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Browse entries in the PDBbind-CN Database

HEADER    STRUCTURAL PROTEIN/DNA                  09-MAY-18   5ZVB              
TITLE     APOBEC3F CHIMERIC CATALYTIC DOMAIN IN COMPLEX WITH DNA(DT9)           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APEBEC3F/SSDNA-T9;                                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: APOBEC-RELATED CYTIDINE DEAMINASE,ARCD,APOBEC-RELATED       
COMPND   5 PROTEIN 9,ARP-9,CEM-15,CEM15,DEOXYCYTIDINE DEAMINASE,A3G,            
COMPND   6 APOLIPOPROTEIN B MRNA-EDITING ENZYME CATALYTIC POLYPEPTIDE-LIKE 3F,  
COMPND   7 A3F;                                                                 
COMPND   8 EC: 3.5.4.-,3.5.4.-;                                                 
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 OTHER_DETAILS: ALL RESIDURES INCLUDES PURIFICATION TAG OF            
COMPND  11 A3F(6HIS+THROMBIN CLEAVAGE TAG+ CHIMERIC A3F)(REFERENCE: K. SIU, ET  
COMPND  12 AL. NAT. COMMUN. 2013, 4, 2593. PDB CODE:4J4J);                      
COMPND  13 MOL_ID: 2;                                                           
COMPND  14 MOLECULE: DNA (5'-D(*AP*TP*TP*TP*TP*CP*AP*AP*T)-3');                 
COMPND  15 CHAIN: C;                                                            
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 OTHER_DETAILS: CHEMICALLY SYNTHESIZED                                
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: APOBEC3G, MDS019, APOBEC3F;                                    
SOURCE   6 EXPRESSION_SYSTEM: PROKARYOTIC ENVIRONMENTAL SAMPLES;                
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 81490;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: DNA-BINDING VECTOR PODB80;                      
SOURCE  11 ORGANISM_TAXID: 62978                                                
KEYWDS    APOBEC3F, HIV-1, DEAMINATION, STRUCTURAL PROTEIN-DNA COMPLEX          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.CHENG,T.L.ZHANG,C.X.WANG,W.X.LAN,J.P.DING,C.Y.CAO                   
REVDAT   2   28-NOV-18 5ZVB    1       TITLE  COMPND JRNL                       
REVDAT   1   21-NOV-18 5ZVB    0                                                
JRNL        AUTH   C.CHENG,T.ZHANG,C.WANG,W.LAN,J.DING,C.CAO                    
JRNL        TITL   CRYSTAL STRUCTURE OF CYTIDINE DEAMINASE HUMAN APOBEC3F       
JRNL        TITL 2 CHIMERIC CATALYTIC DOMAIN IN COMPLEX WITH DNA                
JRNL        REF    CHIN.J.CHEM.                  V.  36  1241 2018              
JRNL        REFN                   ISSN 1001-604X                               
JRNL        DOI    10.1002/CJOC.201800508                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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 : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.01                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 34705                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1803                            
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  2.0520 -  2.0000    0.98     2473   146  0.2130 0.2830        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : MASK                                          
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.104            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.80000                                              
REMARK   3    B22 (A**2) : -0.74000                                             
REMARK   3    B33 (A**2) : -0.06000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID -29 THROUGH 373 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  21.9342  -5.7513   4.3955              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0054 T22:   0.0265                                     
REMARK   3      T33:   0.0749 T12:  -0.0069                                     
REMARK   3      T13:   0.0040 T23:   0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0998 L22:   0.1712                                     
REMARK   3      L33:   0.1388 L12:  -0.0933                                     
REMARK   3      L13:   0.0195 L23:   0.0877                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0135 S12:   0.0128 S13:  -0.0009                       
REMARK   3      S21:  -0.0034 S22:  -0.0161 S23:  -0.0057                       
REMARK   3      S31:   0.0135 S32:  -0.0026 S33:   0.0026                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID -29 THROUGH 373 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.6422 -28.0001 -29.2034              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0174 T22:   0.0165                                     
REMARK   3      T33:   0.0713 T12:  -0.0092                                     
REMARK   3      T13:   0.0013 T23:   0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0163 L22:   0.0632                                     
REMARK   3      L33:   0.5197 L12:   0.0101                                     
REMARK   3      L13:   0.0814 L23:   0.0936                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0158 S12:  -0.0073 S13:   0.0016                       
REMARK   3      S21:   0.0071 S22:  -0.0045 S23:  -0.0240                       
REMARK   3      S31:   0.0579 S32:  -0.0118 S33:  -0.0113                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 9 )                     
REMARK   3    ORIGIN FOR THE GROUP (A):  30.2507 -26.6526 -13.0634              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0257 T22:   0.0286                                     
REMARK   3      T33:   0.1055 T12:  -0.0091                                     
REMARK   3      T13:  -0.0082 T23:  -0.0096                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2870 L22:   0.2872                                     
REMARK   3      L33:   0.1771 L12:  -0.2868                                     
REMARK   3      L13:   0.2221 L23:  -0.2232                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0327 S12:  -0.0475 S13:   0.0141                       
REMARK   3      S21:   0.0292 S22:   0.0425 S23:  -0.0061                       
REMARK   3      S31:  -0.0185 S32:  -0.0423 S33:  -0.0098                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED                 
REMARK   4                                                                      
REMARK   4 5ZVB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300007697.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUN-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 130 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : ADDREF                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37457                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.980                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.010                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 14.30                              
REMARK 200  R MERGE                    (I) : 0.14600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M SODIUM CACODYLATE, PH 6.5, AND     
REMARK 280  30%(V/V) 2-METHYL-2,4-PENTANEDIOL (MPD), VAPOR DIFFUSION,           
REMARK 280  HANGING DROP, TEMPERATURE 291K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       30.49500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.83700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.35100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       46.83700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.49500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       46.35100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 370 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 10210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MSE A   -53                                                      
REMARK 465     ALA A   -52                                                      
REMARK 465     HIS A   -51                                                      
REMARK 465     HIS A   -50                                                      
REMARK 465     HIS A   -49                                                      
REMARK 465     HIS A   -48                                                      
REMARK 465     HIS A   -47                                                      
REMARK 465     HIS A   -46                                                      
REMARK 465     VAL A   -45                                                      
REMARK 465     ASP A   -44                                                      
REMARK 465     ASP A   -43                                                      
REMARK 465     ASP A   -42                                                      
REMARK 465     ASP A   -41                                                      
REMARK 465     LYS A   -40                                                      
REMARK 465     MSE A   -39                                                      
REMARK 465     LEU A   -38                                                      
REMARK 465     VAL A   -37                                                      
REMARK 465     PRO A   -36                                                      
REMARK 465     ARG A   -35                                                      
REMARK 465     GLY A   -34                                                      
REMARK 465     SER A   -33                                                      
REMARK 465     GLU A   -32                                                      
REMARK 465     ASN A   -31                                                      
REMARK 465     LEU A   -30                                                      
REMARK 465     VAL A   242                                                      
REMARK 465     ASP A   243                                                      
REMARK 465     PRO A   244                                                      
REMARK 465     GLU A   245                                                      
REMARK 465     THR A   246                                                      
REMARK 465     MSE B   -53                                                      
REMARK 465     ALA B   -52                                                      
REMARK 465     HIS B   -51                                                      
REMARK 465     HIS B   -50                                                      
REMARK 465     HIS B   -49                                                      
REMARK 465     HIS B   -48                                                      
REMARK 465     HIS B   -47                                                      
REMARK 465     HIS B   -46                                                      
REMARK 465     VAL B   -45                                                      
REMARK 465     ASP B   -44                                                      
REMARK 465     ASP B   -43                                                      
REMARK 465     ASP B   -42                                                      
REMARK 465     ASP B   -41                                                      
REMARK 465     LYS B   -40                                                      
REMARK 465     MSE B   -39                                                      
REMARK 465     LEU B   -38                                                      
REMARK 465     VAL B   -37                                                      
REMARK 465     PRO B   -36                                                      
REMARK 465     ARG B   -35                                                      
REMARK 465     GLY B   -34                                                      
REMARK 465     SER B   -33                                                      
REMARK 465     GLU B   -32                                                      
REMARK 465     ASN B   -31                                                      
REMARK 465     LEU B   -30                                                      
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     GLN B 241    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 245    CG   CD   OE1  OE2                                  
REMARK 470     THR B 246    OG1  CG2                                            
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    ASN B 266       49.06   -100.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 249   ND1                                                    
REMARK 620 2 CYS A 280   SG  112.5                                              
REMARK 620 3 CYS A 283   SG  106.4 123.7                                        
REMARK 620 4 CAC A 402   O1   91.6 109.6 108.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 249   ND1                                                    
REMARK 620 2 CYS B 280   SG  100.9                                              
REMARK 620 3 CYS B 283   SG  103.6 121.4                                        
REMARK 620 4 CAC B 402   O1  119.2  93.6 117.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CAC A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CAC B 402                 
DBREF  5ZVB A  -23    -1  UNP    Q9HC16   ABC3G_HUMAN    197    219             
DBREF  5ZVB A  218   373  UNP    Q8IUX4   ABC3F_HUMAN    218    373             
DBREF  5ZVB B  -23    -1  UNP    Q9HC16   ABC3G_HUMAN    197    219             
DBREF  5ZVB B  218   373  UNP    Q8IUX4   ABC3F_HUMAN    218    373             
DBREF  5ZVB C    1     9  PDB    5ZVB     5ZVB             1      9             
SEQADV 5ZVB MSE A  -53  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB ALA A  -52  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB HIS A  -51  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB HIS A  -50  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB HIS A  -49  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB HIS A  -48  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB HIS A  -47  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB HIS A  -46  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB VAL A  -45  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB ASP A  -44  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB ASP A  -43  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB ASP A  -42  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB ASP A  -41  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB LYS A  -40  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB MSE A  -39  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB LEU A  -38  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB VAL A  -37  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB PRO A  -36  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB ARG A  -35  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB GLY A  -34  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB SER A  -33  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB GLU A  -32  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB ASN A  -31  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB LEU A  -30  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB TYR A  -29  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB PHE A  -28  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB GLN A  -27  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB GLY A  -26  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB SER A  -25  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB ALA A  -24  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB MSE B  -53  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB ALA B  -52  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB HIS B  -51  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB HIS B  -50  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB HIS B  -49  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB HIS B  -48  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB HIS B  -47  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB HIS B  -46  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB VAL B  -45  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB ASP B  -44  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB ASP B  -43  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB ASP B  -42  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB ASP B  -41  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB LYS B  -40  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB MSE B  -39  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB LEU B  -38  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB VAL B  -37  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB PRO B  -36  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB ARG B  -35  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB GLY B  -34  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB SER B  -33  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB GLU B  -32  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB ASN B  -31  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB LEU B  -30  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB TYR B  -29  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB PHE B  -28  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB GLN B  -27  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB GLY B  -26  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB SER B  -25  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVB ALA B  -24  UNP  Q9HC16              EXPRESSION TAG                 
SEQRES   1 A  209  MSE ALA HIS HIS HIS HIS HIS HIS VAL ASP ASP ASP ASP          
SEQRES   2 A  209  LYS MSE LEU VAL PRO ARG GLY SER GLU ASN LEU TYR PHE          
SEQRES   3 A  209  GLN GLY SER ALA MSE ASP PRO PRO THR PHE THR PHE ASN          
SEQRES   4 A  209  PHE ASN ASN GLU PRO TRP VAL ARG GLY ARG HIS GLU THR          
SEQRES   5 A  209  TYR LEU CYS PHE THR MSE GLU VAL VAL LYS HIS HIS SER          
SEQRES   6 A  209  PRO VAL SER TRP LYS ARG GLY VAL PHE ARG ASN GLN VAL          
SEQRES   7 A  209  ASP PRO GLU THR HIS CYS HIS ALA GLU ARG CYS PHE LEU          
SEQRES   8 A  209  SER TRP PHE CYS ASP ASP ILE LEU SER PRO ASN THR ASN          
SEQRES   9 A  209  TYR GLU VAL THR TRP TYR THR SER TRP SER PRO CYS PRO          
SEQRES  10 A  209  GLU CYS ALA GLY GLU VAL ALA GLU PHE LEU ALA ARG HIS          
SEQRES  11 A  209  SER ASN VAL ASN LEU THR ILE PHE THR ALA ARG LEU TYR          
SEQRES  12 A  209  TYR PHE TRP ASP THR ASP TYR GLN GLU GLY LEU ARG SER          
SEQRES  13 A  209  LEU SER GLN GLU GLY ALA SER VAL GLU ILE MSE GLY TYR          
SEQRES  14 A  209  LYS ASP PHE LYS TYR CYS TRP GLU ASN PHE VAL TYR ASN          
SEQRES  15 A  209  ASP ASP GLU PRO PHE LYS PRO TRP LYS GLY LEU LYS TYR          
SEQRES  16 A  209  ASN PHE LEU PHE LEU ASP SER LYS LEU GLN GLU ILE LEU          
SEQRES  17 A  209  GLU                                                          
SEQRES   1 B  209  MSE ALA HIS HIS HIS HIS HIS HIS VAL ASP ASP ASP ASP          
SEQRES   2 B  209  LYS MSE LEU VAL PRO ARG GLY SER GLU ASN LEU TYR PHE          
SEQRES   3 B  209  GLN GLY SER ALA MSE ASP PRO PRO THR PHE THR PHE ASN          
SEQRES   4 B  209  PHE ASN ASN GLU PRO TRP VAL ARG GLY ARG HIS GLU THR          
SEQRES   5 B  209  TYR LEU CYS PHE THR MSE GLU VAL VAL LYS HIS HIS SER          
SEQRES   6 B  209  PRO VAL SER TRP LYS ARG GLY VAL PHE ARG ASN GLN VAL          
SEQRES   7 B  209  ASP PRO GLU THR HIS CYS HIS ALA GLU ARG CYS PHE LEU          
SEQRES   8 B  209  SER TRP PHE CYS ASP ASP ILE LEU SER PRO ASN THR ASN          
SEQRES   9 B  209  TYR GLU VAL THR TRP TYR THR SER TRP SER PRO CYS PRO          
SEQRES  10 B  209  GLU CYS ALA GLY GLU VAL ALA GLU PHE LEU ALA ARG HIS          
SEQRES  11 B  209  SER ASN VAL ASN LEU THR ILE PHE THR ALA ARG LEU TYR          
SEQRES  12 B  209  TYR PHE TRP ASP THR ASP TYR GLN GLU GLY LEU ARG SER          
SEQRES  13 B  209  LEU SER GLN GLU GLY ALA SER VAL GLU ILE MSE GLY TYR          
SEQRES  14 B  209  LYS ASP PHE LYS TYR CYS TRP GLU ASN PHE VAL TYR ASN          
SEQRES  15 B  209  ASP ASP GLU PRO PHE LYS PRO TRP LYS GLY LEU LYS TYR          
SEQRES  16 B  209  ASN PHE LEU PHE LEU ASP SER LYS LEU GLN GLU ILE LEU          
SEQRES  17 B  209  GLU                                                          
SEQRES   1 C    9   DA  DT  DT  DT  DT  DC  DA  DA  DT                          
MODRES 5ZVB MSE A  -23  MET  MODIFIED RESIDUE                                   
MODRES 5ZVB MSE A  222  MET  MODIFIED RESIDUE                                   
MODRES 5ZVB MSE A  331  MET  MODIFIED RESIDUE                                   
MODRES 5ZVB MSE B  -23  MET  MODIFIED RESIDUE                                   
MODRES 5ZVB MSE B  222  MET  MODIFIED RESIDUE                                   
MODRES 5ZVB MSE B  331  MET  MODIFIED RESIDUE                                   
HET    MSE  A -23       8                                                       
HET    MSE  A 222       8                                                       
HET    MSE  A 331       8                                                       
HET    MSE  B -23       8                                                       
HET    MSE  B 222       8                                                       
HET    MSE  B 331       8                                                       
HET     ZN  A 401       1                                                       
HET    CAC  A 402       5                                                       
HET     ZN  B 401       1                                                       
HET    CAC  B 402       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      ZN ZINC ION                                                         
HETNAM     CAC CACODYLATE ION                                                   
HETSYN     CAC DIMETHYLARSINATE                                                 
FORMUL   1  MSE    6(C5 H11 N O2 SE)                                            
FORMUL   4   ZN    2(ZN 2+)                                                     
FORMUL   5  CAC    2(C2 H6 AS O2 1-)                                            
FORMUL   8  HOH   *211(H2 O)                                                    
HELIX    1 AA1 ASP A  -22  ASN A  -13  1                                  10    
HELIX    2 AA2 HIS A  249  ILE A  262  1                                  14    
HELIX    3 AA3 CYS A  280  HIS A  294  1                                  15    
HELIX    4 AA4 ASP A  311  GLU A  324  1                                  14    
HELIX    5 AA5 GLY A  332  PHE A  343  1                                  12    
HELIX    6 AA6 GLY A  356  GLU A  373  1                                  18    
HELIX    7 AA7 ASP B  -22  ASN B  -13  1                                  10    
HELIX    8 AA8 HIS B  249  ILE B  262  1                                  14    
HELIX    9 AA9 CYS B  280  HIS B  294  1                                  15    
HELIX   10 AB1 ASP B  311  GLU B  324  1                                  14    
HELIX   11 AB2 GLY B  332  PHE B  343  1                                  12    
HELIX   12 AB3 GLY B  356  GLU B  373  1                                  18    
SHEET    1 AA1 6 PHE A -28  GLN A -27  0                                        
SHEET    2 AA1 6 SER A 232  ARG A 239  1  O  ARG A 235   N  GLN A -27           
SHEET    3 AA1 6 TYR A  -1  LYS A 226 -1  N  VAL A 224   O  SER A 232           
SHEET    4 AA1 6 THR A 267  TRP A 277 -1  O  THR A 272   N  THR A 221           
SHEET    5 AA1 6 VAL A 297  ARG A 305  1  O  ASN A 298   N  VAL A 271           
SHEET    6 AA1 6 SER A 327  ILE A 330  1  O  SER A 327   N  ILE A 301           
SHEET    1 AA2 6 PHE B -28  GLN B -27  0                                        
SHEET    2 AA2 6 SER B 232  ARG B 239  1  O  ARG B 235   N  GLN B -27           
SHEET    3 AA2 6 TYR B  -1  VAL B 225 -1  N  VAL B 224   O  SER B 232           
SHEET    4 AA2 6 ASN B 268  TRP B 277 -1  O  TYR B 274   N  CYS B 219           
SHEET    5 AA2 6 VAL B 297  ARG B 305  1  O  ASN B 298   N  VAL B 271           
SHEET    6 AA2 6 SER B 327  ILE B 330  1  O  SER B 327   N  ILE B 301           
SSBOND   1 CYS B  248    CYS B  253                          1555   1555  2.41  
LINK         C   ALA A -24                 N   MSE A -23     1555   1555  1.33  
LINK         C   MSE A -23                 N   ASP A -22     1555   1555  1.33  
LINK         C   THR A 221                 N   MSE A 222     1555   1555  1.32  
LINK         C   MSE A 222                 N   GLU A 223     1555   1555  1.33  
LINK         ND1 HIS A 249                ZN    ZN A 401     1555   1555  2.19  
LINK         SG  CYS A 280                ZN    ZN A 401     1555   1555  2.21  
LINK         SG  CYS A 283                ZN    ZN A 401     1555   1555  2.22  
LINK         C   ILE A 330                 N   MSE A 331     1555   1555  1.34  
LINK         C   MSE A 331                 N   GLY A 332     1555   1555  1.32  
LINK         C   ALA B -24                 N   MSE B -23     1555   1555  1.34  
LINK         C   MSE B -23                 N   ASP B -22     1555   1555  1.34  
LINK         C   THR B 221                 N   MSE B 222     1555   1555  1.32  
LINK         C   MSE B 222                 N   GLU B 223     1555   1555  1.33  
LINK         ND1 HIS B 249                ZN    ZN B 401     1555   1555  2.15  
LINK         SG  CYS B 280                ZN    ZN B 401     1555   1555  2.20  
LINK         SG  CYS B 283                ZN    ZN B 401     1555   1555  2.20  
LINK         C   ILE B 330                 N   MSE B 331     1555   1555  1.33  
LINK         C   MSE B 331                 N   GLY B 332     1555   1555  1.33  
LINK        ZN    ZN A 401                 O1  CAC A 402     1555   1555  2.17  
LINK        ZN    ZN B 401                 O1  CAC B 402     1555   1555  2.18  
SITE     1 AC1  4 HIS A 249  CYS A 280  CYS A 283  CAC A 402                    
SITE     1 AC2  8 THR A  -2  ASN A 240  HIS A 249  GLU A 251                    
SITE     2 AC2  8 SER A 278  CYS A 280  CYS A 283   ZN A 401                    
SITE     1 AC3  4 HIS B 249  CYS B 280  CYS B 283  CAC B 402                    
SITE     1 AC4 11 THR B  -2  ASN B 240  HIS B 249  GLU B 251                    
SITE     2 AC4 11 TRP B 277  SER B 278  PRO B 279  CYS B 280                    
SITE     3 AC4 11 TYR B 307   ZN B 401   DT C   9                               
CRYST1   60.990   92.702   93.674  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016396  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010787  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010675        0.00000                         
ATOM      1  N   TYR A -29      37.816   3.507  10.469  1.00 73.18           N  
ANISOU    1  N   TYR A -29     9137   8188  10478  -2931   -795  -1082       N  
ATOM      2  CA  TYR A -29      37.843   3.006   9.066  1.00 73.44           C  
ANISOU    2  CA  TYR A -29     8852   8551  10501  -2335   -330   -971       C  
ATOM      3  C   TYR A -29      36.838   1.861   8.840  1.00 62.10           C  
ANISOU    3  C   TYR A -29     7025   7824   8745  -1318   -532    276       C  
ATOM      4  O   TYR A -29      36.026   1.899   7.906  1.00 55.68           O  
ANISOU    4  O   TYR A -29     7579   5358   8220  -3528   -364    101       O  
ATOM      5  CB  TYR A -29      39.271   2.577   8.686  1.00 80.78           C  
ANISOU    5  CB  TYR A -29     8688   9965  12037  -2242   -256   -275       C  
ATOM      6  CG  TYR A -29      39.430   2.149   7.241  1.00 94.46           C  
ANISOU    6  CG  TYR A -29    11917  11770  12202  -1747    104   -320       C  
ATOM      7  CD1 TYR A -29      39.078   3.012   6.192  1.00 96.91           C  
ANISOU    7  CD1 TYR A -29    11901  12042  12878  -1330   -749   -184       C  
ATOM      8  CD2 TYR A -29      39.942   0.886   6.919  1.00102.79           C  
ANISOU    8  CD2 TYR A -29    13489  12087  13480   -824    270    -25       C  
ATOM      9  CE1 TYR A -29      39.220   2.624   4.867  1.00100.52           C  
ANISOU    9  CE1 TYR A -29    12571  12776  12843  -1092   -830    -60       C  
ATOM     10  CE2 TYR A -29      40.090   0.490   5.595  1.00108.94           C  
ANISOU   10  CE2 TYR A -29    14888  13030  13474   -475    132   -196       C  
ATOM     11  CZ  TYR A -29      39.727   1.362   4.576  1.00107.73           C  
ANISOU   11  CZ  TYR A -29    14150  12941  13841   -832   -588   -303       C  
ATOM     12  OH  TYR A -29      39.873   0.976   3.264  1.00108.67           O  
ANISOU   12  OH  TYR A -29    14065  13778  13446   -284  -1852   -232       O  
ATOM     13  N   PHE A -28      36.903   0.850   9.701  1.00 54.61           N  
ANISOU   13  N   PHE A -28     5591   6891   8264  -1582  -1468   -381       N  
ATOM     14  CA  PHE A -28      35.957  -0.259   9.678  1.00 48.95           C  
ANISOU   14  CA  PHE A -28     5267   6046   7284  -1055   -283   -171       C  
ATOM     15  C   PHE A -28      35.163  -0.243  10.977  1.00 45.42           C  
ANISOU   15  C   PHE A -28     4635   5837   6786   -876   -837   -217       C  
ATOM     16  O   PHE A -28      35.749  -0.370  12.052  1.00 45.92           O  
ANISOU   16  O   PHE A -28     4745   5941   6758  -1168   -927   -396       O  
ATOM     17  CB  PHE A -28      36.712  -1.584   9.521  1.00 45.94           C  
ANISOU   17  CB  PHE A -28     4678   5913   6861  -1229   -420   -205       C  
ATOM     18  CG  PHE A -28      35.835  -2.750   9.147  1.00 43.40           C  
ANISOU   18  CG  PHE A -28     4605   5516   6368   -965   -287   -109       C  
ATOM     19  CD1 PHE A -28      35.183  -3.500  10.128  1.00 38.46           C  
ANISOU   19  CD1 PHE A -28     3906   4725   5980   -848   -550   -385       C  
ATOM     20  CD2 PHE A -28      35.674  -3.113   7.809  1.00 43.04           C  
ANISOU   20  CD2 PHE A -28     4257   5742   6352  -1123   -321   -201       C  
ATOM     21  CE1 PHE A -28      34.377  -4.584   9.778  1.00 34.71           C  
ANISOU   21  CE1 PHE A -28     3352   4647   5187   -654   -770     52       C  
ATOM     22  CE2 PHE A -28      34.870  -4.199   7.452  1.00 40.97           C  
ANISOU   22  CE2 PHE A -28     4319   5382   5864  -1163   -157    131       C  
ATOM     23  CZ  PHE A -28      34.223  -4.937   8.441  1.00 34.49           C  
ANISOU   23  CZ  PHE A -28     3431   4452   5220   -824   -624   -111       C  
ATOM     24  N   GLN A -27      33.842  -0.072  10.873  1.00 40.52           N  
ANISOU   24  N   GLN A -27     4449   5235   5711  -1069   -570   -265       N  
ATOM     25  CA  GLN A -27      32.947  -0.112  12.031  1.00 36.51           C  
ANISOU   25  CA  GLN A -27     3909   4357   5604   -750   -878   -288       C  
ATOM     26  C   GLN A -27      32.624  -1.557  12.429  1.00 39.45           C  
ANISOU   26  C   GLN A -27     4586   4593   5809   -868   -980    145       C  
ATOM     27  O   GLN A -27      32.127  -2.333  11.611  1.00 36.63           O  
ANISOU   27  O   GLN A -27     4000   4350   5566   -839   -830    396       O  
ATOM     28  CB  GLN A -27      31.655   0.661  11.728  1.00 41.06           C  
ANISOU   28  CB  GLN A -27     4437   4969   6195   -407  -1150    -28       C  
ATOM     29  CG  GLN A -27      30.686   0.795  12.899  1.00 46.84           C  
ANISOU   29  CG  GLN A -27     5058   5727   7009   -536   -576    120       C  
ATOM     30  CD  GLN A -27      31.250   1.612  14.044  1.00 51.32           C  
ANISOU   30  CD  GLN A -27     5842   6068   7590   -482   -968   -299       C  
ATOM     31  OE1 GLN A -27      32.005   2.559  13.835  1.00 55.36           O  
ANISOU   31  OE1 GLN A -27     6253   6214   8565   -791   -906   -378       O  
ATOM     32  NE2 GLN A -27      30.884   1.246  15.262  1.00 53.33           N  
ANISOU   32  NE2 GLN A -27     6112   6358   7791    386   -712    273       N  
ATOM     33  N   GLY A -26      32.897  -1.911  13.685  1.00 38.43           N  
ANISOU   33  N   GLY A -26     4172   4726   5700   -752  -1261   -268       N  
ATOM     34  CA  GLY A -26      32.656  -3.274  14.169  1.00 39.15           C  
ANISOU   34  CA  GLY A -26     4317   4929   5630   -124   -661    175       C  
ATOM     35  C   GLY A -26      33.756  -4.255  13.772  1.00 38.64           C  
ANISOU   35  C   GLY A -26     3748   4951   5981   -407   -693     -4       C  
ATOM     36  O   GLY A -26      34.885  -3.860  13.509  1.00 38.17           O  
ANISOU   36  O   GLY A -26     3647   4946   5908   -580   -822   -121       O  
ATOM     37  N   SER A -25      33.421  -5.539  13.712  1.00 37.28           N  
ANISOU   37  N   SER A -25     3697   4857   5609   -243   -715    117       N  
ATOM     38  CA  SER A -25      34.418  -6.584  13.451  1.00 39.31           C  
ANISOU   38  CA  SER A -25     4042   5017   5875    -38   -839   -273       C  
ATOM     39  C   SER A -25      34.124  -7.354  12.170  1.00 35.82           C  
ANISOU   39  C   SER A -25     3300   4930   5380   -174   -610    180       C  
ATOM     40  O   SER A -25      32.985  -7.742  11.938  1.00 34.89           O  
ANISOU   40  O   SER A -25     3575   4456   5223   -600   -697    419       O  
ATOM     41  CB  SER A -25      34.466  -7.558  14.632  1.00 44.72           C  
ANISOU   41  CB  SER A -25     4932   5899   6161    780   -944     83       C  
ATOM     42  OG  SER A -25      35.000  -6.913  15.770  1.00 46.32           O  
ANISOU   42  OG  SER A -25     5028   6008   6563    661  -1068     -4       O  
ATOM     43  N   ALA A -24      35.145  -7.584  11.346  1.00 33.54           N  
ANISOU   43  N   ALA A -24     3162   4460   5122   -471   -594    178       N  
ATOM     44  CA  ALA A -24      34.985  -8.432  10.163  1.00 34.83           C  
ANISOU   44  CA  ALA A -24     3216   4724   5293   -508   -570    -28       C  
ATOM     45  C   ALA A -24      34.729  -9.875  10.601  1.00 34.87           C  
ANISOU   45  C   ALA A -24     3187   4743   5319   -555   -759      1       C  
ATOM     46  O   ALA A -24      35.033 -10.243  11.735  1.00 35.55           O  
ANISOU   46  O   ALA A -24     3581   4730   5197   -454   -728     91       O  
ATOM     47  CB  ALA A -24      36.204  -8.342   9.252  1.00 35.55           C  
ANISOU   47  CB  ALA A -24     3347   4871   5288   -658   -398   -342       C  
HETATM   48  N   MSE A -23      34.154 -10.681   9.715  1.00 31.13           N  
ANISOU   48  N   MSE A -23     2462   4354   5013   -113   -505     47       N  
HETATM   49  CA  MSE A -23      33.785 -12.067  10.056  1.00 31.95           C  
ANISOU   49  CA  MSE A -23     2778   4312   5048    -41   -456    -45       C  
HETATM   50  C   MSE A -23      34.945 -12.970   9.713  1.00 29.74           C  
ANISOU   50  C   MSE A -23     2203   4244   4852   -192   -632     88       C  
HETATM   51  O   MSE A -23      35.666 -12.718   8.749  1.00 32.37           O  
ANISOU   51  O   MSE A -23     2732   4644   4921    141   -336    210       O  
HETATM   52  CB  MSE A -23      32.579 -12.517   9.221  1.00 31.40           C  
ANISOU   52  CB  MSE A -23     2539   4368   5023   -235   -399    330       C  
HETATM   53  CG  MSE A -23      31.238 -12.062   9.783  1.00 37.60           C  
ANISOU   53  CG  MSE A -23     3448   5295   5540    870   -215    221       C  
HETATM   54 SE   MSE A -23      29.817 -12.159   8.394  1.00 40.40          SE  
ANISOU   54 SE   MSE A -23     3812   5417   6120   -102   -479    321      SE  
HETATM   55  CE  MSE A -23      30.438 -10.738   7.182  1.00 32.22           C  
ANISOU   55  CE  MSE A -23     2386   4630   5223    163   -766     38       C  
ATOM     56  N   ASP A -22      35.135 -14.039  10.479  1.00 28.98           N  
ANISOU   56  N   ASP A -22     1798   4507   4703   -103   -566     89       N  
ATOM     57  CA  ASP A -22      36.016 -15.118  10.002  1.00 32.27           C  
ANISOU   57  CA  ASP A -22     2582   4670   5006    121   -386   -130       C  
ATOM     58  C   ASP A -22      35.302 -15.882   8.874  1.00 30.76           C  
ANISOU   58  C   ASP A -22     2493   4400   4791    -78   -192    158       C  
ATOM     59  O   ASP A -22      34.066 -15.847   8.799  1.00 30.24           O  
ANISOU   59  O   ASP A -22     2525   4295   4667    129    -91    195       O  
ATOM     60  CB  ASP A -22      36.524 -16.020  11.148  1.00 35.88           C  
ANISOU   60  CB  ASP A -22     3132   5152   5347    327   -467     90       C  
ATOM     61  CG  ASP A -22      35.417 -16.637  11.961  1.00 41.42           C  
ANISOU   61  CG  ASP A -22     3812   5754   6170     11    -74     70       C  
ATOM     62  OD1 ASP A -22      34.593 -17.391  11.391  1.00 42.46           O  
ANISOU   62  OD1 ASP A -22     3685   6050   6397    164   -496    229       O  
ATOM     63  OD2 ASP A -22      35.405 -16.405  13.192  1.00 43.53           O  
ANISOU   63  OD2 ASP A -22     4753   5534   6251    252    -84   -142       O  
ATOM     64  N   PRO A -21      36.064 -16.528   7.958  1.00 31.27           N  
ANISOU   64  N   PRO A -21     2634   4456   4791    -51   -252     56       N  
ATOM     65  CA  PRO A -21      35.387 -17.186   6.831  1.00 28.89           C  
ANISOU   65  CA  PRO A -21     2170   4310   4496     13   -210    145       C  
ATOM     66  C   PRO A -21      34.271 -18.190   7.182  1.00 30.23           C  
ANISOU   66  C   PRO A -21     2366   4508   4609    -72    -70    227       C  
ATOM     67  O   PRO A -21      33.209 -18.114   6.560  1.00 29.72           O  
ANISOU   67  O   PRO A -21     2430   4167   4691      5   -120    259       O  
ATOM     68  CB  PRO A -21      36.532 -17.874   6.079  1.00 28.56           C  
ANISOU   68  CB  PRO A -21     1938   4629   4283    -56   -226    163       C  
ATOM     69  CG  PRO A -21      37.736 -17.030   6.385  1.00 32.64           C  
ANISOU   69  CG  PRO A -21     2516   4729   5157   -413   -217   -155       C  
ATOM     70  CD  PRO A -21      37.540 -16.553   7.802  1.00 34.37           C  
ANISOU   70  CD  PRO A -21     2685   5177   5195     -1   -133    -86       C  
ATOM     71  N   PRO A -20      34.490 -19.125   8.154  1.00 31.59           N  
ANISOU   71  N   PRO A -20     2624   4641   4736     92   -159    303       N  
ATOM     72  CA  PRO A -20      33.388 -20.069   8.438  1.00 29.31           C  
ANISOU   72  CA  PRO A -20     2248   4470   4419    207   -226    103       C  
ATOM     73  C   PRO A -20      32.114 -19.390   8.947  1.00 29.08           C  
ANISOU   73  C   PRO A -20     2469   4083   4497    330   -229    185       C  
ATOM     74  O   PRO A -20      31.014 -19.867   8.667  1.00 30.04           O  
ANISOU   74  O   PRO A -20     2695   3978   4741    177   -294    -43       O  
ATOM     75  CB  PRO A -20      33.980 -21.006   9.505  1.00 31.04           C  
ANISOU   75  CB  PRO A -20     2292   4717   4783    562    -93    253       C  
ATOM     76  CG  PRO A -20      35.482 -20.881   9.335  1.00 31.88           C  
ANISOU   76  CG  PRO A -20     2374   4764   4973    -53   -223    135       C  
ATOM     77  CD  PRO A -20      35.690 -19.445   8.955  1.00 31.86           C  
ANISOU   77  CD  PRO A -20     2419   4785   4898    -27   -212    152       C  
ATOM     78  N   THR A -19      32.251 -18.279   9.670  1.00 28.50           N  
ANISOU   78  N   THR A -19     2246   4153   4429    199   -252    228       N  
ATOM     79  CA  THR A -19      31.085 -17.502  10.127  1.00 27.69           C  
ANISOU   79  CA  THR A -19     2310   3920   4289    199   -155    304       C  
ATOM     80  C   THR A -19      30.308 -16.900   8.958  1.00 29.16           C  
ANISOU   80  C   THR A -19     2602   4121   4355    200   -233    379       C  
ATOM     81  O   THR A -19      29.067 -16.985   8.917  1.00 29.04           O  
ANISOU   81  O   THR A -19     2654   3645   4733    153    -46    355       O  
ATOM     82  CB  THR A -19      31.505 -16.397  11.117  1.00 30.71           C  
ANISOU   82  CB  THR A -19     2626   4334   4706    196   -378     43       C  
ATOM     83  OG1 THR A -19      32.194 -17.009  12.205  1.00 31.38           O  
ANISOU   83  OG1 THR A -19     2673   4569   4680    236   -364    141       O  
ATOM     84  CG2 THR A -19      30.307 -15.620  11.669  1.00 31.34           C  
ANISOU   84  CG2 THR A -19     2663   4124   5118    255   -336    169       C  
ATOM     85  N   PHE A -18      31.031 -16.315   8.004  1.00 28.03           N  
ANISOU   85  N   PHE A -18     2262   3754   4632    -50   -231    282       N  
ATOM     86  CA  PHE A -18      30.410 -15.771   6.800  1.00 30.55           C  
ANISOU   86  CA  PHE A -18     2738   4263   4603   -172   -412    321       C  
ATOM     87  C   PHE A -18      29.706 -16.862   6.004  1.00 30.01           C  
ANISOU   87  C   PHE A -18     2613   4115   4673     89   -311    183       C  
ATOM     88  O   PHE A -18      28.538 -16.723   5.623  1.00 27.39           O  
ANISOU   88  O   PHE A -18     2427   3630   4349    101    -57    323       O  
ATOM     89  CB  PHE A -18      31.437 -15.064   5.905  1.00 34.44           C  
ANISOU   89  CB  PHE A -18     3439   4776   4871   -487   -122    347       C  
ATOM     90  CG  PHE A -18      30.888 -14.692   4.547  1.00 33.82           C  
ANISOU   90  CG  PHE A -18     3142   4548   5159      3   -284    226       C  
ATOM     91  CD1 PHE A -18      30.156 -13.512   4.380  1.00 29.68           C  
ANISOU   91  CD1 PHE A -18     2803   3983   4489   -596   -109    549       C  
ATOM     92  CD2 PHE A -18      31.071 -15.543   3.440  1.00 29.52           C  
ANISOU   92  CD2 PHE A -18     2073   4532   4611   -351    -98    440       C  
ATOM     93  CE1 PHE A -18      29.628 -13.177   3.142  1.00 29.51           C  
ANISOU   93  CE1 PHE A -18     2644   3930   4635   -365   -236    486       C  
ATOM     94  CE2 PHE A -18      30.550 -15.205   2.200  1.00 31.80           C  
ANISOU   94  CE2 PHE A -18     2704   4690   4688   -231   -117    552       C  
ATOM     95  CZ  PHE A -18      29.827 -14.016   2.050  1.00 31.91           C  
ANISOU   95  CZ  PHE A -18     3169   4139   4814   -500    -18    331       C  
ATOM     96  N   THR A -17      30.427 -17.949   5.749  1.00 29.57           N  
ANISOU   96  N   THR A -17     2472   4076   4687    110   -258    367       N  
ATOM     97  CA  THR A -17      29.884 -19.049   4.957  1.00 29.81           C  
ANISOU   97  CA  THR A -17     2556   4088   4680     44   -292    408       C  
ATOM     98  C   THR A -17      28.590 -19.583   5.575  1.00 30.39           C  
ANISOU   98  C   THR A -17     2691   4039   4815     98    -84    371       C  
ATOM     99  O   THR A -17      27.595 -19.756   4.876  1.00 29.59           O  
ANISOU   99  O   THR A -17     2618   3899   4724     17     30    191       O  
ATOM    100  CB  THR A -17      30.952 -20.134   4.751  1.00 32.03           C  
ANISOU  100  CB  THR A -17     2838   4560   4772    231    178    -36       C  
ATOM    101  OG1 THR A -17      32.022 -19.537   4.018  1.00 33.44           O  
ANISOU  101  OG1 THR A -17     2467   5131   5105     74    -91    -89       O  
ATOM    102  CG2 THR A -17      30.394 -21.324   3.972  1.00 36.26           C  
ANISOU  102  CG2 THR A -17     3406   5053   5318   -102   -328   -135       C  
ATOM    103  N   PHE A -16      28.608 -19.792   6.890  1.00 32.18           N  
ANISOU  103  N   PHE A -16     3181   4281   4763    315     23    384       N  
ATOM    104  CA  PHE A -16      27.434 -20.212   7.641  1.00 30.09           C  
ANISOU  104  CA  PHE A -16     2644   4076   4713    287   -271    286       C  
ATOM    105  C   PHE A -16      26.285 -19.205   7.526  1.00 30.49           C  
ANISOU  105  C   PHE A -16     2757   3991   4836    229   -362    370       C  
ATOM    106  O   PHE A -16      25.147 -19.584   7.229  1.00 27.93           O  
ANISOU  106  O   PHE A -16     2618   3708   4283    207   -143    -12       O  
ATOM    107  CB  PHE A -16      27.809 -20.413   9.117  1.00 30.57           C  
ANISOU  107  CB  PHE A -16     2859   4006   4748    588   -121    393       C  
ATOM    108  CG  PHE A -16      26.696 -20.939   9.966  1.00 31.70           C  
ANISOU  108  CG  PHE A -16     2825   4284   4935    704    -60    568       C  
ATOM    109  CD1 PHE A -16      26.347 -22.299   9.932  1.00 34.13           C  
ANISOU  109  CD1 PHE A -16     3109   4539   5320    383   -189    411       C  
ATOM    110  CD2 PHE A -16      25.993 -20.088  10.819  1.00 32.88           C  
ANISOU  110  CD2 PHE A -16     3486   4075   4932    485     16    306       C  
ATOM    111  CE1 PHE A -16      25.319 -22.782  10.732  1.00 33.29           C  
ANISOU  111  CE1 PHE A -16     3128   4360   5159    577    -68    430       C  
ATOM    112  CE2 PHE A -16      24.954 -20.565  11.614  1.00 31.14           C  
ANISOU  112  CE2 PHE A -16     2745   4197   4888    615   -299    427       C  
ATOM    113  CZ  PHE A -16      24.625 -21.914  11.574  1.00 33.03           C  
ANISOU  113  CZ  PHE A -16     3065   4304   5179    592   -327    245       C  
ATOM    114  N   ASN A -15      26.591 -17.929   7.760  1.00 28.19           N  
ANISOU  114  N   ASN A -15     2464   3870   4376    183   -153    365       N  
ATOM    115  CA  ASN A -15      25.556 -16.902   7.900  1.00 27.84           C  
ANISOU  115  CA  ASN A -15     2803   3521   4252    180   -475    271       C  
ATOM    116  C   ASN A -15      24.982 -16.363   6.622  1.00 26.42           C  
ANISOU  116  C   ASN A -15     2699   3202   4137   -101   -217    402       C  
ATOM    117  O   ASN A -15      23.842 -15.890   6.609  1.00 30.38           O  
ANISOU  117  O   ASN A -15     2853   3908   4779    181   -101   -165       O  
ATOM    118  CB  ASN A -15      26.041 -15.766   8.785  1.00 25.52           C  
ANISOU  118  CB  ASN A -15     2356   3221   4116    152   -336    458       C  
ATOM    119  CG  ASN A -15      25.881 -16.103  10.243  1.00 26.33           C  
ANISOU  119  CG  ASN A -15     2527   3386   4091    344   -434    393       C  
ATOM    120  OD1 ASN A -15      24.778 -16.015  10.793  1.00 29.13           O  
ANISOU  120  OD1 ASN A -15     2760   3920   4386    243   -174    386       O  
ATOM    121  ND2 ASN A -15      26.957 -16.557  10.861  1.00 25.12           N  
ANISOU  121  ND2 ASN A -15     2235   3398   3909    143   -318    383       N  
ATOM    122  N   PHE A -14      25.746 -16.457   5.540  1.00 24.61           N  
ANISOU  122  N   PHE A -14     2257   3063   4030   -283   -285    373       N  
ATOM    123  CA  PHE A -14      25.265 -15.918   4.269  1.00 26.42           C  
ANISOU  123  CA  PHE A -14     2565   3351   4119   -176   -266    573       C  
ATOM    124  C   PHE A -14      24.772 -16.975   3.302  1.00 27.72           C  
ANISOU  124  C   PHE A -14     2731   3331   4468   -262   -307    440       C  
ATOM    125  O   PHE A -14      24.378 -16.650   2.176  1.00 27.68           O  
ANISOU  125  O   PHE A -14     2310   3744   4462    -30   -180    323       O  
ATOM    126  CB  PHE A -14      26.283 -14.942   3.663  1.00 24.89           C  
ANISOU  126  CB  PHE A -14     2162   3416   3879    -26   -263    478       C  
ATOM    127  CG  PHE A -14      26.226 -13.607   4.325  1.00 27.74           C  
ANISOU  127  CG  PHE A -14     2709   3417   4413   -362   -405    342       C  
ATOM    128  CD1 PHE A -14      26.831 -13.416   5.570  1.00 27.43           C  
ANISOU  128  CD1 PHE A -14     2464   3569   4389   -545   -338    451       C  
ATOM    129  CD2 PHE A -14      25.434 -12.592   3.794  1.00 28.93           C  
ANISOU  129  CD2 PHE A -14     3022   3605   4364   -273   -458    424       C  
ATOM    130  CE1 PHE A -14      26.728 -12.194   6.231  1.00 29.00           C  
ANISOU  130  CE1 PHE A -14     2808   3578   4630     24    -77    524       C  
ATOM    131  CE2 PHE A -14      25.315 -11.375   4.442  1.00 26.95           C  
ANISOU  131  CE2 PHE A -14     2252   3518   4468   -241   -379    467       C  
ATOM    132  CZ  PHE A -14      25.954 -11.176   5.670  1.00 27.88           C  
ANISOU  132  CZ  PHE A -14     2913   3485   4192   -248   -377    583       C  
ATOM    133  N   ASN A -13      24.774 -18.226   3.759  1.00 25.72           N  
ANISOU  133  N   ASN A -13     2219   2840   4710   -284    -52    -59       N  
ATOM    134  CA  ASN A -13      24.154 -19.313   3.000  1.00 27.85           C  
ANISOU  134  CA  ASN A -13     2425   2902   5253   -322   -181   -260       C  
ATOM    135  C   ASN A -13      22.712 -18.932   2.642  1.00 29.79           C  
ANISOU  135  C   ASN A -13     2488   3516   5312   -174   -168   -362       C  
ATOM    136  O   ASN A -13      21.963 -18.450   3.503  1.00 28.58           O  
ANISOU  136  O   ASN A -13     2126   3554   5179   -209   -223   -237       O  
ATOM    137  CB  ASN A -13      24.148 -20.609   3.785  1.00 29.91           C  
ANISOU  137  CB  ASN A -13     2633   3178   5552   -290   -146      0       C  
ATOM    138  CG  ASN A -13      23.609 -21.757   2.960  1.00 35.28           C  
ANISOU  138  CG  ASN A -13     3142   3539   6721   -838   -166   -326       C  
ATOM    139  OD1 ASN A -13      22.415 -22.043   2.976  1.00 30.64           O  
ANISOU  139  OD1 ASN A -13     3035   2796   5807   -654      8   -186       O  
ATOM    140  ND2 ASN A -13      24.473 -22.351   2.153  1.00 42.38           N  
ANISOU  140  ND2 ASN A -13     4238   4589   7273   -324    -12   -896       N  
ATOM    141  N   ASN A -12      22.335 -19.124   1.379  1.00 29.52           N  
ANISOU  141  N   ASN A -12     2532   3356   5327   -140   -246   -348       N  
ATOM    142  CA  ASN A -12      21.035 -18.603   0.920  1.00 29.37           C  
ANISOU  142  CA  ASN A -12     2602   3397   5161    -38   -133   -469       C  
ATOM    143  C   ASN A -12      19.945 -19.631   0.623  1.00 30.95           C  
ANISOU  143  C   ASN A -12     2553   3715   5490   -304    304   -492       C  
ATOM    144  O   ASN A -12      19.020 -19.344  -0.129  1.00 35.43           O  
ANISOU  144  O   ASN A -12     3164   4283   6014    -17   -156   -623       O  
ATOM    145  CB  ASN A -12      21.238 -17.619  -0.246  1.00 25.83           C  
ANISOU  145  CB  ASN A -12     1839   3146   4828    -28   -370   -613       C  
ATOM    146  CG  ASN A -12      21.677 -18.297  -1.533  1.00 29.06           C  
ANISOU  146  CG  ASN A -12     2505   3404   5131     58    -90   -727       C  
ATOM    147  OD1 ASN A -12      22.113 -19.460  -1.542  1.00 28.03           O  
ANISOU  147  OD1 ASN A -12     2169   3318   5160    -27    -36   -801       O  
ATOM    148  ND2 ASN A -12      21.532 -17.575  -2.647  1.00 28.39           N  
ANISOU  148  ND2 ASN A -12     2258   3251   5279   -269   -313   -640       N  
ATOM    149  N   GLU A -11      20.041 -20.823   1.209  1.00 31.55           N  
ANISOU  149  N   GLU A -11     2727   3615   5644   -280    418   -552       N  
ATOM    150  CA  GLU A -11      18.902 -21.763   1.195  1.00 35.71           C  
ANISOU  150  CA  GLU A -11     2855   4277   6435   -606    -51   -975       C  
ATOM    151  C   GLU A -11      17.705 -21.049   1.850  1.00 37.48           C  
ANISOU  151  C   GLU A -11     3118   4998   6123   -409     37   -846       C  
ATOM    152  O   GLU A -11      17.843 -20.505   2.955  1.00 35.86           O  
ANISOU  152  O   GLU A -11     2863   4510   6250   -723    599  -1121       O  
ATOM    153  CB  GLU A -11      19.238 -23.030   1.974  1.00 47.24           C  
ANISOU  153  CB  GLU A -11     5203   5533   7212   -601     -1    210       C  
ATOM    154  CG  GLU A -11      18.921 -24.323   1.251  1.00 64.04           C  
ANISOU  154  CG  GLU A -11     8193   6613   9525   -456     54  -1099       C  
ATOM    155  CD  GLU A -11      20.139 -24.899   0.575  1.00 73.47           C  
ANISOU  155  CD  GLU A -11     8192   7820  11904    100    510   -407       C  
ATOM    156  OE1 GLU A -11      21.143 -25.144   1.275  1.00 84.11           O  
ANISOU  156  OE1 GLU A -11     9453  10141  12361  -1623   -934   -578       O  
ATOM    157  OE2 GLU A -11      20.084 -25.124  -0.648  1.00 75.68           O  
ANISOU  157  OE2 GLU A -11     8317   8609  11829    289   -363    249       O  
ATOM    158  N   PRO A -10      16.542 -21.018   1.166  1.00 34.94           N  
ANISOU  158  N   PRO A -10     2742   4522   6010   -425    294   -905       N  
ATOM    159  CA  PRO A -10      15.424 -20.212   1.672  1.00 33.23           C  
ANISOU  159  CA  PRO A -10     2569   4424   5632   -572    221   -933       C  
ATOM    160  C   PRO A -10      14.933 -20.570   3.086  1.00 35.43           C  
ANISOU  160  C   PRO A -10     2737   4857   5867   -597    177   -560       C  
ATOM    161  O   PRO A -10      14.426 -19.691   3.781  1.00 37.35           O  
ANISOU  161  O   PRO A -10     3020   5114   6056   -504    346   -742       O  
ATOM    162  CB  PRO A -10      14.331 -20.442   0.625  1.00 33.41           C  
ANISOU  162  CB  PRO A -10     2432   4454   5805     16     82   -839       C  
ATOM    163  CG  PRO A -10      15.099 -20.699  -0.633  1.00 37.71           C  
ANISOU  163  CG  PRO A -10     3101   5244   5982     59    418   -618       C  
ATOM    164  CD  PRO A -10      16.267 -21.537  -0.191  1.00 35.33           C  
ANISOU  164  CD  PRO A -10     2387   5031   6006   -244    371  -1014       C  
ATOM    165  N   TRP A  -9      15.120 -21.817   3.524  1.00 34.87           N  
ANISOU  165  N   TRP A  -9     3055   4266   5925  -1145    274   -922       N  
ATOM    166  CA  TRP A  -9      14.646 -22.239   4.857  1.00 36.34           C  
ANISOU  166  CA  TRP A  -9     3274   4544   5988  -1013    269   -699       C  
ATOM    167  C   TRP A  -9      15.730 -22.748   5.828  1.00 40.16           C  
ANISOU  167  C   TRP A  -9     3385   4981   6893   -908     54   -368       C  
ATOM    168  O   TRP A  -9      15.459 -23.596   6.667  1.00 46.36           O  
ANISOU  168  O   TRP A  -9     4071   5892   7653  -1276     83    172       O  
ATOM    169  CB  TRP A  -9      13.552 -23.301   4.728  1.00 37.31           C  
ANISOU  169  CB  TRP A  -9     3012   4815   6347   -983    366   -633       C  
ATOM    170  CG  TRP A  -9      12.354 -22.880   3.932  1.00 39.46           C  
ANISOU  170  CG  TRP A  -9     3116   5344   6533   -920    162  -1013       C  
ATOM    171  CD1 TRP A  -9      11.267 -22.204   4.392  1.00 39.25           C  
ANISOU  171  CD1 TRP A  -9     3099   5088   6723  -1113    515  -1190       C  
ATOM    172  CD2 TRP A  -9      12.120 -23.127   2.536  1.00 38.21           C  
ANISOU  172  CD2 TRP A  -9     2944   5182   6390  -1133    389   -862       C  
ATOM    173  NE1 TRP A  -9      10.359 -22.010   3.370  1.00 44.87           N  
ANISOU  173  NE1 TRP A  -9     3707   6554   6787   -741    284  -1318       N  
ATOM    174  CE2 TRP A  -9      10.856 -22.568   2.221  1.00 42.12           C  
ANISOU  174  CE2 TRP A  -9     3302   5745   6957   -677    205  -1183       C  
ATOM    175  CE3 TRP A  -9      12.854 -23.774   1.523  1.00 40.80           C  
ANISOU  175  CE3 TRP A  -9     3522   5200   6778   -847    648   -791       C  
ATOM    176  CZ2 TRP A  -9      10.307 -22.622   0.933  1.00 43.68           C  
ANISOU  176  CZ2 TRP A  -9     3223   6375   6997   -833    205  -1251       C  
ATOM    177  CZ3 TRP A  -9      12.311 -23.838   0.237  1.00 45.01           C  
ANISOU  177  CZ3 TRP A  -9     3613   6177   7310   -651    304  -1051       C  
ATOM    178  CH2 TRP A  -9      11.040 -23.263  -0.046  1.00 51.05           C  
ANISOU  178  CH2 TRP A  -9     3784   7622   7989   -105    467  -1304       C  
ATOM    179  N   VAL A  -8      16.936 -22.218   5.756  1.00 38.93           N  
ANISOU  179  N   VAL A  -8     3525   4453   6812   -936    185   -285       N  
ATOM    180  CA  VAL A  -8      18.034 -22.709   6.616  1.00 41.13           C  
ANISOU  180  CA  VAL A  -8     3997   5020   6608   -921     11     -6       C  
ATOM    181  C   VAL A  -8      17.689 -22.747   8.104  1.00 39.86           C  
ANISOU  181  C   VAL A  -8     3607   4923   6612   -905    227    -68       C  
ATOM    182  O   VAL A  -8      16.999 -21.871   8.618  1.00 40.04           O  
ANISOU  182  O   VAL A  -8     4462   4250   6500   -644   -131    -68       O  
ATOM    183  CB  VAL A  -8      19.336 -21.895   6.469  1.00 42.26           C  
ANISOU  183  CB  VAL A  -8     4037   4884   7132   -959    101     36       C  
ATOM    184  CG1 VAL A  -8      19.946 -22.091   5.106  1.00 49.74           C  
ANISOU  184  CG1 VAL A  -8     5462   6118   7317  -1387    285   -950       C  
ATOM    185  CG2 VAL A  -8      19.108 -20.425   6.775  1.00 41.59           C  
ANISOU  185  CG2 VAL A  -8     4952   4704   6145  -1053     32    215       C  
ATOM    186  N   ARG A  -7      18.166 -23.786   8.777  1.00 40.59           N  
ANISOU  186  N   ARG A  -7     4046   4734   6641  -1114    -62     32       N  
ATOM    187  CA  ARG A  -7      17.997 -23.928  10.219  1.00 38.82           C  
ANISOU  187  CA  ARG A  -7     3537   4641   6571  -1536     70    280       C  
ATOM    188  C   ARG A  -7      19.210 -23.344  10.939  1.00 34.97           C  
ANISOU  188  C   ARG A  -7     3519   3900   5868  -1198    119    345       C  
ATOM    189  O   ARG A  -7      20.322 -23.363  10.410  1.00 37.45           O  
ANISOU  189  O   ARG A  -7     3676   4237   6314  -1237    459    519       O  
ATOM    190  CB  ARG A  -7      17.877 -25.412  10.588  1.00 46.77           C  
ANISOU  190  CB  ARG A  -7     5214   4984   7570  -1501     70    937       C  
ATOM    191  CG  ARG A  -7      16.940 -26.218   9.693  1.00 55.50           C  
ANISOU  191  CG  ARG A  -7     5811   6754   8521  -1818   -298    120       C  
ATOM    192  CD  ARG A  -7      16.463 -27.497  10.356  1.00 64.77           C  
ANISOU  192  CD  ARG A  -7     6794   7326  10490  -2366    398    474       C  
ATOM    193  NE  ARG A  -7      15.556 -27.194  11.464  1.00 68.40           N  
ANISOU  193  NE  ARG A  -7     9153   7070   9765  -2277    874    737       N  
ATOM    194  CZ  ARG A  -7      15.872 -27.333  12.746  1.00 61.00           C  
ANISOU  194  CZ  ARG A  -7     6800   6350  10024  -1791    524    664       C  
ATOM    195  NH1 ARG A  -7      17.056 -27.806  13.087  1.00 60.28           N  
ANISOU  195  NH1 ARG A  -7     6527   5897  10478  -2483   -674    148       N  
ATOM    196  NH2 ARG A  -7      14.994 -27.020  13.683  1.00 67.73           N  
ANISOU  196  NH2 ARG A  -7     8655   6873  10207  -1864   1353    129       N  
ATOM    197  N   GLY A  -6      18.995 -22.846  12.149  1.00 36.10           N  
ANISOU  197  N   GLY A  -6     3677   4155   5884  -1099    158    317       N  
ATOM    198  CA  GLY A  -6      20.102 -22.551  13.062  1.00 35.52           C  
ANISOU  198  CA  GLY A  -6     3650   4114   5730  -1115    273    267       C  
ATOM    199  C   GLY A  -6      20.852 -21.251  12.876  1.00 35.20           C  
ANISOU  199  C   GLY A  -6     3797   4019   5557   -974    366    605       C  
ATOM    200  O   GLY A  -6      21.953 -21.106  13.419  1.00 39.21           O  
ANISOU  200  O   GLY A  -6     3994   4580   6324  -1208     42    457       O  
ATOM    201  N   ARG A  -5      20.274 -20.313  12.122  1.00 33.18           N  
ANISOU  201  N   ARG A  -5     3585   3823   5197   -883    165    278       N  
ATOM    202  CA  ARG A  -5      20.867 -18.972  11.929  1.00 31.32           C  
ANISOU  202  CA  ARG A  -5     3106   3836   4956   -913    208    184       C  
ATOM    203  C   ARG A  -5      20.154 -17.966  12.822  1.00 32.80           C  
ANISOU  203  C   ARG A  -5     3363   3957   5143   -613     63    152       C  
ATOM    204  O   ARG A  -5      19.197 -17.318  12.394  1.00 33.97           O  
ANISOU  204  O   ARG A  -5     3503   4172   5229   -594   -131    397       O  
ATOM    205  CB  ARG A  -5      20.811 -18.522  10.448  1.00 31.79           C  
ANISOU  205  CB  ARG A  -5     3140   3799   5140   -495     90    294       C  
ATOM    206  CG  ARG A  -5      21.980 -19.012   9.576  1.00 30.82           C  
ANISOU  206  CG  ARG A  -5     3271   3322   5117   -612     92     32       C  
ATOM    207  CD  ARG A  -5      21.953 -20.542   9.397  1.00 30.31           C  
ANISOU  207  CD  ARG A  -5     3172   3207   5136   -564    -88     88       C  
ATOM    208  NE  ARG A  -5      22.943 -20.982   8.411  1.00 30.71           N  
ANISOU  208  NE  ARG A  -5     2821   3461   5386   -749    -39    205       N  
ATOM    209  CZ  ARG A  -5      23.193 -22.253   8.099  1.00 35.48           C  
ANISOU  209  CZ  ARG A  -5     3778   3667   6033   -671    209    140       C  
ATOM    210  NH1 ARG A  -5      22.535 -23.236   8.702  1.00 35.58           N  
ANISOU  210  NH1 ARG A  -5     4082   3245   6190   -850     59    -21       N  
ATOM    211  NH2 ARG A  -5      24.116 -22.545   7.188  1.00 34.53           N  
ANISOU  211  NH2 ARG A  -5     3417   3608   6094   -133   -127      0       N  
ATOM    212  N   HIS A  -4      20.607 -17.867  14.072  1.00 30.94           N  
ANISOU  212  N   HIS A  -4     2962   3887   4905   -926    178    406       N  
ATOM    213  CA  HIS A  -4      19.933 -17.042  15.078  1.00 33.96           C  
ANISOU  213  CA  HIS A  -4     3566   4358   4979   -710    232    464       C  
ATOM    214  C   HIS A  -4      20.407 -15.603  15.077  1.00 35.89           C  
ANISOU  214  C   HIS A  -4     3803   4478   5354   -765    231    478       C  
ATOM    215  O   HIS A  -4      19.780 -14.744  15.685  1.00 38.57           O  
ANISOU  215  O   HIS A  -4     3486   5165   6003   -559     66   -110       O  
ATOM    216  CB  HIS A  -4      20.114 -17.660  16.460  1.00 32.35           C  
ANISOU  216  CB  HIS A  -4     3259   4262   4770   -962    306    358       C  
ATOM    217  CG  HIS A  -4      19.523 -19.026  16.558  1.00 37.46           C  
ANISOU  217  CG  HIS A  -4     4177   4446   5607  -1157    295    924       C  
ATOM    218  ND1 HIS A  -4      18.175 -19.236  16.757  1.00 38.93           N  
ANISOU  218  ND1 HIS A  -4     4044   5025   5720   -971    690    605       N  
ATOM    219  CD2 HIS A  -4      20.075 -20.249  16.393  1.00 38.86           C  
ANISOU  219  CD2 HIS A  -4     4269   4619   5878   -903    170    883       C  
ATOM    220  CE1 HIS A  -4      17.930 -20.535  16.760  1.00 41.88           C  
ANISOU  220  CE1 HIS A  -4     4507   5053   6351   -852    319    589       C  
ATOM    221  NE2 HIS A  -4      19.067 -21.171  16.540  1.00 40.29           N  
ANISOU  221  NE2 HIS A  -4     4369   4724   6212  -1078    309    732       N  
ATOM    222  N   GLU A  -3      21.520 -15.355  14.402  1.00 33.04           N  
ANISOU  222  N   GLU A  -3     3448   4081   5023   -560    -14    767       N  
ATOM    223  CA  GLU A  -3      22.078 -14.019  14.304  1.00 31.73           C  
ANISOU  223  CA  GLU A  -3     3546   3906   4601   -464    -44    567       C  
ATOM    224  C   GLU A  -3      21.656 -13.363  12.978  1.00 28.51           C  
ANISOU  224  C   GLU A  -3     2691   3702   4438   -173     93    277       C  
ATOM    225  O   GLU A  -3      21.391 -14.044  11.990  1.00 30.54           O  
ANISOU  225  O   GLU A  -3     2796   3942   4863   -211   -543    274       O  
ATOM    226  CB  GLU A  -3      23.614 -14.111  14.413  1.00 37.74           C  
ANISOU  226  CB  GLU A  -3     3724   4641   5975   -195   -428    600       C  
ATOM    227  CG  GLU A  -3      24.345 -12.776  14.450  1.00 40.71           C  
ANISOU  227  CG  GLU A  -3     4024   5106   6336   -618    340    407       C  
ATOM    228  CD  GLU A  -3      24.004 -11.943  15.675  1.00 42.86           C  
ANISOU  228  CD  GLU A  -3     4939   5359   5987   -141   -255    451       C  
ATOM    229  OE1 GLU A  -3      23.117 -11.064  15.576  1.00 40.64           O  
ANISOU  229  OE1 GLU A  -3     4758   5040   5643   -370   -395    361       O  
ATOM    230  OE2 GLU A  -3      24.611 -12.174  16.735  1.00 43.52           O  
ANISOU  230  OE2 GLU A  -3     4803   5573   6158    133   -417    607       O  
ATOM    231  N   THR A  -2      21.566 -12.037  12.978  1.00 28.90           N  
ANISOU  231  N   THR A  -2     2689   3834   4456   -118    139    336       N  
ATOM    232  CA  THR A  -2      21.472 -11.249  11.766  1.00 28.79           C  
ANISOU  232  CA  THR A  -2     2791   4111   4035   -128    246    190       C  
ATOM    233  C   THR A  -2      22.790 -10.489  11.621  1.00 29.09           C  
ANISOU  233  C   THR A  -2     3025   3877   4150   -227     -3    184       C  
ATOM    234  O   THR A  -2      23.166  -9.711  12.517  1.00 29.94           O  
ANISOU  234  O   THR A  -2     3109   3861   4404   -116    -35    201       O  
ATOM    235  CB  THR A  -2      20.310 -10.243  11.821  1.00 33.14           C  
ANISOU  235  CB  THR A  -2     3291   4485   4813    243     40    118       C  
ATOM    236  OG1 THR A  -2      19.064 -10.958  11.879  1.00 37.51           O  
ANISOU  236  OG1 THR A  -2     3515   5169   5566   -128    259   -301       O  
ATOM    237  CG2 THR A  -2      20.311  -9.346  10.581  1.00 33.36           C  
ANISOU  237  CG2 THR A  -2     3327   4417   4930    377    534    112       C  
ATOM    238  N   TYR A  -1      23.496 -10.749  10.517  1.00 28.05           N  
ANISOU  238  N   TYR A  -1     3471   3086   4098    -72     91     78       N  
ATOM    239  CA  TYR A  -1      24.653  -9.957  10.139  1.00 28.31           C  
ANISOU  239  CA  TYR A  -1     3744   3019   3991   -182     26    -24       C  
ATOM    240  C   TYR A  -1      24.263  -8.907   9.118  1.00 30.90           C  
ANISOU  240  C   TYR A  -1     4497   3246   3995   -125   -124     72       C  
ATOM    241  O   TYR A  -1      23.559  -9.159   8.146  1.00 29.35           O  
ANISOU  241  O   TYR A  -1     4058   3179   3913     21   -129    530       O  
ATOM    242  CB  TYR A  -1      25.777 -10.800   9.566  1.00 29.36           C  
ANISOU  242  CB  TYR A  -1     4004   3131   4018   -205    377   -193       C  
ATOM    243  CG  TYR A  -1      26.552 -11.492  10.645  1.00 33.40           C  
ANISOU  243  CG  TYR A  -1     4467   3957   4266     48    176      3       C  
ATOM    244  CD1 TYR A  -1      26.109 -12.707  11.169  1.00 33.60           C  
ANISOU  244  CD1 TYR A  -1     4276   3955   4536    -75    615   -250       C  
ATOM    245  CD2 TYR A  -1      27.719 -10.918  11.166  1.00 37.20           C  
ANISOU  245  CD2 TYR A  -1     4779   4555   4800   -492    348     48       C  
ATOM    246  CE1 TYR A  -1      26.824 -13.350  12.171  1.00 39.51           C  
ANISOU  246  CE1 TYR A  -1     5135   4767   5107     84    116   -153       C  
ATOM    247  CE2 TYR A  -1      28.442 -11.551  12.161  1.00 37.05           C  
ANISOU  247  CE2 TYR A  -1     4462   4566   5048    -96    234   -385       C  
ATOM    248  CZ  TYR A  -1      27.983 -12.755  12.663  1.00 39.69           C  
ANISOU  248  CZ  TYR A  -1     4922   4674   5484    -39    414   -162       C  
ATOM    249  OH  TYR A  -1      28.680 -13.364  13.653  1.00 41.76           O  
ANISOU  249  OH  TYR A  -1     5256   5086   5523    151    131   -259       O  
ATOM    250  N   LEU A 218      24.793  -7.665   9.555  1.00 26.26           N  
ANISOU  250  N   LEU A 218     3642   2715   3620   -155    -91    299       N  
ATOM    251  CA  LEU A 218      24.445  -6.500   8.751  1.00 25.19           C  
ANISOU  251  CA  LEU A 218     3732   2328   3510    -99    -96     76       C  
ATOM    252  C   LEU A 218      25.694  -5.756   8.289  1.00 28.55           C  
ANISOU  252  C   LEU A 218     4092   2844   3911   -304    209    202       C  
ATOM    253  O   LEU A 218      26.232  -4.918   9.012  1.00 30.35           O  
ANISOU  253  O   LEU A 218     4079   3134   4318   -227   -251    160       O  
ATOM    254  CB  LEU A 218      23.533  -5.558   9.539  1.00 25.51           C  
ANISOU  254  CB  LEU A 218     3684   2323   3685   -150    -11     75       C  
ATOM    255  CG  LEU A 218      22.818  -4.473   8.730  1.00 29.15           C  
ANISOU  255  CG  LEU A 218     4240   2789   4044    132   -236    384       C  
ATOM    256  CD1 LEU A 218      21.695  -3.848   9.544  1.00 29.92           C  
ANISOU  256  CD1 LEU A 218     4017   3192   4159    272   -524     54       C  
ATOM    257  CD2 LEU A 218      23.803  -3.412   8.265  1.00 30.33           C  
ANISOU  257  CD2 LEU A 218     4384   3085   4055     18    186    332       C  
ATOM    258  N   CYS A 219      26.149  -6.069   7.080  1.00 28.20           N  
ANISOU  258  N   CYS A 219     4163   2814   3734    -16     66    401       N  
ATOM    259  CA  CYS A 219      27.333  -5.432   6.520  1.00 30.11           C  
ANISOU  259  CA  CYS A 219     4363   3163   3912   -381    147    271       C  
ATOM    260  C   CYS A 219      26.881  -4.187   5.786  1.00 33.40           C  
ANISOU  260  C   CYS A 219     4919   3225   4545   -512   -298    477       C  
ATOM    261  O   CYS A 219      25.791  -4.175   5.212  1.00 31.66           O  
ANISOU  261  O   CYS A 219     4795   2993   4238   -277   -204    537       O  
ATOM    262  CB  CYS A 219      28.049  -6.344   5.532  1.00 27.20           C  
ANISOU  262  CB  CYS A 219     3985   2879   3469   -964    -58     64       C  
ATOM    263  SG  CYS A 219      28.414  -8.004   6.130  1.00 32.42           S  
ANISOU  263  SG  CYS A 219     4295   3404   4618   -346   -383    350       S  
ATOM    264  N   PHE A 220      27.697  -3.139   5.802  1.00 30.74           N  
ANISOU  264  N   PHE A 220     4665   2985   4028   -431     39    470       N  
ATOM    265  CA  PHE A 220      27.305  -1.907   5.110  1.00 30.61           C  
ANISOU  265  CA  PHE A 220     4738   2931   3961   -444   -272    358       C  
ATOM    266  C   PHE A 220      28.473  -1.229   4.419  1.00 33.47           C  
ANISOU  266  C   PHE A 220     5264   3294   4158   -464      5    699       C  
ATOM    267  O   PHE A 220      29.621  -1.360   4.859  1.00 34.05           O  
ANISOU  267  O   PHE A 220     5158   3090   4690   -808   -500     96       O  
ATOM    268  CB  PHE A 220      26.593  -0.920   6.064  1.00 33.11           C  
ANISOU  268  CB  PHE A 220     4962   3266   4352   -335     34    284       C  
ATOM    269  CG  PHE A 220      27.524  -0.200   7.023  1.00 35.76           C  
ANISOU  269  CG  PHE A 220     5274   3299   5013   -602   -100    320       C  
ATOM    270  CD1 PHE A 220      27.876  -0.777   8.252  1.00 36.79           C  
ANISOU  270  CD1 PHE A 220     5373   3896   4709   -550     77    172       C  
ATOM    271  CD2 PHE A 220      28.052   1.058   6.694  1.00 32.15           C  
ANISOU  271  CD2 PHE A 220     4868   3008   4340   -157     84    204       C  
ATOM    272  CE1 PHE A 220      28.733  -0.115   9.129  1.00 34.26           C  
ANISOU  272  CE1 PHE A 220     4837   3434   4743   -424    129    430       C  
ATOM    273  CE2 PHE A 220      28.917   1.715   7.559  1.00 34.48           C  
ANISOU  273  CE2 PHE A 220     5299   3223   4577   -579    -70    408       C  
ATOM    274  CZ  PHE A 220      29.255   1.134   8.784  1.00 34.22           C  
ANISOU  274  CZ  PHE A 220     5067   3220   4714   -302   -231    390       C  
ATOM    275  N   THR A 221      28.172  -0.534   3.320  1.00 32.35           N  
ANISOU  275  N   THR A 221     5227   3058   4005   -242    105    423       N  
ATOM    276  CA  THR A 221      29.059   0.483   2.780  1.00 37.15           C  
ANISOU  276  CA  THR A 221     5796   3520   4797   -838      9    689       C  
ATOM    277  C   THR A 221      28.248   1.764   2.647  1.00 40.17           C  
ANISOU  277  C   THR A 221     6148   3804   5308   -768    -75    855       C  
ATOM    278  O   THR A 221      27.012   1.737   2.503  1.00 39.77           O  
ANISOU  278  O   THR A 221     6069   3653   5387   -129   -711    898       O  
ATOM    279  CB  THR A 221      29.684   0.119   1.411  1.00 44.13           C  
ANISOU  279  CB  THR A 221     7077   4690   4997   -245    285    588       C  
ATOM    280  OG1 THR A 221      28.650  -0.007   0.435  1.00 51.26           O  
ANISOU  280  OG1 THR A 221     7875   5787   5813   -427   -280    549       O  
ATOM    281  CG2 THR A 221      30.460  -1.187   1.477  1.00 43.11           C  
ANISOU  281  CG2 THR A 221     6163   4575   5640   -544    146    414       C  
HETATM  282  N   MSE A 222      28.947   2.884   2.709  1.00 36.69           N  
ANISOU  282  N   MSE A 222     5883   3473   4584   -653    149    528       N  
HETATM  283  CA  MSE A 222      28.307   4.174   2.652  1.00 39.94           C  
ANISOU  283  CA  MSE A 222     6267   3806   5101   -638   -304    726       C  
HETATM  284  C   MSE A 222      29.215   5.119   1.924  1.00 42.91           C  
ANISOU  284  C   MSE A 222     6991   3897   5414   -810    -72   1246       C  
HETATM  285  O   MSE A 222      30.408   5.205   2.226  1.00 43.71           O  
ANISOU  285  O   MSE A 222     6836   3733   6035   -930   -246    888       O  
HETATM  286  CB  MSE A 222      28.002   4.582   4.096  1.00 39.60           C  
ANISOU  286  CB  MSE A 222     6278   3807   4960  -1437   -147    542       C  
HETATM  287  CG  MSE A 222      27.855   6.073   4.323  1.00 49.42           C  
ANISOU  287  CG  MSE A 222     7806   3979   6991     40   -544    980       C  
HETATM  288 SE   MSE A 222      27.534   6.397   6.241  1.00 60.02          SE  
ANISOU  288 SE   MSE A 222     9174   6060   7569   -234    159    507      SE  
HETATM  289  CE  MSE A 222      28.850   5.281   7.152  1.00 57.83           C  
ANISOU  289  CE  MSE A 222     8732   6779   6462   -152    170    515       C  
ATOM    290  N   GLU A 223      28.650   5.814   0.941  1.00 45.19           N  
ANISOU  290  N   GLU A 223     7195   4377   5596   -383     76   1115       N  
ATOM    291  CA  GLU A 223      29.321   6.953   0.331  1.00 45.35           C  
ANISOU  291  CA  GLU A 223     6996   4238   5995   -958   -118   1267       C  
ATOM    292  C   GLU A 223      28.795   8.232   0.976  1.00 48.23           C  
ANISOU  292  C   GLU A 223     7859   4587   5879   -878   -251    710       C  
ATOM    293  O   GLU A 223      27.579   8.477   1.008  1.00 48.04           O  
ANISOU  293  O   GLU A 223     8142   3960   6151   -823   -418    818       O  
ATOM    294  CB  GLU A 223      29.105   6.962  -1.184  1.00 48.23           C  
ANISOU  294  CB  GLU A 223     7762   3544   7015  -1873    346   1810       C  
ATOM    295  CG  GLU A 223      29.885   8.034  -1.939  1.00 53.03           C  
ANISOU  295  CG  GLU A 223     8198   4644   7305  -3938   1218   3140       C  
ATOM    296  CD  GLU A 223      29.798   7.903  -3.456  1.00 74.07           C  
ANISOU  296  CD  GLU A 223    11414   7905   8823  -1493   -642   1647       C  
ATOM    297  OE1 GLU A 223      30.780   8.262  -4.140  1.00 85.25           O  
ANISOU  297  OE1 GLU A 223    12418  10836   9135  -1314    391   1394       O  
ATOM    298  OE2 GLU A 223      28.760   7.447  -3.978  1.00 81.00           O  
ANISOU  298  OE2 GLU A 223    11936  10539   8301  -1311  -1135    859       O  
ATOM    299  N   VAL A 224      29.726   9.019   1.502  1.00 46.79           N  
ANISOU  299  N   VAL A 224     7094   4518   6164  -1292    487   1138       N  
ATOM    300  CA  VAL A 224      29.450  10.291   2.163  1.00 49.91           C  
ANISOU  300  CA  VAL A 224     7825   4634   6505   -916   -231    950       C  
ATOM    301  C   VAL A 224      29.804  11.417   1.182  1.00 54.06           C  
ANISOU  301  C   VAL A 224     8692   4829   7017   -888   -367   1353       C  
ATOM    302  O   VAL A 224      30.969  11.597   0.819  1.00 53.19           O  
ANISOU  302  O   VAL A 224     8306   4439   7463  -1285    -68   -104       O  
ATOM    303  CB  VAL A 224      30.265  10.417   3.475  1.00 47.70           C  
ANISOU  303  CB  VAL A 224     7605   4136   6383   -522   -133   1024       C  
ATOM    304  CG1 VAL A 224      30.009  11.742   4.176  1.00 45.09           C  
ANISOU  304  CG1 VAL A 224     7277   3814   6041   -922    154   1338       C  
ATOM    305  CG2 VAL A 224      29.970   9.261   4.422  1.00 50.50           C  
ANISOU  305  CG2 VAL A 224     8360   4259   6569   -428    637   1472       C  
ATOM    306  N   VAL A 225      28.789  12.156   0.742  1.00 55.04           N  
ANISOU  306  N   VAL A 225     8944   4786   7179   -941   -859   1181       N  
ATOM    307  CA  VAL A 225      28.953  13.175  -0.303  1.00 56.57           C  
ANISOU  307  CA  VAL A 225     9419   5014   7060  -1247   -528   1188       C  
ATOM    308  C   VAL A 225      28.632  14.560   0.261  1.00 59.84           C  
ANISOU  308  C   VAL A 225     9668   5123   7944   -725   -158   1391       C  
ATOM    309  O   VAL A 225      27.484  14.842   0.615  1.00 56.54           O  
ANISOU  309  O   VAL A 225     9485   3337   8660     22   -839   1030       O  
ATOM    310  CB  VAL A 225      28.071  12.876  -1.554  1.00 56.75           C  
ANISOU  310  CB  VAL A 225     9451   4994   7116   -693   -818   1564       C  
ATOM    311  CG1 VAL A 225      28.225  13.959  -2.613  1.00 56.19           C  
ANISOU  311  CG1 VAL A 225     9074   5098   7177  -1455   -137   1390       C  
ATOM    312  CG2 VAL A 225      28.391  11.504  -2.152  1.00 54.30           C  
ANISOU  312  CG2 VAL A 225     8843   5509   6279  -1189  -1337    869       C  
ATOM    313  N   LYS A 226      29.654  15.407   0.348  1.00 66.80           N  
ANISOU  313  N   LYS A 226    10088   6281   9010  -1464   -165   1021       N  
ATOM    314  CA  LYS A 226      29.501  16.792   0.799  1.00 67.42           C  
ANISOU  314  CA  LYS A 226    10021   6182   9412  -1023   -452   1283       C  
ATOM    315  C   LYS A 226      30.058  17.739  -0.262  1.00 71.00           C  
ANISOU  315  C   LYS A 226    11523   6283   9169  -1161   -544   1297       C  
ATOM    316  O   LYS A 226      31.184  17.552  -0.731  1.00 69.04           O  
ANISOU  316  O   LYS A 226    11771   4654   9805  -1371   -464    626       O  
ATOM    317  CB  LYS A 226      30.213  16.990   2.137  1.00 71.74           C  
ANISOU  317  CB  LYS A 226    10593   7119   9543  -1297   -805   1425       C  
ATOM    318  CG  LYS A 226      29.961  18.331   2.800  1.00 76.46           C  
ANISOU  318  CG  LYS A 226    10801   7370  10878  -1528   -571   1035       C  
ATOM    319  CD  LYS A 226      30.757  18.442   4.090  1.00 82.48           C  
ANISOU  319  CD  LYS A 226    12192   8335  10810   -737   -856   1072       C  
ATOM    320  CE  LYS A 226      30.576  19.803   4.736  1.00 85.96           C  
ANISOU  320  CE  LYS A 226    13152   8678  10830   -303   -400    664       C  
ATOM    321  NZ  LYS A 226      29.177  19.992   5.207  1.00 90.49           N  
ANISOU  321  NZ  LYS A 226    13388   7643  13351    431   -697  -1671       N  
ATOM    322  N   HIS A 227      29.281  18.767  -0.607  1.00 73.58           N  
ANISOU  322  N   HIS A 227    10882   7192   9882  -1213  -1376   1446       N  
ATOM    323  CA  HIS A 227      29.557  19.613  -1.777  1.00 83.27           C  
ANISOU  323  CA  HIS A 227    13031   8289  10317  -1299   -970   1954       C  
ATOM    324  C   HIS A 227      31.000  20.095  -1.974  1.00 84.50           C  
ANISOU  324  C   HIS A 227    13523   7397  11185  -1770  -1537   1782       C  
ATOM    325  O   HIS A 227      31.542  19.969  -3.078  1.00 99.72           O  
ANISOU  325  O   HIS A 227    15601   9939  12348   -579   -454   1788       O  
ATOM    326  CB  HIS A 227      28.583  20.790  -1.866  1.00 91.28           C  
ANISOU  326  CB  HIS A 227    13070   8839  12773   -949  -1021   1329       C  
ATOM    327  CG  HIS A 227      28.726  21.588  -3.125  1.00103.14           C  
ANISOU  327  CG  HIS A 227    14621  11157  13408  -1166  -1377   2326       C  
ATOM    328  ND1 HIS A 227      29.035  21.011  -4.340  1.00107.02           N  
ANISOU  328  ND1 HIS A 227    15012  11470  14180   -457  -1469   1796       N  
ATOM    329  CD2 HIS A 227      28.599  22.915  -3.361  1.00107.39           C  
ANISOU  329  CD2 HIS A 227    15418  10942  14442  -1472  -1266   2121       C  
ATOM    330  CE1 HIS A 227      29.100  21.949  -5.268  1.00110.80           C  
ANISOU  330  CE1 HIS A 227    15965  11831  14301  -1542   -928   2005       C  
ATOM    331  NE2 HIS A 227      28.835  23.113  -4.701  1.00109.67           N  
ANISOU  331  NE2 HIS A 227    15995  11009  14662  -2370   -929   2309       N  
ATOM    332  N   HIS A 228      31.612  20.649  -0.929  1.00 75.42           N  
ANISOU  332  N   HIS A 228    12524   5522  10608  -1379  -1087   2021       N  
ATOM    333  CA  HIS A 228      32.946  21.248  -1.078  1.00 78.48           C  
ANISOU  333  CA  HIS A 228    12402   7430   9985  -1419   -894   1876       C  
ATOM    334  C   HIS A 228      34.091  20.429  -0.488  1.00 79.03           C  
ANISOU  334  C   HIS A 228    12368   7090  10568  -1358   -691   1802       C  
ATOM    335  O   HIS A 228      35.198  20.943  -0.272  1.00 81.23           O  
ANISOU  335  O   HIS A 228    12584   8002  10276  -1981    319   1356       O  
ATOM    336  CB  HIS A 228      32.947  22.680  -0.551  1.00 81.05           C  
ANISOU  336  CB  HIS A 228    12453   7342  11000  -2138   -847   1785       C  
ATOM    337  CG  HIS A 228      32.225  23.636  -1.443  1.00 86.45           C  
ANISOU  337  CG  HIS A 228    13824   7507  11512  -1612  -1388   1985       C  
ATOM    338  ND1 HIS A 228      32.632  23.896  -2.735  1.00 89.03           N  
ANISOU  338  ND1 HIS A 228    14166   8209  11451  -1753  -1169   1487       N  
ATOM    339  CD2 HIS A 228      31.118  24.387  -1.237  1.00 91.51           C  
ANISOU  339  CD2 HIS A 228    14002   8347  12421  -1154  -1820   1655       C  
ATOM    340  CE1 HIS A 228      31.811  24.772  -3.283  1.00 94.95           C  
ANISOU  340  CE1 HIS A 228    14238   9904  11934   -702  -1589   2077       C  
ATOM    341  NE2 HIS A 228      30.885  25.088  -2.395  1.00 98.36           N  
ANISOU  341  NE2 HIS A 228    14592  10410  12369    389  -1854   1916       N  
ATOM    342  N   SER A 229      33.813  19.148  -0.263  1.00 72.32           N  
ANISOU  342  N   SER A 229    11525   7096   8856  -1421     89   1979       N  
ATOM    343  CA  SER A 229      34.777  18.194   0.275  1.00 73.95           C  
ANISOU  343  CA  SER A 229    11736   7039   9322  -1305   -572   1339       C  
ATOM    344  C   SER A 229      34.903  17.011  -0.685  1.00 68.54           C  
ANISOU  344  C   SER A 229    10688   6723   8629  -1497   -646   1737       C  
ATOM    345  O   SER A 229      33.975  16.754  -1.457  1.00 66.66           O  
ANISOU  345  O   SER A 229    10683   5890   8752  -1712   -773   2599       O  
ATOM    346  CB  SER A 229      34.311  17.695   1.651  1.00 77.23           C  
ANISOU  346  CB  SER A 229    12148   7588   9606  -1499   -767   2043       C  
ATOM    347  OG  SER A 229      34.087  18.773   2.545  1.00 83.26           O  
ANISOU  347  OG  SER A 229    12461   9377   9797  -1389  -1398   1002       O  
ATOM    348  N   PRO A 230      36.044  16.284  -0.651  1.00 70.19           N  
ANISOU  348  N   PRO A 230    10753   6410   9504  -1586   -318   1805       N  
ATOM    349  CA  PRO A 230      36.087  15.043  -1.433  1.00 70.73           C  
ANISOU  349  CA  PRO A 230    10926   6719   9226  -1823    191   1598       C  
ATOM    350  C   PRO A 230      35.111  14.011  -0.853  1.00 65.00           C  
ANISOU  350  C   PRO A 230    10639   5955   8101  -1495   -116   1271       C  
ATOM    351  O   PRO A 230      34.892  13.988   0.365  1.00 62.98           O  
ANISOU  351  O   PRO A 230     9579   5961   8390  -2322    119   1534       O  
ATOM    352  CB  PRO A 230      37.536  14.569  -1.266  1.00 76.84           C  
ANISOU  352  CB  PRO A 230    11278   8308   9607  -1381    284   1001       C  
ATOM    353  CG  PRO A 230      38.015  15.211  -0.004  1.00 75.40           C  
ANISOU  353  CG  PRO A 230    11233   7685   9730  -1467   -213   1462       C  
ATOM    354  CD  PRO A 230      37.321  16.540   0.047  1.00 74.78           C  
ANISOU  354  CD  PRO A 230    11110   7436   9863  -1694   -571   1472       C  
ATOM    355  N   VAL A 231      34.515  13.190  -1.713  1.00 60.92           N  
ANISOU  355  N   VAL A 231     9822   6101   7223  -1482    445   1328       N  
ATOM    356  CA  VAL A 231      33.629  12.115  -1.248  1.00 62.47           C  
ANISOU  356  CA  VAL A 231     9594   6185   7956  -1389   -119   1528       C  
ATOM    357  C   VAL A 231      34.433  11.143  -0.373  1.00 61.52           C  
ANISOU  357  C   VAL A 231     9617   6465   7290  -1369    289   1785       C  
ATOM    358  O   VAL A 231      35.629  10.915  -0.615  1.00 62.84           O  
ANISOU  358  O   VAL A 231     9519   6844   7511  -1988   1023   2109       O  
ATOM    359  CB  VAL A 231      32.832  11.412  -2.397  1.00 61.56           C  
ANISOU  359  CB  VAL A 231     9376   6276   7736   -889    -62   1212       C  
ATOM    360  CG1 VAL A 231      32.834  12.247  -3.676  1.00 64.03           C  
ANISOU  360  CG1 VAL A 231     9651   6727   7949  -1120    704   1363       C  
ATOM    361  CG2 VAL A 231      33.322   9.996  -2.684  1.00 62.01           C  
ANISOU  361  CG2 VAL A 231    10369   6388   6801   -622     33   1142       C  
ATOM    362  N   SER A 232      33.784  10.618   0.664  1.00 51.55           N  
ANISOU  362  N   SER A 232     7836   5054   6695  -1159   -372   1260       N  
ATOM    363  CA  SER A 232      34.424   9.705   1.590  1.00 46.68           C  
ANISOU  363  CA  SER A 232     7420   4189   6124  -1283    355   1143       C  
ATOM    364  C   SER A 232      33.559   8.463   1.780  1.00 48.79           C  
ANISOU  364  C   SER A 232     7611   4246   6681  -1237    263   1438       C  
ATOM    365  O   SER A 232      32.377   8.451   1.427  1.00 51.49           O  
ANISOU  365  O   SER A 232     7715   5025   6823  -1983     41   1730       O  
ATOM    366  CB  SER A 232      34.679  10.386   2.936  1.00 56.03           C  
ANISOU  366  CB  SER A 232     8726   5759   6803  -1736     68    364       C  
ATOM    367  OG  SER A 232      33.458  10.688   3.589  1.00 61.17           O  
ANISOU  367  OG  SER A 232     9379   6501   7361   -897    104    826       O  
ATOM    368  N   TRP A 233      34.159   7.424   2.338  1.00 45.34           N  
ANISOU  368  N   TRP A 233     7081   4414   5731  -1032    519   1377       N  
ATOM    369  CA  TRP A 233      33.513   6.120   2.438  1.00 47.87           C  
ANISOU  369  CA  TRP A 233     7223   4618   6346  -1230    275   1041       C  
ATOM    370  C   TRP A 233      33.654   5.544   3.820  1.00 47.66           C  
ANISOU  370  C   TRP A 233     7161   4704   6244  -1469    197   1061       C  
ATOM    371  O   TRP A 233      34.683   5.738   4.470  1.00 48.70           O  
ANISOU  371  O   TRP A 233     7252   4713   6538  -2424     34    -35       O  
ATOM    372  CB  TRP A 233      34.137   5.144   1.450  1.00 50.70           C  
ANISOU  372  CB  TRP A 233     7971   4903   6390  -1147    706    916       C  
ATOM    373  CG  TRP A 233      33.923   5.516   0.040  1.00 55.10           C  
ANISOU  373  CG  TRP A 233     8567   5649   6719   -987    136   1319       C  
ATOM    374  CD1 TRP A 233      34.676   6.380  -0.708  1.00 55.48           C  
ANISOU  374  CD1 TRP A 233     9061   5281   6737   -981     84   1290       C  
ATOM    375  CD2 TRP A 233      32.886   5.035  -0.818  1.00 60.21           C  
ANISOU  375  CD2 TRP A 233     9282   6603   6992  -1186     80    852       C  
ATOM    376  NE1 TRP A 233      34.166   6.468  -1.977  1.00 57.79           N  
ANISOU  376  NE1 TRP A 233     9407   5809   6739  -1104    -26    610       N  
ATOM    377  CE2 TRP A 233      33.067   5.655  -2.075  1.00 59.32           C  
ANISOU  377  CE2 TRP A 233     9270   6052   7215  -1187    299   1041       C  
ATOM    378  CE3 TRP A 233      31.817   4.134  -0.647  1.00 61.75           C  
ANISOU  378  CE3 TRP A 233     9377   6750   7335  -1163    355    342       C  
ATOM    379  CZ2 TRP A 233      32.221   5.405  -3.165  1.00 65.87           C  
ANISOU  379  CZ2 TRP A 233     9844   7476   7708  -1264     32    764       C  
ATOM    380  CZ3 TRP A 233      30.972   3.885  -1.730  1.00 62.03           C  
ANISOU  380  CZ3 TRP A 233     8907   6622   8038   -977     60    799       C  
ATOM    381  CH2 TRP A 233      31.181   4.521  -2.975  1.00 67.01           C  
ANISOU  381  CH2 TRP A 233    10204   7285   7970  -1178    436    835       C  
ATOM    382  N   LYS A 234      32.624   4.825   4.267  1.00 39.25           N  
ANISOU  382  N   LYS A 234     6198   3539   5175   -727   -255    718       N  
ATOM    383  CA  LYS A 234      32.726   4.034   5.488  1.00 36.94           C  
ANISOU  383  CA  LYS A 234     5898   3167   4969  -1049    -41    621       C  
ATOM    384  C   LYS A 234      32.124   2.655   5.267  1.00 35.50           C  
ANISOU  384  C   LYS A 234     5552   3140   4795   -913     63    683       C  
ATOM    385  O   LYS A 234      31.252   2.475   4.422  1.00 38.46           O  
ANISOU  385  O   LYS A 234     6103   3576   4933  -1042   -154    872       O  
ATOM    386  CB  LYS A 234      32.063   4.732   6.669  1.00 41.64           C  
ANISOU  386  CB  LYS A 234     5896   4441   5483   -610    181    321       C  
ATOM    387  CG  LYS A 234      32.751   6.015   7.123  1.00 50.98           C  
ANISOU  387  CG  LYS A 234     7578   4616   7176  -1187   -180    309       C  
ATOM    388  CD  LYS A 234      32.026   6.669   8.286  1.00 58.33           C  
ANISOU  388  CD  LYS A 234     8256   6242   7661   -628    343    215       C  
ATOM    389  CE  LYS A 234      33.001   7.237   9.312  1.00 60.16           C  
ANISOU  389  CE  LYS A 234     8401   6307   8149  -1652    340    365       C  
ATOM    390  NZ  LYS A 234      34.019   8.139   8.713  1.00 58.76           N  
ANISOU  390  NZ  LYS A 234     9074   4806   8445  -1166   -281   -217       N  
ATOM    391  N   ARG A 235      32.614   1.677   6.017  1.00 35.27           N  
ANISOU  391  N   ARG A 235     5359   3261   4779   -866   -243    446       N  
ATOM    392  CA  ARG A 235      32.159   0.302   5.877  1.00 36.74           C  
ANISOU  392  CA  ARG A 235     5776   3371   4812  -1062     43    557       C  
ATOM    393  C   ARG A 235      32.190  -0.318   7.254  1.00 37.49           C  
ANISOU  393  C   ARG A 235     5752   3616   4876   -984    -94    651       C  
ATOM    394  O   ARG A 235      32.897   0.175   8.136  1.00 38.44           O  
ANISOU  394  O   ARG A 235     5710   3608   5286  -1428     20    410       O  
ATOM    395  CB  ARG A 235      33.037  -0.461   4.865  1.00 41.90           C  
ANISOU  395  CB  ARG A 235     6545   4274   5099   -896    332    215       C  
ATOM    396  CG  ARG A 235      34.431  -0.823   5.354  1.00 53.13           C  
ANISOU  396  CG  ARG A 235     7504   5996   6683     96   -290   1507       C  
ATOM    397  CD  ARG A 235      35.539  -0.527   4.350  1.00 69.21           C  
ANISOU  397  CD  ARG A 235     9395   8585   8314   -842    971   1347       C  
ATOM    398  NE  ARG A 235      35.332  -1.174   3.051  1.00 81.97           N  
ANISOU  398  NE  ARG A 235    12126   9430   9586   -902     29    346       N  
ATOM    399  CZ  ARG A 235      35.354  -0.548   1.872  1.00 83.03           C  
ANISOU  399  CZ  ARG A 235    12250   9390   9906   -902   1095    560       C  
ATOM    400  NH1 ARG A 235      35.145  -1.236   0.756  1.00 82.88           N  
ANISOU  400  NH1 ARG A 235    12596   9580   9313     25    791    682       N  
ATOM    401  NH2 ARG A 235      35.595   0.756   1.797  1.00 85.68           N  
ANISOU  401  NH2 ARG A 235    11517   9522  11512   -844   1933   2646       N  
ATOM    402  N   GLY A 236      31.404  -1.375   7.450  1.00 37.73           N  
ANISOU  402  N   GLY A 236     4561   4122   5650  -1252  -1172   -150       N  
ATOM    403  CA  GLY A 236      31.447  -2.121   8.695  1.00 35.89           C  
ANISOU  403  CA  GLY A 236     4268   3549   5820  -1670  -1110   -141       C  
ATOM    404  C   GLY A 236      30.414  -3.222   8.787  1.00 32.12           C  
ANISOU  404  C   GLY A 236     3780   3335   5087  -1342  -1219   -186       C  
ATOM    405  O   GLY A 236      29.805  -3.578   7.798  1.00 30.54           O  
ANISOU  405  O   GLY A 236     3243   3265   5095  -1299  -1117      9       O  
ATOM    406  N   VAL A 237      30.252  -3.765   9.990  1.00 31.40           N  
ANISOU  406  N   VAL A 237     3897   3152   4882  -1160  -1214   -172       N  
ATOM    407  CA  VAL A 237      29.399  -4.926  10.263  1.00 31.57           C  
ANISOU  407  CA  VAL A 237     3737   3344   4914  -1119   -915    -91       C  
ATOM    408  C   VAL A 237      28.693  -4.689  11.597  1.00 30.09           C  
ANISOU  408  C   VAL A 237     3592   3103   4735   -695  -1180    -63       C  
ATOM    409  O   VAL A 237      29.331  -4.359  12.596  1.00 31.23           O  
ANISOU  409  O   VAL A 237     4075   3305   4484   -933  -1024    -83       O  
ATOM    410  CB  VAL A 237      30.236  -6.247  10.350  1.00 32.64           C  
ANISOU  410  CB  VAL A 237     3760   3442   5198  -1019   -833    193       C  
ATOM    411  CG1 VAL A 237      29.363  -7.427  10.779  1.00 29.98           C  
ANISOU  411  CG1 VAL A 237     3210   3345   4834   -713   -940    308       C  
ATOM    412  CG2 VAL A 237      30.920  -6.569   9.018  1.00 32.54           C  
ANISOU  412  CG2 VAL A 237     3513   3710   5139   -808   -696    563       C  
ATOM    413  N   PHE A 238      27.377  -4.836  11.601  1.00 30.64           N  
ANISOU  413  N   PHE A 238     3707   3075   4860   -810   -930   -254       N  
ATOM    414  CA  PHE A 238      26.595  -4.802  12.825  1.00 34.21           C  
ANISOU  414  CA  PHE A 238     4360   3826   4810   -662   -696    -92       C  
ATOM    415  C   PHE A 238      25.983  -6.173  12.999  1.00 32.07           C  
ANISOU  415  C   PHE A 238     3844   3536   4804   -218   -491    -15       C  
ATOM    416  O   PHE A 238      25.682  -6.849  12.016  1.00 31.57           O  
ANISOU  416  O   PHE A 238     3702   3445   4845   -511   -877    312       O  
ATOM    417  CB  PHE A 238      25.486  -3.738  12.746  1.00 37.59           C  
ANISOU  417  CB  PHE A 238     5050   4044   5188   -299   -933   -151       C  
ATOM    418  CG  PHE A 238      25.976  -2.330  12.945  1.00 39.71           C  
ANISOU  418  CG  PHE A 238     5169   4392   5524   -776  -1054   -368       C  
ATOM    419  CD1 PHE A 238      26.051  -1.774  14.227  1.00 36.63           C  
ANISOU  419  CD1 PHE A 238     4803   3833   5282   -371   -988   -105       C  
ATOM    420  CD2 PHE A 238      26.358  -1.545  11.848  1.00 34.98           C  
ANISOU  420  CD2 PHE A 238     4159   3354   5777   -775  -1091   -534       C  
ATOM    421  CE1 PHE A 238      26.514  -0.468  14.420  1.00 40.78           C  
ANISOU  421  CE1 PHE A 238     5338   4278   5875   -897  -1188   -155       C  
ATOM    422  CE2 PHE A 238      26.817  -0.250  12.042  1.00 36.04           C  
ANISOU  422  CE2 PHE A 238     5286   3147   5258   -731  -1073   -376       C  
ATOM    423  CZ  PHE A 238      26.897   0.290  13.324  1.00 36.41           C  
ANISOU  423  CZ  PHE A 238     5025   3424   5382   -519  -1123   -603       C  
ATOM    424  N   ARG A 239      25.831  -6.578  14.253  1.00 34.68           N  
ANISOU  424  N   ARG A 239     4272   4091   4813     95   -896    218       N  
ATOM    425  CA  ARG A 239      25.075  -7.776  14.639  1.00 38.93           C  
ANISOU  425  CA  ARG A 239     4677   4575   5539   -232   -376    336       C  
ATOM    426  C   ARG A 239      23.955  -7.360  15.583  1.00 40.06           C  
ANISOU  426  C   ARG A 239     5053   4624   5543     43   -222    298       C  
ATOM    427  O   ARG A 239      23.896  -6.202  16.014  1.00 37.22           O  
ANISOU  427  O   ARG A 239     4896   4296   4946   -727   -596    367       O  
ATOM    428  CB  ARG A 239      25.973  -8.746  15.400  1.00 44.47           C  
ANISOU  428  CB  ARG A 239     5424   4824   6646    -21   -302   1166       C  
ATOM    429  CG  ARG A 239      27.088  -9.371  14.598  1.00 51.59           C  
ANISOU  429  CG  ARG A 239     6085   6353   7164    132    101    530       C  
ATOM    430  CD  ARG A 239      27.793 -10.435  15.427  1.00 56.32           C  
ANISOU  430  CD  ARG A 239     6792   6961   7646    139   -551    852       C  
ATOM    431  NE  ARG A 239      28.349  -9.885  16.657  1.00 64.20           N  
ANISOU  431  NE  ARG A 239     8064   8212   8114    318   -668    278       N  
ATOM    432  CZ  ARG A 239      28.682 -10.603  17.724  1.00 73.16           C  
ANISOU  432  CZ  ARG A 239     9049   9840   8908    693   -930   1029       C  
ATOM    433  NH1 ARG A 239      28.525 -11.925  17.727  1.00 73.77           N  
ANISOU  433  NH1 ARG A 239     8417   9931   9679    248    269    672       N  
ATOM    434  NH2 ARG A 239      29.173  -9.991  18.797  1.00 70.99           N  
ANISOU  434  NH2 ARG A 239     8798   9033   9142   1148    193   -225       N  
ATOM    435  N   ASN A 240      23.085  -8.306  15.940  1.00 39.02           N  
ANISOU  435  N   ASN A 240     4750   4771   5301     27   -315    438       N  
ATOM    436  CA  ASN A 240      22.099  -8.052  17.002  1.00 41.50           C  
ANISOU  436  CA  ASN A 240     5223   5220   5322    293    -62    169       C  
ATOM    437  C   ASN A 240      22.740  -7.708  18.354  1.00 46.33           C  
ANISOU  437  C   ASN A 240     5714   6150   5739    310   -572    125       C  
ATOM    438  O   ASN A 240      23.800  -8.240  18.700  1.00 43.89           O  
ANISOU  438  O   ASN A 240     5555   5577   5540     -6   -355    375       O  
ATOM    439  CB  ASN A 240      21.140  -9.244  17.168  1.00 43.96           C  
ANISOU  439  CB  ASN A 240     5400   5496   5806     84    225   -120       C  
ATOM    440  CG  ASN A 240      20.255  -9.463  15.946  1.00 45.28           C  
ANISOU  440  CG  ASN A 240     5505   5398   6299    312   -304    505       C  
ATOM    441  OD1 ASN A 240      19.934  -8.519  15.205  1.00 39.06           O  
ANISOU  441  OD1 ASN A 240     4753   4238   5848    287    276   -109       O  
ATOM    442  ND2 ASN A 240      19.855 -10.712  15.729  1.00 44.89           N  
ANISOU  442  ND2 ASN A 240     6305   4655   6096    656   -471   1040       N  
ATOM    443  N   GLN A 241      22.076  -6.804  19.082  1.00 52.94           N  
ANISOU  443  N   GLN A 241     7052   6261   6802    631     44    -52       N  
ATOM    444  CA  GLN A 241      22.389  -6.394  20.465  1.00 63.47           C  
ANISOU  444  CA  GLN A 241     8798   7902   7416    668  -1636      9       C  
ATOM    445  C   GLN A 241      23.829  -5.920  20.650  1.00 72.34           C  
ANISOU  445  C   GLN A 241     9034   9376   9075     51   -863   -495       C  
ATOM    446  O   GLN A 241      24.120  -4.731  20.502  1.00 76.05           O  
ANISOU  446  O   GLN A 241     9956   8874  10063    715   -837   -454       O  
ATOM    447  CB  GLN A 241      22.027  -7.508  21.455  1.00 68.81           C  
ANISOU  447  CB  GLN A 241     9338   8831   7976     84    204    162       C  
ATOM    448  CG  GLN A 241      22.023  -7.102  22.919  1.00 75.90           C  
ANISOU  448  CG  GLN A 241     9970  10275   8593    749    367   -548       C  
ATOM    449  CD  GLN A 241      21.791  -8.276  23.864  1.00 79.80           C  
ANISOU  449  CD  GLN A 241    10318  11256   8745    900    192    111       C  
ATOM    450  OE1 GLN A 241      21.730  -9.438  23.443  1.00 85.69           O  
ANISOU  450  OE1 GLN A 241    10446  10962  11148    -89    352    216       O  
ATOM    451  NE2 GLN A 241      21.663  -7.976  25.152  1.00 69.72           N  
ANISOU  451  NE2 GLN A 241     7778  10203   8508   2008   -187     61       N  
ATOM    452  N   HIS A 247      17.397  -0.308  20.173  1.00 73.91           N  
ANISOU  452  N   HIS A 247    11052   8336   8692    -70    483  -2705       N  
ATOM    453  CA  HIS A 247      18.658  -0.450  19.459  1.00 75.14           C  
ANISOU  453  CA  HIS A 247    10416   8649   9483    131    -50  -2010       C  
ATOM    454  C   HIS A 247      19.175  -1.907  19.546  1.00 77.86           C  
ANISOU  454  C   HIS A 247    10316   8887  10379    324   -130   -844       C  
ATOM    455  O   HIS A 247      20.343  -2.182  19.299  1.00 71.03           O  
ANISOU  455  O   HIS A 247    10394   7779   8813   -366   -128  -1793       O  
ATOM    456  CB  HIS A 247      19.633   0.665  19.930  1.00 70.13           C  
ANISOU  456  CB  HIS A 247    10587   8024   8033    177   -258  -1371       C  
ATOM    457  CG  HIS A 247      21.077   0.269  20.007  1.00 81.69           C  
ANISOU  457  CG  HIS A 247    10948   9767  10322    744    -94  -2101       C  
ATOM    458  ND1 HIS A 247      21.550  -0.659  20.912  1.00 94.94           N  
ANISOU  458  ND1 HIS A 247    13563  11136  11371    328   -333   -874       N  
ATOM    459  CD2 HIS A 247      22.162   0.715  19.330  1.00 84.88           C  
ANISOU  459  CD2 HIS A 247    12710   9234  10306   -337   -159   -855       C  
ATOM    460  CE1 HIS A 247      22.856  -0.797  20.761  1.00 99.65           C  
ANISOU  460  CE1 HIS A 247    13335  12340  12187   -248   -298  -1297       C  
ATOM    461  NE2 HIS A 247      23.253   0.030  19.810  1.00 94.11           N  
ANISOU  461  NE2 HIS A 247    12296  11749  11710   -153   -968  -1373       N  
ATOM    462  N   CYS A 248      18.278  -2.845  19.858  1.00 74.80           N  
ANISOU  462  N   CYS A 248    10264   7941  10216   1316    268   -274       N  
ATOM    463  CA  CYS A 248      18.653  -4.255  19.984  1.00 59.11           C  
ANISOU  463  CA  CYS A 248     8197   7224   7036    697    416  -1258       C  
ATOM    464  C   CYS A 248      19.020  -4.904  18.644  1.00 48.63           C  
ANISOU  464  C   CYS A 248     6284   6154   6037    519   -430   -263       C  
ATOM    465  O   CYS A 248      20.188  -5.275  18.459  1.00 43.89           O  
ANISOU  465  O   CYS A 248     6283   5392   4998    401   -221    -95       O  
ATOM    466  CB  CYS A 248      17.596  -5.059  20.751  1.00 63.85           C  
ANISOU  466  CB  CYS A 248     8869   6807   8583    973   1557  -1654       C  
ATOM    467  SG  CYS A 248      17.840  -5.054  22.546  1.00 85.71           S  
ANISOU  467  SG  CYS A 248    10976  11827   9761    922  -1379  -2379       S  
ATOM    468  N   HIS A 249      18.066  -5.025  17.713  1.00 35.91           N  
ANISOU  468  N   HIS A 249     5047   3678   4916    625    379   -105       N  
ATOM    469  CA  HIS A 249      18.360  -5.678  16.415  1.00 36.00           C  
ANISOU  469  CA  HIS A 249     4792   4077   4809    554     45   -209       C  
ATOM    470  C   HIS A 249      19.383  -4.893  15.603  1.00 38.21           C  
ANISOU  470  C   HIS A 249     5199   4017   5300    155   -257    140       C  
ATOM    471  O   HIS A 249      19.483  -3.675  15.751  1.00 39.02           O  
ANISOU  471  O   HIS A 249     5428   4103   5292     61   -103   -450       O  
ATOM    472  CB  HIS A 249      17.094  -5.874  15.574  1.00 35.27           C  
ANISOU  472  CB  HIS A 249     4638   3798   4964    728     -6   -106       C  
ATOM    473  CG  HIS A 249      16.181  -6.943  16.087  1.00 41.00           C  
ANISOU  473  CG  HIS A 249     5431   4221   5924    430    334    149       C  
ATOM    474  ND1 HIS A 249      14.937  -7.177  15.541  1.00 39.19           N  
ANISOU  474  ND1 HIS A 249     5147   4377   5365    768    549    242       N  
ATOM    475  CD2 HIS A 249      16.324  -7.837  17.095  1.00 45.13           C  
ANISOU  475  CD2 HIS A 249     6365   4581   6199    914    404    389       C  
ATOM    476  CE1 HIS A 249      14.355  -8.172  16.187  1.00 44.68           C  
ANISOU  476  CE1 HIS A 249     6088   4418   6470    714    739    496       C  
ATOM    477  NE2 HIS A 249      15.175  -8.591  17.134  1.00 48.11           N  
ANISOU  477  NE2 HIS A 249     6357   5252   6667    933    915   1133       N  
ATOM    478  N   ALA A 250      20.117  -5.600  14.743  1.00 36.05           N  
ANISOU  478  N   ALA A 250     5272   3729   4694    107   -353    459       N  
ATOM    479  CA  ALA A 250      21.195  -5.023  13.921  1.00 33.85           C  
ANISOU  479  CA  ALA A 250     4928   3257   4674   -128   -896    450       C  
ATOM    480  C   ALA A 250      20.785  -3.760  13.182  1.00 32.38           C  
ANISOU  480  C   ALA A 250     4733   3227   4343   -216   -900    370       C  
ATOM    481  O   ALA A 250      21.544  -2.782  13.162  1.00 31.11           O  
ANISOU  481  O   ALA A 250     4698   3015   4107    -87  -1059    294       O  
ATOM    482  CB  ALA A 250      21.719  -6.056  12.928  1.00 32.70           C  
ANISOU  482  CB  ALA A 250     4713   3131   4577   -145   -386    625       C  
ATOM    483  N   GLU A 251      19.588  -3.786  12.584  1.00 29.17           N  
ANISOU  483  N   GLU A 251     4464   2748   3871    -25   -661    253       N  
ATOM    484  CA  GLU A 251      19.057  -2.648  11.819  1.00 30.08           C  
ANISOU  484  CA  GLU A 251     4437   2725   4264     -5   -637    339       C  
ATOM    485  C   GLU A 251      18.943  -1.405  12.713  1.00 31.85           C  
ANISOU  485  C   GLU A 251     4706   3183   4212    172   -870    124       C  
ATOM    486  O   GLU A 251      19.357  -0.301  12.331  1.00 33.52           O  
ANISOU  486  O   GLU A 251     4733   3294   4708   -109   -644    -27       O  
ATOM    487  CB  GLU A 251      17.702  -3.003  11.172  1.00 33.91           C  
ANISOU  487  CB  GLU A 251     4708   3461   4714     27   -936    133       C  
ATOM    488  CG  GLU A 251      17.717  -4.221  10.229  1.00 34.77           C  
ANISOU  488  CG  GLU A 251     4830   3465   4914     -4   -717    131       C  
ATOM    489  CD  GLU A 251      17.412  -5.552  10.915  1.00 37.36           C  
ANISOU  489  CD  GLU A 251     5199   3660   5335    171   -675    440       C  
ATOM    490  OE1 GLU A 251      17.901  -5.830  12.029  1.00 37.88           O  
ANISOU  490  OE1 GLU A 251     5262   4016   5113   -212   -690    369       O  
ATOM    491  OE2 GLU A 251      16.678  -6.357  10.316  1.00 43.71           O  
ANISOU  491  OE2 GLU A 251     5632   4755   6221    -52  -1236    213       O  
ATOM    492  N   ARG A 252      18.429  -1.598  13.923  1.00 33.06           N  
ANISOU  492  N   ARG A 252     4487   3672   4401     74   -655    107       N  
ATOM    493  CA  ARG A 252      18.318  -0.509  14.884  1.00 35.12           C  
ANISOU  493  CA  ARG A 252     5283   3567   4492     10   -843     96       C  
ATOM    494  C   ARG A 252      19.678  -0.045  15.430  1.00 36.78           C  
ANISOU  494  C   ARG A 252     5166   3839   4969    -40   -710    113       C  
ATOM    495  O   ARG A 252      19.853   1.149  15.698  1.00 35.32           O  
ANISOU  495  O   ARG A 252     4830   3796   4793    304   -789    -21       O  
ATOM    496  CB  ARG A 252      17.397  -0.902  16.037  1.00 41.37           C  
ANISOU  496  CB  ARG A 252     6047   4608   5062   -148   -330    530       C  
ATOM    497  CG  ARG A 252      15.954  -1.182  15.642  1.00 50.07           C  
ANISOU  497  CG  ARG A 252     6828   5541   6653   -284  -1054    205       C  
ATOM    498  CD  ARG A 252      15.100  -1.466  16.872  1.00 62.57           C  
ANISOU  498  CD  ARG A 252     8159   8025   7587   -173    -11    493       C  
ATOM    499  NE  ARG A 252      15.063  -0.329  17.798  1.00 73.53           N  
ANISOU  499  NE  ARG A 252    10769   8202   8965    491   -239   -111       N  
ATOM    500  CZ  ARG A 252      14.539  -0.353  19.021  1.00 81.18           C  
ANISOU  500  CZ  ARG A 252    11318   9934   9592   -390    471   -136       C  
ATOM    501  NH1 ARG A 252      13.998  -1.460  19.515  1.00 84.43           N  
ANISOU  501  NH1 ARG A 252    11868   9707  10506   -502    291   -251       N  
ATOM    502  NH2 ARG A 252      14.567   0.743  19.763  1.00 85.70           N  
ANISOU  502  NH2 ARG A 252    12280  10254  10029   -872   1359   -438       N  
ATOM    503  N   CYS A 253      20.627  -0.977  15.600  1.00 35.35           N  
ANISOU  503  N   CYS A 253     5293   3708   4428    -75  -1174    486       N  
ATOM    504  CA  CYS A 253      22.007  -0.630  15.998  1.00 33.53           C  
ANISOU  504  CA  CYS A 253     5026   3244   4469   -182   -667    443       C  
ATOM    505  C   CYS A 253      22.631   0.254  14.948  1.00 31.92           C  
ANISOU  505  C   CYS A 253     4981   3111   4033    137   -982    486       C  
ATOM    506  O   CYS A 253      23.277   1.260  15.280  1.00 34.67           O  
ANISOU  506  O   CYS A 253     5016   3592   4562    -69  -1055    180       O  
ATOM    507  CB  CYS A 253      22.885  -1.877  16.191  1.00 37.35           C  
ANISOU  507  CB  CYS A 253     5142   3804   5244    322   -683    -17       C  
ATOM    508  SG  CYS A 253      22.328  -2.949  17.517  1.00 48.65           S  
ANISOU  508  SG  CYS A 253     7077   5053   6356    213   -941    890       S  
ATOM    509  N   PHE A 254      22.432  -0.104  13.679  1.00 32.26           N  
ANISOU  509  N   PHE A 254     4928   3074   4255    104   -873    -27       N  
ATOM    510  CA  PHE A 254      22.917   0.743  12.589  1.00 35.03           C  
ANISOU  510  CA  PHE A 254     5244   3521   4542    105   -642    250       C  
ATOM    511  C   PHE A 254      22.340   2.159  12.641  1.00 34.53           C  
ANISOU  511  C   PHE A 254     4963   3560   4595    131   -464     44       C  
ATOM    512  O   PHE A 254      23.092   3.125  12.523  1.00 33.83           O  
ANISOU  512  O   PHE A 254     5014   3446   4392    -19   -806   -328       O  
ATOM    513  CB  PHE A 254      22.681   0.138  11.195  1.00 35.62           C  
ANISOU  513  CB  PHE A 254     5350   3419   4765   -110   -967    118       C  
ATOM    514  CG  PHE A 254      23.173   1.030  10.076  1.00 35.80           C  
ANISOU  514  CG  PHE A 254     5367   3497   4736    162   -709     48       C  
ATOM    515  CD1 PHE A 254      22.369   2.068   9.586  1.00 35.04           C  
ANISOU  515  CD1 PHE A 254     5242   3450   4619    170   -676    -98       C  
ATOM    516  CD2 PHE A 254      24.454   0.868   9.542  1.00 33.36           C  
ANISOU  516  CD2 PHE A 254     4872   3123   4676   -255   -963     40       C  
ATOM    517  CE1 PHE A 254      22.826   2.920   8.591  1.00 34.23           C  
ANISOU  517  CE1 PHE A 254     5307   3206   4492    184   -581   -381       C  
ATOM    518  CE2 PHE A 254      24.903   1.711   8.522  1.00 32.57           C  
ANISOU  518  CE2 PHE A 254     4730   3036   4608    254   -978     67       C  
ATOM    519  CZ  PHE A 254      24.095   2.735   8.060  1.00 32.46           C  
ANISOU  519  CZ  PHE A 254     4761   3067   4503    189   -995     71       C  
ATOM    520  N   LEU A 255      21.015   2.272  12.780  1.00 30.68           N  
ANISOU  520  N   LEU A 255     4616   3004   4035     36   -932     55       N  
ATOM    521  CA  LEU A 255      20.341   3.597  12.801  1.00 32.78           C  
ANISOU  521  CA  LEU A 255     4957   3110   4388    184   -838    145       C  
ATOM    522  C   LEU A 255      20.817   4.476  13.953  1.00 36.61           C  
ANISOU  522  C   LEU A 255     5678   3904   4326    235   -713   -141       C  
ATOM    523  O   LEU A 255      21.072   5.678  13.774  1.00 39.14           O  
ANISOU  523  O   LEU A 255     5610   4014   5247    303   -770    -64       O  
ATOM    524  CB  LEU A 255      18.815   3.440  12.863  1.00 35.31           C  
ANISOU  524  CB  LEU A 255     5054   3721   4638    716   -379   -330       C  
ATOM    525  CG  LEU A 255      18.081   2.743  11.710  1.00 36.36           C  
ANISOU  525  CG  LEU A 255     5085   4034   4695    318   -617    -50       C  
ATOM    526  CD1 LEU A 255      16.582   2.734  11.964  1.00 38.62           C  
ANISOU  526  CD1 LEU A 255     5333   4213   5125    455   -438   -182       C  
ATOM    527  CD2 LEU A 255      18.394   3.406  10.376  1.00 35.93           C  
ANISOU  527  CD2 LEU A 255     5354   3733   4563    674   -410   -262       C  
ATOM    528  N   SER A 256      20.961   3.863  15.125  1.00 35.09           N  
ANISOU  528  N   SER A 256     5259   3785   4286     22   -625    -63       N  
ATOM    529  CA  SER A 256      21.402   4.559  16.323  1.00 35.87           C  
ANISOU  529  CA  SER A 256     5546   3726   4355     25   -717    -16       C  
ATOM    530  C   SER A 256      22.856   5.051  16.187  1.00 38.46           C  
ANISOU  530  C   SER A 256     5735   4101   4777    -60   -874   -103       C  
ATOM    531  O   SER A 256      23.133   6.198  16.508  1.00 38.09           O  
ANISOU  531  O   SER A 256     5673   4167   4631     38   -778   -273       O  
ATOM    532  CB  SER A 256      21.202   3.668  17.545  1.00 37.83           C  
ANISOU  532  CB  SER A 256     6156   3907   4309    454   -325     61       C  
ATOM    533  OG  SER A 256      21.829   4.229  18.673  1.00 51.61           O  
ANISOU  533  OG  SER A 256     7558   6234   5816   -360  -1115   -488       O  
ATOM    534  N   TRP A 257      23.761   4.204  15.683  1.00 35.87           N  
ANISOU  534  N   TRP A 257     5524   3780   4322    -44   -856    314       N  
ATOM    535  CA  TRP A 257      25.143   4.613  15.415  1.00 37.49           C  
ANISOU  535  CA  TRP A 257     5552   3996   4696    179   -756    169       C  
ATOM    536  C   TRP A 257      25.213   5.750  14.378  1.00 38.58           C  
ANISOU  536  C   TRP A 257     5885   3921   4853   -152  -1011     85       C  
ATOM    537  O   TRP A 257      25.894   6.766  14.598  1.00 34.44           O  
ANISOU  537  O   TRP A 257     5258   3635   4193    135   -816    -35       O  
ATOM    538  CB  TRP A 257      25.982   3.408  14.955  1.00 38.71           C  
ANISOU  538  CB  TRP A 257     6126   3622   4957    133   -637    326       C  
ATOM    539  CG  TRP A 257      27.308   3.779  14.321  1.00 37.68           C  
ANISOU  539  CG  TRP A 257     5711   3721   4882    255   -906    -65       C  
ATOM    540  CD1 TRP A 257      28.462   4.125  14.975  1.00 41.23           C  
ANISOU  540  CD1 TRP A 257     5949   4087   5628   -155  -1008    140       C  
ATOM    541  CD2 TRP A 257      27.606   3.849  12.919  1.00 36.76           C  
ANISOU  541  CD2 TRP A 257     5519   3609   4838    136  -1010     62       C  
ATOM    542  NE1 TRP A 257      29.456   4.401  14.064  1.00 39.77           N  
ANISOU  542  NE1 TRP A 257     5444   4210   5457   -578  -1282     -4       N  
ATOM    543  CE2 TRP A 257      28.962   4.237  12.799  1.00 39.33           C  
ANISOU  543  CE2 TRP A 257     5948   3741   5255   -182  -1035    199       C  
ATOM    544  CE3 TRP A 257      26.863   3.613  11.749  1.00 36.41           C  
ANISOU  544  CE3 TRP A 257     5487   3535   4812    549  -1064    205       C  
ATOM    545  CZ2 TRP A 257      29.596   4.391  11.554  1.00 39.19           C  
ANISOU  545  CZ2 TRP A 257     5949   3585   5356   -326  -1089    236       C  
ATOM    546  CZ3 TRP A 257      27.493   3.780  10.507  1.00 38.69           C  
ANISOU  546  CZ3 TRP A 257     5810   3504   5386    353   -711    309       C  
ATOM    547  CH2 TRP A 257      28.848   4.169  10.428  1.00 36.65           C  
ANISOU  547  CH2 TRP A 257     5828   3001   5094    139   -874    172       C  
ATOM    548  N   PHE A 258      24.503   5.570  13.262  1.00 35.96           N  
ANISOU  548  N   PHE A 258     5398   3752   4512    163   -708     35       N  
ATOM    549  CA  PHE A 258      24.474   6.569  12.194  1.00 36.72           C  
ANISOU  549  CA  PHE A 258     5457   3775   4718    347   -936     80       C  
ATOM    550  C   PHE A 258      24.023   7.938  12.722  1.00 38.29           C  
ANISOU  550  C   PHE A 258     5764   4055   4727    231   -572   -186       C  
ATOM    551  O   PHE A 258      24.677   8.958  12.452  1.00 38.40           O  
ANISOU  551  O   PHE A 258     5476   4165   4947    116   -545   -165       O  
ATOM    552  CB  PHE A 258      23.590   6.098  11.033  1.00 36.16           C  
ANISOU  552  CB  PHE A 258     5400   3654   4685    366   -627   -340       C  
ATOM    553  CG  PHE A 258      23.591   7.035   9.857  1.00 40.27           C  
ANISOU  553  CG  PHE A 258     6258   4046   4996    375   -855    -56       C  
ATOM    554  CD1 PHE A 258      24.647   7.030   8.952  1.00 45.31           C  
ANISOU  554  CD1 PHE A 258     6638   4794   5784    832   -462   -113       C  
ATOM    555  CD2 PHE A 258      22.555   7.947   9.673  1.00 43.15           C  
ANISOU  555  CD2 PHE A 258     6080   4683   5629    359  -1378   -335       C  
ATOM    556  CE1 PHE A 258      24.660   7.897   7.870  1.00 48.66           C  
ANISOU  556  CE1 PHE A 258     7205   4705   6576    566   -367    311       C  
ATOM    557  CE2 PHE A 258      22.561   8.825   8.590  1.00 47.79           C  
ANISOU  557  CE2 PHE A 258     6864   5119   6173    -50   -538     60       C  
ATOM    558  CZ  PHE A 258      23.615   8.795   7.686  1.00 45.90           C  
ANISOU  558  CZ  PHE A 258     6783   4683   5972    366   -388    629       C  
ATOM    559  N   CYS A 259      22.932   7.960  13.493  1.00 34.27           N  
ANISOU  559  N   CYS A 259     5340   3423   4258    194   -938    -85       N  
ATOM    560  CA  CYS A 259      22.427   9.215  14.050  1.00 36.50           C  
ANISOU  560  CA  CYS A 259     5600   3859   4405    247   -725   -444       C  
ATOM    561  C   CYS A 259      23.362   9.834  15.088  1.00 37.82           C  
ANISOU  561  C   CYS A 259     5680   4009   4680     55   -867   -248       C  
ATOM    562  O   CYS A 259      23.514  11.046  15.125  1.00 38.64           O  
ANISOU  562  O   CYS A 259     5705   3888   5088    408   -636   -482       O  
ATOM    563  CB  CYS A 259      21.024   9.032  14.624  1.00 39.62           C  
ANISOU  563  CB  CYS A 259     5931   4381   4741   -105   -457   -379       C  
ATOM    564  SG  CYS A 259      19.796   8.820  13.307  1.00 45.73           S  
ANISOU  564  SG  CYS A 259     6259   5529   5585    141  -1076   -279       S  
ATOM    565  N   ASP A 260      23.996   8.997  15.906  1.00 35.79           N  
ANISOU  565  N   ASP A 260     5550   3727   4318    -94   -615   -190       N  
ATOM    566  CA  ASP A 260      24.846   9.476  16.988  1.00 40.52           C  
ANISOU  566  CA  ASP A 260     6101   4588   4706   -395   -968   -150       C  
ATOM    567  C   ASP A 260      26.256   9.876  16.562  1.00 37.81           C  
ANISOU  567  C   ASP A 260     5791   4064   4511    103  -1018     25       C  
ATOM    568  O   ASP A 260      26.848  10.725  17.199  1.00 41.62           O  
ANISOU  568  O   ASP A 260     5575   4774   5463   -314  -1507     83       O  
ATOM    569  CB  ASP A 260      24.934   8.431  18.101  1.00 42.62           C  
ANISOU  569  CB  ASP A 260     6569   4711   4914   -183   -929    -49       C  
ATOM    570  CG  ASP A 260      23.648   8.295  18.886  1.00 44.08           C  
ANISOU  570  CG  ASP A 260     6769   4983   4993   -454   -712   -340       C  
ATOM    571  OD1 ASP A 260      22.683   9.067  18.665  1.00 47.08           O  
ANISOU  571  OD1 ASP A 260     7083   5082   5723   -272   -665   -427       O  
ATOM    572  OD2 ASP A 260      23.610   7.399  19.743  1.00 47.43           O  
ANISOU  572  OD2 ASP A 260     7368   5294   5359   -676   -895   -109       O  
ATOM    573  N   ASP A 261      26.772   9.275  15.497  1.00 40.60           N  
ANISOU  573  N   ASP A 261     6447   4004   4973    423   -695   -104       N  
ATOM    574  CA  ASP A 261      28.158   9.486  15.074  1.00 46.76           C  
ANISOU  574  CA  ASP A 261     6670   5128   5967   -258   -885   -337       C  
ATOM    575  C   ASP A 261      28.335  10.121  13.700  1.00 49.06           C  
ANISOU  575  C   ASP A 261     7508   4934   6199   -144   -623   -167       C  
ATOM    576  O   ASP A 261      29.369  10.727  13.441  1.00 54.33           O  
ANISOU  576  O   ASP A 261     7684   5760   7196   -938   -831   -614       O  
ATOM    577  CB  ASP A 261      28.921   8.160  15.078  1.00 51.53           C  
ANISOU  577  CB  ASP A 261     7224   5627   6726    270   -914   -188       C  
ATOM    578  CG  ASP A 261      29.278   7.678  16.472  1.00 56.03           C  
ANISOU  578  CG  ASP A 261     8098   6319   6872   -156  -1323    -61       C  
ATOM    579  OD1 ASP A 261      28.764   8.221  17.474  1.00 60.28           O  
ANISOU  579  OD1 ASP A 261     8305   6710   7889   -117   -876   -680       O  
ATOM    580  OD2 ASP A 261      30.083   6.729  16.559  1.00 56.52           O  
ANISOU  580  OD2 ASP A 261     7282   6376   7818   -544  -1734   -134       O  
ATOM    581  N   ILE A 262      27.358   9.959  12.808  1.00 43.82           N  
ANISOU  581  N   ILE A 262     6419   4417   5813    167    -83    247       N  
ATOM    582  CA  ILE A 262      27.599  10.251  11.382  1.00 44.51           C  
ANISOU  582  CA  ILE A 262     6974   4109   5827      0    104    127       C  
ATOM    583  C   ILE A 262      26.785  11.408  10.798  1.00 41.69           C  
ANISOU  583  C   ILE A 262     7037   3298   5506   -404    303     36       C  
ATOM    584  O   ILE A 262      27.359  12.323  10.212  1.00 46.17           O  
ANISOU  584  O   ILE A 262     7049   4233   6258   -822    283    683       O  
ATOM    585  CB  ILE A 262      27.448   8.976  10.488  1.00 44.78           C  
ANISOU  585  CB  ILE A 262     6869   4250   5893   -618    271     50       C  
ATOM    586  CG1 ILE A 262      28.189   7.768  11.086  1.00 49.79           C  
ANISOU  586  CG1 ILE A 262     7694   4562   6662   -375   -153    183       C  
ATOM    587  CG2 ILE A 262      27.929   9.236   9.060  1.00 46.55           C  
ANISOU  587  CG2 ILE A 262     7557   4379   5751   -191    236    194       C  
ATOM    588  CD1 ILE A 262      29.699   7.911  11.222  1.00 51.85           C  
ANISOU  588  CD1 ILE A 262     7536   5175   6988   -665    643   -536       C  
ATOM    589  N   LEU A 263      25.465  11.364  10.953  1.00 43.48           N  
ANISOU  589  N   LEU A 263     7087   3347   6085   -254    294    353       N  
ATOM    590  CA  LEU A 263      24.558  12.285  10.242  1.00 49.32           C  
ANISOU  590  CA  LEU A 263     8067   4179   6492    319    -78    370       C  
ATOM    591  C   LEU A 263      24.964  13.751  10.412  1.00 50.62           C  
ANISOU  591  C   LEU A 263     8188   4266   6777     68    426    496       C  
ATOM    592  O   LEU A 263      25.042  14.242  11.535  1.00 54.27           O  
ANISOU  592  O   LEU A 263     8507   5354   6759     95    380    276       O  
ATOM    593  CB  LEU A 263      23.102  12.078  10.686  1.00 54.16           C  
ANISOU  593  CB  LEU A 263     8329   4937   7312    184    315    -53       C  
ATOM    594  CG  LEU A 263      22.090  12.995   9.971  1.00 63.01           C  
ANISOU  594  CG  LEU A 263     9281   6310   8350    615   -208    353       C  
ATOM    595  CD1 LEU A 263      21.427  12.302   8.785  1.00 65.30           C  
ANISOU  595  CD1 LEU A 263     9165   6948   8698    279   -314    151       C  
ATOM    596  CD2 LEU A 263      21.045  13.538  10.936  1.00 61.09           C  
ANISOU  596  CD2 LEU A 263    10097   5444   7667    713  -1053   -945       C  
ATOM    597  N   SER A 264      25.233  14.429   9.293  1.00 49.07           N  
ANISOU  597  N   SER A 264     8493   4116   6034    157   -147    176       N  
ATOM    598  CA  SER A 264      25.628  15.851   9.297  1.00 53.93           C  
ANISOU  598  CA  SER A 264     9278   4304   6907   -124     -7    327       C  
ATOM    599  C   SER A 264      24.833  16.666   8.279  1.00 57.57           C  
ANISOU  599  C   SER A 264    10046   4502   7322    322      0    483       C  
ATOM    600  O   SER A 264      24.360  16.101   7.271  1.00 52.31           O  
ANISOU  600  O   SER A 264     9878   3477   6521    898    426    873       O  
ATOM    601  CB  SER A 264      27.129  16.004   9.023  1.00 52.27           C  
ANISOU  601  CB  SER A 264     9130   4279   6449   -536    290    -91       C  
ATOM    602  OG  SER A 264      27.881  15.260   9.963  1.00 53.80           O  
ANISOU  602  OG  SER A 264     8502   5640   6299   -336    145   -184       O  
ATOM    603  N   PRO A 265      24.681  17.993   8.529  1.00 58.65           N  
ANISOU  603  N   PRO A 265    10310   4506   7467    -95    291    227       N  
ATOM    604  CA  PRO A 265      23.991  18.861   7.571  1.00 63.10           C  
ANISOU  604  CA  PRO A 265    11326   4524   8123    174    304    725       C  
ATOM    605  C   PRO A 265      24.754  18.980   6.256  1.00 62.96           C  
ANISOU  605  C   PRO A 265    11328   4752   7840    355    -44    692       C  
ATOM    606  O   PRO A 265      25.979  18.752   6.219  1.00 62.59           O  
ANISOU  606  O   PRO A 265    11104   3898   8779    325   1045   1141       O  
ATOM    607  CB  PRO A 265      23.949  20.223   8.283  1.00 66.13           C  
ANISOU  607  CB  PRO A 265    11326   5187   8612    717    231    130       C  
ATOM    608  CG  PRO A 265      25.036  20.173   9.297  1.00 64.60           C  
ANISOU  608  CG  PRO A 265    10940   5052   8552    136    217    917       C  
ATOM    609  CD  PRO A 265      25.087  18.740   9.735  1.00 58.61           C  
ANISOU  609  CD  PRO A 265    10005   4657   7605   -517    365    196       C  
ATOM    610  N   ASN A 266      24.015  19.321   5.197  1.00 59.20           N  
ANISOU  610  N   ASN A 266    11208   3667   7617    609     79    565       N  
ATOM    611  CA  ASN A 266      24.550  19.534   3.843  1.00 61.18           C  
ANISOU  611  CA  ASN A 266    11489   4101   7655    115    -32    968       C  
ATOM    612  C   ASN A 266      25.306  18.338   3.274  1.00 61.29           C  
ANISOU  612  C   ASN A 266    11291   4255   7741     58    301   1105       C  
ATOM    613  O   ASN A 266      26.232  18.503   2.472  1.00 66.60           O  
ANISOU  613  O   ASN A 266    11913   5247   8142    109    743   1552       O  
ATOM    614  CB  ASN A 266      25.420  20.799   3.789  1.00 64.03           C  
ANISOU  614  CB  ASN A 266    11752   4150   8426   -218    202    839       C  
ATOM    615  CG  ASN A 266      24.712  22.012   4.343  1.00 68.35           C  
ANISOU  615  CG  ASN A 266    12561   4765   8641    359    336    749       C  
ATOM    616  OD1 ASN A 266      23.611  22.352   3.906  1.00 72.81           O  
ANISOU  616  OD1 ASN A 266    12925   5956   8781    605    133   1822       O  
ATOM    617  ND2 ASN A 266      25.339  22.674   5.316  1.00 69.51           N  
ANISOU  617  ND2 ASN A 266    12988   4383   9039   -390    758    620       N  
ATOM    618  N   THR A 267      24.899  17.139   3.690  1.00 53.00           N  
ANISOU  618  N   THR A 267     9433   3917   6786    212   -325    573       N  
ATOM    619  CA  THR A 267      25.559  15.920   3.277  1.00 50.94           C  
ANISOU  619  CA  THR A 267     9597   3359   6398   -154    376   1086       C  
ATOM    620  C   THR A 267      24.532  14.901   2.805  1.00 56.35           C  
ANISOU  620  C   THR A 267     9696   4703   7011   -302     66    887       C  
ATOM    621  O   THR A 267      23.495  14.695   3.449  1.00 51.63           O  
ANISOU  621  O   THR A 267     9220   3616   6779   -340   -304   1258       O  
ATOM    622  CB  THR A 267      26.419  15.329   4.416  1.00 52.51           C  
ANISOU  622  CB  THR A 267     9651   4225   6072   -163    226    745       C  
ATOM    623  OG1 THR A 267      27.280  16.341   4.947  1.00 56.08           O  
ANISOU  623  OG1 THR A 267     9636   4436   7234   -674    598    638       O  
ATOM    624  CG2 THR A 267      27.277  14.181   3.912  1.00 54.92           C  
ANISOU  624  CG2 THR A 267     9408   4185   7273   -219    433    582       C  
ATOM    625  N   ASN A 268      24.828  14.282   1.666  1.00 58.01           N  
ANISOU  625  N   ASN A 268    10348   4785   6907   -103     35    996       N  
ATOM    626  CA  ASN A 268      24.051  13.170   1.171  1.00 57.80           C  
ANISOU  626  CA  ASN A 268     9917   4691   7353    458   -174    690       C  
ATOM    627  C   ASN A 268      24.748  11.857   1.473  1.00 51.63           C  
ANISOU  627  C   ASN A 268     8996   4174   6445   -329    -10    852       C  
ATOM    628  O   ASN A 268      25.981  11.780   1.479  1.00 51.75           O  
ANISOU  628  O   ASN A 268     8662   4908   6092   -495    718    824       O  
ATOM    629  CB  ASN A 268      23.774  13.330  -0.322  1.00 66.95           C  
ANISOU  629  CB  ASN A 268    11941   6022   7475    279   -333   1288       C  
ATOM    630  CG  ASN A 268      22.551  14.190  -0.597  1.00 78.15           C  
ANISOU  630  CG  ASN A 268    13065   7105   9522   1360   -225   1083       C  
ATOM    631  OD1 ASN A 268      22.227  15.109   0.162  1.00 73.72           O  
ANISOU  631  OD1 ASN A 268    12158   6553   9299   1768  -1038   1370       O  
ATOM    632  ND2 ASN A 268      21.863  13.894  -1.691  1.00 91.09           N  
ANISOU  632  ND2 ASN A 268    14607   9552  10448   1452   -951    299       N  
ATOM    633  N   TYR A 269      23.947  10.834   1.745  1.00 43.80           N  
ANISOU  633  N   TYR A 269     8166   3557   4916    259     98   1106       N  
ATOM    634  CA  TYR A 269      24.480   9.518   2.102  1.00 42.64           C  
ANISOU  634  CA  TYR A 269     7690   3578   4932    189   -148    923       C  
ATOM    635  C   TYR A 269      23.900   8.453   1.194  1.00 45.33           C  
ANISOU  635  C   TYR A 269     7858   4081   5283    140   -148    431       C  
ATOM    636  O   TYR A 269      22.667   8.349   1.041  1.00 44.18           O  
ANISOU  636  O   TYR A 269     7685   3728   5371    462   -144    381       O  
ATOM    637  CB  TYR A 269      24.184   9.189   3.567  1.00 37.98           C  
ANISOU  637  CB  TYR A 269     6858   2847   4724    353   -363    807       C  
ATOM    638  CG  TYR A 269      24.727  10.211   4.543  1.00 42.57           C  
ANISOU  638  CG  TYR A 269     7387   3410   5376   -120   -271    431       C  
ATOM    639  CD1 TYR A 269      23.964  11.331   4.911  1.00 44.41           C  
ANISOU  639  CD1 TYR A 269     7415   3735   5722     -3    153    364       C  
ATOM    640  CD2 TYR A 269      26.004  10.066   5.101  1.00 40.12           C  
ANISOU  640  CD2 TYR A 269     7009   3434   4801   -413     18    544       C  
ATOM    641  CE1 TYR A 269      24.464  12.280   5.796  1.00 44.46           C  
ANISOU  641  CE1 TYR A 269     7705   3848   5339    134   -121    536       C  
ATOM    642  CE2 TYR A 269      26.509  11.009   5.990  1.00 37.92           C  
ANISOU  642  CE2 TYR A 269     6603   2963   4839   -237    599    483       C  
ATOM    643  CZ  TYR A 269      25.741  12.107   6.332  1.00 39.00           C  
ANISOU  643  CZ  TYR A 269     6993   2680   5144   -304    452    590       C  
ATOM    644  OH  TYR A 269      26.235  13.028   7.217  1.00 41.06           O  
ANISOU  644  OH  TYR A 269     7003   3563   5035   -239    329    183       O  
ATOM    645  N   GLU A 270      24.798   7.685   0.583  1.00 43.09           N  
ANISOU  645  N   GLU A 270     7104   4102   5164     94    -59    987       N  
ATOM    646  CA  GLU A 270      24.424   6.552  -0.257  1.00 47.46           C  
ANISOU  646  CA  GLU A 270     8127   4292   5612    304   -491    737       C  
ATOM    647  C   GLU A 270      24.816   5.291   0.499  1.00 43.21           C  
ANISOU  647  C   GLU A 270     6957   4316   5144     69     38    778       C  
ATOM    648  O   GLU A 270      26.000   4.938   0.563  1.00 37.75           O  
ANISOU  648  O   GLU A 270     6599   3379   4362    -56    -75    619       O  
ATOM    649  CB  GLU A 270      25.116   6.611  -1.628  1.00 54.68           C  
ANISOU  649  CB  GLU A 270     8849   5706   6220   -313     14    816       C  
ATOM    650  CG  GLU A 270      24.822   7.861  -2.453  1.00 63.69           C  
ANISOU  650  CG  GLU A 270    11438   6541   6219    579   -371   1696       C  
ATOM    651  CD  GLU A 270      23.348   8.036  -2.807  1.00 76.86           C  
ANISOU  651  CD  GLU A 270    11760   8739   8701    690   -394    956       C  
ATOM    652  OE1 GLU A 270      22.883   9.196  -2.781  1.00 78.29           O  
ANISOU  652  OE1 GLU A 270    11558   8822   9366    974    864   2314       O  
ATOM    653  OE2 GLU A 270      22.657   7.031  -3.114  1.00 78.45           O  
ANISOU  653  OE2 GLU A 270    11887   9321   8599    447   -892    521       O  
ATOM    654  N   VAL A 271      23.814   4.644   1.094  1.00 37.21           N  
ANISOU  654  N   VAL A 271     6072   3500   4566     41   -695    420       N  
ATOM    655  CA  VAL A 271      24.047   3.519   2.003  1.00 38.73           C  
ANISOU  655  CA  VAL A 271     6331   3699   4684    -48   -255    637       C  
ATOM    656  C   VAL A 271      23.567   2.225   1.359  1.00 38.20           C  
ANISOU  656  C   VAL A 271     5819   3732   4961    292   -499    475       C  
ATOM    657  O   VAL A 271      22.462   2.161   0.782  1.00 36.41           O  
ANISOU  657  O   VAL A 271     5502   3670   4662    379   -166    628       O  
ATOM    658  CB  VAL A 271      23.372   3.750   3.382  1.00 38.47           C  
ANISOU  658  CB  VAL A 271     6077   3779   4759    190   -292    604       C  
ATOM    659  CG1 VAL A 271      23.646   2.607   4.355  1.00 33.78           C  
ANISOU  659  CG1 VAL A 271     5063   3292   4479   -368   -355    325       C  
ATOM    660  CG2 VAL A 271      23.857   5.059   3.996  1.00 42.62           C  
ANISOU  660  CG2 VAL A 271     6572   4023   5596     69   -345    261       C  
ATOM    661  N   THR A 272      24.420   1.207   1.451  1.00 32.80           N  
ANISOU  661  N   THR A 272     4626   3585   4252   -216   -843    279       N  
ATOM    662  CA  THR A 272      24.091  -0.138   1.016  1.00 30.75           C  
ANISOU  662  CA  THR A 272     4484   3267   3931    175   -538    372       C  
ATOM    663  C   THR A 272      24.244  -1.083   2.182  1.00 31.10           C  
ANISOU  663  C   THR A 272     4509   3302   4004   -192   -225    519       C  
ATOM    664  O   THR A 272      25.302  -1.108   2.827  1.00 31.68           O  
ANISOU  664  O   THR A 272     4316   3578   4141   -239   -331    432       O  
ATOM    665  CB  THR A 272      24.987  -0.580  -0.152  1.00 35.97           C  
ANISOU  665  CB  THR A 272     5254   3992   4419    -66     -2    302       C  
ATOM    666  OG1 THR A 272      24.931   0.420  -1.169  1.00 38.62           O  
ANISOU  666  OG1 THR A 272     5652   4663   4359     69     -9    671       O  
ATOM    667  CG2 THR A 272      24.524  -1.934  -0.744  1.00 34.48           C  
ANISOU  667  CG2 THR A 272     4617   4175   4307   -324    181    150       C  
ATOM    668  N   TRP A 273      23.179  -1.842   2.465  1.00 28.48           N  
ANISOU  668  N   TRP A 273     3674   3262   3884    158   -472    263       N  
ATOM    669  CA  TRP A 273      23.246  -2.947   3.430  1.00 28.34           C  
ANISOU  669  CA  TRP A 273     3575   3249   3943     45   -213    365       C  
ATOM    670  C   TRP A 273      23.326  -4.289   2.715  1.00 31.84           C  
ANISOU  670  C   TRP A 273     4041   3535   4518    -25   -403     43       C  
ATOM    671  O   TRP A 273      22.684  -4.482   1.673  1.00 32.39           O  
ANISOU  671  O   TRP A 273     4258   3780   4265      0   -338    -12       O  
ATOM    672  CB  TRP A 273      22.015  -2.984   4.317  1.00 27.89           C  
ANISOU  672  CB  TRP A 273     3806   3001   3787    154   -202    169       C  
ATOM    673  CG  TRP A 273      21.854  -1.854   5.291  1.00 26.91           C  
ANISOU  673  CG  TRP A 273     3692   2879   3653    210   -388    243       C  
ATOM    674  CD1 TRP A 273      22.736  -0.831   5.555  1.00 27.60           C  
ANISOU  674  CD1 TRP A 273     3688   3018   3778     83   -277    366       C  
ATOM    675  CD2 TRP A 273      20.750  -1.674   6.177  1.00 28.53           C  
ANISOU  675  CD2 TRP A 273     3656   3219   3965    333   -338    146       C  
ATOM    676  NE1 TRP A 273      22.219  -0.004   6.536  1.00 29.53           N  
ANISOU  676  NE1 TRP A 273     3999   3102   4117    317   -377    234       N  
ATOM    677  CE2 TRP A 273      21.001  -0.501   6.933  1.00 29.91           C  
ANISOU  677  CE2 TRP A 273     4055   3137   4170    262   -312    197       C  
ATOM    678  CE3 TRP A 273      19.552  -2.380   6.393  1.00 33.98           C  
ANISOU  678  CE3 TRP A 273     4155   3895   4860      8    -24    225       C  
ATOM    679  CZ2 TRP A 273      20.099  -0.023   7.898  1.00 34.05           C  
ANISOU  679  CZ2 TRP A 273     4282   4110   4546    408   -181    -58       C  
ATOM    680  CZ3 TRP A 273      18.651  -1.900   7.358  1.00 35.43           C  
ANISOU  680  CZ3 TRP A 273     4311   4177   4971    596   -281     18       C  
ATOM    681  CH2 TRP A 273      18.941  -0.736   8.100  1.00 35.61           C  
ANISOU  681  CH2 TRP A 273     4495   4039   4996    314   -361    228       C  
ATOM    682  N   TYR A 274      24.105  -5.208   3.289  1.00 31.81           N  
ANISOU  682  N   TYR A 274     3828   3520   4735    -59   -324    153       N  
ATOM    683  CA  TYR A 274      24.113  -6.615   2.890  1.00 28.97           C  
ANISOU  683  CA  TYR A 274     3373   3572   4061    -93    100     96       C  
ATOM    684  C   TYR A 274      23.782  -7.380   4.147  1.00 26.81           C  
ANISOU  684  C   TYR A 274     2919   3197   4070    -40   -143     78       C  
ATOM    685  O   TYR A 274      24.624  -7.486   5.039  1.00 28.53           O  
ANISOU  685  O   TYR A 274     3317   3253   4267    -56   -311    448       O  
ATOM    686  CB  TYR A 274      25.494  -7.046   2.365  1.00 27.45           C  
ANISOU  686  CB  TYR A 274     2996   3475   3958    -11   -542    187       C  
ATOM    687  CG  TYR A 274      25.960  -6.273   1.153  1.00 31.25           C  
ANISOU  687  CG  TYR A 274     3693   4139   4038   -348   -110     84       C  
ATOM    688  CD1 TYR A 274      25.620  -6.690  -0.145  1.00 28.62           C  
ANISOU  688  CD1 TYR A 274     3062   3811   4000   -128   -232    169       C  
ATOM    689  CD2 TYR A 274      26.738  -5.119   1.298  1.00 33.76           C  
ANISOU  689  CD2 TYR A 274     3980   4132   4713   -477   -502    273       C  
ATOM    690  CE1 TYR A 274      26.038  -5.974  -1.256  1.00 30.84           C  
ANISOU  690  CE1 TYR A 274     3873   4143   3701   -226   -574    187       C  
ATOM    691  CE2 TYR A 274      27.163  -4.398   0.189  1.00 35.61           C  
ANISOU  691  CE2 TYR A 274     4274   4715   4542   -570   -270    102       C  
ATOM    692  CZ  TYR A 274      26.812  -4.836  -1.077  1.00 35.21           C  
ANISOU  692  CZ  TYR A 274     4566   4186   4624   -435   -421    248       C  
ATOM    693  OH  TYR A 274      27.238  -4.131  -2.150  1.00 39.32           O  
ANISOU  693  OH  TYR A 274     5234   5103   4600   -278   -193    499       O  
ATOM    694  N   THR A 275      22.542  -7.862   4.241  1.00 26.16           N  
ANISOU  694  N   THR A 275     2943   2953   4044    -35   -234      5       N  
ATOM    695  CA  THR A 275      22.037  -8.458   5.474  1.00 27.83           C  
ANISOU  695  CA  THR A 275     3048   3421   4102    -29   -374    313       C  
ATOM    696  C   THR A 275      21.886  -9.960   5.271  1.00 30.28           C  
ANISOU  696  C   THR A 275     3396   3557   4552   -189   -349     78       C  
ATOM    697  O   THR A 275      21.531 -10.402   4.175  1.00 29.58           O  
ANISOU  697  O   THR A 275     3097   3468   4671     40   -483     32       O  
ATOM    698  CB  THR A 275      20.672  -7.847   5.913  1.00 31.99           C  
ANISOU  698  CB  THR A 275     3234   3851   5069    126   -410   -289       C  
ATOM    699  OG1 THR A 275      19.694  -8.065   4.883  1.00 31.07           O  
ANISOU  699  OG1 THR A 275     3023   3878   4904    277   -374   -210       O  
ATOM    700  CG2 THR A 275      20.778  -6.338   6.163  1.00 30.78           C  
ANISOU  700  CG2 THR A 275     3227   3755   4713    204   -797   -250       C  
ATOM    701  N   SER A 276      22.148 -10.745   6.314  1.00 28.37           N  
ANISOU  701  N   SER A 276     2697   3444   4636    -77   -533     28       N  
ATOM    702  CA  SER A 276      21.953 -12.200   6.201  1.00 28.05           C  
ANISOU  702  CA  SER A 276     2639   3522   4495   -207   -290    153       C  
ATOM    703  C   SER A 276      20.462 -12.561   6.249  1.00 29.06           C  
ANISOU  703  C   SER A 276     2634   3711   4694   -200   -224    -84       C  
ATOM    704  O   SER A 276      20.029 -13.461   5.539  1.00 28.09           O  
ANISOU  704  O   SER A 276     2209   3628   4834     -8    -78   -155       O  
ATOM    705  CB  SER A 276      22.753 -12.952   7.254  1.00 25.28           C  
ANISOU  705  CB  SER A 276     2311   2956   4335   -196     10    114       C  
ATOM    706  OG  SER A 276      22.337 -12.634   8.573  1.00 25.44           O  
ANISOU  706  OG  SER A 276     2460   2922   4282   -255    -61     76       O  
ATOM    707  N   TRP A 277      19.690 -11.850   7.073  1.00 29.64           N  
ANISOU  707  N   TRP A 277     2736   3659   4865   -175     46     81       N  
ATOM    708  CA  TRP A 277      18.224 -11.987   7.117  1.00 29.84           C  
ANISOU  708  CA  TRP A 277     2674   4036   4627    124   -242    -61       C  
ATOM    709  C   TRP A 277      17.629 -10.626   6.793  1.00 33.50           C  
ANISOU  709  C   TRP A 277     3156   4258   5314    178   -761     79       C  
ATOM    710  O   TRP A 277      18.219  -9.596   7.143  1.00 32.19           O  
ANISOU  710  O   TRP A 277     2946   3942   5341    357   -517    -84       O  
ATOM    711  CB  TRP A 277      17.719 -12.355   8.521  1.00 26.62           C  
ANISOU  711  CB  TRP A 277     2059   3441   4613     18   -141    -74       C  
ATOM    712  CG  TRP A 277      17.861 -13.788   8.988  1.00 28.13           C  
ANISOU  712  CG  TRP A 277     2086   3544   5055   -151     99    -42       C  
ATOM    713  CD1 TRP A 277      18.581 -14.220  10.071  1.00 32.30           C  
ANISOU  713  CD1 TRP A 277     2864   4133   5275    263    -40    253       C  
ATOM    714  CD2 TRP A 277      17.237 -14.948   8.434  1.00 28.27           C  
ANISOU  714  CD2 TRP A 277     2040   3760   4939   -104     71   -252       C  
ATOM    715  NE1 TRP A 277      18.454 -15.577  10.218  1.00 34.21           N  
ANISOU  715  NE1 TRP A 277     2968   4283   5745   -537     32      6       N  
ATOM    716  CE2 TRP A 277      17.631 -16.055   9.230  1.00 33.14           C  
ANISOU  716  CE2 TRP A 277     2548   4306   5736     35   -131    125       C  
ATOM    717  CE3 TRP A 277      16.369 -15.166   7.352  1.00 29.27           C  
ANISOU  717  CE3 TRP A 277     2146   3873   5100   -117    -47   -458       C  
ATOM    718  CZ2 TRP A 277      17.203 -17.369   8.966  1.00 33.46           C  
ANISOU  718  CZ2 TRP A 277     2623   4369   5720    153   -187   -341       C  
ATOM    719  CZ3 TRP A 277      15.934 -16.490   7.087  1.00 28.68           C  
ANISOU  719  CZ3 TRP A 277     1659   3758   5477     82    164   -218       C  
ATOM    720  CH2 TRP A 277      16.352 -17.562   7.897  1.00 30.49           C  
ANISOU  720  CH2 TRP A 277     2190   3882   5512     31     94   -120       C  
ATOM    721  N   SER A 278      16.449 -10.622   6.170  1.00 29.06           N  
ANISOU  721  N   SER A 278     2464   3720   4858    412    -40    -70       N  
ATOM    722  CA  SER A 278      15.704  -9.383   5.947  1.00 28.98           C  
ANISOU  722  CA  SER A 278     2639   3629   4743    256   -254    140       C  
ATOM    723  C   SER A 278      15.024  -8.933   7.262  1.00 31.28           C  
ANISOU  723  C   SER A 278     3218   3889   4778    344   -282    -82       C  
ATOM    724  O   SER A 278      14.947  -9.723   8.211  1.00 28.36           O  
ANISOU  724  O   SER A 278     2432   3581   4762    438   -242   -245       O  
ATOM    725  CB  SER A 278      14.702  -9.569   4.794  1.00 31.17           C  
ANISOU  725  CB  SER A 278     2759   3975   5108    340   -561    -10       C  
ATOM    726  OG  SER A 278      13.714 -10.530   5.130  1.00 31.94           O  
ANISOU  726  OG  SER A 278     2488   4395   5253    270   -332   -524       O  
ATOM    727  N   PRO A 279      14.539  -7.671   7.339  1.00 34.01           N  
ANISOU  727  N   PRO A 279     3721   3975   5226    488   -344   -208       N  
ATOM    728  CA  PRO A 279      14.090  -7.159   8.651  1.00 32.37           C  
ANISOU  728  CA  PRO A 279     3051   3965   5281    646   -243    -42       C  
ATOM    729  C   PRO A 279      12.754  -7.697   9.167  1.00 35.72           C  
ANISOU  729  C   PRO A 279     3534   4319   5718    257   -119   -352       C  
ATOM    730  O   PRO A 279      11.882  -8.062   8.375  1.00 35.38           O  
ANISOU  730  O   PRO A 279     2834   4367   6241    521   -225   -360       O  
ATOM    731  CB  PRO A 279      13.970  -5.647   8.412  1.00 33.67           C  
ANISOU  731  CB  PRO A 279     3770   3776   5247    582    -44   -526       C  
ATOM    732  CG  PRO A 279      14.838  -5.377   7.214  1.00 35.90           C  
ANISOU  732  CG  PRO A 279     4126   4114   5400    471    -81   -214       C  
ATOM    733  CD  PRO A 279      14.626  -6.582   6.343  1.00 33.40           C  
ANISOU  733  CD  PRO A 279     3397   4055   5238    666   -667   -107       C  
ATOM    734  N   CYS A 280      12.606  -7.731  10.491  1.00 35.31           N  
ANISOU  734  N   CYS A 280     3670   4131   5616    405    155   -324       N  
ATOM    735  CA  CYS A 280      11.298  -7.952  11.131  1.00 36.86           C  
ANISOU  735  CA  CYS A 280     3280   4827   5898    458    -78   -461       C  
ATOM    736  C   CYS A 280      10.389  -6.718  10.891  1.00 37.69           C  
ANISOU  736  C   CYS A 280     3451   4914   5953    597    -55   -552       C  
ATOM    737  O   CYS A 280      10.877  -5.677  10.435  1.00 35.45           O  
ANISOU  737  O   CYS A 280     2915   4793   5760    767    -61   -488       O  
ATOM    738  CB  CYS A 280      11.476  -8.242  12.635  1.00 37.03           C  
ANISOU  738  CB  CYS A 280     3563   4724   5782    213    264   -341       C  
ATOM    739  SG  CYS A 280      11.805  -6.792  13.679  1.00 37.99           S  
ANISOU  739  SG  CYS A 280     3699   4832   5901     64    -21   -314       S  
ATOM    740  N   PRO A 281       9.071  -6.826  11.177  1.00 38.49           N  
ANISOU  740  N   PRO A 281     3282   5191   6149    594   -325   -869       N  
ATOM    741  CA  PRO A 281       8.227  -5.647  10.906  1.00 41.16           C  
ANISOU  741  CA  PRO A 281     3780   5263   6594    868   -120   -824       C  
ATOM    742  C   PRO A 281       8.540  -4.403  11.748  1.00 38.77           C  
ANISOU  742  C   PRO A 281     3371   4954   6403    890    -51   -412       C  
ATOM    743  O   PRO A 281       8.404  -3.295  11.238  1.00 34.88           O  
ANISOU  743  O   PRO A 281     2812   4454   5984    690   -398   -593       O  
ATOM    744  CB  PRO A 281       6.792  -6.147  11.160  1.00 48.19           C  
ANISOU  744  CB  PRO A 281     4087   6659   7563    484    105   -691       C  
ATOM    745  CG  PRO A 281       6.926  -7.466  11.839  1.00 52.95           C  
ANISOU  745  CG  PRO A 281     4602   6911   8605   1053    479   -361       C  
ATOM    746  CD  PRO A 281       8.260  -8.027  11.457  1.00 43.93           C  
ANISOU  746  CD  PRO A 281     4271   5589   6829    281    468   -606       C  
ATOM    747  N   GLU A 282       8.966  -4.586  13.002  1.00 41.66           N  
ANISOU  747  N   GLU A 282     3835   5725   6268    403     28   -512       N  
ATOM    748  CA  GLU A 282       9.312  -3.461  13.894  1.00 44.45           C  
ANISOU  748  CA  GLU A 282     4432   5560   6895    257    184   -692       C  
ATOM    749  C   GLU A 282      10.532  -2.714  13.349  1.00 41.27           C  
ANISOU  749  C   GLU A 282     4151   4960   6568    667    122   -604       C  
ATOM    750  O   GLU A 282      10.516  -1.493  13.274  1.00 38.19           O  
ANISOU  750  O   GLU A 282     3737   4919   5854   1216    320   -893       O  
ATOM    751  CB  GLU A 282       9.577  -3.929  15.337  1.00 46.86           C  
ANISOU  751  CB  GLU A 282     4914   6111   6778    189   -239   -849       C  
ATOM    752  CG  GLU A 282       8.359  -4.471  16.090  1.00 60.24           C  
ANISOU  752  CG  GLU A 282     5658   8567   8664    719   1334   -869       C  
ATOM    753  CD  GLU A 282       7.792  -5.776  15.519  1.00 74.48           C  
ANISOU  753  CD  GLU A 282     8504   8933  10859    283    655  -1112       C  
ATOM    754  OE1 GLU A 282       6.564  -5.992  15.658  1.00 81.26           O  
ANISOU  754  OE1 GLU A 282     8242  10751  11882   1979   1752   -977       O  
ATOM    755  OE2 GLU A 282       8.554  -6.585  14.924  1.00 69.66           O  
ANISOU  755  OE2 GLU A 282     7116   9055  10296    449   1712    604       O  
ATOM    756  N   CYS A 283      11.570  -3.454  12.948  1.00 38.99           N  
ANISOU  756  N   CYS A 283     3875   4953   5984    441    116   -519       N  
ATOM    757  CA  CYS A 283      12.750  -2.845  12.319  1.00 36.88           C  
ANISOU  757  CA  CYS A 283     3801   4715   5497    510    -92   -453       C  
ATOM    758  C   CYS A 283      12.419  -2.154  11.005  1.00 37.67           C  
ANISOU  758  C   CYS A 283     3739   4733   5840    697   -471   -442       C  
ATOM    759  O   CYS A 283      12.851  -1.009  10.773  1.00 38.61           O  
ANISOU  759  O   CYS A 283     3948   4340   6382    971   -706   -329       O  
ATOM    760  CB  CYS A 283      13.853  -3.878  12.085  1.00 39.57           C  
ANISOU  760  CB  CYS A 283     3970   4922   6142    747   -201   -399       C  
ATOM    761  SG  CYS A 283      14.765  -4.236  13.586  1.00 41.21           S  
ANISOU  761  SG  CYS A 283     4568   4927   6162    347   -181     30       S  
ATOM    762  N   ALA A 284      11.663  -2.850  10.151  1.00 34.07           N  
ANISOU  762  N   ALA A 284     3182   4429   5331    767   -270   -437       N  
ATOM    763  CA  ALA A 284      11.253  -2.304   8.863  1.00 34.71           C  
ANISOU  763  CA  ALA A 284     3737   4124   5326    849   -339   -405       C  
ATOM    764  C   ALA A 284      10.551  -0.955   9.030  1.00 37.54           C  
ANISOU  764  C   ALA A 284     3901   4502   5857   1206   -315   -482       C  
ATOM    765  O   ALA A 284      10.840  -0.015   8.293  1.00 39.31           O  
ANISOU  765  O   ALA A 284     4477   4639   5819   1240   -758    -76       O  
ATOM    766  CB  ALA A 284      10.353  -3.293   8.122  1.00 40.44           C  
ANISOU  766  CB  ALA A 284     4097   5387   5879    375   -585   -692       C  
ATOM    767  N   GLY A 285       9.658  -0.868  10.019  1.00 37.24           N  
ANISOU  767  N   GLY A 285     4062   4322   5765   1139   -316   -711       N  
ATOM    768  CA  GLY A 285       8.898   0.358  10.308  1.00 37.60           C  
ANISOU  768  CA  GLY A 285     4152   4336   5796   1255   -722   -723       C  
ATOM    769  C   GLY A 285       9.810   1.468  10.804  1.00 36.70           C  
ANISOU  769  C   GLY A 285     3892   4244   5807   1222   -509   -685       C  
ATOM    770  O   GLY A 285       9.656   2.636  10.430  1.00 38.71           O  
ANISOU  770  O   GLY A 285     4096   4462   6150   1224   -565   -375       O  
ATOM    771  N   GLU A 286      10.772   1.104  11.640  1.00 36.30           N  
ANISOU  771  N   GLU A 286     4030   4264   5496   1137   -444   -663       N  
ATOM    772  CA  GLU A 286      11.743   2.086  12.143  1.00 38.53           C  
ANISOU  772  CA  GLU A 286     4389   4570   5677    746   -346   -550       C  
ATOM    773  C   GLU A 286      12.668   2.613  11.034  1.00 36.79           C  
ANISOU  773  C   GLU A 286     4734   3911   5331    936   -435   -365       C  
ATOM    774  O   GLU A 286      12.888   3.816  10.924  1.00 36.12           O  
ANISOU  774  O   GLU A 286     4785   3793   5146   1123   -603   -891       O  
ATOM    775  CB  GLU A 286      12.539   1.512  13.310  1.00 40.74           C  
ANISOU  775  CB  GLU A 286     4999   4459   6020   1410   -416   -163       C  
ATOM    776  CG  GLU A 286      13.037   2.582  14.267  1.00 59.94           C  
ANISOU  776  CG  GLU A 286     7641   6762   8371     28  -1084  -1416       C  
ATOM    777  CD  GLU A 286      13.910   2.012  15.366  1.00 71.80           C  
ANISOU  777  CD  GLU A 286     9214   9373   8692    510   -604    126       C  
ATOM    778  OE1 GLU A 286      13.515   0.976  15.946  1.00 72.30           O  
ANISOU  778  OE1 GLU A 286    10090   8935   8445    399   1055   -656       O  
ATOM    779  OE2 GLU A 286      14.981   2.604  15.648  1.00 68.78           O  
ANISOU  779  OE2 GLU A 286     9287   9060   7785    473   -878    -10       O  
ATOM    780  N   VAL A 287      13.181   1.716  10.196  1.00 36.38           N  
ANISOU  780  N   VAL A 287     4420   4001   5400   1047   -394   -235       N  
ATOM    781  CA  VAL A 287      13.983   2.121   9.035  1.00 36.13           C  
ANISOU  781  CA  VAL A 287     4565   4021   5141    927   -482    -29       C  
ATOM    782  C   VAL A 287      13.163   3.003   8.059  1.00 36.51           C  
ANISOU  782  C   VAL A 287     4570   3949   5351   1134   -678   -265       C  
ATOM    783  O   VAL A 287      13.670   4.009   7.545  1.00 39.04           O  
ANISOU  783  O   VAL A 287     5376   3973   5484    996   -904    -17       O  
ATOM    784  CB  VAL A 287      14.618   0.903   8.310  1.00 37.82           C  
ANISOU  784  CB  VAL A 287     4783   4169   5415   1126   -482   -119       C  
ATOM    785  CG1 VAL A 287      15.475   1.352   7.140  1.00 40.94           C  
ANISOU  785  CG1 VAL A 287     5099   4873   5582    687   -134   -105       C  
ATOM    786  CG2 VAL A 287      15.476   0.076   9.257  1.00 35.37           C  
ANISOU  786  CG2 VAL A 287     4497   3617   5325    912   -234   -185       C  
ATOM    787  N   ALA A 288      11.905   2.635   7.813  1.00 37.32           N  
ANISOU  787  N   ALA A 288     4469   4049   5663   1314   -590   -123       N  
ATOM    788  CA  ALA A 288      11.039   3.410   6.906  1.00 38.88           C  
ANISOU  788  CA  ALA A 288     4929   4236   5605   1514   -817   -252       C  
ATOM    789  C   ALA A 288      10.801   4.831   7.425  1.00 40.04           C  
ANISOU  789  C   ALA A 288     5081   4314   5818   1516   -832   -264       C  
ATOM    790  O   ALA A 288      10.845   5.793   6.659  1.00 43.16           O  
ANISOU  790  O   ALA A 288     5762   4482   6152   1042  -1084     15       O  
ATOM    791  CB  ALA A 288       9.721   2.692   6.690  1.00 42.54           C  
ANISOU  791  CB  ALA A 288     5040   5411   5710   1489  -1356   -367       C  
ATOM    792  N   GLU A 289      10.565   4.955   8.729  1.00 39.22           N  
ANISOU  792  N   GLU A 289     4539   4457   5903   1162   -779   -477       N  
ATOM    793  CA  GLU A 289      10.353   6.258   9.370  1.00 42.96           C  
ANISOU  793  CA  GLU A 289     5069   4464   6790   1514   -826   -527       C  
ATOM    794  C   GLU A 289      11.643   7.088   9.390  1.00 39.98           C  
ANISOU  794  C   GLU A 289     5457   3682   6050   1519   -724   -466       C  
ATOM    795  O   GLU A 289      11.609   8.296   9.208  1.00 38.09           O  
ANISOU  795  O   GLU A 289     4591   3778   6102   1846   -759    -34       O  
ATOM    796  CB  GLU A 289       9.730   6.050  10.759  1.00 49.84           C  
ANISOU  796  CB  GLU A 289     5888   5938   7110   1729   -454     59       C  
ATOM    797  CG  GLU A 289      10.204   6.930  11.907  1.00 67.59           C  
ANISOU  797  CG  GLU A 289     8190   7739   9753    352  -1111  -1354       C  
ATOM    798  CD  GLU A 289       9.868   6.327  13.269  1.00 86.16           C  
ANISOU  798  CD  GLU A 289    11099  10920  10717    714   -561   -108       C  
ATOM    799  OE1 GLU A 289       8.750   5.781  13.426  1.00 97.36           O  
ANISOU  799  OE1 GLU A 289    11259  13263  12468    672   1576   -870       O  
ATOM    800  OE2 GLU A 289      10.712   6.395  14.193  1.00 75.95           O  
ANISOU  800  OE2 GLU A 289    10210   8770   9875    116    141  -2895       O  
ATOM    801  N   PHE A 290      12.772   6.413   9.590  1.00 41.24           N  
ANISOU  801  N   PHE A 290     5171   4299   6199   1408   -733   -519       N  
ATOM    802  CA  PHE A 290      14.098   7.028   9.481  1.00 36.60           C  
ANISOU  802  CA  PHE A 290     5126   3324   5454   1310   -561   -203       C  
ATOM    803  C   PHE A 290      14.304   7.649   8.101  1.00 39.76           C  
ANISOU  803  C   PHE A 290     5748   3898   5461   1474   -894     40       C  
ATOM    804  O   PHE A 290      14.749   8.806   7.987  1.00 43.86           O  
ANISOU  804  O   PHE A 290     6367   4266   6032    913  -1199   -167       O  
ATOM    805  CB  PHE A 290      15.187   5.984   9.762  1.00 34.81           C  
ANISOU  805  CB  PHE A 290     4824   3310   5092   1156   -818   -504       C  
ATOM    806  CG  PHE A 290      16.589   6.488   9.522  1.00 39.74           C  
ANISOU  806  CG  PHE A 290     5257   3961   5880    943   -346     35       C  
ATOM    807  CD1 PHE A 290      17.242   7.247  10.492  1.00 41.23           C  
ANISOU  807  CD1 PHE A 290     5974   3609   6080    849   -540     67       C  
ATOM    808  CD2 PHE A 290      17.259   6.198   8.333  1.00 43.91           C  
ANISOU  808  CD2 PHE A 290     6109   5298   5274    674   -414    397       C  
ATOM    809  CE1 PHE A 290      18.534   7.711  10.273  1.00 48.26           C  
ANISOU  809  CE1 PHE A 290     6532   5337   6467    450    -30    247       C  
ATOM    810  CE2 PHE A 290      18.556   6.660   8.111  1.00 45.25           C  
ANISOU  810  CE2 PHE A 290     6646   4758   5785    246   -733    572       C  
ATOM    811  CZ  PHE A 290      19.189   7.417   9.083  1.00 43.10           C  
ANISOU  811  CZ  PHE A 290     6044   4350   5980    392   -450    444       C  
ATOM    812  N   LEU A 291      13.972   6.879   7.063  1.00 39.00           N  
ANISOU  812  N   LEU A 291     5744   3539   5534   1307   -702    131       N  
ATOM    813  CA  LEU A 291      14.085   7.334   5.679  1.00 38.03           C  
ANISOU  813  CA  LEU A 291     5540   3599   5308   1526  -1010     -6       C  
ATOM    814  C   LEU A 291      13.140   8.484   5.367  1.00 38.40           C  
ANISOU  814  C   LEU A 291     5942   3526   5122   1548   -974   -120       C  
ATOM    815  O   LEU A 291      13.510   9.400   4.634  1.00 40.15           O  
ANISOU  815  O   LEU A 291     6051   3758   5445   1558  -1285    312       O  
ATOM    816  CB  LEU A 291      13.898   6.169   4.691  1.00 38.50           C  
ANISOU  816  CB  LEU A 291     5701   3739   5187   1327  -1248     27       C  
ATOM    817  CG  LEU A 291      15.004   5.094   4.643  1.00 40.20           C  
ANISOU  817  CG  LEU A 291     5789   3843   5639   1337   -878     91       C  
ATOM    818  CD1 LEU A 291      14.577   3.970   3.720  1.00 38.34           C  
ANISOU  818  CD1 LEU A 291     5531   3738   5295   1597   -630     88       C  
ATOM    819  CD2 LEU A 291      16.369   5.630   4.209  1.00 42.85           C  
ANISOU  819  CD2 LEU A 291     6041   4934   5305   1063   -561    235       C  
ATOM    820  N   ALA A 292      11.934   8.449   5.938  1.00 38.74           N  
ANISOU  820  N   ALA A 292     5888   3487   5343   1622  -1046   -545       N  
ATOM    821  CA  ALA A 292      10.973   9.547   5.769  1.00 43.63           C  
ANISOU  821  CA  ALA A 292     6415   4077   6086   2110  -1206   -236       C  
ATOM    822  C   ALA A 292      11.509  10.801   6.440  1.00 44.16           C  
ANISOU  822  C   ALA A 292     6571   4001   6203   1844   -954    -96       C  
ATOM    823  O   ALA A 292      11.391  11.892   5.902  1.00 47.43           O  
ANISOU  823  O   ALA A 292     7032   4446   6543   2047  -1267    222       O  
ATOM    824  CB  ALA A 292       9.611   9.180   6.346  1.00 46.97           C  
ANISOU  824  CB  ALA A 292     6189   5400   6255   2021  -1584   -263       C  
ATOM    825  N   ARG A 293      12.123  10.622   7.607  1.00 43.25           N  
ANISOU  825  N   ARG A 293     6306   4157   5967   1369   -776   -100       N  
ATOM    826  CA  ARG A 293      12.664  11.728   8.402  1.00 43.91           C  
ANISOU  826  CA  ARG A 293     6588   4017   6076   1606   -749   -191       C  
ATOM    827  C   ARG A 293      13.937  12.336   7.788  1.00 43.68           C  
ANISOU  827  C   ARG A 293     7184   3562   5850   1431   -683     59       C  
ATOM    828  O   ARG A 293      14.198  13.520   7.961  1.00 44.78           O  
ANISOU  828  O   ARG A 293     7313   3580   6119   1261    108     69       O  
ATOM    829  CB  ARG A 293      12.912  11.240   9.844  1.00 43.47           C  
ANISOU  829  CB  ARG A 293     6871   3565   6081   1347   -611   -117       C  
ATOM    830  CG  ARG A 293      13.395  12.262  10.855  1.00 46.90           C  
ANISOU  830  CG  ARG A 293     7312   4185   6320   1505   -388   -689       C  
ATOM    831  CD  ARG A 293      12.358  13.352  11.098  1.00 51.97           C  
ANISOU  831  CD  ARG A 293     7446   4497   7801   1811   -246   -386       C  
ATOM    832  NE  ARG A 293      12.853  14.397  11.991  1.00 53.53           N  
ANISOU  832  NE  ARG A 293     7535   4931   7870   2127  -1070   -371       N  
ATOM    833  CZ  ARG A 293      13.687  15.369  11.627  1.00 61.15           C  
ANISOU  833  CZ  ARG A 293     8945   5642   8644   1393   -853     67       C  
ATOM    834  NH1 ARG A 293      14.153  15.435  10.380  1.00 59.82           N  
ANISOU  834  NH1 ARG A 293     9514   4663   8551   1104   -758   -589       N  
ATOM    835  NH2 ARG A 293      14.071  16.277  12.516  1.00 64.44           N  
ANISOU  835  NH2 ARG A 293    10495   5684   8302   2691   -280   -712       N  
ATOM    836  N   HIS A 294      14.711  11.520   7.068  1.00 44.48           N  
ANISOU  836  N   HIS A 294     6735   4371   5793   1768   -575    381       N  
ATOM    837  CA  HIS A 294      16.019  11.931   6.547  1.00 41.77           C  
ANISOU  837  CA  HIS A 294     7014   3496   5361   1399   -635    428       C  
ATOM    838  C   HIS A 294      16.105  11.746   5.042  1.00 41.62           C  
ANISOU  838  C   HIS A 294     7097   3213   5501   1349   -458    639       C  
ATOM    839  O   HIS A 294      16.587  10.722   4.537  1.00 41.11           O  
ANISOU  839  O   HIS A 294     6665   3409   5547   1342   -899    316       O  
ATOM    840  CB  HIS A 294      17.127  11.161   7.259  1.00 42.33           C  
ANISOU  840  CB  HIS A 294     6314   4065   5703   1418   -625    306       C  
ATOM    841  CG  HIS A 294      17.178  11.422   8.730  1.00 43.74           C  
ANISOU  841  CG  HIS A 294     6909   3931   5778   1044   -683    218       C  
ATOM    842  ND1 HIS A 294      16.665  10.543   9.662  1.00 44.42           N  
ANISOU  842  ND1 HIS A 294     6628   4220   6029   1069   -618    257       N  
ATOM    843  CD2 HIS A 294      17.659  12.476   9.429  1.00 45.38           C  
ANISOU  843  CD2 HIS A 294     7462   3577   6202    827   -648    268       C  
ATOM    844  CE1 HIS A 294      16.841  11.040  10.873  1.00 46.37           C  
ANISOU  844  CE1 HIS A 294     7443   4072   6104   1015    -81   -102       C  
ATOM    845  NE2 HIS A 294      17.441  12.212  10.759  1.00 49.03           N  
ANISOU  845  NE2 HIS A 294     8013   4443   6172    511   -297   -445       N  
ATOM    846  N   SER A 295      15.644  12.770   4.332  1.00 43.75           N  
ANISOU  846  N   SER A 295     7389   3355   5878   1462   -929    625       N  
ATOM    847  CA  SER A 295      15.548  12.757   2.877  1.00 43.06           C  
ANISOU  847  CA  SER A 295     7660   2909   5793   2397  -1192   1281       C  
ATOM    848  C   SER A 295      16.905  12.699   2.171  1.00 50.18           C  
ANISOU  848  C   SER A 295     8335   4247   6483   1524   -797    209       C  
ATOM    849  O   SER A 295      16.980  12.313   0.999  1.00 48.87           O  
ANISOU  849  O   SER A 295     8506   4086   5974   1040  -1248    818       O  
ATOM    850  CB  SER A 295      14.769  13.986   2.409  1.00 51.90           C  
ANISOU  850  CB  SER A 295     8837   4256   6624   1846   -923   1010       C  
ATOM    851  OG  SER A 295      13.989  13.637   1.288  1.00 64.28           O  
ANISOU  851  OG  SER A 295    10112   7090   7220    231  -1772    907       O  
ATOM    852  N   ASN A 296      17.963  13.085   2.888  1.00 47.17           N  
ANISOU  852  N   ASN A 296     8594   3638   5688   1280   -753    446       N  
ATOM    853  CA  ASN A 296      19.340  13.060   2.371  1.00 47.09           C  
ANISOU  853  CA  ASN A 296     8269   3763   5857    755   -889    975       C  
ATOM    854  C   ASN A 296      20.011  11.679   2.480  1.00 46.95           C  
ANISOU  854  C   ASN A 296     8153   3838   5849    776   -269    451       C  
ATOM    855  O   ASN A 296      21.177  11.505   2.084  1.00 44.65           O  
ANISOU  855  O   ASN A 296     7965   3946   5053    898   -586    436       O  
ATOM    856  CB  ASN A 296      20.187  14.138   3.070  1.00 46.85           C  
ANISOU  856  CB  ASN A 296     7984   3825   5990    813   -583    687       C  
ATOM    857  CG  ASN A 296      20.261  13.947   4.583  1.00 48.32           C  
ANISOU  857  CG  ASN A 296     8577   3766   6016    891   -498    470       C  
ATOM    858  OD1 ASN A 296      19.325  13.452   5.212  1.00 49.61           O  
ANISOU  858  OD1 ASN A 296     8069   4488   6292    775   -740    488       O  
ATOM    859  ND2 ASN A 296      21.380  14.342   5.172  1.00 48.56           N  
ANISOU  859  ND2 ASN A 296     8532   4400   5517    226    -35    402       N  
ATOM    860  N   VAL A 297      19.277  10.705   3.022  1.00 41.22           N  
ANISOU  860  N   VAL A 297     7412   3314   4935    797   -982    383       N  
ATOM    861  CA  VAL A 297      19.756   9.330   3.079  1.00 42.54           C  
ANISOU  861  CA  VAL A 297     6958   3612   5592   1023   -962    647       C  
ATOM    862  C   VAL A 297      19.064   8.439   2.038  1.00 44.30           C  
ANISOU  862  C   VAL A 297     7300   4118   5411    950   -559    273       C  
ATOM    863  O   VAL A 297      17.835   8.311   2.024  1.00 44.25           O  
ANISOU  863  O   VAL A 297     7170   4584   5058    246  -1215    -45       O  
ATOM    864  CB  VAL A 297      19.614   8.718   4.494  1.00 43.66           C  
ANISOU  864  CB  VAL A 297     7038   3966   5584    719   -604    591       C  
ATOM    865  CG1 VAL A 297      20.158   7.290   4.522  1.00 42.15           C  
ANISOU  865  CG1 VAL A 297     7016   3692   5303    472   -592    261       C  
ATOM    866  CG2 VAL A 297      20.343   9.573   5.525  1.00 43.97           C  
ANISOU  866  CG2 VAL A 297     7823   3603   5281    446   -343    392       C  
ATOM    867  N   ASN A 298      19.875   7.837   1.174  1.00 40.18           N  
ANISOU  867  N   ASN A 298     6806   3576   4884    936   -552    869       N  
ATOM    868  CA  ASN A 298      19.411   6.848   0.209  1.00 44.76           C  
ANISOU  868  CA  ASN A 298     7322   4029   5654    844  -1027    638       C  
ATOM    869  C   ASN A 298      19.858   5.453   0.644  1.00 41.37           C  
ANISOU  869  C   ASN A 298     6505   3998   5213    691   -753    654       C  
ATOM    870  O   ASN A 298      21.052   5.226   0.829  1.00 40.55           O  
ANISOU  870  O   ASN A 298     6381   3844   5180    764   -791    735       O  
ATOM    871  CB  ASN A 298      19.953   7.174  -1.183  1.00 55.00           C  
ANISOU  871  CB  ASN A 298     8775   5967   6154    816    124    513       C  
ATOM    872  CG  ASN A 298      19.254   6.397  -2.280  1.00 68.36           C  
ANISOU  872  CG  ASN A 298    10963   7368   7643    631  -1021    -97       C  
ATOM    873  OD1 ASN A 298      18.044   6.531  -2.484  1.00 77.21           O  
ANISOU  873  OD1 ASN A 298    11104   9683   8547   1085   -307    512       O  
ATOM    874  ND2 ASN A 298      20.019   5.587  -3.008  1.00 70.80           N  
ANISOU  874  ND2 ASN A 298    11179   7216   8505   1361   -689    488       N  
ATOM    875  N   LEU A 299      18.904   4.534   0.805  1.00 38.17           N  
ANISOU  875  N   LEU A 299     5918   3900   4683    828   -632    516       N  
ATOM    876  CA  LEU A 299      19.212   3.176   1.259  1.00 39.94           C  
ANISOU  876  CA  LEU A 299     6384   3756   5033    616   -513    492       C  
ATOM    877  C   LEU A 299      18.926   2.090   0.213  1.00 40.71           C  
ANISOU  877  C   LEU A 299     5875   4587   5004    920   -944    177       C  
ATOM    878  O   LEU A 299      17.811   1.993  -0.311  1.00 36.97           O  
ANISOU  878  O   LEU A 299     5516   3890   4638   1200   -800    361       O  
ATOM    879  CB  LEU A 299      18.479   2.845   2.577  1.00 39.56           C  
ANISOU  879  CB  LEU A 299     6051   3913   5064    842   -516    438       C  
ATOM    880  CG  LEU A 299      18.718   1.448   3.192  1.00 35.34           C  
ANISOU  880  CG  LEU A 299     4801   3931   4694    619   -347    452       C  
ATOM    881  CD1 LEU A 299      20.190   1.206   3.520  1.00 32.61           C  
ANISOU  881  CD1 LEU A 299     4809   3233   4346    941   -407    294       C  
ATOM    882  CD2 LEU A 299      17.862   1.238   4.431  1.00 31.14           C  
ANISOU  882  CD2 LEU A 299     4478   3077   4276    715   -667    360       C  
ATOM    883  N   THR A 300      19.942   1.268  -0.044  1.00 35.77           N  
ANISOU  883  N   THR A 300     5260   4189   4141    591   -942    329       N  
ATOM    884  CA  THR A 300      19.819   0.059  -0.850  1.00 37.30           C  
ANISOU  884  CA  THR A 300     5479   4082   4610    728   -782    268       C  
ATOM    885  C   THR A 300      20.074  -1.148   0.030  1.00 38.04           C  
ANISOU  885  C   THR A 300     5376   4250   4825    255   -698    533       C  
ATOM    886  O   THR A 300      21.141  -1.256   0.641  1.00 37.74           O  
ANISOU  886  O   THR A 300     5151   4117   5071    478   -688    476       O  
ATOM    887  CB  THR A 300      20.814   0.075  -2.031  1.00 38.67           C  
ANISOU  887  CB  THR A 300     5406   4298   4988    246   -481    393       C  
ATOM    888  OG1 THR A 300      20.540   1.218  -2.847  1.00 43.05           O  
ANISOU  888  OG1 THR A 300     5996   5352   5010    900   -386    820       O  
ATOM    889  CG2 THR A 300      20.720  -1.217  -2.894  1.00 39.71           C  
ANISOU  889  CG2 THR A 300     5626   4813   4645    587   -610    253       C  
ATOM    890  N   ILE A 301      19.094  -2.051   0.091  1.00 34.64           N  
ANISOU  890  N   ILE A 301     4501   4044   4615    638   -434    157       N  
ATOM    891  CA  ILE A 301      19.229  -3.280   0.878  1.00 33.67           C  
ANISOU  891  CA  ILE A 301     4157   4078   4557    398   -507    241       C  
ATOM    892  C   ILE A 301      19.337  -4.517  -0.023  1.00 39.19           C  
ANISOU  892  C   ILE A 301     4840   4417   5632    721   -677   -243       C  
ATOM    893  O   ILE A 301      18.477  -4.752  -0.891  1.00 40.84           O  
ANISOU  893  O   ILE A 301     5118   4563   5836    441   -838   -239       O  
ATOM    894  CB  ILE A 301      18.081  -3.468   1.895  1.00 33.53           C  
ANISOU  894  CB  ILE A 301     3970   4042   4724    766   -439    216       C  
ATOM    895  CG1 ILE A 301      17.971  -2.243   2.822  1.00 36.54           C  
ANISOU  895  CG1 ILE A 301     4490   4233   5157    468   -618   -147       C  
ATOM    896  CG2 ILE A 301      18.288  -4.751   2.711  1.00 32.71           C  
ANISOU  896  CG2 ILE A 301     3808   3823   4795    530     99    202       C  
ATOM    897  CD1 ILE A 301      16.703  -2.206   3.662  1.00 41.11           C  
ANISOU  897  CD1 ILE A 301     4857   5302   5458   1189   -292   -214       C  
ATOM    898  N   PHE A 302      20.415  -5.272   0.186  1.00 34.00           N  
ANISOU  898  N   PHE A 302     4225   3972   4719    184   -612    195       N  
ATOM    899  CA  PHE A 302      20.611  -6.596  -0.393  1.00 31.93           C  
ANISOU  899  CA  PHE A 302     3645   4038   4449    186   -130    189       C  
ATOM    900  C   PHE A 302      20.490  -7.598   0.752  1.00 31.54           C  
ANISOU  900  C   PHE A 302     3563   3805   4614    109   -400    146       C  
ATOM    901  O   PHE A 302      21.156  -7.444   1.771  1.00 34.00           O  
ANISOU  901  O   PHE A 302     3961   4180   4775   -154   -609    294       O  
ATOM    902  CB  PHE A 302      22.006  -6.725  -1.034  1.00 29.06           C  
ANISOU  902  CB  PHE A 302     3223   3547   4272    472   -575    141       C  
ATOM    903  CG  PHE A 302      22.165  -5.965  -2.320  1.00 32.93           C  
ANISOU  903  CG  PHE A 302     3998   4285   4229    482   -239    199       C  
ATOM    904  CD1 PHE A 302      21.670  -6.477  -3.523  1.00 37.33           C  
ANISOU  904  CD1 PHE A 302     4454   4988   4740    411   -731     46       C  
ATOM    905  CD2 PHE A 302      22.822  -4.732  -2.337  1.00 37.54           C  
ANISOU  905  CD2 PHE A 302     4447   4752   5062     49   -540    322       C  
ATOM    906  CE1 PHE A 302      21.818  -5.766  -4.715  1.00 40.01           C  
ANISOU  906  CE1 PHE A 302     5209   5093   4897    147   -193     69       C  
ATOM    907  CE2 PHE A 302      22.974  -4.020  -3.522  1.00 40.35           C  
ANISOU  907  CE2 PHE A 302     5152   5078   5097   -362   -216    328       C  
ATOM    908  CZ  PHE A 302      22.471  -4.537  -4.715  1.00 40.94           C  
ANISOU  908  CZ  PHE A 302     5319   5153   5084    -28   -283    128       C  
ATOM    909  N   THR A 303      19.637  -8.607   0.601  1.00 29.12           N  
ANISOU  909  N   THR A 303     3272   3514   4277    314   -327     19       N  
ATOM    910  CA  THR A 303      19.500  -9.617   1.642  1.00 26.53           C  
ANISOU  910  CA  THR A 303     2604   3426   4050     78   -632    -74       C  
ATOM    911  C   THR A 303      19.809 -11.036   1.126  1.00 30.03           C  
ANISOU  911  C   THR A 303     3174   3714   4518    241   -555   -303       C  
ATOM    912  O   THR A 303      19.400 -11.418   0.031  1.00 28.05           O  
ANISOU  912  O   THR A 303     2618   3588   4450    375   -543   -214       O  
ATOM    913  CB  THR A 303      18.115  -9.516   2.320  1.00 30.62           C  
ANISOU  913  CB  THR A 303     2851   4022   4759    105   -368   -187       C  
ATOM    914  OG1 THR A 303      18.089 -10.333   3.496  1.00 32.10           O  
ANISOU  914  OG1 THR A 303     3111   4156   4928    458   -427    -77       O  
ATOM    915  CG2 THR A 303      16.956  -9.916   1.361  1.00 32.95           C  
ANISOU  915  CG2 THR A 303     3130   4575   4813    295   -737   -158       C  
ATOM    916  N   ALA A 304      20.549 -11.810   1.910  1.00 31.94           N  
ANISOU  916  N   ALA A 304     3011   4071   5053    319   -549    -70       N  
ATOM    917  CA  ALA A 304      20.825 -13.210   1.550  1.00 30.77           C  
ANISOU  917  CA  ALA A 304     2658   4027   5003    -39   -541   -194       C  
ATOM    918  C   ALA A 304      19.546 -14.059   1.548  1.00 28.27           C  
ANISOU  918  C   ALA A 304     2288   3795   4657    263   -560   -219       C  
ATOM    919  O   ALA A 304      19.321 -14.849   0.631  1.00 29.02           O  
ANISOU  919  O   ALA A 304     2117   4116   4792    -35   -889   -209       O  
ATOM    920  CB  ALA A 304      21.860 -13.812   2.498  1.00 30.14           C  
ANISOU  920  CB  ALA A 304     2302   4422   4724   -149   -497   -294       C  
ATOM    921  N   ARG A 305      18.729 -13.878   2.587  1.00 28.94           N  
ANISOU  921  N   ARG A 305     2436   3688   4870    143   -464   -221       N  
ATOM    922  CA  ARG A 305      17.525 -14.662   2.833  1.00 30.47           C  
ANISOU  922  CA  ARG A 305     2488   4078   5009     50   -334   -172       C  
ATOM    923  C   ARG A 305      16.369 -13.758   3.251  1.00 33.94           C  
ANISOU  923  C   ARG A 305     2763   4412   5719    211   -567   -564       C  
ATOM    924  O   ARG A 305      16.583 -12.635   3.747  1.00 30.78           O  
ANISOU  924  O   ARG A 305     2193   4101   5399    328   -820   -325       O  
ATOM    925  CB  ARG A 305      17.785 -15.669   3.950  1.00 28.44           C  
ANISOU  925  CB  ARG A 305     2129   3711   4966     69   -175   -325       C  
ATOM    926  CG  ARG A 305      18.826 -16.741   3.636  1.00 28.13           C  
ANISOU  926  CG  ARG A 305     1827   3729   5131    103   -537   -328       C  
ATOM    927  CD  ARG A 305      18.882 -17.757   4.777  1.00 31.03           C  
ANISOU  927  CD  ARG A 305     2585   3914   5289    -97   -298   -189       C  
ATOM    928  NE  ARG A 305      19.134 -17.091   6.055  1.00 30.80           N  
ANISOU  928  NE  ARG A 305     2482   3864   5356   -219   -235   -269       N  
ATOM    929  CZ  ARG A 305      20.338 -16.759   6.525  1.00 30.50           C  
ANISOU  929  CZ  ARG A 305     2469   4181   4937    -89   -234   -287       C  
ATOM    930  NH1 ARG A 305      21.442 -17.080   5.851  1.00 28.18           N  
ANISOU  930  NH1 ARG A 305     2020   3691   4995   -471   -329   -131       N  
ATOM    931  NH2 ARG A 305      20.435 -16.112   7.686  1.00 26.34           N  
ANISOU  931  NH2 ARG A 305     1677   3444   4886   -509   -451    -18       N  
ATOM    932  N   LEU A 306      15.149 -14.264   3.079  1.00 31.03           N  
ANISOU  932  N   LEU A 306     2496   4168   5123    422   -458   -476       N  
ATOM    933  CA  LEU A 306      13.955 -13.539   3.491  1.00 31.07           C  
ANISOU  933  CA  LEU A 306     2294   4353   5155    297   -469   -439       C  
ATOM    934  C   LEU A 306      13.428 -14.142   4.768  1.00 31.23           C  
ANISOU  934  C   LEU A 306     2043   4494   5329    430   -230   -560       C  
ATOM    935  O   LEU A 306      13.105 -15.334   4.836  1.00 35.48           O  
ANISOU  935  O   LEU A 306     3093   4567   5820    220    -93   -421       O  
ATOM    936  CB  LEU A 306      12.887 -13.549   2.393  1.00 31.15           C  
ANISOU  936  CB  LEU A 306     2194   4190   5449    200   -604   -572       C  
ATOM    937  CG  LEU A 306      13.237 -12.852   1.072  1.00 34.46           C  
ANISOU  937  CG  LEU A 306     2926   4708   5459    153   -731   -311       C  
ATOM    938  CD1 LEU A 306      12.154 -13.068   0.018  1.00 35.03           C  
ANISOU  938  CD1 LEU A 306     2809   4753   5747     90   -798   -540       C  
ATOM    939  CD2 LEU A 306      13.454 -11.359   1.301  1.00 33.84           C  
ANISOU  939  CD2 LEU A 306     2731   4550   5573    615   -806   -374       C  
ATOM    940  N   TYR A 307      13.350 -13.300   5.787  1.00 30.15           N  
ANISOU  940  N   TYR A 307     1947   4215   5294    182   -434   -452       N  
ATOM    941  CA  TYR A 307      12.944 -13.722   7.107  1.00 32.25           C  
ANISOU  941  CA  TYR A 307     2541   4420   5289     88    -76   -635       C  
ATOM    942  C   TYR A 307      11.396 -13.792   7.164  1.00 35.33           C  
ANISOU  942  C   TYR A 307     2595   4650   6177    119   -141   -495       C  
ATOM    943  O   TYR A 307      10.710 -12.795   6.895  1.00 35.64           O  
ANISOU  943  O   TYR A 307     2755   4844   5941    359   -440   -519       O  
ATOM    944  CB  TYR A 307      13.545 -12.737   8.115  1.00 29.11           C  
ANISOU  944  CB  TYR A 307     2009   3647   5405    296    -97   -343       C  
ATOM    945  CG  TYR A 307      13.471 -13.152   9.560  1.00 34.62           C  
ANISOU  945  CG  TYR A 307     2651   4867   5636   -100   -143   -226       C  
ATOM    946  CD1 TYR A 307      14.060 -14.344  10.005  1.00 37.51           C  
ANISOU  946  CD1 TYR A 307     3220   4681   6350   -111   -119   -212       C  
ATOM    947  CD2 TYR A 307      12.828 -12.342  10.491  1.00 36.56           C  
ANISOU  947  CD2 TYR A 307     3142   4649   6099   -413     65   -546       C  
ATOM    948  CE1 TYR A 307      13.993 -14.710  11.342  1.00 42.98           C  
ANISOU  948  CE1 TYR A 307     4244   5380   6705   -147     83    146       C  
ATOM    949  CE2 TYR A 307      12.753 -12.700  11.828  1.00 41.84           C  
ANISOU  949  CE2 TYR A 307     3710   5770   6414    -77    -12    -69       C  
ATOM    950  CZ  TYR A 307      13.331 -13.882  12.246  1.00 44.41           C  
ANISOU  950  CZ  TYR A 307     4115   5508   7249    -92     64   -248       C  
ATOM    951  OH  TYR A 307      13.253 -14.224  13.569  1.00 50.92           O  
ANISOU  951  OH  TYR A 307     5049   6725   7573   -512     23    280       O  
ATOM    952  N   TYR A 308      10.855 -14.977   7.472  1.00 31.03           N  
ANISOU  952  N   TYR A 308     1919   4323   5549    271   -373   -678       N  
ATOM    953  CA  TYR A 308       9.389 -15.202   7.501  1.00 33.91           C  
ANISOU  953  CA  TYR A 308     2018   4745   6120     85   -196   -922       C  
ATOM    954  C   TYR A 308       8.654 -14.646   6.284  1.00 35.86           C  
ANISOU  954  C   TYR A 308     2417   4948   6257    184   -360   -833       C  
ATOM    955  O   TYR A 308       7.636 -13.966   6.443  1.00 38.41           O  
ANISOU  955  O   TYR A 308     2634   5351   6606    493   -444  -1092       O  
ATOM    956  CB  TYR A 308       8.749 -14.597   8.769  1.00 36.66           C  
ANISOU  956  CB  TYR A 308     2323   5260   6345    200    194   -896       C  
ATOM    957  CG  TYR A 308       9.000 -15.378  10.021  1.00 43.18           C  
ANISOU  957  CG  TYR A 308     3689   5786   6929    258     -7   -441       C  
ATOM    958  CD1 TYR A 308       8.424 -16.641  10.202  1.00 47.40           C  
ANISOU  958  CD1 TYR A 308     4134   6169   7707   -397    356   -957       C  
ATOM    959  CD2 TYR A 308       9.805 -14.856  11.045  1.00 42.63           C  
ANISOU  959  CD2 TYR A 308     3696   5139   7361    -33    204   -780       C  
ATOM    960  CE1 TYR A 308       8.659 -17.374  11.356  1.00 48.65           C  
ANISOU  960  CE1 TYR A 308     4837   5401   8246   -965    487   -606       C  
ATOM    961  CE2 TYR A 308      10.036 -15.579  12.209  1.00 46.14           C  
ANISOU  961  CE2 TYR A 308     4260   6077   7191   -237    -13   -806       C  
ATOM    962  CZ  TYR A 308       9.458 -16.835  12.352  1.00 49.01           C  
ANISOU  962  CZ  TYR A 308     4182   6537   7900   -494    438   -431       C  
ATOM    963  OH  TYR A 308       9.685 -17.560  13.485  1.00 54.38           O  
ANISOU  963  OH  TYR A 308     5560   6690   8410   -921   1258     42       O  
ATOM    964  N   PHE A 309       9.155 -14.930   5.079  1.00 36.67           N  
ANISOU  964  N   PHE A 309     2296   5230   6407   -169   -257   -796       N  
ATOM    965  CA  PHE A 309       8.576 -14.368   3.844  1.00 37.56           C  
ANISOU  965  CA  PHE A 309     2457   5436   6376    385   -393   -935       C  
ATOM    966  C   PHE A 309       7.119 -14.785   3.597  1.00 38.85           C  
ANISOU  966  C   PHE A 309     2405   5603   6750    573   -513  -1058       C  
ATOM    967  O   PHE A 309       6.403 -14.131   2.845  1.00 39.69           O  
ANISOU  967  O   PHE A 309     2423   5903   6753    667   -564  -1133       O  
ATOM    968  CB  PHE A 309       9.444 -14.700   2.620  1.00 36.99           C  
ANISOU  968  CB  PHE A 309     2290   5374   6390    315   -404   -946       C  
ATOM    969  CG  PHE A 309       9.552 -16.178   2.312  1.00 39.59           C  
ANISOU  969  CG  PHE A 309     2642   5342   7058    336   -247   -986       C  
ATOM    970  CD1 PHE A 309       8.533 -16.844   1.614  1.00 43.87           C  
ANISOU  970  CD1 PHE A 309     3650   6301   6716    180   -902  -1171       C  
ATOM    971  CD2 PHE A 309      10.687 -16.903   2.687  1.00 39.31           C  
ANISOU  971  CD2 PHE A 309     2922   5503   6510    334   -545   -860       C  
ATOM    972  CE1 PHE A 309       8.637 -18.203   1.324  1.00 45.16           C  
ANISOU  972  CE1 PHE A 309     3571   6396   7189    329   -614  -1134       C  
ATOM    973  CE2 PHE A 309      10.800 -18.262   2.392  1.00 39.16           C  
ANISOU  973  CE2 PHE A 309     2608   5551   6718    258    -93   -865       C  
ATOM    974  CZ  PHE A 309       9.771 -18.912   1.710  1.00 42.58           C  
ANISOU  974  CZ  PHE A 309     3266   6090   6820    157   -413  -1219       C  
ATOM    975  N   TRP A 310       6.695 -15.874   4.228  1.00 40.54           N  
ANISOU  975  N   TRP A 310     2702   5682   7018    363   -185  -1147       N  
ATOM    976  CA  TRP A 310       5.321 -16.364   4.095  1.00 43.48           C  
ANISOU  976  CA  TRP A 310     2738   6180   7600    394   -508  -1160       C  
ATOM    977  C   TRP A 310       4.340 -15.704   5.065  1.00 47.19           C  
ANISOU  977  C   TRP A 310     3323   6787   7819    453    -44  -1288       C  
ATOM    978  O   TRP A 310       3.138 -15.931   4.972  1.00 48.87           O  
ANISOU  978  O   TRP A 310     3569   6074   8925   -259   -517   -976       O  
ATOM    979  CB  TRP A 310       5.274 -17.877   4.267  1.00 41.80           C  
ANISOU  979  CB  TRP A 310     2006   6202   7674     12   -546  -1307       C  
ATOM    980  CG  TRP A 310       5.810 -18.329   5.584  1.00 43.70           C  
ANISOU  980  CG  TRP A 310     2819   6163   7619    306    -63   -949       C  
ATOM    981  CD1 TRP A 310       5.099 -18.550   6.724  1.00 43.29           C  
ANISOU  981  CD1 TRP A 310     2900   5904   7645    311    126  -1285       C  
ATOM    982  CD2 TRP A 310       7.183 -18.594   5.904  1.00 41.45           C  
ANISOU  982  CD2 TRP A 310     2792   5634   7320    220   -121  -1159       C  
ATOM    983  NE1 TRP A 310       5.935 -18.947   7.732  1.00 44.89           N  
ANISOU  983  NE1 TRP A 310     3008   6466   7582    -65    -20  -1122       N  
ATOM    984  CE2 TRP A 310       7.221 -18.987   7.260  1.00 41.90           C  
ANISOU  984  CE2 TRP A 310     2914   5745   7260    -51    -62  -1302       C  
ATOM    985  CE3 TRP A 310       8.379 -18.552   5.172  1.00 40.28           C  
ANISOU  985  CE3 TRP A 310     2600   5471   7232    -44   -305   -715       C  
ATOM    986  CZ2 TRP A 310       8.415 -19.340   7.909  1.00 39.93           C  
ANISOU  986  CZ2 TRP A 310     2823   5376   6972   -251     63  -1055       C  
ATOM    987  CZ3 TRP A 310       9.581 -18.901   5.819  1.00 37.15           C  
ANISOU  987  CZ3 TRP A 310     2249   5214   6650   -245   -110  -1072       C  
ATOM    988  CH2 TRP A 310       9.582 -19.289   7.174  1.00 38.37           C  
ANISOU  988  CH2 TRP A 310     2601   5120   6858   -303    -94   -949       C  
ATOM    989  N   ASP A 311       4.849 -14.895   5.992  1.00 49.22           N  
ANISOU  989  N   ASP A 311     3615   7096   7991    378    -76  -1482       N  
ATOM    990  CA  ASP A 311       4.014 -14.216   6.987  1.00 46.98           C  
ANISOU  990  CA  ASP A 311     3591   6383   7875    533   -215  -1381       C  
ATOM    991  C   ASP A 311       3.658 -12.815   6.489  1.00 46.43           C  
ANISOU  991  C   ASP A 311     3201   6781   7657    778    -25  -1066       C  
ATOM    992  O   ASP A 311       4.548 -12.034   6.141  1.00 43.75           O  
ANISOU  992  O   ASP A 311     2327   6712   7582   1040   -350   -968       O  
ATOM    993  CB  ASP A 311       4.765 -14.161   8.327  1.00 47.86           C  
ANISOU  993  CB  ASP A 311     3670   6775   7737    228     28  -1182       C  
ATOM    994  CG  ASP A 311       3.946 -13.540   9.454  1.00 52.73           C  
ANISOU  994  CG  ASP A 311     4080   7528   8424    588    595  -1278       C  
ATOM    995  OD1 ASP A 311       3.442 -12.409   9.315  1.00 54.69           O  
ANISOU  995  OD1 ASP A 311     4472   7740   8566    397    340   -799       O  
ATOM    996  OD2 ASP A 311       3.836 -14.180  10.514  1.00 59.88           O  
ANISOU  996  OD2 ASP A 311     5534   7939   9278    701   1250   -729       O  
ATOM    997  N   THR A 312       2.360 -12.495   6.497  1.00 45.24           N  
ANISOU  997  N   THR A 312     3071   6683   7433    544   -159  -1087       N  
ATOM    998  CA  THR A 312       1.842 -11.214   5.985  1.00 47.03           C  
ANISOU  998  CA  THR A 312     3291   6791   7785    879   -721  -1309       C  
ATOM    999  C   THR A 312       2.387  -9.985   6.714  1.00 48.53           C  
ANISOU  999  C   THR A 312     3483   6857   8096   1113   -813  -1455       C  
ATOM   1000  O   THR A 312       2.647  -8.962   6.080  1.00 49.58           O  
ANISOU 1000  O   THR A 312     3698   7274   7865   1175  -1233   -833       O  
ATOM   1001  CB  THR A 312       0.280 -11.156   5.949  1.00 52.45           C  
ANISOU 1001  CB  THR A 312     3365   7620   8942   1172   -450  -1979       C  
ATOM   1002  OG1 THR A 312      -0.246 -10.999   7.270  1.00 61.61           O  
ANISOU 1002  OG1 THR A 312     4713   9262   9432    797    188  -1319       O  
ATOM   1003  CG2 THR A 312      -0.311 -12.414   5.334  1.00 48.93           C  
ANISOU 1003  CG2 THR A 312     2693   7642   8257    354   -272  -1329       C  
ATOM   1004  N   ASP A 313       2.566 -10.086   8.034  1.00 49.20           N  
ANISOU 1004  N   ASP A 313     3310   7361   8020   1392    -87  -1456       N  
ATOM   1005  CA  ASP A 313       3.186  -9.008   8.821  1.00 51.28           C  
ANISOU 1005  CA  ASP A 313     3718   7212   8552   1171     -2  -1503       C  
ATOM   1006  C   ASP A 313       4.594  -8.657   8.328  1.00 48.14           C  
ANISOU 1006  C   ASP A 313     4084   6596   7611    943     19  -1215       C  
ATOM   1007  O   ASP A 313       4.946  -7.480   8.251  1.00 45.83           O  
ANISOU 1007  O   ASP A 313     3763   6284   7364   1413     39   -939       O  
ATOM   1008  CB  ASP A 313       3.234  -9.357  10.312  1.00 58.91           C  
ANISOU 1008  CB  ASP A 313     5110   8636   8636   1161   -146  -1416       C  
ATOM   1009  CG  ASP A 313       1.851  -9.489  10.935  1.00 68.79           C  
ANISOU 1009  CG  ASP A 313     5528  10156  10453    875    441  -1273       C  
ATOM   1010  OD1 ASP A 313       0.908  -8.814  10.471  1.00 69.51           O  
ANISOU 1010  OD1 ASP A 313     6298   9839  10273   1753   1258  -1479       O  
ATOM   1011  OD2 ASP A 313       1.710 -10.267  11.902  1.00 72.40           O  
ANISOU 1011  OD2 ASP A 313     5651  11178  10677   1017   1580   -919       O  
ATOM   1012  N   TYR A 314       5.383  -9.679   7.991  1.00 44.89           N  
ANISOU 1012  N   TYR A 314     3322   6578   7155    896    132   -675       N  
ATOM   1013  CA  TYR A 314       6.740  -9.480   7.474  1.00 38.96           C  
ANISOU 1013  CA  TYR A 314     2964   5202   6637   1107   -370   -549       C  
ATOM   1014  C   TYR A 314       6.729  -8.956   6.037  1.00 40.30           C  
ANISOU 1014  C   TYR A 314     3029   5703   6579   1065   -848   -576       C  
ATOM   1015  O   TYR A 314       7.560  -8.111   5.660  1.00 40.32           O  
ANISOU 1015  O   TYR A 314     2693   5434   7193   1230   -996   -215       O  
ATOM   1016  CB  TYR A 314       7.575 -10.772   7.612  1.00 33.80           C  
ANISOU 1016  CB  TYR A 314     2337   4524   5982    527   -221  -1038       C  
ATOM   1017  CG  TYR A 314       7.926 -11.072   9.058  1.00 36.05           C  
ANISOU 1017  CG  TYR A 314     2719   4672   6306    741   -270   -638       C  
ATOM   1018  CD1 TYR A 314       6.939 -11.482   9.973  1.00 40.13           C  
ANISOU 1018  CD1 TYR A 314     3392   5038   6814    563    268   -755       C  
ATOM   1019  CD2 TYR A 314       9.245 -10.928   9.525  1.00 34.16           C  
ANISOU 1019  CD2 TYR A 314     2714   4143   6123    531   -185   -763       C  
ATOM   1020  CE1 TYR A 314       7.255 -11.739  11.300  1.00 40.96           C  
ANISOU 1020  CE1 TYR A 314     3656   5025   6879    657     32   -908       C  
ATOM   1021  CE2 TYR A 314       9.566 -11.186  10.849  1.00 37.20           C  
ANISOU 1021  CE2 TYR A 314     3563   4490   6079    247   -200   -811       C  
ATOM   1022  CZ  TYR A 314       8.570 -11.594  11.725  1.00 44.91           C  
ANISOU 1022  CZ  TYR A 314     3499   6226   7340    279    331   -889       C  
ATOM   1023  OH  TYR A 314       8.881 -11.853  13.036  1.00 55.60           O  
ANISOU 1023  OH  TYR A 314     6097   7166   7860    821   -503   -431       O  
ATOM   1024  N   GLN A 315       5.774  -9.443   5.250  1.00 39.07           N  
ANISOU 1024  N   GLN A 315     2832   5098   6915    993   -536  -1100       N  
ATOM   1025  CA  GLN A 315       5.558  -8.953   3.884  1.00 47.48           C  
ANISOU 1025  CA  GLN A 315     4341   6682   7015    890   -972   -840       C  
ATOM   1026  C   GLN A 315       5.246  -7.449   3.888  1.00 50.79           C  
ANISOU 1026  C   GLN A 315     4787   6913   7598   1527   -302   -658       C  
ATOM   1027  O   GLN A 315       5.857  -6.682   3.134  1.00 43.75           O  
ANISOU 1027  O   GLN A 315     3498   6229   6893   1650   -496  -1049       O  
ATOM   1028  CB  GLN A 315       4.437  -9.737   3.190  1.00 46.59           C  
ANISOU 1028  CB  GLN A 315     3818   6589   7293   1096   -477  -1443       C  
ATOM   1029  CG  GLN A 315       4.761 -11.214   2.986  1.00 44.57           C  
ANISOU 1029  CG  GLN A 315     3334   6354   7246   1116   -896   -825       C  
ATOM   1030  CD  GLN A 315       3.602 -12.010   2.418  1.00 46.84           C  
ANISOU 1030  CD  GLN A 315     3706   6557   7533   1102   -916  -1444       C  
ATOM   1031  OE1 GLN A 315       2.552 -11.462   2.124  1.00 50.13           O  
ANISOU 1031  OE1 GLN A 315     3487   7017   8544   1115  -1136  -2026       O  
ATOM   1032  NE2 GLN A 315       3.794 -13.309   2.255  1.00 43.83           N  
ANISOU 1032  NE2 GLN A 315     3179   6358   7116    997   -754  -1604       N  
ATOM   1033  N   GLU A 316       4.330  -7.023   4.762  1.00 51.17           N  
ANISOU 1033  N   GLU A 316     4411   6996   8034   1377   -538   -961       N  
ATOM   1034  CA  GLU A 316       4.022  -5.600   4.874  1.00 51.70           C  
ANISOU 1034  CA  GLU A 316     4501   7173   7967   1743   -886  -1461       C  
ATOM   1035  C   GLU A 316       5.230  -4.750   5.255  1.00 49.78           C  
ANISOU 1035  C   GLU A 316     4698   6880   7333   1586  -1134   -654       C  
ATOM   1036  O   GLU A 316       5.380  -3.632   4.753  1.00 53.06           O  
ANISOU 1036  O   GLU A 316     5928   6447   7786   2241   -683   -806       O  
ATOM   1037  CB  GLU A 316       2.853  -5.325   5.823  1.00 54.19           C  
ANISOU 1037  CB  GLU A 316     4865   7477   8248   1303   -606  -1516       C  
ATOM   1038  CG  GLU A 316       1.593  -4.862   5.095  1.00 64.60           C  
ANISOU 1038  CG  GLU A 316     5410   9197   9935   3217  -1699  -1596       C  
ATOM   1039  CD  GLU A 316       1.811  -3.663   4.160  1.00 76.45           C  
ANISOU 1039  CD  GLU A 316     8004  10593  10450   2318  -1042  -1366       C  
ATOM   1040  OE1 GLU A 316       1.279  -3.703   3.031  1.00 75.90           O  
ANISOU 1040  OE1 GLU A 316     7057  10720  11059   2522  -1506  -2485       O  
ATOM   1041  OE2 GLU A 316       2.507  -2.683   4.535  1.00 75.40           O  
ANISOU 1041  OE2 GLU A 316     7586  10792  10268   2597   -467  -2140       O  
ATOM   1042  N   GLY A 317       6.086  -5.296   6.121  1.00 42.57           N  
ANISOU 1042  N   GLY A 317     3511   5918   6744   1286   -657  -1016       N  
ATOM   1043  CA  GLY A 317       7.318  -4.621   6.530  1.00 41.89           C  
ANISOU 1043  CA  GLY A 317     3793   5629   6491    989   -692   -368       C  
ATOM   1044  C   GLY A 317       8.208  -4.331   5.339  1.00 39.58           C  
ANISOU 1044  C   GLY A 317     3715   5235   6088   1413   -893   -737       C  
ATOM   1045  O   GLY A 317       8.701  -3.213   5.173  1.00 42.55           O  
ANISOU 1045  O   GLY A 317     4658   4980   6529   1547  -1321   -712       O  
ATOM   1046  N   LEU A 318       8.398  -5.342   4.498  1.00 38.38           N  
ANISOU 1046  N   LEU A 318     3547   5175   5859   1091  -1013   -710       N  
ATOM   1047  CA  LEU A 318       9.189  -5.197   3.278  1.00 37.58           C  
ANISOU 1047  CA  LEU A 318     3509   4912   5856   1243   -858   -763       C  
ATOM   1048  C   LEU A 318       8.590  -4.170   2.324  1.00 42.82           C  
ANISOU 1048  C   LEU A 318     4613   5549   6106   1540   -903   -459       C  
ATOM   1049  O   LEU A 318       9.311  -3.344   1.756  1.00 42.32           O  
ANISOU 1049  O   LEU A 318     4658   5247   6173   1193  -1105   -591       O  
ATOM   1050  CB  LEU A 318       9.345  -6.548   2.593  1.00 37.83           C  
ANISOU 1050  CB  LEU A 318     3508   4818   6045   1143   -732   -832       C  
ATOM   1051  CG  LEU A 318      10.140  -7.577   3.420  1.00 40.77           C  
ANISOU 1051  CG  LEU A 318     3913   5444   6133   1057  -1081   -422       C  
ATOM   1052  CD1 LEU A 318      10.182  -8.917   2.707  1.00 43.60           C  
ANISOU 1052  CD1 LEU A 318     4652   5652   6261   1641   -941   -692       C  
ATOM   1053  CD2 LEU A 318      11.552  -7.107   3.764  1.00 39.23           C  
ANISOU 1053  CD2 LEU A 318     3840   5114   5949   1086  -1042    222       C  
ATOM   1054  N   ARG A 319       7.266  -4.222   2.180  1.00 46.65           N  
ANISOU 1054  N   ARG A 319     4659   6210   6854   1581  -1283   -783       N  
ATOM   1055  CA  ARG A 319       6.524  -3.284   1.352  1.00 47.30           C  
ANISOU 1055  CA  ARG A 319     4793   5952   7227   1616  -1298   -842       C  
ATOM   1056  C   ARG A 319       6.685  -1.851   1.843  1.00 43.82           C  
ANISOU 1056  C   ARG A 319     4178   5889   6583   2034   -994   -764       C  
ATOM   1057  O   ARG A 319       6.925  -0.954   1.039  1.00 46.21           O  
ANISOU 1057  O   ARG A 319     5319   5241   6997   2325  -1514   -573       O  
ATOM   1058  CB  ARG A 319       5.045  -3.682   1.274  1.00 47.90           C  
ANISOU 1058  CB  ARG A 319     4814   6244   7140   1711  -1595   -913       C  
ATOM   1059  CG  ARG A 319       4.819  -4.959   0.465  1.00 46.92           C  
ANISOU 1059  CG  ARG A 319     4477   6067   7281   2152  -1153  -1154       C  
ATOM   1060  CD  ARG A 319       3.390  -5.476   0.570  1.00 54.79           C  
ANISOU 1060  CD  ARG A 319     5027   7475   8315   1761  -1125  -1375       C  
ATOM   1061  NE  ARG A 319       2.434  -4.561  -0.038  1.00 56.14           N  
ANISOU 1061  NE  ARG A 319     4411   7576   9342   2826  -2142  -1402       N  
ATOM   1062  CZ  ARG A 319       2.175  -4.480  -1.342  1.00 72.23           C  
ANISOU 1062  CZ  ARG A 319     8033   9915   9493   2348  -1175  -1402       C  
ATOM   1063  NH1 ARG A 319       1.275  -3.604  -1.781  1.00 77.33           N  
ANISOU 1063  NH1 ARG A 319     8036  10110  11234   3082  -1088   -866       N  
ATOM   1064  NH2 ARG A 319       2.803  -5.265  -2.214  1.00 68.19           N  
ANISOU 1064  NH2 ARG A 319     5066   9397  11444   3498   -501   -483       N  
ATOM   1065  N   SER A 320       6.604  -1.645   3.155  1.00 42.13           N  
ANISOU 1065  N   SER A 320     3319   5976   6711   1873  -1029   -806       N  
ATOM   1066  CA  SER A 320       6.688  -0.289   3.705  1.00 50.10           C  
ANISOU 1066  CA  SER A 320     5568   6014   7454   1351  -1125   -896       C  
ATOM   1067  C   SER A 320       8.087   0.309   3.505  1.00 45.65           C  
ANISOU 1067  C   SER A 320     5196   5508   6641   1764  -1115   -778       C  
ATOM   1068  O   SER A 320       8.210   1.496   3.230  1.00 48.66           O  
ANISOU 1068  O   SER A 320     5420   5607   7458   2225   -679   -525       O  
ATOM   1069  CB  SER A 320       6.266  -0.250   5.173  1.00 53.66           C  
ANISOU 1069  CB  SER A 320     6042   6397   7948   1531   -429   -624       C  
ATOM   1070  OG  SER A 320       7.326  -0.675   6.008  1.00 63.68           O  
ANISOU 1070  OG  SER A 320     6917   9148   8131   1937  -2088    -97       O  
ATOM   1071  N   LEU A 321       9.129  -0.518   3.630  1.00 46.31           N  
ANISOU 1071  N   LEU A 321     5119   5514   6962   1612   -681   -295       N  
ATOM   1072  CA  LEU A 321      10.494  -0.119   3.271  1.00 42.53           C  
ANISOU 1072  CA  LEU A 321     4957   5090   6111   1537  -1074   -325       C  
ATOM   1073  C   LEU A 321      10.597   0.349   1.824  1.00 45.01           C  
ANISOU 1073  C   LEU A 321     5589   5306   6204   1441  -1165   -227       C  
ATOM   1074  O   LEU A 321      11.183   1.398   1.543  1.00 45.60           O  
ANISOU 1074  O   LEU A 321     6412   4936   5977   1224  -1644   -299       O  
ATOM   1075  CB  LEU A 321      11.485  -1.271   3.495  1.00 41.86           C  
ANISOU 1075  CB  LEU A 321     5095   4789   6018   1389  -1278   -336       C  
ATOM   1076  CG  LEU A 321      11.983  -1.487   4.921  1.00 41.43           C  
ANISOU 1076  CG  LEU A 321     4834   4948   5960   1276  -1116   -245       C  
ATOM   1077  CD1 LEU A 321      12.863  -2.730   4.995  1.00 40.52           C  
ANISOU 1077  CD1 LEU A 321     4946   4805   5643   1166   -758     11       C  
ATOM   1078  CD2 LEU A 321      12.737  -0.247   5.375  1.00 42.30           C  
ANISOU 1078  CD2 LEU A 321     4736   5457   5876    883  -1704    -11       C  
ATOM   1079  N   SER A 322      10.030  -0.438   0.913  1.00 43.71           N  
ANISOU 1079  N   SER A 322     4872   5468   6264   1389  -1351   -180       N  
ATOM   1080  CA  SER A 322      10.076  -0.131  -0.513  1.00 45.86           C  
ANISOU 1080  CA  SER A 322     5560   5668   6197   1757  -1316   -288       C  
ATOM   1081  C   SER A 322       9.318   1.169  -0.805  1.00 46.92           C  
ANISOU 1081  C   SER A 322     5839   5928   6061   1902  -1515   -239       C  
ATOM   1082  O   SER A 322       9.801   2.034  -1.552  1.00 45.45           O  
ANISOU 1082  O   SER A 322     5972   6067   5229   1554  -1553   -378       O  
ATOM   1083  CB  SER A 322       9.534  -1.314  -1.324  1.00 51.04           C  
ANISOU 1083  CB  SER A 322     5722   6478   7191    960  -1224   -697       C  
ATOM   1084  OG  SER A 322       9.657  -1.097  -2.720  1.00 52.16           O  
ANISOU 1084  OG  SER A 322     6173   6510   7134    982  -1267   -950       O  
ATOM   1085  N   GLN A 323       8.166   1.331  -0.155  1.00 47.82           N  
ANISOU 1085  N   GLN A 323     5782   5851   6533   2458  -1468   -271       N  
ATOM   1086  CA  GLN A 323       7.313   2.506  -0.359  1.00 49.22           C  
ANISOU 1086  CA  GLN A 323     6269   5599   6830   2408  -1239   -714       C  
ATOM   1087  C   GLN A 323       7.946   3.802   0.152  1.00 52.18           C  
ANISOU 1087  C   GLN A 323     6556   6150   7118   1945  -1499   -572       C  
ATOM   1088  O   GLN A 323       7.590   4.879  -0.315  1.00 59.07           O  
ANISOU 1088  O   GLN A 323     8136   6853   7456   2151  -2318    222       O  
ATOM   1089  CB  GLN A 323       5.939   2.282   0.275  1.00 52.94           C  
ANISOU 1089  CB  GLN A 323     5846   6803   7466   2654  -1784    -18       C  
ATOM   1090  CG  GLN A 323       5.066   1.294  -0.500  1.00 67.02           C  
ANISOU 1090  CG  GLN A 323     7939   8327   9196   1850  -2027  -1305       C  
ATOM   1091  CD  GLN A 323       3.932   0.690   0.322  1.00 74.89           C  
ANISOU 1091  CD  GLN A 323     8466   9515  10471   2032  -1469   -821       C  
ATOM   1092  OE1 GLN A 323       3.750   1.007   1.503  1.00 77.62           O  
ANISOU 1092  OE1 GLN A 323     8005  10460  11025   2325   -890  -1317       O  
ATOM   1093  NE2 GLN A 323       3.162  -0.196  -0.307  1.00 73.09           N  
ANISOU 1093  NE2 GLN A 323     7930   9824  10014   2535  -2673   -334       N  
ATOM   1094  N   GLU A 324       8.878   3.703   1.104  1.00 51.42           N  
ANISOU 1094  N   GLU A 324     6545   6151   6841   2003  -1485    -75       N  
ATOM   1095  CA  GLU A 324       9.626   4.882   1.575  1.00 51.08           C  
ANISOU 1095  CA  GLU A 324     6796   5977   6635   2112  -1509   -241       C  
ATOM   1096  C   GLU A 324      10.932   5.112   0.810  1.00 51.60           C  
ANISOU 1096  C   GLU A 324     7347   5754   6504   1768  -1162    -94       C  
ATOM   1097  O   GLU A 324      11.725   5.963   1.207  1.00 56.79           O  
ANISOU 1097  O   GLU A 324     7720   5796   8060   1610  -1169   -259       O  
ATOM   1098  CB  GLU A 324       9.914   4.825   3.092  1.00 47.13           C  
ANISOU 1098  CB  GLU A 324     6161   5178   6564   2330  -1502    124       C  
ATOM   1099  CG  GLU A 324       8.702   4.935   4.005  1.00 53.12           C  
ANISOU 1099  CG  GLU A 324     7323   6137   6724   1999   -916   -218       C  
ATOM   1100  CD  GLU A 324       7.930   6.244   3.875  1.00 63.85           C  
ANISOU 1100  CD  GLU A 324     8633   6799   8827   2846  -1124   -508       C  
ATOM   1101  OE1 GLU A 324       8.537   7.310   3.617  1.00 64.11           O  
ANISOU 1101  OE1 GLU A 324     8730   6895   8733   2735  -1597   -146       O  
ATOM   1102  OE2 GLU A 324       6.694   6.203   4.045  1.00 72.35           O  
ANISOU 1102  OE2 GLU A 324     8942   9105   9443   2266   -360   -253       O  
ATOM   1103  N   GLY A 325      11.166   4.347  -0.256  1.00 46.54           N  
ANISOU 1103  N   GLY A 325     6065   5239   6379   1647  -2368   -236       N  
ATOM   1104  CA  GLY A 325      12.275   4.622  -1.174  1.00 49.01           C  
ANISOU 1104  CA  GLY A 325     7000   5205   6414   1692  -1830   -174       C  
ATOM   1105  C   GLY A 325      13.514   3.750  -1.041  1.00 46.51           C  
ANISOU 1105  C   GLY A 325     6657   5222   5790   1301  -2167    -47       C  
ATOM   1106  O   GLY A 325      14.464   3.905  -1.811  1.00 47.85           O  
ANISOU 1106  O   GLY A 325     6959   5306   5915   1023  -1797   -509       O  
ATOM   1107  N   ALA A 326      13.522   2.841  -0.068  1.00 43.73           N  
ANISOU 1107  N   ALA A 326     6243   4578   5794   1168  -2273   -430       N  
ATOM   1108  CA  ALA A 326      14.574   1.833   0.000  1.00 44.62           C  
ANISOU 1108  CA  ALA A 326     5795   5203   5955   1234  -2309   -109       C  
ATOM   1109  C   ALA A 326      14.380   0.844  -1.143  1.00 48.97           C  
ANISOU 1109  C   ALA A 326     6538   5534   6534   1083  -1565   -716       C  
ATOM   1110  O   ALA A 326      13.257   0.395  -1.391  1.00 50.18           O  
ANISOU 1110  O   ALA A 326     6940   5414   6710    944  -2145  -1633       O  
ATOM   1111  CB  ALA A 326      14.556   1.110   1.338  1.00 43.11           C  
ANISOU 1111  CB  ALA A 326     5347   4892   6138    536  -1541    -19       C  
ATOM   1112  N   SER A 327      15.453   0.536  -1.865  1.00 44.58           N  
ANISOU 1112  N   SER A 327     6012   5050   5875   1020  -1954    -74       N  
ATOM   1113  CA  SER A 327      15.395  -0.570  -2.818  1.00 46.17           C  
ANISOU 1113  CA  SER A 327     6454   5246   5840   1116  -1800   -170       C  
ATOM   1114  C   SER A 327      15.737  -1.845  -2.057  1.00 43.57           C  
ANISOU 1114  C   SER A 327     5601   4721   6233    499  -1786   -313       C  
ATOM   1115  O   SER A 327      16.774  -1.924  -1.373  1.00 43.14           O  
ANISOU 1115  O   SER A 327     5604   4511   6272   1045  -1716    639       O  
ATOM   1116  CB  SER A 327      16.326  -0.354  -4.013  1.00 48.78           C  
ANISOU 1116  CB  SER A 327     7024   6057   5453    832  -1768   -423       C  
ATOM   1117  OG  SER A 327      17.667  -0.197  -3.602  1.00 54.58           O  
ANISOU 1117  OG  SER A 327     7063   6516   7159   1255  -1740     84       O  
ATOM   1118  N   VAL A 328      14.842  -2.821  -2.134  1.00 36.94           N  
ANISOU 1118  N   VAL A 328     4057   4692   5286    919  -1704   -355       N  
ATOM   1119  CA  VAL A 328      15.070  -4.115  -1.487  1.00 39.17           C  
ANISOU 1119  CA  VAL A 328     4827   4627   5427    594  -1450   -237       C  
ATOM   1120  C   VAL A 328      15.372  -5.135  -2.579  1.00 39.50           C  
ANISOU 1120  C   VAL A 328     4652   4674   5680    758  -1597   -365       C  
ATOM   1121  O   VAL A 328      14.593  -5.277  -3.528  1.00 40.60           O  
ANISOU 1121  O   VAL A 328     4719   5254   5451   1340  -1745    -62       O  
ATOM   1122  CB  VAL A 328      13.854  -4.544  -0.625  1.00 41.63           C  
ANISOU 1122  CB  VAL A 328     5117   5062   5637    913  -1310   -203       C  
ATOM   1123  CG1 VAL A 328      14.119  -5.868   0.082  1.00 39.71           C  
ANISOU 1123  CG1 VAL A 328     5298   4536   5252    578  -1173   -561       C  
ATOM   1124  CG2 VAL A 328      13.527  -3.458   0.401  1.00 42.62           C  
ANISOU 1124  CG2 VAL A 328     4958   5193   6042   1558   -983   -173       C  
ATOM   1125  N   GLU A 329      16.510  -5.820  -2.446  1.00 37.32           N  
ANISOU 1125  N   GLU A 329     4337   4702   5138    479  -1662   -103       N  
ATOM   1126  CA  GLU A 329      16.961  -6.838  -3.413  1.00 39.44           C  
ANISOU 1126  CA  GLU A 329     4554   4724   5705    780  -1216   -195       C  
ATOM   1127  C   GLU A 329      17.500  -8.093  -2.711  1.00 36.88           C  
ANISOU 1127  C   GLU A 329     4396   4464   5151    266  -1192   -269       C  
ATOM   1128  O   GLU A 329      17.940  -8.021  -1.568  1.00 35.03           O  
ANISOU 1128  O   GLU A 329     3996   4197   5115    169  -1173   -135       O  
ATOM   1129  CB  GLU A 329      18.072  -6.267  -4.296  1.00 42.22           C  
ANISOU 1129  CB  GLU A 329     5316   5009   5715    299  -1047   -274       C  
ATOM   1130  CG  GLU A 329      17.634  -5.159  -5.231  1.00 54.81           C  
ANISOU 1130  CG  GLU A 329     7884   5977   6963    548  -1520    583       C  
ATOM   1131  CD  GLU A 329      18.779  -4.650  -6.075  1.00 65.60           C  
ANISOU 1131  CD  GLU A 329     8154   8145   8626   -217   -774    -63       C  
ATOM   1132  OE1 GLU A 329      19.227  -3.514  -5.818  1.00 65.13           O  
ANISOU 1132  OE1 GLU A 329     8422   8258   8065   -109   -850   -741       O  
ATOM   1133  OE2 GLU A 329      19.234  -5.391  -6.979  1.00 69.03           O  
ANISOU 1133  OE2 GLU A 329     8891   8162   9175   -249     -4   -210       O  
ATOM   1134  N   ILE A 330      17.466  -9.230  -3.409  1.00 34.24           N  
ANISOU 1134  N   ILE A 330     3590   4460   4957    431  -1070   -256       N  
ATOM   1135  CA  ILE A 330      18.118 -10.461  -2.957  1.00 33.18           C  
ANISOU 1135  CA  ILE A 330     3530   4085   4989    196  -1046   -374       C  
ATOM   1136  C   ILE A 330      19.590 -10.443  -3.417  1.00 33.67           C  
ANISOU 1136  C   ILE A 330     3565   4313   4912    271  -1029   -283       C  
ATOM   1137  O   ILE A 330      19.873 -10.050  -4.548  1.00 34.53           O  
ANISOU 1137  O   ILE A 330     3935   4313   4871    239   -782   -447       O  
ATOM   1138  CB  ILE A 330      17.415 -11.716  -3.529  1.00 31.93           C  
ANISOU 1138  CB  ILE A 330     3103   4122   4904    276  -1145   -292       C  
ATOM   1139  CG1 ILE A 330      15.889 -11.697  -3.258  1.00 32.82           C  
ANISOU 1139  CG1 ILE A 330     3365   4208   4894    600   -674   -595       C  
ATOM   1140  CG2 ILE A 330      18.082 -13.005  -3.017  1.00 29.39           C  
ANISOU 1140  CG2 ILE A 330     2832   3710   4622    111   -926   -626       C  
ATOM   1141  CD1 ILE A 330      15.477 -11.598  -1.793  1.00 27.52           C  
ANISOU 1141  CD1 ILE A 330     2399   3371   4687    346   -949   -315       C  
HETATM 1142  N   MSE A 331      20.515 -10.853  -2.545  1.00 31.07           N  
ANISOU 1142  N   MSE A 331     3169   3883   4753    283   -750   -446       N  
HETATM 1143  CA  MSE A 331      21.939 -10.969  -2.911  1.00 28.51           C  
ANISOU 1143  CA  MSE A 331     2989   3577   4264   -205   -946   -283       C  
HETATM 1144  C   MSE A 331      22.111 -12.053  -3.955  1.00 30.63           C  
ANISOU 1144  C   MSE A 331     3376   3881   4379     65   -733   -382       C  
HETATM 1145  O   MSE A 331      21.547 -13.144  -3.840  1.00 31.44           O  
ANISOU 1145  O   MSE A 331     3205   4086   4652   -114   -831  -1008       O  
HETATM 1146  CB  MSE A 331      22.798 -11.337  -1.700  1.00 27.64           C  
ANISOU 1146  CB  MSE A 331     2572   3639   4289    -87   -791   -253       C  
HETATM 1147  CG  MSE A 331      22.856 -10.188  -0.707  1.00 33.64           C  
ANISOU 1147  CG  MSE A 331     3850   3845   5085   -162   -424   -649       C  
HETATM 1148 SE   MSE A 331      23.796 -10.647   0.968  1.00 40.89          SE  
ANISOU 1148 SE   MSE A 331     4367   5202   5966   -116   -639   -154      SE  
HETATM 1149  CE  MSE A 331      25.599 -10.737   0.179  1.00 27.90           C  
ANISOU 1149  CE  MSE A 331     3001   3249   4348   -418  -1417   -591       C  
ATOM   1150  N   GLY A 332      22.879 -11.742  -4.988  1.00 31.36           N  
ANISOU 1150  N   GLY A 332     3310   4082   4521     52   -760   -226       N  
ATOM   1151  CA  GLY A 332      23.284 -12.716  -5.986  1.00 31.82           C  
ANISOU 1151  CA  GLY A 332     3251   4090   4749   -213   -754   -396       C  
ATOM   1152  C   GLY A 332      24.780 -12.949  -5.842  1.00 30.09           C  
ANISOU 1152  C   GLY A 332     3244   3909   4276   -273   -702    -98       C  
ATOM   1153  O   GLY A 332      25.416 -12.396  -4.940  1.00 28.57           O  
ANISOU 1153  O   GLY A 332     2848   3910   4095    -15   -554    -67       O  
ATOM   1154  N   TYR A 333      25.341 -13.742  -6.751  1.00 33.82           N  
ANISOU 1154  N   TYR A 333     3736   4448   4665    -11   -381   -201       N  
ATOM   1155  CA  TYR A 333      26.769 -14.076  -6.740  1.00 33.66           C  
ANISOU 1155  CA  TYR A 333     3513   4437   4837   -245   -280    -94       C  
ATOM   1156  C   TYR A 333      27.651 -12.854  -6.524  1.00 34.96           C  
ANISOU 1156  C   TYR A 333     3835   4519   4929   -319   -402   -244       C  
ATOM   1157  O   TYR A 333      28.522 -12.876  -5.647  1.00 34.81           O  
ANISOU 1157  O   TYR A 333     4073   4602   4548    -50   -327    -13       O  
ATOM   1158  CB  TYR A 333      27.183 -14.788  -8.037  1.00 34.73           C  
ANISOU 1158  CB  TYR A 333     3749   4602   4844   -237   -170   -107       C  
ATOM   1159  CG  TYR A 333      28.690 -14.995  -8.153  1.00 33.92           C  
ANISOU 1159  CG  TYR A 333     3606   4730   4551   -403   -337   -389       C  
ATOM   1160  CD1 TYR A 333      29.312 -16.110  -7.565  1.00 34.39           C  
ANISOU 1160  CD1 TYR A 333     3644   4689   4734   -309   -321   -507       C  
ATOM   1161  CD2 TYR A 333      29.499 -14.063  -8.831  1.00 36.84           C  
ANISOU 1161  CD2 TYR A 333     4325   5082   4591   -651   -218   -274       C  
ATOM   1162  CE1 TYR A 333      30.700 -16.301  -7.658  1.00 35.85           C  
ANISOU 1162  CE1 TYR A 333     3695   5066   4860   -337   -193   -532       C  
ATOM   1163  CE2 TYR A 333      30.884 -14.244  -8.929  1.00 42.35           C  
ANISOU 1163  CE2 TYR A 333     4404   5859   5825   -651   -337   -181       C  
ATOM   1164  CZ  TYR A 333      31.472 -15.362  -8.342  1.00 41.56           C  
ANISOU 1164  CZ  TYR A 333     4455   5685   5648   -647    171   -352       C  
ATOM   1165  OH  TYR A 333      32.830 -15.538  -8.433  1.00 43.74           O  
ANISOU 1165  OH  TYR A 333     4643   6317   5656   -203   -360  -1058       O  
ATOM   1166  N   LYS A 334      27.429 -11.798  -7.321  1.00 34.63           N  
ANISOU 1166  N   LYS A 334     3901   4573   4682   -401   -188   -132       N  
ATOM   1167  CA  LYS A 334      28.255 -10.585  -7.230  1.00 34.72           C  
ANISOU 1167  CA  LYS A 334     4247   4421   4521   -426   -384    -83       C  
ATOM   1168  C   LYS A 334      28.231  -9.973  -5.824  1.00 33.54           C  
ANISOU 1168  C   LYS A 334     3822   4416   4503   -489   -475    -92       C  
ATOM   1169  O   LYS A 334      29.236  -9.465  -5.366  1.00 34.21           O  
ANISOU 1169  O   LYS A 334     3648   4626   4721   -620   -344   -120       O  
ATOM   1170  CB  LYS A 334      27.890  -9.543  -8.305  1.00 35.60           C  
ANISOU 1170  CB  LYS A 334     4447   4593   4486   -656   -501     79       C  
ATOM   1171  CG  LYS A 334      26.574  -8.808  -8.102  1.00 43.74           C  
ANISOU 1171  CG  LYS A 334     5216   5445   5955    -97   -290    -40       C  
ATOM   1172  CD  LYS A 334      26.465  -7.604  -9.034  1.00 49.09           C  
ANISOU 1172  CD  LYS A 334     6686   5925   6041   -131   -365    239       C  
ATOM   1173  CE  LYS A 334      25.111  -6.918  -8.927  1.00 52.84           C  
ANISOU 1173  CE  LYS A 334     6919   6364   6793     65   -881    241       C  
ATOM   1174  NZ  LYS A 334      24.797  -6.361  -7.572  1.00 53.84           N  
ANISOU 1174  NZ  LYS A 334     7128   6313   7013    240   -300    305       N  
ATOM   1175  N   ASP A 335      27.087 -10.050  -5.137  1.00 31.93           N  
ANISOU 1175  N   ASP A 335     3603   4316   4213     70   -594     56       N  
ATOM   1176  CA  ASP A 335      26.964  -9.449  -3.804  1.00 31.04           C  
ANISOU 1176  CA  ASP A 335     3448   4000   4344   -259   -687   -102       C  
ATOM   1177  C   ASP A 335      27.633 -10.294  -2.716  1.00 30.87           C  
ANISOU 1177  C   ASP A 335     3416   3981   4329   -291   -573    -89       C  
ATOM   1178  O   ASP A 335      28.295  -9.763  -1.822  1.00 31.39           O  
ANISOU 1178  O   ASP A 335     3614   3747   4565   -578   -627    -23       O  
ATOM   1179  CB  ASP A 335      25.492  -9.177  -3.497  1.00 33.26           C  
ANISOU 1179  CB  ASP A 335     3719   4237   4681      2   -603   -235       C  
ATOM   1180  CG  ASP A 335      24.796  -8.479  -4.656  1.00 34.65           C  
ANISOU 1180  CG  ASP A 335     4015   4191   4957   -155   -944   -195       C  
ATOM   1181  OD1 ASP A 335      25.224  -7.371  -5.026  1.00 37.26           O  
ANISOU 1181  OD1 ASP A 335     4486   4501   5169   -376   -588    290       O  
ATOM   1182  OD2 ASP A 335      23.863  -9.062  -5.228  1.00 33.77           O  
ANISOU 1182  OD2 ASP A 335     3630   4373   4825   -143   -867    -81       O  
ATOM   1183  N   PHE A 336      27.478 -11.613  -2.793  1.00 29.88           N  
ANISOU 1183  N   PHE A 336     3124   3962   4265   -255    -42    191       N  
ATOM   1184  CA  PHE A 336      28.258 -12.512  -1.933  1.00 28.19           C  
ANISOU 1184  CA  PHE A 336     2725   3651   4336   -478   -408    -27       C  
ATOM   1185  C   PHE A 336      29.763 -12.343  -2.127  1.00 30.30           C  
ANISOU 1185  C   PHE A 336     2803   4113   4596   -353   -353   -144       C  
ATOM   1186  O   PHE A 336      30.521 -12.312  -1.151  1.00 30.11           O  
ANISOU 1186  O   PHE A 336     2913   4094   4432   -561   -292    -73       O  
ATOM   1187  CB  PHE A 336      27.859 -13.964  -2.176  1.00 27.60           C  
ANISOU 1187  CB  PHE A 336     2456   3584   4444   -182   -279   -315       C  
ATOM   1188  CG  PHE A 336      26.440 -14.273  -1.778  1.00 25.59           C  
ANISOU 1188  CG  PHE A 336     2341   3269   4112   -150   -434   -225       C  
ATOM   1189  CD1 PHE A 336      26.057 -14.220  -0.440  1.00 27.11           C  
ANISOU 1189  CD1 PHE A 336     2577   3453   4268     10   -191   -140       C  
ATOM   1190  CD2 PHE A 336      25.489 -14.616  -2.738  1.00 25.87           C  
ANISOU 1190  CD2 PHE A 336     2356   3273   4197    -52   -512   -198       C  
ATOM   1191  CE1 PHE A 336      24.737 -14.495  -0.062  1.00 26.88           C  
ANISOU 1191  CE1 PHE A 336     2386   3374   4452   -242   -588   -273       C  
ATOM   1192  CE2 PHE A 336      24.170 -14.899  -2.371  1.00 26.49           C  
ANISOU 1192  CE2 PHE A 336     2501   3375   4188   -217   -354   -201       C  
ATOM   1193  CZ  PHE A 336      23.791 -14.828  -1.032  1.00 25.50           C  
ANISOU 1193  CZ  PHE A 336     2674   2980   4033   -116   -600    -68       C  
ATOM   1194  N   LYS A 337      30.191 -12.240  -3.385  1.00 32.79           N  
ANISOU 1194  N   LYS A 337     3389   4363   4705   -424   -192    170       N  
ATOM   1195  CA  LYS A 337      31.607 -12.018  -3.708  1.00 33.66           C  
ANISOU 1195  CA  LYS A 337     3460   4679   4651   -688   -210   -179       C  
ATOM   1196  C   LYS A 337      32.083 -10.702  -3.106  1.00 31.86           C  
ANISOU 1196  C   LYS A 337     3367   4511   4224   -736   -128    152       C  
ATOM   1197  O   LYS A 337      33.146 -10.645  -2.498  1.00 33.75           O  
ANISOU 1197  O   LYS A 337     3130   4737   4955   -459   -228    158       O  
ATOM   1198  CB  LYS A 337      31.823 -12.052  -5.226  1.00 33.97           C  
ANISOU 1198  CB  LYS A 337     3622   4567   4718   -941      5   -186       C  
ATOM   1199  CG  LYS A 337      33.240 -11.740  -5.684  1.00 37.36           C  
ANISOU 1199  CG  LYS A 337     3598   5038   5557   -790     71    -53       C  
ATOM   1200  CD  LYS A 337      33.519 -12.433  -7.006  1.00 47.91           C  
ANISOU 1200  CD  LYS A 337     5870   6427   5905   -895    384   -628       C  
ATOM   1201  CE  LYS A 337      34.111 -11.504  -8.054  1.00 50.87           C  
ANISOU 1201  CE  LYS A 337     6379   5951   6997  -1338   -283    -73       C  
ATOM   1202  NZ  LYS A 337      35.433 -10.942  -7.687  1.00 48.95           N  
ANISOU 1202  NZ  LYS A 337     4845   7251   6503   -463    613     51       N  
ATOM   1203  N   TYR A 338      31.278  -9.651  -3.242  1.00 34.07           N  
ANISOU 1203  N   TYR A 338     3531   4666   4748   -538    -28    -50       N  
ATOM   1204  CA  TYR A 338      31.664  -8.348  -2.701  1.00 35.66           C  
ANISOU 1204  CA  TYR A 338     4068   4764   4716   -576   -244    -84       C  
ATOM   1205  C   TYR A 338      31.803  -8.378  -1.166  1.00 32.18           C  
ANISOU 1205  C   TYR A 338     3287   4208   4731   -804   -322   -165       C  
ATOM   1206  O   TYR A 338      32.733  -7.806  -0.614  1.00 31.83           O  
ANISOU 1206  O   TYR A 338     3074   4393   4623   -863   -141   -250       O  
ATOM   1207  CB  TYR A 338      30.675  -7.271  -3.138  1.00 36.62           C  
ANISOU 1207  CB  TYR A 338     4402   4635   4875   -672   -355    248       C  
ATOM   1208  CG  TYR A 338      31.032  -5.894  -2.632  1.00 39.32           C  
ANISOU 1208  CG  TYR A 338     4974   4949   5016   -881   -253    -74       C  
ATOM   1209  CD1 TYR A 338      30.588  -5.453  -1.373  1.00 32.98           C  
ANISOU 1209  CD1 TYR A 338     3915   4059   4556   -885   -496    432       C  
ATOM   1210  CD2 TYR A 338      31.810  -5.023  -3.412  1.00 39.21           C  
ANISOU 1210  CD2 TYR A 338     4526   4996   5372  -1026   -215    -83       C  
ATOM   1211  CE1 TYR A 338      30.920  -4.188  -0.899  1.00 37.96           C  
ANISOU 1211  CE1 TYR A 338     4727   4480   5213  -1015   -707     -6       C  
ATOM   1212  CE2 TYR A 338      32.132  -3.752  -2.950  1.00 40.40           C  
ANISOU 1212  CE2 TYR A 338     5017   5015   5316  -1167   -401    117       C  
ATOM   1213  CZ  TYR A 338      31.683  -3.347  -1.701  1.00 41.01           C  
ANISOU 1213  CZ  TYR A 338     4971   5335   5276  -1276   -498    121       C  
ATOM   1214  OH  TYR A 338      31.996  -2.101  -1.236  1.00 47.66           O  
ANISOU 1214  OH  TYR A 338     6453   5129   6527  -1586   -446    411       O  
ATOM   1215  N   CYS A 339      30.872  -9.044  -0.494  1.00 28.84           N  
ANISOU 1215  N   CYS A 339     2919   3843   4197   -431   -476     -4       N  
ATOM   1216  CA  CYS A 339      30.915  -9.182   0.963  1.00 28.62           C  
ANISOU 1216  CA  CYS A 339     2745   3857   4271   -559   -465     47       C  
ATOM   1217  C   CYS A 339      32.119  -9.984   1.444  1.00 27.91           C  
ANISOU 1217  C   CYS A 339     2546   3797   4261   -522   -316    -43       C  
ATOM   1218  O   CYS A 339      32.760  -9.624   2.438  1.00 29.05           O  
ANISOU 1218  O   CYS A 339     2538   3964   4534   -650   -586     75       O  
ATOM   1219  CB  CYS A 339      29.616  -9.801   1.480  1.00 28.09           C  
ANISOU 1219  CB  CYS A 339     2723   3611   4336   -778   -580   -268       C  
ATOM   1220  SG  CYS A 339      28.295  -8.583   1.458  1.00 36.68           S  
ANISOU 1220  SG  CYS A 339     3477   4683   5773   -422   -526   -199       S  
ATOM   1221  N   TRP A 340      32.415 -11.071   0.737  1.00 28.14           N  
ANISOU 1221  N   TRP A 340     2567   3773   4352   -305   -116     -4       N  
ATOM   1222  CA  TRP A 340      33.622 -11.882   1.004  1.00 27.02           C  
ANISOU 1222  CA  TRP A 340     2148   4009   4109   -415   -167    -73       C  
ATOM   1223  C   TRP A 340      34.892 -11.040   0.919  1.00 31.25           C  
ANISOU 1223  C   TRP A 340     2656   4435   4781   -889   -254   -183       C  
ATOM   1224  O   TRP A 340      35.844 -11.215   1.713  1.00 32.16           O  
ANISOU 1224  O   TRP A 340     2494   4862   4860  -1123   -199    162       O  
ATOM   1225  CB  TRP A 340      33.694 -13.036  -0.004  1.00 28.07           C  
ANISOU 1225  CB  TRP A 340     2183   4019   4463   -658     77   -179       C  
ATOM   1226  CG  TRP A 340      34.957 -13.882   0.085  1.00 31.93           C  
ANISOU 1226  CG  TRP A 340     2512   4645   4972   -196   -232   -300       C  
ATOM   1227  CD1 TRP A 340      36.088 -13.749  -0.673  1.00 34.80           C  
ANISOU 1227  CD1 TRP A 340     2900   5359   4961   -210     -9   -305       C  
ATOM   1228  CD2 TRP A 340      35.203 -14.968   0.983  1.00 33.51           C  
ANISOU 1228  CD2 TRP A 340     2790   4716   5226   -274   -256   -231       C  
ATOM   1229  NE1 TRP A 340      37.029 -14.695  -0.307  1.00 33.27           N  
ANISOU 1229  NE1 TRP A 340     2649   4959   5030   -438    -95   -345       N  
ATOM   1230  CE2 TRP A 340      36.513 -15.455   0.708  1.00 32.88           C  
ANISOU 1230  CE2 TRP A 340     2714   4878   4900   -325   -168   -294       C  
ATOM   1231  CE3 TRP A 340      34.451 -15.577   2.009  1.00 35.63           C  
ANISOU 1231  CE3 TRP A 340     2961   5129   5447   -184    -49    -47       C  
ATOM   1232  CZ2 TRP A 340      37.082 -16.532   1.407  1.00 32.59           C  
ANISOU 1232  CZ2 TRP A 340     2531   4820   5031   -342   -270   -368       C  
ATOM   1233  CZ3 TRP A 340      35.020 -16.648   2.708  1.00 33.93           C  
ANISOU 1233  CZ3 TRP A 340     2731   5025   5135    -76    -47   -196       C  
ATOM   1234  CH2 TRP A 340      36.331 -17.110   2.403  1.00 33.13           C  
ANISOU 1234  CH2 TRP A 340     2543   4866   5177   -348    -64   -489       C  
ATOM   1235  N   GLU A 341      34.910 -10.131  -0.053  1.00 34.69           N  
ANISOU 1235  N   GLU A 341     3396   4859   4923   -567      4    -10       N  
ATOM   1236  CA  GLU A 341      36.083  -9.304  -0.287  1.00 39.18           C  
ANISOU 1236  CA  GLU A 341     4026   5285   5576  -1113     38   -180       C  
ATOM   1237  C   GLU A 341      36.197  -8.188   0.736  1.00 37.14           C  
ANISOU 1237  C   GLU A 341     3557   5326   5228   -909   -282     -2       C  
ATOM   1238  O   GLU A 341      37.294  -7.754   1.042  1.00 38.32           O  
ANISOU 1238  O   GLU A 341     3440   5631   5487  -1156   -240    349       O  
ATOM   1239  CB  GLU A 341      36.077  -8.751  -1.717  1.00 40.49           C  
ANISOU 1239  CB  GLU A 341     3878   5871   5634   -951    155     73       C  
ATOM   1240  CG  GLU A 341      36.376  -9.829  -2.757  1.00 44.40           C  
ANISOU 1240  CG  GLU A 341     4555   6184   6129   -903     41   -302       C  
ATOM   1241  CD  GLU A 341      36.002  -9.436  -4.174  1.00 47.17           C  
ANISOU 1241  CD  GLU A 341     4882   6657   6383   -711    -62   -117       C  
ATOM   1242  OE1 GLU A 341      35.437  -8.340  -4.378  1.00 45.81           O  
ANISOU 1242  OE1 GLU A 341     5505   5755   6144  -1262    499    609       O  
ATOM   1243  OE2 GLU A 341      36.266 -10.242  -5.090  1.00 47.73           O  
ANISOU 1243  OE2 GLU A 341     4668   6776   6689   -949    389   -357       O  
ATOM   1244  N   ASN A 342      35.068  -7.748   1.290  1.00 34.16           N  
ANISOU 1244  N   ASN A 342     3530   4674   4775   -751   -436    -20       N  
ATOM   1245  CA  ASN A 342      35.057  -6.508   2.064  1.00 33.26           C  
ANISOU 1245  CA  ASN A 342     3254   4649   4733  -1033   -446     13       C  
ATOM   1246  C   ASN A 342      34.766  -6.636   3.551  1.00 31.96           C  
ANISOU 1246  C   ASN A 342     3111   4358   4673   -834   -501    -39       C  
ATOM   1247  O   ASN A 342      35.121  -5.762   4.318  1.00 32.41           O  
ANISOU 1247  O   ASN A 342     3072   4414   4825  -1277   -458     70       O  
ATOM   1248  CB  ASN A 342      34.103  -5.508   1.411  1.00 36.52           C  
ANISOU 1248  CB  ASN A 342     3821   4569   5485   -897   -445    154       C  
ATOM   1249  CG  ASN A 342      34.653  -4.962   0.115  1.00 42.28           C  
ANISOU 1249  CG  ASN A 342     4986   5663   5416  -1354   -725    397       C  
ATOM   1250  OD1 ASN A 342      35.498  -4.078   0.131  1.00 43.80           O  
ANISOU 1250  OD1 ASN A 342     5205   5747   5688  -1511   -331    843       O  
ATOM   1251  ND2 ASN A 342      34.200  -5.502  -1.011  1.00 40.15           N  
ANISOU 1251  ND2 ASN A 342     5254   4624   5376  -1261   -645    393       N  
ATOM   1252  N   PHE A 343      34.139  -7.727   3.969  1.00 32.33           N  
ANISOU 1252  N   PHE A 343     2950   4489   4844   -794   -378    114       N  
ATOM   1253  CA  PHE A 343      33.689  -7.829   5.358  1.00 31.80           C  
ANISOU 1253  CA  PHE A 343     3039   4293   4748   -717   -432     68       C  
ATOM   1254  C   PHE A 343      34.176  -9.097   6.034  1.00 33.84           C  
ANISOU 1254  C   PHE A 343     3115   4696   5047   -111   -552     38       C  
ATOM   1255  O   PHE A 343      33.749  -9.419   7.150  1.00 32.83           O  
ANISOU 1255  O   PHE A 343     3012   4433   5028   -558   -486   -135       O  
ATOM   1256  CB  PHE A 343      32.148  -7.754   5.405  1.00 32.08           C  
ANISOU 1256  CB  PHE A 343     3110   4223   4854   -181   -672    -63       C  
ATOM   1257  CG  PHE A 343      31.593  -6.557   4.702  1.00 31.91           C  
ANISOU 1257  CG  PHE A 343     3375   4094   4653   -324   -509     15       C  
ATOM   1258  CD1 PHE A 343      31.778  -5.272   5.231  1.00 32.72           C  
ANISOU 1258  CD1 PHE A 343     3573   3943   4913   -604   -424    186       C  
ATOM   1259  CD2 PHE A 343      30.919  -6.698   3.494  1.00 32.39           C  
ANISOU 1259  CD2 PHE A 343     3461   4126   4717   -341   -558     63       C  
ATOM   1260  CE1 PHE A 343      31.267  -4.159   4.566  1.00 33.24           C  
ANISOU 1260  CE1 PHE A 343     4115   4174   4340   -543   -755    124       C  
ATOM   1261  CE2 PHE A 343      30.408  -5.589   2.823  1.00 31.58           C  
ANISOU 1261  CE2 PHE A 343     3799   3750   4448   -584   -288     53       C  
ATOM   1262  CZ  PHE A 343      30.576  -4.321   3.364  1.00 29.88           C  
ANISOU 1262  CZ  PHE A 343     3369   3649   4333   -875   -588    230       C  
ATOM   1263  N   VAL A 344      35.059  -9.823   5.350  1.00 32.85           N  
ANISOU 1263  N   VAL A 344     2781   4726   4971   -394   -234    254       N  
ATOM   1264  CA  VAL A 344      35.554 -11.115   5.837  1.00 30.34           C  
ANISOU 1264  CA  VAL A 344     2396   4209   4920   -489   -276   -228       C  
ATOM   1265  C   VAL A 344      37.082 -11.093   5.876  1.00 33.45           C  
ANISOU 1265  C   VAL A 344     2467   5062   5177   -550   -429    -35       C  
ATOM   1266  O   VAL A 344      37.701 -10.552   4.961  1.00 33.17           O  
ANISOU 1266  O   VAL A 344     2438   4875   5289   -710   -503     57       O  
ATOM   1267  CB  VAL A 344      35.068 -12.261   4.926  1.00 29.20           C  
ANISOU 1267  CB  VAL A 344     2144   4340   4611   -326   -443   -172       C  
ATOM   1268  CG1 VAL A 344      35.628 -13.607   5.377  1.00 29.62           C  
ANISOU 1268  CG1 VAL A 344     2469   4047   4737   -434   -551   -401       C  
ATOM   1269  CG2 VAL A 344      33.529 -12.297   4.867  1.00 27.24           C  
ANISOU 1269  CG2 VAL A 344     2151   3640   4556   -489   -585    -98       C  
ATOM   1270  N   TYR A 345      37.686 -11.678   6.919  1.00 32.24           N  
ANISOU 1270  N   TYR A 345     2561   4615   5070   -682   -450   -129       N  
ATOM   1271  CA  TYR A 345      39.127 -11.971   6.903  1.00 38.45           C  
ANISOU 1271  CA  TYR A 345     2793   5872   5942   -182   -492   -112       C  
ATOM   1272  C   TYR A 345      39.407 -13.103   5.909  1.00 41.65           C  
ANISOU 1272  C   TYR A 345     3415   6049   6359   -300   -190   -301       C  
ATOM   1273  O   TYR A 345      39.637 -14.242   6.304  1.00 44.52           O  
ANISOU 1273  O   TYR A 345     3835   6208   6870    313   -387     69       O  
ATOM   1274  CB  TYR A 345      39.645 -12.338   8.300  1.00 38.68           C  
ANISOU 1274  CB  TYR A 345     2861   5827   6007   -420   -648     40       C  
ATOM   1275  CG  TYR A 345      39.632 -11.193   9.281  1.00 45.99           C  
ANISOU 1275  CG  TYR A 345     4143   6603   6726   -395   -599   -445       C  
ATOM   1276  CD1 TYR A 345      40.510 -10.102   9.132  1.00 46.90           C  
ANISOU 1276  CD1 TYR A 345     3997   6782   7041   -518  -1286   -317       C  
ATOM   1277  CD2 TYR A 345      38.749 -11.194  10.369  1.00 44.74           C  
ANISOU 1277  CD2 TYR A 345     3669   6762   6568   -403   -866   -197       C  
ATOM   1278  CE1 TYR A 345      40.495  -9.049  10.030  1.00 46.90           C  
ANISOU 1278  CE1 TYR A 345     3921   6839   7059   -349  -1144   -269       C  
ATOM   1279  CE2 TYR A 345      38.731 -10.142  11.273  1.00 45.91           C  
ANISOU 1279  CE2 TYR A 345     4072   6499   6873   -148  -1067   -116       C  
ATOM   1280  CZ  TYR A 345      39.605  -9.080  11.099  1.00 48.93           C  
ANISOU 1280  CZ  TYR A 345     4382   7033   7174   -442   -988     87       C  
ATOM   1281  OH  TYR A 345      39.590  -8.038  11.992  1.00 58.33           O  
ANISOU 1281  OH  TYR A 345     6081   8180   7900    392  -2085   -802       O  
ATOM   1282  N   ASN A 346      39.377 -12.773   4.618  1.00 40.47           N  
ANISOU 1282  N   ASN A 346     3182   5928   6265   -421    -72   -212       N  
ATOM   1283  CA  ASN A 346      39.470 -13.765   3.546  1.00 41.75           C  
ANISOU 1283  CA  ASN A 346     3407   6217   6236   -582   -209   -240       C  
ATOM   1284  C   ASN A 346      40.887 -14.278   3.254  1.00 44.57           C  
ANISOU 1284  C   ASN A 346     3545   6617   6772   -360   -246   -582       C  
ATOM   1285  O   ASN A 346      41.057 -15.179   2.437  1.00 43.65           O  
ANISOU 1285  O   ASN A 346     3631   6430   6523   -345    102   -343       O  
ATOM   1286  CB  ASN A 346      38.843 -13.213   2.260  1.00 39.74           C  
ANISOU 1286  CB  ASN A 346     3164   5819   6114   -664    -34   -341       C  
ATOM   1287  CG  ASN A 346      39.446 -11.881   1.834  1.00 41.28           C  
ANISOU 1287  CG  ASN A 346     3473   6293   5918   -799    502    -89       C  
ATOM   1288  OD1 ASN A 346      40.650 -11.769   1.636  1.00 38.60           O  
ANISOU 1288  OD1 ASN A 346     3217   5687   5760   -955    -43   -508       O  
ATOM   1289  ND2 ASN A 346      38.599 -10.864   1.693  1.00 42.11           N  
ANISOU 1289  ND2 ASN A 346     3844   6233   5922   -761    -45    283       N  
ATOM   1290  N   ASP A 347      41.885 -13.669   3.897  1.00 42.68           N  
ANISOU 1290  N   ASP A 347     3232   6335   6649   -377   -112   -299       N  
ATOM   1291  CA  ASP A 347      43.314 -14.015   3.740  1.00 45.53           C  
ANISOU 1291  CA  ASP A 347     3235   7155   6908   -325    -98   -667       C  
ATOM   1292  C   ASP A 347      43.740 -14.110   2.257  1.00 47.93           C  
ANISOU 1292  C   ASP A 347     3713   7570   6927   -521     12   -539       C  
ATOM   1293  O   ASP A 347      44.555 -14.959   1.885  1.00 50.34           O  
ANISOU 1293  O   ASP A 347     3577   8243   7307    -63   -535   -751       O  
ATOM   1294  CB  ASP A 347      43.644 -15.297   4.534  1.00 49.90           C  
ANISOU 1294  CB  ASP A 347     4034   7424   7500   -150     57   -348       C  
ATOM   1295  CG  ASP A 347      45.109 -15.366   4.987  1.00 62.52           C  
ANISOU 1295  CG  ASP A 347     4535   9803   9413   -183   -629   -453       C  
ATOM   1296  OD1 ASP A 347      45.904 -14.439   4.706  1.00 62.75           O  
ANISOU 1296  OD1 ASP A 347     5119   9391   9330    -19   -408   -265       O  
ATOM   1297  OD2 ASP A 347      45.468 -16.368   5.640  1.00 69.86           O  
ANISOU 1297  OD2 ASP A 347     5818   9845  10879     49    645    137       O  
ATOM   1298  N   ASP A 348      43.151 -13.236   1.425  1.00 43.83           N  
ANISOU 1298  N   ASP A 348     3346   6773   6533   -977    -66  -1027       N  
ATOM   1299  CA  ASP A 348      43.432 -13.123  -0.025  1.00 46.28           C  
ANISOU 1299  CA  ASP A 348     3738   7143   6701  -1085    -40   -495       C  
ATOM   1300  C   ASP A 348      42.962 -14.312  -0.878  1.00 44.20           C  
ANISOU 1300  C   ASP A 348     3282   6932   6579  -1014    301   -359       C  
ATOM   1301  O   ASP A 348      43.341 -14.438  -2.045  1.00 49.13           O  
ANISOU 1301  O   ASP A 348     5005   6968   6692  -1116    629   -621       O  
ATOM   1302  CB  ASP A 348      44.926 -12.805  -0.290  1.00 54.10           C  
ANISOU 1302  CB  ASP A 348     3898   8879   7777  -1248    543   -439       C  
ATOM   1303  CG  ASP A 348      45.400 -11.562   0.455  1.00 66.09           C  
ANISOU 1303  CG  ASP A 348     6150   9640   9319  -1847    157   -914       C  
ATOM   1304  OD1 ASP A 348      44.809 -10.477   0.244  1.00 69.19           O  
ANISOU 1304  OD1 ASP A 348     5780  10357  10150  -1789    414    153       O  
ATOM   1305  OD2 ASP A 348      46.363 -11.667   1.253  1.00 71.14           O  
ANISOU 1305  OD2 ASP A 348     6187  10383  10458  -1781   -247   -843       O  
ATOM   1306  N   GLU A 349      42.142 -15.175  -0.286  1.00 38.72           N  
ANISOU 1306  N   GLU A 349     2369   6248   6093   -478    102   -596       N  
ATOM   1307  CA  GLU A 349      41.524 -16.300  -0.990  1.00 40.33           C  
ANISOU 1307  CA  GLU A 349     3212   6115   5997   -198    -63   -706       C  
ATOM   1308  C   GLU A 349      40.300 -15.816  -1.759  1.00 38.17           C  
ANISOU 1308  C   GLU A 349     2851   5981   5670   -310    243   -568       C  
ATOM   1309  O   GLU A 349      39.577 -14.973  -1.243  1.00 35.54           O  
ANISOU 1309  O   GLU A 349     2490   5418   5595   -421    -28   -349       O  
ATOM   1310  CB  GLU A 349      41.125 -17.404   0.013  1.00 41.27           C  
ANISOU 1310  CB  GLU A 349     3442   6175   6063    222    429   -416       C  
ATOM   1311  CG  GLU A 349      42.314 -17.983   0.802  1.00 44.72           C  
ANISOU 1311  CG  GLU A 349     3494   7066   6430    -23   -397   -787       C  
ATOM   1312  CD  GLU A 349      43.352 -18.672  -0.086  1.00 51.93           C  
ANISOU 1312  CD  GLU A 349     4125   8054   7551    155    354   -899       C  
ATOM   1313  OE1 GLU A 349      43.045 -18.993  -1.253  1.00 53.63           O  
ANISOU 1313  OE1 GLU A 349     4196   8711   7467    950    448   -874       O  
ATOM   1314  OE2 GLU A 349      44.487 -18.914   0.373  1.00 53.99           O  
ANISOU 1314  OE2 GLU A 349     4467   7586   8458    231   -132  -1110       O  
ATOM   1315  N   PRO A 350      40.076 -16.327  -2.996  1.00 40.17           N  
ANISOU 1315  N   PRO A 350     3245   6294   5723   -540    235   -537       N  
ATOM   1316  CA  PRO A 350      38.866 -15.939  -3.736  1.00 39.37           C  
ANISOU 1316  CA  PRO A 350     3309   5972   5676   -321    348   -414       C  
ATOM   1317  C   PRO A 350      37.583 -16.477  -3.100  1.00 37.76           C  
ANISOU 1317  C   PRO A 350     3137   5554   5653   -411     12   -382       C  
ATOM   1318  O   PRO A 350      37.618 -17.436  -2.332  1.00 38.43           O  
ANISOU 1318  O   PRO A 350     3016   5796   5789    242    -75   -138       O  
ATOM   1319  CB  PRO A 350      39.077 -16.540  -5.142  1.00 40.02           C  
ANISOU 1319  CB  PRO A 350     3226   6224   5754   -618     71   -662       C  
ATOM   1320  CG  PRO A 350      40.145 -17.574  -4.974  1.00 45.60           C  
ANISOU 1320  CG  PRO A 350     4162   6590   6574   -161     -8   -554       C  
ATOM   1321  CD  PRO A 350      41.013 -17.097  -3.843  1.00 42.93           C  
ANISOU 1321  CD  PRO A 350     3670   6492   6148    -67    338   -562       C  
ATOM   1322  N   PHE A 351      36.462 -15.835  -3.405  1.00 35.60           N  
ANISOU 1322  N   PHE A 351     3206   5181   5137   -469     55   -403       N  
ATOM   1323  CA  PHE A 351      35.169 -16.310  -2.952  1.00 36.17           C  
ANISOU 1323  CA  PHE A 351     3014   5166   5560   -323    144   -459       C  
ATOM   1324  C   PHE A 351      34.881 -17.690  -3.550  1.00 35.64           C  
ANISOU 1324  C   PHE A 351     3030   5252   5259   -260     67   -472       C  
ATOM   1325  O   PHE A 351      35.155 -17.896  -4.727  1.00 36.27           O  
ANISOU 1325  O   PHE A 351     3124   5559   5096   -437   -171   -462       O  
ATOM   1326  CB  PHE A 351      34.080 -15.300  -3.347  1.00 37.45           C  
ANISOU 1326  CB  PHE A 351     3487   5400   5342   -252   -211   -248       C  
ATOM   1327  CG  PHE A 351      32.686 -15.775  -3.056  1.00 37.41           C  
ANISOU 1327  CG  PHE A 351     3614   5180   5417   -463   -177   -282       C  
ATOM   1328  CD1 PHE A 351      32.312 -16.154  -1.758  1.00 36.30           C  
ANISOU 1328  CD1 PHE A 351     3341   4811   5638   -594     99   -102       C  
ATOM   1329  CD2 PHE A 351      31.736 -15.841  -4.076  1.00 35.15           C  
ANISOU 1329  CD2 PHE A 351     3316   4563   5475   -544    -86   -441       C  
ATOM   1330  CE1 PHE A 351      31.014 -16.604  -1.496  1.00 32.31           C  
ANISOU 1330  CE1 PHE A 351     2784   4657   4834    -90   -252   -388       C  
ATOM   1331  CE2 PHE A 351      30.443 -16.286  -3.812  1.00 31.51           C  
ANISOU 1331  CE2 PHE A 351     3029   4392   4548    -97     55   -456       C  
ATOM   1332  CZ  PHE A 351      30.093 -16.671  -2.525  1.00 30.42           C  
ANISOU 1332  CZ  PHE A 351     2736   4241   4580   -278    -79   -265       C  
ATOM   1333  N   LYS A 352      34.381 -18.632  -2.738  1.00 35.40           N  
ANISOU 1333  N   LYS A 352     2917   5102   5430    -47   -360   -113       N  
ATOM   1334  CA  LYS A 352      33.946 -19.944  -3.241  1.00 37.81           C  
ANISOU 1334  CA  LYS A 352     3197   5255   5913   -177   -362   -430       C  
ATOM   1335  C   LYS A 352      32.429 -20.039  -3.156  1.00 37.12           C  
ANISOU 1335  C   LYS A 352     3194   5560   5350    237   -235   -300       C  
ATOM   1336  O   LYS A 352      31.885 -20.256  -2.065  1.00 36.93           O  
ANISOU 1336  O   LYS A 352     3056   5411   5563    136   -159   -172       O  
ATOM   1337  CB  LYS A 352      34.528 -21.143  -2.468  1.00 40.19           C  
ANISOU 1337  CB  LYS A 352     3764   5561   5945    298     78   -230       C  
ATOM   1338  CG  LYS A 352      35.978 -21.047  -2.023  1.00 50.24           C  
ANISOU 1338  CG  LYS A 352     4218   7335   7536   -396   -306   -487       C  
ATOM   1339  CD  LYS A 352      36.979 -20.941  -3.155  1.00 55.03           C  
ANISOU 1339  CD  LYS A 352     5416   7724   7768   -746    302   -498       C  
ATOM   1340  CE  LYS A 352      38.376 -20.781  -2.565  1.00 59.28           C  
ANISOU 1340  CE  LYS A 352     5766   8655   8102    684   -557  -1063       C  
ATOM   1341  NZ  LYS A 352      38.378 -20.017  -1.271  1.00 54.29           N  
ANISOU 1341  NZ  LYS A 352     5411   7498   7718   -285  -1884   -656       N  
ATOM   1342  N   PRO A 353      31.740 -19.886  -4.299  1.00 31.65           N  
ANISOU 1342  N   PRO A 353     2671   4556   4799    -98     50   -409       N  
ATOM   1343  CA  PRO A 353      30.268 -20.019  -4.269  1.00 31.00           C  
ANISOU 1343  CA  PRO A 353     2660   4454   4664   -127   -114   -315       C  
ATOM   1344  C   PRO A 353      29.828 -21.462  -3.946  1.00 32.99           C  
ANISOU 1344  C   PRO A 353     2988   4521   5024   -163    -97   -312       C  
ATOM   1345  O   PRO A 353      30.495 -22.409  -4.353  1.00 33.76           O  
ANISOU 1345  O   PRO A 353     3329   4582   4915   -125   -340   -703       O  
ATOM   1346  CB  PRO A 353      29.849 -19.604  -5.688  1.00 29.79           C  
ANISOU 1346  CB  PRO A 353     2367   4477   4474   -443   -191   -463       C  
ATOM   1347  CG  PRO A 353      31.062 -19.842  -6.541  1.00 32.53           C  
ANISOU 1347  CG  PRO A 353     2984   4883   4492   -212    121   -606       C  
ATOM   1348  CD  PRO A 353      32.240 -19.529  -5.640  1.00 33.28           C  
ANISOU 1348  CD  PRO A 353     2712   5099   4831   -301    122   -422       C  
ATOM   1349  N   TRP A 354      28.746 -21.600  -3.185  1.00 33.23           N  
ANISOU 1349  N   TRP A 354     3040   4743   4840   -134    -92   -377       N  
ATOM   1350  CA  TRP A 354      28.187 -22.900  -2.797  1.00 33.73           C  
ANISOU 1350  CA  TRP A 354     3230   4491   5094    166    -62   -434       C  
ATOM   1351  C   TRP A 354      27.179 -23.396  -3.838  1.00 35.29           C  
ANISOU 1351  C   TRP A 354     3541   4504   5363      0   -300   -351       C  
ATOM   1352  O   TRP A 354      26.560 -22.599  -4.569  1.00 30.53           O  
ANISOU 1352  O   TRP A 354     2660   4190   4747   -153   -346   -786       O  
ATOM   1353  CB  TRP A 354      27.516 -22.810  -1.416  1.00 31.69           C  
ANISOU 1353  CB  TRP A 354     2918   4173   4947    299   -172   -157       C  
ATOM   1354  CG  TRP A 354      26.592 -21.598  -1.254  1.00 30.13           C  
ANISOU 1354  CG  TRP A 354     2720   4011   4716     54    -21   -412       C  
ATOM   1355  CD1 TRP A 354      25.257 -21.531  -1.564  1.00 29.74           C  
ANISOU 1355  CD1 TRP A 354     2794   3869   4634     90   -168   -350       C  
ATOM   1356  CD2 TRP A 354      26.953 -20.308  -0.744  1.00 28.81           C  
ANISOU 1356  CD2 TRP A 354     2402   3782   4760    155   -251   -177       C  
ATOM   1357  NE1 TRP A 354      24.762 -20.264  -1.283  1.00 27.92           N  
ANISOU 1357  NE1 TRP A 354     2528   3741   4336   -153   -298   -555       N  
ATOM   1358  CE2 TRP A 354      25.783 -19.499  -0.776  1.00 26.32           C  
ANISOU 1358  CE2 TRP A 354     2255   3470   4272    -60    -66   -429       C  
ATOM   1359  CE3 TRP A 354      28.161 -19.745  -0.279  1.00 31.74           C  
ANISOU 1359  CE3 TRP A 354     2968   4305   4785   -110   -604   -415       C  
ATOM   1360  CZ2 TRP A 354      25.782 -18.162  -0.354  1.00 24.95           C  
ANISOU 1360  CZ2 TRP A 354     2122   3425   3932     77   -166   -347       C  
ATOM   1361  CZ3 TRP A 354      28.160 -18.414   0.157  1.00 32.29           C  
ANISOU 1361  CZ3 TRP A 354     3056   4300   4912    215   -634   -249       C  
ATOM   1362  CH2 TRP A 354      26.967 -17.635   0.120  1.00 29.17           C  
ANISOU 1362  CH2 TRP A 354     2400   4206   4474   -200   -420   -398       C  
ATOM   1363  N   LYS A 355      27.011 -24.712  -3.903  1.00 32.22           N  
ANISOU 1363  N   LYS A 355     2698   4309   5233    271    -60   -472       N  
ATOM   1364  CA  LYS A 355      26.053 -25.294  -4.823  1.00 34.09           C  
ANISOU 1364  CA  LYS A 355     3220   4707   5025     43   -140   -564       C  
ATOM   1365  C   LYS A 355      24.648 -24.810  -4.443  1.00 32.34           C  
ANISOU 1365  C   LYS A 355     3320   4144   4823    -24    -28   -496       C  
ATOM   1366  O   LYS A 355      24.308 -24.735  -3.264  1.00 30.51           O  
ANISOU 1366  O   LYS A 355     2870   3797   4925    -27    131   -418       O  
ATOM   1367  CB  LYS A 355      26.135 -26.821  -4.807  1.00 39.03           C  
ANISOU 1367  CB  LYS A 355     4373   4760   5695   -150   -344   -545       C  
ATOM   1368  CG  LYS A 355      25.168 -27.492  -5.781  1.00 38.09           C  
ANISOU 1368  CG  LYS A 355     3691   4948   5831    -30    140   -931       C  
ATOM   1369  CD  LYS A 355      25.206 -29.004  -5.654  1.00 39.84           C  
ANISOU 1369  CD  LYS A 355     4124   4956   6057   -488    164   -741       C  
ATOM   1370  CE  LYS A 355      24.213 -29.649  -6.612  1.00 40.75           C  
ANISOU 1370  CE  LYS A 355     4866   4849   5767    -23   -169   -972       C  
ATOM   1371  NZ  LYS A 355      24.606 -29.393  -8.024  1.00 43.39           N  
ANISOU 1371  NZ  LYS A 355     5085   5261   6138    125    535   -917       N  
ATOM   1372  N   GLY A 356      23.860 -24.440  -5.445  1.00 31.35           N  
ANISOU 1372  N   GLY A 356     3028   4015   4868    -89   -318   -953       N  
ATOM   1373  CA  GLY A 356      22.514 -23.942  -5.209  1.00 32.96           C  
ANISOU 1373  CA  GLY A 356     3135   4233   5154   -108    279   -646       C  
ATOM   1374  C   GLY A 356      22.409 -22.432  -5.068  1.00 33.36           C  
ANISOU 1374  C   GLY A 356     3141   4291   5242   -189    -48   -753       C  
ATOM   1375  O   GLY A 356      21.294 -21.905  -5.043  1.00 31.45           O  
ANISOU 1375  O   GLY A 356     2843   4169   4938   -389   -359   -590       O  
ATOM   1376  N   LEU A 357      23.549 -21.727  -5.010  1.00 31.92           N  
ANISOU 1376  N   LEU A 357     3096   4090   4939   -143   -332   -633       N  
ATOM   1377  CA  LEU A 357      23.543 -20.267  -4.814  1.00 28.82           C  
ANISOU 1377  CA  LEU A 357     2579   4021   4349   -300   -377   -595       C  
ATOM   1378  C   LEU A 357      22.620 -19.534  -5.792  1.00 29.95           C  
ANISOU 1378  C   LEU A 357     2843   4094   4441   -280   -433   -486       C  
ATOM   1379  O   LEU A 357      21.795 -18.706  -5.361  1.00 32.00           O  
ANISOU 1379  O   LEU A 357     3104   4103   4949   -250   -481   -721       O  
ATOM   1380  CB  LEU A 357      24.970 -19.688  -4.884  1.00 29.36           C  
ANISOU 1380  CB  LEU A 357     2757   3892   4505   -474   -426   -397       C  
ATOM   1381  CG  LEU A 357      25.204 -18.228  -4.466  1.00 28.13           C  
ANISOU 1381  CG  LEU A 357     2528   3837   4322   -258   -671   -392       C  
ATOM   1382  CD1 LEU A 357      26.670 -18.042  -4.086  1.00 26.83           C  
ANISOU 1382  CD1 LEU A 357     2326   3524   4344    -88   -441   -335       C  
ATOM   1383  CD2 LEU A 357      24.862 -17.258  -5.589  1.00 27.41           C  
ANISOU 1383  CD2 LEU A 357     2512   3664   4237    -90   -574   -432       C  
ATOM   1384  N   LYS A 358      22.753 -19.832  -7.089  1.00 27.24           N  
ANISOU 1384  N   LYS A 358     2323   3593   4430   -566   -555   -559       N  
ATOM   1385  CA  LYS A 358      21.935 -19.162  -8.106  1.00 30.89           C  
ANISOU 1385  CA  LYS A 358     3051   4254   4429   -325   -659   -401       C  
ATOM   1386  C   LYS A 358      20.464 -19.602  -8.066  1.00 30.10           C  
ANISOU 1386  C   LYS A 358     3039   4076   4320   -271   -563   -738       C  
ATOM   1387  O   LYS A 358      19.557 -18.754  -8.140  1.00 31.32           O  
ANISOU 1387  O   LYS A 358     2749   4496   4652   -319   -679   -428       O  
ATOM   1388  CB  LYS A 358      22.521 -19.342  -9.507  1.00 33.63           C  
ANISOU 1388  CB  LYS A 358     3791   4366   4618   -241   -239   -422       C  
ATOM   1389  CG  LYS A 358      21.789 -18.546 -10.599  1.00 35.42           C  
ANISOU 1389  CG  LYS A 358     3457   4921   5077   -213   -845   -674       C  
ATOM   1390  CD  LYS A 358      22.639 -18.343 -11.858  1.00 47.38           C  
ANISOU 1390  CD  LYS A 358     5671   6499   5832   -542    108   -234       C  
ATOM   1391  CE  LYS A 358      23.144 -19.664 -12.432  1.00 53.00           C  
ANISOU 1391  CE  LYS A 358     6205   6906   7026   -154     -2   -693       C  
ATOM   1392  NZ  LYS A 358      23.841 -19.557 -13.744  1.00 52.46           N  
ANISOU 1392  NZ  LYS A 358     6668   6455   6809   -461   -127   -514       N  
ATOM   1393  N   TYR A 359      20.227 -20.907  -7.943  1.00 30.97           N  
ANISOU 1393  N   TYR A 359     3063   4207   4496   -412   -478   -385       N  
ATOM   1394  CA  TYR A 359      18.847 -21.407  -7.849  1.00 31.17           C  
ANISOU 1394  CA  TYR A 359     3016   4110   4714   -256   -587   -681       C  
ATOM   1395  C   TYR A 359      18.146 -20.770  -6.647  1.00 32.32           C  
ANISOU 1395  C   TYR A 359     3041   4568   4671     -9   -719   -732       C  
ATOM   1396  O   TYR A 359      16.989 -20.371  -6.749  1.00 32.22           O  
ANISOU 1396  O   TYR A 359     2893   4226   5122   -311   -899  -1024       O  
ATOM   1397  CB  TYR A 359      18.806 -22.927  -7.732  1.00 28.43           C  
ANISOU 1397  CB  TYR A 359     2429   4003   4368   -338   -848   -724       C  
ATOM   1398  CG  TYR A 359      18.974 -23.694  -9.033  1.00 32.22           C  
ANISOU 1398  CG  TYR A 359     3350   4304   4589   -377   -592   -892       C  
ATOM   1399  CD1 TYR A 359      18.326 -23.288 -10.212  1.00 30.58           C  
ANISOU 1399  CD1 TYR A 359     2750   4261   4606    -83   -347   -788       C  
ATOM   1400  CD2 TYR A 359      19.757 -24.861  -9.078  1.00 34.52           C  
ANISOU 1400  CD2 TYR A 359     3504   4673   4939    -24   -116  -1002       C  
ATOM   1401  CE1 TYR A 359      18.456 -24.018 -11.401  1.00 32.15           C  
ANISOU 1401  CE1 TYR A 359     3233   4403   4576   -384   -810   -874       C  
ATOM   1402  CE2 TYR A 359      19.883 -25.598 -10.256  1.00 31.33           C  
ANISOU 1402  CE2 TYR A 359     2927   4382   4593   -593   -372   -757       C  
ATOM   1403  CZ  TYR A 359      19.234 -25.169 -11.411  1.00 31.67           C  
ANISOU 1403  CZ  TYR A 359     3057   4382   4594   -423   -266   -685       C  
ATOM   1404  OH  TYR A 359      19.354 -25.907 -12.559  1.00 33.39           O  
ANISOU 1404  OH  TYR A 359     3077   5054   4554   -852   -321   -720       O  
ATOM   1405  N   ASN A 360      18.863 -20.648  -5.527  1.00 28.68           N  
ANISOU 1405  N   ASN A 360     2455   3905   4535   -237   -504   -667       N  
ATOM   1406  CA  ASN A 360      18.315 -20.013  -4.329  1.00 30.00           C  
ANISOU 1406  CA  ASN A 360     2771   4096   4530   -125   -550   -759       C  
ATOM   1407  C   ASN A 360      17.969 -18.554  -4.568  1.00 32.97           C  
ANISOU 1407  C   ASN A 360     3153   4306   5066     50   -451   -612       C  
ATOM   1408  O   ASN A 360      16.862 -18.105  -4.220  1.00 30.89           O  
ANISOU 1408  O   ASN A 360     2649   4266   4821   -320   -661   -775       O  
ATOM   1409  CB  ASN A 360      19.271 -20.156  -3.151  1.00 28.98           C  
ANISOU 1409  CB  ASN A 360     2324   4060   4624   -477   -413   -605       C  
ATOM   1410  CG  ASN A 360      19.424 -21.599  -2.701  1.00 33.31           C  
ANISOU 1410  CG  ASN A 360     3206   4185   5263   -247   -652   -710       C  
ATOM   1411  OD1 ASN A 360      18.601 -22.453  -3.042  1.00 31.68           O  
ANISOU 1411  OD1 ASN A 360     2578   4269   5187   -269   -377   -682       O  
ATOM   1412  ND2 ASN A 360      20.477 -21.880  -1.944  1.00 31.16           N  
ANISOU 1412  ND2 ASN A 360     2750   4077   5009   -250   -346   -598       N  
ATOM   1413  N   PHE A 361      18.899 -17.834  -5.201  1.00 31.06           N  
ANISOU 1413  N   PHE A 361     2802   4210   4788    -12   -704   -616       N  
ATOM   1414  CA  PHE A 361      18.646 -16.466  -5.620  1.00 33.22           C  
ANISOU 1414  CA  PHE A 361     3288   4336   4996      0   -603   -441       C  
ATOM   1415  C   PHE A 361      17.343 -16.360  -6.427  1.00 37.32           C  
ANISOU 1415  C   PHE A 361     3670   4989   5518     68  -1085   -680       C  
ATOM   1416  O   PHE A 361      16.511 -15.469  -6.167  1.00 34.86           O  
ANISOU 1416  O   PHE A 361     3117   4861   5264   -219  -1074   -829       O  
ATOM   1417  CB  PHE A 361      19.816 -15.896  -6.440  1.00 32.31           C  
ANISOU 1417  CB  PHE A 361     3300   4091   4884   -181   -678   -516       C  
ATOM   1418  CG  PHE A 361      19.465 -14.625  -7.154  1.00 33.67           C  
ANISOU 1418  CG  PHE A 361     3367   4452   4973     71   -741   -276       C  
ATOM   1419  CD1 PHE A 361      19.538 -13.401  -6.483  1.00 37.48           C  
ANISOU 1419  CD1 PHE A 361     4080   4779   5380    -15   -579   -662       C  
ATOM   1420  CD2 PHE A 361      18.995 -14.643  -8.476  1.00 37.85           C  
ANISOU 1420  CD2 PHE A 361     4511   4832   5037    149   -915   -512       C  
ATOM   1421  CE1 PHE A 361      19.178 -12.213  -7.127  1.00 42.79           C  
ANISOU 1421  CE1 PHE A 361     5605   5178   5474    212  -1052   -505       C  
ATOM   1422  CE2 PHE A 361      18.633 -13.459  -9.125  1.00 37.78           C  
ANISOU 1422  CE2 PHE A 361     3758   5067   5527    277  -1261   -460       C  
ATOM   1423  CZ  PHE A 361      18.725 -12.243  -8.443  1.00 39.41           C  
ANISOU 1423  CZ  PHE A 361     4065   5045   5864    147  -1309   -357       C  
ATOM   1424  N   LEU A 362      17.175 -17.255  -7.406  1.00 38.90           N  
ANISOU 1424  N   LEU A 362     3986   5177   5618     95   -959   -865       N  
ATOM   1425  CA  LEU A 362      16.014 -17.202  -8.309  1.00 38.66           C  
ANISOU 1425  CA  LEU A 362     3944   5295   5449    -33   -860   -811       C  
ATOM   1426  C   LEU A 362      14.703 -17.428  -7.565  1.00 35.98           C  
ANISOU 1426  C   LEU A 362     3469   4877   5323   -181  -1198   -934       C  
ATOM   1427  O   LEU A 362      13.727 -16.703  -7.785  1.00 39.57           O  
ANISOU 1427  O   LEU A 362     3889   5501   5643    139  -1362   -884       O  
ATOM   1428  CB  LEU A 362      16.168 -18.169  -9.497  1.00 39.09           C  
ANISOU 1428  CB  LEU A 362     4479   5102   5271    -26  -1020   -747       C  
ATOM   1429  CG  LEU A 362      17.299 -17.843 -10.496  1.00 40.59           C  
ANISOU 1429  CG  LEU A 362     4447   5420   5551   -102   -926   -714       C  
ATOM   1430  CD1 LEU A 362      17.589 -19.029 -11.417  1.00 39.43           C  
ANISOU 1430  CD1 LEU A 362     4262   5521   5197    -66  -1295   -739       C  
ATOM   1431  CD2 LEU A 362      17.018 -16.582 -11.315  1.00 41.13           C  
ANISOU 1431  CD2 LEU A 362     4866   5390   5369     91  -1369   -934       C  
ATOM   1432  N   PHE A 363      14.700 -18.399  -6.658  1.00 34.94           N  
ANISOU 1432  N   PHE A 363     3023   4905   5345     75  -1132   -899       N  
ATOM   1433  CA  PHE A 363      13.535 -18.643  -5.818  1.00 40.00           C  
ANISOU 1433  CA  PHE A 363     4121   5433   5643     17   -551   -768       C  
ATOM   1434  C   PHE A 363      13.177 -17.410  -4.967  1.00 38.16           C  
ANISOU 1434  C   PHE A 363     3456   5321   5719     99  -1419   -886       C  
ATOM   1435  O   PHE A 363      12.031 -16.956  -4.958  1.00 36.56           O  
ANISOU 1435  O   PHE A 363     2845   5375   5671   -343  -1301   -639       O  
ATOM   1436  CB  PHE A 363      13.743 -19.863  -4.915  1.00 36.77           C  
ANISOU 1436  CB  PHE A 363     3358   4907   5705     31   -935  -1073       C  
ATOM   1437  CG  PHE A 363      12.595 -20.099  -3.978  1.00 41.77           C  
ANISOU 1437  CG  PHE A 363     3720   5788   6362    -41   -547   -968       C  
ATOM   1438  CD1 PHE A 363      11.470 -20.822  -4.398  1.00 43.97           C  
ANISOU 1438  CD1 PHE A 363     3876   6087   6744   -253   -938   -678       C  
ATOM   1439  CD2 PHE A 363      12.605 -19.558  -2.688  1.00 42.25           C  
ANISOU 1439  CD2 PHE A 363     3985   5677   6390   -120   -863   -857       C  
ATOM   1440  CE1 PHE A 363      10.388 -21.015  -3.542  1.00 45.55           C  
ANISOU 1440  CE1 PHE A 363     3768   6812   6726   -180   -957   -964       C  
ATOM   1441  CE2 PHE A 363      11.521 -19.748  -1.829  1.00 45.66           C  
ANISOU 1441  CE2 PHE A 363     4156   6085   7107   -695   -575   -902       C  
ATOM   1442  CZ  PHE A 363      10.413 -20.477  -2.260  1.00 44.77           C  
ANISOU 1442  CZ  PHE A 363     3591   6464   6955    101   -612   -995       C  
ATOM   1443  N   LEU A 364      14.169 -16.894  -4.253  1.00 33.42           N  
ANISOU 1443  N   LEU A 364     2847   4551   5299     53   -816   -716       N  
ATOM   1444  CA  LEU A 364      13.997 -15.748  -3.345  1.00 32.64           C  
ANISOU 1444  CA  LEU A 364     2625   4550   5225    203  -1122   -723       C  
ATOM   1445  C   LEU A 364      13.587 -14.460  -4.043  1.00 33.84           C  
ANISOU 1445  C   LEU A 364     2997   4689   5169    266  -1350   -750       C  
ATOM   1446  O   LEU A 364      12.724 -13.738  -3.544  1.00 37.28           O  
ANISOU 1446  O   LEU A 364     3494   4769   5900    427  -1060  -1093       O  
ATOM   1447  CB  LEU A 364      15.281 -15.507  -2.533  1.00 31.11           C  
ANISOU 1447  CB  LEU A 364     2614   4177   5029    169  -1047   -777       C  
ATOM   1448  CG  LEU A 364      15.626 -16.604  -1.524  1.00 32.23           C  
ANISOU 1448  CG  LEU A 364     2705   4361   5178    285   -872   -634       C  
ATOM   1449  CD1 LEU A 364      17.055 -16.402  -1.037  1.00 31.19           C  
ANISOU 1449  CD1 LEU A 364     2775   3991   5082    101   -973   -688       C  
ATOM   1450  CD2 LEU A 364      14.638 -16.639  -0.362  1.00 35.92           C  
ANISOU 1450  CD2 LEU A 364     3054   4849   5745   -107   -446   -650       C  
ATOM   1451  N   ASP A 365      14.200 -14.175  -5.189  1.00 34.22           N  
ANISOU 1451  N   ASP A 365     2697   5015   5288     81  -1323   -582       N  
ATOM   1452  CA  ASP A 365      13.798 -13.020  -5.984  1.00 38.76           C  
ANISOU 1452  CA  ASP A 365     3940   4907   5879     99  -1415   -460       C  
ATOM   1453  C   ASP A 365      12.338 -13.113  -6.448  1.00 41.51           C  
ANISOU 1453  C   ASP A 365     4040   5467   6261    487  -1666   -582       C  
ATOM   1454  O   ASP A 365      11.631 -12.112  -6.460  1.00 41.50           O  
ANISOU 1454  O   ASP A 365     3663   5769   6336    626  -1457   -810       O  
ATOM   1455  CB  ASP A 365      14.712 -12.826  -7.189  1.00 40.27           C  
ANISOU 1455  CB  ASP A 365     4099   5486   5716    344  -1335   -682       C  
ATOM   1456  CG  ASP A 365      14.438 -11.531  -7.893  1.00 47.65           C  
ANISOU 1456  CG  ASP A 365     5565   5823   6714    126  -1330   -151       C  
ATOM   1457  OD1 ASP A 365      14.252 -10.514  -7.197  1.00 49.97           O  
ANISOU 1457  OD1 ASP A 365     5761   6341   6884    266  -1730   -407       O  
ATOM   1458  OD2 ASP A 365      14.363 -11.528  -9.128  1.00 52.06           O  
ANISOU 1458  OD2 ASP A 365     6233   6706   6838   -467  -1457   -312       O  
ATOM   1459  N   SER A 366      11.909 -14.319  -6.820  1.00 43.34           N  
ANISOU 1459  N   SER A 366     4207   5953   6307    -16  -1617   -980       N  
ATOM   1460  CA  SER A 366      10.523 -14.579  -7.213  1.00 42.79           C  
ANISOU 1460  CA  SER A 366     3853   6092   6313    893  -1538   -839       C  
ATOM   1461  C   SER A 366       9.579 -14.235  -6.070  1.00 42.19           C  
ANISOU 1461  C   SER A 366     3583   6012   6435    560  -1527   -707       C  
ATOM   1462  O   SER A 366       8.567 -13.559  -6.289  1.00 40.35           O  
ANISOU 1462  O   SER A 366     3837   5486   6007    566  -1790  -1175       O  
ATOM   1463  CB  SER A 366      10.339 -16.036  -7.643  1.00 48.15           C  
ANISOU 1463  CB  SER A 366     4822   6320   7152    519  -1275  -1168       C  
ATOM   1464  OG  SER A 366       9.012 -16.258  -8.054  1.00 59.48           O  
ANISOU 1464  OG  SER A 366     6045   8305   8250   -382  -2282   -744       O  
ATOM   1465  N   LYS A 367       9.927 -14.678  -4.856  1.00 39.63           N  
ANISOU 1465  N   LYS A 367     3193   5664   6198    280  -1612  -1150       N  
ATOM   1466  CA  LYS A 367       9.123 -14.397  -3.669  1.00 40.87           C  
ANISOU 1466  CA  LYS A 367     3757   5601   6171     99  -1414   -959       C  
ATOM   1467  C   LYS A 367       9.081 -12.915  -3.368  1.00 41.55           C  
ANISOU 1467  C   LYS A 367     3658   5688   6440    362  -1342  -1005       C  
ATOM   1468  O   LYS A 367       8.009 -12.367  -3.079  1.00 43.39           O  
ANISOU 1468  O   LYS A 367     3627   5788   7071    491  -1035   -577       O  
ATOM   1469  CB  LYS A 367       9.623 -15.184  -2.451  1.00 41.10           C  
ANISOU 1469  CB  LYS A 367     2884   6166   6565    -84  -2154  -1006       C  
ATOM   1470  CG  LYS A 367       9.205 -16.654  -2.460  1.00 51.39           C  
ANISOU 1470  CG  LYS A 367     4943   6528   8053   -401  -1415   -763       C  
ATOM   1471  CD  LYS A 367       7.683 -16.830  -2.370  1.00 55.43           C  
ANISOU 1471  CD  LYS A 367     4709   8205   8147   -134  -1473   -615       C  
ATOM   1472  CE  LYS A 367       7.290 -18.264  -2.690  1.00 63.85           C  
ANISOU 1472  CE  LYS A 367     6054   8776   9428   -549  -1198  -1117       C  
ATOM   1473  NZ  LYS A 367       5.813 -18.456  -2.710  1.00 69.20           N  
ANISOU 1473  NZ  LYS A 367     6043   9689  10558   -708  -1381  -1148       N  
ATOM   1474  N   LEU A 368      10.241 -12.266  -3.470  1.00 37.25           N  
ANISOU 1474  N   LEU A 368     3255   5165   5732    661  -1307  -1135       N  
ATOM   1475  CA  LEU A 368      10.328 -10.838  -3.198  1.00 37.08           C  
ANISOU 1475  CA  LEU A 368     3288   4971   5827    629  -1426   -627       C  
ATOM   1476  C   LEU A 368       9.429 -10.014  -4.122  1.00 37.03           C  
ANISOU 1476  C   LEU A 368     3221   5207   5638    490  -1796   -898       C  
ATOM   1477  O   LEU A 368       8.706  -9.117  -3.656  1.00 39.66           O  
ANISOU 1477  O   LEU A 368     3262   5685   6119    707  -1655   -753       O  
ATOM   1478  CB  LEU A 368      11.784 -10.349  -3.255  1.00 36.60           C  
ANISOU 1478  CB  LEU A 368     3308   4990   5607    373  -1587   -767       C  
ATOM   1479  CG  LEU A 368      11.960  -8.876  -2.862  1.00 39.89           C  
ANISOU 1479  CG  LEU A 368     4104   5072   5978    451  -1291   -834       C  
ATOM   1480  CD1 LEU A 368      11.461  -8.593  -1.441  1.00 36.35           C  
ANISOU 1480  CD1 LEU A 368     3430   4611   5769    660  -1587   -607       C  
ATOM   1481  CD2 LEU A 368      13.407  -8.433  -3.038  1.00 38.33           C  
ANISOU 1481  CD2 LEU A 368     3665   4854   6041    940  -1339   -854       C  
ATOM   1482  N   GLN A 369       9.466 -10.320  -5.417  1.00 37.53           N  
ANISOU 1482  N   GLN A 369     3010   5499   5749    584  -1585   -997       N  
ATOM   1483  CA  GLN A 369       8.672  -9.576  -6.399  1.00 43.22           C  
ANISOU 1483  CA  GLN A 369     4212   5913   6295    796  -1931   -525       C  
ATOM   1484  C   GLN A 369       7.176  -9.791  -6.205  1.00 44.33           C  
ANISOU 1484  C   GLN A 369     4033   6195   6615   1010  -1994   -645       C  
ATOM   1485  O   GLN A 369       6.403  -8.850  -6.344  1.00 44.76           O  
ANISOU 1485  O   GLN A 369     4296   6109   6601   1026  -1624   -625       O  
ATOM   1486  CB  GLN A 369       9.110  -9.870  -7.845  1.00 46.69           C  
ANISOU 1486  CB  GLN A 369     5142   6352   6246   1143  -1885   -474       C  
ATOM   1487  CG  GLN A 369      10.562  -9.496  -8.189  1.00 50.24           C  
ANISOU 1487  CG  GLN A 369     5152   6848   7088   1097  -1909   -410       C  
ATOM   1488  CD  GLN A 369      11.107  -8.270  -7.445  1.00 56.18           C  
ANISOU 1488  CD  GLN A 369     6292   7437   7616    562  -2352   -405       C  
ATOM   1489  OE1 GLN A 369      10.432  -7.248  -7.315  1.00 64.92           O  
ANISOU 1489  OE1 GLN A 369     7665   8409   8591   1357  -1402   -813       O  
ATOM   1490  NE2 GLN A 369      12.346  -8.369  -6.966  1.00 49.85           N  
ANISOU 1490  NE2 GLN A 369     5884   6931   6123    286  -1680    -64       N  
ATOM   1491  N   GLU A 370       6.779 -11.015  -5.852  1.00 42.80           N  
ANISOU 1491  N   GLU A 370     3846   5897   6516   1115  -1971  -1265       N  
ATOM   1492  CA  GLU A 370       5.393 -11.281  -5.423  1.00 49.78           C  
ANISOU 1492  CA  GLU A 370     4284   7289   7341    461  -1919  -1199       C  
ATOM   1493  C   GLU A 370       5.000 -10.429  -4.212  1.00 50.74           C  
ANISOU 1493  C   GLU A 370     4644   7320   7315   1059  -2319  -1166       C  
ATOM   1494  O   GLU A 370       3.882  -9.940  -4.141  1.00 53.89           O  
ANISOU 1494  O   GLU A 370     4615   7295   8563   1087  -1694   -348       O  
ATOM   1495  CB  GLU A 370       5.183 -12.749  -5.075  1.00 55.48           C  
ANISOU 1495  CB  GLU A 370     5187   7558   8332    206  -1658   -779       C  
ATOM   1496  CG  GLU A 370       5.209 -13.699  -6.255  1.00 67.01           C  
ANISOU 1496  CG  GLU A 370     6967   9659   8833    184  -1795  -1734       C  
ATOM   1497  CD  GLU A 370       4.974 -15.147  -5.857  1.00 77.73           C  
ANISOU 1497  CD  GLU A 370     8560  10016  10956    106  -1535  -1149       C  
ATOM   1498  OE1 GLU A 370       4.730 -15.966  -6.767  1.00 78.54           O  
ANISOU 1498  OE1 GLU A 370     7925  10845  11070    521  -1559  -1690       O  
ATOM   1499  OE2 GLU A 370       5.028 -15.478  -4.648  1.00 73.36           O  
ANISOU 1499  OE2 GLU A 370     8386   9139  10348   -557  -1631  -2119       O  
ATOM   1500  N   ILE A 371       5.925 -10.246  -3.269  1.00 44.95           N  
ANISOU 1500  N   ILE A 371     3992   6206   6878   1029  -1716  -1185       N  
ATOM   1501  CA  ILE A 371       5.646  -9.432  -2.084  1.00 45.12           C  
ANISOU 1501  CA  ILE A 371     3927   6424   6790    976  -1841  -1212       C  
ATOM   1502  C   ILE A 371       5.557  -7.947  -2.444  1.00 48.44           C  
ANISOU 1502  C   ILE A 371     4549   6691   7165   1351  -1660   -663       C  
ATOM   1503  O   ILE A 371       4.637  -7.247  -2.008  1.00 49.76           O  
ANISOU 1503  O   ILE A 371     4473   7025   7409   1495  -1811   -909       O  
ATOM   1504  CB  ILE A 371       6.676  -9.690  -0.957  1.00 41.99           C  
ANISOU 1504  CB  ILE A 371     3695   5726   6531   1378  -1548   -945       C  
ATOM   1505  CG1 ILE A 371       6.429 -11.076  -0.347  1.00 39.76           C  
ANISOU 1505  CG1 ILE A 371     2522   6788   5796   1584  -2027   -824       C  
ATOM   1506  CG2 ILE A 371       6.634  -8.599   0.121  1.00 41.00           C  
ANISOU 1506  CG2 ILE A 371     3288   5757   6533   1374  -1492   -909       C  
ATOM   1507  CD1 ILE A 371       7.615 -11.637   0.424  1.00 33.63           C  
ANISOU 1507  CD1 ILE A 371     2728   5435   4615   2565  -1941   -461       C  
ATOM   1508  N   LEU A 372       6.497  -7.478  -3.256  1.00 43.46           N  
ANISOU 1508  N   LEU A 372     3746   6065   6700   1426  -2011   -965       N  
ATOM   1509  CA  LEU A 372       6.571  -6.054  -3.573  1.00 48.18           C  
ANISOU 1509  CA  LEU A 372     4930   6215   7161   1178  -2156   -914       C  
ATOM   1510  C   LEU A 372       5.524  -5.576  -4.569  1.00 50.35           C  
ANISOU 1510  C   LEU A 372     4990   7050   7088   1694  -2483   -944       C  
ATOM   1511  O   LEU A 372       5.251  -4.375  -4.643  1.00 55.75           O  
ANISOU 1511  O   LEU A 372     6086   7183   7909   1531  -2359  -1147       O  
ATOM   1512  CB  LEU A 372       7.979  -5.669  -4.032  1.00 46.09           C  
ANISOU 1512  CB  LEU A 372     4812   6048   6649   1110  -2001   -801       C  
ATOM   1513  CG  LEU A 372       9.041  -5.823  -2.938  1.00 45.82           C  
ANISOU 1513  CG  LEU A 372     4777   5866   6766    916  -1967   -540       C  
ATOM   1514  CD1 LEU A 372      10.405  -5.382  -3.443  1.00 46.99           C  
ANISOU 1514  CD1 LEU A 372     4862   5723   7269   1340   -981   -825       C  
ATOM   1515  CD2 LEU A 372       8.658  -5.043  -1.681  1.00 48.11           C  
ANISOU 1515  CD2 LEU A 372     4878   6843   6558   1045  -1628   -506       C  
ATOM   1516  N   GLU A 373       4.937  -6.518  -5.306  1.00 53.22           N  
ANISOU 1516  N   GLU A 373     5089   7252   7879   1306  -2056  -1221       N  
ATOM   1517  CA  GLU A 373       4.009  -6.226  -6.397  1.00 59.81           C  
ANISOU 1517  CA  GLU A 373     5918   8502   8304   1716  -2824  -1052       C  
ATOM   1518  C   GLU A 373       2.777  -5.463  -5.908  1.00 66.54           C  
ANISOU 1518  C   GLU A 373     6531   8683  10068   1927  -3044  -1788       C  
ATOM   1519  O   GLU A 373       2.295  -4.561  -6.591  1.00 67.73           O  
ANISOU 1519  O   GLU A 373     6464   9048  10219   2252  -2198   -952       O  
ATOM   1520  CB  GLU A 373       3.590  -7.534  -7.069  1.00 63.20           C  
ANISOU 1520  CB  GLU A 373     6203   8580   9229   1972  -2360  -1513       C  
ATOM   1521  CG  GLU A 373       2.790  -7.394  -8.352  1.00 72.18           C  
ANISOU 1521  CG  GLU A 373     7757  10401   9266   1484  -3027   -963       C  
ATOM   1522  CD  GLU A 373       2.185  -8.714  -8.799  1.00 80.15           C  
ANISOU 1522  CD  GLU A 373     8540  10609  11302   1322  -2519  -1524       C  
ATOM   1523  OE1 GLU A 373       1.059  -8.693  -9.334  1.00 83.30           O  
ANISOU 1523  OE1 GLU A 373     8842  11366  11440   1067  -2945   -497       O  
ATOM   1524  OE2 GLU A 373       2.827  -9.774  -8.612  1.00 79.32           O  
ANISOU 1524  OE2 GLU A 373     7416  10701  12020   1247  -2380  -1686       O  
TER    1525      GLU A 373                                                      
ATOM   1526  N   TYR B -29     -11.187 -32.632 -31.242  1.00 73.46           N  
ANISOU 1526  N   TYR B -29     7863  10107   9941  -3334  -2795  -1419       N  
ATOM   1527  CA  TYR B -29     -10.826 -31.199 -31.458  1.00 81.01           C  
ANISOU 1527  CA  TYR B -29     9667  10337  10777  -2457  -1822    549       C  
ATOM   1528  C   TYR B -29      -9.461 -30.837 -30.863  1.00 77.22           C  
ANISOU 1528  C   TYR B -29     9657   9955   9729  -2173  -1762    663       C  
ATOM   1529  O   TYR B -29      -8.633 -30.219 -31.533  1.00 75.83           O  
ANISOU 1529  O   TYR B -29     9314   9910   9587  -2291  -1904    236       O  
ATOM   1530  CB  TYR B -29     -11.908 -30.271 -30.882  1.00 81.16           C  
ANISOU 1530  CB  TYR B -29     8848  11234  10752  -2286  -1620   1020       C  
ATOM   1531  CG  TYR B -29     -11.561 -28.797 -30.983  1.00 80.05           C  
ANISOU 1531  CG  TYR B -29     8351  11291  10772  -2508  -1800    510       C  
ATOM   1532  CD1 TYR B -29     -11.836 -28.072 -32.149  1.00 80.93           C  
ANISOU 1532  CD1 TYR B -29     8676  11521  10550  -2870  -1916    435       C  
ATOM   1533  CD2 TYR B -29     -10.943 -28.128 -29.915  1.00 81.65           C  
ANISOU 1533  CD2 TYR B -29    10069  11069   9883  -1689  -1793    519       C  
ATOM   1534  CE1 TYR B -29     -11.511 -26.724 -32.250  1.00 83.76           C  
ANISOU 1534  CE1 TYR B -29     9962  11194  10667  -2007  -1721    465       C  
ATOM   1535  CE2 TYR B -29     -10.608 -26.783 -30.006  1.00 79.15           C  
ANISOU 1535  CE2 TYR B -29     8592  11228  10253  -1850  -1250    367       C  
ATOM   1536  CZ  TYR B -29     -10.895 -26.086 -31.172  1.00 83.90           C  
ANISOU 1536  CZ  TYR B -29    10380  11142  10353  -1625  -1472    334       C  
ATOM   1537  OH  TYR B -29     -10.564 -24.753 -31.261  1.00 82.03           O  
ANISOU 1537  OH  TYR B -29    10441  10909   9818  -1768   -528  -1220       O  
ATOM   1538  N   PHE B -28      -9.274 -31.171 -29.588  1.00 69.98           N  
ANISOU 1538  N   PHE B -28     8149   9146   9294  -2314  -1579    -59       N  
ATOM   1539  CA  PHE B -28      -8.022 -30.935 -28.874  1.00 61.60           C  
ANISOU 1539  CA  PHE B -28     7798   7872   7732  -2228   -928    130       C  
ATOM   1540  C   PHE B -28      -7.407 -32.291 -28.549  1.00 60.54           C  
ANISOU 1540  C   PHE B -28     7293   8080   7629  -2233   -743    302       C  
ATOM   1541  O   PHE B -28      -8.044 -33.135 -27.901  1.00 58.48           O  
ANISOU 1541  O   PHE B -28     7124   7268   7826  -2731   -708   -570       O  
ATOM   1542  CB  PHE B -28      -8.280 -30.131 -27.591  1.00 52.71           C  
ANISOU 1542  CB  PHE B -28     5862   7105   7060  -2447  -1394    525       C  
ATOM   1543  CG  PHE B -28      -7.035 -29.582 -26.940  1.00 47.58           C  
ANISOU 1543  CG  PHE B -28     5532   6606   5939  -1830   -895    425       C  
ATOM   1544  CD1 PHE B -28      -6.331 -30.332 -25.997  1.00 48.49           C  
ANISOU 1544  CD1 PHE B -28     5642   6517   6263  -1796   -908    624       C  
ATOM   1545  CD2 PHE B -28      -6.580 -28.300 -27.247  1.00 49.95           C  
ANISOU 1545  CD2 PHE B -28     5898   6460   6619  -1702   -954    583       C  
ATOM   1546  CE1 PHE B -28      -5.187 -29.822 -25.384  1.00 47.91           C  
ANISOU 1546  CE1 PHE B -28     5690   6617   5894  -1736   -773    647       C  
ATOM   1547  CE2 PHE B -28      -5.438 -27.778 -26.638  1.00 51.05           C  
ANISOU 1547  CE2 PHE B -28     5898   6895   6601  -1592   -996    401       C  
ATOM   1548  CZ  PHE B -28      -4.740 -28.540 -25.703  1.00 51.20           C  
ANISOU 1548  CZ  PHE B -28     6564   6546   6343  -1845   -864    579       C  
ATOM   1549  N   GLN B -27      -6.180 -32.499 -29.019  1.00 55.95           N  
ANISOU 1549  N   GLN B -27     6724   6980   7553  -2430  -1237    113       N  
ATOM   1550  CA  GLN B -27      -5.451 -33.738 -28.772  1.00 51.15           C  
ANISOU 1550  CA  GLN B -27     6307   6565   6563  -2583   -946     21       C  
ATOM   1551  C   GLN B -27      -4.710 -33.661 -27.433  1.00 52.20           C  
ANISOU 1551  C   GLN B -27     6933   6542   6358  -2644  -1010    379       C  
ATOM   1552  O   GLN B -27      -3.973 -32.703 -27.174  1.00 50.57           O  
ANISOU 1552  O   GLN B -27     6307   6367   6537  -2347   -487    720       O  
ATOM   1553  CB  GLN B -27      -4.482 -34.022 -29.929  1.00 51.28           C  
ANISOU 1553  CB  GLN B -27     6927   6266   6290  -3031   -621    461       C  
ATOM   1554  CG  GLN B -27      -3.795 -35.385 -29.874  1.00 59.07           C  
ANISOU 1554  CG  GLN B -27     7799   7024   7619  -2131   -543   -111       C  
ATOM   1555  CD  GLN B -27      -4.755 -36.552 -30.065  1.00 63.70           C  
ANISOU 1555  CD  GLN B -27     8461   7743   7996  -2779  -1081     57       C  
ATOM   1556  OE1 GLN B -27      -5.706 -36.471 -30.842  1.00 63.20           O  
ANISOU 1556  OE1 GLN B -27     8478   7503   8031  -2435  -1068   -687       O  
ATOM   1557  NE2 GLN B -27      -4.501 -37.648 -29.357  1.00 64.80           N  
ANISOU 1557  NE2 GLN B -27     9090   8319   7209  -2092    155    304       N  
ATOM   1558  N   GLY B -26      -4.901 -34.675 -26.590  1.00 52.11           N  
ANISOU 1558  N   GLY B -26     6473   6537   6789  -2710   -796    316       N  
ATOM   1559  CA  GLY B -26      -4.361 -34.667 -25.223  1.00 50.23           C  
ANISOU 1559  CA  GLY B -26     6751   6001   6330  -2173   -428    741       C  
ATOM   1560  C   GLY B -26      -5.101 -33.680 -24.334  1.00 49.14           C  
ANISOU 1560  C   GLY B -26     5830   6572   6268  -2240   -570    648       C  
ATOM   1561  O   GLY B -26      -6.239 -33.313 -24.617  1.00 49.32           O  
ANISOU 1561  O   GLY B -26     5652   7142   5944  -2178   -493    876       O  
ATOM   1562  N   SER B -25      -4.444 -33.235 -23.266  1.00 47.91           N  
ANISOU 1562  N   SER B -25     5847   6316   6039  -2357   -280    813       N  
ATOM   1563  CA  SER B -25      -5.064 -32.346 -22.277  1.00 47.53           C  
ANISOU 1563  CA  SER B -25     5118   6389   6549  -2132    -86    744       C  
ATOM   1564  C   SER B -25      -4.362 -31.006 -22.216  1.00 44.51           C  
ANISOU 1564  C   SER B -25     5228   6001   5680  -1660   -410    683       C  
ATOM   1565  O   SER B -25      -3.121 -30.940 -22.279  1.00 43.67           O  
ANISOU 1565  O   SER B -25     5066   5734   5792  -2441   -793    590       O  
ATOM   1566  CB  SER B -25      -5.037 -32.988 -20.886  1.00 54.19           C  
ANISOU 1566  CB  SER B -25     6676   7468   6443  -2275     74    910       C  
ATOM   1567  OG  SER B -25      -5.290 -34.385 -20.955  1.00 61.36           O  
ANISOU 1567  OG  SER B -25     8891   7809   6611  -2817    541    739       O  
ATOM   1568  N   ALA B -24      -5.157 -29.942 -22.089  1.00 42.11           N  
ANISOU 1568  N   ALA B -24     4827   6112   5057  -1687   -266    733       N  
ATOM   1569  CA  ALA B -24      -4.632 -28.593 -21.882  1.00 44.11           C  
ANISOU 1569  CA  ALA B -24     5186   5884   5688  -1480   -674    655       C  
ATOM   1570  C   ALA B -24      -3.981 -28.525 -20.496  1.00 44.28           C  
ANISOU 1570  C   ALA B -24     5138   5833   5850  -1984   -710    838       C  
ATOM   1571  O   ALA B -24      -4.268 -29.370 -19.633  1.00 42.07           O  
ANISOU 1571  O   ALA B -24     4577   5888   5517  -2079   -187    506       O  
ATOM   1572  CB  ALA B -24      -5.746 -27.566 -22.016  1.00 44.90           C  
ANISOU 1572  CB  ALA B -24     4977   6654   5428  -1370   -456    799       C  
HETATM 1573  N   MSE B -23      -3.096 -27.546 -20.289  1.00 38.30           N  
ANISOU 1573  N   MSE B -23     4148   5511   4890  -1378   -359    558       N  
HETATM 1574  CA  MSE B -23      -2.340 -27.440 -19.033  1.00 34.73           C  
ANISOU 1574  CA  MSE B -23     3501   4988   4705  -1129   -146    780       C  
HETATM 1575  C   MSE B -23      -3.019 -26.575 -18.003  1.00 34.22           C  
ANISOU 1575  C   MSE B -23     3421   5000   4579  -1123   -322    718       C  
HETATM 1576  O   MSE B -23      -3.679 -25.587 -18.346  1.00 36.16           O  
ANISOU 1576  O   MSE B -23     3728   4877   5131  -1189   -347    744       O  
HETATM 1577  CB  MSE B -23      -0.943 -26.874 -19.327  1.00 36.59           C  
ANISOU 1577  CB  MSE B -23     3710   4985   5205  -1533   -289    674       C  
HETATM 1578  CG  MSE B -23      -0.076 -27.881 -20.082  1.00 42.97           C  
ANISOU 1578  CG  MSE B -23     4775   5437   6112   -873   -478    244       C  
HETATM 1579 SE   MSE B -23       1.683 -27.097 -20.533  1.00 48.90          SE  
ANISOU 1579 SE   MSE B -23     5598   6139   6842  -1221     28    600      SE  
HETATM 1580  CE  MSE B -23       1.034 -26.008 -22.038  1.00 55.03           C  
ANISOU 1580  CE  MSE B -23     7446   7638   5824  -1017    446   1020       C  
ATOM   1581  N   ASP B -22      -2.872 -26.958 -16.729  1.00 31.68           N  
ANISOU 1581  N   ASP B -22     2727   4824   4485   -989   -258    602       N  
ATOM   1582  CA  ASP B -22      -3.183 -26.082 -15.596  1.00 33.72           C  
ANISOU 1582  CA  ASP B -22     3210   4872   4731   -769   -368    518       C  
ATOM   1583  C   ASP B -22      -2.204 -24.896 -15.642  1.00 33.50           C  
ANISOU 1583  C   ASP B -22     3337   4712   4680   -657   -141    819       C  
ATOM   1584  O   ASP B -22      -1.053 -25.077 -16.058  1.00 33.76           O  
ANISOU 1584  O   ASP B -22     3376   4608   4843   -778    -54    542       O  
ATOM   1585  CB  ASP B -22      -3.069 -26.841 -14.257  1.00 36.10           C  
ANISOU 1585  CB  ASP B -22     3651   5298   4765   -702      2    698       C  
ATOM   1586  CG  ASP B -22      -4.002 -28.072 -14.180  1.00 39.97           C  
ANISOU 1586  CG  ASP B -22     4165   5586   5432   -916   -184   1042       C  
ATOM   1587  OD1 ASP B -22      -5.117 -28.022 -14.731  1.00 41.17           O  
ANISOU 1587  OD1 ASP B -22     3942   5929   5771   -934    -85    461       O  
ATOM   1588  OD2 ASP B -22      -3.626 -29.095 -13.565  1.00 38.58           O  
ANISOU 1588  OD2 ASP B -22     4025   5584   5046   -416    311    995       O  
ATOM   1589  N   PRO B -21      -2.653 -23.681 -15.246  1.00 34.23           N  
ANISOU 1589  N   PRO B -21     3270   4836   4896   -530   -276    634       N  
ATOM   1590  CA  PRO B -21      -1.719 -22.539 -15.347  1.00 33.94           C  
ANISOU 1590  CA  PRO B -21     3349   4724   4822   -538    -43    665       C  
ATOM   1591  C   PRO B -21      -0.388 -22.697 -14.589  1.00 37.94           C  
ANISOU 1591  C   PRO B -21     3813   5572   5030   -558   -403    637       C  
ATOM   1592  O   PRO B -21       0.663 -22.338 -15.163  1.00 36.53           O  
ANISOU 1592  O   PRO B -21     3773   5255   4849   -391   -303    660       O  
ATOM   1593  CB  PRO B -21      -2.528 -21.352 -14.812  1.00 35.40           C  
ANISOU 1593  CB  PRO B -21     3409   5238   4802   -335     70    481       C  
ATOM   1594  CG  PRO B -21      -3.951 -21.744 -15.018  1.00 38.72           C  
ANISOU 1594  CG  PRO B -21     3792   5292   5626   -494   -829    239       C  
ATOM   1595  CD  PRO B -21      -4.030 -23.244 -14.926  1.00 34.70           C  
ANISOU 1595  CD  PRO B -21     3162   5227   4796   -705     55    860       C  
ATOM   1596  N   PRO B -20      -0.409 -23.229 -13.333  1.00 36.87           N  
ANISOU 1596  N   PRO B -20     3822   5192   4994   -641   -303    661       N  
ATOM   1597  CA  PRO B -20       0.902 -23.353 -12.684  1.00 36.36           C  
ANISOU 1597  CA  PRO B -20     3578   5314   4921   -200    -29    639       C  
ATOM   1598  C   PRO B -20       1.811 -24.397 -13.334  1.00 34.08           C  
ANISOU 1598  C   PRO B -20     3800   4815   4330   -491   -172    438       C  
ATOM   1599  O   PRO B -20       3.033 -24.262 -13.274  1.00 35.93           O  
ANISOU 1599  O   PRO B -20     3751   5278   4621   -495   -507    805       O  
ATOM   1600  CB  PRO B -20       0.549 -23.737 -11.234  1.00 38.88           C  
ANISOU 1600  CB  PRO B -20     3759   6067   4946   -152    336    377       C  
ATOM   1601  CG  PRO B -20      -0.856 -23.234 -11.041  1.00 38.03           C  
ANISOU 1601  CG  PRO B -20     3831   5510   5108     26    -37    321       C  
ATOM   1602  CD  PRO B -20      -1.498 -23.509 -12.369  1.00 38.39           C  
ANISOU 1602  CD  PRO B -20     3604   5755   5225   -377   -191    707       C  
ATOM   1603  N   THR B -19       1.225 -25.401 -13.983  1.00 31.93           N  
ANISOU 1603  N   THR B -19     3130   4624   4376   -421     94    592       N  
ATOM   1604  CA  THR B -19       1.996 -26.412 -14.712  1.00 29.53           C  
ANISOU 1604  CA  THR B -19     3195   4252   3772   -465   -118    599       C  
ATOM   1605  C   THR B -19       2.698 -25.785 -15.923  1.00 32.45           C  
ANISOU 1605  C   THR B -19     3598   4476   4256   -550    121    734       C  
ATOM   1606  O   THR B -19       3.878 -26.073 -16.197  1.00 30.69           O  
ANISOU 1606  O   THR B -19     3402   4118   4140   -882     41    619       O  
ATOM   1607  CB  THR B -19       1.097 -27.572 -15.184  1.00 35.80           C  
ANISOU 1607  CB  THR B -19     4047   4800   4755  -1067    179    354       C  
ATOM   1608  OG1 THR B -19       0.325 -28.062 -14.080  1.00 33.63           O  
ANISOU 1608  OG1 THR B -19     3192   4559   5025   -668    119    703       O  
ATOM   1609  CG2 THR B -19       1.930 -28.725 -15.778  1.00 37.52           C  
ANISOU 1609  CG2 THR B -19     3861   4865   5528   -955    -40    153       C  
ATOM   1610  N   PHE B -18       1.973 -24.947 -16.660  1.00 31.17           N  
ANISOU 1610  N   PHE B -18     3621   4093   4126   -601   -154    419       N  
ATOM   1611  CA  PHE B -18       2.583 -24.228 -17.768  1.00 31.82           C  
ANISOU 1611  CA  PHE B -18     3588   4290   4209   -736   -306    531       C  
ATOM   1612  C   PHE B -18       3.733 -23.348 -17.261  1.00 31.29           C  
ANISOU 1612  C   PHE B -18     3488   4045   4355   -596   -193    500       C  
ATOM   1613  O   PHE B -18       4.844 -23.405 -17.780  1.00 31.62           O  
ANISOU 1613  O   PHE B -18     3646   4130   4239   -614    -15    789       O  
ATOM   1614  CB  PHE B -18       1.544 -23.388 -18.525  1.00 31.15           C  
ANISOU 1614  CB  PHE B -18     3399   4214   4222   -621   -163    521       C  
ATOM   1615  CG  PHE B -18       2.155 -22.426 -19.503  1.00 29.93           C  
ANISOU 1615  CG  PHE B -18     3090   4144   4137   -699   -441    535       C  
ATOM   1616  CD1 PHE B -18       2.547 -22.860 -20.773  1.00 32.33           C  
ANISOU 1616  CD1 PHE B -18     3554   4575   4152   -657   -422    572       C  
ATOM   1617  CD2 PHE B -18       2.367 -21.095 -19.150  1.00 32.88           C  
ANISOU 1617  CD2 PHE B -18     3643   4229   4621   -535   -397    411       C  
ATOM   1618  CE1 PHE B -18       3.131 -21.982 -21.673  1.00 34.05           C  
ANISOU 1618  CE1 PHE B -18     3936   4634   4364  -1076   -620    602       C  
ATOM   1619  CE2 PHE B -18       2.959 -20.210 -20.047  1.00 33.98           C  
ANISOU 1619  CE2 PHE B -18     3632   4648   4627   -348   -312    717       C  
ATOM   1620  CZ  PHE B -18       3.332 -20.660 -21.312  1.00 36.28           C  
ANISOU 1620  CZ  PHE B -18     4571   4448   4764   -567    -97    575       C  
ATOM   1621  N   THR B -17       3.459 -22.553 -16.229  1.00 33.00           N  
ANISOU 1621  N   THR B -17     3798   4410   4330   -554   -223    379       N  
ATOM   1622  CA  THR B -17       4.422 -21.569 -15.748  1.00 33.62           C  
ANISOU 1622  CA  THR B -17     3763   4486   4525   -457   -450    252       C  
ATOM   1623  C   THR B -17       5.708 -22.252 -15.273  1.00 33.46           C  
ANISOU 1623  C   THR B -17     3717   4441   4556   -296   -101    269       C  
ATOM   1624  O   THR B -17       6.807 -21.791 -15.577  1.00 34.01           O  
ANISOU 1624  O   THR B -17     4010   4110   4802   -489   -116    294       O  
ATOM   1625  CB  THR B -17       3.793 -20.666 -14.670  1.00 34.33           C  
ANISOU 1625  CB  THR B -17     3690   4580   4773   -387   -447    233       C  
ATOM   1626  OG1 THR B -17       2.623 -20.043 -15.222  1.00 35.05           O  
ANISOU 1626  OG1 THR B -17     3456   4470   5391   -411   -181    344       O  
ATOM   1627  CG2 THR B -17       4.784 -19.568 -14.219  1.00 35.74           C  
ANISOU 1627  CG2 THR B -17     3734   4656   5186   -511   -254     -1       C  
ATOM   1628  N   PHE B -16       5.557 -23.371 -14.569  1.00 32.08           N  
ANISOU 1628  N   PHE B -16     3354   4351   4484   -497    -65    285       N  
ATOM   1629  CA  PHE B -16       6.692 -24.175 -14.106  1.00 32.88           C  
ANISOU 1629  CA  PHE B -16     3815   4408   4268   -228    114    341       C  
ATOM   1630  C   PHE B -16       7.493 -24.789 -15.262  1.00 30.17           C  
ANISOU 1630  C   PHE B -16     3370   4065   4027   -596    -93    403       C  
ATOM   1631  O   PHE B -16       8.720 -24.674 -15.321  1.00 28.80           O  
ANISOU 1631  O   PHE B -16     3236   3846   3858   -447    -10    321       O  
ATOM   1632  CB  PHE B -16       6.197 -25.280 -13.143  1.00 30.60           C  
ANISOU 1632  CB  PHE B -16     3288   4266   4071   -397     -9    190       C  
ATOM   1633  CG  PHE B -16       7.296 -26.124 -12.568  1.00 31.44           C  
ANISOU 1633  CG  PHE B -16     3488   4346   4110   -280    193    278       C  
ATOM   1634  CD1 PHE B -16       8.109 -25.631 -11.543  1.00 31.84           C  
ANISOU 1634  CD1 PHE B -16     3234   4919   3945   -143    118    478       C  
ATOM   1635  CD2 PHE B -16       7.529 -27.416 -13.050  1.00 31.34           C  
ANISOU 1635  CD2 PHE B -16     3266   4339   4302   -387    275    196       C  
ATOM   1636  CE1 PHE B -16       9.126 -26.416 -11.007  1.00 29.26           C  
ANISOU 1636  CE1 PHE B -16     3013   4127   3974    -31    597    293       C  
ATOM   1637  CE2 PHE B -16       8.534 -28.205 -12.514  1.00 31.71           C  
ANISOU 1637  CE2 PHE B -16     3337   4665   4044   -267    333    161       C  
ATOM   1638  CZ  PHE B -16       9.333 -27.702 -11.488  1.00 30.59           C  
ANISOU 1638  CZ  PHE B -16     3110   4442   4070   -108    451   -135       C  
ATOM   1639  N   ASN B -15       6.789 -25.442 -16.177  1.00 28.61           N  
ANISOU 1639  N   ASN B -15     3569   3697   3603   -595    -39    447       N  
ATOM   1640  CA  ASN B -15       7.454 -26.156 -17.260  1.00 28.51           C  
ANISOU 1640  CA  ASN B -15     3330   3591   3910   -552    -19    333       C  
ATOM   1641  C   ASN B -15       7.971 -25.319 -18.411  1.00 28.73           C  
ANISOU 1641  C   ASN B -15     3457   3634   3823   -818    -98    222       C  
ATOM   1642  O   ASN B -15       8.896 -25.748 -19.115  1.00 30.79           O  
ANISOU 1642  O   ASN B -15     3656   4015   4028   -642    -27    119       O  
ATOM   1643  CB  ASN B -15       6.548 -27.257 -17.791  1.00 31.92           C  
ANISOU 1643  CB  ASN B -15     3471   4060   4596   -902   -196    326       C  
ATOM   1644  CG  ASN B -15       6.536 -28.453 -16.881  1.00 32.88           C  
ANISOU 1644  CG  ASN B -15     3820   4155   4516   -830     52    431       C  
ATOM   1645  OD1 ASN B -15       7.456 -29.254 -16.917  1.00 35.43           O  
ANISOU 1645  OD1 ASN B -15     4455   3824   5182   -690   -252    336       O  
ATOM   1646  ND2 ASN B -15       5.502 -28.575 -16.057  1.00 33.85           N  
ANISOU 1646  ND2 ASN B -15     4295   4495   4071   -806     81    432       N  
ATOM   1647  N   PHE B -14       7.395 -24.130 -18.610  1.00 28.97           N  
ANISOU 1647  N   PHE B -14     3369   3779   3857   -737   -386    444       N  
ATOM   1648  CA  PHE B -14       7.849 -23.267 -19.715  1.00 28.57           C  
ANISOU 1648  CA  PHE B -14     3339   3736   3780   -868   -128    237       C  
ATOM   1649  C   PHE B -14       8.729 -22.088 -19.301  1.00 29.46           C  
ANISOU 1649  C   PHE B -14     3327   3816   4050   -835   -131    155       C  
ATOM   1650  O   PHE B -14       9.078 -21.249 -20.133  1.00 30.71           O  
ANISOU 1650  O   PHE B -14     3491   3998   4178  -1028    -62    254       O  
ATOM   1651  CB  PHE B -14       6.672 -22.850 -20.608  1.00 29.92           C  
ANISOU 1651  CB  PHE B -14     3445   3876   4044   -729   -247    321       C  
ATOM   1652  CG  PHE B -14       6.227 -23.962 -21.544  1.00 31.74           C  
ANISOU 1652  CG  PHE B -14     3831   3950   4275   -976   -333    320       C  
ATOM   1653  CD1 PHE B -14       5.439 -25.010 -21.080  1.00 30.61           C  
ANISOU 1653  CD1 PHE B -14     3572   3935   4120   -882   -253    382       C  
ATOM   1654  CD2 PHE B -14       6.665 -23.991 -22.872  1.00 33.84           C  
ANISOU 1654  CD2 PHE B -14     4413   4124   4319  -1001   -154    166       C  
ATOM   1655  CE1 PHE B -14       5.060 -26.056 -21.938  1.00 31.04           C  
ANISOU 1655  CE1 PHE B -14     3941   4109   3741   -597   -295    306       C  
ATOM   1656  CE2 PHE B -14       6.287 -25.018 -23.737  1.00 30.43           C  
ANISOU 1656  CE2 PHE B -14     3597   3882   4082  -1157    264    291       C  
ATOM   1657  CZ  PHE B -14       5.490 -26.060 -23.265  1.00 28.54           C  
ANISOU 1657  CZ  PHE B -14     3653   3491   3696  -1006   -302    387       C  
ATOM   1658  N   ASN B -13       9.100 -22.036 -18.024  1.00 29.55           N  
ANISOU 1658  N   ASN B -13     3418   3832   3976   -762   -183     76       N  
ATOM   1659  CA  ASN B -13      10.060 -21.035 -17.557  1.00 28.52           C  
ANISOU 1659  CA  ASN B -13     3082   3945   3808   -703      2    107       C  
ATOM   1660  C   ASN B -13      11.348 -21.166 -18.374  1.00 29.01           C  
ANISOU 1660  C   ASN B -13     3184   3723   4113   -496     42    140       C  
ATOM   1661  O   ASN B -13      11.806 -22.287 -18.630  1.00 30.01           O  
ANISOU 1661  O   ASN B -13     3311   3820   4271   -395     90   -106       O  
ATOM   1662  CB  ASN B -13      10.350 -21.195 -16.067  1.00 27.09           C  
ANISOU 1662  CB  ASN B -13     2731   3779   3783   -336     31     60       C  
ATOM   1663  CG  ASN B -13      11.313 -20.138 -15.562  1.00 33.93           C  
ANISOU 1663  CG  ASN B -13     3608   4343   4938   -469   -470   -549       C  
ATOM   1664  OD1 ASN B -13      12.518 -20.374 -15.486  1.00 32.16           O  
ANISOU 1664  OD1 ASN B -13     3332   4345   4540   -588    -24   -134       O  
ATOM   1665  ND2 ASN B -13      10.794 -18.949 -15.272  1.00 32.26           N  
ANISOU 1665  ND2 ASN B -13     3593   4056   4608   -346   -542   -150       N  
ATOM   1666  N   ASN B -12      11.895 -20.035 -18.808  1.00 29.12           N  
ANISOU 1666  N   ASN B -12     3126   3698   4238   -745    -47     65       N  
ATOM   1667  CA  ASN B -12      13.012 -20.057 -19.751  1.00 31.49           C  
ANISOU 1667  CA  ASN B -12     3719   3949   4295   -633    180    167       C  
ATOM   1668  C   ASN B -12      14.364 -19.614 -19.193  1.00 33.68           C  
ANISOU 1668  C   ASN B -12     3761   4267   4766   -612     -6     49       C  
ATOM   1669  O   ASN B -12      15.220 -19.133 -19.951  1.00 35.35           O  
ANISOU 1669  O   ASN B -12     4241   4397   4791   -939    254    -61       O  
ATOM   1670  CB  ASN B -12      12.656 -19.318 -21.062  1.00 28.91           C  
ANISOU 1670  CB  ASN B -12     3518   3485   3980   -865     30   -157       C  
ATOM   1671  CG  ASN B -12      12.552 -17.808 -20.906  1.00 29.59           C  
ANISOU 1671  CG  ASN B -12     3579   3441   4221   -942    114    154       C  
ATOM   1672  OD1 ASN B -12      12.463 -17.275 -19.797  1.00 30.80           O  
ANISOU 1672  OD1 ASN B -12     3638   3695   4367   -894   -288    -35       O  
ATOM   1673  ND2 ASN B -12      12.554 -17.102 -22.045  1.00 28.77           N  
ANISOU 1673  ND2 ASN B -12     3256   3439   4234  -1034   -245     90       N  
ATOM   1674  N   GLU B -11      14.572 -19.789 -17.882  1.00 33.10           N  
ANISOU 1674  N   GLU B -11     3622   4337   4618   -592    260   -154       N  
ATOM   1675  CA  GLU B -11      15.947 -19.767 -17.343  1.00 35.08           C  
ANISOU 1675  CA  GLU B -11     3771   4616   4939   -304     51   -243       C  
ATOM   1676  C   GLU B -11      16.746 -20.827 -18.096  1.00 33.35           C  
ANISOU 1676  C   GLU B -11     3597   4136   4938   -678    259   -108       C  
ATOM   1677  O   GLU B -11      16.211 -21.901 -18.373  1.00 30.32           O  
ANISOU 1677  O   GLU B -11     2918   4306   4295   -459     90   -511       O  
ATOM   1678  CB  GLU B -11      15.992 -20.067 -15.833  1.00 35.57           C  
ANISOU 1678  CB  GLU B -11     3996   4530   4987    -20    -49   -104       C  
ATOM   1679  CG  GLU B -11      15.460 -18.951 -14.947  1.00 39.64           C  
ANISOU 1679  CG  GLU B -11     4608   5212   5238   -377   -413   -884       C  
ATOM   1680  CD  GLU B -11      16.216 -17.651 -15.135  1.00 44.72           C  
ANISOU 1680  CD  GLU B -11     4783   5789   6417   -588   -289   -221       C  
ATOM   1681  OE1 GLU B -11      15.554 -16.599 -15.290  1.00 43.54           O  
ANISOU 1681  OE1 GLU B -11     4947   5522   6073   -435   -117   -760       O  
ATOM   1682  OE2 GLU B -11      17.468 -17.697 -15.150  1.00 40.65           O  
ANISOU 1682  OE2 GLU B -11     4464   5226   5754  -1294   -235   -588       O  
ATOM   1683  N   PRO B -10      18.023 -20.540 -18.426  1.00 34.25           N  
ANISOU 1683  N   PRO B -10     3727   4163   5124   -800    454   -186       N  
ATOM   1684  CA  PRO B -10      18.829 -21.509 -19.195  1.00 34.14           C  
ANISOU 1684  CA  PRO B -10     3631   4247   5092   -672    385   -169       C  
ATOM   1685  C   PRO B -10      18.989 -22.845 -18.463  1.00 32.85           C  
ANISOU 1685  C   PRO B -10     3378   4447   4656   -801    257   -148       C  
ATOM   1686  O   PRO B -10      18.999 -23.904 -19.096  1.00 35.60           O  
ANISOU 1686  O   PRO B -10     3950   4623   4951   -242    451   -351       O  
ATOM   1687  CB  PRO B -10      20.184 -20.794 -19.361  1.00 34.54           C  
ANISOU 1687  CB  PRO B -10     3620   4409   5092   -589    846   -147       C  
ATOM   1688  CG  PRO B -10      19.862 -19.349 -19.216  1.00 35.89           C  
ANISOU 1688  CG  PRO B -10     3864   4417   5354   -776    894   -307       C  
ATOM   1689  CD  PRO B -10      18.755 -19.279 -18.194  1.00 30.31           C  
ANISOU 1689  CD  PRO B -10     2949   3931   4635   -464    188    -95       C  
ATOM   1690  N   TRP B  -9      19.083 -22.790 -17.140  1.00 31.27           N  
ANISOU 1690  N   TRP B  -9     3035   4249   4594   -762    374   -308       N  
ATOM   1691  CA  TRP B  -9      19.103 -23.991 -16.305  1.00 33.28           C  
ANISOU 1691  CA  TRP B  -9     3543   4482   4618   -301    402   -175       C  
ATOM   1692  C   TRP B  -9      17.921 -23.962 -15.350  1.00 31.22           C  
ANISOU 1692  C   TRP B  -9     3283   4202   4375   -228    155   -487       C  
ATOM   1693  O   TRP B  -9      17.681 -22.949 -14.696  1.00 28.75           O  
ANISOU 1693  O   TRP B  -9     2697   3854   4374   -544    -68   -429       O  
ATOM   1694  CB  TRP B  -9      20.414 -24.094 -15.502  1.00 35.45           C  
ANISOU 1694  CB  TRP B  -9     3618   5076   4774   -219    295   -514       C  
ATOM   1695  CG  TRP B  -9      21.643 -24.043 -16.360  1.00 35.10           C  
ANISOU 1695  CG  TRP B  -9     3593   5006   4735   -303    163   -512       C  
ATOM   1696  CD1 TRP B  -9      22.267 -25.096 -16.966  1.00 37.40           C  
ANISOU 1696  CD1 TRP B  -9     3944   5237   5026     71    311   -346       C  
ATOM   1697  CD2 TRP B  -9      22.379 -22.875 -16.723  1.00 38.39           C  
ANISOU 1697  CD2 TRP B  -9     4089   5182   5314   -434    266   -217       C  
ATOM   1698  NE1 TRP B  -9      23.356 -24.655 -17.682  1.00 40.48           N  
ANISOU 1698  NE1 TRP B  -9     4377   5533   5469   -393    334   -116       N  
ATOM   1699  CE2 TRP B  -9      23.452 -23.295 -17.545  1.00 40.18           C  
ANISOU 1699  CE2 TRP B  -9     4371   5547   5348   -288    295   -128       C  
ATOM   1700  CE3 TRP B  -9      22.243 -21.510 -16.426  1.00 40.26           C  
ANISOU 1700  CE3 TRP B  -9     4465   5314   5516   -374   -292   -491       C  
ATOM   1701  CZ2 TRP B  -9      24.384 -22.402 -18.078  1.00 42.08           C  
ANISOU 1701  CZ2 TRP B  -9     4106   6035   5848   -663    109    -92       C  
ATOM   1702  CZ3 TRP B  -9      23.172 -20.618 -16.957  1.00 47.25           C  
ANISOU 1702  CZ3 TRP B  -9     4967   6663   6321   -711    446    -85       C  
ATOM   1703  CH2 TRP B  -9      24.229 -21.072 -17.777  1.00 48.96           C  
ANISOU 1703  CH2 TRP B  -9     5241   6341   7020   -472    381   -708       C  
ATOM   1704  N   VAL B  -8      17.174 -25.067 -15.296  1.00 31.24           N  
ANISOU 1704  N   VAL B  -8     3520   4104   4245   -113    357   -256       N  
ATOM   1705  CA  VAL B  -8      16.097 -25.253 -14.328  1.00 30.35           C  
ANISOU 1705  CA  VAL B  -8     3321   4151   4057   -257    250   -375       C  
ATOM   1706  C   VAL B  -8      16.239 -26.615 -13.646  1.00 32.52           C  
ANISOU 1706  C   VAL B  -8     3679   4571   4106   -255    397    -99       C  
ATOM   1707  O   VAL B  -8      16.712 -27.582 -14.267  1.00 35.25           O  
ANISOU 1707  O   VAL B  -8     3476   5011   4907    261    480   -180       O  
ATOM   1708  CB  VAL B  -8      14.676 -25.111 -14.952  1.00 30.69           C  
ANISOU 1708  CB  VAL B  -8     3607   4042   4010    -77    -30   -229       C  
ATOM   1709  CG1 VAL B  -8      14.426 -23.680 -15.431  1.00 27.52           C  
ANISOU 1709  CG1 VAL B  -8     2985   3677   3792   -402    161   -422       C  
ATOM   1710  CG2 VAL B  -8      14.429 -26.134 -16.083  1.00 27.87           C  
ANISOU 1710  CG2 VAL B  -8     2769   3822   3997     28    125   -141       C  
ATOM   1711  N   ARG B  -7      15.836 -26.709 -12.381  1.00 27.61           N  
ANISOU 1711  N   ARG B  -7     2553   4239   3699   -227   -106   -482       N  
ATOM   1712  CA  ARG B  -7      15.839 -28.029 -11.750  1.00 38.52           C  
ANISOU 1712  CA  ARG B  -7     4602   4713   5319    298    416    129       C  
ATOM   1713  C   ARG B  -7      14.436 -28.577 -11.523  1.00 38.84           C  
ANISOU 1713  C   ARG B  -7     4630   5357   4768    324    709    -42       C  
ATOM   1714  O   ARG B  -7      13.454 -27.816 -11.423  1.00 34.97           O  
ANISOU 1714  O   ARG B  -7     4177   4853   4256    -72    128   -526       O  
ATOM   1715  CB  ARG B  -7      16.714 -28.088 -10.490  1.00 47.88           C  
ANISOU 1715  CB  ARG B  -7     5633   6684   5874    241   -172    -68       C  
ATOM   1716  CG  ARG B  -7      16.317 -27.138  -9.387  1.00 55.90           C  
ANISOU 1716  CG  ARG B  -7     6600   7689   6949     40    884   -577       C  
ATOM   1717  CD  ARG B  -7      17.257 -27.244  -8.196  1.00 65.53           C  
ANISOU 1717  CD  ARG B  -7     6735   9824   8339   -528     58   -370       C  
ATOM   1718  NE  ARG B  -7      16.747 -26.456  -7.072  1.00 72.50           N  
ANISOU 1718  NE  ARG B  -7     8365  10176   9006    163    126   -763       N  
ATOM   1719  CZ  ARG B  -7      17.478 -25.949  -6.080  1.00 64.76           C  
ANISOU 1719  CZ  ARG B  -7     7119   8885   8598   1004    254   -383       C  
ATOM   1720  NH1 ARG B  -7      18.798 -26.117  -6.031  1.00 55.11           N  
ANISOU 1720  NH1 ARG B  -7     6847   6646   7443    855    293   -352       N  
ATOM   1721  NH2 ARG B  -7      16.875 -25.257  -5.126  1.00 67.69           N  
ANISOU 1721  NH2 ARG B  -7     8234   8799   8683   1361    383   -333       N  
ATOM   1722  N   GLY B  -6      14.349 -29.903 -11.516  1.00 39.62           N  
ANISOU 1722  N   GLY B  -6     4892   5246   4914    478    633     77       N  
ATOM   1723  CA  GLY B  -6      13.110 -30.606 -11.217  1.00 42.63           C  
ANISOU 1723  CA  GLY B  -6     5158   5763   5274    118    625    456       C  
ATOM   1724  C   GLY B  -6      12.094 -30.643 -12.337  1.00 43.90           C  
ANISOU 1724  C   GLY B  -6     5632   5770   5275   -190    563    105       C  
ATOM   1725  O   GLY B  -6      10.930 -30.931 -12.085  1.00 49.74           O  
ANISOU 1725  O   GLY B  -6     5953   5850   7095    -54   1572     26       O  
ATOM   1726  N   ARG B  -5      12.511 -30.360 -13.572  1.00 38.38           N  
ANISOU 1726  N   ARG B  -5     4769   4722   5090   -386    376   -166       N  
ATOM   1727  CA  ARG B  -5      11.593 -30.459 -14.711  1.00 36.48           C  
ANISOU 1727  CA  ARG B  -5     4411   4731   4716   -385    559    202       C  
ATOM   1728  C   ARG B  -5      11.694 -31.830 -15.384  1.00 42.21           C  
ANISOU 1728  C   ARG B  -5     5612   4899   5525   -711    784    -21       C  
ATOM   1729  O   ARG B  -5      12.281 -31.960 -16.468  1.00 45.97           O  
ANISOU 1729  O   ARG B  -5     5598   6245   5624   -784    648   -608       O  
ATOM   1730  CB  ARG B  -5      11.790 -29.323 -15.724  1.00 32.96           C  
ANISOU 1730  CB  ARG B  -5     3629   4393   4498   -445    501   -170       C  
ATOM   1731  CG  ARG B  -5      10.988 -28.058 -15.428  1.00 31.50           C  
ANISOU 1731  CG  ARG B  -5     3730   4138   4100   -424    -10    -80       C  
ATOM   1732  CD  ARG B  -5      11.565 -27.298 -14.234  1.00 28.55           C  
ANISOU 1732  CD  ARG B  -5     3175   3920   3753   -214    466   -127       C  
ATOM   1733  NE  ARG B  -5      11.005 -25.953 -14.126  1.00 27.70           N  
ANISOU 1733  NE  ARG B  -5     3065   3754   3706   -352    289    118       N  
ATOM   1734  CZ  ARG B  -5      11.339 -25.056 -13.203  1.00 30.42           C  
ANISOU 1734  CZ  ARG B  -5     3414   4075   4066   -115     27   -178       C  
ATOM   1735  NH1 ARG B  -5      12.244 -25.338 -12.272  1.00 29.95           N  
ANISOU 1735  NH1 ARG B  -5     3233   4165   3979    -75    117   -342       N  
ATOM   1736  NH2 ARG B  -5      10.754 -23.866 -13.210  1.00 29.10           N  
ANISOU 1736  NH2 ARG B  -5     2904   3965   4185   -339     34    -93       N  
ATOM   1737  N   HIS B  -4      11.095 -32.839 -14.748  1.00 35.66           N  
ANISOU 1737  N   HIS B  -4     4251   4587   4710   -181    671    -41       N  
ATOM   1738  CA  HIS B  -4      11.218 -34.234 -15.191  1.00 37.54           C  
ANISOU 1738  CA  HIS B  -4     4855   4642   4764   -278    644     98       C  
ATOM   1739  C   HIS B  -4      10.434 -34.582 -16.459  1.00 39.87           C  
ANISOU 1739  C   HIS B  -4     5178   5095   4873   -277    365    213       C  
ATOM   1740  O   HIS B  -4      10.585 -35.671 -16.997  1.00 45.05           O  
ANISOU 1740  O   HIS B  -4     5762   5405   5949   -250    295   -230       O  
ATOM   1741  CB  HIS B  -4      10.794 -35.187 -14.063  1.00 40.49           C  
ANISOU 1741  CB  HIS B  -4     5449   4984   4949     71    938    396       C  
ATOM   1742  CG  HIS B  -4      11.588 -35.026 -12.810  1.00 47.23           C  
ANISOU 1742  CG  HIS B  -4     6283   6122   5539   -233    515    229       C  
ATOM   1743  ND1 HIS B  -4      11.307 -34.060 -11.871  1.00 51.91           N  
ANISOU 1743  ND1 HIS B  -4     6663   6785   6274     92    500   -151       N  
ATOM   1744  CD2 HIS B  -4      12.644 -35.720 -12.330  1.00 55.05           C  
ANISOU 1744  CD2 HIS B  -4     6660   7399   6857    320     70   -153       C  
ATOM   1745  CE1 HIS B  -4      12.163 -34.157 -10.873  1.00 47.94           C  
ANISOU 1745  CE1 HIS B  -4     6106   6407   5700    101    980    271       C  
ATOM   1746  NE2 HIS B  -4      12.984 -35.158 -11.125  1.00 52.35           N  
ANISOU 1746  NE2 HIS B  -4     6736   7021   6134    715    744     49       N  
ATOM   1747  N   GLU B  -3       9.593 -33.666 -16.920  1.00 35.46           N  
ANISOU 1747  N   GLU B  -3     4751   4292   4429   -725    489     -1       N  
ATOM   1748  CA  GLU B  -3       8.703 -33.904 -18.048  1.00 35.95           C  
ANISOU 1748  CA  GLU B  -3     5160   4113   4385   -777    383    222       C  
ATOM   1749  C   GLU B  -3       9.092 -33.018 -19.209  1.00 37.03           C  
ANISOU 1749  C   GLU B  -3     4919   4710   4440   -833    204    418       C  
ATOM   1750  O   GLU B  -3       9.729 -31.977 -19.006  1.00 36.92           O  
ANISOU 1750  O   GLU B  -3     5002   4223   4803   -664    304    280       O  
ATOM   1751  CB  GLU B  -3       7.276 -33.560 -17.632  1.00 47.86           C  
ANISOU 1751  CB  GLU B  -3     5665   6206   6314   -483    866   -367       C  
ATOM   1752  CG  GLU B  -3       6.488 -34.721 -17.078  1.00 60.74           C  
ANISOU 1752  CG  GLU B  -3     8120   6960   7997  -1399    850    655       C  
ATOM   1753  CD  GLU B  -3       5.646 -35.399 -18.144  1.00 72.25           C  
ANISOU 1753  CD  GLU B  -3     9324   8761   9365  -1375     40    -44       C  
ATOM   1754  OE1 GLU B  -3       6.053 -35.435 -19.333  1.00 74.10           O  
ANISOU 1754  OE1 GLU B  -3     9889   9407   8857  -1355   -483   1334       O  
ATOM   1755  OE2 GLU B  -3       4.571 -35.908 -17.783  1.00 80.49           O  
ANISOU 1755  OE2 GLU B  -3     9240   9340  12003  -1211   1004    825       O  
ATOM   1756  N   THR B  -2       8.733 -33.447 -20.420  1.00 34.38           N  
ANISOU 1756  N   THR B  -2     4841   3870   4349   -537    281    264       N  
ATOM   1757  CA  THR B  -2       8.803 -32.584 -21.594  1.00 36.59           C  
ANISOU 1757  CA  THR B  -2     5137   4421   4343  -1016    354    397       C  
ATOM   1758  C   THR B  -2       7.391 -32.360 -22.108  1.00 38.87           C  
ANISOU 1758  C   THR B  -2     5445   4645   4677  -1058    -98    479       C  
ATOM   1759  O   THR B  -2       6.656 -33.320 -22.364  1.00 40.18           O  
ANISOU 1759  O   THR B  -2     6276   4441   4550  -1280    148    499       O  
ATOM   1760  CB  THR B  -2       9.720 -33.154 -22.698  1.00 41.55           C  
ANISOU 1760  CB  THR B  -2     6035   5001   4749   -584    551    128       C  
ATOM   1761  OG1 THR B  -2      11.045 -33.284 -22.180  1.00 44.34           O  
ANISOU 1761  OG1 THR B  -2     6375   4974   5497    -75     39     16       O  
ATOM   1762  CG2 THR B  -2       9.778 -32.211 -23.925  1.00 42.85           C  
ANISOU 1762  CG2 THR B  -2     6170   4929   5181   -725   1067    271       C  
ATOM   1763  N   TYR B  -1       7.008 -31.090 -22.229  1.00 35.60           N  
ANISOU 1763  N   TYR B  -1     4818   4397   4312  -1030   -131   -154       N  
ATOM   1764  CA  TYR B  -1       5.712 -30.734 -22.801  1.00 35.62           C  
ANISOU 1764  CA  TYR B  -1     4688   4363   4482  -1289      1    270       C  
ATOM   1765  C   TYR B  -1       5.911 -30.219 -24.204  1.00 36.63           C  
ANISOU 1765  C   TYR B  -1     5059   4604   4254  -1163   -228    149       C  
ATOM   1766  O   TYR B  -1       6.855 -29.486 -24.511  1.00 40.05           O  
ANISOU 1766  O   TYR B  -1     5789   4912   4513  -1368     95    796       O  
ATOM   1767  CB  TYR B  -1       4.966 -29.681 -21.978  1.00 35.28           C  
ANISOU 1767  CB  TYR B  -1     4578   4462   4363  -1261    -27    250       C  
ATOM   1768  CG  TYR B  -1       4.395 -30.230 -20.695  1.00 36.95           C  
ANISOU 1768  CG  TYR B  -1     4891   4553   4595  -1058     53    565       C  
ATOM   1769  CD1 TYR B  -1       5.195 -30.360 -19.555  1.00 33.84           C  
ANISOU 1769  CD1 TYR B  -1     4638   3726   4492  -1238     89    180       C  
ATOM   1770  CD2 TYR B  -1       3.054 -30.631 -20.619  1.00 40.84           C  
ANISOU 1770  CD2 TYR B  -1     5087   4976   5453  -1410    226    477       C  
ATOM   1771  CE1 TYR B  -1       4.673 -30.876 -18.373  1.00 36.87           C  
ANISOU 1771  CE1 TYR B  -1     4780   4667   4560   -749    379    411       C  
ATOM   1772  CE2 TYR B  -1       2.523 -31.142 -19.440  1.00 40.14           C  
ANISOU 1772  CE2 TYR B  -1     4778   5235   5236  -1467    182    241       C  
ATOM   1773  CZ  TYR B  -1       3.335 -31.268 -18.327  1.00 42.45           C  
ANISOU 1773  CZ  TYR B  -1     4969   5693   5466  -1237     75    465       C  
ATOM   1774  OH  TYR B  -1       2.822 -31.776 -17.159  1.00 45.32           O  
ANISOU 1774  OH  TYR B  -1     5009   6140   6071  -1340    701    607       O  
ATOM   1775  N   LEU B 218       5.026 -30.784 -25.124  1.00 31.45           N  
ANISOU 1775  N   LEU B 218     4399   3547   4004  -1307   -131    591       N  
ATOM   1776  CA  LEU B 218       5.086 -30.493 -26.551  1.00 33.49           C  
ANISOU 1776  CA  LEU B 218     4819   4078   3825  -1620     49    488       C  
ATOM   1777  C   LEU B 218       3.723 -30.064 -27.085  1.00 36.40           C  
ANISOU 1777  C   LEU B 218     5133   4443   4253  -1415   -449    450       C  
ATOM   1778  O   LEU B 218       2.885 -30.902 -27.418  1.00 37.07           O  
ANISOU 1778  O   LEU B 218     5176   4258   4650  -1568   -219   1031       O  
ATOM   1779  CB  LEU B 218       5.595 -31.711 -27.325  1.00 35.02           C  
ANISOU 1779  CB  LEU B 218     4923   4074   4307  -1251    -23    476       C  
ATOM   1780  CG  LEU B 218       5.850 -31.506 -28.820  1.00 41.00           C  
ANISOU 1780  CG  LEU B 218     6095   5207   4276  -1249    -15     55       C  
ATOM   1781  CD1 LEU B 218       6.726 -32.620 -29.373  1.00 43.80           C  
ANISOU 1781  CD1 LEU B 218     6839   5011   4791  -1078    -20    233       C  
ATOM   1782  CD2 LEU B 218       4.537 -31.423 -29.583  1.00 42.34           C  
ANISOU 1782  CD2 LEU B 218     6372   4793   4921  -1338   -439   -400       C  
ATOM   1783  N   CYS B 219       3.509 -28.755 -27.163  1.00 35.40           N  
ANISOU 1783  N   CYS B 219     4827   4346   4277  -1474   -110    275       N  
ATOM   1784  CA  CYS B 219       2.245 -28.212 -27.657  1.00 37.35           C  
ANISOU 1784  CA  CYS B 219     5316   4473   4401  -1375   -650    478       C  
ATOM   1785  C   CYS B 219       2.366 -28.160 -29.168  1.00 38.35           C  
ANISOU 1785  C   CYS B 219     5318   4774   4479  -1546   -698    403       C  
ATOM   1786  O   CYS B 219       3.466 -27.962 -29.692  1.00 36.72           O  
ANISOU 1786  O   CYS B 219     5082   4409   4459  -1686   -567    255       O  
ATOM   1787  CB  CYS B 219       1.997 -26.807 -27.111  1.00 40.31           C  
ANISOU 1787  CB  CYS B 219     5635   4873   4807   -747   -606    338       C  
ATOM   1788  SG  CYS B 219       1.985 -26.662 -25.310  1.00 38.44           S  
ANISOU 1788  SG  CYS B 219     5051   4664   4891  -1126   -162    188       S  
ATOM   1789  N   PHE B 220       1.259 -28.351 -29.881  1.00 35.06           N  
ANISOU 1789  N   PHE B 220     5018   4244   4056  -1674   -505    522       N  
ATOM   1790  CA  PHE B 220       1.315 -28.238 -31.337  1.00 32.46           C  
ANISOU 1790  CA  PHE B 220     4520   3911   3901  -1918   -644    254       C  
ATOM   1791  C   PHE B 220       0.107 -27.580 -31.962  1.00 35.82           C  
ANISOU 1791  C   PHE B 220     5265   4176   4169  -1424   -734    456       C  
ATOM   1792  O   PHE B 220      -0.995 -27.614 -31.395  1.00 37.47           O  
ANISOU 1792  O   PHE B 220     5128   4244   4863  -1636   -679    201       O  
ATOM   1793  CB  PHE B 220       1.536 -29.611 -31.992  1.00 34.93           C  
ANISOU 1793  CB  PHE B 220     4981   4056   4235  -1526   -690    197       C  
ATOM   1794  CG  PHE B 220       0.318 -30.490 -31.987  1.00 37.13           C  
ANISOU 1794  CG  PHE B 220     5396   4366   4344  -1863   -763    120       C  
ATOM   1795  CD1 PHE B 220       0.021 -31.289 -30.879  1.00 39.48           C  
ANISOU 1795  CD1 PHE B 220     5626   4666   4707  -1965   -522    385       C  
ATOM   1796  CD2 PHE B 220      -0.540 -30.530 -33.099  1.00 39.78           C  
ANISOU 1796  CD2 PHE B 220     5635   4933   4547  -1768   -979    -95       C  
ATOM   1797  CE1 PHE B 220      -1.103 -32.104 -30.876  1.00 39.41           C  
ANISOU 1797  CE1 PHE B 220     5668   4571   4733  -1970   -862    439       C  
ATOM   1798  CE2 PHE B 220      -1.670 -31.343 -33.089  1.00 40.55           C  
ANISOU 1798  CE2 PHE B 220     5998   4789   4617  -1988   -639    204       C  
ATOM   1799  CZ  PHE B 220      -1.948 -32.125 -31.973  1.00 40.27           C  
ANISOU 1799  CZ  PHE B 220     6001   4618   4679  -2019   -988    298       C  
ATOM   1800  N   THR B 221       0.331 -27.016 -33.153  1.00 36.62           N  
ANISOU 1800  N   THR B 221     5399   4324   4190  -1549   -830    470       N  
ATOM   1801  CA  THR B 221      -0.726 -26.639 -34.079  1.00 37.66           C  
ANISOU 1801  CA  THR B 221     5670   4571   4066  -1845  -1239     65       C  
ATOM   1802  C   THR B 221      -0.386 -27.268 -35.427  1.00 39.82           C  
ANISOU 1802  C   THR B 221     6077   4794   4255  -1429   -990    120       C  
ATOM   1803  O   THR B 221       0.775 -27.562 -35.728  1.00 39.51           O  
ANISOU 1803  O   THR B 221     5756   4712   4541  -1857   -745    337       O  
ATOM   1804  CB  THR B 221      -0.882 -25.102 -34.253  1.00 41.62           C  
ANISOU 1804  CB  THR B 221     6231   4899   4682  -1259   -677    376       C  
ATOM   1805  OG1 THR B 221       0.322 -24.546 -34.801  1.00 42.24           O  
ANISOU 1805  OG1 THR B 221     6553   4316   5178  -1442   -602    605       O  
ATOM   1806  CG2 THR B 221      -1.218 -24.412 -32.922  1.00 38.47           C  
ANISOU 1806  CG2 THR B 221     5753   4555   4310  -1821  -1121    222       C  
HETATM 1807  N   MSE B 222      -1.411 -27.488 -36.230  1.00 40.39           N  
ANISOU 1807  N   MSE B 222     6159   4217   4970  -1598  -1291   -199       N  
HETATM 1808  CA  MSE B 222      -1.246 -28.131 -37.525  1.00 41.82           C  
ANISOU 1808  CA  MSE B 222     6375   4734   4779  -1266   -879     71       C  
HETATM 1809  C   MSE B 222      -2.255 -27.554 -38.445  1.00 43.47           C  
ANISOU 1809  C   MSE B 222     6911   4816   4790  -1338  -1357    -88       C  
HETATM 1810  O   MSE B 222      -3.456 -27.551 -38.149  1.00 45.14           O  
ANISOU 1810  O   MSE B 222     6971   5492   4684   -962  -1316    -54       O  
HETATM 1811  CB  MSE B 222      -1.516 -29.622 -37.353  1.00 44.44           C  
ANISOU 1811  CB  MSE B 222     7268   4618   4998  -1559  -1100   -246       C  
HETATM 1812  CG  MSE B 222      -1.106 -30.473 -38.539  1.00 49.85           C  
ANISOU 1812  CG  MSE B 222     7964   6019   4954  -1236  -1406   -498       C  
HETATM 1813 SE   MSE B 222      -1.684 -32.286 -38.043  1.00 63.03          SE  
ANISOU 1813 SE   MSE B 222    10120   6633   7194  -1900   -936   -401      SE  
HETATM 1814  CE  MSE B 222      -0.293 -32.749 -36.731  1.00 51.89           C  
ANISOU 1814  CE  MSE B 222     9179   4082   6454  -2291   -546   -680       C  
ATOM   1815  N   GLU B 223      -1.767 -27.053 -39.571  1.00 43.47           N  
ANISOU 1815  N   GLU B 223     6782   4563   5170  -1373  -1326    -50       N  
ATOM   1816  CA  GLU B 223      -2.625 -26.641 -40.656  1.00 47.21           C  
ANISOU 1816  CA  GLU B 223     7233   5543   5162  -1381  -1686    -55       C  
ATOM   1817  C   GLU B 223      -2.656 -27.773 -41.678  1.00 50.10           C  
ANISOU 1817  C   GLU B 223     7632   5606   5795  -1352  -1674   -365       C  
ATOM   1818  O   GLU B 223      -1.608 -28.211 -42.173  1.00 48.00           O  
ANISOU 1818  O   GLU B 223     7686   5904   4646  -1669  -1210    -24       O  
ATOM   1819  CB  GLU B 223      -2.136 -25.332 -41.275  1.00 50.33           C  
ANISOU 1819  CB  GLU B 223     7733   5748   5642  -1494  -1576    264       C  
ATOM   1820  CG  GLU B 223      -3.140 -24.718 -42.238  1.00 59.88           C  
ANISOU 1820  CG  GLU B 223     8129   7638   6981   -684  -2407    488       C  
ATOM   1821  CD  GLU B 223      -2.772 -23.320 -42.701  1.00 69.73           C  
ANISOU 1821  CD  GLU B 223    10028   7786   8680  -1015  -2181    847       C  
ATOM   1822  OE1 GLU B 223      -3.687 -22.582 -43.113  1.00 69.27           O  
ANISOU 1822  OE1 GLU B 223     9414   7823   9081  -1561  -2493    985       O  
ATOM   1823  OE2 GLU B 223      -1.579 -22.952 -42.657  1.00 72.65           O  
ANISOU 1823  OE2 GLU B 223    10109   7543   9949  -1189   -762   3366       O  
ATOM   1824  N   VAL B 224      -3.863 -28.246 -41.972  1.00 49.41           N  
ANISOU 1824  N   VAL B 224     7701   5557   5514  -1917  -1325   -213       N  
ATOM   1825  CA  VAL B 224      -4.059 -29.388 -42.857  1.00 50.20           C  
ANISOU 1825  CA  VAL B 224     7941   5817   5314  -1981  -1686   -241       C  
ATOM   1826  C   VAL B 224      -4.658 -28.885 -44.168  1.00 51.06           C  
ANISOU 1826  C   VAL B 224     8298   5628   5473  -1977  -1806   -173       C  
ATOM   1827  O   VAL B 224      -5.779 -28.354 -44.193  1.00 50.29           O  
ANISOU 1827  O   VAL B 224     7726   5670   5709  -2221  -2000   -558       O  
ATOM   1828  CB  VAL B 224      -4.939 -30.476 -42.188  1.00 51.24           C  
ANISOU 1828  CB  VAL B 224     7982   6074   5412  -2005  -1495   -221       C  
ATOM   1829  CG1 VAL B 224      -5.205 -31.645 -43.129  1.00 49.50           C  
ANISOU 1829  CG1 VAL B 224     7480   6175   5150  -1933  -1545   -267       C  
ATOM   1830  CG2 VAL B 224      -4.298 -30.972 -40.891  1.00 54.33           C  
ANISOU 1830  CG2 VAL B 224     7923   7153   5565  -1533  -1421     77       C  
ATOM   1831  N   VAL B 225      -3.887 -29.044 -45.246  1.00 49.82           N  
ANISOU 1831  N   VAL B 225     8263   5370   5295  -2620  -1693    -28       N  
ATOM   1832  CA  VAL B 225      -4.270 -28.552 -46.572  1.00 53.56           C  
ANISOU 1832  CA  VAL B 225     8656   6216   5475  -2041  -2272   -179       C  
ATOM   1833  C   VAL B 225      -4.397 -29.699 -47.582  1.00 53.21           C  
ANISOU 1833  C   VAL B 225     8763   6114   5339  -2110  -2172   -212       C  
ATOM   1834  O   VAL B 225      -3.435 -30.423 -47.870  1.00 50.39           O  
ANISOU 1834  O   VAL B 225     9264   5446   4435  -2374  -1409   -402       O  
ATOM   1835  CB  VAL B 225      -3.297 -27.460 -47.094  1.00 54.87           C  
ANISOU 1835  CB  VAL B 225     8521   6681   5644  -2130  -2188    115       C  
ATOM   1836  CG1 VAL B 225      -3.722 -26.951 -48.462  1.00 51.03           C  
ANISOU 1836  CG1 VAL B 225     7754   6110   5526  -2308  -1957    188       C  
ATOM   1837  CG2 VAL B 225      -3.202 -26.296 -46.106  1.00 57.34           C  
ANISOU 1837  CG2 VAL B 225     8539   6217   7029  -2164  -1598   -148       C  
ATOM   1838  N   LYS B 226      -5.602 -29.842 -48.115  1.00 56.46           N  
ANISOU 1838  N   LYS B 226     8948   6590   5912  -2429  -2197   -156       N  
ATOM   1839  CA  LYS B 226      -5.904 -30.874 -49.095  1.00 56.98           C  
ANISOU 1839  CA  LYS B 226     9210   6872   5567  -2679  -2295   -432       C  
ATOM   1840  C   LYS B 226      -6.821 -30.262 -50.137  1.00 58.08           C  
ANISOU 1840  C   LYS B 226     9307   6934   5826  -2697  -2399   -493       C  
ATOM   1841  O   LYS B 226      -7.840 -29.662 -49.788  1.00 59.49           O  
ANISOU 1841  O   LYS B 226     9609   6532   6462  -2565  -1851     49       O  
ATOM   1842  CB  LYS B 226      -6.562 -32.071 -48.407  1.00 61.25           C  
ANISOU 1842  CB  LYS B 226     9769   7218   6284  -2597  -2094   -284       C  
ATOM   1843  CG  LYS B 226      -7.021 -33.163 -49.354  1.00 60.10           C  
ANISOU 1843  CG  LYS B 226     9691   7302   5840  -3121  -2381   -562       C  
ATOM   1844  CD  LYS B 226      -7.687 -34.295 -48.602  1.00 65.73           C  
ANISOU 1844  CD  LYS B 226     9639   8495   6839  -3126  -2515   -159       C  
ATOM   1845  CE  LYS B 226      -7.981 -35.459 -49.537  1.00 67.58           C  
ANISOU 1845  CE  LYS B 226    10705   8078   6893  -3969  -2923   -208       C  
ATOM   1846  NZ  LYS B 226      -8.477 -36.616 -48.754  1.00 70.71           N  
ANISOU 1846  NZ  LYS B 226    10754   8112   7999  -3833  -2359   -904       N  
ATOM   1847  N   HIS B 227      -6.457 -30.412 -51.409  1.00 60.01           N  
ANISOU 1847  N   HIS B 227     9462   7148   6188  -2803  -1709    131       N  
ATOM   1848  CA  HIS B 227      -7.210 -29.802 -52.501  1.00 66.09           C  
ANISOU 1848  CA  HIS B 227    10376   7927   6808  -2704  -2906    -40       C  
ATOM   1849  C   HIS B 227      -8.628 -30.337 -52.583  1.00 66.02           C  
ANISOU 1849  C   HIS B 227    10256   8600   6229  -2652  -2479     58       C  
ATOM   1850  O   HIS B 227      -8.872 -31.506 -52.263  1.00 63.43           O  
ANISOU 1850  O   HIS B 227     9050   8039   7010  -3051  -2355  -1257       O  
ATOM   1851  CB  HIS B 227      -6.492 -29.960 -53.840  1.00 77.71           C  
ANISOU 1851  CB  HIS B 227    11013  10943   7569  -2495  -2252   -568       C  
ATOM   1852  CG  HIS B 227      -6.797 -28.858 -54.810  1.00 94.32           C  
ANISOU 1852  CG  HIS B 227    13586  11894  10358  -2187  -2239    822       C  
ATOM   1853  ND1 HIS B 227      -6.977 -29.074 -56.162  1.00 99.40           N  
ANISOU 1853  ND1 HIS B 227    14711  12496  10558  -2413  -2098   -278       N  
ATOM   1854  CD2 HIS B 227      -6.972 -27.528 -54.614  1.00 98.50           C  
ANISOU 1854  CD2 HIS B 227    14185  12135  11104  -1952  -2112     24       C  
ATOM   1855  CE1 HIS B 227      -7.237 -27.924 -56.758  1.00 98.44           C  
ANISOU 1855  CE1 HIS B 227    14522  12972   9908  -2149  -3055    -33       C  
ATOM   1856  NE2 HIS B 227      -7.243 -26.971 -55.841  1.00102.41           N  
ANISOU 1856  NE2 HIS B 227    15689  11913  11307  -1005  -2014    120       N  
ATOM   1857  N   HIS B 228      -9.549 -29.456 -52.985  1.00 60.48           N  
ANISOU 1857  N   HIS B 228    10020   8100   4857  -3006  -2052    317       N  
ATOM   1858  CA  HIS B 228     -11.002 -29.716 -53.032  1.00 68.19           C  
ANISOU 1858  CA  HIS B 228    10129   8977   6802  -2791  -3211   -462       C  
ATOM   1859  C   HIS B 228     -11.629 -29.894 -51.639  1.00 72.56           C  
ANISOU 1859  C   HIS B 228    10210   9875   7482  -2910  -2889   -342       C  
ATOM   1860  O   HIS B 228     -12.794 -30.289 -51.501  1.00 70.85           O  
ANISOU 1860  O   HIS B 228    10014   9577   7325  -2980  -3540    219       O  
ATOM   1861  CB  HIS B 228     -11.338 -30.902 -53.945  1.00 69.64           C  
ANISOU 1861  CB  HIS B 228    10049   9201   7210  -3740  -3420   -558       C  
ATOM   1862  CG  HIS B 228     -10.741 -30.799 -55.313  1.00 77.92           C  
ANISOU 1862  CG  HIS B 228    11704  10240   7661  -3539  -2734   -500       C  
ATOM   1863  ND1 HIS B 228      -9.637 -31.527 -55.700  1.00 84.38           N  
ANISOU 1863  ND1 HIS B 228    11997  11066   8996  -3281  -2313   -271       N  
ATOM   1864  CD2 HIS B 228     -11.095 -30.053 -56.385  1.00 80.85           C  
ANISOU 1864  CD2 HIS B 228    11622  10501   8594  -3037  -2782     42       C  
ATOM   1865  CE1 HIS B 228      -9.341 -31.239 -56.955  1.00 84.87           C  
ANISOU 1865  CE1 HIS B 228    12380  11170   8696  -2914  -2900     12       C  
ATOM   1866  NE2 HIS B 228     -10.212 -30.349 -57.394  1.00 80.10           N  
ANISOU 1866  NE2 HIS B 228    12314  10812   7306  -3238  -3308   -665       N  
ATOM   1867  N   SER B 229     -10.843 -29.595 -50.613  1.00 72.99           N  
ANISOU 1867  N   SER B 229    10572   9667   7491  -2591  -2801   -771       N  
ATOM   1868  CA  SER B 229     -11.314 -29.615 -49.246  1.00 72.81           C  
ANISOU 1868  CA  SER B 229    10010  10060   7592  -2570  -2772   -524       C  
ATOM   1869  C   SER B 229     -10.928 -28.285 -48.594  1.00 70.10           C  
ANISOU 1869  C   SER B 229     9643   9676   7315  -2391  -2871   -130       C  
ATOM   1870  O   SER B 229      -9.891 -27.712 -48.935  1.00 67.56           O  
ANISOU 1870  O   SER B 229     9496   9315   6858  -2047  -2691   -555       O  
ATOM   1871  CB  SER B 229     -10.708 -30.799 -48.495  1.00 75.28           C  
ANISOU 1871  CB  SER B 229    10775   9520   8306  -2617  -2298   -320       C  
ATOM   1872  OG  SER B 229     -11.694 -31.456 -47.721  1.00 79.30           O  
ANISOU 1872  OG  SER B 229    10538  10266   9324  -3386  -2909    249       O  
ATOM   1873  N   PRO B 230     -11.777 -27.770 -47.682  1.00 73.83           N  
ANISOU 1873  N   PRO B 230    10294  10449   7308  -2017  -2800   -395       N  
ATOM   1874  CA  PRO B 230     -11.374 -26.572 -46.950  1.00 75.29           C  
ANISOU 1874  CA  PRO B 230    10097  10298   8212  -2087  -2850   -426       C  
ATOM   1875  C   PRO B 230     -10.196 -26.867 -46.027  1.00 71.48           C  
ANISOU 1875  C   PRO B 230    10016   9424   7717  -1863  -2324    232       C  
ATOM   1876  O   PRO B 230     -10.088 -27.974 -45.495  1.00 64.99           O  
ANISOU 1876  O   PRO B 230     9307   8707   6679  -1532  -2513   -378       O  
ATOM   1877  CB  PRO B 230     -12.621 -26.220 -46.130  1.00 79.13           C  
ANISOU 1877  CB  PRO B 230     9840  11319   8906  -2043  -2996  -1104       C  
ATOM   1878  CG  PRO B 230     -13.376 -27.498 -46.008  1.00 81.19           C  
ANISOU 1878  CG  PRO B 230    10091  11310   9444  -1948  -1964   -554       C  
ATOM   1879  CD  PRO B 230     -13.136 -28.208 -47.309  1.00 79.99           C  
ANISOU 1879  CD  PRO B 230    10185  11852   8355  -1956  -2868   -177       C  
ATOM   1880  N   VAL B 231      -9.318 -25.884 -45.872  1.00 74.12           N  
ANISOU 1880  N   VAL B 231    10451   9777   7934  -2112  -2412   -343       N  
ATOM   1881  CA  VAL B 231      -8.211 -25.954 -44.922  1.00 78.15           C  
ANISOU 1881  CA  VAL B 231    10574  10518   8600  -1584  -2628    312       C  
ATOM   1882  C   VAL B 231      -8.750 -26.242 -43.510  1.00 73.29           C  
ANISOU 1882  C   VAL B 231    10001   9347   8496  -1022  -2607     82       C  
ATOM   1883  O   VAL B 231      -9.763 -25.667 -43.087  1.00 69.38           O  
ANISOU 1883  O   VAL B 231     9896   9821   6642   -730  -2830   -328       O  
ATOM   1884  CB  VAL B 231      -7.324 -24.678 -44.994  1.00 80.78           C  
ANISOU 1884  CB  VAL B 231    10781  10539   9370  -1739  -2704    685       C  
ATOM   1885  CG1 VAL B 231      -8.160 -23.404 -44.920  1.00 87.78           C  
ANISOU 1885  CG1 VAL B 231    11326  11452  10572  -1141  -1448    549       C  
ATOM   1886  CG2 VAL B 231      -6.238 -24.679 -43.929  1.00 75.53           C  
ANISOU 1886  CG2 VAL B 231    10373   9599   8725  -1244  -2199    976       C  
ATOM   1887  N   SER B 232      -8.097 -27.175 -42.819  1.00 60.93           N  
ANISOU 1887  N   SER B 232     8722   7930   6499  -2134  -2352   -558       N  
ATOM   1888  CA  SER B 232      -8.488 -27.557 -41.464  1.00 57.51           C  
ANISOU 1888  CA  SER B 232     7883   7408   6560  -1876  -2089   -599       C  
ATOM   1889  C   SER B 232      -7.309 -27.469 -40.487  1.00 56.32           C  
ANISOU 1889  C   SER B 232     7611   7369   6419  -1612  -1885   -466       C  
ATOM   1890  O   SER B 232      -6.140 -27.431 -40.900  1.00 52.05           O  
ANISOU 1890  O   SER B 232     7270   5858   6645  -1418  -2096   -490       O  
ATOM   1891  CB  SER B 232      -9.092 -28.958 -41.461  1.00 57.29           C  
ANISOU 1891  CB  SER B 232     7686   7650   6430  -2206  -1745   -242       C  
ATOM   1892  OG  SER B 232      -8.133 -29.903 -41.889  1.00 57.68           O  
ANISOU 1892  OG  SER B 232     8920   6437   6559  -2457  -1316    237       O  
ATOM   1893  N   TRP B 233      -7.635 -27.433 -39.196  1.00 56.05           N  
ANISOU 1893  N   TRP B 233     7234   7696   6364  -1783  -1831   -202       N  
ATOM   1894  CA  TRP B 233      -6.651 -27.243 -38.132  1.00 54.34           C  
ANISOU 1894  CA  TRP B 233     7432   7004   6208  -1662  -1824   -146       C  
ATOM   1895  C   TRP B 233      -6.807 -28.281 -37.035  1.00 53.54           C  
ANISOU 1895  C   TRP B 233     7060   7218   6064  -1584  -1589   -136       C  
ATOM   1896  O   TRP B 233      -7.912 -28.749 -36.759  1.00 55.67           O  
ANISOU 1896  O   TRP B 233     7240   7424   6488  -2114  -2024   -139       O  
ATOM   1897  CB  TRP B 233      -6.762 -25.834 -37.542  1.00 51.96           C  
ANISOU 1897  CB  TRP B 233     6417   7201   6123  -1648  -1514   -480       C  
ATOM   1898  CG  TRP B 233      -6.413 -24.753 -38.524  1.00 58.24           C  
ANISOU 1898  CG  TRP B 233     7802   7423   6903  -1309  -1653     55       C  
ATOM   1899  CD1 TRP B 233      -5.175 -24.210 -38.741  1.00 56.12           C  
ANISOU 1899  CD1 TRP B 233     7593   6814   6913  -1075  -1473    -44       C  
ATOM   1900  CD2 TRP B 233      -7.305 -24.096 -39.437  1.00 62.65           C  
ANISOU 1900  CD2 TRP B 233     8703   7954   7147   -881  -2155   -209       C  
ATOM   1901  NE1 TRP B 233      -5.241 -23.255 -39.730  1.00 55.56           N  
ANISOU 1901  NE1 TRP B 233     7500   6826   6781   -288  -1732   -214       N  
ATOM   1902  CE2 TRP B 233      -6.534 -23.161 -40.174  1.00 59.92           C  
ANISOU 1902  CE2 TRP B 233     7817   8038   6911  -1148  -2402   -610       C  
ATOM   1903  CE3 TRP B 233      -8.683 -24.202 -39.703  1.00 70.84           C  
ANISOU 1903  CE3 TRP B 233     8907   9410   8598  -1340  -2307   -544       C  
ATOM   1904  CZ2 TRP B 233      -7.094 -22.329 -41.160  1.00 68.21           C  
ANISOU 1904  CZ2 TRP B 233     9335   8625   7953   -383  -2234    472       C  
ATOM   1905  CZ3 TRP B 233      -9.245 -23.375 -40.691  1.00 75.35           C  
ANISOU 1905  CZ3 TRP B 233     9724   9901   9005  -1170  -2656   -476       C  
ATOM   1906  CH2 TRP B 233      -8.446 -22.450 -41.406  1.00 74.89           C  
ANISOU 1906  CH2 TRP B 233     9668  10080   8704   -845  -2518   -221       C  
ATOM   1907  N   LYS B 234      -5.678 -28.646 -36.435  1.00 48.66           N  
ANISOU 1907  N   LYS B 234     6622   5971   5894  -2118  -1440   -300       N  
ATOM   1908  CA  LYS B 234      -5.622 -29.509 -35.258  1.00 48.71           C  
ANISOU 1908  CA  LYS B 234     6568   6305   5633  -1724  -1032   -357       C  
ATOM   1909  C   LYS B 234      -4.633 -28.883 -34.270  1.00 49.30           C  
ANISOU 1909  C   LYS B 234     6606   6369   5756  -1974  -1292    -40       C  
ATOM   1910  O   LYS B 234      -3.684 -28.191 -34.676  1.00 44.95           O  
ANISOU 1910  O   LYS B 234     6082   5715   5283  -1522  -1668     43       O  
ATOM   1911  CB  LYS B 234      -5.190 -30.935 -35.637  1.00 46.51           C  
ANISOU 1911  CB  LYS B 234     6513   5598   5560  -2425  -1355   -150       C  
ATOM   1912  CG  LYS B 234      -6.139 -31.636 -36.614  1.00 51.45           C  
ANISOU 1912  CG  LYS B 234     7228   6630   5689  -2262  -1394   -357       C  
ATOM   1913  CD  LYS B 234      -5.618 -33.006 -37.033  1.00 62.07           C  
ANISOU 1913  CD  LYS B 234     8741   7261   7582  -2035   -845   -853       C  
ATOM   1914  CE  LYS B 234      -6.638 -33.772 -37.872  1.00 57.27           C  
ANISOU 1914  CE  LYS B 234     8186   6697   6877  -3427   -769  -1369       C  
ATOM   1915  NZ  LYS B 234      -7.741 -34.318 -37.032  1.00 64.47           N  
ANISOU 1915  NZ  LYS B 234     9716   6713   8066  -3450  -1222   -580       N  
ATOM   1916  N   ARG B 235      -4.873 -29.101 -32.979  1.00 47.55           N  
ANISOU 1916  N   ARG B 235     6182   6299   5585  -1366  -1157   -289       N  
ATOM   1917  CA  ARG B 235      -3.948 -28.643 -31.941  1.00 45.84           C  
ANISOU 1917  CA  ARG B 235     6135   5730   5549  -1500   -988    -74       C  
ATOM   1918  C   ARG B 235      -4.007 -29.576 -30.742  1.00 46.30           C  
ANISOU 1918  C   ARG B 235     6387   5695   5511  -1612   -683   -150       C  
ATOM   1919  O   ARG B 235      -4.960 -30.357 -30.593  1.00 44.37           O  
ANISOU 1919  O   ARG B 235     5875   5569   5413  -1533   -667   -433       O  
ATOM   1920  CB  ARG B 235      -4.231 -27.184 -31.540  1.00 43.73           C  
ANISOU 1920  CB  ARG B 235     5483   5555   5576  -1803  -1298    -37       C  
ATOM   1921  CG  ARG B 235      -5.239 -26.994 -30.422  1.00 55.11           C  
ANISOU 1921  CG  ARG B 235     7189   7657   6093  -1246   -589     54       C  
ATOM   1922  CD  ARG B 235      -6.421 -26.157 -30.864  1.00 62.07           C  
ANISOU 1922  CD  ARG B 235     7409   8834   7340   -994  -1539   -267       C  
ATOM   1923  NE  ARG B 235      -7.410 -26.975 -31.564  1.00 65.08           N  
ANISOU 1923  NE  ARG B 235     7434   9038   8252  -1587   -486   -665       N  
ATOM   1924  CZ  ARG B 235      -7.574 -27.017 -32.886  1.00 63.79           C  
ANISOU 1924  CZ  ARG B 235     7472   8443   8321  -2140  -1416  -1030       C  
ATOM   1925  NH1 ARG B 235      -6.822 -26.280 -33.694  1.00 80.15           N  
ANISOU 1925  NH1 ARG B 235    10277  10082  10093  -1721   -424    294       N  
ATOM   1926  NH2 ARG B 235      -8.505 -27.803 -33.406  1.00 65.00           N  
ANISOU 1926  NH2 ARG B 235     7759   9837   7099  -1257  -1362   -774       N  
ATOM   1927  N   GLY B 236      -2.983 -29.498 -29.898  1.00 44.62           N  
ANISOU 1927  N   GLY B 236     6973   5109   4870  -1734   -714   -199       N  
ATOM   1928  CA  GLY B 236      -2.988 -30.240 -28.650  1.00 43.81           C  
ANISOU 1928  CA  GLY B 236     7024   4961   4659  -2054   -870   -407       C  
ATOM   1929  C   GLY B 236      -1.665 -30.264 -27.925  1.00 43.40           C  
ANISOU 1929  C   GLY B 236     6936   4560   4992  -1801   -682    205       C  
ATOM   1930  O   GLY B 236      -0.773 -29.454 -28.202  1.00 40.33           O  
ANISOU 1930  O   GLY B 236     5996   4356   4970  -1423   -701     96       O  
ATOM   1931  N   VAL B 237      -1.561 -31.197 -26.983  1.00 39.17           N  
ANISOU 1931  N   VAL B 237     6551   4207   4123  -2037   -459   -306       N  
ATOM   1932  CA  VAL B 237      -0.428 -31.277 -26.063  1.00 43.12           C  
ANISOU 1932  CA  VAL B 237     6859   4581   4943  -1714   -849   -323       C  
ATOM   1933  C   VAL B 237      -0.019 -32.735 -25.917  1.00 43.97           C  
ANISOU 1933  C   VAL B 237     7049   4516   5141  -1698   -305    129       C  
ATOM   1934  O   VAL B 237      -0.856 -33.600 -25.657  1.00 39.23           O  
ANISOU 1934  O   VAL B 237     7165   3514   4226  -1637   -740    -41       O  
ATOM   1935  CB  VAL B 237      -0.768 -30.686 -24.661  1.00 44.56           C  
ANISOU 1935  CB  VAL B 237     6771   5281   4879  -1348   -730   -389       C  
ATOM   1936  CG1 VAL B 237       0.432 -30.748 -23.716  1.00 41.57           C  
ANISOU 1936  CG1 VAL B 237     6450   5167   4179  -1164   -303   -816       C  
ATOM   1937  CG2 VAL B 237      -1.259 -29.244 -24.762  1.00 43.71           C  
ANISOU 1937  CG2 VAL B 237     6410   5132   5065  -1580   -573   -259       C  
ATOM   1938  N   PHE B 238       1.265 -33.003 -26.112  1.00 40.49           N  
ANISOU 1938  N   PHE B 238     7001   3897   4483  -1479   -567   -245       N  
ATOM   1939  CA  PHE B 238       1.824 -34.314 -25.800  1.00 42.32           C  
ANISOU 1939  CA  PHE B 238     7397   4067   4614  -1174   -321   -218       C  
ATOM   1940  C   PHE B 238       2.818 -34.134 -24.673  1.00 43.55           C  
ANISOU 1940  C   PHE B 238     7553   4165   4830  -1103   -454   -435       C  
ATOM   1941  O   PHE B 238       3.374 -33.053 -24.503  1.00 38.39           O  
ANISOU 1941  O   PHE B 238     6493   3845   4245   -899   -547    408       O  
ATOM   1942  CB  PHE B 238       2.523 -34.921 -27.020  1.00 43.48           C  
ANISOU 1942  CB  PHE B 238     8234   3558   4728   -991   -472   -687       C  
ATOM   1943  CG  PHE B 238       1.583 -35.550 -28.015  1.00 44.50           C  
ANISOU 1943  CG  PHE B 238     7775   4095   5038  -1240   -420   -465       C  
ATOM   1944  CD1 PHE B 238       1.020 -34.790 -29.039  1.00 48.18           C  
ANISOU 1944  CD1 PHE B 238     8734   4652   4917  -1294   -530   -366       C  
ATOM   1945  CD2 PHE B 238       1.264 -36.908 -27.931  1.00 44.93           C  
ANISOU 1945  CD2 PHE B 238     8548   3904   4619  -1210   -319   -970       C  
ATOM   1946  CE1 PHE B 238       0.143 -35.371 -29.953  1.00 51.25           C  
ANISOU 1946  CE1 PHE B 238     9386   4937   5147  -1558   -787   -821       C  
ATOM   1947  CE2 PHE B 238       0.393 -37.493 -28.840  1.00 49.28           C  
ANISOU 1947  CE2 PHE B 238     8921   4518   5284  -1507   -480   -811       C  
ATOM   1948  CZ  PHE B 238      -0.169 -36.723 -29.854  1.00 51.06           C  
ANISOU 1948  CZ  PHE B 238     8965   4995   5439  -1388   -205   -372       C  
ATOM   1949  N   ARG B 239       3.013 -35.192 -23.895  1.00 50.39           N  
ANISOU 1949  N   ARG B 239     8474   4672   5999  -1262   -246    306       N  
ATOM   1950  CA  ARG B 239       4.115 -35.291 -22.939  1.00 52.55           C  
ANISOU 1950  CA  ARG B 239     9089   5024   5851   -669   -564   -167       C  
ATOM   1951  C   ARG B 239       4.716 -36.702 -23.005  1.00 52.03           C  
ANISOU 1951  C   ARG B 239     9168   5108   5490   -543   -356    390       C  
ATOM   1952  O   ARG B 239       4.237 -37.534 -23.779  1.00 52.72           O  
ANISOU 1952  O   ARG B 239     9489   4833   5708  -1241    184    336       O  
ATOM   1953  CB  ARG B 239       3.645 -34.918 -21.532  1.00 58.18           C  
ANISOU 1953  CB  ARG B 239     9814   6321   5968   -671   -215   -216       C  
ATOM   1954  CG  ARG B 239       2.612 -35.854 -20.942  1.00 67.20           C  
ANISOU 1954  CG  ARG B 239    10282   7230   8019  -1244   -211    358       C  
ATOM   1955  CD  ARG B 239       1.445 -35.076 -20.354  1.00 73.91           C  
ANISOU 1955  CD  ARG B 239    10842   8930   8311   -739   -232   -370       C  
ATOM   1956  NE  ARG B 239       1.733 -34.510 -19.036  1.00 70.79           N  
ANISOU 1956  NE  ARG B 239    10444   8312   8141  -1683     36    159       N  
ATOM   1957  CZ  ARG B 239       1.713 -35.191 -17.889  1.00 72.62           C  
ANISOU 1957  CZ  ARG B 239     9938   9599   8054  -1271   -814    329       C  
ATOM   1958  NH1 ARG B 239       1.450 -36.500 -17.869  1.00 83.54           N  
ANISOU 1958  NH1 ARG B 239    11776   9291  10674   -304   -603   -536       N  
ATOM   1959  NH2 ARG B 239       1.986 -34.566 -16.749  1.00 60.24           N  
ANISOU 1959  NH2 ARG B 239     7729   7930   7228  -1498   1910     74       N  
ATOM   1960  N   ASN B 240       5.771 -36.961 -22.228  1.00 51.27           N  
ANISOU 1960  N   ASN B 240     9036   5139   5304   -134    -34    661       N  
ATOM   1961  CA  ASN B 240       6.362 -38.308 -22.156  1.00 55.22           C  
ANISOU 1961  CA  ASN B 240     9723   5104   6154    150     29    -23       C  
ATOM   1962  C   ASN B 240       5.389 -39.361 -21.647  1.00 63.51           C  
ANISOU 1962  C   ASN B 240    10920   5915   7294   -309    222    765       C  
ATOM   1963  O   ASN B 240       4.583 -39.095 -20.742  1.00 66.18           O  
ANISOU 1963  O   ASN B 240    11891   6286   6968    657    622   2390       O  
ATOM   1964  CB  ASN B 240       7.600 -38.345 -21.260  1.00 55.35           C  
ANISOU 1964  CB  ASN B 240    10152   4508   6369    910   -265    919       C  
ATOM   1965  CG  ASN B 240       8.657 -37.337 -21.655  1.00 59.80           C  
ANISOU 1965  CG  ASN B 240     9382   6318   7019    241    134    -29       C  
ATOM   1966  OD1 ASN B 240       8.879 -37.047 -22.841  1.00 59.17           O  
ANISOU 1966  OD1 ASN B 240    10690   5618   6171   1589   -650   -620       O  
ATOM   1967  ND2 ASN B 240       9.328 -36.794 -20.649  1.00 60.50           N  
ANISOU 1967  ND2 ASN B 240     9514   8156   5318   1127   -766   1092       N  
ATOM   1968  N   GLN B 241       5.468 -40.542 -22.258  1.00 66.99           N  
ANISOU 1968  N   GLN B 241    11622   5843   7985    430    600    582       N  
ATOM   1969  CA  GLN B 241       4.828 -41.748 -21.760  1.00 67.75           C  
ANISOU 1969  CA  GLN B 241    11935   5971   7834    -97    254    694       C  
ATOM   1970  C   GLN B 241       5.846 -42.470 -20.878  1.00 74.00           C  
ANISOU 1970  C   GLN B 241    12006   7094   9016    450    328   1250       C  
ATOM   1971  O   GLN B 241       7.024 -42.585 -21.233  1.00 66.37           O  
ANISOU 1971  O   GLN B 241    11965   5887   7363    918    389   1581       O  
ATOM   1972  CB  GLN B 241       4.377 -42.638 -22.917  1.00 65.19           C  
ANISOU 1972  CB  GLN B 241    11281   5784   7702   -399     91   1048       C  
ATOM   1973  N   VAL B 242       5.383 -42.948 -19.728  1.00 74.81           N  
ANISOU 1973  N   VAL B 242    13177   5597   9648    381    582   1821       N  
ATOM   1974  CA  VAL B 242       6.266 -43.433 -18.658  1.00 80.49           C  
ANISOU 1974  CA  VAL B 242    13135   8024   9424    715    379   1037       C  
ATOM   1975  C   VAL B 242       6.215 -44.961 -18.481  1.00 87.37           C  
ANISOU 1975  C   VAL B 242    14460   8173  10563    888    562   1902       C  
ATOM   1976  O   VAL B 242       7.111 -45.557 -17.867  1.00 84.35           O  
ANISOU 1976  O   VAL B 242    14320   6215  11513    779    448    629       O  
ATOM   1977  CB  VAL B 242       5.999 -42.626 -17.353  1.00 73.34           C  
ANISOU 1977  CB  VAL B 242    12795   6615   8453    561   -560   1809       C  
ATOM   1978  CG1 VAL B 242       6.306 -43.399 -16.079  1.00 71.55           C  
ANISOU 1978  CG1 VAL B 242    11808   7112   8264    959    -56   1927       C  
ATOM   1979  CG2 VAL B 242       6.786 -41.321 -17.386  1.00 76.67           C  
ANISOU 1979  CG2 VAL B 242    11794   7335  10000    231    183   1176       C  
ATOM   1980  N   ASP B 243       5.182 -45.578 -19.056  1.00 92.45           N  
ANISOU 1980  N   ASP B 243    14768   8153  12204    123   1059   1626       N  
ATOM   1981  CA  ASP B 243       4.967 -47.027 -19.008  1.00102.89           C  
ANISOU 1981  CA  ASP B 243    16594   8111  14386    531    830   1454       C  
ATOM   1982  C   ASP B 243       6.247 -47.791 -19.371  1.00100.57           C  
ANISOU 1982  C   ASP B 243    16897   8066  13248    896    866   1966       C  
ATOM   1983  O   ASP B 243       6.760 -47.611 -20.476  1.00 90.51           O  
ANISOU 1983  O   ASP B 243    17114   4540  12735   1785    868   1097       O  
ATOM   1984  CB  ASP B 243       3.828 -47.414 -19.956  1.00103.12           C  
ANISOU 1984  CB  ASP B 243    17030   7269  14881   -149    689   1368       C  
ATOM   1985  CG  ASP B 243       2.932 -48.489 -19.381  1.00105.27           C  
ANISOU 1985  CG  ASP B 243    17146   7205  15644    329    574   1691       C  
ATOM   1986  OD1 ASP B 243       3.272 -49.688 -19.494  1.00101.02           O  
ANISOU 1986  OD1 ASP B 243    17325   6312  14746  -1152   -908    219       O  
ATOM   1987  OD2 ASP B 243       1.874 -48.132 -18.821  1.00112.57           O  
ANISOU 1987  OD2 ASP B 243    16579  10673  15520    258     21     84       O  
ATOM   1988  N   PRO B 244       6.771 -48.629 -18.439  1.00105.45           N  
ANISOU 1988  N   PRO B 244    17647   8329  14088    763    855   2597       N  
ATOM   1989  CA  PRO B 244       8.040 -49.363 -18.640  1.00108.59           C  
ANISOU 1989  CA  PRO B 244    17890   8919  14447   1220    943   2853       C  
ATOM   1990  C   PRO B 244       8.054 -50.264 -19.878  1.00115.67           C  
ANISOU 1990  C   PRO B 244    19206   8806  15934   1957   1347   1842       C  
ATOM   1991  O   PRO B 244       9.130 -50.632 -20.357  1.00115.04           O  
ANISOU 1991  O   PRO B 244    18977   8559  16174   2360    643   1327       O  
ATOM   1992  CB  PRO B 244       8.177 -50.207 -17.363  1.00106.70           C  
ANISOU 1992  CB  PRO B 244    17212   8356  14971   2444    650   3008       C  
ATOM   1993  CG  PRO B 244       6.804 -50.274 -16.788  1.00106.68           C  
ANISOU 1993  CG  PRO B 244    18146   8961  13424    888   1035   3988       C  
ATOM   1994  CD  PRO B 244       6.168 -48.959 -17.133  1.00104.74           C  
ANISOU 1994  CD  PRO B 244    16900   8651  14244   1223   1026   2588       C  
ATOM   1995  N   GLU B 245       6.866 -50.609 -20.376  1.00119.49           N  
ANISOU 1995  N   GLU B 245    19489   9475  16437   1709   1432   1392       N  
ATOM   1996  CA  GLU B 245       6.711 -51.330 -21.634  1.00119.81           C  
ANISOU 1996  CA  GLU B 245    19603   9064  16852    627    925   1576       C  
ATOM   1997  C   GLU B 245       6.648 -50.369 -22.829  1.00120.38           C  
ANISOU 1997  C   GLU B 245    20264   9193  16282    967    597   1185       C  
ATOM   1998  O   GLU B 245       7.473 -50.467 -23.741  1.00131.58           O  
ANISOU 1998  O   GLU B 245    20849  12845  16298   1345    784   1029       O  
ATOM   1999  CB  GLU B 245       5.476 -52.239 -21.590  1.00114.63           C  
ANISOU 1999  CB  GLU B 245    19458   8887  15208    588    831   1387       C  
ATOM   2000  N   THR B 246       5.692 -49.436 -22.804  1.00114.32           N  
ANISOU 2000  N   THR B 246    19667   8683  15085    412    756   1027       N  
ATOM   2001  CA  THR B 246       5.408 -48.561 -23.952  1.00109.08           C  
ANISOU 2001  CA  THR B 246    18357   8138  14949    501    186    497       C  
ATOM   2002  C   THR B 246       5.784 -47.085 -23.737  1.00108.68           C  
ANISOU 2002  C   THR B 246    18179   8465  14648    -78    301    613       C  
ATOM   2003  O   THR B 246       5.042 -46.177 -24.138  1.00108.66           O  
ANISOU 2003  O   THR B 246    17730  10339  13215    202    432   1934       O  
ATOM   2004  CB  THR B 246       3.926 -48.681 -24.381  1.00105.47           C  
ANISOU 2004  CB  THR B 246    17791   7921  14361    188    842   1168       C  
ATOM   2005  N   HIS B 247       6.941 -46.848 -23.117  1.00107.98           N  
ANISOU 2005  N   HIS B 247    17589   8790  14646    420    372    818       N  
ATOM   2006  CA  HIS B 247       7.441 -45.484 -22.905  1.00 99.42           C  
ANISOU 2006  CA  HIS B 247    16769   8582  12421    515    628   1315       C  
ATOM   2007  C   HIS B 247       7.969 -44.866 -24.195  1.00 86.95           C  
ANISOU 2007  C   HIS B 247    15325   6089  11621   1281    168    539       C  
ATOM   2008  O   HIS B 247       8.591 -45.548 -25.021  1.00 83.61           O  
ANISOU 2008  O   HIS B 247    14790   5737  11239   -774   1094    590       O  
ATOM   2009  CB  HIS B 247       8.504 -45.433 -21.790  1.00101.44           C  
ANISOU 2009  CB  HIS B 247    17546   8633  12362    769    301   1144       C  
ATOM   2010  CG  HIS B 247       9.785 -46.139 -22.119  1.00113.03           C  
ANISOU 2010  CG  HIS B 247    18135  10601  14210   1623    708   1282       C  
ATOM   2011  ND1 HIS B 247       9.837 -47.292 -22.874  1.00120.13           N  
ANISOU 2011  ND1 HIS B 247    19309  11252  15082   1781    728    637       N  
ATOM   2012  CD2 HIS B 247      11.064 -45.863 -21.769  1.00113.95           C  
ANISOU 2012  CD2 HIS B 247    18205  10851  14240   1356    714   1363       C  
ATOM   2013  CE1 HIS B 247      11.092 -47.686 -22.990  1.00121.97           C  
ANISOU 2013  CE1 HIS B 247    19601  11549  15193   2035   1333    419       C  
ATOM   2014  NE2 HIS B 247      11.856 -46.838 -22.326  1.00119.46           N  
ANISOU 2014  NE2 HIS B 247    18767  11707  14912   1861   1213    818       N  
ATOM   2015  N   CYS B 248       7.787 -43.554 -24.334  1.00 67.76           N  
ANISOU 2015  N   CYS B 248    12925   5392   7426    381    957   -500       N  
ATOM   2016  CA  CYS B 248       8.265 -42.824 -25.508  1.00 65.71           C  
ANISOU 2016  CA  CYS B 248    12610   4539   7816    284    628   -451       C  
ATOM   2017  C   CYS B 248       8.242 -41.309 -25.280  1.00 57.53           C  
ANISOU 2017  C   CYS B 248    10888   4413   6556    346     44    -16       C  
ATOM   2018  O   CYS B 248       7.211 -40.754 -24.900  1.00 56.42           O  
ANISOU 2018  O   CYS B 248    11274   3407   6753    140     94    -48       O  
ATOM   2019  CB  CYS B 248       7.431 -43.183 -26.739  1.00 71.83           C  
ANISOU 2019  CB  CYS B 248    14593   4277   8422  -1522   -312   -168       C  
ATOM   2020  SG  CYS B 248       5.685 -42.730 -26.617  1.00102.59           S  
ANISOU 2020  SG  CYS B 248    16212   9840  12927    678   -142   -358       S  
ATOM   2021  N   HIS B 249       9.373 -40.643 -25.510  1.00 53.25           N  
ANISOU 2021  N   HIS B 249     9677   4266   6288    808    -12   -316       N  
ATOM   2022  CA  HIS B 249       9.442 -39.201 -25.323  1.00 51.96           C  
ANISOU 2022  CA  HIS B 249     9549   4234   5956    566    -71    -54       C  
ATOM   2023  C   HIS B 249       8.298 -38.554 -26.101  1.00 49.91           C  
ANISOU 2023  C   HIS B 249     9075   4360   5528    174    165     65       C  
ATOM   2024  O   HIS B 249       7.794 -39.137 -27.080  1.00 49.08           O  
ANISOU 2024  O   HIS B 249     8899   4337   5413    341    471   -152       O  
ATOM   2025  CB  HIS B 249      10.793 -38.638 -25.749  1.00 49.69           C  
ANISOU 2025  CB  HIS B 249     9194   4533   5151   1100    529   -322       C  
ATOM   2026  CG  HIS B 249      11.944 -39.099 -24.907  1.00 54.55           C  
ANISOU 2026  CG  HIS B 249     9894   4879   5953   1352    169    -69       C  
ATOM   2027  ND1 HIS B 249      13.257 -38.935 -25.295  1.00 56.92           N  
ANISOU 2027  ND1 HIS B 249    10079   4975   6571   1823    457      5       N  
ATOM   2028  CD2 HIS B 249      11.984 -39.719 -23.702  1.00 55.67           C  
ANISOU 2028  CD2 HIS B 249    10044   4744   6362   1630    344    253       C  
ATOM   2029  CE1 HIS B 249      14.055 -39.430 -24.366  1.00 60.48           C  
ANISOU 2029  CE1 HIS B 249    10486   6004   6489   1635    188     56       C  
ATOM   2030  NE2 HIS B 249      13.307 -39.911 -23.389  1.00 58.38           N  
ANISOU 2030  NE2 HIS B 249    10451   5619   6109   1717   -382    516       N  
ATOM   2031  N   ALA B 250       7.887 -37.368 -25.647  1.00 46.66           N  
ANISOU 2031  N   ALA B 250     8258   4268   5200   -101   -179     15       N  
ATOM   2032  CA  ALA B 250       6.772 -36.606 -26.236  1.00 46.52           C  
ANISOU 2032  CA  ALA B 250     7765   4373   5536   -314   -137    -10       C  
ATOM   2033  C   ALA B 250       6.850 -36.479 -27.759  1.00 44.49           C  
ANISOU 2033  C   ALA B 250     7444   4040   5418   -627   -104      4       C  
ATOM   2034  O   ALA B 250       5.835 -36.608 -28.449  1.00 43.52           O  
ANISOU 2034  O   ALA B 250     7252   4309   4972   -895    202    326       O  
ATOM   2035  CB  ALA B 250       6.689 -35.223 -25.603  1.00 46.40           C  
ANISOU 2035  CB  ALA B 250     7518   4352   5760   -535    362   -191       C  
ATOM   2036  N   GLU B 251       8.060 -36.236 -28.263  1.00 40.87           N  
ANISOU 2036  N   GLU B 251     7034   3938   4556   -208   -377    -96       N  
ATOM   2037  CA  GLU B 251       8.322 -36.027 -29.689  1.00 40.60           C  
ANISOU 2037  CA  GLU B 251     7103   3771   4552   -118    -21   -269       C  
ATOM   2038  C   GLU B 251       7.967 -37.291 -30.467  1.00 45.87           C  
ANISOU 2038  C   GLU B 251     8011   4058   5359   -516   -238   -497       C  
ATOM   2039  O   GLU B 251       7.268 -37.233 -31.486  1.00 46.93           O  
ANISOU 2039  O   GLU B 251     8354   4342   5135   -938   -130    -94       O  
ATOM   2040  CB  GLU B 251       9.795 -35.653 -29.934  1.00 43.26           C  
ANISOU 2040  CB  GLU B 251     7383   4103   4948   -341     86   -308       C  
ATOM   2041  CG  GLU B 251      10.294 -34.408 -29.210  1.00 44.55           C  
ANISOU 2041  CG  GLU B 251     7572   4285   5070   -293     50   -487       C  
ATOM   2042  CD  GLU B 251      10.818 -34.685 -27.803  1.00 48.81           C  
ANISOU 2042  CD  GLU B 251     7774   5222   5547    105   -176    -71       C  
ATOM   2043  OE1 GLU B 251      10.238 -35.508 -27.068  1.00 50.67           O  
ANISOU 2043  OE1 GLU B 251     7904   5429   5918    254   -123    170       O  
ATOM   2044  OE2 GLU B 251      11.815 -34.054 -27.419  1.00 54.31           O  
ANISOU 2044  OE2 GLU B 251     7959   7044   5630   -202   -515   -767       O  
ATOM   2045  N   ARG B 252       8.449 -38.424 -29.960  1.00 47.36           N  
ANISOU 2045  N   ARG B 252     8861   4151   4981   -534   -124   -217       N  
ATOM   2046  CA  ARG B 252       8.152 -39.727 -30.509  1.00 47.73           C  
ANISOU 2046  CA  ARG B 252     8886   4071   5175   -606     -8   -165       C  
ATOM   2047  C   ARG B 252       6.667 -40.036 -30.416  1.00 49.13           C  
ANISOU 2047  C   ARG B 252     8873   4308   5486   -612   -303   -186       C  
ATOM   2048  O   ARG B 252       6.103 -40.602 -31.350  1.00 49.54           O  
ANISOU 2048  O   ARG B 252     9133   4213   5477   -597    144   -722       O  
ATOM   2049  CB  ARG B 252       8.937 -40.791 -29.763  1.00 54.84           C  
ANISOU 2049  CB  ARG B 252    10152   4499   6185    116    141    334       C  
ATOM   2050  CG  ARG B 252      10.246 -41.207 -30.402  1.00 63.22           C  
ANISOU 2050  CG  ARG B 252    10587   6277   7157     -4    533   -440       C  
ATOM   2051  CD  ARG B 252      10.576 -42.624 -29.947  1.00 76.12           C  
ANISOU 2051  CD  ARG B 252    12596   7043   9283    379  -1096    242       C  
ATOM   2052  NE  ARG B 252       9.386 -43.480 -29.966  1.00 79.31           N  
ANISOU 2052  NE  ARG B 252    13449   7044   9641   -198  -1255   -304       N  
ATOM   2053  CZ  ARG B 252       9.167 -44.509 -29.152  1.00 79.86           C  
ANISOU 2053  CZ  ARG B 252    13683   7127   9531     30   -506   -411       C  
ATOM   2054  NH1 ARG B 252       8.039 -45.202 -29.256  1.00 73.21           N  
ANISOU 2054  NH1 ARG B 252    12816   7199   7799    535     84   -147       N  
ATOM   2055  NH2 ARG B 252      10.063 -44.847 -28.232  1.00 85.05           N  
ANISOU 2055  NH2 ARG B 252    14264   8130   9918    270   -760    -87       N  
ATOM   2056  N   CYS B 253       6.034 -39.670 -29.299  1.00 48.31           N  
ANISOU 2056  N   CYS B 253     8834   3913   5608   -483   -383   -265       N  
ATOM   2057  CA  CYS B 253       4.602 -39.930 -29.150  1.00 54.32           C  
ANISOU 2057  CA  CYS B 253     9076   5140   6423   -295   -794     28       C  
ATOM   2058  C   CYS B 253       3.807 -39.083 -30.171  1.00 47.77           C  
ANISOU 2058  C   CYS B 253     8822   3605   5720  -1129   -410    -14       C  
ATOM   2059  O   CYS B 253       2.815 -39.556 -30.726  1.00 49.44           O  
ANISOU 2059  O   CYS B 253     8720   4272   5791   -904   -898    225       O  
ATOM   2060  CB  CYS B 253       4.106 -39.720 -27.710  1.00 60.48           C  
ANISOU 2060  CB  CYS B 253    10386   5635   6959   -473    111   -425       C  
ATOM   2061  SG  CYS B 253       5.075 -40.421 -26.325  1.00 74.32           S  
ANISOU 2061  SG  CYS B 253    12263   8413   7560   -527    227   1374       S  
ATOM   2062  N   PHE B 254       4.270 -37.863 -30.449  1.00 44.19           N  
ANISOU 2062  N   PHE B 254     8082   3685   5023   -994   -384    113       N  
ATOM   2063  CA  PHE B 254       3.658 -37.047 -31.503  1.00 41.68           C  
ANISOU 2063  CA  PHE B 254     7831   3325   4677  -1258   -389    -59       C  
ATOM   2064  C   PHE B 254       3.771 -37.750 -32.851  1.00 44.42           C  
ANISOU 2064  C   PHE B 254     8259   3796   4823  -1202   -290   -248       C  
ATOM   2065  O   PHE B 254       2.783 -37.850 -33.592  1.00 46.79           O  
ANISOU 2065  O   PHE B 254     8585   4052   5138  -1114   -666    -55       O  
ATOM   2066  CB  PHE B 254       4.257 -35.626 -31.599  1.00 41.19           C  
ANISOU 2066  CB  PHE B 254     7447   3434   4770  -1235   -307     71       C  
ATOM   2067  CG  PHE B 254       3.672 -34.814 -32.734  1.00 40.96           C  
ANISOU 2067  CG  PHE B 254     7546   3578   4438  -1357   -226    119       C  
ATOM   2068  CD1 PHE B 254       4.174 -34.935 -34.036  1.00 40.46           C  
ANISOU 2068  CD1 PHE B 254     7378   3500   4495  -1297   -204    -56       C  
ATOM   2069  CD2 PHE B 254       2.578 -33.974 -32.515  1.00 42.34           C  
ANISOU 2069  CD2 PHE B 254     7627   3603   4855  -1384   -341    237       C  
ATOM   2070  CE1 PHE B 254       3.611 -34.229 -35.090  1.00 42.14           C  
ANISOU 2070  CE1 PHE B 254     7671   3679   4659  -1568   -315     60       C  
ATOM   2071  CE2 PHE B 254       2.016 -33.252 -33.567  1.00 41.08           C  
ANISOU 2071  CE2 PHE B 254     7326   3751   4529  -1900   -546     51       C  
ATOM   2072  CZ  PHE B 254       2.536 -33.378 -34.853  1.00 42.04           C  
ANISOU 2072  CZ  PHE B 254     7409   3733   4832  -1795   -330   -291       C  
ATOM   2073  N   LEU B 255       4.976 -38.236 -33.150  1.00 43.80           N  
ANISOU 2073  N   LEU B 255     8086   3592   4963  -1271   -413   -114       N  
ATOM   2074  CA  LEU B 255       5.266 -38.889 -34.420  1.00 49.20           C  
ANISOU 2074  CA  LEU B 255     9269   4170   5253  -1067    -58   -343       C  
ATOM   2075  C   LEU B 255       4.395 -40.104 -34.644  1.00 53.26           C  
ANISOU 2075  C   LEU B 255    10031   4277   5928  -1326   -736   -588       C  
ATOM   2076  O   LEU B 255       3.857 -40.272 -35.733  1.00 53.57           O  
ANISOU 2076  O   LEU B 255    10375   4332   5647  -1379   -433   -903       O  
ATOM   2077  CB  LEU B 255       6.744 -39.271 -34.518  1.00 54.59           C  
ANISOU 2077  CB  LEU B 255     9691   5040   6008   -407    190    -50       C  
ATOM   2078  CG  LEU B 255       7.721 -38.130 -34.809  1.00 55.97           C  
ANISOU 2078  CG  LEU B 255     9749   5398   6119   -732      8   -204       C  
ATOM   2079  CD1 LEU B 255       9.150 -38.665 -34.875  1.00 55.35           C  
ANISOU 2079  CD1 LEU B 255    10230   4654   6144     -7    274   -425       C  
ATOM   2080  CD2 LEU B 255       7.345 -37.380 -36.088  1.00 51.04           C  
ANISOU 2080  CD2 LEU B 255     9178   4435   5778   -806    405   -367       C  
ATOM   2081  N   SER B 256       4.231 -40.921 -33.602  1.00 54.97           N  
ANISOU 2081  N   SER B 256    10229   4477   6177   -859   -440   -315       N  
ATOM   2082  CA  SER B 256       3.438 -42.140 -33.699  1.00 59.46           C  
ANISOU 2082  CA  SER B 256    10708   4902   6982  -1330   -526   -245       C  
ATOM   2083  C   SER B 256       1.967 -41.839 -33.972  1.00 57.39           C  
ANISOU 2083  C   SER B 256    10882   4752   6169  -1404   -762   -380       C  
ATOM   2084  O   SER B 256       1.370 -42.455 -34.852  1.00 57.81           O  
ANISOU 2084  O   SER B 256    10417   4688   6857  -1973  -1157     37       O  
ATOM   2085  CB  SER B 256       3.605 -42.997 -32.446  1.00 63.90           C  
ANISOU 2085  CB  SER B 256    11502   5561   7215   -338  -1227    -98       C  
ATOM   2086  OG  SER B 256       4.948 -43.429 -32.339  1.00 64.13           O  
ANISOU 2086  OG  SER B 256    11657   5666   7043    -97  -1177    573       O  
ATOM   2087  N   TRP B 257       1.408 -40.879 -33.234  1.00 53.73           N  
ANISOU 2087  N   TRP B 257    10304   4003   6107  -1426   -512    361       N  
ATOM   2088  CA  TRP B 257       0.027 -40.443 -33.421  1.00 53.95           C  
ANISOU 2088  CA  TRP B 257    10065   4374   6056  -1721   -454   -144       C  
ATOM   2089  C   TRP B 257      -0.205 -39.874 -34.816  1.00 54.15           C  
ANISOU 2089  C   TRP B 257     9972   4443   6157  -2053   -795    -38       C  
ATOM   2090  O   TRP B 257      -1.206 -40.193 -35.460  1.00 57.79           O  
ANISOU 2090  O   TRP B 257    10190   5025   6741  -2377   -850   -778       O  
ATOM   2091  CB  TRP B 257      -0.352 -39.408 -32.365  1.00 48.73           C  
ANISOU 2091  CB  TRP B 257     9085   4007   5423  -2095   -800     74       C  
ATOM   2092  CG  TRP B 257      -1.616 -38.663 -32.675  1.00 50.19           C  
ANISOU 2092  CG  TRP B 257     9144   4296   5628  -2038   -831    139       C  
ATOM   2093  CD1 TRP B 257      -2.897 -39.129 -32.547  1.00 51.12           C  
ANISOU 2093  CD1 TRP B 257     9230   5022   5168  -2181   -741    217       C  
ATOM   2094  CD2 TRP B 257      -1.723 -37.321 -33.172  1.00 48.81           C  
ANISOU 2094  CD2 TRP B 257     8806   4190   5549  -2201   -715    -46       C  
ATOM   2095  NE1 TRP B 257      -3.792 -38.158 -32.927  1.00 52.62           N  
ANISOU 2095  NE1 TRP B 257     9345   5170   5477  -2211   -648    461       N  
ATOM   2096  CE2 TRP B 257      -3.101 -37.038 -33.314  1.00 51.63           C  
ANISOU 2096  CE2 TRP B 257     8999   4802   5815  -2275  -1235      8       C  
ATOM   2097  CE3 TRP B 257      -0.787 -36.327 -33.509  1.00 45.58           C  
ANISOU 2097  CE3 TRP B 257     8488   3918   4910  -1861   -613    -67       C  
ATOM   2098  CZ2 TRP B 257      -3.570 -35.798 -33.772  1.00 53.43           C  
ANISOU 2098  CZ2 TRP B 257     9227   4849   6224  -2285  -1250    106       C  
ATOM   2099  CZ3 TRP B 257      -1.252 -35.094 -33.972  1.00 46.05           C  
ANISOU 2099  CZ3 TRP B 257     8520   4190   4785  -1929   -771     59       C  
ATOM   2100  CH2 TRP B 257      -2.632 -34.844 -34.105  1.00 51.27           C  
ANISOU 2100  CH2 TRP B 257     8609   5407   5464  -2131   -721   -191       C  
ATOM   2101  N   PHE B 258       0.726 -39.036 -35.266  1.00 50.34           N  
ANISOU 2101  N   PHE B 258     9608   4057   5460  -1904  -1154   -317       N  
ATOM   2102  CA  PHE B 258       0.641 -38.403 -36.574  1.00 49.19           C  
ANISOU 2102  CA  PHE B 258     9175   4294   5220  -1810   -982   -403       C  
ATOM   2103  C   PHE B 258       0.649 -39.441 -37.705  1.00 54.24           C  
ANISOU 2103  C   PHE B 258    10423   4466   5720  -1764   -775   -789       C  
ATOM   2104  O   PHE B 258      -0.254 -39.437 -38.547  1.00 56.00           O  
ANISOU 2104  O   PHE B 258    10249   5033   5995  -1552   -739   -930       O  
ATOM   2105  CB  PHE B 258       1.751 -37.353 -36.755  1.00 48.30           C  
ANISOU 2105  CB  PHE B 258     9293   4057   5001  -1751   -495   -737       C  
ATOM   2106  CG  PHE B 258       1.655 -36.594 -38.046  1.00 56.91           C  
ANISOU 2106  CG  PHE B 258    10403   5472   5747  -1630   -663    208       C  
ATOM   2107  CD1 PHE B 258       0.641 -35.657 -38.251  1.00 55.86           C  
ANISOU 2107  CD1 PHE B 258    10651   4456   6114  -1758   -272   -576       C  
ATOM   2108  CD2 PHE B 258       2.559 -36.834 -39.078  1.00 65.24           C  
ANISOU 2108  CD2 PHE B 258    10427   6920   7438   -842    173    -61       C  
ATOM   2109  CE1 PHE B 258       0.543 -34.961 -39.457  1.00 57.32           C  
ANISOU 2109  CE1 PHE B 258    10691   5041   6046  -1280   -958   -642       C  
ATOM   2110  CE2 PHE B 258       2.465 -36.142 -40.285  1.00 68.60           C  
ANISOU 2110  CE2 PHE B 258    11034   7640   7390  -1280     53     64       C  
ATOM   2111  CZ  PHE B 258       1.459 -35.200 -40.473  1.00 62.30           C  
ANISOU 2111  CZ  PHE B 258    10601   6742   6325  -2001   -428    -47       C  
ATOM   2112  N   CYS B 259       1.650 -40.328 -37.699  1.00 57.99           N  
ANISOU 2112  N   CYS B 259    10917   4849   6267  -1385  -1313   -401       N  
ATOM   2113  CA  CYS B 259       1.794 -41.402 -38.704  1.00 61.65           C  
ANISOU 2113  CA  CYS B 259    11606   5419   6399  -1620  -1087   -898       C  
ATOM   2114  C   CYS B 259       0.641 -42.398 -38.727  1.00 65.52           C  
ANISOU 2114  C   CYS B 259    12273   5320   7301  -1845   -404   -653       C  
ATOM   2115  O   CYS B 259       0.174 -42.781 -39.803  1.00 70.64           O  
ANISOU 2115  O   CYS B 259    12765   6436   7636  -1442   -997   -716       O  
ATOM   2116  CB  CYS B 259       3.095 -42.175 -38.497  1.00 66.75           C  
ANISOU 2116  CB  CYS B 259    12276   5770   7313   -878  -1137   -839       C  
ATOM   2117  SG  CYS B 259       4.578 -41.241 -38.905  1.00 76.51           S  
ANISOU 2117  SG  CYS B 259    12924   8250   7893  -1447   -583   -353       S  
ATOM   2118  N   ASP B 260       0.198 -42.823 -37.545  1.00 60.71           N  
ANISOU 2118  N   ASP B 260    12143   4195   6728  -1623  -1118   -599       N  
ATOM   2119  CA  ASP B 260      -0.845 -43.838 -37.429  1.00 64.90           C  
ANISOU 2119  CA  ASP B 260    12087   5225   7346  -2106   -853   -426       C  
ATOM   2120  C   ASP B 260      -2.244 -43.320 -37.752  1.00 65.45           C  
ANISOU 2120  C   ASP B 260    12093   5642   7131  -2210   -852   -666       C  
ATOM   2121  O   ASP B 260      -2.980 -43.967 -38.497  1.00 70.62           O  
ANISOU 2121  O   ASP B 260    12261   6367   8203  -2764   -837   -449       O  
ATOM   2122  CB  ASP B 260      -0.824 -44.488 -36.038  1.00 65.53           C  
ANISOU 2122  CB  ASP B 260    12425   4889   7583  -2467   -536   -173       C  
ATOM   2123  CG  ASP B 260       0.465 -45.272 -35.761  1.00 72.78           C  
ANISOU 2123  CG  ASP B 260    13339   5960   8352  -1565   -696   -458       C  
ATOM   2124  OD1 ASP B 260       1.317 -45.433 -36.665  1.00 72.24           O  
ANISOU 2124  OD1 ASP B 260    13739   5206   8501   -326   -532    -86       O  
ATOM   2125  OD2 ASP B 260       0.626 -45.733 -34.612  1.00 78.25           O  
ANISOU 2125  OD2 ASP B 260    15674   5271   8784   -630  -1566   -616       O  
ATOM   2126  N   ASP B 261      -2.598 -42.153 -37.214  1.00 62.37           N  
ANISOU 2126  N   ASP B 261    11658   4960   7081  -2656  -1243   -258       N  
ATOM   2127  CA  ASP B 261      -3.991 -41.688 -37.225  1.00 69.58           C  
ANISOU 2127  CA  ASP B 261    11971   6477   7986  -2294  -1088    -94       C  
ATOM   2128  C   ASP B 261      -4.313 -40.531 -38.174  1.00 66.92           C  
ANISOU 2128  C   ASP B 261    11754   6410   7261  -2962  -1023   -159       C  
ATOM   2129  O   ASP B 261      -5.467 -40.367 -38.573  1.00 75.08           O  
ANISOU 2129  O   ASP B 261    11855   7835   8834  -3418  -1478    287       O  
ATOM   2130  CB  ASP B 261      -4.431 -41.293 -35.808  1.00 71.63           C  
ANISOU 2130  CB  ASP B 261    12467   6932   7815  -2913   -888    111       C  
ATOM   2131  CG  ASP B 261      -4.336 -42.439 -34.810  1.00 73.83           C  
ANISOU 2131  CG  ASP B 261    13274   6485   8290  -2638  -1085    -73       C  
ATOM   2132  OD1 ASP B 261      -4.340 -43.623 -35.215  1.00 73.22           O  
ANISOU 2132  OD1 ASP B 261    13004   6639   8175  -3684  -1763   -446       O  
ATOM   2133  OD2 ASP B 261      -4.260 -42.141 -33.600  1.00 71.74           O  
ANISOU 2133  OD2 ASP B 261    11827   7232   8198  -3696  -1109    343       O  
ATOM   2134  N   ILE B 262      -3.312 -39.728 -38.522  1.00 61.46           N  
ANISOU 2134  N   ILE B 262    11327   5335   6689  -2483  -1211   -193       N  
ATOM   2135  CA  ILE B 262      -3.564 -38.461 -39.211  1.00 57.51           C  
ANISOU 2135  CA  ILE B 262    10404   5281   6167  -2701  -1158   -395       C  
ATOM   2136  C   ILE B 262      -3.121 -38.491 -40.666  1.00 60.59           C  
ANISOU 2136  C   ILE B 262    10992   5880   6147  -2283  -1186  -1194       C  
ATOM   2137  O   ILE B 262      -3.916 -38.195 -41.565  1.00 59.02           O  
ANISOU 2137  O   ILE B 262    10323   5931   6170  -2001   -793   -928       O  
ATOM   2138  CB  ILE B 262      -2.905 -37.267 -38.462  1.00 55.56           C  
ANISOU 2138  CB  ILE B 262    10567   4728   5813  -2228  -1107    -95       C  
ATOM   2139  CG1 ILE B 262      -3.396 -37.189 -37.003  1.00 59.69           C  
ANISOU 2139  CG1 ILE B 262    10576   6063   6039  -2663   -852   -371       C  
ATOM   2140  CG2 ILE B 262      -3.108 -35.950 -39.209  1.00 48.85           C  
ANISOU 2140  CG2 ILE B 262     9570   4213   4776  -2678  -1732   -769       C  
ATOM   2141  CD1 ILE B 262      -4.906 -37.119 -36.808  1.00 64.00           C  
ANISOU 2141  CD1 ILE B 262    10667   7150   6499  -2920   -528   -966       C  
ATOM   2142  N   LEU B 263      -1.853 -38.847 -40.873  1.00 62.82           N  
ANISOU 2142  N   LEU B 263    11480   6055   6332  -2183   -906  -1944       N  
ATOM   2143  CA  LEU B 263      -1.192 -38.766 -42.173  1.00 63.52           C  
ANISOU 2143  CA  LEU B 263    11369   6186   6577  -2466   -739   -915       C  
ATOM   2144  C   LEU B 263      -1.985 -39.447 -43.293  1.00 62.56           C  
ANISOU 2144  C   LEU B 263    11741   5599   6428  -2248   -737   -912       C  
ATOM   2145  O   LEU B 263      -2.274 -40.648 -43.230  1.00 59.52           O  
ANISOU 2145  O   LEU B 263    10911   5580   6124  -2441   -932   -843       O  
ATOM   2146  CB  LEU B 263       0.234 -39.323 -42.081  1.00 64.95           C  
ANISOU 2146  CB  LEU B 263    11665   6015   6995  -2029   -749   -386       C  
ATOM   2147  CG  LEU B 263       1.096 -39.276 -43.348  1.00 70.68           C  
ANISOU 2147  CG  LEU B 263    12134   6970   7751  -2013   -136   -321       C  
ATOM   2148  CD1 LEU B 263       1.599 -37.868 -43.654  1.00 67.58           C  
ANISOU 2148  CD1 LEU B 263    11192   6569   7916  -1764  -1184   -590       C  
ATOM   2149  CD2 LEU B 263       2.252 -40.251 -43.209  1.00 77.29           C  
ANISOU 2149  CD2 LEU B 263    13168   7225   8974  -1201     54    142       C  
ATOM   2150  N   SER B 264      -2.346 -38.647 -44.294  1.00 66.47           N  
ANISOU 2150  N   SER B 264    12167   6525   6564  -2162   -781   -529       N  
ATOM   2151  CA  SER B 264      -3.124 -39.094 -45.455  1.00 71.23           C  
ANISOU 2151  CA  SER B 264    12624   7275   7163  -2529  -1067  -1246       C  
ATOM   2152  C   SER B 264      -2.336 -38.792 -46.739  1.00 75.99           C  
ANISOU 2152  C   SER B 264    13191   8027   7653  -2503   -650   -832       C  
ATOM   2153  O   SER B 264      -1.497 -37.886 -46.729  1.00 72.03           O  
ANISOU 2153  O   SER B 264    13167   7819   6379  -2168   -611  -1702       O  
ATOM   2154  CB  SER B 264      -4.490 -38.401 -45.467  1.00 71.91           C  
ANISOU 2154  CB  SER B 264    12326   7689   7306  -2556  -1399   -665       C  
ATOM   2155  OG  SER B 264      -5.248 -38.760 -44.324  1.00 72.86           O  
ANISOU 2155  OG  SER B 264    11739   7240   8702  -3053  -1526    546       O  
ATOM   2156  N   PRO B 265      -2.596 -39.544 -47.842  1.00 82.76           N  
ANISOU 2156  N   PRO B 265    14497   8713   8234  -2557   -833  -1365       N  
ATOM   2157  CA  PRO B 265      -1.724 -39.470 -49.034  1.00 82.61           C  
ANISOU 2157  CA  PRO B 265    14039   8791   8558  -3163   -964   -819       C  
ATOM   2158  C   PRO B 265      -1.457 -38.092 -49.682  1.00 77.90           C  
ANISOU 2158  C   PRO B 265    13571   8370   7656  -1815  -1452   -803       C  
ATOM   2159  O   PRO B 265      -0.313 -37.622 -49.649  1.00 88.57           O  
ANISOU 2159  O   PRO B 265    14121   9584   9947  -2581   -478  -1246       O  
ATOM   2160  CB  PRO B 265      -2.410 -40.406 -50.049  1.00 82.48           C  
ANISOU 2160  CB  PRO B 265    15337   8188   7811  -2246   -309  -1900       C  
ATOM   2161  CG  PRO B 265      -3.784 -40.646 -49.518  1.00 85.84           C  
ANISOU 2161  CG  PRO B 265    14711   8872   9030  -2154   -932  -1630       C  
ATOM   2162  CD  PRO B 265      -3.662 -40.551 -48.028  1.00 86.09           C  
ANISOU 2162  CD  PRO B 265    14459   9191   9061  -2792   -967  -1001       C  
ATOM   2163  N   ASN B 266      -2.489 -37.456 -50.235  1.00 61.42           N  
ANISOU 2163  N   ASN B 266    11816   5767   5753  -3520  -1378  -1504       N  
ATOM   2164  CA  ASN B 266      -2.326 -36.240 -51.037  1.00 61.15           C  
ANISOU 2164  CA  ASN B 266    11175   6374   5685  -2157   -760   -941       C  
ATOM   2165  C   ASN B 266      -2.650 -34.992 -50.216  1.00 55.06           C  
ANISOU 2165  C   ASN B 266    10357   5853   4709  -2896   -888   -541       C  
ATOM   2166  O   ASN B 266      -3.408 -34.130 -50.655  1.00 58.27           O  
ANISOU 2166  O   ASN B 266    10900   5896   5343  -2487   -755   -481       O  
ATOM   2167  CB  ASN B 266      -3.183 -36.283 -52.315  1.00 69.60           C  
ANISOU 2167  CB  ASN B 266    12158   8051   6235  -3130  -1266   -996       C  
ATOM   2168  CG  ASN B 266      -2.771 -37.393 -53.265  1.00 79.34           C  
ANISOU 2168  CG  ASN B 266    13892   8847   7407  -2509   -903  -1629       C  
ATOM   2169  OD1 ASN B 266      -1.590 -37.565 -53.576  1.00 82.78           O  
ANISOU 2169  OD1 ASN B 266    13598  10351   7504  -2829  -1582  -2490       O  
ATOM   2170  ND2 ASN B 266      -3.753 -38.144 -53.749  1.00 85.00           N  
ANISOU 2170  ND2 ASN B 266    14261   9106   8927  -3088   -877  -1598       N  
ATOM   2171  N   THR B 267      -2.067 -34.912 -49.023  1.00 52.30           N  
ANISOU 2171  N   THR B 267     9422   5586   4862  -2835   -975   -799       N  
ATOM   2172  CA  THR B 267      -2.327 -33.831 -48.082  1.00 56.15           C  
ANISOU 2172  CA  THR B 267    10164   6020   5148  -2525   -780   -800       C  
ATOM   2173  C   THR B 267      -0.998 -33.176 -47.682  1.00 56.08           C  
ANISOU 2173  C   THR B 267     9949   5806   5550  -2371   -902   -620       C  
ATOM   2174  O   THR B 267       0.009 -33.878 -47.524  1.00 51.19           O  
ANISOU 2174  O   THR B 267     9675   5700   4072  -2413  -1106   -243       O  
ATOM   2175  CB  THR B 267      -3.068 -34.368 -46.823  1.00 56.24           C  
ANISOU 2175  CB  THR B 267    10333   5635   5397  -2734   -889   -420       C  
ATOM   2176  OG1 THR B 267      -4.223 -35.124 -47.216  1.00 60.43           O  
ANISOU 2176  OG1 THR B 267    10655   6286   6019  -3136  -1265   -491       O  
ATOM   2177  CG2 THR B 267      -3.517 -33.238 -45.914  1.00 50.32           C  
ANISOU 2177  CG2 THR B 267     8544   6230   4344  -2754   -633   -246       C  
ATOM   2178  N   ASN B 268      -1.000 -31.842 -47.550  1.00 53.02           N  
ANISOU 2178  N   ASN B 268     9565   5665   4914  -2472   -725    -11       N  
ATOM   2179  CA  ASN B 268       0.124 -31.099 -46.982  1.00 54.80           C  
ANISOU 2179  CA  ASN B 268     9717   6043   5062  -2791  -1084   -525       C  
ATOM   2180  C   ASN B 268      -0.147 -30.660 -45.552  1.00 57.78           C  
ANISOU 2180  C   ASN B 268    10059   6795   5099  -2452   -870   -198       C  
ATOM   2181  O   ASN B 268      -1.282 -30.295 -45.211  1.00 61.24           O  
ANISOU 2181  O   ASN B 268     9916   6381   6970  -2765   -868   -574       O  
ATOM   2182  CB  ASN B 268       0.469 -29.866 -47.827  1.00 60.91           C  
ANISOU 2182  CB  ASN B 268    11279   6444   5417  -2607  -1169   -123       C  
ATOM   2183  CG  ASN B 268       1.118 -30.219 -49.154  1.00 71.34           C  
ANISOU 2183  CG  ASN B 268    11278   8872   6955  -2420    243   -293       C  
ATOM   2184  OD1 ASN B 268       1.827 -31.220 -49.280  1.00 76.47           O  
ANISOU 2184  OD1 ASN B 268    12067   9048   7937  -1919  -1125   -133       O  
ATOM   2185  ND2 ASN B 268       0.883 -29.382 -50.156  1.00 76.79           N  
ANISOU 2185  ND2 ASN B 268    12295  10093   6789  -2595    401    114       N  
ATOM   2186  N   TYR B 269       0.909 -30.667 -44.736  1.00 47.69           N  
ANISOU 2186  N   TYR B 269     8989   5177   3953  -2074   -334   -297       N  
ATOM   2187  CA  TYR B 269       0.803 -30.389 -43.307  1.00 44.65           C  
ANISOU 2187  CA  TYR B 269     8163   4712   4090  -2268   -734   -223       C  
ATOM   2188  C   TYR B 269       1.809 -29.330 -42.883  1.00 44.75           C  
ANISOU 2188  C   TYR B 269     8161   4205   4636  -3209  -1462  -1500       C  
ATOM   2189  O   TYR B 269       3.005 -29.416 -43.190  1.00 50.46           O  
ANISOU 2189  O   TYR B 269     8544   6028   4598  -2535   -895   -234       O  
ATOM   2190  CB  TYR B 269       1.011 -31.662 -42.483  1.00 47.64           C  
ANISOU 2190  CB  TYR B 269     8685   4846   4570  -2048   -858    -68       C  
ATOM   2191  CG  TYR B 269       0.030 -32.765 -42.783  1.00 52.46           C  
ANISOU 2191  CG  TYR B 269     9417   5175   5340  -2270  -1020   -332       C  
ATOM   2192  CD1 TYR B 269      -1.191 -32.848 -42.097  1.00 52.93           C  
ANISOU 2192  CD1 TYR B 269     9496   5161   5451  -2431   -761   -331       C  
ATOM   2193  CD2 TYR B 269       0.321 -33.739 -43.747  1.00 53.67           C  
ANISOU 2193  CD2 TYR B 269     9595   5613   5181  -2284   -563   -502       C  
ATOM   2194  CE1 TYR B 269      -2.102 -33.863 -42.376  1.00 54.17           C  
ANISOU 2194  CE1 TYR B 269     9896   5356   5329  -2256  -1161   -225       C  
ATOM   2195  CE2 TYR B 269      -0.578 -34.759 -44.034  1.00 56.42           C  
ANISOU 2195  CE2 TYR B 269    10350   5589   5495  -2203   -784   -337       C  
ATOM   2196  CZ  TYR B 269      -1.785 -34.824 -43.345  1.00 55.06           C  
ANISOU 2196  CZ  TYR B 269     9812   5519   5587  -2604  -1165   -783       C  
ATOM   2197  OH  TYR B 269      -2.673 -35.844 -43.631  1.00 54.77           O  
ANISOU 2197  OH  TYR B 269    10001   5170   5636  -2275  -1484   -155       O  
ATOM   2198  N   GLU B 270       1.300 -28.326 -42.182  1.00 51.15           N  
ANISOU 2198  N   GLU B 270     9220   5416   4799  -1884   -812    -45       N  
ATOM   2199  CA  GLU B 270       2.114 -27.252 -41.654  1.00 47.24           C  
ANISOU 2199  CA  GLU B 270     8247   5255   4447  -2448   -590   -302       C  
ATOM   2200  C   GLU B 270       2.056 -27.349 -40.140  1.00 43.57           C  
ANISOU 2200  C   GLU B 270     7703   4456   4396  -1704   -656    -72       C  
ATOM   2201  O   GLU B 270       1.064 -26.957 -39.525  1.00 42.52           O  
ANISOU 2201  O   GLU B 270     7494   4599   4063  -1722   -551    153       O  
ATOM   2202  CB  GLU B 270       1.564 -25.920 -42.146  1.00 57.77           C  
ANISOU 2202  CB  GLU B 270    10141   6110   5699  -1771   -601    637       C  
ATOM   2203  CG  GLU B 270       2.537 -24.765 -42.071  1.00 67.87           C  
ANISOU 2203  CG  GLU B 270    10439   7772   7576  -2796   -591    103       C  
ATOM   2204  CD  GLU B 270       2.087 -23.614 -42.944  1.00 78.43           C  
ANISOU 2204  CD  GLU B 270    12680   8663   8456  -1889   -314    772       C  
ATOM   2205  OE1 GLU B 270       2.260 -23.703 -44.183  1.00 86.22           O  
ANISOU 2205  OE1 GLU B 270    13306  10937   8517  -2275    -29   1064       O  
ATOM   2206  OE2 GLU B 270       1.545 -22.632 -42.394  1.00 77.62           O  
ANISOU 2206  OE2 GLU B 270    13251   8258   7981  -3064   -723   -420       O  
ATOM   2207  N   VAL B 271       3.117 -27.889 -39.547  1.00 43.09           N  
ANISOU 2207  N   VAL B 271     7408   4756   4206  -1778   -723   -247       N  
ATOM   2208  CA  VAL B 271       3.128 -28.232 -38.121  1.00 41.21           C  
ANISOU 2208  CA  VAL B 271     7215   4120   4323  -1748   -361    -43       C  
ATOM   2209  C   VAL B 271       4.025 -27.283 -37.322  1.00 42.33           C  
ANISOU 2209  C   VAL B 271     7207   4582   4293  -1854   -325   -506       C  
ATOM   2210  O   VAL B 271       5.160 -27.005 -37.718  1.00 40.48           O  
ANISOU 2210  O   VAL B 271     6939   4306   4134  -1798   -428   -288       O  
ATOM   2211  CB  VAL B 271       3.570 -29.702 -37.882  1.00 38.11           C  
ANISOU 2211  CB  VAL B 271     6969   3841   3670  -1788   -548   -314       C  
ATOM   2212  CG1 VAL B 271       3.497 -30.061 -36.401  1.00 37.75           C  
ANISOU 2212  CG1 VAL B 271     6789   3786   3768  -1456   -198   -191       C  
ATOM   2213  CG2 VAL B 271       2.708 -30.671 -38.687  1.00 39.70           C  
ANISOU 2213  CG2 VAL B 271     7085   3952   4047  -1791   -355   -229       C  
ATOM   2214  N   THR B 272       3.498 -26.785 -36.205  1.00 39.56           N  
ANISOU 2214  N   THR B 272     6845   4540   3646  -1480   -733    157       N  
ATOM   2215  CA  THR B 272       4.285 -25.995 -35.256  1.00 38.16           C  
ANISOU 2215  CA  THR B 272     6610   3877   4010  -1725   -530     38       C  
ATOM   2216  C   THR B 272       4.306 -26.689 -33.891  1.00 38.48           C  
ANISOU 2216  C   THR B 272     6412   4127   4079  -1471   -519    156       C  
ATOM   2217  O   THR B 272       3.246 -27.041 -33.354  1.00 37.96           O  
ANISOU 2217  O   THR B 272     6444   3767   4211  -1531   -552    177       O  
ATOM   2218  CB  THR B 272       3.738 -24.556 -35.110  1.00 37.61           C  
ANISOU 2218  CB  THR B 272     6387   3982   3920  -1461   -477    -24       C  
ATOM   2219  OG1 THR B 272       3.682 -23.937 -36.393  1.00 40.87           O  
ANISOU 2219  OG1 THR B 272     6884   4570   4073  -1241   -894    104       O  
ATOM   2220  CG2 THR B 272       4.658 -23.699 -34.228  1.00 37.37           C  
ANISOU 2220  CG2 THR B 272     6309   3798   4091  -1678   -845    175       C  
ATOM   2221  N   TRP B 273       5.509 -26.891 -33.350  1.00 35.82           N  
ANISOU 2221  N   TRP B 273     6058   3647   3904  -1357   -280    207       N  
ATOM   2222  CA  TRP B 273       5.682 -27.345 -31.971  1.00 35.65           C  
ANISOU 2222  CA  TRP B 273     5691   3947   3907  -1045   -216     93       C  
ATOM   2223  C   TRP B 273       6.114 -26.216 -31.056  1.00 37.26           C  
ANISOU 2223  C   TRP B 273     5891   4059   4205  -1138   -200    -54       C  
ATOM   2224  O   TRP B 273       6.935 -25.377 -31.434  1.00 36.44           O  
ANISOU 2224  O   TRP B 273     5983   3796   4063  -1157   -571    -11       O  
ATOM   2225  CB  TRP B 273       6.758 -28.423 -31.860  1.00 34.71           C  
ANISOU 2225  CB  TRP B 273     6031   3285   3873  -1110   -540    135       C  
ATOM   2226  CG  TRP B 273       6.436 -29.741 -32.479  1.00 36.56           C  
ANISOU 2226  CG  TRP B 273     6302   3574   4014  -1193   -324   -179       C  
ATOM   2227  CD1 TRP B 273       5.253 -30.132 -33.051  1.00 36.22           C  
ANISOU 2227  CD1 TRP B 273     6369   3591   3801  -1376   -327   -208       C  
ATOM   2228  CD2 TRP B 273       7.308 -30.862 -32.551  1.00 38.78           C  
ANISOU 2228  CD2 TRP B 273     6695   3709   4329   -901   -107   -355       C  
ATOM   2229  NE1 TRP B 273       5.348 -31.424 -33.490  1.00 38.74           N  
ANISOU 2229  NE1 TRP B 273     6890   3549   4280  -1126   -471   -155       N  
ATOM   2230  CE2 TRP B 273       6.596 -31.903 -33.196  1.00 40.28           C  
ANISOU 2230  CE2 TRP B 273     6744   3993   4567  -1156   -174   -364       C  
ATOM   2231  CE3 TRP B 273       8.628 -31.094 -32.139  1.00 38.98           C  
ANISOU 2231  CE3 TRP B 273     6585   3782   4443   -750    140   -456       C  
ATOM   2232  CZ2 TRP B 273       7.163 -33.161 -33.441  1.00 41.17           C  
ANISOU 2232  CZ2 TRP B 273     7100   4023   4517   -918   -259   -378       C  
ATOM   2233  CZ3 TRP B 273       9.190 -32.351 -32.382  1.00 39.37           C  
ANISOU 2233  CZ3 TRP B 273     6649   3752   4556   -684    347   -275       C  
ATOM   2234  CH2 TRP B 273       8.456 -33.362 -33.034  1.00 41.59           C  
ANISOU 2234  CH2 TRP B 273     7067   4039   4697   -688   -309   -398       C  
ATOM   2235  N   TYR B 274       5.580 -26.239 -29.840  1.00 35.91           N  
ANISOU 2235  N   TYR B 274     5652   4005   3988   -988   -518    -80       N  
ATOM   2236  CA  TYR B 274       6.074 -25.424 -28.748  1.00 32.98           C  
ANISOU 2236  CA  TYR B 274     5267   3515   3746  -1221   -339    187       C  
ATOM   2237  C   TYR B 274       6.466 -26.380 -27.632  1.00 34.81           C  
ANISOU 2237  C   TYR B 274     5238   3885   4101   -871   -252    331       C  
ATOM   2238  O   TYR B 274       5.608 -26.973 -26.949  1.00 34.01           O  
ANISOU 2238  O   TYR B 274     5158   3696   4065   -875   -221    410       O  
ATOM   2239  CB  TYR B 274       5.017 -24.422 -28.282  1.00 37.15           C  
ANISOU 2239  CB  TYR B 274     5447   4395   4270   -832   -487    198       C  
ATOM   2240  CG  TYR B 274       4.478 -23.510 -29.375  1.00 37.38           C  
ANISOU 2240  CG  TYR B 274     5664   4167   4372  -1012   -462    367       C  
ATOM   2241  CD1 TYR B 274       3.359 -23.882 -30.132  1.00 38.26           C  
ANISOU 2241  CD1 TYR B 274     5973   4282   4282  -1240   -523    122       C  
ATOM   2242  CD2 TYR B 274       5.070 -22.271 -29.635  1.00 37.90           C  
ANISOU 2242  CD2 TYR B 274     5661   4391   4347  -1238   -409    263       C  
ATOM   2243  CE1 TYR B 274       2.853 -23.049 -31.132  1.00 39.82           C  
ANISOU 2243  CE1 TYR B 274     6196   4397   4536  -1270   -601    278       C  
ATOM   2244  CE2 TYR B 274       4.573 -21.428 -30.630  1.00 37.29           C  
ANISOU 2244  CE2 TYR B 274     5506   4318   4345  -1230   -328    349       C  
ATOM   2245  CZ  TYR B 274       3.465 -21.822 -31.375  1.00 39.79           C  
ANISOU 2245  CZ  TYR B 274     6251   4576   4290  -1467   -720    316       C  
ATOM   2246  OH  TYR B 274       2.960 -20.997 -32.357  1.00 39.72           O  
ANISOU 2246  OH  TYR B 274     6363   4425   4300  -1367   -887    174       O  
ATOM   2247  N   THR B 275       7.770 -26.555 -27.469  1.00 32.14           N  
ANISOU 2247  N   THR B 275     4880   3438   3892   -960   -187    -69       N  
ATOM   2248  CA  THR B 275       8.293 -27.539 -26.529  1.00 33.35           C  
ANISOU 2248  CA  THR B 275     5108   3693   3868   -820    -19    158       C  
ATOM   2249  C   THR B 275       8.965 -26.878 -25.323  1.00 33.60           C  
ANISOU 2249  C   THR B 275     5017   3693   4056   -766    -95     -7       C  
ATOM   2250  O   THR B 275       9.650 -25.855 -25.458  1.00 31.36           O  
ANISOU 2250  O   THR B 275     4411   3691   3813   -718   -292   -226       O  
ATOM   2251  CB  THR B 275       9.318 -28.479 -27.190  1.00 35.73           C  
ANISOU 2251  CB  THR B 275     5225   4096   4255   -624    150   -110       C  
ATOM   2252  OG1 THR B 275      10.407 -27.698 -27.677  1.00 35.54           O  
ANISOU 2252  OG1 THR B 275     5430   4103   3969   -821    179    -19       O  
ATOM   2253  CG2 THR B 275       8.721 -29.243 -28.357  1.00 41.76           C  
ANISOU 2253  CG2 THR B 275     6332   4721   4814   -982   -593   -115       C  
ATOM   2254  N   SER B 276       8.777 -27.475 -24.155  1.00 34.41           N  
ANISOU 2254  N   SER B 276     5135   3830   4108   -572   -109    121       N  
ATOM   2255  CA  SER B 276       9.397 -26.957 -22.933  1.00 35.27           C  
ANISOU 2255  CA  SER B 276     4640   4487   4270   -354   -167    142       C  
ATOM   2256  C   SER B 276      10.918 -27.207 -22.915  1.00 31.51           C  
ANISOU 2256  C   SER B 276     4431   3666   3874   -316    145    102       C  
ATOM   2257  O   SER B 276      11.677 -26.368 -22.455  1.00 31.73           O  
ANISOU 2257  O   SER B 276     4315   3938   3802      8     80   -346       O  
ATOM   2258  CB  SER B 276       8.706 -27.540 -21.702  1.00 32.38           C  
ANISOU 2258  CB  SER B 276     4127   3872   4303   -240     39    -99       C  
ATOM   2259  OG  SER B 276       8.899 -28.940 -21.617  1.00 34.44           O  
ANISOU 2259  OG  SER B 276     4673   3795   4617   -448   -182     11       O  
ATOM   2260  N   TRP B 277      11.342 -28.354 -23.441  1.00 33.20           N  
ANISOU 2260  N   TRP B 277     4622   4014   3979   -161    279    -58       N  
ATOM   2261  CA  TRP B 277      12.759 -28.707 -23.605  1.00 31.87           C  
ANISOU 2261  CA  TRP B 277     4485   3816   3808   -112    117   -111       C  
ATOM   2262  C   TRP B 277      12.994 -29.026 -25.083  1.00 35.75           C  
ANISOU 2262  C   TRP B 277     5245   4403   3933   -123    329    -52       C  
ATOM   2263  O   TRP B 277      12.108 -29.601 -25.736  1.00 37.05           O  
ANISOU 2263  O   TRP B 277     5540   4222   4314   -139    325   -365       O  
ATOM   2264  CB  TRP B 277      13.091 -29.980 -22.816  1.00 35.30           C  
ANISOU 2264  CB  TRP B 277     4832   4242   4336    -60    152    220       C  
ATOM   2265  CG  TRP B 277      13.444 -29.878 -21.334  1.00 37.04           C  
ANISOU 2265  CG  TRP B 277     4845   4722   4507     76     68     82       C  
ATOM   2266  CD1 TRP B 277      12.842 -30.560 -20.318  1.00 36.74           C  
ANISOU 2266  CD1 TRP B 277     4890   4523   4543    710    247    176       C  
ATOM   2267  CD2 TRP B 277      14.507 -29.120 -20.729  1.00 34.54           C  
ANISOU 2267  CD2 TRP B 277     4351   4492   4279    448    436   -225       C  
ATOM   2268  NE1 TRP B 277      13.441 -30.263 -19.120  1.00 37.97           N  
ANISOU 2268  NE1 TRP B 277     5173   4543   4710    429    214     66       N  
ATOM   2269  CE2 TRP B 277      14.470 -29.387 -19.338  1.00 38.34           C  
ANISOU 2269  CE2 TRP B 277     4993   5090   4484    335    381     29       C  
ATOM   2270  CE3 TRP B 277      15.471 -28.221 -21.220  1.00 32.93           C  
ANISOU 2270  CE3 TRP B 277     3961   4538   4011    627    549   -386       C  
ATOM   2271  CZ2 TRP B 277      15.368 -28.796 -18.428  1.00 35.83           C  
ANISOU 2271  CZ2 TRP B 277     4545   4685   4382    591    428     59       C  
ATOM   2272  CZ3 TRP B 277      16.379 -27.642 -20.317  1.00 32.50           C  
ANISOU 2272  CZ3 TRP B 277     4149   4317   3880    648    657   -572       C  
ATOM   2273  CH2 TRP B 277      16.312 -27.931 -18.933  1.00 32.71           C  
ANISOU 2273  CH2 TRP B 277     3828   4725   3875    824    689   -452       C  
ATOM   2274  N   SER B 278      14.173 -28.684 -25.616  1.00 34.74           N  
ANISOU 2274  N   SER B 278     4690   4455   4055    502    182   -144       N  
ATOM   2275  CA  SER B 278      14.537 -29.092 -26.972  1.00 38.49           C  
ANISOU 2275  CA  SER B 278     5590   4735   4298    128    461   -375       C  
ATOM   2276  C   SER B 278      14.827 -30.613 -27.002  1.00 39.38           C  
ANISOU 2276  C   SER B 278     6044   4569   4348   -123     63   -451       C  
ATOM   2277  O   SER B 278      15.100 -31.205 -25.956  1.00 39.19           O  
ANISOU 2277  O   SER B 278     5617   4963   4309    320      2   -695       O  
ATOM   2278  CB  SER B 278      15.721 -28.266 -27.513  1.00 39.47           C  
ANISOU 2278  CB  SER B 278     5562   4505   4928    -75    306   -334       C  
ATOM   2279  OG  SER B 278      16.866 -28.443 -26.714  1.00 40.29           O  
ANISOU 2279  OG  SER B 278     5449   4750   5108    224    431   -404       O  
ATOM   2280  N   PRO B 279      14.753 -31.250 -28.190  1.00 39.06           N  
ANISOU 2280  N   PRO B 279     6011   4581   4246    275    480   -435       N  
ATOM   2281  CA  PRO B 279      14.802 -32.722 -28.238  1.00 40.05           C  
ANISOU 2281  CA  PRO B 279     6328   4514   4375    149    423   -731       C  
ATOM   2282  C   PRO B 279      16.172 -33.332 -27.916  1.00 45.14           C  
ANISOU 2282  C   PRO B 279     6560   5196   5394    560    529   -643       C  
ATOM   2283  O   PRO B 279      17.195 -32.702 -28.177  1.00 43.16           O  
ANISOU 2283  O   PRO B 279     6532   4936   4930    708    880   -786       O  
ATOM   2284  CB  PRO B 279      14.433 -33.040 -29.694  1.00 41.16           C  
ANISOU 2284  CB  PRO B 279     6768   4643   4227    250    426   -561       C  
ATOM   2285  CG  PRO B 279      13.834 -31.793 -30.240  1.00 42.35           C  
ANISOU 2285  CG  PRO B 279     7035   4554   4501   -142    299   -499       C  
ATOM   2286  CD  PRO B 279      14.537 -30.680 -29.533  1.00 40.30           C  
ANISOU 2286  CD  PRO B 279     6484   4723   4104   -121    277   -456       C  
ATOM   2287  N   CYS B 280      16.170 -34.544 -27.348  1.00 45.03           N  
ANISOU 2287  N   CYS B 280     7103   5062   4944    382    610   -789       N  
ATOM   2288  CA  CYS B 280      17.381 -35.373 -27.205  1.00 51.47           C  
ANISOU 2288  CA  CYS B 280     7488   6153   5916    947    459   -726       C  
ATOM   2289  C   CYS B 280      17.867 -35.870 -28.588  1.00 53.60           C  
ANISOU 2289  C   CYS B 280     7810   6555   6001    957    283  -1223       C  
ATOM   2290  O   CYS B 280      17.107 -35.766 -29.562  1.00 47.37           O  
ANISOU 2290  O   CYS B 280     7711   4964   5323    896    790   -569       O  
ATOM   2291  CB  CYS B 280      17.123 -36.548 -26.246  1.00 54.19           C  
ANISOU 2291  CB  CYS B 280     7690   6474   6425     49   -632   -311       C  
ATOM   2292  SG  CYS B 280      16.013 -37.838 -26.858  1.00 47.23           S  
ANISOU 2292  SG  CYS B 280     7880   4807   5259    482    253   -548       S  
ATOM   2293  N   PRO B 281      19.126 -36.394 -28.690  1.00 52.03           N  
ANISOU 2293  N   PRO B 281     8039   5850   5880   1114    395  -1446       N  
ATOM   2294  CA  PRO B 281      19.632 -36.839 -30.003  1.00 56.08           C  
ANISOU 2294  CA  PRO B 281     8510   6791   6003   1049    823  -1378       C  
ATOM   2295  C   PRO B 281      18.809 -37.934 -30.686  1.00 53.03           C  
ANISOU 2295  C   PRO B 281     8501   6027   5620   1266    783  -1071       C  
ATOM   2296  O   PRO B 281      18.654 -37.894 -31.903  1.00 52.70           O  
ANISOU 2296  O   PRO B 281     8497   6110   5413    906   1431   -760       O  
ATOM   2297  CB  PRO B 281      21.063 -37.337 -29.709  1.00 57.25           C  
ANISOU 2297  CB  PRO B 281     8442   6915   6392   1663   1619  -1404       C  
ATOM   2298  CG  PRO B 281      21.175 -37.411 -28.233  1.00 52.70           C  
ANISOU 2298  CG  PRO B 281     7189   6275   6559   2730   1164  -1665       C  
ATOM   2299  CD  PRO B 281      20.201 -36.421 -27.677  1.00 54.87           C  
ANISOU 2299  CD  PRO B 281     8286   6178   6383   1308    475   -823       C  
ATOM   2300  N   GLU B 282      18.284 -38.887 -29.917  1.00 51.94           N  
ANISOU 2300  N   GLU B 282     8282   5692   5757   1419    986  -1223       N  
ATOM   2301  CA  GLU B 282      17.453 -39.961 -30.488  1.00 57.24           C  
ANISOU 2301  CA  GLU B 282     9097   6078   6573   1119    308  -1184       C  
ATOM   2302  C   GLU B 282      16.148 -39.398 -31.066  1.00 53.91           C  
ANISOU 2302  C   GLU B 282     9005   5633   5844    828    478  -1059       C  
ATOM   2303  O   GLU B 282      15.767 -39.732 -32.189  1.00 54.17           O  
ANISOU 2303  O   GLU B 282     9131   5412   6038   1095    640  -1438       O  
ATOM   2304  CB  GLU B 282      17.168 -41.063 -29.456  1.00 63.54           C  
ANISOU 2304  CB  GLU B 282    10456   6771   6913    946    268   -651       C  
ATOM   2305  CG  GLU B 282      18.370 -41.941 -29.105  1.00 75.29           C  
ANISOU 2305  CG  GLU B 282    11685   8346   8573   2115    416   -456       C  
ATOM   2306  CD  GLU B 282      19.453 -41.214 -28.305  1.00 81.78           C  
ANISOU 2306  CD  GLU B 282    11970   9519   9580   1729    793  -1318       C  
ATOM   2307  OE1 GLU B 282      20.646 -41.517 -28.524  1.00 88.52           O  
ANISOU 2307  OE1 GLU B 282    12905   9096  11632   4146   1438   -527       O  
ATOM   2308  OE2 GLU B 282      19.121 -40.338 -27.467  1.00 81.32           O  
ANISOU 2308  OE2 GLU B 282    11960   8975   9962   1505   1523   -669       O  
ATOM   2309  N   CYS B 283      15.488 -38.526 -30.305  1.00 52.83           N  
ANISOU 2309  N   CYS B 283     8504   5283   6285    894    353   -838       N  
ATOM   2310  CA  CYS B 283      14.258 -37.862 -30.761  1.00 48.21           C  
ANISOU 2310  CA  CYS B 283     8212   4914   5190    558    656   -802       C  
ATOM   2311  C   CYS B 283      14.513 -36.978 -31.981  1.00 47.47           C  
ANISOU 2311  C   CYS B 283     7988   5030   5017    471    294   -918       C  
ATOM   2312  O   CYS B 283      13.766 -37.040 -32.963  1.00 43.62           O  
ANISOU 2312  O   CYS B 283     7353   4229   4990    358    652  -1566       O  
ATOM   2313  CB  CYS B 283      13.608 -37.061 -29.629  1.00 44.93           C  
ANISOU 2313  CB  CYS B 283     7663   4424   4982    314    246   -819       C  
ATOM   2314  SG  CYS B 283      12.568 -38.061 -28.524  1.00 50.09           S  
ANISOU 2314  SG  CYS B 283     8169   5249   5613    240    169   -104       S  
ATOM   2315  N   ALA B 284      15.582 -36.185 -31.932  1.00 47.78           N  
ANISOU 2315  N   ALA B 284     7949   4834   5368    403    513   -934       N  
ATOM   2316  CA  ALA B 284      15.963 -35.353 -33.072  1.00 48.47           C  
ANISOU 2316  CA  ALA B 284     7619   5642   5155    370    757   -958       C  
ATOM   2317  C   ALA B 284      16.200 -36.213 -34.313  1.00 51.76           C  
ANISOU 2317  C   ALA B 284     8442   5819   5402    507    337  -1201       C  
ATOM   2318  O   ALA B 284      15.713 -35.880 -35.391  1.00 51.51           O  
ANISOU 2318  O   ALA B 284     8195   6140   5234    326    658   -651       O  
ATOM   2319  CB  ALA B 284      17.187 -34.520 -32.748  1.00 49.01           C  
ANISOU 2319  CB  ALA B 284     7490   5614   5515    312    662  -1053       C  
ATOM   2320  N   GLY B 285      16.920 -37.325 -34.135  1.00 49.52           N  
ANISOU 2320  N   GLY B 285     8328   5400   5084    494    805  -1407       N  
ATOM   2321  CA  GLY B 285      17.189 -38.287 -35.204  1.00 50.98           C  
ANISOU 2321  CA  GLY B 285     8896   5494   4978    454    554  -1264       C  
ATOM   2322  C   GLY B 285      15.940 -38.854 -35.849  1.00 53.80           C  
ANISOU 2322  C   GLY B 285     8720   5858   5862    641    514  -1437       C  
ATOM   2323  O   GLY B 285      15.854 -38.919 -37.077  1.00 59.40           O  
ANISOU 2323  O   GLY B 285     8933   7670   5964   1092    429  -1385       O  
ATOM   2324  N   GLU B 286      14.974 -39.256 -35.024  1.00 51.26           N  
ANISOU 2324  N   GLU B 286     9071   5123   5280    724    316  -1442       N  
ATOM   2325  CA  GLU B 286      13.705 -39.792 -35.522  1.00 52.61           C  
ANISOU 2325  CA  GLU B 286     9375   4985   5628    387    219  -1233       C  
ATOM   2326  C   GLU B 286      12.878 -38.729 -36.247  1.00 50.49           C  
ANISOU 2326  C   GLU B 286     9070   4991   5122     66    223  -1436       C  
ATOM   2327  O   GLU B 286      12.328 -38.994 -37.318  1.00 50.29           O  
ANISOU 2327  O   GLU B 286     8977   4834   5294   -170    337  -2231       O  
ATOM   2328  CB  GLU B 286      12.900 -40.432 -34.398  1.00 56.33           C  
ANISOU 2328  CB  GLU B 286    10124   5634   5645     62    400  -1125       C  
ATOM   2329  CG  GLU B 286      13.523 -41.713 -33.871  1.00 70.64           C  
ANISOU 2329  CG  GLU B 286    12080   6795   7963   1340   -342   -720       C  
ATOM   2330  CD  GLU B 286      12.651 -42.419 -32.855  1.00 88.72           C  
ANISOU 2330  CD  GLU B 286    13976   9105  10626   -438    394     46       C  
ATOM   2331  OE1 GLU B 286      11.472 -42.700 -33.168  1.00 96.65           O  
ANISOU 2331  OE1 GLU B 286    14693   9144  12884   -838   -892    322       O  
ATOM   2332  OE2 GLU B 286      13.153 -42.705 -31.746  1.00 96.36           O  
ANISOU 2332  OE2 GLU B 286    14458  10807  11347    554   -700   -703       O  
ATOM   2333  N   VAL B 287      12.815 -37.525 -35.679  1.00 46.56           N  
ANISOU 2333  N   VAL B 287     8424   4472   4793   -119    677   -802       N  
ATOM   2334  CA  VAL B 287      12.079 -36.431 -36.312  1.00 46.79           C  
ANISOU 2334  CA  VAL B 287     8190   4834   4753   -115    326   -871       C  
ATOM   2335  C   VAL B 287      12.718 -36.063 -37.664  1.00 49.84           C  
ANISOU 2335  C   VAL B 287     8628   5430   4879   -389    413   -652       C  
ATOM   2336  O   VAL B 287      12.010 -35.958 -38.669  1.00 50.93           O  
ANISOU 2336  O   VAL B 287     8092   6015   5243    -69    420   -738       O  
ATOM   2337  CB  VAL B 287      11.917 -35.205 -35.378  1.00 47.16           C  
ANISOU 2337  CB  VAL B 287     8383   4848   4686   -144    317   -853       C  
ATOM   2338  CG1 VAL B 287      11.167 -34.083 -36.083  1.00 47.02           C  
ANISOU 2338  CG1 VAL B 287     7646   4743   5474   -354     12   -808       C  
ATOM   2339  CG2 VAL B 287      11.169 -35.592 -34.109  1.00 44.49           C  
ANISOU 2339  CG2 VAL B 287     8080   3911   4910   -143    258   -629       C  
ATOM   2340  N   ALA B 288      14.046 -35.924 -37.692  1.00 49.47           N  
ANISOU 2340  N   ALA B 288     8589   5193   5013   -511    380  -1211       N  
ATOM   2341  CA  ALA B 288      14.770 -35.565 -38.925  1.00 54.38           C  
ANISOU 2341  CA  ALA B 288     8972   6482   5208   -237    819  -1375       C  
ATOM   2342  C   ALA B 288      14.571 -36.600 -40.043  1.00 56.79           C  
ANISOU 2342  C   ALA B 288     9620   6558   5399   -165    678  -1460       C  
ATOM   2343  O   ALA B 288      14.305 -36.232 -41.195  1.00 54.45           O  
ANISOU 2343  O   ALA B 288     8990   6497   5201   -141    134  -2047       O  
ATOM   2344  CB  ALA B 288      16.253 -35.336 -38.644  1.00 52.09           C  
ANISOU 2344  CB  ALA B 288     8758   5218   5815    -92    983  -1132       C  
ATOM   2345  N   GLU B 289      14.677 -37.883 -39.692  1.00 57.59           N  
ANISOU 2345  N   GLU B 289     9295   6480   6105     53    593  -1464       N  
ATOM   2346  CA  GLU B 289      14.385 -38.970 -40.629  1.00 63.59           C  
ANISOU 2346  CA  GLU B 289    10851   7102   6207   -309    270  -1797       C  
ATOM   2347  C   GLU B 289      12.922 -38.921 -41.099  1.00 62.18           C  
ANISOU 2347  C   GLU B 289    10974   6704   5944     27    544  -1535       C  
ATOM   2348  O   GLU B 289      12.639 -39.096 -42.293  1.00 63.19           O  
ANISOU 2348  O   GLU B 289    11099   7011   5899   -153    367  -1371       O  
ATOM   2349  CB  GLU B 289      14.742 -40.335 -40.010  1.00 70.65           C  
ANISOU 2349  CB  GLU B 289    12093   7843   6908    806    358  -1334       C  
ATOM   2350  CG  GLU B 289      14.023 -41.561 -40.592  1.00 84.55           C  
ANISOU 2350  CG  GLU B 289    13570   8845   9707   -199   -301  -1903       C  
ATOM   2351  CD  GLU B 289      14.403 -41.916 -42.031  1.00 99.78           C  
ANISOU 2351  CD  GLU B 289    16039  11334  10537    522    798  -2135       C  
ATOM   2352  OE1 GLU B 289      13.775 -42.850 -42.577  1.00108.83           O  
ANISOU 2352  OE1 GLU B 289    16927  11485  12936    191    226  -2688       O  
ATOM   2353  OE2 GLU B 289      15.316 -41.294 -42.623  1.00 98.90           O  
ANISOU 2353  OE2 GLU B 289    15741  10099  11737    883    646  -1334       O  
ATOM   2354  N   PHE B 290      12.009 -38.679 -40.157  1.00 56.03           N  
ANISOU 2354  N   PHE B 290    10166   5360   5760   -217    102  -1264       N  
ATOM   2355  CA  PHE B 290      10.588 -38.544 -40.468  1.00 55.72           C  
ANISOU 2355  CA  PHE B 290    10222   5517   5432   -536     18  -1250       C  
ATOM   2356  C   PHE B 290      10.337 -37.452 -41.509  1.00 54.43           C  
ANISOU 2356  C   PHE B 290     9782   5564   5335   -627    183  -1213       C  
ATOM   2357  O   PHE B 290       9.581 -37.665 -42.465  1.00 53.85           O  
ANISOU 2357  O   PHE B 290     9878   5004   5576  -1027    100  -1335       O  
ATOM   2358  CB  PHE B 290       9.774 -38.272 -39.204  1.00 54.72           C  
ANISOU 2358  CB  PHE B 290    10268   4961   5559   -909    232   -909       C  
ATOM   2359  CG  PHE B 290       8.380 -37.806 -39.479  1.00 61.00           C  
ANISOU 2359  CG  PHE B 290    10475   6334   6367   -871    -65   -855       C  
ATOM   2360  CD1 PHE B 290       7.371 -38.727 -39.752  1.00 61.85           C  
ANISOU 2360  CD1 PHE B 290    11177   6524   5799  -1007   -571  -1081       C  
ATOM   2361  CD2 PHE B 290       8.073 -36.440 -39.482  1.00 68.12           C  
ANISOU 2361  CD2 PHE B 290    11584   6753   7543   -538   -165   -348       C  
ATOM   2362  CE1 PHE B 290       6.081 -38.298 -40.019  1.00 65.93           C  
ANISOU 2362  CE1 PHE B 290    11277   6935   6836   -889   -169   -909       C  
ATOM   2363  CE2 PHE B 290       6.782 -36.006 -39.746  1.00 69.14           C  
ANISOU 2363  CE2 PHE B 290    11537   7571   7159  -1315   -957    431       C  
ATOM   2364  CZ  PHE B 290       5.788 -36.939 -40.017  1.00 67.54           C  
ANISOU 2364  CZ  PHE B 290    11765   6753   7142  -1146   -650   -197       C  
ATOM   2365  N   LEU B 291      10.968 -36.294 -41.315  1.00 52.72           N  
ANISOU 2365  N   LEU B 291     9130   5675   5226   -563    530  -1429       N  
ATOM   2366  CA  LEU B 291      10.873 -35.179 -42.271  1.00 55.07           C  
ANISOU 2366  CA  LEU B 291     9634   6052   5235   -797     77  -1265       C  
ATOM   2367  C   LEU B 291      11.438 -35.519 -43.649  1.00 59.51           C  
ANISOU 2367  C   LEU B 291    10283   7028   5300   -723    562   -975       C  
ATOM   2368  O   LEU B 291      10.846 -35.143 -44.664  1.00 58.79           O  
ANISOU 2368  O   LEU B 291     9966   7254   5116   -167    925   -852       O  
ATOM   2369  CB  LEU B 291      11.517 -33.901 -41.714  1.00 52.53           C  
ANISOU 2369  CB  LEU B 291     9131   5769   5059   -826    407  -1118       C  
ATOM   2370  CG  LEU B 291      10.806 -33.265 -40.517  1.00 49.35           C  
ANISOU 2370  CG  LEU B 291     8548   5396   4805   -884    133   -912       C  
ATOM   2371  CD1 LEU B 291      11.627 -32.110 -39.972  1.00 48.63           C  
ANISOU 2371  CD1 LEU B 291     8278   5424   4774  -1009    163   -819       C  
ATOM   2372  CD2 LEU B 291       9.402 -32.790 -40.890  1.00 48.67           C  
ANISOU 2372  CD2 LEU B 291     8347   5009   5134  -1474     41   -352       C  
ATOM   2373  N   ALA B 292      12.560 -36.244 -43.675  1.00 60.97           N  
ANISOU 2373  N   ALA B 292    10422   7070   5674   -593    185  -1562       N  
ATOM   2374  CA  ALA B 292      13.177 -36.708 -44.929  1.00 67.86           C  
ANISOU 2374  CA  ALA B 292    11463   8140   6179   -337    579  -1967       C  
ATOM   2375  C   ALA B 292      12.259 -37.646 -45.715  1.00 69.12           C  
ANISOU 2375  C   ALA B 292    12263   7648   6351   -410    354  -1985       C  
ATOM   2376  O   ALA B 292      12.287 -37.657 -46.944  1.00 69.14           O  
ANISOU 2376  O   ALA B 292    11875   8124   6269     44    100  -1220       O  
ATOM   2377  CB  ALA B 292      14.511 -37.391 -44.654  1.00 66.78           C  
ANISOU 2377  CB  ALA B 292    10996   9105   5272    -89   1542  -2234       C  
ATOM   2378  N   ARG B 293      11.448 -38.419 -44.996  1.00 71.93           N  
ANISOU 2378  N   ARG B 293    11945   7995   7387   -707     19  -1520       N  
ATOM   2379  CA  ARG B 293      10.569 -39.416 -45.608  1.00 75.62           C  
ANISOU 2379  CA  ARG B 293    13035   7963   7733   -767   -216  -1932       C  
ATOM   2380  C   ARG B 293       9.198 -38.853 -45.990  1.00 73.66           C  
ANISOU 2380  C   ARG B 293    12928   7738   7320  -1065   -179  -1917       C  
ATOM   2381  O   ARG B 293       8.455 -39.480 -46.750  1.00 73.67           O  
ANISOU 2381  O   ARG B 293    13059   6404   8527   -863    167  -2132       O  
ATOM   2382  CB  ARG B 293      10.449 -40.649 -44.696  1.00 73.90           C  
ANISOU 2382  CB  ARG B 293    13724   8040   6313   -978    -37  -2430       C  
ATOM   2383  CG  ARG B 293      11.413 -41.790 -45.034  1.00 86.72           C  
ANISOU 2383  CG  ARG B 293    14988   9256   8704    139   -276  -2557       C  
ATOM   2384  CD  ARG B 293      12.836 -41.317 -45.338  1.00 99.92           C  
ANISOU 2384  CD  ARG B 293    15752  11187  11026   -768    -52  -2364       C  
ATOM   2385  NE  ARG B 293      13.469 -42.097 -46.403  1.00106.64           N  
ANISOU 2385  NE  ARG B 293    17084  12240  11192    402    890  -2433       N  
ATOM   2386  CZ  ARG B 293      14.499 -41.689 -47.146  1.00109.67           C  
ANISOU 2386  CZ  ARG B 293    17529  12589  11549   -116    643  -2206       C  
ATOM   2387  NH1 ARG B 293      14.988 -42.491 -48.086  1.00114.73           N  
ANISOU 2387  NH1 ARG B 293    19064  13252  11274    769    602  -2636       N  
ATOM   2388  NH2 ARG B 293      15.042 -40.486 -46.966  1.00 95.35           N  
ANISOU 2388  NH2 ARG B 293    15787  11930   8511    925    897  -3306       N  
ATOM   2389  N   HIS B 294       8.883 -37.661 -45.482  1.00 68.05           N  
ANISOU 2389  N   HIS B 294    11940   7575   6338   -694    254  -1133       N  
ATOM   2390  CA  HIS B 294       7.594 -37.021 -45.736  1.00 64.89           C  
ANISOU 2390  CA  HIS B 294    11669   6835   6148  -1202    129   -996       C  
ATOM   2391  C   HIS B 294       7.773 -35.556 -46.140  1.00 59.08           C  
ANISOU 2391  C   HIS B 294    10415   6729   5304  -1283    174  -1290       C  
ATOM   2392  O   HIS B 294       7.781 -34.663 -45.290  1.00 55.56           O  
ANISOU 2392  O   HIS B 294     9517   6510   5083  -1282   -565   -929       O  
ATOM   2393  CB  HIS B 294       6.676 -37.153 -44.513  1.00 60.46           C  
ANISOU 2393  CB  HIS B 294    11033   6352   5585   -988   -377  -1689       C  
ATOM   2394  CG  HIS B 294       6.508 -38.560 -44.032  1.00 68.54           C  
ANISOU 2394  CG  HIS B 294    12103   6636   7302  -1263    -70  -1171       C  
ATOM   2395  ND1 HIS B 294       7.396 -39.162 -43.166  1.00 71.91           N  
ANISOU 2395  ND1 HIS B 294    12527   7304   7489  -1200   -245  -1096       N  
ATOM   2396  CD2 HIS B 294       5.567 -39.492 -44.311  1.00 72.22           C  
ANISOU 2396  CD2 HIS B 294    12450   7053   7936  -1504     51  -1314       C  
ATOM   2397  CE1 HIS B 294       7.005 -40.401 -42.927  1.00 72.56           C  
ANISOU 2397  CE1 HIS B 294    12978   7545   7045  -1514   -134   -954       C  
ATOM   2398  NE2 HIS B 294       5.896 -40.625 -43.608  1.00 71.22           N  
ANISOU 2398  NE2 HIS B 294    12889   6916   7256  -1864    195  -1406       N  
ATOM   2399  N   SER B 295       7.913 -35.328 -47.447  1.00 59.08           N  
ANISOU 2399  N   SER B 295    11069   6500   4878  -1316   -336  -1877       N  
ATOM   2400  CA  SER B 295       8.107 -33.986 -48.016  1.00 62.67           C  
ANISOU 2400  CA  SER B 295    11063   7126   5621  -1443   -201  -1158       C  
ATOM   2401  C   SER B 295       6.870 -33.096 -47.874  1.00 58.66           C  
ANISOU 2401  C   SER B 295    10767   6797   4724  -1856    408  -1361       C  
ATOM   2402  O   SER B 295       6.980 -31.868 -47.909  1.00 57.20           O  
ANISOU 2402  O   SER B 295     9033   6862   5835  -2932    299   -677       O  
ATOM   2403  CB  SER B 295       8.504 -34.079 -49.494  1.00 69.04           C  
ANISOU 2403  CB  SER B 295    11833   8228   6171  -1354   1123   -285       C  
ATOM   2404  OG  SER B 295       9.748 -34.731 -49.648  1.00 73.54           O  
ANISOU 2404  OG  SER B 295    12242   9636   6063  -1143   1614    297       O  
ATOM   2405  N   ASN B 296       5.705 -33.726 -47.721  1.00 57.92           N  
ANISOU 2405  N   ASN B 296    10337   6973   4694  -1886   -269  -1474       N  
ATOM   2406  CA  ASN B 296       4.434 -33.023 -47.511  1.00 56.88           C  
ANISOU 2406  CA  ASN B 296    10070   6570   4972  -2102   -382  -1220       C  
ATOM   2407  C   ASN B 296       4.253 -32.441 -46.095  1.00 53.36           C  
ANISOU 2407  C   ASN B 296     9562   6016   4693  -2189   -283   -743       C  
ATOM   2408  O   ASN B 296       3.257 -31.767 -45.819  1.00 52.39           O  
ANISOU 2408  O   ASN B 296     9895   5657   4352  -1980   -536   -388       O  
ATOM   2409  CB  ASN B 296       3.255 -33.942 -47.885  1.00 55.43           C  
ANISOU 2409  CB  ASN B 296    10244   6019   4796  -2083   -289  -1017       C  
ATOM   2410  CG  ASN B 296       3.221 -35.226 -47.068  1.00 57.42           C  
ANISOU 2410  CG  ASN B 296    10619   5853   5344  -1930   -229  -1072       C  
ATOM   2411  OD1 ASN B 296       4.261 -35.802 -46.739  1.00 59.89           O  
ANISOU 2411  OD1 ASN B 296    10924   5995   5835  -1549   -683  -1559       O  
ATOM   2412  ND2 ASN B 296       2.017 -35.683 -46.738  1.00 57.14           N  
ANISOU 2412  ND2 ASN B 296    10530   5007   6172  -2372   -583  -1038       N  
ATOM   2413  N   VAL B 297       5.218 -32.696 -45.209  1.00 52.52           N  
ANISOU 2413  N   VAL B 297     9494   5882   4578  -1666     57   -855       N  
ATOM   2414  CA  VAL B 297       5.189 -32.176 -43.834  1.00 48.82           C  
ANISOU 2414  CA  VAL B 297     8916   5200   4431  -1876   -359   -602       C  
ATOM   2415  C   VAL B 297       6.240 -31.085 -43.635  1.00 49.58           C  
ANISOU 2415  C   VAL B 297     8785   5307   4745  -1796     -2   -830       C  
ATOM   2416  O   VAL B 297       7.433 -31.317 -43.826  1.00 49.76           O  
ANISOU 2416  O   VAL B 297     8767   5427   4711  -1847    183   -605       O  
ATOM   2417  CB  VAL B 297       5.408 -33.286 -42.776  1.00 47.18           C  
ANISOU 2417  CB  VAL B 297     8613   4948   4363  -1801   -410   -778       C  
ATOM   2418  CG1 VAL B 297       5.344 -32.706 -41.360  1.00 45.62           C  
ANISOU 2418  CG1 VAL B 297     7917   5272   4144  -1877   -502   -520       C  
ATOM   2419  CG2 VAL B 297       4.392 -34.415 -42.935  1.00 46.21           C  
ANISOU 2419  CG2 VAL B 297     8973   4441   4143  -1692   -221   -568       C  
ATOM   2420  N   ASN B 298       5.783 -29.901 -43.240  1.00 46.99           N  
ANISOU 2420  N   ASN B 298     8431   5107   4314  -1797    -72   -453       N  
ATOM   2421  CA  ASN B 298       6.679 -28.835 -42.822  1.00 46.42           C  
ANISOU 2421  CA  ASN B 298     8027   5257   4353  -1779     -9   -470       C  
ATOM   2422  C   ASN B 298       6.574 -28.586 -41.313  1.00 47.50           C  
ANISOU 2422  C   ASN B 298     8263   5512   4271  -1473   -287   -320       C  
ATOM   2423  O   ASN B 298       5.470 -28.373 -40.789  1.00 47.75           O  
ANISOU 2423  O   ASN B 298     8381   5568   4191  -1864    -51   -193       O  
ATOM   2424  CB  ASN B 298       6.414 -27.558 -43.618  1.00 48.58           C  
ANISOU 2424  CB  ASN B 298     8303   5433   4722  -1752   -123   -117       C  
ATOM   2425  CG  ASN B 298       7.416 -26.462 -43.295  1.00 58.25           C  
ANISOU 2425  CG  ASN B 298     9567   6282   6281  -2620   -218   -553       C  
ATOM   2426  OD1 ASN B 298       8.545 -26.468 -43.787  1.00 64.98           O  
ANISOU 2426  OD1 ASN B 298     9881   7239   7567  -3315    133   -290       O  
ATOM   2427  ND2 ASN B 298       7.010 -25.522 -42.452  1.00 60.57           N  
ANISOU 2427  ND2 ASN B 298     9678   6767   6567  -2124    436   -331       N  
ATOM   2428  N   LEU B 299       7.723 -28.623 -40.630  1.00 42.71           N  
ANISOU 2428  N   LEU B 299     7377   5047   3801  -1883    386   -433       N  
ATOM   2429  CA  LEU B 299       7.788 -28.498 -39.169  1.00 41.33           C  
ANISOU 2429  CA  LEU B 299     7237   4651   3813  -1507    -23   -168       C  
ATOM   2430  C   LEU B 299       8.570 -27.281 -38.702  1.00 43.03           C  
ANISOU 2430  C   LEU B 299     7229   4895   4225  -1526     80   -503       C  
ATOM   2431  O   LEU B 299       9.702 -27.061 -39.145  1.00 42.64           O  
ANISOU 2431  O   LEU B 299     7253   4898   4051  -1056    354     13       O  
ATOM   2432  CB  LEU B 299       8.386 -29.768 -38.532  1.00 44.34           C  
ANISOU 2432  CB  LEU B 299     7600   4857   4390  -1257   -297   -227       C  
ATOM   2433  CG  LEU B 299       8.506 -29.836 -36.994  1.00 42.67           C  
ANISOU 2433  CG  LEU B 299     7245   4653   4314   -940     69   -312       C  
ATOM   2434  CD1 LEU B 299       7.163 -29.669 -36.294  1.00 38.52           C  
ANISOU 2434  CD1 LEU B 299     7114   3816   3704   -990   -243   -372       C  
ATOM   2435  CD2 LEU B 299       9.142 -31.142 -36.554  1.00 43.70           C  
ANISOU 2435  CD2 LEU B 299     7352   4843   4407   -795   -342   -327       C  
ATOM   2436  N   THR B 300       7.957 -26.508 -37.798  1.00 38.88           N  
ANISOU 2436  N   THR B 300     6470   4554   3745  -1446   -231    -61       N  
ATOM   2437  CA  THR B 300       8.625 -25.425 -37.087  1.00 38.96           C  
ANISOU 2437  CA  THR B 300     6906   4404   3491  -1447   -285   -105       C  
ATOM   2438  C   THR B 300       8.641 -25.773 -35.594  1.00 34.69           C  
ANISOU 2438  C   THR B 300     5942   3770   3467  -1221    -50   -161       C  
ATOM   2439  O   THR B 300       7.615 -26.131 -35.029  1.00 36.20           O  
ANISOU 2439  O   THR B 300     6054   3844   3853  -1277     72   -187       O  
ATOM   2440  CB  THR B 300       7.913 -24.072 -37.310  1.00 41.08           C  
ANISOU 2440  CB  THR B 300     6866   4614   4125  -1429   -281    -56       C  
ATOM   2441  OG1 THR B 300       7.881 -23.770 -38.710  1.00 43.13           O  
ANISOU 2441  OG1 THR B 300     7288   4821   4277  -2321    519    337       O  
ATOM   2442  CG2 THR B 300       8.634 -22.938 -36.578  1.00 40.82           C  
ANISOU 2442  CG2 THR B 300     6212   4667   4628  -1632   -246     60       C  
ATOM   2443  N   ILE B 301       9.809 -25.672 -34.971  1.00 33.98           N  
ANISOU 2443  N   ILE B 301     5875   3683   3351  -1277    -41   -260       N  
ATOM   2444  CA  ILE B 301       9.949 -25.945 -33.538  1.00 35.82           C  
ANISOU 2444  CA  ILE B 301     5976   4114   3518  -1078     30      5       C  
ATOM   2445  C   ILE B 301      10.353 -24.675 -32.779  1.00 38.80           C  
ANISOU 2445  C   ILE B 301     6156   4457   4127  -1089     51   -484       C  
ATOM   2446  O   ILE B 301      11.405 -24.098 -33.058  1.00 41.91           O  
ANISOU 2446  O   ILE B 301     6141   4957   4823  -1276     62   -411       O  
ATOM   2447  CB  ILE B 301      10.974 -27.076 -33.252  1.00 36.24           C  
ANISOU 2447  CB  ILE B 301     5996   4185   3586   -822    -21   -237       C  
ATOM   2448  CG1 ILE B 301      10.626 -28.353 -34.034  1.00 40.88           C  
ANISOU 2448  CG1 ILE B 301     6792   4439   4302   -875   -115   -604       C  
ATOM   2449  CG2 ILE B 301      11.043 -27.365 -31.752  1.00 35.94           C  
ANISOU 2449  CG2 ILE B 301     5882   4078   3693   -320    142     68       C  
ATOM   2450  CD1 ILE B 301      11.728 -29.397 -34.036  1.00 42.34           C  
ANISOU 2450  CD1 ILE B 301     7102   4353   4630   -760     10   -921       C  
ATOM   2451  N   PHE B 302       9.496 -24.234 -31.856  1.00 35.72           N  
ANISOU 2451  N   PHE B 302     5708   4159   3702  -1017   -204    112       N  
ATOM   2452  CA  PHE B 302       9.866 -23.205 -30.878  1.00 36.88           C  
ANISOU 2452  CA  PHE B 302     5661   4356   3994   -955   -174   -131       C  
ATOM   2453  C   PHE B 302      10.108 -23.914 -29.549  1.00 37.77           C  
ANISOU 2453  C   PHE B 302     5614   4622   4115   -966   -147    -33       C  
ATOM   2454  O   PHE B 302       9.245 -24.663 -29.069  1.00 38.54           O  
ANISOU 2454  O   PHE B 302     5679   4563   4400   -957   -168     14       O  
ATOM   2455  CB  PHE B 302       8.772 -22.134 -30.709  1.00 38.92           C  
ANISOU 2455  CB  PHE B 302     6006   4387   4394   -903   -175    121       C  
ATOM   2456  CG  PHE B 302       8.538 -21.288 -31.932  1.00 36.18           C  
ANISOU 2456  CG  PHE B 302     5360   4211   4176  -1270      3     27       C  
ATOM   2457  CD1 PHE B 302       9.277 -20.119 -32.148  1.00 37.68           C  
ANISOU 2457  CD1 PHE B 302     5631   4377   4308  -1363    235    291       C  
ATOM   2458  CD2 PHE B 302       7.554 -21.638 -32.857  1.00 36.49           C  
ANISOU 2458  CD2 PHE B 302     5864   4148   3852  -1378    -65     35       C  
ATOM   2459  CE1 PHE B 302       9.052 -19.339 -33.282  1.00 36.93           C  
ANISOU 2459  CE1 PHE B 302     5638   4309   4085  -1654    -78    133       C  
ATOM   2460  CE2 PHE B 302       7.315 -20.859 -33.979  1.00 37.46           C  
ANISOU 2460  CE2 PHE B 302     6006   4121   4104  -1386   -161    145       C  
ATOM   2461  CZ  PHE B 302       8.069 -19.707 -34.196  1.00 39.84           C  
ANISOU 2461  CZ  PHE B 302     6117   4552   4466  -1932   -352     70       C  
ATOM   2462  N   THR B 303      11.273 -23.684 -28.952  1.00 35.17           N  
ANISOU 2462  N   THR B 303     5182   4241   3937   -662     26      2       N  
ATOM   2463  CA  THR B 303      11.573 -24.290 -27.660  1.00 32.65           C  
ANISOU 2463  CA  THR B 303     4401   4075   3929   -943    158    -47       C  
ATOM   2464  C   THR B 303      11.791 -23.252 -26.547  1.00 35.18           C  
ANISOU 2464  C   THR B 303     5018   4333   4013  -1138    415   -166       C  
ATOM   2465  O   THR B 303      12.383 -22.178 -26.776  1.00 30.76           O  
ANISOU 2465  O   THR B 303     4425   3793   3469   -707     85   -103       O  
ATOM   2466  CB  THR B 303      12.740 -25.300 -27.766  1.00 34.02           C  
ANISOU 2466  CB  THR B 303     4749   4276   3901   -630    283     25       C  
ATOM   2467  OG1 THR B 303      12.810 -26.064 -26.561  1.00 33.85           O  
ANISOU 2467  OG1 THR B 303     4989   3812   4059   -521    370    -76       O  
ATOM   2468  CG2 THR B 303      14.091 -24.589 -28.020  1.00 34.39           C  
ANISOU 2468  CG2 THR B 303     4604   4424   4036   -694    180   -280       C  
ATOM   2469  N   ALA B 304      11.285 -23.558 -25.355  1.00 31.80           N  
ANISOU 2469  N   ALA B 304     4619   3663   3798   -834    199    -79       N  
ATOM   2470  CA  ALA B 304      11.447 -22.664 -24.207  1.00 29.80           C  
ANISOU 2470  CA  ALA B 304     3956   3853   3512   -646    190      8       C  
ATOM   2471  C   ALA B 304      12.896 -22.616 -23.748  1.00 31.76           C  
ANISOU 2471  C   ALA B 304     4025   4257   3785   -312    -36     53       C  
ATOM   2472  O   ALA B 304      13.433 -21.542 -23.465  1.00 34.23           O  
ANISOU 2472  O   ALA B 304     4129   4591   4286   -571    362   -131       O  
ATOM   2473  CB  ALA B 304      10.545 -23.093 -23.065  1.00 26.57           C  
ANISOU 2473  CB  ALA B 304     3450   3436   3208   -594    -91   -111       C  
ATOM   2474  N   ARG B 305      13.517 -23.792 -23.711  1.00 30.51           N  
ANISOU 2474  N   ARG B 305     3917   4219   3455   -264    285   -188       N  
ATOM   2475  CA  ARG B 305      14.842 -23.999 -23.156  1.00 31.12           C  
ANISOU 2475  CA  ARG B 305     3621   4577   3623   -459    338   -210       C  
ATOM   2476  C   ARG B 305      15.619 -24.924 -24.075  1.00 33.93           C  
ANISOU 2476  C   ARG B 305     4238   4549   4104   -141    283   -359       C  
ATOM   2477  O   ARG B 305      15.025 -25.722 -24.797  1.00 33.60           O  
ANISOU 2477  O   ARG B 305     4722   4359   3686     84    422   -405       O  
ATOM   2478  CB  ARG B 305      14.742 -24.660 -21.778  1.00 30.38           C  
ANISOU 2478  CB  ARG B 305     3553   4280   3710   -238    176   -164       C  
ATOM   2479  CG  ARG B 305      14.282 -23.772 -20.627  1.00 29.19           C  
ANISOU 2479  CG  ARG B 305     3067   4426   3596     11    298     26       C  
ATOM   2480  CD  ARG B 305      14.296 -24.542 -19.297  1.00 29.32           C  
ANISOU 2480  CD  ARG B 305     3211   4289   3637     71   -116     13       C  
ATOM   2481  NE  ARG B 305      13.630 -25.849 -19.378  1.00 30.92           N  
ANISOU 2481  NE  ARG B 305     3591   4427   3729    -38     78     34       N  
ATOM   2482  CZ  ARG B 305      12.333 -26.060 -19.148  1.00 31.23           C  
ANISOU 2482  CZ  ARG B 305     3709   4168   3986     67    297     13       C  
ATOM   2483  NH1 ARG B 305      11.827 -27.293 -19.269  1.00 29.61           N  
ANISOU 2483  NH1 ARG B 305     3701   3814   3733    312    155    445       N  
ATOM   2484  NH2 ARG B 305      11.534 -25.046 -18.809  1.00 27.55           N  
ANISOU 2484  NH2 ARG B 305     3283   3506   3678   -343    238     91       N  
ATOM   2485  N   LEU B 306      16.945 -24.818 -24.043  1.00 34.32           N  
ANISOU 2485  N   LEU B 306     4176   4829   4033     15    872    -86       N  
ATOM   2486  CA  LEU B 306      17.788 -25.744 -24.767  1.00 34.44           C  
ANISOU 2486  CA  LEU B 306     4375   4788   3922    -35    590   -453       C  
ATOM   2487  C   LEU B 306      18.298 -26.813 -23.814  1.00 36.52           C  
ANISOU 2487  C   LEU B 306     4773   5164   3940    117    695   -233       C  
ATOM   2488  O   LEU B 306      19.015 -26.520 -22.852  1.00 37.09           O  
ANISOU 2488  O   LEU B 306     4765   5132   4195     60    676   -157       O  
ATOM   2489  CB  LEU B 306      18.952 -25.022 -25.465  1.00 37.05           C  
ANISOU 2489  CB  LEU B 306     4596   5271   4211   -210    753   -315       C  
ATOM   2490  CG  LEU B 306      18.644 -23.983 -26.546  1.00 38.06           C  
ANISOU 2490  CG  LEU B 306     4763   5570   4125   -647    532   -221       C  
ATOM   2491  CD1 LEU B 306      19.932 -23.305 -27.001  1.00 38.82           C  
ANISOU 2491  CD1 LEU B 306     4388   5779   4584   -222   1015   -422       C  
ATOM   2492  CD2 LEU B 306      17.918 -24.597 -27.732  1.00 36.42           C  
ANISOU 2492  CD2 LEU B 306     4794   5082   3962   -738    769   -283       C  
ATOM   2493  N   TYR B 307      17.920 -28.054 -24.109  1.00 38.62           N  
ANISOU 2493  N   TYR B 307     4887   5251   4536    233    495   -362       N  
ATOM   2494  CA  TYR B 307      18.250 -29.220 -23.302  1.00 38.96           C  
ANISOU 2494  CA  TYR B 307     5031   5259   4510    639    851   -473       C  
ATOM   2495  C   TYR B 307      19.671 -29.683 -23.613  1.00 36.65           C  
ANISOU 2495  C   TYR B 307     4790   5028   4107    373    832   -284       C  
ATOM   2496  O   TYR B 307      19.962 -30.056 -24.750  1.00 39.58           O  
ANISOU 2496  O   TYR B 307     5667   5039   4329    670    830   -558       O  
ATOM   2497  CB  TYR B 307      17.219 -30.320 -23.604  1.00 40.41           C  
ANISOU 2497  CB  TYR B 307     5159   5466   4727    588    370   -437       C  
ATOM   2498  CG  TYR B 307      17.105 -31.437 -22.590  1.00 42.92           C  
ANISOU 2498  CG  TYR B 307     5652   5626   5029    604    456   -317       C  
ATOM   2499  CD1 TYR B 307      17.166 -31.180 -21.212  1.00 39.96           C  
ANISOU 2499  CD1 TYR B 307     4921   5267   4995    466    353   -378       C  
ATOM   2500  CD2 TYR B 307      16.897 -32.757 -23.009  1.00 44.05           C  
ANISOU 2500  CD2 TYR B 307     5851   5558   5328    792    -71   -378       C  
ATOM   2501  CE1 TYR B 307      17.057 -32.203 -20.285  1.00 42.09           C  
ANISOU 2501  CE1 TYR B 307     5113   5769   5108    678    969   -126       C  
ATOM   2502  CE2 TYR B 307      16.778 -33.791 -22.087  1.00 47.24           C  
ANISOU 2502  CE2 TYR B 307     6547   5774   5627    792    673   -276       C  
ATOM   2503  CZ  TYR B 307      16.858 -33.511 -20.731  1.00 48.70           C  
ANISOU 2503  CZ  TYR B 307     6665   6057   5782    822    423   -464       C  
ATOM   2504  OH  TYR B 307      16.740 -34.537 -19.824  1.00 51.07           O  
ANISOU 2504  OH  TYR B 307     6810   6082   6511     73    200   -140       O  
ATOM   2505  N   TYR B 308      20.549 -29.649 -22.606  1.00 39.02           N  
ANISOU 2505  N   TYR B 308     4973   5550   4301    702    803   -375       N  
ATOM   2506  CA  TYR B 308      21.988 -29.978 -22.755  1.00 40.71           C  
ANISOU 2506  CA  TYR B 308     4898   5979   4590    833    772   -491       C  
ATOM   2507  C   TYR B 308      22.648 -29.228 -23.904  1.00 40.94           C  
ANISOU 2507  C   TYR B 308     4786   6423   4346    798    930   -841       C  
ATOM   2508  O   TYR B 308      23.334 -29.846 -24.723  1.00 41.62           O  
ANISOU 2508  O   TYR B 308     4827   6448   4539   1067    846  -1131       O  
ATOM   2509  CB  TYR B 308      22.220 -31.490 -22.958  1.00 40.77           C  
ANISOU 2509  CB  TYR B 308     4788   6156   4544   1064    836   -826       C  
ATOM   2510  CG  TYR B 308      21.905 -32.342 -21.756  1.00 43.63           C  
ANISOU 2510  CG  TYR B 308     5470   6305   4802   1227    741   -438       C  
ATOM   2511  CD1 TYR B 308      22.866 -32.572 -20.768  1.00 41.09           C  
ANISOU 2511  CD1 TYR B 308     4842   5884   4887   1789   1049   -681       C  
ATOM   2512  CD2 TYR B 308      20.639 -32.922 -21.601  1.00 43.46           C  
ANISOU 2512  CD2 TYR B 308     5520   6002   4989   1389    843   -540       C  
ATOM   2513  CE1 TYR B 308      22.575 -33.353 -19.656  1.00 42.99           C  
ANISOU 2513  CE1 TYR B 308     5171   6445   4715   1728    825   -591       C  
ATOM   2514  CE2 TYR B 308      20.337 -33.704 -20.491  1.00 41.97           C  
ANISOU 2514  CE2 TYR B 308     5048   5866   5033   1564    854   -457       C  
ATOM   2515  CZ  TYR B 308      21.307 -33.913 -19.528  1.00 43.02           C  
ANISOU 2515  CZ  TYR B 308     5519   6056   4770   1522    834   -464       C  
ATOM   2516  OH  TYR B 308      21.013 -34.679 -18.439  1.00 42.06           O  
ANISOU 2516  OH  TYR B 308     5343   5379   5257   2142    641   -201       O  
ATOM   2517  N   PHE B 309      22.454 -27.908 -23.968  1.00 40.93           N  
ANISOU 2517  N   PHE B 309     4585   6441   4525    717    919   -591       N  
ATOM   2518  CA  PHE B 309      23.005 -27.112 -25.082  1.00 41.55           C  
ANISOU 2518  CA  PHE B 309     4741   6730   4315    492   1026   -747       C  
ATOM   2519  C   PHE B 309      24.525 -27.215 -25.228  1.00 42.41           C  
ANISOU 2519  C   PHE B 309     4713   6987   4413    684   1063   -999       C  
ATOM   2520  O   PHE B 309      25.068 -26.941 -26.299  1.00 45.00           O  
ANISOU 2520  O   PHE B 309     4570   7768   4759    373   1209   -743       O  
ATOM   2521  CB  PHE B 309      22.564 -25.644 -25.021  1.00 41.07           C  
ANISOU 2521  CB  PHE B 309     4630   6576   4396    519    726   -553       C  
ATOM   2522  CG  PHE B 309      22.976 -24.916 -23.765  1.00 43.39           C  
ANISOU 2522  CG  PHE B 309     4972   6829   4685    210    993   -887       C  
ATOM   2523  CD1 PHE B 309      24.233 -24.298 -23.671  1.00 45.70           C  
ANISOU 2523  CD1 PHE B 309     4912   7285   5164    145    474   -608       C  
ATOM   2524  CD2 PHE B 309      22.089 -24.809 -22.683  1.00 40.47           C  
ANISOU 2524  CD2 PHE B 309     4587   6201   4585    163    852   -387       C  
ATOM   2525  CE1 PHE B 309      24.599 -23.612 -22.512  1.00 43.25           C  
ANISOU 2525  CE1 PHE B 309     4499   7027   4905    165    969   -609       C  
ATOM   2526  CE2 PHE B 309      22.453 -24.120 -21.527  1.00 42.94           C  
ANISOU 2526  CE2 PHE B 309     4824   6883   4608     -6    682   -427       C  
ATOM   2527  CZ  PHE B 309      23.713 -23.524 -21.444  1.00 42.36           C  
ANISOU 2527  CZ  PHE B 309     4379   6984   4732    263    835   -415       C  
ATOM   2528  N   TRP B 310      25.193 -27.620 -24.154  1.00 45.23           N  
ANISOU 2528  N   TRP B 310     5152   7624   4406    724   1104   -757       N  
ATOM   2529  CA  TRP B 310      26.655 -27.740 -24.108  1.00 48.48           C  
ANISOU 2529  CA  TRP B 310     5122   8262   5034    887   1334   -636       C  
ATOM   2530  C   TRP B 310      27.186 -29.080 -24.635  1.00 54.59           C  
ANISOU 2530  C   TRP B 310     6435   8648   5657   1148   1513  -1245       C  
ATOM   2531  O   TRP B 310      28.369 -29.186 -24.984  1.00 59.78           O  
ANISOU 2531  O   TRP B 310     6545   9618   6548   2097   1524  -1130       O  
ATOM   2532  CB  TRP B 310      27.151 -27.499 -22.677  1.00 48.44           C  
ANISOU 2532  CB  TRP B 310     5051   8141   5211   1013   1136   -800       C  
ATOM   2533  CG  TRP B 310      26.544 -28.440 -21.680  1.00 47.11           C  
ANISOU 2533  CG  TRP B 310     4985   7856   5058   1245   1217   -935       C  
ATOM   2534  CD1 TRP B 310      27.040 -29.651 -21.296  1.00 46.90           C  
ANISOU 2534  CD1 TRP B 310     4952   7712   5154   1246    892   -969       C  
ATOM   2535  CD2 TRP B 310      25.313 -28.258 -20.956  1.00 45.62           C  
ANISOU 2535  CD2 TRP B 310     4827   7555   4951   1135    993  -1009       C  
ATOM   2536  NE1 TRP B 310      26.205 -30.232 -20.370  1.00 48.23           N  
ANISOU 2536  NE1 TRP B 310     5185   7708   5431   1464   1371  -1182       N  
ATOM   2537  CE2 TRP B 310      25.136 -29.403 -20.145  1.00 47.58           C  
ANISOU 2537  CE2 TRP B 310     5241   7580   5257   1412   1161   -943       C  
ATOM   2538  CE3 TRP B 310      24.346 -27.238 -20.912  1.00 44.40           C  
ANISOU 2538  CE3 TRP B 310     4626   7361   4881    905   1074  -1315       C  
ATOM   2539  CZ2 TRP B 310      24.026 -29.564 -19.294  1.00 46.23           C  
ANISOU 2539  CZ2 TRP B 310     5050   7519   4996   1462   1006   -877       C  
ATOM   2540  CZ3 TRP B 310      23.234 -27.397 -20.056  1.00 43.12           C  
ANISOU 2540  CZ3 TRP B 310     4634   6855   4893   1299    999   -760       C  
ATOM   2541  CH2 TRP B 310      23.096 -28.549 -19.258  1.00 44.13           C  
ANISOU 2541  CH2 TRP B 310     4847   7119   4801    995    939   -669       C  
ATOM   2542  N   ASP B 311      26.319 -30.093 -24.680  1.00 53.43           N  
ANISOU 2542  N   ASP B 311     5679   8612   6007   1297   1209  -1218       N  
ATOM   2543  CA  ASP B 311      26.689 -31.440 -25.136  1.00 53.83           C  
ANISOU 2543  CA  ASP B 311     6182   8602   5665   1477   1284  -1177       C  
ATOM   2544  C   ASP B 311      26.697 -31.505 -26.658  1.00 54.95           C  
ANISOU 2544  C   ASP B 311     6747   8363   5769   1481   1491  -1145       C  
ATOM   2545  O   ASP B 311      25.698 -31.177 -27.308  1.00 55.98           O  
ANISOU 2545  O   ASP B 311     6631   8087   6550   1859   1803  -1379       O  
ATOM   2546  CB  ASP B 311      25.711 -32.470 -24.551  1.00 53.86           C  
ANISOU 2546  CB  ASP B 311     6488   8014   5961   1615    943  -1001       C  
ATOM   2547  CG  ASP B 311      26.077 -33.909 -24.884  1.00 55.81           C  
ANISOU 2547  CG  ASP B 311     6286   8683   6233   2552    850  -1423       C  
ATOM   2548  OD1 ASP B 311      26.199 -34.257 -26.069  1.00 58.39           O  
ANISOU 2548  OD1 ASP B 311     6738   9170   6274   2823   1265  -1113       O  
ATOM   2549  OD2 ASP B 311      26.204 -34.719 -23.948  1.00 62.23           O  
ANISOU 2549  OD2 ASP B 311     7684   9572   6388   1813    968  -1061       O  
ATOM   2550  N   THR B 312      27.822 -31.959 -27.211  1.00 58.32           N  
ANISOU 2550  N   THR B 312     7031   8929   6199   1860   1416  -1425       N  
ATOM   2551  CA  THR B 312      28.023 -32.100 -28.661  1.00 61.12           C  
ANISOU 2551  CA  THR B 312     7452   9627   6142   1718   1243  -1443       C  
ATOM   2552  C   THR B 312      26.932 -32.920 -29.368  1.00 58.64           C  
ANISOU 2552  C   THR B 312     7131   9187   5962   1704   1474  -1236       C  
ATOM   2553  O   THR B 312      26.499 -32.557 -30.456  1.00 58.13           O  
ANISOU 2553  O   THR B 312     6908   9523   5654   1504   2054   -902       O  
ATOM   2554  CB  THR B 312      29.456 -32.600 -29.036  1.00 64.66           C  
ANISOU 2554  CB  THR B 312     7566  10784   6215   1785   1820  -1326       C  
ATOM   2555  OG1 THR B 312      29.375 -33.652 -30.005  1.00 73.75           O  
ANISOU 2555  OG1 THR B 312     8527  11060   8435   1526    755  -1929       O  
ATOM   2556  CG2 THR B 312      30.217 -33.133 -27.835  1.00 63.75           C  
ANISOU 2556  CG2 THR B 312     7655   9790   6775   2121   1157  -2217       C  
ATOM   2557  N   ASP B 313      26.491 -34.008 -28.740  1.00 57.79           N  
ANISOU 2557  N   ASP B 313     6966   8837   6151   2106   1368  -1053       N  
ATOM   2558  CA  ASP B 313      25.463 -34.895 -29.312  1.00 63.89           C  
ANISOU 2558  CA  ASP B 313     8333   9066   6876   1906   1034  -1577       C  
ATOM   2559  C   ASP B 313      24.074 -34.249 -29.400  1.00 58.53           C  
ANISOU 2559  C   ASP B 313     8100   8341   5796   1622   1008  -1800       C  
ATOM   2560  O   ASP B 313      23.323 -34.496 -30.351  1.00 54.48           O  
ANISOU 2560  O   ASP B 313     7429   7892   5377   1665   1391  -1757       O  
ATOM   2561  CB  ASP B 313      25.374 -36.205 -28.520  1.00 67.90           C  
ANISOU 2561  CB  ASP B 313     9393   8963   7442   2195   1214  -1427       C  
ATOM   2562  CG  ASP B 313      26.700 -36.950 -28.467  1.00 70.16           C  
ANISOU 2562  CG  ASP B 313     9437   9587   7632   2490   1434  -1498       C  
ATOM   2563  OD1 ASP B 313      27.331 -37.125 -29.528  1.00 71.72           O  
ANISOU 2563  OD1 ASP B 313     9967   9495   7786   3190   1354  -2093       O  
ATOM   2564  OD2 ASP B 313      27.106 -37.364 -27.361  1.00 73.09           O  
ANISOU 2564  OD2 ASP B 313     9915  10113   7741   3053   1237  -1578       O  
ATOM   2565  N   TYR B 314      23.736 -33.437 -28.403  1.00 54.95           N  
ANISOU 2565  N   TYR B 314     7104   7789   5984   1500   1635   -915       N  
ATOM   2566  CA  TYR B 314      22.467 -32.720 -28.404  1.00 50.10           C  
ANISOU 2566  CA  TYR B 314     6917   7152   4965   1305   1609  -1094       C  
ATOM   2567  C   TYR B 314      22.486 -31.592 -29.434  1.00 51.21           C  
ANISOU 2567  C   TYR B 314     6860   7433   5161    761   1227   -860       C  
ATOM   2568  O   TYR B 314      21.482 -31.356 -30.116  1.00 49.73           O  
ANISOU 2568  O   TYR B 314     6335   7252   5307    583   1567   -591       O  
ATOM   2569  CB  TYR B 314      22.139 -32.200 -27.003  1.00 44.31           C  
ANISOU 2569  CB  TYR B 314     5906   6266   4663   1366    885   -870       C  
ATOM   2570  CG  TYR B 314      21.635 -33.270 -26.048  1.00 45.51           C  
ANISOU 2570  CG  TYR B 314     6505   6308   4478   1327   1073  -1009       C  
ATOM   2571  CD1 TYR B 314      22.512 -34.209 -25.480  1.00 46.48           C  
ANISOU 2571  CD1 TYR B 314     6287   6535   4839   1506    836  -1091       C  
ATOM   2572  CD2 TYR B 314      20.279 -33.331 -25.693  1.00 48.43           C  
ANISOU 2572  CD2 TYR B 314     6487   6675   5238    627    783   -988       C  
ATOM   2573  CE1 TYR B 314      22.052 -35.183 -24.599  1.00 51.17           C  
ANISOU 2573  CE1 TYR B 314     7280   6569   5590   1561    837   -825       C  
ATOM   2574  CE2 TYR B 314      19.810 -34.296 -24.804  1.00 49.15           C  
ANISOU 2574  CE2 TYR B 314     7049   6252   5374    905    765   -969       C  
ATOM   2575  CZ  TYR B 314      20.697 -35.222 -24.265  1.00 53.18           C  
ANISOU 2575  CZ  TYR B 314     7378   6807   6019   1296    785   -739       C  
ATOM   2576  OH  TYR B 314      20.228 -36.177 -23.388  1.00 55.13           O  
ANISOU 2576  OH  TYR B 314     9003   6099   5842   1258    971   -946       O  
ATOM   2577  N   GLN B 315      23.637 -30.925 -29.556  1.00 49.05           N  
ANISOU 2577  N   GLN B 315     6389   7443   4803   1019    945  -1367       N  
ATOM   2578  CA  GLN B 315      23.861 -29.888 -30.573  1.00 52.98           C  
ANISOU 2578  CA  GLN B 315     6949   7969   5212    639   1097   -997       C  
ATOM   2579  C   GLN B 315      23.719 -30.443 -31.986  1.00 55.71           C  
ANISOU 2579  C   GLN B 315     7616   8032   5520    740   1399  -1459       C  
ATOM   2580  O   GLN B 315      23.070 -29.830 -32.839  1.00 59.70           O  
ANISOU 2580  O   GLN B 315     8880   8346   5454    418   1299   -843       O  
ATOM   2581  CB  GLN B 315      25.251 -29.287 -30.436  1.00 56.46           C  
ANISOU 2581  CB  GLN B 315     7122   8458   5870    394   1012  -1167       C  
ATOM   2582  CG  GLN B 315      25.462 -28.458 -29.190  1.00 56.63           C  
ANISOU 2582  CG  GLN B 315     6866   8744   5906    475   1016  -1156       C  
ATOM   2583  CD  GLN B 315      26.920 -28.145 -28.974  1.00 58.97           C  
ANISOU 2583  CD  GLN B 315     7018   9256   6131    327   1423  -1283       C  
ATOM   2584  OE1 GLN B 315      27.777 -28.564 -29.752  1.00 56.84           O  
ANISOU 2584  OE1 GLN B 315     6717   9934   4946   1929   2469  -1864       O  
ATOM   2585  NE2 GLN B 315      27.214 -27.406 -27.921  1.00 46.13           N  
ANISOU 2585  NE2 GLN B 315     4356   8373   4794    767   1720  -1129       N  
ATOM   2586  N   GLU B 316      24.330 -31.607 -32.205  1.00 52.24           N  
ANISOU 2586  N   GLU B 316     6556   8204   5088    779   1505  -1231       N  
ATOM   2587  CA  GLU B 316      24.275 -32.330 -33.471  1.00 57.81           C  
ANISOU 2587  CA  GLU B 316     7798   8728   5439    385   1041  -1666       C  
ATOM   2588  C   GLU B 316      22.830 -32.600 -33.868  1.00 54.25           C  
ANISOU 2588  C   GLU B 316     7804   7640   5165    606   1183  -1203       C  
ATOM   2589  O   GLU B 316      22.460 -32.412 -35.026  1.00 53.78           O  
ANISOU 2589  O   GLU B 316     7405   7743   5286   1229   1321  -1047       O  
ATOM   2590  CB  GLU B 316      25.033 -33.650 -33.336  1.00 69.33           C  
ANISOU 2590  CB  GLU B 316     9346   9495   7499   1122    858  -2175       C  
ATOM   2591  CG  GLU B 316      25.871 -34.013 -34.549  1.00 83.34           C  
ANISOU 2591  CG  GLU B 316    11015  12796   7854   1523   2898  -2348       C  
ATOM   2592  CD  GLU B 316      26.954 -35.037 -34.239  1.00105.32           C  
ANISOU 2592  CD  GLU B 316    13309  14923  11785   1757   1521  -1409       C  
ATOM   2593  OE1 GLU B 316      27.483 -35.048 -33.101  1.00103.80           O  
ANISOU 2593  OE1 GLU B 316    13451  15310  10677   1290   2112  -3079       O  
ATOM   2594  OE2 GLU B 316      27.289 -35.829 -35.148  1.00112.91           O  
ANISOU 2594  OE2 GLU B 316    15603  15136  12158   2001   1605  -2571       O  
ATOM   2595  N   GLY B 317      22.024 -33.021 -32.891  1.00 50.47           N  
ANISOU 2595  N   GLY B 317     7214   7032   4929   1192   1396  -2059       N  
ATOM   2596  CA  GLY B 317      20.612 -33.312 -33.093  1.00 54.53           C  
ANISOU 2596  CA  GLY B 317     7644   7248   5825    571   1110  -1128       C  
ATOM   2597  C   GLY B 317      19.836 -32.114 -33.599  1.00 54.87           C  
ANISOU 2597  C   GLY B 317     7844   7334   5669    684   1105  -1154       C  
ATOM   2598  O   GLY B 317      18.985 -32.253 -34.475  1.00 57.30           O  
ANISOU 2598  O   GLY B 317     8683   7235   5850    419    938  -1474       O  
ATOM   2599  N   LEU B 318      20.149 -30.941 -33.050  1.00 54.86           N  
ANISOU 2599  N   LEU B 318     7480   7390   5973    293   1025  -1014       N  
ATOM   2600  CA  LEU B 318      19.513 -29.686 -33.446  1.00 49.16           C  
ANISOU 2600  CA  LEU B 318     6993   6807   4878   -440   1012  -1072       C  
ATOM   2601  C   LEU B 318      19.896 -29.299 -34.862  1.00 50.78           C  
ANISOU 2601  C   LEU B 318     7195   7247   4850   -199   1239  -1332       C  
ATOM   2602  O   LEU B 318      19.039 -28.870 -35.642  1.00 54.69           O  
ANISOU 2602  O   LEU B 318     8161   7216   5402   -405    684   -834       O  
ATOM   2603  CB  LEU B 318      19.875 -28.559 -32.473  1.00 46.86           C  
ANISOU 2603  CB  LEU B 318     6872   6425   4507    182   1281  -1101       C  
ATOM   2604  CG  LEU B 318      19.424 -28.719 -31.014  1.00 45.94           C  
ANISOU 2604  CG  LEU B 318     6661   6195   4599   -163   1257  -1031       C  
ATOM   2605  CD1 LEU B 318      19.721 -27.449 -30.234  1.00 42.37           C  
ANISOU 2605  CD1 LEU B 318     6544   6005   3547    -21   1192   -716       C  
ATOM   2606  CD2 LEU B 318      17.947 -29.086 -30.914  1.00 47.28           C  
ANISOU 2606  CD2 LEU B 318     6460   6593   4908    100   1845   -231       C  
ATOM   2607  N   ARG B 319      21.181 -29.455 -35.178  1.00 48.15           N  
ANISOU 2607  N   ARG B 319     6891   7033   4369    306   1145  -1768       N  
ATOM   2608  CA  ARG B 319      21.699 -29.252 -36.535  1.00 54.14           C  
ANISOU 2608  CA  ARG B 319     7639   8161   4770   -318   1315  -1038       C  
ATOM   2609  C   ARG B 319      21.040 -30.201 -37.531  1.00 53.58           C  
ANISOU 2609  C   ARG B 319     7913   7607   4838     65   1260  -1086       C  
ATOM   2610  O   ARG B 319      20.685 -29.795 -38.640  1.00 53.28           O  
ANISOU 2610  O   ARG B 319     7224   8247   4772   -307   1110  -1009       O  
ATOM   2611  CB  ARG B 319      23.217 -29.442 -36.564  1.00 55.57           C  
ANISOU 2611  CB  ARG B 319     7515   8812   4787    189   2264  -1599       C  
ATOM   2612  CG  ARG B 319      23.983 -28.413 -35.738  1.00 61.28           C  
ANISOU 2612  CG  ARG B 319     8504   9062   5715   -100   1448  -1797       C  
ATOM   2613  CD  ARG B 319      25.489 -28.590 -35.865  1.00 68.45           C  
ANISOU 2613  CD  ARG B 319     8462  10606   6937     14   1822  -1671       C  
ATOM   2614  NE  ARG B 319      25.920 -28.557 -37.266  1.00 71.91           N  
ANISOU 2614  NE  ARG B 319     8161  12164   6996   -230   1745  -1422       N  
ATOM   2615  CZ  ARG B 319      26.215 -27.450 -37.947  1.00 79.81           C  
ANISOU 2615  CZ  ARG B 319     9996  12188   8138     -9   1403  -1038       C  
ATOM   2616  NH1 ARG B 319      26.142 -26.253 -37.369  1.00 76.31           N  
ANISOU 2616  NH1 ARG B 319     8118  12571   8303   1318   1762  -1315       N  
ATOM   2617  NH2 ARG B 319      26.592 -27.542 -39.216  1.00 84.06           N  
ANISOU 2617  NH2 ARG B 319    11140  12446   8353    452   1896   -879       N  
ATOM   2618  N   SER B 320      20.868 -31.455 -37.109  1.00 51.67           N  
ANISOU 2618  N   SER B 320     7398   7296   4939    223   1141  -1289       N  
ATOM   2619  CA  SER B 320      20.265 -32.505 -37.922  1.00 54.94           C  
ANISOU 2619  CA  SER B 320     8029   7611   5232     65   1042  -1526       C  
ATOM   2620  C   SER B 320      18.835 -32.130 -38.317  1.00 54.31           C  
ANISOU 2620  C   SER B 320     8456   7079   5097    -34    837  -1482       C  
ATOM   2621  O   SER B 320      18.442 -32.286 -39.483  1.00 50.28           O  
ANISOU 2621  O   SER B 320     8019   6316   4766    -31   1347  -1277       O  
ATOM   2622  CB  SER B 320      20.284 -33.829 -37.153  1.00 59.34           C  
ANISOU 2622  CB  SER B 320     8677   7847   6022    737    655  -1165       C  
ATOM   2623  OG  SER B 320      20.026 -34.915 -38.012  1.00 66.63           O  
ANISOU 2623  OG  SER B 320    10110   8812   6393    169   1068  -1812       O  
ATOM   2624  N   LEU B 321      18.082 -31.609 -37.343  1.00 52.18           N  
ANISOU 2624  N   LEU B 321     7801   6766   5258   -209   1169   -869       N  
ATOM   2625  CA  LEU B 321      16.715 -31.134 -37.561  1.00 49.89           C  
ANISOU 2625  CA  LEU B 321     8206   6169   4580    -96    875  -1017       C  
ATOM   2626  C   LEU B 321      16.678 -29.991 -38.568  1.00 50.22           C  
ANISOU 2626  C   LEU B 321     8002   6478   4598   -744    700   -947       C  
ATOM   2627  O   LEU B 321      15.904 -30.027 -39.530  1.00 49.53           O  
ANISOU 2627  O   LEU B 321     7981   6423   4413  -1186    857   -720       O  
ATOM   2628  CB  LEU B 321      16.066 -30.708 -36.231  1.00 44.96           C  
ANISOU 2628  CB  LEU B 321     6997   5580   4505   -334    714   -697       C  
ATOM   2629  CG  LEU B 321      15.614 -31.869 -35.342  1.00 44.76           C  
ANISOU 2629  CG  LEU B 321     7229   5633   4143    -91    653   -742       C  
ATOM   2630  CD1 LEU B 321      15.271 -31.405 -33.942  1.00 42.85           C  
ANISOU 2630  CD1 LEU B 321     6830   5178   4271    721    771   -552       C  
ATOM   2631  CD2 LEU B 321      14.443 -32.603 -35.976  1.00 48.33           C  
ANISOU 2631  CD2 LEU B 321     7812   5826   4724   -799    374   -104       C  
ATOM   2632  N   SER B 322      17.539 -28.999 -38.351  1.00 46.69           N  
ANISOU 2632  N   SER B 322     6869   6487   4384   -607   1743  -1092       N  
ATOM   2633  CA  SER B 322      17.580 -27.808 -39.189  1.00 52.38           C  
ANISOU 2633  CA  SER B 322     7817   6988   5097   -920   1010   -551       C  
ATOM   2634  C   SER B 322      17.954 -28.122 -40.645  1.00 58.05           C  
ANISOU 2634  C   SER B 322     9016   7729   5308   -697   1127   -900       C  
ATOM   2635  O   SER B 322      17.356 -27.570 -41.578  1.00 58.27           O  
ANISOU 2635  O   SER B 322     8302   8255   5580   -804   1313   -323       O  
ATOM   2636  CB  SER B 322      18.525 -26.771 -38.585  1.00 52.29           C  
ANISOU 2636  CB  SER B 322     7782   7349   4735   -971   1245   -997       C  
ATOM   2637  OG  SER B 322      18.511 -25.592 -39.359  1.00 55.04           O  
ANISOU 2637  OG  SER B 322     7061   7146   6706   -528   1101   -573       O  
ATOM   2638  N   GLN B 323      18.920 -29.022 -40.828  1.00 60.04           N  
ANISOU 2638  N   GLN B 323     8758   8577   5477   -465   1492   -715       N  
ATOM   2639  CA  GLN B 323      19.342 -29.466 -42.159  1.00 60.19           C  
ANISOU 2639  CA  GLN B 323     9147   8445   5276   -761    886  -1242       C  
ATOM   2640  C   GLN B 323      18.226 -30.141 -42.946  1.00 59.34           C  
ANISOU 2640  C   GLN B 323     9125   8031   5389   -890    954   -855       C  
ATOM   2641  O   GLN B 323      18.134 -29.949 -44.155  1.00 60.81           O  
ANISOU 2641  O   GLN B 323     8837   8987   5280  -1217   1437   -902       O  
ATOM   2642  CB  GLN B 323      20.554 -30.385 -42.071  1.00 65.11           C  
ANISOU 2642  CB  GLN B 323     9677   9103   5957    -58   1082   -804       C  
ATOM   2643  CG  GLN B 323      21.860 -29.647 -41.822  1.00 75.28           C  
ANISOU 2643  CG  GLN B 323    10525  10369   7709   -927   1442  -1548       C  
ATOM   2644  CD  GLN B 323      22.977 -30.553 -41.327  1.00 87.99           C  
ANISOU 2644  CD  GLN B 323    11121  12435   9874    207   1209  -1586       C  
ATOM   2645  OE1 GLN B 323      22.935 -31.776 -41.496  1.00 88.06           O  
ANISOU 2645  OE1 GLN B 323     8822  12437  12199   1236   2851  -1652       O  
ATOM   2646  NE2 GLN B 323      23.989 -29.951 -40.711  1.00 83.88           N  
ANISOU 2646  NE2 GLN B 323    10864  11244   9760    456   2158  -2697       N  
ATOM   2647  N   GLU B 324      17.379 -30.921 -42.271  1.00 58.27           N  
ANISOU 2647  N   GLU B 324     9144   7827   5168   -774    776   -797       N  
ATOM   2648  CA  GLU B 324      16.236 -31.564 -42.941  1.00 55.09           C  
ANISOU 2648  CA  GLU B 324     9468   6849   4612  -1051   1154   -859       C  
ATOM   2649  C   GLU B 324      15.049 -30.615 -43.177  1.00 56.32           C  
ANISOU 2649  C   GLU B 324     9355   6929   5112  -1520    376   -477       C  
ATOM   2650  O   GLU B 324      13.996 -31.040 -43.658  1.00 55.26           O  
ANISOU 2650  O   GLU B 324     9508   6683   4804  -1196    247  -1316       O  
ATOM   2651  CB  GLU B 324      15.781 -32.827 -42.198  1.00 57.71           C  
ANISOU 2651  CB  GLU B 324    10184   6927   4813  -1152   1310   -812       C  
ATOM   2652  CG  GLU B 324      16.734 -34.016 -42.290  1.00 67.46           C  
ANISOU 2652  CG  GLU B 324    10534   8213   6883   -372    804   -779       C  
ATOM   2653  CD  GLU B 324      17.030 -34.464 -43.717  1.00 70.39           C  
ANISOU 2653  CD  GLU B 324    11745   8133   6865   -808    683   -904       C  
ATOM   2654  OE1 GLU B 324      16.117 -34.462 -44.572  1.00 75.31           O  
ANISOU 2654  OE1 GLU B 324    12142   9407   7063   -488    407  -1352       O  
ATOM   2655  OE2 GLU B 324      18.191 -34.826 -43.986  1.00 75.28           O  
ANISOU 2655  OE2 GLU B 324    11741   8533   8326   -211    271   -448       O  
ATOM   2656  N   GLY B 325      15.225 -29.340 -42.831  1.00 54.03           N  
ANISOU 2656  N   GLY B 325     9002   6646   4879  -1263    737   -178       N  
ATOM   2657  CA  GLY B 325      14.246 -28.309 -43.139  1.00 51.68           C  
ANISOU 2657  CA  GLY B 325     8704   6470   4460  -1590    294   -390       C  
ATOM   2658  C   GLY B 325      13.330 -27.909 -42.003  1.00 53.01           C  
ANISOU 2658  C   GLY B 325     9094   6254   4791  -1411    598     -7       C  
ATOM   2659  O   GLY B 325      12.416 -27.105 -42.211  1.00 55.24           O  
ANISOU 2659  O   GLY B 325     8765   7047   5175  -1421     10    -40       O  
ATOM   2660  N   ALA B 326      13.557 -28.466 -40.809  1.00 52.04           N  
ANISOU 2660  N   ALA B 326     8780   6327   4663  -1323    146   -415       N  
ATOM   2661  CA  ALA B 326      12.850 -28.021 -39.614  1.00 48.75           C  
ANISOU 2661  CA  ALA B 326     7927   5933   4659  -1474    207    -21       C  
ATOM   2662  C   ALA B 326      13.399 -26.659 -39.204  1.00 50.89           C  
ANISOU 2662  C   ALA B 326     8376   5892   5067  -1440    301   -278       C  
ATOM   2663  O   ALA B 326      14.611 -26.470 -39.098  1.00 55.81           O  
ANISOU 2663  O   ALA B 326     8498   6898   5809  -1809     75   -677       O  
ATOM   2664  CB  ALA B 326      12.982 -29.031 -38.473  1.00 47.64           C  
ANISOU 2664  CB  ALA B 326     8167   5389   4543  -2124    656   -189       C  
ATOM   2665  N   SER B 327      12.502 -25.701 -39.018  1.00 49.71           N  
ANISOU 2665  N   SER B 327     8422   5685   4777  -1536    230     58       N  
ATOM   2666  CA  SER B 327      12.888 -24.386 -38.523  1.00 50.38           C  
ANISOU 2666  CA  SER B 327     8439   5843   4859  -1610    174   -288       C  
ATOM   2667  C   SER B 327      12.947 -24.502 -36.998  1.00 48.91           C  
ANISOU 2667  C   SER B 327     7648   5988   4947  -1571    259   -147       C  
ATOM   2668  O   SER B 327      11.940 -24.810 -36.361  1.00 50.16           O  
ANISOU 2668  O   SER B 327     7456   6500   5100  -1423    318   -161       O  
ATOM   2669  CB  SER B 327      11.883 -23.333 -38.995  1.00 56.91           C  
ANISOU 2669  CB  SER B 327     8419   6631   6574  -1634   -189    387       C  
ATOM   2670  OG  SER B 327      12.145 -22.069 -38.417  1.00 73.05           O  
ANISOU 2670  OG  SER B 327    11999   7382   8373  -1930   -164   -258       O  
ATOM   2671  N   VAL B 328      14.138 -24.303 -36.431  1.00 45.32           N  
ANISOU 2671  N   VAL B 328     7207   5551   4459  -1692    735   -195       N  
ATOM   2672  CA  VAL B 328      14.365 -24.454 -34.990  1.00 44.35           C  
ANISOU 2672  CA  VAL B 328     6790   5429   4632  -1492    341   -135       C  
ATOM   2673  C   VAL B 328      14.614 -23.084 -34.368  1.00 43.44           C  
ANISOU 2673  C   VAL B 328     6561   5486   4458  -1615    801   -149       C  
ATOM   2674  O   VAL B 328      15.529 -22.358 -34.768  1.00 42.86           O  
ANISOU 2674  O   VAL B 328     6627   5149   4507  -1860    657   -408       O  
ATOM   2675  CB  VAL B 328      15.536 -25.419 -34.671  1.00 43.58           C  
ANISOU 2675  CB  VAL B 328     6749   5528   4280  -1226    409   -285       C  
ATOM   2676  CG1 VAL B 328      15.682 -25.614 -33.169  1.00 38.73           C  
ANISOU 2676  CG1 VAL B 328     5463   5015   4236   -974    663   -295       C  
ATOM   2677  CG2 VAL B 328      15.314 -26.766 -35.339  1.00 45.06           C  
ANISOU 2677  CG2 VAL B 328     6468   5551   5100  -1127    912   -651       C  
ATOM   2678  N   GLU B 329      13.781 -22.738 -33.393  1.00 39.34           N  
ANISOU 2678  N   GLU B 329     6231   4804   3912  -1378    217    -77       N  
ATOM   2679  CA  GLU B 329      13.817 -21.409 -32.800  1.00 38.74           C  
ANISOU 2679  CA  GLU B 329     6341   4542   3836  -1526    287    125       C  
ATOM   2680  C   GLU B 329      13.500 -21.434 -31.312  1.00 38.55           C  
ANISOU 2680  C   GLU B 329     5778   4652   4215  -1654    910   -409       C  
ATOM   2681  O   GLU B 329      13.011 -22.452 -30.787  1.00 35.89           O  
ANISOU 2681  O   GLU B 329     5652   4204   3780  -1388     97   -205       O  
ATOM   2682  CB  GLU B 329      12.892 -20.478 -33.572  1.00 44.03           C  
ANISOU 2682  CB  GLU B 329     7152   4392   5183  -1256    504    125       C  
ATOM   2683  CG  GLU B 329      13.678 -19.677 -34.622  1.00 48.95           C  
ANISOU 2683  CG  GLU B 329     7300   6604   4694  -2879   1860   1430       C  
ATOM   2684  CD  GLU B 329      12.845 -19.203 -35.776  1.00 70.55           C  
ANISOU 2684  CD  GLU B 329    10620   8756   7430   -951    108    370       C  
ATOM   2685  OE1 GLU B 329      11.624 -19.465 -35.792  1.00 73.13           O  
ANISOU 2685  OE1 GLU B 329    10896  10542   6346  -2027   2539   1174       O  
ATOM   2686  OE2 GLU B 329      13.425 -18.568 -36.678  1.00 74.93           O  
ANISOU 2686  OE2 GLU B 329     9711   9268   9489  -2699   2132    -77       O  
ATOM   2687  N   ILE B 330      13.814 -20.325 -30.637  1.00 33.45           N  
ANISOU 2687  N   ILE B 330     4544   4304   3860  -1632    473     35       N  
ATOM   2688  CA  ILE B 330      13.522 -20.188 -29.217  1.00 36.70           C  
ANISOU 2688  CA  ILE B 330     5209   4810   3925  -1303    467   -220       C  
ATOM   2689  C   ILE B 330      12.213 -19.432 -29.045  1.00 36.78           C  
ANISOU 2689  C   ILE B 330     5428   4227   4317  -1386    494    119       C  
ATOM   2690  O   ILE B 330      11.944 -18.490 -29.794  1.00 35.79           O  
ANISOU 2690  O   ILE B 330     5407   3914   4276  -1181     11   -227       O  
ATOM   2691  CB  ILE B 330      14.696 -19.518 -28.471  1.00 39.15           C  
ANISOU 2691  CB  ILE B 330     5868   4812   4194  -1592    266   -203       C  
ATOM   2692  CG1 ILE B 330      15.847 -20.514 -28.386  1.00 42.63           C  
ANISOU 2692  CG1 ILE B 330     5359   6578   4260  -1211   1066  -1085       C  
ATOM   2693  CG2 ILE B 330      14.348 -19.155 -27.038  1.00 36.39           C  
ANISOU 2693  CG2 ILE B 330     4706   4565   4553   -739    625   -450       C  
ATOM   2694  CD1 ILE B 330      16.931 -20.126 -29.290  1.00 43.76           C  
ANISOU 2694  CD1 ILE B 330     6160   5969   4498  -1832    939   -651       C  
HETATM 2695  N   MSE B 331      11.394 -19.889 -28.096  1.00 33.89           N  
ANISOU 2695  N   MSE B 331     4924   3955   3997  -1066    380    -65       N  
HETATM 2696  CA  MSE B 331      10.139 -19.225 -27.747  1.00 33.18           C  
ANISOU 2696  CA  MSE B 331     4659   3732   4214  -1596    400    168       C  
HETATM 2697  C   MSE B 331      10.464 -17.847 -27.237  1.00 36.47           C  
ANISOU 2697  C   MSE B 331     5470   3920   4467  -1386    150   -193       C  
HETATM 2698  O   MSE B 331      11.365 -17.676 -26.407  1.00 37.03           O  
ANISOU 2698  O   MSE B 331     5429   3975   4665  -1763    275   -112       O  
HETATM 2699  CB  MSE B 331       9.365 -20.022 -26.691  1.00 28.05           C  
ANISOU 2699  CB  MSE B 331     4502   2995   3159  -1112    104   -100       C  
HETATM 2700  CG  MSE B 331       8.913 -21.386 -27.260  1.00 30.33           C  
ANISOU 2700  CG  MSE B 331     4605   3124   3793   -903   -348   -465       C  
HETATM 2701 SE   MSE B 331       7.861 -22.371 -25.936  1.00 41.81          SE  
ANISOU 2701 SE   MSE B 331     5720   4885   5279  -1183     29    181      SE  
HETATM 2702  CE  MSE B 331       6.268 -21.229 -25.684  1.00 37.38           C  
ANISOU 2702  CE  MSE B 331     5515   4390   4294  -1188    494   -476       C  
ATOM   2703  N   GLY B 332       9.778 -16.852 -27.791  1.00 34.80           N  
ANISOU 2703  N   GLY B 332     4659   3726   4834  -1630    549    103       N  
ATOM   2704  CA  GLY B 332       9.799 -15.505 -27.234  1.00 35.90           C  
ANISOU 2704  CA  GLY B 332     5201   3889   4550  -1156    483     56       C  
ATOM   2705  C   GLY B 332       8.454 -15.206 -26.600  1.00 34.00           C  
ANISOU 2705  C   GLY B 332     5290   3556   4073  -1140    104    -81       C  
ATOM   2706  O   GLY B 332       7.573 -16.087 -26.517  1.00 34.30           O  
ANISOU 2706  O   GLY B 332     4818   4092   4120  -1160     80    219       O  
ATOM   2707  N   TYR B 333       8.303 -13.959 -26.169  1.00 32.11           N  
ANISOU 2707  N   TYR B 333     5008   3351   3840   -952   -175     66       N  
ATOM   2708  CA  TYR B 333       7.064 -13.462 -25.572  1.00 35.21           C  
ANISOU 2708  CA  TYR B 333     5148   3791   4439  -1055    -95     -6       C  
ATOM   2709  C   TYR B 333       5.821 -13.848 -26.380  1.00 32.86           C  
ANISOU 2709  C   TYR B 333     5040   3209   4236   -967    -22     72       C  
ATOM   2710  O   TYR B 333       4.859 -14.361 -25.813  1.00 31.32           O  
ANISOU 2710  O   TYR B 333     4722   3178   3998   -599   -120    384       O  
ATOM   2711  CB  TYR B 333       7.140 -11.929 -25.373  1.00 36.59           C  
ANISOU 2711  CB  TYR B 333     5888   3671   4341   -896    138     66       C  
ATOM   2712  CG  TYR B 333       5.819 -11.299 -24.994  1.00 41.40           C  
ANISOU 2712  CG  TYR B 333     6099   4256   5373   -509    -80    117       C  
ATOM   2713  CD1 TYR B 333       5.439 -11.175 -23.647  1.00 41.52           C  
ANISOU 2713  CD1 TYR B 333     6124   4252   5399   -793    -13    102       C  
ATOM   2714  CD2 TYR B 333       4.939 -10.831 -25.980  1.00 41.72           C  
ANISOU 2714  CD2 TYR B 333     6450   4374   5028  -1020   -124    172       C  
ATOM   2715  CE1 TYR B 333       4.224 -10.600 -23.303  1.00 45.39           C  
ANISOU 2715  CE1 TYR B 333     6234   5231   5782   -741    -28   -180       C  
ATOM   2716  CE2 TYR B 333       3.721 -10.260 -25.644  1.00 46.61           C  
ANISOU 2716  CE2 TYR B 333     6685   4899   6123   -320   -443    503       C  
ATOM   2717  CZ  TYR B 333       3.372 -10.144 -24.308  1.00 48.30           C  
ANISOU 2717  CZ  TYR B 333     7083   5133   6134   -501   -172    444       C  
ATOM   2718  OH  TYR B 333       2.162  -9.579 -23.989  1.00 54.47           O  
ANISOU 2718  OH  TYR B 333     7873   5598   7224    110   -438   -140       O  
ATOM   2719  N   LYS B 334       5.829 -13.612 -27.696  1.00 34.20           N  
ANISOU 2719  N   LYS B 334     5314   3333   4344   -734   -224    211       N  
ATOM   2720  CA  LYS B 334       4.627 -13.946 -28.482  1.00 38.40           C  
ANISOU 2720  CA  LYS B 334     5967   3699   4924   -971   -711    299       C  
ATOM   2721  C   LYS B 334       4.230 -15.426 -28.445  1.00 34.25           C  
ANISOU 2721  C   LYS B 334     5286   3736   3989   -999   -425    316       C  
ATOM   2722  O   LYS B 334       3.047 -15.750 -28.503  1.00 35.59           O  
ANISOU 2722  O   LYS B 334     5376   4075   4071   -860   -944    184       O  
ATOM   2723  CB  LYS B 334       4.720 -13.445 -29.909  1.00 44.86           C  
ANISOU 2723  CB  LYS B 334     7368   4293   5383  -1210     68    831       C  
ATOM   2724  CG  LYS B 334       5.704 -14.153 -30.803  1.00 53.15           C  
ANISOU 2724  CG  LYS B 334     8361   4994   6838   -758     65    -49       C  
ATOM   2725  CD  LYS B 334       4.991 -14.592 -32.069  1.00 60.88           C  
ANISOU 2725  CD  LYS B 334     8951   6428   7751   -966  -1452    849       C  
ATOM   2726  CE  LYS B 334       4.118 -13.500 -32.678  1.00 50.56           C  
ANISOU 2726  CE  LYS B 334     7987   4662   6560  -1468   -390    174       C  
ATOM   2727  NZ  LYS B 334       3.204 -14.074 -33.701  1.00 51.62           N  
ANISOU 2727  NZ  LYS B 334     7455   6464   5690  -1188   -726    452       N  
ATOM   2728  N   ASP B 335       5.219 -16.302 -28.307  1.00 32.62           N  
ANISOU 2728  N   ASP B 335     4894   3336   4162  -1026   -114    224       N  
ATOM   2729  CA  ASP B 335       5.002 -17.750 -28.277  1.00 33.04           C  
ANISOU 2729  CA  ASP B 335     4836   3472   4245  -1210   -225    218       C  
ATOM   2730  C   ASP B 335       4.508 -18.231 -26.915  1.00 32.91           C  
ANISOU 2730  C   ASP B 335     4677   3675   4151   -843   -269    232       C  
ATOM   2731  O   ASP B 335       3.634 -19.102 -26.842  1.00 34.84           O  
ANISOU 2731  O   ASP B 335     4683   3870   4683   -894   -349    -32       O  
ATOM   2732  CB  ASP B 335       6.289 -18.479 -28.699  1.00 31.80           C  
ANISOU 2732  CB  ASP B 335     5055   3080   3946  -1013   -291    -12       C  
ATOM   2733  CG  ASP B 335       6.821 -17.977 -30.042  1.00 38.35           C  
ANISOU 2733  CG  ASP B 335     5973   4226   4370  -1311     79    232       C  
ATOM   2734  OD1 ASP B 335       6.070 -18.055 -31.033  1.00 40.86           O  
ANISOU 2734  OD1 ASP B 335     6560   4213   4750   -748   -369    941       O  
ATOM   2735  OD2 ASP B 335       7.971 -17.488 -30.113  1.00 41.48           O  
ANISOU 2735  OD2 ASP B 335     6183   4395   5181  -1479    524    773       O  
ATOM   2736  N   PHE B 336       5.060 -17.679 -25.831  1.00 31.71           N  
ANISOU 2736  N   PHE B 336     4315   3765   3966   -553    102      5       N  
ATOM   2737  CA  PHE B 336       4.576 -18.026 -24.490  1.00 28.20           C  
ANISOU 2737  CA  PHE B 336     3842   3118   3751   -773   -312    127       C  
ATOM   2738  C   PHE B 336       3.124 -17.563 -24.355  1.00 31.48           C  
ANISOU 2738  C   PHE B 336     4068   3585   4308   -737   -229    275       C  
ATOM   2739  O   PHE B 336       2.283 -18.304 -23.847  1.00 31.64           O  
ANISOU 2739  O   PHE B 336     4015   3592   4414   -690   -381    394       O  
ATOM   2740  CB  PHE B 336       5.461 -17.405 -23.402  1.00 28.05           C  
ANISOU 2740  CB  PHE B 336     3696   3294   3668   -836    -58    -33       C  
ATOM   2741  CG  PHE B 336       6.866 -17.981 -23.354  1.00 30.37           C  
ANISOU 2741  CG  PHE B 336     3705   3687   4146   -952    -70    188       C  
ATOM   2742  CD1 PHE B 336       7.084 -19.309 -22.961  1.00 32.86           C  
ANISOU 2742  CD1 PHE B 336     4107   3843   4533   -585    205     81       C  
ATOM   2743  CD2 PHE B 336       7.966 -17.199 -23.689  1.00 29.20           C  
ANISOU 2743  CD2 PHE B 336     3846   3600   3649   -945    149     52       C  
ATOM   2744  CE1 PHE B 336       8.370 -19.837 -22.914  1.00 27.82           C  
ANISOU 2744  CE1 PHE B 336     3778   3128   3661   -986    142   -276       C  
ATOM   2745  CE2 PHE B 336       9.260 -17.725 -23.644  1.00 27.35           C  
ANISOU 2745  CE2 PHE B 336     3718   3236   3435  -1164    238    -71       C  
ATOM   2746  CZ  PHE B 336       9.456 -19.036 -23.252  1.00 29.33           C  
ANISOU 2746  CZ  PHE B 336     3994   3422   3727  -1002    281     38       C  
ATOM   2747  N   LYS B 337       2.852 -16.348 -24.848  1.00 31.55           N  
ANISOU 2747  N   LYS B 337     4266   3407   4312   -580   -485     82       N  
ATOM   2748  CA  LYS B 337       1.510 -15.764 -24.860  1.00 34.18           C  
ANISOU 2748  CA  LYS B 337     4437   3710   4839   -584   -455    292       C  
ATOM   2749  C   LYS B 337       0.547 -16.630 -25.668  1.00 34.53           C  
ANISOU 2749  C   LYS B 337     4767   3760   4590   -514   -730    490       C  
ATOM   2750  O   LYS B 337      -0.550 -16.934 -25.201  1.00 38.55           O  
ANISOU 2750  O   LYS B 337     4929   4351   5364   -732   -680    659       O  
ATOM   2751  CB  LYS B 337       1.545 -14.334 -25.412  1.00 37.39           C  
ANISOU 2751  CB  LYS B 337     5327   3893   4984   -631   -347    529       C  
ATOM   2752  CG  LYS B 337       0.235 -13.570 -25.249  1.00 42.99           C  
ANISOU 2752  CG  LYS B 337     5635   4694   6003   -324   -741    209       C  
ATOM   2753  CD  LYS B 337       0.346 -12.151 -25.776  1.00 47.29           C  
ANISOU 2753  CD  LYS B 337     6545   4854   6568   -467  -1009    480       C  
ATOM   2754  CE  LYS B 337      -0.791 -11.280 -25.248  1.00 55.41           C  
ANISOU 2754  CE  LYS B 337     7297   6287   7468   -109   -862    -65       C  
ATOM   2755  NZ  LYS B 337      -2.061 -11.478 -26.001  1.00 52.49           N  
ANISOU 2755  NZ  LYS B 337     6895   5608   7438    302   -801   1081       N  
ATOM   2756  N   TYR B 338       0.964 -17.039 -26.862  1.00 36.62           N  
ANISOU 2756  N   TYR B 338     5293   3760   4858   -407   -487    326       N  
ATOM   2757  CA  TYR B 338       0.151 -17.935 -27.689  1.00 39.92           C  
ANISOU 2757  CA  TYR B 338     5245   4513   5407   -851   -689    407       C  
ATOM   2758  C   TYR B 338      -0.152 -19.254 -26.960  1.00 39.89           C  
ANISOU 2758  C   TYR B 338     5266   4585   5304   -632   -813    635       C  
ATOM   2759  O   TYR B 338      -1.298 -19.735 -26.983  1.00 37.81           O  
ANISOU 2759  O   TYR B 338     4919   4264   5182   -382  -1334    128       O  
ATOM   2760  CB  TYR B 338       0.811 -18.197 -29.045  1.00 40.62           C  
ANISOU 2760  CB  TYR B 338     6010   4380   5042   -913   -678    662       C  
ATOM   2761  CG  TYR B 338      -0.032 -19.029 -30.008  1.00 43.87           C  
ANISOU 2761  CG  TYR B 338     6135   4840   5691  -1083   -975    549       C  
ATOM   2762  CD1 TYR B 338      -0.965 -18.418 -30.858  1.00 47.34           C  
ANISOU 2762  CD1 TYR B 338     6457   5688   5841   -919  -1225    669       C  
ATOM   2763  CD2 TYR B 338       0.123 -20.422 -30.085  1.00 44.18           C  
ANISOU 2763  CD2 TYR B 338     6214   4947   5624  -1042   -728    504       C  
ATOM   2764  CE1 TYR B 338      -1.729 -19.172 -31.744  1.00 47.81           C  
ANISOU 2764  CE1 TYR B 338     7096   5392   5677  -1133  -1097    752       C  
ATOM   2765  CE2 TYR B 338      -0.640 -21.185 -30.965  1.00 47.90           C  
ANISOU 2765  CE2 TYR B 338     6628   5766   5806  -1217  -1181    192       C  
ATOM   2766  CZ  TYR B 338      -1.558 -20.551 -31.790  1.00 51.25           C  
ANISOU 2766  CZ  TYR B 338     7423   5583   6465   -785   -977    758       C  
ATOM   2767  OH  TYR B 338      -2.310 -21.295 -32.659  1.00 57.60           O  
ANISOU 2767  OH  TYR B 338     8297   6772   6813  -1231  -1112    265       O  
ATOM   2768  N   CYS B 339       0.859 -19.827 -26.306  1.00 35.41           N  
ANISOU 2768  N   CYS B 339     4644   3917   4894   -995   -747    331       N  
ATOM   2769  CA  CYS B 339       0.646 -21.074 -25.545  1.00 33.31           C  
ANISOU 2769  CA  CYS B 339     4235   3966   4453   -790   -581    333       C  
ATOM   2770  C   CYS B 339      -0.289 -20.902 -24.359  1.00 33.50           C  
ANISOU 2770  C   CYS B 339     4260   4058   4408   -766   -617    470       C  
ATOM   2771  O   CYS B 339      -1.172 -21.726 -24.142  1.00 34.52           O  
ANISOU 2771  O   CYS B 339     4207   4125   4784   -786   -560    327       O  
ATOM   2772  CB  CYS B 339       1.971 -21.694 -25.127  1.00 34.34           C  
ANISOU 2772  CB  CYS B 339     4576   4069   4401   -665   -775    539       C  
ATOM   2773  SG  CYS B 339       2.825 -22.351 -26.567  1.00 38.85           S  
ANISOU 2773  SG  CYS B 339     5147   4610   5003   -988   -377    164       S  
ATOM   2774  N   TRP B 340      -0.113 -19.812 -23.618  1.00 33.76           N  
ANISOU 2774  N   TRP B 340     4105   4061   4658   -381   -665    300       N  
ATOM   2775  CA  TRP B 340      -1.011 -19.452 -22.523  1.00 34.89           C  
ANISOU 2775  CA  TRP B 340     4188   4281   4788   -631   -460    393       C  
ATOM   2776  C   TRP B 340      -2.469 -19.362 -22.996  1.00 37.82           C  
ANISOU 2776  C   TRP B 340     4353   4918   5100   -624   -621    475       C  
ATOM   2777  O   TRP B 340      -3.388 -19.793 -22.292  1.00 36.53           O  
ANISOU 2777  O   TRP B 340     4069   4715   5092   -744   -893    577       O  
ATOM   2778  CB  TRP B 340      -0.575 -18.113 -21.917  1.00 36.82           C  
ANISOU 2778  CB  TRP B 340     4576   4564   4846   -698   -607    136       C  
ATOM   2779  CG  TRP B 340      -1.433 -17.667 -20.792  1.00 36.90           C  
ANISOU 2779  CG  TRP B 340     4214   4784   5021   -584   -549    217       C  
ATOM   2780  CD1 TRP B 340      -2.487 -16.798 -20.858  1.00 43.34           C  
ANISOU 2780  CD1 TRP B 340     5077   5303   6088     10   -566      2       C  
ATOM   2781  CD2 TRP B 340      -1.345 -18.088 -19.424  1.00 34.53           C  
ANISOU 2781  CD2 TRP B 340     3604   4636   4878   -574   -484    106       C  
ATOM   2782  NE1 TRP B 340      -3.052 -16.640 -19.612  1.00 41.55           N  
ANISOU 2782  NE1 TRP B 340     4455   5344   5986    -48   -475    343       N  
ATOM   2783  CE2 TRP B 340      -2.371 -17.416 -18.714  1.00 37.65           C  
ANISOU 2783  CE2 TRP B 340     4162   4938   5202   -281   -193    138       C  
ATOM   2784  CE3 TRP B 340      -0.497 -18.964 -18.726  1.00 33.83           C  
ANISOU 2784  CE3 TRP B 340     3780   4356   4715   -649   -140    333       C  
ATOM   2785  CZ2 TRP B 340      -2.574 -17.593 -17.342  1.00 37.73           C  
ANISOU 2785  CZ2 TRP B 340     4010   5103   5221   -304   -306     53       C  
ATOM   2786  CZ3 TRP B 340      -0.686 -19.131 -17.352  1.00 32.81           C  
ANISOU 2786  CZ3 TRP B 340     3446   4359   4658   -724    -51    355       C  
ATOM   2787  CH2 TRP B 340      -1.718 -18.446 -16.678  1.00 37.09           C  
ANISOU 2787  CH2 TRP B 340     3979   4806   5305   -343    150    369       C  
ATOM   2788  N   GLU B 341      -2.675 -18.796 -24.183  1.00 38.68           N  
ANISOU 2788  N   GLU B 341     4830   4795   5070   -609   -735    447       N  
ATOM   2789  CA  GLU B 341      -4.031 -18.567 -24.700  1.00 43.14           C  
ANISOU 2789  CA  GLU B 341     5223   5210   5958   -338  -1012    679       C  
ATOM   2790  C   GLU B 341      -4.680 -19.801 -25.323  1.00 43.68           C  
ANISOU 2790  C   GLU B 341     5335   5226   6034   -454  -1010    713       C  
ATOM   2791  O   GLU B 341      -5.903 -19.907 -25.348  1.00 46.67           O  
ANISOU 2791  O   GLU B 341     5466   5633   6632   -627  -1481    962       O  
ATOM   2792  CB  GLU B 341      -4.046 -17.394 -25.683  1.00 41.75           C  
ANISOU 2792  CB  GLU B 341     5256   5039   5567   -133  -1022    547       C  
ATOM   2793  CG  GLU B 341      -3.903 -16.040 -24.984  1.00 45.56           C  
ANISOU 2793  CG  GLU B 341     5240   5219   6848   -351  -1023     78       C  
ATOM   2794  CD  GLU B 341      -3.520 -14.900 -25.919  1.00 54.29           C  
ANISOU 2794  CD  GLU B 341     6212   6300   8113   -444   -848    953       C  
ATOM   2795  OE1 GLU B 341      -3.361 -15.122 -27.145  1.00 65.50           O  
ANISOU 2795  OE1 GLU B 341     8286   8204   8397   -326  -2148   -426       O  
ATOM   2796  OE2 GLU B 341      -3.367 -13.762 -25.418  1.00 53.78           O  
ANISOU 2796  OE2 GLU B 341     6167   6405   7858    -50   -660    632       O  
ATOM   2797  N   ASN B 342      -3.857 -20.733 -25.789  1.00 40.96           N  
ANISOU 2797  N   ASN B 342     5053   4993   5514   -787   -599    616       N  
ATOM   2798  CA  ASN B 342      -4.331 -21.869 -26.575  1.00 42.04           C  
ANISOU 2798  CA  ASN B 342     5025   5405   5542   -693  -1313    660       C  
ATOM   2799  C   ASN B 342      -4.132 -23.265 -25.996  1.00 43.08           C  
ANISOU 2799  C   ASN B 342     5350   5493   5526   -880  -1036    798       C  
ATOM   2800  O   ASN B 342      -4.840 -24.185 -26.395  1.00 45.14           O  
ANISOU 2800  O   ASN B 342     5205   5834   6110  -1110   -960    756       O  
ATOM   2801  CB  ASN B 342      -3.722 -21.807 -27.974  1.00 45.90           C  
ANISOU 2801  CB  ASN B 342     6180   5593   5667   -751   -856    686       C  
ATOM   2802  CG  ASN B 342      -4.192 -20.596 -28.754  1.00 48.59           C  
ANISOU 2802  CG  ASN B 342     6225   5800   6435   -773  -1261    956       C  
ATOM   2803  OD1 ASN B 342      -3.435 -19.643 -28.962  1.00 46.52           O  
ANISOU 2803  OD1 ASN B 342     6159   5596   5920   -604  -1108   1238       O  
ATOM   2804  ND2 ASN B 342      -5.456 -20.615 -29.168  1.00 44.13           N  
ANISOU 2804  ND2 ASN B 342     6008   5426   5332  -1344  -1036    961       N  
ATOM   2805  N   PHE B 343      -3.172 -23.434 -25.083  1.00 39.96           N  
ANISOU 2805  N   PHE B 343     4741   5017   5425   -732   -779    743       N  
ATOM   2806  CA  PHE B 343      -2.888 -24.760 -24.518  1.00 37.25           C  
ANISOU 2806  CA  PHE B 343     4386   4932   4833   -805   -666    603       C  
ATOM   2807  C   PHE B 343      -3.005 -24.814 -22.997  1.00 35.98           C  
ANISOU 2807  C   PHE B 343     4017   4773   4880   -912   -725    589       C  
ATOM   2808  O   PHE B 343      -2.608 -25.803 -22.379  1.00 35.27           O  
ANISOU 2808  O   PHE B 343     3829   4769   4803  -1252   -762    734       O  
ATOM   2809  CB  PHE B 343      -1.498 -25.265 -24.963  1.00 34.63           C  
ANISOU 2809  CB  PHE B 343     4304   4282   4569  -1141   -757    441       C  
ATOM   2810  CG  PHE B 343      -1.278 -25.203 -26.449  1.00 38.35           C  
ANISOU 2810  CG  PHE B 343     5207   4634   4729  -1170   -347    402       C  
ATOM   2811  CD1 PHE B 343      -1.876 -26.132 -27.302  1.00 38.01           C  
ANISOU 2811  CD1 PHE B 343     4782   4914   4746  -1319   -868    738       C  
ATOM   2812  CD2 PHE B 343      -0.470 -24.212 -27.001  1.00 37.82           C  
ANISOU 2812  CD2 PHE B 343     5165   4424   4778  -1003   -562    556       C  
ATOM   2813  CE1 PHE B 343      -1.672 -26.071 -28.673  1.00 38.65           C  
ANISOU 2813  CE1 PHE B 343     5209   4590   4886  -1291   -822    688       C  
ATOM   2814  CE2 PHE B 343      -0.263 -24.144 -28.378  1.00 38.11           C  
ANISOU 2814  CE2 PHE B 343     5620   4143   4716  -1201   -656    399       C  
ATOM   2815  CZ  PHE B 343      -0.866 -25.076 -29.215  1.00 37.25           C  
ANISOU 2815  CZ  PHE B 343     5255   4408   4488  -1154   -930    643       C  
ATOM   2816  N   VAL B 344      -3.550 -23.753 -22.403  1.00 39.09           N  
ANISOU 2816  N   VAL B 344     4441   5257   5153   -747   -649    257       N  
ATOM   2817  CA  VAL B 344      -3.648 -23.622 -20.953  1.00 35.22           C  
ANISOU 2817  CA  VAL B 344     3564   4895   4920   -755   -743    421       C  
ATOM   2818  C   VAL B 344      -5.081 -23.258 -20.566  1.00 36.65           C  
ANISOU 2818  C   VAL B 344     3641   5086   5198   -678   -677    569       C  
ATOM   2819  O   VAL B 344      -5.704 -22.429 -21.226  1.00 37.80           O  
ANISOU 2819  O   VAL B 344     3254   5593   5514   -919  -1381    486       O  
ATOM   2820  CB  VAL B 344      -2.678 -22.536 -20.426  1.00 32.98           C  
ANISOU 2820  CB  VAL B 344     3451   4488   4591   -646   -309    365       C  
ATOM   2821  CG1 VAL B 344      -2.866 -22.308 -18.930  1.00 33.95           C  
ANISOU 2821  CG1 VAL B 344     3750   4480   4669   -645   -369    161       C  
ATOM   2822  CG2 VAL B 344      -1.224 -22.917 -20.700  1.00 31.78           C  
ANISOU 2822  CG2 VAL B 344     3381   4126   4566   -754   -383    819       C  
ATOM   2823  N   TYR B 345      -5.595 -23.865 -19.497  1.00 36.69           N  
ANISOU 2823  N   TYR B 345     3500   5272   5166   -807   -700    483       N  
ATOM   2824  CA  TYR B 345      -6.848 -23.409 -18.894  1.00 40.20           C  
ANISOU 2824  CA  TYR B 345     3677   5902   5694   -490   -721    425       C  
ATOM   2825  C   TYR B 345      -6.606 -22.098 -18.169  1.00 39.72           C  
ANISOU 2825  C   TYR B 345     3505   5873   5714   -360   -275    409       C  
ATOM   2826  O   TYR B 345      -6.477 -22.060 -16.941  1.00 41.85           O  
ANISOU 2826  O   TYR B 345     3917   6073   5908   -203   -527    536       O  
ATOM   2827  CB  TYR B 345      -7.416 -24.451 -17.937  1.00 43.29           C  
ANISOU 2827  CB  TYR B 345     3690   6703   6054   -889   -549    668       C  
ATOM   2828  CG  TYR B 345      -7.933 -25.693 -18.620  1.00 47.91           C  
ANISOU 2828  CG  TYR B 345     4756   6950   6497  -1075   -775    465       C  
ATOM   2829  CD1 TYR B 345      -9.073 -25.647 -19.440  1.00 48.34           C  
ANISOU 2829  CD1 TYR B 345     4738   7274   6351  -1211   -662    925       C  
ATOM   2830  CD2 TYR B 345      -7.297 -26.922 -18.434  1.00 47.34           C  
ANISOU 2830  CD2 TYR B 345     4687   6925   6373   -945   -133    583       C  
ATOM   2831  CE1 TYR B 345      -9.555 -26.793 -20.063  1.00 48.83           C  
ANISOU 2831  CE1 TYR B 345     5023   7628   5902  -1344   -246    491       C  
ATOM   2832  CE2 TYR B 345      -7.778 -28.074 -19.045  1.00 49.96           C  
ANISOU 2832  CE2 TYR B 345     5123   7136   6723   -888   -645    478       C  
ATOM   2833  CZ  TYR B 345      -8.896 -28.003 -19.857  1.00 52.34           C  
ANISOU 2833  CZ  TYR B 345     5380   7948   6558  -1076   -770    785       C  
ATOM   2834  OH  TYR B 345      -9.357 -29.149 -20.458  1.00 65.77           O  
ANISOU 2834  OH  TYR B 345     7950   8877   8159  -2429   -465    278       O  
ATOM   2835  N   ASN B 346      -6.526 -21.022 -18.938  1.00 41.17           N  
ANISOU 2835  N   ASN B 346     4088   5837   5718    155   -798    491       N  
ATOM   2836  CA  ASN B 346      -6.156 -19.723 -18.389  1.00 43.83           C  
ANISOU 2836  CA  ASN B 346     4614   6036   6002   -296   -552    358       C  
ATOM   2837  C   ASN B 346      -7.290 -19.053 -17.595  1.00 47.63           C  
ANISOU 2837  C   ASN B 346     4732   6750   6612     47   -302    427       C  
ATOM   2838  O   ASN B 346      -7.049 -18.084 -16.877  1.00 48.62           O  
ANISOU 2838  O   ASN B 346     4484   6698   7290    658    187    -83       O  
ATOM   2839  CB  ASN B 346      -5.638 -18.803 -19.495  1.00 42.17           C  
ANISOU 2839  CB  ASN B 346     3908   6202   5912   -197   -338    304       C  
ATOM   2840  CG  ASN B 346      -6.615 -18.657 -20.643  1.00 46.56           C  
ANISOU 2840  CG  ASN B 346     4831   6438   6421   -351   -971    435       C  
ATOM   2841  OD1 ASN B 346      -7.745 -18.196 -20.465  1.00 47.46           O  
ANISOU 2841  OD1 ASN B 346     4969   6165   6897     43  -1249    586       O  
ATOM   2842  ND2 ASN B 346      -6.177 -19.041 -21.838  1.00 47.19           N  
ANISOU 2842  ND2 ASN B 346     4685   6543   6701   -127  -1187    234       N  
ATOM   2843  N   ASP B 347      -8.512 -19.579 -17.723  1.00 50.93           N  
ANISOU 2843  N   ASP B 347     4901   7556   6892    -74   -802    405       N  
ATOM   2844  CA  ASP B 347      -9.694 -19.061 -17.009  1.00 54.74           C  
ANISOU 2844  CA  ASP B 347     4964   7964   7871    189   -564    552       C  
ATOM   2845  C   ASP B 347      -9.870 -17.562 -17.294  1.00 52.76           C  
ANISOU 2845  C   ASP B 347     4713   7928   7405    397   -959    293       C  
ATOM   2846  O   ASP B 347     -10.193 -16.775 -16.402  1.00 55.54           O  
ANISOU 2846  O   ASP B 347     5232   7869   8002     60   -527     57       O  
ATOM   2847  CB  ASP B 347      -9.604 -19.368 -15.493  1.00 57.80           C  
ANISOU 2847  CB  ASP B 347     5521   8704   7736   -224  -1011     54       C  
ATOM   2848  CG  ASP B 347     -10.923 -19.137 -14.751  1.00 69.41           C  
ANISOU 2848  CG  ASP B 347     6647  10469   9253    370   -229     58       C  
ATOM   2849  OD1 ASP B 347     -12.013 -19.292 -15.350  1.00 68.12           O  
ANISOU 2849  OD1 ASP B 347     6492  10335   9053    288    119   -297       O  
ATOM   2850  OD2 ASP B 347     -10.869 -18.799 -13.549  1.00 72.73           O  
ANISOU 2850  OD2 ASP B 347     7337  10706   9590      0   -132   -500       O  
ATOM   2851  N   ASP B 348      -9.618 -17.191 -18.554  1.00 49.93           N  
ANISOU 2851  N   ASP B 348     3937   7587   7447    164  -1045    329       N  
ATOM   2852  CA  ASP B 348      -9.674 -15.807 -19.054  1.00 58.51           C  
ANISOU 2852  CA  ASP B 348     5995   7821   8415    243   -927    574       C  
ATOM   2853  C   ASP B 348      -8.665 -14.829 -18.442  1.00 59.02           C  
ANISOU 2853  C   ASP B 348     6185   8050   8187    425  -1098    184       C  
ATOM   2854  O   ASP B 348      -8.731 -13.631 -18.722  1.00 63.00           O  
ANISOU 2854  O   ASP B 348     6549   8140   9248   1103  -1513    610       O  
ATOM   2855  CB  ASP B 348     -11.107 -15.234 -18.991  1.00 63.32           C  
ANISOU 2855  CB  ASP B 348     6473   8291   9293    880   -603    342       C  
ATOM   2856  CG  ASP B 348     -12.022 -15.830 -20.047  1.00 70.03           C  
ANISOU 2856  CG  ASP B 348     7248   9944   9414   1001  -1313    416       C  
ATOM   2857  OD1 ASP B 348     -11.553 -16.094 -21.174  1.00 72.22           O  
ANISOU 2857  OD1 ASP B 348     6428  11124   9886    842  -1114    445       O  
ATOM   2858  OD2 ASP B 348     -13.222 -16.027 -19.757  1.00 78.93           O  
ANISOU 2858  OD2 ASP B 348     8304  11110  10573   -186    153   -385       O  
ATOM   2859  N   GLU B 349      -7.730 -15.327 -17.630  1.00 55.04           N  
ANISOU 2859  N   GLU B 349     5496   7580   7836    437   -423    311       N  
ATOM   2860  CA  GLU B 349      -6.667 -14.476 -17.084  1.00 54.85           C  
ANISOU 2860  CA  GLU B 349     6105   7108   7628    396   -475     51       C  
ATOM   2861  C   GLU B 349      -5.639 -14.144 -18.170  1.00 52.58           C  
ANISOU 2861  C   GLU B 349     5580   6600   7796    133   -573    120       C  
ATOM   2862  O   GLU B 349      -5.309 -15.013 -18.982  1.00 53.45           O  
ANISOU 2862  O   GLU B 349     5966   6736   7605   -358    208    294       O  
ATOM   2863  CB  GLU B 349      -5.988 -15.130 -15.876  1.00 55.62           C  
ANISOU 2863  CB  GLU B 349     6329   7101   7703    662   -574   -145       C  
ATOM   2864  CG  GLU B 349      -6.901 -15.332 -14.668  1.00 62.91           C  
ANISOU 2864  CG  GLU B 349     6736   8615   8550    368    -31    214       C  
ATOM   2865  CD  GLU B 349      -7.165 -14.061 -13.865  1.00 70.37           C  
ANISOU 2865  CD  GLU B 349     7711   9389   9636    604     22   -467       C  
ATOM   2866  OE1 GLU B 349      -6.624 -12.982 -14.198  1.00 72.63           O  
ANISOU 2866  OE1 GLU B 349     8476   8796  10324   1268    616   -352       O  
ATOM   2867  OE2 GLU B 349      -7.921 -14.145 -12.876  1.00 74.02           O  
ANISOU 2867  OE2 GLU B 349     7273  10561  10289      8    133   -187       O  
ATOM   2868  N   PRO B 350      -5.142 -12.885 -18.202  1.00 49.51           N  
ANISOU 2868  N   PRO B 350     5350   6270   7188    674   -566     88       N  
ATOM   2869  CA  PRO B 350      -4.165 -12.512 -19.234  1.00 50.98           C  
ANISOU 2869  CA  PRO B 350     5857   6272   7241    461   -564    304       C  
ATOM   2870  C   PRO B 350      -2.795 -13.117 -18.947  1.00 46.51           C  
ANISOU 2870  C   PRO B 350     5614   5676   6379    307   -399    -40       C  
ATOM   2871  O   PRO B 350      -2.474 -13.365 -17.784  1.00 43.94           O  
ANISOU 2871  O   PRO B 350     4634   5616   6442    -39   -234    104       O  
ATOM   2872  CB  PRO B 350      -4.107 -10.980 -19.131  1.00 52.74           C  
ANISOU 2872  CB  PRO B 350     6606   6317   7114    302   -374    239       C  
ATOM   2873  CG  PRO B 350      -4.500 -10.667 -17.732  1.00 50.89           C  
ANISOU 2873  CG  PRO B 350     6092   6051   7190    316   -704   -548       C  
ATOM   2874  CD  PRO B 350      -5.421 -11.766 -17.274  1.00 51.81           C  
ANISOU 2874  CD  PRO B 350     5820   6649   7214    433   -360   -171       C  
ATOM   2875  N   PHE B 351      -2.003 -13.359 -19.991  1.00 43.36           N  
ANISOU 2875  N   PHE B 351     5104   5084   6284   -277   -501    214       N  
ATOM   2876  CA  PHE B 351      -0.657 -13.909 -19.808  1.00 42.06           C  
ANISOU 2876  CA  PHE B 351     5119   4986   5874   -152   -309     41       C  
ATOM   2877  C   PHE B 351       0.178 -12.926 -19.005  1.00 42.31           C  
ANISOU 2877  C   PHE B 351     5081   5054   5941   -187   -402    145       C  
ATOM   2878  O   PHE B 351       0.188 -11.733 -19.302  1.00 44.18           O  
ANISOU 2878  O   PHE B 351     5591   5028   6166     70   -343    380       O  
ATOM   2879  CB  PHE B 351       0.012 -14.200 -21.157  1.00 42.02           C  
ANISOU 2879  CB  PHE B 351     5141   5078   5746    -72   -317    177       C  
ATOM   2880  CG  PHE B 351       1.461 -14.600 -21.047  1.00 37.45           C  
ANISOU 2880  CG  PHE B 351     4835   4226   5168   -685   -218    178       C  
ATOM   2881  CD1 PHE B 351       1.842 -15.750 -20.341  1.00 34.79           C  
ANISOU 2881  CD1 PHE B 351     4136   4469   4612   -630   -296     84       C  
ATOM   2882  CD2 PHE B 351       2.455 -13.839 -21.669  1.00 35.89           C  
ANISOU 2882  CD2 PHE B 351     4705   4532   4397   -721   -283    -79       C  
ATOM   2883  CE1 PHE B 351       3.179 -16.123 -20.244  1.00 33.22           C  
ANISOU 2883  CE1 PHE B 351     4162   3749   4708   -614    233   -378       C  
ATOM   2884  CE2 PHE B 351       3.791 -14.212 -21.575  1.00 36.94           C  
ANISOU 2884  CE2 PHE B 351     4880   4306   4847   -397    106    175       C  
ATOM   2885  CZ  PHE B 351       4.153 -15.349 -20.857  1.00 34.34           C  
ANISOU 2885  CZ  PHE B 351     4429   3952   4665   -647    232    -68       C  
ATOM   2886  N   LYS B 352       0.851 -13.425 -17.973  1.00 39.60           N  
ANISOU 2886  N   LYS B 352     4605   4981   5457   -198     -6     35       N  
ATOM   2887  CA  LYS B 352       1.721 -12.594 -17.153  1.00 40.62           C  
ANISOU 2887  CA  LYS B 352     4949   4749   5733   -113   -128   -227       C  
ATOM   2888  C   LYS B 352       3.179 -12.993 -17.420  1.00 39.38           C  
ANISOU 2888  C   LYS B 352     4845   4733   5381   -491    185    -86       C  
ATOM   2889  O   LYS B 352       3.627 -14.023 -16.919  1.00 40.86           O  
ANISOU 2889  O   LYS B 352     4808   4827   5887   -300     -3   -314       O  
ATOM   2890  CB  LYS B 352       1.354 -12.756 -15.676  1.00 44.66           C  
ANISOU 2890  CB  LYS B 352     5502   5607   5857   -142    -35    328       C  
ATOM   2891  CG  LYS B 352       2.158 -11.901 -14.701  1.00 54.22           C  
ANISOU 2891  CG  LYS B 352     6892   5939   7769   -395   -424   -668       C  
ATOM   2892  CD  LYS B 352       2.277 -12.560 -13.329  1.00 63.99           C  
ANISOU 2892  CD  LYS B 352     7978   8406   7927   -132   -341   -227       C  
ATOM   2893  CE  LYS B 352       0.948 -12.624 -12.581  1.00 71.88           C  
ANISOU 2893  CE  LYS B 352     8379   9298   9634  -1366    268   -664       C  
ATOM   2894  NZ  LYS B 352       1.036 -13.463 -11.350  1.00 77.36           N  
ANISOU 2894  NZ  LYS B 352     8789  10753   9848  -1379   -465    -60       N  
ATOM   2895  N   PRO B 353       3.918 -12.192 -18.221  1.00 37.36           N  
ANISOU 2895  N   PRO B 353     4779   4123   5292   -343     81   -246       N  
ATOM   2896  CA  PRO B 353       5.314 -12.558 -18.517  1.00 37.37           C  
ANISOU 2896  CA  PRO B 353     4698   4345   5154   -669     92   -157       C  
ATOM   2897  C   PRO B 353       6.160 -12.481 -17.252  1.00 39.97           C  
ANISOU 2897  C   PRO B 353     5186   4770   5227   -436    -88   -200       C  
ATOM   2898  O   PRO B 353       5.968 -11.576 -16.441  1.00 41.18           O  
ANISOU 2898  O   PRO B 353     5411   4824   5409   -652    -59   -416       O  
ATOM   2899  CB  PRO B 353       5.762 -11.490 -19.532  1.00 38.80           C  
ANISOU 2899  CB  PRO B 353     5338   4203   5201   -655    108    -65       C  
ATOM   2900  CG  PRO B 353       4.857 -10.322 -19.284  1.00 43.25           C  
ANISOU 2900  CG  PRO B 353     5842   4424   6168   -423    108     98       C  
ATOM   2901  CD  PRO B 353       3.536 -10.917 -18.868  1.00 40.03           C  
ANISOU 2901  CD  PRO B 353     5366   4502   5339    -54    124     98       C  
ATOM   2902  N   TRP B 354       7.068 -13.429 -17.072  1.00 37.34           N  
ANISOU 2902  N   TRP B 354     4922   4365   4898   -658    355   -128       N  
ATOM   2903  CA  TRP B 354       7.895 -13.430 -15.868  1.00 39.13           C  
ANISOU 2903  CA  TRP B 354     4858   4712   5298   -807    109   -437       C  
ATOM   2904  C   TRP B 354       9.097 -12.529 -16.045  1.00 42.49           C  
ANISOU 2904  C   TRP B 354     5225   5328   5591  -1117    475   -371       C  
ATOM   2905  O   TRP B 354       9.459 -12.183 -17.170  1.00 41.36           O  
ANISOU 2905  O   TRP B 354     5175   5090   5446  -1288    198   -267       O  
ATOM   2906  CB  TRP B 354       8.342 -14.838 -15.496  1.00 37.80           C  
ANISOU 2906  CB  TRP B 354     4707   4619   5036   -755   -204   -685       C  
ATOM   2907  CG  TRP B 354       8.838 -15.638 -16.652  1.00 36.92           C  
ANISOU 2907  CG  TRP B 354     4461   4762   4803  -1037    379   -323       C  
ATOM   2908  CD1 TRP B 354      10.121 -15.720 -17.103  1.00 35.79           C  
ANISOU 2908  CD1 TRP B 354     4297   4550   4750   -832    127   -330       C  
ATOM   2909  CD2 TRP B 354       8.052 -16.492 -17.501  1.00 34.30           C  
ANISOU 2909  CD2 TRP B 354     4030   4570   4432   -842    307   -173       C  
ATOM   2910  NE1 TRP B 354      10.185 -16.570 -18.194  1.00 34.29           N  
ANISOU 2910  NE1 TRP B 354     4230   4140   4659   -969     66   -165       N  
ATOM   2911  CE2 TRP B 354       8.929 -17.057 -18.451  1.00 33.20           C  
ANISOU 2911  CE2 TRP B 354     4087   4086   4441   -797     91   -235       C  
ATOM   2912  CE3 TRP B 354       6.687 -16.830 -17.550  1.00 33.22           C  
ANISOU 2912  CE3 TRP B 354     4025   4194   4403   -830    179   -233       C  
ATOM   2913  CZ2 TRP B 354       8.489 -17.951 -19.444  1.00 32.61           C  
ANISOU 2913  CZ2 TRP B 354     3902   4037   4449   -967    134   -133       C  
ATOM   2914  CZ3 TRP B 354       6.248 -17.720 -18.543  1.00 32.79           C  
ANISOU 2914  CZ3 TRP B 354     3938   4177   4341   -506    253   -238       C  
ATOM   2915  CH2 TRP B 354       7.152 -18.267 -19.476  1.00 29.10           C  
ANISOU 2915  CH2 TRP B 354     3708   3454   3892   -687    208    238       C  
ATOM   2916  N   LYS B 355       9.696 -12.146 -14.921  1.00 43.30           N  
ANISOU 2916  N   LYS B 355     5235   5529   5686   -791    452   -653       N  
ATOM   2917  CA  LYS B 355      10.937 -11.381 -14.896  1.00 45.53           C  
ANISOU 2917  CA  LYS B 355     5664   5556   6079  -1179    417   -718       C  
ATOM   2918  C   LYS B 355      12.024 -12.126 -15.673  1.00 43.55           C  
ANISOU 2918  C   LYS B 355     5363   5429   5754  -1268    341   -541       C  
ATOM   2919  O   LYS B 355      12.231 -13.329 -15.471  1.00 44.85           O  
ANISOU 2919  O   LYS B 355     5134   5709   6196   -655   -126   -455       O  
ATOM   2920  CB  LYS B 355      11.369 -11.146 -13.447  1.00 46.97           C  
ANISOU 2920  CB  LYS B 355     5988   5971   5884  -1080    663  -1071       C  
ATOM   2921  CG  LYS B 355      12.653 -10.342 -13.283  1.00 50.93           C  
ANISOU 2921  CG  LYS B 355     6560   6558   6233  -1507    373  -1204       C  
ATOM   2922  CD  LYS B 355      12.932 -10.056 -11.817  1.00 44.96           C  
ANISOU 2922  CD  LYS B 355     5498   5415   6170  -1239   -282   -584       C  
ATOM   2923  CE  LYS B 355      14.287  -9.400 -11.656  1.00 42.90           C  
ANISOU 2923  CE  LYS B 355     5542   5017   5738  -1379    422   -629       C  
ATOM   2924  NZ  LYS B 355      14.508  -9.051 -10.227  1.00 43.79           N  
ANISOU 2924  NZ  LYS B 355     5711   5155   5770   -749    162   -557       N  
ATOM   2925  N   GLY B 356      12.671 -11.409 -16.587  1.00 44.00           N  
ANISOU 2925  N   GLY B 356     5784   5377   5554  -1464    421   -743       N  
ATOM   2926  CA  GLY B 356      13.793 -11.941 -17.356  1.00 43.59           C  
ANISOU 2926  CA  GLY B 356     5392   5732   5438  -1474    286   -674       C  
ATOM   2927  C   GLY B 356      13.430 -12.706 -18.618  1.00 39.53           C  
ANISOU 2927  C   GLY B 356     4899   4702   5418  -1369    658   -529       C  
ATOM   2928  O   GLY B 356      14.324 -13.178 -19.305  1.00 35.79           O  
ANISOU 2928  O   GLY B 356     4317   4489   4790  -1875    695   -389       O  
ATOM   2929  N   LEU B 357      12.133 -12.819 -18.937  1.00 36.41           N  
ANISOU 2929  N   LEU B 357     5004   4365   4464  -1446    354   -444       N  
ATOM   2930  CA  LEU B 357      11.677 -13.594 -20.106  1.00 32.63           C  
ANISOU 2930  CA  LEU B 357     4410   3702   4285  -1375    149    -65       C  
ATOM   2931  C   LEU B 357      12.417 -13.209 -21.411  1.00 39.57           C  
ANISOU 2931  C   LEU B 357     5494   4796   4744  -1204    885    -27       C  
ATOM   2932  O   LEU B 357      13.020 -14.073 -22.070  1.00 38.09           O  
ANISOU 2932  O   LEU B 357     5872   4070   4527  -1077    259    -65       O  
ATOM   2933  CB  LEU B 357      10.140 -13.489 -20.270  1.00 34.55           C  
ANISOU 2933  CB  LEU B 357     4532   4077   4518  -1110    248   -484       C  
ATOM   2934  CG  LEU B 357       9.404 -14.343 -21.328  1.00 33.09           C  
ANISOU 2934  CG  LEU B 357     4475   3882   4215  -1213    105     -4       C  
ATOM   2935  CD1 LEU B 357       7.919 -14.448 -20.983  1.00 34.86           C  
ANISOU 2935  CD1 LEU B 357     4509   3919   4816   -998    202    -53       C  
ATOM   2936  CD2 LEU B 357       9.605 -13.816 -22.759  1.00 32.31           C  
ANISOU 2936  CD2 LEU B 357     4518   3754   4003  -1087   -283   -172       C  
ATOM   2937  N   LYS B 358      12.379 -11.919 -21.765  1.00 40.77           N  
ANISOU 2937  N   LYS B 358     5754   4631   5104  -1407    643   -195       N  
ATOM   2938  CA  LYS B 358      12.980 -11.426 -23.012  1.00 41.13           C  
ANISOU 2938  CA  LYS B 358     5827   4688   5113  -1628    652   -264       C  
ATOM   2939  C   LYS B 358      14.497 -11.571 -22.984  1.00 43.06           C  
ANISOU 2939  C   LYS B 358     5835   5304   5220  -1552    529   -305       C  
ATOM   2940  O   LYS B 358      15.106 -11.960 -23.986  1.00 41.40           O  
ANISOU 2940  O   LYS B 358     5739   4851   5138  -1766    694    -18       O  
ATOM   2941  CB  LYS B 358      12.601  -9.964 -23.275  1.00 50.78           C  
ANISOU 2941  CB  LYS B 358     7695   4830   6766  -1000      0   -475       C  
ATOM   2942  CG  LYS B 358      11.109  -9.735 -23.498  1.00 60.76           C  
ANISOU 2942  CG  LYS B 358     8337   6310   8437   -313     10   -128       C  
ATOM   2943  CD  LYS B 358      10.785  -9.402 -24.945  1.00 70.50           C  
ANISOU 2943  CD  LYS B 358    10390   7878   8517   -283   -148    -60       C  
ATOM   2944  CE  LYS B 358       9.313  -9.064 -25.134  1.00 72.88           C  
ANISOU 2944  CE  LYS B 358     9591   7638  10460  -1792   -647   -205       C  
ATOM   2945  NZ  LYS B 358       8.915  -7.787 -24.472  1.00 75.66           N  
ANISOU 2945  NZ  LYS B 358    10355   8191  10201   -432  -2078   -718       N  
ATOM   2946  N   TYR B 359      15.091 -11.261 -21.832  1.00 43.43           N  
ANISOU 2946  N   TYR B 359     6175   5163   5164  -1826    563   -123       N  
ATOM   2947  CA  TYR B 359      16.528 -11.426 -21.613  1.00 47.48           C  
ANISOU 2947  CA  TYR B 359     6322   5741   5975  -1618    521   -411       C  
ATOM   2948  C   TYR B 359      16.961 -12.880 -21.827  1.00 44.82           C  
ANISOU 2948  C   TYR B 359     6021   5525   5482  -1925   1080   -125       C  
ATOM   2949  O   TYR B 359      17.975 -13.144 -22.474  1.00 45.21           O  
ANISOU 2949  O   TYR B 359     5453   5811   5913  -2960   1462      0       O  
ATOM   2950  CB  TYR B 359      16.920 -10.956 -20.209  1.00 48.66           C  
ANISOU 2950  CB  TYR B 359     6832   5849   5808  -1909    547   -294       C  
ATOM   2951  CG  TYR B 359      18.395 -11.116 -19.918  1.00 53.24           C  
ANISOU 2951  CG  TYR B 359     6752   6845   6632  -1926    770   -408       C  
ATOM   2952  CD1 TYR B 359      18.901 -12.317 -19.390  1.00 52.21           C  
ANISOU 2952  CD1 TYR B 359     6863   6173   6801  -2488    618   -822       C  
ATOM   2953  CD2 TYR B 359      19.293 -10.074 -20.180  1.00 57.48           C  
ANISOU 2953  CD2 TYR B 359     7704   6866   7267  -2377    890   -465       C  
ATOM   2954  CE1 TYR B 359      20.258 -12.475 -19.136  1.00 57.88           C  
ANISOU 2954  CE1 TYR B 359     6845   7865   7281  -1927    776   -468       C  
ATOM   2955  CE2 TYR B 359      20.651 -10.219 -19.925  1.00 63.66           C  
ANISOU 2955  CE2 TYR B 359     7966   7693   8527  -2221    321   -882       C  
ATOM   2956  CZ  TYR B 359      21.126 -11.418 -19.400  1.00 64.25           C  
ANISOU 2956  CZ  TYR B 359     7984   8034   8392  -2449    598   -331       C  
ATOM   2957  OH  TYR B 359      22.472 -11.567 -19.149  1.00 68.93           O  
ANISOU 2957  OH  TYR B 359     7871   9076   9240  -3915   -827   -899       O  
ATOM   2958  N   ASN B 360      16.193 -13.808 -21.265  1.00 40.83           N  
ANISOU 2958  N   ASN B 360     5212   4991   5309  -1546   1059   -546       N  
ATOM   2959  CA  ASN B 360      16.463 -15.232 -21.392  1.00 36.20           C  
ANISOU 2959  CA  ASN B 360     4486   4724   4542  -1807    911   -361       C  
ATOM   2960  C   ASN B 360      16.327 -15.685 -22.842  1.00 39.36           C  
ANISOU 2960  C   ASN B 360     5179   5102   4671  -1545    685   -398       C  
ATOM   2961  O   ASN B 360      17.124 -16.508 -23.328  1.00 38.46           O  
ANISOU 2961  O   ASN B 360     4526   4951   5134  -1620    986   -158       O  
ATOM   2962  CB  ASN B 360      15.513 -16.039 -20.495  1.00 33.81           C  
ANISOU 2962  CB  ASN B 360     4425   4195   4225  -1614    591   -328       C  
ATOM   2963  CG  ASN B 360      15.807 -15.887 -19.014  1.00 34.38           C  
ANISOU 2963  CG  ASN B 360     4356   4544   4162  -1636    792   -355       C  
ATOM   2964  OD1 ASN B 360      16.852 -15.380 -18.625  1.00 40.41           O  
ANISOU 2964  OD1 ASN B 360     4523   5773   5056  -1787    400   -764       O  
ATOM   2965  ND2 ASN B 360      14.872 -16.329 -18.175  1.00 30.71           N  
ANISOU 2965  ND2 ASN B 360     3675   4015   3978  -1243    590   -558       N  
ATOM   2966  N   PHE B 361      15.317 -15.139 -23.528  1.00 39.18           N  
ANISOU 2966  N   PHE B 361     5440   4644   4802  -1475    559   -160       N  
ATOM   2967  CA  PHE B 361      15.118 -15.401 -24.946  1.00 39.62           C  
ANISOU 2967  CA  PHE B 361     5463   4859   4731  -1457    608   -187       C  
ATOM   2968  C   PHE B 361      16.354 -15.020 -25.762  1.00 43.89           C  
ANISOU 2968  C   PHE B 361     5894   5542   5239  -1847    998   -217       C  
ATOM   2969  O   PHE B 361      16.777 -15.784 -26.625  1.00 45.96           O  
ANISOU 2969  O   PHE B 361     6833   5321   5305  -1762   1375    -68       O  
ATOM   2970  CB  PHE B 361      13.873 -14.685 -25.492  1.00 39.18           C  
ANISOU 2970  CB  PHE B 361     5492   4603   4789  -1643    722    204       C  
ATOM   2971  CG  PHE B 361      13.863 -14.560 -26.990  1.00 41.57           C  
ANISOU 2971  CG  PHE B 361     6076   4924   4795  -1757    556   -279       C  
ATOM   2972  CD1 PHE B 361      13.586 -15.669 -27.793  1.00 38.65           C  
ANISOU 2972  CD1 PHE B 361     5643   4431   4611  -1681      6    222       C  
ATOM   2973  CD2 PHE B 361      14.161 -13.335 -27.608  1.00 46.91           C  
ANISOU 2973  CD2 PHE B 361     7574   4864   5384  -2023    148    -86       C  
ATOM   2974  CE1 PHE B 361      13.605 -15.565 -29.173  1.00 41.07           C  
ANISOU 2974  CE1 PHE B 361     6012   5063   4526  -2427    334   -347       C  
ATOM   2975  CE2 PHE B 361      14.177 -13.224 -28.993  1.00 49.75           C  
ANISOU 2975  CE2 PHE B 361     8111   5300   5489  -2132    257    147       C  
ATOM   2976  CZ  PHE B 361      13.895 -14.340 -29.778  1.00 48.90           C  
ANISOU 2976  CZ  PHE B 361     8044   5244   5291  -1943     86    259       C  
ATOM   2977  N   LEU B 362      16.911 -13.841 -25.490  1.00 47.99           N  
ANISOU 2977  N   LEU B 362     6775   5552   5907  -2133    719    -55       N  
ATOM   2978  CA  LEU B 362      18.106 -13.356 -26.200  1.00 51.36           C  
ANISOU 2978  CA  LEU B 362     6837   6163   6512  -2066   1052   -150       C  
ATOM   2979  C   LEU B 362      19.330 -14.228 -25.940  1.00 45.40           C  
ANISOU 2979  C   LEU B 362     6475   5702   5070  -2344   1244    -96       C  
ATOM   2980  O   LEU B 362      20.067 -14.550 -26.868  1.00 45.04           O  
ANISOU 2980  O   LEU B 362     6480   5467   5164  -2691   1382   -344       O  
ATOM   2981  CB  LEU B 362      18.410 -11.881 -25.860  1.00 51.19           C  
ANISOU 2981  CB  LEU B 362     7140   6171   6136  -2391    704   -172       C  
ATOM   2982  CG  LEU B 362      17.409 -10.789 -26.273  1.00 51.38           C  
ANISOU 2982  CG  LEU B 362     7637   5963   5921  -2372    516   -145       C  
ATOM   2983  CD1 LEU B 362      17.892  -9.416 -25.796  1.00 54.70           C  
ANISOU 2983  CD1 LEU B 362     8108   5746   6927  -2281    611   -142       C  
ATOM   2984  CD2 LEU B 362      17.155 -10.776 -27.779  1.00 50.57           C  
ANISOU 2984  CD2 LEU B 362     7575   5725   5911  -2230    567   -156       C  
ATOM   2985  N   PHE B 363      19.536 -14.611 -24.683  1.00 42.23           N  
ANISOU 2985  N   PHE B 363     5665   5344   5037  -2497   1053   -191       N  
ATOM   2986  CA  PHE B 363      20.633 -15.507 -24.330  1.00 45.20           C  
ANISOU 2986  CA  PHE B 363     5485   6046   5639  -2469    817   -230       C  
ATOM   2987  C   PHE B 363      20.536 -16.846 -25.080  1.00 46.43           C  
ANISOU 2987  C   PHE B 363     5571   6580   5488  -2261   1150   -600       C  
ATOM   2988  O   PHE B 363      21.524 -17.324 -25.637  1.00 46.39           O  
ANISOU 2988  O   PHE B 363     4403   7216   6004  -3156   1049   -844       O  
ATOM   2989  CB  PHE B 363      20.680 -15.721 -22.810  1.00 48.26           C  
ANISOU 2989  CB  PHE B 363     5781   7085   5469  -2183   1116   -652       C  
ATOM   2990  CG  PHE B 363      21.736 -16.694 -22.367  1.00 53.94           C  
ANISOU 2990  CG  PHE B 363     6574   7371   6549  -1741    898   -507       C  
ATOM   2991  CD1 PHE B 363      23.041 -16.259 -22.108  1.00 58.00           C  
ANISOU 2991  CD1 PHE B 363     6877   8328   6832  -1979    670   -617       C  
ATOM   2992  CD2 PHE B 363      21.435 -18.047 -22.211  1.00 54.70           C  
ANISOU 2992  CD2 PHE B 363     6535   7630   6618  -2220    603   -365       C  
ATOM   2993  CE1 PHE B 363      24.019 -17.161 -21.706  1.00 59.95           C  
ANISOU 2993  CE1 PHE B 363     7043   8656   7079  -1752    339   -708       C  
ATOM   2994  CE2 PHE B 363      22.409 -18.955 -21.816  1.00 57.79           C  
ANISOU 2994  CE2 PHE B 363     6747   8357   6854  -1738    890   -156       C  
ATOM   2995  CZ  PHE B 363      23.701 -18.510 -21.559  1.00 63.64           C  
ANISOU 2995  CZ  PHE B 363     7099   8946   8132  -2139    506    -47       C  
ATOM   2996  N   LEU B 364      19.345 -17.446 -25.093  1.00 41.72           N  
ANISOU 2996  N   LEU B 364     5172   5325   5353  -1771    968   -362       N  
ATOM   2997  CA  LEU B 364      19.153 -18.720 -25.765  1.00 41.07           C  
ANISOU 2997  CA  LEU B 364     5260   5591   4754  -1841   1164   -356       C  
ATOM   2998  C   LEU B 364      19.217 -18.600 -27.271  1.00 40.03           C  
ANISOU 2998  C   LEU B 364     4988   5418   4802  -1763   1111   -270       C  
ATOM   2999  O   LEU B 364      19.745 -19.500 -27.931  1.00 39.43           O  
ANISOU 2999  O   LEU B 364     5025   5336   4620  -1473    889   -369       O  
ATOM   3000  CB  LEU B 364      17.838 -19.399 -25.328  1.00 42.43           C  
ANISOU 3000  CB  LEU B 364     5271   5657   5192  -1786   1348   -205       C  
ATOM   3001  CG  LEU B 364      17.792 -19.791 -23.845  1.00 41.11           C  
ANISOU 3001  CG  LEU B 364     4928   5550   5142  -1616   1079   -145       C  
ATOM   3002  CD1 LEU B 364      16.360 -20.056 -23.407  1.00 37.65           C  
ANISOU 3002  CD1 LEU B 364     4630   5196   4477  -1142   1029   -411       C  
ATOM   3003  CD2 LEU B 364      18.681 -20.999 -23.553  1.00 41.90           C  
ANISOU 3003  CD2 LEU B 364     4920   5959   5041  -1127    549   -773       C  
ATOM   3004  N   ASP B 365      18.692 -17.493 -27.812  1.00 38.55           N  
ANISOU 3004  N   ASP B 365     4904   5277   4465  -1990   1119   -199       N  
ATOM   3005  CA  ASP B 365      18.705 -17.267 -29.259  1.00 40.05           C  
ANISOU 3005  CA  ASP B 365     5743   5118   4355  -2389   1114   -257       C  
ATOM   3006  C   ASP B 365      20.138 -17.158 -29.758  1.00 45.03           C  
ANISOU 3006  C   ASP B 365     5803   6430   4876  -1992   1329   -329       C  
ATOM   3007  O   ASP B 365      20.470 -17.714 -30.799  1.00 42.89           O  
ANISOU 3007  O   ASP B 365     5566   5979   4749  -2454   1284   -256       O  
ATOM   3008  CB  ASP B 365      17.876 -16.043 -29.666  1.00 46.88           C  
ANISOU 3008  CB  ASP B 365     6622   5918   5272  -1587   1161   -363       C  
ATOM   3009  CG  ASP B 365      17.692 -15.927 -31.175  1.00 49.35           C  
ANISOU 3009  CG  ASP B 365     6939   6384   5428  -1888    841   -422       C  
ATOM   3010  OD1 ASP B 365      17.411 -16.940 -31.842  1.00 45.25           O  
ANISOU 3010  OD1 ASP B 365     6337   5874   4981  -1347    933   -177       O  
ATOM   3011  OD2 ASP B 365      17.820 -14.806 -31.701  1.00 57.22           O  
ANISOU 3011  OD2 ASP B 365     8085   7202   6452  -2164   1714    262       O  
ATOM   3012  N   SER B 366      20.977 -16.464 -28.989  1.00 48.16           N  
ANISOU 3012  N   SER B 366     6615   6042   5642  -2275   1068   -387       N  
ATOM   3013  CA  SER B 366      22.411 -16.373 -29.269  1.00 52.00           C  
ANISOU 3013  CA  SER B 366     6834   7172   5748  -2379   1523   -217       C  
ATOM   3014  C   SER B 366      23.090 -17.744 -29.259  1.00 50.44           C  
ANISOU 3014  C   SER B 366     6425   7301   5439  -2128   1594   -447       C  
ATOM   3015  O   SER B 366      23.859 -18.055 -30.165  1.00 49.38           O  
ANISOU 3015  O   SER B 366     6391   6823   5549  -2719   1987    119       O  
ATOM   3016  CB  SER B 366      23.101 -15.434 -28.282  1.00 57.42           C  
ANISOU 3016  CB  SER B 366     7843   7971   6000  -3023   1477   -739       C  
ATOM   3017  OG  SER B 366      24.514 -15.565 -28.375  1.00 67.32           O  
ANISOU 3017  OG  SER B 366     8674   9689   7213  -2022   1795  -1301       O  
ATOM   3018  N   LYS B 367      22.787 -18.550 -28.240  1.00 48.07           N  
ANISOU 3018  N   LYS B 367     6056   6988   5219  -1934   1336   -582       N  
ATOM   3019  CA  LYS B 367      23.361 -19.881 -28.093  1.00 50.87           C  
ANISOU 3019  CA  LYS B 367     6066   7276   5986  -1886    965   -494       C  
ATOM   3020  C   LYS B 367      22.926 -20.830 -29.220  1.00 52.22           C  
ANISOU 3020  C   LYS B 367     6384   7723   5734  -1728   1154   -608       C  
ATOM   3021  O   LYS B 367      23.744 -21.610 -29.724  1.00 53.25           O  
ANISOU 3021  O   LYS B 367     5992   8025   6214  -1721   1586   -484       O  
ATOM   3022  CB  LYS B 367      23.031 -20.457 -26.707  1.00 56.72           C  
ANISOU 3022  CB  LYS B 367     6400   8928   6222  -1983   1617   -343       C  
ATOM   3023  CG  LYS B 367      23.835 -21.691 -26.281  1.00 66.69           C  
ANISOU 3023  CG  LYS B 367     8595   9682   7061  -1441    696    215       C  
ATOM   3024  CD  LYS B 367      25.360 -21.507 -26.261  1.00 72.70           C  
ANISOU 3024  CD  LYS B 367     8715  10891   8015  -2080   2183   -423       C  
ATOM   3025  CE  LYS B 367      25.859 -20.346 -25.398  1.00 76.21           C  
ANISOU 3025  CE  LYS B 367     8667  11035   9252  -1998   1185   -577       C  
ATOM   3026  NZ  LYS B 367      25.516 -20.478 -23.955  1.00 84.30           N  
ANISOU 3026  NZ  LYS B 367    10175  12567   9287  -1659    757    232       N  
ATOM   3027  N   LEU B 368      21.652 -20.749 -29.618  1.00 45.48           N  
ANISOU 3027  N   LEU B 368     6131   6195   4953  -1607   1344   -566       N  
ATOM   3028  CA  LEU B 368      21.155 -21.545 -30.737  1.00 46.90           C  
ANISOU 3028  CA  LEU B 368     6247   6658   4911  -1795    980   -252       C  
ATOM   3029  C   LEU B 368      21.853 -21.198 -32.048  1.00 49.03           C  
ANISOU 3029  C   LEU B 368     6302   7199   5126  -1715   1391   -582       C  
ATOM   3030  O   LEU B 368      22.144 -22.091 -32.841  1.00 49.57           O  
ANISOU 3030  O   LEU B 368     6357   7503   4972  -1347   1336   -666       O  
ATOM   3031  CB  LEU B 368      19.631 -21.433 -30.893  1.00 47.63           C  
ANISOU 3031  CB  LEU B 368     6325   6343   5427  -1627   1008   -468       C  
ATOM   3032  CG  LEU B 368      18.957 -22.208 -32.039  1.00 47.43           C  
ANISOU 3032  CG  LEU B 368     6461   6408   5151  -1684   1079   -326       C  
ATOM   3033  CD1 LEU B 368      19.152 -23.721 -31.924  1.00 45.08           C  
ANISOU 3033  CD1 LEU B 368     5692   6294   5141  -1605   1300   -392       C  
ATOM   3034  CD2 LEU B 368      17.479 -21.874 -32.149  1.00 46.89           C  
ANISOU 3034  CD2 LEU B 368     7005   5250   5560   -666    644   -355       C  
ATOM   3035  N   GLN B 369      22.121 -19.910 -32.263  1.00 53.30           N  
ANISOU 3035  N   GLN B 369     6896   7440   5914  -2136   1011   -124       N  
ATOM   3036  CA  GLN B 369      22.786 -19.461 -33.489  1.00 60.60           C  
ANISOU 3036  CA  GLN B 369     8142   8722   6160  -1921   1854   -295       C  
ATOM   3037  C   GLN B 369      24.225 -19.961 -33.588  1.00 60.95           C  
ANISOU 3037  C   GLN B 369     7829   8783   6543  -2168   1687   -306       C  
ATOM   3038  O   GLN B 369      24.661 -20.352 -34.675  1.00 61.60           O  
ANISOU 3038  O   GLN B 369     8057   8738   6609  -2191   1793   -412       O  
ATOM   3039  CB  GLN B 369      22.698 -17.938 -33.675  1.00 63.57           C  
ANISOU 3039  CB  GLN B 369     8836   8642   6675  -2360   2040   -491       C  
ATOM   3040  CG  GLN B 369      21.280 -17.346 -33.709  1.00 70.31           C  
ANISOU 3040  CG  GLN B 369     9473   9141   8099  -2061   1092   -182       C  
ATOM   3041  CD  GLN B 369      20.195 -18.273 -34.269  1.00 69.79           C  
ANISOU 3041  CD  GLN B 369     9211   9695   7610  -2271   1603   -239       C  
ATOM   3042  OE1 GLN B 369      20.318 -18.811 -35.371  1.00 76.57           O  
ANISOU 3042  OE1 GLN B 369    10227  11400   7465  -1771   1717   -495       O  
ATOM   3043  NE2 GLN B 369      19.114 -18.441 -33.509  1.00 59.25           N  
ANISOU 3043  NE2 GLN B 369     8282   7670   6559  -1786    887    -61       N  
ATOM   3044  N   GLU B 370      24.942 -19.953 -32.458  1.00 57.79           N  
ANISOU 3044  N   GLU B 370     8061   7921   5973  -2075   2116   -659       N  
ATOM   3045  CA  GLU B 370      26.258 -20.600 -32.342  1.00 62.33           C  
ANISOU 3045  CA  GLU B 370     7561   9157   6963  -2164   1712   -726       C  
ATOM   3046  C   GLU B 370      26.194 -22.059 -32.790  1.00 58.41           C  
ANISOU 3046  C   GLU B 370     7099   8939   6153  -1803   2164   -595       C  
ATOM   3047  O   GLU B 370      27.007 -22.492 -33.599  1.00 60.23           O  
ANISOU 3047  O   GLU B 370     7089   9333   6462  -1592   2359     67       O  
ATOM   3048  CB  GLU B 370      26.765 -20.558 -30.904  1.00 68.75           C  
ANISOU 3048  CB  GLU B 370     8693  10422   7006  -1584   1537  -1048       C  
ATOM   3049  CG  GLU B 370      27.487 -19.286 -30.490  1.00 76.35           C  
ANISOU 3049  CG  GLU B 370     8885  10960   9162  -2879   1990   -563       C  
ATOM   3050  CD  GLU B 370      27.898 -19.295 -29.022  1.00 89.96           C  
ANISOU 3050  CD  GLU B 370    11332  12839  10007  -1957    332   -205       C  
ATOM   3051  OE1 GLU B 370      28.455 -18.276 -28.558  1.00 99.73           O  
ANISOU 3051  OE1 GLU B 370    12707  13246  11939  -2241   -618   -501       O  
ATOM   3052  OE2 GLU B 370      27.670 -20.311 -28.324  1.00 84.41           O  
ANISOU 3052  OE2 GLU B 370    10513  12931   8627  -1727   -805   -219       O  
ATOM   3053  N   ILE B 371      25.206 -22.789 -32.268  1.00 55.41           N  
ANISOU 3053  N   ILE B 371     7002   8075   5974  -1618   1571   -646       N  
ATOM   3054  CA  ILE B 371      24.988 -24.210 -32.559  1.00 54.73           C  
ANISOU 3054  CA  ILE B 371     6991   8019   5783  -1363   1648   -733       C  
ATOM   3055  C   ILE B 371      24.679 -24.462 -34.040  1.00 58.33           C  
ANISOU 3055  C   ILE B 371     7599   8629   5933  -1267   1577   -908       C  
ATOM   3056  O   ILE B 371      25.211 -25.404 -34.643  1.00 56.18           O  
ANISOU 3056  O   ILE B 371     6420   8720   6207  -1375   2088   -632       O  
ATOM   3057  CB  ILE B 371      23.866 -24.796 -31.653  1.00 54.64           C  
ANISOU 3057  CB  ILE B 371     6953   7973   5832  -1258   1868  -1036       C  
ATOM   3058  CG1 ILE B 371      24.317 -24.811 -30.182  1.00 56.49           C  
ANISOU 3058  CG1 ILE B 371     6783   8579   6101  -1370   1521   -292       C  
ATOM   3059  CG2 ILE B 371      23.452 -26.201 -32.090  1.00 54.29           C  
ANISOU 3059  CG2 ILE B 371     7188   8067   5371  -1559   1686   -773       C  
ATOM   3060  CD1 ILE B 371      23.201 -25.033 -29.174  1.00 54.51           C  
ANISOU 3060  CD1 ILE B 371     7000   8388   5323   -777   1222   -112       C  
ATOM   3061  N   LEU B 372      23.829 -23.616 -34.619  1.00 56.40           N  
ANISOU 3061  N   LEU B 372     7601   8171   5654  -1474   1864   -817       N  
ATOM   3062  CA  LEU B 372      23.343 -23.830 -35.975  1.00 57.14           C  
ANISOU 3062  CA  LEU B 372     7709   8324   5676  -1587   1617   -758       C  
ATOM   3063  C   LEU B 372      24.285 -23.333 -37.068  1.00 62.13           C  
ANISOU 3063  C   LEU B 372     8529   9095   5980  -1797   2335   -950       C  
ATOM   3064  O   LEU B 372      24.160 -23.752 -38.217  1.00 61.47           O  
ANISOU 3064  O   LEU B 372     8129   9369   5858  -2017   2521   -893       O  
ATOM   3065  CB  LEU B 372      21.935 -23.251 -36.159  1.00 53.65           C  
ANISOU 3065  CB  LEU B 372     7641   7851   4893  -1597   1943   -966       C  
ATOM   3066  CG  LEU B 372      20.781 -23.890 -35.373  1.00 53.78           C  
ANISOU 3066  CG  LEU B 372     7360   7536   5538  -1934   1485   -279       C  
ATOM   3067  CD1 LEU B 372      19.485 -23.183 -35.723  1.00 55.60           C  
ANISOU 3067  CD1 LEU B 372     7854   7441   5828  -1465   1844    -48       C  
ATOM   3068  CD2 LEU B 372      20.636 -25.386 -35.621  1.00 57.21           C  
ANISOU 3068  CD2 LEU B 372     8398   7771   5565  -1341   1573   -768       C  
ATOM   3069  N   GLU B 373      25.213 -22.441 -36.718  1.00 71.55           N  
ANISOU 3069  N   GLU B 373     9375  10090   7719  -2147   1783  -1386       N  
ATOM   3070  CA  GLU B 373      26.182 -21.933 -37.694  1.00 81.01           C  
ANISOU 3070  CA  GLU B 373    10268  11866   8646  -2395   2574   -375       C  
ATOM   3071  C   GLU B 373      27.443 -22.789 -37.696  1.00 86.67           C  
ANISOU 3071  C   GLU B 373    10345  11907  10679  -2117   2423   -967       C  
ATOM   3072  O   GLU B 373      27.449 -23.884 -38.257  1.00 84.07           O  
ANISOU 3072  O   GLU B 373     9018  12119  10803  -1779    606  -1375       O  
ATOM   3073  CB  GLU B 373      26.523 -20.463 -37.440  1.00 83.82           C  
ANISOU 3073  CB  GLU B 373     9855  12291   9700  -2618   2637  -1195       C  
ATOM   3074  CG  GLU B 373      27.030 -19.738 -38.687  1.00 95.23           C  
ANISOU 3074  CG  GLU B 373    12041  13767  10373  -2611   2223    127       C  
ATOM   3075  CD  GLU B 373      27.297 -18.255 -38.472  1.00 99.10           C  
ANISOU 3075  CD  GLU B 373    12231  14152  11270  -3036   1760   -562       C  
ATOM   3076  OE1 GLU B 373      27.202 -17.490 -39.459  1.00 96.36           O  
ANISOU 3076  OE1 GLU B 373    11523  13830  11257  -5167   1749   -344       O  
ATOM   3077  OE2 GLU B 373      27.607 -17.848 -37.329  1.00100.35           O  
ANISOU 3077  OE2 GLU B 373    12556  14240  11332  -1693   1961  -1307       O  
TER    3078      GLU B 373                                                      
ATOM   3079  O5'  DA C   1      46.727 -26.416 -12.832  1.00 68.49           O  
ANISOU 3079  O5'  DA C   1     1429  14483  10111    683  -1316    -23       O  
ATOM   3080  C5'  DA C   1      46.336 -27.796 -12.690  1.00 79.55           C  
ANISOU 3080  C5'  DA C   1     6376  13624  10225   2133   1020   -719       C  
ATOM   3081  C4'  DA C   1      45.001 -28.075 -13.350  1.00 93.37           C  
ANISOU 3081  C4'  DA C   1     7574  16124  11778    854    443  -1809       C  
ATOM   3082  O4'  DA C   1      44.182 -28.871 -12.464  1.00 87.69           O  
ANISOU 3082  O4'  DA C   1     7569  14044  11703   1910   1250  -2296       O  
ATOM   3083  C3'  DA C   1      44.138 -26.870 -13.726  1.00 98.58           C  
ANISOU 3083  C3'  DA C   1     8420  16542  12491   1286   1071  -1170       C  
ATOM   3084  O3'  DA C   1      43.351 -27.169 -14.888  1.00106.71           O  
ANISOU 3084  O3'  DA C   1     9429  17457  13658    -67    144   -854       O  
ATOM   3085  C2'  DA C   1      43.224 -26.699 -12.523  1.00 92.01           C  
ANISOU 3085  C2'  DA C   1     8300  14951  11706   1742    548  -1098       C  
ATOM   3086  C1'  DA C   1      43.074 -28.118 -11.981  1.00 84.89           C  
ANISOU 3086  C1'  DA C   1     7158  14803  10291    664   1136  -1953       C  
ATOM   3087  N9   DA C   1      43.039 -28.269 -10.521  1.00 70.21           N  
ANISOU 3087  N9   DA C   1     5067  11335  10271   1263    419  -1992       N  
ATOM   3088  C8   DA C   1      42.482 -29.328  -9.849  1.00 60.62           C  
ANISOU 3088  C8   DA C   1     3441  11527   8064   1933    178  -1929       C  
ATOM   3089  N7   DA C   1      42.593 -29.247  -8.546  1.00 55.07           N  
ANISOU 3089  N7   DA C   1     2960   9958   8005   1918      5  -2075       N  
ATOM   3090  C5   DA C   1      43.276 -28.058  -8.343  1.00 56.62           C  
ANISOU 3090  C5   DA C   1     2676  10709   8126   1410   -146  -2115       C  
ATOM   3091  C6   DA C   1      43.705 -27.404  -7.176  1.00 53.94           C  
ANISOU 3091  C6   DA C   1     1833  11004   7656   1243    436  -2215       C  
ATOM   3092  N6   DA C   1      43.505 -27.883  -5.946  1.00 45.71           N  
ANISOU 3092  N6   DA C   1     1181   8687   7499    456    205  -2532       N  
ATOM   3093  N1   DA C   1      44.359 -26.231  -7.316  1.00 60.44           N  
ANISOU 3093  N1   DA C   1     3667  10755   8540    969   -956  -2185       N  
ATOM   3094  C2   DA C   1      44.573 -25.761  -8.551  1.00 64.46           C  
ANISOU 3094  C2   DA C   1     5793   9446   9251   1282   -352  -1659       C  
ATOM   3095  N3   DA C   1      44.216 -26.281  -9.725  1.00 67.99           N  
ANISOU 3095  N3   DA C   1     4397  11925   9508    857  -1173  -1672       N  
ATOM   3096  C4   DA C   1      43.564 -27.445  -9.551  1.00 67.21           C  
ANISOU 3096  C4   DA C   1     4916  11867   8753   1551   -473  -1123       C  
ATOM   3097  P    DT C   2      43.946 -26.955 -16.374  1.00102.89           P  
ANISOU 3097  P    DT C   2     8414  17366  13312   1101    456  -1973       P  
ATOM   3098  OP1  DT C   2      43.969 -28.274 -17.053  1.00 91.31           O  
ANISOU 3098  OP1  DT C   2     6462  16726  11503   1895    687  -1015       O  
ATOM   3099  OP2  DT C   2      45.195 -26.157 -16.279  1.00110.01           O  
ANISOU 3099  OP2  DT C   2     9638  18298  13864   -171   1533   -436       O  
ATOM   3100  O5'  DT C   2      42.825 -26.083 -17.098  1.00 97.47           O  
ANISOU 3100  O5'  DT C   2     8595  17033  11404    646   1035  -1618       O  
ATOM   3101  C5'  DT C   2      42.170 -24.987 -16.435  1.00 90.51           C  
ANISOU 3101  C5'  DT C   2     7622  16203  10565    409    499  -1544       C  
ATOM   3102  C4'  DT C   2      40.708 -24.931 -16.818  1.00 89.29           C  
ANISOU 3102  C4'  DT C   2     7545  15070  11310    628    815  -1777       C  
ATOM   3103  O4'  DT C   2      40.415 -25.878 -17.872  1.00 88.55           O  
ANISOU 3103  O4'  DT C   2     7124  14791  11729    863    944  -2109       O  
ATOM   3104  C3'  DT C   2      39.733 -25.241 -15.678  1.00 83.57           C  
ANISOU 3104  C3'  DT C   2     6744  14226  10783    879    123  -1568       C  
ATOM   3105  O3'  DT C   2      38.808 -24.164 -15.512  1.00 76.96           O  
ANISOU 3105  O3'  DT C   2     5590  13899   9749    377   -135  -1247       O  
ATOM   3106  C2'  DT C   2      39.025 -26.513 -16.114  1.00 84.91           C  
ANISOU 3106  C2'  DT C   2     6519  14377  11367    796   -617  -1108       C  
ATOM   3107  C1'  DT C   2      39.153 -26.462 -17.623  1.00 91.97           C  
ANISOU 3107  C1'  DT C   2     7717  15679  11548    414   1000  -1645       C  
ATOM   3108  N1   DT C   2      39.117 -27.779 -18.293  1.00101.98           N  
ANISOU 3108  N1   DT C   2     9989  16245  12512    472   1299  -2270       N  
ATOM   3109  C2   DT C   2      38.081 -28.042 -19.164  1.00107.92           C  
ANISOU 3109  C2   DT C   2     9911  17463  13630    399    784  -1788       C  
ATOM   3110  O2   DT C   2      37.192 -27.242 -19.405  1.00111.59           O  
ANISOU 3110  O2   DT C   2    10075  17739  14581    112   -930  -1673       O  
ATOM   3111  N3   DT C   2      38.126 -29.285 -19.746  1.00114.04           N  
ANISOU 3111  N3   DT C   2    10969  17754  14605    296   -219  -2327       N  
ATOM   3112  C4   DT C   2      39.079 -30.268 -19.548  1.00116.79           C  
ANISOU 3112  C4   DT C   2    11682  18089  14602    952   1242  -2429       C  
ATOM   3113  O4   DT C   2      38.989 -31.340 -20.142  1.00119.82           O  
ANISOU 3113  O4   DT C   2    12616  18572  14338   1077   2864  -2964       O  
ATOM   3114  C5   DT C   2      40.137 -29.923 -18.622  1.00116.46           C  
ANISOU 3114  C5   DT C   2    11373  18016  14859    920   1260  -2423       C  
ATOM   3115  C7   DT C   2      41.217 -30.922 -18.344  1.00113.38           C  
ANISOU 3115  C7   DT C   2    10521  18285  14272    875   1108  -3541       C  
ATOM   3116  C6   DT C   2      40.103 -28.712 -18.050  1.00110.00           C  
ANISOU 3116  C6   DT C   2     9914  17577  14304    729    484  -2012       C  
ATOM   3117  P    DT C   3      39.073 -23.055 -14.391  1.00 80.76           P  
ANISOU 3117  P    DT C   3     6517  13762  10405    344   -743  -1098       P  
ATOM   3118  OP1  DT C   3      37.815 -22.290 -14.178  1.00 81.20           O  
ANISOU 3118  OP1  DT C   3     6914  14351   9587    273   2357     96       O  
ATOM   3119  OP2  DT C   3      40.320 -22.331 -14.747  1.00 88.62           O  
ANISOU 3119  OP2  DT C   3     7615  14333  11720    380   -437   1191       O  
ATOM   3120  O5'  DT C   3      39.382 -23.931 -13.099  1.00 70.78           O  
ANISOU 3120  O5'  DT C   3     3977  12816  10098    738   -152  -1941       O  
ATOM   3121  C5'  DT C   3      38.386 -24.786 -12.515  1.00 70.04           C  
ANISOU 3121  C5'  DT C   3     5211  12367   9034    691    213  -1481       C  
ATOM   3122  C4'  DT C   3      38.271 -24.483 -11.041  1.00 65.87           C  
ANISOU 3122  C4'  DT C   3     4596  11464   8968   1060   -645  -1814       C  
ATOM   3123  O4'  DT C   3      39.555 -24.684 -10.408  1.00 55.27           O  
ANISOU 3123  O4'  DT C   3     3381  10094   7525    902    802  -1584       O  
ATOM   3124  C3'  DT C   3      37.854 -23.049 -10.724  1.00 67.25           C  
ANISOU 3124  C3'  DT C   3     4780  11676   9095   1417   -280  -2023       C  
ATOM   3125  O3'  DT C   3      36.940 -23.059  -9.640  1.00 71.10           O  
ANISOU 3125  O3'  DT C   3     5532  12285   9196    742    262   -766       O  
ATOM   3126  C2'  DT C   3      39.138 -22.368 -10.290  1.00 70.24           C  
ANISOU 3126  C2'  DT C   3     5017  11467  10201    771    -51  -1631       C  
ATOM   3127  C1'  DT C   3      39.976 -23.507  -9.733  1.00 62.02           C  
ANISOU 3127  C1'  DT C   3     4181  10938   8443    499    286  -2093       C  
ATOM   3128  N1   DT C   3      41.420 -23.329  -9.983  1.00 57.84           N  
ANISOU 3128  N1   DT C   3     3718   9790   8469   1305   -173  -1784       N  
ATOM   3129  C2   DT C   3      42.260 -23.119  -8.909  1.00 58.51           C  
ANISOU 3129  C2   DT C   3     4175  10043   8012   1506      9  -2081       C  
ATOM   3130  O2   DT C   3      41.878 -23.111  -7.749  1.00 54.14           O  
ANISOU 3130  O2   DT C   3     3967   8605   7997   2360    177  -2779       O  
ATOM   3131  N3   DT C   3      43.579 -22.937  -9.244  1.00 65.40           N  
ANISOU 3131  N3   DT C   3     3925  11577   9343    889   -698   -747       N  
ATOM   3132  C4   DT C   3      44.131 -22.950 -10.513  1.00 70.82           C  
ANISOU 3132  C4   DT C   3     5277  11956   9672   1205   -150  -1192       C  
ATOM   3133  O4   DT C   3      45.335 -22.773 -10.661  1.00 65.98           O  
ANISOU 3133  O4   DT C   3     5052  11427   8589   2268      7  -1734       O  
ATOM   3134  C5   DT C   3      43.192 -23.168 -11.591  1.00 74.72           C  
ANISOU 3134  C5   DT C   3     4936  13432  10020    120    211  -1708       C  
ATOM   3135  C7   DT C   3      43.692 -23.180 -13.001  1.00 65.03           C  
ANISOU 3135  C7   DT C   3     3854  11767   9086  -1599  -1404  -2857       C  
ATOM   3136  C6   DT C   3      41.901 -23.340 -11.277  1.00 66.68           C  
ANISOU 3136  C6   DT C   3     4852  11834   8647    245      7  -1247       C  
ATOM   3137  P    DT C   4      35.971 -21.820  -9.419  1.00 73.68           P  
ANISOU 3137  P    DT C   4     6376  11899   9720    612    345  -1592       P  
ATOM   3138  OP1  DT C   4      35.670 -21.213 -10.743  1.00 78.58           O  
ANISOU 3138  OP1  DT C   4     7270  12573  10011    697    113  -1466       O  
ATOM   3139  OP2  DT C   4      36.555 -20.979  -8.340  1.00 74.52           O  
ANISOU 3139  OP2  DT C   4     6167  11051  11094    249  -1673   -591       O  
ATOM   3140  O5'  DT C   4      34.636 -22.522  -8.910  1.00 65.14           O  
ANISOU 3140  O5'  DT C   4     4596  10492   9659   1017  -1305  -1547       O  
ATOM   3141  C5'  DT C   4      34.240 -23.820  -9.408  1.00 60.26           C  
ANISOU 3141  C5'  DT C   4     4124  10301   8469    913     -9  -1547       C  
ATOM   3142  C4'  DT C   4      33.159 -24.412  -8.529  1.00 55.17           C  
ANISOU 3142  C4'  DT C   4     4496   9011   7452   1133   -327  -1632       C  
ATOM   3143  O4'  DT C   4      33.741 -25.229  -7.483  1.00 49.13           O  
ANISOU 3143  O4'  DT C   4     3983   7923   6762    831    -88  -2061       O  
ATOM   3144  C3'  DT C   4      32.276 -23.389  -7.816  1.00 52.29           C  
ANISOU 3144  C3'  DT C   4     3973   8766   7127    675   -258  -1500       C  
ATOM   3145  O3'  DT C   4      30.969 -23.923  -7.653  1.00 48.01           O  
ANISOU 3145  O3'  DT C   4     3025   8245   6971   1854   -432  -1862       O  
ATOM   3146  C2'  DT C   4      32.927 -23.272  -6.447  1.00 48.60           C  
ANISOU 3146  C2'  DT C   4     3409   8030   7023   1253   -165  -1821       C  
ATOM   3147  C1'  DT C   4      33.452 -24.682  -6.199  1.00 45.90           C  
ANISOU 3147  C1'  DT C   4     2770   8133   6533   1333   -330  -1779       C  
ATOM   3148  N1   DT C   4      34.695 -24.727  -5.401  1.00 43.93           N  
ANISOU 3148  N1   DT C   4     3137   7415   6138   1561   -337  -1732       N  
ATOM   3149  C2   DT C   4      34.651 -25.193  -4.104  1.00 43.47           C  
ANISOU 3149  C2   DT C   4     2963   7587   5964   1671   -422  -1796       C  
ATOM   3150  O2   DT C   4      33.626 -25.581  -3.568  1.00 44.02           O  
ANISOU 3150  O2   DT C   4     2934   7652   6139   1329   -401  -2059       O  
ATOM   3151  N3   DT C   4      35.862 -25.195  -3.455  1.00 43.15           N  
ANISOU 3151  N3   DT C   4     2898   7622   5875   1425   -317  -1972       N  
ATOM   3152  C4   DT C   4      37.081 -24.785  -3.960  1.00 43.30           C  
ANISOU 3152  C4   DT C   4     2749   7537   6165   1895   -285  -1858       C  
ATOM   3153  O4   DT C   4      38.087 -24.841  -3.256  1.00 44.23           O  
ANISOU 3153  O4   DT C   4     3116   7544   6144   1578   -490  -1591       O  
ATOM   3154  C5   DT C   4      37.055 -24.315  -5.331  1.00 42.65           C  
ANISOU 3154  C5   DT C   4     2595   7445   6163   1884   -415  -1857       C  
ATOM   3155  C7   DT C   4      38.323 -23.839  -5.966  1.00 40.86           C  
ANISOU 3155  C7   DT C   4     2729   7660   5134   1543   -506  -2140       C  
ATOM   3156  C6   DT C   4      35.877 -24.303  -5.968  1.00 42.88           C  
ANISOU 3156  C6   DT C   4     2724   7693   5875   1422   -493  -2139       C  
ATOM   3157  P    DT C   5      29.905 -23.951  -8.861  1.00 47.22           P  
ANISOU 3157  P    DT C   5     3347   8140   6452   1186   -304  -1452       P  
ATOM   3158  OP1  DT C   5      29.077 -25.164  -8.680  1.00 49.50           O  
ANISOU 3158  OP1  DT C   5     4239   7108   7459   1098  -1776  -2065       O  
ATOM   3159  OP2  DT C   5      30.575 -23.691 -10.149  1.00 46.42           O  
ANISOU 3159  OP2  DT C   5     2258   8851   6527   1009   -274  -1706       O  
ATOM   3160  O5'  DT C   5      29.035 -22.647  -8.588  1.00 44.25           O  
ANISOU 3160  O5'  DT C   5     3241   7522   6047    978   -517  -1400       O  
ATOM   3161  C5'  DT C   5      28.190 -22.549  -7.443  1.00 37.73           C  
ANISOU 3161  C5'  DT C   5     2491   6039   5804   1039   -769  -1355       C  
ATOM   3162  C4'  DT C   5      27.022 -21.636  -7.747  1.00 35.99           C  
ANISOU 3162  C4'  DT C   5     2386   5995   5291    874   -777  -1097       C  
ATOM   3163  O4'  DT C   5      27.500 -20.291  -8.020  1.00 36.26           O  
ANISOU 3163  O4'  DT C   5     2229   5959   5589    507   -747  -1305       O  
ATOM   3164  C3'  DT C   5      26.173 -22.045  -8.956  1.00 34.23           C  
ANISOU 3164  C3'  DT C   5     2224   5291   5489    720   -713  -1237       C  
ATOM   3165  O3'  DT C   5      24.799 -21.907  -8.605  1.00 35.51           O  
ANISOU 3165  O3'  DT C   5     2392   5545   5551    530   -356  -1209       O  
ATOM   3166  C2'  DT C   5      26.494 -20.985  -9.998  1.00 37.16           C  
ANISOU 3166  C2'  DT C   5     2681   6169   5268    443   -377  -1208       C  
ATOM   3167  C1'  DT C   5      26.778 -19.775  -9.123  1.00 38.33           C  
ANISOU 3167  C1'  DT C   5     2650   6255   5659    198  -1089  -1135       C  
ATOM   3168  N1   DT C   5      27.591 -18.714  -9.782  1.00 39.63           N  
ANISOU 3168  N1   DT C   5     2777   6738   5543     25  -1000  -1321       N  
ATOM   3169  C2   DT C   5      26.943 -17.568 -10.198  1.00 40.24           C  
ANISOU 3169  C2   DT C   5     3026   6460   5803   -296  -1138  -1264       C  
ATOM   3170  O2   DT C   5      25.755 -17.368 -10.015  1.00 40.94           O  
ANISOU 3170  O2   DT C   5     3227   6458   5871     14  -1118  -1237       O  
ATOM   3171  N3   DT C   5      27.743 -16.658 -10.839  1.00 42.71           N  
ANISOU 3171  N3   DT C   5     3332   6602   6294   -799  -1096  -1571       N  
ATOM   3172  C4   DT C   5      29.093 -16.773 -11.100  1.00 45.60           C  
ANISOU 3172  C4   DT C   5     3463   7377   6486   -176   -777  -1561       C  
ATOM   3173  O4   DT C   5      29.686 -15.867 -11.678  1.00 54.35           O  
ANISOU 3173  O4   DT C   5     5757   7930   6963  -1119    110  -1605       O  
ATOM   3174  C5   DT C   5      29.707 -18.002 -10.647  1.00 42.28           C  
ANISOU 3174  C5   DT C   5     2907   7367   5792   -287   -698  -1549       C  
ATOM   3175  C7   DT C   5      31.167 -18.214 -10.882  1.00 42.86           C  
ANISOU 3175  C7   DT C   5     2756   8072   5455   -114   -920  -1796       C  
ATOM   3176  C6   DT C   5      28.933 -18.901 -10.024  1.00 39.89           C  
ANISOU 3176  C6   DT C   5     2674   6992   5490   -361   -920  -1776       C  
ATOM   3177  P    DC C   6      23.779 -23.142  -8.734  1.00 34.41           P  
ANISOU 3177  P    DC C   6     2271   5431   5369    663   -679   -977       P  
ATOM   3178  OP1  DC C   6      22.479 -22.681  -8.211  1.00 31.44           O  
ANISOU 3178  OP1  DC C   6     2268   4696   4979    443   -646   -871       O  
ATOM   3179  OP2  DC C   6      24.428 -24.324  -8.124  1.00 32.59           O  
ANISOU 3179  OP2  DC C   6     1888   5151   5341    654   -657  -1015       O  
ATOM   3180  O5'  DC C   6      23.741 -23.401 -10.302  1.00 33.72           O  
ANISOU 3180  O5'  DC C   6     2125   5296   5389    297   -426  -1058       O  
ATOM   3181  C5'  DC C   6      22.603 -23.114 -11.115  1.00 33.62           C  
ANISOU 3181  C5'  DC C   6     2382   5055   5336    400   -471   -853       C  
ATOM   3182  C4'  DC C   6      22.896 -23.543 -12.534  1.00 36.90           C  
ANISOU 3182  C4'  DC C   6     2884   5774   5359     24   -412  -1069       C  
ATOM   3183  O4'  DC C   6      23.883 -22.664 -13.112  1.00 39.52           O  
ANISOU 3183  O4'  DC C   6     2742   6417   5857     49   -385   -921       O  
ATOM   3184  C3'  DC C   6      23.490 -24.939 -12.659  1.00 39.60           C  
ANISOU 3184  C3'  DC C   6     2880   6214   5950    382   -212  -1056       C  
ATOM   3185  O3'  DC C   6      22.408 -25.850 -12.818  1.00 41.49           O  
ANISOU 3185  O3'  DC C   6     3511   6342   5911    136   -333  -1137       O  
ATOM   3186  C2'  DC C   6      24.304 -24.854 -13.938  1.00 44.36           C  
ANISOU 3186  C2'  DC C   6     3607   6959   6287   -264     34   -991       C  
ATOM   3187  C1'  DC C   6      24.734 -23.386 -13.993  1.00 41.20           C  
ANISOU 3187  C1'  DC C   6     2931   6857   5866   -158   -227  -1226       C  
ATOM   3188  N1   DC C   6      26.117 -23.114 -13.582  1.00 42.69           N  
ANISOU 3188  N1   DC C   6     2838   7472   5910     71   -230  -1524       N  
ATOM   3189  C2   DC C   6      26.732 -21.939 -14.034  1.00 48.96           C  
ANISOU 3189  C2   DC C   6     3944   8044   6613   -464   -145  -1229       C  
ATOM   3190  O2   DC C   6      26.108 -21.192 -14.803  1.00 51.37           O  
ANISOU 3190  O2   DC C   6     4827   8168   6521   -467   -218  -1008       O  
ATOM   3191  N3   DC C   6      27.992 -21.658 -13.632  1.00 48.64           N  
ANISOU 3191  N3   DC C   6     3817   8139   6523   -321     -5  -1275       N  
ATOM   3192  C4   DC C   6      28.626 -22.485 -12.797  1.00 49.87           C  
ANISOU 3192  C4   DC C   6     3598   8327   7023    172   -142  -1524       C  
ATOM   3193  N4   DC C   6      29.864 -22.163 -12.423  1.00 49.44           N  
ANISOU 3193  N4   DC C   6     3553   8822   6406   -150     24  -1404       N  
ATOM   3194  C5   DC C   6      28.015 -23.675 -12.303  1.00 46.75           C  
ANISOU 3194  C5   DC C   6     3353   8087   6323    421    -80  -1758       C  
ATOM   3195  C6   DC C   6      26.768 -23.943 -12.710  1.00 44.50           C  
ANISOU 3195  C6   DC C   6     3248   7309   6348    608     64  -1613       C  
ATOM   3196  P    DA C   7      22.538 -27.356 -12.330  1.00 42.44           P  
ANISOU 3196  P    DA C   7     3766   6282   6076    340     -7  -1164       P  
ATOM   3197  OP1  DA C   7      21.152 -27.913 -12.283  1.00 38.93           O  
ANISOU 3197  OP1  DA C   7     3493   5778   5520    852     61  -1448       O  
ATOM   3198  OP2  DA C   7      23.421 -27.409 -11.156  1.00 42.76           O  
ANISOU 3198  OP2  DA C   7     3393   6441   6411    864   -225   -829       O  
ATOM   3199  O5'  DA C   7      23.350 -28.042 -13.511  1.00 44.61           O  
ANISOU 3199  O5'  DA C   7     3895   6331   6723    487    193  -1263       O  
ATOM   3200  C5'  DA C   7      22.682 -28.325 -14.746  1.00 46.20           C  
ANISOU 3200  C5'  DA C   7     4750   6347   6456    843     95  -1270       C  
ATOM   3201  C4'  DA C   7      23.640 -28.973 -15.714  1.00 45.67           C  
ANISOU 3201  C4'  DA C   7     4040   7031   6280    493    264   -929       C  
ATOM   3202  O4'  DA C   7      24.516 -27.959 -16.244  1.00 46.77           O  
ANISOU 3202  O4'  DA C   7     4635   6936   6196    154    314  -1270       O  
ATOM   3203  C3'  DA C   7      24.546 -30.051 -15.111  1.00 42.81           C  
ANISOU 3203  C3'  DA C   7     3560   6734   5970    601    524  -1246       C  
ATOM   3204  O3'  DA C   7      24.623 -31.157 -16.010  1.00 45.96           O  
ANISOU 3204  O3'  DA C   7     4282   6931   6246    239    -12  -1455       O  
ATOM   3205  C2'  DA C   7      25.905 -29.378 -15.031  1.00 46.83           C  
ANISOU 3205  C2'  DA C   7     4031   6995   6765    138    141  -1521       C  
ATOM   3206  C1'  DA C   7      25.845 -28.434 -16.215  1.00 50.27           C  
ANISOU 3206  C1'  DA C   7     4418   8116   6563    172    -41  -1297       C  
ATOM   3207  N9   DA C   7      26.725 -27.275 -16.127  1.00 54.15           N  
ANISOU 3207  N9   DA C   7     4728   8656   7188   -108    670  -1952       N  
ATOM   3208  C8   DA C   7      27.557 -26.916 -15.094  1.00 52.59           C  
ANISOU 3208  C8   DA C   7     3994   9109   6877    334    911  -2087       C  
ATOM   3209  N7   DA C   7      28.223 -25.809 -15.313  1.00 61.22           N  
ANISOU 3209  N7   DA C   7     5857   9262   8142   -239    521  -1826       N  
ATOM   3210  C5   DA C   7      27.811 -25.417 -16.580  1.00 63.05           C  
ANISOU 3210  C5   DA C   7     5927   9629   8398   -346    247  -1784       C  
ATOM   3211  C6   DA C   7      28.157 -24.320 -17.392  1.00 62.93           C  
ANISOU 3211  C6   DA C   7     5843   9826   8241   -685    -54  -1670       C  
ATOM   3212  N6   DA C   7      29.031 -23.378 -17.029  1.00 65.10           N  
ANISOU 3212  N6   DA C   7     4238  10629   9866  -1163    430  -1359       N  
ATOM   3213  N1   DA C   7      27.561 -24.218 -18.600  1.00 59.32           N  
ANISOU 3213  N1   DA C   7     5378   9242   7917   -604    302  -1825       N  
ATOM   3214  C2   DA C   7      26.681 -25.163 -18.962  1.00 63.48           C  
ANISOU 3214  C2   DA C   7     5622   9774   8723  -1144    282  -1495       C  
ATOM   3215  N3   DA C   7      26.276 -26.240 -18.289  1.00 60.66           N  
ANISOU 3215  N3   DA C   7     5224   9505   8316    -27    256  -1356       N  
ATOM   3216  C4   DA C   7      26.884 -26.308 -17.090  1.00 59.59           C  
ANISOU 3216  C4   DA C   7     5340   9273   8030     29    420  -1381       C  
ATOM   3217  P    DA C   8      24.447 -32.653 -15.469  1.00 47.96           P  
ANISOU 3217  P    DA C   8     4825   6687   6710   1421    212  -1323       P  
ATOM   3218  OP1  DA C   8      25.307 -32.823 -14.275  1.00 45.15           O  
ANISOU 3218  OP1  DA C   8     4261   6376   6517    500    180  -1261       O  
ATOM   3219  OP2  DA C   8      24.575 -33.559 -16.635  1.00 45.59           O  
ANISOU 3219  OP2  DA C   8     4393   6502   6425    673    -28  -1183       O  
ATOM   3220  O5'  DA C   8      22.960 -32.675 -14.897  1.00 47.55           O  
ANISOU 3220  O5'  DA C   8     5006   6386   6671    679    194   -706       O  
ATOM   3221  C5'  DA C   8      21.828 -32.814 -15.764  1.00 42.40           C  
ANISOU 3221  C5'  DA C   8     4221   5584   6302    692    534   -756       C  
ATOM   3222  C4'  DA C   8      20.578 -32.390 -15.032  1.00 38.72           C  
ANISOU 3222  C4'  DA C   8     3987   5293   5431    582    133   -706       C  
ATOM   3223  O4'  DA C   8      20.634 -30.971 -14.783  1.00 38.89           O  
ANISOU 3223  O4'  DA C   8     3958   5345   5473    515      4   -626       O  
ATOM   3224  C3'  DA C   8      19.290 -32.605 -15.817  1.00 42.12           C  
ANISOU 3224  C3'  DA C   8     4273   5442   6287    486   -210   -703       C  
ATOM   3225  O3'  DA C   8      18.792 -33.901 -15.525  1.00 43.17           O  
ANISOU 3225  O3'  DA C   8     4788   5331   6282    732      1   -358       O  
ATOM   3226  C2'  DA C   8      18.375 -31.521 -15.272  1.00 39.19           C  
ANISOU 3226  C2'  DA C   8     4081   5230   5577    266     -6   -386       C  
ATOM   3227  C1'  DA C   8      19.343 -30.393 -14.929  1.00 38.20           C  
ANISOU 3227  C1'  DA C   8     3890   5200   5422    336    -34   -517       C  
ATOM   3228  N9   DA C   8      19.426 -29.318 -15.923  1.00 38.29           N  
ANISOU 3228  N9   DA C   8     3885   5197   5466     28   -419   -516       N  
ATOM   3229  C8   DA C   8      19.273 -27.981 -15.654  1.00 38.24           C  
ANISOU 3229  C8   DA C   8     4134   5212   5184   -100   -156   -536       C  
ATOM   3230  N7   DA C   8      19.360 -27.214 -16.712  1.00 35.61           N  
ANISOU 3230  N7   DA C   8     3492   4775   5262   -350   -428   -577       N  
ATOM   3231  C5   DA C   8      19.579 -28.104 -17.753  1.00 36.23           C  
ANISOU 3231  C5   DA C   8     3538   4894   5333   -485   -119   -548       C  
ATOM   3232  C6   DA C   8      19.753 -27.917 -19.138  1.00 38.39           C  
ANISOU 3232  C6   DA C   8     4065   5152   5366   -638    289   -574       C  
ATOM   3233  N6   DA C   8      19.743 -26.718 -19.729  1.00 37.62           N  
ANISOU 3233  N6   DA C   8     3878   5039   5374   -170    453   -673       N  
ATOM   3234  N1   DA C   8      19.946 -29.015 -19.902  1.00 39.11           N  
ANISOU 3234  N1   DA C   8     4472   5082   5307   -904    -52   -571       N  
ATOM   3235  C2   DA C   8      19.969 -30.215 -19.305  1.00 39.23           C  
ANISOU 3235  C2   DA C   8     4193   5147   5563   -573    511   -458       C  
ATOM   3236  N3   DA C   8      19.825 -30.517 -18.014  1.00 37.75           N  
ANISOU 3236  N3   DA C   8     3750   5137   5457    129    211   -511       N  
ATOM   3237  C4   DA C   8      19.627 -29.405 -17.283  1.00 36.31           C  
ANISOU 3237  C4   DA C   8     3628   4724   5443   -720   -304   -609       C  
ATOM   3238  P    DT C   9      17.918 -34.690 -16.600  1.00 45.22           P  
ANISOU 3238  P    DT C   9     5281   5255   6646    452   -145   -481       P  
ATOM   3239  OP1  DT C   9      18.829 -35.368 -17.546  1.00 47.22           O  
ANISOU 3239  OP1  DT C   9     5679   5225   7038    379   -111   -882       O  
ATOM   3240  OP2  DT C   9      16.893 -33.765 -17.138  1.00 47.59           O  
ANISOU 3240  OP2  DT C   9     5107   5984   6989    228    -68    172       O  
ATOM   3241  O5'  DT C   9      17.201 -35.774 -15.696  1.00 51.34           O  
ANISOU 3241  O5'  DT C   9     6088   6007   7410    -69   -269    122       O  
ATOM   3242  C5'  DT C   9      16.421 -35.380 -14.552  1.00 55.12           C  
ANISOU 3242  C5'  DT C   9     6609   6585   7746    777   -386   -300       C  
ATOM   3243  C4'  DT C   9      15.350 -36.417 -14.302  1.00 58.04           C  
ANISOU 3243  C4'  DT C   9     7022   6996   8034    690   -451    269       C  
ATOM   3244  O4'  DT C   9      14.217 -36.142 -15.161  1.00 50.59           O  
ANISOU 3244  O4'  DT C   9     6073   5276   7872    616    -27    587       O  
ATOM   3245  C3'  DT C   9      15.776 -37.860 -14.598  1.00 64.89           C  
ANISOU 3245  C3'  DT C   9     8106   7137   9413   1458   -575    497       C  
ATOM   3246  O3'  DT C   9      15.361 -38.747 -13.551  1.00 71.18           O  
ANISOU 3246  O3'  DT C   9     7563   8956  10527    -34   2098    -57       O  
ATOM   3247  C2'  DT C   9      15.128 -38.166 -15.941  1.00 62.04           C  
ANISOU 3247  C2'  DT C   9     7715   6443   9414   1080   -163    174       C  
ATOM   3248  C1'  DT C   9      13.882 -37.293 -15.923  1.00 53.73           C  
ANISOU 3248  C1'  DT C   9     7116   5269   8027    432   -390    582       C  
ATOM   3249  N1   DT C   9      13.372 -36.841 -17.247  1.00 55.00           N  
ANISOU 3249  N1   DT C   9     7518   5268   8109    360   -256    735       N  
ATOM   3250  C2   DT C   9      12.605 -37.712 -17.994  1.00 60.90           C  
ANISOU 3250  C2   DT C   9     7835   6323   8981   -158   -601    568       C  
ATOM   3251  O2   DT C   9      12.348 -38.850 -17.638  1.00 68.10           O  
ANISOU 3251  O2   DT C   9     9180   6539  10154   -760   -223    757       O  
ATOM   3252  N3   DT C   9      12.152 -37.197 -19.186  1.00 61.16           N  
ANISOU 3252  N3   DT C   9     8333   5812   9089   -540   -923    489       N  
ATOM   3253  C4   DT C   9      12.378 -35.929 -19.692  1.00 60.88           C  
ANISOU 3253  C4   DT C   9     8584   6143   8403   -862   -917    598       C  
ATOM   3254  O4   DT C   9      11.903 -35.605 -20.779  1.00 59.55           O  
ANISOU 3254  O4   DT C   9     8439   5533   8655   -666   -716   1382       O  
ATOM   3255  C5   DT C   9      13.184 -35.067 -18.853  1.00 52.69           C  
ANISOU 3255  C5   DT C   9     7376   4966   7676   -538   -200    848       C  
ATOM   3256  C7   DT C   9      13.481 -33.674 -19.312  1.00 45.81           C  
ANISOU 3256  C7   DT C   9     6323   4732   6351     27     28    683       C  
ATOM   3257  C6   DT C   9      13.633 -35.559 -17.690  1.00 49.66           C  
ANISOU 3257  C6   DT C   9     5999   5132   7737    454   -253    501       C  
TER    3258       DT C   9                                                      
HETATM 3259 ZN    ZN A 401      13.960  -6.299  13.786  1.00 40.39          ZN  
ANISOU 3259 ZN    ZN A 401     4886   4968   5491    -84    -45    221      ZN  
HETATM 3260 AS   CAC A 402      16.097  -8.984  12.618  0.80110.02          AS  
ANISOU 3260 AS   CAC A 402    13418  14220  14163   1669  -1158    140      AS  
HETATM 3261  O1  CAC A 402      15.068  -7.591  12.445  0.80 47.81           O  
ANISOU 3261  O1  CAC A 402     5223   8051   4893  -3352    727  -1279       O  
HETATM 3262  O2  CAC A 402      17.573  -8.519  13.413  0.80 63.22           O  
ANISOU 3262  O2  CAC A 402    10584   6266   7167   3986   1675   -587       O  
HETATM 3263  C1  CAC A 402      16.511  -9.715  10.845  0.80 68.02           C  
ANISOU 3263  C1  CAC A 402     5933   8610  11299   -488  -3872   1549       C  
HETATM 3264  C2  CAC A 402      15.177 -10.346  13.689  0.80 79.34           C  
ANISOU 3264  C2  CAC A 402    10120  11891   8134   2708   -294  -2373       C  
HETATM 3265 ZN    ZN B 401      13.836 -37.528 -26.813  1.00 50.81          ZN  
ANISOU 3265 ZN    ZN B 401     6951   6161   6193    218   -158   -307      ZN  
HETATM 3266 AS   CAC B 402      13.321 -35.060 -24.739  0.80 55.21          AS  
ANISOU 3266 AS   CAC B 402     7407   6237   7331    138    352    -70      AS  
HETATM 3267  O1  CAC B 402      14.008 -35.413 -26.296  0.80 53.95           O  
ANISOU 3267  O1  CAC B 402     7910   5852   6733    308    -95   -410       O  
HETATM 3268  O2  CAC B 402      11.637 -35.503 -24.752  0.80 48.76           O  
ANISOU 3268  O2  CAC B 402     6933   5403   6188    397   -999   -927       O  
HETATM 3269  C1  CAC B 402      14.231 -36.008 -23.289  0.80 48.85           C  
ANISOU 3269  C1  CAC B 402     7265   5199   6094    -64   -809  -1727       C  
HETATM 3270  C2  CAC B 402      13.418 -33.127 -24.448  0.80 43.67           C  
ANISOU 3270  C2  CAC B 402     6618   5775   4198   -128   -443    304       C  
HETATM 3271  O   HOH A 501      27.530 -15.102  14.874  1.00 41.57           O  
ANISOU 3271  O   HOH A 501     5258   5237   5299    363   -253    375       O  
HETATM 3272  O   HOH A 502      37.633  -6.648  12.403  1.00 46.45           O  
ANISOU 3272  O   HOH A 502     4614   5237   7798    -79   -679   -899       O  
HETATM 3273  O   HOH A 503      28.670  12.861   7.495  1.00 40.75           O  
ANISOU 3273  O   HOH A 503     4497   5389   5596   -372    197   -505       O  
HETATM 3274  O   HOH A 504      22.187 -24.316  -1.798  1.00 46.60           O  
ANISOU 3274  O   HOH A 504     5251   5402   7053   -716    456    270       O  
HETATM 3275  O   HOH A 505      11.532 -10.065   6.351  1.00 35.46           O  
ANISOU 3275  O   HOH A 505     3455   5004   5014    552    216   -395       O  
HETATM 3276  O   HOH A 506      20.782  -9.094  -6.738  1.00 53.22           O  
ANISOU 3276  O   HOH A 506     6379   7141   6701   -464    620   -468       O  
HETATM 3277  O   HOH A 507      26.187 -14.188  16.922  1.00 50.80           O  
ANISOU 3277  O   HOH A 507     6058   6674   6567    -51     88    294       O  
HETATM 3278  O   HOH A 508      36.133 -14.530  14.814  1.00 51.08           O  
ANISOU 3278  O   HOH A 508     7575   7087   4744  -1445  -1094   1293       O  
HETATM 3279  O   HOH A 509      15.164 -13.345 -10.801  1.00 45.88           O  
ANISOU 3279  O   HOH A 509     6130   5844   5457    738  -1408    215       O  
HETATM 3280  O   HOH A 510      17.742  -6.949   8.018  1.00 38.43           O  
ANISOU 3280  O   HOH A 510     4492   4755   5354   -118    618   -510       O  
HETATM 3281  O   HOH A 511      29.630  15.570   5.821  1.00 54.35           O  
ANISOU 3281  O   HOH A 511     5971   7639   7039   1352    838    395       O  
HETATM 3282  O   HOH A 512      30.697 -25.018  -4.124  1.00 51.39           O  
ANISOU 3282  O   HOH A 512     5241   6027   8258    522     89   -716       O  
HETATM 3283  O   HOH A 513      15.122   8.999   2.596  1.00 34.77           O  
ANISOU 3283  O   HOH A 513     4150   4147   4914    565   -616    295       O  
HETATM 3284  O   HOH A 514      31.636 -21.439   0.271  1.00 40.15           O  
ANISOU 3284  O   HOH A 514     3324   5921   6007   1104    -17    103       O  
HETATM 3285  O   HOH A 515      22.406 -15.095   9.799  1.00 27.28           O  
ANISOU 3285  O   HOH A 515     2721   3271   4369   -276   -124    -47       O  
HETATM 3286  O   HOH A 516      36.524  -8.251  17.451  1.00 51.42           O  
ANISOU 3286  O   HOH A 516     6099   6096   7341    366  -1897   -203       O  
HETATM 3287  O   HOH A 517      15.241 -21.755  -8.162  1.00 49.02           O  
ANISOU 3287  O   HOH A 517     4658   7086   6881   -694  -1445  -1007       O  
HETATM 3288  O   HOH A 518      23.658 -24.381   0.655  1.00 51.10           O  
ANISOU 3288  O   HOH A 518     6730   5553   7133   -445    553   -826       O  
HETATM 3289  O   HOH A 519      21.809   3.277  -1.746  1.00 41.65           O  
ANISOU 3289  O   HOH A 519     5624   5005   5193    566    -27    160       O  
HETATM 3290  O   HOH A 520      21.144  -1.952  -6.808  1.00 65.21           O  
ANISOU 3290  O   HOH A 520     7809   8339   8627    779     96   -854       O  
HETATM 3291  O   HOH A 521      22.877  -8.334  -7.594  1.00 55.22           O  
ANISOU 3291  O   HOH A 521     6680   7314   6983    768  -1617   -407       O  
HETATM 3292  O   HOH A 522      14.208   6.893   0.865  1.00 39.79           O  
ANISOU 3292  O   HOH A 522     4701   5130   5284    725   -373    270       O  
HETATM 3293  O   HOH A 523      33.673  -7.793  -6.317  1.00 49.78           O  
ANISOU 3293  O   HOH A 523     5698   6214   6998  -1595    462   1168       O  
HETATM 3294  O   HOH A 524      14.527 -26.028   7.315  1.00 51.35           O  
ANISOU 3294  O   HOH A 524     6343   6692   6475  -1146    121    838       O  
HETATM 3295  O   HOH A 525      32.142  13.913   1.555  1.00 48.76           O  
ANISOU 3295  O   HOH A 525     5731   6279   6514  -1826   1051   -254       O  
HETATM 3296  O   HOH A 526      27.304  -5.685  -4.365  1.00 47.20           O  
ANISOU 3296  O   HOH A 526     6518   6122   5292   -772    120    394       O  
HETATM 3297  O   HOH A 527      27.081 -20.760   2.410  1.00 40.50           O  
ANISOU 3297  O   HOH A 527     4188   5865   5335    298     62   -517       O  
HETATM 3298  O   HOH A 528      31.002  -8.079  -6.890  1.00 40.19           O  
ANISOU 3298  O   HOH A 528     5102   5442   4726  -1043    132   -185       O  
HETATM 3299  O   HOH A 529      30.864 -22.395   7.689  1.00 35.22           O  
ANISOU 3299  O   HOH A 529     4156   4056   5169    813    395   -216       O  
HETATM 3300  O   HOH A 530      13.399 -15.574 -10.235  1.00 41.47           O  
ANISOU 3300  O   HOH A 530     4416   5858   5482    385   -515   -492       O  
HETATM 3301  O   HOH A 531       2.013 -10.816  -5.912  1.00 55.59           O  
ANISOU 3301  O   HOH A 531     6322   7319   7481    499  -1546    333       O  
HETATM 3302  O   HOH A 532      34.307 -20.811   4.765  1.00 39.10           O  
ANISOU 3302  O   HOH A 532     3617   5574   5664   1521   -496   -180       O  
HETATM 3303  O   HOH A 533       7.462 -13.159  -8.749  1.00 47.74           O  
ANISOU 3303  O   HOH A 533     5327   6585   6226    848   -625    743       O  
HETATM 3304  O   HOH A 534      36.859   7.656   2.656  1.00 50.35           O  
ANISOU 3304  O   HOH A 534     5773   5706   7650   -372    536    -70       O  
HETATM 3305  O   HOH A 535      13.081   5.638  12.952  1.00 48.04           O  
ANISOU 3305  O   HOH A 535     6289   5394   6569   -854    591   -414       O  
HETATM 3306  O   HOH A 536      18.228 -12.482  13.999  1.00 56.37           O  
ANISOU 3306  O   HOH A 536     6882   7284   7248   -344    -61    -55       O  
HETATM 3307  O   HOH A 537      14.371  -6.373  -6.037  1.00 48.45           O  
ANISOU 3307  O   HOH A 537     5823   6941   5643    300   -699    266       O  
HETATM 3308  O   HOH A 538      19.716 -23.834  16.336  1.00 49.64           O  
ANISOU 3308  O   HOH A 538     6225   5177   7458   -838    129    563       O  
HETATM 3309  O   HOH A 539       7.044  -1.337  -3.538  1.00 61.74           O  
ANISOU 3309  O   HOH A 539     7095   8266   8097   1592  -1239    600       O  
HETATM 3310  O   HOH A 540      19.329 -25.075  -3.488  1.00 49.57           O  
ANISOU 3310  O   HOH A 540     6083   5819   6932  -1100    -17   -352       O  
HETATM 3311  O   HOH A 541      14.449 -17.037   3.011  1.00 33.45           O  
ANISOU 3311  O   HOH A 541     3575   4017   5116   -146   -134   -270       O  
HETATM 3312  O   HOH A 542      34.324 -18.344   0.016  1.00 36.50           O  
ANISOU 3312  O   HOH A 542     3985   4927   4957    -69   -213    -41       O  
HETATM 3313  O   HOH A 543      22.309  -5.338  -8.232  1.00 50.37           O  
ANISOU 3313  O   HOH A 543     7389   5810   5938    454   -636   -219       O  
HETATM 3314  O   HOH A 544      45.106 -17.639   2.756  1.00 61.09           O  
ANISOU 3314  O   HOH A 544     5945   8701   8566    231  -2377    525       O  
HETATM 3315  O   HOH A 545      40.802 -15.651   8.405  1.00 42.49           O  
ANISOU 3315  O   HOH A 545     3800   6551   5793    695   -441    -90       O  
HETATM 3316  O   HOH A 546      16.339  -9.025  -6.107  1.00 34.16           O  
ANISOU 3316  O   HOH A 546     4214   4306   4458    373   -739     12       O  
HETATM 3317  O   HOH A 547      23.938 -15.371  -8.533  1.00 44.89           O  
ANISOU 3317  O   HOH A 547     5900   6241   4912     59  -1045   -462       O  
HETATM 3318  O   HOH A 548      17.222   3.115  -2.809  1.00 59.64           O  
ANISOU 3318  O   HOH A 548     8099   7543   7018    361  -1086  -1506       O  
HETATM 3319  O   HOH A 549      36.888 -13.374  -4.681  1.00 50.78           O  
ANISOU 3319  O   HOH A 549     5496   6697   7099   1394    714   1666       O  
HETATM 3320  O   HOH A 550      20.452 -15.023  -1.930  1.00 30.04           O  
ANISOU 3320  O   HOH A 550     2902   3910   4599     71   -304   -244       O  
HETATM 3321  O   HOH A 551      30.697  -6.160  14.257  1.00 39.77           O  
ANISOU 3321  O   HOH A 551     4875   4914   5321    278    361    359       O  
HETATM 3322  O   HOH A 552      26.799   2.451  -0.652  1.00 41.27           O  
ANISOU 3322  O   HOH A 552     5385   5254   5039   -199    942    435       O  
HETATM 3323  O   HOH A 553      16.193   4.985   0.205  1.00 42.82           O  
ANISOU 3323  O   HOH A 553     4904   5662   5700    883   -312     14       O  
HETATM 3324  O   HOH A 554       7.269  -6.529  -7.678  1.00 52.87           O  
ANISOU 3324  O   HOH A 554     7300   6370   6418    492   -513    -98       O  
HETATM 3325  O   HOH A 555      28.434 -26.333  -2.089  1.00 46.45           O  
ANISOU 3325  O   HOH A 555     6082   5064   6502    937  -1367     51       O  
HETATM 3326  O   HOH A 556      31.350 -12.435  13.675  1.00 46.61           O  
ANISOU 3326  O   HOH A 556     5511   6215   5981    477   -717   1099       O  
HETATM 3327  O   HOH A 557       3.887  -5.268   9.660  1.00 58.99           O  
ANISOU 3327  O   HOH A 557     6725   6916   8773   1299   -123    437       O  
HETATM 3328  O   HOH A 558      26.087 -17.837 -13.510  1.00 61.54           O  
ANISOU 3328  O   HOH A 558     7137   8298   7945   -258   -414  -1284       O  
HETATM 3329  O   HOH A 559      41.379 -20.403  -3.070  1.00 65.32           O  
ANISOU 3329  O   HOH A 559     7245   7091  10483   1272   -823    443       O  
HETATM 3330  O   HOH A 560      18.375  14.706   7.577  1.00 51.48           O  
ANISOU 3330  O   HOH A 560     6662   6338   6560   -580   -491  -1413       O  
HETATM 3331  O   HOH A 561      31.708 -18.800   1.290  1.00 33.80           O  
ANISOU 3331  O   HOH A 561     3157   4649   5034    117     -1    442       O  
HETATM 3332  O   HOH A 562      25.501 -26.047  -1.038  1.00 51.99           O  
ANISOU 3332  O   HOH A 562     5703   6804   7246   -747   -447     61       O  
HETATM 3333  O   HOH A 563       9.261  -7.154   7.733  1.00 41.90           O  
ANISOU 3333  O   HOH A 563     4569   5377   5971    169    -66   -349       O  
HETATM 3334  O   HOH A 564      24.827   1.120  17.665  1.00 42.76           O  
ANISOU 3334  O   HOH A 564     5611   5137   5495   -817  -1063   -445       O  
HETATM 3335  O   HOH A 565      15.420  -4.194  18.399  1.00 49.46           O  
ANISOU 3335  O   HOH A 565     5844   6075   6872   1185    215      6       O  
HETATM 3336  O   HOH A 566      17.716   2.951  16.453  1.00 52.62           O  
ANISOU 3336  O   HOH A 566     6022   6833   7134    520    385    541       O  
HETATM 3337  O   HOH A 567       5.053 -19.273  10.450  1.00 36.21           O  
ANISOU 3337  O   HOH A 567     2665   5422   5671   -647   -157   -563       O  
HETATM 3338  O   HOH A 568      19.300 -26.015   7.324  1.00 51.60           O  
ANISOU 3338  O   HOH A 568     6205   6873   6528    -31   -778    210       O  
HETATM 3339  O   HOH A 569      24.759 -25.226   6.298  1.00 62.16           O  
ANISOU 3339  O   HOH A 569     6526   7277   9814   1126    760   -287       O  
HETATM 3340  O   HOH A 570       1.739 -17.197   2.769  1.00 60.14           O  
ANISOU 3340  O   HOH A 570     5274   8808   8768    378  -1531   -602       O  
HETATM 3341  O   HOH A 571      35.445  -5.520  -3.692  1.00 48.72           O  
ANISOU 3341  O   HOH A 571     5913   6532   6065  -1136    402    451       O  
HETATM 3342  O   HOH A 572      47.968 -15.956   7.095  1.00 53.93           O  
ANISOU 3342  O   HOH A 572     4935   8398   7158    975    931   -272       O  
HETATM 3343  O   HOH A 573      23.060  16.330  12.084  1.00 47.74           O  
ANISOU 3343  O   HOH A 573     5593   5425   7122     -8    115   -894       O  
HETATM 3344  O   HOH A 574       5.943 -15.215  -9.329  1.00 58.45           O  
ANISOU 3344  O   HOH A 574     6659   8332   7215   -200    663    -10       O  
HETATM 3345  O   HOH A 575      27.234  -4.957  16.264  1.00 42.78           O  
ANISOU 3345  O   HOH A 575     5258   5884   5111   -291   -613   -122       O  
HETATM 3346  O   HOH A 576      11.762 -12.748  -9.807  1.00 50.43           O  
ANISOU 3346  O   HOH A 576     4807   7353   7000    873   -634   -670       O  
HETATM 3347  O   HOH A 577      33.259 -14.325  12.875  1.00 30.94           O  
ANISOU 3347  O   HOH A 577     3451   4428   3876   -349   -293    515       O  
HETATM 3348  O   HOH A 578      42.442 -11.540   5.901  1.00 43.68           O  
ANISOU 3348  O   HOH A 578     4947   5466   6183  -1056     24   -673       O  
HETATM 3349  O   HOH A 579      25.477 -11.829  -9.605  1.00 40.68           O  
ANISOU 3349  O   HOH A 579     5036   5125   5294   -128   -567   -189       O  
HETATM 3350  O   HOH A 580      18.333  -8.217  -7.587  1.00 55.43           O  
ANISOU 3350  O   HOH A 580     6791   6948   7320    826   -216   -713       O  
HETATM 3351  O   HOH A 581      26.452 -22.989   5.309  1.00 41.09           O  
ANISOU 3351  O   HOH A 581     4154   5501   5955    170   -707    407       O  
HETATM 3352  O   HOH A 582      21.445  17.624   5.364  1.00 72.11           O  
ANISOU 3352  O   HOH A 582    10670   5992  10737   1285   -291    116       O  
HETATM 3353  O   HOH A 583      16.189 -24.628   2.798  1.00 50.55           O  
ANISOU 3353  O   HOH A 583     4927   6144   8132   -727     66    342       O  
HETATM 3354  O   HOH A 584      14.289  10.658   0.291  1.00 51.62           O  
ANISOU 3354  O   HOH A 584     7078   6119   6415    544  -1578     30       O  
HETATM 3355  O   HOH A 585      17.208  15.894  13.568  1.00 53.88           O  
ANISOU 3355  O   HOH A 585     6735   6535   7200   1246    -79    574       O  
HETATM 3356  O   HOH A 586      -2.392  -8.770  10.925  1.00 73.16           O  
ANISOU 3356  O   HOH A 586    10409   8286   9100    143    830    267       O  
HETATM 3357  O   HOH A 587       1.534 -17.790   7.260  1.00 46.62           O  
ANISOU 3357  O   HOH A 587     3187   6931   7595   -903    941    217       O  
HETATM 3358  O   HOH A 588      27.753 -23.192   1.980  1.00 52.05           O  
ANISOU 3358  O   HOH A 588     7307   6162   6308  -1861    302    538       O  
HETATM 3359  O   HOH A 589      18.573  -8.099  19.632  1.00 55.28           O  
ANISOU 3359  O   HOH A 589     7165   6523   7315    583   -348      7       O  
HETATM 3360  O   HOH A 590       7.400   6.005   7.611  1.00 67.01           O  
ANISOU 3360  O   HOH A 590     8454   8222   8784    749  -1078    569       O  
HETATM 3361  O   HOH A 591      35.766 -20.203   1.222  1.00 48.34           O  
ANISOU 3361  O   HOH A 591     5384   6594   6388    827    349   -413       O  
HETATM 3362  O   HOH A 592      28.495 -23.452   7.047  1.00 36.10           O  
ANISOU 3362  O   HOH A 592     3982   4525   5207    392   -274   -319       O  
HETATM 3363  O   HOH A 593      18.654  11.322  14.199  1.00 58.56           O  
ANISOU 3363  O   HOH A 593     6380   7606   8263    724  -1608   1915       O  
HETATM 3364  O   HOH A 594      21.467  16.945  10.184  1.00 57.83           O  
ANISOU 3364  O   HOH A 594     8866   6586   6519    284  -1596   -436       O  
HETATM 3365  O   HOH A 595      13.090  -4.016  16.429  1.00 66.51           O  
ANISOU 3365  O   HOH A 595     7591   8441   9237   2648   -742   -142       O  
HETATM 3366  O   HOH A 596      29.338  -5.655  -6.269  1.00 50.93           O  
ANISOU 3366  O   HOH A 596     6332   6665   6355     10  -1281   -367       O  
HETATM 3367  O   HOH A 597      14.260   8.278  -1.567  1.00 60.44           O  
ANISOU 3367  O   HOH A 597     7274   8092   7598   -174    -92    542       O  
HETATM 3368  O   HOH A 598      43.065 -19.455  -5.544  1.00 46.70           O  
ANISOU 3368  O   HOH A 598     5243   5327   7170    535   -639   -364       O  
HETATM 3369  O   HOH A 599      23.397 -10.387  -9.335  1.00 55.78           O  
ANISOU 3369  O   HOH A 599     7227   7621   6343   1774   -958     57       O  
HETATM 3370  O   HOH A 600      38.569 -20.479   7.438  1.00 37.97           O  
ANISOU 3370  O   HOH A 600     3764   5760   4899   1008   -517    -70       O  
HETATM 3371  O   HOH A 601      40.629 -18.659   7.737  1.00 47.32           O  
ANISOU 3371  O   HOH A 601     5290   7188   5502   1038   1007    814       O  
HETATM 3372  O   HOH A 602      30.378 -23.470   1.278  1.00 52.10           O  
ANISOU 3372  O   HOH A 602     7303   7336   5154    440   -586    896       O  
HETATM 3373  O   HOH A 603      34.759  -3.722  -5.822  1.00 59.49           O  
ANISOU 3373  O   HOH A 603     7756   7840   7006   -566   1614    340       O  
HETATM 3374  O   HOH A 604      27.680 -25.677   8.752  1.00 56.29           O  
ANISOU 3374  O   HOH A 604     7335   5562   8489  -1106   -674   -526       O  
HETATM 3375  O   HOH B 501      -4.643 -37.118 -49.014  1.00 63.62           O  
ANISOU 3375  O   HOH B 501     9197   7769   7205  -1350  -1178   -505       O  
HETATM 3376  O   HOH B 502       8.912 -31.501 -10.705  1.00 42.31           O  
ANISOU 3376  O   HOH B 502     4773   4966   6334   -482    621    942       O  
HETATM 3377  O   HOH B 503      18.503 -30.242 -27.426  1.00 42.36           O  
ANISOU 3377  O   HOH B 503     5340   5432   5322    151    554   -170       O  
HETATM 3378  O   HOH B 504      -6.948 -31.533 -32.929  1.00 55.83           O  
ANISOU 3378  O   HOH B 504     7501   7785   5926  -1111  -1295   -371       O  
HETATM 3379  O   HOH B 505       3.913 -16.012 -15.320  1.00 48.88           O  
ANISOU 3379  O   HOH B 505     5813   6410   6348   -421   -142    552       O  
HETATM 3380  O   HOH B 506      12.234  -8.901 -17.029  1.00 54.95           O  
ANISOU 3380  O   HOH B 506     6368   8450   6059    425    265    690       O  
HETATM 3381  O   HOH B 507       0.848 -19.382 -13.444  1.00 39.69           O  
ANISOU 3381  O   HOH B 507     4361   5607   5110    118    -14    215       O  
HETATM 3382  O   HOH B 508      -7.434 -26.886 -15.145  1.00 41.24           O  
ANISOU 3382  O   HOH B 508     4649   5529   5490    351   -443    249       O  
HETATM 3383  O   HOH B 509      -2.350 -13.244 -15.168  1.00 57.23           O  
ANISOU 3383  O   HOH B 509     7230   7101   7414    -55  -1538    333       O  
HETATM 3384  O   HOH B 510     -10.679 -37.994 -49.280  1.00 48.98           O  
ANISOU 3384  O   HOH B 510     6679   5275   6655   -246   -942    435       O  
HETATM 3385  O   HOH B 511       3.098 -18.513 -31.439  1.00 49.70           O  
ANISOU 3385  O   HOH B 511     6759   6134   5990    217  -1422   -205       O  
HETATM 3386  O   HOH B 512      11.395 -31.214 -27.722  1.00 47.92           O  
ANISOU 3386  O   HOH B 512     6458   6025   5721   -128    175   -772       O  
HETATM 3387  O   HOH B 513      20.689 -36.967 -33.343  1.00 57.39           O  
ANISOU 3387  O   HOH B 513     8224   6883   6700    846    532   -683       O  
HETATM 3388  O   HOH B 514       9.047 -38.021 -18.295  1.00 55.82           O  
ANISOU 3388  O   HOH B 514     6736   4598   9875    411    -64    -50       O  
HETATM 3389  O   HOH B 515      18.487 -23.817 -21.720  1.00 40.69           O  
ANISOU 3389  O   HOH B 515     5354   4819   5287     60    112   -118       O  
HETATM 3390  O   HOH B 516      20.929 -27.462  -6.976  1.00 43.61           O  
ANISOU 3390  O   HOH B 516     5258   5658   5651    777    149   -256       O  
HETATM 3391  O   HOH B 517      12.607 -18.761 -24.277  1.00 31.47           O  
ANISOU 3391  O   HOH B 517     4131   3623   4203   -623    238   -128       O  
HETATM 3392  O   HOH B 518      -4.376 -32.086 -52.128  1.00 68.00           O  
ANISOU 3392  O   HOH B 518     8437   7274  10124  -1234   -175   -260       O  
HETATM 3393  O   HOH B 519      -5.177 -35.691 -42.635  1.00 48.00           O  
ANISOU 3393  O   HOH B 519     5712   6023   6500   -445   -840   -721       O  
HETATM 3394  O   HOH B 520       0.838 -14.257 -28.953  1.00 37.31           O  
ANISOU 3394  O   HOH B 520     4136   4657   5380   -144    -80    894       O  
HETATM 3395  O   HOH B 521       8.497 -31.154 -15.262  1.00 37.45           O  
ANISOU 3395  O   HOH B 521     5369   4344   4514    179   -228    -27       O  
HETATM 3396  O   HOH B 522       1.166 -41.317 -29.449  1.00 51.93           O  
ANISOU 3396  O   HOH B 522     7541   5398   6791   -272   -403    -26       O  
HETATM 3397  O   HOH B 523       5.877 -25.156 -39.995  1.00 43.89           O  
ANISOU 3397  O   HOH B 523     6549   4864   5263   -605     -8   -380       O  
HETATM 3398  O   HOH B 524      14.998 -18.189 -32.165  1.00 42.13           O  
ANISOU 3398  O   HOH B 524     6574   4800   4633   -228    755   -471       O  
HETATM 3399  O   HOH B 525      11.668 -22.039 -11.388  1.00 49.65           O  
ANISOU 3399  O   HOH B 525     5710   6530   6623  -1361    159   -880       O  
HETATM 3400  O   HOH B 526       0.844 -21.997 -33.936  1.00 52.69           O  
ANISOU 3400  O   HOH B 526     7806   5949   6264   -928   -889      9       O  
HETATM 3401  O   HOH B 527       9.701 -32.528 -44.783  1.00 47.93           O  
ANISOU 3401  O   HOH B 527     6592   5138   6481   -499  -1164   -766       O  
HETATM 3402  O   HOH B 528      12.380 -26.765  -9.126  1.00 46.67           O  
ANISOU 3402  O   HOH B 528     5174   6988   5570     24   -265    825       O  
HETATM 3403  O   HOH B 529       4.049 -22.524 -11.404  1.00 36.83           O  
ANISOU 3403  O   HOH B 529     4420   4830   4743   -114    479     44       O  
HETATM 3404  O   HOH B 530      10.108 -28.898 -41.968  1.00 45.16           O  
ANISOU 3404  O   HOH B 530     5252   5554   6352  -1284    319  -1005       O  
HETATM 3405  O   HOH B 531       5.266 -17.377 -33.574  1.00 49.79           O  
ANISOU 3405  O   HOH B 531     5574   7097   6244    425   -265   -423       O  
HETATM 3406  O   HOH B 532       8.149 -15.935 -32.376  1.00 41.53           O  
ANISOU 3406  O   HOH B 532     5009   5153   5616   -483    731      6       O  
HETATM 3407  O   HOH B 533      10.878 -16.434 -31.293  1.00 39.25           O  
ANISOU 3407  O   HOH B 533     5361   4880   4669   -450    587    415       O  
HETATM 3408  O   HOH B 534      -7.387 -27.521 -47.750  1.00 65.33           O  
ANISOU 3408  O   HOH B 534     8570   7154   9099    962  -4084    250       O  
HETATM 3409  O   HOH B 535       0.619 -16.101 -17.254  1.00 38.85           O  
ANISOU 3409  O   HOH B 535     4731   4765   5265   -374    607    122       O  
HETATM 3410  O   HOH B 536      19.376 -33.165 -29.952  1.00 48.92           O  
ANISOU 3410  O   HOH B 536     6958   5340   6289    666   -136  -1204       O  
HETATM 3411  O   HOH B 537      -3.127 -13.394 -22.671  1.00 53.83           O  
ANISOU 3411  O   HOH B 537     6609   6746   7096    533   -278    527       O  
HETATM 3412  O   HOH B 538       9.487 -29.201 -18.855  1.00 35.61           O  
ANISOU 3412  O   HOH B 538     5123   3512   4894   -693   -221    352       O  
HETATM 3413  O   HOH B 539      -7.794 -29.692 -45.589  1.00 53.68           O  
ANISOU 3413  O   HOH B 539     6114   7019   7261    171  -1296   -661       O  
HETATM 3414  O   HOH B 540       9.697 -19.353 -37.814  1.00 58.40           O  
ANISOU 3414  O   HOH B 540     8771   6423   6994   -334     92   -837       O  
HETATM 3415  O   HOH B 541      -7.498 -22.707 -14.420  1.00 42.00           O  
ANISOU 3415  O   HOH B 541     4389   5536   6032    205   -163     76       O  
HETATM 3416  O   HOH B 542       2.957 -17.893 -16.979  1.00 45.39           O  
ANISOU 3416  O   HOH B 542     5094   6090   6060  -1223   -291    587       O  
HETATM 3417  O   HOH B 543      15.261 -24.421  -8.288  1.00 51.42           O  
ANISOU 3417  O   HOH B 543     5198   7774   6564   -755   -574   -469       O  
HETATM 3418  O   HOH B 544      -7.088 -24.521 -28.027  1.00 55.70           O  
ANISOU 3418  O   HOH B 544     6393   7410   7359   -896   -577    227       O  
HETATM 3419  O   HOH B 545      10.491 -12.218 -26.298  1.00 40.68           O  
ANISOU 3419  O   HOH B 545     5485   4410   5560  -1052    993   -338       O  
HETATM 3420  O   HOH B 546       3.938 -19.599 -34.578  1.00 54.80           O  
ANISOU 3420  O   HOH B 546     6672   7212   6936  -1390   -869   -608       O  
HETATM 3421  O   HOH B 547      17.304 -41.674 -33.510  1.00 55.42           O  
ANISOU 3421  O   HOH B 547     8353   6796   5908    964    -41   -830       O  
HETATM 3422  O   HOH B 548      -6.996 -29.188 -13.001  1.00 33.71           O  
ANISOU 3422  O   HOH B 548     4262   4326   4217    187     59    273       O  
HETATM 3423  O   HOH B 549      17.305  -8.817 -10.137  1.00 58.03           O  
ANISOU 3423  O   HOH B 549     7919   6831   7296   -365   -605    202       O  
HETATM 3424  O   HOH B 550       0.807 -24.902 -37.625  1.00 46.93           O  
ANISOU 3424  O   HOH B 550     6686   4799   6345   -478   -691    827       O  
HETATM 3425  O   HOH B 551       8.719 -13.333 -12.568  1.00 47.48           O  
ANISOU 3425  O   HOH B 551     6577   6496   4966   -807    -69  -1042       O  
HETATM 3426  O   HOH B 552      15.054 -29.827 -14.661  1.00 32.49           O  
ANISOU 3426  O   HOH B 552     3918   4072   4353    218    540     33       O  
HETATM 3427  O   HOH B 553       7.858 -19.174 -15.499  1.00 41.24           O  
ANISOU 3427  O   HOH B 553     4004   4879   6786    594    511    724       O  
HETATM 3428  O   HOH B 554      -5.978 -14.945 -21.722  1.00 57.49           O  
ANISOU 3428  O   HOH B 554     6813   6549   8482  -1548  -1765    126       O  
HETATM 3429  O   HOH B 555      -9.812 -21.728 -19.030  1.00 43.74           O  
ANISOU 3429  O   HOH B 555     4303   6333   5980    731   -974    172       O  
HETATM 3430  O   HOH B 556       8.885  -9.947 -18.815  1.00 49.70           O  
ANISOU 3430  O   HOH B 556     6604   5794   6485   -990    389   -476       O  
HETATM 3431  O   HOH B 557      13.587 -20.545 -12.861  1.00 42.70           O  
ANISOU 3431  O   HOH B 557     5087   5442   5695    684    489    668       O  
HETATM 3432  O   HOH B 558      12.791 -16.692 -14.614  1.00 40.41           O  
ANISOU 3432  O   HOH B 558     4663   4910   5780   -643      2   -895       O  
HETATM 3433  O   HOH B 559       7.946 -12.279 -29.082  1.00 39.68           O  
ANISOU 3433  O   HOH B 559     4436   5012   5628   -398    265    418       O  
HETATM 3434  O   HOH B 560      -5.342 -18.503 -14.612  1.00 47.79           O  
ANISOU 3434  O   HOH B 560     5134   6496   6527   -194    146    433       O  
HETATM 3435  O   HOH B 561      20.247 -35.880 -45.722  1.00 74.54           O  
ANISOU 3435  O   HOH B 561    10800   9492   8028  -2965   1476  -1648       O  
HETATM 3436  O   HOH B 562      14.858 -24.261 -11.181  1.00 35.17           O  
ANISOU 3436  O   HOH B 562     4053   4746   4562   -896    345   -314       O  
HETATM 3437  O   HOH B 563      26.091 -32.832 -19.094  1.00 49.39           O  
ANISOU 3437  O   HOH B 563     6253   5867   6644    555    282  -2170       O  
HETATM 3438  O   HOH B 564      -1.383 -29.425 -16.080  1.00 39.00           O  
ANISOU 3438  O   HOH B 564     4280   4954   5583   -612    570   -328       O  
HETATM 3439  O   HOH B 565      15.931 -21.906 -12.521  1.00 40.29           O  
ANISOU 3439  O   HOH B 565     4667   5269   5373     85   -924   -840       O  
HETATM 3440  O   HOH B 566      -7.107 -34.193 -32.178  1.00 62.63           O  
ANISOU 3440  O   HOH B 566     7894   8173   7727  -1137  -1151    170       O  
HETATM 3441  O   HOH B 567      10.958  -9.682 -20.347  1.00 43.89           O  
ANISOU 3441  O   HOH B 567     6199   4863   5615   -666     24   -140       O  
HETATM 3442  O   HOH B 568      13.724  -9.529 -19.764  1.00 38.18           O  
ANISOU 3442  O   HOH B 568     4978   4296   5231   -558   -251   -510       O  
HETATM 3443  O   HOH B 569      -6.995 -18.070 -28.560  1.00 64.02           O  
ANISOU 3443  O   HOH B 569     5876   9487   8961   -340   -425    210       O  
HETATM 3444  O   HOH B 570      11.672 -42.237 -26.710  1.00 55.29           O  
ANISOU 3444  O   HOH B 570     9009   4725   7271   -336   -242  -1221       O  
HETATM 3445  O   HOH B 571       0.785 -37.293 -24.038  1.00 46.00           O  
ANISOU 3445  O   HOH B 571     5729   5405   6342   -961   -311    882       O  
HETATM 3446  O   HOH B 572       5.205 -43.982 -29.127  1.00 56.31           O  
ANISOU 3446  O   HOH B 572     9246   4943   7206   -636     -7      5       O  
HETATM 3447  O   HOH B 573      17.225 -31.263 -11.898  1.00 42.97           O  
ANISOU 3447  O   HOH B 573     6738   4594   4992    181    244   -120       O  
HETATM 3448  O   HOH B 574       8.137 -33.325 -13.423  1.00 45.52           O  
ANISOU 3448  O   HOH B 574     5230   5652   6414     40   1407     71       O  
HETATM 3449  O   HOH B 575       1.348 -16.499 -32.258  1.00 52.22           O  
ANISOU 3449  O   HOH B 575     7111   6098   6630  -1139   -472    699       O  
HETATM 3450  O   HOH B 576       8.753 -21.101 -12.717  1.00 43.37           O  
ANISOU 3450  O   HOH B 576     5087   5596   5796   -567   -246    241       O  
HETATM 3451  O   HOH B 577      12.776 -32.905  -8.357  1.00 53.33           O  
ANISOU 3451  O   HOH B 577     6927   7885   5447     50    821    647       O  
HETATM 3452  O   HOH B 578      13.468 -41.184 -28.515  1.00 54.37           O  
ANISOU 3452  O   HOH B 578     7331   6001   7325    384  -1003    241       O  
HETATM 3453  O   HOH B 579       5.666 -12.448 -12.819  1.00 53.14           O  
ANISOU 3453  O   HOH B 579     6332   7703   6153  -1002   -439   -181       O  
HETATM 3454  O   HOH B 580       6.799 -22.156 -11.152  1.00 36.24           O  
ANISOU 3454  O   HOH B 580     4274   4507   4986   -332   -378   -246       O  
HETATM 3455  O   HOH B 581      12.690 -17.932 -12.058  1.00 51.78           O  
ANISOU 3455  O   HOH B 581     5436   6712   7524   -592   -893    187       O  
HETATM 3456  O   HOH B 582       1.187 -16.358 -13.933  1.00 54.35           O  
ANISOU 3456  O   HOH B 582     6852   6297   7499   -601   1385    625       O  
HETATM 3457  O   HOH B 583      -1.046 -15.469 -14.763  1.00 51.25           O  
ANISOU 3457  O   HOH B 583     8086   5696   5691   -535   -180    232       O  
HETATM 3458  O   HOH B 584      10.921 -13.438 -30.339  1.00 61.05           O  
ANISOU 3458  O   HOH B 584     7937   6569   8689   -980   -481    981       O  
HETATM 3459  O   HOH B 585      -6.583 -20.518 -12.763  1.00 51.81           O  
ANISOU 3459  O   HOH B 585     5930   6372   7383   2289    204    997       O  
HETATM 3460  O   HOH B 586      -3.470 -20.466 -11.207  1.00 47.04           O  
ANISOU 3460  O   HOH B 586     6670   4488   6715   -625    958    205       O  
HETATM 3461  O   HOH B 587      -1.533 -18.687 -12.308  1.00 46.18           O  
ANISOU 3461  O   HOH B 587     5263   5969   6313   -630    330    764       O  
HETATM 3462  O   HOH B 588      -3.276 -17.064 -13.659  1.00 41.67           O  
ANISOU 3462  O   HOH B 588     4994   5120   5717    151    414   -508       O  
HETATM 3463  O   HOH C 101      30.472 -25.499 -14.290  1.00 64.53           O  
ANISOU 3463  O   HOH C 101     7935   8452   8130   2875    952  -2875       O  
HETATM 3464  O   HOH C 102      20.107 -30.085 -11.436  1.00 49.20           O  
ANISOU 3464  O   HOH C 102     5976   6890   5827    356   -360   -246       O  
HETATM 3465  O   HOH C 103      26.638 -25.894  -9.105  1.00 43.40           O  
ANISOU 3465  O   HOH C 103     4575   5715   6199    608  -1062    -15       O  
HETATM 3466  O   HOH C 104      30.854 -25.935 -11.500  1.00 55.07           O  
ANISOU 3466  O   HOH C 104     5326   7389   8209   2723  -1095   -981       O  
HETATM 3467  O   HOH C 105      23.343 -26.714  -8.531  1.00 34.93           O  
ANISOU 3467  O   HOH C 105     4029   4776   4466   -306    -47   -218       O  
HETATM 3468  O   HOH C 106      26.034 -26.996 -11.582  1.00 51.17           O  
ANISOU 3468  O   HOH C 106     6028   6941   6471    648     64   -579       O  
HETATM 3469  O   HOH C 107      24.367 -29.921 -10.709  1.00 50.52           O  
ANISOU 3469  O   HOH C 107     5840   6622   6732    779    561  -1010       O  
HETATM 3470  O   HOH C 108      45.336 -23.524 -15.473  1.00 64.27           O  
ANISOU 3470  O   HOH C 108     7954   6443  10023    536    251   1230       O  
HETATM 3471  O   HOH C 109      15.063 -31.762 -16.555  1.00 43.49           O  
ANISOU 3471  O   HOH C 109     4684   6213   5624      2   -223   -914       O  
HETATM 3472  O   HOH C 110      26.211 -14.495 -11.676  1.00 60.77           O  
ANISOU 3472  O   HOH C 110     8408   8330   6348    505  -1417    575       O  
HETATM 3473  O   HOH C 111      48.307 -26.066 -10.565  1.00 34.91           O  
ANISOU 3473  O   HOH C 111     4330   4169   4763    452     25     23       O  
HETATM 3474  O   HOH C 112      41.910 -20.365 -13.571  1.00 65.35           O  
ANISOU 3474  O   HOH C 112    10392   9291   5145    501   -589    739       O  
HETATM 3475  O   HOH C 113      40.925 -20.968  -6.165  1.00 47.13           O  
ANISOU 3475  O   HOH C 113     4719   6071   7113    782    108   -120       O  
HETATM 3476  O   HOH C 114      38.995 -19.823  -7.483  1.00 60.90           O  
ANISOU 3476  O   HOH C 114     6164   8473   8499   -625  -1600  -1489       O  
HETATM 3477  O   HOH C 115      26.999 -19.286 -16.710  1.00 54.32           O  
ANISOU 3477  O   HOH C 115     6123   7375   7140  -2402    567    -96       O  
HETATM 3478  O   HOH C 116      46.919 -23.297 -13.079  1.00 41.85           O  
ANISOU 3478  O   HOH C 116     5136   4821   5943   -299    943    654       O  
HETATM 3479  O   HOH C 117      22.457 -31.876 -12.006  1.00 55.73           O  
ANISOU 3479  O   HOH C 117     7249   6935   6991   -349    646   -547       O  
HETATM 3480  O   HOH C 118      35.542 -26.581  -0.748  1.00 51.26           O  
ANISOU 3480  O   HOH C 118     3151   8727   7596    -76   -539  -1039       O  
HETATM 3481  O   HOH C 119      30.577 -25.320  -0.707  1.00 56.63           O  
ANISOU 3481  O   HOH C 119     6098   8223   7196    118  -1039     87       O  
CONECT   45   48                                                                
CONECT   48   45   49                                                           
CONECT   49   48   50   52                                                      
CONECT   50   49   51   56                                                      
CONECT   51   50                                                                
CONECT   52   49   53                                                           
CONECT   53   52   54                                                           
CONECT   54   53   55                                                           
CONECT   55   54                                                                
CONECT   56   50                                                                
CONECT  277  282                                                                
CONECT  282  277  283                                                           
CONECT  283  282  284  286                                                      
CONECT  284  283  285  290                                                      
CONECT  285  284                                                                
CONECT  286  283  287                                                           
CONECT  287  286  288                                                           
CONECT  288  287  289                                                           
CONECT  289  288                                                                
CONECT  290  284                                                                
CONECT  474 3259                                                                
CONECT  739 3259                                                                
CONECT  761 3259                                                                
CONECT 1136 1142                                                                
CONECT 1142 1136 1143                                                           
CONECT 1143 1142 1144 1146                                                      
CONECT 1144 1143 1145 1150                                                      
CONECT 1145 1144                                                                
CONECT 1146 1143 1147                                                           
CONECT 1147 1146 1148                                                           
CONECT 1148 1147 1149                                                           
CONECT 1149 1148                                                                
CONECT 1150 1144                                                                
CONECT 1570 1573                                                                
CONECT 1573 1570 1574                                                           
CONECT 1574 1573 1575 1577                                                      
CONECT 1575 1574 1576 1581                                                      
CONECT 1576 1575                                                                
CONECT 1577 1574 1578                                                           
CONECT 1578 1577 1579                                                           
CONECT 1579 1578 1580                                                           
CONECT 1580 1579                                                                
CONECT 1581 1575                                                                
CONECT 1802 1807                                                                
CONECT 1807 1802 1808                                                           
CONECT 1808 1807 1809 1811                                                      
CONECT 1809 1808 1810 1815                                                      
CONECT 1810 1809                                                                
CONECT 1811 1808 1812                                                           
CONECT 1812 1811 1813                                                           
CONECT 1813 1812 1814                                                           
CONECT 1814 1813                                                                
CONECT 1815 1809                                                                
CONECT 2020 2061                                                                
CONECT 2027 3265                                                                
CONECT 2061 2020                                                                
CONECT 2292 3265                                                                
CONECT 2314 3265                                                                
CONECT 2689 2695                                                                
CONECT 2695 2689 2696                                                           
CONECT 2696 2695 2697 2699                                                      
CONECT 2697 2696 2698 2703                                                      
CONECT 2698 2697                                                                
CONECT 2699 2696 2700                                                           
CONECT 2700 2699 2701                                                           
CONECT 2701 2700 2702                                                           
CONECT 2702 2701                                                                
CONECT 2703 2697                                                                
CONECT 3259  474  739  761 3261                                                 
CONECT 3260 3261 3262 3263 3264                                                 
CONECT 3261 3259 3260                                                           
CONECT 3262 3260                                                                
CONECT 3263 3260                                                                
CONECT 3264 3260                                                                
CONECT 3265 2027 2292 2314 3267                                                 
CONECT 3266 3267 3268 3269 3270                                                 
CONECT 3267 3265 3266                                                           
CONECT 3268 3266                                                                
CONECT 3269 3266                                                                
CONECT 3270 3266                                                                
MASTER      376    0   10   12   12    0    7    6 3478    3   80   35          
END

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Related entries of code: 5zvb

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
5w2m	RCSB PDB PDBbind	184aa, >5W2M_1\|Chains... at 90%
5zva	RCSB PDB PDBbind	209aa, >5ZVA_1\|Chains... *
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
1si2	RCSB PDB PDBbind	9-mer
1si3	RCSB PDB PDBbind	9-mer
3gib	RCSB PDB PDBbind	9-mer
3h15	RCSB PDB PDBbind	9-mer
3k5q	RCSB PDB PDBbind	9-mer
3k5y	RCSB PDB PDBbind	9-mer
3k5z	RCSB PDB PDBbind	9-mer
3k61	RCSB PDB PDBbind	9-mer
3k62	RCSB PDB PDBbind	9-mer
3k64	RCSB PDB PDBbind	9-mer
5yki	RCSB PDB PDBbind	9-mer

Entry Information

PDB ID	5zvb
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	APOBEC3F Chimeric Catalytic Domain (A3Fc-D2)
Ligand Name	9-mer
EC.Number	E.C.3.5.4.38
Resolution	2(Å)
Affinity (Kd/Ki/IC50)	Kd=40.38uM
Release Year	2018
Protein/NA Sequence	Check fasta file
Primary Reference	(2018) Chin.J.Chem. Vol. 36: pp. 1241-1248

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): Q9HC16
Entrez Gene ID	NCBI Entrez Gene ID: 60489
ASD	Information of known allosteric effects of PDB entries

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