL A  36     5111   3520   3733    459   -780   -539       C  
ATOM    262  C   VAL A  36     -17.711 -17.537   7.806  1.00 32.92           C  
ANISOU  262  C   VAL A  36     5055   3687   3766    365   -658   -457       C  
ATOM    263  O   VAL A  36     -18.367 -17.565   6.757  1.00 33.77           O  
ANISOU  263  O   VAL A  36     5150   3835   3846    344   -656   -471       O  
ATOM    264  CB  VAL A  36     -15.756 -19.025   7.227  1.00 33.15           C  
ANISOU  264  CB  VAL A  36     5148   3669   3779    614   -798   -685       C  
ATOM    265  CG1 VAL A  36     -14.977 -17.753   6.935  1.00 33.40           C  
ANISOU  265  CG1 VAL A  36     5028   3877   3786    648   -661   -689       C  
ATOM    266  CG2 VAL A  36     -14.831 -20.107   7.763  1.00 36.54           C  
ANISOU  266  CG2 VAL A  36     5664   3980   4237    728   -926   -775       C  
ATOM    267  N   TYR A  37     -17.688 -16.487   8.622  1.00 30.72           N  
ANISOU  267  N   TYR A  37     4705   3458   3508    314   -566   -376       N  
ATOM    268  CA  TYR A  37     -18.424 -15.259   8.355  1.00 31.19           C  
ANISOU  268  CA  TYR A  37     4667   3616   3568    236   -458   -298       C  
ATOM    269  C   TYR A  37     -17.482 -14.217   7.769  1.00 30.01           C  
ANISOU  269  C   TYR A  37     4406   3602   3395    303   -366   -325       C  
ATOM    270  O   TYR A  37     -16.365 -14.031   8.261  1.00 29.53           O  
ANISOU  270  O   TYR A  37     4315   3563   3343    368   -347   -361       O  
ATOM    271  CB  TYR A  37     -19.071 -14.712   9.631  1.00 29.77           C  
ANISOU  271  CB  TYR A  37     4478   3404   3428    133   -415   -200       C  
ATOM    272  CG  TYR A  37     -19.945 -15.697  10.380  1.00 31.28           C  
ANISOU  272  CG  TYR A  37     4779   3472   3636     42   -491   -162       C  
ATOM    273  CD1 TYR A  37     -19.387 -16.666  11.207  1.00 31.97           C  
ANISOU  273  CD1 TYR A  37     4978   3446   3723     67   -579   -179       C  
ATOM    274  CD2 TYR A  37     -21.329 -15.647  10.273  1.00 30.67           C  
ANISOU  274  CD2 TYR A  37     4692   3390   3572    -73   -480   -105       C  
ATOM    275  CE1 TYR A  37     -20.183 -17.563  11.896  1.00 31.49           C  
ANISOU  275  CE1 TYR A  37     5029   3267   3668    -34   -648   -129       C  
ATOM    276  CE2 TYR A  37     -22.132 -16.540  10.960  1.00 32.60           C  
ANISOU  276  CE2 TYR A  37     5029   3529   3827   -176   -539    -66       C  
ATOM    277  CZ  TYR A  37     -21.554 -17.495  11.769  1.00 32.84           C  
ANISOU  277  CZ  TYR A  37     5184   3445   3850   -163   -621    -72       C  
ATOM    278  OH  TYR A  37     -22.349 -18.385  12.453  1.00 33.56           O  
ANISOU  278  OH  TYR A  37     5380   3427   3945   -284   -681    -20       O  
ATOM    279  N   CYS A  38     -17.937 -13.532   6.724  1.00 30.13           N  
ANISOU  279  N   CYS A  38     4362   3708   3379    281   -312   -303       N  
ATOM    280  CA  CYS A  38     -17.121 -12.541   6.040  1.00 28.43           C  
ANISOU  280  CA  CYS A  38     4051   3623   3129    322   -223   -314       C  
ATOM    281  C   CYS A  38     -18.043 -11.591   5.288  1.00 27.87           C  
ANISOU  281  C   CYS A  38     3933   3614   3041    255   -173   -237       C  
ATOM    282  O   CYS A  38     -19.199 -11.938   5.011  1.00 29.21           O  
ANISOU  282  O   CYS A  38     4142   3742   3214    203   -222   -210       O  
ATOM    283  CB  CYS A  38     -16.124 -13.209   5.077  1.00 33.69           C  
ANISOU  283  CB  CYS A  38     4720   4348   3732    428   -246   -434       C  
ATOM    284  SG  CYS A  38     -16.857 -13.829   3.546  1.00 34.54           S  
ANISOU  284  SG  CYS A  38     4874   4487   3762    435   -296   -479       S  
ATOM    285  N   PRO A  39     -17.574 -10.387   4.958  1.00 27.88           N  
ANISOU  285  N   PRO A  39     3854   3712   3029    250    -84   -198       N  
ATOM    286  CA  PRO A  39     -18.405  -9.462   4.177  1.00 26.84           C  
ANISOU  286  CA  PRO A  39     3689   3629   2878    195    -53   -120       C  
ATOM    287  C   PRO A  39     -18.746 -10.044   2.812  1.00 28.83           C  
ANISOU  287  C   PRO A  39     3982   3927   3045    216    -99   -159       C  
ATOM    288  O   PRO A  39     -17.906 -10.658   2.150  1.00 29.35           O  
ANISOU  288  O   PRO A  39     4063   4047   3042    284   -104   -248       O  
ATOM    289  CB  PRO A  39     -17.528  -8.211   4.054  1.00 27.47           C  
ANISOU  289  CB  PRO A  39     3692   3795   2951    193     42    -82       C  
ATOM    290  CG  PRO A  39     -16.569  -8.304   5.193  1.00 25.68           C  
ANISOU  290  CG  PRO A  39     3442   3540   2774    222     64   -121       C  
ATOM    291  CD  PRO A  39     -16.305  -9.765   5.379  1.00 26.48           C  
ANISOU  291  CD  PRO A  39     3611   3589   2863    285    -15   -216       C  
ATOM    292  N   ARG A  40     -19.997  -9.839   2.391  1.00 25.38           N  
ANISOU  292  N   ARG A  40     3556   3473   2613    163   -136   -103       N  
ATOM    293  CA  ARG A  40     -20.486 -10.488   1.180  1.00 25.88           C  
ANISOU  293  CA  ARG A  40     3667   3566   2599    178   -200   -144       C  
ATOM    294  C   ARG A  40     -19.878  -9.908  -0.091  1.00 27.26           C  
ANISOU  294  C   ARG A  40     3825   3871   2663    205   -152   -144       C  
ATOM    295  O   ARG A  40     -19.928 -10.565  -1.136  1.00 27.77           O  
ANISOU  295  O   ARG A  40     3932   3981   2637    238   -196   -208       O  
ATOM    296  CB  ARG A  40     -22.012 -10.405   1.108  1.00 25.27           C  
ANISOU  296  CB  ARG A  40     3596   3440   2563    112   -260    -87       C  
ATOM    297  CG  ARG A  40     -22.570  -9.004   0.913  1.00 28.46           C  
ANISOU  297  CG  ARG A  40     3941   3884   2989     71   -222     17       C  
ATOM    298  CD  ARG A  40     -24.063  -9.055   0.628  1.00 26.11           C  
ANISOU  298  CD  ARG A  40     3640   3555   2724     24   -298     47       C  
ATOM    299  NE  ARG A  40     -24.693  -7.741   0.728  1.00 25.78           N  
ANISOU  299  NE  ARG A  40     3535   3523   2735     -6   -277    138       N  
ATOM    300  CZ  ARG A  40     -25.971  -7.504   0.449  1.00 28.44           C  
ANISOU  300  CZ  ARG A  40     3846   3848   3111    -37   -341    169       C  
ATOM    301  NH1 ARG A  40     -26.758  -8.493   0.048  1.00 29.23           N  
ANISOU  301  NH1 ARG A  40     3976   3931   3199    -54   -426    119       N  
ATOM    302  NH2 ARG A  40     -26.462  -6.278   0.568  1.00 28.70           N  
ANISOU  302  NH2 ARG A  40     3821   3882   3200    -48   -329    243       N  
ATOM    303  N   HIS A  41     -19.303  -8.706  -0.036  1.00 26.59           N  
ANISOU  303  N   HIS A  41     3681   3845   2576    186    -64    -76       N  
ATOM    304  CA  HIS A  41     -18.715  -8.114  -1.232  1.00 28.47           C  
ANISOU  304  CA  HIS A  41     3908   4211   2698    190    -10    -62       C  
ATOM    305  C   HIS A  41     -17.361  -8.720  -1.590  1.00 31.38           C  
ANISOU  305  C   HIS A  41     4264   4670   2989    256     37   -174       C  
ATOM    306  O   HIS A  41     -16.680  -8.195  -2.478  1.00 31.05           O  
ANISOU  306  O   HIS A  41     4199   4755   2845    250    106   -168       O  
ATOM    307  CB  HIS A  41     -18.599  -6.592  -1.079  1.00 27.82           C  
ANISOU  307  CB  HIS A  41     3775   4150   2644    133     61     59       C  
ATOM    308  CG  HIS A  41     -17.544  -6.146  -0.113  1.00 27.35           C  
ANISOU  308  CG  HIS A  41     3655   4087   2648    134    140     53       C  
ATOM    309  ND1 HIS A  41     -17.847  -5.622   1.125  1.00 28.32           N  
ANISOU  309  ND1 HIS A  41     3747   4117   2895    107    145    100       N  
ATOM    310  CD2 HIS A  41     -16.194  -6.116  -0.213  1.00 30.52           C  
ANISOU  310  CD2 HIS A  41     4014   4577   3006    158    216     -2       C  
ATOM    311  CE1 HIS A  41     -16.728  -5.305   1.753  1.00 27.51           C  
ANISOU  311  CE1 HIS A  41     3594   4037   2823    115    212     78       C  
ATOM    312  NE2 HIS A  41     -15.711  -5.595   0.962  1.00 26.98           N  
ANISOU  312  NE2 HIS A  41     3512   4078   2659    145    256     16       N  
ATOM    313  N   VAL A  42     -16.957  -9.806  -0.926  1.00 29.75           N  
ANISOU  313  N   VAL A  42     4072   4403   2828    317     -2   -279       N  
ATOM    314  CA  VAL A  42     -15.781 -10.553  -1.352  1.00 32.97           C  
ANISOU  314  CA  VAL A  42     4469   4893   3167    401     18   -414       C  
ATOM    315  C   VAL A  42     -16.007 -11.186  -2.719  1.00 34.76           C  
ANISOU  315  C   VAL A  42     4744   5198   3267    433    -20   -487       C  
ATOM    316  O   VAL A  42     -15.045 -11.445  -3.451  1.00 35.24           O  
ANISOU  316  O   VAL A  42     4778   5383   3230    489     27   -587       O  
ATOM    317  CB  VAL A  42     -15.411 -11.617  -0.292  1.00 33.62           C  
ANISOU  317  CB  VAL A  42     4572   4865   3337    467    -45   -506       C  
ATOM    318  CG1 VAL A  42     -16.468 -12.713  -0.232  1.00 30.28           C  
ANISOU  318  CG1 VAL A  42     4245   4318   2942    470   -168   -534       C  
ATOM    319  CG2 VAL A  42     -14.033 -12.205  -0.569  1.00 33.05           C  
ANISOU  319  CG2 VAL A  42     4461   4879   3218    568    -20   -652       C  
ATOM    320  N   ILE A  43     -17.268 -11.428  -3.089  1.00 29.22           N  
ANISOU  320  N   ILE A  43     4107   4434   2560    399   -104   -446       N  
ATOM    321  CA  ILE A  43     -17.592 -12.002  -4.394  1.00 30.69           C  
ANISOU  321  CA  ILE A  43     4348   4692   2623    425   -153   -514       C  
ATOM    322  C   ILE A  43     -17.613 -10.969  -5.506  1.00 32.73           C  
ANISOU  322  C   ILE A  43     4593   5090   2754    376    -89   -432       C  
ATOM    323  O   ILE A  43     -17.756 -11.339  -6.679  1.00 34.74           O  
ANISOU  323  O   ILE A  43     4891   5432   2877    396   -117   -488       O  
ATOM    324  CB  ILE A  43     -18.959 -12.709  -4.353  1.00 31.99           C  
ANISOU  324  CB  ILE A  43     4584   4733   2837    401   -281   -508       C  
ATOM    325  CG1 ILE A  43     -20.087 -11.675  -4.289  1.00 28.34           C  
ANISOU  325  CG1 ILE A  43     4109   4245   2415    310   -288   -355       C  
ATOM    326  CG2 ILE A  43     -19.034 -13.657  -3.166  1.00 30.30           C  
ANISOU  326  CG2 ILE A  43     4398   4365   2750    422   -346   -558       C  
ATOM    327  CD1 ILE A  43     -21.471 -12.278  -4.207  1.00 29.04           C  
ANISOU  327  CD1 ILE A  43     4243   4227   2563    275   -406   -349       C  
ATOM    328  N   CYS A  44     -17.475  -9.688  -5.176  1.00 32.86           N  
ANISOU  328  N   CYS A  44     4558   5126   2801    310    -10   -302       N  
ATOM    329  CA  CYS A  44     -17.590  -8.618  -6.155  1.00 35.48           C  
ANISOU  329  CA  CYS A  44     4896   5564   3022    248     37   -196       C  
ATOM    330  C   CYS A  44     -16.241  -8.304  -6.786  1.00 39.12           C  
ANISOU  330  C   CYS A  44     5312   6194   3359    252    158   -236       C  
ATOM    331  O   CYS A  44     -15.214  -8.263  -6.102  1.00 37.94           O  
ANISOU  331  O   CYS A  44     5091   6062   3264    272    233   -282       O  
ATOM    332  CB  CYS A  44     -18.153  -7.355  -5.502  1.00 35.85           C  
ANISOU  332  CB  CYS A  44     4918   5531   3171    172     50    -34       C  
ATOM    333  SG  CYS A  44     -19.890  -7.449  -5.022  1.00 33.96           S  
ANISOU  333  SG  CYS A  44     4714   5138   3052    150    -80     27       S  
ATOM    334  N   THR A  45     -16.253  -8.093  -8.099  1.00 42.64           N  
ANISOU  334  N   THR A  45     5796   6772   3633    228    176   -221       N  
ATOM    335  CA  THR A  45     -15.128  -7.460  -8.762  1.00 43.88           C  
ANISOU  335  CA  THR A  45     5910   7104   3659    190    308   -212       C  
ATOM    336  C   THR A  45     -15.162  -5.959  -8.486  1.00 45.25           C  
ANISOU  336  C   THR A  45     6065   7253   3874     84    364    -25       C  
ATOM    337  O   THR A  45     -16.140  -5.422  -7.961  1.00 42.74           O  
ANISOU  337  O   THR A  45     5776   6796   3668     52    292     88       O  
ATOM    338  CB  THR A  45     -15.163  -7.733 -10.266  1.00 45.21           C  
ANISOU  338  CB  THR A  45     6137   7429   3610    191    309   -253       C  
ATOM    339  OG1 THR A  45     -16.267  -7.034 -10.856  1.00 43.71           O  
ANISOU  339  OG1 THR A  45     6030   7205   3372    124    238   -103       O  
ATOM    340  CG2 THR A  45     -15.316  -9.225 -10.536  1.00 46.14           C  
ANISOU  340  CG2 THR A  45     6287   7542   3702    300    227   -442       C  
ATOM    341  N   SER A  46     -14.073  -5.272  -8.839  1.00 60.17           N  
ANISOU  341  N   SER A  46     7904   9280   5678     25    494      2       N  
ATOM    342  CA  SER A  46     -14.052  -3.820  -8.683  1.00 59.01           C  
ANISOU  342  CA  SER A  46     7752   9106   5562    -86    542    182       C  
ATOM    343  C   SER A  46     -15.170  -3.155  -9.477  1.00 59.06           C  
ANISOU  343  C   SER A  46     7865   9078   5497   -143    461    332       C  
ATOM    344  O   SER A  46     -15.622  -2.062  -9.117  1.00 61.60           O  
ANISOU  344  O   SER A  46     8205   9298   5904   -208    438    484       O  
ATOM    345  CB  SER A  46     -12.691  -3.265  -9.103  1.00 60.09           C  
ANISOU  345  CB  SER A  46     7821   9416   5594   -157    697    183       C  
ATOM    346  OG  SER A  46     -12.823  -1.967  -9.654  1.00 66.07           O  
ANISOU  346  OG  SER A  46     8628  10192   6282   -284    729    369       O  
ATOM    347  N   GLU A  47     -15.630  -3.800 -10.552  1.00 47.30           N  
ANISOU  347  N   GLU A  47     6447   7668   3856   -112    406    285       N  
ATOM    348  CA  GLU A  47     -16.746  -3.272 -11.328  1.00 48.20           C  
ANISOU  348  CA  GLU A  47     6665   7747   3900   -152    305    415       C  
ATOM    349  C   GLU A  47     -18.083  -3.568 -10.660  1.00 45.98           C  
ANISOU  349  C   GLU A  47     6404   7284   3782    -98    159    422       C  
ATOM    350  O   GLU A  47     -18.994  -2.732 -10.691  1.00 45.92           O  
ANISOU  350  O   GLU A  47     6440   7184   3822   -135     79    560       O  
ATOM    351  CB  GLU A  47     -16.713  -3.854 -12.741  1.00 51.72           C  
ANISOU  351  CB  GLU A  47     7181   8359   4111   -141    299    354       C  
ATOM    352  CG  GLU A  47     -17.931  -3.545 -13.589  1.00 56.61           C  
ANISOU  352  CG  GLU A  47     7914   8946   4649   -161    167    460       C  
ATOM    353  CD  GLU A  47     -17.588  -3.429 -15.059  1.00 62.11           C  
ANISOU  353  CD  GLU A  47     8689   9837   5072   -210    207    483       C  
ATOM    354  OE1 GLU A  47     -16.458  -2.999 -15.370  1.00 65.78           O  
ANISOU  354  OE1 GLU A  47     9125  10445   5425   -280    354    501       O  
ATOM    355  OE2 GLU A  47     -18.442  -3.775 -15.901  1.00 62.15           O  
ANISOU  355  OE2 GLU A  47     8783   9861   4971   -185     93    480       O  
ATOM    356  N   ASP A  48     -18.219  -4.750 -10.052  1.00 40.71           N  
ANISOU  356  N   ASP A  48     5702   6562   3202    -14    120    274       N  
ATOM    357  CA  ASP A  48     -19.465  -5.099  -9.376  1.00 41.43           C  
ANISOU  357  CA  ASP A  48     5802   6492   3445     21     -6    274       C  
ATOM    358  C   ASP A  48     -19.767  -4.148  -8.224  1.00 38.22           C  
ANISOU  358  C   ASP A  48     5349   5952   3222    -14     -2    381       C  
ATOM    359  O   ASP A  48     -20.938  -3.925  -7.899  1.00 38.15           O  
ANISOU  359  O   ASP A  48     5349   5831   3315    -14   -101    435       O  
ATOM    360  CB  ASP A  48     -19.403  -6.540  -8.864  1.00 40.31           C  
ANISOU  360  CB  ASP A  48     5640   6313   3362    102    -38    103       C  
ATOM    361  CG  ASP A  48     -19.250  -7.553  -9.983  1.00 43.01           C  
ANISOU  361  CG  ASP A  48     6035   6769   3539    151    -66    -23       C  
ATOM    362  OD1 ASP A  48     -19.719  -7.278 -11.107  1.00 44.21           O  
ANISOU  362  OD1 ASP A  48     6252   6996   3550    125   -109     28       O  
ATOM    363  OD2 ASP A  48     -18.662  -8.627  -9.736  1.00 42.46           O  
ANISOU  363  OD2 ASP A  48     5945   6710   3480    219    -54   -177       O  
ATOM    364  N   MET A  49     -18.729  -3.578  -7.605  1.00 43.23           N  
ANISOU  364  N   MET A  49     5923   6601   3900    -44    111    402       N  
ATOM    365  CA  MET A  49     -18.917  -2.737  -6.425  1.00 41.26           C  
ANISOU  365  CA  MET A  49     5625   6225   3827    -70    118    479       C  
ATOM    366  C   MET A  49     -19.814  -1.536  -6.705  1.00 40.20           C  
ANISOU  366  C   MET A  49     5532   6022   3720   -119     53    635       C  
ATOM    367  O   MET A  49     -20.496  -1.049  -5.795  1.00 37.06           O  
ANISOU  367  O   MET A  49     5103   5498   3481   -116      8    677       O  
ATOM    368  CB  MET A  49     -17.561  -2.260  -5.902  1.00 40.24           C  
ANISOU  368  CB  MET A  49     5429   6142   3718   -102    247    475       C  
ATOM    369  CG  MET A  49     -16.595  -3.374  -5.540  1.00 44.01           C  
ANISOU  369  CG  MET A  49     5855   6682   4187    -41    304    315       C  
ATOM    370  SD  MET A  49     -17.069  -4.241  -4.035  1.00 44.71           S  
ANISOU  370  SD  MET A  49     5912   6617   4460     28    240    228       S  
ATOM    371  CE  MET A  49     -15.548  -5.107  -3.654  1.00 39.45           C  
ANISOU  371  CE  MET A  49     5181   6032   3777     88    321     73       C  
ATOM    372  N   LEU A  50     -19.829  -1.047  -7.947  1.00 37.35           N  
ANISOU  372  N   LEU A  50     5242   5745   3204   -161     41    719       N  
ATOM    373  CA  LEU A  50     -20.537   0.196  -8.241  1.00 38.42           C  
ANISOU  373  CA  LEU A  50     5428   5808   3362   -208    -28    879       C  
ATOM    374  C   LEU A  50     -22.050   0.022  -8.148  1.00 35.70           C  
ANISOU  374  C   LEU A  50     5098   5361   3107   -157   -178    883       C  
ATOM    375  O   LEU A  50     -22.757   0.932  -7.701  1.00 38.13           O  
ANISOU  375  O   LEU A  50     5396   5553   3538   -162   -241    970       O  
ATOM    376  CB  LEU A  50     -20.134   0.712  -9.622  1.00 42.02           C  
ANISOU  376  CB  LEU A  50     5972   6384   3610   -273     -7    976       C  
ATOM    377  CG  LEU A  50     -18.628   0.778  -9.892  1.00 44.39           C  
ANISOU  377  CG  LEU A  50     6248   6826   3793   -334    152    957       C  
ATOM    378  CD1 LEU A  50     -18.348   1.182 -11.334  1.00 46.64           C  
ANISOU  378  CD1 LEU A  50     6628   7247   3844   -408    172   1050       C  
ATOM    379  CD2 LEU A  50     -17.951   1.731  -8.918  1.00 43.45           C  
ANISOU  379  CD2 LEU A  50     6066   6634   3811   -388    232   1019       C  
ATOM    380  N   ASN A  51     -22.569  -1.134  -8.564  1.00 37.70           N  
ANISOU  380  N   ASN A  51     5367   5654   3304   -107   -240    780       N  
ATOM    381  CA  ASN A  51     -24.003  -1.392  -8.484  1.00 37.93           C  
ANISOU  381  CA  ASN A  51     5395   5599   3420    -67   -380    769       C  
ATOM    382  C   ASN A  51     -24.262  -2.893  -8.437  1.00 40.86           C  
ANISOU  382  C   ASN A  51     5752   5992   3780    -21   -410    617       C  
ATOM    383  O   ASN A  51     -24.719  -3.478  -9.427  1.00 40.53           O  
ANISOU  383  O   ASN A  51     5767   6010   3622     -3   -488    581       O  
ATOM    384  CB  ASN A  51     -24.734  -0.761  -9.671  1.00 43.99           C  
ANISOU  384  CB  ASN A  51     6246   6386   4082    -79   -492    875       C  
ATOM    385  CG  ASN A  51     -26.230  -0.663  -9.446  1.00 45.55           C  
ANISOU  385  CG  ASN A  51     6418   6482   4409    -41   -640    883       C  
ATOM    386  OD1 ASN A  51     -26.713  -0.839  -8.326  1.00 45.61           O  
ANISOU  386  OD1 ASN A  51     6338   6399   4591    -19   -644    830       O  
ATOM    387  ND2 ASN A  51     -26.972  -0.377 -10.509  1.00 52.18           N  
ANISOU  387  ND2 ASN A  51     7328   7342   5156    -34   -765    947       N  
ATOM    388  N   PRO A  52     -23.996  -3.547  -7.306  1.00 33.39           N  
ANISOU  388  N   PRO A  52     4742   4993   2952     -2   -359    527       N  
ATOM    389  CA  PRO A  52     -24.060  -5.012  -7.258  1.00 31.67           C  
ANISOU  389  CA  PRO A  52     4528   4786   2719     37   -385    384       C  
ATOM    390  C   PRO A  52     -25.444  -5.562  -6.951  1.00 33.36           C  
ANISOU  390  C   PRO A  52     4724   4915   3038     46   -504    350       C  
ATOM    391  O   PRO A  52     -26.169  -5.069  -6.085  1.00 33.48           O  
ANISOU  391  O   PRO A  52     4681   4840   3201     31   -526    392       O  
ATOM    392  CB  PRO A  52     -23.084  -5.351  -6.124  1.00 32.22           C  
ANISOU  392  CB  PRO A  52     4545   4828   2870     46   -281    322       C  
ATOM    393  CG  PRO A  52     -23.188  -4.180  -5.197  1.00 30.47           C  
ANISOU  393  CG  PRO A  52     4268   4529   2779     14   -245    421       C  
ATOM    394  CD  PRO A  52     -23.532  -2.969  -6.032  1.00 33.73           C  
ANISOU  394  CD  PRO A  52     4716   4963   3137    -17   -278    551       C  
ATOM    395  N   ASN A  53     -25.804  -6.611  -7.688  1.00 33.04           N  
ANISOU  395  N   ASN A  53     4730   4910   2915     67   -579    261       N  
ATOM    396  CA  ASN A  53     -26.960  -7.450  -7.377  1.00 33.06           C  
ANISOU  396  CA  ASN A  53     4713   4837   3011     66   -684    197       C  
ATOM    397  C   ASN A  53     -26.397  -8.706  -6.721  1.00 30.99           C  
ANISOU  397  C   ASN A  53     4454   4540   2780     81   -648     76       C  
ATOM    398  O   ASN A  53     -26.048  -9.678  -7.392  1.00 33.03           O  
ANISOU  398  O   ASN A  53     4769   4842   2938    113   -675    -23       O  
ATOM    399  CB  ASN A  53     -27.771  -7.765  -8.630  1.00 35.43           C  
ANISOU  399  CB  ASN A  53     5066   5187   3207     75   -808    178       C  
ATOM    400  CG  ASN A  53     -29.105  -8.421  -8.317  1.00 34.31           C  
ANISOU  400  CG  ASN A  53     4887   4968   3180     58   -924    128       C  
ATOM    401  OD1 ASN A  53     -29.180  -9.367  -7.533  1.00 36.93           O  
ANISOU  401  OD1 ASN A  53     5198   5235   3598     44   -918     46       O  
ATOM    402  ND2 ASN A  53     -30.168  -7.919  -8.936  1.00 37.82           N  
ANISOU  402  ND2 ASN A  53     5323   5422   3625     54  -1036    177       N  
ATOM    403  N   TYR A  54     -26.302  -8.675  -5.388  1.00 32.46           N  
ANISOU  403  N   TYR A  54     4585   4643   3105     63   -594     83       N  
ATOM    404  CA  TYR A  54     -25.607  -9.736  -4.664  1.00 32.39           C  
ANISOU  404  CA  TYR A  54     4590   4591   3126     81   -559    -13       C  
ATOM    405  C   TYR A  54     -26.273 -11.092  -4.857  1.00 32.54           C  
ANISOU  405  C   TYR A  54     4653   4560   3151     78   -663   -113       C  
ATOM    406  O   TYR A  54     -25.594 -12.124  -4.829  1.00 32.96           O  
ANISOU  406  O   TYR A  54     4754   4598   3173    114   -665   -212       O  
ATOM    407  CB  TYR A  54     -25.529  -9.391  -3.177  1.00 29.89           C  
ANISOU  407  CB  TYR A  54     4214   4194   2951     52   -496     25       C  
ATOM    408  CG  TYR A  54     -24.488  -8.346  -2.853  1.00 28.91           C  
ANISOU  408  CG  TYR A  54     4057   4108   2819     63   -385     86       C  
ATOM    409  CD1 TYR A  54     -23.148  -8.688  -2.731  1.00 29.05           C  
ANISOU  409  CD1 TYR A  54     4088   4163   2786    102   -312     30       C  
ATOM    410  CD2 TYR A  54     -24.844  -7.016  -2.673  1.00 30.89           C  
ANISOU  410  CD2 TYR A  54     4260   4355   3121     36   -361    193       C  
ATOM    411  CE1 TYR A  54     -22.193  -7.736  -2.434  1.00 26.42           C  
ANISOU  411  CE1 TYR A  54     3716   3870   2453    101   -212     81       C  
ATOM    412  CE2 TYR A  54     -23.896  -6.057  -2.375  1.00 28.75           C  
ANISOU  412  CE2 TYR A  54     3964   4110   2852     35   -266    249       C  
ATOM    413  CZ  TYR A  54     -22.572  -6.422  -2.258  1.00 27.57           C  
ANISOU  413  CZ  TYR A  54     3822   4004   2649     62   -188    194       C  
ATOM    414  OH  TYR A  54     -21.623  -5.470  -1.964  1.00 29.16           O  
ANISOU  414  OH  TYR A  54     3988   4235   2856     51    -95    245       O  
ATOM    415  N   GLU A  55     -27.593 -11.114  -5.051  1.00 34.32           N  
ANISOU  415  N   GLU A  55     4860   4754   3425     37   -757    -93       N  
ATOM    416  CA  GLU A  55     -28.273 -12.379  -5.304  1.00 37.19           C  
ANISOU  416  CA  GLU A  55     5265   5069   3797     20   -864   -187       C  
ATOM    417  C   GLU A  55     -27.834 -12.982  -6.633  1.00 37.91           C  
ANISOU  417  C   GLU A  55     5437   5236   3733     76   -913   -272       C  
ATOM    418  O   GLU A  55     -27.577 -14.189  -6.718  1.00 37.06           O  
ANISOU  418  O   GLU A  55     5387   5087   3607     96   -958   -384       O  
ATOM    419  CB  GLU A  55     -29.788 -12.175  -5.277  1.00 38.67           C  
ANISOU  419  CB  GLU A  55     5396   5227   4071    -41   -952   -151       C  
ATOM    420  CG  GLU A  55     -30.366 -11.980  -3.883  1.00 37.71           C  
ANISOU  420  CG  GLU A  55     5195   5027   4108   -106   -914   -109       C  
ATOM    421  CD  GLU A  55     -30.102 -10.596  -3.324  1.00 41.20           C  
ANISOU  421  CD  GLU A  55     5569   5491   4592    -94   -822    -10       C  
ATOM    422  OE1 GLU A  55     -29.833  -9.672  -4.121  1.00 40.21           O  
ANISOU  422  OE1 GLU A  55     5451   5435   4393    -53   -814     45       O  
ATOM    423  OE2 GLU A  55     -30.162 -10.432  -2.088  1.00 46.95           O  
ANISOU  423  OE2 GLU A  55     6247   6168   5426   -132   -759     12       O  
ATOM    424  N   ASP A  56     -27.731 -12.157  -7.677  1.00 33.90           N  
ANISOU  424  N   ASP A  56     4939   4836   3106    100   -909   -222       N  
ATOM    425  CA  ASP A  56     -27.292 -12.658  -8.975  1.00 35.76           C  
ANISOU  425  CA  ASP A  56     5250   5166   3170    150   -945   -304       C  
ATOM    426  C   ASP A  56     -25.811 -13.014  -8.960  1.00 37.06           C  
ANISOU  426  C   ASP A  56     5441   5382   3257    208   -844   -377       C  
ATOM    427  O   ASP A  56     -25.396 -13.998  -9.585  1.00 39.06           O  
ANISOU  427  O   ASP A  56     5753   5666   3422    259   -879   -507       O  
ATOM    428  CB  ASP A  56     -27.579 -11.623 -10.062  1.00 39.69           C  
ANISOU  428  CB  ASP A  56     5760   5771   3548    148   -965   -215       C  
ATOM    429  CG  ASP A  56     -29.060 -11.451 -10.325  1.00 42.49           C  
ANISOU  429  CG  ASP A  56     6094   6089   3961    112  -1097   -177       C  
ATOM    430  OD1 ASP A  56     -29.852 -12.286  -9.843  1.00 42.14           O  
ANISOU  430  OD1 ASP A  56     6029   5956   4028     82  -1173   -240       O  
ATOM    431  OD2 ASP A  56     -29.431 -10.477 -11.013  1.00 42.32           O  
ANISOU  431  OD2 ASP A  56     6078   6128   3876    110  -1130    -82       O  
ATOM    432  N   LEU A  57     -24.997 -12.224  -8.256  1.00 33.96           N  
ANISOU  432  N   LEU A  57     5000   5001   2901    207   -723   -307       N  
ATOM    433  CA  LEU A  57     -23.564 -12.496  -8.201  1.00 35.37           C  
ANISOU  433  CA  LEU A  57     5182   5239   3017    263   -625   -380       C  
ATOM    434  C   LEU A  57     -23.273 -13.784  -7.441  1.00 35.25           C  
ANISOU  434  C   LEU A  57     5188   5119   3088    300   -659   -502       C  
ATOM    435  O   LEU A  57     -22.424 -14.580  -7.858  1.00 36.70           O  
ANISOU  435  O   LEU A  57     5405   5345   3195    372   -654   -631       O  
ATOM    436  CB  LEU A  57     -22.830 -11.319  -7.561  1.00 36.11           C  
ANISOU  436  CB  LEU A  57     5212   5360   3147    241   -498   -274       C  
ATOM    437  CG  LEU A  57     -22.827 -10.000  -8.338  1.00 35.65           C  
ANISOU  437  CG  LEU A  57     5149   5405   2993    205   -454   -150       C  
ATOM    438  CD1 LEU A  57     -22.205  -8.890  -7.506  1.00 34.93           C  
ANISOU  438  CD1 LEU A  57     4994   5302   2975    174   -344    -47       C  
ATOM    439  CD2 LEU A  57     -22.094 -10.155  -9.660  1.00 39.59           C  
ANISOU  439  CD2 LEU A  57     5693   6062   3286    236   -422   -209       C  
ATOM    440  N   LEU A  58     -23.967 -14.006  -6.321  1.00 31.98           N  
ANISOU  440  N   LEU A  58     4756   4566   2829    252   -697   -465       N  
ATOM    441  CA  LEU A  58     -23.732 -15.207  -5.526  1.00 32.81           C  
ANISOU  441  CA  LEU A  58     4898   4552   3016    274   -740   -558       C  
ATOM    442  C   LEU A  58     -24.178 -16.467  -6.256  1.00 34.28           C  
ANISOU  442  C   LEU A  58     5163   4699   3162    297   -866   -682       C  
ATOM    443  O   LEU A  58     -23.614 -17.544  -6.030  1.00 37.34           O  
ANISOU  443  O   LEU A  58     5603   5018   3566    352   -906   -797       O  
ATOM    444  CB  LEU A  58     -24.449 -15.090  -4.180  1.00 35.39           C  
ANISOU  444  CB  LEU A  58     5192   4754   3501    197   -746   -475       C  
ATOM    445  CG  LEU A  58     -24.226 -16.214  -3.166  1.00 32.39           C  
ANISOU  445  CG  LEU A  58     4860   4236   3211    199   -787   -537       C  
ATOM    446  CD1 LEU A  58     -22.743 -16.401  -2.889  1.00 32.30           C  
ANISOU  446  CD1 LEU A  58     4855   4246   3170    289   -725   -602       C  
ATOM    447  CD2 LEU A  58     -24.986 -15.934  -1.879  1.00 33.08           C  
ANISOU  447  CD2 LEU A  58     4910   4229   3428    105   -774   -440       C  
ATOM    448  N   ILE A  59     -25.179 -16.356  -7.132  1.00 35.82           N  
ANISOU  448  N   ILE A  59     5371   4931   3310    262   -941   -667       N  
ATOM    449  CA  ILE A  59     -25.681 -17.529  -7.843  1.00 41.33           C  
ANISOU  449  CA  ILE A  59     6143   5587   3974    276  -1072   -789       C  
ATOM    450  C   ILE A  59     -24.614 -18.087  -8.778  1.00 41.30           C  
ANISOU  450  C   ILE A  59     6190   5674   3827    382  -1063   -931       C  
ATOM    451  O   ILE A  59     -24.449 -19.308  -8.896  1.00 44.86           O  
ANISOU  451  O   ILE A  59     6708   6051   4284    430  -1147  -1070       O  
ATOM    452  CB  ILE A  59     -26.978 -17.177  -8.594  1.00 41.85           C  
ANISOU  452  CB  ILE A  59     6198   5686   4015    216  -1157   -740       C  
ATOM    453  CG1 ILE A  59     -28.165 -17.190  -7.629  1.00 40.83           C  
ANISOU  453  CG1 ILE A  59     6025   5436   4051    114  -1204   -664       C  
ATOM    454  CG2 ILE A  59     -27.223 -18.142  -9.745  1.00 41.17           C  
ANISOU  454  CG2 ILE A  59     6192   5622   3830    253  -1275   -877       C  
ATOM    455  CD1 ILE A  59     -29.455 -16.701  -8.244  1.00 41.11           C  
ANISOU  455  CD1 ILE A  59     6022   5510   4087     59  -1285   -612       C  
ATOM    456  N   ARG A  60     -23.858 -17.209  -9.441  1.00 51.40           N  
ANISOU  456  N   ARG A  60     7438   7116   4976    420   -959   -903       N  
ATOM    457  CA  ARG A  60     -22.790 -17.661 -10.323  1.00 55.54           C  
ANISOU  457  CA  ARG A  60     7992   7758   5354    518   -928  -1045       C  
ATOM    458  C   ARG A  60     -21.614 -18.268  -9.569  1.00 55.71           C  
ANISOU  458  C   ARG A  60     8001   7732   5432    596   -880  -1141       C  
ATOM    459  O   ARG A  60     -20.702 -18.802 -10.208  1.00 54.69           O  
ANISOU  459  O   ARG A  60     7888   7691   5202    691   -862  -1290       O  
ATOM    460  CB  ARG A  60     -22.297 -16.501 -11.191  1.00 54.62           C  
ANISOU  460  CB  ARG A  60     7840   7837   5076    514   -817   -973       C  
ATOM    461  CG  ARG A  60     -23.397 -15.558 -11.653  1.00 57.76           C  
ANISOU  461  CG  ARG A  60     8236   8264   5444    432   -853   -826       C  
ATOM    462  CD  ARG A  60     -22.857 -14.497 -12.598  1.00 59.83           C  
ANISOU  462  CD  ARG A  60     8491   8713   5529    425   -757   -755       C  
ATOM    463  NE  ARG A  60     -21.645 -13.869 -12.083  1.00 63.71           N  
ANISOU  463  NE  ARG A  60     8920   9264   6024    434   -604   -719       N  
ATOM    464  CZ  ARG A  60     -21.383 -12.568 -12.166  1.00 64.03           C  
ANISOU  464  CZ  ARG A  60     8925   9384   6020    378   -508   -572       C  
ATOM    465  NH1 ARG A  60     -20.252 -12.085 -11.669  1.00 64.39           N  
ANISOU  465  NH1 ARG A  60     8909   9479   6078    382   -374   -554       N  
ATOM    466  NH2 ARG A  60     -22.251 -11.751 -12.746  1.00 62.77           N  
ANISOU  466  NH2 ARG A  60     8795   9247   5809    320   -557   -443       N  
ATOM    467  N   LYS A  61     -21.610 -18.203  -8.240  1.00 45.89           N  
ANISOU  467  N   LYS A  61     6731   6360   4345    562   -862  -1068       N  
ATOM    468  CA  LYS A  61     -20.516 -18.737  -7.442  1.00 46.24           C  
ANISOU  468  CA  LYS A  61     6768   6350   4453    637   -832  -1149       C  
ATOM    469  C   LYS A  61     -20.819 -20.161  -6.996  1.00 45.91           C  
ANISOU  469  C   LYS A  61     6814   6124   4507    664   -974  -1254       C  
ATOM    470  O   LYS A  61     -21.931 -20.468  -6.559  1.00 49.18           O  
ANISOU  470  O   LYS A  61     7268   6406   5013    577  -1061  -1192       O  
ATOM    471  CB  LYS A  61     -20.260 -17.856  -6.218  1.00 43.53           C  
ANISOU  471  CB  LYS A  61     6354   5970   4214    587   -738  -1011       C  
ATOM    472  CG  LYS A  61     -19.819 -16.441  -6.551  1.00 45.56           C  
ANISOU  472  CG  LYS A  61     6529   6388   4393    559   -600   -908       C  
ATOM    473  CD  LYS A  61     -18.508 -16.443  -7.319  1.00 44.95           C  
ANISOU  473  CD  LYS A  61     6420   6474   4186    648   -516  -1020       C  
ATOM    474  CE  LYS A  61     -18.097 -15.033  -7.706  1.00 46.44           C  
ANISOU  474  CE  LYS A  61     6537   6820   4290    598   -380   -905       C  
ATOM    475  NZ  LYS A  61     -16.839 -15.015  -8.503  1.00 49.85           N  
ANISOU  475  NZ  LYS A  61     6926   7433   4581    665   -284  -1014       N  
ATOM    476  N   SER A  62     -19.821 -21.028  -7.113  1.00 51.25           N  
ANISOU  476  N   SER A  62     7518   6791   5163    784   -999  -1417       N  
ATOM    477  CA  SER A  62     -19.869 -22.380  -6.579  1.00 52.24           C  
ANISOU  477  CA  SER A  62     7736   6722   5389    825  -1137  -1520       C  
ATOM    478  C   SER A  62     -19.044 -22.437  -5.298  1.00 50.84           C  
ANISOU  478  C   SER A  62     7540   6457   5319    860  -1107  -1496       C  
ATOM    479  O   SER A  62     -18.478 -21.436  -4.848  1.00 53.12           O  
ANISOU  479  O   SER A  62     7739   6838   5606    849   -979  -1408       O  
ATOM    480  CB  SER A  62     -19.364 -23.391  -7.613  1.00 56.17           C  
ANISOU  480  CB  SER A  62     8288   7254   5799    952  -1216  -1738       C  
ATOM    481  OG  SER A  62     -20.146 -23.346  -8.795  1.00 59.21           O  
ANISOU  481  OG  SER A  62     8697   7724   6075    918  -1252  -1762       O  
ATOM    482  N   ASN A  63     -18.983 -23.627  -4.699  1.00 48.10           N  
ANISOU  482  N   ASN A  63     7289   5920   5068    900  -1236  -1574       N  
ATOM    483  CA  ASN A  63     -18.211 -23.788  -3.471  1.00 45.95           C  
ANISOU  483  CA  ASN A  63     7018   5549   4894    940  -1234  -1556       C  
ATOM    484  C   ASN A  63     -16.717 -23.637  -3.729  1.00 48.25           C  
ANISOU  484  C   ASN A  63     7230   5974   5130   1092  -1159  -1682       C  
ATOM    485  O   ASN A  63     -15.993 -23.073  -2.899  1.00 46.15           O  
ANISOU  485  O   ASN A  63     6898   5732   4905   1106  -1081  -1626       O  
ATOM    486  CB  ASN A  63     -18.509 -25.143  -2.832  1.00 48.25           C  
ANISOU  486  CB  ASN A  63     7448   5592   5291    946  -1408  -1605       C  
ATOM    487  CG  ASN A  63     -19.818 -25.152  -2.073  1.00 47.88           C  
ANISOU  487  CG  ASN A  63     7456   5408   5328    771  -1451  -1443       C  
ATOM    488  OD1 ASN A  63     -20.287 -24.113  -1.608  1.00 44.91           O  
ANISOU  488  OD1 ASN A  63     7004   5098   4961    664  -1344  -1287       O  
ATOM    489  ND2 ASN A  63     -20.411 -26.331  -1.932  1.00 45.54           N  
ANISOU  489  ND2 ASN A  63     7290   4918   5097    737  -1608  -1484       N  
ATOM    490  N   HIS A  64     -16.237 -24.126  -4.875  1.00 47.20           N  
ANISOU  490  N   HIS A  64     7096   5938   4900   1204  -1180  -1862       N  
ATOM    491  CA  HIS A  64     -14.806 -24.119  -5.156  1.00 47.66           C  
ANISOU  491  CA  HIS A  64     7069   6131   4907   1355  -1115  -2013       C  
ATOM    492  C   HIS A  64     -14.263 -22.731  -5.471  1.00 49.07           C  
ANISOU  492  C   HIS A  64     7104   6548   4992   1319   -919  -1935       C  
ATOM    493  O   HIS A  64     -13.045 -22.583  -5.617  1.00 47.34           O  
ANISOU  493  O   HIS A  64     6791   6461   4735   1423   -842  -2044       O  
ATOM    494  CB  HIS A  64     -14.493 -25.075  -6.310  1.00 49.07           C  
ANISOU  494  CB  HIS A  64     7286   6355   5004   1486  -1192  -2243       C  
ATOM    495  CG  HIS A  64     -15.039 -24.633  -7.633  1.00 51.67           C  
ANISOU  495  CG  HIS A  64     7597   6858   5178   1436  -1132  -2250       C  
ATOM    496  ND1 HIS A  64     -14.414 -23.691  -8.421  1.00 53.30           N  
ANISOU  496  ND1 HIS A  64     7687   7325   5238   1444   -968  -2258       N  
ATOM    497  CD2 HIS A  64     -16.150 -25.011  -8.309  1.00 50.38           C  
ANISOU  497  CD2 HIS A  64     7522   6645   4976   1373  -1223  -2247       C  
ATOM    498  CE1 HIS A  64     -15.117 -23.504  -9.523  1.00 53.99           C  
ANISOU  498  CE1 HIS A  64     7803   7514   5198   1392   -962  -2254       C  
ATOM    499  NE2 HIS A  64     -16.176 -24.293  -9.480  1.00 54.24           N  
ANISOU  499  NE2 HIS A  64     7953   7363   5294   1353  -1118  -2252       N  
ATOM    500  N   ASN A  65     -15.121 -21.718  -5.583  1.00 45.23           N  
ANISOU  500  N   ASN A  65     6596   6117   4471   1176   -842  -1755       N  
ATOM    501  CA  ASN A  65     -14.665 -20.356  -5.828  1.00 46.83           C  
ANISOU  501  CA  ASN A  65     6680   6519   4596   1126   -669  -1660       C  
ATOM    502  C   ASN A  65     -14.196 -19.651  -4.562  1.00 44.87           C  
ANISOU  502  C   ASN A  65     6366   6231   4452   1090   -600  -1545       C  
ATOM    503  O   ASN A  65     -13.706 -18.520  -4.649  1.00 42.11           O  
ANISOU  503  O   ASN A  65     5916   6029   4055   1049   -460  -1470       O  
ATOM    504  CB  ASN A  65     -15.780 -19.537  -6.487  1.00 45.51           C  
ANISOU  504  CB  ASN A  65     6524   6415   4354    997   -633  -1516       C  
ATOM    505  CG  ASN A  65     -16.053 -19.966  -7.916  1.00 49.61           C  
ANISOU  505  CG  ASN A  65     7086   7038   4727   1031   -669  -1629       C  
ATOM    506  OD1 ASN A  65     -17.201 -20.194  -8.299  1.00 47.40           O  
ANISOU  506  OD1 ASN A  65     6880   6692   4439    969   -758  -1588       O  
ATOM    507  ND2 ASN A  65     -14.998 -20.076  -8.714  1.00 49.58           N  
ANISOU  507  ND2 ASN A  65     7028   7206   4604   1130   -601  -1779       N  
ATOM    508  N   PHE A  66     -14.330 -20.287  -3.398  1.00 43.94           N  
ANISOU  508  N   PHE A  66     6310   5915   4470   1100   -698  -1528       N  
ATOM    509  CA  PHE A  66     -13.952 -19.699  -2.116  1.00 45.46           C  
ANISOU  509  CA  PHE A  66     6456   6057   4760   1066   -651  -1422       C  
ATOM    510  C   PHE A  66     -12.794 -20.497  -1.533  1.00 46.14           C  
ANISOU  510  C   PHE A  66     6537   6086   4908   1207   -711  -1564       C  
ATOM    511  O   PHE A  66     -12.959 -21.666  -1.168  1.00 48.94           O  
ANISOU  511  O   PHE A  66     7000   6266   5328   1264   -860  -1636       O  
ATOM    512  CB  PHE A  66     -15.134 -19.677  -1.150  1.00 43.71           C  
ANISOU  512  CB  PHE A  66     6312   5661   4636    944   -711  -1265       C  
ATOM    513  CG  PHE A  66     -16.316 -18.915  -1.660  1.00 41.37           C  
ANISOU  513  CG  PHE A  66     6009   5411   4297    817   -668  -1136       C  
ATOM    514  CD1 PHE A  66     -16.356 -17.534  -1.577  1.00 42.70           C  
ANISOU  514  CD1 PHE A  66     6088   5688   4447    741   -540  -1006       C  
ATOM    515  CD2 PHE A  66     -17.389 -19.581  -2.225  1.00 42.92           C  
ANISOU  515  CD2 PHE A  66     6291   5536   4480    778   -767  -1150       C  
ATOM    516  CE1 PHE A  66     -17.446 -16.833  -2.050  1.00 41.54           C  
ANISOU  516  CE1 PHE A  66     5938   5576   4270    638   -518   -892       C  
ATOM    517  CE2 PHE A  66     -18.481 -18.885  -2.697  1.00 43.11           C  
ANISOU  517  CE2 PHE A  66     6303   5606   4472    671   -741  -1039       C  
ATOM    518  CZ  PHE A  66     -18.511 -17.509  -2.609  1.00 43.31           C  
ANISOU  518  CZ  PHE A  66     6240   5737   4480    607   -620   -911       C  
ATOM    519  N   LEU A  67     -11.627 -19.862  -1.446  1.00 44.98           N  
ANISOU  519  N   LEU A  67     6266   6082   4743   1260   -604  -1604       N  
ATOM    520  CA  LEU A  67     -10.434 -20.469  -0.862  1.00 43.48           C  
ANISOU  520  CA  LEU A  67     6043   5861   4617   1401   -654  -1741       C  
ATOM    521  C   LEU A  67     -10.287 -19.940   0.560  1.00 43.78           C  
ANISOU  521  C   LEU A  67     6065   5810   4757   1348   -644  -1612       C  
ATOM    522  O   LEU A  67      -9.841 -18.809   0.769  1.00 42.96           O  
ANISOU  522  O   LEU A  67     5848   5832   4643   1295   -513  -1537       O  
ATOM    523  CB  LEU A  67      -9.197 -20.174  -1.707  1.00 46.86           C  
ANISOU  523  CB  LEU A  67     6326   6520   4958   1498   -544  -1892       C  
ATOM    524  CG  LEU A  67      -9.099 -20.721  -3.145  1.00 54.53           C  
ANISOU  524  CG  LEU A  67     7296   7617   5808   1574   -542  -2058       C  
ATOM    525  CD1 LEU A  67     -10.110 -20.113  -4.124  1.00 53.78           C  
ANISOU  525  CD1 LEU A  67     7230   7609   5595   1446   -474  -1949       C  
ATOM    526  CD2 LEU A  67      -7.677 -20.613  -3.704  1.00 56.46           C  
ANISOU  526  CD2 LEU A  67     7385   8079   5989   1691   -444  -2238       C  
ATOM    527  N   VAL A  68     -10.661 -20.763   1.536  1.00 40.60           N  
ANISOU  527  N   VAL A  68     5785   5191   4450   1357   -786  -1585       N  
ATOM    528  CA  VAL A  68     -10.563 -20.408   2.947  1.00 39.50           C  
ANISOU  528  CA  VAL A  68     5655   4956   4398   1310   -796  -1470       C  
ATOM    529  C   VAL A  68      -9.320 -21.066   3.524  1.00 42.79           C  
ANISOU  529  C   VAL A  68     6054   5329   4875   1468   -882  -1608       C  
ATOM    530  O   VAL A  68      -9.003 -22.217   3.200  1.00 42.83           O  
ANISOU  530  O   VAL A  68     6124   5256   4894   1596  -1010  -1759       O  
ATOM    531  CB  VAL A  68     -11.833 -20.822   3.716  1.00 37.79           C  
ANISOU  531  CB  VAL A  68     5586   4537   4234   1194   -889  -1333       C  
ATOM    532  CG1 VAL A  68     -11.743 -20.397   5.175  1.00 35.75           C  
ANISOU  532  CG1 VAL A  68     5337   4200   4046   1139   -887  -1214       C  
ATOM    533  CG2 VAL A  68     -13.065 -20.215   3.061  1.00 34.35           C  
ANISOU  533  CG2 VAL A  68     5151   4153   3747   1055   -816  -1220       C  
ATOM    534  N   GLN A  69      -8.602 -20.331   4.371  1.00 47.96           N  
ANISOU  534  N   GLN A  69     6620   6033   5569   1466   -822  -1564       N  
ATOM    535  CA  GLN A  69      -7.315 -20.792   4.870  1.00 50.00           C  
ANISOU  535  CA  GLN A  69     6830   6285   5883   1622   -893  -1702       C  
ATOM    536  C   GLN A  69      -7.108 -20.284   6.287  1.00 47.08           C  
ANISOU  536  C   GLN A  69     6460   5846   5581   1574   -901  -1588       C  
ATOM    537  O   GLN A  69      -7.224 -19.082   6.541  1.00 43.32           O  
ANISOU  537  O   GLN A  69     5899   5469   5092   1462   -767  -1471       O  
ATOM    538  CB  GLN A  69      -6.180 -20.313   3.958  1.00 52.99           C  
ANISOU  538  CB  GLN A  69     7022   6904   6210   1709   -773  -1850       C  
ATOM    539  CG  GLN A  69      -4.806 -20.834   4.332  1.00 56.69           C  
ANISOU  539  CG  GLN A  69     7411   7389   6739   1889   -848  -2027       C  
ATOM    540  CD  GLN A  69      -3.860 -20.868   3.148  1.00 61.12           C  
ANISOU  540  CD  GLN A  69     7818   8168   7238   2001   -766  -2228       C  
ATOM    541  OE1 GLN A  69      -4.182 -20.369   2.069  1.00 61.90           O  
ANISOU  541  OE1 GLN A  69     7866   8421   7234   1928   -636  -2217       O  
ATOM    542  NE2 GLN A  69      -2.685 -21.455   3.343  1.00 64.59           N  
ANISOU  542  NE2 GLN A  69     8171   8630   7740   2142   -842  -2370       N  
ATOM    543  N   ALA A  70      -6.805 -21.201   7.201  1.00 50.98           N  
ANISOU  543  N   ALA A  70     7058   6166   6145   1661  -1068  -1623       N  
ATOM    544  CA  ALA A  70      -6.508 -20.881   8.595  1.00 52.28           C  
ANISOU  544  CA  ALA A  70     7240   6259   6366   1637  -1104  -1535       C  
ATOM    545  C   ALA A  70      -5.048 -21.249   8.840  1.00 54.51           C  
ANISOU  545  C   ALA A  70     7437   6576   6699   1823  -1181  -1705       C  
ATOM    546  O   ALA A  70      -4.731 -22.378   9.219  1.00 57.04           O  
ANISOU  546  O   ALA A  70     7865   6738   7069   1948  -1366  -1788       O  
ATOM    547  CB  ALA A  70      -7.445 -21.622   9.544  1.00 51.62           C  
ANISOU  547  CB  ALA A  70     7365   5937   6310   1564  -1242  -1411       C  
ATOM    548  N   GLY A  71      -4.158 -20.284   8.624  1.00 55.33           N  
ANISOU  548  N   GLY A  71     7344   6883   6795   1839  -1046  -1757       N  
ATOM    549  CA  GLY A  71      -2.737 -20.559   8.673  1.00 59.15           C  
ANISOU  549  CA  GLY A  71     7705   7443   7326   2017  -1098  -1943       C  
ATOM    550  C   GLY A  71      -2.323 -21.464   7.532  1.00 63.63           C  
ANISOU  550  C   GLY A  71     8244   8057   7876   2168  -1145  -2147       C  
ATOM    551  O   GLY A  71      -2.291 -21.036   6.373  1.00 64.81           O  
ANISOU  551  O   GLY A  71     8282   8390   7954   2143  -1002  -2203       O  
ATOM    552  N   ASN A  72      -2.003 -22.718   7.845  1.00 91.66           N  
ANISOU  552  N   ASN A  72    11885  11459  11483   2274  -1342  -2206       N  
ATOM    553  CA  ASN A  72      -1.741 -23.721   6.822  1.00 93.37           C  
ANISOU  553  CA  ASN A  72    12087  11701  11687   2362  -1405  -2334       C  
ATOM    554  C   ASN A  72      -2.922 -24.649   6.585  1.00 94.16           C  
ANISOU  554  C   ASN A  72    12400  11602  11775   2329  -1516  -2281       C  
ATOM    555  O   ASN A  72      -3.029 -25.230   5.500  1.00 96.57           O  
ANISOU  555  O   ASN A  72    12695  11951  12045   2366  -1519  -2371       O  
ATOM    556  CB  ASN A  72      -0.508 -24.552   7.193  1.00 97.14           C  
ANISOU  556  CB  ASN A  72    12506  12166  12237   2506  -1557  -2453       C  
ATOM    557  CG  ASN A  72       0.739 -23.704   7.351  1.00 99.91           C  
ANISOU  557  CG  ASN A  72    12632  12726  12605   2535  -1455  -2525       C  
ATOM    558  OD1 ASN A  72       1.360 -23.684   8.412  1.00100.79           O  
ANISOU  558  OD1 ASN A  72    12734  12784  12777   2574  -1546  -2514       O  
ATOM    559  ND2 ASN A  72       1.107 -22.992   6.291  1.00 98.23           N  
ANISOU  559  ND2 ASN A  72    12239  12754  12331   2504  -1267  -2596       N  
ATOM    560  N   VAL A  73      -3.804 -24.806   7.576  1.00 77.00           N  
ANISOU  560  N   VAL A  73    10418   9212   9628   2250  -1607  -2136       N  
ATOM    561  CA  VAL A  73      -5.010 -25.599   7.383  1.00 74.95           C  
ANISOU  561  CA  VAL A  73    10357   8764   9356   2183  -1700  -2068       C  
ATOM    562  C   VAL A  73      -5.840 -25.001   6.257  1.00 74.47           C  
ANISOU  562  C   VAL A  73    10266   8820   9209   2096  -1546  -2069       C  
ATOM    563  O   VAL A  73      -5.964 -23.775   6.128  1.00 70.90           O  
ANISOU  563  O   VAL A  73     9701   8531   8707   1996  -1365  -1993       O  
ATOM    564  CB  VAL A  73      -5.825 -25.677   8.686  1.00 72.98           C  
ANISOU  564  CB  VAL A  73    10304   8289   9137   2078  -1792  -1894       C  
ATOM    565  CG1 VAL A  73      -6.790 -26.858   8.642  1.00 75.47           C  
ANISOU  565  CG1 VAL A  73    10826   8384   9464   2024  -1943  -1835       C  
ATOM    566  CG2 VAL A  73      -4.904 -25.769   9.890  1.00 74.35           C  
ANISOU  566  CG2 VAL A  73    10469   8412   9368   2147  -1891  -1878       C  
ATOM    567  N   GLN A  74      -6.406 -25.874   5.425  1.00 88.45           N  
ANISOU  567  N   GLN A  74    12119  10527  10961   2100  -1614  -2111       N  
ATOM    568  CA  GLN A  74      -7.270 -25.481   4.317  1.00 87.08           C  
ANISOU  568  CA  GLN A  74    11941  10447  10699   2018  -1502  -2115       C  
ATOM    569  C   GLN A  74      -8.652 -26.081   4.540  1.00 87.10           C  
ANISOU  569  C   GLN A  74    12152  10231  10713   1898  -1606  -1999       C  
ATOM    570  O   GLN A  74      -8.797 -27.309   4.573  1.00 89.82           O  
ANISOU  570  O   GLN A  74    12612  10407  11108   1938  -1771  -2023       O  
ATOM    571  CB  GLN A  74      -6.682 -25.937   2.979  1.00 89.36           C  
ANISOU  571  CB  GLN A  74    12117  10891  10946   2120  -1475  -2278       C  
ATOM    572  CG  GLN A  74      -5.693 -24.956   2.377  1.00 89.53           C  
ANISOU  572  CG  GLN A  74    11914  11197  10906   2159  -1292  -2361       C  
ATOM    573  CD  GLN A  74      -6.259 -24.229   1.177  1.00 90.98           C  
ANISOU  573  CD  GLN A  74    12046  11560  10963   2078  -1132  -2365       C  
ATOM    574  OE1 GLN A  74      -7.469 -24.019   1.079  1.00 89.04           O  
ANISOU  574  OE1 GLN A  74    11915  11239  10675   1962  -1125  -2261       O  
ATOM    575  NE2 GLN A  74      -5.389 -23.844   0.252  1.00 93.23           N  
ANISOU  575  NE2 GLN A  74    12154  12088  11183   2123  -1004  -2470       N  
ATOM    576  N   LEU A  75      -9.658 -25.214   4.694  1.00 59.32           N  
ANISOU  576  N   LEU A  75     8629   6753   7157   1703  -1486  -1806       N  
ATOM    577  CA  LEU A  75     -11.009 -25.616   5.064  1.00 58.74           C  
ANISOU  577  CA  LEU A  75     8717   6502   7100   1548  -1556  -1658       C  
ATOM    578  C   LEU A  75     -11.906 -25.685   3.838  1.00 60.35           C  
ANISOU  578  C   LEU A  75     8927   6762   7240   1485  -1519  -1680       C  
ATOM    579  O   LEU A  75     -12.009 -24.719   3.070  1.00 57.48           O  
ANISOU  579  O   LEU A  75     8435   6602   6801   1440  -1360  -1662       O  
ATOM    580  CB  LEU A  75     -11.607 -24.655   6.083  1.00 57.49           C  
ANISOU  580  CB  LEU A  75     8546   6350   6948   1376  -1458  -1444       C  
ATOM    581  CG  LEU A  75     -10.682 -24.185   7.194  1.00 55.99           C  
ANISOU  581  CG  LEU A  75     8303   6176   6797   1422  -1443  -1414       C  
ATOM    582  CD1 LEU A  75     -11.462 -23.296   8.133  1.00 48.60           C  
ANISOU  582  CD1 LEU A  75     7370   5239   5858   1242  -1351  -1209       C  
ATOM    583  CD2 LEU A  75     -10.115 -25.389   7.917  1.00 55.44           C  
ANISOU  583  CD2 LEU A  75     8370   5901   6794   1541  -1649  -1484       C  
ATOM    584  N   ARG A  76     -12.532 -26.843   3.681  1.00 46.49           N  
ANISOU  584  N   ARG A  76     7331   4819   5516   1482  -1678  -1716       N  
ATOM    585  CA  ARG A  76     -13.516 -27.140   2.654  1.00 47.49           C  
ANISOU  585  CA  ARG A  76     7500   4947   5597   1414  -1690  -1735       C  
ATOM    586  C   ARG A  76     -14.772 -26.342   2.860  1.00 39.25           C  
ANISOU  586  C   ARG A  76     6446   3934   4534   1203  -1589  -1536       C  
ATOM    587  O   ARG A  76     -15.369 -26.420   3.924  1.00 44.60           O  
ANISOU  587  O   ARG A  76     7206   4475   5265   1084  -1626  -1391       O  
ATOM    588  CB  ARG A  76     -13.839 -28.618   2.762  1.00 49.73           C  
ANISOU  588  CB  ARG A  76     7973   4975   5946   1449  -1908  -1804       C  
ATOM    589  N   VAL A  77     -15.207 -25.613   1.848  1.00 47.93           N  
ANISOU  589  N   VAL A  77     7449   5209   5552   1156  -1471  -1531       N  
ATOM    590  CA  VAL A  77     -16.526 -25.011   1.893  1.00 46.29           C  
ANISOU  590  CA  VAL A  77     7240   5014   5335    969  -1408  -1367       C  
ATOM    591  C   VAL A  77     -17.499 -26.017   1.294  1.00 46.26           C  
ANISOU  591  C   VAL A  77     7355   4883   5339    921  -1539  -1410       C  
ATOM    592  O   VAL A  77     -17.351 -26.420   0.134  1.00 48.34           O  
ANISOU  592  O   VAL A  77     7617   5204   5546   1008  -1574  -1555       O  
ATOM    593  CB  VAL A  77     -16.536 -23.671   1.154  1.00 44.45           C  
ANISOU  593  CB  VAL A  77     6853   5019   5016    939  -1232  -1325       C  
ATOM    594  CG1 VAL A  77     -17.825 -22.923   1.411  1.00 43.60           C  
ANISOU  594  CG1 VAL A  77     6729   4921   4918    759  -1169  -1150       C  
ATOM    595  CG2 VAL A  77     -15.343 -22.865   1.619  1.00 44.60           C  
ANISOU  595  CG2 VAL A  77     6759   5156   5032   1012  -1124  -1328       C  
ATOM    596  N   ILE A  78     -18.438 -26.481   2.113  1.00 52.22           N  
ANISOU  596  N   ILE A  78     8216   5462   6162    783  -1617  -1295       N  
ATOM    597  CA  ILE A  78     -19.477 -27.411   1.700  1.00 53.06           C  
ANISOU  597  CA  ILE A  78     8437   5432   6292    701  -1743  -1312       C  
ATOM    598  C   ILE A  78     -20.809 -26.687   1.518  1.00 52.18           C  
ANISOU  598  C   ILE A  78     8266   5396   6164    523  -1660  -1181       C  
ATOM    599  O   ILE A  78     -21.866 -27.316   1.511  1.00 54.52           O  
ANISOU  599  O   ILE A  78     8643   5574   6499    402  -1749  -1147       O  
ATOM    600  CB  ILE A  78     -19.602 -28.581   2.691  1.00 55.55           C  
ANISOU  600  CB  ILE A  78     8927   5483   6698    662  -1906  -1285       C  
ATOM    601  CG1 ILE A  78     -19.988 -28.055   4.077  1.00 52.67           C  
ANISOU  601  CG1 ILE A  78     8563   5078   6370    517  -1840  -1091       C  
ATOM    602  CG2 ILE A  78     -18.297 -29.363   2.771  1.00 55.69           C  
ANISOU  602  CG2 ILE A  78     9007   5412   6739    862  -2016  -1435       C  
ATOM    603  CD1 ILE A  78     -20.228 -29.139   5.104  1.00 53.19           C  
ANISOU  603  CD1 ILE A  78     8812   4890   6508    442  -1991  -1030       C  
ATOM    604  N   GLY A  79     -20.770 -25.370   1.390  1.00 42.03           N  
ANISOU  604  N   GLY A  79     6836   4303   4829    505  -1498  -1108       N  
ATOM    605  CA  GLY A  79     -21.976 -24.595   1.183  1.00 44.13           C  
ANISOU  605  CA  GLY A  79     7032   4651   5084    360  -1425   -995       C  
ATOM    606  C   GLY A  79     -21.758 -23.129   1.468  1.00 41.23           C  
ANISOU  606  C   GLY A  79     6527   4450   4691    344  -1258   -894       C  
ATOM    607  O   GLY A  79     -20.844 -22.728   2.191  1.00 40.50           O  
ANISOU  607  O   GLY A  79     6402   4377   4608    400  -1197   -874       O  
ATOM    608  N   HIS A  80     -22.635 -22.310   0.890  1.00 40.91           N  
ANISOU  608  N   HIS A  80     6403   4521   4619    266  -1192   -831       N  
ATOM    609  CA  HIS A  80     -22.558 -20.865   1.050  1.00 39.80           C  
ANISOU  609  CA  HIS A  80     6137   4528   4458    245  -1046   -733       C  
ATOM    610  C   HIS A  80     -23.962 -20.278   1.087  1.00 42.33           C  
ANISOU  610  C   HIS A  80     6405   4872   4808    105  -1022   -626       C  
ATOM    611  O   HIS A  80     -24.872 -20.762   0.407  1.00 42.98           O  
ANISOU  611  O   HIS A  80     6515   4930   4886     55  -1102   -653       O  
ATOM    612  CB  HIS A  80     -21.739 -20.216  -0.075  1.00 38.98           C  
ANISOU  612  CB  HIS A  80     5962   4595   4252    355   -974   -801       C  
ATOM    613  CG  HIS A  80     -22.241 -20.529  -1.450  1.00 42.23           C  
ANISOU  613  CG  HIS A  80     6392   5063   4589    371  -1032   -877       C  
ATOM    614  ND1 HIS A  80     -21.709 -21.535  -2.227  1.00 43.83           N  
ANISOU  614  ND1 HIS A  80     6665   5247   4741    474  -1117  -1033       N  
ATOM    615  CD2 HIS A  80     -23.223 -19.961  -2.191  1.00 42.96           C  
ANISOU  615  CD2 HIS A  80     6445   5234   4645    303  -1024   -825       C  
ATOM    616  CE1 HIS A  80     -22.343 -21.577  -3.386  1.00 41.96           C  
ANISOU  616  CE1 HIS A  80     6433   5079   4433    463  -1154  -1073       C  
ATOM    617  NE2 HIS A  80     -23.266 -20.632  -3.389  1.00 46.16           N  
ANISOU  617  NE2 HIS A  80     6900   5668   4971    360  -1103   -945       N  
ATOM    618  N   SER A  81     -24.125 -19.228   1.891  1.00 38.43           N  
ANISOU  618  N   SER A  81     5828   4425   4348     48   -919   -513       N  
ATOM    619  CA  SER A  81     -25.403 -18.543   2.036  1.00 37.69           C  
ANISOU  619  CA  SER A  81     5663   4365   4294    -70   -887   -419       C  
ATOM    620  C   SER A  81     -25.144 -17.103   2.461  1.00 34.90           C  
ANISOU  620  C   SER A  81     5201   4114   3945    -65   -758   -334       C  
ATOM    621  O   SER A  81     -24.020 -16.727   2.800  1.00 32.91           O  
ANISOU  621  O   SER A  81     4937   3892   3674      8   -696   -340       O  
ATOM    622  CB  SER A  81     -26.308 -19.255   3.046  1.00 36.29           C  
ANISOU  622  CB  SER A  81     5533   4060   4197   -201   -937   -372       C  
ATOM    623  OG  SER A  81     -25.699 -19.301   4.324  1.00 40.72           O  
ANISOU  623  OG  SER A  81     6125   4558   4790   -209   -899   -329       O  
ATOM    624  N   MET A  82     -26.210 -16.302   2.468  1.00 37.20           N  
ANISOU  624  N   MET A  82     5410   4454   4270   -144   -726   -261       N  
ATOM    625  CA  MET A  82     -26.118 -14.864   2.705  1.00 36.42           C  
ANISOU  625  CA  MET A  82     5209   4447   4181   -138   -621   -185       C  
ATOM    626  C   MET A  82     -27.045 -14.477   3.849  1.00 36.22           C  
ANISOU  626  C   MET A  82     5126   4391   4243   -243   -584   -113       C  
ATOM    627  O   MET A  82     -28.243 -14.773   3.802  1.00 38.06           O  
ANISOU  627  O   MET A  82     5340   4606   4517   -329   -630   -105       O  
ATOM    628  CB  MET A  82     -26.484 -14.087   1.435  1.00 37.12           C  
ANISOU  628  CB  MET A  82     5246   4640   4218   -109   -623   -175       C  
ATOM    629  CG  MET A  82     -25.903 -12.686   1.349  1.00 38.03           C  
ANISOU  629  CG  MET A  82     5291   4846   4314    -66   -526   -115       C  
ATOM    630  SD  MET A  82     -25.762 -12.107  -0.356  1.00 37.10           S  
ANISOU  630  SD  MET A  82     5170   4845   4082     -8   -541   -120       S  
ATOM    631  CE  MET A  82     -27.449 -12.302  -0.930  1.00 36.65           C  
ANISOU  631  CE  MET A  82     5094   4775   4054    -72   -647   -111       C  
ATOM    632  N   GLN A  83     -26.498 -13.815   4.874  1.00 36.29           N  
ANISOU  632  N   GLN A  83     5103   4406   4281   -239   -498    -69       N  
ATOM    633  CA  GLN A  83     -27.297 -13.256   5.970  1.00 35.40           C  
ANISOU  633  CA  GLN A  83     4922   4291   4239   -327   -444     -9       C  
ATOM    634  C   GLN A  83     -27.157 -11.730   5.945  1.00 32.99           C  
ANISOU  634  C   GLN A  83     4515   4070   3950   -288   -361     36       C  
ATOM    635  O   GLN A  83     -26.348 -11.137   6.661  1.00 36.55           O  
ANISOU  635  O   GLN A  83     4951   4529   4407   -257   -292     56       O  
ATOM    636  CB  GLN A  83     -26.895 -13.842   7.328  1.00 35.91           C  
ANISOU  636  CB  GLN A  83     5046   4277   4320   -370   -426      3       C  
ATOM    637  CG  GLN A  83     -27.900 -13.520   8.427  1.00 36.88           C  
ANISOU  637  CG  GLN A  83     5108   4404   4501   -484   -376     52       C  
ATOM    638  CD  GLN A  83     -27.657 -14.293   9.706  1.00 37.14           C  
ANISOU  638  CD  GLN A  83     5226   4357   4531   -549   -374     70       C  
ATOM    639  OE1 GLN A  83     -26.721 -15.086   9.801  1.00 36.83           O  
ANISOU  639  OE1 GLN A  83     5294   4243   4455   -500   -425     47       O  
ATOM    640  NE2 GLN A  83     -28.505 -14.064  10.703  1.00 38.39           N  
ANISOU  640  NE2 GLN A  83     5333   4531   4721   -659   -320    109       N  
ATOM    641  N   ASN A  84     -27.957 -11.119   5.075  1.00 37.81           N  
ANISOU  641  N   ASN A  84     5062   4735   4568   -288   -382     50       N  
ATOM    642  CA  ASN A  84     -28.211  -9.698   4.835  1.00 38.59           C  
ANISOU  642  CA  ASN A  84     5069   4899   4696   -262   -340     97       C  
ATOM    643  C   ASN A  84     -27.053  -8.911   4.236  1.00 40.93           C  
ANISOU  643  C   ASN A  84     5375   5240   4936   -178   -299    116       C  
ATOM    644  O   ASN A  84     -27.268  -8.122   3.312  1.00 48.74           O  
ANISOU  644  O   ASN A  84     6335   6278   5904   -148   -314    147       O  
ATOM    645  CB  ASN A  84     -28.546  -8.965   6.145  1.00 39.63           C  
ANISOU  645  CB  ASN A  84     5124   5026   4907   -304   -266    127       C  
ATOM    646  CG  ASN A  84     -29.749  -9.523   6.861  1.00 37.03           C  
ANISOU  646  CG  ASN A  84     4759   4677   4634   -404   -280    115       C  
ATOM    647  OD1 ASN A  84     -30.871  -9.451   6.365  1.00 41.72           O  
ANISOU  647  OD1 ASN A  84     5290   5297   5264   -436   -326    108       O  
ATOM    648  ND2 ASN A  84     -29.528 -10.043   8.063  1.00 38.15           N  
ANISOU  648  ND2 ASN A  84     4934   4779   4783   -460   -239    114       N  
ATOM    649  N   CYS A  85     -25.823  -9.176   4.676  1.00 34.27           N  
ANISOU  649  N   CYS A  85     4578   4383   4061   -142   -256     96       N  
ATOM    650  CA  CYS A  85     -24.656  -8.508   4.108  1.00 31.53           C  
ANISOU  650  CA  CYS A  85     4232   4090   3658    -75   -210    106       C  
ATOM    651  C   CYS A  85     -23.381  -9.296   4.373  1.00 31.74           C  
ANISOU  651  C   CYS A  85     4316   4103   3641    -28   -196     48       C  
ATOM    652  O   CYS A  85     -22.287  -8.862   3.995  1.00 29.25           O  
ANISOU  652  O   CYS A  85     3992   3842   3280     23   -149     40       O  
ATOM    653  CB  CYS A  85     -24.520  -7.083   4.652  1.00 30.52           C  
ANISOU  653  CB  CYS A  85     4031   3979   3586    -78   -138    167       C  
ATOM    654  SG  CYS A  85     -25.461  -5.816   3.753  1.00 31.23           S  
ANISOU  654  SG  CYS A  85     4064   4106   3695    -82   -163    236       S  
ATOM    655  N   VAL A  86     -23.500 -10.423   5.064  1.00 28.29           N  
ANISOU  655  N   VAL A  86     3934   3592   3223    -49   -238      7       N  
ATOM    656  CA  VAL A  86     -22.357 -11.260   5.399  1.00 30.28           C  
ANISOU  656  CA  VAL A  86     4246   3811   3446      6   -249    -54       C  
ATOM    657  C   VAL A  86     -22.534 -12.591   4.697  1.00 30.09           C  
ANISOU  657  C   VAL A  86     4306   3746   3380     24   -343   -124       C  
ATOM    658  O   VAL A  86     -23.661 -13.087   4.556  1.00 30.53           O  
ANISOU  658  O   VAL A  86     4383   3760   3456    -39   -402   -116       O  
ATOM    659  CB  VAL A  86     -22.184 -11.457   6.924  1.00 31.71           C  
ANISOU  659  CB  VAL A  86     4445   3922   3682    -27   -233    -40       C  
ATOM    660  CG1 VAL A  86     -21.892 -10.130   7.612  1.00 29.22           C  
ANISOU  660  CG1 VAL A  86     4048   3649   3406    -34   -143     12       C  
ATOM    661  CG2 VAL A  86     -23.407 -12.128   7.531  1.00 31.66           C  
ANISOU  661  CG2 VAL A  86     4472   3842   3714   -121   -279    -17       C  
ATOM    662  N   LEU A  87     -21.431 -13.159   4.231  1.00 37.99           N  
ANISOU  662  N   LEU A  87     5345   4762   4326    111   -360   -202       N  
ATOM    663  CA  LEU A  87     -21.454 -14.457   3.583  1.00 39.07           C  
ANISOU  663  CA  LEU A  87     5567   4852   4426    147   -457   -290       C  
ATOM    664  C   LEU A  87     -21.115 -15.528   4.608  1.00 41.56           C  
ANISOU  664  C   LEU A  87     5965   5042   4783    154   -519   -324       C  
ATOM    665  O   LEU A  87     -20.088 -15.440   5.289  1.00 39.03           O  
ANISOU  665  O   LEU A  87     5640   4718   4474    207   -491   -341       O  
ATOM    666  CB  LEU A  87     -20.470 -14.496   2.415  1.00 42.17           C  
ANISOU  666  CB  LEU A  87     5951   5341   4729    246   -443   -373       C  
ATOM    667  CG  LEU A  87     -20.602 -15.669   1.444  1.00 42.02           C  
ANISOU  667  CG  LEU A  87     6008   5300   4656    292   -541   -477       C  
ATOM    668  CD1 LEU A  87     -21.951 -15.631   0.750  1.00 44.92           C  
ANISOU  668  CD1 LEU A  87     6383   5670   5013    218   -588   -439       C  
ATOM    669  CD2 LEU A  87     -19.481 -15.624   0.427  1.00 45.27           C  
ANISOU  669  CD2 LEU A  87     6397   5831   4972    395   -505   -570       C  
ATOM    670  N   LYS A  88     -21.984 -16.527   4.722  1.00 40.19           N  
ANISOU  670  N   LYS A  88     5871   4765   4634     94   -611   -331       N  
ATOM    671  CA  LYS A  88     -21.781 -17.640   5.640  1.00 37.07           C  
ANISOU  671  CA  LYS A  88     5580   4230   4274     85   -691   -351       C  
ATOM    672  C   LYS A  88     -21.298 -18.836   4.830  1.00 38.86           C  
ANISOU  672  C   LYS A  88     5896   4400   4468    175   -800   -470       C  
ATOM    673  O   LYS A  88     -22.061 -19.419   4.054  1.00 42.59           O  
ANISOU  673  O   LYS A  88     6407   4845   4929    143   -869   -503       O  
ATOM    674  CB  LYS A  88     -23.067 -17.961   6.399  1.00 37.89           C  
ANISOU  674  CB  LYS A  88     5719   4249   4429    -60   -719   -273       C  
ATOM    675  CG  LYS A  88     -23.529 -16.843   7.323  1.00 37.29           C  
ANISOU  675  CG  LYS A  88     5554   4227   4386   -140   -614   -174       C  
ATOM    676  CD  LYS A  88     -24.488 -17.352   8.386  1.00 40.53           C  
ANISOU  676  CD  LYS A  88     6012   4549   4838   -278   -636   -111       C  
ATOM    677  CE  LYS A  88     -25.805 -17.802   7.777  1.00 44.87           C  
ANISOU  677  CE  LYS A  88     6559   5082   5406   -375   -686   -109       C  
ATOM    678  NZ  LYS A  88     -26.806 -18.143   8.823  1.00 44.33           N  
ANISOU  678  NZ  LYS A  88     6510   4957   5376   -532   -682    -41       N  
ATOM    679  N   LEU A  89     -20.028 -19.191   5.003  1.00 35.32           N  
ANISOU  679  N   LEU A  89     5473   3938   4009    291   -820   -547       N  
ATOM    680  CA  LEU A  89     -19.407 -20.292   4.276  1.00 38.85           C  
ANISOU  680  CA  LEU A  89     5993   4336   4430    403   -922   -684       C  
ATOM    681  C   LEU A  89     -19.302 -21.489   5.213  1.00 39.50           C  
ANISOU  681  C   LEU A  89     6212   4228   4568    402  -1049   -696       C  
ATOM    682  O   LEU A  89     -18.451 -21.512   6.108  1.00 39.01           O  
ANISOU  682  O   LEU A  89     6164   4127   4530    454  -1053   -694       O  
ATOM    683  CB  LEU A  89     -18.033 -19.889   3.748  1.00 39.10           C  
ANISOU  683  CB  LEU A  89     5949   4494   4415    545   -863   -779       C  
ATOM    684  CG  LEU A  89     -17.973 -18.680   2.814  1.00 37.45           C  
ANISOU  684  CG  LEU A  89     5616   4475   4137    543   -736   -759       C  
ATOM    685  CD1 LEU A  89     -16.530 -18.279   2.553  1.00 38.80           C  
ANISOU  685  CD1 LEU A  89     5706   4768   4270    660   -666   -841       C  
ATOM    686  CD2 LEU A  89     -18.690 -18.981   1.511  1.00 39.20           C  
ANISOU  686  CD2 LEU A  89     5859   4737   4297    533   -774   -804       C  
ATOM    687  N   LYS A  90     -20.166 -22.479   5.008  1.00 34.79           N  
ANISOU  687  N   LYS A  90     5720   3507   3992    337  -1159   -706       N  
ATOM    688  CA  LYS A  90     -20.108 -23.691   5.812  1.00 39.39           C  
ANISOU  688  CA  LYS A  90     6454   3887   4624    325  -1297   -711       C  
ATOM    689  C   LYS A  90     -18.899 -24.523   5.409  1.00 41.93           C  
ANISOU  689  C   LYS A  90     6833   4156   4941    507  -1398   -867       C  
ATOM    690  O   LYS A  90     -18.657 -24.751   4.219  1.00 39.77           O  
ANISOU  690  O   LYS A  90     6535   3947   4628    601  -1417   -992       O  
ATOM    691  CB  LYS A  90     -21.390 -24.505   5.649  1.00 38.30           C  
ANISOU  691  CB  LYS A  90     6410   3628   4513    191  -1388   -680       C  
ATOM    692  CG  LYS A  90     -21.616 -25.518   6.761  1.00 41.88           C  
ANISOU  692  CG  LYS A  90     7021   3872   5019    108  -1503   -620       C  
ATOM    693  CD  LYS A  90     -22.819 -26.400   6.473  1.00 46.07           C  
ANISOU  693  CD  LYS A  90     7643   4281   5579    -28  -1601   -604       C  
ATOM    694  CE  LYS A  90     -23.238 -27.180   7.709  1.00 48.68           C  
ANISOU  694  CE  LYS A  90     8119   4424   5952   -166  -1681   -499       C  
ATOM    695  NZ  LYS A  90     -24.350 -28.127   7.418  1.00 50.75           N  
ANISOU  695  NZ  LYS A  90     8476   4556   6249   -309  -1786   -490       N  
ATOM    696  N   VAL A  91     -18.141 -24.977   6.404  1.00 42.73           N  
ANISOU  696  N   VAL A  91     7008   4146   5080    562  -1465   -865       N  
ATOM    697  CA  VAL A  91     -16.939 -25.759   6.166  1.00 43.23           C  
ANISOU  697  CA  VAL A  91     7119   4153   5155    749  -1572  -1019       C  
ATOM    698  C   VAL A  91     -17.100 -27.138   6.792  1.00 42.93           C  
ANISOU  698  C   VAL A  91     7279   3859   5175    737  -1766  -1021       C  
ATOM    699  O   VAL A  91     -17.959 -27.365   7.647  1.00 44.49           O  
ANISOU  699  O   VAL A  91     7572   3937   5397    576  -1796   -882       O  
ATOM    700  CB  VAL A  91     -15.668 -25.061   6.694  1.00 42.78           C  
ANISOU  700  CB  VAL A  91     6962   4197   5094    862  -1501  -1043       C  
ATOM    701  CG1 VAL A  91     -15.337 -23.844   5.836  1.00 41.23           C  
ANISOU  701  CG1 VAL A  91     6580   4246   4838    894  -1329  -1073       C  
ATOM    702  CG2 VAL A  91     -15.843 -24.667   8.145  1.00 41.00           C  
ANISOU  702  CG2 VAL A  91     6769   3914   4896    758  -1475   -889       C  
ATOM    703  N   ASP A  92     -16.255 -28.071   6.346  1.00 52.73           N  
ANISOU  703  N   ASP A  92     8584   5016   6437    909  -1901  -1184       N  
ATOM    704  CA  ASP A  92     -16.340 -29.452   6.805  1.00 52.76           C  
ANISOU  704  CA  ASP A  92     8790   4754   6501    918  -2110  -1203       C  
ATOM    705  C   ASP A  92     -15.639 -29.687   8.136  1.00 53.21           C  
ANISOU  705  C   ASP A  92     8933   4687   6597    954  -2189  -1142       C  
ATOM    706  O   ASP A  92     -15.732 -30.794   8.677  1.00 54.57           O  
ANISOU  706  O   ASP A  92     9264   4658   6814    935  -2350  -1104       O  
ATOM    707  CB  ASP A  92     -15.761 -30.401   5.749  1.00 56.73           C  
ANISOU  707  CB  ASP A  92     9316   5220   7018   1094  -2230  -1405       C  
ATOM    708  CG  ASP A  92     -14.276 -30.182   5.509  1.00 58.89           C  
ANISOU  708  CG  ASP A  92     9462   5631   7284   1313  -2198  -1545       C  
ATOM    709  OD1 ASP A  92     -13.726 -29.167   5.987  1.00 58.41           O  
ANISOU  709  OD1 ASP A  92     9308   5685   7202   1336  -2088  -1524       O  
ATOM    710  OD2 ASP A  92     -13.656 -31.026   4.828  1.00 62.40           O  
ANISOU  710  OD2 ASP A  92     9882   6080   7746   1456  -2279  -1675       O  
ATOM    711  N   THR A  93     -14.947 -28.687   8.674  1.00 44.45           N  
ANISOU  711  N   THR A  93     7698   3726   5466    992  -2067  -1106       N  
ATOM    712  CA  THR A  93     -14.199 -28.826   9.915  1.00 43.87           C  
ANISOU  712  CA  THR A  93     7692   3557   5421   1040  -2141  -1058       C  
ATOM    713  C   THR A  93     -14.694 -27.807  10.927  1.00 43.86           C  
ANISOU  713  C   THR A  93     7641   3636   5386    873  -2000   -871       C  
ATOM    714  O   THR A  93     -14.751 -26.608  10.632  1.00 40.68           O  
ANISOU  714  O   THR A  93     7065   3444   4947    842  -1817   -849       O  
ATOM    715  CB  THR A  93     -12.697 -28.641   9.685  1.00 47.14           C  
ANISOU  715  CB  THR A  93     7994   4072   5848   1272  -2148  -1222       C  
ATOM    716  OG1 THR A  93     -12.246 -29.563   8.684  1.00 51.17           O  
ANISOU  716  OG1 THR A  93     8500   4564   6378   1420  -2248  -1389       O  
ATOM    717  CG2 THR A  93     -11.927 -28.883  10.976  1.00 47.43           C  
ANISOU  717  CG2 THR A  93     8112   3992   5918   1331  -2256  -1180       C  
ATOM    718  N   ALA A  94     -15.053 -28.285  12.114  1.00 42.62           N  
ANISOU  718  N   ALA A  94     7644   3312   5238    765  -2088   -739       N  
ATOM    719  CA  ALA A  94     -15.382 -27.395  13.214  1.00 43.13           C  
ANISOU  719  CA  ALA A  94     7673   3449   5265    627  -1969   -579       C  
ATOM    720  C   ALA A  94     -14.107 -26.805  13.801  1.00 42.29           C  
ANISOU  720  C   ALA A  94     7484   3427   5159    768  -1950   -622       C  
ATOM    721  O   ALA A  94     -13.114 -27.512  13.991  1.00 42.61           O  
ANISOU  721  O   ALA A  94     7596   3361   5233    929  -2103   -714       O  
ATOM    722  CB  ALA A  94     -16.171 -28.137  14.293  1.00 45.20           C  
ANISOU  722  CB  ALA A  94     8139   3515   5519    454  -2068   -424       C  
ATOM    723  N   ASN A  95     -14.133 -25.508  14.076  1.00 37.15           N  
ANISOU  723  N   ASN A  95     6678   2961   4475    712  -1770   -564       N  
ATOM    724  CA  ASN A  95     -12.970 -24.847  14.660  1.00 32.52           C  
ANISOU  724  CA  ASN A  95     6000   2466   3890    827  -1741   -600       C  
ATOM    725  C   ASN A  95     -12.732 -25.382  16.064  1.00 35.01           C  
ANISOU  725  C   ASN A  95     6480   2624   4198    804  -1872   -513       C  
ATOM    726  O   ASN A  95     -13.579 -25.174  16.944  1.00 36.49           O  
ANISOU  726  O   ASN A  95     6739   2783   4343    627  -1827   -359       O  
ATOM    727  CB  ASN A  95     -13.167 -23.330  14.687  1.00 33.34           C  
ANISOU  727  CB  ASN A  95     5919   2785   3966    750  -1527   -546       C  
ATOM    728  CG  ASN A  95     -11.892 -22.575  15.038  1.00 36.57           C  
ANISOU  728  CG  ASN A  95     6201   3309   4384    875  -1486   -611       C  
ATOM    729  OD1 ASN A  95     -10.920 -23.156  15.521  1.00 33.62           O  
ANISOU  729  OD1 ASN A  95     5885   2854   4035   1005  -1621   -677       O  
ATOM    730  ND2 ASN A  95     -11.896 -21.268  14.798  1.00 34.26           N  
ANISOU  730  ND2 ASN A  95     5735   3204   4079    836  -1309   -596       N  
ATOM    731  N   PRO A  96     -11.617 -26.070  16.325  1.00 44.13           N  
ANISOU  731  N   PRO A  96     7700   3679   5388    978  -2037   -606       N  
ATOM    732  CA  PRO A  96     -11.385 -26.601  17.676  1.00 47.64           C  
ANISOU  732  CA  PRO A  96     8320   3964   5816    959  -2181   -514       C  
ATOM    733  C   PRO A  96     -11.115 -25.524  18.712  1.00 45.97           C  
ANISOU  733  C   PRO A  96     8029   3877   5561    908  -2074   -433       C  
ATOM    734  O   PRO A  96     -11.261 -25.794  19.910  1.00 48.19           O  
ANISOU  734  O   PRO A  96     8461   4052   5798    828  -2152   -314       O  
ATOM    735  CB  PRO A  96     -10.170 -27.519  17.489  1.00 50.71           C  
ANISOU  735  CB  PRO A  96     8763   4236   6268   1194  -2386   -668       C  
ATOM    736  CG  PRO A  96      -9.451 -26.944  16.312  1.00 51.45           C  
ANISOU  736  CG  PRO A  96     8629   4522   6397   1345  -2281   -846       C  
ATOM    737  CD  PRO A  96     -10.512 -26.388  15.402  1.00 46.31           C  
ANISOU  737  CD  PRO A  96     7887   3991   5716   1204  -2102   -808       C  
ATOM    738  N   LYS A  97     -10.726 -24.322  18.291  1.00 43.01           N  
ANISOU  738  N   LYS A  97     7431   3720   5192    946  -1903   -493       N  
ATOM    739  CA  LYS A  97     -10.495 -23.205  19.196  1.00 40.63           C  
ANISOU  739  CA  LYS A  97     7039   3543   4856    895  -1793   -429       C  
ATOM    740  C   LYS A  97     -11.707 -22.290  19.325  1.00 39.23           C  
ANISOU  740  C   LYS A  97     6805   3470   4632    691  -1604   -305       C  
ATOM    741  O   LYS A  97     -11.562 -21.155  19.793  1.00 38.85           O  
ANISOU  741  O   LYS A  97     6637   3559   4565    656  -1478   -278       O  
ATOM    742  CB  LYS A  97      -9.278 -22.397  18.738  1.00 41.56           C  
ANISOU  742  CB  LYS A  97     6946   3829   5015   1054  -1727   -570       C  
ATOM    743  CG  LYS A  97      -8.066 -23.249  18.392  1.00 45.25           C  
ANISOU  743  CG  LYS A  97     7424   4229   5542   1274  -1897   -730       C  
ATOM    744  CD  LYS A  97      -7.034 -22.463  17.601  1.00 46.25           C  
ANISOU  744  CD  LYS A  97     7310   4553   5708   1407  -1796   -882       C  
ATOM    745  CE  LYS A  97      -5.633 -23.004  17.841  1.00 50.67           C  
ANISOU  745  CE  LYS A  97     7851   5077   6323   1620  -1958  -1028       C  
ATOM    746  NZ  LYS A  97      -5.152 -23.825  16.696  1.00 55.70           N  
ANISOU  746  NZ  LYS A  97     8457   5696   7009   1782  -2035  -1201       N  
ATOM    747  N   THR A  98     -12.885 -22.747  18.911  1.00 38.29           N  
ANISOU  747  N   THR A  98     6761   3288   4500    562  -1586   -239       N  
ATOM    748  CA  THR A  98     -14.100 -21.953  19.038  1.00 37.05           C  
ANISOU  748  CA  THR A  98     6546   3225   4305    373  -1420   -131       C  
ATOM    749  C   THR A  98     -14.365 -21.631  20.509  1.00 38.70           C  
ANISOU  749  C   THR A  98     6827   3425   4450    255  -1399     -9       C  
ATOM    750  O   THR A  98     -14.517 -22.561  21.313  1.00 39.38           O  
ANISOU  750  O   THR A  98     7108   3356   4498    200  -1528     66       O  
ATOM    751  CB  THR A  98     -15.302 -22.689  18.454  1.00 38.64           C  
ANISOU  751  CB  THR A  98     6832   3340   4507    252  -1437    -84       C  
ATOM    752  OG1 THR A  98     -15.076 -22.961  17.067  1.00 37.07           O  
ANISOU  752  OG1 THR A  98     6567   3161   4357    363  -1456   -205       O  
ATOM    753  CG2 THR A  98     -16.562 -21.847  18.599  1.00 37.88           C  
ANISOU  753  CG2 THR A  98     6657   3355   4382     66  -1268     14       C  
ATOM    754  N   PRO A  99     -14.419 -20.365  20.886  1.00 37.86           N  
ANISOU  754  N   PRO A  99     6582   3476   4327    212  -1247     12       N  
ATOM    755  CA  PRO A  99     -14.733 -20.015  22.278  1.00 34.15           C  
ANISOU  755  CA  PRO A  99     6175   3015   3785     96  -1215    116       C  
ATOM    756  C   PRO A  99     -16.236 -19.927  22.492  1.00 34.96           C  
ANISOU  756  C   PRO A  99     6302   3136   3844   -113  -1112    225       C  
ATOM    757  O   PRO A  99     -17.038 -20.020  21.560  1.00 34.50           O  
ANISOU  757  O   PRO A  99     6196   3092   3820   -166  -1061    218       O  
ATOM    758  CB  PRO A  99     -14.073 -18.641  22.431  1.00 34.41           C  
ANISOU  758  CB  PRO A  99     6026   3213   3834    160  -1098     62       C  
ATOM    759  CG  PRO A  99     -14.216 -18.031  21.071  1.00 32.32           C  
ANISOU  759  CG  PRO A  99     5592   3053   3634    201   -990     -9       C  
ATOM    760  CD  PRO A  99     -14.137 -19.171  20.073  1.00 33.69           C  
ANISOU  760  CD  PRO A  99     5838   3123   3842    272  -1102    -64       C  
ATOM    761  N   LYS A 100     -16.609 -19.754  23.757  1.00 38.70           N  
ANISOU  761  N   LYS A 100     6850   3618   4238   -234  -1084    319       N  
ATOM    762  CA  LYS A 100     -17.989 -19.440  24.097  1.00 39.22           C  
ANISOU  762  CA  LYS A 100     6897   3746   4257   -433   -956    407       C  
ATOM    763  C   LYS A 100     -18.289 -18.012  23.656  1.00 38.86           C  
ANISOU  763  C   LYS A 100     6627   3882   4254   -426   -777    357       C  
ATOM    764  O   LYS A 100     -17.588 -17.076  24.057  1.00 39.79           O  
ANISOU  764  O   LYS A 100     6654   4090   4374   -351   -728    316       O  
ATOM    765  CB  LYS A 100     -18.210 -19.609  25.596  1.00 44.86           C  
ANISOU  765  CB  LYS A 100     7748   4438   4860   -557   -968    510       C  
ATOM    766  CG  LYS A 100     -19.592 -19.212  26.086  1.00 44.98           C  
ANISOU  766  CG  LYS A 100     7726   4547   4817   -766   -819    588       C  
ATOM    767  CD  LYS A 100     -19.797 -19.590  27.551  1.00 53.77           C  
ANISOU  767  CD  LYS A 100     9005   5630   5797   -902   -844    696       C  
ATOM    768  CE  LYS A 100     -18.822 -20.674  28.001  1.00 53.79           C  
ANISOU  768  CE  LYS A 100     9223   5452   5762   -826  -1054    730       C  
ATOM    769  NZ  LYS A 100     -18.875 -20.907  29.469  1.00 57.96           N  
ANISOU  769  NZ  LYS A 100     9915   5963   6145   -943  -1083    837       N  
ATOM    770  N   TYR A 101     -19.318 -17.838  22.828  1.00 34.37           N  
ANISOU  770  N   TYR A 101     5972   3362   3725   -502   -692    359       N  
ATOM    771  CA  TYR A 101     -19.527 -16.559  22.166  1.00 32.84           C  
ANISOU  771  CA  TYR A 101     5575   3316   3588   -467   -553    304       C  
ATOM    772  C   TYR A 101     -21.010 -16.245  22.029  1.00 33.19           C  
ANISOU  772  C   TYR A 101     5548   3429   3634   -620   -441    348       C  
ATOM    773  O   TYR A 101     -21.870 -17.126  22.111  1.00 33.12           O  
ANISOU  773  O   TYR A 101     5633   3353   3599   -746   -474    406       O  
ATOM    774  CB  TYR A 101     -18.861 -16.537  20.781  1.00 31.19           C  
ANISOU  774  CB  TYR A 101     5289   3108   3454   -319   -586    215       C  
ATOM    775  CG  TYR A 101     -19.553 -17.402  19.749  1.00 32.94           C  
ANISOU  775  CG  TYR A 101     5551   3262   3702   -352   -636    213       C  
ATOM    776  CD1 TYR A 101     -19.257 -18.754  19.637  1.00 36.57           C  
ANISOU  776  CD1 TYR A 101     6171   3570   4154   -326   -787    211       C  
ATOM    777  CD2 TYR A 101     -20.497 -16.864  18.881  1.00 33.07           C  
ANISOU  777  CD2 TYR A 101     5449   3362   3756   -404   -544    207       C  
ATOM    778  CE1 TYR A 101     -19.886 -19.548  18.695  1.00 35.32           C  
ANISOU  778  CE1 TYR A 101     6052   3344   4023   -357   -840    199       C  
ATOM    779  CE2 TYR A 101     -21.132 -17.651  17.939  1.00 36.07           C  
ANISOU  779  CE2 TYR A 101     5864   3683   4157   -435   -597    198       C  
ATOM    780  CZ  TYR A 101     -20.821 -18.991  17.849  1.00 37.66           C  
ANISOU  780  CZ  TYR A 101     6225   3735   4350   -414   -742    191       C  
ATOM    781  OH  TYR A 101     -21.450 -19.775  16.909  1.00 42.17           O  
ANISOU  781  OH  TYR A 101     6834   4243   4947   -446   -802    173       O  
ATOM    782  N   LYS A 102     -21.292 -14.959  21.818  1.00 36.67           N  
ANISOU  782  N   LYS A 102     5819   4002   4113   -608   -314    314       N  
ATOM    783  CA  LYS A 102     -22.614 -14.474  21.445  1.00 37.78           C  
ANISOU  783  CA  LYS A 102     5850   4224   4282   -711   -212    326       C  
ATOM    784  C   LYS A 102     -22.468 -13.432  20.345  1.00 36.94           C  
ANISOU  784  C   LYS A 102     5582   4199   4254   -608   -154    263       C  
ATOM    785  O   LYS A 102     -21.390 -12.872  20.127  1.00 33.03           O  
ANISOU  785  O   LYS A 102     5046   3723   3782   -484   -161    218       O  
ATOM    786  CB  LYS A 102     -23.377 -13.842  22.620  1.00 39.49           C  
ANISOU  786  CB  LYS A 102     6022   4530   4450   -832   -103    360       C  
ATOM    787  CG  LYS A 102     -23.414 -14.646  23.901  1.00 45.71           C  
ANISOU  787  CG  LYS A 102     6968   5264   5134   -941   -140    430       C  
ATOM    788  CD  LYS A 102     -24.375 -14.024  24.906  1.00 46.75           C  
ANISOU  788  CD  LYS A 102     7036   5513   5213  -1077    -11    451       C  
ATOM    789  CE  LYS A 102     -23.691 -12.958  25.756  1.00 50.63           C  
ANISOU  789  CE  LYS A 102     7474   6084   5677  -1007     44    411       C  
ATOM    790  NZ  LYS A 102     -23.476 -11.675  25.025  1.00 48.14           N  
ANISOU  790  NZ  LYS A 102     6983   5846   5464   -888    107    331       N  
ATOM    791  N   PHE A 103     -23.576 -13.173  19.657  1.00 29.31           N  
ANISOU  791  N   PHE A 103     4525   3282   3328   -668   -102    264       N  
ATOM    792  CA  PHE A 103     -23.682 -12.090  18.686  1.00 31.01           C  
ANISOU  792  CA  PHE A 103     4593   3578   3612   -596    -44    222       C  
ATOM    793  C   PHE A 103     -24.549 -11.001  19.305  1.00 31.07           C  
ANISOU  793  C   PHE A 103     4480   3686   3638   -662     69    224       C  
ATOM    794  O   PHE A 103     -25.739 -11.218  19.555  1.00 32.24           O  
ANISOU  794  O   PHE A 103     4605   3863   3783   -779    104    244       O  
ATOM    795  CB  PHE A 103     -24.282 -12.578  17.368  1.00 31.53           C  
ANISOU  795  CB  PHE A 103     4644   3624   3711   -598    -86    212       C  
ATOM    796  CG  PHE A 103     -23.355 -13.433  16.551  1.00 28.46           C  
ANISOU  796  CG  PHE A 103     4344   3157   3314   -502   -189    182       C  
ATOM    797  CD1 PHE A 103     -22.010 -13.529  16.866  1.00 27.95           C  
ANISOU  797  CD1 PHE A 103     4332   3060   3229   -401   -228    156       C  
ATOM    798  CD2 PHE A 103     -23.835 -14.136  15.459  1.00 30.28           C  
ANISOU  798  CD2 PHE A 103     4596   3351   3557   -508   -248    166       C  
ATOM    799  CE1 PHE A 103     -21.161 -14.315  16.107  1.00 28.97           C  
ANISOU  799  CE1 PHE A 103     4527   3127   3354   -302   -321    109       C  
ATOM    800  CE2 PHE A 103     -22.993 -14.923  14.697  1.00 27.28           C  
ANISOU  800  CE2 PHE A 103     4292   2905   3166   -412   -341    121       C  
ATOM    801  CZ  PHE A 103     -21.655 -15.013  15.022  1.00 29.39           C  
ANISOU  801  CZ  PHE A 103     4604   3145   3416   -306   -375     89       C  
ATOM    802  N   VAL A 104     -23.957  -9.837  19.556  1.00 29.55           N  
ANISOU  802  N   VAL A 104     4208   3548   3471   -587    122    194       N  
ATOM    803  CA  VAL A 104     -24.686  -8.710  20.119  1.00 29.17           C  
ANISOU  803  CA  VAL A 104     4043   3589   3452   -625    220    176       C  
ATOM    804  C   VAL A 104     -24.599  -7.536  19.156  1.00 29.14           C  
ANISOU  804  C   VAL A 104     3918   3624   3530   -535    247    145       C  
ATOM    805  O   VAL A 104     -23.628  -7.388  18.406  1.00 28.72           O  
ANISOU  805  O   VAL A 104     3874   3544   3492   -442    209    137       O  
ATOM    806  CB  VAL A 104     -24.159  -8.309  21.517  1.00 32.20           C  
ANISOU  806  CB  VAL A 104     4452   3996   3786   -634    259    168       C  
ATOM    807  CG1 VAL A 104     -24.184  -9.502  22.460  1.00 33.85           C  
ANISOU  807  CG1 VAL A 104     4805   4158   3899   -727    220    214       C  
ATOM    808  CG2 VAL A 104     -22.757  -7.730  21.418  1.00 32.31           C  
ANISOU  808  CG2 VAL A 104     4464   3992   3819   -512    233    139       C  
ATOM    809  N   ARG A 105     -25.639  -6.709  19.166  1.00 30.04           N  
ANISOU  809  N   ARG A 105     3917   3802   3695   -567    308    127       N  
ATOM    810  CA  ARG A 105     -25.665  -5.455  18.423  1.00 32.18           C  
ANISOU  810  CA  ARG A 105     4078   4102   4047   -490    329    104       C  
ATOM    811  C   ARG A 105     -25.581  -4.324  19.439  1.00 32.18           C  
ANISOU  811  C   ARG A 105     4011   4144   4071   -477    396     65       C  
ATOM    812  O   ARG A 105     -26.537  -4.075  20.181  1.00 33.97           O  
ANISOU  812  O   ARG A 105     4178   4427   4304   -538    452     37       O  
ATOM    813  CB  ARG A 105     -26.923  -5.340  17.566  1.00 32.67           C  
ANISOU  813  CB  ARG A 105     4058   4193   4163   -516    324    102       C  
ATOM    814  CG  ARG A 105     -26.990  -4.056  16.756  1.00 29.92           C  
ANISOU  814  CG  ARG A 105     3613   3860   3896   -434    327     90       C  
ATOM    815  CD  ARG A 105     -28.182  -4.042  15.817  1.00 32.62           C  
ANISOU  815  CD  ARG A 105     3884   4224   4286   -449    298     90       C  
ATOM    816  NE  ARG A 105     -28.203  -2.838  14.991  1.00 31.64           N  
ANISOU  816  NE  ARG A 105     3689   4099   4233   -367    281     91       N  
ATOM    817  CZ  ARG A 105     -27.609  -2.734  13.807  1.00 30.14           C  
ANISOU  817  CZ  ARG A 105     3536   3880   4035   -310    231    128       C  
ATOM    818  NH1 ARG A 105     -26.946  -3.766  13.302  1.00 27.13           N  
ANISOU  818  NH1 ARG A 105     3251   3475   3584   -313    195    149       N  
ATOM    819  NH2 ARG A 105     -27.678  -1.599  13.125  1.00 30.27           N  
ANISOU  819  NH2 ARG A 105     3499   3890   4111   -250    213    140       N  
ATOM    820  N   ILE A 106     -24.436  -3.647  19.476  1.00 30.93           N  
ANISOU  820  N   ILE A 106     3858   3966   3928   -400    392     54       N  
ATOM    821  CA  ILE A 106     -24.184  -2.622  20.482  1.00 31.73           C  
ANISOU  821  CA  ILE A 106     3912   4094   4050   -384    442     10       C  
ATOM    822  C   ILE A 106     -24.927  -1.342  20.126  1.00 31.25           C  
ANISOU  822  C   ILE A 106     3729   4058   4087   -352    473    -23       C  
ATOM    823  O   ILE A 106     -25.403  -1.175  18.997  1.00 29.20           O  
ANISOU  823  O   ILE A 106     3429   3787   3877   -330    445     -1       O  
ATOM    824  CB  ILE A 106     -22.677  -2.351  20.637  1.00 31.43           C  
ANISOU  824  CB  ILE A 106     3917   4023   4003   -319    418      4       C  
ATOM    825  CG1 ILE A 106     -22.051  -2.044  19.276  1.00 32.38           C  
ANISOU  825  CG1 ILE A 106     4020   4114   4170   -254    383     29       C  
ATOM    826  CG2 ILE A 106     -21.990  -3.533  21.302  1.00 34.87           C  
ANISOU  826  CG2 ILE A 106     4470   4435   4345   -342    380     21       C  
ATOM    827  CD1 ILE A 106     -20.786  -1.231  19.365  1.00 32.96           C  
ANISOU  827  CD1 ILE A 106     4077   4175   4272   -197    384     10       C  
ATOM    828  N   GLN A 107     -25.025  -0.436  21.089  1.00 33.37           N  
ANISOU  828  N   GLN A 107     3942   4355   4380   -346    520    -80       N  
ATOM    829  CA  GLN A 107     -25.652   0.874  21.047  1.00 33.36           C  
ANISOU  829  CA  GLN A 107     3830   4368   4479   -305    544   -132       C  
ATOM    830  C   GLN A 107     -24.622   1.950  20.724  1.00 32.17           C  
ANISOU  830  C   GLN A 107     3672   4159   4391   -230    520   -132       C  
ATOM    831  O   GLN A 107     -23.433   1.791  21.023  1.00 32.71           O  
ANISOU  831  O   GLN A 107     3803   4205   4419   -220    510   -122       O  
ATOM    832  CB  GLN A 107     -26.308   1.189  22.389  1.00 36.79           C  
ANISOU  832  CB  GLN A 107     4212   4870   4895   -342    612   -210       C  
ATOM    833  CG  GLN A 107     -27.394   0.211  22.795  1.00 37.65           C  
ANISOU  833  CG  GLN A 107     4315   5051   4939   -438    651   -211       C  
ATOM    834  CD  GLN A 107     -28.633   0.335  21.933  1.00 41.47           C  
ANISOU  834  CD  GLN A 107     4700   5558   5500   -438    643   -220       C  
ATOM    835  OE1 GLN A 107     -29.077   1.439  21.619  1.00 43.87           O  
ANISOU  835  OE1 GLN A 107     4902   5859   5906   -370    637   -269       O  
ATOM    836  NE2 GLN A 107     -29.199  -0.802  21.544  1.00 44.91           N  
ANISOU  836  NE2 GLN A 107     5165   6009   5889   -514    631   -174       N  
ATOM    837  N   PRO A 108     -25.047   3.049  20.104  1.00 32.57           N  
ANISOU  837  N   PRO A 108     3648   4183   4545   -181    504   -144       N  
ATOM    838  CA  PRO A 108     -24.135   4.184  19.920  1.00 32.43           C  
ANISOU  838  CA  PRO A 108     3624   4104   4594   -128    484   -145       C  
ATOM    839  C   PRO A 108     -23.670   4.719  21.266  1.00 32.52           C  
ANISOU  839  C   PRO A 108     3628   4126   4603   -125    519   -222       C  
ATOM    840  O   PRO A 108     -24.463   4.892  22.194  1.00 34.80           O  
ANISOU  840  O   PRO A 108     3868   4463   4891   -137    560   -296       O  
ATOM    841  CB  PRO A 108     -24.986   5.209  19.159  1.00 35.21           C  
ANISOU  841  CB  PRO A 108     3902   4419   5056    -82    452   -147       C  
ATOM    842  CG  PRO A 108     -26.405   4.783  19.383  1.00 36.20           C  
ANISOU  842  CG  PRO A 108     3965   4608   5183   -103    472   -189       C  
ATOM    843  CD  PRO A 108     -26.364   3.293  19.494  1.00 34.26           C  
ANISOU  843  CD  PRO A 108     3782   4412   4822   -172    491   -153       C  
ATOM    844  N   GLY A 109     -22.367   4.970  21.369  1.00 32.26           N  
ANISOU  844  N   GLY A 109     3637   4056   4564   -112    505   -210       N  
ATOM    845  CA  GLY A 109     -21.746   5.382  22.605  1.00 32.17           C  
ANISOU  845  CA  GLY A 109     3630   4053   4539   -111    524   -280       C  
ATOM    846  C   GLY A 109     -20.999   4.281  23.329  1.00 33.03           C  
ANISOU  846  C   GLY A 109     3818   4200   4531   -144    529   -274       C  
ATOM    847  O   GLY A 109     -20.184   4.580  24.209  1.00 33.74           O  
ANISOU  847  O   GLY A 109     3925   4291   4604   -137    527   -321       O  
ATOM    848  N   GLN A 110     -21.255   3.023  22.985  1.00 30.08           N  
ANISOU  848  N   GLN A 110     3498   3851   4080   -177    522   -219       N  
ATOM    849  CA  GLN A 110     -20.562   1.897  23.588  1.00 32.40           C  
ANISOU  849  CA  GLN A 110     3882   4163   4266   -202    506   -204       C  
ATOM    850  C   GLN A 110     -19.246   1.632  22.865  1.00 32.05           C  
ANISOU  850  C   GLN A 110     3874   4080   4225   -165    457   -166       C  
ATOM    851  O   GLN A 110     -19.064   1.989  21.698  1.00 30.25           O  
ANISOU  851  O   GLN A 110     3613   3825   4055   -140    446   -130       O  
ATOM    852  CB  GLN A 110     -21.440   0.645  23.562  1.00 33.18           C  
ANISOU  852  CB  GLN A 110     4029   4290   4286   -259    512   -164       C  
ATOM    853  CG  GLN A 110     -22.635   0.710  24.499  1.00 36.66           C  
ANISOU  853  CG  GLN A 110     4437   4794   4697   -315    571   -209       C  
ATOM    854  CD  GLN A 110     -22.238   1.036  25.925  1.00 40.96           C  
ANISOU  854  CD  GLN A 110     5002   5375   5185   -326    596   -271       C  
ATOM    855  OE1 GLN A 110     -21.661   0.204  26.626  1.00 43.90           O  
ANISOU  855  OE1 GLN A 110     5472   5752   5455   -355    574   -251       O  
ATOM    856  NE2 GLN A 110     -22.544   2.252  26.362  1.00 42.01           N  
ANISOU  856  NE2 GLN A 110     5049   5528   5384   -297    633   -351       N  
ATOM    857  N   THR A 111     -18.324   0.992  23.576  1.00 26.78           N  
ANISOU  857  N   THR A 111     3271   3416   3487   -161    427   -178       N  
ATOM    858  CA  THR A 111     -16.991   0.720  23.064  1.00 27.69           C  
ANISOU  858  CA  THR A 111     3404   3511   3604   -119    381   -166       C  
ATOM    859  C   THR A 111     -16.786  -0.776  22.859  1.00 25.44           C  
ANISOU  859  C   THR A 111     3209   3219   3237   -118    334   -130       C  
ATOM    860  O   THR A 111     -17.541  -1.609  23.368  1.00 27.63           O  
ANISOU  860  O   THR A 111     3552   3501   3446   -161    330   -111       O  
ATOM    861  CB  THR A 111     -15.914   1.262  24.010  1.00 27.04           C  
ANISOU  861  CB  THR A 111     3315   3432   3527    -97    363   -225       C  
ATOM    862  OG1 THR A 111     -16.112   0.723  25.323  1.00 29.04           O  
ANISOU  862  OG1 THR A 111     3635   3707   3691   -121    353   -250       O  
ATOM    863  CG2 THR A 111     -15.976   2.781  24.072  1.00 26.29           C  
ANISOU  863  CG2 THR A 111     3134   3324   3530    -94    397   -264       C  
ATOM    864  N   PHE A 112     -15.742  -1.103  22.101  1.00 25.52           N  
ANISOU  864  N   PHE A 112     3220   3219   3256    -70    295   -125       N  
ATOM    865  CA  PHE A 112     -15.376  -2.488  21.842  1.00 26.79           C  
ANISOU  865  CA  PHE A 112     3463   3363   3353    -47    234   -108       C  
ATOM    866  C   PHE A 112     -13.949  -2.526  21.321  1.00 24.93           C  
ANISOU  866  C   PHE A 112     3198   3136   3140     20    199   -141       C  
ATOM    867  O   PHE A 112     -13.387  -1.505  20.916  1.00 26.19           O  
ANISOU  867  O   PHE A 112     3269   3318   3363     31    233   -158       O  
ATOM    868  CB  PHE A 112     -16.336  -3.154  20.849  1.00 25.95           C  
ANISOU  868  CB  PHE A 112     3381   3245   3236    -71    238    -60       C  
ATOM    869  CG  PHE A 112     -16.427  -2.453  19.521  1.00 26.89           C  
ANISOU  869  CG  PHE A 112     3422   3379   3415    -56    272    -42       C  
ATOM    870  CD1 PHE A 112     -15.641  -2.854  18.454  1.00 23.70           C  
ANISOU  870  CD1 PHE A 112     3014   2984   3007    -10    248    -44       C  
ATOM    871  CD2 PHE A 112     -17.307  -1.400  19.337  1.00 25.76           C  
ANISOU  871  CD2 PHE A 112     3214   3244   3329    -87    323    -26       C  
ATOM    872  CE1 PHE A 112     -15.728  -2.214  17.231  1.00 24.48           C  
ANISOU  872  CE1 PHE A 112     3054   3105   3142     -7    280    -18       C  
ATOM    873  CE2 PHE A 112     -17.398  -0.756  18.117  1.00 27.64           C  
ANISOU  873  CE2 PHE A 112     3398   3488   3615    -77    341      2       C  
ATOM    874  CZ  PHE A 112     -16.607  -1.164  17.063  1.00 28.90           C  
ANISOU  874  CZ  PHE A 112     3565   3662   3756    -44    322     13       C  
ATOM    875  N   SER A 113     -13.371  -3.723  21.335  1.00 26.57           N  
ANISOU  875  N   SER A 113     3476   3323   3296     63    127   -152       N  
ATOM    876  CA  SER A 113     -12.008  -3.943  20.875  1.00 26.32           C  
ANISOU  876  CA  SER A 113     3408   3310   3281    138     86   -201       C  
ATOM    877  C   SER A 113     -12.020  -4.523  19.468  1.00 26.35           C  
ANISOU  877  C   SER A 113     3405   3324   3283    166     86   -191       C  
ATOM    878  O   SER A 113     -12.809  -5.422  19.163  1.00 26.53           O  
ANISOU  878  O   SER A 113     3504   3310   3265    153     60   -158       O  
ATOM    879  CB  SER A 113     -11.258  -4.886  21.819  1.00 27.31           C  
ANISOU  879  CB  SER A 113     3613   3405   3357    188    -12   -237       C  
ATOM    880  OG  SER A 113     -11.146  -4.328  23.115  1.00 28.78           O  
ANISOU  880  OG  SER A 113     3808   3594   3532    165    -16   -253       O  
ATOM    881  N   VAL A 114     -11.139  -4.006  18.616  1.00 26.24           N  
ANISOU  881  N   VAL A 114     3298   3364   3307    198    116   -222       N  
ATOM    882  CA  VAL A 114     -11.008  -4.453  17.234  1.00 24.94           C  
ANISOU  882  CA  VAL A 114     3116   3232   3130    227    126   -225       C  
ATOM    883  C   VAL A 114      -9.703  -5.223  17.098  1.00 25.68           C  
ANISOU  883  C   VAL A 114     3193   3353   3212    318     67   -309       C  
ATOM    884  O   VAL A 114      -8.636  -4.717  17.468  1.00 26.20           O  
ANISOU  884  O   VAL A 114     3183   3461   3312    343     70   -361       O  
ATOM    885  CB  VAL A 114     -11.047  -3.271  16.249  1.00 25.97           C  
ANISOU  885  CB  VAL A 114     3153   3416   3298    184    214   -193       C  
ATOM    886  CG1 VAL A 114     -10.716  -3.743  14.840  1.00 28.68           C  
ANISOU  886  CG1 VAL A 114     3476   3814   3608    217    225   -207       C  
ATOM    887  CG2 VAL A 114     -12.404  -2.594  16.282  1.00 24.62           C  
ANISOU  887  CG2 VAL A 114     2998   3210   3145    114    253   -120       C  
ATOM    888  N   LEU A 115      -9.789  -6.443  16.574  1.00 22.76           N  
ANISOU  888  N   LEU A 115     2890   2959   2800    370      8   -330       N  
ATOM    889  CA  LEU A 115      -8.608  -7.233  16.230  1.00 24.30           C  
ANISOU  889  CA  LEU A 115     3061   3183   2989    474    -51   -426       C  
ATOM    890  C   LEU A 115      -8.373  -7.050  14.735  1.00 23.68           C  
ANISOU  890  C   LEU A 115     2904   3193   2899    483     17   -448       C  
ATOM    891  O   LEU A 115      -8.945  -7.756  13.904  1.00 26.35           O  
ANISOU  891  O   LEU A 115     3297   3518   3198    494      2   -441       O  
ATOM    892  CB  LEU A 115      -8.790  -8.700  16.605  1.00 24.54           C  
ANISOU  892  CB  LEU A 115     3222   3120   2982    534   -172   -446       C  
ATOM    893  CG  LEU A 115      -7.658  -9.637  16.174  1.00 26.22           C  
ANISOU  893  CG  LEU A 115     3417   3350   3196    661   -251   -559       C  
ATOM    894  CD1 LEU A 115      -6.334  -9.200  16.776  1.00 26.12           C  
ANISOU  894  CD1 LEU A 115     3306   3394   3224    719   -268   -637       C  
ATOM    895  CD2 LEU A 115      -7.968 -11.077  16.549  1.00 25.10           C  
ANISOU  895  CD2 LEU A 115     3427   3085   3023    713   -386   -567       C  
ATOM    896  N   ALA A 116      -7.531  -6.078  14.394  1.00 26.33           N  
ANISOU  896  N   ALA A 116     3114   3625   3266    468     92   -472       N  
ATOM    897  CA  ALA A 116      -7.222  -5.813  12.996  1.00 29.00           C  
ANISOU  897  CA  ALA A 116     3375   4065   3578    461    168   -488       C  
ATOM    898  C   ALA A 116      -6.396  -6.954  12.416  1.00 30.37           C  
ANISOU  898  C   ALA A 116     3533   4285   3720    573    117   -604       C  
ATOM    899  O   ALA A 116      -5.391  -7.369  13.001  1.00 30.78           O  
ANISOU  899  O   ALA A 116     3548   4348   3800    654     58   -697       O  
ATOM    900  CB  ALA A 116      -6.474  -4.489  12.859  1.00 31.29           C  
ANISOU  900  CB  ALA A 116     3538   4443   3908    400    261   -481       C  
ATOM    901  N   CYS A 117      -6.827  -7.462  11.264  1.00 30.48           N  
ANISOU  901  N   CYS A 117     3577   4327   3677    584    132   -608       N  
ATOM    902  CA  CYS A 117      -6.160  -8.568  10.597  1.00 31.88           C  
ANISOU  902  CA  CYS A 117     3745   4549   3819    696     83   -730       C  
ATOM    903  C   CYS A 117      -5.962  -8.232   9.126  1.00 35.12           C  
ANISOU  903  C   CYS A 117     4080   5097   4168    673    184   -748       C  
ATOM    904  O   CYS A 117      -6.661  -7.386   8.561  1.00 33.87           O  
ANISOU  904  O   CYS A 117     3925   4962   3983    572    262   -644       O  
ATOM    905  CB  CYS A 117      -6.957  -9.873  10.732  1.00 31.53           C  
ANISOU  905  CB  CYS A 117     3848   4378   3753    749    -32   -735       C  
ATOM    906  SG  CYS A 117      -7.389 -10.320  12.428  1.00 32.16           S  
ANISOU  906  SG  CYS A 117     4049   4292   3877    747   -147   -685       S  
ATOM    907  N   TYR A 118      -4.990  -8.903   8.511  1.00 38.15           N  
ANISOU  907  N   TYR A 118     4396   5575   4524    772    176   -885       N  
ATOM    908  CA  TYR A 118      -4.703  -8.737   7.091  1.00 37.81           C  
ANISOU  908  CA  TYR A 118     4282   5683   4402    758    271   -924       C  
ATOM    909  C   TYR A 118      -4.329 -10.092   6.515  1.00 41.15           C  
ANISOU  909  C   TYR A 118     4722   6127   4785    896    199  -1075       C  
ATOM    910  O   TYR A 118      -3.391 -10.733   6.998  1.00 39.33           O  
ANISOU  910  O   TYR A 118     4444   5901   4600   1012    131  -1205       O  
ATOM    911  CB  TYR A 118      -3.584  -7.715   6.866  1.00 41.37           C  
ANISOU  911  CB  TYR A 118     4567   6292   4861    708    389   -950       C  
ATOM    912  CG  TYR A 118      -3.989  -6.312   7.246  1.00 43.76           C  
ANISOU  912  CG  TYR A 118     4859   6569   5199    565    461   -800       C  
ATOM    913  CD1 TYR A 118      -3.765  -5.824   8.527  1.00 45.54           C  
ANISOU  913  CD1 TYR A 118     5068   6719   5517    548    428   -776       C  
ATOM    914  CD2 TYR A 118      -4.621  -5.483   6.331  1.00 45.12           C  
ANISOU  914  CD2 TYR A 118     5048   6784   5312    452    550   -686       C  
ATOM    915  CE1 TYR A 118      -4.147  -4.544   8.881  1.00 45.92           C  
ANISOU  915  CE1 TYR A 118     5108   6734   5604    426    485   -653       C  
ATOM    916  CE2 TYR A 118      -5.003  -4.206   6.674  1.00 45.42           C  
ANISOU  916  CE2 TYR A 118     5084   6781   5393    332    600   -555       C  
ATOM    917  CZ  TYR A 118      -4.767  -3.738   7.950  1.00 46.94           C  
ANISOU  917  CZ  TYR A 118     5253   6896   5684    320    569   -544       C  
ATOM    918  OH  TYR A 118      -5.150  -2.462   8.296  1.00 45.28           O  
ANISOU  918  OH  TYR A 118     5043   6639   5524    209    612   -428       O  
ATOM    919  N   ASN A 119      -5.068 -10.520   5.488  1.00 51.20           N  
ANISOU  919  N   ASN A 119     6066   7409   5978    890    203  -1066       N  
ATOM    920  CA  ASN A 119      -4.885 -11.835   4.869  1.00 52.28           C  
ANISOU  920  CA  ASN A 119     6240   7549   6074   1020    124  -1211       C  
ATOM    921  C   ASN A 119      -5.061 -12.957   5.891  1.00 52.79           C  
ANISOU  921  C   ASN A 119     6417   7430   6213   1117    -43  -1252       C  
ATOM    922  O   ASN A 119      -4.366 -13.975   5.851  1.00 54.14           O  
ANISOU  922  O   ASN A 119     6581   7592   6397   1259   -131  -1407       O  
ATOM    923  CB  ASN A 119      -3.525 -11.938   4.173  1.00 56.33           C  
ANISOU  923  CB  ASN A 119     6598   8253   6552   1102    190  -1378       C  
ATOM    924  CG  ASN A 119      -3.311 -10.843   3.148  1.00 58.95           C  
ANISOU  924  CG  ASN A 119     6828   8775   6797    988    360  -1328       C  
ATOM    925  OD1 ASN A 119      -4.036 -10.757   2.156  1.00 62.77           O  
ANISOU  925  OD1 ASN A 119     7368   9296   7184    931    403  -1274       O  
ATOM    926  ND2 ASN A 119      -2.314  -9.999   3.382  1.00 63.13           N  
ANISOU  926  ND2 ASN A 119     7209   9422   7356    946    453  -1343       N  
ATOM    927  N   GLY A 120      -6.001 -12.769   6.815  1.00 40.44           N  
ANISOU  927  N   GLY A 120     4958   5715   4692   1039    -89  -1115       N  
ATOM    928  CA  GLY A 120      -6.315 -13.773   7.809  1.00 39.97           C  
ANISOU  928  CA  GLY A 120     5027   5473   4686   1098   -242  -1120       C  
ATOM    929  C   GLY A 120      -5.386 -13.828   9.002  1.00 38.30           C  
ANISOU  929  C   GLY A 120     4781   5224   4548   1165   -306  -1166       C  
ATOM    930  O   GLY A 120      -5.579 -14.684   9.874  1.00 41.00           O  
ANISOU  930  O   GLY A 120     5242   5410   4926   1214   -443  -1165       O  
ATOM    931  N   SER A 121      -4.388 -12.948   9.075  1.00 37.18           N  
ANISOU  931  N   SER A 121     4484   5217   4427   1162   -217  -1202       N  
ATOM    932  CA  SER A 121      -3.429 -12.956  10.168  1.00 36.35           C  
ANISOU  932  CA  SER A 121     4328   5090   4392   1230   -282  -1259       C  
ATOM    933  C   SER A 121      -3.631 -11.736  11.051  1.00 33.54           C  
ANISOU  933  C   SER A 121     3945   4730   4070   1107   -215  -1132       C  
ATOM    934  O   SER A 121      -3.685 -10.611  10.539  1.00 33.46           O  
ANISOU  934  O   SER A 121     3843   4828   4042   1004    -77  -1072       O  
ATOM    935  CB  SER A 121      -1.995 -12.973   9.627  1.00 39.02           C  
ANISOU  935  CB  SER A 121     4491   5594   4741   1334   -247  -1431       C  
ATOM    936  OG  SER A 121      -1.632 -14.270   9.188  1.00 45.95           O  
ANISOU  936  OG  SER A 121     5402   6445   5614   1491   -357  -1582       O  
ATOM    937  N   PRO A 122      -3.756 -11.915  12.366  1.00 35.21           N  
ANISOU  937  N   PRO A 122     4239   4816   4324   1112   -312  -1088       N  
ATOM    938  CA  PRO A 122      -3.938 -10.757  13.250  1.00 31.78           C  
ANISOU  938  CA  PRO A 122     3778   4379   3919   1003   -252   -984       C  
ATOM    939  C   PRO A 122      -2.735  -9.827  13.218  1.00 34.94           C  
ANISOU  939  C   PRO A 122     3995   4923   4358   1003   -172  -1051       C  
ATOM    940  O   PRO A 122      -1.583 -10.262  13.260  1.00 35.95           O  
ANISOU  940  O   PRO A 122     4034   5109   4516   1116   -225  -1187       O  
ATOM    941  CB  PRO A 122      -4.125 -11.394  14.633  1.00 34.12           C  
ANISOU  941  CB  PRO A 122     4204   4523   4236   1036   -392   -958       C  
ATOM    942  CG  PRO A 122      -4.635 -12.767  14.343  1.00 35.17           C  
ANISOU  942  CG  PRO A 122     4478   4545   4340   1104   -504   -979       C  
ATOM    943  CD  PRO A 122      -3.947 -13.189  13.077  1.00 33.43           C  
ANISOU  943  CD  PRO A 122     4164   4428   4108   1200   -483  -1112       C  
ATOM    944  N   SER A 123      -3.019  -8.530  13.144  1.00 35.95           N  
ANISOU  944  N   SER A 123     4062   5104   4492    874    -51   -958       N  
ATOM    945  CA  SER A 123      -2.009  -7.483  13.051  1.00 38.29           C  
ANISOU  945  CA  SER A 123     4190   5533   4828    834     41   -996       C  
ATOM    946  C   SER A 123      -1.870  -6.661  14.318  1.00 38.63           C  
ANISOU  946  C   SER A 123     4219   5528   4929    781     25   -951       C  
ATOM    947  O   SER A 123      -0.751  -6.302  14.695  1.00 35.98           O  
ANISOU  947  O   SER A 123     3760   5265   4644    807     22  -1034       O  
ATOM    948  CB  SER A 123      -2.337  -6.544  11.884  1.00 39.60           C  
ANISOU  948  CB  SER A 123     4294   5797   4954    719    191   -925       C  
ATOM    949  OG  SER A 123      -1.236  -5.709  11.570  1.00 45.94           O  
ANISOU  949  OG  SER A 123     4927   6743   5783    680    282   -978       O  
ATOM    950  N   GLY A 124      -2.978  -6.354  14.978  1.00 26.13           N  
ANISOU  950  N   GLY A 124     2754   3832   3340    707     15   -832       N  
ATOM    951  CA  GLY A 124      -2.931  -5.525  16.164  1.00 26.65           C  
ANISOU  951  CA  GLY A 124     2814   3858   3454    653      6   -795       C  
ATOM    952  C   GLY A 124      -4.306  -5.426  16.782  1.00 26.44           C  
ANISOU  952  C   GLY A 124     2928   3714   3404    585     -6   -678       C  
ATOM    953  O   GLY A 124      -5.305  -5.888  16.221  1.00 26.20           O  
ANISOU  953  O   GLY A 124     2985   3640   3329    566      3   -619       O  
ATOM    954  N   VAL A 125      -4.342  -4.811  17.961  1.00 29.32           N  
ANISOU  954  N   VAL A 125     3306   4037   3798    547    -26   -654       N  
ATOM    955  CA  VAL A 125      -5.551  -4.708  18.767  1.00 28.66           C  
ANISOU  955  CA  VAL A 125     3342   3857   3690    487    -38   -564       C  
ATOM    956  C   VAL A 125      -5.688  -3.268  19.241  1.00 29.07           C  
ANISOU  956  C   VAL A 125     3333   3922   3791    396     35   -527       C  
ATOM    957  O   VAL A 125      -4.701  -2.643  19.642  1.00 28.17           O  
ANISOU  957  O   VAL A 125     3126   3854   3726    400     34   -585       O  
ATOM    958  CB  VAL A 125      -5.505  -5.680  19.968  1.00 30.51           C  
ANISOU  958  CB  VAL A 125     3692   4011   3891    548   -166   -584       C  
ATOM    959  CG1 VAL A 125      -6.779  -5.597  20.775  1.00 32.16           C  
ANISOU  959  CG1 VAL A 125     4018   4141   4060    471   -162   -493       C  
ATOM    960  CG2 VAL A 125      -5.264  -7.105  19.501  1.00 33.18           C  
ANISOU  960  CG2 VAL A 125     4094   4318   4196    648   -258   -631       C  
ATOM    961  N   TYR A 126      -6.909  -2.738  19.194  1.00 26.58           N  
ANISOU  961  N   TYR A 126     3067   3565   3469    318     91   -439       N  
ATOM    962  CA  TYR A 126      -7.147  -1.388  19.685  1.00 28.13           C  
ANISOU  962  CA  TYR A 126     3218   3755   3716    242    147   -411       C  
ATOM    963  C   TYR A 126      -8.623  -1.217  20.005  1.00 26.49           C  
ANISOU  963  C   TYR A 126     3093   3485   3488    187    170   -336       C  
ATOM    964  O   TYR A 126      -9.482  -1.934  19.484  1.00 25.61           O  
ANISOU  964  O   TYR A 126     3048   3350   3333    186    168   -292       O  
ATOM    965  CB  TYR A 126      -6.686  -0.325  18.679  1.00 28.78           C  
ANISOU  965  CB  TYR A 126     3185   3896   3853    191    233   -400       C  
ATOM    966  CG  TYR A 126      -7.265  -0.463  17.289  1.00 30.07           C  
ANISOU  966  CG  TYR A 126     3356   4081   3988    169    288   -341       C  
ATOM    967  CD1 TYR A 126      -8.494   0.099  16.966  1.00 31.09           C  
ANISOU  967  CD1 TYR A 126     3526   4165   4122    110    329   -256       C  
ATOM    968  CD2 TYR A 126      -6.574  -1.142  16.294  1.00 31.37           C  
ANISOU  968  CD2 TYR A 126     3481   4318   4119    215    294   -381       C  
ATOM    969  CE1 TYR A 126      -9.022  -0.021  15.694  1.00 31.97           C  
ANISOU  969  CE1 TYR A 126     3648   4297   4201     92    366   -202       C  
ATOM    970  CE2 TYR A 126      -7.095  -1.266  15.020  1.00 33.20           C  
ANISOU  970  CE2 TYR A 126     3726   4578   4312    194    341   -331       C  
ATOM    971  CZ  TYR A 126      -8.318  -0.704  14.725  1.00 32.63           C  
ANISOU  971  CZ  TYR A 126     3703   4454   4240    132    373   -237       C  
ATOM    972  OH  TYR A 126      -8.839  -0.826  13.458  1.00 33.57           O  
ANISOU  972  OH  TYR A 126     3840   4602   4315    114    408   -188       O  
ATOM    973  N   GLN A 127      -8.901  -0.250  20.874  1.00 30.88           N  
ANISOU  973  N   GLN A 127     3636   4019   4079    142    190   -334       N  
ATOM    974  CA  GLN A 127     -10.253   0.018  21.336  1.00 32.24           C  
ANISOU  974  CA  GLN A 127     3865   4146   4237     94    216   -286       C  
ATOM    975  C   GLN A 127     -10.914   1.086  20.475  1.00 34.03           C  
ANISOU  975  C   GLN A 127     4038   4368   4524     42    288   -236       C  
ATOM    976  O   GLN A 127     -10.284   2.079  20.099  1.00 33.07           O  
ANISOU  976  O   GLN A 127     3839   4260   4467     21    319   -242       O  
ATOM    977  CB  GLN A 127     -10.238   0.464  22.797  1.00 33.19           C  
ANISOU  977  CB  GLN A 127     4004   4252   4356     82    194   -326       C  
ATOM    978  CG  GLN A 127     -11.609   0.525  23.436  1.00 38.82           C  
ANISOU  978  CG  GLN A 127     4777   4938   5035     38    220   -295       C  
ATOM    979  CD  GLN A 127     -11.991  -0.761  24.134  1.00 36.37           C  
ANISOU  979  CD  GLN A 127     4580   4615   4624     45    168   -282       C  
ATOM    980  OE1 GLN A 127     -11.435  -1.823  23.856  1.00 37.80           O  
ANISOU  980  OE1 GLN A 127     4808   4788   4767     89    108   -280       O  
ATOM    981  NE2 GLN A 127     -12.942  -0.670  25.056  1.00 36.68           N  
ANISOU  981  NE2 GLN A 127     4666   4652   4620     -1    190   -275       N  
ATOM    982  N   CYS A 128     -12.193   0.877  20.175  1.00 34.44           N  
ANISOU  982  N   CYS A 128     4135   4396   4555     19    308   -183       N  
ATOM    983  CA  CYS A 128     -12.975   1.803  19.372  1.00 35.77           C  
ANISOU  983  CA  CYS A 128     4266   4549   4776    -19    356   -132       C  
ATOM    984  C   CYS A 128     -14.325   2.035  20.035  1.00 33.74           C  
ANISOU  984  C   CYS A 128     4035   4263   4524    -44    369   -123       C  
ATOM    985  O   CYS A 128     -14.749   1.277  20.910  1.00 32.74           O  
ANISOU  985  O   CYS A 128     3965   4138   4339    -46    351   -141       O  
ATOM    986  CB  CYS A 128     -13.180   1.278  17.945  1.00 36.27           C  
ANISOU  986  CB  CYS A 128     4338   4632   4812    -13    365    -82       C  
ATOM    987  SG  CYS A 128     -11.857   1.699  16.794  1.00 40.35           S  
ANISOU  987  SG  CYS A 128     4784   5201   5346    -13    391    -79       S  
ATOM    988  N   ALA A 129     -14.997   3.098  19.605  1.00 30.44           N  
ANISOU  988  N   ALA A 129     3574   3819   4174    -67    400    -97       N  
ATOM    989  CA  ALA A 129     -16.329   3.433  20.083  1.00 29.94           C  
ANISOU  989  CA  ALA A 129     3510   3738   4130    -83    415   -101       C  
ATOM    990  C   ALA A 129     -17.276   3.572  18.901  1.00 28.77           C  
ANISOU  990  C   ALA A 129     3349   3576   4006    -89    421    -41       C  
ATOM    991  O   ALA A 129     -16.897   4.094  17.848  1.00 31.58           O  
ANISOU  991  O   ALA A 129     3684   3918   4396    -90    420      4       O  
ATOM    992  CB  ALA A 129     -16.319   4.730  20.899  1.00 30.91           C  
ANISOU  992  CB  ALA A 129     3585   3830   4328    -87    428   -152       C  
ATOM    993  N   MET A 130     -18.504   3.092  19.076  1.00 26.97           N  
ANISOU  993  N   MET A 130     3134   3358   3756   -100    425    -39       N  
ATOM    994  CA  MET A 130     -19.550   3.286  18.078  1.00 26.60           C  
ANISOU  994  CA  MET A 130     3066   3300   3740   -102    419      6       C  
ATOM    995  C   MET A 130     -20.056   4.718  18.195  1.00 29.36           C  
ANISOU  995  C   MET A 130     3355   3608   4193    -91    423    -11       C  
ATOM    996  O   MET A 130     -20.773   5.055  19.143  1.00 30.60           O  
ANISOU  996  O   MET A 130     3480   3770   4377    -90    441    -70       O  
ATOM    997  CB  MET A 130     -20.678   2.279  18.277  1.00 27.78           C  
ANISOU  997  CB  MET A 130     3236   3478   3839   -125    419      4       C  
ATOM    998  CG  MET A 130     -21.801   2.392  17.257  1.00 29.17           C  
ANISOU  998  CG  MET A 130     3384   3651   4049   -124    402     42       C  
ATOM    999  SD  MET A 130     -21.248   2.103  15.564  1.00 28.37           S  
ANISOU  999  SD  MET A 130     3317   3544   3920   -108    367    116       S  
ATOM   1000  CE  MET A 130     -20.812   0.367  15.638  1.00 26.86           C  
ANISOU 1000  CE  MET A 130     3204   3381   3620   -120    353    110       C  
ATOM   1001  N   ARG A 131     -19.670   5.566  17.239  1.00 29.31           N  
ANISOU 1001  N   ARG A 131     3335   3560   4240    -83    406     38       N  
ATOM   1002  CA  ARG A 131     -20.038   6.971  17.280  1.00 30.07           C  
ANISOU 1002  CA  ARG A 131     3389   3592   4444    -69    391     29       C  
ATOM   1003  C   ARG A 131     -21.557   7.129  17.227  1.00 33.58           C  
ANISOU 1003  C   ARG A 131     3797   4031   4931    -46    375     12       C  
ATOM   1004  O   ARG A 131     -22.271   6.223  16.788  1.00 30.58           O  
ANISOU 1004  O   ARG A 131     3426   3694   4499    -52    371     34       O  
ATOM   1005  CB  ARG A 131     -19.392   7.726  16.118  1.00 31.94           C  
ANISOU 1005  CB  ARG A 131     3639   3781   4717    -81    368    108       C  
ATOM   1006  CG  ARG A 131     -17.878   7.610  16.046  1.00 33.20           C  
ANISOU 1006  CG  ARG A 131     3813   3962   4840   -111    391    120       C  
ATOM   1007  CD  ARG A 131     -17.215   8.129  17.306  1.00 32.90           C  
ANISOU 1007  CD  ARG A 131     3750   3906   4845   -114    404     42       C  
ATOM   1008  NE  ARG A 131     -17.643   9.486  17.630  1.00 34.15           N  
ANISOU 1008  NE  ARG A 131     3881   3979   5116   -106    380     20       N  
ATOM   1009  CZ  ARG A 131     -17.192  10.180  18.669  1.00 34.79           C  
ANISOU 1009  CZ  ARG A 131     3939   4028   5253   -106    380    -55       C  
ATOM   1010  NH1 ARG A 131     -16.295   9.643  19.485  1.00 33.78           N  
ANISOU 1010  NH1 ARG A 131     3812   3952   5073   -115    401   -108       N  
ATOM   1011  NH2 ARG A 131     -17.635  11.409  18.892  1.00 32.63           N  
ANISOU 1011  NH2 ARG A 131     3644   3665   5088    -91    350    -82       N  
ATOM   1012  N   PRO A 132     -22.074   8.272  17.687  1.00 28.60           N  
ANISOU 1012  N   PRO A 132     3119   3348   4401    -16    360    -38       N  
ATOM   1013  CA  PRO A 132     -23.520   8.517  17.566  1.00 28.86           C  
ANISOU 1013  CA  PRO A 132     3097   3378   4489     18    337    -66       C  
ATOM   1014  C   PRO A 132     -24.035   8.434  16.139  1.00 29.91           C  
ANISOU 1014  C   PRO A 132     3246   3492   4628     28    283     23       C  
ATOM   1015  O   PRO A 132     -25.208   8.095  15.936  1.00 31.03           O  
ANISOU 1015  O   PRO A 132     3346   3666   4778     45    266      6       O  
ATOM   1016  CB  PRO A 132     -23.681   9.927  18.146  1.00 30.11           C  
ANISOU 1016  CB  PRO A 132     3210   3462   4768     62    314   -134       C  
ATOM   1017  CG  PRO A 132     -22.556  10.055  19.115  1.00 30.16           C  
ANISOU 1017  CG  PRO A 132     3237   3470   4752     38    351   -178       C  
ATOM   1018  CD  PRO A 132     -21.407   9.297  18.510  1.00 28.51           C  
ANISOU 1018  CD  PRO A 132     3092   3285   4456     -9    363    -94       C  
ATOM   1019  N   ASN A 133     -23.201   8.731  15.142  1.00 29.36           N  
ANISOU 1019  N   ASN A 133     3230   3379   4548     12    257    115       N  
ATOM   1020  CA  ASN A 133     -23.586   8.596  13.743  1.00 28.45           C  
ANISOU 1020  CA  ASN A 133     3145   3256   4411     15    206    206       C  
ATOM   1021  C   ASN A 133     -23.240   7.223  13.171  1.00 27.25           C  
ANISOU 1021  C   ASN A 133     3037   3183   4133    -19    231    244       C  
ATOM   1022  O   ASN A 133     -23.197   7.065  11.945  1.00 27.67           O  
ANISOU 1022  O   ASN A 133     3131   3240   4142    -26    197    323       O  
ATOM   1023  CB  ASN A 133     -22.950   9.710  12.905  1.00 30.24           C  
ANISOU 1023  CB  ASN A 133     3412   3394   4682      7    162    291       C  
ATOM   1024  CG  ASN A 133     -21.446   9.559  12.758  1.00 30.79           C  
ANISOU 1024  CG  ASN A 133     3526   3485   4689    -49    210    332       C  
ATOM   1025  OD1 ASN A 133     -20.805   8.808  13.492  1.00 28.71           O  
ANISOU 1025  OD1 ASN A 133     3256   3282   4371    -66    267    279       O  
ATOM   1026  ND2 ASN A 133     -20.874  10.286  11.805  1.00 29.69           N  
ANISOU 1026  ND2 ASN A 133     3430   3295   4555    -81    184    426       N  
ATOM   1027  N   PHE A 134     -22.980   6.240  14.036  1.00 30.60           N  
ANISOU 1027  N   PHE A 134     3463   3668   4497    -39    283    189       N  
ATOM   1028  CA  PHE A 134     -22.812   4.838  13.649  1.00 29.44           C  
ANISOU 1028  CA  PHE A 134     3358   3584   4243    -62    294    206       C  
ATOM   1029  C   PHE A 134     -21.610   4.622  12.733  1.00 28.73           C  
ANISOU 1029  C   PHE A 134     3321   3506   4087    -75    298    266       C  
ATOM   1030  O   PHE A 134     -21.637   3.768  11.844  1.00 29.43           O  
ANISOU 1030  O   PHE A 134     3448   3633   4102    -79    282    298       O  
ATOM   1031  CB  PHE A 134     -24.085   4.286  13.005  1.00 27.75           C  
ANISOU 1031  CB  PHE A 134     3132   3393   4018    -57    255    218       C  
ATOM   1032  CG  PHE A 134     -25.211   4.085  13.976  1.00 31.18           C  
ANISOU 1032  CG  PHE A 134     3505   3852   4489    -61    270    146       C  
ATOM   1033  CD1 PHE A 134     -25.239   2.975  14.803  1.00 29.91           C  
ANISOU 1033  CD1 PHE A 134     3361   3739   4263   -101    311    106       C  
ATOM   1034  CD2 PHE A 134     -26.237   5.011  14.070  1.00 33.28           C  
ANISOU 1034  CD2 PHE A 134     3697   4094   4854    -26    243    114       C  
ATOM   1035  CE1 PHE A 134     -26.273   2.788  15.702  1.00 32.71           C  
ANISOU 1035  CE1 PHE A 134     3659   4133   4638   -123    338     43       C  
ATOM   1036  CE2 PHE A 134     -27.273   4.830  14.966  1.00 32.82           C  
ANISOU 1036  CE2 PHE A 134     3566   4080   4826    -34    270     34       C  
ATOM   1037  CZ  PHE A 134     -27.291   3.717  15.783  1.00 34.55           C  
ANISOU 1037  CZ  PHE A 134     3801   4361   4967    -91    324      2       C  
ATOM   1038  N   THR A 135     -20.549   5.392  12.942  1.00 27.18           N  
ANISOU 1038  N   THR A 135     3124   3285   3919    -84    320    272       N  
ATOM   1039  CA  THR A 135     -19.252   5.133  12.339  1.00 26.41           C  
ANISOU 1039  CA  THR A 135     3056   3222   3758   -105    343    303       C  
ATOM   1040  C   THR A 135     -18.249   4.847  13.448  1.00 24.08           C  
ANISOU 1040  C   THR A 135     2748   2946   3454   -108    380    237       C  
ATOM   1041  O   THR A 135     -18.563   4.940  14.637  1.00 26.67           O  
ANISOU 1041  O   THR A 135     3057   3256   3819    -99    386    178       O  
ATOM   1042  CB  THR A 135     -18.782   6.315  11.480  1.00 27.19           C  
ANISOU 1042  CB  THR A 135     3158   3282   3891   -131    335    378       C  
ATOM   1043  OG1 THR A 135     -18.692   7.494  12.291  1.00 26.85           O  
ANISOU 1043  OG1 THR A 135     3084   3166   3953   -135    333    356       O  
ATOM   1044  CG2 THR A 135     -19.752   6.563  10.335  1.00 28.51           C  
ANISOU 1044  CG2 THR A 135     3350   3428   4052   -123    283    451       C  
ATOM   1045  N   ILE A 136     -17.032   4.473  13.055  1.00 26.81           N  
ANISOU 1045  N   ILE A 136     3103   3337   3746   -118    402    241       N  
ATOM   1046  CA  ILE A 136     -15.943   4.268  14.001  1.00 28.54           C  
ANISOU 1046  CA  ILE A 136     3304   3576   3963   -114    424    178       C  
ATOM   1047  C   ILE A 136     -14.670   4.861  13.416  1.00 29.91           C  
ANISOU 1047  C   ILE A 136     3449   3774   4141   -145    452    200       C  
ATOM   1048  O   ILE A 136     -14.504   4.947  12.195  1.00 30.11           O  
ANISOU 1048  O   ILE A 136     3484   3830   4128   -167    463    260       O  
ATOM   1049  CB  ILE A 136     -15.726   2.776  14.361  1.00 29.32           C  
ANISOU 1049  CB  ILE A 136     3438   3721   3982    -83    413    130       C  
ATOM   1050  CG1 ILE A 136     -15.240   1.985  13.146  1.00 26.70           C  
ANISOU 1050  CG1 ILE A 136     3126   3446   3574    -72    413    150       C  
ATOM   1051  CG2 ILE A 136     -16.991   2.157  14.947  1.00 26.92           C  
ANISOU 1051  CG2 ILE A 136     3165   3397   3668    -77    392    116       C  
ATOM   1052  CD1 ILE A 136     -14.828   0.568  13.476  1.00 30.25           C  
ANISOU 1052  CD1 ILE A 136     3612   3924   3957    -31    389     93       C  
ATOM   1053  N   LYS A 137     -13.771   5.278  14.301  1.00 35.17           N  
ANISOU 1053  N   LYS A 137     4079   4436   4850   -154    465    149       N  
ATOM   1054  CA  LYS A 137     -12.474   5.834  13.926  1.00 36.05           C  
ANISOU 1054  CA  LYS A 137     4144   4578   4974   -195    496    154       C  
ATOM   1055  C   LYS A 137     -11.419   4.776  14.241  1.00 36.09           C  
ANISOU 1055  C   LYS A 137     4128   4662   4923   -160    501     80       C  
ATOM   1056  O   LYS A 137     -10.890   4.715  15.352  1.00 37.89           O  
ANISOU 1056  O   LYS A 137     4334   4884   5177   -141    486     10       O  
ATOM   1057  CB  LYS A 137     -12.200   7.143  14.664  1.00 37.87           C  
ANISOU 1057  CB  LYS A 137     4340   4740   5308   -232    494    142       C  
ATOM   1058  CG  LYS A 137     -13.279   8.198  14.477  1.00 38.62           C  
ANISOU 1058  CG  LYS A 137     4458   4739   5475   -248    470    199       C  
ATOM   1059  CD  LYS A 137     -13.013   9.421  15.341  1.00 43.57           C  
ANISOU 1059  CD  LYS A 137     5057   5287   6211   -274    457    165       C  
ATOM   1060  CE  LYS A 137     -12.986   9.060  16.817  1.00 40.19           C  
ANISOU 1060  CE  LYS A 137     4613   4865   5790   -230    446     58       C  
ATOM   1061  NZ  LYS A 137     -12.893  10.265  17.686  1.00 46.48           N  
ANISOU 1061  NZ  LYS A 137     5387   5581   6692   -246    426     11       N  
ATOM   1062  N   GLY A 138     -11.118   3.939  13.252  1.00 36.82           N  
ANISOU 1062  N   GLY A 138     4228   4827   4936   -144    515     89       N  
ATOM   1063  CA  GLY A 138     -10.148   2.879  13.439  1.00 37.89           C  
ANISOU 1063  CA  GLY A 138     4341   5033   5022    -93    508      9       C  
ATOM   1064  C   GLY A 138      -8.965   2.975  12.498  1.00 38.67           C  
ANISOU 1064  C   GLY A 138     4372   5229   5091   -118    558     -1       C  
ATOM   1065  O   GLY A 138      -8.652   4.055  11.988  1.00 40.02           O  
ANISOU 1065  O   GLY A 138     4505   5407   5292   -195    603     52       O  
ATOM   1066  N   SER A 139      -8.296   1.847  12.266  1.00 35.65           N  
ANISOU 1066  N   SER A 139     3975   4922   4648    -56    549    -74       N  
ATOM   1067  CA  SER A 139      -7.152   1.770  11.359  1.00 36.58           C  
ANISOU 1067  CA  SER A 139     4014   5159   4726    -69    603   -108       C  
ATOM   1068  C   SER A 139      -7.345   0.531  10.490  1.00 36.90           C  
ANISOU 1068  C   SER A 139     4094   5254   4671     -2    591   -138       C  
ATOM   1069  O   SER A 139      -7.043  -0.587  10.918  1.00 38.64           O  
ANISOU 1069  O   SER A 139     4326   5482   4875     88    537   -227       O  
ATOM   1070  CB  SER A 139      -5.836   1.715  12.128  1.00 38.42           C  
ANISOU 1070  CB  SER A 139     4154   5440   5003    -44    598   -209       C  
ATOM   1071  OG  SER A 139      -4.765   1.346  11.278  1.00 39.85           O  
ANISOU 1071  OG  SER A 139     4249   5756   5138    -34    646   -271       O  
ATOM   1072  N   PHE A 140      -7.845   0.732   9.273  1.00 40.61           N  
ANISOU 1072  N   PHE A 140     4592   5757   5079    -45    629    -67       N  
ATOM   1073  CA  PHE A 140      -8.206  -0.363   8.378  1.00 40.83           C  
ANISOU 1073  CA  PHE A 140     4670   5830   5014     12    612    -91       C  
ATOM   1074  C   PHE A 140      -7.598  -0.104   7.006  1.00 44.22           C  
ANISOU 1074  C   PHE A 140     5052   6390   5360    -35    692    -79       C  
ATOM   1075  O   PHE A 140      -8.041   0.798   6.288  1.00 46.13           O  
ANISOU 1075  O   PHE A 140     5316   6631   5580   -121    731     29       O  
ATOM   1076  CB  PHE A 140      -9.726  -0.507   8.284  1.00 38.41           C  
ANISOU 1076  CB  PHE A 140     4467   5428   4700     10    563    -15       C  
ATOM   1077  CG  PHE A 140     -10.377  -0.930   9.571  1.00 37.69           C  
ANISOU 1077  CG  PHE A 140     4425   5229   4668     49    493    -34       C  
ATOM   1078  CD1 PHE A 140     -10.330  -2.251   9.987  1.00 36.84           C  
ANISOU 1078  CD1 PHE A 140     4358   5104   4535    129    431   -112       C  
ATOM   1079  CD2 PHE A 140     -11.040  -0.007  10.363  1.00 36.56           C  
ANISOU 1079  CD2 PHE A 140     4290   5000   4599      2    488     24       C  
ATOM   1080  CE1 PHE A 140     -10.930  -2.642  11.170  1.00 37.28           C  
ANISOU 1080  CE1 PHE A 140     4469   5066   4630    147    372   -116       C  
ATOM   1081  CE2 PHE A 140     -11.643  -0.392  11.546  1.00 35.73           C  
ANISOU 1081  CE2 PHE A 140     4227   4815   4531     29    437      4       C  
ATOM   1082  CZ  PHE A 140     -11.588  -1.711  11.950  1.00 34.78           C  
ANISOU 1082  CZ  PHE A 140     4154   4685   4375     93    382    -59       C  
ATOM   1083  N   LEU A 141      -6.592  -0.894   6.639  1.00 42.33           N  
ANISOU 1083  N   LEU A 141     4748   6266   5071     23    714   -191       N  
ATOM   1084  CA  LEU A 141      -5.968  -0.792   5.330  1.00 44.02           C  
ANISOU 1084  CA  LEU A 141     4909   6632   5186    -17    800   -200       C  
ATOM   1085  C   LEU A 141      -6.671  -1.719   4.340  1.00 44.27           C  
ANISOU 1085  C   LEU A 141     5020   6688   5110     36    773   -212       C  
ATOM   1086  O   LEU A 141      -7.681  -2.356   4.649  1.00 39.23           O  
ANISOU 1086  O   LEU A 141     4478   5943   4486     90    688   -200       O  
ATOM   1087  CB  LEU A 141      -4.481  -1.135   5.409  1.00 45.19           C  
ANISOU 1087  CB  LEU A 141     4923   6911   5335     22    844   -336       C  
ATOM   1088  CG  LEU A 141      -3.476  -0.120   5.944  1.00 51.63           C  
ANISOU 1088  CG  LEU A 141     5623   7766   6228    -58    903   -337       C  
ATOM   1089  CD1 LEU A 141      -2.430  -0.850   6.761  1.00 51.92           C  
ANISOU 1089  CD1 LEU A 141     5563   7842   6320     46    864   -494       C  
ATOM   1090  CD2 LEU A 141      -2.826   0.635   4.799  1.00 51.45           C  
ANISOU 1090  CD2 LEU A 141     5525   7895   6129   -176   1027   -296       C  
ATOM   1091  N   ASN A 142      -6.126  -1.793   3.128  1.00 46.35           N  
ANISOU 1091  N   ASN A 142     5244   7105   5263     13    849   -238       N  
ATOM   1092  CA  ASN A 142      -6.597  -2.761   2.147  1.00 45.15           C  
ANISOU 1092  CA  ASN A 142     5155   7000   4999     74    824   -281       C  
ATOM   1093  C   ASN A 142      -6.254  -4.169   2.619  1.00 45.31           C  
ANISOU 1093  C   ASN A 142     5168   7006   5040    220    749   -441       C  
ATOM   1094  O   ASN A 142      -5.078  -4.499   2.809  1.00 44.16           O  
ANISOU 1094  O   ASN A 142     4917   6953   4908    274    777   -565       O  
ATOM   1095  CB  ASN A 142      -5.973  -2.481   0.782  1.00 47.19           C  
ANISOU 1095  CB  ASN A 142     5364   7446   5121     13    932   -285       C  
ATOM   1096  CG  ASN A 142      -6.799  -1.519  -0.049  1.00 48.61           C  
ANISOU 1096  CG  ASN A 142     5625   7613   5233   -105    959   -116       C  
ATOM   1097  OD1 ASN A 142      -8.020  -1.649  -0.139  1.00 46.75           O  
ANISOU 1097  OD1 ASN A 142     5499   7267   4996    -91    880    -44       O  
ATOM   1098  ND2 ASN A 142      -6.136  -0.546  -0.662  1.00 52.96           N  
ANISOU 1098  ND2 ASN A 142     6122   8275   5728   -225   1066    -49       N  
ATOM   1099  N   GLY A 143      -7.279  -4.995   2.817  1.00 39.51           N  
ANISOU 1099  N   GLY A 143     4545   6153   4314    281    648   -439       N  
ATOM   1100  CA  GLY A 143      -7.108  -6.332   3.349  1.00 41.98           C  
ANISOU 1100  CA  GLY A 143     4883   6412   4657    411    553   -569       C  
ATOM   1101  C   GLY A 143      -7.576  -6.504   4.776  1.00 38.81           C  
ANISOU 1101  C   GLY A 143     4534   5843   4367    432    464   -540       C  
ATOM   1102  O   GLY A 143      -7.458  -7.610   5.318  1.00 39.14           O  
ANISOU 1102  O   GLY A 143     4615   5819   4438    531    372   -632       O  
ATOM   1103  N   SER A 144      -8.103  -5.452   5.402  1.00 36.06           N  
ANISOU 1103  N   SER A 144     4195   5424   4081    341    485   -418       N  
ATOM   1104  CA  SER A 144      -8.577  -5.508   6.778  1.00 34.98           C  
ANISOU 1104  CA  SER A 144     4106   5147   4037    348    415   -388       C  
ATOM   1105  C   SER A 144     -10.066  -5.792   6.890  1.00 31.14           C  
ANISOU 1105  C   SER A 144     3733   4546   3554    324    354   -309       C  
ATOM   1106  O   SER A 144     -10.543  -6.066   7.997  1.00 28.83           O  
ANISOU 1106  O   SER A 144     3491   4143   3320    331    293   -295       O  
ATOM   1107  CB  SER A 144      -8.268  -4.193   7.497  1.00 35.70           C  
ANISOU 1107  CB  SER A 144     4132   5230   4202    269    470   -322       C  
ATOM   1108  OG  SER A 144      -8.915  -3.116   6.847  1.00 41.06           O  
ANISOU 1108  OG  SER A 144     4820   5918   4865    170    527   -203       O  
ATOM   1109  N   CYS A 145     -10.809  -5.715   5.788  1.00 29.33           N  
ANISOU 1109  N   CYS A 145     3541   4345   3257    290    369   -259       N  
ATOM   1110  CA  CYS A 145     -12.222  -6.062   5.821  1.00 25.98           C  
ANISOU 1110  CA  CYS A 145     3210   3824   2838    270    305   -200       C  
ATOM   1111  C   CYS A 145     -12.396  -7.498   6.295  1.00 27.37           C  
ANISOU 1111  C   CYS A 145     3458   3921   3019    343    209   -279       C  
ATOM   1112  O   CYS A 145     -11.652  -8.398   5.894  1.00 28.20           O  
ANISOU 1112  O   CYS A 145     3563   4069   3084    424    182   -386       O  
ATOM   1113  CB  CYS A 145     -12.847  -5.874   4.440  1.00 27.58           C  
ANISOU 1113  CB  CYS A 145     3438   4084   2957    237    323   -153       C  
ATOM   1114  SG  CYS A 145     -12.818  -4.167   3.853  1.00 30.00           S  
ANISOU 1114  SG  CYS A 145     3693   4453   3254    137    414    -31       S  
ATOM   1115  N   GLY A 146     -13.380  -7.708   7.164  1.00 25.25           N  
ANISOU 1115  N   GLY A 146     3253   3539   2802    313    155   -230       N  
ATOM   1116  CA  GLY A 146     -13.578  -8.976   7.820  1.00 24.63           C  
ANISOU 1116  CA  GLY A 146     3257   3366   2738    358     61   -281       C  
ATOM   1117  C   GLY A 146     -13.079  -9.022   9.249  1.00 24.10           C  
ANISOU 1117  C   GLY A 146     3192   3237   2729    372     37   -293       C  
ATOM   1118  O   GLY A 146     -13.486  -9.914  10.003  1.00 25.46           O  
ANISOU 1118  O   GLY A 146     3451   3309   2915    379    -43   -298       O  
ATOM   1119  N   SER A 147     -12.202  -8.097   9.635  1.00 27.19           N  
ANISOU 1119  N   SER A 147     3496   3685   3150    370     99   -295       N  
ATOM   1120  CA  SER A 147     -11.808  -7.982  11.032  1.00 27.90           C  
ANISOU 1120  CA  SER A 147     3587   3722   3293    374     75   -299       C  
ATOM   1121  C   SER A 147     -13.018  -7.618  11.883  1.00 25.36           C  
ANISOU 1121  C   SER A 147     3313   3321   3001    292     74   -210       C  
ATOM   1122  O   SER A 147     -13.907  -6.879  11.453  1.00 26.20           O  
ANISOU 1122  O   SER A 147     3401   3440   3115    228    122   -141       O  
ATOM   1123  CB  SER A 147     -10.707  -6.934  11.195  1.00 28.71           C  
ANISOU 1123  CB  SER A 147     3576   3905   3426    374    145   -318       C  
ATOM   1124  OG  SER A 147      -9.782  -6.996  10.124  1.00 30.29           O  
ANISOU 1124  OG  SER A 147     3707   4214   3589    419    183   -385       O  
ATOM   1125  N   VAL A 148     -13.049  -8.146  13.103  1.00 25.71           N  
ANISOU 1125  N   VAL A 148     3420   3289   3060    297     16   -216       N  
ATOM   1126  CA  VAL A 148     -14.243  -8.081  13.932  1.00 25.06           C  
ANISOU 1126  CA  VAL A 148     3392   3140   2989    218     12   -146       C  
ATOM   1127  C   VAL A 148     -13.970  -7.265  15.187  1.00 24.36           C  
ANISOU 1127  C   VAL A 148     3272   3048   2934    192     40   -132       C  
ATOM   1128  O   VAL A 148     -12.832  -7.155  15.655  1.00 23.73           O  
ANISOU 1128  O   VAL A 148     3163   2988   2866    244     26   -183       O  
ATOM   1129  CB  VAL A 148     -14.752  -9.491  14.305  1.00 23.52           C  
ANISOU 1129  CB  VAL A 148     3322   2852   2763    219    -82   -149       C  
ATOM   1130  CG1 VAL A 148     -15.161 -10.252  13.054  1.00 27.27           C  
ANISOU 1130  CG1 VAL A 148     3829   3323   3208    237   -115   -167       C  
ATOM   1131  CG2 VAL A 148     -13.689 -10.254  15.078  1.00 26.56           C  
ANISOU 1131  CG2 VAL A 148     3760   3193   3140    293   -164   -207       C  
ATOM   1132  N   GLY A 149     -15.039  -6.680  15.725  1.00 23.88           N  
ANISOU 1132  N   GLY A 149     3212   2970   2891    114     79    -74       N  
ATOM   1133  CA  GLY A 149     -15.010  -6.018  17.015  1.00 21.63           C  
ANISOU 1133  CA  GLY A 149     2914   2678   2627     83    101    -68       C  
ATOM   1134  C   GLY A 149     -15.733  -6.873  18.038  1.00 23.18           C  
ANISOU 1134  C   GLY A 149     3212   2814   2783     37     56    -44       C  
ATOM   1135  O   GLY A 149     -16.674  -7.596  17.704  1.00 23.72           O  
ANISOU 1135  O   GLY A 149     3334   2850   2827     -4     37    -13       O  
ATOM   1136  N   PHE A 150     -15.293  -6.791  19.292  1.00 22.26           N  
ANISOU 1136  N   PHE A 150     3122   2684   2651     36     39    -58       N  
ATOM   1137  CA  PHE A 150     -15.801  -7.711  20.299  1.00 24.69           C  
ANISOU 1137  CA  PHE A 150     3546   2936   2900    -11    -11    -30       C  
ATOM   1138  C   PHE A 150     -15.620  -7.128  21.692  1.00 27.29           C  
ANISOU 1138  C   PHE A 150     3878   3281   3211    -38      7    -36       C  
ATOM   1139  O   PHE A 150     -14.774  -6.260  21.924  1.00 27.33           O  
ANISOU 1139  O   PHE A 150     3810   3322   3251      6     26    -78       O  
ATOM   1140  CB  PHE A 150     -15.101  -9.072  20.206  1.00 23.56           C  
ANISOU 1140  CB  PHE A 150     3508   2726   2720     50   -123    -50       C  
ATOM   1141  CG  PHE A 150     -13.624  -9.014  20.488  1.00 24.09           C  
ANISOU 1141  CG  PHE A 150     3553   2802   2798    149   -175   -114       C  
ATOM   1142  CD1 PHE A 150     -12.726  -8.694  19.483  1.00 24.95           C  
ANISOU 1142  CD1 PHE A 150     3568   2962   2952    229   -161   -172       C  
ATOM   1143  CD2 PHE A 150     -13.135  -9.279  21.757  1.00 30.06           C  
ANISOU 1143  CD2 PHE A 150     4381   3525   3516    158   -238   -118       C  
ATOM   1144  CE1 PHE A 150     -11.368  -8.637  19.738  1.00 27.04           C  
ANISOU 1144  CE1 PHE A 150     3792   3248   3234    316   -205   -241       C  
ATOM   1145  CE2 PHE A 150     -11.779  -9.223  22.019  1.00 29.42           C  
ANISOU 1145  CE2 PHE A 150     4269   3456   3452    254   -296   -186       C  
ATOM   1146  CZ  PHE A 150     -10.895  -8.903  21.008  1.00 27.97           C  
ANISOU 1146  CZ  PHE A 150     3975   3328   3326    334   -278   -252       C  
ATOM   1147  N   ASN A 151     -16.440  -7.626  22.614  1.00 31.11           N  
ANISOU 1147  N   ASN A 151     4448   3741   3633   -118      1      4       N  
ATOM   1148  CA  ASN A 151     -16.273  -7.436  24.046  1.00 30.35           C  
ANISOU 1148  CA  ASN A 151     4396   3653   3482   -148     -3      1       C  
ATOM   1149  C   ASN A 151     -16.185  -8.803  24.713  1.00 32.29           C  
ANISOU 1149  C   ASN A 151     4805   3825   3641   -170   -102     40       C  
ATOM   1150  O   ASN A 151     -16.664  -9.807  24.178  1.00 31.79           O  
ANISOU 1150  O   ASN A 151     4815   3703   3562   -196   -145     78       O  
ATOM   1151  CB  ASN A 151     -17.431  -6.630  24.652  1.00 32.18           C  
ANISOU 1151  CB  ASN A 151     4578   3943   3707   -241     98     14       C  
ATOM   1152  CG  ASN A 151     -17.338  -5.148  24.346  1.00 32.20           C  
ANISOU 1152  CG  ASN A 151     4438   4002   3795   -209    174    -32       C  
ATOM   1153  OD1 ASN A 151     -16.544  -4.426  24.948  1.00 33.60           O  
ANISOU 1153  OD1 ASN A 151     4582   4199   3986   -171    173    -77       O  
ATOM   1154  ND2 ASN A 151     -18.160  -4.685  23.412  1.00 31.76           N  
ANISOU 1154  ND2 ASN A 151     4302   3965   3800   -226    229    -20       N  
ATOM   1155  N   ILE A 152     -15.563  -8.842  25.886  1.00 33.61           N  
ANISOU 1155  N   ILE A 152     5036   3985   3749   -160   -150     32       N  
ATOM   1156  CA  ILE A 152     -15.401 -10.073  26.652  1.00 35.46           C  
ANISOU 1156  CA  ILE A 152     5443   4139   3891   -180   -260     78       C  
ATOM   1157  C   ILE A 152     -16.223  -9.919  27.928  1.00 41.77           C  
ANISOU 1157  C   ILE A 152     6303   4976   4592   -303   -207    123       C  
ATOM   1158  O   ILE A 152     -15.836  -9.184  28.843  1.00 40.45           O  
ANISOU 1158  O   ILE A 152     6112   4863   4394   -295   -186     90       O  
ATOM   1159  CB  ILE A 152     -13.928 -10.371  26.955  1.00 32.90           C  
ANISOU 1159  CB  ILE A 152     5158   3774   3568    -59   -381     30       C  
ATOM   1160  CG1 ILE A 152     -13.151 -10.581  25.653  1.00 33.37           C  
ANISOU 1160  CG1 ILE A 152     5146   3815   3718     57   -421    -27       C  
ATOM   1161  CG2 ILE A 152     -13.804 -11.596  27.849  1.00 42.11           C  
ANISOU 1161  CG2 ILE A 152     6520   4845   4634    -81   -510     87       C  
ATOM   1162  CD1 ILE A 152     -11.705 -10.974  25.858  1.00 36.62           C  
ANISOU 1162  CD1 ILE A 152     5578   4192   4142    187   -547    -90       C  
ATOM   1163  N   ASP A 153     -17.403 -10.542  27.943  1.00 53.37           N  
ANISOU 1163  N   ASP A 153     7835   6430   6013   -423   -174    192       N  
ATOM   1164  CA  ASP A 153     -18.326 -10.433  29.104  1.00 57.10           C  
ANISOU 1164  CA  ASP A 153     8354   6961   6381   -562   -102    234       C  
ATOM   1165  C   ASP A 153     -18.145 -11.645  30.021  1.00 59.67           C  
ANISOU 1165  C   ASP A 153     8888   7203   6580   -621   -212    313       C  
ATOM   1166  O   ASP A 153     -18.470 -12.764  29.594  1.00 61.11           O  
ANISOU 1166  O   ASP A 153     9176   7291   6752   -664   -279    375       O  
ATOM   1167  CB  ASP A 153     -19.774 -10.242  28.647  1.00 57.24           C  
ANISOU 1167  CB  ASP A 153     8290   7035   6422   -672     15    253       C  
ATOM   1168  CG  ASP A 153     -19.998  -8.928  27.920  1.00 58.44           C  
ANISOU 1168  CG  ASP A 153     8248   7267   6689   -615    114    180       C  
ATOM   1169  OD1 ASP A 153     -19.317  -7.948  28.270  1.00 57.61           O  
ANISOU 1169  OD1 ASP A 153     8073   7205   6610   -543    134    120       O  
ATOM   1170  OD2 ASP A 153     -20.849  -8.896  27.013  1.00 57.83           O  
ANISOU 1170  OD2 ASP A 153     8096   7202   6674   -645    162    186       O  
ATOM   1171  N   TYR A 154     -17.657 -11.411  31.240  1.00 67.45           N  
ANISOU 1171  N   TYR A 154     9938   8218   7471   -625   -235    310       N  
ATOM   1172  CA  TYR A 154     -17.417 -12.508  32.212  1.00 73.06           C  
ANISOU 1172  CA  TYR A 154    10867   8848   8046   -680   -353    394       C  
ATOM   1173  C   TYR A 154     -16.562 -13.586  31.528  1.00 73.16           C  
ANISOU 1173  C   TYR A 154    10980   8708   8110   -573   -523    410       C  
ATOM   1174  O   TYR A 154     -15.332 -13.429  31.500  1.00 74.84           O  
ANISOU 1174  O   TYR A 154    11176   8894   8366   -426   -618    347       O  
ATOM   1175  CB  TYR A 154     -18.739 -12.968  32.843  1.00 72.28           C  
ANISOU 1175  CB  TYR A 154    10851   8782   7829   -881   -274    485       C  
ATOM   1176  CG  TYR A 154     -18.630 -14.126  33.805  1.00 74.84           C  
ANISOU 1176  CG  TYR A 154    11417   9016   8002   -969   -390    594       C  
ATOM   1177  CD1 TYR A 154     -19.595 -15.118  33.838  1.00 76.70           C  
ANISOU 1177  CD1 TYR A 154    11772   9198   8171  -1133   -387    701       C  
ATOM   1178  CD2 TYR A 154     -17.528 -14.266  34.631  1.00 75.04           C  
ANISOU 1178  CD2 TYR A 154    11558   8998   7956   -888   -518    595       C  
ATOM   1179  CE1 TYR A 154     -19.487 -16.202  34.692  1.00 77.71           C  
ANISOU 1179  CE1 TYR A 154    12141   9226   8159  -1224   -504    816       C  
ATOM   1180  CE2 TYR A 154     -17.405 -15.343  35.492  1.00 75.48           C  
ANISOU 1180  CE2 TYR A 154    11852   8956   7870   -963   -644    705       C  
ATOM   1181  CZ  TYR A 154     -18.387 -16.315  35.521  1.00 76.03           C  
ANISOU 1181  CZ  TYR A 154    12052   8966   7870  -1135   -637    822       C  
ATOM   1182  OH  TYR A 154     -18.272 -17.378  36.367  1.00 79.87           O  
ANISOU 1182  OH  TYR A 154    12790   9343   8213  -1222   -768    944       O  
ATOM   1183  N   ASP A 155     -17.197 -14.610  30.951  1.00 55.45           N  
ANISOU 1183  N   ASP A 155     8823   6373   5873   -641   -560    476       N  
ATOM   1184  CA  ASP A 155     -16.478 -15.723  30.279  1.00 55.95           C  
ANISOU 1184  CA  ASP A 155     8991   6280   5986   -540   -729    481       C  
ATOM   1185  C   ASP A 155     -17.097 -15.915  28.897  1.00 54.13           C  
ANISOU 1185  C   ASP A 155     8672   6033   5861   -542   -682    462       C  
ATOM   1186  O   ASP A 155     -17.238 -17.071  28.463  1.00 54.87           O  
ANISOU 1186  O   ASP A 155     8891   5997   5962   -557   -787    505       O  
ATOM   1187  CB  ASP A 155     -16.652 -17.023  31.064  1.00 58.53           C  
ANISOU 1187  CB  ASP A 155     9567   6474   6196   -635   -859    597       C  
ATOM   1188  CG  ASP A 155     -18.082 -17.537  31.058  1.00 58.81           C  
ANISOU 1188  CG  ASP A 155     9661   6504   6180   -840   -780    693       C  
ATOM   1189  OD1 ASP A 155     -18.980 -16.786  30.628  1.00 57.68           O  
ANISOU 1189  OD1 ASP A 155     9355   6482   6078   -908   -615    664       O  
ATOM   1190  OD2 ASP A 155     -18.287 -18.686  31.488  1.00 62.99           O  
ANISOU 1190  OD2 ASP A 155    10398   6905   6630   -931   -889    795       O  
ATOM   1191  N   CYS A 156     -17.451 -14.813  28.241  1.00 46.28           N  
ANISOU 1191  N   CYS A 156     7479   5160   4946   -526   -540    399       N  
ATOM   1192  CA  CYS A 156     -18.120 -14.917  26.957  1.00 44.25           C  
ANISOU 1192  CA  CYS A 156     7138   4901   4776   -536   -493    384       C  
ATOM   1193  C   CYS A 156     -17.600 -13.848  26.012  1.00 41.54           C  
ANISOU 1193  C   CYS A 156     6602   4640   4540   -410   -428    287       C  
ATOM   1194  O   CYS A 156     -17.427 -12.688  26.400  1.00 40.69           O  
ANISOU 1194  O   CYS A 156     6382   4635   4443   -392   -340    248       O  
ATOM   1195  CB  CYS A 156     -19.633 -14.776  27.114  1.00 43.46           C  
ANISOU 1195  CB  CYS A 156     7005   4865   4641   -714   -369    439       C  
ATOM   1196  SG  CYS A 156     -20.484 -14.554  25.554  1.00 43.98           S  
ANISOU 1196  SG  CYS A 156     6925   4964   4822   -715   -297    403       S  
ATOM   1197  N   VAL A 157     -17.351 -14.244  24.771  1.00 37.74           N  
ANISOU 1197  N   VAL A 157     6091   4114   4134   -328   -473    249       N  
ATOM   1198  CA  VAL A 157     -16.902 -13.323  23.735  1.00 34.07           C  
ANISOU 1198  CA  VAL A 157     5457   3727   3761   -225   -410    170       C  
ATOM   1199  C   VAL A 157     -18.128 -12.814  22.989  1.00 32.18           C  
ANISOU 1199  C   VAL A 157     5115   3552   3560   -308   -296    186       C  
ATOM   1200  O   VAL A 157     -18.827 -13.585  22.324  1.00 32.14           O  
ANISOU 1200  O   VAL A 157     5154   3496   3562   -356   -323    211       O  
ATOM   1201  CB  VAL A 157     -15.913 -14.000  22.777  1.00 32.91           C  
ANISOU 1201  CB  VAL A 157     5326   3516   3663    -86   -516    109       C  
ATOM   1202  CG1 VAL A 157     -15.580 -13.068  21.626  1.00 32.26           C  
ANISOU 1202  CG1 VAL A 157     5073   3527   3659     -9   -436     40       C  
ATOM   1203  CG2 VAL A 157     -14.654 -14.406  23.524  1.00 33.58           C  
ANISOU 1203  CG2 VAL A 157     5489   3546   3724     13   -636     78       C  
ATOM   1204  N   SER A 158     -18.387 -11.516  23.093  1.00 29.74           N  
ANISOU 1204  N   SER A 158     4669   3349   3281   -320   -180    164       N  
ATOM   1205  CA  SER A 158     -19.550 -10.898  22.463  1.00 29.59           C  
ANISOU 1205  CA  SER A 158     4541   3395   3305   -387    -79    172       C  
ATOM   1206  C   SER A 158     -19.085 -10.173  21.205  1.00 27.82           C  
ANISOU 1206  C   SER A 158     4197   3210   3162   -287    -55    122       C  
ATOM   1207  O   SER A 158     -18.578  -9.051  21.274  1.00 27.54           O  
ANISOU 1207  O   SER A 158     4064   3235   3166   -238     -1     87       O  
ATOM   1208  CB  SER A 158     -20.250  -9.951  23.431  1.00 29.46           C  
ANISOU 1208  CB  SER A 158     4460   3464   3270   -467     26    178       C  
ATOM   1209  OG  SER A 158     -20.935 -10.673  24.440  1.00 35.18           O  
ANISOU 1209  OG  SER A 158     5290   4172   3906   -590     22    234       O  
ATOM   1210  N   PHE A 159     -19.256 -10.822  20.056  1.00 29.00           N  
ANISOU 1210  N   PHE A 159     4362   3325   3334   -264    -97    119       N  
ATOM   1211  CA  PHE A 159     -18.936 -10.201  18.779  1.00 26.43           C  
ANISOU 1211  CA  PHE A 159     3932   3044   3065   -187    -69     81       C  
ATOM   1212  C   PHE A 159     -19.999  -9.166  18.435  1.00 25.68           C  
ANISOU 1212  C   PHE A 159     3725   3019   3013   -243     25     99       C  
ATOM   1213  O   PHE A 159     -21.198  -9.457  18.485  1.00 27.37           O  
ANISOU 1213  O   PHE A 159     3947   3232   3222   -333     41    130       O  
ATOM   1214  CB  PHE A 159     -18.844 -11.256  17.677  1.00 27.73           C  
ANISOU 1214  CB  PHE A 159     4154   3155   3226   -146   -147     64       C  
ATOM   1215  CG  PHE A 159     -17.730 -12.243  17.873  1.00 26.86           C  
ANISOU 1215  CG  PHE A 159     4143   2972   3090    -64   -253     28       C  
ATOM   1216  CD1 PHE A 159     -16.419 -11.892  17.597  1.00 24.60           C  
ANISOU 1216  CD1 PHE A 159     3804   2721   2823     52   -263    -35       C  
ATOM   1217  CD2 PHE A 159     -17.994 -13.524  18.329  1.00 26.27           C  
ANISOU 1217  CD2 PHE A 159     4214   2791   2977   -103   -348     55       C  
ATOM   1218  CE1 PHE A 159     -15.391 -12.798  17.774  1.00 24.53           C  
ANISOU 1218  CE1 PHE A 159     3872   2648   2800    143   -369    -84       C  
ATOM   1219  CE2 PHE A 159     -16.971 -14.435  18.508  1.00 26.99           C  
ANISOU 1219  CE2 PHE A 159     4402   2800   3053    -13   -465     17       C  
ATOM   1220  CZ  PHE A 159     -15.668 -14.072  18.230  1.00 25.92           C  
ANISOU 1220  CZ  PHE A 159     4200   2707   2941    118   -477    -59       C  
ATOM   1221  N   CYS A 160     -19.559  -7.959  18.083  1.00 24.82           N  
ANISOU 1221  N   CYS A 160     3511   2968   2951   -191     80     76       N  
ATOM   1222  CA  CYS A 160     -20.476  -6.854  17.837  1.00 24.64           C  
ANISOU 1222  CA  CYS A 160     3384   2999   2980   -228    155     88       C  
ATOM   1223  C   CYS A 160     -20.276  -6.148  16.506  1.00 23.95           C  
ANISOU 1223  C   CYS A 160     3221   2942   2936   -173    170     84       C  
ATOM   1224  O   CYS A 160     -21.171  -5.401  16.094  1.00 25.33           O  
ANISOU 1224  O   CYS A 160     3326   3146   3154   -199    207    101       O  
ATOM   1225  CB  CYS A 160     -20.366  -5.809  18.958  1.00 24.00           C  
ANISOU 1225  CB  CYS A 160     3251   2952   2918   -240    214     73       C  
ATOM   1226  SG  CYS A 160     -18.707  -5.134  19.181  1.00 25.21           S  
ANISOU 1226  SG  CYS A 160     3379   3112   3087   -153    208     33       S  
ATOM   1227  N   TYR A 161     -19.157  -6.356  15.816  1.00 21.37           N  
ANISOU 1227  N   TYR A 161     2907   2616   2597   -101    141     62       N  
ATOM   1228  CA  TYR A 161     -18.835  -5.553  14.648  1.00 22.42           C  
ANISOU 1228  CA  TYR A 161     2970   2793   2757    -62    168     65       C  
ATOM   1229  C   TYR A 161     -18.006  -6.374  13.671  1.00 24.25           C  
ANISOU 1229  C   TYR A 161     3238   3031   2946     -1    124     34       C  
ATOM   1230  O   TYR A 161     -17.201  -7.211  14.083  1.00 23.84           O  
ANISOU 1230  O   TYR A 161     3240   2952   2866     40     78     -5       O  
ATOM   1231  CB  TYR A 161     -18.076  -4.285  15.061  1.00 22.25           C  
ANISOU 1231  CB  TYR A 161     2876   2799   2779    -44    220     57       C  
ATOM   1232  CG  TYR A 161     -17.643  -3.397  13.917  1.00 23.13           C  
ANISOU 1232  CG  TYR A 161     2926   2951   2913    -21    250     73       C  
ATOM   1233  CD1 TYR A 161     -18.518  -2.477  13.356  1.00 24.72           C  
ANISOU 1233  CD1 TYR A 161     3081   3158   3154    -49    274    117       C  
ATOM   1234  CD2 TYR A 161     -16.352  -3.468  13.409  1.00 23.66           C  
ANISOU 1234  CD2 TYR A 161     2978   3053   2958     26    253     43       C  
ATOM   1235  CE1 TYR A 161     -18.123  -1.659  12.314  1.00 23.11           C  
ANISOU 1235  CE1 TYR A 161     2838   2982   2959    -39    295    147       C  
ATOM   1236  CE2 TYR A 161     -15.949  -2.655  12.368  1.00 24.84           C  
ANISOU 1236  CE2 TYR A 161     3076   3249   3114     28    290     67       C  
ATOM   1237  CZ  TYR A 161     -16.838  -1.753  11.823  1.00 25.22           C  
ANISOU 1237  CZ  TYR A 161     3099   3292   3194     -9    309    126       C  
ATOM   1238  OH  TYR A 161     -16.439  -0.941  10.786  1.00 25.21           O  
ANISOU 1238  OH  TYR A 161     3063   3328   3187    -18    339    165       O  
ATOM   1239  N   MET A 162     -18.227  -6.139  12.379  1.00 23.01           N  
ANISOU 1239  N   MET A 162     3052   2910   2781     10    133     48       N  
ATOM   1240  CA  MET A 162     -17.371  -6.661  11.321  1.00 26.47           C  
ANISOU 1240  CA  MET A 162     3501   3382   3172     71    112      9       C  
ATOM   1241  C   MET A 162     -17.170  -5.556  10.296  1.00 25.48           C  
ANISOU 1241  C   MET A 162     3306   3326   3048     70    167     38       C  
ATOM   1242  O   MET A 162     -18.144  -4.959   9.829  1.00 27.94           O  
ANISOU 1242  O   MET A 162     3600   3640   3377     31    177     92       O  
ATOM   1243  CB  MET A 162     -17.969  -7.908  10.658  1.00 27.31           C  
ANISOU 1243  CB  MET A 162     3682   3458   3236     76     44    -10       C  
ATOM   1244  CG  MET A 162     -17.179  -8.395   9.448  1.00 29.17           C  
ANISOU 1244  CG  MET A 162     3923   3743   3416    144     27    -64       C  
ATOM   1245  SD  MET A 162     -17.757  -9.969   8.779  1.00 29.14           S  
ANISOU 1245  SD  MET A 162     4019   3686   3367    162    -71   -109       S  
ATOM   1246  CE  MET A 162     -16.959 -11.127   9.887  1.00 30.20           C  
ANISOU 1246  CE  MET A 162     4233   3733   3508    211   -144   -168       C  
ATOM   1247  N   HIS A 163     -15.914  -5.287   9.952  1.00 24.73           N  
ANISOU 1247  N   HIS A 163     3172   3288   2936    110    199      5       N  
ATOM   1248  CA  HIS A 163     -15.580  -4.130   9.133  1.00 25.09           C  
ANISOU 1248  CA  HIS A 163     3155   3398   2982     90    260     46       C  
ATOM   1249  C   HIS A 163     -15.868  -4.389   7.659  1.00 27.04           C  
ANISOU 1249  C   HIS A 163     3422   3697   3156     95    252     58       C  
ATOM   1250  O   HIS A 163     -15.585  -5.471   7.136  1.00 24.81           O  
ANISOU 1250  O   HIS A 163     3176   3437   2814    142    218     -4       O  
ATOM   1251  CB  HIS A 163     -14.110  -3.760   9.318  1.00 23.87           C  
ANISOU 1251  CB  HIS A 163     2941   3298   2831    114    303      2       C  
ATOM   1252  CG  HIS A 163     -13.680  -2.587   8.497  1.00 27.41           C  
ANISOU 1252  CG  HIS A 163     3329   3810   3273     74    370     51       C  
ATOM   1253  ND1 HIS A 163     -14.222  -1.331   8.657  1.00 27.31           N  
ANISOU 1253  ND1 HIS A 163     3296   3762   3318     15    395    130       N  
ATOM   1254  CD2 HIS A 163     -12.767  -2.481   7.503  1.00 28.06           C  
ANISOU 1254  CD2 HIS A 163     3374   3991   3297     78    416     32       C  
ATOM   1255  CE1 HIS A 163     -13.656  -0.499   7.801  1.00 27.62           C  
ANISOU 1255  CE1 HIS A 163     3299   3861   3336    -22    446    171       C  
ATOM   1256  NE2 HIS A 163     -12.772  -1.172   7.088  1.00 27.52           N  
ANISOU 1256  NE2 HIS A 163     3272   3939   3246      8    468    115       N  
ATOM   1257  N   HIS A 164     -16.430  -3.383   6.990  1.00 25.19           N  
ANISOU 1257  N   HIS A 164     3168   3477   2925     51    276    135       N  
ATOM   1258  CA  HIS A 164     -16.806  -3.489   5.584  1.00 24.44           C  
ANISOU 1258  CA  HIS A 164     3099   3434   2753     48    264    161       C  
ATOM   1259  C   HIS A 164     -16.213  -2.405   4.695  1.00 26.22           C  
ANISOU 1259  C   HIS A 164     3292   3731   2940     14    323    219       C  
ATOM   1260  O   HIS A 164     -15.771  -2.706   3.583  1.00 27.83           O  
ANISOU 1260  O   HIS A 164     3507   4021   3046     24    339    203       O  
ATOM   1261  CB  HIS A 164     -18.336  -3.452   5.443  1.00 24.11           C  
ANISOU 1261  CB  HIS A 164     3088   3337   2737     22    208    212       C  
ATOM   1262  CG  HIS A 164     -19.008  -4.760   5.724  1.00 24.69           C  
ANISOU 1262  CG  HIS A 164     3210   3366   2804     39    144    159       C  
ATOM   1263  ND1 HIS A 164     -19.721  -5.450   4.767  1.00 24.86           N  
ANISOU 1263  ND1 HIS A 164     3276   3400   2770     44     88    150       N  
ATOM   1264  CD2 HIS A 164     -19.088  -5.498   6.857  1.00 24.20           C  
ANISOU 1264  CD2 HIS A 164     3168   3244   2783     42    122    118       C  
ATOM   1265  CE1 HIS A 164     -20.208  -6.558   5.297  1.00 23.30           C  
ANISOU 1265  CE1 HIS A 164     3120   3145   2588     46     35    104       C  
ATOM   1266  NE2 HIS A 164     -19.836  -6.612   6.563  1.00 25.67           N  
ANISOU 1266  NE2 HIS A 164     3411   3401   2943     42     55     90       N  
ATOM   1267  N   MET A 165     -16.186  -1.151   5.148  1.00 31.70           N  
ANISOU 1267  N   MET A 165     3948   4391   3705    -31    355    284       N  
ATOM   1268  CA  MET A 165     -16.027  -0.029   4.233  1.00 30.21           C  
ANISOU 1268  CA  MET A 165     3754   4238   3486    -83    388    372       C  
ATOM   1269  C   MET A 165     -15.341   1.138   4.927  1.00 32.75           C  
ANISOU 1269  C   MET A 165     4023   4531   3888   -126    438    404       C  
ATOM   1270  O   MET A 165     -15.294   1.218   6.156  1.00 30.96           O  
ANISOU 1270  O   MET A 165     3768   4246   3750   -113    435    366       O  
ATOM   1271  CB  MET A 165     -17.388   0.429   3.703  1.00 33.04           C  
ANISOU 1271  CB  MET A 165     4154   4545   3856    -99    327    452       C  
ATOM   1272  CG  MET A 165     -18.310   0.878   4.827  1.00 35.21           C  
ANISOU 1272  CG  MET A 165     4409   4715   4256    -97    291    461       C  
ATOM   1273  SD  MET A 165     -20.062   0.917   4.418  1.00 45.00           S  
ANISOU 1273  SD  MET A 165     5675   5902   5522    -88    202    504       S  
ATOM   1274  CE  MET A 165     -20.169  -0.436   3.258  1.00 30.97           C  
ANISOU 1274  CE  MET A 165     3952   4202   3612    -64    168    466       C  
ATOM   1275  N   GLU A 166     -14.838   2.066   4.115  1.00 38.07           N  
ANISOU 1275  N   GLU A 166     4693   5248   4526   -186    480    477       N  
ATOM   1276  CA  GLU A 166     -14.268   3.317   4.594  1.00 37.96           C  
ANISOU 1276  CA  GLU A 166     4639   5194   4589   -246    518    525       C  
ATOM   1277  C   GLU A 166     -15.093   4.486   4.072  1.00 39.28           C  
ANISOU 1277  C   GLU A 166     4852   5287   4786   -294    478    647       C  
ATOM   1278  O   GLU A 166     -15.588   4.455   2.940  1.00 37.31           O  
ANISOU 1278  O   GLU A 166     4658   5067   4451   -305    452    710       O  
ATOM   1279  CB  GLU A 166     -12.806   3.474   4.157  1.00 42.22           C  
ANISOU 1279  CB  GLU A 166     5129   5843   5070   -294    604    509       C  
ATOM   1280  CG  GLU A 166     -12.087   4.637   4.827  1.00 43.56           C  
ANISOU 1280  CG  GLU A 166     5247   5970   5334   -360    641    537       C  
ATOM   1281  CD  GLU A 166     -10.852   5.080   4.069  1.00 47.47           C  
ANISOU 1281  CD  GLU A 166     5698   6576   5762   -445    728    561       C  
ATOM   1282  OE1 GLU A 166     -10.875   6.187   3.490  1.00 48.22           O  
ANISOU 1282  OE1 GLU A 166     5822   6643   5854   -538    741    676       O  
ATOM   1283  OE2 GLU A 166      -9.857   4.326   4.056  1.00 48.38           O  
ANISOU 1283  OE2 GLU A 166     5748   6806   5828   -420    781    463       O  
ATOM   1284  N   LEU A 167     -15.239   5.513   4.903  1.00 39.24           N  
ANISOU 1284  N   LEU A 167     4827   5180   4901   -315    465    674       N  
ATOM   1285  CA  LEU A 167     -16.001   6.707   4.578  1.00 43.41           C  
ANISOU 1285  CA  LEU A 167     5397   5610   5486   -348    411    779       C  
ATOM   1286  C   LEU A 167     -15.090   7.765   3.971  1.00 43.43           C  
ANISOU 1286  C   LEU A 167     5411   5621   5470   -446    454    870       C  
ATOM   1287  O   LEU A 167     -13.873   7.743   4.178  1.00 43.89           O  
ANISOU 1287  O   LEU A 167     5417   5746   5513   -490    531    834       O  
ATOM   1288  CB  LEU A 167     -16.676   7.255   5.836  1.00 41.39           C  
ANISOU 1288  CB  LEU A 167     5113   5236   5378   -312    368    744       C  
ATOM   1289  CG  LEU A 167     -18.044   6.716   6.275  1.00 40.78           C  
ANISOU 1289  CG  LEU A 167     5036   5117   5341   -238    304    699       C  
ATOM   1290  CD1 LEU A 167     -19.165   7.356   5.469  1.00 43.70           C  
ANISOU 1290  CD1 LEU A 167     5451   5425   5726   -230    221    784       C  
ATOM   1291  CD2 LEU A 167     -18.124   5.194   6.202  1.00 38.55           C  
ANISOU 1291  CD2 LEU A 167     4755   4921   4971   -198    316    628       C  
ATOM   1292  N   PRO A 168     -15.646   8.712   3.207  1.00 43.29           N  
ANISOU 1292  N   PRO A 168     5460   5534   5452   -488    400    992       N  
ATOM   1293  CA  PRO A 168     -14.808   9.801   2.674  1.00 47.61           C  
ANISOU 1293  CA  PRO A 168     6033   6071   5986   -601    436   1096       C  
ATOM   1294  C   PRO A 168     -14.141  10.620   3.760  1.00 47.46           C  
ANISOU 1294  C   PRO A 168     5958   5974   6100   -639    460   1066       C  
ATOM   1295  O   PRO A 168     -13.125  11.272   3.497  1.00 51.22           O  
ANISOU 1295  O   PRO A 168     6425   6472   6563   -745    518   1118       O  
ATOM   1296  CB  PRO A 168     -15.799  10.648   1.864  1.00 49.88           C  
ANISOU 1296  CB  PRO A 168     6418   6258   6276   -615    337   1229       C  
ATOM   1297  CG  PRO A 168     -17.145  10.289   2.403  1.00 49.32           C  
ANISOU 1297  CG  PRO A 168     6340   6113   6284   -500    246   1170       C  
ATOM   1298  CD  PRO A 168     -17.049   8.845   2.782  1.00 42.34           C  
ANISOU 1298  CD  PRO A 168     5400   5341   5347   -437    296   1043       C  
ATOM   1299  N   THR A 169     -14.675  10.594   4.977  1.00 67.71           N  
ANISOU 1299  N   THR A 169     8484   8455   8788   -562    421    980       N  
ATOM   1300  CA  THR A 169     -14.104  11.301   6.113  1.00 67.23           C  
ANISOU 1300  CA  THR A 169     8370   8321   8853   -584    436    930       C  
ATOM   1301  C   THR A 169     -12.820  10.661   6.622  1.00 66.93           C  
ANISOU 1301  C   THR A 169     8250   8397   8784   -604    526    836       C  
ATOM   1302  O   THR A 169     -11.989  11.359   7.213  1.00 69.56           O  
ANISOU 1302  O   THR A 169     8540   8699   9192   -662    553    819       O  
ATOM   1303  CB  THR A 169     -15.149  11.350   7.240  1.00 67.23           C  
ANISOU 1303  CB  THR A 169     8352   8221   8970   -488    369    853       C  
ATOM   1304  OG1 THR A 169     -16.377  11.880   6.721  1.00 71.20           O  
ANISOU 1304  OG1 THR A 169     8917   8630   9507   -455    278    925       O  
ATOM   1305  CG2 THR A 169     -14.687  12.206   8.400  1.00 68.50           C  
ANISOU 1305  CG2 THR A 169     8471   8294   9262   -505    370    800       C  
ATOM   1306  N   GLY A 170     -12.616   9.374   6.358  1.00 44.14           N  
ANISOU 1306  N   GLY A 170     5342   5638   5792   -556    565    773       N  
ATOM   1307  CA  GLY A 170     -11.579   8.607   7.009  1.00 44.05           C  
ANISOU 1307  CA  GLY A 170     5250   5720   5767   -537    624    660       C  
ATOM   1308  C   GLY A 170     -12.083   7.747   8.145  1.00 40.92           C  
ANISOU 1308  C   GLY A 170     4837   5301   5411   -433    589    551       C  
ATOM   1309  O   GLY A 170     -11.274   7.094   8.816  1.00 42.33           O  
ANISOU 1309  O   GLY A 170     4959   5539   5586   -405    617    455       O  
ATOM   1310  N   VAL A 171     -13.390   7.732   8.381  1.00 34.61           N  
ANISOU 1310  N   VAL A 171     4082   4419   4648   -380    525    565       N  
ATOM   1311  CA  VAL A 171     -13.987   6.896   9.401  1.00 31.39           C  
ANISOU 1311  CA  VAL A 171     3666   3997   4263   -300    497    475       C  
ATOM   1312  C   VAL A 171     -14.536   5.641   8.725  1.00 31.83           C  
ANISOU 1312  C   VAL A 171     3758   4118   4218   -253    483    465       C  
ATOM   1313  O   VAL A 171     -14.629   5.549   7.512  1.00 31.74           O  
ANISOU 1313  O   VAL A 171     3780   4150   4128   -273    486    527       O  
ATOM   1314  CB  VAL A 171     -15.085   7.647  10.196  1.00 32.91           C  
ANISOU 1314  CB  VAL A 171     3867   4072   4564   -276    443    475       C  
ATOM   1315  CG1 VAL A 171     -14.502   8.880  10.872  1.00 34.50           C  
ANISOU 1315  CG1 VAL A 171     4038   4200   4869   -319    449    472       C  
ATOM   1316  CG2 VAL A 171     -16.251   8.025   9.295  1.00 34.19           C  
ANISOU 1316  CG2 VAL A 171     4078   4186   4726   -270    390    559       C  
ATOM   1317  N   HIS A 172     -14.890   4.651   9.543  1.00 28.97           N  
ANISOU 1317  N   HIS A 172     3396   3759   3854   -194    465    387       N  
ATOM   1318  CA  HIS A 172     -15.200   3.321   9.044  1.00 29.18           C  
ANISOU 1318  CA  HIS A 172     3455   3841   3790   -153    449    359       C  
ATOM   1319  C   HIS A 172     -16.611   2.908   9.438  1.00 30.01           C  
ANISOU 1319  C   HIS A 172     3589   3893   3920   -122    397    353       C  
ATOM   1320  O   HIS A 172     -17.188   3.415  10.405  1.00 27.74           O  
ANISOU 1320  O   HIS A 172     3284   3543   3714   -120    384    338       O  
ATOM   1321  CB  HIS A 172     -14.180   2.307   9.569  1.00 30.57           C  
ANISOU 1321  CB  HIS A 172     3612   4076   3929   -117    468    268       C  
ATOM   1322  CG  HIS A 172     -12.762   2.673   9.262  1.00 31.58           C  
ANISOU 1322  CG  HIS A 172     3686   4273   4041   -146    523    254       C  
ATOM   1323  ND1 HIS A 172     -11.948   3.323  10.166  1.00 31.21           N  
ANISOU 1323  ND1 HIS A 172     3585   4209   4064   -166    544    222       N  
ATOM   1324  CD2 HIS A 172     -12.016   2.493   8.146  1.00 32.68           C  
ANISOU 1324  CD2 HIS A 172     3810   4509   4099   -163    564    261       C  
ATOM   1325  CE1 HIS A 172     -10.760   3.520   9.622  1.00 34.76           C  
ANISOU 1325  CE1 HIS A 172     3981   4742   4485   -199    596    211       C  
ATOM   1326  NE2 HIS A 172     -10.775   3.026   8.397  1.00 33.59           N  
ANISOU 1326  NE2 HIS A 172     3853   4668   4241   -199    615    234       N  
ATOM   1327  N   ALA A 173     -17.160   1.970   8.668  1.00 24.72           N  
ANISOU 1327  N   ALA A 173     2958   3256   3177   -101    369    355       N  
ATOM   1328  CA  ALA A 173     -18.509   1.471   8.879  1.00 22.28           C  
ANISOU 1328  CA  ALA A 173     2670   2911   2884    -85    320    349       C  
ATOM   1329  C   ALA A 173     -18.538  -0.030   8.636  1.00 22.75           C  
ANISOU 1329  C   ALA A 173     2771   3010   2865    -59    298    301       C  
ATOM   1330  O   ALA A 173     -17.739  -0.566   7.863  1.00 23.63           O  
ANISOU 1330  O   ALA A 173     2900   3180   2899    -44    310    286       O  
ATOM   1331  CB  ALA A 173     -19.520   2.173   7.963  1.00 23.70           C  
ANISOU 1331  CB  ALA A 173     2860   3067   3078    -96    280    422       C  
ATOM   1332  N   GLY A 174     -19.468  -0.702   9.304  1.00 21.47           N  
ANISOU 1332  N   GLY A 174     2621   2812   2722    -56    267    272       N  
ATOM   1333  CA  GLY A 174     -19.591  -2.135   9.178  1.00 22.17           C  
ANISOU 1333  CA  GLY A 174     2760   2913   2750    -40    232    230       C  
ATOM   1334  C   GLY A 174     -20.929  -2.622   9.687  1.00 21.57           C  
ANISOU 1334  C   GLY A 174     2693   2799   2703    -65    197    224       C  
ATOM   1335  O   GLY A 174     -21.862  -1.843   9.891  1.00 22.19           O  
ANISOU 1335  O   GLY A 174     2729   2859   2843    -85    197    250       O  
ATOM   1336  N   THR A 175     -21.008  -3.932   9.897  1.00 23.03           N  
ANISOU 1336  N   THR A 175     2932   2973   2847    -65    164    185       N  
ATOM   1337  CA  THR A 175     -22.235  -4.600  10.304  1.00 23.31           C  
ANISOU 1337  CA  THR A 175     2982   2978   2897   -108    131    180       C  
ATOM   1338  C   THR A 175     -22.031  -5.310  11.635  1.00 23.35           C  
ANISOU 1338  C   THR A 175     3024   2948   2899   -130    136    150       C  
ATOM   1339  O   THR A 175     -20.911  -5.445  12.134  1.00 20.70           O  
ANISOU 1339  O   THR A 175     2712   2608   2546    -99    147    126       O  
ATOM   1340  CB  THR A 175     -22.687  -5.622   9.252  1.00 24.54           C  
ANISOU 1340  CB  THR A 175     3187   3138   3000   -106     70    171       C  
ATOM   1341  OG1 THR A 175     -21.788  -6.738   9.257  1.00 23.59           O  
ANISOU 1341  OG1 THR A 175     3138   3003   2824    -75     44    126       O  
ATOM   1342  CG2 THR A 175     -22.698  -5.003   7.867  1.00 22.64           C  
ANISOU 1342  CG2 THR A 175     2928   2941   2733    -80     59    202       C  
ATOM   1343  N   ASP A 176     -23.140  -5.770  12.211  1.00 26.41           N  
ANISOU 1343  N   ASP A 176     3416   3316   3302   -191    124    152       N  
ATOM   1344  CA  ASP A 176     -23.060  -6.754  13.276  1.00 25.28           C  
ANISOU 1344  CA  ASP A 176     3340   3135   3130   -230    112    136       C  
ATOM   1345  C   ASP A 176     -22.780  -8.124  12.660  1.00 26.38           C  
ANISOU 1345  C   ASP A 176     3572   3234   3215   -216     39    119       C  
ATOM   1346  O   ASP A 176     -22.655  -8.271  11.441  1.00 27.70           O  
ANISOU 1346  O   ASP A 176     3743   3418   3364   -175      9    110       O  
ATOM   1347  CB  ASP A 176     -24.338  -6.750  14.117  1.00 26.07           C  
ANISOU 1347  CB  ASP A 176     3409   3240   3257   -316    136    145       C  
ATOM   1348  CG  ASP A 176     -25.602  -6.938  13.288  1.00 30.46           C  
ANISOU 1348  CG  ASP A 176     3928   3812   3836   -356    109    153       C  
ATOM   1349  OD1 ASP A 176     -25.528  -7.487  12.169  1.00 29.36           O  
ANISOU 1349  OD1 ASP A 176     3824   3660   3672   -329     52    153       O  
ATOM   1350  OD2 ASP A 176     -26.683  -6.537  13.768  1.00 30.74           O  
ANISOU 1350  OD2 ASP A 176     3890   3877   3914   -412    141    151       O  
ATOM   1351  N   LEU A 177     -22.685  -9.148  13.501  1.00 25.96           N  
ANISOU 1351  N   LEU A 177     3605   3127   3134   -250      5    113       N  
ATOM   1352  CA  LEU A 177     -22.373 -10.475  12.988  1.00 25.60           C  
ANISOU 1352  CA  LEU A 177     3659   3022   3047   -229    -79     89       C  
ATOM   1353  C   LEU A 177     -23.581 -11.172  12.375  1.00 28.84           C  
ANISOU 1353  C   LEU A 177     4089   3411   3459   -297   -123     98       C  
ATOM   1354  O   LEU A 177     -23.470 -12.340  11.985  1.00 29.28           O  
ANISOU 1354  O   LEU A 177     4235   3403   3486   -291   -203     75       O  
ATOM   1355  CB  LEU A 177     -21.762 -11.338  14.093  1.00 25.14           C  
ANISOU 1355  CB  LEU A 177     3702   2892   2957   -236   -120     85       C  
ATOM   1356  CG  LEU A 177     -20.231 -11.318  14.130  1.00 25.24           C  
ANISOU 1356  CG  LEU A 177     3730   2903   2955   -127   -139     41       C  
ATOM   1357  CD1 LEU A 177     -19.658 -11.835  12.819  1.00 29.16           C  
ANISOU 1357  CD1 LEU A 177     4241   3404   3434    -42   -188    -13       C  
ATOM   1358  CD2 LEU A 177     -19.703  -9.919  14.428  1.00 27.48           C  
ANISOU 1358  CD2 LEU A 177     3911   3261   3267    -98    -55     43       C  
ATOM   1359  N   GLU A 178     -24.722 -10.491  12.279  1.00 25.38           N  
ANISOU 1359  N   GLU A 178     3563   3020   3059   -356    -82    123       N  
ATOM   1360  CA  GLU A 178     -25.878 -10.984  11.545  1.00 30.13           C  
ANISOU 1360  CA  GLU A 178     4156   3619   3672   -413   -125    124       C  
ATOM   1361  C   GLU A 178     -26.045 -10.291  10.198  1.00 28.56           C  
ANISOU 1361  C   GLU A 178     3891   3477   3483   -354   -133    117       C  
ATOM   1362  O   GLU A 178     -27.039 -10.531   9.506  1.00 31.33           O  
ANISOU 1362  O   GLU A 178     4219   3838   3847   -392   -174    114       O  
ATOM   1363  CB  GLU A 178     -27.147 -10.823  12.384  1.00 29.97           C  
ANISOU 1363  CB  GLU A 178     4078   3620   3690   -528    -84    147       C  
ATOM   1364  CG  GLU A 178     -27.215 -11.760  13.580  1.00 30.50           C  
ANISOU 1364  CG  GLU A 178     4232   3629   3726   -620    -89    166       C  
ATOM   1365  CD  GLU A 178     -28.512 -11.632  14.354  1.00 36.44           C  
ANISOU 1365  CD  GLU A 178     4916   4426   4504   -748    -35    183       C  
ATOM   1366  OE1 GLU A 178     -29.117 -10.540  14.327  1.00 37.54           O  
ANISOU 1366  OE1 GLU A 178     4925   4646   4692   -740     26    171       O  
ATOM   1367  OE2 GLU A 178     -28.925 -12.624  14.990  1.00 38.33           O  
ANISOU 1367  OE2 GLU A 178     5231   4618   4714   -859    -55    206       O  
ATOM   1368  N   GLY A 179     -25.101  -9.434   9.818  1.00 24.79           N  
ANISOU 1368  N   GLY A 179     3385   3038   2996   -269    -98    117       N  
ATOM   1369  CA  GLY A 179     -25.111  -8.808   8.513  1.00 23.71           C  
ANISOU 1369  CA  GLY A 179     3208   2953   2846   -218   -108    122       C  
ATOM   1370  C   GLY A 179     -25.860  -7.500   8.411  1.00 25.56           C  
ANISOU 1370  C   GLY A 179     3343   3232   3138   -227    -73    159       C  
ATOM   1371  O   GLY A 179     -26.023  -6.987   7.299  1.00 26.69           O  
ANISOU 1371  O   GLY A 179     3464   3411   3268   -194    -96    175       O  
ATOM   1372  N   ASN A 180     -26.319  -6.938   9.524  1.00 28.86           N  
ANISOU 1372  N   ASN A 180     3703   3648   3614   -268    -23    169       N  
ATOM   1373  CA  ASN A 180     -27.070  -5.690   9.498  1.00 28.12           C  
ANISOU 1373  CA  ASN A 180     3510   3587   3589   -265      1    189       C  
ATOM   1374  C   ASN A 180     -26.123  -4.523   9.748  1.00 28.37           C  
ANISOU 1374  C   ASN A 180     3518   3625   3638   -213     54    208       C  
ATOM   1375  O   ASN A 180     -25.434  -4.484  10.773  1.00 28.89           O  
ANISOU 1375  O   ASN A 180     3596   3677   3704   -216    101    194       O  
ATOM   1376  CB  ASN A 180     -28.189  -5.714  10.534  1.00 30.85           C  
ANISOU 1376  CB  ASN A 180     3792   3940   3991   -338     27    172       C  
ATOM   1377  CG  ASN A 180     -29.141  -6.877  10.334  1.00 32.98           C  
ANISOU 1377  CG  ASN A 180     4080   4204   4248   -412    -22    156       C  
ATOM   1378  OD1 ASN A 180     -29.221  -7.780  11.167  1.00 33.14           O  
ANISOU 1378  OD1 ASN A 180     4146   4199   4246   -483    -11    147       O  
ATOM   1379  ND2 ASN A 180     -29.870  -6.861   9.223  1.00 32.07           N  
ANISOU 1379  ND2 ASN A 180     3933   4107   4145   -401    -85    156       N  
ATOM   1380  N   PHE A 181     -26.096  -3.576   8.815  1.00 27.65           N  
ANISOU 1380  N   PHE A 181     3396   3549   3559   -170     40    241       N  
ATOM   1381  CA  PHE A 181     -25.178  -2.450   8.909  1.00 23.65           C  
ANISOU 1381  CA  PHE A 181     2874   3041   3071   -133     83    266       C  
ATOM   1382  C   PHE A 181     -25.544  -1.535  10.069  1.00 25.57           C  
ANISOU 1382  C   PHE A 181     3048   3267   3400   -143    125    253       C  
ATOM   1383  O   PHE A 181     -26.722  -1.292  10.346  1.00 24.14           O  
ANISOU 1383  O   PHE A 181     2804   3089   3279   -160    113    237       O  
ATOM   1384  CB  PHE A 181     -25.183  -1.652   7.605  1.00 27.40           C  
ANISOU 1384  CB  PHE A 181     3348   3530   3534   -102     48    319       C  
ATOM   1385  CG  PHE A 181     -24.085  -2.031   6.660  1.00 27.84           C  
ANISOU 1385  CG  PHE A 181     3468   3617   3493    -81     51    333       C  
ATOM   1386  CD1 PHE A 181     -22.779  -1.635   6.900  1.00 24.72           C  
ANISOU 1386  CD1 PHE A 181     3080   3232   3082    -68    108    336       C  
ATOM   1387  CD2 PHE A 181     -24.356  -2.787   5.532  1.00 26.34           C  
ANISOU 1387  CD2 PHE A 181     3322   3457   3228    -74     -3    331       C  
ATOM   1388  CE1 PHE A 181     -21.766  -1.988   6.033  1.00 25.59           C  
ANISOU 1388  CE1 PHE A 181     3232   3391   3102    -50    121    336       C  
ATOM   1389  CE2 PHE A 181     -23.347  -3.141   4.661  1.00 25.90           C  
ANISOU 1389  CE2 PHE A 181     3318   3447   3076    -51      7    328       C  
ATOM   1390  CZ  PHE A 181     -22.051  -2.744   4.912  1.00 25.42           C  
ANISOU 1390  CZ  PHE A 181     3254   3405   2999    -40     74    329       C  
ATOM   1391  N   TYR A 182     -24.520  -1.034  10.755  1.00 23.88           N  
ANISOU 1391  N   TYR A 182     2838   3041   3194   -130    175    247       N  
ATOM   1392  CA  TYR A 182     -24.694   0.079  11.677  1.00 25.21           C  
ANISOU 1392  CA  TYR A 182     2944   3191   3444   -126    210    232       C  
ATOM   1393  C   TYR A 182     -24.782   1.365  10.865  1.00 25.34           C  
ANISOU 1393  C   TYR A 182     2931   3184   3514    -92    184    277       C  
ATOM   1394  O   TYR A 182     -23.858   1.694  10.113  1.00 27.30           O  
ANISOU 1394  O   TYR A 182     3216   3429   3729    -80    184    322       O  
ATOM   1395  CB  TYR A 182     -23.537   0.149  12.672  1.00 21.65           C  
ANISOU 1395  CB  TYR A 182     2512   2733   2981   -126    260    206       C  
ATOM   1396  CG  TYR A 182     -23.489  -0.986  13.671  1.00 24.82           C  
ANISOU 1396  CG  TYR A 182     2952   3144   3334   -159    276    167       C  
ATOM   1397  CD1 TYR A 182     -24.300  -0.981  14.799  1.00 23.79           C  
ANISOU 1397  CD1 TYR A 182     2787   3023   3229   -196    304    130       C  
ATOM   1398  CD2 TYR A 182     -22.619  -2.054  13.496  1.00 21.38           C  
ANISOU 1398  CD2 TYR A 182     2592   2709   2824   -153    260    165       C  
ATOM   1399  CE1 TYR A 182     -24.254  -2.013  15.718  1.00 22.65           C  
ANISOU 1399  CE1 TYR A 182     2694   2885   3027   -240    315    110       C  
ATOM   1400  CE2 TYR A 182     -22.566  -3.091  14.409  1.00 22.32           C  
ANISOU 1400  CE2 TYR A 182     2763   2818   2898   -184    257    140       C  
ATOM   1401  CZ  TYR A 182     -23.385  -3.065  15.518  1.00 24.58           C  
ANISOU 1401  CZ  TYR A 182     3027   3111   3202   -234    285    121       C  
ATOM   1402  OH  TYR A 182     -23.334  -4.095  16.429  1.00 23.37           O  
ANISOU 1402  OH  TYR A 182     2942   2946   2991   -278    279    111       O  
ATOM   1403  N   GLY A 183     -25.893   2.084  11.000  1.00 27.21           N  
ANISOU 1403  N   GLY A 183     3101   3404   3834    -79    160    265       N  
ATOM   1404  CA  GLY A 183     -26.093   3.313  10.271  1.00 26.88           C  
ANISOU 1404  CA  GLY A 183     3041   3321   3853    -42    114    311       C  
ATOM   1405  C   GLY A 183     -26.882   3.114   8.993  1.00 28.86           C  
ANISOU 1405  C   GLY A 183     3302   3582   4082    -29     37    355       C  
ATOM   1406  O   GLY A 183     -27.290   1.998   8.654  1.00 28.95           O  
ANISOU 1406  O   GLY A 183     3330   3635   4034    -51     21    341       O  
ATOM   1407  N   PRO A 184     -27.108   4.198   8.255  1.00 31.24           N  
ANISOU 1407  N   PRO A 184     3602   3837   4429      5    -22    409       N  
ATOM   1408  CA  PRO A 184     -27.890   4.122   7.015  1.00 29.98           C  
ANISOU 1408  CA  PRO A 184     3459   3685   4247     24   -112    454       C  
ATOM   1409  C   PRO A 184     -27.131   3.564   5.821  1.00 33.50           C  
ANISOU 1409  C   PRO A 184     3998   4167   4565      3   -122    520       C  
ATOM   1410  O   PRO A 184     -27.640   3.646   4.699  1.00 37.25           O  
ANISOU 1410  O   PRO A 184     4502   4646   5005     19   -201    569       O  
ATOM   1411  CB  PRO A 184     -28.265   5.591   6.776  1.00 34.90           C  
ANISOU 1411  CB  PRO A 184     4062   4230   4969     71   -179    494       C  
ATOM   1412  CG  PRO A 184     -27.092   6.343   7.308  1.00 32.29           C  
ANISOU 1412  CG  PRO A 184     3760   3854   4656     56   -117    515       C  
ATOM   1413  CD  PRO A 184     -26.618   5.565   8.514  1.00 32.90           C  
ANISOU 1413  CD  PRO A 184     3809   3976   4714     26    -20    435       C  
ATOM   1414  N   PHE A 185     -25.948   2.998   6.029  1.00 28.94           N  
ANISOU 1414  N   PHE A 185     3463   3619   3912    -26    -47    514       N  
ATOM   1415  CA  PHE A 185     -25.063   2.651   4.929  1.00 30.03           C  
ANISOU 1415  CA  PHE A 185     3679   3802   3930    -41    -41    565       C  
ATOM   1416  C   PHE A 185     -25.464   1.333   4.275  1.00 31.55           C  
ANISOU 1416  C   PHE A 185     3901   4050   4035    -43    -75    535       C  
ATOM   1417  O   PHE A 185     -26.007   0.429   4.917  1.00 29.70           O  
ANISOU 1417  O   PHE A 185     3641   3823   3821    -51    -74    468       O  
ATOM   1418  CB  PHE A 185     -23.619   2.567   5.422  1.00 29.78           C  
ANISOU 1418  CB  PHE A 185     3664   3789   3864    -62     48    552       C  
ATOM   1419  CG  PHE A 185     -23.198   3.745   6.252  1.00 29.27           C  
ANISOU 1419  CG  PHE A 185     3564   3664   3892    -67     82    563       C  
ATOM   1420  CD1 PHE A 185     -23.038   4.993   5.673  1.00 30.43           C  
ANISOU 1420  CD1 PHE A 185     3730   3764   4067    -75     56    644       C  
ATOM   1421  CD2 PHE A 185     -22.971   3.608   7.611  1.00 27.87           C  
ANISOU 1421  CD2 PHE A 185     3345   3473   3773    -68    132    492       C  
ATOM   1422  CE1 PHE A 185     -22.654   6.082   6.433  1.00 30.38           C  
ANISOU 1422  CE1 PHE A 185     3698   3691   4157    -82     77    648       C  
ATOM   1423  CE2 PHE A 185     -22.586   4.693   8.377  1.00 27.19           C  
ANISOU 1423  CE2 PHE A 185     3227   3332   3771    -70    157    491       C  
ATOM   1424  CZ  PHE A 185     -22.428   5.931   7.786  1.00 29.13           C  
ANISOU 1424  CZ  PHE A 185     3488   3524   4057    -76    128    565       C  
ATOM   1425  N   VAL A 186     -25.191   1.241   2.976  1.00 30.77           N  
ANISOU 1425  N   VAL A 186     3865   3992   3834    -43   -107    585       N  
ATOM   1426  CA  VAL A 186     -25.365   0.020   2.201  1.00 30.86           C  
ANISOU 1426  CA  VAL A 186     3919   4060   3745    -41   -140    551       C  
ATOM   1427  C   VAL A 186     -24.028  -0.329   1.564  1.00 28.41           C  
ANISOU 1427  C   VAL A 186     3667   3816   3313    -48    -83    556       C  
ATOM   1428  O   VAL A 186     -23.194   0.547   1.311  1.00 32.18           O  
ANISOU 1428  O   VAL A 186     4157   4303   3768    -64    -39    615       O  
ATOM   1429  CB  VAL A 186     -26.466   0.164   1.127  1.00 33.69           C  
ANISOU 1429  CB  VAL A 186     4293   4426   4082    -27   -247    589       C  
ATOM   1430  CG1 VAL A 186     -27.806   0.476   1.776  1.00 34.85           C  
ANISOU 1430  CG1 VAL A 186     4360   4522   4360    -14   -302    565       C  
ATOM   1431  CG2 VAL A 186     -26.094   1.243   0.120  1.00 34.42           C  
ANISOU 1431  CG2 VAL A 186     4438   4522   4119    -27   -270    692       C  
ATOM   1432  N   ASP A 187     -23.818  -1.622   1.311  1.00 27.69           N  
ANISOU 1432  N   ASP A 187     3607   3768   3146    -40    -85    487       N  
ATOM   1433  CA  ASP A 187     -22.555  -2.090   0.737  1.00 24.61           C  
ANISOU 1433  CA  ASP A 187     3258   3453   2642    -33    -31    462       C  
ATOM   1434  C   ASP A 187     -22.591  -1.914  -0.783  1.00 30.60           C  
ANISOU 1434  C   ASP A 187     4071   4281   3274    -35    -66    510       C  
ATOM   1435  O   ASP A 187     -22.650  -2.866  -1.564  1.00 29.92           O  
ANISOU 1435  O   ASP A 187     4028   4249   3092    -17   -100    459       O  
ATOM   1436  CB  ASP A 187     -22.275  -3.532   1.141  1.00 26.10           C  
ANISOU 1436  CB  ASP A 187     3461   3646   2808    -10    -30    358       C  
ATOM   1437  CG  ASP A 187     -23.455  -4.450   0.901  1.00 26.43           C  
ANISOU 1437  CG  ASP A 187     3525   3664   2854     -9   -118    320       C  
ATOM   1438  OD1 ASP A 187     -24.545  -3.950   0.554  1.00 28.86           O  
ANISOU 1438  OD1 ASP A 187     3817   3953   3193    -22   -179    368       O  
ATOM   1439  OD2 ASP A 187     -23.289  -5.678   1.062  1.00 29.45           O  
ANISOU 1439  OD2 ASP A 187     3938   4040   3212      6   -136    240       O  
ATOM   1440  N   ARG A 188     -22.554  -0.648  -1.193  1.00 29.96           N  
ANISOU 1440  N   ARG A 188     3996   4193   3193    -61    -63    612       N  
ATOM   1441  CA  ARG A 188     -22.471  -0.264  -2.594  1.00 32.32           C  
ANISOU 1441  CA  ARG A 188     4360   4560   3361    -78    -89    684       C  
ATOM   1442  C   ARG A 188     -21.560   0.948  -2.705  1.00 33.31           C  
ANISOU 1442  C   ARG A 188     4491   4694   3472   -127    -19    777       C  
ATOM   1443  O   ARG A 188     -21.611   1.848  -1.861  1.00 33.04           O  
ANISOU 1443  O   ARG A 188     4417   4574   3561   -140     -8    817       O  
ATOM   1444  CB  ARG A 188     -23.855   0.051  -3.178  1.00 33.64           C  
ANISOU 1444  CB  ARG A 188     4551   4686   3544    -65   -212    737       C  
ATOM   1445  CG  ARG A 188     -23.833   0.490  -4.635  1.00 37.83           C  
ANISOU 1445  CG  ARG A 188     5164   5281   3928    -85   -254    824       C  
ATOM   1446  CD  ARG A 188     -25.176   1.055  -5.068  1.00 40.31           C  
ANISOU 1446  CD  ARG A 188     5496   5534   4285    -66   -390    889       C  
ATOM   1447  NE  ARG A 188     -25.134   1.587  -6.427  1.00 44.08           N  
ANISOU 1447  NE  ARG A 188     6069   6065   4616    -88   -441    991       N  
ATOM   1448  CZ  ARG A 188     -26.109   2.301  -6.981  1.00 45.38           C  
ANISOU 1448  CZ  ARG A 188     6269   6177   4795    -73   -568   1075       C  
ATOM   1449  NH1 ARG A 188     -27.209   2.571  -6.291  1.00 47.00           N  
ANISOU 1449  NH1 ARG A 188     6407   6284   5167    -29   -652   1056       N  
ATOM   1450  NH2 ARG A 188     -25.986   2.744  -8.224  1.00 48.73           N  
ANISOU 1450  NH2 ARG A 188     6796   6654   5064   -101   -614   1175       N  
ATOM   1451  N   GLN A 189     -20.727   0.969  -3.745  1.00 35.56           N  
ANISOU 1451  N   GLN A 189     4822   5086   3604   -160     29    806       N  
ATOM   1452  CA  GLN A 189     -19.739   2.032  -3.928  1.00 34.16           C  
ANISOU 1452  CA  GLN A 189     4651   4934   3396   -228    108    894       C  
ATOM   1453  C   GLN A 189     -20.418   3.234  -4.581  1.00 38.09           C  
ANISOU 1453  C   GLN A 189     5214   5370   3888   -266     30   1042       C  
ATOM   1454  O   GLN A 189     -20.312   3.481  -5.785  1.00 37.59           O  
ANISOU 1454  O   GLN A 189     5228   5379   3676   -306     16   1120       O  
ATOM   1455  CB  GLN A 189     -18.561   1.529  -4.753  1.00 36.97           C  
ANISOU 1455  CB  GLN A 189     5018   5445   3582   -256    203    856       C  
ATOM   1456  CG  GLN A 189     -17.385   2.487  -4.812  1.00 35.79           C  
ANISOU 1456  CG  GLN A 189     4851   5340   3405   -342    308    927       C  
ATOM   1457  CD  GLN A 189     -16.168   1.870  -5.472  1.00 39.34           C  
ANISOU 1457  CD  GLN A 189     5281   5966   3702   -363    418    855       C  
ATOM   1458  OE1 GLN A 189     -15.786   0.741  -5.165  1.00 39.65           O  
ANISOU 1458  OE1 GLN A 189     5271   6057   3736   -296    444    712       O  
ATOM   1459  NE2 GLN A 189     -15.557   2.607  -6.392  1.00 38.37           N  
ANISOU 1459  NE2 GLN A 189     5195   5934   3450   -458    479    952       N  
ATOM   1460  N   THR A 190     -21.134   3.997  -3.756  1.00 37.64           N  
ANISOU 1460  N   THR A 190     5129   5177   3995   -249    -29   1078       N  
ATOM   1461  CA  THR A 190     -21.816   5.198  -4.218  1.00 39.45           C  
ANISOU 1461  CA  THR A 190     5417   5318   4254   -268   -123   1210       C  
ATOM   1462  C   THR A 190     -21.931   6.181  -3.061  1.00 40.29           C  
ANISOU 1462  C   THR A 190     5472   5289   4549   -264   -128   1228       C  
ATOM   1463  O   THR A 190     -21.791   5.813  -1.892  1.00 38.52           O  
ANISOU 1463  O   THR A 190     5165   5040   4431   -236    -78   1130       O  
ATOM   1464  CB  THR A 190     -23.202   4.882  -4.791  1.00 39.93           C  
ANISOU 1464  CB  THR A 190     5510   5356   4307   -208   -262   1212       C  
ATOM   1465  OG1 THR A 190     -23.756   6.063  -5.385  1.00 43.08           O  
ANISOU 1465  OG1 THR A 190     5979   5674   4717   -222   -366   1348       O  
ATOM   1466  CG2 THR A 190     -24.133   4.387  -3.695  1.00 38.62           C  
ANISOU 1466  CG2 THR A 190     5253   5121   4301   -139   -303   1107       C  
ATOM   1467  N   ALA A 191     -22.203   7.439  -3.407  1.00 40.20           N  
ANISOU 1467  N   ALA A 191     5517   5184   4572   -292   -198   1353       N  
ATOM   1468  CA  ALA A 191     -22.220   8.520  -2.426  1.00 41.40           C  
ANISOU 1468  CA  ALA A 191     5633   5199   4897   -293   -209   1375       C  
ATOM   1469  C   ALA A 191     -23.245   8.254  -1.330  1.00 39.44           C  
ANISOU 1469  C   ALA A 191     5296   4880   4811   -202   -258   1266       C  
ATOM   1470  O   ALA A 191     -24.434   8.069  -1.609  1.00 42.37           O  
ANISOU 1470  O   ALA A 191     5664   5227   5206   -140   -366   1255       O  
ATOM   1471  CB  ALA A 191     -22.515   9.848  -3.120  1.00 41.83           C  
ANISOU 1471  CB  ALA A 191     5784   5148   4961   -327   -309   1530       C  
ATOM   1472  N   GLN A 192     -22.776   8.235  -0.083  1.00 45.75           N  
ANISOU 1472  N   GLN A 192     6016   5655   5713   -200   -179   1184       N  
ATOM   1473  CA  GLN A 192     -23.628   8.021   1.083  1.00 44.96           C  
ANISOU 1473  CA  GLN A 192     5827   5501   5755   -130   -203   1078       C  
ATOM   1474  C   GLN A 192     -23.115   8.895   2.216  1.00 45.54           C  
ANISOU 1474  C   GLN A 192     5856   5490   5958   -142   -158   1057       C  
ATOM   1475  O   GLN A 192     -21.953   8.773   2.615  1.00 47.03           O  
ANISOU 1475  O   GLN A 192     6032   5718   6119   -192    -57   1037       O  
ATOM   1476  CB  GLN A 192     -23.637   6.548   1.507  1.00 44.26           C  
ANISOU 1476  CB  GLN A 192     5688   5509   5621   -109   -144    961       C  
ATOM   1477  CG  GLN A 192     -24.177   5.591   0.458  1.00 42.94           C  
ANISOU 1477  CG  GLN A 192     5559   5420   5334    -94   -194    960       C  
ATOM   1478  CD  GLN A 192     -24.118   4.146   0.906  1.00 40.11           C  
ANISOU 1478  CD  GLN A 192     5164   5136   4940    -80   -144    848       C  
ATOM   1479  OE1 GLN A 192     -24.680   3.782   1.938  1.00 42.65           O  
ANISOU 1479  OE1 GLN A 192     5419   5428   5357    -54   -141    768       O  
ATOM   1480  NE2 GLN A 192     -23.432   3.314   0.132  1.00 39.95           N  
ANISOU 1480  NE2 GLN A 192     5190   5211   4778    -99   -107    838       N  
ATOM   1481  N   ALA A 193     -23.974   9.765   2.736  1.00 46.96           N  
ANISOU 1481  N   ALA A 193     6006   5555   6280    -92   -238   1049       N  
ATOM   1482  CA  ALA A 193     -23.587  10.686   3.795  1.00 48.43           C  
ANISOU 1482  CA  ALA A 193     6156   5649   6597    -95   -211   1020       C  
ATOM   1483  C   ALA A 193     -23.751  10.034   5.161  1.00 45.15           C  
ANISOU 1483  C   ALA A 193     5641   5266   6246    -59   -147    878       C  
ATOM   1484  O   ALA A 193     -24.749   9.356   5.425  1.00 47.07           O  
ANISOU 1484  O   ALA A 193     5833   5544   6509     -7   -173    806       O  
ATOM   1485  CB  ALA A 193     -24.416  11.968   3.725  1.00 48.32           C  
ANISOU 1485  CB  ALA A 193     6158   5489   6710    -48   -335   1066       C  
ATOM   1486  N   ALA A 194     -22.732  10.211   5.995  1.00 34.22           N  
ANISOU 1486  N   ALA A 194     4235   3879   4886    -96    -63    842       N  
ATOM   1487  CA  ALA A 194     -22.845   9.801   7.407  1.00 34.22           C  
ANISOU 1487  CA  ALA A 194     4154   3895   4952    -66    -10    715       C  
ATOM   1488  C   ALA A 194     -23.544  10.965   8.118  1.00 36.26           C  
ANISOU 1488  C   ALA A 194     4373   4037   5366    -16    -70    680       C  
ATOM   1489  O   ALA A 194     -23.445  12.116   7.643  1.00 40.55           O  
ANISOU 1489  O   ALA A 194     4964   4478   5966    -24   -133    758       O  
ATOM   1490  CB  ALA A 194     -21.478   9.537   7.985  1.00 33.41           C  
ANISOU 1490  CB  ALA A 194     4046   3837   4811   -117     88    687       C  
ATOM   1491  N   GLY A 195     -24.195  10.710   9.250  1.00 41.41           N  
ANISOU 1491  N   GLY A 195     4947   4703   6085     31    -51    562       N  
ATOM   1492  CA  GLY A 195     -24.884  11.817   9.939  1.00 47.43           C  
ANISOU 1492  CA  GLY A 195     5660   5364   6996     90   -107    506       C  
ATOM   1493  C   GLY A 195     -23.925  12.761  10.646  1.00 45.74           C  
ANISOU 1493  C   GLY A 195     5458   5073   6850     63    -80    492       C  
ATOM   1494  O   GLY A 195     -22.750  12.382  10.868  1.00 42.75           O  
ANISOU 1494  O   GLY A 195     5099   4742   6403     -1     -1    501       O  
ATOM   1495  N   THR A 196     -24.397  13.964  10.988  1.00 41.70           N  
ANISOU 1495  N   THR A 196     4929   4440   6476    114   -153    463       N  
ATOM   1496  CA  THR A 196     -23.542  14.901  11.760  1.00 37.80           C  
ANISOU 1496  CA  THR A 196     4440   3860   6061     90   -136    432       C  
ATOM   1497  C   THR A 196     -23.127  14.165  13.033  1.00 37.82           C  
ANISOU 1497  C   THR A 196     4382   3960   6026     79    -31    314       C  
ATOM   1498  O   THR A 196     -24.012  13.647  13.733  1.00 39.26           O  
ANISOU 1498  O   THR A 196     4495   4206   6216    131    -12    212       O  
ATOM   1499  CB  THR A 196     -24.299  16.167  12.170  1.00 37.63           C  
ANISOU 1499  CB  THR A 196     4395   3699   6205    170   -232    374       C  
ATOM   1500  OG1 THR A 196     -24.534  16.950  11.002  1.00 43.45           O  
ANISOU 1500  OG1 THR A 196     5210   4320   6978    174   -346    499       O  
ATOM   1501  CG2 THR A 196     -23.540  16.986  13.190  1.00 41.13           C  
ANISOU 1501  CG2 THR A 196     4829   4067   6732    154   -211    304       C  
ATOM   1502  N   ASP A 197     -21.830  14.097  13.309  1.00 40.55           N  
ANISOU 1502  N   ASP A 197     4753   4326   6330     10     32    329       N  
ATOM   1503  CA  ASP A 197     -21.415  13.358  14.491  1.00 42.00           C  
ANISOU 1503  CA  ASP A 197     4890   4599   6467      3    115    224       C  
ATOM   1504  C   ASP A 197     -21.448  14.267  15.710  1.00 43.84           C  
ANISOU 1504  C   ASP A 197     5083   4764   6811     37    106    112       C  
ATOM   1505  O   ASP A 197     -21.135  15.458  15.623  1.00 50.01           O  
ANISOU 1505  O   ASP A 197     5887   5423   7693     31     52    131       O  
ATOM   1506  CB  ASP A 197     -20.012  12.778  14.310  1.00 43.07           C  
ANISOU 1506  CB  ASP A 197     5058   4800   6508    -73    180    270       C  
ATOM   1507  CG  ASP A 197     -19.694  11.703  15.329  1.00 41.33           C  
ANISOU 1507  CG  ASP A 197     4806   4685   6213    -71    250    180       C  
ATOM   1508  OD1 ASP A 197     -20.644  11.105  15.878  1.00 40.46           O  
ANISOU 1508  OD1 ASP A 197     4665   4623   6086    -29    259    115       O  
ATOM   1509  OD2 ASP A 197     -18.497  11.458  15.585  1.00 38.87           O  
ANISOU 1509  OD2 ASP A 197     4501   4409   5859   -115    292    176       O  
ATOM   1510  N   THR A 198     -21.832  13.698  16.846  1.00 37.33           N  
ANISOU 1510  N   THR A 198     4204   4019   5963     67    156     -6       N  
ATOM   1511  CA  THR A 198     -21.911  14.420  18.104  1.00 38.15           C  
ANISOU 1511  CA  THR A 198     4264   4086   6147    103    158   -134       C  
ATOM   1512  C   THR A 198     -20.975  13.779  19.121  1.00 38.00           C  
ANISOU 1512  C   THR A 198     4243   4150   6046     62    231   -193       C  
ATOM   1513  O   THR A 198     -20.480  12.665  18.932  1.00 36.81           O  
ANISOU 1513  O   THR A 198     4116   4090   5780     21    278   -148       O  
ATOM   1514  CB  THR A 198     -23.350  14.444  18.637  1.00 42.24           C  
ANISOU 1514  CB  THR A 198     4709   4632   6710    181    148   -239       C  
ATOM   1515  OG1 THR A 198     -23.854  13.105  18.718  1.00 40.51           O  
ANISOU 1515  OG1 THR A 198     4469   4548   6376    165    208   -242       O  
ATOM   1516  CG2 THR A 198     -24.245  15.259  17.714  1.00 44.43           C  
ANISOU 1516  CG2 THR A 198     4981   4807   7093    239     51   -197       C  
ATOM   1517  N   THR A 199     -20.731  14.501  20.210  1.00 35.18           N  
ANISOU 1517  N   THR A 199     3862   3756   5749     79    230   -300       N  
ATOM   1518  CA  THR A 199     -19.843  14.032  21.263  1.00 33.37           C  
ANISOU 1518  CA  THR A 199     3634   3596   5448     48    282   -365       C  
ATOM   1519  C   THR A 199     -20.645  13.274  22.312  1.00 35.05           C  
ANISOU 1519  C   THR A 199     3812   3920   5587     76    334   -466       C  
ATOM   1520  O   THR A 199     -21.689  13.751  22.770  1.00 32.90           O  
ANISOU 1520  O   THR A 199     3488   3642   5371    130    328   -556       O  
ATOM   1521  CB  THR A 199     -19.098  15.204  21.905  1.00 34.42           C  
ANISOU 1521  CB  THR A 199     3764   3636   5678     43    249   -432       C  
ATOM   1522  OG1 THR A 199     -18.334  15.891  20.906  1.00 36.32           O  
ANISOU 1522  OG1 THR A 199     4042   3776   5983     -6    206   -326       O  
ATOM   1523  CG2 THR A 199     -18.161  14.709  22.994  1.00 33.27           C  
ANISOU 1523  CG2 THR A 199     3621   3568   5454     14    290   -503       C  
ATOM   1524  N   ILE A 200     -20.153  12.096  22.692  1.00 32.66           N  
ANISOU 1524  N   ILE A 200     3536   3718   5155     38    384   -454       N  
ATOM   1525  CA  ILE A 200     -20.819  11.265  23.688  1.00 30.62           C  
ANISOU 1525  CA  ILE A 200     3264   3568   4804     40    436   -528       C  
ATOM   1526  C   ILE A 200     -20.609  11.895  25.059  1.00 31.30           C  
ANISOU 1526  C   ILE A 200     3330   3662   4902     57    448   -660       C  
ATOM   1527  O   ILE A 200     -19.542  11.750  25.666  1.00 30.07           O  
ANISOU 1527  O   ILE A 200     3208   3519   4698     31    448   -678       O  
ATOM   1528  CB  ILE A 200     -20.298   9.818  23.645  1.00 30.56           C  
ANISOU 1528  CB  ILE A 200     3311   3644   4657     -7    466   -464       C  
ATOM   1529  CG1 ILE A 200     -20.196   9.339  22.195  1.00 29.23           C  
ANISOU 1529  CG1 ILE A 200     3168   3455   4483    -21    446   -341       C  
ATOM   1530  CG2 ILE A 200     -21.208   8.902  24.447  1.00 30.02           C  
ANISOU 1530  CG2 ILE A 200     3239   3677   4491    -21    517   -510       C  
ATOM   1531  CD1 ILE A 200     -19.387   8.073  22.020  1.00 28.59           C  
ANISOU 1531  CD1 ILE A 200     3144   3429   4289    -54    457   -285       C  
ATOM   1532  N   THR A 201     -21.634  12.596  25.551  1.00 31.88           N  
ANISOU 1532  N   THR A 201     3342   3731   5039    106    452   -763       N  
ATOM   1533  CA  THR A 201     -21.480  13.425  26.743  1.00 31.62           C  
ANISOU 1533  CA  THR A 201     3285   3690   5038    134    452   -904       C  
ATOM   1534  C   THR A 201     -21.185  12.585  27.979  1.00 29.32           C  
ANISOU 1534  C   THR A 201     3023   3521   4597     97    509   -962       C  
ATOM   1535  O   THR A 201     -20.296  12.921  28.771  1.00 30.44           O  
ANISOU 1535  O   THR A 201     3190   3652   4723     91    494  -1022       O  
ATOM   1536  CB  THR A 201     -22.737  14.269  26.957  1.00 32.11           C  
ANISOU 1536  CB  THR A 201     3267   3736   5199    206    447  -1016       C  
ATOM   1537  OG1 THR A 201     -23.028  15.007  25.763  1.00 33.38           O  
ANISOU 1537  OG1 THR A 201     3416   3773   5496    244    376   -948       O  
ATOM   1538  CG2 THR A 201     -22.537  15.239  28.110  1.00 35.03           C  
ANISOU 1538  CG2 THR A 201     3612   4083   5613    246    438  -1174       C  
ATOM   1539  N   VAL A 202     -21.925  11.489  28.168  1.00 29.74           N  
ANISOU 1539  N   VAL A 202     3079   3687   4535     67    568   -942       N  
ATOM   1540  CA  VAL A 202     -21.722  10.653  29.349  1.00 31.53           C  
ANISOU 1540  CA  VAL A 202     3349   4026   4604     22    618   -982       C  
ATOM   1541  C   VAL A 202     -20.322  10.054  29.353  1.00 29.99           C  
ANISOU 1541  C   VAL A 202     3239   3812   4342    -13    582   -907       C  
ATOM   1542  O   VAL A 202     -19.761   9.770  30.419  1.00 28.34           O  
ANISOU 1542  O   VAL A 202     3075   3657   4035    -32    587   -957       O  
ATOM   1543  CB  VAL A 202     -22.814   9.565  29.427  1.00 32.46           C  
ANISOU 1543  CB  VAL A 202     3460   4256   4618    -23    684   -956       C  
ATOM   1544  CG1 VAL A 202     -22.702   8.600  28.255  1.00 33.52           C  
ANISOU 1544  CG1 VAL A 202     3637   4366   4734    -55    663   -807       C  
ATOM   1545  CG2 VAL A 202     -22.744   8.822  30.756  1.00 31.77           C  
ANISOU 1545  CG2 VAL A 202     3424   4285   4362    -78    736  -1002       C  
ATOM   1546  N   ASN A 203     -19.726   9.871  28.172  1.00 26.03           N  
ANISOU 1546  N   ASN A 203     2757   3242   3890    -18    542   -794       N  
ATOM   1547  CA  ASN A 203     -18.362   9.360  28.105  1.00 24.86           C  
ANISOU 1547  CA  ASN A 203     2669   3082   3695    -40    506   -738       C  
ATOM   1548  C   ASN A 203     -17.353  10.419  28.533  1.00 26.33           C  
ANISOU 1548  C   ASN A 203     2840   3207   3959    -24    463   -806       C  
ATOM   1549  O   ASN A 203     -16.361  10.104  29.202  1.00 27.35           O  
ANISOU 1549  O   ASN A 203     3006   3362   4025    -37    440   -829       O  
ATOM   1550  CB  ASN A 203     -18.056   8.868  26.691  1.00 25.17           C  
ANISOU 1550  CB  ASN A 203     2721   3082   3759    -51    486   -612       C  
ATOM   1551  CG  ASN A 203     -18.678   7.516  26.397  1.00 25.16           C  
ANISOU 1551  CG  ASN A 203     2761   3144   3655    -77    512   -544       C  
ATOM   1552  OD1 ASN A 203     -19.451   6.988  27.196  1.00 25.33           O  
ANISOU 1552  OD1 ASN A 203     2795   3236   3593    -97    550   -580       O  
ATOM   1553  ND2 ASN A 203     -18.343   6.951  25.243  1.00 24.10           N  
ANISOU 1553  ND2 ASN A 203     2646   2988   3521    -83    493   -447       N  
ATOM   1554  N   VAL A 204     -17.583  11.678  28.150  1.00 25.81           N  
ANISOU 1554  N   VAL A 204     2722   3051   4033      3    443   -839       N  
ATOM   1555  CA  VAL A 204     -16.691  12.758  28.565  1.00 25.86           C  
ANISOU 1555  CA  VAL A 204     2713   2986   4126      9    397   -909       C  
ATOM   1556  C   VAL A 204     -16.686  12.888  30.082  1.00 25.88           C  
ANISOU 1556  C   VAL A 204     2722   3049   4061     22    405  -1047       C  
ATOM   1557  O   VAL A 204     -15.629  13.058  30.703  1.00 26.58           O  
ANISOU 1557  O   VAL A 204     2829   3135   4136     10    368  -1092       O  
ATOM   1558  CB  VAL A 204     -17.097  14.081  27.888  1.00 27.61           C  
ANISOU 1558  CB  VAL A 204     2892   3083   4515     35    363   -917       C  
ATOM   1559  CG1 VAL A 204     -16.299  15.241  28.464  1.00 28.93           C  
ANISOU 1559  CG1 VAL A 204     3047   3166   4777     36    312  -1007       C  
ATOM   1560  CG2 VAL A 204     -16.901  13.994  26.389  1.00 26.34           C  
ANISOU 1560  CG2 VAL A 204     2740   2864   4405     10    347   -772       C  
ATOM   1561  N   LEU A 205     -17.865  12.805  30.702  1.00 29.61           N  
ANISOU 1561  N   LEU A 205     3176   3589   4484     45    454  -1120       N  
ATOM   1562  CA  LEU A 205     -17.946  12.918  32.154  1.00 32.36           C  
ANISOU 1562  CA  LEU A 205     3533   4015   4747     53    473  -1255       C  
ATOM   1563  C   LEU A 205     -17.231  11.759  32.838  1.00 32.62           C  
ANISOU 1563  C   LEU A 205     3643   4139   4611     10    475  -1221       C  
ATOM   1564  O   LEU A 205     -16.532  11.957  33.838  1.00 32.79           O  
ANISOU 1564  O   LEU A 205     3692   4185   4581     11    446  -1304       O  
ATOM   1565  CB  LEU A 205     -19.408  12.987  32.591  1.00 35.46           C  
ANISOU 1565  CB  LEU A 205     3879   4484   5113     77    541  -1338       C  
ATOM   1566  CG  LEU A 205     -20.208  14.149  31.999  1.00 34.14           C  
ANISOU 1566  CG  LEU A 205     3631   4224   5118    139    524  -1392       C  
ATOM   1567  CD1 LEU A 205     -21.699  13.936  32.198  1.00 35.36           C  
ANISOU 1567  CD1 LEU A 205     3722   4474   5240    160    595  -1452       C  
ATOM   1568  CD2 LEU A 205     -19.764  15.470  32.607  1.00 33.87           C  
ANISOU 1568  CD2 LEU A 205     3575   4106   5188    185    470  -1528       C  
ATOM   1569  N   ALA A 206     -17.392  10.543  32.310  1.00 31.43           N  
ANISOU 1569  N   ALA A 206     3534   4033   4375    -23    498  -1102       N  
ATOM   1570  CA  ALA A 206     -16.660   9.402  32.852  1.00 28.68           C  
ANISOU 1570  CA  ALA A 206     3272   3747   3879    -56    478  -1057       C  
ATOM   1571  C   ALA A 206     -15.157   9.604  32.720  1.00 29.71           C  
ANISOU 1571  C   ALA A 206     3413   3819   4056    -46    400  -1046       C  
ATOM   1572  O   ALA A 206     -14.387   9.207  33.602  1.00 32.39           O  
ANISOU 1572  O   ALA A 206     3806   4200   4301    -51    359  -1079       O  
ATOM   1573  CB  ALA A 206     -17.094   8.117  32.148  1.00 29.04           C  
ANISOU 1573  CB  ALA A 206     3359   3822   3852    -88    503   -930       C  
ATOM   1574  N   TRP A 207     -14.722  10.225  31.622  1.00 30.34           N  
ANISOU 1574  N   TRP A 207     3441   3808   4280    -37    377  -1001       N  
ATOM   1575  CA  TRP A 207     -13.305  10.513  31.436  1.00 31.68           C  
ANISOU 1575  CA  TRP A 207     3599   3931   4507    -40    313   -999       C  
ATOM   1576  C   TRP A 207     -12.829  11.612  32.377  1.00 32.96           C  
ANISOU 1576  C   TRP A 207     3735   4066   4722    -30    275  -1129       C  
ATOM   1577  O   TRP A 207     -11.675  11.591  32.820  1.00 33.40           O  
ANISOU 1577  O   TRP A 207     3797   4128   4766    -34    217  -1162       O  
ATOM   1578  CB  TRP A 207     -13.048  10.893  29.978  1.00 29.95           C  
ANISOU 1578  CB  TRP A 207     3333   3633   4413    -51    312   -908       C  
ATOM   1579  CG  TRP A 207     -11.660  11.364  29.689  1.00 33.90           C  
ANISOU 1579  CG  TRP A 207     3798   4090   4992    -70    262   -910       C  
ATOM   1580  CD1 TRP A 207     -10.524  10.608  29.663  1.00 34.83           C  
ANISOU 1580  CD1 TRP A 207     3924   4252   5059    -76    226   -887       C  
ATOM   1581  CD2 TRP A 207     -11.262  12.699  29.358  1.00 35.24           C  
ANISOU 1581  CD2 TRP A 207     3914   4165   5310    -91    238   -938       C  
ATOM   1582  NE1 TRP A 207      -9.442  11.393  29.346  1.00 36.92           N  
ANISOU 1582  NE1 TRP A 207     4129   4470   5430   -103    193   -905       N  
ATOM   1583  CE2 TRP A 207      -9.869  12.680  29.154  1.00 36.90           C  
ANISOU 1583  CE2 TRP A 207     4093   4378   5549   -122    200   -929       C  
ATOM   1584  CE3 TRP A 207     -11.949  13.909  29.220  1.00 35.15           C  
ANISOU 1584  CE3 TRP A 207     3877   4062   5417    -87    239   -972       C  
ATOM   1585  CZ2 TRP A 207      -9.149  13.825  28.819  1.00 38.28           C  
ANISOU 1585  CZ2 TRP A 207     4215   4470   5860   -167    172   -945       C  
ATOM   1586  CZ3 TRP A 207     -11.233  15.044  28.888  1.00 36.98           C  
ANISOU 1586  CZ3 TRP A 207     4071   4193   5785   -123    199   -984       C  
ATOM   1587  CH2 TRP A 207      -9.848  14.993  28.689  1.00 36.18           C  
ANISOU 1587  CH2 TRP A 207     3942   4101   5704   -172    171   -966       C  
ATOM   1588  N   LEU A 208     -13.698  12.576  32.696  1.00 34.66           N  
ANISOU 1588  N   LEU A 208     3918   4252   5001    -10    300  -1213       N  
ATOM   1589  CA  LEU A 208     -13.339  13.595  33.675  1.00 34.78           C  
ANISOU 1589  CA  LEU A 208     3915   4240   5058      6    260  -1356       C  
ATOM   1590  C   LEU A 208     -13.237  13.010  35.077  1.00 35.37           C  
ANISOU 1590  C   LEU A 208     4048   4428   4965      9    257  -1438       C  
ATOM   1591  O   LEU A 208     -12.395  13.447  35.869  1.00 38.51           O  
ANISOU 1591  O   LEU A 208     4449   4822   5359     12    198  -1529       O  
ATOM   1592  CB  LEU A 208     -14.353  14.738  33.646  1.00 35.63           C  
ANISOU 1592  CB  LEU A 208     3975   4285   5278     40    281  -1437       C  
ATOM   1593  CG  LEU A 208     -14.289  15.660  32.426  1.00 37.57           C  
ANISOU 1593  CG  LEU A 208     4176   4388   5710     37    253  -1377       C  
ATOM   1594  CD1 LEU A 208     -15.382  16.716  32.490  1.00 35.80           C  
ANISOU 1594  CD1 LEU A 208     3912   4098   5592     88    257  -1468       C  
ATOM   1595  CD2 LEU A 208     -12.917  16.308  32.314  1.00 36.30           C  
ANISOU 1595  CD2 LEU A 208     4004   4146   5643      0    182  -1382       C  
ATOM   1596  N   TYR A 209     -14.083  12.029  35.402  1.00 34.51           N  
ANISOU 1596  N   TYR A 209     3985   4417   4710      0    316  -1404       N  
ATOM   1597  CA  TYR A 209     -13.955  11.341  36.682  1.00 33.05           C  
ANISOU 1597  CA  TYR A 209     3876   4341   4341    -11    310  -1453       C  
ATOM   1598  C   TYR A 209     -12.644  10.569  36.759  1.00 34.67           C  
ANISOU 1598  C   TYR A 209     4135   4550   4487    -21    230  -1394       C  
ATOM   1599  O   TYR A 209     -11.993  10.545  37.809  1.00 34.14           O  
ANISOU 1599  O   TYR A 209     4112   4526   4333    -16    174  -1469       O  
ATOM   1600  CB  TYR A 209     -15.144  10.404  36.901  1.00 32.39           C  
ANISOU 1600  CB  TYR A 209     3835   4356   4116    -39    394  -1407       C  
ATOM   1601  CG  TYR A 209     -16.373  11.088  37.455  1.00 34.50           C  
ANISOU 1601  CG  TYR A 209     4053   4677   4378    -27    471  -1524       C  
ATOM   1602  CD1 TYR A 209     -16.417  11.522  38.773  1.00 36.86           C  
ANISOU 1602  CD1 TYR A 209     4368   5050   4584    -20    476  -1668       C  
ATOM   1603  CD2 TYR A 209     -17.492  11.297  36.659  1.00 35.13           C  
ANISOU 1603  CD2 TYR A 209     4063   4739   4544    -18    535  -1500       C  
ATOM   1604  CE1 TYR A 209     -17.541  12.148  39.282  1.00 39.06           C  
ANISOU 1604  CE1 TYR A 209     4590   5392   4859     -2    552  -1794       C  
ATOM   1605  CE2 TYR A 209     -18.618  11.922  37.158  1.00 36.89           C  
ANISOU 1605  CE2 TYR A 209     4224   5019   4773      4    602  -1623       C  
ATOM   1606  CZ  TYR A 209     -18.637  12.345  38.470  1.00 39.74           C  
ANISOU 1606  CZ  TYR A 209     4596   5460   5042     13    615  -1774       C  
ATOM   1607  OH  TYR A 209     -19.758  12.967  38.970  1.00 40.04           O  
ANISOU 1607  OH  TYR A 209     4561   5568   5085     42    687  -1914       O  
ATOM   1608  N   ALA A 210     -12.243   9.933  35.654  1.00 33.35           N  
ANISOU 1608  N   ALA A 210     3964   4343   4366    -28    217  -1269       N  
ATOM   1609  CA  ALA A 210     -10.960   9.238  35.621  1.00 34.00           C  
ANISOU 1609  CA  ALA A 210     4077   4427   4415    -22    136  -1227       C  
ATOM   1610  C   ALA A 210      -9.808  10.194  35.897  1.00 34.11           C  
ANISOU 1610  C   ALA A 210     4034   4398   4530    -11     63  -1319       C  
ATOM   1611  O   ALA A 210      -8.841   9.835  36.578  1.00 36.43           O  
ANISOU 1611  O   ALA A 210     4359   4724   4759      2    -18  -1355       O  
ATOM   1612  CB  ALA A 210     -10.771   8.548  34.270  1.00 31.88           C  
ANISOU 1612  CB  ALA A 210     3792   4123   4197    -25    144  -1098       C  
ATOM   1613  N   ALA A 211      -9.894  11.420  35.373  1.00 32.67           N  
ANISOU 1613  N   ALA A 211     3769   4134   4508    -17     81  -1357       N  
ATOM   1614  CA  ALA A 211      -8.856  12.411  35.636  1.00 33.44           C  
ANISOU 1614  CA  ALA A 211     3811   4180   4714    -23     12  -1448       C  
ATOM   1615  C   ALA A 211      -8.821  12.795  37.109  1.00 34.65           C  
ANISOU 1615  C   ALA A 211     4001   4378   4787     -6    -28  -1591       C  
ATOM   1616  O   ALA A 211      -7.742  12.966  37.688  1.00 35.16           O  
ANISOU 1616  O   ALA A 211     4057   4450   4853     -4   -112  -1660       O  
ATOM   1617  CB  ALA A 211      -9.078  13.645  34.764  1.00 31.83           C  
ANISOU 1617  CB  ALA A 211     3532   3864   4698    -42     36  -1447       C  
ATOM   1618  N   VAL A 212      -9.994  12.943  37.730  1.00 43.62           N  
ANISOU 1618  N   VAL A 212     5170   5554   5848      7     32  -1646       N  
ATOM   1619  CA  VAL A 212     -10.048  13.258  39.155  1.00 44.49           C  
ANISOU 1619  CA  VAL A 212     5321   5728   5855     22      5  -1789       C  
ATOM   1620  C   VAL A 212      -9.465  12.114  39.976  1.00 44.56           C  
ANISOU 1620  C   VAL A 212     5422   5834   5674     21    -49  -1765       C  
ATOM   1621  O   VAL A 212      -8.751  12.338  40.961  1.00 46.87           O  
ANISOU 1621  O   VAL A 212     5739   6158   5911     32   -128  -1866       O  
ATOM   1622  CB  VAL A 212     -11.494  13.579  39.578  1.00 44.31           C  
ANISOU 1622  CB  VAL A 212     5303   5750   5784     35     97  -1855       C  
ATOM   1623  CG1 VAL A 212     -11.560  13.873  41.069  1.00 48.07           C  
ANISOU 1623  CG1 VAL A 212     5823   6312   6130     48     79  -2011       C  
ATOM   1624  CG2 VAL A 212     -12.032  14.755  38.778  1.00 44.13           C  
ANISOU 1624  CG2 VAL A 212     5192   5613   5960     52    125  -1885       C  
ATOM   1625  N   ILE A 213      -9.759  10.872  39.582  1.00 41.48           N  
ANISOU 1625  N   ILE A 213     5090   5486   5184     10    -19  -1633       N  
ATOM   1626  CA  ILE A 213      -9.210   9.716  40.285  1.00 40.75           C  
ANISOU 1626  CA  ILE A 213     5101   5465   4918     11    -87  -1593       C  
ATOM   1627  C   ILE A 213      -7.692   9.684  40.168  1.00 39.41           C  
ANISOU 1627  C   ILE A 213     4899   5258   4815     36   -207  -1604       C  
ATOM   1628  O   ILE A 213      -6.997   9.249  41.096  1.00 41.79           O  
ANISOU 1628  O   ILE A 213     5268   5609   5002     53   -302  -1643       O  
ATOM   1629  CB  ILE A 213      -9.852   8.418  39.752  1.00 42.74           C  
ANISOU 1629  CB  ILE A 213     5421   5743   5076     -9    -38  -1445       C  
ATOM   1630  CG1 ILE A 213     -11.356   8.410  40.034  1.00 42.98           C  
ANISOU 1630  CG1 ILE A 213     5476   5833   5022    -43     80  -1448       C  
ATOM   1631  CG2 ILE A 213      -9.202   7.190  40.372  1.00 43.05           C  
ANISOU 1631  CG2 ILE A 213     5577   5826   4952     -2   -129  -1390       C  
ATOM   1632  CD1 ILE A 213     -12.104   7.295  39.334  1.00 43.42           C  
ANISOU 1632  CD1 ILE A 213     5576   5899   5024    -75    138  -1306       C  
ATOM   1633  N   ASN A 214      -7.149  10.162  39.048  1.00 46.35           N  
ANISOU 1633  N   ASN A 214     5674   6058   5878     34   -207  -1574       N  
ATOM   1634  CA  ASN A 214      -5.713  10.135  38.804  1.00 46.76           C  
ANISOU 1634  CA  ASN A 214     5669   6088   6009     49   -306  -1587       C  
ATOM   1635  C   ASN A 214      -5.033  11.466  39.116  1.00 48.05           C  
ANISOU 1635  C   ASN A 214     5746   6206   6304     36   -353  -1716       C  
ATOM   1636  O   ASN A 214      -3.907  11.698  38.664  1.00 47.68           O  
ANISOU 1636  O   ASN A 214     5615   6131   6371     29   -412  -1727       O  
ATOM   1637  CB  ASN A 214      -5.433   9.718  37.359  1.00 42.70           C  
ANISOU 1637  CB  ASN A 214     5093   5533   5598     44   -275  -1471       C  
ATOM   1638  CG  ASN A 214      -5.565   8.221  37.152  1.00 48.54           C  
ANISOU 1638  CG  ASN A 214     5918   6314   6212     69   -285  -1364       C  
ATOM   1639  OD1 ASN A 214      -4.614   7.468  37.363  1.00 47.50           O  
ANISOU 1639  OD1 ASN A 214     5805   6207   6034    107   -381  -1362       O  
ATOM   1640  ND2 ASN A 214      -6.748   7.782  36.739  1.00 46.29           N  
ANISOU 1640  ND2 ASN A 214     5683   6030   5877     52   -195  -1279       N  
ATOM   1641  N   GLY A 215      -5.690  12.344  39.874  1.00 57.81           N  
ANISOU 1641  N   GLY A 215     6997   7438   7529     31   -328  -1820       N  
ATOM   1642  CA  GLY A 215      -5.064  13.529  40.416  1.00 57.89           C  
ANISOU 1642  CA  GLY A 215     6949   7407   7639     23   -393  -1962       C  
ATOM   1643  C   GLY A 215      -5.342  14.819  39.669  1.00 60.43           C  
ANISOU 1643  C   GLY A 215     7183   7614   8162     -9   -347  -1988       C  
ATOM   1644  O   GLY A 215      -5.152  15.898  40.242  1.00 64.48           O  
ANISOU 1644  O   GLY A 215     7668   8081   8750    -16   -390  -2120       O  
ATOM   1645  N   ASP A 216      -5.778  14.745  38.413  1.00 54.69           N  
ANISOU 1645  N   ASP A 216     6422   6835   7524    -29   -271  -1865       N  
ATOM   1646  CA  ASP A 216      -6.040  15.946  37.624  1.00 55.96           C  
ANISOU 1646  CA  ASP A 216     6514   6874   7874    -62   -239  -1868       C  
ATOM   1647  C   ASP A 216      -7.358  16.561  38.082  1.00 57.67           C  
ANISOU 1647  C   ASP A 216     6763   7071   8078    -32   -186  -1943       C  
ATOM   1648  O   ASP A 216      -8.433  16.011  37.818  1.00 56.98           O  
ANISOU 1648  O   ASP A 216     6711   7022   7918    -11   -105  -1876       O  
ATOM   1649  CB  ASP A 216      -6.071  15.612  36.136  1.00 53.36           C  
ANISOU 1649  CB  ASP A 216     6147   6506   7622    -93   -182  -1710       C  
ATOM   1650  CG  ASP A 216      -4.706  15.731  35.483  1.00 58.31           C  
ANISOU 1650  CG  ASP A 216     6693   7108   8353   -143   -230  -1677       C  
ATOM   1651  OD1 ASP A 216      -3.751  16.149  36.171  1.00 61.13           O  
ANISOU 1651  OD1 ASP A 216     7016   7469   8743   -157   -312  -1780       O  
ATOM   1652  OD2 ASP A 216      -4.589  15.407  34.283  1.00 58.27           O  
ANISOU 1652  OD2 ASP A 216     6654   7090   8394   -172   -184  -1554       O  
ATOM   1653  N   ARG A 217      -7.280  17.705  38.768  1.00 55.18           N  
ANISOU 1653  N   ARG A 217     6429   6696   7839    -27   -233  -2091       N  
ATOM   1654  CA  ARG A 217      -8.456  18.340  39.351  1.00 55.43           C  
ANISOU 1654  CA  ARG A 217     6481   6720   7859     16   -193  -2201       C  
ATOM   1655  C   ARG A 217      -8.564  19.826  39.029  1.00 55.81           C  
ANISOU 1655  C   ARG A 217     6479   6610   8118     11   -225  -2279       C  
ATOM   1656  O   ARG A 217      -9.431  20.504  39.593  1.00 57.67           O  
ANISOU 1656  O   ARG A 217     6720   6826   8364     60   -211  -2406       O  
ATOM   1657  CB  ARG A 217      -8.466  18.162  40.874  1.00 54.64           C  
ANISOU 1657  CB  ARG A 217     6437   6734   7591     50   -222  -2347       C  
ATOM   1658  CG  ARG A 217      -8.303  16.734  41.352  1.00 56.42           C  
ANISOU 1658  CG  ARG A 217     6736   7104   7598     51   -213  -2275       C  
ATOM   1659  CD  ARG A 217      -8.312  16.673  42.869  1.00 59.93           C  
ANISOU 1659  CD  ARG A 217     7245   7655   7868     75   -248  -2419       C  
ATOM   1660  NE  ARG A 217      -9.666  16.582  43.409  1.00 59.94           N  
ANISOU 1660  NE  ARG A 217     7285   7742   7748     98   -150  -2470       N  
ATOM   1661  CZ  ARG A 217     -10.391  17.626  43.800  1.00 62.39           C  
ANISOU 1661  CZ  ARG A 217     7561   8027   8117    131   -121  -2621       C  
ATOM   1662  NH1 ARG A 217     -11.614  17.441  44.278  1.00 62.53           N  
ANISOU 1662  NH1 ARG A 217     7599   8147   8014    151    -22  -2670       N  
ATOM   1663  NH2 ARG A 217      -9.900  18.854  43.710  1.00 63.56           N  
ANISOU 1663  NH2 ARG A 217     7652   8048   8451    142   -192  -2728       N  
ATOM   1664  N   TRP A 218      -7.710  20.354  38.148  1.00 48.17           N  
ANISOU 1664  N   TRP A 218     5462   5527   7315    -49   -270  -2212       N  
ATOM   1665  CA  TRP A 218      -7.674  21.795  37.918  1.00 48.08           C  
ANISOU 1665  CA  TRP A 218     5418   5346   7506    -68   -322  -2284       C  
ATOM   1666  C   TRP A 218      -8.955  22.321  37.289  1.00 49.99           C  
ANISOU 1666  C   TRP A 218     5664   5498   7833    -27   -272  -2257       C  
ATOM   1667  O   TRP A 218      -9.245  23.517  37.408  1.00 51.31           O  
ANISOU 1667  O   TRP A 218     5823   5530   8142     -9   -322  -2360       O  
ATOM   1668  CB  TRP A 218      -6.480  22.163  37.034  1.00 48.63           C  
ANISOU 1668  CB  TRP A 218     5436   5321   7720   -164   -370  -2193       C  
ATOM   1669  CG  TRP A 218      -6.518  21.575  35.646  1.00 47.56           C  
ANISOU 1669  CG  TRP A 218     5285   5182   7602   -205   -304  -1992       C  
ATOM   1670  CD1 TRP A 218      -5.846  20.471  35.207  1.00 45.98           C  
ANISOU 1670  CD1 TRP A 218     5068   5090   7313   -232   -276  -1881       C  
ATOM   1671  CD2 TRP A 218      -7.248  22.073  34.514  1.00 48.61           C  
ANISOU 1671  CD2 TRP A 218     5421   5200   7849   -218   -268  -1885       C  
ATOM   1672  NE1 TRP A 218      -6.117  20.247  33.879  1.00 45.44           N  
ANISOU 1672  NE1 TRP A 218     4990   4988   7288   -264   -217  -1719       N  
ATOM   1673  CE2 TRP A 218      -6.975  21.216  33.430  1.00 45.64           C  
ANISOU 1673  CE2 TRP A 218     5031   4878   7433   -260   -212  -1712       C  
ATOM   1674  CE3 TRP A 218      -8.109  23.157  34.314  1.00 48.52           C  
ANISOU 1674  CE3 TRP A 218     5426   5042   7968   -192   -287  -1924       C  
ATOM   1675  CZ2 TRP A 218      -7.531  21.409  32.167  1.00 45.10           C  
ANISOU 1675  CZ2 TRP A 218     4968   4729   7438   -283   -172  -1572       C  
ATOM   1676  CZ3 TRP A 218      -8.660  23.346  33.060  1.00 48.01           C  
ANISOU 1676  CZ3 TRP A 218     5369   4888   7984   -210   -256  -1780       C  
ATOM   1677  CH2 TRP A 218      -8.370  22.477  32.004  1.00 48.04           C  
ANISOU 1677  CH2 TRP A 218     5363   4957   7934   -259   -198  -1603       C  
ATOM   1678  N   PHE A 219      -9.720  21.464  36.619  1.00 46.34           N  
ANISOU 1678  N   PHE A 219     5213   5101   7293     -8   -188  -2128       N  
ATOM   1679  CA  PHE A 219     -10.942  21.871  35.942  1.00 46.69           C  
ANISOU 1679  CA  PHE A 219     5253   5070   7416     34   -147  -2094       C  
ATOM   1680  C   PHE A 219     -12.155  21.856  36.855  1.00 44.28           C  
ANISOU 1680  C   PHE A 219     4956   4847   7021    123   -102  -2233       C  
ATOM   1681  O   PHE A 219     -13.191  22.413  36.488  1.00 47.23           O  
ANISOU 1681  O   PHE A 219     5312   5151   7482    176    -86  -2256       O  
ATOM   1682  CB  PHE A 219     -11.219  20.952  34.754  1.00 42.87           C  
ANISOU 1682  CB  PHE A 219     4772   4625   6893     10    -80  -1896       C  
ATOM   1683  CG  PHE A 219     -11.139  19.494  35.100  1.00 41.98           C  
ANISOU 1683  CG  PHE A 219     4684   4688   6577     11    -23  -1843       C  
ATOM   1684  CD1 PHE A 219     -12.247  18.818  35.588  1.00 41.10           C  
ANISOU 1684  CD1 PHE A 219     4595   4691   6330     62     47  -1871       C  
ATOM   1685  CD2 PHE A 219      -9.952  18.801  34.944  1.00 43.47           C  
ANISOU 1685  CD2 PHE A 219     4874   4927   6715    -42    -44  -1769       C  
ATOM   1686  CE1 PHE A 219     -12.170  17.476  35.908  1.00 40.29           C  
ANISOU 1686  CE1 PHE A 219     4532   4734   6043     52     89  -1811       C  
ATOM   1687  CE2 PHE A 219      -9.869  17.461  35.262  1.00 40.56           C  
ANISOU 1687  CE2 PHE A 219     4541   4701   6169    -34    -10  -1720       C  
ATOM   1688  CZ  PHE A 219     -10.980  16.796  35.744  1.00 40.99           C  
ANISOU 1688  CZ  PHE A 219     4634   4852   6087      9     54  -1735       C  
ATOM   1689  N   LEU A 220     -12.062  21.225  38.019  1.00 39.55           N  
ANISOU 1689  N   LEU A 220     4382   4399   6245    139    -81  -2325       N  
ATOM   1690  CA  LEU A 220     -13.181  21.236  38.943  1.00 41.48           C  
ANISOU 1690  CA  LEU A 220     4629   4742   6389    210    -27  -2467       C  
ATOM   1691  C   LEU A 220     -13.454  22.660  39.379  1.00 47.41           C  
ANISOU 1691  C   LEU A 220     5353   5373   7288    266    -88  -2653       C  
ATOM   1692  O   LEU A 220     -12.562  23.372  39.846  1.00 45.89           O  
ANISOU 1692  O   LEU A 220     5166   5105   7165    248   -176  -2748       O  
ATOM   1693  CB  LEU A 220     -12.890  20.365  40.160  1.00 41.82           C  
ANISOU 1693  CB  LEU A 220     4720   4964   6204    202     -6  -2528       C  
ATOM   1694  CG  LEU A 220     -12.731  18.881  39.839  1.00 40.81           C  
ANISOU 1694  CG  LEU A 220     4634   4953   5919    158     46  -2356       C  
ATOM   1695  CD1 LEU A 220     -12.400  18.122  41.103  1.00 41.59           C  
ANISOU 1695  CD1 LEU A 220     4797   5207   5797    149     44  -2418       C  
ATOM   1696  CD2 LEU A 220     -14.004  18.370  39.202  1.00 37.17           C  
ANISOU 1696  CD2 LEU A 220     4157   4534   5433    174    145  -2271       C  
ATOM   1697  N   ASN A 221     -14.696  23.080  39.225  1.00 56.48           N  
ANISOU 1697  N   ASN A 221     6466   6501   8492    338    -48  -2715       N  
ATOM   1698  CA  ASN A 221     -15.083  24.385  39.719  1.00 57.40           C  
ANISOU 1698  CA  ASN A 221     6557   6512   8742    412   -107  -2917       C  
ATOM   1699  C   ASN A 221     -16.066  24.174  40.864  1.00 61.20           C  
ANISOU 1699  C   ASN A 221     7019   7175   9059    480    -30  -3073       C  
ATOM   1700  O   ASN A 221     -16.616  23.083  41.062  1.00 59.57           O  
ANISOU 1700  O   ASN A 221     6815   7143   8676    470     76  -3040       O  
ATOM   1701  CB  ASN A 221     -15.691  25.283  38.621  1.00 59.52           C  
ANISOU 1701  CB  ASN A 221     6795   6585   9237    453   -151  -2873       C  
ATOM   1702  CG  ASN A 221     -16.948  24.699  38.016  1.00 57.17           C  
ANISOU 1702  CG  ASN A 221     6460   6362   8901    498    -62  -2797       C  
ATOM   1703  OD1 ASN A 221     -17.713  24.002  38.682  1.00 56.08           O  
ANISOU 1703  OD1 ASN A 221     6299   6411   8598    529     34  -2864       O  
ATOM   1704  ND2 ASN A 221     -17.193  25.015  36.754  1.00 58.46           N  
ANISOU 1704  ND2 ASN A 221     6616   6379   9215    496    -97  -2660       N  
ATOM   1705  N   ARG A 222     -16.223  25.213  41.671  1.00 85.90           N  
ANISOU 1705  N   ARG A 222    10132  10282  12225    531    -84  -3209       N  
ATOM   1706  CA  ARG A 222     -17.220  25.219  42.721  1.00 87.03           C  
ANISOU 1706  CA  ARG A 222    10245  10595  12228    591    -16  -3339       C  
ATOM   1707  C   ARG A 222     -18.474  25.956  42.288  1.00 91.33           C  
ANISOU 1707  C   ARG A 222    10718  11083  12902    678    -10  -3378       C  
ATOM   1708  O   ARG A 222     -18.808  26.959  42.934  1.00 91.83           O  
ANISOU 1708  O   ARG A 222    10752  11121  13016    742    -58  -3515       O  
ATOM   1709  CB  ARG A 222     -16.624  25.797  44.013  1.00 92.66           C  
ANISOU 1709  CB  ARG A 222    10985  11349  12872    598    -73  -3481       C  
ATOM   1710  CG  ARG A 222     -17.398  25.550  45.344  1.00 94.96           C  
ANISOU 1710  CG  ARG A 222    11267  11863  12952    632     11  -3613       C  
ATOM   1711  CD  ARG A 222     -17.079  24.217  46.022  1.00 97.52           C  
ANISOU 1711  CD  ARG A 222    11654  12389  13012    564     90  -3570       C  
ATOM   1712  NE  ARG A 222     -17.934  23.158  45.514  1.00 97.84           N  
ANISOU 1712  NE  ARG A 222    11676  12541  12957    542    210  -3472       N  
ATOM   1713  CZ  ARG A 222     -19.144  22.843  45.976  1.00100.26           C  
ANISOU 1713  CZ  ARG A 222    11940  13012  13142    561    321  -3518       C  
ATOM   1714  NH1 ARG A 222     -19.786  21.854  45.379  1.00 97.43           N  
ANISOU 1714  NH1 ARG A 222    11568  12735  12717    526    419  -3408       N  
ATOM   1715  NH2 ARG A 222     -19.704  23.456  47.015  1.00102.96           N  
ANISOU 1715  NH2 ARG A 222    12251  13445  13425    608    338  -3669       N  
ATOM   1716  N   PHE A 223     -19.057  25.554  41.142  1.00 59.54           N  
ANISOU 1716  N   PHE A 223     6664   7012   8949    682     27  -3258       N  
ATOM   1717  CA  PHE A 223     -20.425  25.733  40.662  1.00 57.82           C  
ANISOU 1717  CA  PHE A 223     6369   6805   8792    754     65  -3266       C  
ATOM   1718  C   PHE A 223     -21.083  24.405  40.253  1.00 59.30           C  
ANISOU 1718  C   PHE A 223     6535   7145   8849    722    193  -3169       C  
ATOM   1719  O   PHE A 223     -20.422  23.401  39.975  1.00 58.50           O  
ANISOU 1719  O   PHE A 223     6486   7084   8658    646    235  -3062       O  
ATOM   1720  CB  PHE A 223     -20.448  26.666  39.459  1.00 57.44           C  
ANISOU 1720  CB  PHE A 223     6316   6512   8996    790    -44  -3193       C  
ATOM   1721  CG  PHE A 223     -19.803  27.994  39.704  1.00 59.94           C  
ANISOU 1721  CG  PHE A 223     6661   6654   9460    810   -177  -3264       C  
ATOM   1722  CD1 PHE A 223     -18.567  28.303  39.160  1.00 59.87           C  
ANISOU 1722  CD1 PHE A 223     6717   6471   9560    737   -264  -3170       C  
ATOM   1723  CD2 PHE A 223     -20.414  28.920  40.534  1.00 62.32           C  
ANISOU 1723  CD2 PHE A 223     6922   6974   9785    894   -213  -3432       C  
ATOM   1724  CE1 PHE A 223     -17.970  29.540  39.408  1.00 62.30           C  
ANISOU 1724  CE1 PHE A 223     7051   6619  10001    743   -387  -3233       C  
ATOM   1725  CE2 PHE A 223     -19.822  30.152  40.788  1.00 64.66           C  
ANISOU 1725  CE2 PHE A 223     7246   7105  10215    912   -339  -3503       C  
ATOM   1726  CZ  PHE A 223     -18.601  30.461  40.223  1.00 65.56           C  
ANISOU 1726  CZ  PHE A 223     7429   7042  10439    833   -426  -3399       C  
ATOM   1727  N   THR A 224     -22.410  24.432  40.176  1.00 55.92           N  
ANISOU 1727  N   THR A 224     6026   6798   8423    780    247  -3209       N  
ATOM   1728  CA  THR A 224     -23.210  23.300  39.738  1.00 54.26           C  
ANISOU 1728  CA  THR A 224     5779   6726   8113    752    362  -3123       C  
ATOM   1729  C   THR A 224     -24.278  23.807  38.784  1.00 53.19           C  
ANISOU 1729  C   THR A 224     5562   6502   8144    829    329  -3103       C  
ATOM   1730  O   THR A 224     -24.478  25.014  38.630  1.00 57.53           O  
ANISOU 1730  O   THR A 224     6089   6908   8863    907    224  -3171       O  
ATOM   1731  CB  THR A 224     -23.852  22.572  40.924  1.00 53.73           C  
ANISOU 1731  CB  THR A 224     5686   6921   7809    720    488  -3206       C  
ATOM   1732  OG1 THR A 224     -24.221  21.247  40.525  1.00 54.63           O  
ANISOU 1732  OG1 THR A 224     5799   7162   7796    652    598  -3087       O  
ATOM   1733  CG2 THR A 224     -25.092  23.323  41.406  1.00 56.14           C  
ANISOU 1733  CG2 THR A 224     5888   7292   8151    803    498  -3351       C  
ATOM   1734  N   THR A 225     -24.984  22.862  38.168  1.00 68.64           N  
ANISOU 1734  N   THR A 225     7480   8552  10049    805    414  -3010       N  
ATOM   1735  CA  THR A 225     -25.903  23.151  37.086  1.00 67.15           C  
ANISOU 1735  CA  THR A 225     7224   8277  10012    868    377  -2959       C  
ATOM   1736  C   THR A 225     -27.132  22.266  37.227  1.00 66.91           C  
ANISOU 1736  C   THR A 225     7106   8459   9856    852    499  -2966       C  
ATOM   1737  O   THR A 225     -27.239  21.451  38.149  1.00 66.75           O  
ANISOU 1737  O   THR A 225     7087   8642   9632    783    613  -3000       O  
ATOM   1738  CB  THR A 225     -25.232  22.924  35.730  1.00 66.02           C  
ANISOU 1738  CB  THR A 225     7138   7958   9987    842    322  -2782       C  
ATOM   1739  OG1 THR A 225     -26.100  23.386  34.693  1.00 67.74           O  
ANISOU 1739  OG1 THR A 225     7302   8072  10365    914    258  -2737       O  
ATOM   1740  CG2 THR A 225     -24.951  21.439  35.520  1.00 62.67           C  
ANISOU 1740  CG2 THR A 225     6747   7667   9397    740    430  -2645       C  
ATOM   1741  N   THR A 226     -28.065  22.441  36.299  1.00 52.23           N  
ANISOU 1741  N   THR A 226     5176   6550   8120    908    467  -2929       N  
ATOM   1742  CA  THR A 226     -29.227  21.581  36.152  1.00 50.80           C  
ANISOU 1742  CA  THR A 226     4906   6544   7853    885    568  -2909       C  
ATOM   1743  C   THR A 226     -29.119  20.794  34.852  1.00 49.34           C  
ANISOU 1743  C   THR A 226     4740   6296   7711    850    570  -2728       C  
ATOM   1744  O   THR A 226     -28.333  21.128  33.960  1.00 48.36           O  
ANISOU 1744  O   THR A 226     4683   5976   7717    867    479  -2628       O  
ATOM   1745  CB  THR A 226     -30.531  22.390  36.165  1.00 54.16           C  
ANISOU 1745  CB  THR A 226     5213   6984   8381    985    526  -3032       C  
ATOM   1746  OG1 THR A 226     -30.517  23.355  35.104  1.00 54.87           O  
ANISOU 1746  OG1 THR A 226     5312   6839   8696   1078    375  -2992       O  
ATOM   1747  CG2 THR A 226     -30.709  23.105  37.496  1.00 56.46           C  
ANISOU 1747  CG2 THR A 226     5473   7359   8619   1020    535  -3223       C  
ATOM   1748  N   LEU A 227     -29.928  19.737  34.754  1.00 48.94           N  
ANISOU 1748  N   LEU A 227     4630   6417   7547    793    676  -2682       N  
ATOM   1749  CA  LEU A 227     -29.929  18.927  33.541  1.00 47.78           C  
ANISOU 1749  CA  LEU A 227     4491   6231   7432    758    683  -2516       C  
ATOM   1750  C   LEU A 227     -30.425  19.729  32.347  1.00 49.10           C  
ANISOU 1750  C   LEU A 227     4617   6222   7816    861    556  -2480       C  
ATOM   1751  O   LEU A 227     -29.925  19.564  31.227  1.00 47.04           O  
ANISOU 1751  O   LEU A 227     4420   5826   7625    844    491  -2312       O  
ATOM   1752  CB  LEU A 227     -30.785  17.677  33.739  1.00 48.72           C  
ANISOU 1752  CB  LEU A 227     4551   6572   7388    668    816  -2482       C  
ATOM   1753  CG  LEU A 227     -30.410  16.466  32.880  1.00 48.35           C  
ANISOU 1753  CG  LEU A 227     4578   6526   7266    563    838  -2261       C  
ATOM   1754  CD1 LEU A 227     -28.904  16.253  32.877  1.00 46.49           C  
ANISOU 1754  CD1 LEU A 227     4505   6191   6969    496    794  -2126       C  
ATOM   1755  CD2 LEU A 227     -31.130  15.222  33.372  1.00 46.12           C  
ANISOU 1755  CD2 LEU A 227     4254   6469   6800    453    978  -2250       C  
ATOM   1756  N   ASN A 228     -31.407  20.605  32.563  1.00 53.00           N  
ANISOU 1756  N   ASN A 228     5026   6717   8394    950    502  -2606       N  
ATOM   1757  CA  ASN A 228     -31.884  21.454  31.479  1.00 53.35           C  
ANISOU 1757  CA  ASN A 228     5045   6585   8642   1054    361  -2576       C  
ATOM   1758  C   ASN A 228     -30.797  22.424  31.034  1.00 53.81           C  
ANISOU 1758  C   ASN A 228     5213   6390   8844   1094    228  -2526       C  
ATOM   1759  O   ASN A 228     -30.358  22.392  29.879  1.00 54.80           O  
ANISOU 1759  O   ASN A 228     5397   6360   9065   1094    156  -2375       O  
ATOM   1760  CB  ASN A 228     -33.143  22.206  31.916  1.00 57.46           C  
ANISOU 1760  CB  ASN A 228     5451   7166   9216   1144    329  -2741       C  
ATOM   1761  CG  ASN A 228     -34.415  21.521  31.461  1.00 55.69           C  
ANISOU 1761  CG  ASN A 228     5113   7079   8967   1140    376  -2728       C  
ATOM   1762  OD1 ASN A 228     -34.445  20.870  30.417  1.00 57.89           O  
ANISOU 1762  OD1 ASN A 228     5402   7324   9268   1113    366  -2584       O  
ATOM   1763  ND2 ASN A 228     -35.475  21.666  32.242  1.00 56.61           N  
ANISOU 1763  ND2 ASN A 228     5116   7354   9040   1163    427  -2884       N  
ATOM   1764  N   ASP A 229     -30.313  23.261  31.959  1.00 51.91           N  
ANISOU 1764  N   ASP A 229     5004   6108   8610   1116    198  -2645       N  
ATOM   1765  CA  ASP A 229     -29.356  24.305  31.602  1.00 51.42           C  
ANISOU 1765  CA  ASP A 229     5041   5802   8695   1145     62  -2608       C  
ATOM   1766  C   ASP A 229     -28.097  23.735  30.958  1.00 50.98           C  
ANISOU 1766  C   ASP A 229     5092   5648   8631   1059     70  -2440       C  
ATOM   1767  O   ASP A 229     -27.518  24.368  30.068  1.00 51.00           O  
ANISOU 1767  O   ASP A 229     5172   5430   8777   1069    -48  -2334       O  
ATOM   1768  CB  ASP A 229     -28.988  25.126  32.838  1.00 53.35           C  
ANISOU 1768  CB  ASP A 229     5298   6052   8922   1164     46  -2770       C  
ATOM   1769  CG  ASP A 229     -30.147  25.959  33.350  1.00 57.74           C  
ANISOU 1769  CG  ASP A 229     5754   6653   9530   1267      6  -2940       C  
ATOM   1770  OD1 ASP A 229     -31.059  26.266  32.553  1.00 58.09           O  
ANISOU 1770  OD1 ASP A 229     5745   6641   9684   1340    -65  -2922       O  
ATOM   1771  OD2 ASP A 229     -30.147  26.307  34.550  1.00 62.47           O  
ANISOU 1771  OD2 ASP A 229     6330   7347  10061   1277     41  -3097       O  
ATOM   1772  N   PHE A 230     -27.657  22.549  31.386  1.00 49.36           N  
ANISOU 1772  N   PHE A 230     4900   5604   8250    963    201  -2402       N  
ATOM   1773  CA  PHE A 230     -26.495  21.936  30.752  1.00 48.08           C  
ANISOU 1773  CA  PHE A 230     4860   5391   8016    840    195  -2175       C  
ATOM   1774  C   PHE A 230     -26.816  21.484  29.333  1.00 45.69           C  
ANISOU 1774  C   PHE A 230     4573   5039   7748    818    160  -1978       C  
ATOM   1775  O   PHE A 230     -26.021  21.702  28.412  1.00 45.03           O  
ANISOU 1775  O   PHE A 230     4581   4806   7722    773     84  -1813       O  
ATOM   1776  CB  PHE A 230     -25.988  20.756  31.581  1.00 46.08           C  
ANISOU 1776  CB  PHE A 230     4638   5334   7537    731    321  -2152       C  
ATOM   1777  CG  PHE A 230     -24.909  19.961  30.898  1.00 43.93           C  
ANISOU 1777  CG  PHE A 230     4471   5035   7185    616    321  -1930       C  
ATOM   1778  CD1 PHE A 230     -23.592  20.391  30.924  1.00 44.87           C  
ANISOU 1778  CD1 PHE A 230     4676   5039   7335    572    262  -1882       C  
ATOM   1779  CD2 PHE A 230     -25.211  18.788  30.223  1.00 43.58           C  
ANISOU 1779  CD2 PHE A 230     4432   5084   7040    555    378  -1781       C  
ATOM   1780  CE1 PHE A 230     -22.597  19.665  30.293  1.00 43.13           C  
ANISOU 1780  CE1 PHE A 230     4535   4808   7044    473    265  -1696       C  
ATOM   1781  CE2 PHE A 230     -24.222  18.060  29.590  1.00 41.48           C  
ANISOU 1781  CE2 PHE A 230     4258   4798   6705    462    375  -1596       C  
ATOM   1782  CZ  PHE A 230     -22.913  18.499  29.626  1.00 39.21           C  
ANISOU 1782  CZ  PHE A 230     4044   4406   6446    425    321  -1557       C  
ATOM   1783  N   ASN A 231     -27.974  20.845  29.140  1.00 47.31           N  
ANISOU 1783  N   ASN A 231     4687   5376   7913    843    218  -1994       N  
ATOM   1784  CA  ASN A 231     -28.351  20.372  27.813  1.00 47.47           C  
ANISOU 1784  CA  ASN A 231     4718   5362   7957    825    182  -1819       C  
ATOM   1785  C   ASN A 231     -28.533  21.515  26.823  1.00 48.82           C  
ANISOU 1785  C   ASN A 231     4908   5310   8331    915     26  -1782       C  
ATOM   1786  O   ASN A 231     -28.462  21.286  25.611  1.00 47.84           O  
ANISOU 1786  O   ASN A 231     4838   5113   8226    884    -29  -1602       O  
ATOM   1787  CB  ASN A 231     -29.630  19.537  27.895  1.00 46.11           C  
ANISOU 1787  CB  ASN A 231     4430   5377   7715    836    268  -1871       C  
ATOM   1788  CG  ASN A 231     -29.372  18.130  28.395  1.00 47.67           C  
ANISOU 1788  CG  ASN A 231     4651   5764   7696    709    404  -1809       C  
ATOM   1789  OD1 ASN A 231     -28.244  17.638  28.346  1.00 45.40           O  
ANISOU 1789  OD1 ASN A 231     4477   5456   7318    618    417  -1684       O  
ATOM   1790  ND2 ASN A 231     -30.419  17.472  28.879  1.00 46.03           N  
ANISOU 1790  ND2 ASN A 231     4338   5742   7409    700    502  -1897       N  
ATOM   1791  N   LEU A 232     -28.770  22.736  27.308  1.00 55.08           N  
ANISOU 1791  N   LEU A 232     5665   5990   9272   1025    -53  -1948       N  
ATOM   1792  CA  LEU A 232     -28.751  23.891  26.418  1.00 55.81           C  
ANISOU 1792  CA  LEU A 232     5809   5836   9561   1099   -220  -1897       C  
ATOM   1793  C   LEU A 232     -27.337  24.175  25.922  1.00 56.03           C  
ANISOU 1793  C   LEU A 232     5986   5709   9594    995   -273  -1726       C  
ATOM   1794  O   LEU A 232     -27.139  24.493  24.744  1.00 56.67           O  
ANISOU 1794  O   LEU A 232     6145   5638   9748    977   -371  -1557       O  
ATOM   1795  CB  LEU A 232     -29.338  25.116  27.124  1.00 60.89           C  
ANISOU 1795  CB  LEU A 232     6396   6411  10328   1222   -300  -2102       C  
ATOM   1796  CG  LEU A 232     -30.858  25.313  27.044  1.00 63.71           C  
ANISOU 1796  CG  LEU A 232     6636   6854  10716   1321   -331  -2196       C  
ATOM   1797  CD1 LEU A 232     -31.592  24.576  28.157  1.00 63.21           C  
ANISOU 1797  CD1 LEU A 232     6449   7063  10504   1309   -177  -2352       C  
ATOM   1798  CD2 LEU A 232     -31.213  26.800  27.047  1.00 67.54           C  
ANISOU 1798  CD2 LEU A 232     7138   7173  11352   1420   -491  -2276       C  
ATOM   1799  N   VAL A 233     -26.342  24.059  26.805  1.00 50.80           N  
ANISOU 1799  N   VAL A 233     5363   5090   8850    921   -208  -1766       N  
ATOM   1800  CA  VAL A 233     -24.952  24.213  26.385  1.00 50.96           C  
ANISOU 1800  CA  VAL A 233     5503   4995   8863    808   -241  -1611       C  
ATOM   1801  C   VAL A 233     -24.519  23.028  25.530  1.00 49.35           C  
ANISOU 1801  C   VAL A 233     5346   4887   8517    695   -173  -1399       C  
ATOM   1802  O   VAL A 233     -23.742  23.180  24.580  1.00 48.29           O  
ANISOU 1802  O   VAL A 233     5300   4641   8406    620   -224  -1226       O  
ATOM   1803  CB  VAL A 233     -24.040  24.389  27.614  1.00 51.40           C  
ANISOU 1803  CB  VAL A 233     5574   5084   8872    768   -198  -1732       C  
ATOM   1804  CG1 VAL A 233     -22.575  24.453  27.197  1.00 49.31           C  
ANISOU 1804  CG1 VAL A 233     5412   4728   8595    642   -222  -1578       C  
ATOM   1805  CG2 VAL A 233     -24.431  25.636  28.394  1.00 51.82           C  
ANISOU 1805  CG2 VAL A 233     5589   5026   9076    884   -278  -1950       C  
ATOM   1806  N   ALA A 234     -25.022  21.833  25.848  1.00 47.17           N  
ANISOU 1806  N   ALA A 234     5012   4818   8091    678    -58  -1414       N  
ATOM   1807  CA  ALA A 234     -24.587  20.627  25.150  1.00 45.06           C  
ANISOU 1807  CA  ALA A 234     4790   4646   7683    576      6  -1234       C  
ATOM   1808  C   ALA A 234     -24.934  20.686  23.667  1.00 45.06           C  
ANISOU 1808  C   ALA A 234     4824   4555   7742    579    -68  -1072       C  
ATOM   1809  O   ALA A 234     -24.098  20.375  22.810  1.00 45.79           O  
ANISOU 1809  O   ALA A 234     4997   4612   7789    492    -75   -901       O  
ATOM   1810  CB  ALA A 234     -25.211  19.393  25.805  1.00 43.09           C  
ANISOU 1810  CB  ALA A 234     4476   4618   7277    560    129  -1291       C  
ATOM   1811  N   MET A 235     -26.167  21.089  23.341  1.00 47.57           N  
ANISOU 1811  N   MET A 235     5078   4840   8157    682   -128  -1128       N  
ATOM   1812  CA  MET A 235     -26.577  21.126  21.940  1.00 50.87           C  
ANISOU 1812  CA  MET A 235     5531   5177   8620    693   -211   -976       C  
ATOM   1813  C   MET A 235     -25.871  22.240  21.173  1.00 48.92           C  
ANISOU 1813  C   MET A 235     5389   4705   8493    677   -335   -868       C  
ATOM   1814  O   MET A 235     -25.735  22.156  19.948  1.00 50.05           O  
ANISOU 1814  O   MET A 235     5604   4787   8627    636   -387   -692       O  
ATOM   1815  CB  MET A 235     -28.095  21.276  21.833  1.00 53.10           C  
ANISOU 1815  CB  MET A 235     5708   5486   8982    815   -255  -1077       C  
ATOM   1816  CG  MET A 235     -28.625  21.220  20.401  1.00 58.69           C  
ANISOU 1816  CG  MET A 235     6447   6128   9724    833   -348   -927       C  
ATOM   1817  SD  MET A 235     -30.236  21.993  20.174  1.00 75.05           S  
ANISOU 1817  SD  MET A 235     8409   8137  11968   1009   -473  -1054       S  
ATOM   1818  CE  MET A 235     -31.099  21.380  21.617  1.00 61.88           C  
ANISOU 1818  CE  MET A 235     6567   6701  10244   1051   -330  -1295       C  
ATOM   1819  N   LYS A 236     -25.412  23.285  21.863  1.00 52.07           N  
ANISOU 1819  N   LYS A 236     5806   4979   9000    702   -385   -967       N  
ATOM   1820  CA  LYS A 236     -24.670  24.337  21.175  1.00 51.42           C  
ANISOU 1820  CA  LYS A 236     5832   4675   9029    663   -501   -855       C  
ATOM   1821  C   LYS A 236     -23.345  23.812  20.637  1.00 52.51           C  
ANISOU 1821  C   LYS A 236     6056   4840   9054    506   -441   -678       C  
ATOM   1822  O   LYS A 236     -22.937  24.164  19.525  1.00 50.62           O  
ANISOU 1822  O   LYS A 236     5907   4485   8840    444   -508   -505       O  
ATOM   1823  CB  LYS A 236     -24.435  25.528  22.107  1.00 53.30           C  
ANISOU 1823  CB  LYS A 236     6069   4774   9408    716   -567  -1013       C  
ATOM   1824  CG  LYS A 236     -24.228  26.840  21.362  1.00 59.19           C  
ANISOU 1824  CG  LYS A 236     6915   5248  10324    724   -732   -930       C  
ATOM   1825  CD  LYS A 236     -23.456  27.859  22.186  1.00 61.52           C  
ANISOU 1825  CD  LYS A 236     7244   5402  10728    708   -782  -1035       C  
ATOM   1826  CE  LYS A 236     -22.483  28.645  21.314  1.00 60.33           C  
ANISOU 1826  CE  LYS A 236     7230   5041  10651    592   -876   -851       C  
ATOM   1827  NZ  LYS A 236     -21.671  27.755  20.436  1.00 61.32           N  
ANISOU 1827  NZ  LYS A 236     7404   5272  10622    440   -787   -636       N  
ATOM   1828  N   TYR A 237     -22.664  22.961  21.404  1.00 47.71           N  
ANISOU 1828  N   TYR A 237     5420   4390   8317    441   -319   -720       N  
ATOM   1829  CA  TYR A 237     -21.383  22.393  21.005  1.00 45.62           C  
ANISOU 1829  CA  TYR A 237     5214   4174   7946    305   -257   -582       C  
ATOM   1830  C   TYR A 237     -21.522  20.989  20.428  1.00 42.67           C  
ANISOU 1830  C   TYR A 237     4830   3971   7410    267   -169   -483       C  
ATOM   1831  O   TYR A 237     -20.542  20.236  20.407  1.00 41.87           O  
ANISOU 1831  O   TYR A 237     4750   3964   7198    177    -94   -421       O  
ATOM   1832  CB  TYR A 237     -20.419  22.385  22.191  1.00 44.63           C  
ANISOU 1832  CB  TYR A 237     5072   4095   7790    261   -201   -690       C  
ATOM   1833  CG  TYR A 237     -20.021  23.767  22.651  1.00 47.94           C  
ANISOU 1833  CG  TYR A 237     5517   4332   8367    271   -292   -770       C  
ATOM   1834  CD1 TYR A 237     -19.014  24.470  22.004  1.00 49.90           C  
ANISOU 1834  CD1 TYR A 237     5842   4437   8681    170   -349   -648       C  
ATOM   1835  CD2 TYR A 237     -20.652  24.370  23.730  1.00 50.46           C  
ANISOU 1835  CD2 TYR A 237     5783   4622   8767    376   -322   -971       C  
ATOM   1836  CE1 TYR A 237     -18.645  25.734  22.419  1.00 52.58           C  
ANISOU 1836  CE1 TYR A 237     6212   4595   9172    168   -441   -719       C  
ATOM   1837  CE2 TYR A 237     -20.290  25.634  24.154  1.00 52.60           C  
ANISOU 1837  CE2 TYR A 237     6083   4716   9189    390   -416  -1055       C  
ATOM   1838  CZ  TYR A 237     -19.286  26.311  23.495  1.00 52.80           C  
ANISOU 1838  CZ  TYR A 237     6192   4585   9286    283   -480   -925       C  
ATOM   1839  OH  TYR A 237     -18.924  27.570  23.915  1.00 55.36           O  
ANISOU 1839  OH  TYR A 237     6550   4717   9766    286   -582  -1007       O  
ATOM   1840  N   ASN A 238     -22.719  20.628  19.959  1.00 46.77           N  
ANISOU 1840  N   ASN A 238     5315   4532   7924    338   -185   -477       N  
ATOM   1841  CA  ASN A 238     -22.979  19.319  19.358  1.00 46.27           C  
ANISOU 1841  CA  ASN A 238     5244   4617   7719    307   -117   -390       C  
ATOM   1842  C   ASN A 238     -22.635  18.187  20.321  1.00 41.95           C  
ANISOU 1842  C   ASN A 238     4659   4245   7037    272      3   -461       C  
ATOM   1843  O   ASN A 238     -22.093  17.152  19.929  1.00 43.02           O  
ANISOU 1843  O   ASN A 238     4822   4478   7047    204     64   -372       O  
ATOM   1844  CB  ASN A 238     -22.234  19.159  18.032  1.00 46.25           C  
ANISOU 1844  CB  ASN A 238     5328   4578   7666    218   -134   -194       C  
ATOM   1845  CG  ASN A 238     -22.921  19.882  16.892  1.00 52.89           C  
ANISOU 1845  CG  ASN A 238     6214   5289   8594    257   -250    -98       C  
ATOM   1846  OD1 ASN A 238     -24.147  20.003  16.870  1.00 54.84           O  
ANISOU 1846  OD1 ASN A 238     6412   5527   8900    356   -302   -159       O  
ATOM   1847  ND2 ASN A 238     -22.137  20.370  15.939  1.00 53.97           N  
ANISOU 1847  ND2 ASN A 238     6442   5328   8735    175   -293     54       N  
ATOM   1848  N   TYR A 239     -22.935  18.399  21.596  1.00 37.56           N  
ANISOU 1848  N   TYR A 239     4044   3726   6503    321     31   -627       N  
ATOM   1849  CA  TYR A 239     -22.889  17.333  22.578  1.00 34.87           C  
ANISOU 1849  CA  TYR A 239     3669   3554   6028    298    135   -702       C  
ATOM   1850  C   TYR A 239     -24.268  16.710  22.690  1.00 38.09           C  
ANISOU 1850  C   TYR A 239     4002   4069   6400    349    169   -759       C  
ATOM   1851  O   TYR A 239     -25.293  17.385  22.569  1.00 39.98           O  
ANISOU 1851  O   TYR A 239     4184   4258   6747    433    116   -826       O  
ATOM   1852  CB  TYR A 239     -22.438  17.848  23.945  1.00 35.41           C  
ANISOU 1852  CB  TYR A 239     3718   3624   6113    310    153   -852       C  
ATOM   1853  CG  TYR A 239     -20.942  17.847  24.142  1.00 35.07           C  
ANISOU 1853  CG  TYR A 239     3732   3559   6034    230    161   -808       C  
ATOM   1854  CD1 TYR A 239     -20.102  18.435  23.208  1.00 38.95           C  
ANISOU 1854  CD1 TYR A 239     4278   3926   6593    179    104   -688       C  
ATOM   1855  CD2 TYR A 239     -20.370  17.270  25.269  1.00 36.41           C  
ANISOU 1855  CD2 TYR A 239     3899   3835   6098    202    223   -887       C  
ATOM   1856  CE1 TYR A 239     -18.734  18.443  23.384  1.00 38.31           C  
ANISOU 1856  CE1 TYR A 239     4230   3839   6486    102    115   -659       C  
ATOM   1857  CE2 TYR A 239     -19.001  17.274  25.455  1.00 36.83           C  
ANISOU 1857  CE2 TYR A 239     3992   3873   6128    137    220   -857       C  
ATOM   1858  CZ  TYR A 239     -18.188  17.863  24.509  1.00 35.09           C  
ANISOU 1858  CZ  TYR A 239     3808   3538   5986     87    169   -749       C  
ATOM   1859  OH  TYR A 239     -16.825  17.871  24.687  1.00 35.51           O  
ANISOU 1859  OH  TYR A 239     3882   3588   6021     17    169   -729       O  
ATOM   1860  N   GLU A 240     -24.275  15.372  22.640  1.00 51.14           N  
ANISOU 1860  N   GLU A 240     5664   5857   7911    293    244   -705       N  
ATOM   1861  CA  GLU A 240     -25.508  14.542  22.715  1.00 50.55           C  
ANISOU 1861  CA  GLU A 240     5523   5905   7780    310    291   -741       C  
ATOM   1862  C   GLU A 240     -26.079  14.809  24.097  1.00 49.79           C  
ANISOU 1862  C   GLU A 240     5349   5882   7685    349    342   -921       C  
ATOM   1863  O   GLU A 240     -25.277  14.804  25.048  1.00 49.11           O  
ANISOU 1863  O   GLU A 240     5294   5823   7543    318    380   -974       O  
ATOM   1864  CB  GLU A 240     -25.105  13.069  22.687  1.00 52.68           C  
ANISOU 1864  CB  GLU A 240     5839   6291   7888    226    362   -660       C  
ATOM   1865  CG  GLU A 240     -25.589  12.311  21.470  1.00 50.90           C  
ANISOU 1865  CG  GLU A 240     5625   6083   7630    207    344   -544       C  
ATOM   1866  CD  GLU A 240     -25.697  10.824  21.749  1.00 54.48           C  
ANISOU 1866  CD  GLU A 240     6095   6667   7937    141    417   -520       C  
ATOM   1867  OE1 GLU A 240     -24.896  10.325  22.565  1.00 54.51           O  
ANISOU 1867  OE1 GLU A 240     6143   6717   7851     96    465   -535       O  
ATOM   1868  OE2 GLU A 240     -26.587  10.176  21.166  1.00 56.84           O  
ANISOU 1868  OE2 GLU A 240     6365   7015   8215    134    416   -487       O  
ATOM   1869  N   PRO A 241     -27.531  14.997  24.432  1.00 35.60           N  
ANISOU 1869  N   PRO A 241     3436   4152   5939    417    356  -1048       N  
ATOM   1870  CA  PRO A 241     -28.215  15.351  25.674  1.00 35.98           C  
ANISOU 1870  CA  PRO A 241     3391   4286   5994    464    410  -1239       C  
ATOM   1871  C   PRO A 241     -27.946  14.351  26.795  1.00 37.16           C  
ANISOU 1871  C   PRO A 241     3558   4595   5968    378    526  -1275       C  
ATOM   1872  O   PRO A 241     -27.840  13.142  26.572  1.00 39.31           O  
ANISOU 1872  O   PRO A 241     3873   4948   6116    294    574  -1171       O  
ATOM   1873  CB  PRO A 241     -29.697  15.358  25.291  1.00 39.03           C  
ANISOU 1873  CB  PRO A 241     3657   4725   6447    525    400  -1298       C  
ATOM   1874  CG  PRO A 241     -29.717  15.397  23.788  1.00 35.05           C  
ANISOU 1874  CG  PRO A 241     3198   4108   6012    538    303  -1143       C  
ATOM   1875  CD  PRO A 241     -28.495  14.659  23.361  1.00 38.34           C  
ANISOU 1875  CD  PRO A 241     3742   4507   6319    438    320   -980       C  
ATOM   1876  N   LEU A 242     -27.853  14.879  28.011  1.00 38.72           N  
ANISOU 1876  N   LEU A 242     3727   4833   6154    403    562  -1427       N  
ATOM   1877  CA  LEU A 242     -27.658  14.063  29.201  1.00 39.98           C  
ANISOU 1877  CA  LEU A 242     3906   5145   6139    328    666  -1477       C  
ATOM   1878  C   LEU A 242     -29.007  13.761  29.840  1.00 41.90           C  
ANISOU 1878  C   LEU A 242     4031   5554   6334    330    756  -1603       C  
ATOM   1879  O   LEU A 242     -29.826  14.665  30.037  1.00 43.15           O  
ANISOU 1879  O   LEU A 242     4079   5712   6606    424    744  -1752       O  
ATOM   1880  CB  LEU A 242     -26.745  14.773  30.202  1.00 39.39           C  
ANISOU 1880  CB  LEU A 242     3874   5035   6057    344    655  -1574       C  
ATOM   1881  CG  LEU A 242     -25.952  13.859  31.138  1.00 40.09           C  
ANISOU 1881  CG  LEU A 242     4048   5228   5958    252    719  -1550       C  
ATOM   1882  CD1 LEU A 242     -24.872  13.111  30.370  1.00 40.96           C  
ANISOU 1882  CD1 LEU A 242     4267   5273   6023    188    680  -1363       C  
ATOM   1883  CD2 LEU A 242     -25.350  14.656  32.281  1.00 41.00           C  
ANISOU 1883  CD2 LEU A 242     4176   5336   6066    282    712  -1693       C  
ATOM   1884  N   THR A 243     -29.233  12.492  30.158  1.00 43.72           N  
ANISOU 1884  N   THR A 243     4284   5926   6403    225    845  -1546       N  
ATOM   1885  CA  THR A 243     -30.474  12.036  30.765  1.00 43.41           C  
ANISOU 1885  CA  THR A 243     4135   6066   6293    192    948  -1646       C  
ATOM   1886  C   THR A 243     -30.226  11.611  32.207  1.00 45.94           C  
ANISOU 1886  C   THR A 243     4492   6528   6434    117   1049  -1721       C  
ATOM   1887  O   THR A 243     -29.086  11.529  32.672  1.00 42.87           O  
ANISOU 1887  O   THR A 243     4222   6097   5970     89   1028  -1679       O  
ATOM   1888  CB  THR A 243     -31.077  10.875  29.965  1.00 46.56           C  
ANISOU 1888  CB  THR A 243     4529   6518   6645    112    970  -1516       C  
ATOM   1889  OG1 THR A 243     -30.264   9.706  30.128  1.00 44.47           O  
ANISOU 1889  OG1 THR A 243     4403   6274   6221     -3    996  -1378       O  
ATOM   1890  CG2 THR A 243     -31.151  11.229  28.487  1.00 42.66           C  
ANISOU 1890  CG2 THR A 243     4027   5878   6304    180    860  -1421       C  
ATOM   1891  N   GLN A 244     -31.323  11.349  32.921  1.00 44.53           N  
ANISOU 1891  N   GLN A 244     4208   6529   6183     80   1157  -1836       N  
ATOM   1892  CA  GLN A 244     -31.209  10.831  34.279  1.00 47.33           C  
ANISOU 1892  CA  GLN A 244     4604   7043   6338    -12   1264  -1894       C  
ATOM   1893  C   GLN A 244     -30.590   9.439  34.289  1.00 45.40           C  
ANISOU 1893  C   GLN A 244     4510   6817   5923   -151   1281  -1708       C  
ATOM   1894  O   GLN A 244     -29.890   9.080  35.243  1.00 45.69           O  
ANISOU 1894  O   GLN A 244     4653   6903   5805   -212   1309  -1701       O  
ATOM   1895  CB  GLN A 244     -32.582  10.824  34.955  1.00 50.18           C  
ANISOU 1895  CB  GLN A 244     4806   7606   6653    -35   1387  -2054       C  
ATOM   1896  CG  GLN A 244     -32.589  10.306  36.386  1.00 52.91           C  
ANISOU 1896  CG  GLN A 244     5207   8124   6772   -146   1492  -2096       C  
ATOM   1897  CD  GLN A 244     -31.696  11.108  37.311  1.00 50.40           C  
ANISOU 1897  CD  GLN A 244     4954   7775   6420    -85   1465  -2200       C  
ATOM   1898  OE1 GLN A 244     -31.599  12.330  37.198  1.00 53.33           O  
ANISOU 1898  OE1 GLN A 244     5271   8044   6950     50   1388  -2312       O  
ATOM   1899  NE2 GLN A 244     -31.036  10.419  38.236  1.00 51.65           N  
ANISOU 1899  NE2 GLN A 244     5238   8015   6370   -188   1517  -2159       N  
ATOM   1900  N   ASP A 245     -30.833   8.648  33.239  1.00 41.41           N  
ANISOU 1900  N   ASP A 245     4019   6268   5445   -196   1253  -1562       N  
ATOM   1901  CA  ASP A 245     -30.151   7.364  33.105  1.00 40.83           C  
ANISOU 1901  CA  ASP A 245     4100   6176   5239   -307   1242  -1385       C  
ATOM   1902  C   ASP A 245     -28.639   7.549  33.079  1.00 37.23           C  
ANISOU 1902  C   ASP A 245     3780   5586   4781   -268   1152  -1316       C  
ATOM   1903  O   ASP A 245     -27.903   6.800  33.732  1.00 36.41           O  
ANISOU 1903  O   ASP A 245     3803   5506   4526   -341   1158  -1252       O  
ATOM   1904  CB  ASP A 245     -30.621   6.646  31.840  1.00 38.71           C  
ANISOU 1904  CB  ASP A 245     3818   5859   5030   -337   1207  -1257       C  
ATOM   1905  CG  ASP A 245     -32.036   6.116  31.960  1.00 44.97           C  
ANISOU 1905  CG  ASP A 245     4495   6804   5788   -417   1302  -1300       C  
ATOM   1906  OD1 ASP A 245     -32.571   6.092  33.087  1.00 47.20           O  
ANISOU 1906  OD1 ASP A 245     4728   7243   5963   -476   1409  -1407       O  
ATOM   1907  OD2 ASP A 245     -32.612   5.721  30.924  1.00 46.13           O  
ANISOU 1907  OD2 ASP A 245     4597   6921   6010   -426   1270  -1232       O  
ATOM   1908  N   HIS A 246     -28.158   8.546  32.331  1.00 37.87           N  
ANISOU 1908  N   HIS A 246     3836   5524   5030   -157   1063  -1327       N  
ATOM   1909  CA  HIS A 246     -26.725   8.819  32.285  1.00 35.91           C  
ANISOU 1909  CA  HIS A 246     3694   5156   4794   -125    982  -1274       C  
ATOM   1910  C   HIS A 246     -26.190   9.194  33.661  1.00 37.24           C  
ANISOU 1910  C   HIS A 246     3900   5384   4868   -126   1008  -1385       C  
ATOM   1911  O   HIS A 246     -25.062   8.835  34.017  1.00 36.45           O  
ANISOU 1911  O   HIS A 246     3912   5250   4687   -153    967  -1328       O  
ATOM   1912  CB  HIS A 246     -26.436   9.931  31.277  1.00 35.54           C  
ANISOU 1912  CB  HIS A 246     3602   4953   4946    -20    892  -1275       C  
ATOM   1913  CG  HIS A 246     -26.741   9.558  29.859  1.00 36.01           C  
ANISOU 1913  CG  HIS A 246     3652   4945   5085    -18    849  -1149       C  
ATOM   1914  ND1 HIS A 246     -27.200  10.469  28.932  1.00 38.21           N  
ANISOU 1914  ND1 HIS A 246     3854   5132   5533     66    792  -1165       N  
ATOM   1915  CD2 HIS A 246     -26.650   8.374  29.209  1.00 36.63           C  
ANISOU 1915  CD2 HIS A 246     3796   5032   5092    -86    846  -1010       C  
ATOM   1916  CE1 HIS A 246     -27.380   9.862  27.773  1.00 37.06           C  
ANISOU 1916  CE1 HIS A 246     3725   4949   5405     46    760  -1038       C  
ATOM   1917  NE2 HIS A 246     -27.054   8.590  27.914  1.00 37.71           N  
ANISOU 1917  NE2 HIS A 246     3889   5092   5346    -45    795   -948       N  
ATOM   1918  N   VAL A 247     -26.987   9.921  34.448  1.00 34.34           N  
ANISOU 1918  N   VAL A 247     3432   5108   4508    -93   1070  -1555       N  
ATOM   1919  CA  VAL A 247     -26.574  10.269  35.804  1.00 34.57           C  
ANISOU 1919  CA  VAL A 247     3494   5211   4429    -96   1100  -1676       C  
ATOM   1920  C   VAL A 247     -26.461   9.016  36.664  1.00 35.01           C  
ANISOU 1920  C   VAL A 247     3656   5397   4250   -223   1164  -1608       C  
ATOM   1921  O   VAL A 247     -25.495   8.849  37.419  1.00 36.30           O  
ANISOU 1921  O   VAL A 247     3928   5560   4304   -244   1133  -1600       O  
ATOM   1922  CB  VAL A 247     -27.553  11.290  36.413  1.00 36.03           C  
ANISOU 1922  CB  VAL A 247     3538   5480   4671    -28   1159  -1888       C  
ATOM   1923  CG1 VAL A 247     -27.200  11.569  37.866  1.00 37.95           C  
ANISOU 1923  CG1 VAL A 247     3819   5825   4776    -39   1201  -2023       C  
ATOM   1924  CG2 VAL A 247     -27.552  12.576  35.600  1.00 36.92           C  
ANISOU 1924  CG2 VAL A 247     3571   5433   5022    104   1069  -1949       C  
ATOM   1925  N   ASP A 248     -27.440   8.114  36.560  1.00 36.68           N  
ANISOU 1925  N   ASP A 248     3840   5715   4382   -312   1245  -1556       N  
ATOM   1926  CA  ASP A 248     -27.413   6.892  37.358  1.00 39.34           C  
ANISOU 1926  CA  ASP A 248     4290   6166   4493   -448   1302  -1478       C  
ATOM   1927  C   ASP A 248     -26.251   5.990  36.956  1.00 39.20           C  
ANISOU 1927  C   ASP A 248     4433   6033   4427   -480   1207  -1301       C  
ATOM   1928  O   ASP A 248     -25.657   5.319  37.809  1.00 37.67           O  
ANISOU 1928  O   ASP A 248     4370   5880   4061   -548   1200  -1256       O  
ATOM   1929  CB  ASP A 248     -28.742   6.149  37.224  1.00 41.62           C  
ANISOU 1929  CB  ASP A 248     4505   6580   4728   -547   1405  -1455       C  
ATOM   1930  CG  ASP A 248     -29.913   6.951  37.756  1.00 43.32           C  
ANISOU 1930  CG  ASP A 248     4548   6941   4970   -520   1511  -1648       C  
ATOM   1931  OD1 ASP A 248     -29.690   7.850  38.595  1.00 46.52           O  
ANISOU 1931  OD1 ASP A 248     4927   7387   5363   -456   1525  -1800       O  
ATOM   1932  OD2 ASP A 248     -31.058   6.683  37.335  1.00 45.50           O  
ANISOU 1932  OD2 ASP A 248     4709   7295   5284   -560   1577  -1659       O  
ATOM   1933  N   ILE A 249     -25.917   5.957  35.664  1.00 36.15           N  
ANISOU 1933  N   ILE A 249     4042   5508   4187   -429   1128  -1204       N  
ATOM   1934  CA  ILE A 249     -24.808   5.125  35.200  1.00 32.95           C  
ANISOU 1934  CA  ILE A 249     3771   4998   3749   -446   1038  -1054       C  
ATOM   1935  C   ILE A 249     -23.493   5.599  35.807  1.00 33.18           C  
ANISOU 1935  C   ILE A 249     3873   4974   3760   -393    966  -1090       C  
ATOM   1936  O   ILE A 249     -22.629   4.790  36.167  1.00 33.48           O  
ANISOU 1936  O   ILE A 249     4042   4996   3684   -430    913  -1010       O  
ATOM   1937  CB  ILE A 249     -24.754   5.117  33.660  1.00 33.56           C  
ANISOU 1937  CB  ILE A 249     3812   4953   3987   -396    978   -964       C  
ATOM   1938  CG1 ILE A 249     -25.988   4.423  33.082  1.00 35.34           C  
ANISOU 1938  CG1 ILE A 249     3984   5233   4211   -462   1035   -914       C  
ATOM   1939  CG2 ILE A 249     -23.493   4.427  33.166  1.00 35.08           C  
ANISOU 1939  CG2 ILE A 249     4124   5041   4162   -391    884   -840       C  
ATOM   1940  CD1 ILE A 249     -26.162   4.630  31.592  1.00 32.07           C  
ANISOU 1940  CD1 ILE A 249     3510   4718   3959   -403    982   -856       C  
ATOM   1941  N   LEU A 250     -23.326   6.914  35.944  1.00 34.35           N  
ANISOU 1941  N   LEU A 250     3939   5091   4023   -305    953  -1217       N  
ATOM   1942  CA  LEU A 250     -22.111   7.487  36.511  1.00 36.50           C  
ANISOU 1942  CA  LEU A 250     4262   5312   4296   -257    881  -1269       C  
ATOM   1943  C   LEU A 250     -22.049   7.377  38.029  1.00 39.27           C  
ANISOU 1943  C   LEU A 250     4674   5784   4462   -300    918  -1356       C  
ATOM   1944  O   LEU A 250     -21.078   7.855  38.625  1.00 42.36           O  
ANISOU 1944  O   LEU A 250     5107   6146   4841   -262    855  -1415       O  
ATOM   1945  CB  LEU A 250     -21.985   8.956  36.098  1.00 35.79           C  
ANISOU 1945  CB  LEU A 250     4069   5129   4402   -157    847  -1374       C  
ATOM   1946  CG  LEU A 250     -21.764   9.225  34.609  1.00 33.76           C  
ANISOU 1946  CG  LEU A 250     3772   4734   4323   -112    789  -1282       C  
ATOM   1947  CD1 LEU A 250     -22.197  10.637  34.250  1.00 33.86           C  
ANISOU 1947  CD1 LEU A 250     3673   4676   4517    -29    777  -1389       C  
ATOM   1948  CD2 LEU A 250     -20.308   8.996  34.234  1.00 30.05           C  
ANISOU 1948  CD2 LEU A 250     3380   4170   3869   -106    698  -1194       C  
ATOM   1949  N   GLY A 251     -23.055   6.771  38.657  1.00 38.30           N  
ANISOU 1949  N   GLY A 251     4556   5803   4194   -385   1017  -1367       N  
ATOM   1950  CA  GLY A 251     -23.115   6.615  40.093  1.00 39.35           C  
ANISOU 1950  CA  GLY A 251     4752   6073   4126   -442   1066  -1442       C  
ATOM   1951  C   GLY A 251     -21.846   6.093  40.744  1.00 41.10           C  
ANISOU 1951  C   GLY A 251     5131   6266   4221   -458    973  -1382       C  
ATOM   1952  O   GLY A 251     -21.342   6.680  41.707  1.00 41.55           O  
ANISOU 1952  O   GLY A 251     5212   6361   4213   -430    951  -1493       O  
ATOM   1953  N   PRO A 252     -21.316   4.967  40.252  1.00 39.13           N  
ANISOU 1953  N   PRO A 252     4990   5947   3931   -499    907  -1216       N  
ATOM   1954  CA  PRO A 252     -20.063   4.448  40.827  1.00 39.42           C  
ANISOU 1954  CA  PRO A 252     5171   5947   3861   -498    798  -1162       C  
ATOM   1955  C   PRO A 252     -18.901   5.422  40.743  1.00 40.97           C  
ANISOU 1955  C   PRO A 252     5331   6050   4185   -391    701  -1242       C  
ATOM   1956  O   PRO A 252     -18.044   5.425  41.635  1.00 43.12           O  
ANISOU 1956  O   PRO A 252     5687   6339   4358   -381    631  -1278       O  
ATOM   1957  CB  PRO A 252     -19.800   3.183  40.000  1.00 39.57           C  
ANISOU 1957  CB  PRO A 252     5278   5883   3875   -534    740   -983       C  
ATOM   1958  CG  PRO A 252     -21.148   2.747  39.557  1.00 37.69           C  
ANISOU 1958  CG  PRO A 252     4988   5702   3631   -611    849   -939       C  
ATOM   1959  CD  PRO A 252     -21.918   4.010  39.306  1.00 40.37           C  
ANISOU 1959  CD  PRO A 252     5152   6075   4110   -556    930  -1078       C  
ATOM   1960  N   LEU A 253     -18.843   6.251  39.699  1.00 39.73           N  
ANISOU 1960  N   LEU A 253     5056   5795   4246   -317    690  -1268       N  
ATOM   1961  CA  LEU A 253     -17.755   7.216  39.586  1.00 38.81           C  
ANISOU 1961  CA  LEU A 253     4900   5586   4260   -234    603  -1340       C  
ATOM   1962  C   LEU A 253     -17.980   8.421  40.491  1.00 40.06           C  
ANISOU 1962  C   LEU A 253     4997   5797   4426   -200    633  -1523       C  
ATOM   1963  O   LEU A 253     -17.028   8.943  41.082  1.00 38.70           O  
ANISOU 1963  O   LEU A 253     4848   5601   4255   -164    556  -1600       O  
ATOM   1964  CB  LEU A 253     -17.594   7.658  38.132  1.00 35.88           C  
ANISOU 1964  CB  LEU A 253     4439   5089   4105   -184    579  -1288       C  
ATOM   1965  CG  LEU A 253     -17.044   6.591  37.184  1.00 32.36           C  
ANISOU 1965  CG  LEU A 253     4049   4578   3668   -198    526  -1128       C  
ATOM   1966  CD1 LEU A 253     -16.915   7.138  35.772  1.00 31.87           C  
ANISOU 1966  CD1 LEU A 253     3896   4408   3806   -154    513  -1088       C  
ATOM   1967  CD2 LEU A 253     -15.707   6.070  37.687  1.00 32.51           C  
ANISOU 1967  CD2 LEU A 253     4163   4580   3611   -187    421  -1104       C  
ATOM   1968  N   SER A 254     -19.229   8.878  40.609  1.00 41.28           N  
ANISOU 1968  N   SER A 254     5067   6024   4592   -205    738  -1607       N  
ATOM   1969  CA  SER A 254     -19.525   9.986  41.510  1.00 42.87           C  
ANISOU 1969  CA  SER A 254     5208   6285   4795   -165    770  -1801       C  
ATOM   1970  C   SER A 254     -19.366   9.581  42.969  1.00 43.38           C  
ANISOU 1970  C   SER A 254     5375   6488   4620   -216    785  -1859       C  
ATOM   1971  O   SER A 254     -18.971  10.406  43.800  1.00 45.92           O  
ANISOU 1971  O   SER A 254     5691   6831   4926   -174    755  -2008       O  
ATOM   1972  CB  SER A 254     -20.940  10.507  41.256  1.00 40.96           C  
ANISOU 1972  CB  SER A 254     4840   6097   4625   -149    878  -1886       C  
ATOM   1973  OG  SER A 254     -21.908   9.515  41.550  1.00 43.51           O  
ANISOU 1973  OG  SER A 254     5186   6560   4785   -241    982  -1830       O  
ATOM   1974  N   ALA A 255     -19.663   8.322  43.298  1.00 39.18           N  
ANISOU 1974  N   ALA A 255     4945   6047   3895   -311    824  -1742       N  
ATOM   1975  CA  ALA A 255     -19.523   7.866  44.677  1.00 42.27           C  
ANISOU 1975  CA  ALA A 255     5454   6571   4035   -374    833  -1775       C  
ATOM   1976  C   ALA A 255     -18.057   7.736  45.072  1.00 43.25           C  
ANISOU 1976  C   ALA A 255     5688   6626   4121   -342    686  -1750       C  
ATOM   1977  O   ALA A 255     -17.688   8.033  46.214  1.00 44.92           O  
ANISOU 1977  O   ALA A 255     5956   6913   4198   -340    659  -1853       O  
ATOM   1978  CB  ALA A 255     -20.250   6.535  44.866  1.00 42.86           C  
ANISOU 1978  CB  ALA A 255     5621   6746   3920   -498    908  -1638       C  
ATOM   1979  N   GLN A 256     -17.207   7.294  44.142  1.00 57.51           N  
ANISOU 1979  N   GLN A 256     7517   8294   6041   -314    588  -1622       N  
ATOM   1980  CA  GLN A 256     -15.791   7.130  44.453  1.00 57.80           C  
ANISOU 1980  CA  GLN A 256     7637   8268   6056   -277    442  -1602       C  
ATOM   1981  C   GLN A 256     -15.108   8.477  44.660  1.00 55.40           C  
ANISOU 1981  C   GLN A 256     7249   7914   5887   -196    384  -1764       C  
ATOM   1982  O   GLN A 256     -14.259   8.619  45.547  1.00 58.52           O  
ANISOU 1982  O   GLN A 256     7708   8330   6196   -179    295  -1830       O  
ATOM   1983  CB  GLN A 256     -15.098   6.342  43.341  1.00 55.00           C  
ANISOU 1983  CB  GLN A 256     7306   7791   5800   -262    362  -1443       C  
ATOM   1984  CG  GLN A 256     -13.617   6.097  43.580  1.00 57.02           C  
ANISOU 1984  CG  GLN A 256     7631   7986   6047   -217    207  -1426       C  
ATOM   1985  CD  GLN A 256     -12.941   5.413  42.408  1.00 56.76           C  
ANISOU 1985  CD  GLN A 256     7594   7841   6130   -189    137  -1296       C  
ATOM   1986  OE1 GLN A 256     -13.594   5.022  41.440  1.00 54.45           O  
ANISOU 1986  OE1 GLN A 256     7268   7516   5904   -210    201  -1205       O  
ATOM   1987  NE2 GLN A 256     -11.623   5.266  42.488  1.00 52.84           N  
ANISOU 1987  NE2 GLN A 256     7125   7293   5658   -138      2  -1295       N  
ATOM   1988  N   THR A 257     -15.468   9.477  43.856  1.00 40.16           N  
ANISOU 1988  N   THR A 257     5180   5908   4169   -148    425  -1827       N  
ATOM   1989  CA  THR A 257     -14.843  10.789  43.942  1.00 43.21           C  
ANISOU 1989  CA  THR A 257     5488   6220   4708    -79    364  -1971       C  
ATOM   1990  C   THR A 257     -15.587  11.752  44.856  1.00 45.07           C  
ANISOU 1990  C   THR A 257     5677   6542   4907    -60    430  -2166       C  
ATOM   1991  O   THR A 257     -15.022  12.785  45.232  1.00 44.43           O  
ANISOU 1991  O   THR A 257     5558   6412   4911     -9    366  -2306       O  
ATOM   1992  CB  THR A 257     -14.732  11.416  42.548  1.00 40.30           C  
ANISOU 1992  CB  THR A 257     5009   5703   4599    -39    352  -1929       C  
ATOM   1993  OG1 THR A 257     -16.043  11.595  41.999  1.00 39.06           O  
ANISOU 1993  OG1 THR A 257     4778   5562   4499    -41    463  -1927       O  
ATOM   1994  CG2 THR A 257     -13.920  10.523  41.624  1.00 40.02           C  
ANISOU 1994  CG2 THR A 257     5010   5594   4603    -52    289  -1757       C  
ATOM   1995  N   GLY A 258     -16.830  11.445  45.220  1.00 47.46           N  
ANISOU 1995  N   GLY A 258     5974   6972   5087   -100    555  -2186       N  
ATOM   1996  CA  GLY A 258     -17.612  12.370  46.014  1.00 47.95           C  
ANISOU 1996  CA  GLY A 258     5971   7127   5122    -72    630  -2388       C  
ATOM   1997  C   GLY A 258     -18.043  13.614  45.274  1.00 48.19           C  
ANISOU 1997  C   GLY A 258     5857   7048   5406     10    640  -2493       C  
ATOM   1998  O   GLY A 258     -18.400  14.610  45.908  1.00 52.18           O  
ANISOU 1998  O   GLY A 258     6303   7587   5937     62    660  -2691       O  
ATOM   1999  N   ILE A 259     -18.021  13.584  43.944  1.00 45.62           N  
ANISOU 1999  N   ILE A 259     5479   6588   5266     25    621  -2368       N  
ATOM   2000  CA  ILE A 259     -18.370  14.727  43.109  1.00 45.10           C  
ANISOU 2000  CA  ILE A 259     5294   6392   5449     99    610  -2436       C  
ATOM   2001  C   ILE A 259     -19.626  14.358  42.333  1.00 48.14           C  
ANISOU 2001  C   ILE A 259     5611   6810   5871     88    709  -2368       C  
ATOM   2002  O   ILE A 259     -19.597  13.452  41.489  1.00 45.59           O  
ANISOU 2002  O   ILE A 259     5316   6460   5545     42    714  -2186       O  
ATOM   2003  CB  ILE A 259     -17.228  15.115  42.162  1.00 45.38           C  
ANISOU 2003  CB  ILE A 259     5328   6241   5675    120    494  -2349       C  
ATOM   2004  CG1 ILE A 259     -15.950  15.385  42.957  1.00 46.46           C  
ANISOU 2004  CG1 ILE A 259     5524   6358   5770    121    391  -2417       C  
ATOM   2005  CG2 ILE A 259     -17.613  16.328  41.328  1.00 43.08           C  
ANISOU 2005  CG2 ILE A 259     4932   5805   5632    187    474  -2409       C  
ATOM   2006  CD1 ILE A 259     -14.725  15.562  42.095  1.00 45.42           C  
ANISOU 2006  CD1 ILE A 259     5389   6074   5795    118    286  -2319       C  
ATOM   2007  N   ALA A 260     -20.725  15.054  42.615  1.00 45.24           N  
ANISOU 2007  N   ALA A 260     5146   6503   5541    135    783  -2523       N  
ATOM   2008  CA  ALA A 260     -21.991  14.766  41.958  1.00 43.48           C  
ANISOU 2008  CA  ALA A 260     4839   6326   5356    131    875  -2485       C  
ATOM   2009  C   ALA A 260     -21.888  15.010  40.454  1.00 42.05           C  
ANISOU 2009  C   ALA A 260     4615   5966   5397    167    812  -2359       C  
ATOM   2010  O   ALA A 260     -21.037  15.765  39.974  1.00 42.81           O  
ANISOU 2010  O   ALA A 260     4716   5898   5650    211    710  -2353       O  
ATOM   2011  CB  ALA A 260     -23.110  15.618  42.556  1.00 43.76           C  
ANISOU 2011  CB  ALA A 260     4757   6454   5414    196    951  -2707       C  
ATOM   2012  N   VAL A 261     -22.775  14.350  39.706  1.00 43.44           N  
ANISOU 2012  N   VAL A 261     4750   6178   5578    137    876  -2257       N  
ATOM   2013  CA  VAL A 261     -22.748  14.454  38.249  1.00 42.78           C  
ANISOU 2013  CA  VAL A 261     4636   5942   5675    163    820  -2125       C  
ATOM   2014  C   VAL A 261     -23.040  15.882  37.806  1.00 43.14           C  
ANISOU 2014  C   VAL A 261     4589   5856   5948    270    764  -2242       C  
ATOM   2015  O   VAL A 261     -22.380  16.416  36.906  1.00 41.91           O  
ANISOU 2015  O   VAL A 261     4446   5526   5950    297    670  -2166       O  
ATOM   2016  CB  VAL A 261     -23.734  13.451  37.621  1.00 42.08           C  
ANISOU 2016  CB  VAL A 261     4519   5933   5535    110    898  -2011       C  
ATOM   2017  CG1 VAL A 261     -23.892  13.718  36.133  1.00 40.19           C  
ANISOU 2017  CG1 VAL A 261     4235   5548   5487    151    841  -1906       C  
ATOM   2018  CG2 VAL A 261     -23.253  12.031  37.850  1.00 41.32           C  
ANISOU 2018  CG2 VAL A 261     4540   5914   5247      3    920  -1863       C  
ATOM   2019  N   LEU A 262     -24.029  16.526  38.432  1.00 43.06           N  
ANISOU 2019  N   LEU A 262     4485   5924   5953    331    817  -2431       N  
ATOM   2020  CA  LEU A 262     -24.360  17.897  38.060  1.00 46.47           C  
ANISOU 2020  CA  LEU A 262     4833   6218   6607    446    748  -2556       C  
ATOM   2021  C   LEU A 262     -23.224  18.859  38.384  1.00 42.43           C  
ANISOU 2021  C   LEU A 262     4374   5564   6182    480    642  -2625       C  
ATOM   2022  O   LEU A 262     -23.072  19.887  37.713  1.00 45.22           O  
ANISOU 2022  O   LEU A 262     4705   5733   6745    548    546  -2642       O  
ATOM   2023  CB  LEU A 262     -25.652  18.333  38.751  1.00 46.27           C  
ANISOU 2023  CB  LEU A 262     4687   6323   6571    512    827  -2765       C  
ATOM   2024  CG  LEU A 262     -26.928  17.681  38.211  1.00 47.70           C  
ANISOU 2024  CG  LEU A 262     4779   6610   6736    494    908  -2709       C  
ATOM   2025  CD1 LEU A 262     -28.162  18.237  38.907  1.00 53.66           C  
ANISOU 2025  CD1 LEU A 262     5428   7479   7483    539    939  -2850       C  
ATOM   2026  CD2 LEU A 262     -27.028  17.865  36.704  1.00 44.84           C  
ANISOU 2026  CD2 LEU A 262     4396   6076   6566    535    828  -2579       C  
ATOM   2027  N   ASP A 263     -22.417  18.549  39.402  1.00 45.10           N  
ANISOU 2027  N   ASP A 263     4788   5982   6365    430    650  -2662       N  
ATOM   2028  CA  ASP A 263     -21.231  19.354  39.674  1.00 45.06           C  
ANISOU 2028  CA  ASP A 263     4836   5846   6440    446    542  -2713       C  
ATOM   2029  C   ASP A 263     -20.216  19.219  38.545  1.00 44.97           C  
ANISOU 2029  C   ASP A 263     4879   5674   6534    402    458  -2512       C  
ATOM   2030  O   ASP A 263     -19.667  20.218  38.065  1.00 46.18           O  
ANISOU 2030  O   ASP A 263     5029   5648   6871    433    361  -2525       O  
ATOM   2031  CB  ASP A 263     -20.614  18.945  41.015  1.00 46.23           C  
ANISOU 2031  CB  ASP A 263     5053   6130   6380    401    564  -2792       C  
ATOM   2032  CG  ASP A 263     -19.613  19.966  41.543  1.00 53.53           C  
ANISOU 2032  CG  ASP A 263     6006   6943   7389    434    457  -2915       C  
ATOM   2033  OD1 ASP A 263     -19.534  20.137  42.778  1.00 56.44           O  
ANISOU 2033  OD1 ASP A 263     6394   7419   7630    442    470  -3069       O  
ATOM   2034  OD2 ASP A 263     -18.896  20.588  40.734  1.00 55.08           O  
ANISOU 2034  OD2 ASP A 263     6208   6948   7770    441    357  -2848       O  
ATOM   2035  N   MET A 264     -19.956  17.985  38.105  1.00 44.41           N  
ANISOU 2035  N   MET A 264     4859   5668   6348    324    496  -2329       N  
ATOM   2036  CA  MET A 264     -19.009  17.774  37.015  1.00 40.66           C  
ANISOU 2036  CA  MET A 264     4425   5067   5956    282    430  -2147       C  
ATOM   2037  C   MET A 264     -19.486  18.422  35.723  1.00 38.48           C  
ANISOU 2037  C   MET A 264     4099   4644   5879    321    394  -2080       C  
ATOM   2038  O   MET A 264     -18.664  18.870  34.914  1.00 40.27           O  
ANISOU 2038  O   MET A 264     4346   4724   6230    303    318  -1989       O  
ATOM   2039  CB  MET A 264     -18.777  16.277  36.803  1.00 41.46           C  
ANISOU 2039  CB  MET A 264     4587   5272   5892    206    477  -1982       C  
ATOM   2040  CG  MET A 264     -17.628  15.959  35.862  1.00 37.49           C  
ANISOU 2040  CG  MET A 264     4128   4671   5445    163    414  -1819       C  
ATOM   2041  SD  MET A 264     -16.023  16.358  36.580  1.00 38.80           S  
ANISOU 2041  SD  MET A 264     4339   4794   5609    143    323  -1877       S  
ATOM   2042  CE  MET A 264     -15.863  15.052  37.794  1.00 36.60           C  
ANISOU 2042  CE  MET A 264     4140   4701   5064    104    362  -1883       C  
ATOM   2043  N   CYS A 265     -20.803  18.486  35.513  1.00 41.15           N  
ANISOU 2043  N   CYS A 265     4368   5023   6244    371    445  -2123       N  
ATOM   2044  CA  CYS A 265     -21.329  19.109  34.303  1.00 42.72           C  
ANISOU 2044  CA  CYS A 265     4523   5080   6627    418    396  -2062       C  
ATOM   2045  C   CYS A 265     -21.038  20.603  34.266  1.00 43.24           C  
ANISOU 2045  C   CYS A 265     4577   4964   6888    482    293  -2166       C  
ATOM   2046  O   CYS A 265     -20.854  21.170  33.183  1.00 42.21           O  
ANISOU 2046  O   CYS A 265     4458   4667   6912    488    216  -2065       O  
ATOM   2047  CB  CYS A 265     -22.831  18.857  34.195  1.00 44.02           C  
ANISOU 2047  CB  CYS A 265     4604   5342   6779    465    466  -2111       C  
ATOM   2048  SG  CYS A 265     -23.260  17.285  33.426  1.00 43.72           S  
ANISOU 2048  SG  CYS A 265     4582   5420   6611    386    544  -1915       S  
ATOM   2049  N   ALA A 266     -20.999  21.257  35.429  1.00 46.39           N  
ANISOU 2049  N   ALA A 266     4960   5386   7280    526    284  -2364       N  
ATOM   2050  CA  ALA A 266     -20.600  22.659  35.466  1.00 45.36           C  
ANISOU 2050  CA  ALA A 266     4832   5068   7337    579    173  -2468       C  
ATOM   2051  C   ALA A 266     -19.138  22.828  35.076  1.00 45.93           C  
ANISOU 2051  C   ALA A 266     4977   5017   7456    495     98  -2349       C  
ATOM   2052  O   ALA A 266     -18.777  23.830  34.448  1.00 45.00           O  
ANISOU 2052  O   ALA A 266     4875   4701   7523    502     -1  -2325       O  
ATOM   2053  CB  ALA A 266     -20.854  23.245  36.853  1.00 48.39           C  
ANISOU 2053  CB  ALA A 266     5183   5518   7684    644    183  -2721       C  
ATOM   2054  N   SER A 267     -18.287  21.865  35.439  1.00 51.71           N  
ANISOU 2054  N   SER A 267     5756   5865   8028    413    140  -2276       N  
ATOM   2055  CA  SER A 267     -16.898  21.903  34.994  1.00 50.51           C  
ANISOU 2055  CA  SER A 267     5653   5621   7917    331     78  -2161       C  
ATOM   2056  C   SER A 267     -16.800  21.692  33.489  1.00 49.86           C  
ANISOU 2056  C   SER A 267     5582   5450   7914    288     66  -1951       C  
ATOM   2057  O   SER A 267     -16.017  22.368  32.811  1.00 51.43           O  
ANISOU 2057  O   SER A 267     5800   5497   8243    243     -7  -1879       O  
ATOM   2058  CB  SER A 267     -16.079  20.849  35.740  1.00 49.86           C  
ANISOU 2058  CB  SER A 267     5610   5693   7642    271    117  -2140       C  
ATOM   2059  OG  SER A 267     -16.111  21.072  37.139  1.00 54.04           O  
ANISOU 2059  OG  SER A 267     6142   6307   8085    304    120  -2331       O  
ATOM   2060  N   LEU A 268     -17.590  20.760  32.948  1.00 39.86           N  
ANISOU 2060  N   LEU A 268     4303   4279   6562    292    138  -1852       N  
ATOM   2061  CA  LEU A 268     -17.607  20.546  31.505  1.00 37.93           C  
ANISOU 2061  CA  LEU A 268     4070   3961   6380    259    128  -1663       C  
ATOM   2062  C   LEU A 268     -18.181  21.749  30.769  1.00 39.52           C  
ANISOU 2062  C   LEU A 268     4256   3982   6776    311     52  -1668       C  
ATOM   2063  O   LEU A 268     -17.735  22.069  29.661  1.00 41.60           O  
ANISOU 2063  O   LEU A 268     4551   4123   7133    265      2  -1526       O  
ATOM   2064  CB  LEU A 268     -18.406  19.285  31.173  1.00 38.27           C  
ANISOU 2064  CB  LEU A 268     4104   4148   6288    257    214  -1576       C  
ATOM   2065  CG  LEU A 268     -18.554  18.926  29.693  1.00 37.87           C  
ANISOU 2065  CG  LEU A 268     4065   4047   6276    229    210  -1390       C  
ATOM   2066  CD1 LEU A 268     -17.189  18.779  29.040  1.00 38.01           C  
ANISOU 2066  CD1 LEU A 268     4129   4014   6301    145    181  -1260       C  
ATOM   2067  CD2 LEU A 268     -19.372  17.655  29.528  1.00 35.04           C  
ANISOU 2067  CD2 LEU A 268     3697   3835   5782    226    291  -1331       C  
ATOM   2068  N   LYS A 269     -19.168  22.422  31.366  1.00 48.16           N  
ANISOU 2068  N   LYS A 269     5305   5061   7934    408     38  -1833       N  
ATOM   2069  CA  LYS A 269     -19.703  23.645  30.779  1.00 49.35           C  
ANISOU 2069  CA  LYS A 269     5446   5020   8284    476    -58  -1860       C  
ATOM   2070  C   LYS A 269     -18.619  24.707  30.640  1.00 49.45           C  
ANISOU 2070  C   LYS A 269     5512   4842   8436    428   -160  -1849       C  
ATOM   2071  O   LYS A 269     -18.520  25.374  29.604  1.00 51.78           O  
ANISOU 2071  O   LYS A 269     5843   4963   8868    408   -240  -1736       O  
ATOM   2072  CB  LYS A 269     -20.861  24.163  31.633  1.00 52.03           C  
ANISOU 2072  CB  LYS A 269     5715   5393   8660    599    -54  -2078       C  
ATOM   2073  CG  LYS A 269     -21.392  25.530  31.236  1.00 53.77           C  
ANISOU 2073  CG  LYS A 269     5926   5402   9102    693   -175  -2149       C  
ATOM   2074  CD  LYS A 269     -22.724  25.803  31.920  1.00 56.15           C  
ANISOU 2074  CD  LYS A 269     6133   5778   9426    829   -154  -2360       C  
ATOM   2075  CE  LYS A 269     -22.931  27.287  32.174  1.00 61.80           C  
ANISOU 2075  CE  LYS A 269     6850   6334  10298    907   -282  -2472       C  
ATOM   2076  NZ  LYS A 269     -23.311  28.011  30.930  1.00 61.39           N  
ANISOU 2076  NZ  LYS A 269     6828   6081  10417    943   -403  -2351       N  
ATOM   2077  N   GLU A 270     -17.789  24.867  31.673  1.00 49.92           N  
ANISOU 2077  N   GLU A 270     5579   4931   8457    398   -164  -1962       N  
ATOM   2078  CA  GLU A 270     -16.705  25.843  31.615  1.00 52.96           C  
ANISOU 2078  CA  GLU A 270     6006   5143   8973    338   -260  -1962       C  
ATOM   2079  C   GLU A 270     -15.661  25.451  30.578  1.00 52.38           C  
ANISOU 2079  C   GLU A 270     5973   5040   8890    210   -257  -1744       C  
ATOM   2080  O   GLU A 270     -15.123  26.316  29.875  1.00 50.67           O  
ANISOU 2080  O   GLU A 270     5794   4642   8816    150   -338  -1664       O  
ATOM   2081  CB  GLU A 270     -16.061  25.984  32.994  1.00 52.21           C  
ANISOU 2081  CB  GLU A 270     5904   5112   8821    335   -262  -2140       C  
ATOM   2082  CG  GLU A 270     -15.294  27.277  33.201  1.00 57.61           C  
ANISOU 2082  CG  GLU A 270     6616   5597   9676    308   -380  -2218       C  
ATOM   2083  CD  GLU A 270     -16.116  28.331  33.915  1.00 63.69           C  
ANISOU 2083  CD  GLU A 270     7368   6271  10560    430   -447  -2438       C  
ATOM   2084  OE1 GLU A 270     -17.054  28.879  33.299  1.00 63.92           O  
ANISOU 2084  OE1 GLU A 270     7392   6208  10688    502   -488  -2406       O  
ATOM   2085  OE2 GLU A 270     -15.826  28.608  35.098  1.00 66.70           O  
ANISOU 2085  OE2 GLU A 270     7738   6726  10878    448   -457  -2589       O  
ATOM   2086  N   LEU A 271     -15.360  24.154  30.470  1.00 42.44           N  
ANISOU 2086  N   LEU A 271     4707   3958   7461    163   -164  -1648       N  
ATOM   2087  CA  LEU A 271     -14.347  23.704  29.521  1.00 41.14           C  
ANISOU 2087  CA  LEU A 271     4566   3792   7274     50   -152  -1462       C  
ATOM   2088  C   LEU A 271     -14.794  23.928  28.081  1.00 42.22           C  
ANISOU 2088  C   LEU A 271     4729   3824   7489     33   -173  -1294       C  
ATOM   2089  O   LEU A 271     -13.972  24.244  27.212  1.00 44.90           O  
ANISOU 2089  O   LEU A 271     5098   4075   7887    -65   -201  -1161       O  
ATOM   2090  CB  LEU A 271     -14.024  22.230  29.759  1.00 40.06           C  
ANISOU 2090  CB  LEU A 271     4418   3862   6940     25    -59  -1416       C  
ATOM   2091  CG  LEU A 271     -13.297  21.899  31.063  1.00 41.16           C  
ANISOU 2091  CG  LEU A 271     4548   4108   6984     19    -51  -1544       C  
ATOM   2092  CD1 LEU A 271     -13.159  20.395  31.233  1.00 37.70           C  
ANISOU 2092  CD1 LEU A 271     4114   3857   6353      8     27  -1485       C  
ATOM   2093  CD2 LEU A 271     -11.934  22.574  31.105  1.00 41.87           C  
ANISOU 2093  CD2 LEU A 271     4637   4108   7163    -66   -116  -1550       C  
ATOM   2094  N   LEU A 272     -16.090  23.765  27.809  1.00 40.27           N  
ANISOU 2094  N   LEU A 272     4470   3593   7237    122   -159  -1297       N  
ATOM   2095  CA  LEU A 272     -16.589  23.975  26.454  1.00 41.58           C  
ANISOU 2095  CA  LEU A 272     4667   3662   7471    117   -192  -1142       C  
ATOM   2096  C   LEU A 272     -16.647  25.457  26.106  1.00 46.29           C  
ANISOU 2096  C   LEU A 272     5304   4018   8267    125   -315  -1149       C  
ATOM   2097  O   LEU A 272     -16.398  25.842  24.958  1.00 44.31           O  
ANISOU 2097  O   LEU A 272     5107   3649   8081     59   -362   -986       O  
ATOM   2098  CB  LEU A 272     -17.966  23.335  26.298  1.00 42.85           C  
ANISOU 2098  CB  LEU A 272     4792   3918   7572    212   -150  -1154       C  
ATOM   2099  CG  LEU A 272     -17.959  21.807  26.315  1.00 41.34           C  
ANISOU 2099  CG  LEU A 272     4582   3937   7190    184    -39  -1095       C  
ATOM   2100  CD1 LEU A 272     -19.307  21.246  26.752  1.00 41.24           C  
ANISOU 2100  CD1 LEU A 272     4515   4041   7114    276     12  -1184       C  
ATOM   2101  CD2 LEU A 272     -17.561  21.288  24.948  1.00 41.46           C  
ANISOU 2101  CD2 LEU A 272     4636   3949   7168    108    -28   -889       C  
ATOM   2102  N   GLN A 273     -16.974  26.304  27.082  1.00 49.98           N  
ANISOU 2102  N   GLN A 273     5753   4409   8830    205   -372  -1338       N  
ATOM   2103  CA  GLN A 273     -17.118  27.730  26.817  1.00 53.68           C  
ANISOU 2103  CA  GLN A 273     6267   4629   9501    229   -506  -1362       C  
ATOM   2104  C   GLN A 273     -15.779  28.457  26.813  1.00 53.84           C  
ANISOU 2104  C   GLN A 273     6335   4519   9602    102   -562  -1324       C  
ATOM   2105  O   GLN A 273     -15.627  29.456  26.103  1.00 56.43           O  
ANISOU 2105  O   GLN A 273     6730   4633  10080     58   -666  -1240       O  
ATOM   2106  CB  GLN A 273     -18.051  28.368  27.849  1.00 54.93           C  
ANISOU 2106  CB  GLN A 273     6380   4753   9737    377   -552  -1599       C  
ATOM   2107  CG  GLN A 273     -19.499  27.910  27.755  1.00 54.77           C  
ANISOU 2107  CG  GLN A 273     6300   4829   9680    506   -517  -1647       C  
ATOM   2108  CD  GLN A 273     -20.351  28.441  28.892  1.00 55.54           C  
ANISOU 2108  CD  GLN A 273     6332   4938   9832    649   -538  -1907       C  
ATOM   2109  OE1 GLN A 273     -21.578  28.483  28.799  1.00 59.28           O  
ANISOU 2109  OE1 GLN A 273     6750   5432  10341    769   -547  -1978       O  
ATOM   2110  NE2 GLN A 273     -19.701  28.852  29.975  1.00 54.43           N  
ANISOU 2110  NE2 GLN A 273     6190   4793   9697    638   -546  -2061       N  
ATOM   2111  N   ASN A 274     -14.803  27.980  27.587  1.00 60.04           N  
ANISOU 2111  N   ASN A 274     7089   5426  10296     36   -502  -1382       N  
ATOM   2112  CA  ASN A 274     -13.527  28.666  27.723  1.00 61.07           C  
ANISOU 2112  CA  ASN A 274     7245   5450  10508    -85   -555  -1376       C  
ATOM   2113  C   ASN A 274     -12.337  27.888  27.182  1.00 62.53           C  
ANISOU 2113  C   ASN A 274     7419   5748  10589   -229   -480  -1224       C  
ATOM   2114  O   ASN A 274     -11.227  28.433  27.166  1.00 62.64           O  
ANISOU 2114  O   ASN A 274     7443   5685  10675   -348   -517  -1203       O  
ATOM   2115  CB  ASN A 274     -13.259  29.009  29.197  1.00 61.60           C  
ANISOU 2115  CB  ASN A 274     7279   5540  10588    -38   -578  -1608       C  
ATOM   2116  CG  ASN A 274     -14.367  29.839  29.812  1.00 66.52           C  
ANISOU 2116  CG  ASN A 274     7901   6056  11317    110   -652  -1791       C  
ATOM   2117  OD1 ASN A 274     -14.847  29.541  30.906  1.00 65.84           O  
ANISOU 2117  OD1 ASN A 274     7766   6097  11152    208   -612  -1974       O  
ATOM   2118  ND2 ASN A 274     -14.780  30.889  29.112  1.00 65.25           N  
ANISOU 2118  ND2 ASN A 274     7794   5681  11316    128   -760  -1734       N  
ATOM   2119  N   GLY A 275     -12.523  26.650  26.738  1.00 54.54           N  
ANISOU 2119  N   GLY A 275     6384   4917   9420   -223   -379  -1127       N  
ATOM   2120  CA  GLY A 275     -11.389  25.857  26.312  1.00 53.07           C  
ANISOU 2120  CA  GLY A 275     6176   4853   9134   -340   -309  -1013       C  
ATOM   2121  C   GLY A 275     -10.547  25.411  27.498  1.00 52.75           C  
ANISOU 2121  C   GLY A 275     6084   4939   9019   -349   -282  -1148       C  
ATOM   2122  O   GLY A 275     -10.926  25.542  28.663  1.00 51.80           O  
ANISOU 2122  O   GLY A 275     5950   4842   8889   -262   -301  -1323       O  
ATOM   2123  N   MET A 276      -9.370  24.876  27.175  1.00 55.54           N  
ANISOU 2123  N   MET A 276     6408   5382   9315   -455   -240  -1069       N  
ATOM   2124  CA  MET A 276      -8.458  24.368  28.190  1.00 54.84           C  
ANISOU 2124  CA  MET A 276     6267   5419   9150   -467   -226  -1180       C  
ATOM   2125  C   MET A 276      -7.368  25.358  28.577  1.00 59.23           C  
ANISOU 2125  C   MET A 276     6802   5869   9832   -564   -300  -1248       C  
ATOM   2126  O   MET A 276      -6.620  25.088  29.523  1.00 55.31           O  
ANISOU 2126  O   MET A 276     6263   5462   9291   -567   -310  -1363       O  
ATOM   2127  CB  MET A 276      -7.815  23.058  27.720  1.00 55.72           C  
ANISOU 2127  CB  MET A 276     6342   5711   9118   -504   -144  -1082       C  
ATOM   2128  CG  MET A 276      -8.395  21.824  28.390  1.00 54.08           C  
ANISOU 2128  CG  MET A 276     6133   5670   8743   -398    -90  -1136       C  
ATOM   2129  SD  MET A 276      -7.762  20.284  27.705  1.00 54.11           S  
ANISOU 2129  SD  MET A 276     6110   5856   8595   -426    -10  -1015       S  
ATOM   2130  CE  MET A 276      -9.292  19.404  27.402  1.00 49.20           C  
ANISOU 2130  CE  MET A 276     5535   5295   7865   -326     47   -961       C  
ATOM   2131  N   ASN A 277      -7.260  26.487  27.872  1.00 59.70           N  
ANISOU 2131  N   ASN A 277     6896   5739  10049   -647   -358  -1176       N  
ATOM   2132  CA  ASN A 277      -6.329  27.563  28.218  1.00 61.01           C  
ANISOU 2132  CA  ASN A 277     7051   5772  10357   -750   -439  -1240       C  
ATOM   2133  C   ASN A 277      -4.878  27.087  28.252  1.00 60.57           C  
ANISOU 2133  C   ASN A 277     6914   5842  10258   -867   -405  -1226       C  
ATOM   2134  O   ASN A 277      -4.056  27.622  29.000  1.00 63.28           O  
ANISOU 2134  O   ASN A 277     7221   6150  10672   -920   -465  -1341       O  
ATOM   2135  CB  ASN A 277      -6.707  28.212  29.554  1.00 63.74           C  
ANISOU 2135  CB  ASN A 277     7408   6047  10762   -655   -520  -1458       C  
ATOM   2136  CG  ASN A 277      -7.338  29.580  29.380  1.00 69.28           C  
ANISOU 2136  CG  ASN A 277     8179   6497  11648   -642   -622  -1482       C  
ATOM   2137  OD1 ASN A 277      -8.084  29.814  28.428  1.00 69.65           O  
ANISOU 2137  OD1 ASN A 277     8280   6447  11738   -630   -626  -1355       O  
ATOM   2138  ND2 ASN A 277      -7.046  30.489  30.302  1.00 70.84           N  
ANISOU 2138  ND2 ASN A 277     8380   6581  11956   -641   -716  -1650       N  
ATOM   2139  N   GLY A 278      -4.547  26.083  27.442  1.00 52.14           N  
ANISOU 2139  N   GLY A 278     5813   4923   9077   -903   -313  -1094       N  
ATOM   2140  CA  GLY A 278      -3.185  25.605  27.337  1.00 53.35           C  
ANISOU 2140  CA  GLY A 278     5874   5203   9193  -1007   -278  -1079       C  
ATOM   2141  C   GLY A 278      -2.825  24.448  28.243  1.00 49.17           C  
ANISOU 2141  C   GLY A 278     5288   4871   8523   -919   -253  -1187       C  
ATOM   2142  O   GLY A 278      -1.686  23.968  28.179  1.00 50.32           O  
ANISOU 2142  O   GLY A 278     5347   5133   8637   -986   -231  -1187       O  
ATOM   2143  N   ARG A 279      -3.746  23.985  29.084  1.00 50.73           N  
ANISOU 2143  N   ARG A 279     5530   5113   8634   -774   -258  -1279       N  
ATOM   2144  CA  ARG A 279      -3.468  22.881  29.987  1.00 49.36           C  
ANISOU 2144  CA  ARG A 279     5326   5115   8315   -693   -245  -1371       C  
ATOM   2145  C   ARG A 279      -3.924  21.561  29.369  1.00 46.04           C  
ANISOU 2145  C   ARG A 279     4917   4829   7745   -634   -160  -1261       C  
ATOM   2146  O   ARG A 279      -4.458  21.513  28.259  1.00 46.27           O  
ANISOU 2146  O   ARG A 279     4974   4824   7781   -654   -109  -1124       O  
ATOM   2147  CB  ARG A 279      -4.137  23.119  31.339  1.00 50.80           C  
ANISOU 2147  CB  ARG A 279     5551   5280   8470   -586   -298  -1539       C  
ATOM   2148  CG  ARG A 279      -3.328  23.992  32.279  1.00 53.27           C  
ANISOU 2148  CG  ARG A 279     5832   5530   8876   -628   -391  -1692       C  
ATOM   2149  CD  ARG A 279      -4.168  24.443  33.456  1.00 53.14           C  
ANISOU 2149  CD  ARG A 279     5870   5473   8848   -524   -438  -1857       C  
ATOM   2150  NE  ARG A 279      -5.324  25.227  33.032  1.00 53.69           N  
ANISOU 2150  NE  ARG A 279     5995   5394   9009   -487   -438  -1834       N  
ATOM   2151  CZ  ARG A 279      -6.230  25.729  33.863  1.00 56.94           C  
ANISOU 2151  CZ  ARG A 279     6448   5757   9430   -390   -470  -1975       C  
ATOM   2152  NH1 ARG A 279      -6.121  25.526  35.169  1.00 54.80           N  
ANISOU 2152  NH1 ARG A 279     6175   5578   9067   -329   -498  -2143       N  
ATOM   2153  NH2 ARG A 279      -7.252  26.430  33.389  1.00 57.31           N  
ANISOU 2153  NH2 ARG A 279     6534   5666   9574   -349   -479  -1954       N  
ATOM   2154  N   THR A 280      -3.707  20.470  30.101  1.00 44.08           N  
ANISOU 2154  N   THR A 280     4658   4730   7360   -562   -153  -1323       N  
ATOM   2155  CA  THR A 280      -4.046  19.135  29.635  1.00 44.33           C  
ANISOU 2155  CA  THR A 280     4706   4888   7250   -506    -86  -1234       C  
ATOM   2156  C   THR A 280      -4.843  18.399  30.703  1.00 42.33           C  
ANISOU 2156  C   THR A 280     4512   4709   6862   -392    -90  -1315       C  
ATOM   2157  O   THR A 280      -4.808  18.745  31.887  1.00 44.05           O  
ANISOU 2157  O   THR A 280     4742   4923   7071   -358   -144  -1450       O  
ATOM   2158  CB  THR A 280      -2.793  18.318  29.279  1.00 42.66           C  
ANISOU 2158  CB  THR A 280     4417   4798   6993   -545    -74  -1205       C  
ATOM   2159  OG1 THR A 280      -1.982  18.148  30.448  1.00 43.73           O  
ANISOU 2159  OG1 THR A 280     4518   4996   7101   -520   -144  -1340       O  
ATOM   2160  CG2 THR A 280      -1.981  19.016  28.197  1.00 43.73           C  
ANISOU 2160  CG2 THR A 280     4483   4884   7247   -676    -53  -1123       C  
ATOM   2161  N   ILE A 281      -5.567  17.374  30.263  1.00 40.02           N  
ANISOU 2161  N   ILE A 281     4260   4489   6459   -340    -30  -1229       N  
ATOM   2162  CA  ILE A 281      -6.313  16.483  31.144  1.00 38.85           C  
ANISOU 2162  CA  ILE A 281     4171   4427   6163   -252    -20  -1277       C  
ATOM   2163  C   ILE A 281      -5.948  15.055  30.769  1.00 38.17           C  
ANISOU 2163  C   ILE A 281     4090   4457   5956   -232      5  -1199       C  
ATOM   2164  O   ILE A 281      -6.249  14.609  29.655  1.00 39.69           O  
ANISOU 2164  O   ILE A 281     4283   4655   6141   -243     59  -1081       O  
ATOM   2165  CB  ILE A 281      -7.832  16.697  31.041  1.00 40.26           C  
ANISOU 2165  CB  ILE A 281     4400   4562   6335   -207     25  -1260       C  
ATOM   2166  CG1 ILE A 281      -8.208  18.111  31.481  1.00 39.46           C  
ANISOU 2166  CG1 ILE A 281     4294   4338   6360   -208    -14  -1358       C  
ATOM   2167  CG2 ILE A 281      -8.568  15.673  31.882  1.00 37.45           C  
ANISOU 2167  CG2 ILE A 281     4101   4315   5815   -140     50  -1294       C  
ATOM   2168  CD1 ILE A 281      -9.691  18.400  31.398  1.00 39.97           C  
ANISOU 2168  CD1 ILE A 281     4390   4361   6436   -151     21  -1364       C  
ATOM   2169  N   LEU A 282      -5.300  14.343  31.693  1.00 38.86           N  
ANISOU 2169  N   LEU A 282     4186   4632   5947   -198    -43  -1268       N  
ATOM   2170  CA  LEU A 282      -4.822  12.981  31.450  1.00 39.53           C  
ANISOU 2170  CA  LEU A 282     4280   4814   5926   -167    -45  -1212       C  
ATOM   2171  C   LEU A 282      -3.933  12.924  30.210  1.00 42.31           C  
ANISOU 2171  C   LEU A 282     4549   5173   6353   -216    -24  -1138       C  
ATOM   2172  O   LEU A 282      -4.000  11.989  29.409  1.00 42.21           O  
ANISOU 2172  O   LEU A 282     4544   5209   6284   -198     13  -1051       O  
ATOM   2173  CB  LEU A 282      -5.989  11.997  31.334  1.00 37.20           C  
ANISOU 2173  CB  LEU A 282     4070   4556   5509   -120      6  -1140       C  
ATOM   2174  CG  LEU A 282      -6.660  11.578  32.644  1.00 36.76           C  
ANISOU 2174  CG  LEU A 282     4099   4546   5323    -74    -12  -1208       C  
ATOM   2175  CD1 LEU A 282      -7.838  10.653  32.374  1.00 34.82           C  
ANISOU 2175  CD1 LEU A 282     3924   4332   4973    -52     49  -1124       C  
ATOM   2176  CD2 LEU A 282      -5.656  10.915  33.574  1.00 37.45           C  
ANISOU 2176  CD2 LEU A 282     4206   4701   5322    -44    -98  -1270       C  
ATOM   2177  N   GLY A 283      -3.091  13.942  30.051  1.00 53.95           N  
ANISOU 2177  N   GLY A 283     5943   6602   7956   -286    -46  -1176       N  
ATOM   2178  CA  GLY A 283      -2.176  13.991  28.927  1.00 52.31           C  
ANISOU 2178  CA  GLY A 283     5643   6415   7817   -353    -16  -1114       C  
ATOM   2179  C   GLY A 283      -2.819  14.287  27.591  1.00 55.89           C  
ANISOU 2179  C   GLY A 283     6107   6816   8311   -402     64   -985       C  
ATOM   2180  O   GLY A 283      -2.272  13.904  26.552  1.00 57.44           O  
ANISOU 2180  O   GLY A 283     6250   7066   8507   -438    107   -914       O  
ATOM   2181  N   SER A 284      -3.967  14.961  27.585  1.00 41.91           N  
ANISOU 2181  N   SER A 284     4402   4948   6573   -400     81   -958       N  
ATOM   2182  CA  SER A 284      -4.652  15.320  26.352  1.00 39.99           C  
ANISOU 2182  CA  SER A 284     4179   4643   6371   -441    139   -835       C  
ATOM   2183  C   SER A 284      -5.112  16.768  26.418  1.00 42.78           C  
ANISOU 2183  C   SER A 284     4550   4850   6855   -488    115   -846       C  
ATOM   2184  O   SER A 284      -5.633  17.217  27.443  1.00 42.56           O  
ANISOU 2184  O   SER A 284     4555   4772   6843   -441     74   -944       O  
ATOM   2185  CB  SER A 284      -5.855  14.404  26.091  1.00 41.53           C  
ANISOU 2185  CB  SER A 284     4448   4870   6460   -366    178   -774       C  
ATOM   2186  OG  SER A 284      -6.435  14.676  24.826  1.00 43.96           O  
ANISOU 2186  OG  SER A 284     4774   5130   6801   -402    224   -653       O  
ATOM   2187  N   ALA A 285      -4.916  17.492  25.319  1.00 39.51           N  
ANISOU 2187  N   ALA A 285     4118   4365   6527   -579    138   -749       N  
ATOM   2188  CA  ALA A 285      -5.374  18.869  25.194  1.00 42.13           C  
ANISOU 2188  CA  ALA A 285     4482   4533   6992   -626    104   -737       C  
ATOM   2189  C   ALA A 285      -6.778  18.967  24.610  1.00 42.50           C  
ANISOU 2189  C   ALA A 285     4604   4511   7034   -575    120   -658       C  
ATOM   2190  O   ALA A 285      -7.242  20.076  24.324  1.00 43.06           O  
ANISOU 2190  O   ALA A 285     4710   4434   7217   -604     83   -630       O  
ATOM   2191  CB  ALA A 285      -4.394  19.676  24.339  1.00 42.92           C  
ANISOU 2191  CB  ALA A 285     4536   4580   7192   -770    109   -663       C  
ATOM   2192  N   LEU A 286      -7.457  17.837  24.426  1.00 40.98           N  
ANISOU 2192  N   LEU A 286     4436   4415   6719   -499    163   -623       N  
ATOM   2193  CA  LEU A 286      -8.824  17.804  23.931  1.00 39.45           C  
ANISOU 2193  CA  LEU A 286     4301   4177   6513   -443    176   -562       C  
ATOM   2194  C   LEU A 286      -9.667  16.934  24.853  1.00 39.87           C  
ANISOU 2194  C   LEU A 286     4374   4310   6464   -339    188   -643       C  
ATOM   2195  O   LEU A 286      -9.151  16.093  25.592  1.00 36.47           O  
ANISOU 2195  O   LEU A 286     3929   3985   5942   -314    195   -705       O  
ATOM   2196  CB  LEU A 286      -8.899  17.262  22.495  1.00 40.68           C  
ANISOU 2196  CB  LEU A 286     4469   4373   6616   -478    225   -412       C  
ATOM   2197  CG  LEU A 286      -8.308  18.105  21.364  1.00 43.63           C  
ANISOU 2197  CG  LEU A 286     4840   4671   7066   -594    226   -298       C  
ATOM   2198  CD1 LEU A 286      -8.082  17.243  20.131  1.00 43.72           C  
ANISOU 2198  CD1 LEU A 286     4849   4786   6978   -625    290   -180       C  
ATOM   2199  CD2 LEU A 286      -9.212  19.283  21.036  1.00 47.99           C  
ANISOU 2199  CD2 LEU A 286     5452   5052   7731   -596    172   -254       C  
ATOM   2200  N   LEU A 287     -10.979  17.147  24.799  1.00 38.63           N  
ANISOU 2200  N   LEU A 287     4252   4104   6322   -280    186   -640       N  
ATOM   2201  CA  LEU A 287     -11.906  16.349  25.588  1.00 36.24           C  
ANISOU 2201  CA  LEU A 287     3966   3885   5921   -198    210   -707       C  
ATOM   2202  C   LEU A 287     -12.124  14.998  24.917  1.00 33.28           C  
ANISOU 2202  C   LEU A 287     3607   3616   5423   -189    260   -614       C  
ATOM   2203  O   LEU A 287     -12.389  14.927  23.712  1.00 35.26           O  
ANISOU 2203  O   LEU A 287     3869   3845   5685   -209    275   -502       O  
ATOM   2204  CB  LEU A 287     -13.232  17.089  25.760  1.00 36.46           C  
ANISOU 2204  CB  LEU A 287     4003   3832   6019   -140    192   -754       C  
ATOM   2205  CG  LEU A 287     -13.135  18.432  26.491  1.00 36.18           C  
ANISOU 2205  CG  LEU A 287     3957   3680   6111   -132    133   -868       C  
ATOM   2206  CD1 LEU A 287     -14.423  19.228  26.353  1.00 38.99           C  
ANISOU 2206  CD1 LEU A 287     4316   3938   6560    -66    104   -900       C  
ATOM   2207  CD2 LEU A 287     -12.788  18.223  27.958  1.00 34.31           C  
ANISOU 2207  CD2 LEU A 287     3708   3519   5809   -106    132  -1015       C  
ATOM   2208  N   GLU A 288     -12.011  13.927  25.698  1.00 35.20           N  
ANISOU 2208  N   GLU A 288     3861   3967   5545   -159    279   -662       N  
ATOM   2209  CA  GLU A 288     -12.067  12.563  25.187  1.00 35.56           C  
ANISOU 2209  CA  GLU A 288     3931   4106   5475   -150    312   -587       C  
ATOM   2210  C   GLU A 288     -13.428  11.950  25.496  1.00 33.15           C  
ANISOU 2210  C   GLU A 288     3656   3840   5098   -105    341   -596       C  
ATOM   2211  O   GLU A 288     -13.915  12.048  26.627  1.00 32.66           O  
ANISOU 2211  O   GLU A 288     3601   3801   5008    -77    342   -692       O  
ATOM   2212  CB  GLU A 288     -10.950  11.716  25.799  1.00 35.61           C  
ANISOU 2212  CB  GLU A 288     3937   4196   5398   -151    298   -625       C  
ATOM   2213  CG  GLU A 288     -10.913  10.281  25.309  1.00 38.19           C  
ANISOU 2213  CG  GLU A 288     4295   4604   5612   -134    318   -560       C  
ATOM   2214  CD  GLU A 288     -10.547  10.175  23.842  1.00 40.54           C  
ANISOU 2214  CD  GLU A 288     4570   4899   5935   -165    339   -459       C  
ATOM   2215  OE1 GLU A 288      -9.735  10.999  23.369  1.00 38.63           O  
ANISOU 2215  OE1 GLU A 288     4280   4621   5775   -214    335   -446       O  
ATOM   2216  OE2 GLU A 288     -11.070   9.268  23.163  1.00 42.11           O  
ANISOU 2216  OE2 GLU A 288     4800   5133   6065   -148    361   -394       O  
ATOM   2217  N   ASP A 289     -14.034  11.309  24.489  1.00 31.49           N  
ANISOU 2217  N   ASP A 289     3462   3648   4854   -103    365   -502       N  
ATOM   2218  CA  ASP A 289     -15.387  10.779  24.618  1.00 29.41           C  
ANISOU 2218  CA  ASP A 289     3215   3420   4539    -73    392   -503       C  
ATOM   2219  C   ASP A 289     -15.491   9.317  24.192  1.00 30.49           C  
ANISOU 2219  C   ASP A 289     3391   3633   4560    -78    412   -435       C  
ATOM   2220  O   ASP A 289     -16.588   8.850  23.869  1.00 28.87           O  
ANISOU 2220  O   ASP A 289     3195   3449   4326    -69    433   -404       O  
ATOM   2221  CB  ASP A 289     -16.377  11.628  23.814  1.00 30.51           C  
ANISOU 2221  CB  ASP A 289     3331   3484   4779    -59    385   -468       C  
ATOM   2222  CG  ASP A 289     -16.283  11.387  22.318  1.00 31.09           C  
ANISOU 2222  CG  ASP A 289     3417   3539   4858    -81    382   -342       C  
ATOM   2223  OD1 ASP A 289     -15.178  11.076  21.824  1.00 33.10           O  
ANISOU 2223  OD1 ASP A 289     3680   3811   5085   -116    383   -293       O  
ATOM   2224  OD2 ASP A 289     -17.321  11.510  21.634  1.00 32.62           O  
ANISOU 2224  OD2 ASP A 289     3608   3708   5080    -62    376   -300       O  
ATOM   2225  N   GLU A 290     -14.382   8.577  24.186  1.00 30.16           N  
ANISOU 2225  N   GLU A 290     3371   3631   4458    -88    400   -418       N  
ATOM   2226  CA  GLU A 290     -14.398   7.174  23.795  1.00 31.03           C  
ANISOU 2226  CA  GLU A 290     3525   3798   4466    -84    404   -364       C  
ATOM   2227  C   GLU A 290     -14.146   6.239  24.974  1.00 30.87           C  
ANISOU 2227  C   GLU A 290     3557   3833   4340    -74    388   -413       C  
ATOM   2228  O   GLU A 290     -13.715   5.098  24.777  1.00 29.30           O  
ANISOU 2228  O   GLU A 290     3402   3666   4064    -66    368   -380       O  
ATOM   2229  CB  GLU A 290     -13.386   6.923  22.676  1.00 33.39           C  
ANISOU 2229  CB  GLU A 290     3811   4102   4774    -93    396   -304       C  
ATOM   2230  CG  GLU A 290     -13.663   7.732  21.416  1.00 33.55           C  
ANISOU 2230  CG  GLU A 290     3801   4074   4872   -115    410   -234       C  
ATOM   2231  CD  GLU A 290     -13.654   6.886  20.157  1.00 35.77           C  
ANISOU 2231  CD  GLU A 290     4101   4390   5099   -116    420   -155       C  
ATOM   2232  OE1 GLU A 290     -12.982   5.833  20.148  1.00 36.46           O  
ANISOU 2232  OE1 GLU A 290     4207   4532   5114   -100    412   -163       O  
ATOM   2233  OE2 GLU A 290     -14.324   7.272  19.176  1.00 34.60           O  
ANISOU 2233  OE2 GLU A 290     3952   4212   4982   -127    428    -89       O  
ATOM   2234  N   PHE A 291     -14.407   6.701  26.195  1.00 29.72           N  
ANISOU 2234  N   PHE A 291     3414   3696   4184    -73    390   -492       N  
ATOM   2235  CA  PHE A 291     -14.355   5.873  27.394  1.00 32.77           C  
ANISOU 2235  CA  PHE A 291     3863   4136   4452    -74    376   -532       C  
ATOM   2236  C   PHE A 291     -15.741   5.844  28.019  1.00 33.44           C  
ANISOU 2236  C   PHE A 291     3961   4254   4491    -92    425   -557       C  
ATOM   2237  O   PHE A 291     -16.236   6.877  28.482  1.00 34.15           O  
ANISOU 2237  O   PHE A 291     4003   4335   4638    -86    449   -628       O  
ATOM   2238  CB  PHE A 291     -13.337   6.409  28.404  1.00 34.82           C  
ANISOU 2238  CB  PHE A 291     4116   4398   4717    -62    335   -616       C  
ATOM   2239  CG  PHE A 291     -11.909   6.296  27.957  1.00 34.08           C  
ANISOU 2239  CG  PHE A 291     3999   4293   4656    -48    286   -606       C  
ATOM   2240  CD1 PHE A 291     -11.208   5.113  28.123  1.00 36.93           C  
ANISOU 2240  CD1 PHE A 291     4414   4689   4930    -27    237   -589       C  
ATOM   2241  CD2 PHE A 291     -11.261   7.379  27.389  1.00 36.49           C  
ANISOU 2241  CD2 PHE A 291     4227   4554   5082    -59    284   -619       C  
ATOM   2242  CE1 PHE A 291      -9.891   5.009  27.719  1.00 38.02           C  
ANISOU 2242  CE1 PHE A 291     4511   4831   5104     -5    193   -598       C  
ATOM   2243  CE2 PHE A 291      -9.943   7.282  26.983  1.00 39.75           C  
ANISOU 2243  CE2 PHE A 291     4602   4976   5525    -56    250   -618       C  
ATOM   2244  CZ  PHE A 291      -9.258   6.096  27.148  1.00 37.58           C  
ANISOU 2244  CZ  PHE A 291     4363   4749   5165    -24    206   -615       C  
ATOM   2245  N   THR A 292     -16.365   4.669  28.035  1.00 28.04           N  
ANISOU 2245  N   THR A 292     3336   3609   3707   -116    438   -506       N  
ATOM   2246  CA  THR A 292     -17.639   4.521  28.716  1.00 29.84           C  
ANISOU 2246  CA  THR A 292     3572   3891   3875   -150    493   -532       C  
ATOM   2247  C   THR A 292     -17.429   4.570  30.228  1.00 29.19           C  
ANISOU 2247  C   THR A 292     3532   3862   3699   -164    493   -610       C  
ATOM   2248  O   THR A 292     -16.307   4.403  30.713  1.00 29.52           O  
ANISOU 2248  O   THR A 292     3617   3894   3703   -147    436   -624       O  
ATOM   2249  CB  THR A 292     -18.310   3.205  28.327  1.00 32.06           C  
ANISOU 2249  CB  THR A 292     3911   4196   4074   -191    503   -450       C  
ATOM   2250  OG1 THR A 292     -17.575   2.108  28.885  1.00 29.68           O  
ANISOU 2250  OG1 THR A 292     3715   3904   3659   -204    454   -420       O  
ATOM   2251  CG2 THR A 292     -18.370   3.058  26.816  1.00 30.54           C  
ANISOU 2251  CG2 THR A 292     3690   3956   3959   -173    491   -377       C  
ATOM   2252  N   PRO A 293     -18.494   4.823  30.996  1.00 26.54           N  
ANISOU 2252  N   PRO A 293     3176   3589   3320   -193    556   -669       N  
ATOM   2253  CA  PRO A 293     -18.372   4.683  32.457  1.00 29.39           C  
ANISOU 2253  CA  PRO A 293     3595   4019   3553   -219    562   -734       C  
ATOM   2254  C   PRO A 293     -17.888   3.307  32.879  1.00 29.68           C  
ANISOU 2254  C   PRO A 293     3759   4074   3442   -258    518   -658       C  
ATOM   2255  O   PRO A 293     -17.135   3.190  33.854  1.00 31.67           O  
ANISOU 2255  O   PRO A 293     4078   4346   3608   -255    472   -691       O  
ATOM   2256  CB  PRO A 293     -19.796   4.970  32.950  1.00 29.00           C  
ANISOU 2256  CB  PRO A 293     3493   4052   3474   -255    655   -795       C  
ATOM   2257  CG  PRO A 293     -20.363   5.878  31.915  1.00 28.61           C  
ANISOU 2257  CG  PRO A 293     3330   3949   3591   -210    673   -812       C  
ATOM   2258  CD  PRO A 293     -19.784   5.419  30.605  1.00 28.58           C  
ANISOU 2258  CD  PRO A 293     3345   3862   3651   -194    620   -699       C  
ATOM   2259  N   PHE A 294     -18.301   2.258  32.163  1.00 37.58           N  
ANISOU 2259  N   PHE A 294     4802   5060   4416   -292    518   -558       N  
ATOM   2260  CA  PHE A 294     -17.795   0.919  32.447  1.00 36.59           C  
ANISOU 2260  CA  PHE A 294     4809   4925   4169   -320    455   -480       C  
ATOM   2261  C   PHE A 294     -16.295   0.834  32.197  1.00 36.88           C  
ANISOU 2261  C   PHE A 294     4871   4898   4244   -248    354   -475       C  
ATOM   2262  O   PHE A 294     -15.562   0.225  32.984  1.00 38.89           O  
ANISOU 2262  O   PHE A 294     5223   5154   4399   -244    282   -469       O  
ATOM   2263  CB  PHE A 294     -18.545  -0.111  31.600  1.00 40.48           C  
ANISOU 2263  CB  PHE A 294     5333   5398   4649   -366    468   -383       C  
ATOM   2264  CG  PHE A 294     -18.138  -1.535  31.865  1.00 43.81           C  
ANISOU 2264  CG  PHE A 294     5903   5790   4954   -398    394   -300       C  
ATOM   2265  CD1 PHE A 294     -18.796  -2.289  32.823  1.00 46.83           C  
ANISOU 2265  CD1 PHE A 294     6385   6222   5186   -494    417   -266       C  
ATOM   2266  CD2 PHE A 294     -17.113  -2.125  31.144  1.00 43.73           C  
ANISOU 2266  CD2 PHE A 294     5932   5702   4981   -334    300   -259       C  
ATOM   2267  CE1 PHE A 294     -18.430  -3.599  33.065  1.00 47.00           C  
ANISOU 2267  CE1 PHE A 294     6560   6195   5103   -526    334   -180       C  
ATOM   2268  CE2 PHE A 294     -16.744  -3.434  31.382  1.00 43.40           C  
ANISOU 2268  CE2 PHE A 294     6030   5616   4842   -350    216   -191       C  
ATOM   2269  CZ  PHE A 294     -17.402  -4.173  32.344  1.00 49.06           C  
ANISOU 2269  CZ  PHE A 294     6863   6364   5416   -446    226   -146       C  
ATOM   2270  N   ASP A 295     -15.822   1.435  31.100  1.00 31.97           N  
ANISOU 2270  N   ASP A 295     4160   4226   3763   -193    345   -478       N  
ATOM   2271  CA  ASP A 295     -14.393   1.417  30.798  1.00 31.27           C  
ANISOU 2271  CA  ASP A 295     4068   4095   3720   -131    262   -485       C  
ATOM   2272  C   ASP A 295     -13.583   2.065  31.913  1.00 34.71           C  
ANISOU 2272  C   ASP A 295     4503   4551   4135   -110    223   -572       C  
ATOM   2273  O   ASP A 295     -12.511   1.571  32.280  1.00 34.43           O  
ANISOU 2273  O   ASP A 295     4517   4505   4059    -74    134   -578       O  
ATOM   2274  CB  ASP A 295     -14.125   2.126  29.469  1.00 31.41           C  
ANISOU 2274  CB  ASP A 295     3980   4071   3884    -98    281   -476       C  
ATOM   2275  CG  ASP A 295     -14.690   1.377  28.279  1.00 30.36           C  
ANISOU 2275  CG  ASP A 295     3856   3917   3764   -107    297   -393       C  
ATOM   2276  OD1 ASP A 295     -14.984   0.171  28.416  1.00 32.43           O  
ANISOU 2276  OD1 ASP A 295     4210   4180   3931   -129    272   -342       O  
ATOM   2277  OD2 ASP A 295     -14.842   1.998  27.205  1.00 28.80           O  
ANISOU 2277  OD2 ASP A 295     3580   3697   3667    -96    329   -377       O  
ATOM   2278  N   VAL A 296     -14.082   3.174  32.462  1.00 30.51           N  
ANISOU 2278  N   VAL A 296     3912   4047   3635   -123    278   -648       N  
ATOM   2279  CA  VAL A 296     -13.361   3.871  33.522  1.00 32.02           C  
ANISOU 2279  CA  VAL A 296     4099   4257   3809   -104    239   -745       C  
ATOM   2280  C   VAL A 296     -13.366   3.045  34.803  1.00 34.45           C  
ANISOU 2280  C   VAL A 296     4531   4620   3938   -131    203   -746       C  
ATOM   2281  O   VAL A 296     -12.330   2.881  35.459  1.00 37.23           O  
ANISOU 2281  O   VAL A 296     4930   4974   4244   -101    114   -777       O  
ATOM   2282  CB  VAL A 296     -13.965   5.269  33.747  1.00 29.13           C  
ANISOU 2282  CB  VAL A 296     3642   3897   3527   -106    304   -837       C  
ATOM   2283  CG1 VAL A 296     -13.261   5.972  34.894  1.00 31.30           C  
ANISOU 2283  CG1 VAL A 296     3919   4193   3779    -88    259   -948       C  
ATOM   2284  CG2 VAL A 296     -13.879   6.093  32.471  1.00 30.54           C  
ANISOU 2284  CG2 VAL A 296     3718   4005   3881    -83    321   -820       C  
ATOM   2285  N   VAL A 297     -14.532   2.515  35.180  1.00 37.34           N  
ANISOU 2285  N   VAL A 297     4954   5037   4197   -195    269   -710       N  
ATOM   2286  CA  VAL A 297     -14.620   1.676  36.372  1.00 43.56           C  
ANISOU 2286  CA  VAL A 297     5876   5880   4795   -242    241   -691       C  
ATOM   2287  C   VAL A 297     -13.776   0.418  36.201  1.00 45.87           C  
ANISOU 2287  C   VAL A 297     6279   6117   5030   -221    128   -602       C  
ATOM   2288  O   VAL A 297     -13.132  -0.050  37.148  1.00 50.28           O  
ANISOU 2288  O   VAL A 297     6944   6687   5472   -215     41   -605       O  
ATOM   2289  CB  VAL A 297     -16.092   1.340  36.681  1.00 41.72           C  
ANISOU 2289  CB  VAL A 297     5668   5718   4465   -332    348   -663       C  
ATOM   2290  CG1 VAL A 297     -16.189   0.234  37.722  1.00 45.09           C  
ANISOU 2290  CG1 VAL A 297     6259   6190   4685   -404    316   -603       C  
ATOM   2291  CG2 VAL A 297     -16.831   2.583  37.151  1.00 42.27           C  
ANISOU 2291  CG2 VAL A 297     5634   5857   4569   -338    445   -782       C  
ATOM   2292  N   ARG A 298     -13.760  -0.141  34.988  1.00 47.09           N  
ANISOU 2292  N   ARG A 298     6414   6210   5267   -202    118   -529       N  
ATOM   2293  CA  ARG A 298     -12.942  -1.321  34.721  1.00 50.29           C  
ANISOU 2293  CA  ARG A 298     6914   6556   5639   -165      5   -461       C  
ATOM   2294  C   ARG A 298     -11.466  -1.042  34.975  1.00 50.31           C  
ANISOU 2294  C   ARG A 298     6895   6538   5682    -78   -104   -525       C  
ATOM   2295  O   ARG A 298     -10.743  -1.904  35.488  1.00 52.33           O  
ANISOU 2295  O   ARG A 298     7258   6770   5855    -47   -221   -502       O  
ATOM   2296  CB  ARG A 298     -13.152  -1.791  33.282  1.00 48.42           C  
ANISOU 2296  CB  ARG A 298     6635   6264   5498   -149     21   -398       C  
ATOM   2297  N   GLN A 299     -11.002   0.156  34.627  1.00 54.89           N  
ANISOU 2297  N   GLN A 299     7338   7125   6393    -42    -75   -605       N  
ATOM   2298  CA  GLN A 299      -9.596   0.507  34.766  1.00 55.26           C  
ANISOU 2298  CA  GLN A 299     7336   7160   6499     30   -169   -673       C  
ATOM   2299  C   GLN A 299      -9.244   1.064  36.141  1.00 58.73           C  
ANISOU 2299  C   GLN A 299     7806   7645   6864     28   -212   -758       C  
ATOM   2300  O   GLN A 299      -8.065   1.327  36.400  1.00 62.36           O  
ANISOU 2300  O   GLN A 299     8230   8101   7365     83   -303   -823       O  
ATOM   2301  CB  GLN A 299      -9.199   1.520  33.684  1.00 53.99           C  
ANISOU 2301  CB  GLN A 299     7015   6980   6517     54   -121   -712       C  
ATOM   2302  CG  GLN A 299      -7.709   1.545  33.371  1.00 52.65           C  
ANISOU 2302  CG  GLN A 299     6780   6798   6426    122   -212   -758       C  
ATOM   2303  CD  GLN A 299      -7.400   2.168  32.026  1.00 49.16           C  
ANISOU 2303  CD  GLN A 299     6203   6339   6138    127   -156   -755       C  
ATOM   2304  OE1 GLN A 299      -6.323   2.726  31.823  1.00 49.04           O  
ANISOU 2304  OE1 GLN A 299     6091   6330   6213    153   -190   -815       O  
ATOM   2305  NE2 GLN A 299      -8.343   2.070  31.096  1.00 47.37           N  
ANISOU 2305  NE2 GLN A 299     5969   6094   5935     96    -71   -684       N  
ATOM   2306  N   CYS A 300     -10.222   1.253  37.028  1.00 67.42           N  
ANISOU 2306  N   CYS A 300     8966   8796   7854    -36   -148   -767       N  
ATOM   2307  CA  CYS A 300      -9.949   1.756  38.367  1.00 69.24           C  
ANISOU 2307  CA  CYS A 300     9236   9081   7992    -41   -185   -854       C  
ATOM   2308  C   CYS A 300     -10.200   0.737  39.471  1.00 71.42           C  
ANISOU 2308  C   CYS A 300     9690   9395   8054    -81   -237   -801       C  
ATOM   2309  O   CYS A 300      -9.730   0.944  40.596  1.00 75.59           O  
ANISOU 2309  O   CYS A 300    10274   9965   8483    -73   -303   -863       O  
ATOM   2310  CB  CYS A 300     -10.771   3.026  38.640  1.00 68.43           C  
ANISOU 2310  CB  CYS A 300     9047   9024   7931    -76    -69   -942       C  
ATOM   2311  SG  CYS A 300     -10.414   4.398  37.509  1.00 70.84           S  
ANISOU 2311  SG  CYS A 300     9163   9269   8484    -38    -28  -1006       S  
ATOM   2312  N   SER A 301     -10.924  -0.347  39.187  1.00 71.89           N  
ANISOU 2312  N   SER A 301     9844   9437   8034   -131   -214   -685       N  
ATOM   2313  CA  SER A 301     -11.065  -1.461  40.115  1.00 75.32           C  
ANISOU 2313  CA  SER A 301    10467   9883   8267   -178   -282   -608       C  
ATOM   2314  C   SER A 301     -10.358  -2.720  39.627  1.00 75.98           C  
ANISOU 2314  C   SER A 301    10644   9873   8353   -127   -416   -517       C  
ATOM   2315  O   SER A 301     -10.362  -3.734  40.334  1.00 78.89           O  
ANISOU 2315  O   SER A 301    11188  10224   8564   -159   -502   -440       O  
ATOM   2316  CB  SER A 301     -12.548  -1.759  40.371  1.00 74.35           C  
ANISOU 2316  CB  SER A 301    10400   9819   8030   -299   -152   -548       C  
ATOM   2317  OG  SER A 301     -13.086  -2.620  39.379  1.00 75.02           O  
ANISOU 2317  OG  SER A 301    10502   9843   8158   -327   -127   -442       O  
TER    2318      SER A 301                                                      
HETATM 2319  C1  NNA A 401     -16.908   3.554  -0.184  1.00 34.67           C  
ANISOU 2319  C1  NNA A 401     4483   4872   3820   -299    362    816       C  
HETATM 2320  O2  NNA A 401     -17.315   3.223  -1.312  1.00 35.83           O  
ANISOU 2320  O2  NNA A 401     4690   5077   3849   -297    328    846       O  
HETATM 2321  N3  NNA A 401     -17.628   4.303   0.679  1.00 34.73           N  
ANISOU 2321  N3  NNA A 401     4477   4748   3971   -289    310    847       N  
HETATM 2322  C4  NNA A 401     -18.967   4.874   0.431  1.00 35.98           C  
ANISOU 2322  C4  NNA A 401     4678   4812   4180   -271    206    919       C  
HETATM 2323  C5  NNA A 401     -19.990   3.751   0.189  1.00 32.54           C  
ANISOU 2323  C5  NNA A 401     4255   4397   3711   -207    139    858       C  
HETATM 2324  C6  NNA A 401     -19.419   5.701   1.646  1.00 33.56           C  
ANISOU 2324  C6  NNA A 401     4328   4376   4047   -256    178    915       C  
HETATM 2325  C7  NNA A 401     -20.240   2.905   1.428  1.00 32.14           C  
ANISOU 2325  C7  NNA A 401     4146   4317   3748   -158    147    744       C  
HETATM 2326  C8  NNA A 401     -19.674   4.844   2.878  1.00 32.98           C  
ANISOU 2326  C8  NNA A 401     4192   4290   4049   -201    191    794       C  
HETATM 2327  C9  NNA A 401     -20.698   3.768   2.586  1.00 32.58           C  
ANISOU 2327  C9  NNA A 401     4154   4264   3960   -152    132    748       C  
HETATM 2328  C10 NNA A 401     -18.907   5.781  -0.822  1.00 38.10           C  
ANISOU 2328  C10 NNA A 401     5025   5092   4360   -335    182   1056       C  
HETATM 2329  S11 NNA A 401     -17.820   7.189  -0.787  1.00 39.11           S  
ANISOU 2329  S11 NNA A 401     5160   5186   4516   -440    245   1158       S  
HETATM 2330  O12 NNA A 401     -16.570   6.802  -0.204  1.00 38.65           O  
ANISOU 2330  O12 NNA A 401     5028   5203   4453   -464    358   1076       O  
HETATM 2331  O13 NNA A 401     -18.531   8.311  -0.250  1.00 41.22           O  
ANISOU 2331  O13 NNA A 401     5438   5296   4929   -432    166   1218       O  
HETATM 2332  C14 NNA A 401     -17.471   7.606  -2.502  1.00 41.41           C  
ANISOU 2332  C14 NNA A 401     5555   5566   4615   -531    252   1298       C  
HETATM 2333  C15 NNA A 401     -18.738   8.170  -3.137  1.00 43.56           C  
ANISOU 2333  C15 NNA A 401     5914   5743   4893   -507    114   1401       C  
HETATM 2334  C16 NNA A 401     -17.055   6.336  -3.235  1.00 42.34           C  
ANISOU 2334  C16 NNA A 401     5668   5854   4567   -513    311   1219       C  
HETATM 2335  C17 NNA A 401     -16.355   8.640  -2.558  1.00 43.61           C  
ANISOU 2335  C17 NNA A 401     5836   5843   4891   -649    330   1383       C  
HETATM 2336  N18 NNA A 401     -15.693   3.171   0.266  1.00 33.99           N  
ANISOU 2336  N18 NNA A 401     4335   4854   3724   -304    450    736       N  
HETATM 2337  C19 NNA A 401     -14.894   2.209  -0.475  1.00 33.74           C  
ANISOU 2337  C19 NNA A 401     4295   4968   3556   -290    506    662       C  
HETATM 2338  C20 NNA A 401     -13.475   2.714  -0.788  1.00 35.68           C  
ANISOU 2338  C20 NNA A 401     4492   5321   3746   -364    617    671       C  
HETATM 2339  C21 NNA A 401     -13.547   3.918  -1.731  1.00 36.16           C  
ANISOU 2339  C21 NNA A 401     4611   5386   3743   -469    628    826       C  
HETATM 2340  C22 NNA A 401     -12.741   3.141   0.486  1.00 35.59           C  
ANISOU 2340  C22 NNA A 401     4399   5256   3868   -375    657    632       C  
HETATM 2341  C23 NNA A 401     -12.668   1.609  -1.476  1.00 36.00           C  
ANISOU 2341  C23 NNA A 401     4505   5522   3651   -329    675    561       C  
HETATM 2342  C24 NNA A 401     -14.924   0.871   0.263  1.00 34.20           C  
ANISOU 2342  C24 NNA A 401     4325   5023   3647   -199    485    523       C  
HETATM 2343  O25 NNA A 401     -14.413   0.730   1.370  1.00 32.04           O  
ANISOU 2343  O25 NNA A 401     3996   4715   3464   -176    507    459       O  
HETATM 2344  N26 NNA A 401     -15.562  -0.146  -0.337  1.00 33.08           N  
ANISOU 2344  N26 NNA A 401     4230   4907   3431   -147    431    477       N  
HETATM 2345  C27 NNA A 401     -16.217  -0.089  -1.651  1.00 34.29           C  
ANISOU 2345  C27 NNA A 401     4455   5106   3469   -164    390    540       C  
HETATM 2346  C28 NNA A 401     -15.631  -1.457   0.308  1.00 31.89           C  
ANISOU 2346  C28 NNA A 401     4071   4736   3309    -68    397    354       C  
HETATM 2347  C29 NNA A 401     -16.673  -2.214  -0.495  1.00 31.88           C  
ANISOU 2347  C29 NNA A 401     4138   4736   3241    -38    316    344       C  
HETATM 2348  C30 NNA A 401     -16.961  -1.406  -1.746  1.00 34.53           C  
ANISOU 2348  C30 NNA A 401     4517   5125   3477    -91    315    450       C  
HETATM 2349  C31 NNA A 401     -18.060  -1.671  -0.754  1.00 32.88           C  
ANISOU 2349  C31 NNA A 401     4307   4787   3399    -60    237    438       C  
HETATM 2350  C32 NNA A 401     -19.142  -2.653  -1.148  1.00 33.16           C  
ANISOU 2350  C32 NNA A 401     4390   4802   3409    -23    144    396       C  
HETATM 2351  C33 NNA A 401     -18.577  -0.568   0.144  1.00 32.19           C  
ANISOU 2351  C33 NNA A 401     4191   4592   3447    -91    226    516       C  
HETATM 2352  C34 NNA A 401     -14.285  -2.171   0.227  1.00 36.00           C  
ANISOU 2352  C34 NNA A 401     4545   5363   3770    -32    463    242       C  
HETATM 2353  O35 NNA A 401     -13.766  -2.415  -0.861  1.00 34.57           O  
ANISOU 2353  O35 NNA A 401     4368   5304   3461    -35    502    216       O  
HETATM 2354  N36 NNA A 401     -13.718  -2.477   1.394  1.00 31.49           N  
ANISOU 2354  N36 NNA A 401     3925   4751   3290      3    472    172       N  
HETATM 2355  C37 NNA A 401     -12.340  -2.983   1.483  1.00 33.69           C  
ANISOU 2355  C37 NNA A 401     4138   5124   3540     42    529     62       C  
HETATM 2356  C38 NNA A 401     -11.454  -1.962   2.201  1.00 34.00           C  
ANISOU 2356  C38 NNA A 401     4097   5167   3654    -10    598     91       C  
HETATM 2357  C39 NNA A 401     -11.399  -0.619   1.510  1.00 36.49           C  
ANISOU 2357  C39 NNA A 401     4407   5520   3938   -116    658    215       C  
HETATM 2358  C40 NNA A 401     -10.717   0.437   2.344  1.00 38.81           C  
ANISOU 2358  C40 NNA A 401     4633   5782   4331   -176    706    250       C  
HETATM 2359  C41 NNA A 401      -9.306   0.088   2.752  1.00 42.23           C  
ANISOU 2359  C41 NNA A 401     4965   6306   4773   -151    765    136       C  
HETATM 2360  O42 NNA A 401     -13.289  -5.216   1.656  1.00 31.19           O  
ANISOU 2360  O42 NNA A 401     3918   4721   3212    172    386    -74       O  
HETATM 2361  C43 NNA A 401     -12.282  -4.356   2.179  1.00 32.25           C  
ANISOU 2361  C43 NNA A 401     3970   4892   3390    140    464    -61       C  
HETATM 2362  O44 NNA A 401     -10.118  -4.971   2.949  1.00 35.77           O  
ANISOU 2362  O44 NNA A 401     4290   5434   3867    228    516   -242       O  
HETATM 2363  N45 NNA A 401     -10.648  -5.498   0.811  1.00 35.76           N  
ANISOU 2363  N45 NNA A 401     4354   5563   3671    229    527   -250       N  
HETATM 2364  C46 NNA A 401      -9.382  -6.119   0.528  1.00 35.68           C  
ANISOU 2364  C46 NNA A 401     4269   5675   3613    297    569   -393       C  
HETATM 2365  C47 NNA A 401      -8.455  -5.405  -0.391  1.00 37.84           C  
ANISOU 2365  C47 NNA A 401     4459   6127   3791    237    692   -391       C  
HETATM 2366  C48 NNA A 401      -9.155  -6.634  -0.849  1.00 35.08           C  
ANISOU 2366  C48 NNA A 401     4198   5741   3390    324    601   -466       C  
HETATM 2367  C49 NNA A 401     -10.918  -4.971   2.009  1.00 34.72           C  
ANISOU 2367  C49 NNA A 401     4217   5315   3660    201    506   -190       C  
HETATM 2368  O   HOH A 501      -8.272  13.701  42.776  1.00 56.94           O  
ANISOU 2368  O   HOH A 501     7019   7464   7151     55   -216  -2138       O  
HETATM 2369  O   HOH A 502       0.554   2.321  39.506  1.00 50.58           O  
ANISOU 2369  O   HOH A 502     6428   6704   6086    490  -1158  -1411       O  
HETATM 2370  O   HOH A 503     -11.089   4.739  21.019  1.00 32.94           O  
ANISOU 2370  O   HOH A 503     3759   4159   4600    -62    369   -248       O  
HETATM 2371  O   HOH A 504     -23.766 -21.045   4.355  1.00 42.18           O  
ANISOU 2371  O   HOH A 504     6502   4579   4944    -28  -1037   -483       O  
HETATM 2372  O   HOH A 505      -8.324  12.959  23.593  1.00 55.00           O  
ANISOU 2372  O   HOH A 505     6270   6598   8030   -310    299   -501       O  
HETATM 2373  O   HOH A 506     -22.948 -28.093  10.934  1.00 59.76           O  
ANISOU 2373  O   HOH A 506     9807   5524   7377   -355  -1778   -248       O  
HETATM 2374  O   HOH A 507      -4.716  24.183  36.642  1.00 59.13           O  
ANISOU 2374  O   HOH A 507     6685   6395   9388   -323   -521  -2258       O  
HETATM 2375  O   HOH A 508     -24.928 -14.700  11.530  1.00 42.20           O  
ANISOU 2375  O   HOH A 508     6030   4896   5109   -426   -360     70       O  
HETATM 2376  O   HOH A 509     -27.695  18.150  22.464  1.00 46.54           O  
ANISOU 2376  O   HOH A 509     4854   5082   7749    611     40   -993       O  
HETATM 2377  O   HOH A 510     -28.324   0.717   6.736  1.00 33.71           O  
ANISOU 2377  O   HOH A 510     3980   4290   4539    -57    -96    372       O  
HETATM 2378  O   HOH A 511     -27.816  26.100  35.541  1.00 56.94           O  
ANISOU 2378  O   HOH A 511     5800   6600   9235   1144     74  -3064       O  
HETATM 2379  O   HOH A 512     -30.102  -5.413   7.127  1.00 48.98           O  
ANISOU 2379  O   HOH A 512     6022   6288   6298   -283   -166    195       O  
HETATM 2380  O   HOH A 513     -11.467   5.431  17.743  1.00 48.88           O  
ANISOU 2380  O   HOH A 513     5736   6181   6655   -125    443    -75       O  
HETATM 2381  O   HOH A 514     -12.921 -24.197  -0.763  1.00 46.39           O  
ANISOU 2381  O   HOH A 514     6900   5603   5122   1427  -1180  -1846       O  
HETATM 2382  O   HOH A 515     -28.971  -1.248   9.087  1.00 58.20           O  
ANISOU 2382  O   HOH A 515     7032   7429   7653   -163      2    239       O  
HETATM 2383  O   HOH A 516      -9.528 -18.874  19.869  1.00 42.27           O  
ANISOU 2383  O   HOH A 516     6694   4318   5051    834  -1300   -432       O  
HETATM 2384  O   HOH A 517     -11.738   0.344   5.256  1.00 53.88           O  
ANISOU 2384  O   HOH A 517     6550   7423   6497   -100    586    211       O  
HETATM 2385  O   HOH A 518     -27.375   4.859   2.422  1.00 44.45           O  
ANISOU 2385  O   HOH A 518     5541   5529   5817     31   -321    750       O  
HETATM 2386  O   HOH A 519     -21.315   1.314  10.545  1.00 28.17           O  
ANISOU 2386  O   HOH A 519     3380   3566   3757    -83    261    304       O  
HETATM 2387  O   HOH A 520     -28.871  -7.981  14.798  1.00 65.52           O  
ANISOU 2387  O   HOH A 520     8282   8300   8313   -625    148    146       O  
HETATM 2388  O   HOH A 521     -24.239   7.826  22.169  1.00 45.64           O  
ANISOU 2388  O   HOH A 521     5136   5704   6501    -17    512   -392       O  
HETATM 2389  O   HOH A 522     -18.826  17.938  19.355  1.00 45.66           O  
ANISOU 2389  O   HOH A 522     5276   4691   7382      0     63   -202       O  
HETATM 2390  O   HOH A 523     -19.546 -29.103   8.791  1.00 62.56           O  
ANISOU 2390  O   HOH A 523    10176   5840   7753    306  -2017   -716       O  
HETATM 2391  O   HOH A 524     -19.098  26.280  35.314  1.00 59.11           O  
ANISOU 2391  O   HOH A 524     6635   6228   9597    648   -166  -2662       O  
HETATM 2392  O   HOH A 525     -15.130  18.569  22.804  1.00 45.33           O  
ANISOU 2392  O   HOH A 525     5178   4695   7351   -131    124   -499       O  
HETATM 2393  O   HOH A 526     -23.421  -9.019  16.341  1.00 31.07           O  
ANISOU 2393  O   HOH A 526     4270   3763   3772   -394     79    147       O  
HETATM 2394  O   HOH A 527     -28.039  -8.865 -12.624  1.00 53.03           O  
ANISOU 2394  O   HOH A 527     7531   7696   4921    133  -1023     62       O  
HETATM 2395  O   HOH A 528     -14.071  23.803  33.960  1.00 60.26           O  
ANISOU 2395  O   HOH A 528     6942   6467   9487    179   -144  -2052       O  
HETATM 2396  O   HOH A 529     -10.696  -9.772  13.685  1.00 33.92           O  
ANISOU 2396  O   HOH A 529     4484   4311   4092    495   -128   -398       O  
HETATM 2397  O   HOH A 530     -15.219  -2.007  25.555  1.00 31.58           O  
ANISOU 2397  O   HOH A 530     4157   3997   3845   -102    222   -190       O  
HETATM 2398  O   HOH A 531     -27.136   7.839  17.796  1.00 36.71           O  
ANISOU 2398  O   HOH A 531     3917   4496   5536     61    332   -188       O  
HETATM 2399  O   HOH A 532      -6.742  22.707  23.999  1.00 48.26           O  
ANISOU 2399  O   HOH A 532     5397   4772   8168   -767    -29   -608       O  
HETATM 2400  O   HOH A 533     -26.861  -2.495  -5.667  1.00 55.04           O  
ANISOU 2400  O   HOH A 533     7358   7481   6074      5   -546    607       O  
HETATM 2401  O   HOH A 534     -14.102  12.637  19.878  1.00 42.19           O  
ANISOU 2401  O   HOH A 534     4822   4837   6372   -204    354   -145       O  
HETATM 2402  O   HOH A 535      -3.698   3.006  24.171  1.00 32.79           O  
ANISOU 2402  O   HOH A 535     3507   4375   4576    143     62   -687       O  
HETATM 2403  O   HOH A 536     -27.504  -0.014  17.702  1.00 33.75           O  
ANISOU 2403  O   HOH A 536     3826   4394   4604   -300    426    -23       O  
HETATM 2404  O   HOH A 537      -4.609 -17.621   8.217  1.00 53.38           O  
ANISOU 2404  O   HOH A 537     6881   6930   6471   1562   -682  -1544       O  
HETATM 2405  O   HOH A 538     -24.060  10.044  39.947  1.00 43.82           O  
ANISOU 2405  O   HOH A 538     4978   6591   5079   -196   1101  -1858       O  
HETATM 2406  O   HOH A 539     -12.284 -30.006  14.756  1.00 49.25           O  
ANISOU 2406  O   HOH A 539     8758   3822   6134   1078  -2525   -758       O  
HETATM 2407  O   HOH A 540     -14.448   5.082  17.057  1.00 31.84           O  
ANISOU 2407  O   HOH A 540     3664   3962   4471   -110    435     18       O  
HETATM 2408  O   HOH A 541     -21.030 -20.529  13.608  1.00 48.62           O  
ANISOU 2408  O   HOH A 541     7586   5056   5832   -215   -915    -41       O  
HETATM 2409  O   HOH A 542     -21.068 -25.339  -5.336  1.00 52.71           O  
ANISOU 2409  O   HOH A 542     8067   6251   5709    784  -1514  -1634       O  
HETATM 2410  O   HOH A 543     -14.431   9.302  27.376  1.00 29.39           O  
ANISOU 2410  O   HOH A 543     3283   3573   4311    -64    384   -655       O  
HETATM 2411  O   HOH A 544      -2.411 -16.562  19.252  1.00 48.54           O  
ANISOU 2411  O   HOH A 544     6644   5686   6112   1533  -1318  -1118       O  
HETATM 2412  O   HOH A 545     -17.946  10.124  11.721  1.00 36.26           O  
ANISOU 2412  O   HOH A 545     4286   4202   5291   -200    296    461       O  
HETATM 2413  O   HOH A 546     -10.729 -23.563   0.863  1.00 44.49           O  
ANISOU 2413  O   HOH A 546     6503   5423   4980   1573  -1110  -1877       O  
HETATM 2414  O   HOH A 547     -21.801   3.422  -8.557  1.00 52.15           O  
ANISOU 2414  O   HOH A 547     7278   7318   5217   -306   -191   1259       O  
HETATM 2415  O   HOH A 548     -25.124   8.247  10.225  1.00 38.66           O  
ANISOU 2415  O   HOH A 548     4513   4544   5633     40     37    413       O  
HETATM 2416  O   HOH A 549     -10.837   0.764  30.175  1.00 43.35           O  
ANISOU 2416  O   HOH A 549     5582   5564   5326     22     46   -518       O  
HETATM 2417  O   HOH A 550     -11.134  -2.851  27.135  1.00 39.08           O  
ANISOU 2417  O   HOH A 550     5181   4926   4740     85    -35   -320       O  
HETATM 2418  O   HOH A 551     -19.050  -1.211  25.707  1.00 37.96           O  
ANISOU 2418  O   HOH A 551     4877   4883   4665   -268    413   -162       O  
HETATM 2419  O   HOH A 552     -20.643   1.869  30.654  1.00 38.91           O  
ANISOU 2419  O   HOH A 552     4870   5253   4661   -358    630   -484       O  
HETATM 2420  O   HOH A 553      -2.293 -22.630   0.807  1.00 72.13           O  
ANISOU 2420  O   HOH A 553     9039   9795   8572   2240   -816  -2609       O  
HETATM 2421  O   HOH A 554     -19.860  -6.661  22.312  1.00 33.79           O  
ANISOU 2421  O   HOH A 554     4663   4168   4008   -327    192     69       O  
HETATM 2422  O   HOH A 555     -22.809   1.971  36.381  1.00 38.34           O  
ANISOU 2422  O   HOH A 555     4897   5654   4018   -625    904   -758       O  
HETATM 2423  O   HOH A 556     -26.755  -3.120   2.125  1.00 31.66           O  
ANISOU 2423  O   HOH A 556     4044   4197   3788    -58   -232    389       O  
HETATM 2424  O   HOH A 557     -31.840  -9.902  13.759  1.00 46.16           O  
ANISOU 2424  O   HOH A 557     5771   5867   5900   -857     54    134       O  
HETATM 2425  O   HOH A 558      -6.288   4.642  37.108  1.00 49.83           O  
ANISOU 2425  O   HOH A 558     6357   6536   6042    114   -333  -1119       O  
HETATM 2426  O   HOH A 559     -11.726  11.120   1.010  1.00 47.84           O  
ANISOU 2426  O   HOH A 559     6050   6302   5825   -937    658   1269       O  
HETATM 2427  O   HOH A 560     -30.020  14.711  37.470  1.00 55.85           O  
ANISOU 2427  O   HOH A 560     5636   8078   7504    281   1200  -2501       O  
HETATM 2428  O   HOH A 561     -24.476   3.822  24.934  1.00 41.95           O  
ANISOU 2428  O   HOH A 561     4834   5510   5596   -237    661   -398       O  
HETATM 2429  O   HOH A 562     -27.852  -3.713   6.547  1.00 32.31           O  
ANISOU 2429  O   HOH A 562     3967   4174   4133   -161   -102    270       O  
HETATM 2430  O   HOH A 563     -20.483  -6.221   2.094  1.00 32.38           O  
ANISOU 2430  O   HOH A 563     4304   4449   3550     65      1    140       O  
HETATM 2431  O   HOH A 564     -11.588  -1.631  -2.567  1.00 51.38           O  
ANISOU 2431  O   HOH A 564     6412   7744   5366   -135    707    214       O  
HETATM 2432  O   HOH A 565     -28.781   0.226  15.058  1.00 39.08           O  
ANISOU 2432  O   HOH A 565     4437   5046   5367   -242    304     38       O  
HETATM 2433  O   HOH A 566     -10.208   1.330  27.451  1.00 36.45           O  
ANISOU 2433  O   HOH A 566     4530   4661   4658     55    104   -477       O  
HETATM 2434  O   HOH A 567     -28.719  11.312  24.529  1.00 46.86           O  
ANISOU 2434  O   HOH A 567     4846   5953   7007    214    560   -928       O  
HETATM 2435  O   HOH A 568      -2.057   7.896  32.896  1.00 43.87           O  
ANISOU 2435  O   HOH A 568     4932   5685   6051     71   -308  -1241       O  
HETATM 2436  O   HOH A 569      -6.566   0.761  22.234  1.00 30.12           O  
ANISOU 2436  O   HOH A 569     3404   3976   4066    172    132   -478       O  
HETATM 2437  O   HOH A 570     -19.083 -21.173 -10.515  1.00 53.34           O  
ANISOU 2437  O   HOH A 570     7789   7469   5008    936   -961  -1702       O  
HETATM 2438  O   HOH A 571      -8.757 -13.471  24.879  1.00 58.18           O  
ANISOU 2438  O   HOH A 571     8405   6749   6950    562   -935   -266       O  
HETATM 2439  O   HOH A 572     -16.195  20.340  41.978  1.00 54.77           O  
ANISOU 2439  O   HOH A 572     6316   6907   7586    343    214  -2851       O  
HETATM 2440  O   HOH A 573     -21.930   5.473  26.730  1.00 29.17           O  
ANISOU 2440  O   HOH A 573     3265   3831   3989   -163    630   -520       O  
HETATM 2441  O   HOH A 574     -10.816   8.005  11.580  1.00 54.74           O  
ANISOU 2441  O   HOH A 574     6455   6977   7366   -383    581    322       O  
HETATM 2442  O   HOH A 575     -31.683  19.027  37.024  1.00 54.19           O  
ANISOU 2442  O   HOH A 575     5155   7544   7891    709    899  -2908       O  
HETATM 2443  O   HOH A 576     -30.421   7.644  28.006  1.00 45.74           O  
ANISOU 2443  O   HOH A 576     4660   6378   6339   -122    938  -1062       O  
HETATM 2444  O   HOH A 577     -28.223   1.560  12.783  1.00 32.40           O  
ANISOU 2444  O   HOH A 577     3614   4120   4577   -127    193    135       O  
HETATM 2445  O   HOH A 578     -24.505  12.314  41.029  1.00 43.18           O  
ANISOU 2445  O   HOH A 578     4737   6547   5122    -43   1121  -2235       O  
HETATM 2446  O   HOH A 579      -4.137   6.117  26.142  1.00 44.27           O  
ANISOU 2446  O   HOH A 579     4922   5724   6175      4     81   -755       O  
HETATM 2447  O   HOH A 580     -13.997 -11.063  -6.257  1.00 48.48           O  
ANISOU 2447  O   HOH A 580     6426   7439   4557    500    165   -678       O  
HETATM 2448  O   HOH A 581      -6.916  10.792  27.826  1.00 66.79           O  
ANISOU 2448  O   HOH A 581     7807   8301   9271   -152    160   -825       O  
HETATM 2449  O   HOH A 582     -20.360  17.302  44.582  1.00 53.57           O  
ANISOU 2449  O   HOH A 582     6153   7572   6627    268    718  -2985       O  
HETATM 2450  O   HOH A 583      -4.653  19.154  39.037  1.00 52.63           O  
ANISOU 2450  O   HOH A 583     5990   6249   7758   -118   -431  -2233       O  
HETATM 2451  O   HOH A 584     -30.588 -12.231   4.062  1.00 55.95           O  
ANISOU 2451  O   HOH A 584     7318   7023   6918   -423   -544     10       O  
HETATM 2452  O   HOH A 585     -20.840 -20.453  22.575  1.00 42.47           O  
ANISOU 2452  O   HOH A 585     7307   4112   4716   -734   -874    486       O  
HETATM 2453  O   HOH A 586     -12.165   2.245  25.780  1.00 43.08           O  
ANISOU 2453  O   HOH A 586     5300   5474   5593    -12    248   -386       O  
HETATM 2454  O   HOH A 587     -28.488  -6.948  -3.895  1.00 36.39           O  
ANISOU 2454  O   HOH A 587     4924   5010   3893     -8   -646    235       O  
HETATM 2455  O   HOH A 588     -12.046 -19.771  -8.012  1.00 66.10           O  
ANISOU 2455  O   HOH A 588     8894   9506   6715   1310   -401  -1965       O  
HETATM 2456  O   HOH A 589     -31.161 -10.138  11.315  1.00 38.61           O  
ANISOU 2456  O   HOH A 589     4882   4856   4932   -704    -92    128       O  
HETATM 2457  O   HOH A 590     -12.414  -5.103  -1.655  1.00 37.00           O  
ANISOU 2457  O   HOH A 590     4654   5793   3610    140    504   -100       O  
HETATM 2458  O   HOH A 591     -19.985  25.801  18.773  1.00 68.54           O  
ANISOU 2458  O   HOH A 591     8389   6447  11205    152   -585   -256       O  
HETATM 2459  O   HOH A 592     -22.559  -6.251 -11.704  1.00 45.91           O  
ANISOU 2459  O   HOH A 592     6564   7054   3826     69   -373    252       O  
HETATM 2460  O   HOH A 593      -2.101  28.260  31.294  1.00 53.06           O  
ANISOU 2460  O   HOH A 593     5810   4892   9457   -984   -606  -1691       O  
HETATM 2461  O   HOH A 594     -14.453 -19.873  25.970  1.00 51.08           O  
ANISOU 2461  O   HOH A 594     8591   5110   5708    -70  -1296    322       O  
HETATM 2462  O   HOH A 595     -24.638  11.134  26.714  1.00 41.72           O  
ANISOU 2462  O   HOH A 595     4466   5252   6133    102    599   -903       O  
HETATM 2463  O   HOH A 596     -27.932  -1.988   4.581  1.00 37.71           O  
ANISOU 2463  O   HOH A 596     4650   4880   4800    -87   -177    368       O  
HETATM 2464  O   HOH A 597     -25.874 -15.266  19.620  1.00 47.08           O  
ANISOU 2464  O   HOH A 597     6910   5433   5545   -967   -162    356       O  
HETATM 2465  O   HOH A 598     -24.488  -7.213 -10.441  1.00 35.19           O  
ANISOU 2465  O   HOH A 598     5157   5461   2753    103   -558    185       O  
HETATM 2466  O   HOH A 599     -30.042  -7.801   1.936  1.00 54.10           O  
ANISOU 2466  O   HOH A 599     6918   6994   6643   -196   -478    162       O  
HETATM 2467  O   HOH A 600     -14.750 -25.997  -1.538  1.00 54.58           O  
ANISOU 2467  O   HOH A 600     8192   6367   6180   1362  -1436  -1901       O  
HETATM 2468  O   HOH A 601     -24.414 -24.039  -1.021  1.00 46.57           O  
ANISOU 2468  O   HOH A 601     7252   5131   5313    196  -1438   -982       O  
HETATM 2469  O   HOH A 602     -31.571 -14.303  14.853  1.00 51.01           O  
ANISOU 2469  O   HOH A 602     6818   6212   6352  -1165   -102    225       O  
HETATM 2470  O   HOH A 603     -11.786  -7.286  -9.629  1.00 59.51           O  
ANISOU 2470  O   HOH A 603     7692   9512   5406    188    633   -407       O  
HETATM 2471  O   HOH A 604     -29.648  -6.086   3.753  1.00 57.61           O  
ANISOU 2471  O   HOH A 604     7257   7421   7213   -193   -334    220       O  
HETATM 2472  O   HOH A 605     -31.487   0.223  19.611  1.00 57.11           O  
ANISOU 2472  O   HOH A 605     6462   7588   7650   -440    568   -225       O  
HETATM 2473  O   HOH A 606     -28.287 -17.255   0.270  1.00 53.47           O  
ANISOU 2473  O   HOH A 606     7492   6531   6294   -213   -924   -344       O  
HETATM 2474  O   HOH A 607     -17.843  11.153   9.438  1.00 45.61           O  
ANISOU 2474  O   HOH A 607     5561   5334   6435   -275    245    670       O  
HETATM 2475  O   HOH A 608     -17.872   3.397  44.068  1.00 51.21           O  
ANISOU 2475  O   HOH A 608     7062   7556   4839   -558    595  -1166       O  
HETATM 2476  O   HOH A 609      -4.117  22.995  25.463  1.00 50.06           O  
ANISOU 2476  O   HOH A 609     5470   5088   8460   -905    -71   -807       O  
HETATM 2477  O   HOH A 610     -14.927 -20.932 -11.781  1.00 60.54           O  
ANISOU 2477  O   HOH A 610     8474   8915   5612   1245   -622  -2092       O  
HETATM 2478  O   HOH A 611     -29.859 -17.316   9.245  1.00 52.27           O  
ANISOU 2478  O   HOH A 611     7303   6084   6475   -818   -590     46       O  
HETATM 2479  O   HOH A 612     -23.011   4.219  28.897  1.00 52.65           O  
ANISOU 2479  O   HOH A 612     6293   6985   6726   -279    731   -590       O  
HETATM 2480  O   HOH A 613     -29.504  18.450  24.353  1.00 62.69           O  
ANISOU 2480  O   HOH A 613     6674   7307   9839    744    123  -1360       O  
HETATM 2481  O   HOH A 614     -27.016 -19.033  -1.425  1.00 49.50           O  
ANISOU 2481  O   HOH A 614     7166   5994   5649    -50  -1068   -562       O  
HETATM 2482  O   HOH A 615     -21.342  -6.731  24.554  1.00 53.58           O  
ANISOU 2482  O   HOH A 615     7219   6741   6397   -508    278     90       O  
HETATM 2483  O   HOH A 616     -28.963 -10.614   1.903  1.00 38.20           O  
ANISOU 2483  O   HOH A 616     5090   4904   4519   -215   -525     38       O  
HETATM 2484  O   HOH A 617     -31.388 -12.385  10.142  1.00 48.59           O  
ANISOU 2484  O   HOH A 617     6308   6012   6142   -772   -250    110       O  
HETATM 2485  O   HOH A 618      -6.703  -8.582  -2.565  1.00 55.35           O  
ANISOU 2485  O   HOH A 618     6603   8686   5744    535    692   -891       O  
HETATM 2486  O   HOH A 619     -24.591 -23.535   3.400  1.00 65.84           O  
ANISOU 2486  O   HOH A 619     9718   7333   7965    -64  -1311   -623       O  
HETATM 2487  O   HOH A 620     -29.569  12.380  40.632  1.00 48.33           O  
ANISOU 2487  O   HOH A 620     4912   7587   5863    -54   1448  -2458       O  
HETATM 2488  O   HOH A 621      -5.458  -8.083   0.327  1.00 45.74           O  
ANISOU 2488  O   HOH A 621     5245   7296   4840    572    654   -904       O  
HETATM 2489  O   HOH A 622     -26.335  -9.399  16.637  1.00 40.63           O  
ANISOU 2489  O   HOH A 622     5403   5022   5012   -610    124    177       O  
HETATM 2490  O   HOH A 623     -29.661  -5.102  -6.033  1.00 54.59           O  
ANISOU 2490  O   HOH A 623     7260   7393   6088     22   -809    394       O  
HETATM 2491  O   HOH A 624     -30.292 -13.154   1.428  1.00 53.26           O  
ANISOU 2491  O   HOH A 624     7093   6713   6431   -321   -705    -76       O  
HETATM 2492  O   HOH A 625     -28.865  -3.651  -8.332  1.00 48.46           O  
ANISOU 2492  O   HOH A 625     6638   6750   5026     42   -845    561       O  
HETATM 2493  O   HOH A 626     -13.347  13.144   0.492  1.00 60.15           O  
ANISOU 2493  O   HOH A 626     7802   7556   7496   -980    460   1515       O  
HETATM 2494  O   HOH A 627      -7.604 -19.804  21.243  1.00 50.92           O  
ANISOU 2494  O   HOH A 627     7900   5282   6165   1060  -1588   -526       O  
HETATM 2495  O   HOH A 628     -17.537   4.400  46.715  1.00 58.99           O  
ANISOU 2495  O   HOH A 628     8137   8760   5516   -571    597  -1412       O  
HETATM 2496  O   HOH A 629     -28.559  -3.220   0.197  1.00 42.83           O  
ANISOU 2496  O   HOH A 629     5472   5648   5153    -43   -416    414       O  
HETATM 2497  O   HOH A 630     -24.037   6.280  25.815  1.00 47.49           O  
ANISOU 2497  O   HOH A 630     5435   6162   6449   -132    661   -557       O  
HETATM 2498  O   HOH A 631     -13.597 -18.087 -11.930  1.00 59.54           O  
ANISOU 2498  O   HOH A 631     8127   9174   5323   1089   -236  -1823       O  
HETATM 2499  O   HOH A 632     -31.969 -14.961  12.573  1.00 49.30           O  
ANISOU 2499  O   HOH A 632     6603   5947   6180  -1096   -255    171       O  
HETATM 2500  O   HOH A 633     -30.333 -15.584   7.386  1.00 55.58           O  
ANISOU 2500  O   HOH A 633     7521   6688   6907   -686   -558      8       O  
HETATM 2501  O   HOH A 634     -26.616   1.810  26.118  1.00 49.23           O  
ANISOU 2501  O   HOH A 634     5760   6622   6323   -428    777   -404       O  
HETATM 2502  O   HOH A 635     -27.304   7.121  11.654  1.00 38.73           O  
ANISOU 2502  O   HOH A 635     4372   4650   5694     76     57    235       O  
HETATM 2503  O   HOH A 636      -1.385  30.730  30.448  1.00 59.24           O  
ANISOU 2503  O   HOH A 636     6653   5312  10545  -1220   -729  -1590       O  
HETATM 2504  O   HOH A 637     -28.293   4.634  -0.337  1.00 61.81           O  
ANISOU 2504  O   HOH A 637     7869   7786   7832     50   -514    874       O  
HETATM 2505  O   HOH A 638     -31.138 -16.256  16.629  1.00 56.75           O  
ANISOU 2505  O   HOH A 638     7824   6774   6963  -1362   -148    323       O  
HETATM 2506  O   HOH A 639     -25.948  -1.234  25.984  1.00 51.23           O  
ANISOU 2506  O   HOH A 639     6277   6834   6356   -579    712   -211       O  
HETATM 2507  O   HOH A 640      -0.835  26.308  32.926  1.00 52.66           O  
ANISOU 2507  O   HOH A 640     5634   5234   9139   -888   -585  -1874       O  
HETATM 2508  O   HOH A 641     -12.402  18.164  20.410  1.00 58.38           O  
ANISOU 2508  O   HOH A 641     6854   6392   8935   -379    178   -197       O  
HETATM 2509  O   HOH A 642      -4.624   5.446  22.515  0.50 39.37           O  
ANISOU 2509  O   HOH A 642     4250   5155   5553      0    246      0       O  
HETATM 2510  O   HOH A 643      -3.078  32.851  31.130  1.00 66.41           O  
ANISOU 2510  O   HOH A 643     7752   5877  11604  -1051   -894  -1703       O  
HETATM 2511  O   HOH A 644     -13.447 -32.346   0.112  1.00 57.16           O  
ANISOU 2511  O   HOH A 644     9012   5756   6951   1744  -2265  -2188       O  
HETATM 2512  O   HOH A 645     -30.474  -1.487   3.991  1.00 43.02           O  
ANISOU 2512  O   HOH A 645     5203   5555   5590    -77   -321    359       O  
HETATM 2513  O   HOH A 646     -29.566   5.945  17.948  1.00 48.08           O  
ANISOU 2513  O   HOH A 646     5239   6123   6905     -9    379   -252       O  
CONECT 1114 2361                                                                
CONECT 2319 2320 2321 2336                                                      
CONECT 2320 2319                                                                
CONECT 2321 2319 2322                                                           
CONECT 2322 2321 2323 2324 2328                                                 
CONECT 2323 2322 2325                                                           
CONECT 2324 2322 2326                                                           
CONECT 2325 2323 2327                                                           
CONECT 2326 2324 2327                                                           
CONECT 2327 2325 2326                                                           
CONECT 2328 2322 2329                                                           
CONECT 2329 2328 2330 2331 2332                                                 
CONECT 2330 2329                                                                
CONECT 2331 2329                                                                
CONECT 2332 2329 2333 2334 2335                                                 
CONECT 2333 2332                                                                
CONECT 2334 2332                                                                
CONECT 2335 2332                                                                
CONECT 2336 2319 2337                                                           
CONECT 2337 2336 2338 2342                                                      
CONECT 2338 2337 2339 2340 2341                                                 
CONECT 2339 2338                                                                
CONECT 2340 2338                                                                
CONECT 2341 2338                                                                
CONECT 2342 2337 2343 2344                                                      
CONECT 2343 2342                                                                
CONECT 2344 2342 2345 2346                                                      
CONECT 2345 2344 2348                                                           
CONECT 2346 2344 2347 2352                                                      
CONECT 2347 2346 2348 2349                                                      
CONECT 2348 2345 2347 2349                                                      
CONECT 2349 2347 2348 2350 2351                                                 
CONECT 2350 2349                                                                
CONECT 2351 2349                                                                
CONECT 2352 2346 2353 2354                                                      
CONECT 2353 2352                                                                
CONECT 2354 2352 2355                                                           
CONECT 2355 2354 2356 2361                                                      
CONECT 2356 2355 2357                                                           
CONECT 2357 2356 2358                                                           
CONECT 2358 2357 2359                                                           
CONECT 2359 2358                                                                
CONECT 2360 2361                                                                
CONECT 2361 1114 2355 2360 2367                                                 
CONECT 2362 2367                                                                
CONECT 2363 2364 2367                                                           
CONECT 2364 2363 2365 2366                                                      
CONECT 2365 2364 2366                                                           
CONECT 2366 2364 2365                                                           
CONECT 2367 2361 2362 2363                                                      
MASTER      307    0    1   11   15    0    0    6 2512    1   50   24          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.