HEADER    STRUCTURAL PROTEIN                      02-JUL-21   7F8Y              
TITLE     CRYSTAL STRUCTURE OF THE CHOLECYSTOKININ RECEPTOR CCKAR IN COMPLEX    
TITLE    2 WITH DEVAZEPIDE                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FUSION PROTEIN OF CHOLECYSTOKININ RECEPTOR TYPE A AND      
COMPND   3 ENDOLYSIN;                                                           
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: CCK-A RECEPTOR,CCK-AR,CHOLECYSTOKININ-1 RECEPTOR,CCK1-R,    
COMPND   6 LYSIS PROTEIN,LYSOZYME,MURAMIDASE;                                   
COMPND   7 EC: 3.2.1.17;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;          
SOURCE   3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4;                            
SOURCE   4 ORGANISM_TAXID: 9606, 10665;                                         
SOURCE   5 GENE: CCKAR, CCKRA;                                                  
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    G PROTEIN-COULPED RECEPTOR, CHOLECYSTOKININ RECEPTOR CCKAR,           
KEYWDS   2 DEVAZEPIDE, STRUCTURAL PROTEIN                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.ZHANG,C.HE,M.WANG,Q.ZHOU,D.YANG,Y.ZHU,B.WU,Q.ZHAO                   
REVDAT   2   16-FEB-22 7F8Y    1       JRNL                                     
REVDAT   1   13-OCT-21 7F8Y    0                                                
JRNL        AUTH   X.ZHANG,C.HE,M.WANG,Q.ZHOU,D.YANG,Y.ZHU,W.FENG,H.ZHANG,      
JRNL        AUTH 2 A.DAI,X.CHU,J.WANG,Z.YANG,Y.JIANG,U.SENSFUSS,Q.TAN,S.HAN,    
JRNL        AUTH 3 S.REEDTZ-RUNGE,H.E.XU,S.ZHAO,M.W.WANG,B.WU,Q.ZHAO            
JRNL        TITL   STRUCTURES OF THE HUMAN CHOLECYSTOKININ RECEPTORS BOUND TO   
JRNL        TITL 2 AGONISTS AND ANTAGONISTS.                                    
JRNL        REF    NAT.CHEM.BIOL.                V.  17  1230 2021              
JRNL        REFN                   ESSN 1552-4469                               
JRNL        PMID   34556863                                                     
JRNL        DOI    10.1038/S41589-021-00866-8                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.19.2_4158                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.77                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 39065                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3524                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.7700 -  7.2800    0.90     1442   134  0.1630 0.2055        
REMARK   3     2  7.2700 -  5.7900    0.92     1454   148  0.2078 0.2269        
REMARK   3     3  5.7900 -  5.0600    0.87     1371   143  0.2106 0.2555        
REMARK   3     4  5.0600 -  4.6000    0.90     1426   147  0.1809 0.2594        
REMARK   3     5  4.6000 -  4.2700    0.91     1442   144  0.1759 0.2355        
REMARK   3     6  4.2700 -  4.0200    0.90     1425   153  0.1970 0.2300        
REMARK   3     7  4.0200 -  3.8200    0.90     1434   143  0.1918 0.2945        
REMARK   3     8  3.8200 -  3.6500    0.87     1354   134  0.2078 0.2594        
REMARK   3     9  3.6500 -  3.5100    0.89     1439   147  0.2194 0.3039        
REMARK   3    10  3.5100 -  3.3900    0.91     1443   128  0.2399 0.2952        
REMARK   3    11  3.3900 -  3.2900    0.91     1435   150  0.2293 0.2778        
REMARK   3    12  3.2900 -  3.1900    0.91     1466   148  0.2279 0.2888        
REMARK   3    13  3.1900 -  3.1100    0.90     1442   140  0.2473 0.3131        
REMARK   3    14  3.1100 -  3.0300    0.91     1420   141  0.2617 0.2840        
REMARK   3    15  3.0300 -  2.9600    0.92     1471   147  0.2707 0.3611        
REMARK   3    16  2.9600 -  2.9000    0.92     1444   137  0.2805 0.3277        
REMARK   3    17  2.9000 -  2.8400    0.88     1436   134  0.2882 0.3243        
REMARK   3    18  2.8400 -  2.7900    0.89     1427   132  0.3011 0.3576        
REMARK   3    19  2.7900 -  2.7400    0.89     1378   138  0.2983 0.3348        
REMARK   3    20  2.7400 -  2.6900    0.90     1463   147  0.3060 0.3374        
REMARK   3    21  2.6900 -  2.6500    0.87     1381   135  0.3304 0.3473        
REMARK   3    22  2.6500 -  2.6100    0.89     1394   128  0.3177 0.4274        
REMARK   3    23  2.6100 -  2.5700    0.88     1409   146  0.3411 0.3855        
REMARK   3    24  2.5700 -  2.5300    0.87     1398   145  0.3621 0.3595        
REMARK   3    25  2.5300 -  2.5000    0.87     1347   135  0.3923 0.4002        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.463            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.539           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 68.07                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 80.06                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           3576                                  
REMARK   3   ANGLE     :  1.103           4857                                  
REMARK   3   CHIRALITY :  0.055            571                                  
REMARK   3   PLANARITY :  0.006            593                                  
REMARK   3   DIHEDRAL  : 16.292           1283                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   8.9282  17.7892  24.3409              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5165 T22:   0.4774                                     
REMARK   3      T33:   0.5152 T12:   0.0671                                     
REMARK   3      T13:  -0.0143 T23:   0.0147                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2152 L22:  -0.0921                                     
REMARK   3      L33:   0.9114 L12:   0.2287                                     
REMARK   3      L13:  -0.2586 L23:  -0.0103                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0871 S12:   0.0381 S13:   0.0458                       
REMARK   3      S21:   0.0234 S22:  -0.0280 S23:   0.0188                       
REMARK   3      S31:   0.0139 S32:  -0.0078 S33:   0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7F8Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-JUL-21.                  
REMARK 100 THE DEPOSITION ID IS D_1300022826.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUN-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JAN 26, 2018           
REMARK 200  DATA SCALING SOFTWARE          : XSCALE VERSION JAN 26, 2018        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39065                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 1.19.2                                         
REMARK 200 STARTING MODEL: 5ZBQ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.5, 25% (V/V) PEG400    
REMARK 280  AND 350 MM AMMONIUM ACETATE, LIPIDIC CUBIC PHASE, TEMPERATURE       
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       36.21000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ASP A    -8                                                      
REMARK 465     TYR A    -7                                                      
REMARK 465     LYS A    -6                                                      
REMARK 465     ASP A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     ASN A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     ASN A    13                                                      
REMARK 465     ILE A    14                                                      
REMARK 465     THR A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     PRO A    17                                                      
REMARK 465     CYS A    18                                                      
REMARK 465     GLU A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     LEU A    22                                                      
REMARK 465     GLU A    23                                                      
REMARK 465     ASN A    24                                                      
REMARK 465     GLU A    25                                                      
REMARK 465     THR A    26                                                      
REMARK 465     LEU A    27                                                      
REMARK 465     PHE A    28                                                      
REMARK 465     CYS A    29                                                      
REMARK 465     LEU A    30                                                      
REMARK 465     ASP A    31                                                      
REMARK 465     GLN A    32                                                      
REMARK 465     PRO A    33                                                      
REMARK 465     ARG A    34                                                      
REMARK 465     PRO A    35                                                      
REMARK 465     SER A    36                                                      
REMARK 465     ARG A   376                                                      
REMARK 465     PHE A   377                                                      
REMARK 465     ARG A   378                                                      
REMARK 465     LEU A   379                                                      
REMARK 465     GLY A   380                                                      
REMARK 465     PHE A   381                                                      
REMARK 465     MET A   382                                                      
REMARK 465     ALA A   383                                                      
REMARK 465     THR A   384                                                      
REMARK 465     PHE A   385                                                      
REMARK 465     PRO A   386                                                      
REMARK 465     CYS A   387                                                      
REMARK 465     CYS A   388                                                      
REMARK 465     PRO A   389                                                      
REMARK 465     ASN A   390                                                      
REMARK 465     PRO A   391                                                      
REMARK 465     GLY A   392                                                      
REMARK 465     PRO A   393                                                      
REMARK 465     PRO A   394                                                      
REMARK 465     GLY A   395                                                      
REMARK 465     ALA A   396                                                      
REMARK 465     ARG A   397                                                      
REMARK 465     GLY A   398                                                      
REMARK 465     GLU A   399                                                      
REMARK 465     VAL A   400                                                      
REMARK 465     GLY A   401                                                      
REMARK 465     GLU A   402                                                      
REMARK 465     GLU A   403                                                      
REMARK 465     GLU A   404                                                      
REMARK 465     GLU A   405                                                      
REMARK 465     GLY A   406                                                      
REMARK 465     GLU A   407                                                      
REMARK 465     PHE A   408                                                      
REMARK 465     LEU A   409                                                      
REMARK 465     GLU A   410                                                      
REMARK 465     VAL A   411                                                      
REMARK 465     LEU A   412                                                      
REMARK 465     PHE A   413                                                      
REMARK 465     GLN A   414                                                      
REMARK 465     GLY A   415                                                      
REMARK 465     PRO A   416                                                      
REMARK 465     HIS A   417                                                      
REMARK 465     HIS A   418                                                      
REMARK 465     HIS A   419                                                      
REMARK 465     HIS A   420                                                      
REMARK 465     HIS A   421                                                      
REMARK 465     HIS A   422                                                      
REMARK 465     HIS A   423                                                      
REMARK 465     HIS A   424                                                      
REMARK 465     HIS A   425                                                      
REMARK 465     HIS A   426                                                      
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     GLU A  38    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  70    CG   CD   CE   NZ                                   
REMARK 470     LEU A 147    CG   CD1  CD2                                       
REMARK 470     ARG A 150    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 153    CG   CD   OE1  NE2                                  
REMARK 470     ILE A1289    CG1  CG2  CD1                                       
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    ARG A  73       76.58    -67.31                                   
REMARK 500    CYS A  94      -41.87   -137.95                                   
REMARK 500    PHE A  97       20.67    -72.22                                   
REMARK 500    SER A 149       60.31   -114.57                                   
REMARK 500    ASN A 188      -71.69    -48.84                                   
REMARK 500    ASN A 189       47.96    -89.36                                   
REMARK 500    ASN A 202     -159.89   -155.49                                   
REMARK 500    PHE A 218      -66.37   -136.70                                   
REMARK 500    ILE A1268       74.48   -101.37                                   
REMARK 500    ASN A1292       92.44    -66.04                                   
REMARK 500    PHE A1353       55.54    -90.54                                   
REMARK 500    ASP A 339       68.11   -157.76                                   
REMARK 500    ASN A 374       53.14    -93.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7F8Y A   37   240  UNP    P32238   CCKAR_HUMAN     37    240             
DBREF  7F8Y A 1241  1400  UNP    P00720   ENLYS_BPT4       2    161             
DBREF  7F8Y A  302   406  UNP    P32238   CCKAR_HUMAN    302    406             
SEQADV 7F8Y ASP A   -8  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y TYR A   -7  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y LYS A   -6  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y ASP A   -5  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y ASP A   -4  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y ASP A   -3  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y ASP A   -2  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y GLY A   -1  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y ALA A    0  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y PRO A    1  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y ASP A    2  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y VAL A    3  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y VAL A    4  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y ASP A    5  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y SER A    6  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y LEU A    7  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y LEU A    8  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y VAL A    9  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y ASN A   10  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y GLY A   11  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y SER A   12  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y ASN A   13  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y ILE A   14  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y THR A   15  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y PRO A   16  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y PRO A   17  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y CYS A   18  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y GLU A   19  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y LEU A   20  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y GLY A   21  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y LEU A   22  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y GLU A   23  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y ASN A   24  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y GLU A   25  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y THR A   26  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y LEU A   27  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y PHE A   28  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y CYS A   29  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y LEU A   30  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y ASP A   31  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y GLN A   32  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y PRO A   33  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y ARG A   34  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y PRO A   35  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y SER A   36  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y ASN A   87  UNP  P32238    ASP    87 ENGINEERED MUTATION            
SEQADV 7F8Y TRP A  130  UNP  P32238    PHE   130 ENGINEERED MUTATION            
SEQADV 7F8Y GLY A 1251  UNP  P00720    ARG    12 ENGINEERED MUTATION            
SEQADV 7F8Y THR A 1293  UNP  P00720    CYS    54 ENGINEERED MUTATION            
SEQADV 7F8Y ALA A 1336  UNP  P00720    CYS    97 ENGINEERED MUTATION            
SEQADV 7F8Y ARG A 1376  UNP  P00720    ILE   137 ENGINEERED MUTATION            
SEQADV 7F8Y GLU A  407  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y PHE A  408  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y LEU A  409  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y GLU A  410  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y VAL A  411  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y LEU A  412  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y PHE A  413  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y GLN A  414  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y GLY A  415  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y PRO A  416  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y HIS A  417  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y HIS A  418  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y HIS A  419  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y HIS A  420  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y HIS A  421  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y HIS A  422  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y HIS A  423  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y HIS A  424  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y HIS A  425  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8Y HIS A  426  UNP  P32238              EXPRESSION TAG                 
SEQRES   1 A  534  ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO ASP VAL VAL          
SEQRES   2 A  534  ASP SER LEU LEU VAL ASN GLY SER ASN ILE THR PRO PRO          
SEQRES   3 A  534  CYS GLU LEU GLY LEU GLU ASN GLU THR LEU PHE CYS LEU          
SEQRES   4 A  534  ASP GLN PRO ARG PRO SER LYS GLU TRP GLN PRO ALA VAL          
SEQRES   5 A  534  GLN ILE LEU LEU TYR SER LEU ILE PHE LEU LEU SER VAL          
SEQRES   6 A  534  LEU GLY ASN THR LEU VAL ILE THR VAL LEU ILE ARG ASN          
SEQRES   7 A  534  LYS ARG MET ARG THR VAL THR ASN ILE PHE LEU LEU SER          
SEQRES   8 A  534  LEU ALA VAL SER ASN LEU MET LEU CYS LEU PHE CYS MET          
SEQRES   9 A  534  PRO PHE ASN LEU ILE PRO ASN LEU LEU LYS ASP PHE ILE          
SEQRES  10 A  534  PHE GLY SER ALA VAL CYS LYS THR THR THR TYR PHE MET          
SEQRES  11 A  534  GLY THR SER VAL SER VAL SER THR TRP ASN LEU VAL ALA          
SEQRES  12 A  534  ILE SER LEU GLU ARG TYR GLY ALA ILE CYS LYS PRO LEU          
SEQRES  13 A  534  GLN SER ARG VAL TRP GLN THR LYS SER HIS ALA LEU LYS          
SEQRES  14 A  534  VAL ILE ALA ALA THR TRP CYS LEU SER PHE THR ILE MET          
SEQRES  15 A  534  THR PRO TYR PRO ILE TYR SER ASN LEU VAL PRO PHE THR          
SEQRES  16 A  534  LYS ASN ASN ASN GLN THR ALA ASN MET CYS ARG PHE LEU          
SEQRES  17 A  534  LEU PRO ASN ASP VAL MET GLN GLN SER TRP HIS THR PHE          
SEQRES  18 A  534  LEU LEU LEU ILE LEU PHE LEU ILE PRO GLY ILE VAL MET          
SEQRES  19 A  534  MET VAL ALA TYR GLY LEU ILE SER LEU GLU LEU TYR GLN          
SEQRES  20 A  534  GLY ILE ASN ILE PHE GLU MET LEU ARG ILE ASP GLU GLY          
SEQRES  21 A  534  LEU ARG LEU LYS ILE TYR LYS ASP THR GLU GLY TYR TYR          
SEQRES  22 A  534  THR ILE GLY ILE GLY HIS LEU LEU THR LYS SER PRO SER          
SEQRES  23 A  534  LEU ASN ALA ALA LYS SER GLU LEU ASP LYS ALA ILE GLY          
SEQRES  24 A  534  ARG ASN THR ASN GLY VAL ILE THR LYS ASP GLU ALA GLU          
SEQRES  25 A  534  LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY          
SEQRES  26 A  534  ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER          
SEQRES  27 A  534  LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE ASN MET VAL          
SEQRES  28 A  534  PHE GLN MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN          
SEQRES  29 A  534  SER LEU ARG MET LEU GLN GLN LYS ARG TRP ASP GLU ALA          
SEQRES  30 A  534  ALA VAL ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR          
SEQRES  31 A  534  PRO ASN ARG ALA LYS ARG VAL ILE THR THR PHE ARG THR          
SEQRES  32 A  534  GLY THR TRP ASP ALA TYR ALA ALA ASN LEU MET ALA LYS          
SEQRES  33 A  534  LYS ARG VAL ILE ARG MET LEU ILE VAL ILE VAL VAL LEU          
SEQRES  34 A  534  PHE PHE LEU CYS TRP MET PRO ILE PHE SER ALA ASN ALA          
SEQRES  35 A  534  TRP ARG ALA TYR ASP THR ALA SER ALA GLU ARG ARG LEU          
SEQRES  36 A  534  SER GLY THR PRO ILE SER PHE ILE LEU LEU LEU SER TYR          
SEQRES  37 A  534  THR SER SER CYS VAL ASN PRO ILE ILE TYR CYS PHE MET          
SEQRES  38 A  534  ASN LYS ARG PHE ARG LEU GLY PHE MET ALA THR PHE PRO          
SEQRES  39 A  534  CYS CYS PRO ASN PRO GLY PRO PRO GLY ALA ARG GLY GLU          
SEQRES  40 A  534  VAL GLY GLU GLU GLU GLU GLY GLU PHE LEU GLU VAL LEU          
SEQRES  41 A  534  PHE GLN GLY PRO HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES  42 A  534  HIS                                                          
HET    1OZ  A1501      31                                                       
HETNAM     1OZ N-[(3S)-1-METHYL-2-OXIDANYLIDENE-5-PHENYL-3H-1,4-                
HETNAM   2 1OZ  BENZODIAZEPIN-3-YL]-1H-INDOLE-2-CARBOXAMIDE                     
FORMUL   2  1OZ    C25 H20 N4 O2                                                
HELIX    1 AA1 TRP A   39  ASN A   69  1                                  31    
HELIX    2 AA2 LYS A   70  ARG A   73  5                                   4    
HELIX    3 AA3 THR A   74  CYS A   94  1                                  21    
HELIX    4 AA4 MET A   95  LYS A  105  1                                  11    
HELIX    5 AA5 GLY A  110  LYS A  145  1                                  36    
HELIX    6 AA6 ARG A  150  GLN A  153  5                                   4    
HELIX    7 AA7 THR A  154  MET A  173  1                                  20    
HELIX    8 AA8 THR A  174  TYR A  179  1                                   6    
HELIX    9 AA9 ASN A  202  PHE A  218  1                                  17    
HELIX   10 AB1 PHE A  218  GLY A  239  1                                  22    
HELIX   11 AB2 ASN A 1241  GLY A 1251  1                                  11    
HELIX   12 AB3 SER A 1277  GLY A 1290  1                                  14    
HELIX   13 AB4 THR A 1298  ASN A 1320  1                                  23    
HELIX   14 AB5 LYS A 1322  LEU A 1330  1                                   9    
HELIX   15 AB6 ASP A 1331  GLY A 1352  1                                  22    
HELIX   16 AB7 PHE A 1353  GLN A 1362  1                                  10    
HELIX   17 AB8 ARG A 1364  ALA A 1373  1                                  10    
HELIX   18 AB9 SER A 1375  THR A 1381  1                                   7    
HELIX   19 AC1 THR A 1381  GLY A 1395  1                                  15    
HELIX   20 AC2 TRP A 1397  TYR A 1400  5                                   4    
HELIX   21 AC3 ALA A  302  ASP A  339  1                                  38    
HELIX   22 AC4 ASP A  339  SER A  348  1                                  10    
HELIX   23 AC5 GLY A  349  SER A  362  1                                  14    
HELIX   24 AC6 CYS A  364  PHE A  372  1                                   9    
SHEET    1 AA1 2 SER A 180  THR A 186  0                                        
SHEET    2 AA1 2 THR A 192  PHE A 198 -1  O  MET A 195   N  VAL A 183           
SHEET    1 AA2 3 ARG A1253  LYS A1258  0                                        
SHEET    2 AA2 3 TYR A1264  GLY A1267 -1  O  THR A1265   N  TYR A1257           
SHEET    3 AA2 3 HIS A1270  THR A1273 -1  O  HIS A1270   N  ILE A1266           
SSBOND   1 CYS A  114    CYS A  196                          1555   1555  2.06  
CRYST1   54.780   72.420   86.140  90.00 107.28  90.00 P 1 21 1      2          
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      0.018255  0.000000  0.005680        0.00000                         
SCALE2      0.000000  0.013808  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012158        0.00000                         
ATOM      1  N   LYS A  37      23.040  30.982  63.587  1.00158.39           N  
ANISOU    1  N   LYS A  37    19824  20968  19388   -887    110    179       N  
ATOM      2  CA  LYS A  37      24.166  31.676  64.268  1.00158.58           C  
ANISOU    2  CA  LYS A  37    19819  21122  19313  -1015    138    202       C  
ATOM      3  C   LYS A  37      24.327  33.088  63.695  1.00153.96           C  
ANISOU    3  C   LYS A  37    19312  20484  18701  -1091    150    168       C  
ATOM      4  O   LYS A  37      23.375  33.886  63.796  1.00153.55           O  
ANISOU    4  O   LYS A  37    19332  20308  18702  -1113    158    104       O  
ATOM      5  CB  LYS A  37      25.458  30.874  64.099  1.00158.46           C  
ANISOU    5  CB  LYS A  37    19724  21263  19220   -993    133    284       C  
ATOM      6  CG  LYS A  37      25.296  29.365  64.201  1.00151.45           C  
ANISOU    6  CG  LYS A  37    18778  20401  18367   -879    116    325       C  
ATOM      7  CD  LYS A  37      26.448  28.608  63.589  1.00146.20           C  
ANISOU    7  CD  LYS A  37    18056  19852  17640   -822    107    404       C  
ATOM      8  CE  LYS A  37      27.790  29.028  64.146  1.00143.45           C  
ANISOU    8  CE  LYS A  37    17649  19681  17174   -926    129    448       C  
ATOM      9  NZ  LYS A  37      28.862  28.090  63.744  1.00142.33           N  
ANISOU    9  NZ  LYS A  37    17437  19669  16973   -856    121    530       N  
ATOM     10  N   GLU A  38      25.491  33.383  63.118  1.00147.12           N  
ANISOU   10  N   GLU A  38    18436  19711  17754  -1129    151    210       N  
ATOM     11  CA  GLU A  38      25.721  34.708  62.558  1.00141.57           C  
ANISOU   11  CA  GLU A  38    17812  18963  17016  -1207    164    182       C  
ATOM     12  C   GLU A  38      25.640  34.734  61.038  1.00140.53           C  
ANISOU   12  C   GLU A  38    17728  18752  16916  -1120    134    189       C  
ATOM     13  O   GLU A  38      25.071  35.669  60.470  1.00140.13           O  
ANISOU   13  O   GLU A  38    17767  18579  16898  -1130    135    144       O  
ATOM     14  CB  GLU A  38      27.083  35.244  63.015  1.00139.84           C  
ANISOU   14  CB  GLU A  38    17557  18904  16670  -1338    191    215       C  
ATOM     15  N   TRP A  39      26.150  33.714  60.359  1.00142.14           N  
ANISOU   15  N   TRP A  39    17876  19017  17112  -1030    107    244       N  
ATOM     16  CA  TRP A  39      26.074  33.822  58.881  1.00145.84           C  
ANISOU   16  CA  TRP A  39    18394  19410  17610   -958     80    248       C  
ATOM     17  C   TRP A  39      24.746  33.277  58.363  1.00137.83           C  
ANISOU   17  C   TRP A  39    17410  18248  16710   -837     57    217       C  
ATOM     18  O   TRP A  39      24.079  33.969  57.582  1.00139.06           O  
ANISOU   18  O   TRP A  39    17644  18281  16912   -817     48    180       O  
ATOM     19  CB  TRP A  39      27.265  33.133  58.209  1.00155.04           C  
ANISOU   19  CB  TRP A  39    19496  20702  18709   -923     64    317       C  
ATOM     20  CG  TRP A  39      27.458  31.689  58.553  1.00161.76           C  
ANISOU   20  CG  TRP A  39    20260  21632  19569   -837     56    366       C  
ATOM     21  CD1 TRP A  39      28.309  31.182  59.488  1.00170.40           C  
ANISOU   21  CD1 TRP A  39    21270  22882  20592   -874     72    412       C  
ATOM     22  CD2 TRP A  39      26.830  30.554  57.934  1.00158.45           C  
ANISOU   22  CD2 TRP A  39    19830  21145  19227   -699     32    378       C  
ATOM     23  NE1 TRP A  39      28.239  29.816  59.507  1.00169.01           N  
ANISOU   23  NE1 TRP A  39    21038  22732  20447   -764     61    453       N  
ATOM     24  CE2 TRP A  39      27.342  29.403  58.563  1.00160.46           C  
ANISOU   24  CE2 TRP A  39    20001  21512  19454   -658     37    431       C  
ATOM     25  CE3 TRP A  39      25.877  30.394  56.925  1.00156.09           C  
ANISOU   25  CE3 TRP A  39    19586  20705  19015   -608      9    350       C  
ATOM     26  CZ2 TRP A  39      26.936  28.118  58.214  1.00154.85           C  
ANISOU   26  CZ2 TRP A  39    19269  20769  18800   -532     23    454       C  
ATOM     27  CZ3 TRP A  39      25.477  29.123  56.577  1.00151.65           C  
ANISOU   27  CZ3 TRP A  39    18996  20117  18506   -490     -6    371       C  
ATOM     28  CH2 TRP A  39      26.001  28.001  57.215  1.00150.10           C  
ANISOU   28  CH2 TRP A  39    18725  20026  18281   -454      2    421       C  
ATOM     29  N   GLN A  40      24.350  32.115  58.861  1.00132.85           N  
ANISOU   29  N   GLN A  40    16723  17632  16119   -766     50    232       N  
ATOM     30  CA  GLN A  40      23.173  31.431  58.309  1.00129.85           C  
ANISOU   30  CA  GLN A  40    16366  17133  15839   -649     28    208       C  
ATOM     31  C   GLN A  40      22.039  32.359  57.891  1.00119.79           C  
ANISOU   31  C   GLN A  40    15179  15707  14630   -644     24    144       C  
ATOM     32  O   GLN A  40      21.539  32.201  56.768  1.00121.34           O  
ANISOU   32  O   GLN A  40    15408  15820  14875   -562      1    139       O  
ATOM     33  CB  GLN A  40      22.664  30.389  59.317  1.00137.40           C  
ANISOU   33  CB  GLN A  40    17269  18108  16828   -613     32    210       C  
ATOM     34  CG  GLN A  40      23.540  29.158  59.406  1.00151.67           C  
ANISOU   34  CG  GLN A  40    18998  20037  18594   -564     29    278       C  
ATOM     35  CD  GLN A  40      23.417  28.452  60.746  1.00163.68           C  
ANISOU   35  CD  GLN A  40    20463  21617  20112   -578     44    286       C  
ATOM     36  OE1 GLN A  40      22.821  28.981  61.687  1.00168.49           O  
ANISOU   36  OE1 GLN A  40    21085  22194  20738   -644     58    241       O  
ATOM     37  NE2 GLN A  40      23.982  27.250  60.838  1.00164.82           N  
ANISOU   37  NE2 GLN A  40    20545  21846  20232   -516     42    345       N  
ATOM     38  N   PRO A  41      21.597  33.330  58.697  1.00104.28           N  
ANISOU   38  N   PRO A  41    13255  13699  12668   -726     48     95       N  
ATOM     39  CA  PRO A  41      20.546  34.236  58.208  1.00 93.99           C  
ANISOU   39  CA  PRO A  41    12038  12251  11424   -710     46     38       C  
ATOM     40  C   PRO A  41      20.969  35.030  56.986  1.00 92.57           C  
ANISOU   40  C   PRO A  41    11917  12034  11221   -714     36     47       C  
ATOM     41  O   PRO A  41      20.126  35.311  56.125  1.00 93.47           O  
ANISOU   41  O   PRO A  41    12086  12034  11394   -648     20     21       O  
ATOM     42  CB  PRO A  41      20.279  35.159  59.404  1.00 87.07           C  
ANISOU   42  CB  PRO A  41    11190  11359  10534   -812     80     -8       C  
ATOM     43  CG  PRO A  41      20.896  34.488  60.557  1.00 88.97           C  
ANISOU   43  CG  PRO A  41    11350  11726  10730   -862     94     20       C  
ATOM     44  CD  PRO A  41      22.038  33.699  60.048  1.00 97.25           C  
ANISOU   44  CD  PRO A  41    12337  12891  11724   -837     79     90       C  
ATOM     45  N   ALA A  42      22.250  35.396  56.882  1.00 93.16           N  
ANISOU   45  N   ALA A  42    11980  12210  11208   -791     45     84       N  
ATOM     46  CA  ALA A  42      22.709  36.181  55.740  1.00 91.87           C  
ANISOU   46  CA  ALA A  42    11875  12018  11015   -805     37     92       C  
ATOM     47  C   ALA A  42      22.621  35.375  54.456  1.00 93.06           C  
ANISOU   47  C   ALA A  42    12008  12146  11203   -692      0    121       C  
ATOM     48  O   ALA A  42      22.050  35.837  53.462  1.00 98.95           O  
ANISOU   48  O   ALA A  42    12816  12788  11991   -646    -16    102       O  
ATOM     49  CB  ALA A  42      24.138  36.673  55.968  1.00 90.90           C  
ANISOU   49  CB  ALA A  42    11735  12024  10779   -920     55    124       C  
ATOM     50  N   VAL A  43      23.174  34.162  54.459  1.00 90.93           N  
ANISOU   50  N   VAL A  43    11657  11973  10918   -643    -13    169       N  
ATOM     51  CA  VAL A  43      23.100  33.323  53.268  1.00 86.90           C  
ANISOU   51  CA  VAL A  43    11130  11444  10443   -536    -43    197       C  
ATOM     52  C   VAL A  43      21.648  33.044  52.909  1.00 89.14           C  
ANISOU   52  C   VAL A  43    11447  11594  10827   -445    -57    157       C  
ATOM     53  O   VAL A  43      21.279  32.998  51.725  1.00 98.52           O  
ANISOU   53  O   VAL A  43    12664  12715  12052   -378    -79    157       O  
ATOM     54  CB  VAL A  43      23.899  32.025  53.477  1.00 88.18           C  
ANISOU   54  CB  VAL A  43    11203  11730  10573   -496    -47    254       C  
ATOM     55  CG1 VAL A  43      23.798  31.142  52.238  1.00 91.49           C  
ANISOU   55  CG1 VAL A  43    11611  12123  11029   -387    -74    279       C  
ATOM     56  CG2 VAL A  43      25.354  32.355  53.766  1.00 87.45           C  
ANISOU   56  CG2 VAL A  43    11073  11781  10372   -586    -34    294       C  
ATOM     57  N   GLN A  44      20.797  32.877  53.920  1.00 84.24           N  
ANISOU   57  N   GLN A  44    10820  10938  10248   -444    -44    122       N  
ATOM     58  CA  GLN A  44      19.380  32.649  53.667  1.00 83.24           C  
ANISOU   58  CA  GLN A  44    10722  10696  10209   -364    -55     81       C  
ATOM     59  C   GLN A  44      18.746  33.846  52.955  1.00 82.93           C  
ANISOU   59  C   GLN A  44    10768  10546  10198   -367    -59     44       C  
ATOM     60  O   GLN A  44      18.174  33.701  51.868  1.00 74.87           O  
ANISOU   60  O   GLN A  44     9769   9457   9222   -290    -81     40       O  
ATOM     61  CB  GLN A  44      18.672  32.324  54.985  1.00 79.80           C  
ANISOU   61  CB  GLN A  44    10263  10257   9802   -377    -39     49       C  
ATOM     62  CG  GLN A  44      18.882  30.868  55.412  1.00 92.48           C  
ANISOU   62  CG  GLN A  44    11793  11937  11407   -330    -43     84       C  
ATOM     63  CD  GLN A  44      18.406  30.579  56.828  1.00116.41           C  
ANISOU   63  CD  GLN A  44    14795  14986  14450   -362    -26     58       C  
ATOM     64  OE1 GLN A  44      18.534  29.457  57.324  1.00127.15           O  
ANISOU   64  OE1 GLN A  44    16099  16402  15808   -332    -25     84       O  
ATOM     65  NE2 GLN A  44      17.861  31.595  57.491  1.00123.92           N  
ANISOU   65  NE2 GLN A  44    15786  15885  15412   -424    -10      8       N  
ATOM     66  N   ILE A  45      18.850  35.040  53.552  1.00 83.32           N  
ANISOU   66  N   ILE A  45    10865  10574  10218   -456    -35     16       N  
ATOM     67  CA  ILE A  45      18.349  36.262  52.918  1.00 78.46           C  
ANISOU   67  CA  ILE A  45    10339   9852   9620   -462    -33    -16       C  
ATOM     68  C   ILE A  45      18.892  36.393  51.501  1.00 88.20           C  
ANISOU   68  C   ILE A  45    11593  11082  10835   -434    -57     17       C  
ATOM     69  O   ILE A  45      18.148  36.662  50.551  1.00 83.89           O  
ANISOU   69  O   ILE A  45    11092  10445  10338   -369    -73      3       O  
ATOM     70  CB  ILE A  45      18.713  37.489  53.773  1.00 76.70           C  
ANISOU   70  CB  ILE A  45    10166   9629   9348   -579      3    -41       C  
ATOM     71  CG1 ILE A  45      17.944  37.448  55.097  1.00 76.38           C  
ANISOU   71  CG1 ILE A  45    10113   9570   9337   -599     25    -83       C  
ATOM     72  CG2 ILE A  45      18.477  38.790  53.009  1.00 78.66           C  
ANISOU   72  CG2 ILE A  45    10515   9776   9595   -593      8    -63       C  
ATOM     73  CD1 ILE A  45      18.486  38.384  56.160  1.00 79.41           C  
ANISOU   73  CD1 ILE A  45    10524   9986   9661   -727     65   -102       C  
ATOM     74  N   LEU A  46      20.202  36.194  51.347  1.00 90.69           N  
ANISOU   74  N   LEU A  46    11873  11504  11079   -483    -58     62       N  
ATOM     75  CA  LEU A  46      20.847  36.239  50.040  1.00 80.14           C  
ANISOU   75  CA  LEU A  46    10548  10183   9719   -463    -81     96       C  
ATOM     76  C   LEU A  46      20.215  35.248  49.075  1.00 85.15           C  
ANISOU   76  C   LEU A  46    11155  10780  10418   -345   -111    107       C  
ATOM     77  O   LEU A  46      19.668  35.637  48.039  1.00 88.12           O  
ANISOU   77  O   LEU A  46    11579  11073  10830   -298   -128     97       O  
ATOM     78  CB  LEU A  46      22.332  35.939  50.205  1.00 79.73           C  
ANISOU   78  CB  LEU A  46    10442  10274   9578   -527    -78    143       C  
ATOM     79  CG  LEU A  46      23.203  35.968  48.959  1.00 82.16           C  
ANISOU   79  CG  LEU A  46    10751  10622   9844   -522   -100    181       C  
ATOM     80  CD1 LEU A  46      23.725  37.370  48.754  1.00 87.05           C  
ANISOU   80  CD1 LEU A  46    11446  11226  10404   -622    -87    168       C  
ATOM     81  CD2 LEU A  46      24.345  35.010  49.148  1.00 86.00           C  
ANISOU   81  CD2 LEU A  46    11149  11256  10272   -526   -102    233       C  
ATOM     82  N   LEU A  47      20.290  33.950  49.392  1.00 83.93           N  
ANISOU   82  N   LEU A  47    10925  10688  10275   -296   -116    130       N  
ATOM     83  CA  LEU A  47      19.844  32.936  48.433  1.00 79.39           C  
ANISOU   83  CA  LEU A  47    10326  10090   9750   -192   -140    145       C  
ATOM     84  C   LEU A  47      18.354  33.035  48.165  1.00 77.81           C  
ANISOU   84  C   LEU A  47    10163   9772   9629   -127   -147    101       C  
ATOM     85  O   LEU A  47      17.920  32.919  47.014  1.00 85.01           O  
ANISOU   85  O   LEU A  47    11092  10634  10576    -65   -167    103       O  
ATOM     86  CB  LEU A  47      20.181  31.532  48.924  1.00 73.98           C  
ANISOU   86  CB  LEU A  47     9563   9488   9059   -154   -137    176       C  
ATOM     87  CG  LEU A  47      21.643  31.117  48.840  1.00 76.94           C  
ANISOU   87  CG  LEU A  47     9887   9988   9358   -183   -136    232       C  
ATOM     88  CD1 LEU A  47      21.735  29.603  48.866  1.00 75.43           C  
ANISOU   88  CD1 LEU A  47     9633   9846   9180   -106   -137    264       C  
ATOM     89  CD2 LEU A  47      22.307  31.700  47.600  1.00 69.49           C  
ANISOU   89  CD2 LEU A  47     8972   9049   8383   -196   -153    251       C  
ATOM     90  N   TYR A  48      17.555  33.224  49.215  1.00 75.25           N  
ANISOU   90  N   TYR A  48     9847   9412   9333   -140   -130     61       N  
ATOM     91  CA  TYR A  48      16.114  33.345  49.041  1.00 69.82           C  
ANISOU   91  CA  TYR A  48     9190   8623   8716    -79   -136     18       C  
ATOM     92  C   TYR A  48      15.772  34.534  48.154  1.00 66.35           C  
ANISOU   92  C   TYR A  48     8824   8099   8287    -76   -143      2       C  
ATOM     93  O   TYR A  48      14.967  34.424  47.229  1.00 70.59           O  
ANISOU   93  O   TYR A  48     9377   8576   8870     -3   -161     -6       O  
ATOM     94  CB  TYR A  48      15.431  33.478  50.405  1.00 77.06           C  
ANISOU   94  CB  TYR A  48    10105   9524   9652   -107   -115    -24       C  
ATOM     95  CG  TYR A  48      14.853  32.189  50.965  1.00 88.97           C  
ANISOU   95  CG  TYR A  48    11556  11057  11193    -58   -116    -30       C  
ATOM     96  CD1 TYR A  48      13.560  31.780  50.633  1.00 92.58           C  
ANISOU   96  CD1 TYR A  48    12017  11449  11710     18   -127    -61       C  
ATOM     97  CD2 TYR A  48      15.587  31.394  51.838  1.00 92.03           C  
ANISOU   97  CD2 TYR A  48    11886  11535  11546    -89   -105     -4       C  
ATOM     98  CE1 TYR A  48      13.020  30.614  51.148  1.00 94.52           C  
ANISOU   98  CE1 TYR A  48    12217  11716  11979     55   -126    -70       C  
ATOM     99  CE2 TYR A  48      15.055  30.226  52.365  1.00 96.18           C  
ANISOU   99  CE2 TYR A  48    12368  12078  12099    -46   -105     -9       C  
ATOM    100  CZ  TYR A  48      13.772  29.834  52.017  1.00 99.33           C  
ANISOU  100  CZ  TYR A  48    12777  12407  12556     22   -115    -44       C  
ATOM    101  OH  TYR A  48      13.240  28.664  52.540  1.00 94.72           O  
ANISOU  101  OH  TYR A  48    12155  11840  11993     58   -113    -51       O  
ATOM    102  N   SER A  49      16.378  35.683  48.418  1.00 73.37           N  
ANISOU  102  N   SER A  49     9762   8984   9132   -157   -128     -1       N  
ATOM    103  CA  SER A  49      15.998  36.876  47.676  1.00 81.26           C  
ANISOU  103  CA  SER A  49    10842   9893  10140   -155   -130    -18       C  
ATOM    104  C   SER A  49      16.475  36.798  46.237  1.00 86.91           C  
ANISOU  104  C   SER A  49    11565  10613  10846   -124   -157     18       C  
ATOM    105  O   SER A  49      15.815  37.312  45.327  1.00 89.00           O  
ANISOU  105  O   SER A  49    11876  10798  11142    -76   -170      9       O  
ATOM    106  CB  SER A  49      16.560  38.116  48.366  1.00 92.58           C  
ANISOU  106  CB  SER A  49    12335  11319  11522   -258   -101    -32       C  
ATOM    107  OG  SER A  49      17.953  38.010  48.606  1.00 99.40           O  
ANISOU  107  OG  SER A  49    13170  12288  12311   -339    -94      2       O  
ATOM    108  N   LEU A  50      17.624  36.161  46.019  1.00 86.97           N  
ANISOU  108  N   LEU A  50    11523  10717  10806   -150   -165     60       N  
ATOM    109  CA  LEU A  50      18.120  35.937  44.671  1.00 79.15           C  
ANISOU  109  CA  LEU A  50    10528   9742   9805   -120   -191     94       C  
ATOM    110  C   LEU A  50      17.205  34.993  43.907  1.00 80.44           C  
ANISOU  110  C   LEU A  50    10660   9871  10033    -16   -211     94       C  
ATOM    111  O   LEU A  50      16.824  35.267  42.764  1.00 89.41           O  
ANISOU  111  O   LEU A  50    11826  10955  11192     26   -230     96       O  
ATOM    112  CB  LEU A  50      19.523  35.365  44.747  1.00 73.17           C  
ANISOU  112  CB  LEU A  50     9716   9105   8981   -165   -192    138       C  
ATOM    113  CG  LEU A  50      20.504  35.720  43.657  1.00 77.93           C  
ANISOU  113  CG  LEU A  50    10333   9742   9534   -193   -209    170       C  
ATOM    114  CD1 LEU A  50      20.894  37.190  43.755  1.00 76.48           C  
ANISOU  114  CD1 LEU A  50    10228   9529   9302   -284   -196    156       C  
ATOM    115  CD2 LEU A  50      21.704  34.828  43.846  1.00 82.74           C  
ANISOU  115  CD2 LEU A  50    10868  10482  10088   -212   -209    213       C  
ATOM    116  N   ILE A  51      16.855  33.861  44.525  1.00 71.61           N  
ANISOU  116  N   ILE A  51     9483   8786   8940     22   -206     91       N  
ATOM    117  CA  ILE A  51      16.002  32.872  43.872  1.00 68.78           C  
ANISOU  117  CA  ILE A  51     9096   8404   8635    112   -220     88       C  
ATOM    118  C   ILE A  51      14.602  33.426  43.640  1.00 74.52           C  
ANISOU  118  C   ILE A  51     9865   9033   9418    158   -224     48       C  
ATOM    119  O   ILE A  51      13.906  33.012  42.709  1.00 77.68           O  
ANISOU  119  O   ILE A  51    10259   9402   9854    225   -240     47       O  
ATOM    120  CB  ILE A  51      15.977  31.584  44.712  1.00 61.92           C  
ANISOU  120  CB  ILE A  51     8164   7590   7771    132   -209     92       C  
ATOM    121  CG1 ILE A  51      17.279  30.821  44.553  1.00 71.56           C  
ANISOU  121  CG1 ILE A  51     9338   8908   8944    118   -210    142       C  
ATOM    122  CG2 ILE A  51      14.853  30.687  44.310  1.00 60.36           C  
ANISOU  122  CG2 ILE A  51     7949   7356   7630    213   -216     75       C  
ATOM    123  CD1 ILE A  51      17.354  29.634  45.469  1.00 77.90           C  
ANISOU  123  CD1 ILE A  51    10087   9767   9746    135   -195    151       C  
ATOM    124  N   PHE A  52      14.166  34.368  44.468  1.00 78.74           N  
ANISOU  124  N   PHE A  52    10441   9522   9956    125   -208     14       N  
ATOM    125  CA  PHE A  52      12.899  35.048  44.227  1.00 82.87           C  
ANISOU  125  CA  PHE A  52    11008   9953  10524    171   -210    -22       C  
ATOM    126  C   PHE A  52      12.981  35.925  42.987  1.00 87.63           C  
ANISOU  126  C   PHE A  52    11666  10507  11123    183   -225     -7       C  
ATOM    127  O   PHE A  52      12.108  35.863  42.112  1.00 89.32           O  
ANISOU  127  O   PHE A  52    11884  10677  11375    253   -241    -12       O  
ATOM    128  CB  PHE A  52      12.537  35.861  45.467  1.00 77.54           C  
ANISOU  128  CB  PHE A  52    10368   9245   9849    127   -184    -60       C  
ATOM    129  CG  PHE A  52      11.261  36.657  45.365  1.00 72.48           C  
ANISOU  129  CG  PHE A  52     9776   8512   9250    175   -180    -98       C  
ATOM    130  CD1 PHE A  52      10.043  36.091  45.722  1.00 67.56           C  
ANISOU  130  CD1 PHE A  52     9123   7874   8674    235   -181   -130       C  
ATOM    131  CD2 PHE A  52      11.293  38.002  45.009  1.00 68.94           C  
ANISOU  131  CD2 PHE A  52     9407   7996   8790    157   -173   -102       C  
ATOM    132  CE1 PHE A  52       8.880  36.836  45.689  1.00 66.00           C  
ANISOU  132  CE1 PHE A  52     8966   7602   8510    282   -176   -165       C  
ATOM    133  CE2 PHE A  52      10.133  38.756  44.973  1.00 70.13           C  
ANISOU  133  CE2 PHE A  52     9605   8064   8977    207   -167   -135       C  
ATOM    134  CZ  PHE A  52       8.924  38.169  45.308  1.00 68.66           C  
ANISOU  134  CZ  PHE A  52     9381   7870   8837    273   -169   -166       C  
ATOM    135  N   LEU A  53      14.044  36.729  42.881  1.00 88.15           N  
ANISOU  135  N   LEU A  53    11770  10584  11137    113   -221     13       N  
ATOM    136  CA  LEU A  53      14.193  37.625  41.739  1.00 84.65           C  
ANISOU  136  CA  LEU A  53    11385  10093  10684    115   -235     27       C  
ATOM    137  C   LEU A  53      14.252  36.845  40.439  1.00 83.35           C  
ANISOU  137  C   LEU A  53    11182   9952  10534    170   -264     57       C  
ATOM    138  O   LEU A  53      13.493  37.121  39.508  1.00 87.06           O  
ANISOU  138  O   LEU A  53    11676  10367  11036    227   -279     55       O  
ATOM    139  CB  LEU A  53      15.439  38.485  41.907  1.00 92.80           C  
ANISOU  139  CB  LEU A  53    12461  11150  11649     18   -224     43       C  
ATOM    140  CG  LEU A  53      15.304  39.404  43.115  1.00109.34           C  
ANISOU  140  CG  LEU A  53    14606  13209  13728    -42   -190     10       C  
ATOM    141  CD1 LEU A  53      16.626  40.075  43.464  1.00120.02           C  
ANISOU  141  CD1 LEU A  53    15991  14610  15003   -154   -174     24       C  
ATOM    142  CD2 LEU A  53      14.220  40.423  42.857  1.00107.28           C  
ANISOU  142  CD2 LEU A  53    14423  12834  13504      1   -184    -18       C  
ATOM    143  N   LEU A  54      15.143  35.852  40.364  1.00 82.48           N  
ANISOU  143  N   LEU A  54    11012   9929  10399    155   -270     86       N  
ATOM    144  CA  LEU A  54      15.245  35.038  39.157  1.00 87.93           C  
ANISOU  144  CA  LEU A  54    11664  10644  11100    203   -294    114       C  
ATOM    145  C   LEU A  54      13.904  34.417  38.790  1.00 83.91           C  
ANISOU  145  C   LEU A  54    11134  10095  10652    288   -300     94       C  
ATOM    146  O   LEU A  54      13.522  34.399  37.616  1.00 88.03           O  
ANISOU  146  O   LEU A  54    11661  10593  11193    332   -319    104       O  
ATOM    147  CB  LEU A  54      16.291  33.937  39.339  1.00 85.42           C  
ANISOU  147  CB  LEU A  54    11283  10425  10750    185   -293    144       C  
ATOM    148  CG  LEU A  54      17.760  34.311  39.491  1.00 87.02           C  
ANISOU  148  CG  LEU A  54    11487  10695  10881    105   -290    173       C  
ATOM    149  CD1 LEU A  54      18.596  33.056  39.644  1.00 90.80           C  
ANISOU  149  CD1 LEU A  54    11894  11272  11335    112   -288    204       C  
ATOM    150  CD2 LEU A  54      18.220  35.099  38.302  1.00 84.39           C  
ANISOU  150  CD2 LEU A  54    11197  10344  10525     85   -311    190       C  
ATOM    151  N   SER A  55      13.178  33.902  39.781  1.00 78.17           N  
ANISOU  151  N   SER A  55    10382   9367   9951    309   -284     66       N  
ATOM    152  CA  SER A  55      11.938  33.188  39.500  1.00 82.00           C  
ANISOU  152  CA  SER A  55    10841   9830  10485    382   -288     46       C  
ATOM    153  C   SER A  55      10.837  34.144  39.063  1.00 84.07           C  
ANISOU  153  C   SER A  55    11149  10016  10778    422   -295     23       C  
ATOM    154  O   SER A  55      10.054  33.827  38.162  1.00 79.11           O  
ANISOU  154  O   SER A  55    10508   9374  10177    480   -308     22       O  
ATOM    155  CB  SER A  55      11.511  32.386  40.730  1.00 86.78           C  
ANISOU  155  CB  SER A  55    11409  10460  11104    385   -270     20       C  
ATOM    156  OG  SER A  55      10.407  31.543  40.461  1.00 89.02           O  
ANISOU  156  OG  SER A  55    11663  10736  11424    447   -272      2       O  
ATOM    157  N   VAL A  56      10.768  35.320  39.682  1.00 84.68           N  
ANISOU  157  N   VAL A  56    11282  10046  10848    392   -283      5       N  
ATOM    158  CA  VAL A  56       9.781  36.321  39.286  1.00 84.07           C  
ANISOU  158  CA  VAL A  56    11255   9891  10795    435   -285    -13       C  
ATOM    159  C   VAL A  56      10.114  36.870  37.902  1.00 97.67           C  
ANISOU  159  C   VAL A  56    13011  11592  12508    445   -306     19       C  
ATOM    160  O   VAL A  56       9.306  36.795  36.967  1.00101.24           O  
ANISOU  160  O   VAL A  56    13456  12024  12987    508   -321     22       O  
ATOM    161  CB  VAL A  56       9.706  37.435  40.346  1.00 77.55           C  
ANISOU  161  CB  VAL A  56    10488   9017   9961    396   -261    -40       C  
ATOM    162  CG1 VAL A  56       9.263  38.759  39.742  1.00 81.81           C  
ANISOU  162  CG1 VAL A  56    11106   9474  10506    420   -262    -42       C  
ATOM    163  CG2 VAL A  56       8.759  37.022  41.441  1.00 75.41           C  
ANISOU  163  CG2 VAL A  56    10188   8746   9719    420   -245    -81       C  
ATOM    164  N   LEU A  57      11.322  37.415  37.748  1.00101.10           N  
ANISOU  164  N   LEU A  57    13478  12037  12899    378   -307     43       N  
ATOM    165  CA  LEU A  57      11.769  37.884  36.443  1.00 96.54           C  
ANISOU  165  CA  LEU A  57    12930  11446  12306    377   -329     74       C  
ATOM    166  C   LEU A  57      11.695  36.765  35.412  1.00 94.75           C  
ANISOU  166  C   LEU A  57    12639  11267  12095    421   -351     96       C  
ATOM    167  O   LEU A  57      11.126  36.937  34.328  1.00100.39           O  
ANISOU  167  O   LEU A  57    13361  11954  12829    468   -368    106       O  
ATOM    168  CB  LEU A  57      13.189  38.442  36.565  1.00 92.93           C  
ANISOU  168  CB  LEU A  57    12506  11014  11789    287   -326     95       C  
ATOM    169  CG  LEU A  57      13.990  38.862  35.333  1.00 89.25           C  
ANISOU  169  CG  LEU A  57    12067  10553  11292    261   -348    129       C  
ATOM    170  CD1 LEU A  57      14.831  40.072  35.679  1.00 85.44           C  
ANISOU  170  CD1 LEU A  57    11661  10047  10756    177   -335    130       C  
ATOM    171  CD2 LEU A  57      14.880  37.726  34.856  1.00 88.77           C  
ANISOU  171  CD2 LEU A  57    11934  10582  11211    248   -364    158       C  
ATOM    172  N   GLY A  58      12.235  35.593  35.754  1.00 87.56           N  
ANISOU  172  N   GLY A  58    11667  10427  11176    406   -348    104       N  
ATOM    173  CA  GLY A  58      12.307  34.511  34.784  1.00 79.17           C  
ANISOU  173  CA  GLY A  58    10550   9409  10123    439   -363    125       C  
ATOM    174  C   GLY A  58      10.948  34.101  34.255  1.00 78.45           C  
ANISOU  174  C   GLY A  58    10438   9294  10076    513   -368    109       C  
ATOM    175  O   GLY A  58      10.744  34.005  33.043  1.00 78.81           O  
ANISOU  175  O   GLY A  58    10476   9339  10131    542   -386    126       O  
ATOM    176  N   ASN A  59       9.992  33.871  35.156  1.00 73.02           N  
ANISOU  176  N   ASN A  59     9738   8592   9414    541   -352     74       N  
ATOM    177  CA  ASN A  59       8.714  33.339  34.710  1.00 66.84           C  
ANISOU  177  CA  ASN A  59     8926   7805   8666    606   -355     57       C  
ATOM    178  C   ASN A  59       7.847  34.413  34.067  1.00 71.24           C  
ANISOU  178  C   ASN A  59     9523   8305   9239    649   -366     54       C  
ATOM    179  O   ASN A  59       7.179  34.135  33.068  1.00 82.32           O  
ANISOU  179  O   ASN A  59    10904   9715  10657    694   -378     60       O  
ATOM    180  CB  ASN A  59       7.972  32.657  35.864  1.00 69.72           C  
ANISOU  180  CB  ASN A  59     9261   8183   9047    620   -336     21       C  
ATOM    181  CG  ASN A  59       8.707  31.424  36.389  1.00 72.41           C  
ANISOU  181  CG  ASN A  59     9558   8581   9373    592   -324     28       C  
ATOM    182  OD1 ASN A  59       8.634  30.330  35.811  1.00 68.36           O  
ANISOU  182  OD1 ASN A  59     9007   8104   8863    611   -324     37       O  
ATOM    183  ND2 ASN A  59       9.420  31.600  37.495  1.00 71.84           N  
ANISOU  183  ND2 ASN A  59     9495   8519   9282    544   -311     26       N  
ATOM    184  N   THR A  60       7.824  35.639  34.594  1.00 65.73           N  
ANISOU  184  N   THR A  60     8885   7552   8537    636   -359     44       N  
ATOM    185  CA  THR A  60       7.008  36.652  33.928  1.00 78.83           C  
ANISOU  185  CA  THR A  60    10587   9156  10211    686   -368     45       C  
ATOM    186  C   THR A  60       7.536  36.937  32.526  1.00 86.97           C  
ANISOU  186  C   THR A  60    11632  10185  11228    683   -391     84       C  
ATOM    187  O   THR A  60       6.758  37.153  31.589  1.00 93.29           O  
ANISOU  187  O   THR A  60    12431  10972  12044    737   -404     94       O  
ATOM    188  CB  THR A  60       6.947  37.943  34.740  1.00 82.03           C  
ANISOU  188  CB  THR A  60    11064   9492  10610    672   -351     28       C  
ATOM    189  OG1 THR A  60       8.249  38.537  34.777  1.00 92.19           O  
ANISOU  189  OG1 THR A  60    12398  10769  11860    599   -350     49       O  
ATOM    190  CG2 THR A  60       6.461  37.666  36.136  1.00 80.11           C  
ANISOU  190  CG2 THR A  60    10805   9254  10379    670   -328    -12       C  
ATOM    191  N   LEU A  61       8.856  36.926  32.364  1.00 86.71           N  
ANISOU  191  N   LEU A  61    11610  10173  11164    618   -397    108       N  
ATOM    192  CA  LEU A  61       9.454  36.976  31.037  1.00 82.54           C  
ANISOU  192  CA  LEU A  61    11082   9658  10621    607   -420    144       C  
ATOM    193  C   LEU A  61       8.879  35.890  30.131  1.00 75.39           C  
ANISOU  193  C   LEU A  61    10111   8798   9737    652   -432    152       C  
ATOM    194  O   LEU A  61       8.299  36.185  29.080  1.00 73.44           O  
ANISOU  194  O   LEU A  61     9866   8536   9500    692   -448    165       O  
ATOM    195  CB  LEU A  61      10.962  36.822  31.162  1.00 75.58           C  
ANISOU  195  CB  LEU A  61    10202   8815   9698    530   -422    164       C  
ATOM    196  CG  LEU A  61      11.719  37.398  29.992  1.00 72.48           C  
ANISOU  196  CG  LEU A  61     9841   8418   9280    501   -445    197       C  
ATOM    197  CD1 LEU A  61      12.231  38.760  30.406  1.00 73.06           C  
ANISOU  197  CD1 LEU A  61     9999   8438   9322    452   -438    197       C  
ATOM    198  CD2 LEU A  61      12.829  36.433  29.542  1.00 69.21           C  
ANISOU  198  CD2 LEU A  61     9375   8081   8841    462   -455    220       C  
ATOM    199  N   VAL A  62       9.024  34.622  30.540  1.00 67.39           N  
ANISOU  199  N   VAL A  62     9038   7840   8726    645   -421    142       N  
ATOM    200  CA  VAL A  62       8.493  33.506  29.760  1.00 64.96           C  
ANISOU  200  CA  VAL A  62     8672   7576   8434    679   -425    145       C  
ATOM    201  C   VAL A  62       7.025  33.733  29.417  1.00 78.58           C  
ANISOU  201  C   VAL A  62    10391   9282  10186    744   -427    129       C  
ATOM    202  O   VAL A  62       6.590  33.469  28.289  1.00 84.98           O  
ANISOU  202  O   VAL A  62    11176  10112  11001    770   -439    143       O  
ATOM    203  CB  VAL A  62       8.689  32.182  30.513  1.00 60.00           C  
ANISOU  203  CB  VAL A  62     7997   6997   7805    667   -405    131       C  
ATOM    204  CG1 VAL A  62       7.817  31.092  29.914  1.00 56.09           C  
ANISOU  204  CG1 VAL A  62     7451   6535   7326    706   -400    122       C  
ATOM    205  CG2 VAL A  62      10.137  31.767  30.484  1.00 56.73           C  
ANISOU  205  CG2 VAL A  62     7574   6620   7361    616   -406    156       C  
ATOM    206  N   ILE A  63       6.238  34.237  30.373  1.00 78.12           N  
ANISOU  206  N   ILE A  63    10352   9191  10140    769   -414    100       N  
ATOM    207  CA  ILE A  63       4.820  34.473  30.104  1.00 78.09           C  
ANISOU  207  CA  ILE A  63    10337   9177  10156    836   -415     84       C  
ATOM    208  C   ILE A  63       4.640  35.611  29.109  1.00 89.73           C  
ANISOU  208  C   ILE A  63    11853  10612  11630    865   -433    111       C  
ATOM    209  O   ILE A  63       3.880  35.494  28.141  1.00 95.40           O  
ANISOU  209  O   ILE A  63    12544  11351  12354    908   -444    122       O  
ATOM    210  CB  ILE A  63       4.064  34.773  31.404  1.00 76.37           C  
ANISOU  210  CB  ILE A  63    10132   8935   9950    857   -396     45       C  
ATOM    211  CG1 ILE A  63       4.057  33.560  32.336  1.00 76.15           C  
ANISOU  211  CG1 ILE A  63    10058   8952   9924    834   -378     18       C  
ATOM    212  CG2 ILE A  63       2.658  35.239  31.092  1.00 73.87           C  
ANISOU  212  CG2 ILE A  63     9811   8609   9648    930   -398     33       C  
ATOM    213  CD1 ILE A  63       3.990  33.954  33.793  1.00 64.86           C  
ANISOU  213  CD1 ILE A  63     8653   7494   8497    820   -361    -14       C  
ATOM    214  N   THR A  64       5.299  36.748  29.351  1.00 92.25           N  
ANISOU  214  N   THR A  64    12241  10872  11937    840   -435    122       N  
ATOM    215  CA  THR A  64       5.069  37.914  28.503  1.00 93.40           C  
ANISOU  215  CA  THR A  64    12439  10969  12081    871   -449    146       C  
ATOM    216  C   THR A  64       5.546  37.663  27.074  1.00 93.34           C  
ANISOU  216  C   THR A  64    12410  10990  12063    858   -473    184       C  
ATOM    217  O   THR A  64       4.914  38.124  26.118  1.00 96.22           O  
ANISOU  217  O   THR A  64    12780  11346  12433    904   -487    204       O  
ATOM    218  CB  THR A  64       5.761  39.144  29.088  1.00 96.06           C  
ANISOU  218  CB  THR A  64    12862  11235  12401    835   -441    148       C  
ATOM    219  OG1 THR A  64       7.151  38.859  29.268  1.00 98.58           O  
ANISOU  219  OG1 THR A  64    13186  11575  12694    752   -443    159       O  
ATOM    220  CG2 THR A  64       5.139  39.545  30.435  1.00 92.04           C  
ANISOU  220  CG2 THR A  64    12379  10689  11904    854   -414    111       C  
ATOM    221  N   VAL A  65       6.657  36.938  26.906  1.00 86.72           N  
ANISOU  221  N   VAL A  65    11548  10192  11209    796   -479    195       N  
ATOM    222  CA  VAL A  65       7.096  36.563  25.566  1.00 84.68           C  
ANISOU  222  CA  VAL A  65    11263   9969  10941    782   -500    227       C  
ATOM    223  C   VAL A  65       6.029  35.723  24.877  1.00 97.59           C  
ANISOU  223  C   VAL A  65    12832  11652  12594    831   -501    223       C  
ATOM    224  O   VAL A  65       5.661  35.981  23.725  1.00105.68           O  
ANISOU  224  O   VAL A  65    13849  12683  13620    856   -519    247       O  
ATOM    225  CB  VAL A  65       8.445  35.826  25.628  1.00 79.50           C  
ANISOU  225  CB  VAL A  65    10587   9354  10264    713   -501    236       C  
ATOM    226  CG1 VAL A  65       8.573  34.863  24.473  1.00 75.36           C  
ANISOU  226  CG1 VAL A  65    10006   8888   9741    710   -513    254       C  
ATOM    227  CG2 VAL A  65       9.592  36.812  25.592  1.00 80.55           C  
ANISOU  227  CG2 VAL A  65    10784   9454  10366    657   -512    255       C  
ATOM    228  N   LEU A  66       5.502  34.715  25.581  1.00 94.42           N  
ANISOU  228  N   LEU A  66    12383  11288  12204    843   -482    193       N  
ATOM    229  CA  LEU A  66       4.519  33.815  24.983  1.00 86.71           C  
ANISOU  229  CA  LEU A  66    11343  10365  11236    877   -478    186       C  
ATOM    230  C   LEU A  66       3.200  34.528  24.706  1.00 89.50           C  
ANISOU  230  C   LEU A  66    11699  10707  11599    946   -482    183       C  
ATOM    231  O   LEU A  66       2.573  34.293  23.669  1.00 89.74           O  
ANISOU  231  O   LEU A  66    11693  10778  11629    971   -491    197       O  
ATOM    232  CB  LEU A  66       4.296  32.606  25.888  1.00 80.58           C  
ANISOU  232  CB  LEU A  66    10526   9627  10463    867   -453    152       C  
ATOM    233  CG  LEU A  66       5.500  31.661  25.911  1.00 79.01           C  
ANISOU  233  CG  LEU A  66    10313   9456  10253    812   -447    161       C  
ATOM    234  CD1 LEU A  66       5.398  30.556  27.011  1.00 65.39           C  
ANISOU  234  CD1 LEU A  66     8560   7756   8528    801   -420    129       C  
ATOM    235  CD2 LEU A  66       5.733  31.080  24.509  1.00 68.49           C  
ANISOU  235  CD2 LEU A  66     8948   8163   8913    800   -457    186       C  
ATOM    236  N   ILE A  67       2.756  35.393  25.622  1.00 95.92           N  
ANISOU  236  N   ILE A  67    12554  11471  12420    977   -474    166       N  
ATOM    237  CA  ILE A  67       1.540  36.167  25.378  1.00 98.23           C  
ANISOU  237  CA  ILE A  67    12853  11751  12720   1051   -477    167       C  
ATOM    238  C   ILE A  67       1.742  37.109  24.197  1.00110.05           C  
ANISOU  238  C   ILE A  67    14384  13219  14210   1067   -500    210       C  
ATOM    239  O   ILE A  67       0.820  37.347  23.407  1.00118.56           O  
ANISOU  239  O   ILE A  67    15440  14320  15288   1123   -508    226       O  
ATOM    240  CB  ILE A  67       1.121  36.926  26.652  1.00 88.29           C  
ANISOU  240  CB  ILE A  67    11639  10439  11470   1079   -460    139       C  
ATOM    241  CG1 ILE A  67       0.498  35.972  27.678  1.00 88.72           C  
ANISOU  241  CG1 ILE A  67    11645  10535  11531   1081   -440     94       C  
ATOM    242  CG2 ILE A  67       0.158  38.072  26.334  1.00 82.26           C  
ANISOU  242  CG2 ILE A  67    10906   9640  10710   1158   -464    150       C  
ATOM    243  CD1 ILE A  67       0.178  36.654  29.021  1.00 84.84           C  
ANISOU  243  CD1 ILE A  67    11194   9994  11048   1099   -422     62       C  
ATOM    244  N   ARG A  68       2.956  37.645  24.045  1.00110.03           N  
ANISOU  244  N   ARG A  68    14436  13172  14198   1015   -510    232       N  
ATOM    245  CA  ARG A  68       3.249  38.528  22.918  1.00107.59           C  
ANISOU  245  CA  ARG A  68    14165  12833  13879   1020   -532    273       C  
ATOM    246  C   ARG A  68       3.138  37.782  21.595  1.00100.65           C  
ANISOU  246  C   ARG A  68    13223  12023  12997   1015   -550    296       C  
ATOM    247  O   ARG A  68       2.315  38.126  20.742  1.00103.14           O  
ANISOU  247  O   ARG A  68    13523  12354  13313   1067   -560    318       O  
ATOM    248  CB  ARG A  68       4.646  39.136  23.069  1.00105.44           C  
ANISOU  248  CB  ARG A  68    13961  12511  13590    951   -539    286       C  
ATOM    249  CG  ARG A  68       4.670  40.644  23.073  1.00107.89           C  
ANISOU  249  CG  ARG A  68    14366  12737  13892    971   -541    302       C  
ATOM    250  CD  ARG A  68       6.030  41.165  23.503  1.00112.13           C  
ANISOU  250  CD  ARG A  68    14970  13231  14405    891   -540    305       C  
ATOM    251  NE  ARG A  68       7.072  40.935  22.506  1.00115.37           N  
ANISOU  251  NE  ARG A  68    15371  13670  14794    830   -564    333       N  
ATOM    252  CZ  ARG A  68       8.357  41.219  22.696  1.00115.80           C  
ANISOU  252  CZ  ARG A  68    15469  13712  14819    751   -567    338       C  
ATOM    253  NH1 ARG A  68       8.762  41.738  23.853  1.00116.60           N  
ANISOU  253  NH1 ARG A  68    15625  13770  14906    719   -546    317       N  
ATOM    254  NH2 ARG A  68       9.237  40.984  21.733  1.00113.17           N  
ANISOU  254  NH2 ARG A  68    15122  13414  14466    700   -590    363       N  
ATOM    255  N   ASN A  69       3.995  36.783  21.414  1.00 93.56           N  
ANISOU  255  N   ASN A  69    12289  11167  12092    953   -551    294       N  
ATOM    256  CA  ASN A  69       4.096  36.098  20.102  1.00100.58           C  
ANISOU  256  CA  ASN A  69    13125  12115  12975    935   -565    317       C  
ATOM    257  C   ASN A  69       3.088  34.970  19.888  1.00 98.38           C  
ANISOU  257  C   ASN A  69    12767  11911  12701    959   -551    299       C  
ATOM    258  O   ASN A  69       3.237  33.915  20.495  1.00 89.49           O  
ANISOU  258  O   ASN A  69    11609  10815  11576    933   -531    272       O  
ATOM    259  CB  ASN A  69       5.528  35.643  19.847  1.00106.20           C  
ANISOU  259  CB  ASN A  69    13841  12838  13675    858   -573    328       C  
ATOM    260  CG  ASN A  69       6.496  36.709  20.291  1.00112.05           C  
ANISOU  260  CG  ASN A  69    14660  13513  14403    826   -582    338       C  
ATOM    261  OD1 ASN A  69       6.101  37.632  20.993  1.00112.67           O  
ANISOU  261  OD1 ASN A  69    14790  13534  14485    857   -575    330       O  
ATOM    262  ND2 ASN A  69       7.746  36.600  19.882  1.00114.69           N  
ANISOU  262  ND2 ASN A  69    15004  13857  14718    762   -594    354       N  
ATOM    263  N   LYS A  70       2.099  35.212  19.032  1.00104.79           N  
ANISOU  263  N   LYS A  70    13550  12753  13511   1006   -559    316       N  
ATOM    264  CA  LYS A  70       1.210  34.129  18.631  1.00106.35           C  
ANISOU  264  CA  LYS A  70    13671  13033  13704   1016   -546    301       C  
ATOM    265  C   LYS A  70       1.983  32.997  17.961  1.00107.65           C  
ANISOU  265  C   LYS A  70    13799  13244  13861    950   -542    305       C  
ATOM    266  O   LYS A  70       1.616  31.825  18.110  1.00109.02           O  
ANISOU  266  O   LYS A  70    13924  13471  14029    934   -519    279       O  
ATOM    267  CB  LYS A  70       0.121  34.654  17.699  1.00107.63           C  
ANISOU  267  CB  LYS A  70    13806  13230  13858   1073   -557    326       C  
ATOM    268  N   ARG A  71       3.071  33.345  17.282  1.00107.36           N  
ANISOU  268  N   ARG A  71    13789  13183  13821    909   -563    334       N  
ATOM    269  CA  ARG A  71       3.874  32.317  16.580  1.00106.43           C  
ANISOU  269  CA  ARG A  71    13637  13107  13695    848   -560    339       C  
ATOM    270  C   ARG A  71       4.452  31.330  17.595  1.00106.65           C  
ANISOU  270  C   ARG A  71    13662  13137  13724    817   -534    308       C  
ATOM    271  O   ARG A  71       4.613  30.159  17.238  1.00105.31           O  
ANISOU  271  O   ARG A  71    13452  13013  13547    786   -516    300       O  
ATOM    272  CB  ARG A  71       4.992  32.984  15.777  1.00108.58           C  
ANISOU  272  CB  ARG A  71    13943  13353  13961    811   -589    374       C  
ATOM    273  CG  ARG A  71       6.369  32.389  16.024  1.00112.63           C  
ANISOU  273  CG  ARG A  71    14466  13864  14467    750   -585    370       C  
ATOM    274  CD  ARG A  71       7.395  32.876  15.020  1.00118.89           C  
ANISOU  274  CD  ARG A  71    15277  14651  15246    706   -614    404       C  
ATOM    275  NE  ARG A  71       7.714  34.289  15.170  1.00123.37           N  
ANISOU  275  NE  ARG A  71    15912  15156  15809    712   -638    422       N  
ATOM    276  CZ  ARG A  71       8.708  34.763  15.910  1.00120.63           C  
ANISOU  276  CZ  ARG A  71    15616  14768  15450    681   -641    420       C  
ATOM    277  NH1 ARG A  71       9.492  33.935  16.580  1.00110.37           N  
ANISOU  277  NH1 ARG A  71    14302  13489  14144    646   -624    402       N  
ATOM    278  NH2 ARG A  71       8.915  36.064  15.978  1.00123.60           N  
ANISOU  278  NH2 ARG A  71    16060  15085  15817    682   -659    435       N  
ATOM    279  N   MET A  72       4.726  31.786  18.819  1.00107.28           N  
ANISOU  279  N   MET A  72    13785  13167  13811    826   -530    293       N  
ATOM    280  CA  MET A  72       5.342  30.922  19.818  1.00104.32           C  
ANISOU  280  CA  MET A  72    13408  12793  13435    797   -506    268       C  
ATOM    281  C   MET A  72       4.358  29.901  20.389  1.00105.14           C  
ANISOU  281  C   MET A  72    13472  12934  13541    816   -476    233       C  
ATOM    282  O   MET A  72       4.768  28.794  20.749  1.00115.45           O  
ANISOU  282  O   MET A  72    14761  14262  14842    788   -453    218       O  
ATOM    283  CB  MET A  72       5.931  31.779  20.940  1.00105.57           C  
ANISOU  283  CB  MET A  72    13622  12892  13595    794   -511    264       C  
ATOM    284  CG  MET A  72       7.226  32.476  20.591  1.00105.39           C  
ANISOU  284  CG  MET A  72    13641  12843  13560    752   -533    292       C  
ATOM    285  SD  MET A  72       8.561  31.299  20.397  1.00104.38           S  
ANISOU  285  SD  MET A  72    13485  12759  13415    693   -524    299       S  
ATOM    286  CE  MET A  72       9.978  32.309  20.834  1.00105.14           C  
ANISOU  286  CE  MET A  72    13640  12819  13490    647   -542    316       C  
ATOM    287  N   ARG A  73       3.067  30.239  20.469  1.00 96.10           N  
ANISOU  287  N   ARG A  73    12314  11801  12401    864   -474    220       N  
ATOM    288  CA  ARG A  73       2.071  29.399  21.140  1.00 89.95           C  
ANISOU  288  CA  ARG A  73    11502  11058  11619    880   -447    182       C  
ATOM    289  C   ARG A  73       1.853  28.089  20.382  1.00 91.67           C  
ANISOU  289  C   ARG A  73    11670  11340  11820    850   -426    175       C  
ATOM    290  O   ARG A  73       0.857  27.888  19.684  1.00101.96           O  
ANISOU  290  O   ARG A  73    12935  12695  13111    865   -421    173       O  
ATOM    291  CB  ARG A  73       0.752  30.148  21.300  1.00 99.09           C  
ANISOU  291  CB  ARG A  73    12651  12220  12778    940   -452    173       C  
ATOM    292  CG  ARG A  73       0.715  31.221  22.393  1.00 97.60           C  
ANISOU  292  CG  ARG A  73    12513  11968  12604    974   -458    164       C  
ATOM    293  CD  ARG A  73       0.463  32.608  21.789  1.00 96.11           C  
ANISOU  293  CD  ARG A  73    12354  11745  12419   1018   -483    195       C  
ATOM    294  NE  ARG A  73      -0.780  33.239  22.229  1.00 94.59           N  
ANISOU  294  NE  ARG A  73    12159  11552  12228   1086   -480    181       N  
ATOM    295  CZ  ARG A  73      -1.882  33.341  21.488  1.00107.05           C  
ANISOU  295  CZ  ARG A  73    13695  13183  13794   1132   -484    190       C  
ATOM    296  NH1 ARG A  73      -1.908  32.845  20.256  1.00115.87           N  
ANISOU  296  NH1 ARG A  73    14771  14356  14898   1112   -491    212       N  
ATOM    297  NH2 ARG A  73      -2.961  33.947  21.973  1.00106.26           N  
ANISOU  297  NH2 ARG A  73    13595  13086  13694   1199   -480    177       N  
ATOM    298  N   THR A  74       2.800  27.172  20.530  1.00 87.99           N  
ANISOU  298  N   THR A  74    11208  10874  11351    807   -409    173       N  
ATOM    299  CA  THR A  74       2.600  25.793  20.117  1.00 86.99           C  
ANISOU  299  CA  THR A  74    11047  10797  11207    778   -378    158       C  
ATOM    300  C   THR A  74       1.923  25.014  21.246  1.00 89.27           C  
ANISOU  300  C   THR A  74    11331  11097  11490    783   -347    116       C  
ATOM    301  O   THR A  74       1.736  25.524  22.350  1.00 98.79           O  
ANISOU  301  O   THR A  74    12558  12272  12708    807   -351    100       O  
ATOM    302  CB  THR A  74       3.934  25.157  19.741  1.00 81.24           C  
ANISOU  302  CB  THR A  74    10328  10062  10476    735   -371    176       C  
ATOM    303  OG1 THR A  74       4.650  24.835  20.936  1.00 80.35           O  
ANISOU  303  OG1 THR A  74    10243   9919  10369    730   -358    164       O  
ATOM    304  CG2 THR A  74       4.758  26.138  18.940  1.00 79.30           C  
ANISOU  304  CG2 THR A  74    10097   9795  10237    728   -408    214       C  
ATOM    305  N   VAL A  75       1.528  23.772  20.959  1.00 78.86           N  
ANISOU  305  N   VAL A  75     9988   9824  10151    757   -313     96       N  
ATOM    306  CA  VAL A  75       0.887  22.968  21.995  1.00 79.46           C  
ANISOU  306  CA  VAL A  75    10064   9912  10216    756   -282     55       C  
ATOM    307  C   VAL A  75       1.850  22.747  23.157  1.00 78.75           C  
ANISOU  307  C   VAL A  75    10009   9773  10139    750   -275     51       C  
ATOM    308  O   VAL A  75       1.482  22.896  24.328  1.00 82.38           O  
ANISOU  308  O   VAL A  75    10480  10216  10605    766   -272     27       O  
ATOM    309  CB  VAL A  75       0.386  21.628  21.425  1.00 73.08           C  
ANISOU  309  CB  VAL A  75     9234   9157   9378    719   -242     35       C  
ATOM    310  CG1 VAL A  75       0.123  20.650  22.567  1.00 72.94           C  
ANISOU  310  CG1 VAL A  75     9230   9136   9346    707   -206     -4       C  
ATOM    311  CG2 VAL A  75      -0.869  21.817  20.652  1.00 69.93           C  
ANISOU  311  CG2 VAL A  75     8793   8820   8957    726   -244     27       C  
ATOM    312  N   THR A  76       3.106  22.418  22.851  1.00 70.40           N  
ANISOU  312  N   THR A  76     8967   8697   9084    727   -272     77       N  
ATOM    313  CA  THR A  76       4.069  22.165  23.913  1.00 73.70           C  
ANISOU  313  CA  THR A  76     9412   9081   9508    722   -264     78       C  
ATOM    314  C   THR A  76       4.302  23.413  24.764  1.00 84.98           C  
ANISOU  314  C   THR A  76    10861  10470  10956    743   -295     84       C  
ATOM    315  O   THR A  76       4.475  23.309  25.985  1.00 92.85           O  
ANISOU  315  O   THR A  76    11874  11448  11956    745   -286     68       O  
ATOM    316  CB  THR A  76       5.378  21.621  23.324  1.00 62.29           C  
ANISOU  316  CB  THR A  76     7975   7635   8058    698   -257    108       C  
ATOM    317  OG1 THR A  76       5.185  20.253  22.937  1.00 64.71           O  
ANISOU  317  OG1 THR A  76     8273   7967   8345    678   -216     94       O  
ATOM    318  CG2 THR A  76       6.519  21.660  24.350  1.00 50.54           C  
ANISOU  318  CG2 THR A  76     6510   6119   6573    697   -258    120       C  
ATOM    319  N   ASN A  77       4.273  24.603  24.154  1.00 80.63           N  
ANISOU  319  N   ASN A  77    10314   9906  10415    756   -328    104       N  
ATOM    320  CA  ASN A  77       4.542  25.821  24.913  1.00 75.37           C  
ANISOU  320  CA  ASN A  77     9678   9197   9764    772   -353    110       C  
ATOM    321  C   ASN A  77       3.331  26.332  25.678  1.00 85.35           C  
ANISOU  321  C   ASN A  77    10942  10453  11036    806   -353     79       C  
ATOM    322  O   ASN A  77       3.506  27.058  26.665  1.00 89.15           O  
ANISOU  322  O   ASN A  77    11450  10897  11527    814   -360     72       O  
ATOM    323  CB  ASN A  77       5.047  26.928  23.996  1.00 72.53           C  
ANISOU  323  CB  ASN A  77     9333   8817   9407    772   -386    145       C  
ATOM    324  CG  ASN A  77       6.418  26.652  23.486  1.00 81.37           C  
ANISOU  324  CG  ASN A  77    10459   9941  10518    736   -391    174       C  
ATOM    325  OD1 ASN A  77       7.254  26.102  24.196  1.00 87.90           O  
ANISOU  325  OD1 ASN A  77    11293  10767  11338    717   -376    173       O  
ATOM    326  ND2 ASN A  77       6.662  27.001  22.242  1.00 88.74           N  
ANISOU  326  ND2 ASN A  77    11386  10883  11448    727   -411    201       N  
ATOM    327  N   ILE A  78       2.116  26.005  25.237  1.00 84.11           N  
ANISOU  327  N   ILE A  78    10753  10334  10871    825   -344     60       N  
ATOM    328  CA  ILE A  78       0.939  26.339  26.031  1.00 73.72           C  
ANISOU  328  CA  ILE A  78     9431   9022   9557    858   -341     28       C  
ATOM    329  C   ILE A  78       1.029  25.655  27.389  1.00 72.02           C  
ANISOU  329  C   ILE A  78     9224   8799   9342    842   -318     -4       C  
ATOM    330  O   ILE A  78       0.688  26.237  28.429  1.00 67.34           O  
ANISOU  330  O   ILE A  78     8646   8182   8759    861   -321    -25       O  
ATOM    331  CB  ILE A  78      -0.340  25.958  25.263  1.00 69.06           C  
ANISOU  331  CB  ILE A  78     8799   8494   8949    874   -333     14       C  
ATOM    332  CG1 ILE A  78      -0.458  26.810  24.004  1.00 71.68           C  
ANISOU  332  CG1 ILE A  78     9121   8831   9281    895   -359     49       C  
ATOM    333  CG2 ILE A  78      -1.568  26.188  26.080  1.00 56.16           C  
ANISOU  333  CG2 ILE A  78     7152   6877   7311    907   -328    -23       C  
ATOM    334  CD1 ILE A  78      -1.836  26.754  23.360  1.00 75.80           C  
ANISOU  334  CD1 ILE A  78     9599   9419   9784    921   -356     38       C  
ATOM    335  N   PHE A  79       1.538  24.426  27.407  1.00 69.01           N  
ANISOU  335  N   PHE A  79     8838   8435   8948    808   -293     -7       N  
ATOM    336  CA  PHE A  79       1.809  23.765  28.675  1.00 66.83           C  
ANISOU  336  CA  PHE A  79     8574   8148   8670    793   -272    -29       C  
ATOM    337  C   PHE A  79       2.925  24.469  29.444  1.00 66.32           C  
ANISOU  337  C   PHE A  79     8540   8039   8621    786   -286    -10       C  
ATOM    338  O   PHE A  79       2.741  24.843  30.605  1.00 71.95           O  
ANISOU  338  O   PHE A  79     9265   8732   9341    791   -286    -31       O  
ATOM    339  CB  PHE A  79       2.143  22.305  28.422  1.00 63.18           C  
ANISOU  339  CB  PHE A  79     8106   7710   8188    763   -240    -31       C  
ATOM    340  CG  PHE A  79       0.950  21.488  28.102  1.00 69.47           C  
ANISOU  340  CG  PHE A  79     8880   8553   8964    758   -216    -63       C  
ATOM    341  CD1 PHE A  79      -0.071  21.363  29.028  1.00 70.48           C  
ANISOU  341  CD1 PHE A  79     9000   8694   9083    765   -207   -104       C  
ATOM    342  CD2 PHE A  79       0.828  20.853  26.879  1.00 75.18           C  
ANISOU  342  CD2 PHE A  79     9588   9309   9669    741   -202    -53       C  
ATOM    343  CE1 PHE A  79      -1.194  20.617  28.745  1.00 73.67           C  
ANISOU  343  CE1 PHE A  79     9383   9149   9458    754   -184   -136       C  
ATOM    344  CE2 PHE A  79      -0.288  20.107  26.591  1.00 79.81           C  
ANISOU  344  CE2 PHE A  79    10153   9943  10226    728   -177    -84       C  
ATOM    345  CZ  PHE A  79      -1.304  19.985  27.530  1.00 77.72           C  
ANISOU  345  CZ  PHE A  79     9882   9697   9951    733   -168   -126       C  
ATOM    346  N   LEU A  80       4.089  24.676  28.817  1.00 63.28           N  
ANISOU  346  N   LEU A  80     8166   7642   8235    770   -298     28       N  
ATOM    347  CA  LEU A  80       5.155  25.430  29.475  1.00 57.48           C  
ANISOU  347  CA  LEU A  80     7460   6876   7506    757   -312     46       C  
ATOM    348  C   LEU A  80       4.681  26.807  29.915  1.00 55.54           C  
ANISOU  348  C   LEU A  80     7235   6593   7274    777   -332     37       C  
ATOM    349  O   LEU A  80       5.373  27.476  30.689  1.00 68.31           O  
ANISOU  349  O   LEU A  80     8879   8182   8893    761   -338     43       O  
ATOM    350  CB  LEU A  80       6.386  25.596  28.565  1.00 49.75           C  
ANISOU  350  CB  LEU A  80     6487   5897   6518    736   -326     88       C  
ATOM    351  CG  LEU A  80       7.216  24.403  28.074  1.00 58.50           C  
ANISOU  351  CG  LEU A  80     7581   7035   7611    717   -307    106       C  
ATOM    352  CD1 LEU A  80       8.426  24.874  27.256  1.00 56.31           C  
ANISOU  352  CD1 LEU A  80     7312   6760   7325    698   -328    146       C  
ATOM    353  CD2 LEU A  80       7.644  23.452  29.176  1.00 52.03           C  
ANISOU  353  CD2 LEU A  80     6762   6224   6783    708   -279     97       C  
ATOM    354  N   LEU A  81       3.527  27.251  29.430  1.00 56.97           N  
ANISOU  354  N   LEU A  81     7406   6777   7462    810   -341     24       N  
ATOM    355  CA  LEU A  81       2.954  28.509  29.886  1.00 65.10           C  
ANISOU  355  CA  LEU A  81     8460   7772   8505    839   -354     14       C  
ATOM    356  C   LEU A  81       2.121  28.309  31.151  1.00 65.37           C  
ANISOU  356  C   LEU A  81     8488   7808   8544    851   -338    -29       C  
ATOM    357  O   LEU A  81       2.083  29.188  32.014  1.00 69.16           O  
ANISOU  357  O   LEU A  81     8995   8250   9033    858   -342    -41       O  
ATOM    358  CB  LEU A  81       2.107  29.126  28.772  1.00 65.46           C  
ANISOU  358  CB  LEU A  81     8496   7824   8552    878   -371     25       C  
ATOM    359  CG  LEU A  81       1.332  30.371  29.188  1.00 78.57           C  
ANISOU  359  CG  LEU A  81    10180   9448  10224    922   -381     13       C  
ATOM    360  CD1 LEU A  81       2.015  31.584  28.615  1.00 86.67           C  
ANISOU  360  CD1 LEU A  81    11252  10426  11254    924   -402     49       C  
ATOM    361  CD2 LEU A  81      -0.120  30.280  28.733  1.00 81.75           C  
ANISOU  361  CD2 LEU A  81    10546   9893  10623    970   -379     -3       C  
ATOM    362  N   SER A  82       1.518  27.120  31.258  1.00 56.69           N  
ANISOU  362  N   SER A  82     7354   6751   7433    847   -318    -53       N  
ATOM    363  CA  SER A  82       0.754  26.724  32.469  1.00 61.33           C  
ANISOU  363  CA  SER A  82     7932   7350   8021    849   -302    -97       C  
ATOM    364  C   SER A  82       1.778  26.391  33.559  1.00 67.53           C  
ANISOU  364  C   SER A  82     8735   8115   8806    812   -290    -96       C  
ATOM    365  O   SER A  82       1.495  26.650  34.745  1.00 74.24           O  
ANISOU  365  O   SER A  82     9592   8951   9662    810   -285   -124       O  
ATOM    366  CB  SER A  82      -0.148  25.552  32.181  1.00 58.93           C  
ANISOU  366  CB  SER A  82     7593   7100   7698    848   -282   -122       C  
ATOM    367  OG  SER A  82      -0.530  24.902  33.385  1.00 63.45           O  
ANISOU  367  OG  SER A  82     8160   7682   8264    833   -263   -160       O  
ATOM    368  N   LEU A  83       2.925  25.836  33.146  1.00 60.76           N  
ANISOU  368  N   LEU A  83     7882   7263   7942    785   -287    -64       N  
ATOM    369  CA  LEU A  83       4.017  25.521  34.053  1.00 62.08           C  
ANISOU  369  CA  LEU A  83     8061   7423   8104    752   -277    -54       C  
ATOM    370  C   LEU A  83       4.629  26.790  34.629  1.00 72.14           C  
ANISOU  370  C   LEU A  83     9366   8660   9385    741   -292    -44       C  
ATOM    371  O   LEU A  83       4.915  26.863  35.835  1.00 78.15           O  
ANISOU  371  O   LEU A  83    10134   9413  10145    721   -284    -56       O  
ATOM    372  CB  LEU A  83       5.074  24.703  33.321  1.00 50.96           C  
ANISOU  372  CB  LEU A  83     6647   6034   6681    734   -270    -19       C  
ATOM    373  CG  LEU A  83       6.102  24.011  34.195  1.00 54.53           C  
ANISOU  373  CG  LEU A  83     7103   6496   7121    708   -253     -7       C  
ATOM    374  CD1 LEU A  83       5.410  22.847  34.898  1.00 57.12           C  
ANISOU  374  CD1 LEU A  83     7419   6842   7444    710   -225    -38       C  
ATOM    375  CD2 LEU A  83       7.294  23.544  33.349  1.00 61.65           C  
ANISOU  375  CD2 LEU A  83     8002   7416   8008    697   -252     36       C  
ATOM    376  N   ALA A  84       4.817  27.810  33.787  1.00 66.70           N  
ANISOU  376  N   ALA A  84     8696   7946   8700    751   -314    -21       N  
ATOM    377  CA  ALA A  84       5.391  29.065  34.259  1.00 69.21           C  
ANISOU  377  CA  ALA A  84     9052   8225   9020    736   -325    -12       C  
ATOM    378  C   ALA A  84       4.412  29.854  35.114  1.00 69.43           C  
ANISOU  378  C   ALA A  84     9096   8222   9062    758   -322    -48       C  
ATOM    379  O   ALA A  84       4.836  30.712  35.896  1.00 70.75           O  
ANISOU  379  O   ALA A  84     9298   8357   9229    736   -321    -50       O  
ATOM    380  CB  ALA A  84       5.847  29.914  33.076  1.00 74.64           C  
ANISOU  380  CB  ALA A  84     9763   8893   9704    738   -347     22       C  
ATOM    381  N   VAL A  85       3.112  29.586  34.989  1.00 68.71           N  
ANISOU  381  N   VAL A  85     8982   8144   8981    798   -319    -76       N  
ATOM    382  CA  VAL A  85       2.164  30.258  35.863  1.00 69.68           C  
ANISOU  382  CA  VAL A  85     9115   8244   9116    822   -315   -112       C  
ATOM    383  C   VAL A  85       2.193  29.633  37.255  1.00 68.51           C  
ANISOU  383  C   VAL A  85     8956   8110   8967    792   -296   -142       C  
ATOM    384  O   VAL A  85       2.171  30.348  38.261  1.00 73.86           O  
ANISOU  384  O   VAL A  85     9656   8757   9650    782   -291   -162       O  
ATOM    385  CB  VAL A  85       0.758  30.254  35.236  1.00 63.68           C  
ANISOU  385  CB  VAL A  85     8331   7505   8361    877   -319   -130       C  
ATOM    386  CG1 VAL A  85      -0.282  30.729  36.247  1.00 58.07           C  
ANISOU  386  CG1 VAL A  85     7621   6784   7659    904   -311   -173       C  
ATOM    387  CG2 VAL A  85       0.746  31.190  34.053  1.00 58.44           C  
ANISOU  387  CG2 VAL A  85     7687   6818   7700    909   -338    -98       C  
ATOM    388  N   SER A  86       2.310  28.312  37.315  1.00 62.01           N  
ANISOU  388  N   SER A  86     8100   7328   8133    775   -285   -145       N  
ATOM    389  CA  SER A  86       2.407  27.653  38.638  1.00 64.07           C  
ANISOU  389  CA  SER A  86     8351   7602   8389    744   -267   -170       C  
ATOM    390  C   SER A  86       3.718  28.077  39.300  1.00 71.40           C  
ANISOU  390  C   SER A  86     9303   8514   9312    701   -266   -147       C  
ATOM    391  O   SER A  86       3.719  28.258  40.508  1.00 76.50           O  
ANISOU  391  O   SER A  86     9954   9153   9960    678   -256   -169       O  
ATOM    392  CB  SER A  86       2.328  26.179  38.508  1.00 64.31           C  
ANISOU  392  CB  SER A  86     8353   7675   8407    736   -252   -174       C  
ATOM    393  OG  SER A  86       3.412  25.724  37.732  1.00 81.20           O  
ANISOU  393  OG  SER A  86    10494   9824  10536    722   -253   -131       O  
ATOM    394  N   ASN A  87       4.799  28.195  38.532  1.00 73.75           N  
ANISOU  394  N   ASN A  87     9611   8812   9599    686   -274   -104       N  
ATOM    395  CA  ASN A  87       6.058  28.655  39.105  1.00 64.29           C  
ANISOU  395  CA  ASN A  87     8433   7608   8386    641   -273    -80       C  
ATOM    396  C   ASN A  87       5.920  30.065  39.663  1.00 66.80           C  
ANISOU  396  C   ASN A  87     8790   7881   8711    631   -276    -95       C  
ATOM    397  O   ASN A  87       6.543  30.398  40.671  1.00 85.15           O  
ANISOU  397  O   ASN A  87    11126  10202  11023    588   -266    -98       O  
ATOM    398  CB  ASN A  87       7.181  28.605  38.067  1.00 64.90           C  
ANISOU  398  CB  ASN A  87     8514   7699   8447    628   -283    -34       C  
ATOM    399  CG  ASN A  87       7.564  27.194  37.675  1.00 66.37           C  
ANISOU  399  CG  ASN A  87     8666   7929   8621    632   -274    -16       C  
ATOM    400  OD1 ASN A  87       6.863  26.241  37.993  1.00 62.49           O  
ANISOU  400  OD1 ASN A  87     8154   7453   8136    647   -259    -39       O  
ATOM    401  ND2 ASN A  87       8.673  27.061  36.937  1.00 77.22           N  
ANISOU  401  ND2 ASN A  87    10039   9322   9977    617   -280     24       N  
ATOM    402  N   LEU A  88       5.118  30.911  39.020  1.00 58.62           N  
ANISOU  402  N   LEU A  88     7775   6807   7689    670   -287   -104       N  
ATOM    403  CA  LEU A  88       4.898  32.257  39.539  1.00 70.66           C  
ANISOU  403  CA  LEU A  88     9346   8280   9221    668   -285   -120       C  
ATOM    404  C   LEU A  88       4.006  32.222  40.770  1.00 81.35           C  
ANISOU  404  C   LEU A  88    10691   9631  10588    673   -270   -167       C  
ATOM    405  O   LEU A  88       4.202  32.999  41.712  1.00 86.94           O  
ANISOU  405  O   LEU A  88    11429  10309  11294    644   -258   -182       O  
ATOM    406  CB  LEU A  88       4.261  33.141  38.466  1.00 73.70           C  
ANISOU  406  CB  LEU A  88     9758   8627   9617    718   -299   -112       C  
ATOM    407  CG  LEU A  88       4.881  34.459  37.991  1.00 75.40           C  
ANISOU  407  CG  LEU A  88    10035   8790   9823    705   -306    -87       C  
ATOM    408  CD1 LEU A  88       3.770  35.349  37.423  1.00 73.09           C  
ANISOU  408  CD1 LEU A  88     9770   8454   9548    771   -312    -95       C  
ATOM    409  CD2 LEU A  88       5.704  35.198  39.056  1.00 70.22           C  
ANISOU  409  CD2 LEU A  88     9422   8108   9150    644   -291    -92       C  
ATOM    410  N   MET A  89       3.006  31.340  40.763  1.00 82.47           N  
ANISOU  410  N   MET A  89    10792   9804  10740    708   -268   -192       N  
ATOM    411  CA  MET A  89       2.111  31.208  41.905  1.00 80.94           C  
ANISOU  411  CA  MET A  89    10583   9614  10555    712   -256   -239       C  
ATOM    412  C   MET A  89       2.889  30.746  43.140  1.00 79.80           C  
ANISOU  412  C   MET A  89    10432   9489  10401    651   -242   -244       C  
ATOM    413  O   MET A  89       2.859  31.390  44.197  1.00 85.73           O  
ANISOU  413  O   MET A  89    11201  10217  11155    626   -231   -268       O  
ATOM    414  CB  MET A  89       0.969  30.246  41.531  1.00 81.31           C  
ANISOU  414  CB  MET A  89    10586   9702  10606    751   -258   -262       C  
ATOM    415  CG  MET A  89       0.229  29.588  42.695  1.00 89.92           C  
ANISOU  415  CG  MET A  89    11649  10819  11697    740   -245   -309       C  
ATOM    416  SD  MET A  89      -1.064  28.423  42.189  1.00 90.77           S  
ANISOU  416  SD  MET A  89    11709  10983  11796    775   -245   -337       S  
ATOM    417  CE  MET A  89      -2.300  29.582  41.591  1.00 96.90           C  
ANISOU  417  CE  MET A  89    12492  11743  12583    844   -256   -353       C  
ATOM    418  N   LEU A  90       3.622  29.643  43.009  1.00 64.81           N  
ANISOU  418  N   LEU A  90     8506   7631   8488    628   -240   -220       N  
ATOM    419  CA  LEU A  90       4.508  29.190  44.070  1.00 64.46           C  
ANISOU  419  CA  LEU A  90     8452   7612   8429    574   -227   -213       C  
ATOM    420  C   LEU A  90       5.473  30.285  44.509  1.00 72.63           C  
ANISOU  420  C   LEU A  90     9522   8623   9451    528   -224   -197       C  
ATOM    421  O   LEU A  90       5.807  30.389  45.699  1.00 73.68           O  
ANISOU  421  O   LEU A  90     9653   8765   9575    483   -210   -210       O  
ATOM    422  CB  LEU A  90       5.279  27.963  43.592  1.00 56.65           C  
ANISOU  422  CB  LEU A  90     7437   6666   7423    568   -225   -178       C  
ATOM    423  CG  LEU A  90       6.317  27.305  44.498  1.00 59.66           C  
ANISOU  423  CG  LEU A  90     7801   7084   7782    522   -211   -159       C  
ATOM    424  CD1 LEU A  90       5.638  26.614  45.655  1.00 56.15           C  
ANISOU  424  CD1 LEU A  90     7336   6656   7342    513   -198   -196       C  
ATOM    425  CD2 LEU A  90       7.163  26.325  43.675  1.00 62.16           C  
ANISOU  425  CD2 LEU A  90     8102   7435   8081    531   -211   -115       C  
ATOM    426  N   CYS A  91       5.922  31.096  43.568  1.00 66.61           N  
ANISOU  426  N   CYS A  91     8791   7833   8683    534   -235   -170       N  
ATOM    427  CA  CYS A  91       6.976  32.071  43.916  1.00 74.96           C  
ANISOU  427  CA  CYS A  91     9886   8875   9719    479   -230   -151       C  
ATOM    428  C   CYS A  91       6.431  33.276  44.682  1.00 82.66           C  
ANISOU  428  C   CYS A  91    10904   9798  10704    469   -217   -186       C  
ATOM    429  O   CYS A  91       7.161  33.793  45.515  1.00 92.18           O  
ANISOU  429  O   CYS A  91    12130  11004  11889    408   -203   -186       O  
ATOM    430  CB  CYS A  91       7.700  32.515  42.658  1.00 96.41           C  
ANISOU  430  CB  CYS A  91    12628  11582  12422    482   -245   -111       C  
ATOM    431  SG  CYS A  91       8.713  33.984  42.931  1.00118.36           S  
ANISOU  431  SG  CYS A  91    15471  14330  15172    416   -238    -97       S  
ATOM    432  N   LEU A  92       5.194  33.686  44.422  1.00 82.81           N  
ANISOU  432  N   LEU A  92    10935   9777  10750    526   -221   -216       N  
ATOM    433  CA  LEU A  92       4.617  34.869  45.060  1.00 81.98           C  
ANISOU  433  CA  LEU A  92    10877   9617  10656    527   -207   -249       C  
ATOM    434  C   LEU A  92       3.661  34.545  46.195  1.00 86.32           C  
ANISOU  434  C   LEU A  92    11400  10176  11223    534   -195   -298       C  
ATOM    435  O   LEU A  92       3.492  35.368  47.098  1.00 90.05           O  
ANISOU  435  O   LEU A  92    11904  10614  11697    510   -176   -326       O  
ATOM    436  CB  LEU A  92       3.869  35.729  44.034  1.00 76.07           C  
ANISOU  436  CB  LEU A  92    10166   8815   9922    593   -217   -246       C  
ATOM    437  CG  LEU A  92       4.672  36.227  42.828  1.00 72.28           C  
ANISOU  437  CG  LEU A  92     9721   8315   9427    591   -230   -201       C  
ATOM    438  CD1 LEU A  92       3.735  36.434  41.667  1.00 67.28           C  
ANISOU  438  CD1 LEU A  92     9090   7660   8812    671   -246   -195       C  
ATOM    439  CD2 LEU A  92       5.407  37.515  43.140  1.00 67.05           C  
ANISOU  439  CD2 LEU A  92     9132   7600   8743    540   -215   -194       C  
ATOM    440  N   PHE A  93       3.030  33.378  46.181  1.00 87.88           N  
ANISOU  440  N   PHE A  93    11542  10418  11430    562   -202   -311       N  
ATOM    441  CA  PHE A  93       2.048  33.049  47.199  1.00 85.88           C  
ANISOU  441  CA  PHE A  93    11262  10178  11189    569   -193   -360       C  
ATOM    442  C   PHE A  93       2.563  32.059  48.230  1.00 81.11           C  
ANISOU  442  C   PHE A  93    10620   9624  10573    513   -184   -365       C  
ATOM    443  O   PHE A  93       1.780  31.621  49.071  1.00 90.17           O  
ANISOU  443  O   PHE A  93    11741  10790  11729    512   -178   -405       O  
ATOM    444  CB  PHE A  93       0.771  32.500  46.548  1.00 93.80           C  
ANISOU  444  CB  PHE A  93    12234  11200  12207    639   -205   -380       C  
ATOM    445  CG  PHE A  93       0.068  33.490  45.643  1.00102.33           C  
ANISOU  445  CG  PHE A  93    13345  12237  13299    704   -213   -379       C  
ATOM    446  CD1 PHE A  93       0.404  34.839  45.650  1.00108.38           C  
ANISOU  446  CD1 PHE A  93    14172  12941  14067    700   -204   -371       C  
ATOM    447  CD2 PHE A  93      -0.940  33.069  44.794  1.00 98.93           C  
ANISOU  447  CD2 PHE A  93    12884  11832  12873    767   -225   -385       C  
ATOM    448  CE1 PHE A  93      -0.245  35.744  44.823  1.00106.25           C  
ANISOU  448  CE1 PHE A  93    13935  12629  13806    766   -210   -366       C  
ATOM    449  CE2 PHE A  93      -1.588  33.967  43.968  1.00103.76           C  
ANISOU  449  CE2 PHE A  93    13520  12411  13492    831   -232   -380       C  
ATOM    450  CZ  PHE A  93      -1.241  35.309  43.987  1.00105.28           C  
ANISOU  450  CZ  PHE A  93    13776  12536  13689    834   -224   -369       C  
ATOM    451  N   CYS A  94       3.840  31.676  48.187  1.00 75.61           N  
ANISOU  451  N   CYS A  94     9919   8955   9855    467   -184   -324       N  
ATOM    452  CA  CYS A  94       4.350  30.724  49.171  1.00 73.74           C  
ANISOU  452  CA  CYS A  94     9646   8769   9604    419   -174   -322       C  
ATOM    453  C   CYS A  94       5.729  31.092  49.696  1.00 86.47           C  
ANISOU  453  C   CYS A  94    11269  10398  11188    350   -164   -291       C  
ATOM    454  O   CYS A  94       5.990  30.957  50.893  1.00101.29           O  
ANISOU  454  O   CYS A  94    13131  12300  13055    299   -149   -304       O  
ATOM    455  CB  CYS A  94       4.422  29.307  48.601  1.00 74.01           C  
ANISOU  455  CB  CYS A  94     9642   8848   9633    444   -182   -301       C  
ATOM    456  SG  CYS A  94       2.901  28.699  47.879  1.00 85.37           S  
ANISOU  456  SG  CYS A  94    11062  10285  11092    513   -192   -334       S  
ATOM    457  N   MET A  95       6.624  31.533  48.821  1.00 84.68           N  
ANISOU  457  N   MET A  95    11066  10164  10944    344   -170   -250       N  
ATOM    458  CA  MET A  95       8.014  31.712  49.237  1.00 86.70           C  
ANISOU  458  CA  MET A  95    11324  10456  11162    276   -161   -216       C  
ATOM    459  C   MET A  95       8.199  32.773  50.317  1.00 92.48           C  
ANISOU  459  C   MET A  95    12087  11168  11882    212   -141   -239       C  
ATOM    460  O   MET A  95       8.936  32.506  51.282  1.00102.32           O  
ANISOU  460  O   MET A  95    13310  12466  13103    151   -127   -230       O  
ATOM    461  CB  MET A  95       8.898  32.004  48.020  1.00 84.66           C  
ANISOU  461  CB  MET A  95    11086  10197  10884    280   -174   -170       C  
ATOM    462  CG  MET A  95      10.379  32.090  48.377  1.00 87.29           C  
ANISOU  462  CG  MET A  95    11414  10584  11170    210   -165   -131       C  
ATOM    463  SD  MET A  95      11.554  31.807  47.036  1.00 91.48           S  
ANISOU  463  SD  MET A  95    11938  11151  11670    217   -182    -72       S  
ATOM    464  CE  MET A  95      10.811  32.811  45.768  1.00 96.71           C  
ANISOU  464  CE  MET A  95    12656  11729  12358    264   -198    -83       C  
ATOM    465  N   PRO A  96       7.591  33.964  50.247  1.00 86.88           N  
ANISOU  465  N   PRO A  96    11430  10391  11188    221   -135   -268       N  
ATOM    466  CA  PRO A  96       7.810  34.918  51.348  1.00 83.14           C  
ANISOU  466  CA  PRO A  96    10990   9900  10700    152   -109   -292       C  
ATOM    467  C   PRO A  96       7.292  34.373  52.667  1.00 80.06           C  
ANISOU  467  C   PRO A  96    10560   9538  10321    130    -97   -329       C  
ATOM    468  O   PRO A  96       8.001  34.381  53.679  1.00 88.18           O  
ANISOU  468  O   PRO A  96    11574  10607  11322     55    -80   -326       O  
ATOM    469  CB  PRO A  96       7.051  36.174  50.890  1.00 81.49           C  
ANISOU  469  CB  PRO A  96    10848   9603  10511    188   -104   -318       C  
ATOM    470  CG  PRO A  96       6.730  35.952  49.442  1.00 77.08           C  
ANISOU  470  CG  PRO A  96    10291   9028   9969    264   -130   -294       C  
ATOM    471  CD  PRO A  96       6.577  34.470  49.311  1.00 78.99           C  
ANISOU  471  CD  PRO A  96    10462   9331  10220    294   -146   -284       C  
ATOM    472  N   PHE A  97       6.080  33.837  52.658  1.00 75.41           N  
ANISOU  472  N   PHE A  97     9947   8936   9768    191   -107   -362       N  
ATOM    473  CA  PHE A  97       5.472  33.229  53.827  1.00 74.87           C  
ANISOU  473  CA  PHE A  97     9839   8896   9711    175    -99   -400       C  
ATOM    474  C   PHE A  97       6.123  31.889  54.166  1.00 85.92           C  
ANISOU  474  C   PHE A  97    11182  10372  11092    153   -104   -370       C  
ATOM    475  O   PHE A  97       5.529  31.062  54.869  1.00 85.65           O  
ANISOU  475  O   PHE A  97    11110  10364  11069    156   -104   -396       O  
ATOM    476  CB  PHE A  97       3.963  33.084  53.597  1.00 76.55           C  
ANISOU  476  CB  PHE A  97    10047   9079   9961    248   -109   -443       C  
ATOM    477  CG  PHE A  97       3.330  34.302  52.962  1.00 81.70           C  
ANISOU  477  CG  PHE A  97    10754   9659  10630    294   -107   -460       C  
ATOM    478  CD1 PHE A  97       3.106  35.458  53.706  1.00 81.94           C  
ANISOU  478  CD1 PHE A  97    10829   9642  10663    266    -84   -493       C  
ATOM    479  CD2 PHE A  97       2.980  34.295  51.618  1.00 81.03           C  
ANISOU  479  CD2 PHE A  97    10679   9553  10556    365   -126   -440       C  
ATOM    480  CE1 PHE A  97       2.540  36.577  53.116  1.00 85.74           C  
ANISOU  480  CE1 PHE A  97    11367  10052  11158    314    -79   -504       C  
ATOM    481  CE2 PHE A  97       2.412  35.403  51.021  1.00 82.26           C  
ANISOU  481  CE2 PHE A  97    10885   9644  10724    413   -124   -450       C  
ATOM    482  CZ  PHE A  97       2.190  36.546  51.759  1.00 88.40           C  
ANISOU  482  CZ  PHE A  97    11712  10372  11506    391   -100   -481       C  
ATOM    483  N   ASN A  98       7.346  31.670  53.681  1.00 88.85           N  
ANISOU  483  N   ASN A  98    11548  10778  11433    131   -107   -317       N  
ATOM    484  CA  ASN A  98       8.206  30.606  54.190  1.00 91.94           C  
ANISOU  484  CA  ASN A  98    11892  11246  11797     99   -104   -283       C  
ATOM    485  C   ASN A  98       9.561  31.106  54.654  1.00 93.72           C  
ANISOU  485  C   ASN A  98    12119  11514  11976     22    -90   -249       C  
ATOM    486  O   ASN A  98      10.037  30.670  55.702  1.00106.08           O  
ANISOU  486  O   ASN A  98    13649  13137  13520    -29    -78   -242       O  
ATOM    487  CB  ASN A  98       8.415  29.506  53.146  1.00 99.10           C  
ANISOU  487  CB  ASN A  98    12775  12176  12703    156   -121   -245       C  
ATOM    488  CG  ASN A  98       7.645  28.253  53.475  1.00102.30           C  
ANISOU  488  CG  ASN A  98    13144  12599  13125    190   -123   -264       C  
ATOM    489  OD1 ASN A  98       6.581  28.316  54.086  1.00103.56           O  
ANISOU  489  OD1 ASN A  98    13302  12737  13308    194   -121   -314       O  
ATOM    490  ND2 ASN A  98       8.185  27.103  53.088  1.00101.98           N  
ANISOU  490  ND2 ASN A  98    13077  12600  13069    212   -126   -225       N  
ATOM    491  N   LEU A  99      10.201  32.013  53.913  1.00 89.79           N  
ANISOU  491  N   LEU A  99    11661  10995  11459      7    -91   -227       N  
ATOM    492  CA  LEU A  99      11.464  32.582  54.380  1.00 90.12           C  
ANISOU  492  CA  LEU A  99    11708  11084  11448    -78    -75   -199       C  
ATOM    493  C   LEU A  99      11.251  33.428  55.624  1.00 93.63           C  
ANISOU  493  C   LEU A  99    12172  11515  11887   -149    -49   -240       C  
ATOM    494  O   LEU A  99      11.944  33.256  56.632  1.00 91.42           O  
ANISOU  494  O   LEU A  99    11860  11302  11572   -220    -33   -229       O  
ATOM    495  CB  LEU A  99      12.118  33.436  53.291  1.00 93.63           C  
ANISOU  495  CB  LEU A  99    12200  11505  11870    -83    -81   -173       C  
ATOM    496  CG  LEU A  99      13.138  34.453  53.841  1.00 92.48           C  
ANISOU  496  CG  LEU A  99    12082  11385  11670   -184    -58   -164       C  
ATOM    497  CD1 LEU A  99      14.523  33.834  54.035  1.00 85.86           C  
ANISOU  497  CD1 LEU A  99    11193  10657  10773   -231    -56   -110       C  
ATOM    498  CD2 LEU A  99      13.213  35.732  52.997  1.00 95.84           C  
ANISOU  498  CD2 LEU A  99    12586  11742  12088   -193    -56   -167       C  
ATOM    499  N   ILE A 100      10.313  34.376  55.558  1.00 92.88           N  
ANISOU  499  N   ILE A 100    12130  11336  11824   -133    -43   -285       N  
ATOM    500  CA  ILE A 100      10.077  35.262  56.691  1.00 92.06           C  
ANISOU  500  CA  ILE A 100    12054  11209  11716   -200    -14   -327       C  
ATOM    501  C   ILE A 100       9.766  34.468  57.967  1.00 85.88           C  
ANISOU  501  C   ILE A 100    11214  10477  10941   -226     -8   -349       C  
ATOM    502  O   ILE A 100      10.451  34.675  58.972  1.00 91.13           O  
ANISOU  502  O   ILE A 100    11865  11192  11570   -314     14   -346       O  
ATOM    503  CB  ILE A 100       9.002  36.302  56.341  1.00 96.44           C  
ANISOU  503  CB  ILE A 100    12675  11660  12307   -157     -8   -372       C  
ATOM    504  CG1 ILE A 100       9.258  36.906  54.964  1.00 98.63           C  
ANISOU  504  CG1 ILE A 100    13004  11891  12580   -118    -20   -344       C  
ATOM    505  CG2 ILE A 100       8.993  37.426  57.355  1.00106.31           C  
ANISOU  505  CG2 ILE A 100    13971  12879  13542   -235     28   -409       C  
ATOM    506  CD1 ILE A 100       8.253  37.980  54.597  1.00100.37           C  
ANISOU  506  CD1 ILE A 100    13295  12010  12833    -71    -12   -382       C  
ATOM    507  N   PRO A 101       8.792  33.550  57.973  1.00 77.34           N  
ANISOU  507  N   PRO A 101    10096   9389   9898   -160    -25   -370       N  
ATOM    508  CA  PRO A 101       8.587  32.778  59.211  1.00 71.49           C  
ANISOU  508  CA  PRO A 101     9303   8701   9159   -194    -18   -388       C  
ATOM    509  C   PRO A 101       9.776  31.912  59.595  1.00 75.26           C  
ANISOU  509  C   PRO A 101     9728   9274   9594   -236    -17   -335       C  
ATOM    510  O   PRO A 101      10.051  31.759  60.788  1.00 82.37           O  
ANISOU  510  O   PRO A 101    10596  10225  10474   -302     -2   -341       O  
ATOM    511  CB  PRO A 101       7.341  31.944  58.882  1.00 72.46           C  
ANISOU  511  CB  PRO A 101     9406   8797   9326   -109    -39   -416       C  
ATOM    512  CG  PRO A 101       6.627  32.747  57.849  1.00 74.78           C  
ANISOU  512  CG  PRO A 101     9753   9013   9649    -47    -47   -434       C  
ATOM    513  CD  PRO A 101       7.727  33.272  56.997  1.00 74.40           C  
ANISOU  513  CD  PRO A 101     9734   8964   9570    -62    -47   -385       C  
ATOM    514  N   ASN A 102      10.483  31.326  58.625  1.00 76.21           N  
ANISOU  514  N   ASN A 102     9835   9423   9696   -198    -33   -282       N  
ATOM    515  CA  ASN A 102      11.620  30.477  58.966  1.00 81.23           C  
ANISOU  515  CA  ASN A 102    10420  10154  10288   -227    -30   -228       C  
ATOM    516  C   ASN A 102      12.809  31.317  59.403  1.00 88.22           C  
ANISOU  516  C   ASN A 102    11311  11092  11118   -319    -10   -204       C  
ATOM    517  O   ASN A 102      13.649  30.855  60.182  1.00 91.56           O  
ANISOU  517  O   ASN A 102    11686  11604  11499   -370      0   -172       O  
ATOM    518  CB  ASN A 102      11.990  29.585  57.777  1.00 89.16           C  
ANISOU  518  CB  ASN A 102    11411  11174  11291   -154    -50   -181       C  
ATOM    519  CG  ASN A 102      12.452  28.190  58.200  1.00 95.69           C  
ANISOU  519  CG  ASN A 102    12180  12077  12100   -138    -51   -143       C  
ATOM    520  OD1 ASN A 102      13.651  27.961  58.410  1.00102.22           O  
ANISOU  520  OD1 ASN A 102    12976  12983  12877   -172    -43    -92       O  
ATOM    521  ND2 ASN A 102      11.496  27.246  58.326  1.00 85.05           N  
ANISOU  521  ND2 ASN A 102    10820  10707  10788    -87    -58   -167       N  
ATOM    522  N   LEU A 103      12.885  32.555  58.920  1.00 94.18           N  
ANISOU  522  N   LEU A 103    12124  11793  11866   -344     -3   -217       N  
ATOM    523  CA  LEU A 103      13.938  33.464  59.352  1.00 97.26           C  
ANISOU  523  CA  LEU A 103    12530  12227  12197   -444     21   -202       C  
ATOM    524  C   LEU A 103      13.667  33.987  60.754  1.00 89.65           C  
ANISOU  524  C   LEU A 103    11566  11269  11228   -526     49   -244       C  
ATOM    525  O   LEU A 103      14.603  34.174  61.541  1.00 87.54           O  
ANISOU  525  O   LEU A 103    11275  11083  10904   -618     70   -225       O  
ATOM    526  CB  LEU A 103      14.055  34.631  58.368  1.00103.70           C  
ANISOU  526  CB  LEU A 103    13420  12974  13006   -446     22   -207       C  
ATOM    527  CG  LEU A 103      15.277  34.826  57.477  1.00 97.12           C  
ANISOU  527  CG  LEU A 103    12595  12188  12120   -465     16   -154       C  
ATOM    528  CD1 LEU A 103      15.276  36.267  57.003  1.00103.58           C  
ANISOU  528  CD1 LEU A 103    13500  12931  12926   -502     30   -175       C  
ATOM    529  CD2 LEU A 103      16.561  34.499  58.222  1.00 93.64           C  
ANISOU  529  CD2 LEU A 103    12098  11873  11607   -546     30   -112       C  
ATOM    530  N   LEU A 104      12.391  34.257  61.069  1.00 89.68           N  
ANISOU  530  N   LEU A 104    11596  11192  11286   -498     51   -303       N  
ATOM    531  CA  LEU A 104      11.984  34.723  62.393  1.00 95.95           C  
ANISOU  531  CA  LEU A 104    12390  11984  12082   -570     77   -350       C  
ATOM    532  C   LEU A 104      11.748  33.584  63.381  1.00 98.96           C  
ANISOU  532  C   LEU A 104    12698  12429  12473   -572     72   -352       C  
ATOM    533  O   LEU A 104      11.700  33.833  64.590  1.00 97.55           O  
ANISOU  533  O   LEU A 104    12504  12278  12282   -649     94   -379       O  
ATOM    534  CB  LEU A 104      10.696  35.545  62.303  1.00 95.14           C  
ANISOU  534  CB  LEU A 104    12348  11769  12032   -533     83   -414       C  
ATOM    535  CG  LEU A 104      10.555  36.749  61.377  1.00 95.86           C  
ANISOU  535  CG  LEU A 104    12524  11770  12127   -513     91   -425       C  
ATOM    536  CD1 LEU A 104       9.104  37.172  61.321  1.00 94.43           C  
ANISOU  536  CD1 LEU A 104    12381  11492  12006   -448     90   -484       C  
ATOM    537  CD2 LEU A 104      11.403  37.894  61.861  1.00102.91           C  
ANISOU  537  CD2 LEU A 104    13464  12670  12967   -624    129   -426       C  
ATOM    538  N   LYS A 105      11.582  32.351  62.892  1.00 98.75           N  
ANISOU  538  N   LYS A 105    12631  12424  12466   -493     44   -325       N  
ATOM    539  CA  LYS A 105      11.219  31.198  63.715  1.00 97.77           C  
ANISOU  539  CA  LYS A 105    12448  12346  12354   -483     37   -329       C  
ATOM    540  C   LYS A 105       9.852  31.395  64.365  1.00101.06           C  
ANISOU  540  C   LYS A 105    12877  12702  12819   -476     39   -401       C  
ATOM    541  O   LYS A 105       9.549  30.796  65.399  1.00108.95           O  
ANISOU  541  O   LYS A 105    13834  13739  13822   -504     42   -418       O  
ATOM    542  CB  LYS A 105      12.287  30.898  64.770  1.00 98.96           C  
ANISOU  542  CB  LYS A 105    12546  12606  12450   -568     54   -292       C  
ATOM    543  CG  LYS A 105      13.709  30.930  64.245  1.00109.12           C  
ANISOU  543  CG  LYS A 105    13819  13964  13676   -591     57   -225       C  
ATOM    544  CD  LYS A 105      14.710  30.784  65.374  1.00122.83           C  
ANISOU  544  CD  LYS A 105    15500  15816  15352   -683     78   -193       C  
ATOM    545  CE  LYS A 105      14.432  31.774  66.514  1.00127.31           C  
ANISOU  545  CE  LYS A 105    16084  16375  15914   -786    107   -244       C  
ATOM    546  NZ  LYS A 105      14.582  33.192  66.082  1.00128.27           N  
ANISOU  546  NZ  LYS A 105    16275  16440  16020   -833    125   -268       N  
ATOM    547  N   ASP A 106       9.011  32.227  63.756  1.00 97.32           N  
ANISOU  547  N   ASP A 106    12459  12137  12381   -436     38   -442       N  
ATOM    548  CA  ASP A 106       7.664  32.479  64.257  1.00 92.90           C  
ANISOU  548  CA  ASP A 106    11912  11520  11866   -419     39   -511       C  
ATOM    549  C   ASP A 106       6.775  32.795  63.068  1.00 88.96           C  
ANISOU  549  C   ASP A 106    11458  10938  11406   -324     23   -530       C  
ATOM    550  O   ASP A 106       6.976  33.815  62.406  1.00 85.57           O  
ANISOU  550  O   ASP A 106    11084  10458  10973   -320     32   -527       O  
ATOM    551  CB  ASP A 106       7.661  33.636  65.252  1.00 98.75           C  
ANISOU  551  CB  ASP A 106    12680  12243  12596   -508     72   -552       C  
ATOM    552  CG  ASP A 106       6.335  33.787  65.987  1.00104.80           C  
ANISOU  552  CG  ASP A 106    13448  12968  13404   -498     76   -624       C  
ATOM    553  OD1 ASP A 106       5.372  33.045  65.689  1.00101.60           O  
ANISOU  553  OD1 ASP A 106    13024  12547  13033   -423     52   -644       O  
ATOM    554  OD2 ASP A 106       6.264  34.658  66.883  1.00107.59           O  
ANISOU  554  OD2 ASP A 106    13822  13307  13750   -571    106   -661       O  
ATOM    555  N   PHE A 107       5.798  31.936  62.796  1.00 89.24           N  
ANISOU  555  N   PHE A 107    11470  10962  11473   -253      1   -550       N  
ATOM    556  CA  PHE A 107       4.817  32.241  61.760  1.00 93.44           C  
ANISOU  556  CA  PHE A 107    12036  11425  12040   -165    -14   -573       C  
ATOM    557  C   PHE A 107       3.911  33.347  62.288  1.00 93.30           C  
ANISOU  557  C   PHE A 107    12056  11349  12046   -174      4   -636       C  
ATOM    558  O   PHE A 107       3.006  33.104  63.088  1.00 93.99           O  
ANISOU  558  O   PHE A 107    12120  11440  12152   -177      4   -685       O  
ATOM    559  CB  PHE A 107       4.028  30.997  61.369  1.00 94.37           C  
ANISOU  559  CB  PHE A 107    12118  11559  12178    -96    -39   -579       C  
ATOM    560  CG  PHE A 107       3.200  31.181  60.128  1.00 88.91           C  
ANISOU  560  CG  PHE A 107    11454  10815  11512     -6    -55   -589       C  
ATOM    561  CD1 PHE A 107       3.762  31.001  58.881  1.00 91.06           C  
ANISOU  561  CD1 PHE A 107    11740  11082  11777     38    -68   -539       C  
ATOM    562  CD2 PHE A 107       1.869  31.564  60.215  1.00 88.29           C  
ANISOU  562  CD2 PHE A 107    11386  10698  11463     35    -57   -647       C  
ATOM    563  CE1 PHE A 107       3.003  31.193  57.722  1.00 94.44           C  
ANISOU  563  CE1 PHE A 107    12190  11466  12228    117    -82   -546       C  
ATOM    564  CE2 PHE A 107       1.101  31.747  59.073  1.00 95.05           C  
ANISOU  564  CE2 PHE A 107    12262  11514  12337    119    -72   -653       C  
ATOM    565  CZ  PHE A 107       1.665  31.563  57.820  1.00 94.99           C  
ANISOU  565  CZ  PHE A 107    12267  11501  12323    159    -84   -602       C  
ATOM    566  N   ILE A 108       4.167  34.578  61.840  1.00 86.88           N  
ANISOU  566  N   ILE A 108    11304  10478  11228   -179     20   -634       N  
ATOM    567  CA  ILE A 108       3.486  35.761  62.356  1.00 83.30           C  
ANISOU  567  CA  ILE A 108    10897   9962  10790   -192     45   -688       C  
ATOM    568  C   ILE A 108       2.324  36.206  61.481  1.00 83.86           C  
ANISOU  568  C   ILE A 108    11004   9964  10896    -91     34   -715       C  
ATOM    569  O   ILE A 108       1.603  37.146  61.858  1.00 81.50           O  
ANISOU  569  O   ILE A 108    10743   9609  10613    -84     55   -762       O  
ATOM    570  CB  ILE A 108       4.479  36.929  62.527  1.00 79.81           C  
ANISOU  570  CB  ILE A 108    10512   9496  10315   -269     78   -672       C  
ATOM    571  CG1 ILE A 108       5.016  37.373  61.167  1.00 71.90           C  
ANISOU  571  CG1 ILE A 108     9558   8457   9302   -227     69   -627       C  
ATOM    572  CG2 ILE A 108       5.636  36.506  63.397  1.00 80.86           C  
ANISOU  572  CG2 ILE A 108    10604   9712  10406   -372     89   -643       C  
ATOM    573  CD1 ILE A 108       5.714  38.707  61.227  1.00 77.69           C  
ANISOU  573  CD1 ILE A 108    10366   9146  10005   -293    104   -624       C  
ATOM    574  N   PHE A 109       2.136  35.590  60.318  1.00 79.62           N  
ANISOU  574  N   PHE A 109    10453   9430  10369    -13      5   -686       N  
ATOM    575  CA  PHE A 109       0.979  35.899  59.501  1.00 84.68           C  
ANISOU  575  CA  PHE A 109    11115  10021  11039     85     -6   -709       C  
ATOM    576  C   PHE A 109      -0.231  35.156  60.058  1.00 90.15           C  
ANISOU  576  C   PHE A 109    11757  10745  11752    116    -19   -759       C  
ATOM    577  O   PHE A 109      -0.140  34.396  61.030  1.00 98.25           O  
ANISOU  577  O   PHE A 109    12736  11823  12770     61    -19   -773       O  
ATOM    578  CB  PHE A 109       1.259  35.549  58.037  1.00 87.37           C  
ANISOU  578  CB  PHE A 109    11461  10360  11378    148    -31   -659       C  
ATOM    579  CG  PHE A 109       2.562  36.115  57.509  1.00 79.38           C  
ANISOU  579  CG  PHE A 109    10490   9332  10339    108    -23   -608       C  
ATOM    580  CD1 PHE A 109       2.662  37.453  57.144  1.00 72.68           C  
ANISOU  580  CD1 PHE A 109     9716   8412   9488    112     -4   -609       C  
ATOM    581  CD2 PHE A 109       3.686  35.304  57.386  1.00 70.28           C  
ANISOU  581  CD2 PHE A 109     9303   8240   9159     67    -32   -559       C  
ATOM    582  CE1 PHE A 109       3.852  37.968  56.669  1.00 70.91           C  
ANISOU  582  CE1 PHE A 109     9532   8178   9233     68      4   -565       C  
ATOM    583  CE2 PHE A 109       4.885  35.821  56.917  1.00 69.18           C  
ANISOU  583  CE2 PHE A 109     9197   8098   8989     27    -26   -514       C  
ATOM    584  CZ  PHE A 109       4.963  37.150  56.555  1.00 69.93           C  
ANISOU  584  CZ  PHE A 109     9366   8123   9080     23     -8   -518       C  
ATOM    585  N   GLY A 110      -1.381  35.374  59.443  1.00 88.23           N  
ANISOU  585  N   GLY A 110    11521  10471  11530    202    -29   -785       N  
ATOM    586  CA  GLY A 110      -2.611  34.845  59.996  1.00 90.05           C  
ANISOU  586  CA  GLY A 110    11709  10733  11774    229    -37   -839       C  
ATOM    587  C   GLY A 110      -2.719  33.334  59.908  1.00 83.75           C  
ANISOU  587  C   GLY A 110    10849  10004  10968    230    -62   -829       C  
ATOM    588  O   GLY A 110      -1.911  32.643  59.293  1.00 84.85           O  
ANISOU  588  O   GLY A 110    10979  10167  11095    225    -74   -778       O  
ATOM    589  N   SER A 111      -3.756  32.806  60.556  1.00 84.83           N  
ANISOU  589  N   SER A 111    10946  10176  11110    236    -69   -881       N  
ATOM    590  CA  SER A 111      -4.110  31.412  60.323  1.00 84.31           C  
ANISOU  590  CA  SER A 111    10832  10169  11033    249    -91   -879       C  
ATOM    591  C   SER A 111      -4.543  31.192  58.879  1.00 83.00           C  
ANISOU  591  C   SER A 111    10669   9999  10867    333   -109   -856       C  
ATOM    592  O   SER A 111      -4.364  30.096  58.337  1.00 79.36           O  
ANISOU  592  O   SER A 111    10185   9575  10394    340   -123   -830       O  
ATOM    593  CB  SER A 111      -5.217  30.977  61.290  1.00 76.52           C  
ANISOU  593  CB  SER A 111     9806   9222  10047    235    -94   -945       C  
ATOM    594  OG  SER A 111      -5.307  29.563  61.361  1.00 73.40           O  
ANISOU  594  OG  SER A 111     9370   8884   9634    218   -109   -941       O  
ATOM    595  N   ALA A 112      -5.096  32.225  58.238  1.00 79.44           N  
ANISOU  595  N   ALA A 112    10250   9503  10430    398   -106   -865       N  
ATOM    596  CA  ALA A 112      -5.530  32.099  56.853  1.00 74.81           C  
ANISOU  596  CA  ALA A 112     9664   8916   9842    477   -122   -842       C  
ATOM    597  C   ALA A 112      -4.335  31.991  55.915  1.00 76.60           C  
ANISOU  597  C   ALA A 112     9915   9126  10065    472   -127   -774       C  
ATOM    598  O   ALA A 112      -4.258  31.063  55.096  1.00 78.90           O  
ANISOU  598  O   ALA A 112    10185   9449  10345    493   -142   -747       O  
ATOM    599  CB  ALA A 112      -6.407  33.287  56.475  1.00 75.99           C  
ANISOU  599  CB  ALA A 112     9843   9024  10005    550   -117   -865       C  
ATOM    600  N   VAL A 113      -3.403  32.945  56.004  1.00 69.32           N  
ANISOU  600  N   VAL A 113     9038   8153   9146    443   -112   -748       N  
ATOM    601  CA  VAL A 113      -2.147  32.844  55.264  1.00 66.91           C  
ANISOU  601  CA  VAL A 113     8753   7839   8830    425   -116   -686       C  
ATOM    602  C   VAL A 113      -1.516  31.471  55.441  1.00 72.03           C  
ANISOU  602  C   VAL A 113     9359   8546   9462    383   -124   -661       C  
ATOM    603  O   VAL A 113      -0.903  30.927  54.517  1.00 73.11           O  
ANISOU  603  O   VAL A 113     9493   8695   9590    398   -135   -614       O  
ATOM    604  CB  VAL A 113      -1.186  33.961  55.705  1.00 71.97           C  
ANISOU  604  CB  VAL A 113     9444   8434   9468    372    -94   -670       C  
ATOM    605  CG1 VAL A 113       0.212  33.704  55.177  1.00 68.39           C  
ANISOU  605  CG1 VAL A 113     9000   7992   8995    334    -98   -609       C  
ATOM    606  CG2 VAL A 113      -1.703  35.301  55.246  1.00 80.81           C  
ANISOU  606  CG2 VAL A 113    10620   9484  10600    424    -84   -683       C  
ATOM    607  N   CYS A 114      -1.636  30.899  56.636  1.00 75.20           N  
ANISOU  607  N   CYS A 114     9730   8984   9860    332   -118   -691       N  
ATOM    608  CA  CYS A 114      -1.076  29.575  56.866  1.00 65.67           C  
ANISOU  608  CA  CYS A 114     8488   7830   8635    297   -123   -667       C  
ATOM    609  C   CYS A 114      -1.792  28.518  56.020  1.00 59.84           C  
ANISOU  609  C   CYS A 114     7726   7119   7892    350   -138   -668       C  
ATOM    610  O   CYS A 114      -1.152  27.632  55.446  1.00 54.41           O  
ANISOU  610  O   CYS A 114     7029   6452   7190    351   -143   -626       O  
ATOM    611  CB  CYS A 114      -1.140  29.257  58.360  1.00 61.61           C  
ANISOU  611  CB  CYS A 114     7947   7345   8115    231   -112   -701       C  
ATOM    612  SG  CYS A 114      -0.932  27.530  58.772  1.00 73.85           S  
ANISOU  612  SG  CYS A 114     9454   8959   9645    203   -118   -688       S  
ATOM    613  N   LYS A 115      -3.117  28.592  55.925  1.00 67.35           N  
ANISOU  613  N   LYS A 115     8666   8074   8851    392   -145   -716       N  
ATOM    614  CA  LYS A 115      -3.842  27.668  55.058  1.00 68.93           C  
ANISOU  614  CA  LYS A 115     8844   8305   9039    437   -157   -720       C  
ATOM    615  C   LYS A 115      -3.593  27.979  53.584  1.00 68.42           C  
ANISOU  615  C   LYS A 115     8800   8218   8978    492   -165   -677       C  
ATOM    616  O   LYS A 115      -3.545  27.064  52.756  1.00 61.69           O  
ANISOU  616  O   LYS A 115     7937   7389   8112    509   -171   -654       O  
ATOM    617  CB  LYS A 115      -5.341  27.712  55.361  1.00 69.64           C  
ANISOU  617  CB  LYS A 115     8912   8419   9129    464   -161   -784       C  
ATOM    618  CG  LYS A 115      -5.686  27.413  56.801  1.00 77.91           C  
ANISOU  618  CG  LYS A 115     9938   9492  10172    409   -155   -832       C  
ATOM    619  CD  LYS A 115      -7.105  27.816  57.117  1.00 75.59           C  
ANISOU  619  CD  LYS A 115     9626   9216   9880    440   -158   -896       C  
ATOM    620  CE  LYS A 115      -7.550  27.282  58.456  1.00 70.58           C  
ANISOU  620  CE  LYS A 115     8964   8619   9235    382   -155   -947       C  
ATOM    621  NZ  LYS A 115      -7.349  25.811  58.557  1.00 68.29           N  
ANISOU  621  NZ  LYS A 115     8656   8372   8920    344   -158   -937       N  
ATOM    622  N   THR A 116      -3.446  29.263  53.239  1.00 72.69           N  
ANISOU  622  N   THR A 116     9374   8710   9535    517   -164   -667       N  
ATOM    623  CA  THR A 116      -3.236  29.655  51.845  1.00 74.74           C  
ANISOU  623  CA  THR A 116     9655   8945   9797    569   -173   -627       C  
ATOM    624  C   THR A 116      -1.883  29.180  51.335  1.00 76.55           C  
ANISOU  624  C   THR A 116     9894   9176  10018    540   -174   -568       C  
ATOM    625  O   THR A 116      -1.789  28.551  50.275  1.00 77.44           O  
ANISOU  625  O   THR A 116     9998   9303  10122    568   -183   -539       O  
ATOM    626  CB  THR A 116      -3.336  31.174  51.699  1.00 75.74           C  
ANISOU  626  CB  THR A 116     9824   9013   9940    598   -168   -629       C  
ATOM    627  OG1 THR A 116      -4.694  31.598  51.880  1.00 79.97           O  
ANISOU  627  OG1 THR A 116    10350   9553  10483    647   -169   -678       O  
ATOM    628  CG2 THR A 116      -2.861  31.593  50.344  1.00 75.15           C  
ANISOU  628  CG2 THR A 116     9776   8910   9866    637   -178   -580       C  
ATOM    629  N   THR A 117      -0.819  29.491  52.077  1.00 76.88           N  
ANISOU  629  N   THR A 117     9950   9204  10056    483   -164   -549       N  
ATOM    630  CA  THR A 117       0.535  29.175  51.636  1.00 76.52           C  
ANISOU  630  CA  THR A 117     9912   9166   9996    457   -164   -491       C  
ATOM    631  C   THR A 117       0.727  27.673  51.457  1.00 74.94           C  
ANISOU  631  C   THR A 117     9680   9014   9781    453   -166   -474       C  
ATOM    632  O   THR A 117       1.483  27.234  50.585  1.00 72.13           O  
ANISOU  632  O   THR A 117     9326   8666   9415    463   -170   -428       O  
ATOM    633  CB  THR A 117       1.535  29.735  52.646  1.00 80.52           C  
ANISOU  633  CB  THR A 117    10432   9667  10494    389   -150   -481       C  
ATOM    634  OG1 THR A 117       1.472  31.169  52.617  1.00 85.33           O  
ANISOU  634  OG1 THR A 117    11085  10222  11113    392   -144   -491       O  
ATOM    635  CG2 THR A 117       2.951  29.303  52.323  1.00 84.06           C  
ANISOU  635  CG2 THR A 117    10879  10140  10921    358   -149   -422       C  
ATOM    636  N   THR A 118       0.054  26.864  52.269  1.00 70.32           N  
ANISOU  636  N   THR A 118     9067   8458   9192    438   -161   -511       N  
ATOM    637  CA  THR A 118       0.197  25.424  52.109  1.00 66.94           C  
ANISOU  637  CA  THR A 118     8619   8070   8747    435   -158   -495       C  
ATOM    638  C   THR A 118      -0.639  24.928  50.933  1.00 68.00           C  
ANISOU  638  C   THR A 118     8749   8210   8878    488   -166   -502       C  
ATOM    639  O   THR A 118      -0.219  24.027  50.186  1.00 58.13           O  
ANISOU  639  O   THR A 118     7498   6975   7615    498   -163   -470       O  
ATOM    640  CB  THR A 118      -0.185  24.731  53.420  1.00 68.07           C  
ANISOU  640  CB  THR A 118     8741   8243   8882    394   -149   -532       C  
ATOM    641  OG1 THR A 118       0.615  25.275  54.482  1.00 68.03           O  
ANISOU  641  OG1 THR A 118     8736   8235   8877    342   -142   -523       O  
ATOM    642  CG2 THR A 118       0.116  23.274  53.350  1.00 67.12           C  
ANISOU  642  CG2 THR A 118     8609   8154   8740    387   -141   -511       C  
ATOM    643  N   TYR A 119      -1.806  25.549  50.729  1.00 70.77           N  
ANISOU  643  N   TYR A 119     9097   8552   9239    522   -174   -543       N  
ATOM    644  CA  TYR A 119      -2.693  25.189  49.628  1.00 61.13           C  
ANISOU  644  CA  TYR A 119     7867   7348   8012    569   -180   -552       C  
ATOM    645  C   TYR A 119      -2.019  25.409  48.278  1.00 65.36           C  
ANISOU  645  C   TYR A 119     8419   7865   8550    599   -187   -500       C  
ATOM    646  O   TYR A 119      -1.967  24.500  47.444  1.00 69.02           O  
ANISOU  646  O   TYR A 119     8876   8350   8999    609   -185   -481       O  
ATOM    647  CB  TYR A 119      -3.977  26.007  49.714  1.00 57.47           C  
ANISOU  647  CB  TYR A 119     7395   6884   7556    605   -187   -600       C  
ATOM    648  CG  TYR A 119      -5.098  25.441  48.881  1.00 66.64           C  
ANISOU  648  CG  TYR A 119     8534   8086   8700    642   -192   -621       C  
ATOM    649  CD1 TYR A 119      -5.214  24.077  48.679  1.00 65.86           C  
ANISOU  649  CD1 TYR A 119     8422   8027   8575    621   -184   -623       C  
ATOM    650  CD2 TYR A 119      -6.040  26.269  48.295  1.00 65.96           C  
ANISOU  650  CD2 TYR A 119     8442   8001   8618    698   -201   -638       C  
ATOM    651  CE1 TYR A 119      -6.247  23.557  47.944  1.00 63.23           C  
ANISOU  651  CE1 TYR A 119     8069   7737   8218    645   -184   -645       C  
ATOM    652  CE2 TYR A 119      -7.074  25.758  47.556  1.00 59.37           C  
ANISOU  652  CE2 TYR A 119     7580   7216   7760    727   -204   -657       C  
ATOM    653  CZ  TYR A 119      -7.177  24.405  47.375  1.00 64.45           C  
ANISOU  653  CZ  TYR A 119     8210   7902   8375    697   -196   -662       C  
ATOM    654  OH  TYR A 119      -8.223  23.900  46.625  1.00 66.04           O  
ANISOU  654  OH  TYR A 119     8386   8160   8546    718   -195   -683       O  
ATOM    655  N   PHE A 120      -1.489  26.615  48.050  1.00 64.52           N  
ANISOU  655  N   PHE A 120     8337   7718   8460    609   -194   -478       N  
ATOM    656  CA  PHE A 120      -0.895  26.928  46.756  1.00 68.31           C  
ANISOU  656  CA  PHE A 120     8833   8179   8942    636   -203   -431       C  
ATOM    657  C   PHE A 120       0.389  26.149  46.512  1.00 73.53           C  
ANISOU  657  C   PHE A 120     9496   8852   9589    606   -197   -383       C  
ATOM    658  O   PHE A 120       0.706  25.839  45.363  1.00 70.82           O  
ANISOU  658  O   PHE A 120     9155   8513   9241    627   -202   -350       O  
ATOM    659  CB  PHE A 120      -0.656  28.433  46.645  1.00 67.59           C  
ANISOU  659  CB  PHE A 120     8776   8039   8866    649   -209   -422       C  
ATOM    660  CG  PHE A 120      -1.908  29.198  46.394  1.00 73.32           C  
ANISOU  660  CG  PHE A 120     9504   8752   9603    702   -215   -455       C  
ATOM    661  CD1 PHE A 120      -2.839  28.725  45.483  1.00 87.48           C  
ANISOU  661  CD1 PHE A 120    11272  10577  11390    747   -222   -463       C  
ATOM    662  CD2 PHE A 120      -2.186  30.352  47.084  1.00 74.35           C  
ANISOU  662  CD2 PHE A 120     9659   8844   9747    706   -210   -479       C  
ATOM    663  CE1 PHE A 120      -4.007  29.411  45.245  1.00 91.11           C  
ANISOU  663  CE1 PHE A 120    11728  11037  11855    802   -228   -490       C  
ATOM    664  CE2 PHE A 120      -3.362  31.042  46.859  1.00 81.79           C  
ANISOU  664  CE2 PHE A 120    10602   9778  10698    764   -213   -508       C  
ATOM    665  CZ  PHE A 120      -4.269  30.569  45.940  1.00 89.71           C  
ANISOU  665  CZ  PHE A 120    11574  10819  11692    814   -223   -512       C  
ATOM    666  N   MET A 121       1.117  25.794  47.567  1.00 71.03           N  
ANISOU  666  N   MET A 121     9176   8546   9266    560   -187   -378       N  
ATOM    667  CA  MET A 121       2.338  25.022  47.378  1.00 61.31           C  
ANISOU  667  CA  MET A 121     7943   7333   8018    539   -180   -330       C  
ATOM    668  C   MET A 121       2.027  23.635  46.834  1.00 57.30           C  
ANISOU  668  C   MET A 121     7422   6854   7497    555   -171   -328       C  
ATOM    669  O   MET A 121       2.711  23.150  45.932  1.00 67.51           O  
ANISOU  669  O   MET A 121     8719   8153   8781    567   -170   -287       O  
ATOM    670  CB  MET A 121       3.107  24.929  48.696  1.00 63.92           C  
ANISOU  670  CB  MET A 121     8269   7679   8340    488   -169   -325       C  
ATOM    671  CG  MET A 121       4.376  24.103  48.638  1.00 58.61           C  
ANISOU  671  CG  MET A 121     7589   7035   7645    471   -160   -274       C  
ATOM    672  SD  MET A 121       5.766  25.211  48.888  1.00 76.30           S  
ANISOU  672  SD  MET A 121     9842   9275   9875    431   -162   -234       S  
ATOM    673  CE  MET A 121       7.069  24.031  49.230  1.00 75.71           C  
ANISOU  673  CE  MET A 121     9745   9254   9768    412   -148   -182       C  
ATOM    674  N   GLY A 122       1.005  22.975  47.373  1.00 54.75           N  
ANISOU  674  N   GLY A 122     7085   6548   7168    553   -164   -372       N  
ATOM    675  CA  GLY A 122       0.644  21.655  46.888  1.00 49.47           C  
ANISOU  675  CA  GLY A 122     6411   5903   6480    561   -151   -375       C  
ATOM    676  C   GLY A 122      -0.135  21.711  45.593  1.00 63.37           C  
ANISOU  676  C   GLY A 122     8170   7667   8240    598   -158   -382       C  
ATOM    677  O   GLY A 122      -0.043  20.792  44.766  1.00 65.85           O  
ANISOU  677  O   GLY A 122     8488   7994   8539    606   -146   -365       O  
ATOM    678  N   THR A 123      -0.911  22.779  45.391  1.00 60.52           N  
ANISOU  678  N   THR A 123     7805   7295   7895    623   -174   -406       N  
ATOM    679  CA  THR A 123      -1.574  22.947  44.109  1.00 60.37           C  
ANISOU  679  CA  THR A 123     7780   7283   7873    661   -182   -405       C  
ATOM    680  C   THR A 123      -0.548  23.105  43.004  1.00 63.72           C  
ANISOU  680  C   THR A 123     8218   7691   8302    673   -188   -350       C  
ATOM    681  O   THR A 123      -0.631  22.448  41.962  1.00 66.69           O  
ANISOU  681  O   THR A 123     8590   8084   8666    684   -182   -335       O  
ATOM    682  CB  THR A 123      -2.509  24.143  44.153  1.00 66.90           C  
ANISOU  682  CB  THR A 123     8601   8101   8715    693   -198   -434       C  
ATOM    683  OG1 THR A 123      -3.671  23.791  44.912  1.00 67.92           O  
ANISOU  683  OG1 THR A 123     8711   8263   8834    687   -192   -490       O  
ATOM    684  CG2 THR A 123      -2.936  24.533  42.737  1.00 71.41           C  
ANISOU  684  CG2 THR A 123     9168   8677   9286    737   -209   -418       C  
ATOM    685  N   SER A 124       0.442  23.953  43.248  1.00 66.41           N  
ANISOU  685  N   SER A 124     8575   8000   8657    664   -196   -320       N  
ATOM    686  CA  SER A 124       1.504  24.211  42.248  1.00 54.15           C  
ANISOU  686  CA  SER A 124     7036   6434   7105    669   -204   -268       C  
ATOM    687  C   SER A 124       2.209  22.911  41.861  1.00 61.87           C  
ANISOU  687  C   SER A 124     8009   7434   8064    657   -188   -239       C  
ATOM    688  O   SER A 124       2.283  22.619  40.681  1.00 76.58           O  
ANISOU  688  O   SER A 124     9871   9303   9922    675   -189   -218       O  
ATOM    689  CB  SER A 124       2.478  25.211  42.760  1.00 56.97           C  
ANISOU  689  CB  SER A 124     7411   6763   7470    648   -212   -246       C  
ATOM    690  OG  SER A 124       3.721  25.056  42.111  1.00 77.94           O  
ANISOU  690  OG  SER A 124    10075   9423  10116    638   -213   -196       O  
ATOM    691  N   VAL A 125       2.714  22.178  42.839  1.00 55.54           N  
ANISOU  691  N   VAL A 125     7206   6645   7252    630   -172   -238       N  
ATOM    692  CA  VAL A 125       3.443  20.918  42.547  1.00 51.86           C  
ANISOU  692  CA  VAL A 125     6742   6197   6766    625   -152   -207       C  
ATOM    693  C   VAL A 125       2.564  19.982  41.721  1.00 48.56           C  
ANISOU  693  C   VAL A 125     6323   5792   6336    640   -138   -226       C  
ATOM    694  O   VAL A 125       3.099  19.281  40.886  1.00 51.74           O  
ANISOU  694  O   VAL A 125     6732   6200   6727    647   -126   -197       O  
ATOM    695  CB  VAL A 125       3.895  20.250  43.851  1.00 46.00           C  
ANISOU  695  CB  VAL A 125     5999   5468   6012    598   -134   -208       C  
ATOM    696  CG1 VAL A 125       4.467  18.874  43.598  1.00 45.43           C  
ANISOU  696  CG1 VAL A 125     5934   5410   5918    602   -109   -180       C  
ATOM    697  CG2 VAL A 125       4.903  21.112  44.567  1.00 59.20           C  
ANISOU  697  CG2 VAL A 125     7670   7137   7688    576   -145   -183       C  
ATOM    698  N   SER A 126       1.260  19.979  41.958  1.00 52.78           N  
ANISOU  698  N   SER A 126     6848   6336   6869    642   -138   -275       N  
ATOM    699  CA  SER A 126       0.370  19.078  41.241  1.00 55.27           C  
ANISOU  699  CA  SER A 126     7161   6675   7164    646   -122   -298       C  
ATOM    700  C   SER A 126       0.189  19.547  39.799  1.00 60.32           C  
ANISOU  700  C   SER A 126     7794   7317   7808    671   -135   -281       C  
ATOM    701  O   SER A 126       0.372  18.778  38.851  1.00 63.16           O  
ANISOU  701  O   SER A 126     8159   7686   8152    671   -120   -263       O  
ATOM    702  CB  SER A 126      -0.972  19.020  41.976  1.00 58.83           C  
ANISOU  702  CB  SER A 126     7600   7146   7606    636   -121   -356       C  
ATOM    703  OG  SER A 126      -1.699  17.835  41.695  1.00 66.27           O  
ANISOU  703  OG  SER A 126     8546   8118   8516    621    -96   -382       O  
ATOM    704  N   VAL A 127      -0.100  20.825  39.647  1.00 59.68           N  
ANISOU  704  N   VAL A 127     7704   7224   7747    692   -162   -284       N  
ATOM    705  CA  VAL A 127      -0.265  21.382  38.287  1.00 48.25           C  
ANISOU  705  CA  VAL A 127     6250   5778   6305    719   -177   -264       C  
ATOM    706  C   VAL A 127       1.023  21.105  37.524  1.00 60.12           C  
ANISOU  706  C   VAL A 127     7766   7269   7809    713   -174   -213       C  
ATOM    707  O   VAL A 127       0.945  20.580  36.432  1.00 72.58           O  
ANISOU  707  O   VAL A 127     9340   8863   9375    717   -166   -201       O  
ATOM    708  CB  VAL A 127      -0.522  22.892  38.367  1.00 56.21           C  
ANISOU  708  CB  VAL A 127     7257   6763   7336    745   -204   -266       C  
ATOM    709  CG1 VAL A 127      -0.082  23.597  37.104  1.00 66.03           C  
ANISOU  709  CG1 VAL A 127     8507   7993   8590    766   -222   -227       C  
ATOM    710  CG2 VAL A 127      -1.968  23.207  38.679  1.00 56.10           C  
ANISOU  710  CG2 VAL A 127     7225   6772   7319    765   -208   -314       C  
ATOM    711  N   SER A 128       2.169  21.394  38.127  1.00 56.20           N  
ANISOU  711  N   SER A 128     7282   6751   7320    701   -178   -185       N  
ATOM    712  CA  SER A 128       3.437  21.277  37.412  1.00 57.89           C  
ANISOU  712  CA  SER A 128     7504   6959   7531    698   -179   -136       C  
ATOM    713  C   SER A 128       3.705  19.845  36.987  1.00 60.62           C  
ANISOU  713  C   SER A 128     7853   7324   7856    692   -150   -125       C  
ATOM    714  O   SER A 128       4.044  19.578  35.825  1.00 67.77           O  
ANISOU  714  O   SER A 128     8759   8235   8756    698   -148   -100       O  
ATOM    715  CB  SER A 128       4.574  21.805  38.272  1.00 53.32           C  
ANISOU  715  CB  SER A 128     6935   6367   6956    681   -186   -111       C  
ATOM    716  OG  SER A 128       4.557  23.215  38.277  1.00 54.25           O  
ANISOU  716  OG  SER A 128     7060   6461   7090    685   -212   -111       O  
ATOM    717  N   THR A 129       3.547  18.912  37.919  1.00 56.49           N  
ANISOU  717  N   THR A 129     7336   6807   7319    678   -125   -144       N  
ATOM    718  CA  THR A 129       3.799  17.509  37.627  1.00 57.28           C  
ANISOU  718  CA  THR A 129     7449   6917   7396    674    -91   -135       C  
ATOM    719  C   THR A 129       2.893  17.001  36.508  1.00 55.61           C  
ANISOU  719  C   THR A 129     7236   6720   7171    675    -78   -154       C  
ATOM    720  O   THR A 129       3.295  16.166  35.695  1.00 45.10           O  
ANISOU  720  O   THR A 129     5918   5393   5826    674    -55   -134       O  
ATOM    721  CB  THR A 129       3.606  16.697  38.903  1.00 59.05           C  
ANISOU  721  CB  THR A 129     7685   7144   7608    658    -67   -157       C  
ATOM    722  OG1 THR A 129       4.603  17.099  39.849  1.00 70.35           O  
ANISOU  722  OG1 THR A 129     9114   8570   9046    654    -76   -131       O  
ATOM    723  CG2 THR A 129       3.774  15.237  38.636  1.00 59.74           C  
ANISOU  723  CG2 THR A 129     7797   7234   7668    655    -27   -150       C  
ATOM    724  N   TRP A 130       1.663  17.461  36.466  1.00 47.30           N  
ANISOU  724  N   TRP A 130     6169   5682   6121    675    -90   -193       N  
ATOM    725  CA  TRP A 130       0.792  16.924  35.452  1.00 58.05           C  
ANISOU  725  CA  TRP A 130     7525   7070   7463    670    -75   -211       C  
ATOM    726  C   TRP A 130       0.888  17.710  34.155  1.00 61.29           C  
ANISOU  726  C   TRP A 130     7919   7484   7885    687    -98   -186       C  
ATOM    727  O   TRP A 130       0.655  17.131  33.096  1.00 63.09           O  
ANISOU  727  O   TRP A 130     8144   7732   8095    679    -82   -183       O  
ATOM    728  CB  TRP A 130      -0.633  16.793  36.016  1.00 60.12           C  
ANISOU  728  CB  TRP A 130     7776   7360   7708    659    -70   -267       C  
ATOM    729  CG  TRP A 130      -0.590  15.591  36.878  1.00 63.42           C  
ANISOU  729  CG  TRP A 130     8219   7774   8102    632    -35   -285       C  
ATOM    730  CD1 TRP A 130      -0.262  15.544  38.197  1.00 64.63           C  
ANISOU  730  CD1 TRP A 130     8383   7911   8263    626    -35   -290       C  
ATOM    731  CD2 TRP A 130      -0.744  14.227  36.458  1.00 60.15           C  
ANISOU  731  CD2 TRP A 130     7832   7371   7652    608      8   -293       C  
ATOM    732  NE1 TRP A 130      -0.248  14.242  38.635  1.00 65.99           N  
ANISOU  732  NE1 TRP A 130     8585   8082   8407    603      3   -302       N  
ATOM    733  CE2 TRP A 130      -0.533  13.415  37.586  1.00 57.79           C  
ANISOU  733  CE2 TRP A 130     7560   7056   7340    592     31   -304       C  
ATOM    734  CE3 TRP A 130      -1.056  13.615  35.244  1.00 54.54           C  
ANISOU  734  CE3 TRP A 130     7126   6680   6917    595     31   -293       C  
ATOM    735  CZ2 TRP A 130      -0.630  12.032  37.537  1.00 57.01           C  
ANISOU  735  CZ2 TRP A 130     7501   6956   7204    566     78   -314       C  
ATOM    736  CZ3 TRP A 130      -1.143  12.230  35.202  1.00 47.96           C  
ANISOU  736  CZ3 TRP A 130     6331   5846   6045    565     79   -306       C  
ATOM    737  CH2 TRP A 130      -0.935  11.463  36.328  1.00 60.33           C  
ANISOU  737  CH2 TRP A 130     7932   7392   7600    552    103   -316       C  
ATOM    738  N   ASN A 131       1.331  18.968  34.210  1.00 55.99           N  
ANISOU  738  N   ASN A 131     7240   6792   7241    706   -133   -165       N  
ATOM    739  CA  ASN A 131       1.750  19.649  32.993  1.00 63.01           C  
ANISOU  739  CA  ASN A 131     8122   7679   8141    720   -154   -131       C  
ATOM    740  C   ASN A 131       2.922  18.922  32.339  1.00 70.58           C  
ANISOU  740  C   ASN A 131     9093   8633   9092    710   -138    -93       C  
ATOM    741  O   ASN A 131       2.917  18.670  31.126  1.00 80.45           O  
ANISOU  741  O   ASN A 131    10336   9898  10334    707   -134    -79       O  
ATOM    742  CB  ASN A 131       2.104  21.103  33.295  1.00 47.35           C  
ANISOU  742  CB  ASN A 131     6140   5668   6184    737   -190   -116       C  
ATOM    743  CG  ASN A 131       0.879  21.977  33.425  1.00 62.22           C  
ANISOU  743  CG  ASN A 131     8009   7557   8074    760   -208   -146       C  
ATOM    744  OD1 ASN A 131       0.979  23.164  33.730  1.00 56.27           O  
ANISOU  744  OD1 ASN A 131     7264   6777   7341    776   -232   -141       O  
ATOM    745  ND2 ASN A 131      -0.301  21.389  33.186  1.00 73.71           N  
ANISOU  745  ND2 ASN A 131     9446   9051   9511    760   -193   -180       N  
ATOM    746  N   LEU A 132       3.912  18.549  33.135  1.00 62.07           N  
ANISOU  746  N   LEU A 132     8031   7540   8014    704   -128    -75       N  
ATOM    747  CA  LEU A 132       5.069  17.834  32.557  1.00 51.90           C  
ANISOU  747  CA  LEU A 132     6753   6251   6714    701   -111    -37       C  
ATOM    748  C   LEU A 132       4.607  16.506  31.958  1.00 53.47           C  
ANISOU  748  C   LEU A 132     6962   6464   6889    691    -70    -51       C  
ATOM    749  O   LEU A 132       5.198  16.086  30.980  1.00 54.59           O  
ANISOU  749  O   LEU A 132     7108   6611   7024    690    -59    -25       O  
ATOM    750  CB  LEU A 132       6.113  17.638  33.649  1.00 44.68           C  
ANISOU  750  CB  LEU A 132     5850   5329   5799    701   -104    -16       C  
ATOM    751  CG  LEU A 132       6.910  18.890  33.978  1.00 56.29           C  
ANISOU  751  CG  LEU A 132     7313   6791   7283    701   -139      8       C  
ATOM    752  CD1 LEU A 132       7.718  18.701  35.244  1.00 59.95           C  
ANISOU  752  CD1 LEU A 132     7782   7257   7740    695   -131     21       C  
ATOM    753  CD2 LEU A 132       7.813  19.257  32.825  1.00 45.55           C  
ANISOU  753  CD2 LEU A 132     5950   5436   5922    703   -155     47       C  
ATOM    754  N   VAL A 133       3.598  15.869  32.540  1.00 51.16           N  
ANISOU  754  N   VAL A 133     6677   6179   6582    679    -48    -92       N  
ATOM    755  CA  VAL A 133       3.104  14.614  31.987  1.00 53.60           C  
ANISOU  755  CA  VAL A 133     7003   6501   6861    660     -4   -110       C  
ATOM    756  C   VAL A 133       2.403  14.859  30.656  1.00 59.95           C  
ANISOU  756  C   VAL A 133     7786   7332   7660    652    -11   -116       C  
ATOM    757  O   VAL A 133       2.566  14.094  29.701  1.00 56.10           O  
ANISOU  757  O   VAL A 133     7309   6852   7154    638     17   -108       O  
ATOM    758  CB  VAL A 133       2.165  13.920  32.983  1.00 52.02           C  
ANISOU  758  CB  VAL A 133     6818   6307   6640    642     20   -155       C  
ATOM    759  CG1 VAL A 133       1.308  12.858  32.279  1.00 46.67           C  
ANISOU  759  CG1 VAL A 133     6156   5652   5926    612     62   -184       C  
ATOM    760  CG2 VAL A 133       2.966  13.284  34.086  1.00 54.30           C  
ANISOU  760  CG2 VAL A 133     7135   6572   6927    647     40   -142       C  
ATOM    761  N   ALA A 134       1.585  15.908  30.593  1.00 46.53           N  
ANISOU  761  N   ALA A 134     6058   5649   5973    661    -45   -133       N  
ATOM    762  CA  ALA A 134       0.908  16.249  29.360  1.00 52.23           C  
ANISOU  762  CA  ALA A 134     6754   6403   6688    657    -55   -135       C  
ATOM    763  C   ALA A 134       1.914  16.493  28.243  1.00 60.89           C  
ANISOU  763  C   ALA A 134     7848   7490   7797    662    -66    -90       C  
ATOM    764  O   ALA A 134       1.729  16.018  27.118  1.00 66.09           O  
ANISOU  764  O   ALA A 134     8500   8173   8439    644    -49    -86       O  
ATOM    765  CB  ALA A 134       0.033  17.475  29.579  1.00 48.74           C  
ANISOU  765  CB  ALA A 134     6283   5975   6261    679    -93   -150       C  
ATOM    766  N   ILE A 135       2.988  17.198  28.564  1.00 62.37           N  
ANISOU  766  N   ILE A 135     8040   7647   8009    680    -93    -57       N  
ATOM    767  CA  ILE A 135       4.032  17.490  27.547  1.00 52.41           C  
ANISOU  767  CA  ILE A 135     6777   6381   6758    682   -107    -14       C  
ATOM    768  C   ILE A 135       4.570  16.170  26.997  1.00 58.31           C  
ANISOU  768  C   ILE A 135     7541   7132   7483    665    -64     -4       C  
ATOM    769  O   ILE A 135       4.494  15.967  25.796  1.00 76.04           O  
ANISOU  769  O   ILE A 135     9776   9395   9720    652    -58      4       O  
ATOM    770  CB  ILE A 135       5.131  18.367  28.161  1.00 46.44           C  
ANISOU  770  CB  ILE A 135     6026   5597   6021    697   -138     16       C  
ATOM    771  CG1 ILE A 135       4.678  19.821  28.242  1.00 47.32           C  
ANISOU  771  CG1 ILE A 135     6126   5699   6153    712   -180     14       C  
ATOM    772  CG2 ILE A 135       6.412  18.223  27.377  1.00 45.40           C  
ANISOU  772  CG2 ILE A 135     5897   5464   5887    693   -140     57       C  
ATOM    773  CD1 ILE A 135       5.620  20.718  28.968  1.00 46.37           C  
ANISOU  773  CD1 ILE A 135     6018   5553   6047    717   -206     35       C  
ATOM    774  N   SER A 136       5.074  15.303  27.864  1.00 55.29           N  
ANISOU  774  N   SER A 136     7184   6732   7090    667    -34     -5       N  
ATOM    775  CA  SER A 136       5.612  14.007  27.448  1.00 55.57           C  
ANISOU  775  CA  SER A 136     7246   6764   7103    658     14      5       C  
ATOM    776  C   SER A 136       4.624  13.238  26.579  1.00 56.82           C  
ANISOU  776  C   SER A 136     7409   6944   7237    628     48    -24       C  
ATOM    777  O   SER A 136       5.032  12.449  25.728  1.00 61.63           O  
ANISOU  777  O   SER A 136     8032   7554   7830    616     81    -12       O  
ATOM    778  CB  SER A 136       5.963  13.157  28.686  1.00 52.64           C  
ANISOU  778  CB  SER A 136     6907   6372   6721    668     45      1       C  
ATOM    779  OG  SER A 136       4.790  12.533  29.258  1.00 45.65           O  
ANISOU  779  OG  SER A 136     6037   5490   5817    649     72    -45       O  
ATOM    780  N   LEU A 137       3.326  13.417  26.818  1.00 58.70           N  
ANISOU  780  N   LEU A 137     7634   7203   7466    614     45    -63       N  
ATOM    781  CA  LEU A 137       2.291  12.669  26.113  1.00 62.54           C  
ANISOU  781  CA  LEU A 137     8123   7722   7919    578     80    -95       C  
ATOM    782  C   LEU A 137       1.998  13.278  24.744  1.00 67.08           C  
ANISOU  782  C   LEU A 137     8661   8332   8496    567     58    -84       C  
ATOM    783  O   LEU A 137       1.624  12.561  23.813  1.00 60.98           O  
ANISOU  783  O   LEU A 137     7890   7584   7694    533     92    -94       O  
ATOM    784  CB  LEU A 137       1.010  12.623  26.966  1.00 49.98           C  
ANISOU  784  CB  LEU A 137     6528   6152   6309    565     84   -142       C  
ATOM    785  CG  LEU A 137       0.640  11.303  27.678  1.00 57.88           C  
ANISOU  785  CG  LEU A 137     7574   7145   7274    538    139   -175       C  
ATOM    786  CD1 LEU A 137       1.831  10.579  28.257  1.00 54.97           C  
ANISOU  786  CD1 LEU A 137     7248   6726   6910    555    165   -149       C  
ATOM    787  CD2 LEU A 137      -0.369  11.524  28.776  1.00 48.86           C  
ANISOU  787  CD2 LEU A 137     6422   6018   6122    534    128   -216       C  
ATOM    788  N   GLU A 138       2.175  14.590  24.601  1.00 70.38           N  
ANISOU  788  N   GLU A 138     9047   8750   8945    594      4    -62       N  
ATOM    789  CA  GLU A 138       1.966  15.231  23.315  1.00 68.93           C  
ANISOU  789  CA  GLU A 138     8829   8596   8765    588    -20    -45       C  
ATOM    790  C   GLU A 138       3.178  15.037  22.402  1.00 75.33           C  
ANISOU  790  C   GLU A 138     9647   9392   9584    583    -17     -7       C  
ATOM    791  O   GLU A 138       3.023  14.704  21.225  1.00 75.84           O  
ANISOU  791  O   GLU A 138     9699   9484   9633    555     -2     -3       O  
ATOM    792  CB  GLU A 138       1.648  16.705  23.535  1.00 71.09           C  
ANISOU  792  CB  GLU A 138     9075   8870   9066    621    -75    -37       C  
ATOM    793  CG  GLU A 138       1.605  17.522  22.280  1.00 86.22           C  
ANISOU  793  CG  GLU A 138    10960  10809  10990    623   -106    -11       C  
ATOM    794  CD  GLU A 138       2.928  18.199  21.998  1.00 96.80           C  
ANISOU  794  CD  GLU A 138    12309  12114  12357    637   -138     32       C  
ATOM    795  OE1 GLU A 138       3.777  18.267  22.920  1.00 86.65           O  
ANISOU  795  OE1 GLU A 138    11047  10790  11085    651   -142     41       O  
ATOM    796  OE2 GLU A 138       3.112  18.662  20.847  1.00110.11           O  
ANISOU  796  OE2 GLU A 138    13975  13815  14046    630   -158     56       O  
ATOM    797  N   ARG A 139       4.394  15.217  22.920  1.00 72.76           N  
ANISOU  797  N   ARG A 139     9338   9028   9277    605    -30     21       N  
ATOM    798  CA  ARG A 139       5.568  14.855  22.135  1.00 63.78           C  
ANISOU  798  CA  ARG A 139     8208   7884   8140    600    -20     54       C  
ATOM    799  C   ARG A 139       5.546  13.378  21.762  1.00 63.28           C  
ANISOU  799  C   ARG A 139     8173   7823   8047    575     43     41       C  
ATOM    800  O   ARG A 139       6.101  12.987  20.730  1.00 68.29           O  
ANISOU  800  O   ARG A 139     8807   8464   8675    560     58     58       O  
ATOM    801  CB  ARG A 139       6.864  15.171  22.895  1.00 60.51           C  
ANISOU  801  CB  ARG A 139     7807   7440   7742    628    -39     85       C  
ATOM    802  CG  ARG A 139       7.000  16.586  23.418  1.00 59.76           C  
ANISOU  802  CG  ARG A 139     7698   7336   7673    648    -94     97       C  
ATOM    803  CD  ARG A 139       7.503  17.586  22.388  1.00 54.40           C  
ANISOU  803  CD  ARG A 139     6998   6666   7006    644   -136    127       C  
ATOM    804  NE  ARG A 139       6.437  18.014  21.497  1.00 74.03           N  
ANISOU  804  NE  ARG A 139     9460   9174   9492    633   -149    115       N  
ATOM    805  CZ  ARG A 139       6.395  17.744  20.198  1.00 86.77           C  
ANISOU  805  CZ  ARG A 139    11058  10813  11097    610   -142    124       C  
ATOM    806  NH1 ARG A 139       7.378  17.054  19.639  1.00 99.81           N  
ANISOU  806  NH1 ARG A 139    12717  12465  12740    597   -122    143       N  
ATOM    807  NH2 ARG A 139       5.378  18.175  19.459  1.00 81.37           N  
ANISOU  807  NH2 ARG A 139    10348  10158  10411    601   -155    114       N  
ATOM    808  N   TYR A 140       4.955  12.532  22.600  1.00 63.35           N  
ANISOU  808  N   TYR A 140     8210   7822   8036    569     82      9       N  
ATOM    809  CA  TYR A 140       4.840  11.134  22.207  1.00 64.34           C  
ANISOU  809  CA  TYR A 140     8371   7946   8128    540    148     -7       C  
ATOM    810  C   TYR A 140       3.894  10.993  21.027  1.00 70.34           C  
ANISOU  810  C   TYR A 140     9111   8750   8866    495    162    -27       C  
ATOM    811  O   TYR A 140       4.163  10.233  20.089  1.00 72.33           O  
ANISOU  811  O   TYR A 140     9378   9006   9099    467    201    -23       O  
ATOM    812  CB  TYR A 140       4.364  10.272  23.376  1.00 53.59           C  
ANISOU  812  CB  TYR A 140     7051   6566   6746    538    187    -38       C  
ATOM    813  CG  TYR A 140       4.068   8.847  22.970  1.00 48.76           C  
ANISOU  813  CG  TYR A 140     6486   5950   6093    501    260    -60       C  
ATOM    814  CD1 TYR A 140       5.086   7.921  22.835  1.00 53.64           C  
ANISOU  814  CD1 TYR A 140     7147   6532   6702    514    303    -38       C  
ATOM    815  CD2 TYR A 140       2.772   8.431  22.701  1.00 52.99           C  
ANISOU  815  CD2 TYR A 140     7023   6519   6593    453    287   -103       C  
ATOM    816  CE1 TYR A 140       4.823   6.610  22.453  1.00 55.87           C  
ANISOU  816  CE1 TYR A 140     7481   6802   6944    480    376    -59       C  
ATOM    817  CE2 TYR A 140       2.501   7.124  22.308  1.00 61.09           C  
ANISOU  817  CE2 TYR A 140     8098   7540   7574    410    359   -126       C  
ATOM    818  CZ  TYR A 140       3.529   6.219  22.188  1.00 65.23           C  
ANISOU  818  CZ  TYR A 140     8673   8018   8093    424    404   -104       C  
ATOM    819  OH  TYR A 140       3.272   4.912  21.811  1.00 76.65           O  
ANISOU  819  OH  TYR A 140    10178   9450   9493    381    481   -128       O  
ATOM    820  N   GLY A 141       2.767  11.701  21.072  1.00 68.21           N  
ANISOU  820  N   GLY A 141     8806   8516   8594    487    133    -49       N  
ATOM    821  CA  GLY A 141       1.860  11.687  19.946  1.00 74.85           C  
ANISOU  821  CA  GLY A 141     9618   9412   9411    445    142    -64       C  
ATOM    822  C   GLY A 141       2.515  12.196  18.677  1.00 70.90           C  
ANISOU  822  C   GLY A 141     9088   8923   8927    442    117    -28       C  
ATOM    823  O   GLY A 141       2.366  11.606  17.611  1.00 77.15           O  
ANISOU  823  O   GLY A 141     9878   9742   9695    399    150    -32       O  
ATOM    824  N   ALA A 142       3.270  13.288  18.782  1.00 62.69           N  
ANISOU  824  N   ALA A 142     8030   7862   7926    481     62      6       N  
ATOM    825  CA  ALA A 142       3.822  13.912  17.590  1.00 56.14           C  
ANISOU  825  CA  ALA A 142     7172   7047   7111    476     31     40       C  
ATOM    826  C   ALA A 142       4.925  13.053  16.988  1.00 64.24           C  
ANISOU  826  C   ALA A 142     8222   8054   8131    461     66     57       C  
ATOM    827  O   ALA A 142       4.957  12.822  15.777  1.00 81.53           O  
ANISOU  827  O   ALA A 142    10396  10272  10310    426     78     64       O  
ATOM    828  CB  ALA A 142       4.341  15.312  17.919  1.00 48.29           C  
ANISOU  828  CB  ALA A 142     6161   6034   6155    517    -35     69       C  
ATOM    829  N   ILE A 143       5.820  12.539  17.823  1.00 66.74           N  
ANISOU  829  N   ILE A 143     8577   8329   8454    487     84     65       N  
ATOM    830  CA  ILE A 143       7.014  11.869  17.323  1.00 62.46           C  
ANISOU  830  CA  ILE A 143     8054   7769   7908    487    110     89       C  
ATOM    831  C   ILE A 143       6.732  10.407  16.985  1.00 69.37           C  
ANISOU  831  C   ILE A 143     8968   8641   8748    454    187     65       C  
ATOM    832  O   ILE A 143       7.271   9.869  16.016  1.00 81.90           O  
ANISOU  832  O   ILE A 143    10562  10232  10326    434    214     75       O  
ATOM    833  CB  ILE A 143       8.137  12.020  18.369  1.00 61.60           C  
ANISOU  833  CB  ILE A 143     7964   7624   7816    535     95    114       C  
ATOM    834  CG1 ILE A 143       8.600  13.481  18.440  1.00 65.66           C  
ANISOU  834  CG1 ILE A 143     8445   8144   8359    556     23    141       C  
ATOM    835  CG2 ILE A 143       9.283  11.033  18.132  1.00 51.14           C  
ANISOU  835  CG2 ILE A 143     6670   6283   6480    546    138    133       C  
ATOM    836  CD1 ILE A 143       9.402  13.787  19.662  1.00 61.44           C  
ANISOU  836  CD1 ILE A 143     7924   7585   7836    594      6    157       C  
ATOM    837  N   CYS A 144       5.895   9.738  17.769  1.00 72.25           N  
ANISOU  837  N   CYS A 144     9363   8997   9091    445    224     30       N  
ATOM    838  CA  CYS A 144       5.728   8.292  17.672  1.00 79.79           C  
ANISOU  838  CA  CYS A 144    10372   9937  10009    416    303      7       C  
ATOM    839  C   CYS A 144       4.470   7.874  16.937  1.00 86.42           C  
ANISOU  839  C   CYS A 144    11205  10819  10811    351    337    -31       C  
ATOM    840  O   CYS A 144       4.411   6.753  16.425  1.00 91.49           O  
ANISOU  840  O   CYS A 144    11888  11455  11418    312    404    -47       O  
ATOM    841  CB  CYS A 144       5.702   7.661  19.072  1.00 75.00           C  
ANISOU  841  CB  CYS A 144     9814   9290   9393    443    332     -8       C  
ATOM    842  SG  CYS A 144       7.328   7.425  19.791  1.00 75.63           S  
ANISOU  842  SG  CYS A 144     9922   9321   9493    509    333     35       S  
ATOM    843  N   LYS A 145       3.441   8.713  16.925  1.00 86.75           N  
ANISOU  843  N   LYS A 145    11201  10907  10854    338    296    -46       N  
ATOM    844  CA  LYS A 145       2.199   8.413  16.215  1.00 89.92           C  
ANISOU  844  CA  LYS A 145    11585  11367  11214    276    324    -79       C  
ATOM    845  C   LYS A 145       1.727   9.673  15.497  1.00103.03           C  
ANISOU  845  C   LYS A 145    13173  13083  12892    276    261    -64       C  
ATOM    846  O   LYS A 145       0.660  10.215  15.794  1.00115.63           O  
ANISOU  846  O   LYS A 145    14735  14721  14477    275    238    -82       O  
ATOM    847  CB  LYS A 145       1.156   7.873  17.189  1.00 80.07           C  
ANISOU  847  CB  LYS A 145    10365  10127   9932    258    355   -123       C  
ATOM    848  CG  LYS A 145       1.637   6.632  17.901  1.00 82.15           C  
ANISOU  848  CG  LYS A 145    10706  10330  10176    259    418   -135       C  
ATOM    849  CD  LYS A 145       0.521   5.825  18.533  1.00 93.90           C  
ANISOU  849  CD  LYS A 145    12231  11833  11613    216    466   -185       C  
ATOM    850  CE  LYS A 145       1.089   4.548  19.156  1.00105.72           C  
ANISOU  850  CE  LYS A 145    13815  13262  13090    219    533   -192       C  
ATOM    851  NZ  LYS A 145       0.064   3.757  19.905  1.00114.15           N  
ANISOU  851  NZ  LYS A 145    14928  14337  14106    176    579   -242       N  
ATOM    852  N   PRO A 146       2.526  10.177  14.530  1.00 95.02           N  
ANISOU  852  N   PRO A 146    12131  12069  11902    281    233    -28       N  
ATOM    853  CA  PRO A 146       2.209  11.469  13.906  1.00 96.49           C  
ANISOU  853  CA  PRO A 146    12254  12298  12109    291    168     -6       C  
ATOM    854  C   PRO A 146       0.889  11.465  13.148  1.00111.73           C  
ANISOU  854  C   PRO A 146    14144  14308  14000    241    180    -28       C  
ATOM    855  O   PRO A 146      -0.018  12.236  13.478  1.00111.87           O  
ANISOU  855  O   PRO A 146    14126  14363  14018    260    145    -35       O  
ATOM    856  CB  PRO A 146       3.401  11.708  12.969  1.00 91.65           C  
ANISOU  856  CB  PRO A 146    11633  11670  11520    293    150     32       C  
ATOM    857  CG  PRO A 146       3.971  10.369  12.719  1.00 87.99           C  
ANISOU  857  CG  PRO A 146    11217  11181  11035    264    219     22       C  
ATOM    858  CD  PRO A 146       3.750   9.582  13.969  1.00 89.83           C  
ANISOU  858  CD  PRO A 146    11502  11376  11252    279    259     -5       C  
ATOM    859  N   LEU A 147       0.762  10.570  12.169  1.00122.91           N  
ANISOU  859  N   LEU A 147    15565  15754  15380    177    233    -41       N  
ATOM    860  CA  LEU A 147      -0.478  10.485  11.353  1.00130.87           C  
ANISOU  860  CA  LEU A 147    16531  16852  16342    118    250    -61       C  
ATOM    861  C   LEU A 147      -1.491   9.568  12.041  1.00132.16           C  
ANISOU  861  C   LEU A 147    16724  17037  16452     81    306   -111       C  
ATOM    862  O   LEU A 147      -2.360   9.019  11.339  1.00139.65           O  
ANISOU  862  O   LEU A 147    17657  18057  17346     11    348   -136       O  
ATOM    863  CB  LEU A 147      -0.122   9.952   9.963  1.00131.10           C  
ANISOU  863  CB  LEU A 147    16553  16906  16353     57    284    -53       C  
ATOM    864  N   GLN A 148      -1.373   9.416  13.360  1.00125.01           N  
ANISOU  864  N   GLN A 148    15860  16078  15560    122    306   -125       N  
ATOM    865  CA  GLN A 148      -2.279   8.569  14.124  1.00122.76           C  
ANISOU  865  CA  GLN A 148    15609  15809  15225     89    356   -172       C  
ATOM    866  C   GLN A 148      -2.781   9.216  15.404  1.00128.90           C  
ANISOU  866  C   GLN A 148    16376  16580  16018    141    315   -183       C  
ATOM    867  O   GLN A 148      -3.795   8.758  15.945  1.00135.70           O  
ANISOU  867  O   GLN A 148    17246  17480  16834    111    343   -225       O  
ATOM    868  CB  GLN A 148      -1.593   7.239  14.477  1.00122.24           C  
ANISOU  868  CB  GLN A 148    15628  15673  15144     69    425   -187       C  
ATOM    869  CG  GLN A 148      -0.893   6.582  13.285  1.00125.68           C  
ANISOU  869  CG  GLN A 148    16082  16098  15570     27    468   -174       C  
ATOM    870  CD  GLN A 148       0.251   5.661  13.685  1.00125.19           C  
ANISOU  870  CD  GLN A 148    16099  15947  15522     48    514   -166       C  
ATOM    871  OE1 GLN A 148       0.102   4.804  14.558  1.00126.60           O  
ANISOU  871  OE1 GLN A 148    16341  16088  15675     44    561   -193       O  
ATOM    872  NE2 GLN A 148       1.405   5.837  13.041  1.00120.58           N  
ANISOU  872  NE2 GLN A 148    15510  15331  14974     73    500   -129       N  
ATOM    873  N   SER A 149      -2.067  10.237  15.883  1.00127.61           N  
ANISOU  873  N   SER A 149    16200  16371  15916    214    253   -149       N  
ATOM    874  CA  SER A 149      -2.438  10.959  17.128  1.00124.95           C  
ANISOU  874  CA  SER A 149    15854  16020  15601    267    212   -157       C  
ATOM    875  C   SER A 149      -2.810  12.394  16.767  1.00123.28           C  
ANISOU  875  C   SER A 149    15577  15848  15416    307    144   -132       C  
ATOM    876  O   SER A 149      -2.148  13.316  17.258  1.00123.36           O  
ANISOU  876  O   SER A 149    15585  15809  15476    366     95   -104       O  
ATOM    877  CB  SER A 149      -1.297  10.960  18.088  1.00116.93           C  
ANISOU  877  CB  SER A 149    14882  14916  14628    316    201   -139       C  
ATOM    878  OG  SER A 149      -0.403  12.013  17.768  1.00114.21           O  
ANISOU  878  OG  SER A 149    14513  14545  14335    362    145    -94       O  
ATOM    879  N   ARG A 150      -3.831  12.549  15.933  1.00119.79           N  
ANISOU  879  N   ARG A 150    15085  15493  14936    274    146   -141       N  
ATOM    880  CA  ARG A 150      -4.271  13.883  15.455  1.00116.53           C  
ANISOU  880  CA  ARG A 150    14610  15125  14542    313     87   -114       C  
ATOM    881  C   ARG A 150      -4.905  14.764  16.535  1.00118.36           C  
ANISOU  881  C   ARG A 150    14826  15358  14789    373     47   -124       C  
ATOM    882  O   ARG A 150      -4.630  15.966  16.493  1.00119.35           O  
ANISOU  882  O   ARG A 150    14931  15462  14956    429     -8    -90       O  
ATOM    883  CB  ARG A 150      -5.235  13.726  14.278  1.00119.54           C  
ANISOU  883  CB  ARG A 150    14938  15610  14870    261    104   -120       C  
ATOM    884  N   VAL A 151      -5.706  14.235  17.462  1.00114.99           N  
ANISOU  884  N   VAL A 151    14411  14952  14329    360     73   -168       N  
ATOM    885  CA  VAL A 151      -6.381  15.207  18.381  1.00109.34           C  
ANISOU  885  CA  VAL A 151    13671  14246  13627    420     31   -176       C  
ATOM    886  C   VAL A 151      -5.456  15.698  19.495  1.00102.93           C  
ANISOU  886  C   VAL A 151    12899  13335  12874    474      2   -163       C  
ATOM    887  O   VAL A 151      -5.621  16.843  19.931  1.00 94.36           O  
ANISOU  887  O   VAL A 151    11795  12239  11819    532    -44   -150       O  
ATOM    888  CB  VAL A 151      -7.724  14.704  18.930  1.00104.60           C  
ANISOU  888  CB  VAL A 151    13054  13722  12968    392     58   -226       C  
ATOM    889  CG1 VAL A 151      -7.537  13.666  20.023  1.00100.47           C  
ANISOU  889  CG1 VAL A 151    12590  13152  12433    364     99   -265       C  
ATOM    890  CG2 VAL A 151      -8.557  15.870  19.426  1.00102.33           C  
ANISOU  890  CG2 VAL A 151    12721  13470  12689    456     12   -227       C  
ATOM    891  N   TRP A 152      -4.525  14.860  19.932  1.00106.69           N  
ANISOU  891  N   TRP A 152    13430  13746  13361    454     32   -166       N  
ATOM    892  CA  TRP A 152      -3.588  15.276  20.999  1.00111.45           C  
ANISOU  892  CA  TRP A 152    14068  14265  14014    500      7   -152       C  
ATOM    893  C   TRP A 152      -2.828  16.514  20.527  1.00112.13           C  
ANISOU  893  C   TRP A 152    14138  14318  14148    545    -46   -104       C  
ATOM    894  O   TRP A 152      -2.152  17.110  21.360  1.00115.18           O  
ANISOU  894  O   TRP A 152    14545  14646  14572    583    -73    -91       O  
ATOM    895  CB  TRP A 152      -2.615  14.138  21.318  1.00115.22           C  
ANISOU  895  CB  TRP A 152    14602  14686  14491    474     49   -154       C  
ATOM    896  CG  TRP A 152      -2.601  13.722  22.754  1.00121.10           C  
ANISOU  896  CG  TRP A 152    15384  15393  15237    484     63   -180       C  
ATOM    897  CD1 TRP A 152      -2.691  12.452  23.241  1.00122.03           C  
ANISOU  897  CD1 TRP A 152    15545  15501  15322    447    117   -210       C  
ATOM    898  CD2 TRP A 152      -2.480  14.581  23.898  1.00121.33           C  
ANISOU  898  CD2 TRP A 152    15411  15386  15301    532     24   -178       C  
ATOM    899  NE1 TRP A 152      -2.644  12.462  24.607  1.00118.54           N  
ANISOU  899  NE1 TRP A 152    15125  15023  14892    469    111   -226       N  
ATOM    900  CE2 TRP A 152      -2.514  13.753  25.038  1.00118.12           C  
ANISOU  900  CE2 TRP A 152    15043  14956  14880    519     55   -208       C  
ATOM    901  CE3 TRP A 152      -2.351  15.961  24.071  1.00117.64           C  
ANISOU  901  CE3 TRP A 152    14919  14905  14873    581    -31   -156       C  
ATOM    902  CZ2 TRP A 152      -2.424  14.265  26.328  1.00111.93           C  
ANISOU  902  CZ2 TRP A 152    14266  14139  14122    552     31   -215       C  
ATOM    903  CZ3 TRP A 152      -2.255  16.465  25.346  1.00108.98           C  
ANISOU  903  CZ3 TRP A 152    13834  13772  13800    612    -51   -164       C  
ATOM    904  CH2 TRP A 152      -2.291  15.626  26.456  1.00106.30           C  
ANISOU  904  CH2 TRP A 152    13526  13414  13447    597    -21   -194       C  
ATOM    905  N   GLN A 153      -2.940  16.881  19.248  1.00 97.95           N  
ANISOU  905  N   GLN A 153    12308  12563  12346    535    -59    -80       N  
ATOM    906  CA  GLN A 153      -2.174  18.015  18.758  1.00 84.71           C  
ANISOU  906  CA  GLN A 153    10623  10852  10711    572   -108    -35       C  
ATOM    907  C   GLN A 153      -3.036  19.233  18.499  1.00 85.08           C  
ANISOU  907  C   GLN A 153    10628  10937  10761    613   -149    -24       C  
ATOM    908  O   GLN A 153      -2.580  20.158  17.821  1.00 87.85           O  
ANISOU  908  O   GLN A 153    10969  11273  11137    636   -186     15       O  
ATOM    909  CB  GLN A 153      -1.411  17.660  17.482  1.00 68.24           C  
ANISOU  909  CB  GLN A 153     8534   8771   8624    536    -99     -6       C  
ATOM    910  N   THR A 154      -4.267  19.263  19.006  1.00 85.19           N  
ANISOU  910  N   THR A 154    10619  11001  10749    625   -142    -55       N  
ATOM    911  CA  THR A 154      -5.099  20.450  18.858  1.00 99.13           C  
ANISOU  911  CA  THR A 154    12347  12802  12518    676   -180    -43       C  
ATOM    912  C   THR A 154      -4.929  21.341  20.079  1.00100.84           C  
ANISOU  912  C   THR A 154    12589  12954  12770    733   -209    -46       C  
ATOM    913  O   THR A 154      -4.892  20.850  21.213  1.00 99.66           O  
ANISOU  913  O   THR A 154    12466  12778  12623    727   -191    -77       O  
ATOM    914  CB  THR A 154      -6.577  20.100  18.645  1.00110.12           C  
ANISOU  914  CB  THR A 154    13689  14297  13854    663   -159    -74       C  
ATOM    915  OG1 THR A 154      -7.334  21.307  18.458  1.00121.20           O  
ANISOU  915  OG1 THR A 154    15054  15736  15260    724   -196    -56       O  
ATOM    916  CG2 THR A 154      -7.152  19.281  19.791  1.00103.82           C  
ANISOU  916  CG2 THR A 154    12906  13511  13029    643   -127   -126       C  
ATOM    917  N   LYS A 155      -4.794  22.647  19.834  1.00100.38           N  
ANISOU  917  N   LYS A 155    12528  12870  12740    785   -251    -12       N  
ATOM    918  CA  LYS A 155      -4.706  23.615  20.919  1.00 94.89           C  
ANISOU  918  CA  LYS A 155    11860  12116  12078    838   -276    -14       C  
ATOM    919  C   LYS A 155      -5.964  23.644  21.772  1.00 94.23           C  
ANISOU  919  C   LYS A 155    11755  12076  11972    865   -268    -54       C  
ATOM    920  O   LYS A 155      -5.905  24.079  22.929  1.00 93.08           O  
ANISOU  920  O   LYS A 155    11635  11882  11848    894   -276    -70       O  
ATOM    921  CB  LYS A 155      -4.430  25.014  20.365  1.00 87.04           C  
ANISOU  921  CB  LYS A 155    10872  11089  11110    886   -318     30       C  
ATOM    922  CG  LYS A 155      -2.963  25.311  20.227  1.00 86.25           C  
ANISOU  922  CG  LYS A 155    10815  10913  11043    870   -334     62       C  
ATOM    923  CD  LYS A 155      -2.708  26.655  19.578  1.00 91.30           C  
ANISOU  923  CD  LYS A 155    11467  11522  11702    908   -373    105       C  
ATOM    924  CE  LYS A 155      -1.674  26.494  18.468  1.00 90.44           C  
ANISOU  924  CE  LYS A 155    11362  11404  11597    868   -382    140       C  
ATOM    925  NZ  LYS A 155      -1.088  27.787  18.029  1.00 92.18           N  
ANISOU  925  NZ  LYS A 155    11612  11574  11839    894   -420    181       N  
ATOM    926  N   SER A 156      -7.100  23.215  21.218  1.00 86.35           N  
ANISOU  926  N   SER A 156    10707  11174  10928    854   -252    -70       N  
ATOM    927  CA  SER A 156      -8.334  23.192  21.990  1.00 81.37           C  
ANISOU  927  CA  SER A 156    10049  10598  10268    877   -243   -110       C  
ATOM    928  C   SER A 156      -8.304  22.098  23.040  1.00 79.77           C  
ANISOU  928  C   SER A 156     9870  10386  10053    831   -210   -158       C  
ATOM    929  O   SER A 156      -8.795  22.290  24.156  1.00 84.98           O  
ANISOU  929  O   SER A 156    10535  11040  10714    855   -212   -189       O  
ATOM    930  CB  SER A 156      -9.528  23.007  21.059  1.00 85.88           C  
ANISOU  930  CB  SER A 156    10557  11289  10786    872   -234   -113       C  
ATOM    931  OG  SER A 156     -10.704  22.739  21.798  1.00 91.93           O  
ANISOU  931  OG  SER A 156    11294  12123  11512    878   -219   -159       O  
ATOM    932  N   HIS A 157      -7.740  20.945  22.697  1.00 82.99           N  
ANISOU  932  N   HIS A 157    10295  10790  10446    766   -179   -163       N  
ATOM    933  CA  HIS A 157      -7.526  19.907  23.688  1.00 90.83           C  
ANISOU  933  CA  HIS A 157    11323  11759  11431    725   -146   -201       C  
ATOM    934  C   HIS A 157      -6.506  20.366  24.724  1.00 92.43           C  
ANISOU  934  C   HIS A 157    11572  11862  11686    751   -165   -191       C  
ATOM    935  O   HIS A 157      -6.688  20.138  25.924  1.00 84.48           O  
ANISOU  935  O   HIS A 157    10582  10836  10679    751   -156   -223       O  
ATOM    936  CB  HIS A 157      -7.096  18.631  22.964  1.00 91.19           C  
ANISOU  936  CB  HIS A 157    11382  11817  11449    656   -106   -202       C  
ATOM    937  CG  HIS A 157      -6.746  17.494  23.860  1.00 94.28           C  
ANISOU  937  CG  HIS A 157    11818  12173  11831    615    -68   -234       C  
ATOM    938  ND1 HIS A 157      -7.675  16.878  24.674  1.00100.81           N  
ANISOU  938  ND1 HIS A 157    12644  13042  12619    592    -44   -284       N  
ATOM    939  CD2 HIS A 157      -5.574  16.848  24.062  1.00 93.24           C  
ANISOU  939  CD2 HIS A 157    11734  11972  11719    594    -50   -221       C  
ATOM    940  CE1 HIS A 157      -7.087  15.905  25.346  1.00102.13           C  
ANISOU  940  CE1 HIS A 157    12860  13161  12784    558    -12   -300       C  
ATOM    941  NE2 HIS A 157      -5.813  15.865  24.990  1.00 98.74           N  
ANISOU  941  NE2 HIS A 157    12461  12666  12391    562    -15   -261       N  
ATOM    942  N   ALA A 158      -5.442  21.034  24.269  1.00 86.39           N  
ANISOU  942  N   ALA A 158    10826  11038  10961    770   -190   -146       N  
ATOM    943  CA  ALA A 158      -4.399  21.513  25.167  1.00 77.41           C  
ANISOU  943  CA  ALA A 158     9731   9815   9867    788   -206   -133       C  
ATOM    944  C   ALA A 158      -4.962  22.407  26.270  1.00 78.47           C  
ANISOU  944  C   ALA A 158     9866   9932  10016    833   -226   -153       C  
ATOM    945  O   ALA A 158      -4.570  22.288  27.435  1.00 76.22           O  
ANISOU  945  O   ALA A 158     9610   9604   9747    829   -221   -170       O  
ATOM    946  CB  ALA A 158      -3.337  22.256  24.366  1.00 70.72           C  
ANISOU  946  CB  ALA A 158     8897   8923   9050    800   -234    -82       C  
ATOM    947  N   LEU A 159      -5.873  23.312  25.928  1.00 71.14           N  
ANISOU  947  N   LEU A 159     8908   9040   9083    878   -247   -150       N  
ATOM    948  CA  LEU A 159      -6.484  24.143  26.953  1.00 75.74           C  
ANISOU  948  CA  LEU A 159     9493   9609   9678    925   -261   -171       C  
ATOM    949  C   LEU A 159      -7.557  23.399  27.748  1.00 82.49           C  
ANISOU  949  C   LEU A 159    10324  10522  10497    910   -238   -225       C  
ATOM    950  O   LEU A 159      -7.961  23.875  28.815  1.00 80.67           O  
ANISOU  950  O   LEU A 159    10099  10275  10276    937   -244   -251       O  
ATOM    951  CB  LEU A 159      -7.070  25.406  26.316  1.00 80.13           C  
ANISOU  951  CB  LEU A 159    10028  10178  10238    988   -289   -146       C  
ATOM    952  CG  LEU A 159      -6.119  26.297  25.522  1.00 83.33           C  
ANISOU  952  CG  LEU A 159    10460  10527  10675   1006   -315    -93       C  
ATOM    953  CD1 LEU A 159      -6.908  27.137  24.534  1.00 88.31           C  
ANISOU  953  CD1 LEU A 159    11058  11201  11293   1058   -334    -67       C  
ATOM    954  CD2 LEU A 159      -5.318  27.183  26.446  1.00 87.41           C  
ANISOU  954  CD2 LEU A 159    11029  10952  11231   1025   -331    -86       C  
ATOM    955  N   LYS A 160      -8.030  22.250  27.254  1.00 86.73           N  
ANISOU  955  N   LYS A 160    10838  11125  10990    862   -209   -245       N  
ATOM    956  CA  LYS A 160      -8.906  21.393  28.051  1.00 86.11           C  
ANISOU  956  CA  LYS A 160    10747  11098  10872    832   -183   -299       C  
ATOM    957  C   LYS A 160      -8.115  20.680  29.140  1.00 83.02           C  
ANISOU  957  C   LYS A 160    10402  10644  10497    796   -165   -316       C  
ATOM    958  O   LYS A 160      -8.557  20.589  30.290  1.00 88.96           O  
ANISOU  958  O   LYS A 160    11159  11398  11246    796   -161   -354       O  
ATOM    959  CB  LYS A 160      -9.615  20.379  27.144  1.00 95.92           C  
ANISOU  959  CB  LYS A 160    11958  12432  12056    783   -153   -314       C  
ATOM    960  CG  LYS A 160     -10.076  19.081  27.833  1.00105.61           C  
ANISOU  960  CG  LYS A 160    13196  13693  13238    721   -113   -366       C  
ATOM    961  CD  LYS A 160     -10.217  17.912  26.832  1.00105.65           C  
ANISOU  961  CD  LYS A 160    13196  13754  13194    654    -74   -371       C  
ATOM    962  CE  LYS A 160     -10.855  16.657  27.455  1.00101.30           C  
ANISOU  962  CE  LYS A 160    12659  13245  12586    590    -32   -426       C  
ATOM    963  NZ  LYS A 160      -9.964  15.887  28.375  1.00 93.62           N  
ANISOU  963  NZ  LYS A 160    11747  12189  11633    562    -11   -435       N  
ATOM    964  N   VAL A 161      -6.939  20.163  28.787  1.00 77.59           N  
ANISOU  964  N   VAL A 161     9747   9906   9827    767   -155   -288       N  
ATOM    965  CA  VAL A 161      -6.089  19.479  29.750  1.00 72.64           C  
ANISOU  965  CA  VAL A 161     9163   9222   9213    739   -137   -296       C  
ATOM    966  C   VAL A 161      -5.609  20.451  30.816  1.00 77.54           C  
ANISOU  966  C   VAL A 161     9802   9783   9878    774   -164   -290       C  
ATOM    967  O   VAL A 161      -5.673  20.167  32.018  1.00 82.62           O  
ANISOU  967  O   VAL A 161    10460  10410  10522    763   -156   -320       O  
ATOM    968  CB  VAL A 161      -4.912  18.811  29.026  1.00 70.30           C  
ANISOU  968  CB  VAL A 161     8893   8892   8924    710   -121   -261       C  
ATOM    969  CG1 VAL A 161      -3.875  18.368  30.030  1.00 74.88           C  
ANISOU  969  CG1 VAL A 161     9516   9410   9525    698   -111   -257       C  
ATOM    970  CG2 VAL A 161      -5.420  17.633  28.213  1.00 72.04           C  
ANISOU  970  CG2 VAL A 161     9107   9170   9097    662    -83   -277       C  
ATOM    971  N   ILE A 162      -5.140  21.622  30.390  1.00 72.53           N  
ANISOU  971  N   ILE A 162     9169   9113   9276    814   -196   -253       N  
ATOM    972  CA  ILE A 162      -4.673  22.640  31.325  1.00 70.65           C  
ANISOU  972  CA  ILE A 162     8953   8815   9075    843   -219   -247       C  
ATOM    973  C   ILE A 162      -5.778  23.017  32.310  1.00 84.63           C  
ANISOU  973  C   ILE A 162    10708  10608  10839    865   -222   -291       C  
ATOM    974  O   ILE A 162      -5.550  23.097  33.525  1.00 87.89           O  
ANISOU  974  O   ILE A 162    11140  10987  11267    859   -220   -310       O  
ATOM    975  CB  ILE A 162      -4.139  23.851  30.547  1.00 66.32           C  
ANISOU  975  CB  ILE A 162     8412   8231   8554    878   -249   -202       C  
ATOM    976  CG1 ILE A 162      -2.808  23.453  29.904  1.00 73.94           C  
ANISOU  976  CG1 ILE A 162     9399   9166   9529    848   -246   -163       C  
ATOM    977  CG2 ILE A 162      -3.961  25.062  31.433  1.00 55.71           C  
ANISOU  977  CG2 ILE A 162     7093   6835   7241    911   -269   -202       C  
ATOM    978  CD1 ILE A 162      -2.199  24.513  29.026  1.00 78.16           C  
ANISOU  978  CD1 ILE A 162     9944   9670  10084    871   -275   -118       C  
ATOM    979  N   ALA A 163      -6.999  23.217  31.813  1.00 84.66           N  
ANISOU  979  N   ALA A 163    10672  10676  10816    890   -225   -308       N  
ATOM    980  CA  ALA A 163      -8.107  23.515  32.715  1.00 84.22           C  
ANISOU  980  CA  ALA A 163    10597  10653  10748    913   -226   -352       C  
ATOM    981  C   ALA A 163      -8.369  22.355  33.676  1.00 81.16           C  
ANISOU  981  C   ALA A 163    10212  10288  10336    862   -200   -398       C  
ATOM    982  O   ALA A 163      -8.599  22.573  34.873  1.00 87.86           O  
ANISOU  982  O   ALA A 163    11068  11122  11194    866   -202   -429       O  
ATOM    983  CB  ALA A 163      -9.369  23.852  31.916  1.00 80.57           C  
ANISOU  983  CB  ALA A 163    10086  10273  10254    950   -232   -359       C  
ATOM    984  N   ALA A 164      -8.336  21.115  33.179  1.00 70.05           N  
ANISOU  984  N   ALA A 164     8804   8915   8895    812   -173   -404       N  
ATOM    985  CA  ALA A 164      -8.596  19.979  34.059  1.00 67.86           C  
ANISOU  985  CA  ALA A 164     8539   8656   8590    762   -145   -447       C  
ATOM    986  C   ALA A 164      -7.464  19.768  35.058  1.00 71.59           C  
ANISOU  986  C   ALA A 164     9054   9052   9095    744   -142   -438       C  
ATOM    987  O   ALA A 164      -7.669  19.163  36.116  1.00 76.99           O  
ANISOU  987  O   ALA A 164     9748   9738   9765    715   -127   -473       O  
ATOM    988  CB  ALA A 164      -8.800  18.703  33.248  1.00 59.50           C  
ANISOU  988  CB  ALA A 164     7478   7645   7483    710   -112   -454       C  
ATOM    989  N   THR A 165      -6.267  20.248  34.745  1.00 65.17           N  
ANISOU  989  N   THR A 165     8263   8178   8320    758   -155   -390       N  
ATOM    990  CA  THR A 165      -5.169  20.111  35.690  1.00 59.64           C  
ANISOU  990  CA  THR A 165     7598   7417   7646    743   -152   -377       C  
ATOM    991  C   THR A 165      -5.329  21.088  36.847  1.00 61.72           C  
ANISOU  991  C   THR A 165     7862   7655   7936    765   -172   -395       C  
ATOM    992  O   THR A 165      -5.214  20.699  38.011  1.00 64.16           O  
ANISOU  992  O   THR A 165     8182   7950   8244    741   -162   -418       O  
ATOM    993  CB  THR A 165      -3.836  20.313  34.980  1.00 56.78           C  
ANISOU  993  CB  THR A 165     7256   7009   7309    747   -159   -322       C  
ATOM    994  OG1 THR A 165      -3.693  19.316  33.960  1.00 66.04           O  
ANISOU  994  OG1 THR A 165     8431   8206   8456    723   -136   -309       O  
ATOM    995  CG2 THR A 165      -2.697  20.158  35.954  1.00 54.78           C  
ANISOU  995  CG2 THR A 165     7032   6708   7075    731   -155   -307       C  
ATOM    996  N   TRP A 166      -5.630  22.355  36.550  1.00 62.96           N  
ANISOU  996  N   TRP A 166     8007   7802   8112    811   -198   -386       N  
ATOM    997  CA  TRP A 166      -5.770  23.345  37.612  1.00 67.79           C  
ANISOU  997  CA  TRP A 166     8624   8383   8748    832   -212   -403       C  
ATOM    998  C   TRP A 166      -6.980  23.049  38.486  1.00 81.77           C  
ANISOU  998  C   TRP A 166    10372  10200  10496    827   -204   -460       C  
ATOM    999  O   TRP A 166      -6.924  23.201  39.710  1.00 90.57           O  
ANISOU  999  O   TRP A 166    11497  11294  11623    815   -204   -485       O  
ATOM   1000  CB  TRP A 166      -5.872  24.746  37.010  1.00 72.42           C  
ANISOU 1000  CB  TRP A 166     9213   8948   9358    886   -237   -378       C  
ATOM   1001  CG  TRP A 166      -4.561  25.251  36.487  1.00 77.55           C  
ANISOU 1001  CG  TRP A 166     9894   9540  10032    885   -248   -326       C  
ATOM   1002  CD1 TRP A 166      -3.965  24.913  35.304  1.00 70.94           C  
ANISOU 1002  CD1 TRP A 166     9057   8706   9190    877   -248   -288       C  
ATOM   1003  CD2 TRP A 166      -3.672  26.172  37.133  1.00 77.16           C  
ANISOU 1003  CD2 TRP A 166     9878   9426  10011    884   -258   -309       C  
ATOM   1004  NE1 TRP A 166      -2.763  25.561  35.177  1.00 65.69           N  
ANISOU 1004  NE1 TRP A 166     8423   7987   8548    874   -261   -248       N  
ATOM   1005  CE2 TRP A 166      -2.564  26.349  36.282  1.00 72.20           C  
ANISOU 1005  CE2 TRP A 166     9270   8770   9392    876   -266   -260       C  
ATOM   1006  CE3 TRP A 166      -3.705  26.860  38.344  1.00 74.72           C  
ANISOU 1006  CE3 TRP A 166     9586   9085   9718    885   -259   -332       C  
ATOM   1007  CZ2 TRP A 166      -1.499  27.190  36.607  1.00 67.65           C  
ANISOU 1007  CZ2 TRP A 166     8730   8139   8836    866   -275   -233       C  
ATOM   1008  CZ3 TRP A 166      -2.650  27.697  38.661  1.00 76.56           C  
ANISOU 1008  CZ3 TRP A 166     9856   9260   9972    874   -266   -305       C  
ATOM   1009  CH2 TRP A 166      -1.563  27.854  37.797  1.00 73.38           C  
ANISOU 1009  CH2 TRP A 166     9474   8834   9573    863   -274   -256       C  
ATOM   1010  N   CYS A 167      -8.086  22.625  37.875  1.00 84.81           N  
ANISOU 1010  N   CYS A 167    10723  10656  10844    833   -198   -484       N  
ATOM   1011  CA  CYS A 167      -9.298  22.367  38.641  1.00 79.66           C  
ANISOU 1011  CA  CYS A 167    10044  10060  10162    827   -192   -541       C  
ATOM   1012  C   CYS A 167      -9.130  21.158  39.545  1.00 75.09           C  
ANISOU 1012  C   CYS A 167     9482   9485   9564    765   -169   -570       C  
ATOM   1013  O   CYS A 167      -9.518  21.197  40.716  1.00 76.45           O  
ANISOU 1013  O   CYS A 167     9651   9660   9736    753   -169   -609       O  
ATOM   1014  CB  CYS A 167     -10.482  22.170  37.696  1.00 87.12           C  
ANISOU 1014  CB  CYS A 167    10947  11092  11063    842   -189   -556       C  
ATOM   1015  SG  CYS A 167     -10.913  23.677  36.799  1.00 99.96           S  
ANISOU 1015  SG  CYS A 167    12550  12723  12706    926   -216   -525       S  
ATOM   1016  N   LEU A 168      -8.573  20.068  39.022  1.00 67.37           N  
ANISOU 1016  N   LEU A 168     8523   8507   8570    726   -148   -552       N  
ATOM   1017  CA  LEU A 168      -8.365  18.898  39.864  1.00 68.65           C  
ANISOU 1017  CA  LEU A 168     8707   8665   8711    671   -123   -576       C  
ATOM   1018  C   LEU A 168      -7.265  19.133  40.897  1.00 71.71           C  
ANISOU 1018  C   LEU A 168     9124   8985   9139    665   -128   -557       C  
ATOM   1019  O   LEU A 168      -7.286  18.525  41.973  1.00 65.38           O  
ANISOU 1019  O   LEU A 168     8334   8181   8327    630   -116   -584       O  
ATOM   1020  CB  LEU A 168      -8.028  17.686  39.006  1.00 65.57           C  
ANISOU 1020  CB  LEU A 168     8336   8285   8291    636    -93   -559       C  
ATOM   1021  CG  LEU A 168      -9.228  17.242  38.189  1.00 81.80           C  
ANISOU 1021  CG  LEU A 168    10364  10422  10294    622    -80   -589       C  
ATOM   1022  CD1 LEU A 168      -8.799  16.258  37.106  1.00 87.63           C  
ANISOU 1022  CD1 LEU A 168    11124  11164  11008    592    -51   -565       C  
ATOM   1023  CD2 LEU A 168     -10.288  16.642  39.091  1.00 88.41           C  
ANISOU 1023  CD2 LEU A 168    11193  11312  11087    585    -67   -651       C  
ATOM   1024  N   SER A 169      -6.282  19.979  40.582  1.00 71.33           N  
ANISOU 1024  N   SER A 169     9088   8885   9131    693   -145   -510       N  
ATOM   1025  CA  SER A 169      -5.183  20.200  41.513  1.00 63.11           C  
ANISOU 1025  CA  SER A 169     8070   7790   8119    682   -148   -490       C  
ATOM   1026  C   SER A 169      -5.645  21.001  42.716  1.00 61.18           C  
ANISOU 1026  C   SER A 169     7817   7539   7892    687   -161   -524       C  
ATOM   1027  O   SER A 169      -5.224  20.731  43.844  1.00 59.33           O  
ANISOU 1027  O   SER A 169     7593   7286   7662    656   -155   -534       O  
ATOM   1028  CB  SER A 169      -4.026  20.903  40.815  1.00 67.58           C  
ANISOU 1028  CB  SER A 169     8652   8312   8716    703   -162   -433       C  
ATOM   1029  OG  SER A 169      -3.288  19.979  40.046  1.00 73.33           O  
ANISOU 1029  OG  SER A 169     9393   9037   9430    688   -144   -400       O  
ATOM   1030  N   PHE A 170      -6.522  21.979  42.497  1.00 68.67           N  
ANISOU 1030  N   PHE A 170     8744   8503   8846    726   -178   -543       N  
ATOM   1031  CA  PHE A 170      -7.150  22.657  43.629  1.00 83.35           C  
ANISOU 1031  CA  PHE A 170    10593  10362  10715    732   -187   -584       C  
ATOM   1032  C   PHE A 170      -8.044  21.718  44.427  1.00 81.99           C  
ANISOU 1032  C   PHE A 170    10404  10241  10508    695   -173   -639       C  
ATOM   1033  O   PHE A 170      -8.197  21.900  45.641  1.00 86.16           O  
ANISOU 1033  O   PHE A 170    10931  10762  11044    677   -174   -671       O  
ATOM   1034  CB  PHE A 170      -7.956  23.868  43.152  1.00 80.35           C  
ANISOU 1034  CB  PHE A 170    10196   9990  10344    791   -204   -591       C  
ATOM   1035  CG  PHE A 170      -7.117  25.074  42.906  1.00 80.66           C  
ANISOU 1035  CG  PHE A 170    10262   9964  10421    821   -218   -550       C  
ATOM   1036  CD1 PHE A 170      -6.540  25.749  43.973  1.00 77.16           C  
ANISOU 1036  CD1 PHE A 170     9841   9471  10004    807   -219   -553       C  
ATOM   1037  CD2 PHE A 170      -6.883  25.525  41.619  1.00 80.09           C  
ANISOU 1037  CD2 PHE A 170    10195   9883  10355    857   -228   -509       C  
ATOM   1038  CE1 PHE A 170      -5.743  26.866  43.760  1.00 78.52           C  
ANISOU 1038  CE1 PHE A 170    10045   9584  10204    826   -228   -517       C  
ATOM   1039  CE2 PHE A 170      -6.088  26.642  41.395  1.00 85.82           C  
ANISOU 1039  CE2 PHE A 170    10952  10547  11111    878   -239   -471       C  
ATOM   1040  CZ  PHE A 170      -5.518  27.316  42.467  1.00 85.58           C  
ANISOU 1040  CZ  PHE A 170    10948  10466  11103    862   -238   -476       C  
ATOM   1041  N   THR A 171      -8.629  20.708  43.776  1.00 69.62           N  
ANISOU 1041  N   THR A 171     8826   8725   8900    678   -159   -653       N  
ATOM   1042  CA  THR A 171      -9.584  19.856  44.475  1.00 63.38           C  
ANISOU 1042  CA  THR A 171     8023   7990   8070    640   -146   -709       C  
ATOM   1043  C   THR A 171      -8.877  18.863  45.387  1.00 64.63           C  
ANISOU 1043  C   THR A 171     8211   8122   8224    585   -127   -710       C  
ATOM   1044  O   THR A 171      -9.124  18.838  46.597  1.00 74.30           O  
ANISOU 1044  O   THR A 171     9432   9349   9448    560   -129   -745       O  
ATOM   1045  CB  THR A 171     -10.474  19.133  43.472  1.00 68.94           C  
ANISOU 1045  CB  THR A 171     8708   8763   8722    632   -133   -725       C  
ATOM   1046  OG1 THR A 171     -11.410  20.069  42.912  1.00 78.32           O  
ANISOU 1046  OG1 THR A 171     9857   9994   9906    684   -151   -736       O  
ATOM   1047  CG2 THR A 171     -11.225  17.971  44.137  1.00 67.10           C  
ANISOU 1047  CG2 THR A 171     8475   8581   8437    574   -112   -778       C  
ATOM   1048  N   ILE A 172      -7.985  18.039  44.834  1.00 55.86           N  
ANISOU 1048  N   ILE A 172     7129   6986   7108    568   -109   -670       N  
ATOM   1049  CA  ILE A 172      -7.315  17.033  45.653  1.00 62.66           C  
ANISOU 1049  CA  ILE A 172     8021   7826   7961    524    -89   -666       C  
ATOM   1050  C   ILE A 172      -6.453  17.646  46.760  1.00 70.60           C  
ANISOU 1050  C   ILE A 172     9032   8786   9006    522   -101   -650       C  
ATOM   1051  O   ILE A 172      -6.056  16.933  47.686  1.00 72.02           O  
ANISOU 1051  O   ILE A 172     9230   8957   9179    486    -87   -654       O  
ATOM   1052  CB  ILE A 172      -6.424  16.110  44.801  1.00 68.92           C  
ANISOU 1052  CB  ILE A 172     8847   8597   8744    516    -65   -621       C  
ATOM   1053  CG1 ILE A 172      -5.266  16.915  44.214  1.00 74.78           C  
ANISOU 1053  CG1 ILE A 172     9592   9294   9529    554    -80   -561       C  
ATOM   1054  CG2 ILE A 172      -7.216  15.424  43.722  1.00 80.29           C  
ANISOU 1054  CG2 ILE A 172    10285  10081  10141    507    -47   -637       C  
ATOM   1055  CD1 ILE A 172      -4.185  16.065  43.635  1.00 79.40           C  
ANISOU 1055  CD1 ILE A 172    10209   9853  10109    548    -58   -513       C  
ATOM   1056  N   MET A 173      -6.120  18.933  46.673  1.00 70.29           N  
ANISOU 1056  N   MET A 173     8982   8720   9006    558   -124   -630       N  
ATOM   1057  CA  MET A 173      -5.265  19.590  47.654  1.00 61.67           C  
ANISOU 1057  CA  MET A 173     7897   7589   7947    549   -133   -614       C  
ATOM   1058  C   MET A 173      -6.054  20.251  48.798  1.00 63.38           C  
ANISOU 1058  C   MET A 173     8094   7817   8171    540   -144   -665       C  
ATOM   1059  O   MET A 173      -5.441  20.786  49.729  1.00 67.19           O  
ANISOU 1059  O   MET A 173     8580   8271   8676    524   -148   -659       O  
ATOM   1060  CB  MET A 173      -4.367  20.627  46.951  1.00 50.19           C  
ANISOU 1060  CB  MET A 173     6451   6095   6525    584   -147   -564       C  
ATOM   1061  CG  MET A 173      -2.979  20.141  46.466  1.00 50.53           C  
ANISOU 1061  CG  MET A 173     6516   6113   6572    578   -138   -503       C  
ATOM   1062  SD  MET A 173      -2.637  18.425  46.866  1.00 60.49           S  
ANISOU 1062  SD  MET A 173     7794   7389   7800    540   -107   -499       S  
ATOM   1063  CE  MET A 173      -1.361  17.927  45.714  1.00 59.05           C  
ANISOU 1063  CE  MET A 173     7632   7187   7616    557    -96   -431       C  
ATOM   1064  N   THR A 174      -7.394  20.203  48.772  1.00 57.11           N  
ANISOU 1064  N   THR A 174     7277   7069   7354    547   -147   -717       N  
ATOM   1065  CA  THR A 174      -8.222  20.869  49.779  1.00 62.31           C  
ANISOU 1065  CA  THR A 174     7914   7743   8018    544   -157   -769       C  
ATOM   1066  C   THR A 174      -7.966  20.395  51.202  1.00 70.79           C  
ANISOU 1066  C   THR A 174     8992   8813   9090    490   -150   -791       C  
ATOM   1067  O   THR A 174      -8.339  21.111  52.135  1.00 85.72           O  
ANISOU 1067  O   THR A 174    10869  10704  10996    484   -159   -825       O  
ATOM   1068  CB  THR A 174      -9.718  20.696  49.505  1.00 57.31           C  
ANISOU 1068  CB  THR A 174     7251   7176   7349    556   -160   -822       C  
ATOM   1069  OG1 THR A 174      -9.984  19.328  49.200  1.00 58.88           O  
ANISOU 1069  OG1 THR A 174     7456   7412   7502    519   -141   -833       O  
ATOM   1070  CG2 THR A 174     -10.175  21.575  48.379  1.00 56.62           C  
ANISOU 1070  CG2 THR A 174     7148   7097   7267    619   -172   -809       C  
ATOM   1071  N   PRO A 175      -7.426  19.194  51.432  1.00 66.29           N  
ANISOU 1071  N   PRO A 175     8441   8244   8500    449   -133   -776       N  
ATOM   1072  CA  PRO A 175      -6.924  18.887  52.780  1.00 63.68           C  
ANISOU 1072  CA  PRO A 175     8117   7904   8176    402   -127   -782       C  
ATOM   1073  C   PRO A 175      -5.962  19.916  53.349  1.00 64.91           C  
ANISOU 1073  C   PRO A 175     8274   8018   8370    404   -136   -752       C  
ATOM   1074  O   PRO A 175      -6.002  20.184  54.556  1.00 68.56           O  
ANISOU 1074  O   PRO A 175     8726   8481   8841    370   -138   -778       O  
ATOM   1075  CB  PRO A 175      -6.253  17.529  52.576  1.00 61.36           C  
ANISOU 1075  CB  PRO A 175     7851   7606   7856    378   -105   -750       C  
ATOM   1076  CG  PRO A 175      -7.146  16.873  51.613  1.00 64.95           C  
ANISOU 1076  CG  PRO A 175     8309   8094   8275    387    -96   -771       C  
ATOM   1077  CD  PRO A 175      -7.650  17.948  50.678  1.00 65.30           C  
ANISOU 1077  CD  PRO A 175     8331   8145   8336    437   -114   -773       C  
ATOM   1078  N   TYR A 176      -5.110  20.515  52.529  1.00 61.47           N  
ANISOU 1078  N   TYR A 176     7850   7548   7957    436   -140   -701       N  
ATOM   1079  CA  TYR A 176      -4.138  21.441  53.099  1.00 59.61           C  
ANISOU 1079  CA  TYR A 176     7620   7278   7750    427   -145   -673       C  
ATOM   1080  C   TYR A 176      -4.817  22.622  53.774  1.00 59.81           C  
ANISOU 1080  C   TYR A 176     7633   7296   7795    430   -155   -717       C  
ATOM   1081  O   TYR A 176      -4.536  22.858  54.959  1.00 72.61           O  
ANISOU 1081  O   TYR A 176     9250   8914   9424    388   -152   -730       O  
ATOM   1082  CB  TYR A 176      -3.093  21.844  52.046  1.00 52.47           C  
ANISOU 1082  CB  TYR A 176     6734   6343   6859    456   -147   -611       C  
ATOM   1083  CG  TYR A 176      -2.068  20.758  51.832  1.00 54.08           C  
ANISOU 1083  CG  TYR A 176     6950   6552   7047    442   -133   -562       C  
ATOM   1084  CD1 TYR A 176      -1.200  20.385  52.858  1.00 48.49           C  
ANISOU 1084  CD1 TYR A 176     6242   5847   6334    402   -123   -543       C  
ATOM   1085  CD2 TYR A 176      -1.976  20.085  50.606  1.00 63.59           C  
ANISOU 1085  CD2 TYR A 176     8166   7758   8238    469   -127   -536       C  
ATOM   1086  CE1 TYR A 176      -0.263  19.397  52.693  1.00 47.74           C  
ANISOU 1086  CE1 TYR A 176     6158   5759   6222    397   -108   -496       C  
ATOM   1087  CE2 TYR A 176      -1.032  19.066  50.424  1.00 65.33           C  
ANISOU 1087  CE2 TYR A 176     8401   7980   8442    461   -110   -492       C  
ATOM   1088  CZ  TYR A 176      -0.191  18.722  51.483  1.00 66.05           C  
ANISOU 1088  CZ  TYR A 176     8492   8075   8529    428   -101   -472       C  
ATOM   1089  OH  TYR A 176       0.736  17.720  51.333  1.00 68.52           O  
ANISOU 1089  OH  TYR A 176     8820   8392   8824    429    -82   -425       O  
ATOM   1090  N   PRO A 177      -5.740  23.350  53.147  1.00 61.43           N  
ANISOU 1090  N   PRO A 177     7831   7502   8006    476   -165   -741       N  
ATOM   1091  CA  PRO A 177      -6.423  24.419  53.895  1.00 66.50           C  
ANISOU 1091  CA  PRO A 177     8465   8137   8665    482   -170   -786       C  
ATOM   1092  C   PRO A 177      -7.321  23.907  55.008  1.00 75.42           C  
ANISOU 1092  C   PRO A 177     9570   9308   9778    445   -169   -847       C  
ATOM   1093  O   PRO A 177      -7.535  24.629  55.994  1.00 75.28           O  
ANISOU 1093  O   PRO A 177     9547   9282   9776    428   -168   -880       O  
ATOM   1094  CB  PRO A 177      -7.243  25.151  52.824  1.00 55.82           C  
ANISOU 1094  CB  PRO A 177     7109   6783   7315    550   -180   -792       C  
ATOM   1095  CG  PRO A 177      -7.434  24.140  51.766  1.00 70.50           C  
ANISOU 1095  CG  PRO A 177     8962   8676   9149    565   -180   -775       C  
ATOM   1096  CD  PRO A 177      -6.175  23.311  51.743  1.00 70.19           C  
ANISOU 1096  CD  PRO A 177     8941   8620   9108    527   -171   -728       C  
ATOM   1097  N   ILE A 178      -7.867  22.693  54.885  1.00 75.61           N  
ANISOU 1097  N   ILE A 178     9582   9378   9769    429   -166   -866       N  
ATOM   1098  CA  ILE A 178      -8.808  22.232  55.901  1.00 73.78           C  
ANISOU 1098  CA  ILE A 178     9327   9189   9516    392   -165   -929       C  
ATOM   1099  C   ILE A 178      -8.077  21.899  57.198  1.00 69.50           C  
ANISOU 1099  C   ILE A 178     8789   8638   8980    328   -158   -927       C  
ATOM   1100  O   ILE A 178      -8.577  22.170  58.292  1.00 61.70           O  
ANISOU 1100  O   ILE A 178     7784   7665   7995    296   -161   -974       O  
ATOM   1101  CB  ILE A 178      -9.618  21.029  55.389  1.00 69.09           C  
ANISOU 1101  CB  ILE A 178     8725   8650   8878    385   -161   -952       C  
ATOM   1102  CG1 ILE A 178     -10.526  21.450  54.246  1.00 72.77           C  
ANISOU 1102  CG1 ILE A 178     9175   9141   9331    444   -169   -963       C  
ATOM   1103  CG2 ILE A 178     -10.499  20.483  56.481  1.00 65.19           C  
ANISOU 1103  CG2 ILE A 178     8211   8202   8356    336   -161  -1016       C  
ATOM   1104  CD1 ILE A 178     -11.278  20.277  53.637  1.00 68.49           C  
ANISOU 1104  CD1 ILE A 178     8627   8657   8738    431   -161   -983       C  
ATOM   1105  N   TYR A 179      -6.878  21.325  57.103  1.00 62.07           N  
ANISOU 1105  N   TYR A 179     7868   7675   8040    308   -149   -871       N  
ATOM   1106  CA  TYR A 179      -6.211  20.754  58.263  1.00 58.31           C  
ANISOU 1106  CA  TYR A 179     7392   7203   7560    248   -140   -864       C  
ATOM   1107  C   TYR A 179      -4.895  21.442  58.604  1.00 65.95           C  
ANISOU 1107  C   TYR A 179     8368   8136   8553    235   -137   -814       C  
ATOM   1108  O   TYR A 179      -4.092  20.876  59.350  1.00 77.22           O  
ANISOU 1108  O   TYR A 179     9796   9571   9973    192   -128   -789       O  
ATOM   1109  CB  TYR A 179      -5.969  19.261  58.046  1.00 55.11           C  
ANISOU 1109  CB  TYR A 179     7002   6815   7121    231   -128   -843       C  
ATOM   1110  CG  TYR A 179      -7.217  18.417  58.071  1.00 69.57           C  
ANISOU 1110  CG  TYR A 179     8828   8689   8917    217   -126   -899       C  
ATOM   1111  CD1 TYR A 179      -7.807  18.049  59.274  1.00 70.91           C  
ANISOU 1111  CD1 TYR A 179     8984   8889   9071    164   -127   -950       C  
ATOM   1112  CD2 TYR A 179      -7.787  17.958  56.893  1.00 70.35           C  
ANISOU 1112  CD2 TYR A 179     8935   8802   8992    249   -123   -902       C  
ATOM   1113  CE1 TYR A 179      -8.935  17.262  59.304  1.00 70.52           C  
ANISOU 1113  CE1 TYR A 179     8931   8883   8980    144   -125  -1003       C  
ATOM   1114  CE2 TYR A 179      -8.916  17.170  56.909  1.00 67.64           C  
ANISOU 1114  CE2 TYR A 179     8587   8505   8606    228   -119   -954       C  
ATOM   1115  CZ  TYR A 179      -9.492  16.824  58.112  1.00 69.87           C  
ANISOU 1115  CZ  TYR A 179     8858   8818   8871    175   -120  -1005       C  
ATOM   1116  OH  TYR A 179     -10.625  16.036  58.143  1.00 72.03           O  
ANISOU 1116  OH  TYR A 179     9130   9143   9095    146   -116  -1060       O  
ATOM   1117  N   SER A 180      -4.649  22.637  58.086  1.00 57.23           N  
ANISOU 1117  N   SER A 180     7273   6999   7474    268   -142   -799       N  
ATOM   1118  CA  SER A 180      -3.462  23.396  58.440  1.00 54.29           C  
ANISOU 1118  CA  SER A 180     6910   6599   7119    246   -137   -758       C  
ATOM   1119  C   SER A 180      -3.862  24.480  59.425  1.00 65.15           C  
ANISOU 1119  C   SER A 180     8279   7963   8512    220   -136   -803       C  
ATOM   1120  O   SER A 180      -4.807  25.238  59.171  1.00 59.88           O  
ANISOU 1120  O   SER A 180     7612   7282   7856    257   -142   -842       O  
ATOM   1121  CB  SER A 180      -2.780  24.007  57.210  1.00 52.02           C  
ANISOU 1121  CB  SER A 180     6646   6278   6843    291   -140   -708       C  
ATOM   1122  OG  SER A 180      -2.235  22.968  56.394  1.00 59.60           O  
ANISOU 1122  OG  SER A 180     7612   7248   7785    307   -137   -662       O  
ATOM   1123  N   ASN A 181      -3.144  24.538  60.550  1.00 65.09           N  
ANISOU 1123  N   ASN A 181     8264   7964   8504    159   -127   -795       N  
ATOM   1124  CA  ASN A 181      -3.463  25.464  61.620  1.00 72.85           C  
ANISOU 1124  CA  ASN A 181     9240   8938   9500    121   -122   -839       C  
ATOM   1125  C   ASN A 181      -2.181  25.992  62.227  1.00 67.02           C  
ANISOU 1125  C   ASN A 181     8510   8193   8764     68   -109   -800       C  
ATOM   1126  O   ASN A 181      -1.128  25.356  62.152  1.00 67.51           O  
ANISOU 1126  O   ASN A 181     8568   8273   8809     49   -105   -746       O  
ATOM   1127  CB  ASN A 181      -4.315  24.804  62.711  1.00 76.53           C  
ANISOU 1127  CB  ASN A 181     9677   9444   9956     81   -124   -896       C  
ATOM   1128  CG  ASN A 181      -5.671  24.374  62.203  1.00 76.18           C  
ANISOU 1128  CG  ASN A 181     9623   9418   9903    124   -136   -943       C  
ATOM   1129  OD1 ASN A 181      -6.585  25.198  62.089  1.00 77.75           O  
ANISOU 1129  OD1 ASN A 181     9820   9607  10114    158   -140   -986       O  
ATOM   1130  ND2 ASN A 181      -5.808  23.082  61.868  1.00 72.51           N  
ANISOU 1130  ND2 ASN A 181     9154   8984   9413    126   -139   -933       N  
ATOM   1131  N   LEU A 182      -2.283  27.183  62.815  1.00 63.51           N  
ANISOU 1131  N   LEU A 182     8075   7722   8334     44    -99   -829       N  
ATOM   1132  CA  LEU A 182      -1.250  27.638  63.735  1.00 62.07           C  
ANISOU 1132  CA  LEU A 182     7892   7546   8146    -30    -83   -808       C  
ATOM   1133  C   LEU A 182      -1.122  26.635  64.868  1.00 61.32           C  
ANISOU 1133  C   LEU A 182     7760   7506   8034    -90    -81   -815       C  
ATOM   1134  O   LEU A 182      -2.117  26.190  65.429  1.00 62.36           O  
ANISOU 1134  O   LEU A 182     7871   7656   8168    -96    -88   -867       O  
ATOM   1135  CB  LEU A 182      -1.582  29.026  64.280  1.00 60.49           C  
ANISOU 1135  CB  LEU A 182     7713   7308   7963    -51    -68   -850       C  
ATOM   1136  CG  LEU A 182      -1.497  30.113  63.208  1.00 65.36           C  
ANISOU 1136  CG  LEU A 182     8376   7865   8591      3    -64   -834       C  
ATOM   1137  CD1 LEU A 182      -1.280  31.488  63.793  1.00 69.50           C  
ANISOU 1137  CD1 LEU A 182     8934   8348   9122    -37    -40   -854       C  
ATOM   1138  CD2 LEU A 182      -0.390  29.787  62.205  1.00 60.00           C  
ANISOU 1138  CD2 LEU A 182     7710   7190   7899     20    -70   -762       C  
ATOM   1139  N   VAL A 183       0.100  26.221  65.157  1.00 55.19           N  
ANISOU 1139  N   VAL A 183     6973   6761   7238   -132    -74   -760       N  
ATOM   1140  CA  VAL A 183       0.357  25.340  66.287  1.00 59.68           C  
ANISOU 1140  CA  VAL A 183     7506   7381   7787   -191    -70   -757       C  
ATOM   1141  C   VAL A 183       1.228  26.113  67.275  1.00 67.89           C  
ANISOU 1141  C   VAL A 183     8537   8440   8818   -271    -52   -746       C  
ATOM   1142  O   VAL A 183       2.411  26.358  66.994  1.00 64.74           O  
ANISOU 1142  O   VAL A 183     8144   8053   8402   -285    -43   -688       O  
ATOM   1143  CB  VAL A 183       1.017  24.023  65.864  1.00 57.27           C  
ANISOU 1143  CB  VAL A 183     7193   7108   7459   -169    -74   -699       C  
ATOM   1144  CG1 VAL A 183       1.618  23.325  67.080  1.00 54.72           C  
ANISOU 1144  CG1 VAL A 183     6836   6841   7112   -235    -66   -680       C  
ATOM   1145  CG2 VAL A 183      -0.009  23.121  65.178  1.00 57.52           C  
ANISOU 1145  CG2 VAL A 183     7231   7130   7493   -112    -88   -724       C  
ATOM   1146  N   PRO A 184       0.694  26.511  68.431  1.00 78.77           N  
ANISOU 1146  N   PRO A 184     9899   9828  10203   -329    -44   -800       N  
ATOM   1147  CA  PRO A 184       1.480  27.324  69.366  1.00 79.64           C  
ANISOU 1147  CA  PRO A 184    10002   9956  10302   -412    -23   -793       C  
ATOM   1148  C   PRO A 184       2.583  26.507  70.008  1.00 80.38           C  
ANISOU 1148  C   PRO A 184    10059  10119  10362   -465    -17   -737       C  
ATOM   1149  O   PRO A 184       2.389  25.343  70.368  1.00 88.90           O  
ANISOU 1149  O   PRO A 184    11111  11234  11431   -463    -28   -732       O  
ATOM   1150  CB  PRO A 184       0.453  27.775  70.412  1.00 70.93           C  
ANISOU 1150  CB  PRO A 184     8889   8846   9216   -454    -18   -872       C  
ATOM   1151  CG  PRO A 184      -0.831  27.058  70.095  1.00 74.01           C  
ANISOU 1151  CG  PRO A 184     9272   9227   9621   -395    -40   -916       C  
ATOM   1152  CD  PRO A 184      -0.557  26.023  69.038  1.00 77.06           C  
ANISOU 1152  CD  PRO A 184     9664   9620   9997   -331    -55   -865       C  
ATOM   1153  N   PHE A 185       3.752  27.128  70.133  1.00 74.11           N  
ANISOU 1153  N   PHE A 185     9266   9347   9544   -512      0   -693       N  
ATOM   1154  CA  PHE A 185       4.870  26.585  70.890  1.00 78.78           C  
ANISOU 1154  CA  PHE A 185     9817  10017  10098   -574     10   -640       C  
ATOM   1155  C   PHE A 185       5.519  27.734  71.653  1.00 86.41           C  
ANISOU 1155  C   PHE A 185    10782  11003  11045   -666     36   -644       C  
ATOM   1156  O   PHE A 185       5.074  28.885  71.580  1.00 80.89           O  
ANISOU 1156  O   PHE A 185    10120  10248  10366   -679     48   -690       O  
ATOM   1157  CB  PHE A 185       5.872  25.851  69.990  1.00 78.99           C  
ANISOU 1157  CB  PHE A 185     9842  10072  10099   -523      4   -560       C  
ATOM   1158  CG  PHE A 185       6.614  26.751  69.035  1.00 85.79           C  
ANISOU 1158  CG  PHE A 185    10736  10909  10952   -508     11   -527       C  
ATOM   1159  CD1 PHE A 185       5.946  27.437  68.032  1.00 84.06           C  
ANISOU 1159  CD1 PHE A 185    10564  10612  10764   -450      3   -557       C  
ATOM   1160  CD2 PHE A 185       7.987  26.898  69.127  1.00 85.26           C  
ANISOU 1160  CD2 PHE A 185    10651  10903  10841   -550     24   -464       C  
ATOM   1161  CE1 PHE A 185       6.632  28.255  67.151  1.00 77.89           C  
ANISOU 1161  CE1 PHE A 185     9816   9806   9972   -438      9   -526       C  
ATOM   1162  CE2 PHE A 185       8.673  27.715  68.243  1.00 81.17           C  
ANISOU 1162  CE2 PHE A 185    10165  10366  10310   -542     30   -436       C  
ATOM   1163  CZ  PHE A 185       7.992  28.393  67.257  1.00 76.60           C  
ANISOU 1163  CZ  PHE A 185     9637   9702   9764   -487     22   -468       C  
ATOM   1164  N   THR A 186       6.565  27.419  72.411  1.00 99.44           N  
ANISOU 1164  N   THR A 186    12392  12736  12656   -733     49   -597       N  
ATOM   1165  CA  THR A 186       7.168  28.384  73.317  1.00105.98           C  
ANISOU 1165  CA  THR A 186    13211  13599  13458   -839     77   -604       C  
ATOM   1166  C   THR A 186       8.669  28.422  73.104  1.00101.01           C  
ANISOU 1166  C   THR A 186    12565  13039  12775   -869     90   -525       C  
ATOM   1167  O   THR A 186       9.314  27.379  72.952  1.00 93.99           O  
ANISOU 1167  O   THR A 186    11641  12209  11862   -838     79   -464       O  
ATOM   1168  CB  THR A 186       6.851  28.039  74.753  1.00113.81           C  
ANISOU 1168  CB  THR A 186    14157  14641  14446   -915     83   -635       C  
ATOM   1169  OG1 THR A 186       7.195  26.669  74.975  1.00123.50           O  
ANISOU 1169  OG1 THR A 186    15338  15931  15653   -894     68   -586       O  
ATOM   1170  CG2 THR A 186       5.362  28.240  75.016  1.00109.01           C  
ANISOU 1170  CG2 THR A 186    13566  13966  13885   -898     74   -721       C  
ATOM   1171  N   LYS A 187       9.191  29.648  73.041  1.00103.21           N  
ANISOU 1171  N   LYS A 187    12873  13308  13034   -926    114   -529       N  
ATOM   1172  CA  LYS A 187      10.611  29.896  72.691  1.00106.36           C  
ANISOU 1172  CA  LYS A 187    13264  13770  13377   -958    127   -460       C  
ATOM   1173  C   LYS A 187      11.525  29.980  73.913  1.00114.42           C  
ANISOU 1173  C   LYS A 187    14232  14901  14342  -1075    152   -435       C  
ATOM   1174  O   LYS A 187      11.144  29.508  74.991  1.00112.22           O  
ANISOU 1174  O   LYS A 187    13911  14657  14068  -1116    153   -456       O  
ATOM   1175  CB  LYS A 187      10.727  31.166  71.846  1.00101.24           C  
ANISOU 1175  CB  LYS A 187    12684  13053  12730   -958    140   -475       C  
ATOM   1176  CG  LYS A 187      10.957  30.939  70.361  1.00 94.20           C  
ANISOU 1176  CG  LYS A 187    11822  12125  11845   -860    119   -436       C  
ATOM   1177  CD  LYS A 187      10.187  31.913  69.511  1.00 92.00           C  
ANISOU 1177  CD  LYS A 187    11618  11733  11606   -816    118   -482       C  
ATOM   1178  CE  LYS A 187      10.998  32.495  68.378  1.00 96.71           C  
ANISOU 1178  CE  LYS A 187    12255  12314  12177   -798    120   -441       C  
ATOM   1179  NZ  LYS A 187      10.585  33.884  68.075  1.00 99.37           N  
ANISOU 1179  NZ  LYS A 187    12668  12561  12528   -815    140   -486       N  
ATOM   1180  N   ASN A 188      12.690  30.596  73.705  1.00115.07           N  
ANISOU 1180  N   ASN A 188    14317  15036  14368  -1128    172   -391       N  
ATOM   1181  CA  ASN A 188      13.764  30.702  74.689  1.00115.34           C  
ANISOU 1181  CA  ASN A 188    14297  15192  14333  -1239    197   -354       C  
ATOM   1182  C   ASN A 188      13.291  31.176  76.058  1.00114.02           C  
ANISOU 1182  C   ASN A 188    14115  15038  14170  -1345    221   -411       C  
ATOM   1183  O   ASN A 188      13.260  30.392  77.014  1.00104.82           O  
ANISOU 1183  O   ASN A 188    12888  13942  12998  -1372    217   -401       O  
ATOM   1184  CB  ASN A 188      14.850  31.650  74.175  1.00119.65           C  
ANISOU 1184  CB  ASN A 188    14870  15770  14822  -1293    220   -322       C  
ATOM   1185  CG  ASN A 188      15.481  31.172  72.875  1.00121.87           C  
ANISOU 1185  CG  ASN A 188    15158  16059  15090  -1200    197   -260       C  
ATOM   1186  OD1 ASN A 188      14.877  30.409  72.122  1.00123.28           O  
ANISOU 1186  OD1 ASN A 188    15347  16178  15318  -1087    167   -258       O  
ATOM   1187  ND2 ASN A 188      16.706  31.621  72.609  1.00121.29           N  
ANISOU 1187  ND2 ASN A 188    15076  16062  14946  -1253    213   -212       N  
ATOM   1188  N   ASN A 189      12.931  32.452  76.167  1.00121.75           N  
ANISOU 1188  N   ASN A 189    15152  15949  15158  -1404    248   -469       N  
ATOM   1189  CA  ASN A 189      12.521  33.020  77.449  1.00132.86           C  
ANISOU 1189  CA  ASN A 189    16550  17364  16566  -1512    277   -527       C  
ATOM   1190  C   ASN A 189      11.022  32.864  77.668  1.00132.17           C  
ANISOU 1190  C   ASN A 189    16482  17182  16554  -1459    261   -601       C  
ATOM   1191  O   ASN A 189      10.331  33.810  78.049  1.00140.28           O  
ANISOU 1191  O   ASN A 189    17553  18141  17605  -1502    284   -670       O  
ATOM   1192  CB  ASN A 189      12.945  34.483  77.539  1.00141.57           C  
ANISOU 1192  CB  ASN A 189    17710  18448  17633  -1612    322   -553       C  
ATOM   1193  CG  ASN A 189      12.704  35.088  78.927  1.00150.04           C  
ANISOU 1193  CG  ASN A 189    18771  19545  18694  -1741    359   -607       C  
ATOM   1194  OD1 ASN A 189      12.452  34.375  79.904  1.00152.20           O  
ANISOU 1194  OD1 ASN A 189    18978  19877  18974  -1770    351   -612       O  
ATOM   1195  ND2 ASN A 189      12.774  36.412  79.010  1.00152.78           N  
ANISOU 1195  ND2 ASN A 189    19184  19842  19022  -1820    402   -647       N  
ATOM   1196  N   ASN A 190      10.506  31.656  77.438  1.00125.71           N  
ANISOU 1196  N   ASN A 190    15632  16363  15770  -1366    222   -588       N  
ATOM   1197  CA  ASN A 190       9.085  31.380  77.632  1.00119.60           C  
ANISOU 1197  CA  ASN A 190    14869  15513  15060  -1316    204   -656       C  
ATOM   1198  C   ASN A 190       8.253  32.387  76.833  1.00111.19           C  
ANISOU 1198  C   ASN A 190    13884  14324  14038  -1264    209   -712       C  
ATOM   1199  O   ASN A 190       7.377  33.083  77.349  1.00107.98           O  
ANISOU 1199  O   ASN A 190    13505  13861  13662  -1293    224   -784       O  
ATOM   1200  CB  ASN A 190       8.741  31.383  79.132  1.00121.03           C  
ANISOU 1200  CB  ASN A 190    15007  15741  15239  -1416    219   -699       C  
ATOM   1201  CG  ASN A 190       7.258  31.212  79.409  1.00116.77           C  
ANISOU 1201  CG  ASN A 190    14478  15130  14759  -1376    202   -777       C  
ATOM   1202  OD1 ASN A 190       6.618  32.112  79.956  1.00117.95           O  
ANISOU 1202  OD1 ASN A 190    14655  15234  14929  -1428    225   -846       O  
ATOM   1203  ND2 ASN A 190       6.702  30.064  79.023  1.00110.57           N  
ANISOU 1203  ND2 ASN A 190    13674  14336  13999  -1286    165   -768       N  
ATOM   1204  N   GLN A 191       8.586  32.497  75.555  1.00108.44           N  
ANISOU 1204  N   GLN A 191    13575  13937  13690  -1188    198   -675       N  
ATOM   1205  CA  GLN A 191       7.971  33.463  74.655  1.00107.49           C  
ANISOU 1205  CA  GLN A 191    13533  13706  13603  -1132    203   -714       C  
ATOM   1206  C   GLN A 191       7.117  32.720  73.638  1.00 99.34           C  
ANISOU 1206  C   GLN A 191    12510  12617  12617   -999    163   -717       C  
ATOM   1207  O   GLN A 191       7.619  31.854  72.910  1.00 86.11           O  
ANISOU 1207  O   GLN A 191    10814  10973  10931   -940    140   -658       O  
ATOM   1208  CB  GLN A 191       9.036  34.307  73.961  1.00106.15           C  
ANISOU 1208  CB  GLN A 191    13406  13534  13390  -1160    224   -672       C  
ATOM   1209  CG  GLN A 191       8.508  35.544  73.271  1.00102.71           C  
ANISOU 1209  CG  GLN A 191    13060  12985  12979  -1132    240   -715       C  
ATOM   1210  CD  GLN A 191       9.620  36.296  72.577  1.00108.65           C  
ANISOU 1210  CD  GLN A 191    13857  13743  13684  -1165    260   -670       C  
ATOM   1211  OE1 GLN A 191      10.798  36.014  72.798  1.00112.12           O  
ANISOU 1211  OE1 GLN A 191    14255  14280  14065  -1229    266   -615       O  
ATOM   1212  NE2 GLN A 191       9.258  37.244  71.722  1.00112.62           N  
ANISOU 1212  NE2 GLN A 191    14441  14144  14205  -1121    269   -693       N  
ATOM   1213  N   THR A 192       5.822  33.007  73.648  1.00100.67           N  
ANISOU 1213  N   THR A 192    12706  12710  12835   -956    158   -785       N  
ATOM   1214  CA  THR A 192       4.876  32.282  72.773  1.00103.54           C  
ANISOU 1214  CA  THR A 192    13072  13028  13238   -837    122   -795       C  
ATOM   1215  C   THR A 192       5.084  32.665  71.312  1.00 93.31           C  
ANISOU 1215  C   THR A 192    11829  11676  11949   -756    114   -764       C  
ATOM   1216  O   THR A 192       5.233  33.852  71.024  1.00 89.67           O  
ANISOU 1216  O   THR A 192    11424  11161  11484   -773    137   -776       O  
ATOM   1217  CB  THR A 192       3.432  32.541  73.202  1.00111.08           C  
ANISOU 1217  CB  THR A 192    14038  13931  14237   -816    120   -878       C  
ATOM   1218  OG1 THR A 192       3.164  33.904  72.886  1.00120.99           O  
ANISOU 1218  OG1 THR A 192    15358  15107  15504   -811    145   -912       O  
ATOM   1219  CG2 THR A 192       3.217  32.313  74.679  1.00107.71           C  
ANISOU 1219  CG2 THR A 192    13564  13556  13804   -906    130   -915       C  
ATOM   1220  N   ALA A 193       5.095  31.651  70.451  1.00 84.07           N  
ANISOU 1220  N   ALA A 193    10642  10518  10785   -675     83   -725       N  
ATOM   1221  CA  ALA A 193       5.198  31.800  69.011  1.00 84.45           C  
ANISOU 1221  CA  ALA A 193    10728  10517  10840   -591     70   -695       C  
ATOM   1222  C   ALA A 193       4.193  30.871  68.350  1.00 78.98           C  
ANISOU 1222  C   ALA A 193    10025   9802  10181   -493     38   -709       C  
ATOM   1223  O   ALA A 193       3.522  30.071  69.011  1.00 78.92           O  
ANISOU 1223  O   ALA A 193     9981   9821  10185   -495     27   -738       O  
ATOM   1224  CB  ALA A 193       6.616  31.490  68.510  1.00 87.69           C  
ANISOU 1224  CB  ALA A 193    11127  10982  11208   -605     70   -616       C  
ATOM   1225  N   ASN A 194       4.093  30.970  67.030  1.00 67.15           N  
ANISOU 1225  N   ASN A 194     8560   8258   8695   -412     24   -689       N  
ATOM   1226  CA  ASN A 194       3.290  30.022  66.284  1.00 62.48           C  
ANISOU 1226  CA  ASN A 194     7958   7657   8126   -324     -3   -694       C  
ATOM   1227  C   ASN A 194       4.100  29.462  65.135  1.00 74.18           C  
ANISOU 1227  C   ASN A 194     9443   9151   9592   -276    -16   -627       C  
ATOM   1228  O   ASN A 194       4.942  30.145  64.543  1.00 80.69           O  
ANISOU 1228  O   ASN A 194    10296   9962  10401   -282     -8   -590       O  
ATOM   1229  CB  ASN A 194       2.020  30.656  65.744  1.00 67.35           C  
ANISOU 1229  CB  ASN A 194     8609   8204   8778   -259     -9   -748       C  
ATOM   1230  CG  ASN A 194       0.967  30.820  66.796  1.00 67.32           C  
ANISOU 1230  CG  ASN A 194     8590   8197   8792   -285     -4   -819       C  
ATOM   1231  OD1 ASN A 194       0.645  31.940  67.192  1.00 62.78           O  
ANISOU 1231  OD1 ASN A 194     8044   7581   8227   -308     16   -859       O  
ATOM   1232  ND2 ASN A 194       0.402  29.702  67.245  1.00 67.49           N  
ANISOU 1232  ND2 ASN A 194     8569   8261   8814   -282    -20   -838       N  
ATOM   1233  N   MET A 195       3.832  28.213  64.815  1.00 70.86           N  
ANISOU 1233  N   MET A 195     8996   8754   9173   -229    -34   -612       N  
ATOM   1234  CA  MET A 195       4.299  27.666  63.558  1.00 69.60           C  
ANISOU 1234  CA  MET A 195     8846   8592   9007   -166    -47   -560       C  
ATOM   1235  C   MET A 195       3.104  27.159  62.773  1.00 65.10           C  
ANISOU 1235  C   MET A 195     8284   7988   8463    -88    -65   -592       C  
ATOM   1236  O   MET A 195       2.130  26.669  63.353  1.00 63.99           O  
ANISOU 1236  O   MET A 195     8125   7853   8333    -88    -70   -639       O  
ATOM   1237  CB  MET A 195       5.315  26.563  63.780  1.00 70.86           C  
ANISOU 1237  CB  MET A 195     8971   8818   9134   -183    -46   -501       C  
ATOM   1238  CG  MET A 195       4.817  25.444  64.606  1.00 82.16           C  
ANISOU 1238  CG  MET A 195    10369  10284  10564   -193    -49   -519       C  
ATOM   1239  SD  MET A 195       6.071  24.164  64.650  1.00 93.14           S  
ANISOU 1239  SD  MET A 195    11728  11744  11915   -192    -45   -438       S  
ATOM   1240  CE  MET A 195       5.211  22.922  65.608  1.00 86.03           C  
ANISOU 1240  CE  MET A 195    10804  10867  11017   -201    -48   -472       C  
ATOM   1241  N   CYS A 196       3.171  27.316  61.452  1.00 70.24           N  
ANISOU 1241  N   CYS A 196     8961   8606   9120    -26    -75   -567       N  
ATOM   1242  CA  CYS A 196       2.115  26.843  60.572  1.00 54.94           C  
ANISOU 1242  CA  CYS A 196     7029   6644   7201     47    -90   -590       C  
ATOM   1243  C   CYS A 196       2.320  25.367  60.297  1.00 64.08           C  
ANISOU 1243  C   CYS A 196     8166   7839   8343     68    -96   -559       C  
ATOM   1244  O   CYS A 196       3.382  24.959  59.825  1.00 77.91           O  
ANISOU 1244  O   CYS A 196     9916   9609  10075     72    -93   -499       O  
ATOM   1245  CB  CYS A 196       2.104  27.642  59.276  1.00 55.57           C  
ANISOU 1245  CB  CYS A 196     7146   6677   7293    101    -97   -575       C  
ATOM   1246  SG  CYS A 196       0.914  27.021  58.019  1.00 69.81           S  
ANISOU 1246  SG  CYS A 196     8950   8462   9110    191   -116   -593       S  
ATOM   1247  N   ARG A 197       1.309  24.558  60.589  1.00 66.70           N  
ANISOU 1247  N   ARG A 197     8484   8182   8678     79   -101   -599       N  
ATOM   1248  CA  ARG A 197       1.498  23.116  60.551  1.00 61.21           C  
ANISOU 1248  CA  ARG A 197     7776   7520   7962     87   -100   -574       C  
ATOM   1249  C   ARG A 197       0.269  22.407  59.979  1.00 58.93           C  
ANISOU 1249  C   ARG A 197     7491   7223   7676    130   -108   -613       C  
ATOM   1250  O   ARG A 197      -0.870  22.825  60.215  1.00 61.18           O  
ANISOU 1250  O   ARG A 197     7773   7500   7975    134   -114   -673       O  
ATOM   1251  CB  ARG A 197       1.824  22.606  61.958  1.00 67.07           C  
ANISOU 1251  CB  ARG A 197     8491   8304   8688     23    -90   -576       C  
ATOM   1252  CG  ARG A 197       2.385  21.214  61.994  1.00 66.83           C  
ANISOU 1252  CG  ARG A 197     8454   8306   8632     29    -83   -532       C  
ATOM   1253  CD  ARG A 197       3.825  21.182  61.559  1.00 52.46           C  
ANISOU 1253  CD  ARG A 197     6634   6504   6794     37    -76   -456       C  
ATOM   1254  NE  ARG A 197       4.528  20.280  62.444  1.00 64.88           N  
ANISOU 1254  NE  ARG A 197     8185   8126   8340      6    -64   -421       N  
ATOM   1255  CZ  ARG A 197       4.485  18.958  62.339  1.00 69.37           C  
ANISOU 1255  CZ  ARG A 197     8760   8706   8892     33    -57   -402       C  
ATOM   1256  NH1 ARG A 197       3.788  18.395  61.360  1.00 59.98           N  
ANISOU 1256  NH1 ARG A 197     7598   7483   7708     84    -60   -418       N  
ATOM   1257  NH2 ARG A 197       5.146  18.195  63.206  1.00 77.79           N  
ANISOU 1257  NH2 ARG A 197     9809   9817   9932      8    -45   -367       N  
ATOM   1258  N   PHE A 198       0.508  21.314  59.250  1.00 52.09           N  
ANISOU 1258  N   PHE A 198     6633   6365   6793    161   -105   -579       N  
ATOM   1259  CA  PHE A 198      -0.532  20.552  58.557  1.00 55.26           C  
ANISOU 1259  CA  PHE A 198     7043   6765   7188    198   -108   -609       C  
ATOM   1260  C   PHE A 198      -0.709  19.215  59.271  1.00 49.22           C  
ANISOU 1260  C   PHE A 198     6275   6029   6398    170    -97   -617       C  
ATOM   1261  O   PHE A 198       0.158  18.339  59.186  1.00 51.49           O  
ANISOU 1261  O   PHE A 198     6571   6326   6667    172    -84   -566       O  
ATOM   1262  CB  PHE A 198      -0.165  20.368  57.069  1.00 60.26           C  
ANISOU 1262  CB  PHE A 198     7696   7380   7820    252   -108   -566       C  
ATOM   1263  CG  PHE A 198      -0.995  19.344  56.336  1.00 55.85           C  
ANISOU 1263  CG  PHE A 198     7149   6828   7245    280   -105   -585       C  
ATOM   1264  CD1 PHE A 198      -2.337  19.598  56.018  1.00 54.17           C  
ANISOU 1264  CD1 PHE A 198     6930   6616   7034    297   -114   -642       C  
ATOM   1265  CD2 PHE A 198      -0.427  18.148  55.927  1.00 48.07           C  
ANISOU 1265  CD2 PHE A 198     6180   5849   6237    289    -89   -545       C  
ATOM   1266  CE1 PHE A 198      -3.111  18.646  55.327  1.00 49.86           C  
ANISOU 1266  CE1 PHE A 198     6394   6086   6465    313   -108   -661       C  
ATOM   1267  CE2 PHE A 198      -1.180  17.186  55.239  1.00 48.02           C  
ANISOU 1267  CE2 PHE A 198     6189   5846   6209    307    -80   -564       C  
ATOM   1268  CZ  PHE A 198      -2.527  17.438  54.937  1.00 48.54           C  
ANISOU 1268  CZ  PHE A 198     6249   5920   6275    315    -90   -622       C  
ATOM   1269  N   LEU A 199      -1.845  19.050  59.956  1.00 49.66           N  
ANISOU 1269  N   LEU A 199     6321   6099   6450    145   -102   -681       N  
ATOM   1270  CA  LEU A 199      -2.063  17.921  60.856  1.00 56.67           C  
ANISOU 1270  CA  LEU A 199     7206   7014   7312    105    -92   -697       C  
ATOM   1271  C   LEU A 199      -3.389  17.251  60.559  1.00 58.78           C  
ANISOU 1271  C   LEU A 199     7482   7292   7560    111    -94   -752       C  
ATOM   1272  O   LEU A 199      -4.448  17.866  60.718  1.00 59.90           O  
ANISOU 1272  O   LEU A 199     7608   7443   7710    108   -106   -812       O  
ATOM   1273  CB  LEU A 199      -2.050  18.363  62.320  1.00 50.22           C  
ANISOU 1273  CB  LEU A 199     6363   6216   6502     46    -95   -723       C  
ATOM   1274  CG  LEU A 199      -0.747  18.828  62.952  1.00 54.71           C  
ANISOU 1274  CG  LEU A 199     6919   6793   7077     17    -89   -672       C  
ATOM   1275  CD1 LEU A 199      -1.053  19.229  64.401  1.00 50.89           C  
ANISOU 1275  CD1 LEU A 199     6407   6330   6597    -49    -92   -715       C  
ATOM   1276  CD2 LEU A 199       0.347  17.747  62.866  1.00 49.88           C  
ANISOU 1276  CD2 LEU A 199     6317   6196   6440     24    -74   -603       C  
ATOM   1277  N   LEU A 200      -3.331  15.991  60.196  1.00 62.09           N  
ANISOU 1277  N   LEU A 200     7927   7715   7950    117    -78   -735       N  
ATOM   1278  CA  LEU A 200      -4.523  15.201  59.943  1.00 66.20           C  
ANISOU 1278  CA  LEU A 200     8461   8252   8440    110    -74   -786       C  
ATOM   1279  C   LEU A 200      -4.937  14.469  61.219  1.00 67.51           C  
ANISOU 1279  C   LEU A 200     8625   8443   8581     51    -70   -823       C  
ATOM   1280  O   LEU A 200      -4.126  14.276  62.132  1.00 62.54           O  
ANISOU 1280  O   LEU A 200     7992   7816   7954     22    -65   -792       O  
ATOM   1281  CB  LEU A 200      -4.265  14.230  58.786  1.00 58.06           C  
ANISOU 1281  CB  LEU A 200     7468   7208   7386    144    -55   -750       C  
ATOM   1282  CG  LEU A 200      -4.062  14.846  57.393  1.00 58.61           C  
ANISOU 1282  CG  LEU A 200     7539   7257   7474    200    -60   -722       C  
ATOM   1283  CD1 LEU A 200      -3.256  13.878  56.528  1.00 60.02           C  
ANISOU 1283  CD1 LEU A 200     7754   7416   7635    226    -37   -664       C  
ATOM   1284  CD2 LEU A 200      -5.399  15.166  56.739  1.00 50.33           C  
ANISOU 1284  CD2 LEU A 200     6480   6228   6417    213    -71   -778       C  
ATOM   1285  N   PRO A 201      -6.199  14.047  61.313  1.00 68.47           N  
ANISOU 1285  N   PRO A 201     8749   8591   8675     28    -72   -888       N  
ATOM   1286  CA  PRO A 201      -6.724  13.522  62.589  1.00 62.15           C  
ANISOU 1286  CA  PRO A 201     7943   7820   7852    -35    -73   -933       C  
ATOM   1287  C   PRO A 201      -5.837  12.519  63.326  1.00 65.23           C  
ANISOU 1287  C   PRO A 201     8357   8202   8224    -65    -54   -890       C  
ATOM   1288  O   PRO A 201      -5.917  12.471  64.558  1.00 70.66           O  
ANISOU 1288  O   PRO A 201     9029   8910   8910   -116    -60   -912       O  
ATOM   1289  CB  PRO A 201      -8.049  12.887  62.155  1.00 60.02           C  
ANISOU 1289  CB  PRO A 201     7687   7580   7540    -48    -70   -994       C  
ATOM   1290  CG  PRO A 201      -8.511  13.765  61.035  1.00 57.17           C  
ANISOU 1290  CG  PRO A 201     7308   7219   7196      5    -81  -1004       C  
ATOM   1291  CD  PRO A 201      -7.257  14.155  60.291  1.00 67.71           C  
ANISOU 1291  CD  PRO A 201     8653   8509   8564     55    -77   -927       C  
ATOM   1292  N   ASN A 202      -5.006  11.725  62.655  1.00 60.89           N  
ANISOU 1292  N   ASN A 202     7846   7627   7662    -33    -32   -828       N  
ATOM   1293  CA  ASN A 202      -4.147  10.816  63.420  1.00 60.27           C  
ANISOU 1293  CA  ASN A 202     7790   7544   7566    -53    -13   -782       C  
ATOM   1294  C   ASN A 202      -2.919  10.484  62.579  1.00 62.25           C  
ANISOU 1294  C   ASN A 202     8066   7766   7821      2      6   -700       C  
ATOM   1295  O   ASN A 202      -2.562  11.243  61.677  1.00 64.12           O  
ANISOU 1295  O   ASN A 202     8289   7989   8084     45     -2   -676       O  
ATOM   1296  CB  ASN A 202      -4.917   9.564  63.874  1.00 61.68           C  
ANISOU 1296  CB  ASN A 202     8008   7733   7696    -98      3   -822       C  
ATOM   1297  CG  ASN A 202      -5.621   8.862  62.739  1.00 69.86           C  
ANISOU 1297  CG  ASN A 202     9088   8758   8697    -80     20   -843       C  
ATOM   1298  OD1 ASN A 202      -5.165   8.888  61.601  1.00 81.33           O  
ANISOU 1298  OD1 ASN A 202    10556  10186  10158    -29     31   -803       O  
ATOM   1299  ND2 ASN A 202      -6.747   8.226  63.046  1.00 71.18           N  
ANISOU 1299  ND2 ASN A 202     9275   8948   8822   -130     24   -908       N  
ATOM   1300  N   ASP A 203      -2.243   9.382  62.910  1.00 61.55           N  
ANISOU 1300  N   ASP A 203     8012   7668   7705      2     32   -654       N  
ATOM   1301  CA  ASP A 203      -1.001   9.033  62.236  1.00 60.77           C  
ANISOU 1301  CA  ASP A 203     7934   7548   7607     57     52   -572       C  
ATOM   1302  C   ASP A 203      -1.261   8.173  61.022  1.00 71.80           C  
ANISOU 1302  C   ASP A 203     9387   8914   8979     92     77   -568       C  
ATOM   1303  O   ASP A 203      -0.588   8.329  59.998  1.00 87.93           O  
ANISOU 1303  O   ASP A 203    11435  10939  11034    144     84   -522       O  
ATOM   1304  CB  ASP A 203      -0.037   8.312  63.180  1.00 65.22           C  
ANISOU 1304  CB  ASP A 203     8506   8121   8153     51     69   -516       C  
ATOM   1305  CG  ASP A 203       0.634   9.265  64.171  1.00 87.64           C  
ANISOU 1305  CG  ASP A 203    11285  10996  11019     26     48   -497       C  
ATOM   1306  OD1 ASP A 203       0.292  10.474  64.165  1.00 92.41           O  
ANISOU 1306  OD1 ASP A 203    11847  11610  11655     11     22   -532       O  
ATOM   1307  OD2 ASP A 203       1.502   8.805  64.951  1.00 89.92           O  
ANISOU 1307  OD2 ASP A 203    11569  11304  11292     22     60   -445       O  
ATOM   1308  N   VAL A 204      -2.223   7.265  61.116  1.00 67.51           N  
ANISOU 1308  N   VAL A 204     8886   8368   8398     59     93   -616       N  
ATOM   1309  CA  VAL A 204      -2.599   6.490  59.945  1.00 63.33           C  
ANISOU 1309  CA  VAL A 204     8411   7812   7839     80    120   -622       C  
ATOM   1310  C   VAL A 204      -3.029   7.403  58.798  1.00 69.74           C  
ANISOU 1310  C   VAL A 204     9194   8629   8676    106    101   -642       C  
ATOM   1311  O   VAL A 204      -2.665   7.172  57.638  1.00 83.48           O  
ANISOU 1311  O   VAL A 204    10958  10345  10414    148    118   -610       O  
ATOM   1312  CB  VAL A 204      -3.679   5.471  60.325  1.00 66.42           C  
ANISOU 1312  CB  VAL A 204     8850   8207   8178     25    140   -681       C  
ATOM   1313  CG1 VAL A 204      -4.498   5.093  59.107  1.00 72.36           C  
ANISOU 1313  CG1 VAL A 204     9639   8954   8903     27    157   -716       C  
ATOM   1314  CG2 VAL A 204      -3.009   4.248  60.920  1.00 61.78           C  
ANISOU 1314  CG2 VAL A 204     8320   7594   7558     24    175   -636       C  
ATOM   1315  N   MET A 205      -3.773   8.470  59.091  1.00 65.22           N  
ANISOU 1315  N   MET A 205     8570   8085   8128     85     67   -694       N  
ATOM   1316  CA  MET A 205      -4.180   9.366  58.011  1.00 67.84           C  
ANISOU 1316  CA  MET A 205     8875   8421   8482    116     49   -709       C  
ATOM   1317  C   MET A 205      -3.008  10.195  57.499  1.00 71.75           C  
ANISOU 1317  C   MET A 205     9346   8896   9018    167     38   -645       C  
ATOM   1318  O   MET A 205      -2.872  10.385  56.282  1.00 66.46           O  
ANISOU 1318  O   MET A 205     8683   8214   8357    207     41   -625       O  
ATOM   1319  CB  MET A 205      -5.315  10.274  58.462  1.00 67.53           C  
ANISOU 1319  CB  MET A 205     8790   8416   8452     87     18   -780       C  
ATOM   1320  CG  MET A 205      -6.535   9.500  58.895  1.00 78.55           C  
ANISOU 1320  CG  MET A 205    10205   9842   9800     34     26   -849       C  
ATOM   1321  SD  MET A 205      -7.903  10.601  59.227  1.00 85.37           S  
ANISOU 1321  SD  MET A 205    11009  10754  10672     13     -9   -932       S  
ATOM   1322  CE  MET A 205      -8.180  11.241  57.572  1.00 86.54           C  
ANISOU 1322  CE  MET A 205    11146  10903  10833     72    -14   -922       C  
ATOM   1323  N   GLN A 206      -2.163  10.712  58.409  1.00 65.12           N  
ANISOU 1323  N   GLN A 206     8479   8062   8204    161     27   -613       N  
ATOM   1324  CA  GLN A 206      -0.973  11.445  57.975  1.00 63.46           C  
ANISOU 1324  CA  GLN A 206     8248   7840   8024    201     19   -550       C  
ATOM   1325  C   GLN A 206      -0.116  10.598  57.044  1.00 60.75           C  
ANISOU 1325  C   GLN A 206     7944   7475   7665    246     47   -489       C  
ATOM   1326  O   GLN A 206       0.436  11.109  56.066  1.00 56.73           O  
ANISOU 1326  O   GLN A 206     7427   6954   7174    285     41   -455       O  
ATOM   1327  CB  GLN A 206      -0.143  11.908  59.175  1.00 60.37           C  
ANISOU 1327  CB  GLN A 206     7824   7466   7647    178     10   -523       C  
ATOM   1328  CG  GLN A 206      -0.548  13.273  59.710  1.00 73.45           C  
ANISOU 1328  CG  GLN A 206     9436   9136   9335    153    -20   -562       C  
ATOM   1329  CD  GLN A 206       0.062  14.425  58.929  1.00 77.09           C  
ANISOU 1329  CD  GLN A 206     9879   9584   9827    187    -34   -532       C  
ATOM   1330  OE1 GLN A 206      -0.353  15.584  59.053  1.00 83.74           O  
ANISOU 1330  OE1 GLN A 206    10696  10426  10695    178    -54   -565       O  
ATOM   1331  NE2 GLN A 206       1.069  14.106  58.123  1.00 80.36           N  
ANISOU 1331  NE2 GLN A 206    10309   9989  10237    226    -22   -468       N  
ATOM   1332  N   GLN A 207       0.012   9.302  57.341  1.00 55.99           N  
ANISOU 1332  N   GLN A 207     7384   6862   7026    239     78   -475       N  
ATOM   1333  CA  GLN A 207       0.835   8.415  56.531  1.00 58.96           C  
ANISOU 1333  CA  GLN A 207     7802   7214   7384    284    110   -416       C  
ATOM   1334  C   GLN A 207       0.115   7.984  55.259  1.00 64.96           C  
ANISOU 1334  C   GLN A 207     8599   7955   8129    297    126   -442       C  
ATOM   1335  O   GLN A 207       0.761   7.744  54.232  1.00 67.63           O  
ANISOU 1335  O   GLN A 207     8956   8273   8466    340    142   -399       O  
ATOM   1336  CB  GLN A 207       1.259   7.202  57.367  1.00 57.56           C  
ANISOU 1336  CB  GLN A 207     7665   7031   7173    277    141   -389       C  
ATOM   1337  CG  GLN A 207       2.158   7.618  58.525  1.00 67.88           C  
ANISOU 1337  CG  GLN A 207     8931   8368   8494    269    128   -349       C  
ATOM   1338  CD  GLN A 207       2.327   6.559  59.611  1.00 71.97           C  
ANISOU 1338  CD  GLN A 207     9479   8889   8979    250    151   -334       C  
ATOM   1339  OE1 GLN A 207       1.765   5.465  59.540  1.00 78.62           O  
ANISOU 1339  OE1 GLN A 207    10380   9705   9786    241    180   -355       O  
ATOM   1340  NE2 GLN A 207       3.106   6.892  60.629  1.00 64.53           N  
ANISOU 1340  NE2 GLN A 207     8496   7979   8043    241    141   -298       N  
ATOM   1341  N   SER A 208      -1.208   7.867  55.310  1.00 66.07           N  
ANISOU 1341  N   SER A 208     8746   8105   8251    257    122   -513       N  
ATOM   1342  CA  SER A 208      -1.952   7.551  54.103  1.00 65.38           C  
ANISOU 1342  CA  SER A 208     8685   8012   8144    262    136   -541       C  
ATOM   1343  C   SER A 208      -1.857   8.685  53.100  1.00 65.28           C  
ANISOU 1343  C   SER A 208     8631   8003   8168    296    109   -531       C  
ATOM   1344  O   SER A 208      -1.715   8.455  51.893  1.00 67.60           O  
ANISOU 1344  O   SER A 208     8945   8284   8457    324    124   -512       O  
ATOM   1345  CB  SER A 208      -3.403   7.254  54.451  1.00 62.53           C  
ANISOU 1345  CB  SER A 208     8332   7676   7751    207    136   -620       C  
ATOM   1346  OG  SER A 208      -3.488   5.965  55.028  1.00 62.72           O  
ANISOU 1346  OG  SER A 208     8415   7686   7729    176    171   -626       O  
ATOM   1347  N   TRP A 209      -1.907   9.918  53.586  1.00 63.14           N  
ANISOU 1347  N   TRP A 209     8306   7750   7934    294     72   -543       N  
ATOM   1348  CA  TRP A 209      -1.824  11.064  52.701  1.00 53.02           C  
ANISOU 1348  CA  TRP A 209     6991   6469   6686    327     46   -534       C  
ATOM   1349  C   TRP A 209      -0.495  11.087  51.969  1.00 65.41           C  
ANISOU 1349  C   TRP A 209     8568   8016   8270    371     54   -461       C  
ATOM   1350  O   TRP A 209      -0.443  11.407  50.780  1.00 69.26           O  
ANISOU 1350  O   TRP A 209     9054   8496   8767    400     50   -448       O  
ATOM   1351  CB  TRP A 209      -2.011  12.334  53.505  1.00 51.14           C  
ANISOU 1351  CB  TRP A 209     6705   6245   6481    315     11   -557       C  
ATOM   1352  CG  TRP A 209      -1.797  13.544  52.743  1.00 53.83           C  
ANISOU 1352  CG  TRP A 209     7018   6579   6855    348    -13   -542       C  
ATOM   1353  CD1 TRP A 209      -0.699  14.370  52.785  1.00 47.47           C  
ANISOU 1353  CD1 TRP A 209     6196   5762   6079    367    -26   -494       C  
ATOM   1354  CD2 TRP A 209      -2.714  14.124  51.826  1.00 50.81           C  
ANISOU 1354  CD2 TRP A 209     6623   6205   6478    366    -27   -574       C  
ATOM   1355  NE1 TRP A 209      -0.890  15.438  51.940  1.00 58.36           N  
ANISOU 1355  NE1 TRP A 209     7559   7134   7483    394    -47   -496       N  
ATOM   1356  CE2 TRP A 209      -2.114  15.303  51.327  1.00 54.52           C  
ANISOU 1356  CE2 TRP A 209     7073   6659   6983    398    -48   -543       C  
ATOM   1357  CE3 TRP A 209      -3.985  13.755  51.359  1.00 53.15           C  
ANISOU 1357  CE3 TRP A 209     6922   6525   6747    357    -22   -626       C  
ATOM   1358  CZ2 TRP A 209      -2.738  16.114  50.372  1.00 47.98           C  
ANISOU 1358  CZ2 TRP A 209     6230   5833   6168    427    -65   -558       C  
ATOM   1359  CZ3 TRP A 209      -4.614  14.573  50.421  1.00 58.66           C  
ANISOU 1359  CZ3 TRP A 209     7598   7235   7456    385    -40   -641       C  
ATOM   1360  CH2 TRP A 209      -3.981  15.741  49.936  1.00 56.57           C  
ANISOU 1360  CH2 TRP A 209     7316   6948   7231    423    -61   -605       C  
ATOM   1361  N   HIS A 210       0.594  10.728  52.657  1.00 70.00           N  
ANISOU 1361  N   HIS A 210     9156   8592   8850    376     65   -412       N  
ATOM   1362  CA  HIS A 210       1.894  10.739  52.002  1.00 61.03           C  
ANISOU 1362  CA  HIS A 210     8022   7444   7722    419     72   -342       C  
ATOM   1363  C   HIS A 210       2.021   9.621  50.996  1.00 57.74           C  
ANISOU 1363  C   HIS A 210     7654   7006   7278    444    108   -322       C  
ATOM   1364  O   HIS A 210       2.647   9.812  49.956  1.00 61.91           O  
ANISOU 1364  O   HIS A 210     8181   7526   7816    479    109   -284       O  
ATOM   1365  CB  HIS A 210       3.013  10.661  53.027  1.00 64.97           C  
ANISOU 1365  CB  HIS A 210     8509   7956   8219    419     75   -294       C  
ATOM   1366  CG  HIS A 210       3.255  11.958  53.718  1.00 72.49           C  
ANISOU 1366  CG  HIS A 210     9412   8929   9201    400     42   -298       C  
ATOM   1367  ND1 HIS A 210       2.740  12.241  54.962  1.00 75.08           N  
ANISOU 1367  ND1 HIS A 210     9720   9273   9533    356     30   -336       N  
ATOM   1368  CD2 HIS A 210       3.905  13.072  53.311  1.00 73.33           C  
ANISOU 1368  CD2 HIS A 210     9490   9042   9332    413     20   -271       C  
ATOM   1369  CE1 HIS A 210       3.084  13.469  55.304  1.00 75.31           C  
ANISOU 1369  CE1 HIS A 210     9712   9315   9588    344      5   -333       C  
ATOM   1370  NE2 HIS A 210       3.793  13.993  54.319  1.00 74.91           N  
ANISOU 1370  NE2 HIS A 210     9657   9257   9548    377     -2   -294       N  
ATOM   1371  N   THR A 211       1.456   8.454  51.283  1.00 58.46           N  
ANISOU 1371  N   THR A 211     7790   7088   7334    423    140   -346       N  
ATOM   1372  CA  THR A 211       1.380   7.434  50.250  1.00 60.04           C  
ANISOU 1372  CA  THR A 211     8043   7265   7506    439    178   -338       C  
ATOM   1373  C   THR A 211       0.658   7.982  49.036  1.00 64.65           C  
ANISOU 1373  C   THR A 211     8612   7853   8097    440    165   -368       C  
ATOM   1374  O   THR A 211       1.117   7.829  47.898  1.00 68.13           O  
ANISOU 1374  O   THR A 211     9066   8281   8539    470    178   -337       O  
ATOM   1375  CB  THR A 211       0.647   6.209  50.774  1.00 64.86           C  
ANISOU 1375  CB  THR A 211     8708   7863   8071    403    214   -374       C  
ATOM   1376  OG1 THR A 211       1.370   5.660  51.884  1.00 77.80           O  
ANISOU 1376  OG1 THR A 211    10364   9497   9701    407    228   -339       O  
ATOM   1377  CG2 THR A 211       0.483   5.174  49.660  1.00 56.74           C  
ANISOU 1377  CG2 THR A 211     7742   6809   7009    411    259   -372       C  
ATOM   1378  N   PHE A 212      -0.461   8.657  49.277  1.00 61.23           N  
ANISOU 1378  N   PHE A 212     8148   7444   7671    409    138   -426       N  
ATOM   1379  CA  PHE A 212      -1.217   9.310  48.223  1.00 57.71           C  
ANISOU 1379  CA  PHE A 212     7680   7014   7234    412    121   -455       C  
ATOM   1380  C   PHE A 212      -0.322  10.198  47.360  1.00 63.08           C  
ANISOU 1380  C   PHE A 212     8332   7685   7950    456    100   -405       C  
ATOM   1381  O   PHE A 212      -0.199   9.983  46.150  1.00 68.74           O  
ANISOU 1381  O   PHE A 212     9062   8395   8661    475    112   -388       O  
ATOM   1382  CB  PHE A 212      -2.347  10.105  48.867  1.00 53.04           C  
ANISOU 1382  CB  PHE A 212     7050   6455   6650    384     89   -516       C  
ATOM   1383  CG  PHE A 212      -3.210  10.787  47.903  1.00 56.68           C  
ANISOU 1383  CG  PHE A 212     7482   6938   7114    392     71   -545       C  
ATOM   1384  CD1 PHE A 212      -3.958  10.050  46.998  1.00 50.08           C  
ANISOU 1384  CD1 PHE A 212     6671   6119   6240    376     97   -570       C  
ATOM   1385  CD2 PHE A 212      -3.295  12.171  47.890  1.00 56.06           C  
ANISOU 1385  CD2 PHE A 212     7357   6869   7075    413     32   -547       C  
ATOM   1386  CE1 PHE A 212      -4.768  10.678  46.092  1.00 50.38           C  
ANISOU 1386  CE1 PHE A 212     6678   6187   6276    384     80   -594       C  
ATOM   1387  CE2 PHE A 212      -4.117  12.809  46.970  1.00 57.47           C  
ANISOU 1387  CE2 PHE A 212     7511   7071   7255    427     16   -571       C  
ATOM   1388  CZ  PHE A 212      -4.851  12.056  46.067  1.00 50.29           C  
ANISOU 1388  CZ  PHE A 212     6618   6185   6306    414     39   -592       C  
ATOM   1389  N   LEU A 213       0.331  11.189  47.973  1.00 58.74           N  
ANISOU 1389  N   LEU A 213     7747   7137   7434    468     69   -382       N  
ATOM   1390  CA  LEU A 213       1.209  12.078  47.219  1.00 57.12           C  
ANISOU 1390  CA  LEU A 213     7518   6925   7258    502     48   -337       C  
ATOM   1391  C   LEU A 213       2.319  11.304  46.517  1.00 65.27           C  
ANISOU 1391  C   LEU A 213     8579   7942   8280    531     76   -279       C  
ATOM   1392  O   LEU A 213       2.698  11.634  45.386  1.00 63.18           O  
ANISOU 1392  O   LEU A 213     8309   7673   8025    556     70   -254       O  
ATOM   1393  CB  LEU A 213       1.824  13.128  48.139  1.00 59.29           C  
ANISOU 1393  CB  LEU A 213     7760   7206   7562    499     20   -322       C  
ATOM   1394  CG  LEU A 213       0.949  14.113  48.902  1.00 58.43           C  
ANISOU 1394  CG  LEU A 213     7622   7109   7472    476     -9   -372       C  
ATOM   1395  CD1 LEU A 213       1.823  14.964  49.842  1.00 57.03           C  
ANISOU 1395  CD1 LEU A 213     7421   6934   7315    467    -26   -347       C  
ATOM   1396  CD2 LEU A 213       0.144  14.968  47.960  1.00 46.75           C  
ANISOU 1396  CD2 LEU A 213     6126   5630   6007    491    -30   -398       C  
ATOM   1397  N   LEU A 214       2.870  10.282  47.175  1.00 66.51           N  
ANISOU 1397  N   LEU A 214     8766   8092   8414    532    106   -256       N  
ATOM   1398  CA  LEU A 214       3.906   9.495  46.515  1.00 67.06           C  
ANISOU 1398  CA  LEU A 214     8864   8146   8468    567    136   -200       C  
ATOM   1399  C   LEU A 214       3.422   8.985  45.165  1.00 65.36           C  
ANISOU 1399  C   LEU A 214     8676   7917   8239    572    158   -213       C  
ATOM   1400  O   LEU A 214       4.187   8.982  44.201  1.00 71.27           O  
ANISOU 1400  O   LEU A 214     9428   8660   8993    602    164   -172       O  
ATOM   1401  CB  LEU A 214       4.361   8.325  47.394  1.00 59.27           C  
ANISOU 1401  CB  LEU A 214     7915   7151   7454    570    173   -178       C  
ATOM   1402  CG  LEU A 214       5.453   7.426  46.781  1.00 70.18           C  
ANISOU 1402  CG  LEU A 214     9331   8517   8817    615    210   -118       C  
ATOM   1403  CD1 LEU A 214       6.813   8.148  46.598  1.00 68.57           C  
ANISOU 1403  CD1 LEU A 214     9087   8335   8631    651    188    -56       C  
ATOM   1404  CD2 LEU A 214       5.638   6.109  47.540  1.00 69.42           C  
ANISOU 1404  CD2 LEU A 214     9287   8403   8685    621    254   -104       C  
ATOM   1405  N   LEU A 215       2.143   8.608  45.074  1.00 62.68           N  
ANISOU 1405  N   LEU A 215     8355   7580   7880    538    169   -270       N  
ATOM   1406  CA  LEU A 215       1.608   7.914  43.907  1.00 59.88           C  
ANISOU 1406  CA  LEU A 215     8034   7218   7501    531    199   -287       C  
ATOM   1407  C   LEU A 215       1.238   8.877  42.795  1.00 59.10           C  
ANISOU 1407  C   LEU A 215     7896   7137   7423    537    169   -295       C  
ATOM   1408  O   LEU A 215       1.661   8.699  41.658  1.00 64.45           O  
ANISOU 1408  O   LEU A 215     8582   7806   8098    556    182   -268       O  
ATOM   1409  CB  LEU A 215       0.377   7.096  44.287  1.00 61.11           C  
ANISOU 1409  CB  LEU A 215     8224   7380   7616    484    225   -346       C  
ATOM   1410  CG  LEU A 215       0.662   5.694  44.792  1.00 69.50           C  
ANISOU 1410  CG  LEU A 215     9354   8413   8641    477    277   -336       C  
ATOM   1411  CD1 LEU A 215      -0.614   5.063  45.294  1.00 75.46           C  
ANISOU 1411  CD1 LEU A 215    10139   9179   9354    420    295   -401       C  
ATOM   1412  CD2 LEU A 215       1.310   4.844  43.688  1.00 65.74           C  
ANISOU 1412  CD2 LEU A 215     8925   7908   8147    502    321   -299       C  
ATOM   1413  N   ILE A 216       0.426   9.891  43.101  1.00 58.96           N  
ANISOU 1413  N   ILE A 216     7835   7142   7423    523    131   -333       N  
ATOM   1414  CA  ILE A 216      -0.082  10.787  42.078  1.00 60.70           C  
ANISOU 1414  CA  ILE A 216     8022   7381   7659    531    104   -344       C  
ATOM   1415  C   ILE A 216       0.796  11.998  41.871  1.00 66.02           C  
ANISOU 1415  C   ILE A 216     8661   8048   8375    564     66   -303       C  
ATOM   1416  O   ILE A 216       0.399  12.905  41.132  1.00 82.33           O  
ANISOU 1416  O   ILE A 216    10698  10126  10458    574     39   -310       O  
ATOM   1417  CB  ILE A 216      -1.502  11.280  42.411  1.00 69.21           C  
ANISOU 1417  CB  ILE A 216     9073   8493   8730    506     85   -406       C  
ATOM   1418  CG1 ILE A 216      -1.519  11.926  43.799  1.00 64.80           C  
ANISOU 1418  CG1 ILE A 216     8494   7935   8194    501     59   -420       C  
ATOM   1419  CG2 ILE A 216      -2.475  10.133  42.359  1.00 81.05           C  
ANISOU 1419  CG2 ILE A 216    10606  10010  10179    466    122   -450       C  
ATOM   1420  CD1 ILE A 216      -1.890  13.397  43.790  1.00 56.05           C  
ANISOU 1420  CD1 ILE A 216     7339   6838   7118    518     15   -432       C  
ATOM   1421  N   LEU A 217       1.970  12.057  42.488  1.00 56.12           N  
ANISOU 1421  N   LEU A 217     7409   6779   7134    580     64   -260       N  
ATOM   1422  CA  LEU A 217       2.915  13.120  42.181  1.00 49.54           C  
ANISOU 1422  CA  LEU A 217     6549   5944   6332    604     33   -218       C  
ATOM   1423  C   LEU A 217       4.300  12.619  41.803  1.00 50.24           C  
ANISOU 1423  C   LEU A 217     6652   6023   6414    628     50   -158       C  
ATOM   1424  O   LEU A 217       5.119  13.425  41.360  1.00 56.71           O  
ANISOU 1424  O   LEU A 217     7450   6845   7251    644     27   -123       O  
ATOM   1425  CB  LEU A 217       3.062  14.086  43.359  1.00 47.73           C  
ANISOU 1425  CB  LEU A 217     6294   5718   6124    595      4   -224       C  
ATOM   1426  CG  LEU A 217       1.934  15.005  43.810  1.00 55.51           C  
ANISOU 1426  CG  LEU A 217     7255   6710   7124    580    -23   -275       C  
ATOM   1427  CD1 LEU A 217       2.495  15.875  44.927  1.00 50.36           C  
ANISOU 1427  CD1 LEU A 217     6586   6057   6493    571    -44   -266       C  
ATOM   1428  CD2 LEU A 217       1.383  15.852  42.680  1.00 56.68           C  
ANISOU 1428  CD2 LEU A 217     7387   6861   7286    597    -45   -284       C  
ATOM   1429  N   PHE A 218       4.588  11.331  41.966  1.00 46.70           N  
ANISOU 1429  N   PHE A 218     6239   5565   5938    632     91   -146       N  
ATOM   1430  CA  PHE A 218       5.881  10.792  41.581  1.00 59.68           C  
ANISOU 1430  CA  PHE A 218     7897   7204   7573    662    112    -88       C  
ATOM   1431  C   PHE A 218       5.742   9.456  40.856  1.00 62.07           C  
ANISOU 1431  C   PHE A 218     8249   7489   7847    669    161    -87       C  
ATOM   1432  O   PHE A 218       6.072   9.368  39.675  1.00 73.84           O  
ANISOU 1432  O   PHE A 218     9743   8976   9337    683    169    -68       O  
ATOM   1433  CB  PHE A 218       6.783  10.644  42.805  1.00 68.70           C  
ANISOU 1433  CB  PHE A 218     9036   8356   8710    672    115    -55       C  
ATOM   1434  CG  PHE A 218       7.043  11.940  43.519  1.00 82.18           C  
ANISOU 1434  CG  PHE A 218    10699  10083  10442    659     72    -53       C  
ATOM   1435  CD1 PHE A 218       7.729  12.966  42.889  1.00 87.45           C  
ANISOU 1435  CD1 PHE A 218    11338  10762  11126    669     42    -25       C  
ATOM   1436  CD2 PHE A 218       6.601  12.140  44.817  1.00 76.26           C  
ANISOU 1436  CD2 PHE A 218     9940   9340   9695    633     64    -80       C  
ATOM   1437  CE1 PHE A 218       7.960  14.167  43.544  1.00 81.99           C  
ANISOU 1437  CE1 PHE A 218    10616  10085  10452    651      8    -25       C  
ATOM   1438  CE2 PHE A 218       6.839  13.331  45.465  1.00 64.55           C  
ANISOU 1438  CE2 PHE A 218     8421   7873   8232    617     29    -80       C  
ATOM   1439  CZ  PHE A 218       7.515  14.345  44.832  1.00 71.72           C  
ANISOU 1439  CZ  PHE A 218     9307   8789   9154    625      3    -53       C  
ATOM   1440  N   LEU A 219       5.282   8.411  41.540  1.00 51.73           N  
ANISOU 1440  N   LEU A 219     6980   6166   6510    655    197   -109       N  
ATOM   1441  CA  LEU A 219       5.219   7.099  40.912  1.00 61.91           C  
ANISOU 1441  CA  LEU A 219     8326   7430   7766    659    252   -107       C  
ATOM   1442  C   LEU A 219       4.450   7.142  39.591  1.00 70.84           C  
ANISOU 1442  C   LEU A 219     9460   8564   8893    639    256   -136       C  
ATOM   1443  O   LEU A 219       4.985   6.780  38.536  1.00 74.51           O  
ANISOU 1443  O   LEU A 219     9939   9019   9352    657    277   -109       O  
ATOM   1444  CB  LEU A 219       4.599   6.082  41.864  1.00 69.85           C  
ANISOU 1444  CB  LEU A 219     9380   8421   8741    635    287   -137       C  
ATOM   1445  CG  LEU A 219       5.581   5.573  42.917  1.00 79.70           C  
ANISOU 1445  CG  LEU A 219    10642   9659   9980    665    303    -93       C  
ATOM   1446  CD1 LEU A 219       5.146   4.217  43.440  1.00 81.37           C  
ANISOU 1446  CD1 LEU A 219    10925   9842  10151    650    356   -111       C  
ATOM   1447  CD2 LEU A 219       7.001   5.523  42.370  1.00 79.72           C  
ANISOU 1447  CD2 LEU A 219    10639   9663   9988    719    310    -25       C  
ATOM   1448  N   ILE A 220       3.194   7.577  39.623  1.00 63.41           N  
ANISOU 1448  N   ILE A 220     8500   7640   7951    601    238   -190       N  
ATOM   1449  CA  ILE A 220       2.359   7.489  38.431  1.00 59.06           C  
ANISOU 1449  CA  ILE A 220     7952   7101   7386    578    248   -220       C  
ATOM   1450  C   ILE A 220       2.859   8.463  37.376  1.00 64.49           C  
ANISOU 1450  C   ILE A 220     8597   7801   8105    601    213   -190       C  
ATOM   1451  O   ILE A 220       3.050   8.050  36.228  1.00 69.98           O  
ANISOU 1451  O   ILE A 220     9307   8493   8790    602    236   -177       O  
ATOM   1452  CB  ILE A 220       0.886   7.731  38.756  1.00 60.58           C  
ANISOU 1452  CB  ILE A 220     8130   7323   7565    535    235   -284       C  
ATOM   1453  CG1 ILE A 220       0.332   6.538  39.538  1.00 62.18           C  
ANISOU 1453  CG1 ILE A 220     8387   7514   7724    501    280   -317       C  
ATOM   1454  CG2 ILE A 220       0.115   7.988  37.481  1.00 63.45           C  
ANISOU 1454  CG2 ILE A 220     8474   7715   7919    517    232   -306       C  
ATOM   1455  CD1 ILE A 220      -1.070   6.771  40.079  1.00 58.58           C  
ANISOU 1455  CD1 ILE A 220     7913   7094   7250    457    265   -382       C  
ATOM   1456  N   PRO A 221       3.098   9.742  37.686  1.00 64.32           N  
ANISOU 1456  N   PRO A 221     8526   7792   8120    616    161   -179       N  
ATOM   1457  CA  PRO A 221       3.712  10.615  36.664  1.00 61.81           C  
ANISOU 1457  CA  PRO A 221     8177   7481   7828    638    131   -145       C  
ATOM   1458  C   PRO A 221       5.109  10.179  36.246  1.00 71.50           C  
ANISOU 1458  C   PRO A 221     9419   8693   9054    668    149    -89       C  
ATOM   1459  O   PRO A 221       5.509  10.381  35.085  1.00 73.68           O  
ANISOU 1459  O   PRO A 221     9686   8973   9336    677    144    -67       O  
ATOM   1460  CB  PRO A 221       3.757  11.975  37.360  1.00 64.33           C  
ANISOU 1460  CB  PRO A 221     8454   7808   8179    645     80   -145       C  
ATOM   1461  CG  PRO A 221       2.719  11.905  38.419  1.00 68.12           C  
ANISOU 1461  CG  PRO A 221     8935   8295   8652    622     80   -194       C  
ATOM   1462  CD  PRO A 221       2.743  10.504  38.896  1.00 68.46           C  
ANISOU 1462  CD  PRO A 221     9025   8326   8662    610    128   -200       C  
ATOM   1463  N   GLY A 222       5.867   9.586  37.174  1.00 78.49           N  
ANISOU 1463  N   GLY A 222    10326   9567   9930    685    169    -65       N  
ATOM   1464  CA  GLY A 222       7.220   9.158  36.851  1.00 72.41           C  
ANISOU 1464  CA  GLY A 222     9567   8792   9155    720    186     -9       C  
ATOM   1465  C   GLY A 222       7.288   8.076  35.788  1.00 64.28           C  
ANISOU 1465  C   GLY A 222     8578   7745   8101    725    235     -3       C  
ATOM   1466  O   GLY A 222       8.078   8.169  34.851  1.00 63.22           O  
ANISOU 1466  O   GLY A 222     8435   7615   7971    745    234     31       O  
ATOM   1467  N   ILE A 223       6.477   7.026  35.926  1.00 59.77           N  
ANISOU 1467  N   ILE A 223     8055   7154   7501    703    280    -37       N  
ATOM   1468  CA  ILE A 223       6.563   5.932  34.967  1.00 64.25           C  
ANISOU 1468  CA  ILE A 223     8670   7700   8040    702    335    -33       C  
ATOM   1469  C   ILE A 223       5.924   6.335  33.643  1.00 63.28           C  
ANISOU 1469  C   ILE A 223     8527   7594   7922    673    324    -55       C  
ATOM   1470  O   ILE A 223       6.440   6.018  32.567  1.00 66.21           O  
ANISOU 1470  O   ILE A 223     8909   7961   8288    682    344    -33       O  
ATOM   1471  CB  ILE A 223       5.945   4.632  35.524  1.00 66.34           C  
ANISOU 1471  CB  ILE A 223     9005   7936   8266    682    393    -62       C  
ATOM   1472  CG1 ILE A 223       4.566   4.867  36.138  1.00 76.59           C  
ANISOU 1472  CG1 ILE A 223    10296   9249   9557    633    378   -122       C  
ATOM   1473  CG2 ILE A 223       6.880   4.032  36.540  1.00 70.58           C  
ANISOU 1473  CG2 ILE A 223     9570   8453   8795    724    415    -23       C  
ATOM   1474  CD1 ILE A 223       4.195   3.808  37.208  1.00 81.40           C  
ANISOU 1474  CD1 ILE A 223    10964   9833  10131    618    421   -143       C  
ATOM   1475  N   VAL A 224       4.802   7.051  33.701  1.00 60.56           N  
ANISOU 1475  N   VAL A 224     8151   7274   7585    640    292    -98       N  
ATOM   1476  CA  VAL A 224       4.170   7.566  32.486  1.00 61.81           C  
ANISOU 1476  CA  VAL A 224     8280   7458   7747    615    275   -115       C  
ATOM   1477  C   VAL A 224       5.182   8.317  31.627  1.00 60.87           C  
ANISOU 1477  C   VAL A 224     8127   7345   7658    644    244    -69       C  
ATOM   1478  O   VAL A 224       5.333   8.046  30.436  1.00 72.63           O  
ANISOU 1478  O   VAL A 224     9620   8838   9138    636    261    -60       O  
ATOM   1479  CB  VAL A 224       2.964   8.449  32.850  1.00 57.55           C  
ANISOU 1479  CB  VAL A 224     7701   6949   7216    591    236   -158       C  
ATOM   1480  CG1 VAL A 224       2.522   9.249  31.670  1.00 52.47           C  
ANISOU 1480  CG1 VAL A 224     7016   6336   6584    581    207   -162       C  
ATOM   1481  CG2 VAL A 224       1.832   7.576  33.354  1.00 57.05           C  
ANISOU 1481  CG2 VAL A 224     7673   6890   7113    550    273   -210       C  
ATOM   1482  N   MET A 225       5.913   9.249  32.222  1.00 58.94           N  
ANISOU 1482  N   MET A 225     7849   7104   7442    673    199    -41       N  
ATOM   1483  CA  MET A 225       6.881  10.016  31.452  1.00 62.64           C  
ANISOU 1483  CA  MET A 225     8286   7582   7932    694    167      1       C  
ATOM   1484  C   MET A 225       8.151   9.240  31.144  1.00 72.16           C  
ANISOU 1484  C   MET A 225     9515   8776   9126    723    199     45       C  
ATOM   1485  O   MET A 225       8.881   9.614  30.223  1.00 76.89           O  
ANISOU 1485  O   MET A 225    10094   9387   9733    733    184     75       O  
ATOM   1486  CB  MET A 225       7.259  11.292  32.192  1.00 56.45           C  
ANISOU 1486  CB  MET A 225     7463   6808   7177    707    112     15       C  
ATOM   1487  CG  MET A 225       6.148  12.293  32.301  1.00 58.36           C  
ANISOU 1487  CG  MET A 225     7677   7061   7436    688     75    -21       C  
ATOM   1488  SD  MET A 225       6.842  13.771  33.013  1.00 74.27           S  
ANISOU 1488  SD  MET A 225     9659   9080   9481    703     18      2       S  
ATOM   1489  CE  MET A 225       7.376  13.079  34.573  1.00 69.74           C  
ANISOU 1489  CE  MET A 225     9105   8497   8895    712     42     10       C  
ATOM   1490  N   MET A 226       8.454   8.191  31.896  1.00 69.94           N  
ANISOU 1490  N   MET A 226     9276   8476   8824    740    243     52       N  
ATOM   1491  CA  MET A 226       9.635   7.409  31.563  1.00 70.25           C  
ANISOU 1491  CA  MET A 226     9339   8506   8848    776    278     96       C  
ATOM   1492  C   MET A 226       9.345   6.444  30.421  1.00 74.53           C  
ANISOU 1492  C   MET A 226     9921   9030   9368    761    329     84       C  
ATOM   1493  O   MET A 226      10.208   6.204  29.569  1.00 83.46           O  
ANISOU 1493  O   MET A 226    11053  10163  10495    782    343    116       O  
ATOM   1494  CB  MET A 226      10.129   6.664  32.789  1.00 78.63           C  
ANISOU 1494  CB  MET A 226    10432   9552   9892    807    307    114       C  
ATOM   1495  CG  MET A 226      11.389   5.905  32.569  1.00 97.42           C  
ANISOU 1495  CG  MET A 226    12833  11927  12254    856    343    165       C  
ATOM   1496  SD  MET A 226      11.759   5.069  34.091  1.00126.31           S  
ANISOU 1496  SD  MET A 226    16528  15572  15891    892    376    184       S  
ATOM   1497  CE  MET A 226      12.502   6.391  35.044  1.00130.31           C  
ANISOU 1497  CE  MET A 226    16964  16128  16420    903    309    214       C  
ATOM   1498  N   VAL A 227       8.141   5.875  30.388  1.00 63.05           N  
ANISOU 1498  N   VAL A 227     8500   7563   7895    721    360     36       N  
ATOM   1499  CA  VAL A 227       7.751   5.090  29.230  1.00 62.79           C  
ANISOU 1499  CA  VAL A 227     8500   7520   7838    693    407     19       C  
ATOM   1500  C   VAL A 227       7.664   5.991  28.005  1.00 63.12           C  
ANISOU 1500  C   VAL A 227     8490   7594   7900    673    368     21       C  
ATOM   1501  O   VAL A 227       8.190   5.659  26.939  1.00 70.64           O  
ANISOU 1501  O   VAL A 227     9449   8544   8846    675    389     39       O  
ATOM   1502  CB  VAL A 227       6.428   4.357  29.488  1.00 61.75           C  
ANISOU 1502  CB  VAL A 227     8410   7377   7673    643    447    -36       C  
ATOM   1503  CG1 VAL A 227       5.845   3.897  28.158  1.00 66.61           C  
ANISOU 1503  CG1 VAL A 227     9043   8001   8266    597    482    -60       C  
ATOM   1504  CG2 VAL A 227       6.667   3.163  30.365  1.00 63.46           C  
ANISOU 1504  CG2 VAL A 227     8699   7553   7862    661    504    -33       C  
ATOM   1505  N   ALA A 228       7.064   7.173  28.159  1.00 56.47           N  
ANISOU 1505  N   ALA A 228     7595   6778   7082    659    309      5       N  
ATOM   1506  CA  ALA A 228       6.864   8.073  27.027  1.00 53.75           C  
ANISOU 1506  CA  ALA A 228     7204   6464   6755    641    271      7       C  
ATOM   1507  C   ALA A 228       8.193   8.583  26.477  1.00 67.18           C  
ANISOU 1507  C   ALA A 228     8879   8170   8475    673    244     57       C  
ATOM   1508  O   ALA A 228       8.491   8.412  25.289  1.00 80.76           O  
ANISOU 1508  O   ALA A 228    10596   9898  10191    662    255     68       O  
ATOM   1509  CB  ALA A 228       5.959   9.242  27.429  1.00 47.76           C  
ANISOU 1509  CB  ALA A 228     6401   5729   6016    628    216    -18       C  
ATOM   1510  N   TYR A 229       9.003   9.236  27.314  1.00 63.87           N  
ANISOU 1510  N   TYR A 229     8441   7753   8076    706    208     85       N  
ATOM   1511  CA  TYR A 229      10.298   9.717  26.833  1.00 61.41           C  
ANISOU 1511  CA  TYR A 229     8105   7455   7774    731    183    132       C  
ATOM   1512  C   TYR A 229      11.199   8.572  26.412  1.00 63.46           C  
ANISOU 1512  C   TYR A 229     8398   7704   8012    756    235    158       C  
ATOM   1513  O   TYR A 229      12.116   8.777  25.609  1.00 69.33           O  
ANISOU 1513  O   TYR A 229     9122   8464   8757    767    224    190       O  
ATOM   1514  CB  TYR A 229      10.977  10.595  27.890  1.00 53.17           C  
ANISOU 1514  CB  TYR A 229     7035   6421   6745    755    139    155       C  
ATOM   1515  CG  TYR A 229      10.355  11.963  27.904  1.00 57.89           C  
ANISOU 1515  CG  TYR A 229     7596   7030   7368    734     82    139       C  
ATOM   1516  CD1 TYR A 229      10.217  12.658  26.726  1.00 56.36           C  
ANISOU 1516  CD1 TYR A 229     7378   6851   7186    716     54    141       C  
ATOM   1517  CD2 TYR A 229       9.850  12.533  29.067  1.00 61.08           C  
ANISOU 1517  CD2 TYR A 229     7994   7429   7783    732     60    120       C  
ATOM   1518  CE1 TYR A 229       9.649  13.884  26.671  1.00 60.11           C  
ANISOU 1518  CE1 TYR A 229     7826   7332   7681    703      5    130       C  
ATOM   1519  CE2 TYR A 229       9.254  13.795  29.021  1.00 68.56           C  
ANISOU 1519  CE2 TYR A 229     8914   8384   8754    718     12    105       C  
ATOM   1520  CZ  TYR A 229       9.159  14.461  27.796  1.00 63.99           C  
ANISOU 1520  CZ  TYR A 229     8314   7815   8183    706    -15    112       C  
ATOM   1521  OH  TYR A 229       8.588  15.702  27.638  1.00 63.71           O  
ANISOU 1521  OH  TYR A 229     8256   7783   8169    698    -59    101       O  
ATOM   1522  N   GLY A 230      10.927   7.366  26.901  1.00 61.94           N  
ANISOU 1522  N   GLY A 230     8257   7481   7794    762    294    144       N  
ATOM   1523  CA  GLY A 230      11.681   6.215  26.444  1.00 67.61           C  
ANISOU 1523  CA  GLY A 230     9018   8183   8490    788    352    167       C  
ATOM   1524  C   GLY A 230      11.303   5.779  25.041  1.00 70.74           C  
ANISOU 1524  C   GLY A 230     9427   8576   8876    753    382    150       C  
ATOM   1525  O   GLY A 230      12.173   5.432  24.244  1.00 71.63           O  
ANISOU 1525  O   GLY A 230     9544   8691   8982    772    401    177       O  
ATOM   1526  N   LEU A 231       9.999   5.782  24.725  1.00 69.32           N  
ANISOU 1526  N   LEU A 231     9252   8396   8691    701    388    104       N  
ATOM   1527  CA  LEU A 231       9.544   5.436  23.375  1.00 60.79           C  
ANISOU 1527  CA  LEU A 231     8178   7323   7598    657    415     85       C  
ATOM   1528  C   LEU A 231       9.936   6.514  22.369  1.00 64.50           C  
ANISOU 1528  C   LEU A 231     8585   7828   8092    649    359    106       C  
ATOM   1529  O   LEU A 231      10.489   6.212  21.301  1.00 71.46           O  
ANISOU 1529  O   LEU A 231     9467   8716   8969    644    378    121       O  
ATOM   1530  CB  LEU A 231       8.033   5.215  23.369  1.00 50.36           C  
ANISOU 1530  CB  LEU A 231     6871   6007   6258    600    434     32       C  
ATOM   1531  CG  LEU A 231       7.580   3.964  24.141  1.00 57.13           C  
ANISOU 1531  CG  LEU A 231     7801   6827   7079    593    501      6       C  
ATOM   1532  CD1 LEU A 231       6.086   3.782  24.110  1.00 52.47           C  
ANISOU 1532  CD1 LEU A 231     7221   6254   6463    530    517    -48       C  
ATOM   1533  CD2 LEU A 231       8.240   2.737  23.609  1.00 62.57           C  
ANISOU 1533  CD2 LEU A 231     8553   7480   7741    604    574     20       C  
ATOM   1534  N   ILE A 232       9.657   7.780  22.701  1.00 62.24           N  
ANISOU 1534  N   ILE A 232     8248   7565   7833    648    292    106       N  
ATOM   1535  CA  ILE A 232      10.153   8.914  21.918  1.00 53.46           C  
ANISOU 1535  CA  ILE A 232     7083   6484   6745    646    233    130       C  
ATOM   1536  C   ILE A 232      11.628   8.740  21.597  1.00 68.73           C  
ANISOU 1536  C   ILE A 232     9016   8420   8679    680    236    174       C  
ATOM   1537  O   ILE A 232      12.067   8.955  20.461  1.00 83.16           O  
ANISOU 1537  O   ILE A 232    10821  10266  10508    667    226    189       O  
ATOM   1538  CB  ILE A 232       9.927  10.230  22.679  1.00 60.33           C  
ANISOU 1538  CB  ILE A 232     7916   7366   7642    656    167    131       C  
ATOM   1539  CG1 ILE A 232       8.458  10.639  22.679  1.00 72.59           C  
ANISOU 1539  CG1 ILE A 232     9455   8929   9197    623    154     91       C  
ATOM   1540  CG2 ILE A 232      10.813  11.329  22.123  1.00 54.31           C  
ANISOU 1540  CG2 ILE A 232     7112   6624   6898    664    112    166       C  
ATOM   1541  CD1 ILE A 232       8.227  11.973  23.381  1.00 72.33           C  
ANISOU 1541  CD1 ILE A 232     9389   8902   9190    636     92     92       C  
ATOM   1542  N   SER A 233      12.421   8.366  22.605  1.00 66.66           N  
ANISOU 1542  N   SER A 233     8774   8145   8410    726    250    197       N  
ATOM   1543  CA  SER A 233      13.865   8.287  22.425  1.00 64.98           C  
ANISOU 1543  CA  SER A 233     8552   7947   8191    764    248    241       C  
ATOM   1544  C   SER A 233      14.239   7.155  21.477  1.00 62.18           C  
ANISOU 1544  C   SER A 233     8230   7581   7815    768    308    246       C  
ATOM   1545  O   SER A 233      15.160   7.300  20.670  1.00 65.39           O  
ANISOU 1545  O   SER A 233     8614   8011   8220    777    298    274       O  
ATOM   1546  CB  SER A 233      14.565   8.110  23.781  1.00 67.04           C  
ANISOU 1546  CB  SER A 233     8822   8205   8444    813    252    266       C  
ATOM   1547  OG  SER A 233      14.900   9.366  24.372  1.00 63.61           O  
ANISOU 1547  OG  SER A 233     8344   7798   8026    814    187    281       O  
ATOM   1548  N   LEU A 234      13.553   6.015  21.582  1.00 63.67           N  
ANISOU 1548  N   LEU A 234     8474   7733   7984    759    374    219       N  
ATOM   1549  CA  LEU A 234      13.763   4.917  20.645  1.00 67.11           C  
ANISOU 1549  CA  LEU A 234     8950   8150   8398    754    440    218       C  
ATOM   1550  C   LEU A 234      13.542   5.371  19.204  1.00 69.72           C  
ANISOU 1550  C   LEU A 234     9246   8508   8737    704    420    208       C  
ATOM   1551  O   LEU A 234      14.392   5.167  18.333  1.00 65.01           O  
ANISOU 1551  O   LEU A 234     8642   7922   8135    713    431    230       O  
ATOM   1552  CB  LEU A 234      12.808   3.770  20.973  1.00 65.61           C  
ANISOU 1552  CB  LEU A 234     8830   7916   8182    733    510    181       C  
ATOM   1553  CG  LEU A 234      13.165   2.746  22.026  1.00 74.48           C  
ANISOU 1553  CG  LEU A 234    10016   9000   9284    783    564    192       C  
ATOM   1554  CD1 LEU A 234      12.552   1.423  21.598  1.00 81.25           C  
ANISOU 1554  CD1 LEU A 234    10952   9813  10107    754    652    161       C  
ATOM   1555  CD2 LEU A 234      14.669   2.642  22.221  1.00 79.95           C  
ANISOU 1555  CD2 LEU A 234    10699   9703   9975    856    563    246       C  
ATOM   1556  N   GLU A 235      12.378   5.960  18.935  1.00 67.56           N  
ANISOU 1556  N   GLU A 235     8950   8248   8474    651    393    175       N  
ATOM   1557  CA  GLU A 235      12.081   6.480  17.612  1.00 61.73           C  
ANISOU 1557  CA  GLU A 235     8173   7540   7742    602    370    168       C  
ATOM   1558  C   GLU A 235      13.176   7.423  17.140  1.00 64.38           C  
ANISOU 1558  C   GLU A 235     8456   7906   8097    622    311    207       C  
ATOM   1559  O   GLU A 235      13.832   7.164  16.130  1.00 84.93           O  
ANISOU 1559  O   GLU A 235    11054  10522  10694    614    325    221       O  
ATOM   1560  CB  GLU A 235      10.728   7.185  17.631  1.00 80.09           C  
ANISOU 1560  CB  GLU A 235    10471   9884  10075    558    337    135       C  
ATOM   1561  CG  GLU A 235      10.226   7.610  16.269  1.00 96.32           C  
ANISOU 1561  CG  GLU A 235    12489  11975  12133    504    320    125       C  
ATOM   1562  CD  GLU A 235       9.432   6.521  15.571  1.00107.19           C  
ANISOU 1562  CD  GLU A 235    13901  13350  13476    451    391     91       C  
ATOM   1563  OE1 GLU A 235       9.166   5.475  16.210  1.00110.27           O  
ANISOU 1563  OE1 GLU A 235    14350  13706  13840    455    452     71       O  
ATOM   1564  OE2 GLU A 235       9.072   6.721  14.388  1.00109.52           O  
ANISOU 1564  OE2 GLU A 235    14166  13679  13766    403    387     84       O  
ATOM   1565  N   LEU A 236      13.415   8.509  17.876  1.00 55.42           N  
ANISOU 1565  N   LEU A 236     7288   6786   6983    643    247    223       N  
ATOM   1566  CA  LEU A 236      14.417   9.481  17.446  1.00 57.78           C  
ANISOU 1566  CA  LEU A 236     7542   7118   7295    652    190    257       C  
ATOM   1567  C   LEU A 236      15.787   8.855  17.211  1.00 63.28           C  
ANISOU 1567  C   LEU A 236     8246   7822   7974    688    216    290       C  
ATOM   1568  O   LEU A 236      16.619   9.442  16.514  1.00 69.95           O  
ANISOU 1568  O   LEU A 236     9055   8701   8820    684    180    314       O  
ATOM   1569  CB  LEU A 236      14.560  10.613  18.464  1.00 52.91           C  
ANISOU 1569  CB  LEU A 236     6900   6508   6694    671    129    269       C  
ATOM   1570  CG  LEU A 236      13.342  11.486  18.787  1.00 62.95           C  
ANISOU 1570  CG  LEU A 236     8158   7776   7986    645     92    242       C  
ATOM   1571  CD1 LEU A 236      13.780  12.697  19.583  1.00 64.30           C  
ANISOU 1571  CD1 LEU A 236     8304   7955   8170    662     32    260       C  
ATOM   1572  CD2 LEU A 236      12.627  11.939  17.529  1.00 69.47           C  
ANISOU 1572  CD2 LEU A 236     8957   8619   8818    599     74    228       C  
ATOM   1573  N   TYR A 237      16.051   7.681  17.768  1.00 68.76           N  
ANISOU 1573  N   TYR A 237     8987   8489   8648    726    278    292       N  
ATOM   1574  CA  TYR A 237      17.352   7.073  17.538  1.00 65.47           C  
ANISOU 1574  CA  TYR A 237     8578   8086   8213    770    306    326       C  
ATOM   1575  C   TYR A 237      17.384   6.373  16.190  1.00 78.08           C  
ANISOU 1575  C   TYR A 237    10189   9679   9800    743    349    316       C  
ATOM   1576  O   TYR A 237      18.398   6.418  15.481  1.00 87.36           O  
ANISOU 1576  O   TYR A 237    11341  10885  10968    755    342    342       O  
ATOM   1577  CB  TYR A 237      17.676   6.095  18.655  1.00 52.30           C  
ANISOU 1577  CB  TYR A 237     6957   6388   6525    829    358    338       C  
ATOM   1578  CG  TYR A 237      18.894   5.262  18.398  1.00 57.57           C  
ANISOU 1578  CG  TYR A 237     7640   7065   7168    882    401    371       C  
ATOM   1579  CD1 TYR A 237      18.797   4.040  17.740  1.00 65.04           C  
ANISOU 1579  CD1 TYR A 237     8639   7975   8096    885    478    360       C  
ATOM   1580  CD2 TYR A 237      20.136   5.666  18.851  1.00 63.88           C  
ANISOU 1580  CD2 TYR A 237     8404   7910   7957    931    370    414       C  
ATOM   1581  CE1 TYR A 237      19.906   3.262  17.511  1.00 74.02           C  
ANISOU 1581  CE1 TYR A 237     9795   9119   9211    942    521    391       C  
ATOM   1582  CE2 TYR A 237      21.254   4.893  18.635  1.00 79.93           C  
ANISOU 1582  CE2 TYR A 237    10448   9959   9963    988    410    447       C  
ATOM   1583  CZ  TYR A 237      21.134   3.693  17.959  1.00 88.28           C  
ANISOU 1583  CZ  TYR A 237    11559  10976  11007    997    486    436       C  
ATOM   1584  OH  TYR A 237      22.250   2.922  17.735  1.00104.17           O  
ANISOU 1584  OH  TYR A 237    13584  13003  12992   1060    529    469       O  
ATOM   1585  N   GLN A 238      16.272   5.736  15.824  1.00 75.65           N  
ANISOU 1585  N   GLN A 238     9916   9340   9488    701    395    279       N  
ATOM   1586  CA  GLN A 238      16.189   5.008  14.568  1.00 71.79           C  
ANISOU 1586  CA  GLN A 238     9446   8846   8986    666    445    265       C  
ATOM   1587  C   GLN A 238      16.300   5.930  13.353  1.00 70.31           C  
ANISOU 1587  C   GLN A 238     9198   8704   8814    618    390    269       C  
ATOM   1588  O   GLN A 238      16.728   5.482  12.280  1.00 83.82           O  
ANISOU 1588  O   GLN A 238    10909  10424  10514    600    419    271       O  
ATOM   1589  CB  GLN A 238      14.911   4.175  14.580  1.00 64.13           C  
ANISOU 1589  CB  GLN A 238     8527   7838   8000    624    505    221       C  
ATOM   1590  CG  GLN A 238      15.163   2.876  15.326  1.00 70.52           C  
ANISOU 1590  CG  GLN A 238     9414   8598   8785    670    584    222       C  
ATOM   1591  CD  GLN A 238      13.926   2.069  15.589  1.00 90.36           C  
ANISOU 1591  CD  GLN A 238    11987  11072  11276    630    643    179       C  
ATOM   1592  OE1 GLN A 238      13.046   1.952  14.737  1.00 94.82           O  
ANISOU 1592  OE1 GLN A 238    12552  11645  11831    559    662    146       O  
ATOM   1593  NE2 GLN A 238      13.848   1.494  16.785  1.00100.70           N  
ANISOU 1593  NE2 GLN A 238    13345  12342  12573    670    674    179       N  
ATOM   1594  N   GLY A 239      15.942   7.196  13.502  1.00 59.30           N  
ANISOU 1594  N   GLY A 239     7755   7335   7442    598    316    270       N  
ATOM   1595  CA  GLY A 239      16.409   8.221  12.597  1.00 68.63           C  
ANISOU 1595  CA  GLY A 239     8880   8560   8636    572    253    287       C  
ATOM   1596  C   GLY A 239      15.674   8.295  11.267  1.00 73.46           C  
ANISOU 1596  C   GLY A 239     9473   9189   9251    504    256    266       C  
ATOM   1597  O   GLY A 239      14.571   7.773  11.070  1.00 75.70           O  
ANISOU 1597  O   GLY A 239     9779   9458   9527    466    296    233       O  
ATOM   1598  N   ILE A 240      16.339   8.966  10.329  1.00 72.68           N  
ANISOU 1598  N   ILE A 240     9330   9126   9157    483    212    285       N  
ATOM   1599  CA  ILE A 240      15.763   9.255   9.023  1.00 73.86           C  
ANISOU 1599  CA  ILE A 240     9450   9302   9310    417    200    272       C  
ATOM   1600  C   ILE A 240      15.660   7.990   8.171  1.00 70.92           C  
ANISOU 1600  C   ILE A 240     9107   8920   8917    387    279    253       C  
ATOM   1601  O   ILE A 240      16.447   7.043   8.299  1.00 74.56           O  
ANISOU 1601  O   ILE A 240     9604   9362   9363    423    332    260       O  
ATOM   1602  CB  ILE A 240      16.630  10.318   8.335  1.00 69.31           C  
ANISOU 1602  CB  ILE A 240     8824   8768   8745    406    131    300       C  
ATOM   1603  CG1 ILE A 240      16.943  11.446   9.331  1.00 51.80           C  
ANISOU 1603  CG1 ILE A 240     6590   6552   6540    440     64    321       C  
ATOM   1604  CG2 ILE A 240      15.960  10.825   7.062  1.00 71.54           C  
ANISOU 1604  CG2 ILE A 240     9069   9080   9034    338    106    291       C  
ATOM   1605  CD1 ILE A 240      15.827  12.439   9.484  1.00 55.24           C  
ANISOU 1605  CD1 ILE A 240     7008   6985   6994    417     19    309       C  
ATOM   1606  N   ASN A1241      14.653   7.955   7.318  1.00 58.51           N  
ANISOU 1606  N   ASN A1241     7523   7365   7342    322    292    228       N  
ATOM   1607  CA  ASN A1241      14.467   6.848   6.400  1.00 60.81           C  
ANISOU 1607  CA  ASN A1241     7841   7653   7610    277    366    207       C  
ATOM   1608  C   ASN A1241      14.006   7.420   5.061  1.00 67.14           C  
ANISOU 1608  C   ASN A1241     8590   8504   8415    204    337    202       C  
ATOM   1609  O   ASN A1241      13.850   8.637   4.898  1.00 70.62           O  
ANISOU 1609  O   ASN A1241     8980   8976   8876    195    260    217       O  
ATOM   1610  CB  ASN A1241      13.450   5.864   6.959  1.00 56.06           C  
ANISOU 1610  CB  ASN A1241     7296   7016   6986    265    438    172       C  
ATOM   1611  CG  ASN A1241      12.141   6.547   7.253  1.00 70.29           C  
ANISOU 1611  CG  ASN A1241     9073   8839   8794    235    403    153       C  
ATOM   1612  OD1 ASN A1241      11.428   6.981   6.340  1.00 76.55           O  
ANISOU 1612  OD1 ASN A1241     9826   9676   9585    175    384    144       O  
ATOM   1613  ND2 ASN A1241      11.837   6.703   8.536  1.00 85.33           N  
ANISOU 1613  ND2 ASN A1241    10998  10717  10705    279    391    151       N  
ATOM   1614  N   ILE A1242      13.752   6.530   4.101  1.00 65.79           N  
ANISOU 1614  N   ILE A1242     8435   8339   8222    148    401    180       N  
ATOM   1615  CA  ILE A1242      13.392   6.978   2.759  1.00 62.90           C  
ANISOU 1615  CA  ILE A1242     8017   8026   7856     74    378    177       C  
ATOM   1616  C   ILE A1242      12.159   7.867   2.798  1.00 62.23           C  
ANISOU 1616  C   ILE A1242     7892   7975   7777     43    331    171       C  
ATOM   1617  O   ILE A1242      12.097   8.889   2.106  1.00 68.69           O  
ANISOU 1617  O   ILE A1242     8654   8836   8611     18    266    188       O  
ATOM   1618  CB  ILE A1242      13.201   5.771   1.822  1.00 69.67           C  
ANISOU 1618  CB  ILE A1242     8904   8883   8682     12    466    150       C  
ATOM   1619  CG1 ILE A1242      12.811   6.238   0.415  1.00 72.17           C  
ANISOU 1619  CG1 ILE A1242     9162   9263   8997    -71    443    148       C  
ATOM   1620  CG2 ILE A1242      12.191   4.794   2.408  1.00 76.72           C  
ANISOU 1620  CG2 ILE A1242     9857   9746   9546     -4    543    114       C  
ATOM   1621  CD1 ILE A1242      13.938   7.007  -0.342  1.00 63.72           C  
ANISOU 1621  CD1 ILE A1242     8041   8221   7948    -66    380    180       C  
ATOM   1622  N   PHE A1243      11.181   7.527   3.640  1.00 65.16           N  
ANISOU 1622  N   PHE A1243     8294   8328   8136     49    360    147       N  
ATOM   1623  CA  PHE A1243       9.942   8.304   3.674  1.00 61.37           C  
ANISOU 1623  CA  PHE A1243     7774   7886   7656     23    321    139       C  
ATOM   1624  C   PHE A1243      10.183   9.720   4.186  1.00 60.17           C  
ANISOU 1624  C   PHE A1243     7585   7738   7540     74    228    169       C  
ATOM   1625  O   PHE A1243       9.743  10.694   3.562  1.00 66.24           O  
ANISOU 1625  O   PHE A1243     8301   8550   8318     49    173    182       O  
ATOM   1626  CB  PHE A1243       8.895   7.581   4.512  1.00 57.37           C  
ANISOU 1626  CB  PHE A1243     7311   7364   7124     19    375    104       C  
ATOM   1627  CG  PHE A1243       8.601   6.196   4.034  1.00 56.64           C  
ANISOU 1627  CG  PHE A1243     7265   7264   6989    -38    472     71       C  
ATOM   1628  CD1 PHE A1243       7.618   5.971   3.100  1.00 61.78           C  
ANISOU 1628  CD1 PHE A1243     7893   7972   7608   -123    501     48       C  
ATOM   1629  CD2 PHE A1243       9.306   5.116   4.519  1.00 56.51           C  
ANISOU 1629  CD2 PHE A1243     7321   7188   6964     -7    537     64       C  
ATOM   1630  CE1 PHE A1243       7.347   4.683   2.645  1.00 70.87           C  
ANISOU 1630  CE1 PHE A1243     9094   9118   8716   -184    597     15       C  
ATOM   1631  CE2 PHE A1243       9.038   3.823   4.075  1.00 60.69           C  
ANISOU 1631  CE2 PHE A1243     7905   7703   7452    -61    633     33       C  
ATOM   1632  CZ  PHE A1243       8.065   3.611   3.132  1.00 66.54           C  
ANISOU 1632  CZ  PHE A1243     8624   8498   8159   -153    663      6       C  
ATOM   1633  N   GLU A1244      10.920   9.863   5.292  1.00 51.63           N  
ANISOU 1633  N   GLU A1244     6531   6612   6475    142    210    183       N  
ATOM   1634  CA  GLU A1244      11.213  11.207   5.782  1.00 63.80           C  
ANISOU 1634  CA  GLU A1244     8042   8154   8045    184    126    211       C  
ATOM   1635  C   GLU A1244      12.089  11.959   4.799  1.00 69.38           C  
ANISOU 1635  C   GLU A1244     8710   8888   8765    167     75    240       C  
ATOM   1636  O   GLU A1244      11.942  13.179   4.635  1.00 69.12           O  
ANISOU 1636  O   GLU A1244     8641   8874   8748    168      6    259       O  
ATOM   1637  CB  GLU A1244      11.897  11.166   7.158  1.00 71.99           C  
ANISOU 1637  CB  GLU A1244     9115   9145   9093    253    122    220       C  
ATOM   1638  CG  GLU A1244      11.416  10.062   8.098  1.00 93.79           C  
ANISOU 1638  CG  GLU A1244    11929  11870  11836    271    190    192       C  
ATOM   1639  CD  GLU A1244       9.923  10.151   8.461  1.00103.11           C  
ANISOU 1639  CD  GLU A1244    13107  13062  13008    250    196    163       C  
ATOM   1640  OE1 GLU A1244       9.269  11.183   8.167  1.00100.85           O  
ANISOU 1640  OE1 GLU A1244    12777  12809  12733    236    142    168       O  
ATOM   1641  OE2 GLU A1244       9.404   9.167   9.035  1.00101.35           O  
ANISOU 1641  OE2 GLU A1244    12928  12817  12763    248    257    135       O  
ATOM   1642  N   MET A1245      13.019  11.239   4.153  1.00 66.89           N  
ANISOU 1642  N   MET A1245     8402   8573   8439    153    108    244       N  
ATOM   1643  CA  MET A1245      13.901  11.836   3.150  1.00 62.61           C  
ANISOU 1643  CA  MET A1245     7823   8062   7904    130     64    269       C  
ATOM   1644  C   MET A1245      13.107  12.386   1.972  1.00 57.29           C  
ANISOU 1644  C   MET A1245     7102   7435   7229     65     38    268       C  
ATOM   1645  O   MET A1245      13.287  13.544   1.573  1.00 57.04           O  
ANISOU 1645  O   MET A1245     7034   7426   7212     59    -32    292       O  
ATOM   1646  CB  MET A1245      14.922  10.800   2.681  1.00 65.00           C  
ANISOU 1646  CB  MET A1245     8146   8360   8192    127    116    268       C  
ATOM   1647  CG  MET A1245      15.932  11.290   1.640  1.00 61.57           C  
ANISOU 1647  CG  MET A1245     7673   7961   7760    102     76    290       C  
ATOM   1648  SD  MET A1245      16.728   9.867   0.850  1.00 64.27           S  
ANISOU 1648  SD  MET A1245     8038   8303   8080     84    157    278       S  
ATOM   1649  CE  MET A1245      18.144  10.621   0.037  1.00 63.23           C  
ANISOU 1649  CE  MET A1245     7860   8214   7950     75     93    308       C  
ATOM   1650  N   LEU A1246      12.191  11.583   1.422  1.00 52.39           N  
ANISOU 1650  N   LEU A1246     6484   6834   6589     15     96    241       N  
ATOM   1651  CA  LEU A1246      11.372  12.076   0.316  1.00 55.44           C  
ANISOU 1651  CA  LEU A1246     6820   7276   6970    -48     75    242       C  
ATOM   1652  C   LEU A1246      10.382  13.155   0.766  1.00 65.18           C  
ANISOU 1652  C   LEU A1246     8029   8524   8214    -28     20    251       C  
ATOM   1653  O   LEU A1246      10.041  14.044  -0.029  1.00 62.87           O  
ANISOU 1653  O   LEU A1246     7689   8272   7926    -55    -29    269       O  
ATOM   1654  CB  LEU A1246      10.656  10.916  -0.361  1.00 54.02           C  
ANISOU 1654  CB  LEU A1246     6648   7120   6758   -113    155    210       C  
ATOM   1655  CG  LEU A1246      11.599  10.113  -1.258  1.00 69.93           C  
ANISOU 1655  CG  LEU A1246     8672   9136   8764   -149    197    207       C  
ATOM   1656  CD1 LEU A1246      11.065   8.730  -1.535  1.00 74.60           C  
ANISOU 1656  CD1 LEU A1246     9300   9725   9321   -198    296    170       C  
ATOM   1657  CD2 LEU A1246      11.883  10.847  -2.566  1.00 63.94           C  
ANISOU 1657  CD2 LEU A1246     7853   8430   8011   -200    148    228       C  
ATOM   1658  N   ARG A1247       9.927  13.124   2.033  1.00 62.58           N  
ANISOU 1658  N   ARG A1247     7729   8159   7888     22     27    239       N  
ATOM   1659  CA  ARG A1247       9.045  14.195   2.503  1.00 58.82           C  
ANISOU 1659  CA  ARG A1247     7231   7694   7423     49    -25    247       C  
ATOM   1660  C   ARG A1247       9.770  15.535   2.546  1.00 63.84           C  
ANISOU 1660  C   ARG A1247     7852   8316   8086     82   -106    284       C  
ATOM   1661  O   ARG A1247       9.178  16.580   2.245  1.00 62.82           O  
ANISOU 1661  O   ARG A1247     7692   8212   7966     82   -156    300       O  
ATOM   1662  CB  ARG A1247       8.461  13.861   3.874  1.00 60.94           C  
ANISOU 1662  CB  ARG A1247     7537   7928   7690     93      1    225       C  
ATOM   1663  CG  ARG A1247       7.093  13.255   3.774  1.00 73.44           C  
ANISOU 1663  CG  ARG A1247     9112   9548   9242     56     48    194       C  
ATOM   1664  CD  ARG A1247       6.422  13.009   5.125  1.00 75.29           C  
ANISOU 1664  CD  ARG A1247     9380   9756   9472     96     68    170       C  
ATOM   1665  NE  ARG A1247       5.745  11.714   5.089  1.00 77.96           N  
ANISOU 1665  NE  ARG A1247     9743  10107   9770     51    148    132       N  
ATOM   1666  CZ  ARG A1247       6.186  10.622   5.703  1.00 73.68           C  
ANISOU 1666  CZ  ARG A1247     9259   9517   9218     60    207    112       C  
ATOM   1667  NH1 ARG A1247       7.284  10.674   6.466  1.00 61.85           N  
ANISOU 1667  NH1 ARG A1247     7794   7961   7746    117    192    129       N  
ATOM   1668  NH2 ARG A1247       5.505   9.488   5.568  1.00 70.23           N  
ANISOU 1668  NH2 ARG A1247     8850   9094   8740      9    282     77       N  
ATOM   1669  N   ILE A1248      11.054  15.530   2.903  1.00 61.96           N  
ANISOU 1669  N   ILE A1248     7638   8044   7859    109   -118    297       N  
ATOM   1670  CA  ILE A1248      11.804  16.782   2.891  1.00 63.22           C  
ANISOU 1670  CA  ILE A1248     7787   8196   8036    128   -191    329       C  
ATOM   1671  C   ILE A1248      12.053  17.247   1.462  1.00 68.21           C  
ANISOU 1671  C   ILE A1248     8379   8872   8666     75   -223    348       C  
ATOM   1672  O   ILE A1248      11.948  18.441   1.157  1.00 69.37           O  
ANISOU 1672  O   ILE A1248     8508   9028   8823     75   -285    372       O  
ATOM   1673  CB  ILE A1248      13.113  16.629   3.681  1.00 65.33           C  
ANISOU 1673  CB  ILE A1248     8087   8429   8308    167   -194    337       C  
ATOM   1674  CG1 ILE A1248      12.808  16.301   5.132  1.00 50.14           C  
ANISOU 1674  CG1 ILE A1248     6199   6465   6387    220   -169    322       C  
ATOM   1675  CG2 ILE A1248      13.939  17.906   3.612  1.00 64.42           C  
ANISOU 1675  CG2 ILE A1248     7962   8312   8201    174   -267    368       C  
ATOM   1676  CD1 ILE A1248      13.824  15.364   5.730  1.00 49.74           C  
ANISOU 1676  CD1 ILE A1248     6179   6391   6327    247   -128    319       C  
ATOM   1677  N   ASP A1249      12.345  16.317   0.552  1.00 74.14           N  
ANISOU 1677  N   ASP A1249     9118   9648   9402     27   -180    337       N  
ATOM   1678  CA  ASP A1249      12.680  16.723  -0.810  1.00 66.81           C  
ANISOU 1678  CA  ASP A1249     8151   8763   8472    -28   -210    355       C  
ATOM   1679  C   ASP A1249      11.463  17.118  -1.640  1.00 73.61           C  
ANISOU 1679  C   ASP A1249     8970   9671   9327    -68   -221    357       C  
ATOM   1680  O   ASP A1249      11.585  17.963  -2.535  1.00 77.02           O  
ANISOU 1680  O   ASP A1249     9370  10133   9763    -98   -272    382       O  
ATOM   1681  CB  ASP A1249      13.447  15.607  -1.509  1.00 60.70           C  
ANISOU 1681  CB  ASP A1249     7379   8002   7684    -66   -159    342       C  
ATOM   1682  CG  ASP A1249      14.913  15.581  -1.133  1.00 63.08           C  
ANISOU 1682  CG  ASP A1249     7700   8279   7987    -35   -173    354       C  
ATOM   1683  OD1 ASP A1249      15.458  16.661  -0.791  1.00 58.44           O  
ANISOU 1683  OD1 ASP A1249     7112   7684   7409    -10   -238    378       O  
ATOM   1684  OD2 ASP A1249      15.515  14.481  -1.185  1.00 64.13           O  
ANISOU 1684  OD2 ASP A1249     7852   8406   8108    -35   -116    339       O  
ATOM   1685  N   GLU A1250      10.301  16.523  -1.381  1.00 77.17           N  
ANISOU 1685  N   GLU A1250     9421  10136   9765    -73   -175    334       N  
ATOM   1686  CA  GLU A1250       9.106  16.750  -2.197  1.00 75.83           C  
ANISOU 1686  CA  GLU A1250     9206  10027   9581   -115   -176    335       C  
ATOM   1687  C   GLU A1250       8.121  17.724  -1.579  1.00 80.11           C  
ANISOU 1687  C   GLU A1250     9739  10570  10130    -68   -216    347       C  
ATOM   1688  O   GLU A1250       7.543  18.547  -2.294  1.00 84.25           O  
ANISOU 1688  O   GLU A1250    10222  11138  10651    -82   -255    370       O  
ATOM   1689  CB  GLU A1250       8.369  15.424  -2.454  1.00 72.65           C  
ANISOU 1689  CB  GLU A1250     8803   9655   9147   -164    -93    299       C  
ATOM   1690  CG  GLU A1250       9.182  14.369  -3.176  1.00 79.96           C  
ANISOU 1690  CG  GLU A1250     9739  10581  10061   -215    -41    284       C  
ATOM   1691  CD  GLU A1250       9.351  14.677  -4.644  1.00 96.56           C  
ANISOU 1691  CD  GLU A1250    11790  12740  12157   -283    -64    302       C  
ATOM   1692  OE1 GLU A1250       8.984  15.790  -5.079  1.00107.88           O  
ANISOU 1692  OE1 GLU A1250    13183  14207  13599   -283   -126    330       O  
ATOM   1693  OE2 GLU A1250       9.841  13.796  -5.374  1.00102.81           O  
ANISOU 1693  OE2 GLU A1250    12584  13544  12936   -336    -16    287       O  
ATOM   1694  N   GLY A1251       7.897  17.626  -0.269  1.00 75.63           N  
ANISOU 1694  N   GLY A1251     9209   9958   9570    -11   -204    332       N  
ATOM   1695  CA  GLY A1251       6.922  18.447   0.391  1.00 71.77           C  
ANISOU 1695  CA  GLY A1251     8714   9470   9085     36   -234    338       C  
ATOM   1696  C   GLY A1251       5.541  17.827   0.307  1.00 86.26           C  
ANISOU 1696  C   GLY A1251    10525  11360  10890     12   -188    312       C  
ATOM   1697  O   GLY A1251       5.373  16.646  -0.022  1.00 89.19           O  
ANISOU 1697  O   GLY A1251    10897  11756  11236    -39   -124    284       O  
ATOM   1698  N   LEU A1252       4.537  18.650   0.624  1.00 89.79           N  
ANISOU 1698  N   LEU A1252    10952  11830  11336     49   -218    322       N  
ATOM   1699  CA  LEU A1252       3.133  18.303   0.425  1.00 88.65           C  
ANISOU 1699  CA  LEU A1252    10770  11758  11156     27   -186    305       C  
ATOM   1700  C   LEU A1252       2.423  19.474  -0.236  1.00 95.59           C  
ANISOU 1700  C   LEU A1252    11597  12690  12032     42   -238    340       C  
ATOM   1701  O   LEU A1252       2.386  20.572   0.326  1.00 97.58           O  
ANISOU 1701  O   LEU A1252    11862  12907  12309    108   -290    363       O  
ATOM   1702  CB  LEU A1252       2.447  17.957   1.743  1.00 84.16           C  
ANISOU 1702  CB  LEU A1252    10229  11168  10580     69   -159    273       C  
ATOM   1703  CG  LEU A1252       1.743  16.603   1.767  1.00 89.49           C  
ANISOU 1703  CG  LEU A1252    10905  11884  11211     15    -81    230       C  
ATOM   1704  CD1 LEU A1252       0.910  16.464   3.020  1.00 85.88           C  
ANISOU 1704  CD1 LEU A1252    10468  11418  10744     57    -65    202       C  
ATOM   1705  CD2 LEU A1252       0.892  16.425   0.527  1.00100.86           C  
ANISOU 1705  CD2 LEU A1252    12285  13426  12611    -52    -63    233       C  
ATOM   1706  N   ARG A1253       1.881  19.241  -1.431  1.00 96.33           N  
ANISOU 1706  N   ARG A1253    11637  12868  12095    -20   -224    347       N  
ATOM   1707  CA  ARG A1253       0.955  20.160  -2.083  1.00 98.09           C  
ANISOU 1707  CA  ARG A1253    11803  13163  12304     -8   -261    379       C  
ATOM   1708  C   ARG A1253      -0.362  19.417  -2.269  1.00 94.73           C  
ANISOU 1708  C   ARG A1253    11333  12834  11825    -48   -209    354       C  
ATOM   1709  O   ARG A1253      -0.406  18.393  -2.962  1.00 86.37           O  
ANISOU 1709  O   ARG A1253    10258  11824  10735   -130   -156    331       O  
ATOM   1710  CB  ARG A1253       1.501  20.659  -3.427  1.00 98.23           C  
ANISOU 1710  CB  ARG A1253    11787  13208  12327    -50   -296    417       C  
ATOM   1711  CG  ARG A1253       2.977  21.068  -3.400  1.00106.01           C  
ANISOU 1711  CG  ARG A1253    12816  14108  13353    -40   -334    433       C  
ATOM   1712  CD  ARG A1253       3.193  22.582  -3.288  1.00116.94           C  
ANISOU 1712  CD  ARG A1253    14212  15454  14765     23   -409    476       C  
ATOM   1713  NE  ARG A1253       4.178  23.056  -4.268  1.00125.03           N  
ANISOU 1713  NE  ARG A1253    15233  16471  15804    -14   -448    506       N  
ATOM   1714  CZ  ARG A1253       4.705  24.279  -4.292  1.00126.69           C  
ANISOU 1714  CZ  ARG A1253    15466  16635  16035     22   -511    542       C  
ATOM   1715  NH1 ARG A1253       4.363  25.174  -3.376  1.00132.60           N  
ANISOU 1715  NH1 ARG A1253    16247  17338  16798    100   -540    553       N  
ATOM   1716  NH2 ARG A1253       5.584  24.608  -5.231  1.00120.56           N  
ANISOU 1716  NH2 ARG A1253    14684  15859  15264    -22   -543    564       N  
ATOM   1717  N   LEU A1254      -1.421  19.911  -1.615  1.00 92.62           N  
ANISOU 1717  N   LEU A1254    11050  12597  11544      8   -220    354       N  
ATOM   1718  CA  LEU A1254      -2.726  19.260  -1.694  1.00 89.82           C  
ANISOU 1718  CA  LEU A1254    10651  12344  11131    -27   -173    328       C  
ATOM   1719  C   LEU A1254      -3.387  19.507  -3.043  1.00 91.85           C  
ANISOU 1719  C   LEU A1254    10830  12718  11351    -75   -179    357       C  
ATOM   1720  O   LEU A1254      -4.237  18.715  -3.474  1.00 95.64           O  
ANISOU 1720  O   LEU A1254    11269  13297  11774   -142   -128    333       O  
ATOM   1721  CB  LEU A1254      -3.645  19.761  -0.576  1.00 89.13           C  
ANISOU 1721  CB  LEU A1254    10566  12260  11039     52   -186    320       C  
ATOM   1722  CG  LEU A1254      -3.413  19.556   0.939  1.00 90.54           C  
ANISOU 1722  CG  LEU A1254    10810  12348  11243    105   -177    288       C  
ATOM   1723  CD1 LEU A1254      -3.591  18.100   1.393  1.00 86.53           C  
ANISOU 1723  CD1 LEU A1254    10329  11847  10701     46   -103    232       C  
ATOM   1724  CD2 LEU A1254      -2.079  20.121   1.415  1.00 90.33           C  
ANISOU 1724  CD2 LEU A1254    10843  12200  11279    151   -217    305       C  
ATOM   1725  N   LYS A1255      -3.028  20.601  -3.707  1.00 86.33           N  
ANISOU 1725  N   LYS A1255    10110  12013  10679    -46   -240    407       N  
ATOM   1726  CA  LYS A1255      -3.618  20.967  -4.984  1.00 96.81           C  
ANISOU 1726  CA  LYS A1255    11361  13449  11973    -83   -253    443       C  
ATOM   1727  C   LYS A1255      -2.619  20.745  -6.111  1.00 96.29           C  
ANISOU 1727  C   LYS A1255    11291  13373  11921   -158   -257    457       C  
ATOM   1728  O   LYS A1255      -1.400  20.764  -5.907  1.00 87.08           O  
ANISOU 1728  O   LYS A1255    10179  12106  10799   -152   -273    454       O  
ATOM   1729  CB  LYS A1255      -4.098  22.426  -4.978  1.00105.12           C  
ANISOU 1729  CB  LYS A1255    12390  14513  13039      8   -319    495       C  
ATOM   1730  CG  LYS A1255      -3.044  23.463  -4.605  1.00104.27           C  
ANISOU 1730  CG  LYS A1255    12342  14282  12994     75   -380    524       C  
ATOM   1731  CD  LYS A1255      -3.671  24.851  -4.441  1.00106.69           C  
ANISOU 1731  CD  LYS A1255    12636  14594  13307    173   -434    570       C  
ATOM   1732  CE  LYS A1255      -4.443  25.267  -5.691  1.00113.44           C  
ANISOU 1732  CE  LYS A1255    13409  15568  14123    153   -448    614       C  
ATOM   1733  NZ  LYS A1255      -5.207  26.545  -5.542  1.00117.52           N  
ANISOU 1733  NZ  LYS A1255    13912  16103  14639    256   -492    660       N  
ATOM   1734  N   ILE A1256      -3.160  20.517  -7.310  1.00100.79           N  
ANISOU 1734  N   ILE A1256    11791  14057  12448   -231   -240    470       N  
ATOM   1735  CA  ILE A1256      -2.325  20.197  -8.460  1.00 93.64           C  
ANISOU 1735  CA  ILE A1256    10873  13158  11549   -314   -236    478       C  
ATOM   1736  C   ILE A1256      -1.337  21.328  -8.698  1.00 92.33           C  
ANISOU 1736  C   ILE A1256    10731  12916  11437   -267   -310    523       C  
ATOM   1737  O   ILE A1256      -1.653  22.508  -8.506  1.00 92.61           O  
ANISOU 1737  O   ILE A1256    10760  12942  11486   -188   -366    563       O  
ATOM   1738  CB  ILE A1256      -3.216  19.913  -9.681  1.00101.47           C  
ANISOU 1738  CB  ILE A1256    11777  14296  12480   -396   -211    490       C  
ATOM   1739  CG1 ILE A1256      -3.001  18.484 -10.177  1.00101.43           C  
ANISOU 1739  CG1 ILE A1256    11775  14320  12443   -513   -133    443       C  
ATOM   1740  CG2 ILE A1256      -3.013  20.955 -10.794  1.00110.66           C  
ANISOU 1740  CG2 ILE A1256    12893  15496  13656   -396   -273    550       C  
ATOM   1741  CD1 ILE A1256      -4.119  17.978 -11.073  1.00105.75           C  
ANISOU 1741  CD1 ILE A1256    12242  15023  12916   -601    -88    439       C  
ATOM   1742  N   TYR A1257      -0.107  20.965  -9.060  1.00 93.82           N  
ANISOU 1742  N   TYR A1257    10952  13044  11653   -314   -309    514       N  
ATOM   1743  CA  TYR A1257       0.955  21.945  -9.244  1.00 96.09           C  
ANISOU 1743  CA  TYR A1257    11268  13255  11985   -281   -375    550       C  
ATOM   1744  C   TYR A1257       1.956  21.422 -10.268  1.00 89.83           C  
ANISOU 1744  C   TYR A1257    10468  12465  11197   -370   -366    545       C  
ATOM   1745  O   TYR A1257       1.869  20.280 -10.728  1.00 86.66           O  
ANISOU 1745  O   TYR A1257    10049  12110  10769   -451   -304    512       O  
ATOM   1746  CB  TYR A1257       1.638  22.277  -7.911  1.00 97.31           C  
ANISOU 1746  CB  TYR A1257    11502  13290  12183   -200   -396    538       C  
ATOM   1747  CG  TYR A1257       2.552  21.205  -7.356  1.00 93.77           C  
ANISOU 1747  CG  TYR A1257    11105  12775  11747   -226   -351    494       C  
ATOM   1748  CD1 TYR A1257       2.035  20.082  -6.720  1.00 92.69           C  
ANISOU 1748  CD1 TYR A1257    10981  12650  11588   -241   -283    448       C  
ATOM   1749  CD2 TYR A1257       3.936  21.332  -7.444  1.00 92.88           C  
ANISOU 1749  CD2 TYR A1257    11032  12592  11667   -234   -376    499       C  
ATOM   1750  CE1 TYR A1257       2.876  19.104  -6.186  1.00 96.58           C  
ANISOU 1750  CE1 TYR A1257    11527  13078  12092   -257   -240    411       C  
ATOM   1751  CE2 TYR A1257       4.783  20.361  -6.916  1.00 94.57           C  
ANISOU 1751  CE2 TYR A1257    11292  12749  11890   -249   -334    462       C  
ATOM   1752  CZ  TYR A1257       4.250  19.250  -6.283  1.00 97.65           C  
ANISOU 1752  CZ  TYR A1257    11697  13145  12260   -257   -266    420       C  
ATOM   1753  OH  TYR A1257       5.079  18.277  -5.752  1.00 94.58           O  
ANISOU 1753  OH  TYR A1257    11359  12699  11880   -265   -221    387       O  
ATOM   1754  N   LYS A1258       2.914  22.269 -10.628  1.00 90.71           N  
ANISOU 1754  N   LYS A1258    10598  12527  11341   -358   -425    577       N  
ATOM   1755  CA  LYS A1258       3.940  21.888 -11.584  1.00 98.10           C  
ANISOU 1755  CA  LYS A1258    11527  13464  12283   -437   -424    575       C  
ATOM   1756  C   LYS A1258       5.318  21.991 -10.953  1.00 99.55           C  
ANISOU 1756  C   LYS A1258    11780  13540  12505   -408   -446    565       C  
ATOM   1757  O   LYS A1258       5.614  22.937 -10.221  1.00100.25           O  
ANISOU 1757  O   LYS A1258    11910  13562  12618   -334   -495    585       O  
ATOM   1758  CB  LYS A1258       3.877  22.736 -12.841  1.00108.70           C  
ANISOU 1758  CB  LYS A1258    12817  14867  13619   -472   -475    623       C  
ATOM   1759  CG  LYS A1258       3.294  24.113 -12.630  1.00116.08           C  
ANISOU 1759  CG  LYS A1258    13748  15796  14560   -390   -537    671       C  
ATOM   1760  CD  LYS A1258       3.216  24.854 -13.959  1.00111.35           C  
ANISOU 1760  CD  LYS A1258    13095  15263  13949   -431   -582    720       C  
ATOM   1761  CE  LYS A1258       3.016  23.885 -15.109  1.00105.38           C  
ANISOU 1761  CE  LYS A1258    12272  14607  13160   -543   -536    705       C  
ATOM   1762  NZ  LYS A1258       1.890  24.295 -15.971  1.00113.13           N  
ANISOU 1762  NZ  LYS A1258    13175  15705  14105   -559   -545    744       N  
ATOM   1763  N   ASP A1259       6.153  21.013 -11.262  1.00 98.17           N  
ANISOU 1763  N   ASP A1259    11616  13355  12330   -469   -407    535       N  
ATOM   1764  CA  ASP A1259       7.470  20.869 -10.670  1.00 98.66           C  
ANISOU 1764  CA  ASP A1259    11736  13330  12419   -447   -414    521       C  
ATOM   1765  C   ASP A1259       8.479  21.725 -11.443  1.00108.57           C  
ANISOU 1765  C   ASP A1259    12988  14576  13690   -470   -479    553       C  
ATOM   1766  O   ASP A1259       8.111  22.629 -12.198  1.00110.39           O  
ANISOU 1766  O   ASP A1259    13182  14846  13915   -481   -527    590       O  
ATOM   1767  CB  ASP A1259       7.836  19.383 -10.636  1.00 95.42           C  
ANISOU 1767  CB  ASP A1259    11341  12917  11997   -494   -336    474       C  
ATOM   1768  CG  ASP A1259       7.710  18.717 -11.998  1.00 98.27           C  
ANISOU 1768  CG  ASP A1259    11650  13357  12332   -596   -301    467       C  
ATOM   1769  OD1 ASP A1259       7.627  19.436 -13.015  1.00101.35           O  
ANISOU 1769  OD1 ASP A1259    11991  13798  12718   -634   -346    500       O  
ATOM   1770  OD2 ASP A1259       7.684  17.471 -12.062  1.00 99.32           O  
ANISOU 1770  OD2 ASP A1259    11791  13499  12447   -642   -226    428       O  
ATOM   1771  N   THR A1260       9.769  21.444 -11.264  1.00113.05           N  
ANISOU 1771  N   THR A1260    13591  15092  14270   -477   -481    539       N  
ATOM   1772  CA  THR A1260      10.799  22.179 -11.987  1.00116.74           C  
ANISOU 1772  CA  THR A1260    14055  15555  14744   -507   -540    564       C  
ATOM   1773  C   THR A1260      10.693  21.947 -13.490  1.00120.08           C  
ANISOU 1773  C   THR A1260    14416  16058  15151   -600   -536    572       C  
ATOM   1774  O   THR A1260      10.893  22.874 -14.283  1.00126.47           O  
ANISOU 1774  O   THR A1260    15204  16890  15960   -625   -596    607       O  
ATOM   1775  CB  THR A1260      12.176  21.770 -11.474  1.00110.04           C  
ANISOU 1775  CB  THR A1260    13251  14652  13906   -498   -535    543       C  
ATOM   1776  OG1 THR A1260      13.108  21.762 -12.565  1.00115.15           O  
ANISOU 1776  OG1 THR A1260    13874  15330  14548   -568   -555    549       O  
ATOM   1777  CG2 THR A1260      12.095  20.391 -10.862  1.00 99.49           C  
ANISOU 1777  CG2 THR A1260    11933  13302  12566   -491   -454    501       C  
ATOM   1778  N   GLU A1261      10.365  20.720 -13.902  1.00118.69           N  
ANISOU 1778  N   GLU A1261    14214  15926  14957   -656   -465    540       N  
ATOM   1779  CA  GLU A1261      10.214  20.428 -15.325  1.00115.22           C  
ANISOU 1779  CA  GLU A1261    13712  15567  14498   -752   -454    544       C  
ATOM   1780  C   GLU A1261       8.968  21.043 -15.942  1.00110.63           C  
ANISOU 1780  C   GLU A1261    13075  15060  13899   -767   -474    576       C  
ATOM   1781  O   GLU A1261       8.842  21.021 -17.166  1.00111.61           O  
ANISOU 1781  O   GLU A1261    13142  15257  14006   -846   -478    589       O  
ATOM   1782  CB  GLU A1261      10.168  18.916 -15.572  1.00119.66           C  
ANISOU 1782  CB  GLU A1261    14269  16154  15042   -812   -364    498       C  
ATOM   1783  CG  GLU A1261      11.522  18.289 -15.725  1.00128.33           C  
ANISOU 1783  CG  GLU A1261    15394  17218  16149   -837   -346    475       C  
ATOM   1784  CD  GLU A1261      12.538  19.271 -16.271  1.00135.85           C  
ANISOU 1784  CD  GLU A1261    16338  18164  17115   -848   -425    505       C  
ATOM   1785  OE1 GLU A1261      12.368  19.729 -17.425  1.00137.47           O  
ANISOU 1785  OE1 GLU A1261    16490  18431  17310   -914   -457    528       O  
ATOM   1786  OE2 GLU A1261      13.492  19.597 -15.530  1.00136.08           O  
ANISOU 1786  OE2 GLU A1261    16414  18130  17160   -794   -456    506       O  
ATOM   1787  N   GLY A1262       8.050  21.575 -15.145  1.00110.43           N  
ANISOU 1787  N   GLY A1262    13060  15024  13875   -693   -486    590       N  
ATOM   1788  CA  GLY A1262       6.759  21.989 -15.658  1.00113.46           C  
ANISOU 1788  CA  GLY A1262    13386  15489  14235   -700   -493    618       C  
ATOM   1789  C   GLY A1262       5.713  20.896 -15.735  1.00107.12           C  
ANISOU 1789  C   GLY A1262    12548  14757  13397   -742   -414    587       C  
ATOM   1790  O   GLY A1262       4.648  21.124 -16.323  1.00110.35           O  
ANISOU 1790  O   GLY A1262    12895  15256  13775   -764   -414    609       O  
ATOM   1791  N   TYR A1263       5.977  19.720 -15.161  1.00 96.71           N  
ANISOU 1791  N   TYR A1263    11266  13403  12075   -755   -347    538       N  
ATOM   1792  CA  TYR A1263       5.050  18.601 -15.249  1.00 86.10           C  
ANISOU 1792  CA  TYR A1263     9898  12123  10692   -808   -265    503       C  
ATOM   1793  C   TYR A1263       4.026  18.678 -14.127  1.00 91.81           C  
ANISOU 1793  C   TYR A1263    10639  12841  11406   -733   -251    496       C  
ATOM   1794  O   TYR A1263       4.302  19.203 -13.043  1.00 94.49           O  
ANISOU 1794  O   TYR A1263    11029  13098  11775   -642   -284    500       O  
ATOM   1795  CB  TYR A1263       5.800  17.266 -15.194  1.00 78.88           C  
ANISOU 1795  CB  TYR A1263     9024  11171   9775   -858   -193    453       C  
ATOM   1796  CG  TYR A1263       6.571  16.932 -16.463  1.00 90.74           C  
ANISOU 1796  CG  TYR A1263    10497  12706  11274   -952   -186    451       C  
ATOM   1797  CD1 TYR A1263       6.266  17.561 -17.678  1.00 92.51           C  
ANISOU 1797  CD1 TYR A1263    10650  13015  11484  -1011   -224    486       C  
ATOM   1798  CD2 TYR A1263       7.602  15.992 -16.451  1.00 90.58           C  
ANISOU 1798  CD2 TYR A1263    10520  12634  11263   -980   -140    416       C  
ATOM   1799  CE1 TYR A1263       6.964  17.266 -18.825  1.00 96.40           C  
ANISOU 1799  CE1 TYR A1263    11115  13540  11974  -1100   -219    483       C  
ATOM   1800  CE2 TYR A1263       8.311  15.690 -17.600  1.00 92.58           C  
ANISOU 1800  CE2 TYR A1263    10745  12917  11512  -1064   -133    412       C  
ATOM   1801  CZ  TYR A1263       7.985  16.334 -18.786  1.00101.70           C  
ANISOU 1801  CZ  TYR A1263    11829  14157  12655  -1128   -173    444       C  
ATOM   1802  OH  TYR A1263       8.678  16.051 -19.943  1.00107.65           O  
ANISOU 1802  OH  TYR A1263    12553  14945  13405  -1216   -168    440       O  
ATOM   1803  N   TYR A1264       2.834  18.138 -14.388  1.00 94.49           N  
ANISOU 1803  N   TYR A1264    10933  13272  11698   -778   -201    483       N  
ATOM   1804  CA  TYR A1264       1.742  18.220 -13.421  1.00 90.51           C  
ANISOU 1804  CA  TYR A1264    10433  12781  11175   -715   -188    476       C  
ATOM   1805  C   TYR A1264       1.907  17.179 -12.326  1.00 81.01           C  
ANISOU 1805  C   TYR A1264     9298  11509   9973   -698   -126    423       C  
ATOM   1806  O   TYR A1264       2.031  15.983 -12.608  1.00 74.01           O  
ANISOU 1806  O   TYR A1264     8424  10634   9061   -775    -53    383       O  
ATOM   1807  CB  TYR A1264       0.399  18.064 -14.124  1.00 92.57           C  
ANISOU 1807  CB  TYR A1264    10616  13180  11377   -771   -160    483       C  
ATOM   1808  CG  TYR A1264      -0.006  19.328 -14.828  1.00 89.61           C  
ANISOU 1808  CG  TYR A1264    10179  12868  11003   -746   -232    544       C  
ATOM   1809  CD1 TYR A1264       0.063  20.543 -14.174  1.00 89.88           C  
ANISOU 1809  CD1 TYR A1264    10237  12841  11073   -636   -302    581       C  
ATOM   1810  CD2 TYR A1264      -0.407  19.319 -16.154  1.00 94.61           C  
ANISOU 1810  CD2 TYR A1264    10734  13615  11599   -832   -227    565       C  
ATOM   1811  CE1 TYR A1264      -0.283  21.713 -14.799  1.00 92.76           C  
ANISOU 1811  CE1 TYR A1264    10555  13253  11437   -606   -366    639       C  
ATOM   1812  CE2 TYR A1264      -0.760  20.500 -16.795  1.00 99.58           C  
ANISOU 1812  CE2 TYR A1264    11308  14299  12227   -803   -294    626       C  
ATOM   1813  CZ  TYR A1264      -0.691  21.697 -16.098  1.00 95.72           C  
ANISOU 1813  CZ  TYR A1264    10852  13742  11776   -686   -363    663       C  
ATOM   1814  OH  TYR A1264      -1.030  22.895 -16.676  1.00 96.19           O  
ANISOU 1814  OH  TYR A1264    10868  13845  11835   -647   -427    725       O  
ATOM   1815  N   THR A1265       1.893  17.651 -11.077  1.00 85.69           N  
ANISOU 1815  N   THR A1265     9937  12029  10593   -599   -153    424       N  
ATOM   1816  CA  THR A1265       2.254  16.871  -9.899  1.00 84.59           C  
ANISOU 1816  CA  THR A1265     9870  11805  10465   -564   -110    383       C  
ATOM   1817  C   THR A1265       1.279  17.196  -8.772  1.00 80.94           C  
ANISOU 1817  C   THR A1265     9418  11342   9996   -489   -115    378       C  
ATOM   1818  O   THR A1265       0.626  18.241  -8.786  1.00 78.81           O  
ANISOU 1818  O   THR A1265     9111  11108   9726   -440   -167    414       O  
ATOM   1819  CB  THR A1265       3.712  17.169  -9.488  1.00 87.29           C  
ANISOU 1819  CB  THR A1265    10269  12038  10860   -519   -147    390       C  
ATOM   1820  OG1 THR A1265       4.576  16.938 -10.613  1.00100.68           O  
ANISOU 1820  OG1 THR A1265    11948  13747  12560   -590   -147    396       O  
ATOM   1821  CG2 THR A1265       4.164  16.299  -8.343  1.00 76.10           C  
ANISOU 1821  CG2 THR A1265     8922  10538   9452   -486   -100    351       C  
ATOM   1822  N   ILE A1266       1.174  16.280  -7.797  1.00 78.89           N  
ANISOU 1822  N   ILE A1266     9209  11040   9727   -479    -59    334       N  
ATOM   1823  CA  ILE A1266       0.286  16.443  -6.648  1.00 79.08           C  
ANISOU 1823  CA  ILE A1266     9247  11059   9741   -413    -57    322       C  
ATOM   1824  C   ILE A1266       0.830  15.672  -5.449  1.00 78.16           C  
ANISOU 1824  C   ILE A1266     9210  10847   9642   -381    -19    284       C  
ATOM   1825  O   ILE A1266       1.675  14.783  -5.579  1.00 77.64           O  
ANISOU 1825  O   ILE A1266     9183  10735   9581   -420     24    262       O  
ATOM   1826  CB  ILE A1266      -1.158  15.977  -6.959  1.00 79.76           C  
ANISOU 1826  CB  ILE A1266     9280  11264   9762   -466    -11    304       C  
ATOM   1827  CG1 ILE A1266      -2.143  16.549  -5.934  1.00 81.60           C  
ANISOU 1827  CG1 ILE A1266     9508  11511   9987   -386    -33    306       C  
ATOM   1828  CG2 ILE A1266      -1.233  14.451  -7.033  1.00 77.16           C  
ANISOU 1828  CG2 ILE A1266     8980  10947   9390   -553     83    252       C  
ATOM   1829  CD1 ILE A1266      -3.544  16.761  -6.477  1.00 90.49           C  
ANISOU 1829  CD1 ILE A1266    10554  12775  11054   -412    -27    316       C  
ATOM   1830  N   GLY A1267       0.345  16.043  -4.267  1.00 74.70           N  
ANISOU 1830  N   GLY A1267     8792  10377   9212   -305    -35    278       N  
ATOM   1831  CA  GLY A1267       0.628  15.281  -3.062  1.00 78.76           C  
ANISOU 1831  CA  GLY A1267     9376  10815   9734   -277      5    241       C  
ATOM   1832  C   GLY A1267       2.071  15.417  -2.635  1.00 75.45           C  
ANISOU 1832  C   GLY A1267     9011  10290   9366   -235    -20    251       C  
ATOM   1833  O   GLY A1267       2.607  16.523  -2.495  1.00 76.64           O  
ANISOU 1833  O   GLY A1267     9160  10403   9556   -178    -89    286       O  
ATOM   1834  N   ILE A1268       2.713  14.275  -2.424  1.00 72.66           N  
ANISOU 1834  N   ILE A1268     8707   9891   9008   -263     39    220       N  
ATOM   1835  CA  ILE A1268       4.132  14.247  -2.087  1.00 73.17           C  
ANISOU 1835  CA  ILE A1268     8820   9869   9114   -229     24    229       C  
ATOM   1836  C   ILE A1268       4.890  13.880  -3.357  1.00 69.45           C  
ANISOU 1836  C   ILE A1268     8332   9418   8640   -296     38    236       C  
ATOM   1837  O   ILE A1268       5.324  12.738  -3.526  1.00 71.12           O  
ANISOU 1837  O   ILE A1268     8576   9611   8835   -337    104    210       O  
ATOM   1838  CB  ILE A1268       4.402  13.266  -0.916  1.00 71.56           C  
ANISOU 1838  CB  ILE A1268     8684   9596   8907   -201     79    195       C  
ATOM   1839  CG1 ILE A1268       3.489  13.608   0.270  1.00 62.77           C  
ANISOU 1839  CG1 ILE A1268     7580   8477   7791   -146     67    184       C  
ATOM   1840  CG2 ILE A1268       5.869  13.287  -0.483  1.00 64.17           C  
ANISOU 1840  CG2 ILE A1268     7792   8581   8010   -156     61    208       C  
ATOM   1841  CD1 ILE A1268       3.588  12.631   1.425  1.00 66.33           C  
ANISOU 1841  CD1 ILE A1268     8097   8870   8236   -124    122    149       C  
ATOM   1842  N   GLY A1269       4.997  14.831  -4.283  1.00 75.34           N  
ANISOU 1842  N   GLY A1269     9026  10204   9397   -310    -20    272       N  
ATOM   1843  CA  GLY A1269       5.735  14.619  -5.527  1.00 69.07           C  
ANISOU 1843  CA  GLY A1269     8209   9433   8601   -376    -16    281       C  
ATOM   1844  C   GLY A1269       5.183  13.541  -6.441  1.00 70.22           C  
ANISOU 1844  C   GLY A1269     8335   9644   8703   -472     58    254       C  
ATOM   1845  O   GLY A1269       5.952  12.808  -7.079  1.00 61.74           O  
ANISOU 1845  O   GLY A1269     7274   8559   7624   -522     96    242       O  
ATOM   1846  N   HIS A1270       3.866  13.421  -6.535  1.00 73.14           N  
ANISOU 1846  N   HIS A1270     8672  10085   9034   -502     82    242       N  
ATOM   1847  CA  HIS A1270       3.289  12.405  -7.398  1.00 72.80           C  
ANISOU 1847  CA  HIS A1270     8610  10112   8940   -603    156    214       C  
ATOM   1848  C   HIS A1270       3.104  12.989  -8.793  1.00 84.79           C  
ANISOU 1848  C   HIS A1270    10051  11717  10448   -664    123    243       C  
ATOM   1849  O   HIS A1270       2.285  13.889  -8.995  1.00 86.66           O  
ANISOU 1849  O   HIS A1270    10232  12018  10676   -649     76    271       O  
ATOM   1850  CB  HIS A1270       1.978  11.881  -6.843  1.00 69.97           C  
ANISOU 1850  CB  HIS A1270     8252   9799   8533   -618    206    182       C  
ATOM   1851  CG  HIS A1270       1.379  10.819  -7.698  1.00 85.44           C  
ANISOU 1851  CG  HIS A1270    10197  11833  10432   -731    288    150       C  
ATOM   1852  ND1 HIS A1270       1.817   9.513  -7.673  1.00 87.19           N  
ANISOU 1852  ND1 HIS A1270    10482  12010  10635   -780    373    110       N  
ATOM   1853  CD2 HIS A1270       0.418  10.879  -8.649  1.00 90.05           C  
ANISOU 1853  CD2 HIS A1270    10712  12535  10968   -808    300    154       C  
ATOM   1854  CE1 HIS A1270       1.128   8.808  -8.554  1.00 88.87           C  
ANISOU 1854  CE1 HIS A1270    10671  12308  10790   -888    436     87       C  
ATOM   1855  NE2 HIS A1270       0.274   9.613  -9.160  1.00 90.85           N  
ANISOU 1855  NE2 HIS A1270    10836  12661  11020   -909    393    113       N  
ATOM   1856  N   LEU A1271       3.864  12.465  -9.751  1.00 91.91           N  
ANISOU 1856  N   LEU A1271    10951  12621  11348   -732    150    238       N  
ATOM   1857  CA  LEU A1271       3.746  12.890 -11.138  1.00 92.48           C  
ANISOU 1857  CA  LEU A1271    10951  12778  11408   -804    125    263       C  
ATOM   1858  C   LEU A1271       2.485  12.306 -11.755  1.00 88.14           C  
ANISOU 1858  C   LEU A1271    10357  12338  10795   -893    184    244       C  
ATOM   1859  O   LEU A1271       2.266  11.091 -11.703  1.00 87.90           O  
ANISOU 1859  O   LEU A1271    10362  12310  10728   -952    271    199       O  
ATOM   1860  CB  LEU A1271       4.976  12.452 -11.936  1.00 98.71           C  
ANISOU 1860  CB  LEU A1271    11753  13537  12214   -852    139    259       C  
ATOM   1861  CG  LEU A1271       5.063  12.838 -13.417  1.00 93.62           C  
ANISOU 1861  CG  LEU A1271    11039  12972  11562   -932    113    284       C  
ATOM   1862  CD1 LEU A1271       5.102  14.334 -13.536  1.00 93.16           C  
ANISOU 1862  CD1 LEU A1271    10938  12925  11534   -877     10    336       C  
ATOM   1863  CD2 LEU A1271       6.293  12.223 -14.058  1.00 90.02           C  
ANISOU 1863  CD2 LEU A1271    10606  12479  11120   -978    139    270       C  
ATOM   1864  N   LEU A1272       1.658  13.174 -12.346  1.00 88.61           N  
ANISOU 1864  N   LEU A1272    10339  12490  10837   -903    137    278       N  
ATOM   1865  CA  LEU A1272       0.362  12.784 -12.891  1.00 85.31           C  
ANISOU 1865  CA  LEU A1272     9865  12196  10352   -981    184    266       C  
ATOM   1866  C   LEU A1272       0.443  12.489 -14.375  1.00 91.61           C  
ANISOU 1866  C   LEU A1272    10609  13077  11123  -1096    207    270       C  
ATOM   1867  O   LEU A1272       0.082  11.393 -14.811  1.00 91.60           O  
ANISOU 1867  O   LEU A1272    10612  13123  11070  -1195    292    231       O  
ATOM   1868  CB  LEU A1272      -0.692  13.869 -12.615  1.00 80.52           C  
ANISOU 1868  CB  LEU A1272     9203  11657   9736   -920    124    302       C  
ATOM   1869  CG  LEU A1272      -1.010  13.935 -11.107  1.00 79.83           C  
ANISOU 1869  CG  LEU A1272     9168  11502   9660   -824    121    285       C  
ATOM   1870  CD1 LEU A1272      -1.861  15.130 -10.717  1.00 79.91           C  
ANISOU 1870  CD1 LEU A1272     9133  11556   9673   -741     55    323       C  
ATOM   1871  CD2 LEU A1272      -1.669  12.643 -10.666  1.00 79.03           C  
ANISOU 1871  CD2 LEU A1272     9100  11423   9504   -881    215    229       C  
ATOM   1872  N   THR A1273       0.945  13.436 -15.154  1.00 98.19           N  
ANISOU 1872  N   THR A1273    11396  13924  11987  -1089    135    316       N  
ATOM   1873  CA  THR A1273       1.201  13.182 -16.560  1.00 98.46           C  
ANISOU 1873  CA  THR A1273    11381  14027  12003  -1198    152    320       C  
ATOM   1874  C   THR A1273       2.273  14.142 -17.045  1.00 99.44           C  
ANISOU 1874  C   THR A1273    11494  14106  12184  -1164     69    362       C  
ATOM   1875  O   THR A1273       2.403  15.262 -16.541  1.00 97.89           O  
ANISOU 1875  O   THR A1273    11299  13870  12024  -1069    -11    400       O  
ATOM   1876  CB  THR A1273      -0.061  13.336 -17.403  1.00 95.64           C  
ANISOU 1876  CB  THR A1273    10934  13822  11584  -1270    162    337       C  
ATOM   1877  OG1 THR A1273       0.199  12.855 -18.731  1.00 92.83           O  
ANISOU 1877  OG1 THR A1273    10536  13530  11204  -1392    196    331       O  
ATOM   1878  CG2 THR A1273      -0.466  14.798 -17.467  1.00 94.71           C  
ANISOU 1878  CG2 THR A1273    10757  13743  11485  -1193     67    399       C  
ATOM   1879  N   LYS A1274       3.049  13.679 -18.023  1.00102.27           N  
ANISOU 1879  N   LYS A1274    11844  14470  12544  -1247     90    353       N  
ATOM   1880  CA  LYS A1274       4.027  14.546 -18.651  1.00 98.01           C  
ANISOU 1880  CA  LYS A1274    11286  13907  12047  -1236     14    390       C  
ATOM   1881  C   LYS A1274       3.380  15.467 -19.674  1.00 98.59           C  
ANISOU 1881  C   LYS A1274    11268  14089  12102  -1272    -40    438       C  
ATOM   1882  O   LYS A1274       3.898  16.562 -19.921  1.00107.36           O  
ANISOU 1882  O   LYS A1274    12364  15179  13248  -1230   -124    482       O  
ATOM   1883  CB  LYS A1274       5.131  13.702 -19.295  1.00103.79           C  
ANISOU 1883  CB  LYS A1274    12042  14605  12787  -1308     56    360       C  
ATOM   1884  CG  LYS A1274       6.099  13.033 -18.313  1.00106.79           C  
ANISOU 1884  CG  LYS A1274    12514  14864  13198  -1250     88    326       C  
ATOM   1885  CD  LYS A1274       7.328  12.473 -19.044  1.00109.91           C  
ANISOU 1885  CD  LYS A1274    12925  15230  13607  -1306    110    309       C  
ATOM   1886  CE  LYS A1274       8.423  11.979 -18.099  1.00113.89           C  
ANISOU 1886  CE  LYS A1274    13512  15618  14142  -1233    128    286       C  
ATOM   1887  NZ  LYS A1274       8.073  10.711 -17.369  1.00118.91           N  
ANISOU 1887  NZ  LYS A1274    14212  16214  14752  -1233    228    238       N  
ATOM   1888  N   SER A1275       2.254  15.055 -20.250  1.00 93.44           N  
ANISOU 1888  N   SER A1275    10557  13554  11391  -1349      8    433       N  
ATOM   1889  CA  SER A1275       1.457  15.867 -21.168  1.00104.89           C  
ANISOU 1889  CA  SER A1275    11914  15125  12814  -1380    -36    481       C  
ATOM   1890  C   SER A1275       1.237  17.276 -20.618  1.00106.47           C  
ANISOU 1890  C   SER A1275    12108  15300  13045  -1259   -128    535       C  
ATOM   1891  O   SER A1275       1.157  17.462 -19.395  1.00101.73           O  
ANISOU 1891  O   SER A1275    11563  14623  12466  -1160   -138    527       O  
ATOM   1892  CB  SER A1275       0.117  15.187 -21.440  1.00110.56           C  
ANISOU 1892  CB  SER A1275    12580  15970  13457  -1456     35    463       C  
ATOM   1893  OG  SER A1275      -0.750  16.048 -22.149  1.00118.54           O  
ANISOU 1893  OG  SER A1275    13499  17103  14438  -1464    -11    515       O  
ATOM   1894  N   PRO A1276       1.152  18.297 -21.479  1.00102.41           N  
ANISOU 1894  N   PRO A1276    11533  14845  12534  -1263   -196    591       N  
ATOM   1895  CA  PRO A1276       0.908  19.658 -20.984  1.00 97.10           C  
ANISOU 1895  CA  PRO A1276    10862  14145  11888  -1147   -279    644       C  
ATOM   1896  C   PRO A1276      -0.535  19.928 -20.608  1.00100.34           C  
ANISOU 1896  C   PRO A1276    11228  14642  12255  -1101   -271    662       C  
ATOM   1897  O   PRO A1276      -0.794  20.945 -19.947  1.00100.47           O  
ANISOU 1897  O   PRO A1276    11261  14621  12293   -989   -328    698       O  
ATOM   1898  CB  PRO A1276       1.340  20.542 -22.162  1.00 95.88           C  
ANISOU 1898  CB  PRO A1276    10659  14028  11745  -1181   -346    695       C  
ATOM   1899  CG  PRO A1276       1.152  19.681 -23.354  1.00100.44           C  
ANISOU 1899  CG  PRO A1276    11172  14713  12279  -1321   -291    677       C  
ATOM   1900  CD  PRO A1276       1.475  18.278 -22.915  1.00 96.64           C  
ANISOU 1900  CD  PRO A1276    10741  14187  11790  -1371   -202    607       C  
ATOM   1901  N   SER A1277      -1.469  19.054 -20.991  1.00 86.60           N  
ANISOU 1901  N   SER A1277     9435  13018  10452  -1184   -201    638       N  
ATOM   1902  CA  SER A1277      -2.880  19.292 -20.720  1.00 96.58           C  
ANISOU 1902  CA  SER A1277    10646  14386  11665  -1148   -192    655       C  
ATOM   1903  C   SER A1277      -3.164  19.257 -19.225  1.00102.94           C  
ANISOU 1903  C   SER A1277    11516  15112  12485  -1044   -184    630       C  
ATOM   1904  O   SER A1277      -2.654  18.402 -18.500  1.00113.71           O  
ANISOU 1904  O   SER A1277    12951  16387  13865  -1051   -137    577       O  
ATOM   1905  CB  SER A1277      -3.743  18.253 -21.430  1.00103.83           C  
ANISOU 1905  CB  SER A1277    11498  15448  12504  -1275   -110    627       C  
ATOM   1906  OG  SER A1277      -5.114  18.623 -21.391  1.00113.51           O  
ANISOU 1906  OG  SER A1277    12653  16804  13672  -1247   -111    655       O  
ATOM   1907  N   LEU A1278      -3.975  20.205 -18.755  1.00105.15           N  
ANISOU 1907  N   LEU A1278    11773  15421  12759   -943   -229    670       N  
ATOM   1908  CA  LEU A1278      -4.399  20.162 -17.356  1.00105.95           C  
ANISOU 1908  CA  LEU A1278    11925  15464  12866   -850   -217    645       C  
ATOM   1909  C   LEU A1278      -5.589  19.228 -17.177  1.00104.43           C  
ANISOU 1909  C   LEU A1278    11693  15387  12598   -904   -142    608       C  
ATOM   1910  O   LEU A1278      -5.692  18.545 -16.150  1.00 89.17           O  
ANISOU 1910  O   LEU A1278     9818  13401  10663   -886    -98    558       O  
ATOM   1911  CB  LEU A1278      -4.730  21.570 -16.854  1.00104.19           C  
ANISOU 1911  CB  LEU A1278    11702  15215  12670   -715   -294    701       C  
ATOM   1912  CG  LEU A1278      -5.256  21.750 -15.431  1.00105.38           C  
ANISOU 1912  CG  LEU A1278    11899  15314  12828   -607   -293    684       C  
ATOM   1913  CD1 LEU A1278      -4.137  21.606 -14.389  1.00108.66           C  
ANISOU 1913  CD1 LEU A1278    12418  15558  13308   -560   -300    649       C  
ATOM   1914  CD2 LEU A1278      -5.967  23.091 -15.308  1.00107.24           C  
ANISOU 1914  CD2 LEU A1278    12102  15582  13063   -495   -356    745       C  
ATOM   1915  N   ASN A1279      -6.475  19.174 -18.178  1.00111.69           N  
ANISOU 1915  N   ASN A1279    12516  16469  13451   -976   -124    630       N  
ATOM   1916  CA  ASN A1279      -7.569  18.208 -18.175  1.00112.45           C  
ANISOU 1916  CA  ASN A1279    12571  16693  13463  -1054    -46    592       C  
ATOM   1917  C   ASN A1279      -7.056  16.782 -17.996  1.00107.27           C  
ANISOU 1917  C   ASN A1279    11978  15983  12799  -1153     38    518       C  
ATOM   1918  O   ASN A1279      -7.706  15.964 -17.338  1.00117.32           O  
ANISOU 1918  O   ASN A1279    13270  17284  14024  -1177    101    470       O  
ATOM   1919  CB  ASN A1279      -8.371  18.315 -19.479  1.00115.25           C  
ANISOU 1919  CB  ASN A1279    12809  17232  13747  -1139    -38    628       C  
ATOM   1920  CG  ASN A1279      -9.247  19.555 -19.540  1.00118.49           C  
ANISOU 1920  CG  ASN A1279    13149  17731  14141  -1039   -102    697       C  
ATOM   1921  OD1 ASN A1279      -8.750  20.673 -19.669  1.00124.62           O  
ANISOU 1921  OD1 ASN A1279    13935  18442  14974   -953   -180    751       O  
ATOM   1922  ND2 ASN A1279     -10.559  19.357 -19.481  1.00117.25           N  
ANISOU 1922  ND2 ASN A1279    12921  17727  13901  -1051    -69    697       N  
ATOM   1923  N   ALA A1280      -5.899  16.461 -18.581  1.00 97.12           N  
ANISOU 1923  N   ALA A1280    10726  14620  11554  -1212     42    508       N  
ATOM   1924  CA  ALA A1280      -5.387  15.096 -18.516  1.00 90.06           C  
ANISOU 1924  CA  ALA A1280     9893  13676  10649  -1305    126    442       C  
ATOM   1925  C   ALA A1280      -4.774  14.783 -17.163  1.00103.64           C  
ANISOU 1925  C   ALA A1280    11720  15240  12419  -1224    134    404       C  
ATOM   1926  O   ALA A1280      -4.839  13.635 -16.707  1.00104.05           O  
ANISOU 1926  O   ALA A1280    11824  15267  12442  -1275    214    346       O  
ATOM   1927  CB  ALA A1280      -4.352  14.853 -19.610  1.00 89.12           C  
ANISOU 1927  CB  ALA A1280     9773  13533  10557  -1392    129    444       C  
ATOM   1928  N   ALA A1281      -4.153  15.771 -16.518  1.00 99.31           N  
ANISOU 1928  N   ALA A1281    11208  14584  11943  -1102     57    436       N  
ATOM   1929  CA  ALA A1281      -3.701  15.557 -15.152  1.00 95.25           C  
ANISOU 1929  CA  ALA A1281    10785  13936  11469  -1019     62    405       C  
ATOM   1930  C   ALA A1281      -4.896  15.349 -14.245  1.00100.97           C  
ANISOU 1930  C   ALA A1281    11506  14712  12146   -985     91    383       C  
ATOM   1931  O   ALA A1281      -4.962  14.361 -13.509  1.00111.34           O  
ANISOU 1931  O   ALA A1281    12877  15984  13441  -1006    156    329       O  
ATOM   1932  CB  ALA A1281      -2.851  16.733 -14.672  1.00 88.30           C  
ANISOU 1932  CB  ALA A1281     9941  12943  10668   -902    -28    445       C  
ATOM   1933  N   LYS A1282      -5.876  16.256 -14.320  1.00100.58           N  
ANISOU 1933  N   LYS A1282    11386  14757  12071   -934     47    425       N  
ATOM   1934  CA  LYS A1282      -7.078  16.112 -13.506  1.00101.59           C  
ANISOU 1934  CA  LYS A1282    11500  14952  12148   -901     72    406       C  
ATOM   1935  C   LYS A1282      -7.725  14.750 -13.716  1.00104.91           C  
ANISOU 1935  C   LYS A1282    11912  15461  12487  -1026    171    349       C  
ATOM   1936  O   LYS A1282      -8.247  14.160 -12.766  1.00111.42           O  
ANISOU 1936  O   LYS A1282    12774  16277  13282  -1016    214    306       O  
ATOM   1937  CB  LYS A1282      -8.063  17.244 -13.811  1.00 96.18           C  
ANISOU 1937  CB  LYS A1282    10726  14381  11437   -840     16    463       C  
ATOM   1938  CG  LYS A1282      -7.992  18.431 -12.837  1.00 96.20           C  
ANISOU 1938  CG  LYS A1282    10758  14296  11497   -686    -59    497       C  
ATOM   1939  CD  LYS A1282      -8.967  19.529 -13.281  1.00108.87           C  
ANISOU 1939  CD  LYS A1282    12275  16020  13071   -626   -109    559       C  
ATOM   1940  CE  LYS A1282      -9.899  20.013 -12.159  1.00118.39           C  
ANISOU 1940  CE  LYS A1282    13480  17240  14262   -517   -124    559       C  
ATOM   1941  NZ  LYS A1282     -11.135  20.659 -12.732  1.00121.83           N  
ANISOU 1941  NZ  LYS A1282    13811  17844  14634   -492   -142    607       N  
ATOM   1942  N   SER A1283      -7.660  14.213 -14.933  1.00106.43           N  
ANISOU 1942  N   SER A1283    12064  15734  12643  -1149    210    346       N  
ATOM   1943  CA  SER A1283      -8.210  12.883 -15.181  1.00112.58           C  
ANISOU 1943  CA  SER A1283    12844  16591  13340  -1280    311    290       C  
ATOM   1944  C   SER A1283      -7.356  11.800 -14.530  1.00112.71           C  
ANISOU 1944  C   SER A1283    12974  16467  13384  -1303    372    231       C  
ATOM   1945  O   SER A1283      -7.876  10.933 -13.816  1.00119.46           O  
ANISOU 1945  O   SER A1283    13873  17325  14192  -1332    437    180       O  
ATOM   1946  CB  SER A1283      -8.340  12.638 -16.684  1.00112.82           C  
ANISOU 1946  CB  SER A1283    12800  16744  13323  -1408    338    303       C  
ATOM   1947  OG  SER A1283      -9.223  13.576 -17.265  1.00118.74           O  
ANISOU 1947  OG  SER A1283    13440  17637  14037  -1387    288    359       O  
ATOM   1948  N   GLU A1284      -6.042  11.826 -14.774  1.00105.23           N  
ANISOU 1948  N   GLU A1284    12075  15400  12508  -1292    352    238       N  
ATOM   1949  CA  GLU A1284      -5.146  10.861 -14.146  1.00106.09           C  
ANISOU 1949  CA  GLU A1284    12291  15372  12646  -1298    404    189       C  
ATOM   1950  C   GLU A1284      -5.141  10.989 -12.629  1.00103.41           C  
ANISOU 1950  C   GLU A1284    12019  14932  12340  -1185    387    174       C  
ATOM   1951  O   GLU A1284      -4.715  10.060 -11.933  1.00101.18           O  
ANISOU 1951  O   GLU A1284    11824  14557  12062  -1192    444    128       O  
ATOM   1952  CB  GLU A1284      -3.722  11.033 -14.679  1.00110.80           C  
ANISOU 1952  CB  GLU A1284    12916  15869  13314  -1292    374    207       C  
ATOM   1953  CG  GLU A1284      -3.478  10.441 -16.050  1.00118.24           C  
ANISOU 1953  CG  GLU A1284    13825  16875  14224  -1424    421    198       C  
ATOM   1954  CD  GLU A1284      -3.345   8.925 -16.030  1.00127.88           C  
ANISOU 1954  CD  GLU A1284    15117  18067  15404  -1521    534    134       C  
ATOM   1955  OE1 GLU A1284      -4.337   8.234 -15.728  1.00133.89           O  
ANISOU 1955  OE1 GLU A1284    15884  18895  16094  -1575    600     97       O  
ATOM   1956  OE2 GLU A1284      -2.242   8.420 -16.324  1.00132.17           O  
ANISOU 1956  OE2 GLU A1284    15712  18522  15982  -1544    558    119       O  
ATOM   1957  N   LEU A1285      -5.584  12.131 -12.107  1.00 98.16           N  
ANISOU 1957  N   LEU A1285    11318  14281  11698  -1080    310    213       N  
ATOM   1958  CA  LEU A1285      -5.716  12.288 -10.671  1.00 94.74           C  
ANISOU 1958  CA  LEU A1285    10940  13769  11290   -978    295    198       C  
ATOM   1959  C   LEU A1285      -6.923  11.528 -10.155  1.00111.64           C  
ANISOU 1959  C   LEU A1285    13078  15991  13349  -1023    360    154       C  
ATOM   1960  O   LEU A1285      -6.804  10.703  -9.242  1.00115.79           O  
ANISOU 1960  O   LEU A1285    13683  16443  13870  -1022    411    107       O  
ATOM   1961  CB  LEU A1285      -5.827  13.764 -10.313  1.00 88.13           C  
ANISOU 1961  CB  LEU A1285    10066  12920  10499   -854    196    253       C  
ATOM   1962  CG  LEU A1285      -5.959  13.992  -8.810  1.00 90.51           C  
ANISOU 1962  CG  LEU A1285    10423  13140  10828   -749    178    238       C  
ATOM   1963  CD1 LEU A1285      -4.765  13.385  -8.057  1.00 83.54           C  
ANISOU 1963  CD1 LEU A1285     9641  12101   9999   -727    199    208       C  
ATOM   1964  CD2 LEU A1285      -6.065  15.468  -8.535  1.00 93.94           C  
ANISOU 1964  CD2 LEU A1285    10825  13563  11306   -632     86    293       C  
ATOM   1965  N   ASP A1286      -8.098  11.791 -10.737  1.00122.59           N  
ANISOU 1965  N   ASP A1286    14374  17539  14667  -1065    362    169       N  
ATOM   1966  CA  ASP A1286      -9.319  11.136 -10.280  1.00129.57           C  
ANISOU 1966  CA  ASP A1286    15247  18521  15463  -1112    421    127       C  
ATOM   1967  C   ASP A1286      -9.197   9.621 -10.373  1.00129.33           C  
ANISOU 1967  C   ASP A1286    15282  18475  15381  -1235    527     63       C  
ATOM   1968  O   ASP A1286      -9.672   8.897  -9.489  1.00137.85           O  
ANISOU 1968  O   ASP A1286    16414  19542  16421  -1248    578     15       O  
ATOM   1969  CB  ASP A1286     -10.521  11.636 -11.086  1.00136.98           C  
ANISOU 1969  CB  ASP A1286    16067  19652  16328  -1149    408    158       C  
ATOM   1970  CG  ASP A1286     -10.771  13.124 -10.903  1.00136.59           C  
ANISOU 1970  CG  ASP A1286    15959  19619  16321  -1018    309    221       C  
ATOM   1971  OD1 ASP A1286      -9.860  13.823 -10.414  1.00133.03           O  
ANISOU 1971  OD1 ASP A1286    15555  19030  15961   -915    248    246       O  
ATOM   1972  OD2 ASP A1286     -11.880  13.593 -11.241  1.00137.69           O  
ANISOU 1972  OD2 ASP A1286    16007  19912  16399  -1017    296    246       O  
ATOM   1973  N   LYS A1287      -8.533   9.125 -11.419  1.00119.73           N  
ANISOU 1973  N   LYS A1287    14071  17254  14169  -1326    561     61       N  
ATOM   1974  CA  LYS A1287      -8.332   7.687 -11.563  1.00124.34           C  
ANISOU 1974  CA  LYS A1287    14728  17810  14707  -1441    667      1       C  
ATOM   1975  C   LYS A1287      -7.443   7.118 -10.460  1.00128.30           C  
ANISOU 1975  C   LYS A1287    15349  18135  15262  -1380    688    -31       C  
ATOM   1976  O   LYS A1287      -7.654   5.977 -10.028  1.00134.39           O  
ANISOU 1976  O   LYS A1287    16194  18883  15984  -1443    775    -86       O  
ATOM   1977  CB  LYS A1287      -7.756   7.390 -12.952  1.00128.66           C  
ANISOU 1977  CB  LYS A1287    15250  18385  15251  -1543    694     10       C  
ATOM   1978  CG  LYS A1287      -6.692   6.300 -13.026  1.00128.53           C  
ANISOU 1978  CG  LYS A1287    15334  18244  15256  -1595    764    -30       C  
ATOM   1979  CD  LYS A1287      -6.288   6.077 -14.483  1.00127.26           C  
ANISOU 1979  CD  LYS A1287    15134  18136  15084  -1703    789    -20       C  
ATOM   1980  CE  LYS A1287      -5.091   5.154 -14.627  1.00124.30           C  
ANISOU 1980  CE  LYS A1287    14854  17631  14743  -1736    848    -52       C  
ATOM   1981  NZ  LYS A1287      -4.580   5.136 -16.034  1.00125.60           N  
ANISOU 1981  NZ  LYS A1287    14972  17839  14910  -1824    855    -36       N  
ATOM   1982  N   ALA A1288      -6.473   7.895  -9.962  1.00122.96           N  
ANISOU 1982  N   ALA A1288    14699  17338  14683  -1260    613      3       N  
ATOM   1983  CA  ALA A1288      -5.539   7.358  -8.973  1.00118.77           C  
ANISOU 1983  CA  ALA A1288    14278  16647  14204  -1202    632    -22       C  
ATOM   1984  C   ALA A1288      -6.086   7.412  -7.552  1.00114.05           C  
ANISOU 1984  C   ALA A1288    13717  16014  13603  -1125    624    -41       C  
ATOM   1985  O   ALA A1288      -5.755   6.543  -6.740  1.00121.16           O  
ANISOU 1985  O   ALA A1288    14710  16821  14503  -1121    677    -81       O  
ATOM   1986  CB  ALA A1288      -4.204   8.102  -9.038  1.00117.15           C  
ANISOU 1986  CB  ALA A1288    14085  16331  14097  -1115    560     20       C  
ATOM   1987  N   ILE A1289      -6.898   8.417  -7.221  1.00108.25           N  
ANISOU 1987  N   ILE A1289    12913  15351  12865  -1059    559    -14       N  
ATOM   1988  CA  ILE A1289      -7.485   8.495  -5.887  1.00104.35           C  
ANISOU 1988  CA  ILE A1289    12449  14835  12365   -989    550    -34       C  
ATOM   1989  C   ILE A1289      -8.866   7.848  -5.828  1.00113.82           C  
ANISOU 1989  C   ILE A1289    13623  16164  13458  -1074    613    -75       C  
ATOM   1990  O   ILE A1289      -9.417   7.687  -4.730  1.00109.46           O  
ANISOU 1990  O   ILE A1289    13102  15601  12887  -1038    621   -103       O  
ATOM   1991  CB  ILE A1289      -7.555   9.956  -5.396  1.00 89.36           C  
ANISOU 1991  CB  ILE A1289    10503  12927  10525   -859    447     16       C  
ATOM   1992  N   GLY A1290      -9.443   7.481  -6.976  1.00127.89           N  
ANISOU 1992  N   GLY A1290    15348  18076  15168  -1191    656    -80       N  
ATOM   1993  CA  GLY A1290     -10.695   6.755  -7.021  1.00142.55           C  
ANISOU 1993  CA  GLY A1290    17184  20067  16913  -1292    726   -123       C  
ATOM   1994  C   GLY A1290     -11.953   7.593  -6.912  1.00152.61           C  
ANISOU 1994  C   GLY A1290    18357  21489  18138  -1258    679   -101       C  
ATOM   1995  O   GLY A1290     -13.048   7.066  -7.151  1.00165.74           O  
ANISOU 1995  O   GLY A1290    19982  23295  19697  -1354    734   -132       O  
ATOM   1996  N   ARG A1291     -11.842   8.869  -6.549  1.00140.29           N  
ANISOU 1996  N   ARG A1291    16754  19904  16647  -1126    583    -50       N  
ATOM   1997  CA  ARG A1291     -12.978   9.772  -6.450  1.00130.51           C  
ANISOU 1997  CA  ARG A1291    15419  18799  15369  -1074    534    -23       C  
ATOM   1998  C   ARG A1291     -12.788  10.936  -7.415  1.00137.40           C  
ANISOU 1998  C   ARG A1291    16205  19718  16281  -1026    460     48       C  
ATOM   1999  O   ARG A1291     -11.665  11.255  -7.812  1.00142.30           O  
ANISOU 1999  O   ARG A1291    16853  20234  16982   -999    427     77       O  
ATOM   2000  CB  ARG A1291     -13.147  10.298  -5.014  1.00107.08           C  
ANISOU 2000  CB  ARG A1291    12485  15759  12442   -948    488    -28       C  
ATOM   2001  CG  ARG A1291     -11.872  10.861  -4.430  1.00 98.49           C  
ANISOU 2001  CG  ARG A1291    11463  14486  11473   -837    431     -3       C  
ATOM   2002  CD  ARG A1291     -12.121  11.650  -3.166  1.00102.10           C  
ANISOU 2002  CD  ARG A1291    11930  14893  11970   -708    374      5       C  
ATOM   2003  NE  ARG A1291     -12.130  13.090  -3.404  1.00108.51           N  
ANISOU 2003  NE  ARG A1291    12677  15720  12830   -604    286     69       N  
ATOM   2004  CZ  ARG A1291     -11.317  13.960  -2.812  1.00108.17           C  
ANISOU 2004  CZ  ARG A1291    12672  15548  12881   -491    221     99       C  
ATOM   2005  NH1 ARG A1291     -10.416  13.543  -1.932  1.00110.55           N  
ANISOU 2005  NH1 ARG A1291    13067  15701  13236   -465    231     73       N  
ATOM   2006  NH2 ARG A1291     -11.414  15.253  -3.101  1.00102.50           N  
ANISOU 2006  NH2 ARG A1291    11898  14851  12196   -404    147    157       N  
ATOM   2007  N   ASN A1292     -13.899  11.558  -7.817  1.00140.28           N  
ANISOU 2007  N   ASN A1292    16465  20248  16586  -1020    436     76       N  
ATOM   2008  CA  ASN A1292     -13.829  12.820  -8.546  1.00137.87           C  
ANISOU 2008  CA  ASN A1292    16081  19985  16320   -949    356    150       C  
ATOM   2009  C   ASN A1292     -13.261  13.888  -7.613  1.00138.44           C  
ANISOU 2009  C   ASN A1292    16192  19918  16492   -789    275    182       C  
ATOM   2010  O   ASN A1292     -14.016  14.519  -6.863  1.00138.76           O  
ANISOU 2010  O   ASN A1292    16205  19996  16522   -700    241    191       O  
ATOM   2011  CB  ASN A1292     -15.214  13.239  -9.074  1.00138.49           C  
ANISOU 2011  CB  ASN A1292    16039  20277  16306   -965    351    175       C  
ATOM   2012  CG  ASN A1292     -15.645  12.471 -10.344  1.00137.23           C  
ANISOU 2012  CG  ASN A1292    15818  20269  16054  -1126    416    164       C  
ATOM   2013  OD1 ASN A1292     -14.850  11.760 -10.965  1.00132.02           O  
ANISOU 2013  OD1 ASN A1292    15202  19550  15408  -1219    458    145       O  
ATOM   2014  ND2 ASN A1292     -16.914  12.641 -10.735  1.00136.06           N  
ANISOU 2014  ND2 ASN A1292    15566  20323  15807  -1157    425    177       N  
ATOM   2015  N   THR A1293     -11.933  14.087  -7.632  1.00137.82           N  
ANISOU 2015  N   THR A1293    16177  19682  16506   -754    245    196       N  
ATOM   2016  CA  THR A1293     -11.291  14.938  -6.629  1.00139.98           C  
ANISOU 2016  CA  THR A1293    16505  19812  16870   -618    180    216       C  
ATOM   2017  C   THR A1293     -11.381  16.424  -6.952  1.00145.83           C  
ANISOU 2017  C   THR A1293    17188  20573  17649   -515     93    286       C  
ATOM   2018  O   THR A1293     -11.299  17.246  -6.030  1.00147.94           O  
ANISOU 2018  O   THR A1293    17482  20762  17966   -397     42    302       O  
ATOM   2019  CB  THR A1293      -9.812  14.571  -6.446  1.00129.46           C  
ANISOU 2019  CB  THR A1293    15266  18308  15616   -620    183    204       C  
ATOM   2020  OG1 THR A1293      -9.071  14.976  -7.602  1.00133.13           O  
ANISOU 2020  OG1 THR A1293    15703  18767  16113   -645    153    246       O  
ATOM   2021  CG2 THR A1293      -9.634  13.081  -6.234  1.00121.94           C  
ANISOU 2021  CG2 THR A1293    14378  17327  14627   -720    272    139       C  
ATOM   2022  N   ASN A1294     -11.501  16.783  -8.226  1.00141.20           N  
ANISOU 2022  N   ASN A1294    16527  20081  17041   -558     78    329       N  
ATOM   2023  CA  ASN A1294     -11.649  18.227  -8.532  1.00140.88           C  
ANISOU 2023  CA  ASN A1294    16434  20061  17031   -454     -3    400       C  
ATOM   2024  C   ASN A1294     -10.351  18.983  -8.239  1.00132.69           C  
ANISOU 2024  C   ASN A1294    15469  18850  16098   -374    -63    426       C  
ATOM   2025  O   ASN A1294     -10.437  20.094  -7.702  1.00133.05           O  
ANISOU 2025  O   ASN A1294    15520  18851  16183   -255   -123    462       O  
ATOM   2026  CB  ASN A1294     -12.761  18.846  -7.687  1.00148.88           C  
ANISOU 2026  CB  ASN A1294    17415  21136  18015   -356    -25    407       C  
ATOM   2027  CG  ASN A1294     -13.774  19.605  -8.514  1.00156.15           C  
ANISOU 2027  CG  ASN A1294    18226  22222  18881   -334    -51    462       C  
ATOM   2028  OD1 ASN A1294     -14.573  19.003  -9.225  1.00163.66           O  
ANISOU 2028  OD1 ASN A1294    19104  23333  19745   -428     -6    452       O  
ATOM   2029  ND2 ASN A1294     -13.748  20.924  -8.429  1.00153.44           N  
ANISOU 2029  ND2 ASN A1294    17872  21845  18583   -210   -122    520       N  
ATOM   2030  N   GLY A1295      -9.200  18.401  -8.568  1.00123.64           N  
ANISOU 2030  N   GLY A1295    14376  17610  14991   -437    -45    409       N  
ATOM   2031  CA  GLY A1295      -7.932  19.076  -8.388  1.00112.67           C  
ANISOU 2031  CA  GLY A1295    13048  16072  13690   -375   -100    434       C  
ATOM   2032  C   GLY A1295      -7.384  19.071  -6.984  1.00110.35           C  
ANISOU 2032  C   GLY A1295    12843  15636  13449   -299   -108    405       C  
ATOM   2033  O   GLY A1295      -6.227  19.470  -6.783  1.00110.26           O  
ANISOU 2033  O   GLY A1295    12889  15500  13505   -261   -144    418       O  
ATOM   2034  N   VAL A1296      -8.155  18.629  -6.001  1.00113.97           N  
ANISOU 2034  N   VAL A1296    13314  16114  13876   -279    -74    366       N  
ATOM   2035  CA  VAL A1296      -7.749  18.736  -4.610  1.00112.05           C  
ANISOU 2035  CA  VAL A1296    13149  15747  13680   -200    -86    343       C  
ATOM   2036  C   VAL A1296      -7.909  17.376  -3.944  1.00115.63           C  
ANISOU 2036  C   VAL A1296    13644  16190  14098   -262    -11    277       C  
ATOM   2037  O   VAL A1296      -8.939  16.714  -4.109  1.00117.86           O  
ANISOU 2037  O   VAL A1296    13886  16589  14306   -324     38    250       O  
ATOM   2038  CB  VAL A1296      -8.550  19.833  -3.884  1.00104.36           C  
ANISOU 2038  CB  VAL A1296    12152  14788  12710    -85   -134    369       C  
ATOM   2039  CG1 VAL A1296      -8.287  19.794  -2.370  1.00115.09           C  
ANISOU 2039  CG1 VAL A1296    13588  16035  14108    -16   -136    336       C  
ATOM   2040  CG2 VAL A1296      -8.184  21.200  -4.471  1.00 84.15           C  
ANISOU 2040  CG2 VAL A1296     9574  12206  10193    -17   -208    435       C  
ATOM   2041  N   ILE A1297      -6.867  16.947  -3.231  1.00109.78           N  
ANISOU 2041  N   ILE A1297    12988  15315  13408   -251     -1    253       N  
ATOM   2042  CA  ILE A1297      -6.856  15.709  -2.465  1.00102.37           C  
ANISOU 2042  CA  ILE A1297    12107  14340  12447   -295     66    193       C  
ATOM   2043  C   ILE A1297      -6.667  16.066  -0.991  1.00 94.95           C  
ANISOU 2043  C   ILE A1297    11225  13300  11551   -198     40    181       C  
ATOM   2044  O   ILE A1297      -6.335  17.199  -0.646  1.00 91.86           O  
ANISOU 2044  O   ILE A1297    10838  12853  11213   -107    -25    217       O  
ATOM   2045  CB  ILE A1297      -5.751  14.744  -2.942  1.00 92.69           C  
ANISOU 2045  CB  ILE A1297    10933  13049  11237   -370    110    174       C  
ATOM   2046  CG1 ILE A1297      -4.403  15.468  -2.930  1.00 87.57           C  
ANISOU 2046  CG1 ILE A1297    10320  12284  10669   -310     53    209       C  
ATOM   2047  CG2 ILE A1297      -6.069  14.206  -4.344  1.00 87.25           C  
ANISOU 2047  CG2 ILE A1297    10189  12468  10493   -482    151    175       C  
ATOM   2048  CD1 ILE A1297      -3.223  14.562  -2.752  1.00 80.38           C  
ANISOU 2048  CD1 ILE A1297     9483  11273   9786   -341     91    184       C  
ATOM   2049  N   THR A1298      -6.888  15.080  -0.123  1.00 89.38           N  
ANISOU 2049  N   THR A1298    10567  12572  10820   -223     96    129       N  
ATOM   2050  CA  THR A1298      -6.619  15.212   1.303  1.00 85.91           C  
ANISOU 2050  CA  THR A1298    10188  12032  10420   -146     81    112       C  
ATOM   2051  C   THR A1298      -5.181  14.820   1.603  1.00 84.99           C  
ANISOU 2051  C   THR A1298    10149  11784  10360   -141     87    109       C  
ATOM   2052  O   THR A1298      -4.511  14.169   0.795  1.00 86.69           O  
ANISOU 2052  O   THR A1298    10377  11988  10573   -207    119    107       O  
ATOM   2053  CB  THR A1298      -7.541  14.322   2.132  1.00 84.17           C  
ANISOU 2053  CB  THR A1298     9985  11853  10142   -176    137     58       C  
ATOM   2054  OG1 THR A1298      -7.342  12.953   1.754  1.00 86.12           O  
ANISOU 2054  OG1 THR A1298    10268  12104  10349   -279    215     20       O  
ATOM   2055  CG2 THR A1298      -8.999  14.716   1.948  1.00 80.47           C  
ANISOU 2055  CG2 THR A1298     9437  11525   9611   -176    131     59       C  
ATOM   2056  N   LYS A1299      -4.715  15.195   2.803  1.00 81.42           N  
ANISOU 2056  N   LYS A1299     9746  11234   9955    -62     59    107       N  
ATOM   2057  CA  LYS A1299      -3.406  14.714   3.227  1.00 80.58           C  
ANISOU 2057  CA  LYS A1299     9712  11013   9894    -55     71    101       C  
ATOM   2058  C   LYS A1299      -3.392  13.200   3.341  1.00 91.04           C  
ANISOU 2058  C   LYS A1299    11083  12332  11178   -129    154     54       C  
ATOM   2059  O   LYS A1299      -2.361  12.563   3.096  1.00 93.03           O  
ANISOU 2059  O   LYS A1299    11378  12520  11447   -155    182     52       O  
ATOM   2060  CB  LYS A1299      -2.984  15.324   4.557  1.00 83.23           C  
ANISOU 2060  CB  LYS A1299    10089  11256  10278     35     31    104       C  
ATOM   2061  CG  LYS A1299      -1.606  14.810   4.995  1.00 88.39           C  
ANISOU 2061  CG  LYS A1299    10811  11802  10971     43     44    101       C  
ATOM   2062  CD  LYS A1299      -1.366  14.943   6.480  1.00 96.21           C  
ANISOU 2062  CD  LYS A1299    11850  12714  11990    109     33     88       C  
ATOM   2063  CE  LYS A1299      -0.881  16.340   6.833  1.00 96.89           C  
ANISOU 2063  CE  LYS A1299    11932  12754  12129    187    -43    127       C  
ATOM   2064  NZ  LYS A1299       0.400  16.671   6.161  1.00 88.15           N  
ANISOU 2064  NZ  LYS A1299    10833  11602  11057    184    -70    161       N  
ATOM   2065  N   ASP A1300      -4.525  12.600   3.687  1.00100.41           N  
ANISOU 2065  N   ASP A1300    12262  13584  12306   -165    198     15       N  
ATOM   2066  CA  ASP A1300      -4.506  11.163   3.894  1.00111.32           C  
ANISOU 2066  CA  ASP A1300    13701  14949  13646   -235    281    -31       C  
ATOM   2067  C   ASP A1300      -4.413  10.420   2.576  1.00102.36           C  
ANISOU 2067  C   ASP A1300    12554  13865  12474   -334    332    -36       C  
ATOM   2068  O   ASP A1300      -3.818   9.339   2.521  1.00 94.45           O  
ANISOU 2068  O   ASP A1300    11614  12811  11462   -380    394    -60       O  
ATOM   2069  CB  ASP A1300      -5.732  10.721   4.688  1.00131.23           C  
ANISOU 2069  CB  ASP A1300    16224  17526  16110   -252    315    -75       C  
ATOM   2070  CG  ASP A1300      -5.493   9.427   5.429  1.00139.60           C  
ANISOU 2070  CG  ASP A1300    17370  18522  17148   -287    386   -120       C  
ATOM   2071  OD1 ASP A1300      -5.336   8.386   4.752  1.00144.31           O  
ANISOU 2071  OD1 ASP A1300    17997  19128  17706   -371    454   -141       O  
ATOM   2072  OD2 ASP A1300      -5.424   9.461   6.681  1.00136.31           O  
ANISOU 2072  OD2 ASP A1300    16994  18043  16754   -230    375   -134       O  
ATOM   2073  N   GLU A1301      -4.977  10.988   1.507  1.00105.64           N  
ANISOU 2073  N   GLU A1301    12890  14382  12866   -365    309    -12       N  
ATOM   2074  CA  GLU A1301      -4.839  10.378   0.189  1.00106.34           C  
ANISOU 2074  CA  GLU A1301    12960  14522  12921   -462    353    -14       C  
ATOM   2075  C   GLU A1301      -3.447  10.598  -0.396  1.00 92.58           C  
ANISOU 2075  C   GLU A1301    11235  12700  11239   -446    327     19       C  
ATOM   2076  O   GLU A1301      -2.956   9.755  -1.155  1.00 89.44           O  
ANISOU 2076  O   GLU A1301    10860  12297  10826   -520    380      6       O  
ATOM   2077  CB  GLU A1301      -5.908  10.932  -0.749  1.00116.76           C  
ANISOU 2077  CB  GLU A1301    14185  15986  14194   -501    335      4       C  
ATOM   2078  CG  GLU A1301      -7.326  10.626  -0.308  1.00124.98           C  
ANISOU 2078  CG  GLU A1301    15200  17128  15160   -530    367    -30       C  
ATOM   2079  CD  GLU A1301      -8.351  11.523  -0.973  1.00130.77           C  
ANISOU 2079  CD  GLU A1301    15830  17999  15859   -526    326      1       C  
ATOM   2080  OE1 GLU A1301      -8.057  12.723  -1.163  1.00129.17           O  
ANISOU 2080  OE1 GLU A1301    15589  17781  15710   -447    250     51       O  
ATOM   2081  OE2 GLU A1301      -9.452  11.033  -1.301  1.00136.57           O  
ANISOU 2081  OE2 GLU A1301    16522  18858  16508   -601    371    -25       O  
ATOM   2082  N   ALA A1302      -2.805  11.720  -0.058  1.00 82.32           N  
ANISOU 2082  N   ALA A1302     9928  11343  10007   -355    249     59       N  
ATOM   2083  CA  ALA A1302      -1.429  11.946  -0.482  1.00 76.33           C  
ANISOU 2083  CA  ALA A1302     9190  10508   9303   -337    222     87       C  
ATOM   2084  C   ALA A1302      -0.488  10.897   0.107  1.00 79.43           C  
ANISOU 2084  C   ALA A1302     9668  10803   9710   -339    274     61       C  
ATOM   2085  O   ALA A1302       0.348  10.338  -0.608  1.00 89.92           O  
ANISOU 2085  O   ALA A1302    11016  12107  11043   -381    304     62       O  
ATOM   2086  CB  ALA A1302      -0.987  13.357  -0.092  1.00 70.42           C  
ANISOU 2086  CB  ALA A1302     8424   9716   8614   -241    131    131       C  
ATOM   2087  N   GLU A1303      -0.614  10.610   1.405  1.00 74.26           N  
ANISOU 2087  N   GLU A1303     9064  10093   9058   -291    288     37       N  
ATOM   2088  CA  GLU A1303       0.244   9.606   2.029  1.00 70.84           C  
ANISOU 2088  CA  GLU A1303     8712   9568   8634   -285    340     15       C  
ATOM   2089  C   GLU A1303      -0.002   8.219   1.446  1.00 75.65           C  
ANISOU 2089  C   GLU A1303     9355  10200   9186   -381    435    -23       C  
ATOM   2090  O   GLU A1303       0.943   7.451   1.240  1.00 79.87           O  
ANISOU 2090  O   GLU A1303     9942  10674   9730   -395    478    -28       O  
ATOM   2091  CB  GLU A1303       0.034   9.588   3.545  1.00 65.69           C  
ANISOU 2091  CB  GLU A1303     8104   8863   7992   -220    335     -2       C  
ATOM   2092  CG  GLU A1303       0.746  10.702   4.307  1.00 74.10           C  
ANISOU 2092  CG  GLU A1303     9167   9866   9122   -122    257     33       C  
ATOM   2093  CD  GLU A1303       2.224  10.400   4.572  1.00 88.32           C  
ANISOU 2093  CD  GLU A1303    11020  11575  10962    -88    260     47       C  
ATOM   2094  OE1 GLU A1303       2.634   9.216   4.450  1.00 89.58           O  
ANISOU 2094  OE1 GLU A1303    11231  11706  11101   -124    330     26       O  
ATOM   2095  OE2 GLU A1303       2.976  11.351   4.905  1.00 88.08           O  
ANISOU 2095  OE2 GLU A1303    10982  11505  10979    -24    195     80       O  
ATOM   2096  N   LYS A1304      -1.260   7.863   1.198  1.00 78.76           N  
ANISOU 2096  N   LYS A1304     9724  10683   9517   -448    473    -52       N  
ATOM   2097  CA  LYS A1304      -1.530   6.576   0.564  1.00 86.89           C  
ANISOU 2097  CA  LYS A1304    10788  11742  10486   -552    568    -90       C  
ATOM   2098  C   LYS A1304      -0.908   6.534  -0.819  1.00 83.83           C  
ANISOU 2098  C   LYS A1304    10372  11376  10104   -606    574    -70       C  
ATOM   2099  O   LYS A1304      -0.295   5.533  -1.211  1.00 82.08           O  
ANISOU 2099  O   LYS A1304    10205  11111   9870   -654    642    -88       O  
ATOM   2100  CB  LYS A1304      -3.041   6.329   0.491  1.00 93.83           C  
ANISOU 2100  CB  LYS A1304    11634  12731  11288   -620    601   -122       C  
ATOM   2101  CG  LYS A1304      -3.442   4.930   0.056  1.00 96.22           C  
ANISOU 2101  CG  LYS A1304    11985  13059  11514   -734    708   -170       C  
ATOM   2102  CD  LYS A1304      -4.901   4.629   0.419  1.00 99.16           C  
ANISOU 2102  CD  LYS A1304    12342  13526  11807   -789    742   -208       C  
ATOM   2103  CE  LYS A1304      -5.890   5.445  -0.419  1.00103.88           C  
ANISOU 2103  CE  LYS A1304    12828  14270  12371   -824    701   -190       C  
ATOM   2104  NZ  LYS A1304      -5.855   5.063  -1.865  1.00107.08           N  
ANISOU 2104  NZ  LYS A1304    13202  14743  12740   -927    742   -188       N  
ATOM   2105  N   LEU A1305      -1.055   7.632  -1.561  1.00 85.74           N  
ANISOU 2105  N   LEU A1305    10529  11682  10366   -598    504    -32       N  
ATOM   2106  CA  LEU A1305      -0.437   7.771  -2.872  1.00 79.32           C  
ANISOU 2106  CA  LEU A1305     9680  10894   9565   -644    496     -9       C  
ATOM   2107  C   LEU A1305       1.080   7.707  -2.761  1.00 78.59           C  
ANISOU 2107  C   LEU A1305     9635  10693   9531   -594    483      9       C  
ATOM   2108  O   LEU A1305       1.748   6.996  -3.523  1.00 77.84           O  
ANISOU 2108  O   LEU A1305     9563  10581   9430   -647    530      1       O  
ATOM   2109  CB  LEU A1305      -0.882   9.103  -3.471  1.00 76.66           C  
ANISOU 2109  CB  LEU A1305     9248  10636   9242   -625    413     34       C  
ATOM   2110  CG  LEU A1305      -1.099   9.303  -4.960  1.00 81.41           C  
ANISOU 2110  CG  LEU A1305     9778  11333   9820   -706    410     52       C  
ATOM   2111  CD1 LEU A1305      -2.025   8.241  -5.503  1.00 86.40           C  
ANISOU 2111  CD1 LEU A1305    10407  12052  10370   -821    499     10       C  
ATOM   2112  CD2 LEU A1305      -1.709  10.668  -5.122  1.00 79.29           C  
ANISOU 2112  CD2 LEU A1305     9430  11133   9565   -658    326     94       C  
ATOM   2113  N   PHE A1306       1.638   8.452  -1.801  1.00 75.26           N  
ANISOU 2113  N   PHE A1306     9228  10204   9164   -492    420     32       N  
ATOM   2114  CA  PHE A1306       3.080   8.501  -1.615  1.00 76.12           C  
ANISOU 2114  CA  PHE A1306     9375  10223   9324   -438    400     52       C  
ATOM   2115  C   PHE A1306       3.637   7.137  -1.222  1.00 77.87           C  
ANISOU 2115  C   PHE A1306     9683  10375   9531   -450    485     20       C  
ATOM   2116  O   PHE A1306       4.741   6.770  -1.637  1.00 84.22           O  
ANISOU 2116  O   PHE A1306    10512  11134  10353   -449    501     29       O  
ATOM   2117  CB  PHE A1306       3.412   9.566  -0.571  1.00 74.49           C  
ANISOU 2117  CB  PHE A1306     9167   9968   9168   -334    320     80       C  
ATOM   2118  CG  PHE A1306       4.831   9.528  -0.078  1.00 76.82           C  
ANISOU 2118  CG  PHE A1306     9507  10173   9507   -273    306     96       C  
ATOM   2119  CD1 PHE A1306       5.880   9.907  -0.903  1.00 78.68           C  
ANISOU 2119  CD1 PHE A1306     9722  10402   9770   -277    273    124       C  
ATOM   2120  CD2 PHE A1306       5.110   9.143   1.223  1.00 71.39           C  
ANISOU 2120  CD2 PHE A1306     8880   9414   8830   -212    323     84       C  
ATOM   2121  CE1 PHE A1306       7.187   9.889  -0.439  1.00 74.73           C  
ANISOU 2121  CE1 PHE A1306     9258   9832   9302   -220    258    140       C  
ATOM   2122  CE2 PHE A1306       6.412   9.123   1.690  1.00 71.11           C  
ANISOU 2122  CE2 PHE A1306     8881   9308   8829   -154    309    101       C  
ATOM   2123  CZ  PHE A1306       7.454   9.498   0.858  1.00 71.42           C  
ANISOU 2123  CZ  PHE A1306     8897   9348   8892   -158    277    129       C  
ATOM   2124  N   ASN A1307       2.885   6.360  -0.444  1.00 75.55           N  
ANISOU 2124  N   ASN A1307     9436  10071   9198   -462    543    -17       N  
ATOM   2125  CA  ASN A1307       3.373   5.038  -0.070  1.00 78.47           C  
ANISOU 2125  CA  ASN A1307     9897  10370   9550   -472    630    -46       C  
ATOM   2126  C   ASN A1307       3.412   4.102  -1.263  1.00 77.41           C  
ANISOU 2126  C   ASN A1307     9776  10263   9375   -571    707    -67       C  
ATOM   2127  O   ASN A1307       4.319   3.268  -1.369  1.00 68.91           O  
ANISOU 2127  O   ASN A1307     8761   9120   8301   -569    761    -74       O  
ATOM   2128  CB  ASN A1307       2.507   4.459   1.043  1.00 89.38           C  
ANISOU 2128  CB  ASN A1307    11328  11736  10895   -468    672    -82       C  
ATOM   2129  CG  ASN A1307       3.050   4.766   2.410  1.00 92.74           C  
ANISOU 2129  CG  ASN A1307    11790  12084  11364   -363    634    -68       C  
ATOM   2130  OD1 ASN A1307       3.568   3.887   3.091  1.00100.80           O  
ANISOU 2130  OD1 ASN A1307    12889  13028  12381   -337    687    -82       O  
ATOM   2131  ND2 ASN A1307       2.976   6.031   2.806  1.00 86.71           N  
ANISOU 2131  ND2 ASN A1307    10969  11335  10640   -302    544    -39       N  
ATOM   2132  N   GLN A1308       2.427   4.215  -2.159  1.00 84.42           N  
ANISOU 2132  N   GLN A1308    10607  11250  10220   -659    716    -78       N  
ATOM   2133  CA  GLN A1308       2.456   3.461  -3.406  1.00 81.49           C  
ANISOU 2133  CA  GLN A1308    10237  10916   9810   -762    784    -96       C  
ATOM   2134  C   GLN A1308       3.615   3.892  -4.292  1.00 78.42           C  
ANISOU 2134  C   GLN A1308     9817  10513   9468   -750    744    -62       C  
ATOM   2135  O   GLN A1308       4.197   3.066  -5.004  1.00 80.66           O  
ANISOU 2135  O   GLN A1308    10135  10774   9737   -800    808    -75       O  
ATOM   2136  CB  GLN A1308       1.145   3.644  -4.159  1.00 90.52           C  
ANISOU 2136  CB  GLN A1308    11313  12184  10897   -856    791   -108       C  
ATOM   2137  CG  GLN A1308      -0.077   3.053  -3.497  1.00 96.94           C  
ANISOU 2137  CG  GLN A1308    12155  13033  11646   -897    845   -150       C  
ATOM   2138  CD  GLN A1308      -1.293   3.199  -4.382  1.00 98.01           C  
ANISOU 2138  CD  GLN A1308    12216  13307  11718   -997    856   -160       C  
ATOM   2139  OE1 GLN A1308      -2.332   3.703  -3.953  1.00 95.42           O  
ANISOU 2139  OE1 GLN A1308    11843  13050  11364   -989    825   -162       O  
ATOM   2140  NE2 GLN A1308      -1.160   2.779  -5.641  1.00 98.54           N  
ANISOU 2140  NE2 GLN A1308    12264  13419  11756  -1093    900   -166       N  
ATOM   2141  N   ASP A1309       3.959   5.179  -4.256  1.00 73.77           N  
ANISOU 2141  N   ASP A1309     9165   9935   8931   -685    642    -19       N  
ATOM   2142  CA  ASP A1309       5.072   5.685  -5.047  1.00 69.42           C  
ANISOU 2142  CA  ASP A1309     8581   9373   8422   -672    596     14       C  
ATOM   2143  C   ASP A1309       6.395   5.068  -4.610  1.00 72.87           C  
ANISOU 2143  C   ASP A1309     9089   9711   8886   -616    624     15       C  
ATOM   2144  O   ASP A1309       7.145   4.537  -5.437  1.00 75.51           O  
ANISOU 2144  O   ASP A1309     9435  10035   9219   -654    661     12       O  
ATOM   2145  CB  ASP A1309       5.121   7.209  -4.945  1.00 79.10           C  
ANISOU 2145  CB  ASP A1309     9738  10623   9692   -611    483     59       C  
ATOM   2146  CG  ASP A1309       4.073   7.894  -5.817  1.00 93.96           C  
ANISOU 2146  CG  ASP A1309    11536  12615  11550   -671    451     70       C  
ATOM   2147  OD1 ASP A1309       3.747   7.366  -6.902  1.00 93.21           O  
ANISOU 2147  OD1 ASP A1309    11417  12582  11416   -769    499     55       O  
ATOM   2148  OD2 ASP A1309       3.574   8.966  -5.405  1.00 98.32           O  
ANISOU 2148  OD2 ASP A1309    12046  13192  12120   -619    379     95       O  
ATOM   2149  N   VAL A1310       6.714   5.151  -3.312  1.00 73.84           N  
ANISOU 2149  N   VAL A1310     9256   9764   9034   -524    606     20       N  
ATOM   2150  CA  VAL A1310       7.954   4.557  -2.819  1.00 69.62           C  
ANISOU 2150  CA  VAL A1310     8787   9144   8521   -462    634     24       C  
ATOM   2151  C   VAL A1310       7.963   3.063  -3.104  1.00 77.01           C  
ANISOU 2151  C   VAL A1310     9798  10050   9415   -517    749    -14       C  
ATOM   2152  O   VAL A1310       9.003   2.481  -3.441  1.00 82.38           O  
ANISOU 2152  O   VAL A1310    10512  10686  10102   -505    786    -10       O  
ATOM   2153  CB  VAL A1310       8.154   4.847  -1.315  1.00 68.79           C  
ANISOU 2153  CB  VAL A1310     8716   8979   8443   -361    601     35       C  
ATOM   2154  CG1 VAL A1310       9.455   4.220  -0.843  1.00 67.37           C  
ANISOU 2154  CG1 VAL A1310     8597   8721   8279   -296    630     43       C  
ATOM   2155  CG2 VAL A1310       8.168   6.350  -1.035  1.00 59.18           C  
ANISOU 2155  CG2 VAL A1310     7433   7787   7267   -310    490     71       C  
ATOM   2156  N   ASP A1311       6.804   2.417  -2.983  1.00 82.14           N  
ANISOU 2156  N   ASP A1311    10474  10722  10013   -580    812    -51       N  
ATOM   2157  CA  ASP A1311       6.696   1.022  -3.393  1.00 81.32           C  
ANISOU 2157  CA  ASP A1311    10444  10596   9860   -651    928    -90       C  
ATOM   2158  C   ASP A1311       7.088   0.857  -4.858  1.00 84.42           C  
ANISOU 2158  C   ASP A1311    10803  11027  10244   -729    950    -90       C  
ATOM   2159  O   ASP A1311       7.877  -0.029  -5.210  1.00 91.45           O  
ANISOU 2159  O   ASP A1311    11751  11867  11127   -736   1017   -100       O  
ATOM   2160  CB  ASP A1311       5.274   0.522  -3.152  1.00 95.66           C  
ANISOU 2160  CB  ASP A1311    12281  12452  11615   -723    982   -130       C  
ATOM   2161  CG  ASP A1311       5.137  -0.979  -3.357  1.00119.19           C  
ANISOU 2161  CG  ASP A1311    15357  15393  14537   -794   1110   -175       C  
ATOM   2162  OD1 ASP A1311       4.842  -1.406  -4.498  1.00122.37           O  
ANISOU 2162  OD1 ASP A1311    15747  15847  14900   -899   1162   -194       O  
ATOM   2163  OD2 ASP A1311       5.320  -1.730  -2.373  1.00128.52           O  
ANISOU 2163  OD2 ASP A1311    16630  16494  15710   -746   1160   -189       O  
ATOM   2164  N   ALA A1312       6.561   1.722  -5.729  1.00 77.73           N  
ANISOU 2164  N   ALA A1312     9863  10273   9397   -785    893    -76       N  
ATOM   2165  CA  ALA A1312       6.775   1.559  -7.164  1.00 81.29           C  
ANISOU 2165  CA  ALA A1312    10276  10775   9835   -874    916    -78       C  
ATOM   2166  C   ALA A1312       8.218   1.855  -7.550  1.00 83.90           C  
ANISOU 2166  C   ALA A1312    10596  11067  10215   -822    877    -48       C  
ATOM   2167  O   ALA A1312       8.780   1.173  -8.420  1.00 82.97           O  
ANISOU 2167  O   ALA A1312    10498  10942  10085   -873    934    -61       O  
ATOM   2168  CB  ALA A1312       5.813   2.456  -7.941  1.00 76.12           C  
ANISOU 2168  CB  ALA A1312     9521  10235   9166   -941    861    -67       C  
ATOM   2169  N   ALA A1313       8.825   2.867  -6.918  1.00 76.63           N  
ANISOU 2169  N   ALA A1313     9644  10125   9346   -724    782    -10       N  
ATOM   2170  CA  ALA A1313      10.239   3.154  -7.138  1.00 75.81           C  
ANISOU 2170  CA  ALA A1313     9533   9988   9285   -669    743     18       C  
ATOM   2171  C   ALA A1313      11.101   1.952  -6.783  1.00 74.30           C  
ANISOU 2171  C   ALA A1313     9432   9714   9085   -631    827      1       C  
ATOM   2172  O   ALA A1313      12.035   1.602  -7.513  1.00 76.16           O  
ANISOU 2172  O   ALA A1313     9672   9940   9326   -642    850      4       O  
ATOM   2173  CB  ALA A1313      10.662   4.381  -6.322  1.00 61.83           C  
ANISOU 2173  CB  ALA A1313     7727   8205   7562   -571    636     58       C  
ATOM   2174  N   VAL A1314      10.796   1.303  -5.664  1.00 75.90           N  
ANISOU 2174  N   VAL A1314     9710   9857   9273   -585    876    -15       N  
ATOM   2175  CA  VAL A1314      11.620   0.199  -5.196  1.00 75.16           C  
ANISOU 2175  CA  VAL A1314     9707   9678   9172   -534    954    -25       C  
ATOM   2176  C   VAL A1314      11.422  -1.025  -6.075  1.00 77.95           C  
ANISOU 2176  C   VAL A1314    10115  10024   9478   -624   1068    -64       C  
ATOM   2177  O   VAL A1314      12.364  -1.782  -6.325  1.00 85.81           O  
ANISOU 2177  O   VAL A1314    11161  10971  10472   -601   1125    -66       O  
ATOM   2178  CB  VAL A1314      11.304  -0.087  -3.715  1.00 78.26           C  
ANISOU 2178  CB  VAL A1314    10163  10011   9561   -460    969    -30       C  
ATOM   2179  CG1 VAL A1314      11.820  -1.455  -3.293  1.00 70.39           C  
ANISOU 2179  CG1 VAL A1314     9276   8929   8540   -427   1074    -48       C  
ATOM   2180  CG2 VAL A1314      11.916   0.996  -2.877  1.00 77.39           C  
ANISOU 2180  CG2 VAL A1314    10011   9894   9500   -359    867     11       C  
ATOM   2181  N   ARG A1315      10.201  -1.248  -6.558  1.00 83.86           N  
ANISOU 2181  N   ARG A1315    10854  10824  10184   -730   1107    -95       N  
ATOM   2182  CA  ARG A1315       9.998  -2.350  -7.487  1.00 92.94           C  
ANISOU 2182  CA  ARG A1315    12051  11975  11285   -831   1215   -133       C  
ATOM   2183  C   ARG A1315      10.742  -2.099  -8.790  1.00 93.54           C  
ANISOU 2183  C   ARG A1315    12070  12092  11378   -874   1197   -121       C  
ATOM   2184  O   ARG A1315      11.325  -3.020  -9.374  1.00 97.23           O  
ANISOU 2184  O   ARG A1315    12591  12524  11829   -902   1279   -139       O  
ATOM   2185  CB  ARG A1315       8.510  -2.550  -7.749  1.00106.39           C  
ANISOU 2185  CB  ARG A1315    13747  13744  12934   -944   1255   -168       C  
ATOM   2186  CG  ARG A1315       7.794  -3.321  -6.673  1.00116.15           C  
ANISOU 2186  CG  ARG A1315    15072  14929  14130   -933   1320   -198       C  
ATOM   2187  CD  ARG A1315       6.391  -3.673  -7.124  1.00124.64           C  
ANISOU 2187  CD  ARG A1315    16142  16079  15136  -1064   1375   -238       C  
ATOM   2188  NE  ARG A1315       5.434  -3.449  -6.051  1.00128.08           N  
ANISOU 2188  NE  ARG A1315    16584  16526  15555  -1040   1353   -246       N  
ATOM   2189  CZ  ARG A1315       5.230  -4.296  -5.048  1.00128.24           C  
ANISOU 2189  CZ  ARG A1315    16705  16472  15546  -1014   1419   -271       C  
ATOM   2190  NH1 ARG A1315       5.918  -5.431  -4.980  1.00129.68           N  
ANISOU 2190  NH1 ARG A1315    16997  16561  15714  -1002   1513   -288       N  
ATOM   2191  NH2 ARG A1315       4.339  -4.003  -4.112  1.00124.72           N  
ANISOU 2191  NH2 ARG A1315    16255  16047  15086   -997   1390   -279       N  
ATOM   2192  N   GLY A1316      10.733  -0.852  -9.258  1.00 91.82           N  
ANISOU 2192  N   GLY A1316    11746  11948  11194   -880   1091    -90       N  
ATOM   2193  CA  GLY A1316      11.479  -0.516 -10.457  1.00 97.80           C  
ANISOU 2193  CA  GLY A1316    12444  12747  11970   -919   1062    -76       C  
ATOM   2194  C   GLY A1316      12.968  -0.744 -10.307  1.00 98.05           C  
ANISOU 2194  C   GLY A1316    12507  12715  12033   -831   1061    -58       C  
ATOM   2195  O   GLY A1316      13.636  -1.147 -11.263  1.00 97.53           O  
ANISOU 2195  O   GLY A1316    12439  12655  11962   -871   1096    -65       O  
ATOM   2196  N   ILE A1317      13.509  -0.501  -9.109  1.00 90.04           N  
ANISOU 2196  N   ILE A1317    11520  11644  11046   -711   1023    -34       N  
ATOM   2197  CA  ILE A1317      14.912  -0.820  -8.872  1.00 82.12           C  
ANISOU 2197  CA  ILE A1317    10552  10587  10065   -622   1031    -17       C  
ATOM   2198  C   ILE A1317      15.128  -2.321  -8.957  1.00 86.25           C  
ANISOU 2198  C   ILE A1317    11177  11042  10551   -632   1162    -49       C  
ATOM   2199  O   ILE A1317      16.109  -2.791  -9.547  1.00 86.78           O  
ANISOU 2199  O   ILE A1317    11260  11093  10620   -620   1198    -48       O  
ATOM   2200  CB  ILE A1317      15.376  -0.269  -7.515  1.00 78.62           C  
ANISOU 2200  CB  ILE A1317    10116  10105   9652   -496    966     15       C  
ATOM   2201  CG1 ILE A1317      15.313   1.253  -7.501  1.00 69.01           C  
ANISOU 2201  CG1 ILE A1317     8802   8948   8470   -486    838     48       C  
ATOM   2202  CG2 ILE A1317      16.784  -0.760  -7.203  1.00 79.42           C  
ANISOU 2202  CG2 ILE A1317    10258  10154   9763   -402    989     32       C  
ATOM   2203  CD1 ILE A1317      15.968   1.838  -6.314  1.00 65.40           C  
ANISOU 2203  CD1 ILE A1317     8348   8459   8043   -371    774     81       C  
ATOM   2204  N   LEU A1318      14.207  -3.102  -8.390  1.00 85.66           N  
ANISOU 2204  N   LEU A1318    11178  10929  10441   -655   1240    -80       N  
ATOM   2205  CA  LEU A1318      14.431  -4.541  -8.358  1.00 90.30           C  
ANISOU 2205  CA  LEU A1318    11880  11440  10992   -656   1369   -109       C  
ATOM   2206  C   LEU A1318      14.240  -5.178  -9.727  1.00100.15           C  
ANISOU 2206  C   LEU A1318    13133  12714  12205   -779   1447   -143       C  
ATOM   2207  O   LEU A1318      14.961  -6.124 -10.059  1.00109.71           O  
ANISOU 2207  O   LEU A1318    14413  13871  13402   -766   1532   -156       O  
ATOM   2208  CB  LEU A1318      13.533  -5.188  -7.310  1.00 87.47           C  
ANISOU 2208  CB  LEU A1318    11607  11027  10601   -648   1430   -132       C  
ATOM   2209  CG  LEU A1318      14.009  -4.850  -5.882  1.00 80.11           C  
ANISOU 2209  CG  LEU A1318    10692  10046   9700   -510   1376    -99       C  
ATOM   2210  CD1 LEU A1318      12.947  -5.135  -4.857  1.00 84.23           C  
ANISOU 2210  CD1 LEU A1318    11268  10539  10196   -513   1403   -119       C  
ATOM   2211  CD2 LEU A1318      15.305  -5.582  -5.540  1.00 75.25           C  
ANISOU 2211  CD2 LEU A1318    10146   9355   9093   -405   1425    -82       C  
ATOM   2212  N   ARG A1319      13.324  -4.660 -10.553  1.00 99.46           N  
ANISOU 2212  N   ARG A1319    12973  12714  12104   -895   1419   -156       N  
ATOM   2213  CA  ARG A1319      13.030  -5.295 -11.835  1.00 96.49           C  
ANISOU 2213  CA  ARG A1319    12601  12371  11688  -1025   1498   -191       C  
ATOM   2214  C   ARG A1319      13.999  -4.898 -12.946  1.00 99.81           C  
ANISOU 2214  C   ARG A1319    12953  12833  12138  -1041   1459   -174       C  
ATOM   2215  O   ARG A1319      14.118  -5.626 -13.937  1.00100.27           O  
ANISOU 2215  O   ARG A1319    13036  12894  12167  -1126   1540   -203       O  
ATOM   2216  CB  ARG A1319      11.584  -4.990 -12.270  1.00 97.98           C  
ANISOU 2216  CB  ARG A1319    12741  12647  11841  -1150   1494   -212       C  
ATOM   2217  CG  ARG A1319      11.284  -3.538 -12.650  1.00105.29           C  
ANISOU 2217  CG  ARG A1319    13533  13674  12801  -1166   1363   -179       C  
ATOM   2218  CD  ARG A1319      10.025  -3.418 -13.534  1.00117.83           C  
ANISOU 2218  CD  ARG A1319    15065  15364  14343  -1311   1379   -201       C  
ATOM   2219  NE  ARG A1319      10.102  -4.279 -14.723  1.00128.39           N  
ANISOU 2219  NE  ARG A1319    16425  16717  15641  -1427   1474   -235       N  
ATOM   2220  CZ  ARG A1319       9.323  -4.174 -15.801  1.00128.89           C  
ANISOU 2220  CZ  ARG A1319    16426  16879  15667  -1564   1488   -251       C  
ATOM   2221  NH1 ARG A1319       8.395  -3.230 -15.874  1.00125.34           N  
ANISOU 2221  NH1 ARG A1319    15884  16525  15213  -1597   1411   -233       N  
ATOM   2222  NH2 ARG A1319       9.476  -5.016 -16.816  1.00131.48           N  
ANISOU 2222  NH2 ARG A1319    16784  17214  15959  -1666   1581   -283       N  
ATOM   2223  N   ASN A1320      14.699  -3.777 -12.801  1.00100.94           N  
ANISOU 2223  N   ASN A1320    13014  13006  12332   -967   1340   -131       N  
ATOM   2224  CA  ASN A1320      15.619  -3.283 -13.814  1.00102.86           C  
ANISOU 2224  CA  ASN A1320    13185  13295  12601   -982   1290   -114       C  
ATOM   2225  C   ASN A1320      16.979  -3.952 -13.664  1.00107.52           C  
ANISOU 2225  C   ASN A1320    13833  13817  13202   -892   1334   -108       C  
ATOM   2226  O   ASN A1320      17.597  -3.880 -12.598  1.00112.63           O  
ANISOU 2226  O   ASN A1320    14511  14413  13869   -767   1308    -83       O  
ATOM   2227  CB  ASN A1320      15.770  -1.768 -13.693  1.00103.81           C  
ANISOU 2227  CB  ASN A1320    13199  13477  12766   -945   1144    -70       C  
ATOM   2228  CG  ASN A1320      16.478  -1.154 -14.885  1.00104.01           C  
ANISOU 2228  CG  ASN A1320    13140  13569  12811   -991   1087    -56       C  
ATOM   2229  OD1 ASN A1320      17.697  -1.286 -15.046  1.00 96.10           O  
ANISOU 2229  OD1 ASN A1320    12142  12546  11824   -937   1083    -45       O  
ATOM   2230  ND2 ASN A1320      15.713  -0.468 -15.728  1.00106.56           N  
ANISOU 2230  ND2 ASN A1320    13383  13977  13130  -1092   1041    -55       N  
ATOM   2231  N   ALA A1321      17.462  -4.562 -14.747  1.00106.47           N  
ANISOU 2231  N   ALA A1321    13709  13692  13054   -954   1396   -129       N  
ATOM   2232  CA  ALA A1321      18.692  -5.344 -14.704  1.00104.67           C  
ANISOU 2232  CA  ALA A1321    13543  13401  12827   -873   1456   -128       C  
ATOM   2233  C   ALA A1321      19.955  -4.498 -14.552  1.00 94.27           C  
ANISOU 2233  C   ALA A1321    12158  12109  11550   -774   1353    -85       C  
ATOM   2234  O   ALA A1321      21.025  -5.062 -14.303  1.00 91.23           O  
ANISOU 2234  O   ALA A1321    11819  11677  11166   -683   1391    -76       O  
ATOM   2235  CB  ALA A1321      18.793  -6.203 -15.966  1.00113.35           C  
ANISOU 2235  CB  ALA A1321    14667  14505  13896   -977   1553   -166       C  
ATOM   2236  N   LYS A1322      19.878  -3.180 -14.721  1.00 85.57           N  
ANISOU 2236  N   LYS A1322    10951  11083  10479   -791   1228    -57       N  
ATOM   2237  CA  LYS A1322      21.038  -2.338 -14.457  1.00 86.25           C  
ANISOU 2237  CA  LYS A1322    10980  11194  10597   -699   1129    -17       C  
ATOM   2238  C   LYS A1322      21.043  -1.809 -13.027  1.00 90.16           C  
ANISOU 2238  C   LYS A1322    11486  11659  11111   -587   1069     14       C  
ATOM   2239  O   LYS A1322      22.106  -1.659 -12.415  1.00 92.66           O  
ANISOU 2239  O   LYS A1322    11805  11962  11441   -480   1036     42       O  
ATOM   2240  CB  LYS A1322      21.081  -1.159 -15.433  1.00 90.08           C  
ANISOU 2240  CB  LYS A1322    11351  11774  11102   -776   1024     -2       C  
ATOM   2241  CG  LYS A1322      21.480  -1.505 -16.853  1.00 99.28           C  
ANISOU 2241  CG  LYS A1322    12486  12980  12255   -869   1060    -24       C  
ATOM   2242  CD  LYS A1322      21.854  -0.252 -17.644  1.00104.35           C  
ANISOU 2242  CD  LYS A1322    13016  13712  12920   -915    942      0       C  
ATOM   2243  CE  LYS A1322      23.223   0.275 -17.223  1.00103.63           C  
ANISOU 2243  CE  LYS A1322    12899  13628  12847   -809    870     32       C  
ATOM   2244  NZ  LYS A1322      23.605   1.498 -17.978  1.00101.12           N  
ANISOU 2244  NZ  LYS A1322    12480  13395  12546   -859    755     54       N  
ATOM   2245  N   LEU A1323      19.863  -1.526 -12.484  1.00 89.29           N  
ANISOU 2245  N   LEU A1323    11381  11544  11000   -614   1056      9       N  
ATOM   2246  CA  LEU A1323      19.767  -0.956 -11.150  1.00 88.93           C  
ANISOU 2246  CA  LEU A1323    11342  11475  10974   -519    996     36       C  
ATOM   2247  C   LEU A1323      19.890  -2.009 -10.050  1.00 96.27           C  
ANISOU 2247  C   LEU A1323    12376  12314  11886   -430   1082     30       C  
ATOM   2248  O   LEU A1323      20.499  -1.734  -9.009  1.00 99.60           O  
ANISOU 2248  O   LEU A1323    12807  12712  12324   -319   1041     59       O  
ATOM   2249  CB  LEU A1323      18.448  -0.198 -11.013  1.00 81.58           C  
ANISOU 2249  CB  LEU A1323    10370  10579  10046   -580    945     34       C  
ATOM   2250  CG  LEU A1323      18.360   1.101 -11.802  1.00 74.80           C  
ANISOU 2250  CG  LEU A1323     9405   9806   9210   -638    837     54       C  
ATOM   2251  CD1 LEU A1323      17.004   1.743 -11.628  1.00 66.31           C  
ANISOU 2251  CD1 LEU A1323     8298   8764   8135   -689    799     53       C  
ATOM   2252  CD2 LEU A1323      19.444   2.042 -11.346  1.00 78.40           C  
ANISOU 2252  CD2 LEU A1323     9819  10274   9696   -551    739     94       C  
ATOM   2253  N   LYS A1324      19.333  -3.207 -10.248  1.00 92.96           N  
ANISOU 2253  N   LYS A1324    12040  11846  11433   -476   1200     -8       N  
ATOM   2254  CA  LYS A1324      19.323  -4.182  -9.158  1.00100.05           C  
ANISOU 2254  CA  LYS A1324    13045  12655  12313   -395   1282    -14       C  
ATOM   2255  C   LYS A1324      20.722  -4.570  -8.696  1.00101.20           C  
ANISOU 2255  C   LYS A1324    13224  12762  12466   -269   1296     13       C  
ATOM   2256  O   LYS A1324      20.953  -4.601  -7.475  1.00107.00           O  
ANISOU 2256  O   LYS A1324    13994  13456  13207   -165   1285     36       O  
ATOM   2257  CB  LYS A1324      18.512  -5.421  -9.544  1.00104.11           C  
ANISOU 2257  CB  LYS A1324    13652  13123  12783   -478   1413    -61       C  
ATOM   2258  CG  LYS A1324      18.383  -6.403  -8.381  1.00107.86           C  
ANISOU 2258  CG  LYS A1324    14244  13502  13235   -401   1497    -68       C  
ATOM   2259  CD  LYS A1324      17.792  -7.737  -8.789  1.00113.58           C  
ANISOU 2259  CD  LYS A1324    15076  14169  13909   -477   1639   -115       C  
ATOM   2260  CE  LYS A1324      17.671  -8.662  -7.586  1.00110.74           C  
ANISOU 2260  CE  LYS A1324    14837  13712  13527   -397   1718   -119       C  
ATOM   2261  NZ  LYS A1324      18.997  -8.981  -6.976  1.00105.97           N  
ANISOU 2261  NZ  LYS A1324    14269  13055  12938   -249   1726    -83       N  
ATOM   2262  N   PRO A1325      21.681  -4.880  -9.575  1.00 91.53           N  
ANISOU 2262  N   PRO A1325    11987  11552  11237   -269   1321     13       N  
ATOM   2263  CA  PRO A1325      23.052  -5.149  -9.095  1.00 86.56           C  
ANISOU 2263  CA  PRO A1325    11376  10901  10610   -139   1325     44       C  
ATOM   2264  C   PRO A1325      23.620  -4.064  -8.193  1.00 89.60           C  
ANISOU 2264  C   PRO A1325    11696  11324  11023    -49   1208     89       C  
ATOM   2265  O   PRO A1325      24.200  -4.371  -7.149  1.00 97.27           O  
ANISOU 2265  O   PRO A1325    12710  12257  11991     68   1221    114       O  
ATOM   2266  CB  PRO A1325      23.848  -5.271 -10.404  1.00 90.75           C  
ANISOU 2266  CB  PRO A1325    11868  11475  11138   -183   1338     35       C  
ATOM   2267  CG  PRO A1325      22.864  -5.729 -11.402  1.00 88.64           C  
ANISOU 2267  CG  PRO A1325    11620  11207  10852   -322   1404    -10       C  
ATOM   2268  CD  PRO A1325      21.556  -5.093 -11.026  1.00 85.05           C  
ANISOU 2268  CD  PRO A1325    11141  10770  10405   -386   1356    -16       C  
ATOM   2269  N   VAL A1326      23.487  -2.796  -8.589  1.00 91.75           N  
ANISOU 2269  N   VAL A1326    11867  11673  11320   -103   1096    101       N  
ATOM   2270  CA  VAL A1326      23.971  -1.682  -7.776  1.00 87.82           C  
ANISOU 2270  CA  VAL A1326    11309  11213  10844    -33    985    141       C  
ATOM   2271  C   VAL A1326      23.264  -1.670  -6.432  1.00 81.06           C  
ANISOU 2271  C   VAL A1326    10498  10308   9993     19    984    148       C  
ATOM   2272  O   VAL A1326      23.890  -1.491  -5.384  1.00 79.65           O  
ANISOU 2272  O   VAL A1326    10325  10119   9818    123    954    179       O  
ATOM   2273  CB  VAL A1326      23.766  -0.345  -8.520  1.00 83.63           C  
ANISOU 2273  CB  VAL A1326    10675  10765  10337   -116    874    148       C  
ATOM   2274  CG1 VAL A1326      24.384   0.816  -7.732  1.00 79.26           C  
ANISOU 2274  CG1 VAL A1326    10065  10250   9801    -46    762    188       C  
ATOM   2275  CG2 VAL A1326      24.319  -0.414  -9.940  1.00 76.02           C  
ANISOU 2275  CG2 VAL A1326     9668   9851   9366   -185    880    136       C  
ATOM   2276  N   TYR A1327      21.947  -1.862  -6.450  1.00 81.58           N  
ANISOU 2276  N   TYR A1327    10593  10350  10055    -56   1017    118       N  
ATOM   2277  CA  TYR A1327      21.141  -1.784  -5.237  1.00 75.77           C  
ANISOU 2277  CA  TYR A1327     9894   9574   9322    -21   1012    120       C  
ATOM   2278  C   TYR A1327      21.624  -2.775  -4.186  1.00 85.68           C  
ANISOU 2278  C   TYR A1327    11240  10755  10561     87   1085    129       C  
ATOM   2279  O   TYR A1327      21.848  -2.411  -3.023  1.00 87.46           O  
ANISOU 2279  O   TYR A1327    11466  10969  10797    172   1042    156       O  
ATOM   2280  CB  TYR A1327      19.682  -2.051  -5.593  1.00 69.20           C  
ANISOU 2280  CB  TYR A1327     9084   8734   8476   -128   1055     81       C  
ATOM   2281  CG  TYR A1327      18.707  -1.778  -4.490  1.00 68.01           C  
ANISOU 2281  CG  TYR A1327     8952   8560   8328   -112   1034     79       C  
ATOM   2282  CD1 TYR A1327      18.405  -0.475  -4.121  1.00 65.76           C  
ANISOU 2282  CD1 TYR A1327     8592   8322   8072   -109    924    100       C  
ATOM   2283  CD2 TYR A1327      18.077  -2.822  -3.811  1.00 69.31           C  
ANISOU 2283  CD2 TYR A1327     9214   8655   8465   -102   1126     55       C  
ATOM   2284  CE1 TYR A1327      17.496  -0.209  -3.091  1.00 73.49           C  
ANISOU 2284  CE1 TYR A1327     9586   9282   9053    -93    905     97       C  
ATOM   2285  CE2 TYR A1327      17.174  -2.568  -2.800  1.00 68.27           C  
ANISOU 2285  CE2 TYR A1327     9097   8508   8335    -92   1106     50       C  
ATOM   2286  CZ  TYR A1327      16.884  -1.262  -2.450  1.00 69.44           C  
ANISOU 2286  CZ  TYR A1327     9163   8706   8513    -86    995     71       C  
ATOM   2287  OH  TYR A1327      15.983  -1.000  -1.453  1.00 88.00           O  
ANISOU 2287  OH  TYR A1327    11527  11044  10865    -75    975     66       O  
ATOM   2288  N   ASP A1328      21.782  -4.039  -4.585  1.00 89.80           N  
ANISOU 2288  N   ASP A1328    11841  11225  11055     85   1199    107       N  
ATOM   2289  CA  ASP A1328      22.231  -5.075  -3.663  1.00 87.62           C  
ANISOU 2289  CA  ASP A1328    11661  10871  10758    189   1280    117       C  
ATOM   2290  C   ASP A1328      23.590  -4.737  -3.072  1.00 91.26           C  
ANISOU 2290  C   ASP A1328    12089  11357  11230    313   1229    164       C  
ATOM   2291  O   ASP A1328      23.845  -5.021  -1.899  1.00107.94           O  
ANISOU 2291  O   ASP A1328    14245  13431  13338    412   1242    187       O  
ATOM   2292  CB  ASP A1328      22.271  -6.431  -4.370  1.00 89.46           C  
ANISOU 2292  CB  ASP A1328    11985  11048  10959    162   1412     86       C  
ATOM   2293  CG  ASP A1328      20.922  -6.806  -4.991  1.00104.67           C  
ANISOU 2293  CG  ASP A1328    13946  12959  12865     27   1469     36       C  
ATOM   2294  OD1 ASP A1328      19.870  -6.458  -4.415  1.00109.78           O  
ANISOU 2294  OD1 ASP A1328    14592  13606  13515    -10   1442     25       O  
ATOM   2295  OD2 ASP A1328      20.914  -7.453  -6.062  1.00112.47           O  
ANISOU 2295  OD2 ASP A1328    14961  13941  13833    -44   1542      7       O  
ATOM   2296  N   SER A1329      24.464  -4.104  -3.845  1.00 86.91           N  
ANISOU 2296  N   SER A1329    11456  10877  10689    307   1168    180       N  
ATOM   2297  CA  SER A1329      25.770  -3.727  -3.323  1.00 94.29           C  
ANISOU 2297  CA  SER A1329    12351  11851  11626    416   1116    225       C  
ATOM   2298  C   SER A1329      25.700  -2.547  -2.362  1.00 97.62           C  
ANISOU 2298  C   SER A1329    12712  12311  12069    445   1007    253       C  
ATOM   2299  O   SER A1329      26.687  -2.271  -1.672  1.00101.62           O  
ANISOU 2299  O   SER A1329    13193  12847  12570    540    969    292       O  
ATOM   2300  CB  SER A1329      26.742  -3.418  -4.482  1.00 89.82           C  
ANISOU 2300  CB  SER A1329    11716  11356  11058    393   1085    230       C  
ATOM   2301  OG  SER A1329      26.564  -2.121  -5.021  1.00 80.10           O  
ANISOU 2301  OG  SER A1329    10386  10199   9849    314    976    232       O  
ATOM   2302  N   LEU A1330      24.560  -1.866  -2.286  1.00 97.56           N  
ANISOU 2302  N   LEU A1330    12682  12306  12081    368    961    236       N  
ATOM   2303  CA  LEU A1330      24.426  -0.658  -1.492  1.00 82.57           C  
ANISOU 2303  CA  LEU A1330    10726  10444  10204    383    856    259       C  
ATOM   2304  C   LEU A1330      24.016  -0.981  -0.059  1.00 90.53           C  
ANISOU 2304  C   LEU A1330    11792  11396  11210    453    879    267       C  
ATOM   2305  O   LEU A1330      23.315  -1.962   0.209  1.00 94.74           O  
ANISOU 2305  O   LEU A1330    12408  11860  11730    449    966    244       O  
ATOM   2306  CB  LEU A1330      23.404   0.288  -2.125  1.00 71.78           C  
ANISOU 2306  CB  LEU A1330     9303   9111   8859    272    792    239       C  
ATOM   2307  CG  LEU A1330      23.899   1.037  -3.363  1.00 75.31           C  
ANISOU 2307  CG  LEU A1330     9669   9631   9313    208    732    242       C  
ATOM   2308  CD1 LEU A1330      22.822   1.973  -3.934  1.00 72.85           C  
ANISOU 2308  CD1 LEU A1330     9307   9352   9022    105    670    227       C  
ATOM   2309  CD2 LEU A1330      25.173   1.805  -3.045  1.00 77.73           C  
ANISOU 2309  CD2 LEU A1330     9921   9994   9621    274    654    281       C  
ATOM   2310  N   ASP A1331      24.490  -0.146   0.861  1.00 84.74           N  
ANISOU 2310  N   ASP A1331    11016  10694  10486    513    802    301       N  
ATOM   2311  CA  ASP A1331      24.030  -0.094   2.234  1.00 69.87           C  
ANISOU 2311  CA  ASP A1331     9166   8774   8608    564    796    310       C  
ATOM   2312  C   ASP A1331      22.738   0.705   2.311  1.00 76.43           C  
ANISOU 2312  C   ASP A1331     9973   9606   9462    484    745    287       C  
ATOM   2313  O   ASP A1331      22.470   1.564   1.470  1.00 82.40           O  
ANISOU 2313  O   ASP A1331    10667  10408  10234    409    685    280       O  
ATOM   2314  CB  ASP A1331      25.092   0.545   3.126  1.00 68.85           C  
ANISOU 2314  CB  ASP A1331     8994   8689   8477    651    731    354       C  
ATOM   2315  CG  ASP A1331      25.440   1.951   2.687  1.00 77.95           C  
ANISOU 2315  CG  ASP A1331    10052   9920   9644    607    621    368       C  
ATOM   2316  OD1 ASP A1331      24.566   2.835   2.753  1.00 80.70           O  
ANISOU 2316  OD1 ASP A1331    10373  10273  10015    547    563    356       O  
ATOM   2317  OD2 ASP A1331      26.588   2.177   2.256  1.00 88.05           O  
ANISOU 2317  OD2 ASP A1331    11288  11258  10909    632    594    390       O  
ATOM   2318  N   ALA A1332      21.966   0.453   3.377  1.00 79.29           N  
ANISOU 2318  N   ALA A1332    10382   9918   9824    507    766    279       N  
ATOM   2319  CA  ALA A1332      20.589   0.932   3.454  1.00 71.83           C  
ANISOU 2319  CA  ALA A1332     9431   8967   8894    433    742    252       C  
ATOM   2320  C   ALA A1332      20.476   2.440   3.271  1.00 66.38           C  
ANISOU 2320  C   ALA A1332     8653   8337   8231    397    630    264       C  
ATOM   2321  O   ALA A1332      19.481   2.932   2.732  1.00 71.84           O  
ANISOU 2321  O   ALA A1332     9318   9044   8932    318    605    242       O  
ATOM   2322  CB  ALA A1332      19.969   0.523   4.790  1.00 83.71           C  
ANISOU 2322  CB  ALA A1332    10994  10417  10394    477    772    246       C  
ATOM   2323  N   VAL A1333      21.457   3.201   3.742  1.00 62.13           N  
ANISOU 2323  N   VAL A1333     8072   7836   7701    453    563    300       N  
ATOM   2324  CA  VAL A1333      21.363   4.644   3.554  1.00 62.36           C  
ANISOU 2324  CA  VAL A1333     8027   7915   7750    415    460    310       C  
ATOM   2325  C   VAL A1333      21.537   4.995   2.076  1.00 67.88           C  
ANISOU 2325  C   VAL A1333     8679   8661   8453    342    437    304       C  
ATOM   2326  O   VAL A1333      20.823   5.850   1.535  1.00 68.75           O  
ANISOU 2326  O   VAL A1333     8747   8795   8578    275    385    296       O  
ATOM   2327  CB  VAL A1333      22.383   5.367   4.454  1.00 63.61           C  
ANISOU 2327  CB  VAL A1333     8157   8104   7909    484    398    348       C  
ATOM   2328  CG1 VAL A1333      22.178   6.859   4.403  1.00 70.47           C  
ANISOU 2328  CG1 VAL A1333     8966   9012   8798    445    299    357       C  
ATOM   2329  CG2 VAL A1333      22.266   4.895   5.874  1.00 62.25           C  
ANISOU 2329  CG2 VAL A1333     8032   7888   7732    556    430    355       C  
ATOM   2330  N   ARG A1334      22.456   4.319   1.392  1.00 60.80           N  
ANISOU 2330  N   ARG A1334     7786   7775   7538    354    478    309       N  
ATOM   2331  CA  ARG A1334      22.664   4.598  -0.026  1.00 71.22           C  
ANISOU 2331  CA  ARG A1334     9061   9141   8859    282    459    302       C  
ATOM   2332  C   ARG A1334      21.530   4.039  -0.871  1.00 76.71           C  
ANISOU 2332  C   ARG A1334     9777   9816   9554    198    514    264       C  
ATOM   2333  O   ARG A1334      21.089   4.691  -1.824  1.00 75.23           O  
ANISOU 2333  O   ARG A1334     9540   9667   9376    119    473    256       O  
ATOM   2334  CB  ARG A1334      24.022   4.054  -0.480  1.00 71.44           C  
ANISOU 2334  CB  ARG A1334     9085   9194   8866    323    486    317       C  
ATOM   2335  CG  ARG A1334      25.178   4.800   0.191  1.00 68.52           C  
ANISOU 2335  CG  ARG A1334     8676   8869   8489    389    417    355       C  
ATOM   2336  CD  ARG A1334      26.541   4.476  -0.394  1.00 68.63           C  
ANISOU 2336  CD  ARG A1334     8668   8931   8479    420    427    371       C  
ATOM   2337  NE  ARG A1334      27.544   5.440   0.054  1.00 71.39           N  
ANISOU 2337  NE  ARG A1334     8965   9345   8817    454    346    404       N  
ATOM   2338  CZ  ARG A1334      28.373   5.250   1.083  1.00 76.69           C  
ANISOU 2338  CZ  ARG A1334     9645  10029   9467    546    351    433       C  
ATOM   2339  NH1 ARG A1334      28.330   4.115   1.773  1.00 69.36           N  
ANISOU 2339  NH1 ARG A1334     8778   9047   8529    619    434    434       N  
ATOM   2340  NH2 ARG A1334      29.258   6.193   1.410  1.00 64.29           N  
ANISOU 2340  NH2 ARG A1334     8022   8528   7880    562    275    460       N  
ATOM   2341  N   ARG A1335      21.053   2.837  -0.536  1.00 61.05           N  
ANISOU 2341  N   ARG A1335     7868   7774   7555    213    609    242       N  
ATOM   2342  CA  ARG A1335      19.815   2.324  -1.112  1.00 63.92           C  
ANISOU 2342  CA  ARG A1335     8258   8120   7911    129    664    205       C  
ATOM   2343  C   ARG A1335      18.739   3.394  -1.152  1.00 65.91           C  
ANISOU 2343  C   ARG A1335     8459   8403   8180     71    594    199       C  
ATOM   2344  O   ARG A1335      17.952   3.469  -2.101  1.00 73.60           O  
ANISOU 2344  O   ARG A1335     9410   9405   9150    -18    601    178       O  
ATOM   2345  CB  ARG A1335      19.291   1.136  -0.308  1.00 65.04           C  
ANISOU 2345  CB  ARG A1335     8491   8190   8032    160    759    184       C  
ATOM   2346  CG  ARG A1335      20.162  -0.077  -0.352  1.00 76.36           C  
ANISOU 2346  CG  ARG A1335     9988   9581   9442    213    847    186       C  
ATOM   2347  CD  ARG A1335      19.426  -1.310   0.145  1.00 78.59           C  
ANISOU 2347  CD  ARG A1335    10371   9791   9699    214    952    157       C  
ATOM   2348  NE  ARG A1335      20.070  -2.515  -0.371  1.00 84.58           N  
ANISOU 2348  NE  ARG A1335    11193  10511  10432    232   1050    149       N  
ATOM   2349  CZ  ARG A1335      19.607  -3.746  -0.210  1.00 92.45           C  
ANISOU 2349  CZ  ARG A1335    12289  11440  11399    225   1160    122       C  
ATOM   2350  NH1 ARG A1335      18.480  -3.943   0.461  1.00100.07           N  
ANISOU 2350  NH1 ARG A1335    13297  12372  12353    196   1182     99       N  
ATOM   2351  NH2 ARG A1335      20.276  -4.775  -0.723  1.00 95.12           N  
ANISOU 2351  NH2 ARG A1335    12685  11741  11714    246   1247    117       N  
ATOM   2352  N   ALA A1336      18.663   4.214  -0.116  1.00 63.03           N  
ANISOU 2352  N   ALA A1336     8079   8037   7833    120    529    219       N  
ATOM   2353  CA  ALA A1336      17.600   5.207  -0.077  1.00 64.95           C  
ANISOU 2353  CA  ALA A1336     8282   8305   8092     76    468    214       C  
ATOM   2354  C   ALA A1336      17.926   6.367  -0.994  1.00 65.62           C  
ANISOU 2354  C   ALA A1336     8290   8450   8193     34    383    233       C  
ATOM   2355  O   ALA A1336      17.019   7.045  -1.487  1.00 67.46           O  
ANISOU 2355  O   ALA A1336     8485   8714   8434    -25    346    227       O  
ATOM   2356  CB  ALA A1336      17.361   5.693   1.365  1.00 55.99           C  
ANISOU 2356  CB  ALA A1336     7160   7144   6970    141    431    226       C  
ATOM   2357  N   ALA A1337      19.212   6.609  -1.230  1.00 56.67           N  
ANISOU 2357  N   ALA A1337     7135   7337   7061     64    353    257       N  
ATOM   2358  CA  ALA A1337      19.578   7.624  -2.197  1.00 56.37           C  
ANISOU 2358  CA  ALA A1337     7030   7356   7033     16    278    272       C  
ATOM   2359  C   ALA A1337      19.242   7.157  -3.612  1.00 57.18           C  
ANISOU 2359  C   ALA A1337     7115   7485   7125    -71    316    251       C  
ATOM   2360  O   ALA A1337      18.697   7.930  -4.404  1.00 56.82           O  
ANISOU 2360  O   ALA A1337     7020   7480   7087   -137    268    252       O  
ATOM   2361  CB  ALA A1337      21.053   7.981  -2.049  1.00 56.66           C  
ANISOU 2361  CB  ALA A1337     7047   7415   7065     66    237    301       C  
ATOM   2362  N   LEU A1338      19.507   5.882  -3.922  1.00 62.38           N  
ANISOU 2362  N   LEU A1338     7818   8121   7765    -73    407    232       N  
ATOM   2363  CA  LEU A1338      19.119   5.332  -5.220  1.00 65.98           C  
ANISOU 2363  CA  LEU A1338     8264   8598   8207   -163    456    207       C  
ATOM   2364  C   LEU A1338      17.607   5.374  -5.402  1.00 69.45           C  
ANISOU 2364  C   LEU A1338     8701   9045   8642   -231    471    184       C  
ATOM   2365  O   LEU A1338      17.128   5.755  -6.480  1.00 69.62           O  
ANISOU 2365  O   LEU A1338     8674   9117   8663   -315    451    179       O  
ATOM   2366  CB  LEU A1338      19.636   3.897  -5.397  1.00 63.78           C  
ANISOU 2366  CB  LEU A1338     8048   8282   7906   -147    560    188       C  
ATOM   2367  CG  LEU A1338      19.546   3.365  -6.839  1.00 68.19           C  
ANISOU 2367  CG  LEU A1338     8592   8868   8449   -240    609    164       C  
ATOM   2368  CD1 LEU A1338      20.303   4.289  -7.771  1.00 61.87           C  
ANISOU 2368  CD1 LEU A1338     7715   8133   7661   -272    529    184       C  
ATOM   2369  CD2 LEU A1338      20.026   1.897  -7.017  1.00 64.19           C  
ANISOU 2369  CD2 LEU A1338     8158   8315   7917   -224    723    143       C  
ATOM   2370  N   ILE A1339      16.842   5.011  -4.357  1.00 58.91           N  
ANISOU 2370  N   ILE A1339     7414   7667   7302   -197    504    172       N  
ATOM   2371  CA  ILE A1339      15.382   5.120  -4.414  1.00 60.42           C  
ANISOU 2371  CA  ILE A1339     7598   7874   7484   -257    514    151       C  
ATOM   2372  C   ILE A1339      14.959   6.569  -4.575  1.00 58.95           C  
ANISOU 2372  C   ILE A1339     7340   7738   7321   -272    411    174       C  
ATOM   2373  O   ILE A1339      14.033   6.877  -5.332  1.00 63.65           O  
ANISOU 2373  O   ILE A1339     7895   8382   7908   -346    402    166       O  
ATOM   2374  CB  ILE A1339      14.727   4.507  -3.160  1.00 68.47           C  
ANISOU 2374  CB  ILE A1339     8683   8840   8493   -212    562    134       C  
ATOM   2375  CG1 ILE A1339      14.958   3.002  -3.090  1.00 68.19           C  
ANISOU 2375  CG1 ILE A1339     8729   8752   8429   -208    675    108       C  
ATOM   2376  CG2 ILE A1339      13.233   4.819  -3.143  1.00 58.72           C  
ANISOU 2376  CG2 ILE A1339     7429   7637   7247   -267    556    116       C  
ATOM   2377  CD1 ILE A1339      14.858   2.497  -1.726  1.00 60.34           C  
ANISOU 2377  CD1 ILE A1339     7801   7696   7430   -134    708    105       C  
ATOM   2378  N   ASN A1340      15.604   7.480  -3.848  1.00 59.30           N  
ANISOU 2378  N   ASN A1340     7369   7773   7390   -203    336    204       N  
ATOM   2379  CA  ASN A1340      15.274   8.895  -3.993  1.00 63.27           C  
ANISOU 2379  CA  ASN A1340     7812   8314   7913   -213    241    228       C  
ATOM   2380  C   ASN A1340      15.372   9.326  -5.454  1.00 67.82           C  
ANISOU 2380  C   ASN A1340     8330   8950   8488   -291    211    235       C  
ATOM   2381  O   ASN A1340      14.481  10.006  -5.978  1.00 69.35           O  
ANISOU 2381  O   ASN A1340     8481   9186   8683   -339    175    239       O  
ATOM   2382  CB  ASN A1340      16.196   9.731  -3.102  1.00 54.86           C  
ANISOU 2382  CB  ASN A1340     6746   7229   6868   -135    172    258       C  
ATOM   2383  CG  ASN A1340      15.669  11.134  -2.873  1.00 65.42           C  
ANISOU 2383  CG  ASN A1340     8046   8586   8225   -130     86    279       C  
ATOM   2384  OD1 ASN A1340      15.286  11.828  -3.809  1.00 65.25           O  
ANISOU 2384  OD1 ASN A1340     7978   8608   8207   -185     44    287       O  
ATOM   2385  ND2 ASN A1340      15.615  11.551  -1.614  1.00 65.04           N  
ANISOU 2385  ND2 ASN A1340     8022   8503   8189    -64     60    287       N  
ATOM   2386  N   MET A1341      16.432   8.899  -6.122  1.00 66.00           N  
ANISOU 2386  N   MET A1341     8098   8726   8252   -304    228    236       N  
ATOM   2387  CA  MET A1341      16.630   9.298  -7.531  1.00 63.19           C  
ANISOU 2387  CA  MET A1341     7686   8429   7895   -382    199    242       C  
ATOM   2388  C   MET A1341      15.548   8.668  -8.400  1.00 66.98           C  
ANISOU 2388  C   MET A1341     8156   8940   8354   -470    258    215       C  
ATOM   2389  O   MET A1341      14.980   9.366  -9.227  1.00 61.30           O  
ANISOU 2389  O   MET A1341     7381   8276   7636   -531    216    225       O  
ATOM   2390  CB  MET A1341      17.986   8.801  -8.023  1.00 62.80           C  
ANISOU 2390  CB  MET A1341     7640   8380   7839   -376    217    244       C  
ATOM   2391  CG  MET A1341      19.135   9.562  -7.452  1.00 59.88           C  
ANISOU 2391  CG  MET A1341     7262   8006   7482   -310    148    273       C  
ATOM   2392  SD  MET A1341      20.645   9.067  -8.240  1.00 66.24           S  
ANISOU 2392  SD  MET A1341     8058   8837   8275   -316    164    274       S  
ATOM   2393  CE  MET A1341      20.601  10.128  -9.677  1.00 71.22           C  
ANISOU 2393  CE  MET A1341     8612   9539   8910   -412     87    287       C  
ATOM   2394  N   VAL A1342      15.275   7.390  -8.185  1.00 67.49           N  
ANISOU 2394  N   VAL A1342     8275   8970   8396   -476    356    184       N  
ATOM   2395  CA  VAL A1342      14.333   6.659  -9.023  1.00 60.21           C  
ANISOU 2395  CA  VAL A1342     7351   8080   7445   -570    425    154       C  
ATOM   2396  C   VAL A1342      12.934   7.183  -8.807  1.00 71.79           C  
ANISOU 2396  C   VAL A1342     8792   9580   8904   -595    403    152       C  
ATOM   2397  O   VAL A1342      12.091   7.143  -9.703  1.00 78.13           O  
ANISOU 2397  O   VAL A1342     9557  10443   9686   -682    420    141       O  
ATOM   2398  CB  VAL A1342      14.427   5.157  -8.719  1.00 61.25           C  
ANISOU 2398  CB  VAL A1342     7563   8158   7551   -565    539    120       C  
ATOM   2399  CG1 VAL A1342      13.277   4.402  -9.331  1.00 62.64           C  
ANISOU 2399  CG1 VAL A1342     7749   8362   7689   -662    616     84       C  
ATOM   2400  CG2 VAL A1342      15.763   4.603  -9.150  1.00 61.81           C  
ANISOU 2400  CG2 VAL A1342     7652   8207   7624   -547    567    121       C  
ATOM   2401  N   PHE A1343      12.679   7.718  -7.625  1.00 75.10           N  
ANISOU 2401  N   PHE A1343     9226   9968   9340   -520    363    165       N  
ATOM   2402  CA  PHE A1343      11.386   8.310  -7.336  1.00 70.61           C  
ANISOU 2402  CA  PHE A1343     8631   9433   8766   -530    336    166       C  
ATOM   2403  C   PHE A1343      11.179   9.603  -8.118  1.00 73.91           C  
ANISOU 2403  C   PHE A1343     8970   9914   9198   -559    248    198       C  
ATOM   2404  O   PHE A1343      10.048   9.925  -8.495  1.00 76.13           O  
ANISOU 2404  O   PHE A1343     9211  10252   9462   -604    240    197       O  
ATOM   2405  CB  PHE A1343      11.313   8.547  -5.841  1.00 58.02           C  
ANISOU 2405  CB  PHE A1343     7076   7783   7188   -437    316    171       C  
ATOM   2406  CG  PHE A1343      10.007   9.039  -5.359  1.00 58.12           C  
ANISOU 2406  CG  PHE A1343     7070   7822   7192   -436    296    168       C  
ATOM   2407  CD1 PHE A1343       9.650  10.370  -5.503  1.00 61.14           C  
ANISOU 2407  CD1 PHE A1343     7396   8242   7594   -424    209    198       C  
ATOM   2408  CD2 PHE A1343       9.153   8.184  -4.687  1.00 59.45           C  
ANISOU 2408  CD2 PHE A1343     7282   7973   7331   -441    364    135       C  
ATOM   2409  CE1 PHE A1343       8.436  10.830  -5.009  1.00 61.52           C  
ANISOU 2409  CE1 PHE A1343     7427   8317   7633   -413    192    196       C  
ATOM   2410  CE2 PHE A1343       7.965   8.640  -4.194  1.00 63.37           C  
ANISOU 2410  CE2 PHE A1343     7760   8500   7818   -436    345    131       C  
ATOM   2411  CZ  PHE A1343       7.603   9.963  -4.357  1.00 61.34           C  
ANISOU 2411  CZ  PHE A1343     7442   8285   7581   -419    259    162       C  
ATOM   2412  N   GLN A1344      12.256  10.368  -8.345  1.00 71.92           N  
ANISOU 2412  N   GLN A1344     8697   9654   8974   -531    180    227       N  
ATOM   2413  CA  GLN A1344      12.153  11.664  -9.013  1.00 69.07           C  
ANISOU 2413  CA  GLN A1344     8272   9343   8627   -551     92    260       C  
ATOM   2414  C   GLN A1344      12.160  11.546 -10.536  1.00 68.41           C  
ANISOU 2414  C   GLN A1344     8138   9326   8529   -648    100    260       C  
ATOM   2415  O   GLN A1344      11.527  12.365 -11.214  1.00 67.97           O  
ANISOU 2415  O   GLN A1344     8026   9328   8471   -687     53    280       O  
ATOM   2416  CB  GLN A1344      13.299  12.584  -8.571  1.00 59.65           C  
ANISOU 2416  CB  GLN A1344     7083   8117   7464   -486     15    290       C  
ATOM   2417  CG  GLN A1344      13.312  13.952  -9.271  1.00 57.70           C  
ANISOU 2417  CG  GLN A1344     6782   7912   7230   -507    -76    326       C  
ATOM   2418  CD  GLN A1344      14.455  14.854  -8.842  1.00 66.48           C  
ANISOU 2418  CD  GLN A1344     7903   8992   8362   -454   -148    353       C  
ATOM   2419  OE1 GLN A1344      15.362  14.443  -8.109  1.00 74.96           O  
ANISOU 2419  OE1 GLN A1344     9017  10023   9440   -405   -132    346       O  
ATOM   2420  NE2 GLN A1344      14.412  16.094  -9.281  1.00 57.63           N  
ANISOU 2420  NE2 GLN A1344     6749   7896   7251   -465   -226    384       N  
ATOM   2421  N   MET A1345      12.861  10.551 -11.088  1.00 61.94           N  
ANISOU 2421  N   MET A1345     7338   8499   7698   -687    161    238       N  
ATOM   2422  CA  MET A1345      13.106  10.477 -12.523  1.00 74.09           C  
ANISOU 2422  CA  MET A1345     8829  10096   9226   -778    164    238       C  
ATOM   2423  C   MET A1345      12.630   9.189 -13.183  1.00 70.33           C  
ANISOU 2423  C   MET A1345     8366   9641   8714   -860    267    199       C  
ATOM   2424  O   MET A1345      12.692   9.093 -14.415  1.00 79.76           O  
ANISOU 2424  O   MET A1345     9517  10890   9896   -947    275    196       O  
ATOM   2425  CB  MET A1345      14.608  10.641 -12.817  1.00 75.44           C  
ANISOU 2425  CB  MET A1345     9000  10248   9414   -759    131    250       C  
ATOM   2426  CG  MET A1345      15.154  12.003 -12.497  1.00 74.34           C  
ANISOU 2426  CG  MET A1345     8839  10105   9301   -707     26    288       C  
ATOM   2427  SD  MET A1345      16.943  11.969 -12.541  1.00 85.86           S  
ANISOU 2427  SD  MET A1345    10312  11542  10770   -675      3    295       S  
ATOM   2428  CE  MET A1345      17.366  11.344 -10.913  1.00 87.53           C  
ANISOU 2428  CE  MET A1345    10599  11674  10986   -565     43    285       C  
ATOM   2429  N   GLY A1346      12.184   8.206 -12.413  1.00 64.03           N  
ANISOU 2429  N   GLY A1346     7630   8802   7899   -841    346    169       N  
ATOM   2430  CA  GLY A1346      11.722   6.938 -12.927  1.00 63.63           C  
ANISOU 2430  CA  GLY A1346     7607   8761   7808   -919    452    129       C  
ATOM   2431  C   GLY A1346      12.831   5.909 -13.043  1.00 63.94           C  
ANISOU 2431  C   GLY A1346     7702   8747   7847   -911    518    108       C  
ATOM   2432  O   GLY A1346      14.013   6.225 -13.090  1.00 73.72           O  
ANISOU 2432  O   GLY A1346     8936   9964   9111   -866    476    127       O  
ATOM   2433  N   GLU A1347      12.412   4.645 -13.071  1.00 75.40           N  
ANISOU 2433  N   GLU A1347     9210  10178   9262   -955    627     69       N  
ATOM   2434  CA  GLU A1347      13.319   3.528 -13.322  1.00 82.81           C  
ANISOU 2434  CA  GLU A1347    10207  11066  10190   -958    708     45       C  
ATOM   2435  C   GLU A1347      14.252   3.783 -14.508  1.00 85.57           C  
ANISOU 2435  C   GLU A1347    10506  11454  10552  -1002    679     56       C  
ATOM   2436  O   GLU A1347      15.477   3.676 -14.385  1.00 85.00           O  
ANISOU 2436  O   GLU A1347    10452  11343  10500   -942    670     65       O  
ATOM   2437  CB  GLU A1347      12.491   2.263 -13.562  1.00 94.92           C  
ANISOU 2437  CB  GLU A1347    11796  12595  11674  -1038    829      0       C  
ATOM   2438  CG  GLU A1347      13.251   1.120 -14.208  1.00100.72           C  
ANISOU 2438  CG  GLU A1347    12583  13296  12392  -1074    922    -28       C  
ATOM   2439  CD  GLU A1347      12.341  -0.016 -14.636  1.00107.49           C  
ANISOU 2439  CD  GLU A1347    13488  14160  13192  -1178   1041    -74       C  
ATOM   2440  OE1 GLU A1347      11.349  -0.294 -13.915  1.00107.57           O  
ANISOU 2440  OE1 GLU A1347    13536  14162  13176  -1182   1074    -91       O  
ATOM   2441  OE2 GLU A1347      12.614  -0.625 -15.700  1.00106.79           O  
ANISOU 2441  OE2 GLU A1347    13402  14091  13084  -1262   1101    -96       O  
ATOM   2442  N   THR A1348      13.690   4.103 -15.676  1.00 87.02           N  
ANISOU 2442  N   THR A1348    10623  11720  10722  -1108    666     55       N  
ATOM   2443  CA  THR A1348      14.492   4.106 -16.900  1.00 75.88           C  
ANISOU 2443  CA  THR A1348     9171  10346   9315  -1170    660     56       C  
ATOM   2444  C   THR A1348      15.452   5.284 -16.949  1.00 73.91           C  
ANISOU 2444  C   THR A1348     8869  10109   9106  -1115    545     96       C  
ATOM   2445  O   THR A1348      16.604   5.122 -17.353  1.00 66.44           O  
ANISOU 2445  O   THR A1348     7923   9153   8169  -1104    543     97       O  
ATOM   2446  CB  THR A1348      13.581   4.105 -18.131  1.00 77.10           C  
ANISOU 2446  CB  THR A1348     9266  10590   9440  -1305    680     44       C  
ATOM   2447  OG1 THR A1348      12.887   2.851 -18.197  1.00 81.55           O  
ANISOU 2447  OG1 THR A1348     9888  11140   9957  -1369    801      0       O  
ATOM   2448  CG2 THR A1348      14.392   4.319 -19.427  1.00 72.04           C  
ANISOU 2448  CG2 THR A1348     8569   9997   8807  -1372    655     49       C  
ATOM   2449  N   GLY A1349      15.006   6.473 -16.530  1.00 76.31           N  
ANISOU 2449  N   GLY A1349     9130  10436   9428  -1080    452    129       N  
ATOM   2450  CA  GLY A1349      15.883   7.635 -16.583  1.00 76.44           C  
ANISOU 2450  CA  GLY A1349     9103  10465   9477  -1036    345    167       C  
ATOM   2451  C   GLY A1349      17.121   7.479 -15.719  1.00 75.20           C  
ANISOU 2451  C   GLY A1349     8994  10242   9337   -934    337    172       C  
ATOM   2452  O   GLY A1349      18.212   7.915 -16.096  1.00 81.85           O  
ANISOU 2452  O   GLY A1349     9810  11097  10191   -924    287    188       O  
ATOM   2453  N   VAL A1350      16.965   6.848 -14.552  1.00 68.57           N  
ANISOU 2453  N   VAL A1350     8223   9336   8495   -860    388    160       N  
ATOM   2454  CA  VAL A1350      18.083   6.598 -13.653  1.00 62.61           C  
ANISOU 2454  CA  VAL A1350     7515   8523   7751   -758    390    167       C  
ATOM   2455  C   VAL A1350      18.958   5.476 -14.195  1.00 69.15           C  
ANISOU 2455  C   VAL A1350     8375   9335   8564   -772    469    144       C  
ATOM   2456  O   VAL A1350      20.193   5.544 -14.122  1.00 72.27           O  
ANISOU 2456  O   VAL A1350     8770   9724   8966   -720    445    156       O  
ATOM   2457  CB  VAL A1350      17.573   6.271 -12.229  1.00 62.35           C  
ANISOU 2457  CB  VAL A1350     7544   8426   7719   -677    420    163       C  
ATOM   2458  CG1 VAL A1350      18.743   6.026 -11.292  1.00 61.72           C  
ANISOU 2458  CG1 VAL A1350     7509   8295   7648   -571    421    174       C  
ATOM   2459  CG2 VAL A1350      16.677   7.382 -11.679  1.00 60.91           C  
ANISOU 2459  CG2 VAL A1350     7331   8259   7551   -662    344    184       C  
ATOM   2460  N   ALA A1351      18.343   4.423 -14.741  1.00 66.66           N  
ANISOU 2460  N   ALA A1351     8090   9015   8223   -842    567    109       N  
ATOM   2461  CA  ALA A1351      19.135   3.315 -15.265  1.00 71.39           C  
ANISOU 2461  CA  ALA A1351     8727   9592   8805   -853    651     84       C  
ATOM   2462  C   ALA A1351      20.124   3.771 -16.333  1.00 78.87           C  
ANISOU 2462  C   ALA A1351     9612  10594   9760   -891    601     95       C  
ATOM   2463  O   ALA A1351      21.114   3.076 -16.591  1.00 90.27           O  
ANISOU 2463  O   ALA A1351    11080  12020  11196   -869    647     84       O  
ATOM   2464  CB  ALA A1351      18.215   2.228 -15.821  1.00 74.44           C  
ANISOU 2464  CB  ALA A1351     9152   9973   9159   -944    762     43       C  
ATOM   2465  N   GLY A1352      19.883   4.924 -16.951  1.00 74.36           N  
ANISOU 2465  N   GLY A1352     8961  10089   9202   -946    508    116       N  
ATOM   2466  CA  GLY A1352      20.816   5.523 -17.869  1.00 70.16           C  
ANISOU 2466  CA  GLY A1352     8369   9612   8679   -980    445    130       C  
ATOM   2467  C   GLY A1352      21.903   6.351 -17.235  1.00 67.43           C  
ANISOU 2467  C   GLY A1352     8008   9262   8349   -891    358    162       C  
ATOM   2468  O   GLY A1352      22.573   7.097 -17.948  1.00 73.29           O  
ANISOU 2468  O   GLY A1352     8694  10058   9096   -925    287    177       O  
ATOM   2469  N   PHE A1353      22.094   6.271 -15.918  1.00 74.49           N  
ANISOU 2469  N   PHE A1353     8952  10100   9248   -784    361    173       N  
ATOM   2470  CA  PHE A1353      23.227   6.934 -15.267  1.00 72.52           C  
ANISOU 2470  CA  PHE A1353     8695   9853   9008   -700    290    201       C  
ATOM   2471  C   PHE A1353      24.417   5.978 -15.216  1.00 79.19           C  
ANISOU 2471  C   PHE A1353     9572  10680   9836   -646    349    190       C  
ATOM   2472  O   PHE A1353      25.013   5.715 -14.178  1.00 82.26           O  
ANISOU 2472  O   PHE A1353    10002  11033  10222   -544    362    201       O  
ATOM   2473  CB  PHE A1353      22.843   7.426 -13.883  1.00 68.34           C  
ANISOU 2473  CB  PHE A1353     8195   9282   8491   -616    256    220       C  
ATOM   2474  CG  PHE A1353      22.083   8.715 -13.884  1.00 72.58           C  
ANISOU 2474  CG  PHE A1353     8689   9845   9044   -647    167    242       C  
ATOM   2475  CD1 PHE A1353      20.807   8.785 -14.419  1.00 75.94           C  
ANISOU 2475  CD1 PHE A1353     9096  10287   9471   -722    180    233       C  
ATOM   2476  CD2 PHE A1353      22.627   9.851 -13.316  1.00 84.13           C  
ANISOU 2476  CD2 PHE A1353    10133  11317  10516   -600     74    273       C  
ATOM   2477  CE1 PHE A1353      20.090   9.977 -14.407  1.00 80.81           C  
ANISOU 2477  CE1 PHE A1353     9674  10929  10101   -740    100    256       C  
ATOM   2478  CE2 PHE A1353      21.918  11.048 -13.303  1.00 91.35           C  
ANISOU 2478  CE2 PHE A1353    11016  12248  11444   -623     -4    295       C  
ATOM   2479  CZ  PHE A1353      20.645  11.108 -13.850  1.00 88.27           C  
ANISOU 2479  CZ  PHE A1353    10607  11873  11059   -689      9    287       C  
ATOM   2480  N   THR A1354      24.767   5.503 -16.413  1.00 84.49           N  
ANISOU 2480  N   THR A1354    10221  11386  10496   -718    384    170       N  
ATOM   2481  CA  THR A1354      25.636   4.343 -16.580  1.00 79.44           C  
ANISOU 2481  CA  THR A1354     9620  10726   9838   -683    469    150       C  
ATOM   2482  C   THR A1354      26.988   4.529 -15.897  1.00 79.11           C  
ANISOU 2482  C   THR A1354     9578  10693   9789   -578    432    174       C  
ATOM   2483  O   THR A1354      27.502   3.597 -15.263  1.00 73.46           O  
ANISOU 2483  O   THR A1354     8919   9932   9060   -492    504    170       O  
ATOM   2484  CB  THR A1354      25.771   4.069 -18.082  1.00 76.04           C  
ANISOU 2484  CB  THR A1354     9149  10345   9398   -792    493    127       C  
ATOM   2485  OG1 THR A1354      24.565   3.439 -18.526  1.00 74.94           O  
ANISOU 2485  OG1 THR A1354     9035  10185   9254   -873    568     99       O  
ATOM   2486  CG2 THR A1354      26.980   3.190 -18.423  1.00 71.50           C  
ANISOU 2486  CG2 THR A1354     8592   9770   8804   -756    552    113       C  
ATOM   2487  N   ASN A1355      27.579   5.723 -16.007  1.00 81.60           N  
ANISOU 2487  N   ASN A1355     9830  11066  10106   -585    323    200       N  
ATOM   2488  CA  ASN A1355      28.919   5.924 -15.468  1.00 77.18           C  
ANISOU 2488  CA  ASN A1355     9262  10533   9530   -499    287    221       C  
ATOM   2489  C   ASN A1355      28.892   6.151 -13.966  1.00 74.52           C  
ANISOU 2489  C   ASN A1355     8963  10155   9197   -395    270    245       C  
ATOM   2490  O   ASN A1355      29.824   5.733 -13.272  1.00 74.69           O  
ANISOU 2490  O   ASN A1355     9006  10173   9200   -301    291    257       O  
ATOM   2491  CB  ASN A1355      29.607   7.101 -16.165  1.00 81.90           C  
ANISOU 2491  CB  ASN A1355     9783  11213  10121   -555    180    236       C  
ATOM   2492  CG  ASN A1355      29.788   6.881 -17.662  1.00 84.80           C  
ANISOU 2492  CG  ASN A1355    10108  11629  10482   -657    193    213       C  
ATOM   2493  OD1 ASN A1355      29.752   5.752 -18.160  1.00 86.34           O  
ANISOU 2493  OD1 ASN A1355    10330  11803  10671   -670    287    186       O  
ATOM   2494  ND2 ASN A1355      29.996   7.973 -18.388  1.00 86.40           N  
ANISOU 2494  ND2 ASN A1355    10246  11897  10684   -731     99    224       N  
ATOM   2495  N   SER A1356      27.830   6.800 -13.458  1.00 82.02           N  
ANISOU 2495  N   SER A1356     9918  11077  10169   -411    234    253       N  
ATOM   2496  CA  SER A1356      27.629   6.957 -12.013  1.00 76.22           C  
ANISOU 2496  CA  SER A1356     9223  10296   9440   -320    226    271       C  
ATOM   2497  C   SER A1356      27.187   5.649 -11.373  1.00 75.79           C  
ANISOU 2497  C   SER A1356     9245  10168   9384   -263    335    254       C  
ATOM   2498  O   SER A1356      27.688   5.269 -10.305  1.00 66.33           O  
ANISOU 2498  O   SER A1356     8085   8941   8177   -163    359    268       O  
ATOM   2499  CB  SER A1356      26.595   8.044 -11.738  1.00 63.68           C  
ANISOU 2499  CB  SER A1356     7618   8702   7875   -357    156    283       C  
ATOM   2500  OG  SER A1356      27.061   9.300 -12.204  1.00 77.96           O  
ANISOU 2500  OG  SER A1356     9368  10571   9682   -400     54    302       O  
ATOM   2501  N   LEU A1357      26.257   4.943 -12.022  1.00 72.47           N  
ANISOU 2501  N   LEU A1357     8848   9720   8968   -330    405    224       N  
ATOM   2502  CA  LEU A1357      25.841   3.634 -11.534  1.00 74.69           C  
ANISOU 2502  CA  LEU A1357     9209   9929   9241   -290    518    204       C  
ATOM   2503  C   LEU A1357      27.029   2.701 -11.364  1.00 77.44           C  
ANISOU 2503  C   LEU A1357     9592  10265   9568   -207    580    206       C  
ATOM   2504  O   LEU A1357      27.064   1.899 -10.430  1.00 73.54           O  
ANISOU 2504  O   LEU A1357     9165   9711   9065   -122    645    208       O  
ATOM   2505  CB  LEU A1357      24.818   3.021 -12.490  1.00 74.29           C  
ANISOU 2505  CB  LEU A1357     9172   9866   9188   -394    586    168       C  
ATOM   2506  CG  LEU A1357      23.436   3.673 -12.504  1.00 75.70           C  
ANISOU 2506  CG  LEU A1357     9331  10051   9381   -463    550    164       C  
ATOM   2507  CD1 LEU A1357      22.610   3.138 -13.661  1.00 78.18           C  
ANISOU 2507  CD1 LEU A1357     9641  10380   9685   -579    610    131       C  
ATOM   2508  CD2 LEU A1357      22.706   3.510 -11.160  1.00 65.19           C  
ANISOU 2508  CD2 LEU A1357     8056   8659   8055   -396    570    168       C  
ATOM   2509  N   ARG A1358      28.012   2.788 -12.265  1.00 84.62           N  
ANISOU 2509  N   ARG A1358    10455  11232  10464   -230    561    207       N  
ATOM   2510  CA  ARG A1358      29.181   1.923 -12.162  1.00 84.83           C  
ANISOU 2510  CA  ARG A1358    10509  11256  10467   -147    618    210       C  
ATOM   2511  C   ARG A1358      30.028   2.288 -10.949  1.00 92.27           C  
ANISOU 2511  C   ARG A1358    11449  12211  11399    -30    573    247       C  
ATOM   2512  O   ARG A1358      30.462   1.414 -10.190  1.00 90.48           O  
ANISOU 2512  O   ARG A1358    11278  11943  11156     72    641    255       O  
ATOM   2513  CB  ARG A1358      30.007   2.018 -13.437  1.00 75.68           C  
ANISOU 2513  CB  ARG A1358     9293  10167   9296   -204    601    201       C  
ATOM   2514  CG  ARG A1358      30.912   0.826 -13.667  1.00 83.95           C  
ANISOU 2514  CG  ARG A1358    10379  11200  10317   -143    694    191       C  
ATOM   2515  CD  ARG A1358      32.093   1.190 -14.560  1.00 97.32           C  
ANISOU 2515  CD  ARG A1358    12001  12983  11993   -163    646    195       C  
ATOM   2516  NE  ARG A1358      31.675   1.981 -15.717  1.00103.11           N  
ANISOU 2516  NE  ARG A1358    12668  13768  12740   -298    584    180       N  
ATOM   2517  CZ  ARG A1358      31.919   3.279 -15.869  1.00105.16           C  
ANISOU 2517  CZ  ARG A1358    12855  14098  13004   -338    466    199       C  
ATOM   2518  NH1 ARG A1358      32.599   3.946 -14.944  1.00102.26           N  
ANISOU 2518  NH1 ARG A1358    12469  13759  12624   -260    399    231       N  
ATOM   2519  NH2 ARG A1358      31.486   3.907 -16.954  1.00111.62           N  
ANISOU 2519  NH2 ARG A1358    13619  14957  13833   -460    418    186       N  
ATOM   2520  N   MET A1359      30.266   3.585 -10.751  1.00 96.34           N  
ANISOU 2520  N   MET A1359    11902  12783  11920    -44    461    270       N  
ATOM   2521  CA  MET A1359      31.118   4.030  -9.658  1.00 89.58           C  
ANISOU 2521  CA  MET A1359    11035  11952  11048     53    413    305       C  
ATOM   2522  C   MET A1359      30.523   3.653  -8.312  1.00 85.72           C  
ANISOU 2522  C   MET A1359    10610  11391  10568    131    451    314       C  
ATOM   2523  O   MET A1359      31.245   3.203  -7.415  1.00 82.64           O  
ANISOU 2523  O   MET A1359    10246  10996  10159    237    478    336       O  
ATOM   2524  CB  MET A1359      31.331   5.538  -9.753  1.00 87.00           C  
ANISOU 2524  CB  MET A1359    10638  11694  10724      5    289    323       C  
ATOM   2525  CG  MET A1359      32.024   5.954 -11.018  1.00 87.36           C  
ANISOU 2525  CG  MET A1359    10620  11818  10756    -69    245    316       C  
ATOM   2526  SD  MET A1359      32.061   7.735 -11.201  1.00 93.70           S  
ANISOU 2526  SD  MET A1359    11354  12685  11562   -143    105    335       S  
ATOM   2527  CE  MET A1359      32.402   7.892 -12.949  1.00 87.31           C  
ANISOU 2527  CE  MET A1359    10486  11942  10746   -257     84    314       C  
ATOM   2528  N   LEU A1360      29.210   3.858  -8.149  1.00 81.16           N  
ANISOU 2528  N   LEU A1360    10055  10764  10018     80    451    300       N  
ATOM   2529  CA  LEU A1360      28.528   3.440  -6.929  1.00 75.46           C  
ANISOU 2529  CA  LEU A1360     9397   9971   9305    142    492    303       C  
ATOM   2530  C   LEU A1360      28.741   1.959  -6.668  1.00 87.54           C  
ANISOU 2530  C   LEU A1360    11003  11443  10817    212    609    294       C  
ATOM   2531  O   LEU A1360      29.141   1.564  -5.568  1.00 90.23           O  
ANISOU 2531  O   LEU A1360    11381  11757  11146    314    635    315       O  
ATOM   2532  CB  LEU A1360      27.038   3.750  -7.023  1.00 66.25           C  
ANISOU 2532  CB  LEU A1360     8241   8768   8165     64    486    283       C  
ATOM   2533  CG  LEU A1360      26.774   5.248  -7.039  1.00 64.45           C  
ANISOU 2533  CG  LEU A1360     7948   8585   7954     17    371    298       C  
ATOM   2534  CD1 LEU A1360      25.334   5.534  -7.408  1.00 63.14           C  
ANISOU 2534  CD1 LEU A1360     7782   8398   7810    -67    367    278       C  
ATOM   2535  CD2 LEU A1360      27.126   5.870  -5.699  1.00 71.98           C  
ANISOU 2535  CD2 LEU A1360     8904   9537   8907     98    319    328       C  
ATOM   2536  N   GLN A1361      28.488   1.121  -7.674  1.00 93.76           N  
ANISOU 2536  N   GLN A1361    11815  12208  11600    156    685    263       N  
ATOM   2537  CA  GLN A1361      28.679  -0.313  -7.498  1.00 98.57           C  
ANISOU 2537  CA  GLN A1361    12507  12754  12190    218    805    252       C  
ATOM   2538  C   GLN A1361      30.111  -0.631  -7.085  1.00103.32           C  
ANISOU 2538  C   GLN A1361    13105  13386  12765    334    813    283       C  
ATOM   2539  O   GLN A1361      30.345  -1.517  -6.253  1.00105.44           O  
ANISOU 2539  O   GLN A1361    13442  13602  13019    433    884    294       O  
ATOM   2540  CB  GLN A1361      28.309  -1.050  -8.781  1.00 98.20           C  
ANISOU 2540  CB  GLN A1361    12481  12691  12138    129    879    214       C  
ATOM   2541  CG  GLN A1361      28.183  -2.536  -8.585  1.00100.94           C  
ANISOU 2541  CG  GLN A1361    12932  12954  12466    175   1013    195       C  
ATOM   2542  CD  GLN A1361      27.597  -3.227  -9.779  1.00103.20           C  
ANISOU 2542  CD  GLN A1361    13247  13219  12746     70   1091    152       C  
ATOM   2543  OE1 GLN A1361      27.665  -2.720 -10.897  1.00106.70           O  
ANISOU 2543  OE1 GLN A1361    13623  13722  13195    -21   1050    140       O  
ATOM   2544  NE2 GLN A1361      27.013  -4.398  -9.554  1.00105.06           N  
ANISOU 2544  NE2 GLN A1361    13584  13368  12965     76   1207    128       N  
ATOM   2545  N   GLN A1362      31.078   0.098  -7.630  1.00101.05           N  
ANISOU 2545  N   GLN A1362    12739  13188  12469    324    740    298       N  
ATOM   2546  CA  GLN A1362      32.473  -0.098  -7.268  1.00 96.55           C  
ANISOU 2546  CA  GLN A1362    12152  12667  11867    429    738    329       C  
ATOM   2547  C   GLN A1362      32.866   0.588  -5.949  1.00 98.27           C  
ANISOU 2547  C   GLN A1362    12348  12913  12077    510    672    368       C  
ATOM   2548  O   GLN A1362      34.053   0.593  -5.607  1.00103.71           O  
ANISOU 2548  O   GLN A1362    13008  13662  12734    593    657    398       O  
ATOM   2549  CB  GLN A1362      33.360   0.383  -8.412  1.00 83.19           C  
ANISOU 2549  CB  GLN A1362    10381  11066  10160    378    688    326       C  
ATOM   2550  CG  GLN A1362      33.418  -0.585  -9.564  1.00 87.74           C  
ANISOU 2550  CG  GLN A1362    10984  11623  10731    340    775    294       C  
ATOM   2551  CD  GLN A1362      34.261  -0.065 -10.707  1.00 93.60           C  
ANISOU 2551  CD  GLN A1362    11644  12459  11459    282    720    289       C  
ATOM   2552  OE1 GLN A1362      35.459  -0.344 -10.782  1.00 99.66           O  
ANISOU 2552  OE1 GLN A1362    12390  13282  12194    353    729    304       O  
ATOM   2553  NE2 GLN A1362      33.641   0.696 -11.607  1.00 94.65           N  
ANISOU 2553  NE2 GLN A1362    11731  12618  11615    154    663    268       N  
ATOM   2554  N   LYS A1363      31.902   1.144  -5.207  1.00 93.07           N  
ANISOU 2554  N   LYS A1363    11702  12216  11444    487    636    369       N  
ATOM   2555  CA  LYS A1363      32.141   1.844  -3.933  1.00 95.01           C  
ANISOU 2555  CA  LYS A1363    11931  12483  11686    550    573    402       C  
ATOM   2556  C   LYS A1363      33.095   3.034  -4.085  1.00 94.42           C  
ANISOU 2556  C   LYS A1363    11768  12515  11592    535    467    425       C  
ATOM   2557  O   LYS A1363      33.814   3.397  -3.148  1.00 91.34           O  
ANISOU 2557  O   LYS A1363    11357  12168  11178    606    431    458       O  
ATOM   2558  CB  LYS A1363      32.642   0.883  -2.843  1.00 91.61           C  
ANISOU 2558  CB  LYS A1363    11557  12018  11231    682    644    427       C  
ATOM   2559  CG  LYS A1363      31.787  -0.370  -2.711  1.00 87.87           C  
ANISOU 2559  CG  LYS A1363    11182  11437  10769    698    757    404       C  
ATOM   2560  CD  LYS A1363      31.650  -0.823  -1.282  1.00 96.02           C  
ANISOU 2560  CD  LYS A1363    12271  12417  11794    796    792    426       C  
ATOM   2561  CE  LYS A1363      30.382  -1.639  -1.082  1.00102.33           C  
ANISOU 2561  CE  LYS A1363    13160  13108  12611    770    872    396       C  
ATOM   2562  NZ  LYS A1363      29.267  -0.796  -0.533  1.00102.61           N  
ANISOU 2562  NZ  LYS A1363    13185  13126  12678    709    812    385       N  
ATOM   2563  N   ARG A1364      33.091   3.669  -5.259  1.00 92.43           N  
ANISOU 2563  N   ARG A1364    11463  12308  11347    436    417    408       N  
ATOM   2564  CA  ARG A1364      33.889   4.872  -5.495  1.00 85.63           C  
ANISOU 2564  CA  ARG A1364    10523  11545  10467    401    314    425       C  
ATOM   2565  C   ARG A1364      33.004   6.090  -5.249  1.00 81.81           C  
ANISOU 2565  C   ARG A1364    10022  11049  10013    330    232    424       C  
ATOM   2566  O   ARG A1364      32.517   6.751  -6.167  1.00 90.81           O  
ANISOU 2566  O   ARG A1364    11132  12201  11171    231    186    407       O  
ATOM   2567  CB  ARG A1364      34.465   4.857  -6.902  1.00 84.29           C  
ANISOU 2567  CB  ARG A1364    10309  11434  10285    337    306    408       C  
ATOM   2568  CG  ARG A1364      35.255   3.614  -7.219  1.00 87.11           C  
ANISOU 2568  CG  ARG A1364    10688  11796  10615    406    394    406       C  
ATOM   2569  CD  ARG A1364      35.886   3.701  -8.594  1.00102.20           C  
ANISOU 2569  CD  ARG A1364    12545  13774  12510    339    378    389       C  
ATOM   2570  NE  ARG A1364      36.686   2.516  -8.887  1.00115.52           N  
ANISOU 2570  NE  ARG A1364    14255  15468  14170    412    465    387       N  
ATOM   2571  CZ  ARG A1364      37.187   2.222 -10.081  1.00119.51           C  
ANISOU 2571  CZ  ARG A1364    14731  16014  14663    368    483    367       C  
ATOM   2572  NH1 ARG A1364      36.969   3.033 -11.111  1.00124.69           N  
ANISOU 2572  NH1 ARG A1364    15333  16712  15332    246    416    348       N  
ATOM   2573  NH2 ARG A1364      37.901   1.113 -10.242  1.00117.45           N  
ANISOU 2573  NH2 ARG A1364    14497  15752  14376    448    568    367       N  
ATOM   2574  N   TRP A1365      32.801   6.393  -3.969  1.00 72.52           N  
ANISOU 2574  N   TRP A1365     8866   9850   8838    386    214    444       N  
ATOM   2575  CA  TRP A1365      31.772   7.360  -3.599  1.00 75.24           C  
ANISOU 2575  CA  TRP A1365     9211  10161   9215    332    157    440       C  
ATOM   2576  C   TRP A1365      32.152   8.778  -3.999  1.00 72.01           C  
ANISOU 2576  C   TRP A1365     8741   9823   8797    264     50    449       C  
ATOM   2577  O   TRP A1365      31.288   9.562  -4.398  1.00 70.84           O  
ANISOU 2577  O   TRP A1365     8584   9655   8677    187      5    438       O  
ATOM   2578  CB  TRP A1365      31.496   7.305  -2.091  1.00 76.06           C  
ANISOU 2578  CB  TRP A1365     9354  10224   9323    410    167    457       C  
ATOM   2579  CG  TRP A1365      31.481   5.938  -1.497  1.00 74.09           C  
ANISOU 2579  CG  TRP A1365     9164   9920   9068    498    267    458       C  
ATOM   2580  CD1 TRP A1365      32.326   5.462  -0.554  1.00 72.02           C  
ANISOU 2580  CD1 TRP A1365     8915   9676   8775    600    293    486       C  
ATOM   2581  CD2 TRP A1365      30.575   4.866  -1.806  1.00 81.39           C  
ANISOU 2581  CD2 TRP A1365    10149  10762  10013    489    355    430       C  
ATOM   2582  NE1 TRP A1365      32.007   4.163  -0.245  1.00 80.05           N  
ANISOU 2582  NE1 TRP A1365    10000  10622   9796    661    393    479       N  
ATOM   2583  CE2 TRP A1365      30.936   3.772  -1.000  1.00 83.41           C  
ANISOU 2583  CE2 TRP A1365    10458  10983  10251    591    434    443       C  
ATOM   2584  CE3 TRP A1365      29.502   4.724  -2.690  1.00 85.39           C  
ANISOU 2584  CE3 TRP A1365    10670  11227  10547    401    378    396       C  
ATOM   2585  CZ2 TRP A1365      30.257   2.552  -1.042  1.00 84.98           C  
ANISOU 2585  CZ2 TRP A1365    10732  11099  10459    606    534    421       C  
ATOM   2586  CZ3 TRP A1365      28.831   3.510  -2.736  1.00 88.75           C  
ANISOU 2586  CZ3 TRP A1365    11164  11578  10978    412    478    373       C  
ATOM   2587  CH2 TRP A1365      29.211   2.441  -1.919  1.00 89.86           C  
ANISOU 2587  CH2 TRP A1365    11364  11677  11100    512    556    384       C  
ATOM   2588  N   ASP A1366      33.419   9.156  -3.832  1.00 77.86           N  
ANISOU 2588  N   ASP A1366     9442  10647   9494    293     10    472       N  
ATOM   2589  CA  ASP A1366      33.815  10.505  -4.216  1.00 79.71           C  
ANISOU 2589  CA  ASP A1366     9625  10947   9712    221    -89    479       C  
ATOM   2590  C   ASP A1366      33.697  10.686  -5.718  1.00 82.54           C  
ANISOU 2590  C   ASP A1366     9953  11328  10081    126   -107    458       C  
ATOM   2591  O   ASP A1366      33.167  11.699  -6.182  1.00 88.46           O  
ANISOU 2591  O   ASP A1366    10685  12077  10847     45   -172    453       O  
ATOM   2592  CB  ASP A1366      35.237  10.809  -3.747  1.00 88.89           C  
ANISOU 2592  CB  ASP A1366    10751  12206  10816    265   -123    505       C  
ATOM   2593  CG  ASP A1366      35.291  11.310  -2.310  1.00102.74           C  
ANISOU 2593  CG  ASP A1366    12520  13958  12559    317   -148    529       C  
ATOM   2594  OD1 ASP A1366      34.691  12.368  -2.026  1.00103.97           O  
ANISOU 2594  OD1 ASP A1366    12680  14091  12732    267   -207    529       O  
ATOM   2595  OD2 ASP A1366      35.947  10.650  -1.469  1.00105.27           O  
ANISOU 2595  OD2 ASP A1366    12847  14300  12850    409   -108    549       O  
ATOM   2596  N   GLU A1367      34.191   9.715  -6.493  1.00 82.03           N  
ANISOU 2596  N   GLU A1367     9881  11282  10004    136    -50    445       N  
ATOM   2597  CA  GLU A1367      34.052   9.777  -7.946  1.00 82.22           C  
ANISOU 2597  CA  GLU A1367     9875  11326  10038     43    -60    423       C  
ATOM   2598  C   GLU A1367      32.589   9.913  -8.343  1.00 81.07           C  
ANISOU 2598  C   GLU A1367     9753  11109   9942    -24    -52    404       C  
ATOM   2599  O   GLU A1367      32.229  10.808  -9.118  1.00 78.84           O  
ANISOU 2599  O   GLU A1367     9439  10846   9671   -114   -115    399       O  
ATOM   2600  CB  GLU A1367      34.673   8.538  -8.598  1.00 71.38           C  
ANISOU 2600  CB  GLU A1367     8504   9969   8648     74     19    410       C  
ATOM   2601  CG  GLU A1367      36.188   8.513  -8.593  1.00 77.32           C  
ANISOU 2601  CG  GLU A1367     9215  10818   9345    119      1    426       C  
ATOM   2602  CD  GLU A1367      36.755   7.198  -9.114  1.00 89.04           C  
ANISOU 2602  CD  GLU A1367    10710  12308  10814    168     90    414       C  
ATOM   2603  OE1 GLU A1367      36.305   6.723 -10.182  1.00 92.86           O  
ANISOU 2603  OE1 GLU A1367    11199  12765  11320    106    129    386       O  
ATOM   2604  OE2 GLU A1367      37.650   6.629  -8.448  1.00 95.80           O  
ANISOU 2604  OE2 GLU A1367    11570  13195  11634    270    124    434       O  
ATOM   2605  N   ALA A1368      31.725   9.050  -7.785  1.00 73.63           N  
ANISOU 2605  N   ALA A1368     8866  10086   9025     19     23    394       N  
ATOM   2606  CA  ALA A1368      30.307   9.097  -8.119  1.00 65.33           C  
ANISOU 2606  CA  ALA A1368     7834   8974   8013    -42     37    375       C  
ATOM   2607  C   ALA A1368      29.713  10.454  -7.778  1.00 63.93           C  
ANISOU 2607  C   ALA A1368     7641   8797   7853    -79    -51    388       C  
ATOM   2608  O   ALA A1368      28.953  11.034  -8.568  1.00 62.85           O  
ANISOU 2608  O   ALA A1368     7484   8660   7736   -162    -85    379       O  
ATOM   2609  CB  ALA A1368      29.567   7.982  -7.392  1.00 64.92           C  
ANISOU 2609  CB  ALA A1368     7849   8843   7977     17    129    363       C  
ATOM   2610  N   ALA A1369      30.091  10.986  -6.621  1.00 63.50           N  
ANISOU 2610  N   ALA A1369     7595   8746   7787    -19    -88    411       N  
ATOM   2611  CA  ALA A1369      29.551  12.250  -6.140  1.00 62.28           C  
ANISOU 2611  CA  ALA A1369     7436   8582   7646    -44   -163    424       C  
ATOM   2612  C   ALA A1369      29.946  13.389  -7.058  1.00 62.65           C  
ANISOU 2612  C   ALA A1369     7435   8687   7680   -126   -248    430       C  
ATOM   2613  O   ALA A1369      29.186  14.349  -7.234  1.00 70.49           O  
ANISOU 2613  O   ALA A1369     8424   9664   8694   -176   -301    433       O  
ATOM   2614  CB  ALA A1369      30.041  12.517  -4.705  1.00 62.37           C  
ANISOU 2614  CB  ALA A1369     7467   8591   7641     36   -179    445       C  
ATOM   2615  N   VAL A1370      31.150  13.310  -7.626  1.00 67.36           N  
ANISOU 2615  N   VAL A1370     7998   9355   8242   -136   -262    433       N  
ATOM   2616  CA  VAL A1370      31.634  14.351  -8.516  1.00 64.82           C  
ANISOU 2616  CA  VAL A1370     7632   9095   7901   -218   -342    438       C  
ATOM   2617  C   VAL A1370      30.964  14.226  -9.878  1.00 68.04           C  
ANISOU 2617  C   VAL A1370     8019   9499   8334   -303   -334    419       C  
ATOM   2618  O   VAL A1370      30.581  15.228 -10.500  1.00 64.17           O  
ANISOU 2618  O   VAL A1370     7510   9021   7852   -377   -398    424       O  
ATOM   2619  CB  VAL A1370      33.163  14.260  -8.615  1.00 66.78           C  
ANISOU 2619  CB  VAL A1370     7848   9429   8097   -200   -357    445       C  
ATOM   2620  CG1 VAL A1370      33.639  14.668 -10.015  1.00 77.53           C  
ANISOU 2620  CG1 VAL A1370     9162  10855   9442   -293   -400    436       C  
ATOM   2621  CG2 VAL A1370      33.800  15.105  -7.571  1.00 67.30           C  
ANISOU 2621  CG2 VAL A1370     7917   9526   8130   -168   -410    468       C  
ATOM   2622  N   ASN A1371      30.798  12.986 -10.345  1.00 67.33           N  
ANISOU 2622  N   ASN A1371     7936   9392   8253   -294   -252    398       N  
ATOM   2623  CA  ASN A1371      30.219  12.738 -11.656  1.00 64.58           C  
ANISOU 2623  CA  ASN A1371     7566   9048   7923   -378   -235    379       C  
ATOM   2624  C   ASN A1371      28.753  13.099 -11.677  1.00 66.28           C  
ANISOU 2624  C   ASN A1371     7797   9212   8176   -414   -240    376       C  
ATOM   2625  O   ASN A1371      28.281  13.724 -12.631  1.00 67.84           O  
ANISOU 2625  O   ASN A1371     7963   9430   8384   -498   -281    376       O  
ATOM   2626  CB  ASN A1371      30.395  11.276 -12.037  1.00 72.36           C  
ANISOU 2626  CB  ASN A1371     8567  10022   8906   -356   -137    356       C  
ATOM   2627  CG  ASN A1371      30.249  11.053 -13.518  1.00 76.37           C  
ANISOU 2627  CG  ASN A1371     9040  10561   9418   -452   -126    335       C  
ATOM   2628  OD1 ASN A1371      29.442  10.230 -13.951  1.00 79.69           O  
ANISOU 2628  OD1 ASN A1371     9479  10944   9856   -478    -55    313       O  
ATOM   2629  ND2 ASN A1371      31.021  11.804 -14.316  1.00 69.48           N  
ANISOU 2629  ND2 ASN A1371     8116   9760   8524   -511   -195    341       N  
ATOM   2630  N   LEU A1372      28.028  12.739 -10.610  1.00 70.91           N  
ANISOU 2630  N   LEU A1372     8429   9735   8780   -351   -199    376       N  
ATOM   2631  CA  LEU A1372      26.596  13.000 -10.521  1.00 60.89           C  
ANISOU 2631  CA  LEU A1372     7174   8420   7542   -376   -197    373       C  
ATOM   2632  C   LEU A1372      26.271  14.480 -10.507  1.00 60.43           C  
ANISOU 2632  C   LEU A1372     7096   8372   7491   -409   -291    395       C  
ATOM   2633  O   LEU A1372      25.190  14.867 -10.945  1.00 62.13           O  
ANISOU 2633  O   LEU A1372     7302   8576   7727   -456   -304    394       O  
ATOM   2634  CB  LEU A1372      26.030  12.320  -9.287  1.00 60.16           C  
ANISOU 2634  CB  LEU A1372     7135   8263   7461   -296   -137    368       C  
ATOM   2635  CG  LEU A1372      25.528  10.907  -9.525  1.00 60.41           C  
ANISOU 2635  CG  LEU A1372     7196   8260   7495   -295    -34    341       C  
ATOM   2636  CD1 LEU A1372      25.766  10.061  -8.308  1.00 60.49           C  
ANISOU 2636  CD1 LEU A1372     7259   8223   7499   -198     26    340       C  
ATOM   2637  CD2 LEU A1372      24.061  10.996  -9.844  1.00 59.61           C  
ANISOU 2637  CD2 LEU A1372     7096   8137   7415   -349    -22    328       C  
ATOM   2638  N   ALA A1373      27.180  15.316 -10.041  1.00 65.10           N  
ANISOU 2638  N   ALA A1373     7684   8990   8063   -388   -354    414       N  
ATOM   2639  CA  ALA A1373      26.926  16.746 -10.055  1.00 65.38           C  
ANISOU 2639  CA  ALA A1373     7710   9030   8101   -422   -440    435       C  
ATOM   2640  C   ALA A1373      27.248  17.397 -11.397  1.00 63.74           C  
ANISOU 2640  C   ALA A1373     7459   8878   7882   -513   -495    438       C  
ATOM   2641  O   ALA A1373      26.997  18.595 -11.560  1.00 68.66           O  
ANISOU 2641  O   ALA A1373     8078   9504   8506   -549   -566    456       O  
ATOM   2642  CB  ALA A1373      27.716  17.424  -8.920  1.00 63.41           C  
ANISOU 2642  CB  ALA A1373     7481   8782   7829   -368   -483    453       C  
ATOM   2643  N   LYS A1374      27.807  16.653 -12.356  1.00 67.78           N  
ANISOU 2643  N   LYS A1374     7939   9432   8380   -552   -464    422       N  
ATOM   2644  CA  LYS A1374      27.965  17.140 -13.720  1.00 70.02           C  
ANISOU 2644  CA  LYS A1374     8179   9768   8657   -647   -508    422       C  
ATOM   2645  C   LYS A1374      26.760  16.821 -14.602  1.00 70.26           C  
ANISOU 2645  C   LYS A1374     8192   9787   8715   -705   -477    412       C  
ATOM   2646  O   LYS A1374      26.750  17.208 -15.784  1.00 73.92           O  
ANISOU 2646  O   LYS A1374     8616  10295   9176   -789   -511    414       O  
ATOM   2647  CB  LYS A1374      29.222  16.532 -14.362  1.00 73.79           C  
ANISOU 2647  CB  LYS A1374     8627  10306   9104   -666   -493    409       C  
ATOM   2648  CG  LYS A1374      30.551  17.021 -13.826  1.00 71.85           C  
ANISOU 2648  CG  LYS A1374     8379  10104   8818   -637   -540    420       C  
ATOM   2649  CD  LYS A1374      31.622  15.955 -14.069  1.00 71.60           C  
ANISOU 2649  CD  LYS A1374     8329  10116   8759   -612   -489    404       C  
ATOM   2650  CE  LYS A1374      33.011  16.379 -13.637  1.00 68.02           C  
ANISOU 2650  CE  LYS A1374     7864   9727   8255   -588   -533    415       C  
ATOM   2651  NZ  LYS A1374      33.954  15.272 -13.983  1.00 74.74           N  
ANISOU 2651  NZ  LYS A1374     8693  10624   9081   -561   -478    399       N  
ATOM   2652  N   SER A1375      25.767  16.113 -14.060  1.00 66.07           N  
ANISOU 2652  N   SER A1375     7690   9207   8208   -665   -413    402       N  
ATOM   2653  CA  SER A1375      24.608  15.644 -14.800  1.00 62.97           C  
ANISOU 2653  CA  SER A1375     7282   8811   7834   -718   -369    389       C  
ATOM   2654  C   SER A1375      23.609  16.774 -15.021  1.00 68.42           C  
ANISOU 2654  C   SER A1375     7958   9500   8539   -752   -430    411       C  
ATOM   2655  O   SER A1375      23.678  17.833 -14.394  1.00 72.75           O  
ANISOU 2655  O   SER A1375     8522  10032   9089   -720   -494    435       O  
ATOM   2656  CB  SER A1375      23.933  14.487 -14.056  1.00 65.34           C  
ANISOU 2656  CB  SER A1375     7623   9059   8145   -664   -277    368       C  
ATOM   2657  OG  SER A1375      23.378  14.883 -12.813  1.00 59.91           O  
ANISOU 2657  OG  SER A1375     6972   8321   7469   -594   -289    380       O  
ATOM   2658  N   ARG A1376      22.681  16.544 -15.947  1.00 70.10           N  
ANISOU 2658  N   ARG A1376     8141   9736   8760   -818   -407    405       N  
ATOM   2659  CA  ARG A1376      21.601  17.502 -16.151  1.00 65.04           C  
ANISOU 2659  CA  ARG A1376     7484   9098   8131   -841   -454    428       C  
ATOM   2660  C   ARG A1376      20.682  17.542 -14.936  1.00 67.39           C  
ANISOU 2660  C   ARG A1376     7822   9341   8444   -765   -434    431       C  
ATOM   2661  O   ARG A1376      20.212  18.614 -14.542  1.00 71.22           O  
ANISOU 2661  O   ARG A1376     8314   9809   8937   -741   -492    457       O  
ATOM   2662  CB  ARG A1376      20.808  17.138 -17.404  1.00 62.26           C  
ANISOU 2662  CB  ARG A1376     7085   8794   7778   -929   -426    420       C  
ATOM   2663  CG  ARG A1376      19.617  18.012 -17.626  1.00 62.63           C  
ANISOU 2663  CG  ARG A1376     7111   8852   7834   -947   -465    446       C  
ATOM   2664  CD  ARG A1376      18.756  17.490 -18.757  1.00 71.46           C  
ANISOU 2664  CD  ARG A1376     8180  10025   8946  -1032   -424    437       C  
ATOM   2665  NE  ARG A1376      17.555  18.301 -18.922  1.00 72.90           N  
ANISOU 2665  NE  ARG A1376     8339  10228   9132  -1040   -459    465       N  
ATOM   2666  CZ  ARG A1376      17.499  19.406 -19.656  1.00 76.58           C  
ANISOU 2666  CZ  ARG A1376     8772  10729   9597  -1078   -534    499       C  
ATOM   2667  NH1 ARG A1376      18.586  19.840 -20.313  1.00 71.45           N  
ANISOU 2667  NH1 ARG A1376     8108  10099   8941  -1121   -584    506       N  
ATOM   2668  NH2 ARG A1376      16.353  20.079 -19.720  1.00 78.18           N  
ANISOU 2668  NH2 ARG A1376     8955  10948   9802  -1072   -558    526       N  
ATOM   2669  N   TRP A1377      20.393  16.367 -14.364  1.00 60.65           N  
ANISOU 2669  N   TRP A1377     6996   8457   7592   -730   -351    405       N  
ATOM   2670  CA  TRP A1377      19.634  16.251 -13.123  1.00 59.97           C  
ANISOU 2670  CA  TRP A1377     6950   8317   7517   -656   -326    403       C  
ATOM   2671  C   TRP A1377      20.150  17.208 -12.050  1.00 66.81           C  
ANISOU 2671  C   TRP A1377     7848   9148   8389   -586   -388    425       C  
ATOM   2672  O   TRP A1377      19.382  17.998 -11.479  1.00 62.12           O  
ANISOU 2672  O   TRP A1377     7265   8530   7806   -554   -421    441       O  
ATOM   2673  CB  TRP A1377      19.699  14.799 -12.633  1.00 60.92           C  
ANISOU 2673  CB  TRP A1377     7106   8408   7632   -625   -230    371       C  
ATOM   2674  CG  TRP A1377      19.272  14.550 -11.177  1.00 71.17           C  
ANISOU 2674  CG  TRP A1377     8456   9647   8939   -539   -202    366       C  
ATOM   2675  CD1 TRP A1377      18.003  14.594 -10.671  1.00 73.90           C  
ANISOU 2675  CD1 TRP A1377     8812   9974   9292   -524   -185    363       C  
ATOM   2676  CD2 TRP A1377      20.113  14.149 -10.086  1.00 62.84           C  
ANISOU 2676  CD2 TRP A1377     7444   8550   7881   -461   -183    363       C  
ATOM   2677  NE1 TRP A1377      18.005  14.274  -9.345  1.00 62.26           N  
ANISOU 2677  NE1 TRP A1377     7388   8446   7823   -444   -160    356       N  
ATOM   2678  CE2 TRP A1377      19.287  13.997  -8.956  1.00 61.19           C  
ANISOU 2678  CE2 TRP A1377     7272   8295   7682   -404   -158    358       C  
ATOM   2679  CE3 TRP A1377      21.487  13.918  -9.954  1.00 57.82           C  
ANISOU 2679  CE3 TRP A1377     6816   7919   7233   -432   -186    365       C  
ATOM   2680  CZ2 TRP A1377      19.791  13.639  -7.702  1.00 56.58           C  
ANISOU 2680  CZ2 TRP A1377     6734   7666   7098   -322   -137    356       C  
ATOM   2681  CZ3 TRP A1377      21.980  13.564  -8.735  1.00 60.37           C  
ANISOU 2681  CZ3 TRP A1377     7181   8203   7554   -349   -164    366       C  
ATOM   2682  CH2 TRP A1377      21.130  13.420  -7.612  1.00 65.65           C  
ANISOU 2682  CH2 TRP A1377     7888   8822   8235   -295   -139    362       C  
ATOM   2683  N   TYR A1378      21.449  17.145 -11.753  1.00 58.93           N  
ANISOU 2683  N   TYR A1378     6862   8150   7379   -560   -400    425       N  
ATOM   2684  CA  TYR A1378      22.005  18.122 -10.832  1.00 65.05           C  
ANISOU 2684  CA  TYR A1378     7662   8901   8151   -509   -461    446       C  
ATOM   2685  C   TYR A1378      21.612  19.522 -11.265  1.00 61.45           C  
ANISOU 2685  C   TYR A1378     7192   8457   7700   -544   -541    473       C  
ATOM   2686  O   TYR A1378      21.144  20.332 -10.464  1.00 73.44           O  
ANISOU 2686  O   TYR A1378     8737   9939   9228   -501   -574    489       O  
ATOM   2687  CB  TYR A1378      23.531  18.007 -10.736  1.00 59.31           C  
ANISOU 2687  CB  TYR A1378     6937   8198   7400   -498   -475    446       C  
ATOM   2688  CG  TYR A1378      24.087  18.980  -9.730  1.00 59.40           C  
ANISOU 2688  CG  TYR A1378     6976   8191   7402   -452   -532    466       C  
ATOM   2689  CD1 TYR A1378      24.239  20.309 -10.051  1.00 60.19           C  
ANISOU 2689  CD1 TYR A1378     7070   8305   7494   -489   -612    488       C  
ATOM   2690  CD2 TYR A1378      24.402  18.582  -8.435  1.00 59.56           C  
ANISOU 2690  CD2 TYR A1378     7033   8179   7420   -374   -503    462       C  
ATOM   2691  CE1 TYR A1378      24.700  21.219  -9.141  1.00 60.49           C  
ANISOU 2691  CE1 TYR A1378     7139   8324   7519   -455   -659    504       C  
ATOM   2692  CE2 TYR A1378      24.890  19.487  -7.522  1.00 59.05           C  
ANISOU 2692  CE2 TYR A1378     6992   8102   7343   -340   -552    479       C  
ATOM   2693  CZ  TYR A1378      25.035  20.809  -7.889  1.00 67.42           C  
ANISOU 2693  CZ  TYR A1378     8049   9176   8394   -383   -629    499       C  
ATOM   2694  OH  TYR A1378      25.508  21.750  -7.001  1.00 77.33           O  
ANISOU 2694  OH  TYR A1378     9334  10418   9632   -359   -676    514       O  
ATOM   2695  N   ASN A1379      21.781  19.818 -12.539  1.00 67.55           N  
ANISOU 2695  N   ASN A1379     7924   9278   8465   -621   -571    480       N  
ATOM   2696  CA  ASN A1379      21.637  21.193 -12.988  1.00 72.25           C  
ANISOU 2696  CA  ASN A1379     8510   9883   9058   -654   -652    509       C  
ATOM   2697  C   ASN A1379      20.207  21.702 -12.825  1.00 66.27           C  
ANISOU 2697  C   ASN A1379     7756   9104   8321   -636   -658    524       C  
ATOM   2698  O   ASN A1379      20.001  22.900 -12.624  1.00 63.96           O  
ANISOU 2698  O   ASN A1379     7481   8792   8030   -623   -718    551       O  
ATOM   2699  CB  ASN A1379      22.107  21.289 -14.438  1.00 67.74           C  
ANISOU 2699  CB  ASN A1379     7891   9374   8473   -744   -678    511       C  
ATOM   2700  CG  ASN A1379      23.003  22.469 -14.659  1.00 83.06           C  
ANISOU 2700  CG  ASN A1379     9838  11329  10393   -772   -760    533       C  
ATOM   2701  OD1 ASN A1379      22.781  23.257 -15.576  1.00 88.76           O  
ANISOU 2701  OD1 ASN A1379    10537  12076  11111   -830   -810    552       O  
ATOM   2702  ND2 ASN A1379      24.012  22.626 -13.789  1.00 84.53           N  
ANISOU 2702  ND2 ASN A1379    10056  11500  10560   -730   -775    530       N  
ATOM   2703  N   GLN A1380      19.219  20.808 -12.877  1.00 61.83           N  
ANISOU 2703  N   GLN A1380     7180   8544   7770   -634   -594    507       N  
ATOM   2704  CA  GLN A1380      17.803  21.141 -12.808  1.00 69.42           C  
ANISOU 2704  CA  GLN A1380     8133   9500   8743   -621   -591    519       C  
ATOM   2705  C   GLN A1380      17.321  21.335 -11.379  1.00 74.23           C  
ANISOU 2705  C   GLN A1380     8790  10051   9365   -534   -584    518       C  
ATOM   2706  O   GLN A1380      16.562  22.268 -11.095  1.00 72.52           O  
ANISOU 2706  O   GLN A1380     8581   9818   9157   -505   -621    541       O  
ATOM   2707  CB  GLN A1380      16.976  20.034 -13.454  1.00 71.53           C  
ANISOU 2707  CB  GLN A1380     8366   9805   9007   -664   -521    496       C  
ATOM   2708  CG  GLN A1380      17.246  19.838 -14.926  1.00 74.15           C  
ANISOU 2708  CG  GLN A1380     8646  10200   9328   -758   -524    496       C  
ATOM   2709  CD  GLN A1380      16.634  20.922 -15.764  1.00 78.04           C  
ANISOU 2709  CD  GLN A1380     9102  10731   9819   -798   -584    531       C  
ATOM   2710  OE1 GLN A1380      17.313  21.855 -16.201  1.00 81.62           O  
ANISOU 2710  OE1 GLN A1380     9552  11192  10269   -820   -652    554       O  
ATOM   2711  NE2 GLN A1380      15.343  20.805 -16.006  1.00 82.09           N  
ANISOU 2711  NE2 GLN A1380     9587  11273  10331   -809   -559    535       N  
ATOM   2712  N   THR A1381      17.738  20.454 -10.477  1.00 74.74           N  
ANISOU 2712  N   THR A1381     8884  10083   9430   -490   -534    494       N  
ATOM   2713  CA  THR A1381      17.365  20.514  -9.068  1.00 58.29           C  
ANISOU 2713  CA  THR A1381     6845   7946   7358   -410   -521    490       C  
ATOM   2714  C   THR A1381      18.619  20.426  -8.210  1.00 57.74           C  
ANISOU 2714  C   THR A1381     6811   7847   7281   -369   -526    486       C  
ATOM   2715  O   THR A1381      18.898  19.386  -7.603  1.00 64.18           O  
ANISOU 2715  O   THR A1381     7645   8646   8094   -336   -469    464       O  
ATOM   2716  CB  THR A1381      16.389  19.397  -8.706  1.00 57.61           C  
ANISOU 2716  CB  THR A1381     6762   7853   7275   -394   -444    463       C  
ATOM   2717  OG1 THR A1381      16.979  18.129  -8.979  1.00 57.23           O  
ANISOU 2717  OG1 THR A1381     6714   7815   7217   -416   -381    437       O  
ATOM   2718  CG2 THR A1381      15.113  19.522  -9.475  1.00 58.41           C  
ANISOU 2718  CG2 THR A1381     6824   7993   7375   -433   -438    469       C  
ATOM   2719  N   PRO A1382      19.373  21.511  -8.100  1.00 58.37           N  
ANISOU 2719  N   PRO A1382     6904   7922   7353   -368   -593    508       N  
ATOM   2720  CA  PRO A1382      20.665  21.451  -7.400  1.00 61.84           C  
ANISOU 2720  CA  PRO A1382     7367   8352   7776   -340   -601    505       C  
ATOM   2721  C   PRO A1382      20.548  21.120  -5.925  1.00 68.63           C  
ANISOU 2721  C   PRO A1382     8267   9165   8643   -263   -569    496       C  
ATOM   2722  O   PRO A1382      21.264  20.253  -5.406  1.00 64.07           O  
ANISOU 2722  O   PRO A1382     7701   8588   8056   -234   -529    482       O  
ATOM   2723  CB  PRO A1382      21.228  22.863  -7.597  1.00 64.77           C  
ANISOU 2723  CB  PRO A1382     7748   8728   8133   -365   -682    531       C  
ATOM   2724  CG  PRO A1382      20.525  23.399  -8.824  1.00 62.93           C  
ANISOU 2724  CG  PRO A1382     7483   8521   7906   -423   -712    546       C  
ATOM   2725  CD  PRO A1382      19.160  22.793  -8.790  1.00 63.96           C  
ANISOU 2725  CD  PRO A1382     7600   8642   8059   -404   -663    536       C  
ATOM   2726  N   ASN A1383      19.650  21.836  -5.243  1.00 75.19           N  
ANISOU 2726  N   ASN A1383     9122   9957   9490   -228   -588    505       N  
ATOM   2727  CA  ASN A1383      19.555  21.729  -3.791  1.00 56.37           C  
ANISOU 2727  CA  ASN A1383     6777   7528   7112   -158   -568    498       C  
ATOM   2728  C   ASN A1383      19.201  20.312  -3.385  1.00 59.09           C  
ANISOU 2728  C   ASN A1383     7124   7864   7463   -130   -490    472       C  
ATOM   2729  O   ASN A1383      19.854  19.714  -2.523  1.00 73.02           O  
ANISOU 2729  O   ASN A1383     8910   9614   9220    -88   -460    464       O  
ATOM   2730  CB  ASN A1383      18.534  22.729  -3.265  1.00 56.62           C  
ANISOU 2730  CB  ASN A1383     6829   7522   7160   -130   -599    510       C  
ATOM   2731  CG  ASN A1383      18.977  24.168  -3.452  1.00 77.00           C  
ANISOU 2731  CG  ASN A1383     9426  10098   9731   -150   -673    537       C  
ATOM   2732  OD1 ASN A1383      20.150  24.498  -3.251  1.00 78.67           O  
ANISOU 2732  OD1 ASN A1383     9653  10317   9921   -160   -699    543       O  
ATOM   2733  ND2 ASN A1383      18.043  25.034  -3.861  1.00 75.42           N  
ANISOU 2733  ND2 ASN A1383     9226   9888   9544   -156   -704    554       N  
ATOM   2734  N   ARG A1384      18.188  19.745  -4.020  1.00 55.18           N  
ANISOU 2734  N   ARG A1384     6608   7380   6978   -154   -453    460       N  
ATOM   2735  CA  ARG A1384      17.851  18.361  -3.735  1.00 60.61           C  
ANISOU 2735  CA  ARG A1384     7304   8059   7666   -138   -374    432       C  
ATOM   2736  C   ARG A1384      18.972  17.431  -4.161  1.00 63.37           C  
ANISOU 2736  C   ARG A1384     7649   8430   7999   -154   -338    423       C  
ATOM   2737  O   ARG A1384      19.290  16.461  -3.454  1.00 67.18           O  
ANISOU 2737  O   ARG A1384     8158   8890   8476   -112   -283    408       O  
ATOM   2738  CB  ARG A1384      16.557  17.977  -4.441  1.00 54.67           C  
ANISOU 2738  CB  ARG A1384     6528   7327   6918   -176   -341    420       C  
ATOM   2739  CG  ARG A1384      16.303  16.510  -4.390  1.00 54.33           C  
ANISOU 2739  CG  ARG A1384     6496   7279   6867   -180   -255    390       C  
ATOM   2740  CD  ARG A1384      15.041  16.218  -5.117  1.00 63.75           C  
ANISOU 2740  CD  ARG A1384     7663   8504   8056   -228   -226    378       C  
ATOM   2741  NE  ARG A1384      14.552  14.887  -4.812  1.00 65.17           N  
ANISOU 2741  NE  ARG A1384     7867   8670   8224   -228   -140    345       N  
ATOM   2742  CZ  ARG A1384      13.383  14.434  -5.235  1.00 68.61           C  
ANISOU 2742  CZ  ARG A1384     8288   9133   8648   -269    -99    328       C  
ATOM   2743  NH1 ARG A1384      12.604  15.214  -5.960  1.00 64.40           N  
ANISOU 2743  NH1 ARG A1384     7710   8646   8115   -307   -138    343       N  
ATOM   2744  NH2 ARG A1384      12.999  13.203  -4.935  1.00 75.92           N  
ANISOU 2744  NH2 ARG A1384     9245  10044   9558   -274    -17    296       N  
ATOM   2745  N   ALA A1385      19.574  17.701  -5.323  1.00 66.29           N  
ANISOU 2745  N   ALA A1385     7986   8843   8360   -211   -368    432       N  
ATOM   2746  CA  ALA A1385      20.616  16.815  -5.826  1.00 63.39           C  
ANISOU 2746  CA  ALA A1385     7610   8501   7975   -227   -333    422       C  
ATOM   2747  C   ALA A1385      21.849  16.861  -4.938  1.00 63.27           C  
ANISOU 2747  C   ALA A1385     7616   8480   7945   -174   -346    431       C  
ATOM   2748  O   ALA A1385      22.500  15.832  -4.718  1.00 59.47           O  
ANISOU 2748  O   ALA A1385     7146   7999   7451   -145   -292    420       O  
ATOM   2749  CB  ALA A1385      20.982  17.176  -7.257  1.00 56.49           C  
ANISOU 2749  CB  ALA A1385     6692   7679   7092   -304   -368    429       C  
ATOM   2750  N   LYS A1386      22.181  18.044  -4.412  1.00 55.86           N  
ANISOU 2750  N   LYS A1386     6684   7537   7002   -160   -413    452       N  
ATOM   2751  CA  LYS A1386      23.340  18.143  -3.535  1.00 56.13           C  
ANISOU 2751  CA  LYS A1386     6735   7577   7015   -116   -426    461       C  
ATOM   2752  C   LYS A1386      23.157  17.277  -2.286  1.00 55.39           C  
ANISOU 2752  C   LYS A1386     6675   7442   6926    -42   -367    451       C  
ATOM   2753  O   LYS A1386      24.111  16.632  -1.832  1.00 65.28           O  
ANISOU 2753  O   LYS A1386     7935   8709   8159     -3   -339    452       O  
ATOM   2754  CB  LYS A1386      23.599  19.607  -3.182  1.00 60.91           C  
ANISOU 2754  CB  LYS A1386     7348   8182   7612   -124   -504    483       C  
ATOM   2755  CG  LYS A1386      25.018  19.904  -2.731  1.00 69.66           C  
ANISOU 2755  CG  LYS A1386     8458   9325   8684   -112   -532    495       C  
ATOM   2756  CD  LYS A1386      25.028  20.717  -1.441  1.00 77.80           C  
ANISOU 2756  CD  LYS A1386     9524  10326   9711    -73   -561    506       C  
ATOM   2757  CE  LYS A1386      26.425  21.065  -0.989  1.00 82.04           C  
ANISOU 2757  CE  LYS A1386    10059  10908  10203    -70   -589    518       C  
ATOM   2758  NZ  LYS A1386      27.003  22.169  -1.813  1.00 86.20           N  
ANISOU 2758  NZ  LYS A1386    10575  11474  10704   -140   -657    530       N  
ATOM   2759  N   ARG A1387      21.918  17.189  -1.769  1.00 54.53           N  
ANISOU 2759  N   ARG A1387     6587   7289   6842    -22   -345    441       N  
ATOM   2760  CA  ARG A1387      21.608  16.352  -0.608  1.00 53.85           C  
ANISOU 2760  CA  ARG A1387     6537   7163   6763     42   -288    429       C  
ATOM   2761  C   ARG A1387      21.722  14.866  -0.925  1.00 63.05           C  
ANISOU 2761  C   ARG A1387     7710   8327   7921     49   -207    410       C  
ATOM   2762  O   ARG A1387      22.323  14.092  -0.157  1.00 54.12           O  
ANISOU 2762  O   ARG A1387     6603   7184   6778    105   -165    409       O  
ATOM   2763  CB  ARG A1387      20.191  16.629  -0.115  1.00 53.10           C  
ANISOU 2763  CB  ARG A1387     6456   7027   6691     51   -285    420       C  
ATOM   2764  CG  ARG A1387      19.958  17.938   0.535  1.00 53.28           C  
ANISOU 2764  CG  ARG A1387     6488   7034   6722     65   -348    436       C  
ATOM   2765  CD  ARG A1387      18.669  17.873   1.331  1.00 52.30           C  
ANISOU 2765  CD  ARG A1387     6385   6868   6618     95   -326    422       C  
ATOM   2766  NE  ARG A1387      17.513  18.174   0.501  1.00 57.04           N  
ANISOU 2766  NE  ARG A1387     6963   7477   7231     56   -334    418       N  
ATOM   2767  CZ  ARG A1387      17.230  19.395   0.059  1.00 59.44           C  
ANISOU 2767  CZ  ARG A1387     7253   7790   7542     33   -396    436       C  
ATOM   2768  NH1 ARG A1387      18.029  20.410   0.371  1.00 56.25           N  
ANISOU 2768  NH1 ARG A1387     6860   7381   7131     40   -452    456       N  
ATOM   2769  NH2 ARG A1387      16.165  19.606  -0.698  1.00 53.42           N  
ANISOU 2769  NH2 ARG A1387     6467   7043   6787      2   -400    435       N  
ATOM   2770  N   VAL A1388      21.055  14.436  -1.999  1.00 54.09           N  
ANISOU 2770  N   VAL A1388     6559   7202   6792     -5   -179    394       N  
ATOM   2771  CA  VAL A1388      21.094  13.036  -2.414  1.00 56.77           C  
ANISOU 2771  CA  VAL A1388     6911   7536   7122    -10    -96    373       C  
ATOM   2772  C   VAL A1388      22.537  12.601  -2.649  1.00 65.88           C  
ANISOU 2772  C   VAL A1388     8058   8719   8253      9    -87    382       C  
ATOM   2773  O   VAL A1388      22.948  11.505  -2.230  1.00 55.82           O  
ANISOU 2773  O   VAL A1388     6815   7426   6968     56    -20    374       O  
ATOM   2774  CB  VAL A1388      20.220  12.848  -3.676  1.00 66.64           C  
ANISOU 2774  CB  VAL A1388     8136   8806   8376    -88    -78    357       C  
ATOM   2775  CG1 VAL A1388      20.473  11.492  -4.363  1.00 55.45           C  
ANISOU 2775  CG1 VAL A1388     6731   7392   6945   -109      4    335       C  
ATOM   2776  CG2 VAL A1388      18.755  13.033  -3.320  1.00 54.10           C  
ANISOU 2776  CG2 VAL A1388     6558   7196   6803    -95    -72    346       C  
ATOM   2777  N   ILE A1389      23.334  13.477  -3.298  1.00 61.38           N  
ANISOU 2777  N   ILE A1389     7450   8197   7674    -26   -153    399       N  
ATOM   2778  CA  ILE A1389      24.756  13.225  -3.523  1.00 56.92           C  
ANISOU 2778  CA  ILE A1389     6871   7675   7082    -10   -155    409       C  
ATOM   2779  C   ILE A1389      25.519  13.109  -2.198  1.00 66.30           C  
ANISOU 2779  C   ILE A1389     8082   8854   8253     72   -150    424       C  
ATOM   2780  O   ILE A1389      26.292  12.160  -2.008  1.00 69.76           O  
ANISOU 2780  O   ILE A1389     8532   9302   8673    119    -99    424       O  
ATOM   2781  CB  ILE A1389      25.333  14.311  -4.443  1.00 61.05           C  
ANISOU 2781  CB  ILE A1389     7348   8253   7594    -73   -234    422       C  
ATOM   2782  CG1 ILE A1389      24.738  14.142  -5.866  1.00 73.02           C  
ANISOU 2782  CG1 ILE A1389     8836   9785   9121   -154   -223    407       C  
ATOM   2783  CG2 ILE A1389      26.834  14.220  -4.495  1.00 61.09           C  
ANISOU 2783  CG2 ILE A1389     7335   8311   7565    -54   -246    434       C  
ATOM   2784  CD1 ILE A1389      25.075  15.220  -6.922  1.00 58.12           C  
ANISOU 2784  CD1 ILE A1389     6906   7950   7228   -228   -300    420       C  
ATOM   2785  N   THR A1390      25.326  14.069  -1.264  1.00 58.05           N  
ANISOU 2785  N   THR A1390     7046   7796   7215     93   -202    438       N  
ATOM   2786  CA  THR A1390      25.909  13.925   0.081  1.00 61.22           C  
ANISOU 2786  CA  THR A1390     7469   8190   7600    168   -192    452       C  
ATOM   2787  C   THR A1390      25.590  12.560   0.673  1.00 56.60           C  
ANISOU 2787  C   THR A1390     6923   7560   7020    227   -105    439       C  
ATOM   2788  O   THR A1390      26.449  11.909   1.273  1.00 66.36           O  
ANISOU 2788  O   THR A1390     8171   8808   8234    289    -72    450       O  
ATOM   2789  CB  THR A1390      25.407  15.007   1.048  1.00 65.57           C  
ANISOU 2789  CB  THR A1390     8033   8716   8164    178   -244    461       C  
ATOM   2790  OG1 THR A1390      25.975  16.278   0.752  1.00 69.09           O  
ANISOU 2790  OG1 THR A1390     8454   9202   8594    136   -322    477       O  
ATOM   2791  CG2 THR A1390      25.814  14.682   2.461  1.00 72.63           C  
ANISOU 2791  CG2 THR A1390     8954   9598   9046    253   -222    471       C  
ATOM   2792  N   THR A1391      24.358  12.108   0.509  1.00 55.77           N  
ANISOU 2792  N   THR A1391     6842   7408   6941    208    -65    416       N  
ATOM   2793  CA  THR A1391      23.996  10.792   1.006  1.00 55.89           C  
ANISOU 2793  CA  THR A1391     6902   7377   6956    254     22    401       C  
ATOM   2794  C   THR A1391      24.836   9.699   0.357  1.00 57.28           C  
ANISOU 2794  C   THR A1391     7082   7570   7111    267     82    398       C  
ATOM   2795  O   THR A1391      25.296   8.783   1.040  1.00 70.88           O  
ANISOU 2795  O   THR A1391     8839   9274   8819    336    139    403       O  
ATOM   2796  CB  THR A1391      22.499  10.571   0.788  1.00 55.01           C  
ANISOU 2796  CB  THR A1391     6810   7224   6869    213     51    375       C  
ATOM   2797  OG1 THR A1391      21.787  11.737   1.220  1.00 56.26           O  
ANISOU 2797  OG1 THR A1391     6954   7376   7045    199    -13    380       O  
ATOM   2798  CG2 THR A1391      21.986   9.354   1.532  1.00 55.14           C  
ANISOU 2798  CG2 THR A1391     6882   7186   6882    258    136    358       C  
ATOM   2799  N   PHE A1392      25.062   9.793  -0.966  1.00 75.18           N  
ANISOU 2799  N   PHE A1392     9316   9875   9376    204     71    392       N  
ATOM   2800  CA  PHE A1392      25.868   8.808  -1.693  1.00 71.64           C  
ANISOU 2800  CA  PHE A1392     8869   9446   8906    212    126    387       C  
ATOM   2801  C   PHE A1392      27.339   8.875  -1.289  1.00 70.59           C  
ANISOU 2801  C   PHE A1392     8717   9361   8742    272    106    414       C  
ATOM   2802  O   PHE A1392      27.981   7.837  -1.095  1.00 70.85           O  
ANISOU 2802  O   PHE A1392     8775   9390   8755    333    171    417       O  
ATOM   2803  CB  PHE A1392      25.729   9.033  -3.202  1.00 71.48           C  
ANISOU 2803  CB  PHE A1392     8810   9459   8890    121    110    373       C  
ATOM   2804  CG  PHE A1392      24.619   8.235  -3.860  1.00 68.58           C  
ANISOU 2804  CG  PHE A1392     8468   9054   8536     70    177    342       C  
ATOM   2805  CD1 PHE A1392      24.544   6.861  -3.700  1.00 69.90           C  
ANISOU 2805  CD1 PHE A1392     8689   9178   8693    104    276    324       C  
ATOM   2806  CD2 PHE A1392      23.652   8.870  -4.639  1.00 61.69           C  
ANISOU 2806  CD2 PHE A1392     7565   8192   7680    -14    143    330       C  
ATOM   2807  CE1 PHE A1392      23.527   6.138  -4.309  1.00 72.64           C  
ANISOU 2807  CE1 PHE A1392     9062   9494   9043     46    342    293       C  
ATOM   2808  CE2 PHE A1392      22.632   8.159  -5.224  1.00 62.34           C  
ANISOU 2808  CE2 PHE A1392     7666   8252   7766    -67    205    302       C  
ATOM   2809  CZ  PHE A1392      22.571   6.787  -5.068  1.00 67.15           C  
ANISOU 2809  CZ  PHE A1392     8332   8820   8363    -42    305    282       C  
ATOM   2810  N   ARG A1393      27.881  10.089  -1.159  1.00 68.70           N  
ANISOU 2810  N   ARG A1393     8437   9173   8495    257     20    434       N  
ATOM   2811  CA  ARG A1393      29.283  10.274  -0.782  1.00 66.72           C  
ANISOU 2811  CA  ARG A1393     8160   8984   8205    304     -6    460       C  
ATOM   2812  C   ARG A1393      29.581   9.712   0.609  1.00 77.35           C  
ANISOU 2812  C   ARG A1393     9540  10310   9538    401     32    476       C  
ATOM   2813  O   ARG A1393      30.553   8.970   0.802  1.00 78.06           O  
ANISOU 2813  O   ARG A1393     9632  10431   9598    465     71    491       O  
ATOM   2814  CB  ARG A1393      29.623  11.763  -0.829  1.00 61.36           C  
ANISOU 2814  CB  ARG A1393     7440   8356   7516    256   -106    474       C  
ATOM   2815  CG  ARG A1393      31.048  12.085  -1.196  1.00 67.38           C  
ANISOU 2815  CG  ARG A1393     8159   9208   8234    253   -144    491       C  
ATOM   2816  CD  ARG A1393      31.687  12.972  -0.161  1.00 87.51           C  
ANISOU 2816  CD  ARG A1393    10697  11797  10754    278   -199    516       C  
ATOM   2817  NE  ARG A1393      30.773  13.983   0.358  1.00 96.00           N  
ANISOU 2817  NE  ARG A1393    11790  12828  11857    246   -246    514       N  
ATOM   2818  CZ  ARG A1393      31.029  14.745   1.419  1.00 97.68           C  
ANISOU 2818  CZ  ARG A1393    12007  13053  12053    266   -286    532       C  
ATOM   2819  NH1 ARG A1393      32.178  14.615   2.068  1.00 92.52           N  
ANISOU 2819  NH1 ARG A1393    11338  12464  11353    314   -285    552       N  
ATOM   2820  NH2 ARG A1393      30.136  15.638   1.834  1.00102.49           N  
ANISOU 2820  NH2 ARG A1393    12637  13616  12690    238   -323    528       N  
ATOM   2821  N   THR A1394      28.764  10.072   1.603  1.00 76.49           N  
ANISOU 2821  N   THR A1394     9458  10154   9450    415     21    476       N  
ATOM   2822  CA  THR A1394      29.130   9.823   2.994  1.00 74.90           C  
ANISOU 2822  CA  THR A1394     9279   9946   9234    498     38    497       C  
ATOM   2823  C   THR A1394      28.503   8.569   3.580  1.00 81.66           C  
ANISOU 2823  C   THR A1394    10194  10730  10103    555    126    486       C  
ATOM   2824  O   THR A1394      29.073   8.000   4.515  1.00 88.26           O  
ANISOU 2824  O   THR A1394    11049  11569  10918    636    160    506       O  
ATOM   2825  CB  THR A1394      28.759  11.026   3.879  1.00 65.30           C  
ANISOU 2825  CB  THR A1394     8057   8727   8028    484    -30    505       C  
ATOM   2826  OG1 THR A1394      27.339  11.234   3.879  1.00 62.64           O  
ANISOU 2826  OG1 THR A1394     7745   8324   7733    446    -29    482       O  
ATOM   2827  CG2 THR A1394      29.443  12.283   3.388  1.00 65.92           C  
ANISOU 2827  CG2 THR A1394     8087   8874   8086    428   -114    517       C  
ATOM   2828  N   GLY A1395      27.376   8.108   3.040  1.00 76.95           N  
ANISOU 2828  N   GLY A1395     9628  10075   9535    513    166    456       N  
ATOM   2829  CA  GLY A1395      26.642   7.029   3.661  1.00 65.73           C  
ANISOU 2829  CA  GLY A1395     8269   8581   8122    554    246    442       C  
ATOM   2830  C   GLY A1395      25.911   7.447   4.917  1.00 74.75           C  
ANISOU 2830  C   GLY A1395     9433   9688   9282    575    226    443       C  
ATOM   2831  O   GLY A1395      25.510   6.592   5.721  1.00 69.24           O  
ANISOU 2831  O   GLY A1395     8787   8937   8584    624    286    438       O  
ATOM   2832  N   THR A1396      25.738   8.744   5.120  1.00 68.57           N  
ANISOU 2832  N   THR A1396     8613   8929   8510    540    144    450       N  
ATOM   2833  CA  THR A1396      25.067   9.251   6.294  1.00 66.52           C  
ANISOU 2833  CA  THR A1396     8370   8638   8267    556    120    450       C  
ATOM   2834  C   THR A1396      23.869  10.087   5.875  1.00 69.92           C  
ANISOU 2834  C   THR A1396     8790   9048   8728    485     79    429       C  
ATOM   2835  O   THR A1396      23.665  10.396   4.684  1.00 68.94           O  
ANISOU 2835  O   THR A1396     8640   8943   8611    422     59    418       O  
ATOM   2836  CB  THR A1396      26.010  10.099   7.149  1.00 69.09           C  
ANISOU 2836  CB  THR A1396     8666   9012   8571    589     62    481       C  
ATOM   2837  OG1 THR A1396      26.063  11.429   6.616  1.00 74.07           O  
ANISOU 2837  OG1 THR A1396     9255   9679   9207    526    -18    484       O  
ATOM   2838  CG2 THR A1396      27.422   9.479   7.193  1.00 63.07           C  
ANISOU 2838  CG2 THR A1396     7891   8302   7769    648     88    508       C  
ATOM   2839  N   TRP A1397      23.096  10.468   6.894  1.00 59.90           N  
ANISOU 2839  N   TRP A1397     7540   7745   7476    499     65    424       N  
ATOM   2840  CA  TRP A1397      21.893  11.262   6.736  1.00 52.90           C  
ANISOU 2840  CA  TRP A1397     6645   6838   6615    448     28    406       C  
ATOM   2841  C   TRP A1397      22.131  12.727   7.051  1.00 52.48           C  
ANISOU 2841  C   TRP A1397     6562   6810   6566    434    -56    423       C  
ATOM   2842  O   TRP A1397      21.162  13.487   7.171  1.00 54.83           O  
ANISOU 2842  O   TRP A1397     6859   7088   6887    407    -89    412       O  
ATOM   2843  CB  TRP A1397      20.768  10.716   7.624  1.00 52.23           C  
ANISOU 2843  CB  TRP A1397     6604   6698   6544    469     72    384       C  
ATOM   2844  CG  TRP A1397      20.189   9.402   7.223  1.00 63.94           C  
ANISOU 2844  CG  TRP A1397     8124   8148   8022    462    155    359       C  
ATOM   2845  CD1 TRP A1397      20.349   8.213   7.872  1.00 53.41           C  
ANISOU 2845  CD1 TRP A1397     6839   6780   6674    513    226    356       C  
ATOM   2846  CD2 TRP A1397      19.334   9.141   6.098  1.00 71.78           C  
ANISOU 2846  CD2 TRP A1397     9113   9140   9021    396    178    334       C  
ATOM   2847  NE1 TRP A1397      19.645   7.219   7.225  1.00 66.89           N  
ANISOU 2847  NE1 TRP A1397     8580   8459   8375    480    296    327       N  
ATOM   2848  CE2 TRP A1397      19.013   7.759   6.131  1.00 72.03           C  
ANISOU 2848  CE2 TRP A1397     9196   9133   9038    406    268    313       C  
ATOM   2849  CE3 TRP A1397      18.821   9.933   5.061  1.00 70.29           C  
ANISOU 2849  CE3 TRP A1397     8884   8980   8844    329    133    328       C  
ATOM   2850  CZ2 TRP A1397      18.194   7.154   5.167  1.00 61.17           C  
ANISOU 2850  CZ2 TRP A1397     7832   7752   7657    344    316    284       C  
ATOM   2851  CZ3 TRP A1397      17.997   9.330   4.101  1.00 60.10           C  
ANISOU 2851  CZ3 TRP A1397     7597   7689   7550    272    178    302       C  
ATOM   2852  CH2 TRP A1397      17.690   7.954   4.170  1.00 58.93           C  
ANISOU 2852  CH2 TRP A1397     7501   7506   7385    276    269    279       C  
ATOM   2853  N   ASP A1398      23.393  13.141   7.182  1.00 61.98           N  
ANISOU 2853  N   ASP A1398     7744   8060   7746    450    -90    449       N  
ATOM   2854  CA  ASP A1398      23.692  14.534   7.513  1.00 75.20           C  
ANISOU 2854  CA  ASP A1398     9398   9758   9417    430   -166    464       C  
ATOM   2855  C   ASP A1398      22.881  15.502   6.667  1.00 74.32           C  
ANISOU 2855  C   ASP A1398     9272   9639   9328    367   -214    454       C  
ATOM   2856  O   ASP A1398      22.378  16.514   7.171  1.00 76.66           O  
ANISOU 2856  O   ASP A1398     9573   9917   9636    357   -257    456       O  
ATOM   2857  CB  ASP A1398      25.179  14.809   7.330  1.00 81.58           C  
ANISOU 2857  CB  ASP A1398    10177  10634  10187    433   -194    490       C  
ATOM   2858  CG  ASP A1398      26.016  14.215   8.437  1.00 89.06           C  
ANISOU 2858  CG  ASP A1398    11133  11600  11106    501   -164    508       C  
ATOM   2859  OD1 ASP A1398      25.474  13.407   9.232  1.00 95.22           O  
ANISOU 2859  OD1 ASP A1398    11945  12335  11899    548   -112    500       O  
ATOM   2860  OD2 ASP A1398      27.212  14.569   8.517  1.00 91.60           O  
ANISOU 2860  OD2 ASP A1398    11428  11986  11390    506   -192    530       O  
ATOM   2861  N   ALA A1399      22.716  15.185   5.379  1.00 67.11           N  
ANISOU 2861  N   ALA A1399     8342   8739   8419    324   -203    445       N  
ATOM   2862  CA  ALA A1399      22.005  16.087   4.489  1.00 67.62           C  
ANISOU 2862  CA  ALA A1399     8387   8804   8500    265   -248    441       C  
ATOM   2863  C   ALA A1399      20.573  16.332   4.947  1.00 65.21           C  
ANISOU 2863  C   ALA A1399     8100   8452   8223    268   -245    425       C  
ATOM   2864  O   ALA A1399      20.038  17.426   4.743  1.00 63.56           O  
ANISOU 2864  O   ALA A1399     7882   8239   8027    241   -296    429       O  
ATOM   2865  CB  ALA A1399      22.026  15.529   3.067  1.00 76.03           C  
ANISOU 2865  CB  ALA A1399     9430   9894   9564    218   -227    432       C  
ATOM   2866  N   TYR A1400      19.942  15.339   5.573  1.00 65.28           N  
ANISOU 2866  N   TYR A1400     8136   8428   8240    301   -184    406       N  
ATOM   2867  CA  TYR A1400      18.538  15.430   5.962  1.00 67.63           C  
ANISOU 2867  CA  TYR A1400     8448   8690   8559    301   -174    387       C  
ATOM   2868  C   TYR A1400      18.317  15.519   7.475  1.00 71.39           C  
ANISOU 2868  C   TYR A1400     8953   9133   9041    353   -170    385       C  
ATOM   2869  O   TYR A1400      17.170  15.453   7.920  1.00 70.29           O  
ANISOU 2869  O   TYR A1400     8827   8965   8914    358   -155    366       O  
ATOM   2870  CB  TYR A1400      17.780  14.233   5.386  1.00 64.77           C  
ANISOU 2870  CB  TYR A1400     8094   8319   8196    282   -106    362       C  
ATOM   2871  CG  TYR A1400      17.787  14.239   3.885  1.00 69.35           C  
ANISOU 2871  CG  TYR A1400     8643   8935   8773    221   -111    361       C  
ATOM   2872  CD1 TYR A1400      18.866  13.717   3.178  1.00 80.30           C  
ANISOU 2872  CD1 TYR A1400    10020  10348  10144    211    -94    369       C  
ATOM   2873  CD2 TYR A1400      16.742  14.806   3.170  1.00 66.08           C  
ANISOU 2873  CD2 TYR A1400     8205   8533   8370    176   -134    355       C  
ATOM   2874  CE1 TYR A1400      18.899  13.747   1.787  1.00 79.69           C  
ANISOU 2874  CE1 TYR A1400     9912  10305  10064    150   -101    368       C  
ATOM   2875  CE2 TYR A1400      16.763  14.840   1.787  1.00 72.95           C  
ANISOU 2875  CE2 TYR A1400     9042   9440   9236    117   -141    357       C  
ATOM   2876  CZ  TYR A1400      17.840  14.310   1.107  1.00 76.31           C  
ANISOU 2876  CZ  TYR A1400     9459   9887   9646    102   -125    362       C  
ATOM   2877  OH  TYR A1400      17.838  14.336  -0.247  1.00 70.49           O  
ANISOU 2877  OH  TYR A1400     8688   9188   8906     39   -131    361       O  
ATOM   2878  N   ALA A 302      19.373  15.681   8.270  1.00 68.33           N  
ANISOU 2878  N   ALA A 302     8571   8753   8638    388   -184    404       N  
ATOM   2879  CA  ALA A 302      19.266  15.503   9.714  1.00 68.93           C  
ANISOU 2879  CA  ALA A 302     8675   8801   8716    438   -167    401       C  
ATOM   2880  C   ALA A 302      18.734  16.723  10.460  1.00 69.81           C  
ANISOU 2880  C   ALA A 302     8790   8894   8842    438   -218    402       C  
ATOM   2881  O   ALA A 302      18.297  16.569  11.603  1.00 73.68           O  
ANISOU 2881  O   ALA A 302     9301   9355   9338    471   -202    393       O  
ATOM   2882  CB  ALA A 302      20.623  15.123  10.303  1.00 66.51           C  
ANISOU 2882  CB  ALA A 302     8370   8519   8382    476   -157    423       C  
ATOM   2883  N   ALA A 303      18.754  17.910   9.850  1.00 66.44           N  
ANISOU 2883  N   ALA A 303     8346   8480   8420    402   -277    413       N  
ATOM   2884  CA  ALA A 303      18.439  19.147  10.564  1.00 63.48           C  
ANISOU 2884  CA  ALA A 303     7980   8085   8053    405   -324    417       C  
ATOM   2885  C   ALA A 303      17.194  19.026  11.439  1.00 66.81           C  
ANISOU 2885  C   ALA A 303     8422   8466   8497    432   -303    395       C  
ATOM   2886  O   ALA A 303      17.228  19.371  12.622  1.00 76.34           O  
ANISOU 2886  O   ALA A 303     9647   9653   9705    458   -310    394       O  
ATOM   2887  CB  ALA A 303      18.266  20.302   9.579  1.00 58.14           C  
ANISOU 2887  CB  ALA A 303     7290   7417   7382    362   -379    427       C  
ATOM   2888  N   ASN A 304      16.078  18.559  10.875  1.00 72.26           N  
ANISOU 2888  N   ASN A 304     9106   9148   9201    420   -278    375       N  
ATOM   2889  CA  ASN A 304      14.835  18.537  11.645  1.00 66.18           C  
ANISOU 2889  CA  ASN A 304     8351   8349   8447    441   -263    352       C  
ATOM   2890  C   ASN A 304      14.921  17.552  12.800  1.00 67.49           C  
ANISOU 2890  C   ASN A 304     8540   8495   8607    478   -215    339       C  
ATOM   2891  O   ASN A 304      14.533  17.876  13.927  1.00 70.41           O  
ANISOU 2891  O   ASN A 304     8927   8842   8985    503   -221    331       O  
ATOM   2892  CB  ASN A 304      13.650  18.204  10.742  1.00 67.12           C  
ANISOU 2892  CB  ASN A 304     8453   8477   8571    415   -244    334       C  
ATOM   2893  CG  ASN A 304      13.024  19.441  10.137  1.00 80.50           C  
ANISOU 2893  CG  ASN A 304    10130  10179  10279    398   -296    344       C  
ATOM   2894  OD1 ASN A 304      13.123  20.532  10.709  1.00 93.30           O  
ANISOU 2894  OD1 ASN A 304    11762  11780  11908    415   -339    355       O  
ATOM   2895  ND2 ASN A 304      12.367  19.284   8.980  1.00 75.75           N  
ANISOU 2895  ND2 ASN A 304     9501   9604   9675    365   -290    340       N  
ATOM   2896  N   LEU A 305      15.434  16.350  12.533  1.00 67.70           N  
ANISOU 2896  N   LEU A 305     8573   8531   8619    481   -166    338       N  
ATOM   2897  CA  LEU A 305      15.655  15.367  13.582  1.00 62.23           C  
ANISOU 2897  CA  LEU A 305     7907   7820   7916    520   -118    331       C  
ATOM   2898  C   LEU A 305      16.537  15.940  14.685  1.00 74.77           C  
ANISOU 2898  C   LEU A 305     9501   9410   9500    550   -146    352       C  
ATOM   2899  O   LEU A 305      16.280  15.727  15.874  1.00 76.15           O  
ANISOU 2899  O   LEU A 305     9695   9562   9676    579   -130    343       O  
ATOM   2900  CB  LEU A 305      16.281  14.112  12.972  1.00 62.60           C  
ANISOU 2900  CB  LEU A 305     7962   7877   7945    522    -64    334       C  
ATOM   2901  CG  LEU A 305      16.641  12.937  13.877  1.00 68.33           C  
ANISOU 2901  CG  LEU A 305     8722   8584   8656    566     -6    333       C  
ATOM   2902  CD1 LEU A 305      15.450  12.529  14.714  1.00 68.04           C  
ANISOU 2902  CD1 LEU A 305     8713   8512   8627    574     24    303       C  
ATOM   2903  CD2 LEU A 305      17.151  11.766  13.047  1.00 61.46           C  
ANISOU 2903  CD2 LEU A 305     7864   7720   7768    565     50    334       C  
ATOM   2904  N   MET A 306      17.576  16.684  14.303  1.00 76.30           N  
ANISOU 2904  N   MET A 306     9676   9633   9682    538   -188    378       N  
ATOM   2905  CA  MET A 306      18.447  17.329  15.277  1.00 76.52           C  
ANISOU 2905  CA  MET A 306     9705   9673   9697    555   -217    397       C  
ATOM   2906  C   MET A 306      17.679  18.317  16.148  1.00 72.92           C  
ANISOU 2906  C   MET A 306     9260   9186   9259    555   -248    386       C  
ATOM   2907  O   MET A 306      18.015  18.500  17.322  1.00 74.05           O  
ANISOU 2907  O   MET A 306     9414   9327   9394    576   -250    391       O  
ATOM   2908  CB  MET A 306      19.611  18.023  14.556  1.00 80.16           C  
ANISOU 2908  CB  MET A 306    10143  10177  10136    528   -258    424       C  
ATOM   2909  CG  MET A 306      20.661  17.067  13.991  1.00 87.44           C  
ANISOU 2909  CG  MET A 306    11053  11138  11034    539   -228    439       C  
ATOM   2910  SD  MET A 306      21.200  15.839  15.207  1.00103.96           S  
ANISOU 2910  SD  MET A 306    13161  13231  13107    602   -170    447       S  
ATOM   2911  CE  MET A 306      20.451  14.326  14.592  1.00 99.91           C  
ANISOU 2911  CE  MET A 306    12669  12685  12606    616    -98    425       C  
ATOM   2912  N   ALA A 307      16.633  18.943  15.605  1.00 64.45           N  
ANISOU 2912  N   ALA A 307     8185   8094   8207    534   -269    371       N  
ATOM   2913  CA  ALA A 307      15.852  19.879  16.402  1.00 66.47           C  
ANISOU 2913  CA  ALA A 307     8455   8320   8481    540   -296    360       C  
ATOM   2914  C   ALA A 307      14.953  19.148  17.397  1.00 73.27           C  
ANISOU 2914  C   ALA A 307     9332   9156   9353    569   -256    334       C  
ATOM   2915  O   ALA A 307      14.843  19.561  18.557  1.00 79.09           O  
ANISOU 2915  O   ALA A 307    10083   9875  10094    585   -264    328       O  
ATOM   2916  CB  ALA A 307      15.023  20.776  15.491  1.00 58.77           C  
ANISOU 2916  CB  ALA A 307     7472   7337   7522    516   -330    356       C  
ATOM   2917  N   LYS A 308      14.289  18.074  16.953  1.00 61.45           N  
ANISOU 2917  N   LYS A 308     7834   7657   7857    569   -212    315       N  
ATOM   2918  CA  LYS A 308      13.445  17.292  17.848  1.00 59.68           C  
ANISOU 2918  CA  LYS A 308     7628   7411   7636    590   -171    288       C  
ATOM   2919  C   LYS A 308      14.261  16.700  18.997  1.00 57.72           C  
ANISOU 2919  C   LYS A 308     7397   7158   7375    620   -147    297       C  
ATOM   2920  O   LYS A 308      13.839  16.731  20.151  1.00 63.84           O  
ANISOU 2920  O   LYS A 308     8187   7915   8156    638   -142    284       O  
ATOM   2921  CB  LYS A 308      12.742  16.180  17.077  1.00 46.40           C  
ANISOU 2921  CB  LYS A 308     5948   5733   5948    576   -124    268       C  
ATOM   2922  CG  LYS A 308      11.561  16.607  16.257  1.00 53.21           C  
ANISOU 2922  CG  LYS A 308     6792   6604   6820    549   -137    251       C  
ATOM   2923  CD  LYS A 308      11.213  15.423  15.355  1.00 70.61           C  
ANISOU 2923  CD  LYS A 308     8997   8822   9009    524    -85    236       C  
ATOM   2924  CE  LYS A 308       9.943  15.601  14.534  1.00 82.83           C  
ANISOU 2924  CE  LYS A 308    10523  10392  10556    492    -87    217       C  
ATOM   2925  NZ  LYS A 308      10.179  16.358  13.285  1.00 85.18           N  
ANISOU 2925  NZ  LYS A 308    10789  10716  10859    466   -126    238       N  
ATOM   2926  N   LYS A 309      15.426  16.141  18.693  1.00 53.61           N  
ANISOU 2926  N   LYS A 309     6874   6660   6836    628   -132    321       N  
ATOM   2927  CA  LYS A 309      16.264  15.568  19.731  1.00 50.18           C  
ANISOU 2927  CA  LYS A 309     6451   6230   6384    662   -108    336       C  
ATOM   2928  C   LYS A 309      16.667  16.629  20.759  1.00 60.73           C  
ANISOU 2928  C   LYS A 309     7782   7573   7720    665   -149    348       C  
ATOM   2929  O   LYS A 309      16.753  16.341  21.958  1.00 66.72           O  
ANISOU 2929  O   LYS A 309     8552   8325   8473    689   -133    347       O  
ATOM   2930  CB  LYS A 309      17.498  14.910  19.087  1.00 47.81           C  
ANISOU 2930  CB  LYS A 309     6143   5962   6059    673    -89    364       C  
ATOM   2931  CG  LYS A 309      17.247  13.484  18.637  1.00 59.01           C  
ANISOU 2931  CG  LYS A 309     7583   7366   7471    686    -25    353       C  
ATOM   2932  CD  LYS A 309      17.988  13.143  17.357  1.00 74.95           C  
ANISOU 2932  CD  LYS A 309     9589   9413   9478    674    -16    368       C  
ATOM   2933  CE  LYS A 309      19.246  12.339  17.610  1.00 89.48           C  
ANISOU 2933  CE  LYS A 309    11433  11276  11290    717     16    397       C  
ATOM   2934  NZ  LYS A 309      19.038  11.330  18.688  1.00 97.21           N  
ANISOU 2934  NZ  LYS A 309    12448  12225  12261    761     69    392       N  
ATOM   2935  N   ARG A 310      16.918  17.858  20.303  1.00 59.24           N  
ANISOU 2935  N   ARG A 310     7579   7395   7534    638   -201    358       N  
ATOM   2936  CA  ARG A 310      17.320  18.938  21.196  1.00 56.49           C  
ANISOU 2936  CA  ARG A 310     7232   7051   7180    631   -238    368       C  
ATOM   2937  C   ARG A 310      16.204  19.253  22.190  1.00 67.43           C  
ANISOU 2937  C   ARG A 310     8634   8398   8589    639   -237    340       C  
ATOM   2938  O   ARG A 310      16.425  19.323  23.408  1.00 72.22           O  
ANISOU 2938  O   ARG A 310     9248   9004   9189    651   -233    340       O  
ATOM   2939  CB  ARG A 310      17.672  20.172  20.362  1.00 53.59           C  
ANISOU 2939  CB  ARG A 310     6855   6695   6810    594   -289    381       C  
ATOM   2940  CG  ARG A 310      18.701  21.092  20.936  1.00 70.22           C  
ANISOU 2940  CG  ARG A 310     8962   8828   8891    577   -321    402       C  
ATOM   2941  CD  ARG A 310      19.253  22.019  19.869  1.00 88.03           C  
ANISOU 2941  CD  ARG A 310    11211  11102  11133    537   -363    418       C  
ATOM   2942  NE  ARG A 310      20.136  21.302  18.942  1.00102.51           N  
ANISOU 2942  NE  ARG A 310    13022  12981  12946    535   -352    436       N  
ATOM   2943  CZ  ARG A 310      19.954  21.185  17.623  1.00101.32           C  
ANISOU 2943  CZ  ARG A 310    12860  12833  12804    518   -359    436       C  
ATOM   2944  NH1 ARG A 310      18.921  21.755  17.009  1.00 99.04           N  
ANISOU 2944  NH1 ARG A 310    12579  12508  12543    503   -378    421       N  
ATOM   2945  NH2 ARG A 310      20.831  20.497  16.911  1.00 96.96           N  
ANISOU 2945  NH2 ARG A 310    12287  12323  12230    518   -346    452       N  
ATOM   2946  N   VAL A 311      14.992  19.438  21.677  1.00 61.99           N  
ANISOU 2946  N   VAL A 311     7948   7682   7924    632   -241    315       N  
ATOM   2947  CA  VAL A 311      13.843  19.732  22.523  1.00 60.44           C  
ANISOU 2947  CA  VAL A 311     7764   7454   7747    641   -240    286       C  
ATOM   2948  C   VAL A 311      13.616  18.607  23.529  1.00 62.79           C  
ANISOU 2948  C   VAL A 311     8073   7745   8040    665   -195    271       C  
ATOM   2949  O   VAL A 311      13.447  18.847  24.730  1.00 64.97           O  
ANISOU 2949  O   VAL A 311     8358   8008   8319    674   -196    261       O  
ATOM   2950  CB  VAL A 311      12.607  19.960  21.645  1.00 52.80           C  
ANISOU 2950  CB  VAL A 311     6790   6473   6797    633   -247    266       C  
ATOM   2951  CG1 VAL A 311      11.341  19.858  22.471  1.00 46.19           C  
ANISOU 2951  CG1 VAL A 311     5961   5615   5974    648   -233    231       C  
ATOM   2952  CG2 VAL A 311      12.724  21.298  20.907  1.00 53.98           C  
ANISOU 2952  CG2 VAL A 311     6934   6621   6953    615   -297    281       C  
ATOM   2953  N   ILE A 312      13.632  17.361  23.052  1.00 58.25           N  
ANISOU 2953  N   ILE A 312     7501   7176   7455    673   -153    269       N  
ATOM   2954  CA  ILE A 312      13.387  16.228  23.930  1.00 58.63           C  
ANISOU 2954  CA  ILE A 312     7568   7213   7496    695   -106    255       C  
ATOM   2955  C   ILE A 312      14.409  16.188  25.067  1.00 65.05           C  
ANISOU 2955  C   ILE A 312     8383   8038   8294    715   -104    279       C  
ATOM   2956  O   ILE A 312      14.045  15.982  26.233  1.00 61.81           O  
ANISOU 2956  O   ILE A 312     7986   7614   7886    726    -91    264       O  
ATOM   2957  CB  ILE A 312      13.369  14.932  23.108  1.00 45.64           C  
ANISOU 2957  CB  ILE A 312     5934   5569   5838    697    -57    253       C  
ATOM   2958  CG1 ILE A 312      12.082  14.869  22.294  1.00 47.32           C  
ANISOU 2958  CG1 ILE A 312     6145   5773   6060    672    -51    222       C  
ATOM   2959  CG2 ILE A 312      13.474  13.721  23.987  1.00 48.75           C  
ANISOU 2959  CG2 ILE A 312     6356   5950   6216    723     -5    249       C  
ATOM   2960  CD1 ILE A 312      10.808  14.897  23.094  1.00 45.24           C  
ANISOU 2960  CD1 ILE A 312     5891   5492   5805    670    -44    185       C  
ATOM   2961  N   ARG A 313      15.694  16.427  24.761  1.00 71.43           N  
ANISOU 2961  N   ARG A 313     9177   8879   9084    716   -119    314       N  
ATOM   2962  CA  ARG A 313      16.706  16.428  25.820  1.00 67.47           C  
ANISOU 2962  CA  ARG A 313     8671   8404   8561    733   -119    340       C  
ATOM   2963  C   ARG A 313      16.490  17.579  26.800  1.00 62.08           C  
ANISOU 2963  C   ARG A 313     7986   7714   7887    715   -154    331       C  
ATOM   2964  O   ARG A 313      16.768  17.441  27.991  1.00 72.65           O  
ANISOU 2964  O   ARG A 313     9327   9063   9216    726   -144    336       O  
ATOM   2965  CB  ARG A 313      18.121  16.485  25.237  1.00 70.39           C  
ANISOU 2965  CB  ARG A 313     9020   8823   8902    734   -129    379       C  
ATOM   2966  CG  ARG A 313      18.948  17.644  25.800  1.00 87.80           C  
ANISOU 2966  CG  ARG A 313    11208  11062  11089    713   -170    399       C  
ATOM   2967  CD  ARG A 313      20.466  17.450  25.704  1.00100.17           C  
ANISOU 2967  CD  ARG A 313    12752  12695  12614    722   -170    440       C  
ATOM   2968  NE  ARG A 313      20.934  17.269  24.334  1.00107.50           N  
ANISOU 2968  NE  ARG A 313    13669  13642  13534    717   -174    453       N  
ATOM   2969  CZ  ARG A 313      20.911  18.221  23.405  1.00113.32           C  
ANISOU 2969  CZ  ARG A 313    14400  14380  14277    677   -214    449       C  
ATOM   2970  NH1 ARG A 313      20.427  19.424  23.694  1.00120.22           N  
ANISOU 2970  NH1 ARG A 313    15282  15230  15164    643   -252    435       N  
ATOM   2971  NH2 ARG A 313      21.359  17.966  22.180  1.00107.87           N  
ANISOU 2971  NH2 ARG A 313    13697  13710  13578    671   -215    460       N  
ATOM   2972  N   MET A 314      15.999  18.721  26.326  1.00 63.10           N  
ANISOU 2972  N   MET A 314     8114   7828   8034    687   -193    319       N  
ATOM   2973  CA  MET A 314      15.626  19.794  27.244  1.00 67.91           C  
ANISOU 2973  CA  MET A 314     8729   8419   8653    672   -220    305       C  
ATOM   2974  C   MET A 314      14.497  19.351  28.166  1.00 74.80           C  
ANISOU 2974  C   MET A 314     9616   9262   9545    687   -197    271       C  
ATOM   2975  O   MET A 314      14.540  19.583  29.379  1.00 84.97           O  
ANISOU 2975  O   MET A 314    10907  10548  10830    686   -197    265       O  
ATOM   2976  CB  MET A 314      15.208  21.036  26.463  1.00 65.08           C  
ANISOU 2976  CB  MET A 314     8375   8043   8310    647   -260    298       C  
ATOM   2977  CG  MET A 314      14.674  22.144  27.321  1.00 67.63           C  
ANISOU 2977  CG  MET A 314     8713   8338   8647    636   -283    280       C  
ATOM   2978  SD  MET A 314      13.956  23.445  26.295  1.00 71.67           S  
ANISOU 2978  SD  MET A 314     9236   8817   9178    621   -322    272       S  
ATOM   2979  CE  MET A 314      12.218  22.968  26.301  1.00 61.05           C  
ANISOU 2979  CE  MET A 314     7890   7442   7864    648   -304    232       C  
ATOM   2980  N   LEU A 315      13.479  18.695  27.610  1.00 72.76           N  
ANISOU 2980  N   LEU A 315     9362   8982   9301    696   -176    246       N  
ATOM   2981  CA  LEU A 315      12.347  18.283  28.432  1.00 67.18           C  
ANISOU 2981  CA  LEU A 315     8667   8251   8607    704   -156    210       C  
ATOM   2982  C   LEU A 315      12.761  17.252  29.480  1.00 62.51           C  
ANISOU 2982  C   LEU A 315     8085   7667   8000    722   -119    216       C  
ATOM   2983  O   LEU A 315      12.337  17.332  30.634  1.00 66.00           O  
ANISOU 2983  O   LEU A 315     8532   8098   8446    722   -116    197       O  
ATOM   2984  CB  LEU A 315      11.219  17.762  27.545  1.00 55.81           C  
ANISOU 2984  CB  LEU A 315     7230   6800   7177    703   -139    184       C  
ATOM   2985  CG  LEU A 315      10.551  18.894  26.753  1.00 61.48           C  
ANISOU 2985  CG  LEU A 315     7937   7511   7913    690   -177    175       C  
ATOM   2986  CD1 LEU A 315       9.555  18.359  25.737  1.00 57.51           C  
ANISOU 2986  CD1 LEU A 315     7428   7012   7411    685   -160    155       C  
ATOM   2987  CD2 LEU A 315       9.881  19.864  27.690  1.00 64.11           C  
ANISOU 2987  CD2 LEU A 315     8274   7825   8262    692   -200    154       C  
ATOM   2988  N   ILE A 316      13.590  16.283  29.103  1.00 57.96           N  
ANISOU 2988  N   ILE A 316     7510   7108   7402    738    -90    242       N  
ATOM   2989  CA  ILE A 316      14.042  15.309  30.081  1.00 59.66           C  
ANISOU 2989  CA  ILE A 316     7737   7331   7600    762    -54    253       C  
ATOM   2990  C   ILE A 316      14.884  15.994  31.152  1.00 70.78           C  
ANISOU 2990  C   ILE A 316     9130   8766   8997    759    -76    275       C  
ATOM   2991  O   ILE A 316      14.884  15.579  32.316  1.00 64.81           O  
ANISOU 2991  O   ILE A 316     8380   8012   8234    770    -58    273       O  
ATOM   2992  CB  ILE A 316      14.802  14.175  29.374  1.00 60.60           C  
ANISOU 2992  CB  ILE A 316     7864   7463   7697    787    -17    280       C  
ATOM   2993  CG1 ILE A 316      13.803  13.415  28.489  1.00 54.72           C  
ANISOU 2993  CG1 ILE A 316     7141   6689   6960    781     13    250       C  
ATOM   2994  CG2 ILE A 316      15.528  13.265  30.399  1.00 46.94           C  
ANISOU 2994  CG2 ILE A 316     6145   5748   5943    821     18    304       C  
ATOM   2995  CD1 ILE A 316      14.392  12.267  27.701  1.00 51.47           C  
ANISOU 2995  CD1 ILE A 316     6747   6282   6529    802     57    269       C  
ATOM   2996  N   VAL A 317      15.582  17.072  30.801  1.00 71.46           N  
ANISOU 2996  N   VAL A 317     9198   8875   9078    740   -115    295       N  
ATOM   2997  CA  VAL A 317      16.371  17.759  31.807  1.00 56.65           C  
ANISOU 2997  CA  VAL A 317     7309   7031   7186    727   -133    314       C  
ATOM   2998  C   VAL A 317      15.468  18.520  32.760  1.00 61.65           C  
ANISOU 2998  C   VAL A 317     7950   7635   7841    706   -148    280       C  
ATOM   2999  O   VAL A 317      15.739  18.604  33.966  1.00 67.14           O  
ANISOU 2999  O   VAL A 317     8640   8345   8525    700   -144    283       O  
ATOM   3000  CB  VAL A 317      17.403  18.662  31.124  1.00 51.61           C  
ANISOU 3000  CB  VAL A 317     6653   6429   6528    704   -166    343       C  
ATOM   3001  CG1 VAL A 317      17.717  19.854  31.994  1.00 53.45           C  
ANISOU 3001  CG1 VAL A 317     6882   6675   6751    669   -194    344       C  
ATOM   3002  CG2 VAL A 317      18.662  17.857  30.846  1.00 51.80           C  
ANISOU 3002  CG2 VAL A 317     6660   6506   6516    728   -146    385       C  
ATOM   3003  N   ILE A 318      14.374  19.067  32.242  1.00 55.73           N  
ANISOU 3003  N   ILE A 318     7211   6845   7120    696   -165    247       N  
ATOM   3004  CA  ILE A 318      13.452  19.826  33.076  1.00 57.28           C  
ANISOU 3004  CA  ILE A 318     7415   7012   7336    681   -179    213       C  
ATOM   3005  C   ILE A 318      12.746  18.901  34.072  1.00 71.40           C  
ANISOU 3005  C   ILE A 318     9210   8789   9129    695   -147    188       C  
ATOM   3006  O   ILE A 318      12.570  19.239  35.255  1.00 70.70           O  
ANISOU 3006  O   ILE A 318     9121   8698   9042    683   -150    174       O  
ATOM   3007  CB  ILE A 318      12.470  20.585  32.162  1.00 58.44           C  
ANISOU 3007  CB  ILE A 318     7569   7127   7510    676   -202    189       C  
ATOM   3008  CG1 ILE A 318      13.193  21.767  31.509  1.00 63.77           C  
ANISOU 3008  CG1 ILE A 318     8243   7808   8177    655   -237    212       C  
ATOM   3009  CG2 ILE A 318      11.207  21.040  32.896  1.00 48.56           C  
ANISOU 3009  CG2 ILE A 318     6326   5844   6281    675   -206    147       C  
ATOM   3010  CD1 ILE A 318      12.309  22.625  30.654  1.00 61.76           C  
ANISOU 3010  CD1 ILE A 318     7998   7522   7946    653   -262    195       C  
ATOM   3011  N   VAL A 319      12.365  17.707  33.616  1.00 71.70           N  
ANISOU 3011  N   VAL A 319     9257   8821   9166    716   -116    181       N  
ATOM   3012  CA  VAL A 319      11.674  16.750  34.469  1.00 64.01           C  
ANISOU 3012  CA  VAL A 319     8296   7834   8190    725    -83    156       C  
ATOM   3013  C   VAL A 319      12.597  16.252  35.580  1.00 65.32           C  
ANISOU 3013  C   VAL A 319     8459   8024   8334    734    -66    183       C  
ATOM   3014  O   VAL A 319      12.188  16.142  36.739  1.00 71.58           O  
ANISOU 3014  O   VAL A 319     9256   8813   9129    727    -58    164       O  
ATOM   3015  CB  VAL A 319      11.131  15.595  33.605  1.00 56.24           C  
ANISOU 3015  CB  VAL A 319     7330   6838   7202    738    -49    145       C  
ATOM   3016  CG1 VAL A 319      10.638  14.456  34.465  1.00 53.78           C  
ANISOU 3016  CG1 VAL A 319     7040   6514   6879    746     -9    125       C  
ATOM   3017  CG2 VAL A 319      10.033  16.086  32.682  1.00 56.04           C  
ANISOU 3017  CG2 VAL A 319     7302   6797   7195    725    -65    114       C  
ATOM   3018  N   VAL A 320      13.854  15.959  35.254  1.00 58.96           N  
ANISOU 3018  N   VAL A 320     7644   7252   7505    749    -59    229       N  
ATOM   3019  CA  VAL A 320      14.781  15.445  36.256  1.00 60.38           C  
ANISOU 3019  CA  VAL A 320     7816   7466   7658    764    -41    261       C  
ATOM   3020  C   VAL A 320      15.140  16.523  37.285  1.00 66.71           C  
ANISOU 3020  C   VAL A 320     8597   8293   8456    734    -69    264       C  
ATOM   3021  O   VAL A 320      15.265  16.234  38.477  1.00 66.98           O  
ANISOU 3021  O   VAL A 320     8628   8343   8480    733    -56    268       O  
ATOM   3022  CB  VAL A 320      16.029  14.867  35.569  1.00 56.47           C  
ANISOU 3022  CB  VAL A 320     7312   7009   7135    793    -26    310       C  
ATOM   3023  CG1 VAL A 320      17.090  14.502  36.608  1.00 49.75           C  
ANISOU 3023  CG1 VAL A 320     6444   6208   6250    811    -11    350       C  
ATOM   3024  CG2 VAL A 320      15.642  13.662  34.720  1.00 53.51           C  
ANISOU 3024  CG2 VAL A 320     6966   6605   6761    822     13    304       C  
ATOM   3025  N   LEU A 321      15.312  17.779  36.855  1.00 70.76           N  
ANISOU 3025  N   LEU A 321     9100   8809   8975    704   -106    263       N  
ATOM   3026  CA  LEU A 321      15.571  18.843  37.823  1.00 64.74           C  
ANISOU 3026  CA  LEU A 321     8327   8064   8208    668   -128    261       C  
ATOM   3027  C   LEU A 321      14.339  19.127  38.674  1.00 62.24           C  
ANISOU 3027  C   LEU A 321     8023   7706   7920    653   -129    213       C  
ATOM   3028  O   LEU A 321      14.462  19.628  39.797  1.00 68.02           O  
ANISOU 3028  O   LEU A 321     8747   8451   8646    627   -134    208       O  
ATOM   3029  CB  LEU A 321      16.029  20.126  37.119  1.00 58.39           C  
ANISOU 3029  CB  LEU A 321     7520   7266   7400    637   -163    270       C  
ATOM   3030  CG  LEU A 321      17.389  20.061  36.424  1.00 70.68           C  
ANISOU 3030  CG  LEU A 321     9059   8877   8921    640   -167    317       C  
ATOM   3031  CD1 LEU A 321      17.821  21.422  35.904  1.00 74.22           C  
ANISOU 3031  CD1 LEU A 321     9509   9331   9359    598   -202    322       C  
ATOM   3032  CD2 LEU A 321      18.458  19.469  37.333  1.00 68.48           C  
ANISOU 3032  CD2 LEU A 321     8754   8663   8600    648   -147    354       C  
ATOM   3033  N   PHE A 322      13.151  18.817  38.154  1.00 56.78           N  
ANISOU 3033  N   PHE A 322     7348   6971   7256    667   -125    177       N  
ATOM   3034  CA  PHE A 322      11.910  18.996  38.910  1.00 52.92           C  
ANISOU 3034  CA  PHE A 322     6868   6449   6789    657   -125    129       C  
ATOM   3035  C   PHE A 322      11.831  18.018  40.071  1.00 55.56           C  
ANISOU 3035  C   PHE A 322     7203   6794   7113    662    -96    124       C  
ATOM   3036  O   PHE A 322      11.639  18.424  41.218  1.00 53.27           O  
ANISOU 3036  O   PHE A 322     6907   6507   6826    640   -101    107       O  
ATOM   3037  CB  PHE A 322      10.719  18.801  37.985  1.00 45.46           C  
ANISOU 3037  CB  PHE A 322     5936   5470   5867    671   -124     96       C  
ATOM   3038  CG  PHE A 322       9.387  18.967  38.634  1.00 45.22           C  
ANISOU 3038  CG  PHE A 322     5911   5416   5856    664   -125     45       C  
ATOM   3039  CD1 PHE A 322       8.888  20.230  38.915  1.00 45.57           C  
ANISOU 3039  CD1 PHE A 322     5954   5442   5919    649   -152     22       C  
ATOM   3040  CD2 PHE A 322       8.588  17.863  38.894  1.00 44.85           C  
ANISOU 3040  CD2 PHE A 322     5874   5363   5805    672    -97     18       C  
ATOM   3041  CE1 PHE A 322       7.620  20.389  39.504  1.00 45.54           C  
ANISOU 3041  CE1 PHE A 322     5952   5420   5930    647   -153    -27       C  
ATOM   3042  CE2 PHE A 322       7.317  18.021  39.478  1.00 47.48           C  
ANISOU 3042  CE2 PHE A 322     6209   5682   6152    663   -100    -32       C  
ATOM   3043  CZ  PHE A 322       6.842  19.283  39.777  1.00 45.12           C  
ANISOU 3043  CZ  PHE A 322     5902   5370   5872    653   -128    -54       C  
ATOM   3044  N   PHE A 323      11.982  16.721  39.779  1.00 58.17           N  
ANISOU 3044  N   PHE A 323     7543   7128   7429    691    -65    139       N  
ATOM   3045  CA  PHE A 323      11.940  15.691  40.806  1.00 57.94           C  
ANISOU 3045  CA  PHE A 323     7522   7107   7386    700    -34    139       C  
ATOM   3046  C   PHE A 323      13.058  15.868  41.823  1.00 66.99           C  
ANISOU 3046  C   PHE A 323     8646   8299   8510    692    -35    176       C  
ATOM   3047  O   PHE A 323      12.851  15.657  43.018  1.00 84.33           O  
ANISOU 3047  O   PHE A 323    10839  10501  10702    680    -26    166       O  
ATOM   3048  CB  PHE A 323      12.024  14.309  40.163  1.00 57.99           C  
ANISOU 3048  CB  PHE A 323     7552   7104   7377    734      4    154       C  
ATOM   3049  CG  PHE A 323      10.693  13.748  39.716  1.00 76.95           C  
ANISOU 3049  CG  PHE A 323     9980   9466   9791    732     20    106       C  
ATOM   3050  CD1 PHE A 323       9.851  14.478  38.886  1.00 86.26           C  
ANISOU 3050  CD1 PHE A 323    11156  10629  10992    718     -4     75       C  
ATOM   3051  CD2 PHE A 323      10.293  12.474  40.108  1.00 85.89           C  
ANISOU 3051  CD2 PHE A 323    11144  10584  10907    742     60     95       C  
ATOM   3052  CE1 PHE A 323       8.622  13.962  38.463  1.00 87.65           C  
ANISOU 3052  CE1 PHE A 323    11350  10782  11171    712     12     32       C  
ATOM   3053  CE2 PHE A 323       9.067  11.949  39.690  1.00 92.42           C  
ANISOU 3053  CE2 PHE A 323    11997  11383  11737    731     78     50       C  
ATOM   3054  CZ  PHE A 323       8.231  12.701  38.857  1.00 89.93           C  
ANISOU 3054  CZ  PHE A 323    11669  11060  11440    714     53     18       C  
ATOM   3055  N   LEU A 324      14.248  16.254  41.373  1.00 67.40           N  
ANISOU 3055  N   LEU A 324     8678   8388   8541    696    -46    221       N  
ATOM   3056  CA  LEU A 324      15.358  16.432  42.304  1.00 59.53           C  
ANISOU 3056  CA  LEU A 324     7655   7450   7514    685    -46    259       C  
ATOM   3057  C   LEU A 324      15.130  17.625  43.221  1.00 60.75           C  
ANISOU 3057  C   LEU A 324     7797   7608   7677    634    -70    235       C  
ATOM   3058  O   LEU A 324      15.676  17.668  44.326  1.00 63.53           O  
ANISOU 3058  O   LEU A 324     8129   8004   8007    615    -65    252       O  
ATOM   3059  CB  LEU A 324      16.677  16.605  41.539  1.00 58.29           C  
ANISOU 3059  CB  LEU A 324     7479   7343   7327    697    -52    310       C  
ATOM   3060  CG  LEU A 324      17.397  15.368  41.005  1.00 65.58           C  
ANISOU 3060  CG  LEU A 324     8403   8288   8225    751    -21    352       C  
ATOM   3061  CD1 LEU A 324      18.250  15.758  39.854  1.00 68.47           C  
ANISOU 3061  CD1 LEU A 324     8757   8683   8576    756    -36    381       C  
ATOM   3062  CD2 LEU A 324      18.279  14.777  42.080  1.00 81.51           C  
ANISOU 3062  CD2 LEU A 324    10400  10365  10205    768      0    394       C  
ATOM   3063  N   CYS A 325      14.340  18.600  42.782  1.00 58.67           N  
ANISOU 3063  N   CYS A 325     7547   7304   7444    612    -95    197       N  
ATOM   3064  CA  CYS A 325      14.051  19.759  43.615  1.00 58.82           C  
ANISOU 3064  CA  CYS A 325     7562   7316   7472    565   -114    170       C  
ATOM   3065  C   CYS A 325      12.898  19.519  44.585  1.00 57.44           C  
ANISOU 3065  C   CYS A 325     7395   7110   7319    557   -105    124       C  
ATOM   3066  O   CYS A 325      12.772  20.261  45.565  1.00 73.08           O  
ANISOU 3066  O   CYS A 325     9369   9095   9302    519   -113    105       O  
ATOM   3067  CB  CYS A 325      13.750  20.969  42.727  1.00 54.78           C  
ANISOU 3067  CB  CYS A 325     7065   6771   6979    550   -142    154       C  
ATOM   3068  SG  CYS A 325      15.245  21.751  42.010  1.00 71.65           S  
ANISOU 3068  SG  CYS A 325     9190   8953   9078    529   -159    203       S  
ATOM   3069  N   TRP A 326      12.063  18.505  44.334  1.00 53.57           N  
ANISOU 3069  N   TRP A 326     6919   6593   6842    588    -88    103       N  
ATOM   3070  CA  TRP A 326      10.838  18.267  45.083  1.00 54.15           C  
ANISOU 3070  CA  TRP A 326     7002   6637   6935    579    -82     52       C  
ATOM   3071  C   TRP A 326      10.865  16.995  45.908  1.00 56.94           C  
ANISOU 3071  C   TRP A 326     7358   7006   7271    590    -52     59       C  
ATOM   3072  O   TRP A 326      10.087  16.886  46.857  1.00 58.72           O  
ANISOU 3072  O   TRP A 326     7585   7222   7505    570    -48     22       O  
ATOM   3073  CB  TRP A 326       9.625  18.208  44.142  1.00 45.97           C  
ANISOU 3073  CB  TRP A 326     5984   5558   5923    597    -86     13       C  
ATOM   3074  CG  TRP A 326       9.181  19.582  43.717  1.00 59.41           C  
ANISOU 3074  CG  TRP A 326     7687   7237   7648    584   -116    -10       C  
ATOM   3075  CD1 TRP A 326       9.262  20.129  42.450  1.00 60.27           C  
ANISOU 3075  CD1 TRP A 326     7802   7332   7765    598   -132      2       C  
ATOM   3076  CD2 TRP A 326       8.612  20.596  44.557  1.00 59.97           C  
ANISOU 3076  CD2 TRP A 326     7756   7294   7735    556   -131    -45       C  
ATOM   3077  NE1 TRP A 326       8.762  21.419  42.462  1.00 61.88           N  
ANISOU 3077  NE1 TRP A 326     8011   7512   7988    584   -156    -23       N  
ATOM   3078  CE2 TRP A 326       8.361  21.728  43.742  1.00 60.52           C  
ANISOU 3078  CE2 TRP A 326     7836   7338   7822    560   -154    -52       C  
ATOM   3079  CE3 TRP A 326       8.278  20.652  45.917  1.00 63.07           C  
ANISOU 3079  CE3 TRP A 326     8142   7693   8129    529   -125    -72       C  
ATOM   3080  CZ2 TRP A 326       7.795  22.899  44.249  1.00 54.30           C  
ANISOU 3080  CZ2 TRP A 326     7055   6525   7051    541   -168    -84       C  
ATOM   3081  CZ3 TRP A 326       7.724  21.818  46.422  1.00 58.47           C  
ANISOU 3081  CZ3 TRP A 326     7562   7088   7564    506   -141   -106       C  
ATOM   3082  CH2 TRP A 326       7.487  22.926  45.586  1.00 58.85           C  
ANISOU 3082  CH2 TRP A 326     7625   7107   7629    515   -160   -112       C  
ATOM   3083  N   MET A 327      11.703  16.027  45.552  1.00 61.24           N  
ANISOU 3083  N   MET A 327     7905   7572   7791    622    -30    104       N  
ATOM   3084  CA  MET A 327      11.863  14.856  46.401  1.00 59.66           C  
ANISOU 3084  CA  MET A 327     7711   7386   7570    636      1    119       C  
ATOM   3085  C   MET A 327      12.282  15.229  47.817  1.00 66.32           C  
ANISOU 3085  C   MET A 327     8528   8269   8402    603     -4    127       C  
ATOM   3086  O   MET A 327      11.703  14.669  48.764  1.00 60.79           O  
ANISOU 3086  O   MET A 327     7834   7561   7700    592     10    104       O  
ATOM   3087  CB  MET A 327      12.873  13.878  45.786  1.00 61.29           C  
ANISOU 3087  CB  MET A 327     7924   7613   7748    682     27    174       C  
ATOM   3088  CG  MET A 327      12.308  12.510  45.463  1.00 88.92           C  
ANISOU 3088  CG  MET A 327    11465  11077  11242    714     63    164       C  
ATOM   3089  SD  MET A 327      11.927  12.257  43.710  1.00124.07           S  
ANISOU 3089  SD  MET A 327    15944  15492  15706    738     70    154       S  
ATOM   3090  CE  MET A 327      13.556  12.353  42.957  1.00112.19           C  
ANISOU 3090  CE  MET A 327    14417  14031  14178    772     68    224       C  
ATOM   3091  N   PRO A 328      13.246  16.127  48.047  1.00 62.00           N  
ANISOU 3091  N   PRO A 328     7951   7766   7841    580    -21    157       N  
ATOM   3092  CA  PRO A 328      13.714  16.297  49.424  1.00 59.54           C  
ANISOU 3092  CA  PRO A 328     7612   7500   7509    547    -18    170       C  
ATOM   3093  C   PRO A 328      12.614  16.757  50.369  1.00 61.04           C  
ANISOU 3093  C   PRO A 328     7805   7662   7725    504    -27    112       C  
ATOM   3094  O   PRO A 328      12.426  16.139  51.424  1.00 62.19           O  
ANISOU 3094  O   PRO A 328     7946   7822   7862    494    -13    107       O  
ATOM   3095  CB  PRO A 328      14.855  17.319  49.273  1.00 57.32           C  
ANISOU 3095  CB  PRO A 328     7302   7270   7206    521    -36    206       C  
ATOM   3096  CG  PRO A 328      15.337  17.141  47.912  1.00 59.60           C  
ANISOU 3096  CG  PRO A 328     7601   7556   7490    561    -37    234       C  
ATOM   3097  CD  PRO A 328      14.103  16.874  47.107  1.00 63.91           C  
ANISOU 3097  CD  PRO A 328     8182   8028   8074    582    -38    188       C  
ATOM   3098  N   ILE A 329      11.847  17.791  50.007  1.00 55.99           N  
ANISOU 3098  N   ILE A 329     7174   6983   7115    482    -50     67       N  
ATOM   3099  CA  ILE A 329      10.854  18.298  50.948  1.00 52.08           C  
ANISOU 3099  CA  ILE A 329     6680   6467   6642    443    -58     12       C  
ATOM   3100  C   ILE A 329       9.713  17.297  51.120  1.00 61.83           C  
ANISOU 3100  C   ILE A 329     7934   7670   7889    460    -44    -27       C  
ATOM   3101  O   ILE A 329       9.185  17.130  52.228  1.00 71.56           O  
ANISOU 3101  O   ILE A 329     9160   8906   9122    431    -40    -57       O  
ATOM   3102  CB  ILE A 329      10.350  19.692  50.521  1.00 50.93           C  
ANISOU 3102  CB  ILE A 329     6542   6287   6523    422    -82    -23       C  
ATOM   3103  CG1 ILE A 329       9.394  20.287  51.573  1.00 58.38           C  
ANISOU 3103  CG1 ILE A 329     7484   7212   7486    383    -88    -79       C  
ATOM   3104  CG2 ILE A 329       9.626  19.644  49.205  1.00 47.58           C  
ANISOU 3104  CG2 ILE A 329     6140   5818   6120    461    -90    -41       C  
ATOM   3105  CD1 ILE A 329       9.954  20.340  52.983  1.00 59.64           C  
ANISOU 3105  CD1 ILE A 329     7618   7417   7626    335    -79    -69       C  
ATOM   3106  N   PHE A 330       9.323  16.595  50.050  1.00 52.28           N  
ANISOU 3106  N   PHE A 330     6749   6432   6683    500    -36    -29       N  
ATOM   3107  CA  PHE A 330       8.283  15.589  50.226  1.00 47.76           C  
ANISOU 3107  CA  PHE A 330     6199   5836   6113    508    -19    -66       C  
ATOM   3108  C   PHE A 330       8.783  14.416  51.065  1.00 52.14           C  
ANISOU 3108  C   PHE A 330     6757   6414   6638    514      9    -37       C  
ATOM   3109  O   PHE A 330       8.025  13.836  51.852  1.00 64.63           O  
ANISOU 3109  O   PHE A 330     8351   7988   8218    497     20    -71       O  
ATOM   3110  CB  PHE A 330       7.743  15.120  48.877  1.00 46.87           C  
ANISOU 3110  CB  PHE A 330     6113   5692   6005    542    -12    -76       C  
ATOM   3111  CG  PHE A 330       6.688  16.030  48.315  1.00 45.92           C  
ANISOU 3111  CG  PHE A 330     5991   5545   5911    534    -36   -125       C  
ATOM   3112  CD1 PHE A 330       7.042  17.200  47.667  1.00 60.92           C  
ANISOU 3112  CD1 PHE A 330     7879   7440   7826    536    -60   -113       C  
ATOM   3113  CD2 PHE A 330       5.359  15.733  48.461  1.00 45.77           C  
ANISOU 3113  CD2 PHE A 330     5983   5511   5898    525    -33   -182       C  
ATOM   3114  CE1 PHE A 330       6.076  18.050  47.152  1.00 59.14           C  
ANISOU 3114  CE1 PHE A 330     7655   7191   7624    537    -80   -154       C  
ATOM   3115  CE2 PHE A 330       4.392  16.579  47.975  1.00 48.96           C  
ANISOU 3115  CE2 PHE A 330     6381   5898   6322    524    -54   -223       C  
ATOM   3116  CZ  PHE A 330       4.752  17.743  47.315  1.00 50.04           C  
ANISOU 3116  CZ  PHE A 330     6508   6027   6477    534    -77   -207       C  
ATOM   3117  N   SER A 331      10.052  14.072  50.938  1.00 48.20           N  
ANISOU 3117  N   SER A 331     6249   5948   6116    539     21     26       N  
ATOM   3118  CA  SER A 331      10.619  13.014  51.766  1.00 55.65           C  
ANISOU 3118  CA  SER A 331     7196   6919   7030    552     48     63       C  
ATOM   3119  C   SER A 331      10.800  13.453  53.212  1.00 62.55           C  
ANISOU 3119  C   SER A 331     8037   7832   7898    506     40     60       C  
ATOM   3120  O   SER A 331      10.802  12.610  54.113  1.00 67.29           O  
ANISOU 3120  O   SER A 331     8642   8445   8480    505     59     69       O  
ATOM   3121  CB  SER A 331      11.959  12.571  51.193  1.00 53.15           C  
ANISOU 3121  CB  SER A 331     6874   6635   6686    598     64    134       C  
ATOM   3122  OG  SER A 331      11.766  12.207  49.829  1.00 61.35           O  
ANISOU 3122  OG  SER A 331     7942   7637   7732    635     72    133       O  
ATOM   3123  N   ALA A 332      10.984  14.750  53.458  1.00 57.68           N  
ANISOU 3123  N   ALA A 332     7389   7233   7293    467     14     50       N  
ATOM   3124  CA  ALA A 332      11.108  15.209  54.833  1.00 56.61           C  
ANISOU 3124  CA  ALA A 332     7223   7134   7151    415      8     43       C  
ATOM   3125  C   ALA A 332       9.747  15.222  55.528  1.00 49.58           C  
ANISOU 3125  C   ALA A 332     6344   6208   6284    382      3    -27       C  
ATOM   3126  O   ALA A 332       9.639  14.812  56.682  1.00 58.58           O  
ANISOU 3126  O   ALA A 332     7474   7370   7413    355     11    -33       O  
ATOM   3127  CB  ALA A 332      11.769  16.589  54.879  1.00 50.54           C  
ANISOU 3127  CB  ALA A 332     6425   6396   6383    377    -12     53       C  
ATOM   3128  N   ASN A 333       8.694  15.641  54.831  1.00 54.59           N  
ANISOU 3128  N   ASN A 333     6998   6794   6948    385    -10    -80       N  
ATOM   3129  CA  ASN A 333       7.352  15.533  55.397  1.00 54.38           C  
ANISOU 3129  CA  ASN A 333     6982   6741   6938    360    -14   -147       C  
ATOM   3130  C   ASN A 333       6.942  14.078  55.620  1.00 55.42           C  
ANISOU 3130  C   ASN A 333     7141   6865   7050    375     11   -150       C  
ATOM   3131  O   ASN A 333       6.335  13.754  56.641  1.00 67.32           O  
ANISOU 3131  O   ASN A 333     8648   8377   8554    342     14   -184       O  
ATOM   3132  CB  ASN A 333       6.349  16.251  54.506  1.00 47.59           C  
ANISOU 3132  CB  ASN A 333     6135   5840   6106    368    -32   -196       C  
ATOM   3133  CG  ASN A 333       6.578  17.745  54.486  1.00 59.85           C  
ANISOU 3133  CG  ASN A 333     7669   7392   7678    346    -54   -202       C  
ATOM   3134  OD1 ASN A 333       7.068  18.316  55.475  1.00 59.71           O  
ANISOU 3134  OD1 ASN A 333     7629   7401   7656    305    -57   -195       O  
ATOM   3135  ND2 ASN A 333       6.244  18.401  53.359  1.00 47.36           N  
ANISOU 3135  ND2 ASN A 333     6099   5780   6115    371    -68   -213       N  
ATOM   3136  N   ALA A 334       7.261  13.180  54.698  1.00 52.69           N  
ANISOU 3136  N   ALA A 334     6825   6506   6690    422     31   -118       N  
ATOM   3137  CA  ALA A 334       6.868  11.793  54.907  1.00 49.35           C  
ANISOU 3137  CA  ALA A 334     6439   6067   6244    434     60   -122       C  
ATOM   3138  C   ALA A 334       7.601  11.202  56.104  1.00 55.28           C  
ANISOU 3138  C   ALA A 334     7179   6854   6970    426     75    -83       C  
ATOM   3139  O   ALA A 334       7.034  10.412  56.865  1.00 61.14           O  
ANISOU 3139  O   ALA A 334     7942   7590   7699    407     90   -106       O  
ATOM   3140  CB  ALA A 334       7.144  10.969  53.648  1.00 49.03           C  
ANISOU 3140  CB  ALA A 334     6436   6002   6191    487     83    -92       C  
ATOM   3141  N   TRP A 335       8.869  11.568  56.280  1.00 59.64           N  
ANISOU 3141  N   TRP A 335     7699   7450   7512    437     73    -23       N  
ATOM   3142  CA  TRP A 335       9.640  11.043  57.399  1.00 60.34           C  
ANISOU 3142  CA  TRP A 335     7770   7584   7572    432     88     22       C  
ATOM   3143  C   TRP A 335       9.114  11.597  58.723  1.00 62.19           C  
ANISOU 3143  C   TRP A 335     7974   7839   7816    365     71    -20       C  
ATOM   3144  O   TRP A 335       9.084  10.883  59.736  1.00 60.90           O  
ANISOU 3144  O   TRP A 335     7812   7693   7633    350     85    -13       O  
ATOM   3145  CB  TRP A 335      11.123  11.371  57.189  1.00 56.53           C  
ANISOU 3145  CB  TRP A 335     7252   7155   7070    458     88     96       C  
ATOM   3146  CG  TRP A 335      12.088  10.748  58.173  1.00 71.65           C  
ANISOU 3146  CG  TRP A 335     9145   9130   8947    467    107    157       C  
ATOM   3147  CD1 TRP A 335      11.905   9.615  58.911  1.00 83.57           C  
ANISOU 3147  CD1 TRP A 335    10679  10636  10437    478    132    167       C  
ATOM   3148  CD2 TRP A 335      13.384  11.246  58.524  1.00 69.01           C  
ANISOU 3148  CD2 TRP A 335     8758   8874   8587    464    103    218       C  
ATOM   3149  NE1 TRP A 335      13.009   9.374  59.693  1.00 85.73           N  
ANISOU 3149  NE1 TRP A 335    10917  10981  10676    488    143    233       N  
ATOM   3150  CE2 TRP A 335      13.931  10.361  59.473  1.00 75.56           C  
ANISOU 3150  CE2 TRP A 335     9578   9748   9381    479    126    265       C  
ATOM   3151  CE3 TRP A 335      14.138  12.348  58.119  1.00 57.76           C  
ANISOU 3151  CE3 TRP A 335     7296   7490   7160    448     84    237       C  
ATOM   3152  CZ2 TRP A 335      15.202  10.542  60.017  1.00 69.68           C  
ANISOU 3152  CZ2 TRP A 335     8781   9096   8599    480    129    332       C  
ATOM   3153  CZ3 TRP A 335      15.388  12.534  58.671  1.00 64.53           C  
ANISOU 3153  CZ3 TRP A 335     8104   8437   7978    442     88    300       C  
ATOM   3154  CH2 TRP A 335      15.912  11.633  59.608  1.00 64.99           C  
ANISOU 3154  CH2 TRP A 335     8147   8547   8001    459    110    348       C  
ATOM   3155  N   ARG A 336       8.668  12.854  58.720  1.00 59.63           N  
ANISOU 3155  N   ARG A 336     7627   7510   7521    325     43    -63       N  
ATOM   3156  CA  ARG A 336       8.047  13.451  59.894  1.00 62.61           C  
ANISOU 3156  CA  ARG A 336     7978   7899   7910    261     28   -112       C  
ATOM   3157  C   ARG A 336       6.775  12.701  60.284  1.00 66.40           C  
ANISOU 3157  C   ARG A 336     8489   8348   8393    246     34   -171       C  
ATOM   3158  O   ARG A 336       6.550  12.414  61.461  1.00 77.46           O  
ANISOU 3158  O   ARG A 336     9878   9770   9784    205     36   -186       O  
ATOM   3159  CB  ARG A 336       7.750  14.914  59.595  1.00 59.35           C  
ANISOU 3159  CB  ARG A 336     7547   7474   7527    234      3   -149       C  
ATOM   3160  CG  ARG A 336       7.784  15.917  60.731  1.00 54.77           C  
ANISOU 3160  CG  ARG A 336     6930   6924   6954    168    -10   -171       C  
ATOM   3161  CD  ARG A 336       7.345  17.165  60.032  1.00 54.26           C  
ANISOU 3161  CD  ARG A 336     6871   6826   6920    164    -29   -208       C  
ATOM   3162  NE  ARG A 336       7.542  18.427  60.706  1.00 66.56           N  
ANISOU 3162  NE  ARG A 336     8404   8400   8486    108    -38   -224       N  
ATOM   3163  CZ  ARG A 336       7.091  19.559  60.176  1.00 67.99           C  
ANISOU 3163  CZ  ARG A 336     8596   8544   8692    105    -52   -259       C  
ATOM   3164  NH1 ARG A 336       6.453  19.493  59.016  1.00 63.03           N  
ANISOU 3164  NH1 ARG A 336     7996   7871   8083    155    -60   -276       N  
ATOM   3165  NH2 ARG A 336       7.265  20.733  60.774  1.00 68.71           N  
ANISOU 3165  NH2 ARG A 336     8674   8644   8790     53    -56   -275       N  
ATOM   3166  N   ALA A 337       5.945  12.343  59.311  1.00 57.88           N  
ANISOU 3166  N   ALA A 337     7447   7222   7322    273     37   -204       N  
ATOM   3167  CA  ALA A 337       4.725  11.629  59.641  1.00 55.18           C  
ANISOU 3167  CA  ALA A 337     7134   6857   6974    253     43   -262       C  
ATOM   3168  C   ALA A 337       4.976  10.210  60.125  1.00 58.78           C  
ANISOU 3168  C   ALA A 337     7624   7316   7395    263     73   -232       C  
ATOM   3169  O   ALA A 337       4.076   9.610  60.712  1.00 64.93           O  
ANISOU 3169  O   ALA A 337     8424   8085   8162    231     79   -278       O  
ATOM   3170  CB  ALA A 337       3.792  11.579  58.434  1.00 49.53           C  
ANISOU 3170  CB  ALA A 337     6449   6102   6268    276     42   -303       C  
ATOM   3171  N   TYR A 338       6.140   9.637  59.865  1.00 64.82           N  
ANISOU 3171  N   TYR A 338     8397   8092   8140    308     94   -158       N  
ATOM   3172  CA  TYR A 338       6.379   8.256  60.269  1.00 72.55           C  
ANISOU 3172  CA  TYR A 338     9416   9066   9083    328    128   -126       C  
ATOM   3173  C   TYR A 338       7.228   8.138  61.534  1.00 76.01           C  
ANISOU 3173  C   TYR A 338     9820   9556   9503    313    131    -79       C  
ATOM   3174  O   TYR A 338       7.085   7.165  62.280  1.00 84.58           O  
ANISOU 3174  O   TYR A 338    10934  10641  10563    306    152    -73       O  
ATOM   3175  CB  TYR A 338       7.048   7.478  59.125  1.00 65.97           C  
ANISOU 3175  CB  TYR A 338     8624   8208   8233    399    157    -72       C  
ATOM   3176  CG  TYR A 338       6.105   6.853  58.108  1.00 65.27           C  
ANISOU 3176  CG  TYR A 338     8594   8064   8141    411    174   -115       C  
ATOM   3177  CD1 TYR A 338       5.687   7.556  56.966  1.00 68.63           C  
ANISOU 3177  CD1 TYR A 338     9013   8471   8591    418    157   -144       C  
ATOM   3178  CD2 TYR A 338       5.665   5.550  58.262  1.00 61.52           C  
ANISOU 3178  CD2 TYR A 338     8183   7557   7633    414    210   -123       C  
ATOM   3179  CE1 TYR A 338       4.833   6.977  56.031  1.00 67.06           C  
ANISOU 3179  CE1 TYR A 338     8865   8232   8384    425    174   -181       C  
ATOM   3180  CE2 TYR A 338       4.825   4.964  57.334  1.00 64.50           C  
ANISOU 3180  CE2 TYR A 338     8618   7890   8000    417    229   -163       C  
ATOM   3181  CZ  TYR A 338       4.412   5.670  56.222  1.00 67.79           C  
ANISOU 3181  CZ  TYR A 338     9021   8297   8441    421    212   -191       C  
ATOM   3182  OH  TYR A 338       3.572   5.056  55.311  1.00 66.94           O  
ANISOU 3182  OH  TYR A 338     8965   8154   8317    418    234   -229       O  
ATOM   3183  N   ASP A 339       8.092   9.112  61.788  1.00 65.28           N  
ANISOU 3183  N   ASP A 339     8403   8246   8153    303    113    -46       N  
ATOM   3184  CA  ASP A 339       9.044   9.113  62.866  1.00 61.58           C  
ANISOU 3184  CA  ASP A 339     7893   7842   7664    289    117      7       C  
ATOM   3185  C   ASP A 339       9.399  10.578  63.114  1.00 67.36           C  
ANISOU 3185  C   ASP A 339     8564   8614   8415    244     88     -1       C  
ATOM   3186  O   ASP A 339      10.518  11.035  62.883  1.00 71.11           O  
ANISOU 3186  O   ASP A 339     9005   9134   8877    261     87     55       O  
ATOM   3187  CB  ASP A 339      10.285   8.285  62.534  1.00 60.40           C  
ANISOU 3187  CB  ASP A 339     7753   7717   7479    359    145     96       C  
ATOM   3188  CG  ASP A 339      11.160   8.048  63.760  1.00 74.84           C  
ANISOU 3188  CG  ASP A 339     9541   9618   9276    347    153    153       C  
ATOM   3189  OD1 ASP A 339      11.381   8.992  64.545  1.00 76.69           O  
ANISOU 3189  OD1 ASP A 339     9716   9906   9516    289    132    146       O  
ATOM   3190  OD2 ASP A 339      11.599   6.900  63.958  1.00 81.49           O  
ANISOU 3190  OD2 ASP A 339    10412  10464  10086    395    184    204       O  
ATOM   3191  N   THR A 340       8.417  11.321  63.614  1.00 54.05           N  
ANISOU 3191  N   THR A 340     6866   6915   6757    183     66    -73       N  
ATOM   3192  CA  THR A 340       8.562  12.764  63.738  1.00 56.45           C  
ANISOU 3192  CA  THR A 340     7127   7240   7082    140     43    -92       C  
ATOM   3193  C   THR A 340       9.764  13.147  64.591  1.00 63.49           C  
ANISOU 3193  C   THR A 340     7966   8210   7948    110     46    -36       C  
ATOM   3194  O   THR A 340      10.506  14.069  64.233  1.00 74.34           O  
ANISOU 3194  O   THR A 340     9314   9611   9321    104     38    -12       O  
ATOM   3195  CB  THR A 340       7.258  13.352  64.282  1.00 61.62           C  
ANISOU 3195  CB  THR A 340     7780   7867   7765     83     24   -180       C  
ATOM   3196  OG1 THR A 340       7.531  14.336  65.293  1.00 68.80           O  
ANISOU 3196  OG1 THR A 340     8641   8820   8678     17     13   -189       O  
ATOM   3197  CG2 THR A 340       6.372  12.235  64.824  1.00 63.71           C  
ANISOU 3197  CG2 THR A 340     8075   8113   8020     74     34   -213       C  
ATOM   3198  N   ALA A 341      10.007  12.426  65.692  1.00 57.80           N  
ANISOU 3198  N   ALA A 341     7230   7531   7201     91     58    -12       N  
ATOM   3199  CA  ALA A 341      11.126  12.778  66.569  1.00 63.66           C  
ANISOU 3199  CA  ALA A 341     7914   8359   7912     57     62     43       C  
ATOM   3200  C   ALA A 341      12.475  12.672  65.845  1.00 73.53           C  
ANISOU 3200  C   ALA A 341     9151   9655   9132    114     74    126       C  
ATOM   3201  O   ALA A 341      13.315  13.572  65.963  1.00 77.33           O  
ANISOU 3201  O   ALA A 341     9588  10195   9598     82     68    153       O  
ATOM   3202  CB  ALA A 341      11.103  11.919  67.839  1.00 58.59           C  
ANISOU 3202  CB  ALA A 341     7260   7755   7246     32     74     58       C  
ATOM   3203  N   SER A 342      12.709  11.585  65.093  1.00 67.35           N  
ANISOU 3203  N   SER A 342     8406   8847   8336    194     92    166       N  
ATOM   3204  CA  SER A 342      13.937  11.501  64.290  1.00 69.75           C  
ANISOU 3204  CA  SER A 342     8699   9191   8612    254    102    240       C  
ATOM   3205  C   SER A 342      13.996  12.627  63.269  1.00 73.25           C  
ANISOU 3205  C   SER A 342     9140   9614   9079    247     83    218       C  
ATOM   3206  O   SER A 342      14.959  13.395  63.234  1.00 76.50           O  
ANISOU 3206  O   SER A 342     9509  10090   9469    228     78    255       O  
ATOM   3207  CB  SER A 342      14.042  10.165  63.549  1.00 71.70           C  
ANISOU 3207  CB  SER A 342     8997   9399   8846    344    129    278       C  
ATOM   3208  OG  SER A 342      13.946   9.074  64.433  1.00 85.36           O  
ANISOU 3208  OG  SER A 342    10742  11138  10554    355    150    298       O  
ATOM   3209  N   ALA A 343      12.957  12.740  62.436  1.00 71.99           N  
ANISOU 3209  N   ALA A 343     9026   9369   8960    259     73    159       N  
ATOM   3210  CA  ALA A 343      12.927  13.751  61.384  1.00 72.92           C  
ANISOU 3210  CA  ALA A 343     9148   9458   9100    259     55    138       C  
ATOM   3211  C   ALA A 343      13.226  15.138  61.929  1.00 67.46           C  
ANISOU 3211  C   ALA A 343     8415   8808   8410    186     38    123       C  
ATOM   3212  O   ALA A 343      14.042  15.871  61.365  1.00 68.81           O  
ANISOU 3212  O   ALA A 343     8569   9009   8568    185     32    153       O  
ATOM   3213  CB  ALA A 343      11.567  13.745  60.685  1.00 66.29           C  
ANISOU 3213  CB  ALA A 343     8356   8529   8303    269     46     67       C  
ATOM   3214  N   GLU A 344      12.589  15.517  63.032  1.00 66.66           N  
ANISOU 3214  N   GLU A 344     8299   8710   8321    121     32     77       N  
ATOM   3215  CA  GLU A 344      12.801  16.873  63.520  1.00 65.96           C  
ANISOU 3215  CA  GLU A 344     8179   8650   8234     47     20     57       C  
ATOM   3216  C   GLU A 344      14.210  17.054  64.088  1.00 71.12           C  
ANISOU 3216  C   GLU A 344     8781   9406   8835     19     31    125       C  
ATOM   3217  O   GLU A 344      14.793  18.135  63.953  1.00 71.78           O  
ANISOU 3217  O   GLU A 344     8847   9521   8906    -23     25    131       O  
ATOM   3218  CB  GLU A 344      11.735  17.235  64.550  1.00 66.90           C  
ANISOU 3218  CB  GLU A 344     8295   8745   8379    -16     13    -14       C  
ATOM   3219  CG  GLU A 344      10.320  17.089  64.047  1.00 85.35           C  
ANISOU 3219  CG  GLU A 344    10676  10994  10759      8      3    -83       C  
ATOM   3220  CD  GLU A 344       9.279  17.689  64.994  1.00103.37           C  
ANISOU 3220  CD  GLU A 344    12952  13257  13066    -57     -7   -158       C  
ATOM   3221  OE1 GLU A 344       9.285  17.331  66.192  1.00108.56           O  
ANISOU 3221  OE1 GLU A 344    13584  13955  13709   -102      0   -159       O  
ATOM   3222  OE2 GLU A 344       8.455  18.512  64.535  1.00105.66           O  
ANISOU 3222  OE2 GLU A 344    13262  13493  13390    -61    -20   -214       O  
ATOM   3223  N   ARG A 345      14.800  16.027  64.702  1.00 63.70           N  
ANISOU 3223  N   ARG A 345     7817   8526   7860     42     47    180       N  
ATOM   3224  CA  ARG A 345      16.102  16.302  65.286  1.00 79.24           C  
ANISOU 3224  CA  ARG A 345     9728  10604   9773      9     56    243       C  
ATOM   3225  C   ARG A 345      17.185  16.387  64.223  1.00 84.28           C  
ANISOU 3225  C   ARG A 345    10361  11280  10382     58     59    302       C  
ATOM   3226  O   ARG A 345      18.132  17.160  64.383  1.00 89.89           O  
ANISOU 3226  O   ARG A 345    11031  12070  11053     13     59    333       O  
ATOM   3227  CB  ARG A 345      16.470  15.282  66.372  1.00 94.91           C  
ANISOU 3227  CB  ARG A 345    11682  12656  11724     14     73    289       C  
ATOM   3228  CG  ARG A 345      16.609  13.836  65.938  1.00104.65           C  
ANISOU 3228  CG  ARG A 345    12943  13873  12946    112     90    336       C  
ATOM   3229  CD  ARG A 345      17.349  13.033  67.014  1.00108.44           C  
ANISOU 3229  CD  ARG A 345    13380  14445  13376    116    109    402       C  
ATOM   3230  NE  ARG A 345      17.226  11.594  66.799  1.00110.53           N  
ANISOU 3230  NE  ARG A 345    13686  14675  13636    204    128    434       N  
ATOM   3231  CZ  ARG A 345      16.346  10.816  67.424  1.00111.14           C  
ANISOU 3231  CZ  ARG A 345    13795  14703  13729    201    134    403       C  
ATOM   3232  NH1 ARG A 345      15.515  11.338  68.322  1.00107.57           N  
ANISOU 3232  NH1 ARG A 345    13332  14238  13302    116    120    339       N  
ATOM   3233  NH2 ARG A 345      16.299   9.516  67.153  1.00113.31           N  
ANISOU 3233  NH2 ARG A 345    14117  14943  13995    281    157    435       N  
ATOM   3234  N   ARG A 346      17.047  15.647  63.121  1.00 90.61           N  
ANISOU 3234  N   ARG A 346    11202  12026  11198    144     61    315       N  
ATOM   3235  CA  ARG A 346      18.023  15.725  62.035  1.00 89.73           C  
ANISOU 3235  CA  ARG A 346    11087  11945  11061    192     62    366       C  
ATOM   3236  C   ARG A 346      17.811  16.936  61.131  1.00 86.46           C  
ANISOU 3236  C   ARG A 346    10693  11485  10672    163     42    326       C  
ATOM   3237  O   ARG A 346      18.785  17.457  60.584  1.00100.14           O  
ANISOU 3237  O   ARG A 346    12406  13272  12372    160     39    363       O  
ATOM   3238  CB  ARG A 346      17.998  14.443  61.193  1.00 83.65           C  
ANISOU 3238  CB  ARG A 346    10354  11134  10295    293     76    397       C  
ATOM   3239  CG  ARG A 346      19.159  14.333  60.214  1.00 88.60           C  
ANISOU 3239  CG  ARG A 346    10967  11810  10886    349     82    461       C  
ATOM   3240  CD  ARG A 346      20.498  14.753  60.863  1.00 97.37           C  
ANISOU 3240  CD  ARG A 346    12010  13056  11932    314     86    522       C  
ATOM   3241  NE  ARG A 346      21.621  14.766  59.918  1.00 99.55           N  
ANISOU 3241  NE  ARG A 346    12268  13389  12169    360     88    580       N  
ATOM   3242  CZ  ARG A 346      22.068  15.849  59.280  1.00 96.27           C  
ANISOU 3242  CZ  ARG A 346    11841  12994  11742    320     72    572       C  
ATOM   3243  NH1 ARG A 346      21.496  17.031  59.461  1.00 94.05           N  
ANISOU 3243  NH1 ARG A 346    11571  12677  11488    237     53    512       N  
ATOM   3244  NH2 ARG A 346      23.090  15.756  58.446  1.00 96.68           N  
ANISOU 3244  NH2 ARG A 346    11876  13104  11755    363     74    625       N  
ATOM   3245  N   LEU A 347      16.579  17.426  60.970  1.00 73.18           N  
ANISOU 3245  N   LEU A 347     9050   9711   9045    142     28    251       N  
ATOM   3246  CA  LEU A 347      16.318  18.407  59.921  1.00 76.10           C  
ANISOU 3246  CA  LEU A 347     9449  10026   9441    137     11    218       C  
ATOM   3247  C   LEU A 347      15.919  19.794  60.411  1.00 79.61           C  
ANISOU 3247  C   LEU A 347     9893  10454   9900     53      0    165       C  
ATOM   3248  O   LEU A 347      15.918  20.726  59.605  1.00 93.67           O  
ANISOU 3248  O   LEU A 347    11696  12201  11692     43    -12    148       O  
ATOM   3249  CB  LEU A 347      15.226  17.886  58.965  1.00 70.94           C  
ANISOU 3249  CB  LEU A 347     8846   9271   8835    197      5    178       C  
ATOM   3250  CG  LEU A 347      15.486  16.500  58.372  1.00 62.57           C  
ANISOU 3250  CG  LEU A 347     7801   8209   7764    280     21    222       C  
ATOM   3251  CD1 LEU A 347      14.357  15.996  57.465  1.00 54.19           C  
ANISOU 3251  CD1 LEU A 347     6792   7053   6745    327     18    178       C  
ATOM   3252  CD2 LEU A 347      16.812  16.535  57.655  1.00 61.15           C  
ANISOU 3252  CD2 LEU A 347     7600   8091   7545    311     24    289       C  
ATOM   3253  N   SER A 348      15.632  19.976  61.697  1.00 72.16           N  
ANISOU 3253  N   SER A 348     8928   9534   8954    -10      5    141       N  
ATOM   3254  CA  SER A 348      14.893  21.162  62.129  1.00 72.57           C  
ANISOU 3254  CA  SER A 348     8994   9544   9035    -78     -2     75       C  
ATOM   3255  C   SER A 348      15.633  22.466  61.851  1.00 76.26           C  
ANISOU 3255  C   SER A 348     9462  10037   9477   -133     -4     82       C  
ATOM   3256  O   SER A 348      15.012  23.472  61.496  1.00 85.77           O  
ANISOU 3256  O   SER A 348    10702  11173  10712   -154    -12     32       O  
ATOM   3257  CB  SER A 348      14.560  21.059  63.614  1.00 71.56           C  
ANISOU 3257  CB  SER A 348     8839   9448   8904   -140      7     52       C  
ATOM   3258  OG  SER A 348      13.521  20.119  63.814  1.00 75.17           O  
ANISOU 3258  OG  SER A 348     9313   9855   9395   -101      4     20       O  
ATOM   3259  N   GLY A 349      16.933  22.495  62.026  1.00 61.13           N  
ANISOU 3259  N   GLY A 349     7506   8218   7501   -158      6    143       N  
ATOM   3260  CA  GLY A 349      17.571  23.788  61.903  1.00 75.78           C  
ANISOU 3260  CA  GLY A 349     9366  10099   9326   -227      8    142       C  
ATOM   3261  C   GLY A 349      17.800  24.287  60.487  1.00 76.66           C  
ANISOU 3261  C   GLY A 349     9514  10169   9443   -191     -5    149       C  
ATOM   3262  O   GLY A 349      16.866  24.681  59.771  1.00 73.68           O  
ANISOU 3262  O   GLY A 349     9186   9693   9118   -162    -18    102       O  
ATOM   3263  N   THR A 350      19.061  24.310  60.089  1.00 84.16           N  
ANISOU 3263  N   THR A 350    10438  11203  10335   -196     -2    208       N  
ATOM   3264  CA  THR A 350      19.367  24.769  58.748  1.00 88.62           C  
ANISOU 3264  CA  THR A 350    11035  11737  10899   -167    -15    218       C  
ATOM   3265  C   THR A 350      19.020  23.742  57.667  1.00 78.37           C  
ANISOU 3265  C   THR A 350     9752  10388   9636    -60    -27    232       C  
ATOM   3266  O   THR A 350      18.712  24.168  56.551  1.00 74.95           O  
ANISOU 3266  O   THR A 350     9359   9889   9230    -32    -41    215       O  
ATOM   3267  CB  THR A 350      20.837  25.193  58.643  1.00 94.43           C  
ANISOU 3267  CB  THR A 350    11738  12585  11556   -214     -9    272       C  
ATOM   3268  OG1 THR A 350      21.674  24.244  59.312  1.00100.16           O  
ANISOU 3268  OG1 THR A 350    12400  13423  12232   -201      4    331       O  
ATOM   3269  CG2 THR A 350      21.032  26.564  59.267  1.00 90.72           C  
ANISOU 3269  CG2 THR A 350    11281  12132  11057   -327      2    243       C  
ATOM   3270  N   PRO A 351      19.027  22.415  57.922  1.00 78.25           N  
ANISOU 3270  N   PRO A 351     9711  10398   9622      0    -19    262       N  
ATOM   3271  CA  PRO A 351      18.787  21.491  56.798  1.00 70.81           C  
ANISOU 3271  CA  PRO A 351     8791   9409   8706     95    -24    277       C  
ATOM   3272  C   PRO A 351      17.426  21.671  56.149  1.00 74.15           C  
ANISOU 3272  C   PRO A 351     9266   9712   9197    123    -38    214       C  
ATOM   3273  O   PRO A 351      17.351  21.762  54.925  1.00 72.54           O  
ANISOU 3273  O   PRO A 351     9089   9465   9009    164    -49    215       O  
ATOM   3274  CB  PRO A 351      18.939  20.105  57.439  1.00 69.64           C  
ANISOU 3274  CB  PRO A 351     8614   9303   8544    142     -7    313       C  
ATOM   3275  CG  PRO A 351      19.763  20.322  58.635  1.00 71.03           C  
ANISOU 3275  CG  PRO A 351     8738   9583   8666     79      5    344       C  
ATOM   3276  CD  PRO A 351      19.301  21.646  59.156  1.00 80.54           C  
ANISOU 3276  CD  PRO A 351     9956  10760   9885    -12     -2    289       C  
ATOM   3277  N   ILE A 352      16.343  21.752  56.924  1.00 78.11           N  
ANISOU 3277  N   ILE A 352     9780  10164   9735    100    -37    160       N  
ATOM   3278  CA  ILE A 352      15.050  21.949  56.289  1.00 73.18           C  
ANISOU 3278  CA  ILE A 352     9199   9438   9167    128    -50    102       C  
ATOM   3279  C   ILE A 352      14.936  23.360  55.745  1.00 76.02           C  
ANISOU 3279  C   ILE A 352     9588   9757   9539     94    -63     74       C  
ATOM   3280  O   ILE A 352      14.106  23.618  54.866  1.00 76.85           O  
ANISOU 3280  O   ILE A 352     9729   9787   9683    128    -76     41       O  
ATOM   3281  CB  ILE A 352      13.889  21.645  57.253  1.00 65.37           C  
ANISOU 3281  CB  ILE A 352     8214   8412   8211    115    -46     50       C  
ATOM   3282  CG1 ILE A 352      12.593  21.446  56.466  1.00 56.07           C  
ANISOU 3282  CG1 ILE A 352     7074   7146   7083    164    -57      1       C  
ATOM   3283  CG2 ILE A 352      13.731  22.758  58.247  1.00 73.02           C  
ANISOU 3283  CG2 ILE A 352     9178   9388   9180     34    -45     14       C  
ATOM   3284  CD1 ILE A 352      12.497  20.082  55.840  1.00 53.98           C  
ANISOU 3284  CD1 ILE A 352     6817   6874   6819    233    -50     24       C  
ATOM   3285  N   SER A 353      15.753  24.286  56.250  1.00 75.88           N  
ANISOU 3285  N   SER A 353     9557   9790   9483     23    -58     88       N  
ATOM   3286  CA  SER A 353      15.807  25.612  55.653  1.00 78.69           C  
ANISOU 3286  CA  SER A 353     9950  10109   9841    -11    -67     69       C  
ATOM   3287  C   SER A 353      16.245  25.525  54.200  1.00 78.36           C  
ANISOU 3287  C   SER A 353     9923  10056   9795     40    -81    100       C  
ATOM   3288  O   SER A 353      15.602  26.095  53.312  1.00 80.58           O  
ANISOU 3288  O   SER A 353    10245  10262  10109     63    -94     72       O  
ATOM   3289  CB  SER A 353      16.751  26.512  56.447  1.00 94.96           C  
ANISOU 3289  CB  SER A 353    11995  12238  11848   -103    -54     83       C  
ATOM   3290  OG  SER A 353      17.074  27.670  55.695  1.00110.72           O  
ANISOU 3290  OG  SER A 353    14029  14207  13831   -133    -60     79       O  
ATOM   3291  N   PHE A 354      17.331  24.791  53.940  1.00 72.27           N  
ANISOU 3291  N   PHE A 354     9117   9361   8980     62    -77    160       N  
ATOM   3292  CA  PHE A 354      17.877  24.666  52.593  1.00 67.43           C  
ANISOU 3292  CA  PHE A 354     8514   8750   8358    106    -88    193       C  
ATOM   3293  C   PHE A 354      17.092  23.689  51.723  1.00 65.20           C  
ANISOU 3293  C   PHE A 354     8247   8407   8120    191    -94    185       C  
ATOM   3294  O   PHE A 354      17.032  23.871  50.504  1.00 68.99           O  
ANISOU 3294  O   PHE A 354     8750   8850   8614    223   -107    187       O  
ATOM   3295  CB  PHE A 354      19.332  24.235  52.679  1.00 66.23           C  
ANISOU 3295  CB  PHE A 354     8315   8709   8139     99    -80    259       C  
ATOM   3296  CG  PHE A 354      20.268  25.353  52.998  1.00 81.15           C  
ANISOU 3296  CG  PHE A 354    10197  10662   9973     13    -78    272       C  
ATOM   3297  CD1 PHE A 354      20.354  25.866  54.288  1.00 91.07           C  
ANISOU 3297  CD1 PHE A 354    11439  11958  11207    -64    -64    258       C  
ATOM   3298  CD2 PHE A 354      21.071  25.897  52.008  1.00 90.34           C  
ANISOU 3298  CD2 PHE A 354    11371  11851  11104      3    -89    297       C  
ATOM   3299  CE1 PHE A 354      21.231  26.904  54.590  1.00 89.65           C  
ANISOU 3299  CE1 PHE A 354    11255  11840  10968   -152    -58    268       C  
ATOM   3300  CE2 PHE A 354      21.944  26.932  52.296  1.00 96.00           C  
ANISOU 3300  CE2 PHE A 354    12085  12630  11762    -84    -85    307       C  
ATOM   3301  CZ  PHE A 354      22.027  27.434  53.592  1.00 94.85           C  
ANISOU 3301  CZ  PHE A 354    11926  12523  11590   -163    -68    292       C  
ATOM   3302  N   ILE A 355      16.511  22.649  52.330  1.00 60.11           N  
ANISOU 3302  N   ILE A 355     7590   7755   7494    223    -82    176       N  
ATOM   3303  CA  ILE A 355      15.616  21.741  51.622  1.00 57.39           C  
ANISOU 3303  CA  ILE A 355     7267   7349   7189    292    -83    159       C  
ATOM   3304  C   ILE A 355      14.398  22.498  51.103  1.00 63.28           C  
ANISOU 3304  C   ILE A 355     8051   8008   7984    292    -98    101       C  
ATOM   3305  O   ILE A 355      13.971  22.307  49.963  1.00 59.71           O  
ANISOU 3305  O   ILE A 355     7621   7513   7554    338   -107     95       O  
ATOM   3306  CB  ILE A 355      15.220  20.568  52.540  1.00 53.09           C  
ANISOU 3306  CB  ILE A 355     6709   6816   6648    311    -65    157       C  
ATOM   3307  CG1 ILE A 355      16.418  19.653  52.771  1.00 60.60           C  
ANISOU 3307  CG1 ILE A 355     7626   7849   7552    335    -47    223       C  
ATOM   3308  CG2 ILE A 355      14.112  19.743  51.957  1.00 51.55           C  
ANISOU 3308  CG2 ILE A 355     6542   6554   6492    365    -62    126       C  
ATOM   3309  CD1 ILE A 355      16.206  18.700  53.944  1.00 61.91           C  
ANISOU 3309  CD1 ILE A 355     7776   8037   7711    338    -28    227       C  
ATOM   3310  N   LEU A 356      13.821  23.373  51.926  1.00 73.18           N  
ANISOU 3310  N   LEU A 356     9314   9240   9253    244   -101     58       N  
ATOM   3311  CA  LEU A 356      12.748  24.229  51.435  1.00 68.18           C  
ANISOU 3311  CA  LEU A 356     8716   8529   8660    248   -115      7       C  
ATOM   3312  C   LEU A 356      13.243  25.117  50.311  1.00 70.01           C  
ANISOU 3312  C   LEU A 356     8971   8745   8884    248   -129     25       C  
ATOM   3313  O   LEU A 356      12.516  25.380  49.350  1.00 74.91           O  
ANISOU 3313  O   LEU A 356     9618   9309   9536    284   -142      4       O  
ATOM   3314  CB  LEU A 356      12.190  25.084  52.569  1.00 61.15           C  
ANISOU 3314  CB  LEU A 356     7832   7621   7780    194   -111    -38       C  
ATOM   3315  CG  LEU A 356      11.084  24.473  53.424  1.00 68.63           C  
ANISOU 3315  CG  LEU A 356     8771   8550   8755    201   -105    -82       C  
ATOM   3316  CD1 LEU A 356      10.803  25.371  54.627  1.00 69.50           C  
ANISOU 3316  CD1 LEU A 356     8883   8657   8868    137    -98   -120       C  
ATOM   3317  CD2 LEU A 356       9.821  24.237  52.612  1.00 61.05           C  
ANISOU 3317  CD2 LEU A 356     7833   7528   7834    257   -115   -120       C  
ATOM   3318  N   LEU A 357      14.474  25.610  50.431  1.00 72.32           N  
ANISOU 3318  N   LEU A 357     9253   9093   9133    204   -127     63       N  
ATOM   3319  CA  LEU A 357      15.025  26.497  49.416  1.00 67.87           C  
ANISOU 3319  CA  LEU A 357     8714   8519   8555    194   -140     79       C  
ATOM   3320  C   LEU A 357      15.133  25.779  48.084  1.00 66.90           C  
ANISOU 3320  C   LEU A 357     8590   8388   8440    258   -150    106       C  
ATOM   3321  O   LEU A 357      14.741  26.315  47.046  1.00 64.36           O  
ANISOU 3321  O   LEU A 357     8299   8017   8140    278   -166     94       O  
ATOM   3322  CB  LEU A 357      16.395  27.003  49.860  1.00 64.37           C  
ANISOU 3322  CB  LEU A 357     8254   8154   8052    129   -133    117       C  
ATOM   3323  CG  LEU A 357      17.028  27.927  48.834  1.00 74.62           C  
ANISOU 3323  CG  LEU A 357     9580   9446   9327    110   -147    134       C  
ATOM   3324  CD1 LEU A 357      16.120  29.100  48.637  1.00 83.22           C  
ANISOU 3324  CD1 LEU A 357    10723  10445  10450     96   -153     87       C  
ATOM   3325  CD2 LEU A 357      18.396  28.388  49.301  1.00 84.83           C  
ANISOU 3325  CD2 LEU A 357    10854  10829  10551     38   -138    169       C  
ATOM   3326  N   LEU A 358      15.651  24.552  48.111  1.00 63.12           N  
ANISOU 3326  N   LEU A 358     8078   7961   7944    290   -140    141       N  
ATOM   3327  CA  LEU A 358      15.752  23.721  46.923  1.00 60.74           C  
ANISOU 3327  CA  LEU A 358     7776   7654   7648    351   -143    165       C  
ATOM   3328  C   LEU A 358      14.417  23.598  46.218  1.00 63.34           C  
ANISOU 3328  C   LEU A 358     8132   7904   8028    392   -151    124       C  
ATOM   3329  O   LEU A 358      14.374  23.572  44.977  1.00 64.78           O  
ANISOU 3329  O   LEU A 358     8328   8066   8221    424   -162    132       O  
ATOM   3330  CB  LEU A 358      16.269  22.341  47.318  1.00 61.21           C  
ANISOU 3330  CB  LEU A 358     7804   7767   7686    384   -123    201       C  
ATOM   3331  CG  LEU A 358      16.645  21.353  46.232  1.00 62.90           C  
ANISOU 3331  CG  LEU A 358     8015   7990   7894    444   -118    235       C  
ATOM   3332  CD1 LEU A 358      17.614  21.998  45.231  1.00 67.44           C  
ANISOU 3332  CD1 LEU A 358     8587   8594   8442    433   -134    267       C  
ATOM   3333  CD2 LEU A 358      17.251  20.111  46.884  1.00 54.87           C  
ANISOU 3333  CD2 LEU A 358     6970   7029   6848    472    -92    273       C  
ATOM   3334  N   SER A 359      13.319  23.547  46.991  1.00 58.96           N  
ANISOU 3334  N   SER A 359     7585   7314   7503    390   -146     78       N  
ATOM   3335  CA  SER A 359      11.988  23.444  46.399  1.00 59.98           C  
ANISOU 3335  CA  SER A 359     7735   7381   7674    426   -152     36       C  
ATOM   3336  C   SER A 359      11.696  24.642  45.507  1.00 67.64           C  
ANISOU 3336  C   SER A 359     8733   8307   8660    425   -173     23       C  
ATOM   3337  O   SER A 359      11.405  24.490  44.315  1.00 62.49           O  
ANISOU 3337  O   SER A 359     8090   7632   8021    461   -182     27       O  
ATOM   3338  CB  SER A 359      10.930  23.323  47.487  1.00 63.95           C  
ANISOU 3338  CB  SER A 359     8237   7864   8198    416   -145    -12       C  
ATOM   3339  OG  SER A 359      11.228  22.231  48.310  1.00 73.77           O  
ANISOU 3339  OG  SER A 359     9458   9146   9424    416   -126      3       O  
ATOM   3340  N   TYR A 360      11.801  25.848  46.069  1.00 67.84           N  
ANISOU 3340  N   TYR A 360     8774   8320   8682    380   -178      9       N  
ATOM   3341  CA  TYR A 360      11.568  27.058  45.292  1.00 70.50           C  
ANISOU 3341  CA  TYR A 360     9146   8610   9031    378   -195     -1       C  
ATOM   3342  C   TYR A 360      12.519  27.171  44.100  1.00 75.22           C  
ANISOU 3342  C   TYR A 360     9747   9225   9606    383   -207     43       C  
ATOM   3343  O   TYR A 360      12.178  27.803  43.092  1.00 84.24           O  
ANISOU 3343  O   TYR A 360    10916  10327  10763    401   -222     39       O  
ATOM   3344  CB  TYR A 360      11.670  28.267  46.219  1.00 64.19           C  
ANISOU 3344  CB  TYR A 360     8369   7796   8223    322   -190    -21       C  
ATOM   3345  CG  TYR A 360      10.598  28.216  47.278  1.00 69.81           C  
ANISOU 3345  CG  TYR A 360     9078   8485   8961    322   -180    -69       C  
ATOM   3346  CD1 TYR A 360       9.274  28.461  46.950  1.00 67.83           C  
ANISOU 3346  CD1 TYR A 360     8845   8179   8749    363   -187   -110       C  
ATOM   3347  CD2 TYR A 360      10.892  27.887  48.599  1.00 76.45           C  
ANISOU 3347  CD2 TYR A 360     9896   9366   9787    280   -164    -74       C  
ATOM   3348  CE1 TYR A 360       8.281  28.398  47.888  1.00 70.36           C  
ANISOU 3348  CE1 TYR A 360     9159   8484   9090    364   -179   -156       C  
ATOM   3349  CE2 TYR A 360       9.895  27.831  49.555  1.00 74.59           C  
ANISOU 3349  CE2 TYR A 360     9656   9110   9575    277   -156   -120       C  
ATOM   3350  CZ  TYR A 360       8.588  28.089  49.187  1.00 79.34           C  
ANISOU 3350  CZ  TYR A 360    10276   9657  10214    319   -164   -163       C  
ATOM   3351  OH  TYR A 360       7.565  28.043  50.113  1.00 87.00           O  
ANISOU 3351  OH  TYR A 360    11240  10612  11205    317   -158   -212       O  
ATOM   3352  N   THR A 361      13.683  26.526  44.166  1.00 68.41           N  
ANISOU 3352  N   THR A 361     8858   8428   8708    371   -200     85       N  
ATOM   3353  CA  THR A 361      14.647  26.663  43.085  1.00 72.82           C  
ANISOU 3353  CA  THR A 361     9418   9012   9240    370   -212    126       C  
ATOM   3354  C   THR A 361      14.109  26.072  41.796  1.00 79.43           C  
ANISOU 3354  C   THR A 361    10256   9820  10103    427   -221    127       C  
ATOM   3355  O   THR A 361      14.475  26.524  40.707  1.00 89.13           O  
ANISOU 3355  O   THR A 361    11498  11041  11325    429   -237    145       O  
ATOM   3356  CB  THR A 361      15.960  25.999  43.480  1.00 71.76           C  
ANISOU 3356  CB  THR A 361     9246   8960   9058    353   -200    171       C  
ATOM   3357  OG1 THR A 361      16.373  26.523  44.744  1.00 91.95           O  
ANISOU 3357  OG1 THR A 361    11798  11551  11589    296   -190    167       O  
ATOM   3358  CG2 THR A 361      17.035  26.306  42.488  1.00 66.19           C  
ANISOU 3358  CG2 THR A 361     8540   8291   8318    342   -214    210       C  
ATOM   3359  N   SER A 362      13.214  25.088  41.901  1.00 80.57           N  
ANISOU 3359  N   SER A 362    10389   9948  10274    468   -209    106       N  
ATOM   3360  CA  SER A 362      12.673  24.441  40.713  1.00 75.48           C  
ANISOU 3360  CA  SER A 362     9746   9283   9649    515   -213    106       C  
ATOM   3361  C   SER A 362      11.887  25.424  39.859  1.00 76.59           C  
ANISOU 3361  C   SER A 362     9913   9371   9816    524   -233     84       C  
ATOM   3362  O   SER A 362      11.782  25.242  38.638  1.00 74.18           O  
ANISOU 3362  O   SER A 362     9610   9058   9518    549   -242     95       O  
ATOM   3363  CB  SER A 362      11.790  23.263  41.121  1.00 73.68           C  
ANISOU 3363  CB  SER A 362     9508   9049   9439    545   -192     82       C  
ATOM   3364  OG  SER A 362      10.699  23.703  41.916  1.00 79.79           O  
ANISOU 3364  OG  SER A 362    10291   9790  10236    538   -193     35       O  
ATOM   3365  N   SER A 363      11.332  26.471  40.481  1.00 71.20           N  
ANISOU 3365  N   SER A 363     9252   8654   9147    504   -239     54       N  
ATOM   3366  CA  SER A 363      10.502  27.418  39.756  1.00 71.23           C  
ANISOU 3366  CA  SER A 363     9284   8606   9175    522   -256     35       C  
ATOM   3367  C   SER A 363      11.327  28.434  38.981  1.00 76.55           C  
ANISOU 3367  C   SER A 363     9983   9271   9830    499   -274     63       C  
ATOM   3368  O   SER A 363      10.773  29.140  38.129  1.00 92.48           O  
ANISOU 3368  O   SER A 363    12025  11248  11864    519   -289     57       O  
ATOM   3369  CB  SER A 363       9.555  28.147  40.709  1.00 67.31           C  
ANISOU 3369  CB  SER A 363     8805   8071   8698    517   -252     -9       C  
ATOM   3370  OG  SER A 363      10.204  29.265  41.279  1.00 76.05           O  
ANISOU 3370  OG  SER A 363     9940   9167   9788    470   -253     -4       O  
ATOM   3371  N   CYS A 364      12.627  28.532  39.247  1.00 61.55           N  
ANISOU 3371  N   CYS A 364     8080   7414   7893    456   -272     94       N  
ATOM   3372  CA  CYS A 364      13.492  29.393  38.462  1.00 64.50           C  
ANISOU 3372  CA  CYS A 364     8477   7788   8241    427   -288    122       C  
ATOM   3373  C   CYS A 364      14.428  28.580  37.569  1.00 73.40           C  
ANISOU 3373  C   CYS A 364     9576   8968   9346    434   -294    162       C  
ATOM   3374  O   CYS A 364      15.302  29.147  36.911  1.00 77.67           O  
ANISOU 3374  O   CYS A 364    10129   9526   9858    406   -308    188       O  
ATOM   3375  CB  CYS A 364      14.260  30.351  39.376  1.00 65.84           C  
ANISOU 3375  CB  CYS A 364     8670   7969   8376    362   -283    124       C  
ATOM   3376  SG  CYS A 364      15.903  29.843  39.876  1.00 77.39           S  
ANISOU 3376  SG  CYS A 364    10097   9529   9780    312   -274    165       S  
ATOM   3377  N   VAL A 365      14.204  27.272  37.472  1.00 74.06           N  
ANISOU 3377  N   VAL A 365     9625   9074   9440    473   -281    165       N  
ATOM   3378  CA  VAL A 365      15.067  26.407  36.683  1.00 74.80           C  
ANISOU 3378  CA  VAL A 365     9693   9216   9512    486   -280    201       C  
ATOM   3379  C   VAL A 365      14.726  26.487  35.192  1.00 78.23           C  
ANISOU 3379  C   VAL A 365    10135   9624   9964    511   -297    206       C  
ATOM   3380  O   VAL A 365      15.616  26.654  34.349  1.00 75.77           O  
ANISOU 3380  O   VAL A 365     9821   9340   9628    496   -310    236       O  
ATOM   3381  CB  VAL A 365      14.989  24.973  37.244  1.00 72.34           C  
ANISOU 3381  CB  VAL A 365     9350   8933   9202    516   -253    203       C  
ATOM   3382  CG1 VAL A 365      15.085  23.941  36.140  1.00 81.75           C  
ANISOU 3382  CG1 VAL A 365    10528  10137  10397    555   -247    222       C  
ATOM   3383  CG2 VAL A 365      16.102  24.753  38.231  1.00 65.46           C  
ANISOU 3383  CG2 VAL A 365     8458   8123   8291    489   -241    230       C  
ATOM   3384  N   ASN A 366      13.450  26.385  34.838  1.00 75.80           N  
ANISOU 3384  N   ASN A 366     9834   9272   9694    545   -298    177       N  
ATOM   3385  CA  ASN A 366      13.094  26.331  33.420  1.00 74.05           C  
ANISOU 3385  CA  ASN A 366     9613   9035   9486    568   -311    183       C  
ATOM   3386  C   ASN A 366      13.410  27.624  32.654  1.00 75.17           C  
ANISOU 3386  C   ASN A 366     9784   9155   9620    545   -339    196       C  
ATOM   3387  O   ASN A 366      13.910  27.526  31.516  1.00 59.85           O  
ANISOU 3387  O   ASN A 366     7837   7232   7670    544   -352    220       O  
ATOM   3388  CB  ASN A 366      11.612  25.945  33.256  1.00 72.53           C  
ANISOU 3388  CB  ASN A 366     9418   8811   9329    607   -304    149       C  
ATOM   3389  CG  ASN A 366      11.201  24.794  34.160  1.00 79.74           C  
ANISOU 3389  CG  ASN A 366    10314   9739  10246    621   -275    130       C  
ATOM   3390  OD1 ASN A 366      11.935  23.831  34.337  1.00 75.42           O  
ANISOU 3390  OD1 ASN A 366     9750   9227   9681    621   -257    150       O  
ATOM   3391  ND2 ASN A 366      10.013  24.914  34.769  1.00 88.10           N  
ANISOU 3391  ND2 ASN A 366    11377  10771  11327    635   -270     91       N  
ATOM   3392  N   PRO A 367      13.163  28.838  33.179  1.00 81.55           N  
ANISOU 3392  N   PRO A 367    10627   9926  10431    525   -348    181       N  
ATOM   3393  CA  PRO A 367      13.580  30.021  32.410  1.00 80.77           C  
ANISOU 3393  CA  PRO A 367    10564   9805  10319    500   -372    197       C  
ATOM   3394  C   PRO A 367      15.073  30.061  32.162  1.00 84.07           C  
ANISOU 3394  C   PRO A 367    10977  10275  10691    455   -379    232       C  
ATOM   3395  O   PRO A 367      15.489  30.404  31.051  1.00 92.54           O  
ANISOU 3395  O   PRO A 367    12057  11350  11752    445   -399    252       O  
ATOM   3396  CB  PRO A 367      13.106  31.198  33.275  1.00 78.36           C  
ANISOU 3396  CB  PRO A 367    10303   9449  10019    485   -370    173       C  
ATOM   3397  CG  PRO A 367      12.012  30.649  34.073  1.00 79.83           C  
ANISOU 3397  CG  PRO A 367    10472   9622  10237    521   -353    140       C  
ATOM   3398  CD  PRO A 367      12.417  29.239  34.386  1.00 77.62           C  
ANISOU 3398  CD  PRO A 367    10144   9396   9949    526   -337    148       C  
ATOM   3399  N   ILE A 368      15.895  29.695  33.151  1.00 83.94           N  
ANISOU 3399  N   ILE A 368    10943  10306  10646    426   -364    240       N  
ATOM   3400  CA  ILE A 368      17.341  29.647  32.933  1.00 86.61           C  
ANISOU 3400  CA  ILE A 368    11267  10709  10933    386   -369    274       C  
ATOM   3401  C   ILE A 368      17.690  28.629  31.843  1.00 85.19           C  
ANISOU 3401  C   ILE A 368    11050  10566  10752    416   -372    298       C  
ATOM   3402  O   ILE A 368      18.597  28.853  31.029  1.00 82.82           O  
ANISOU 3402  O   ILE A 368    10748  10299  10420    390   -388    324       O  
ATOM   3403  CB  ILE A 368      18.065  29.355  34.264  1.00 75.29           C  
ANISOU 3403  CB  ILE A 368     9813   9328   9466    356   -349    280       C  
ATOM   3404  CG1 ILE A 368      17.863  30.517  35.228  1.00 79.20           C  
ANISOU 3404  CG1 ILE A 368    10349   9789   9954    312   -345    258       C  
ATOM   3405  CG2 ILE A 368      19.561  29.144  34.058  1.00 70.86           C  
ANISOU 3405  CG2 ILE A 368     9226   8853   8847    322   -352    318       C  
ATOM   3406  CD1 ILE A 368      18.301  30.217  36.670  1.00 81.92           C  
ANISOU 3406  CD1 ILE A 368    10671  10180  10273    284   -322    256       C  
ATOM   3407  N   ILE A 369      16.970  27.505  31.804  1.00 80.84           N  
ANISOU 3407  N   ILE A 369    10474  10008  10234    466   -355    287       N  
ATOM   3408  CA  ILE A 369      17.167  26.513  30.754  1.00 78.56           C  
ANISOU 3408  CA  ILE A 369    10158   9745   9948    495   -352    305       C  
ATOM   3409  C   ILE A 369      16.771  27.077  29.391  1.00 81.87           C  
ANISOU 3409  C   ILE A 369    10593  10132  10383    497   -377    306       C  
ATOM   3410  O   ILE A 369      17.487  26.891  28.401  1.00 83.79           O  
ANISOU 3410  O   ILE A 369    10823  10407  10608    488   -388    330       O  
ATOM   3411  CB  ILE A 369      16.382  25.233  31.087  1.00 76.41           C  
ANISOU 3411  CB  ILE A 369     9865   9464   9702    542   -323    289       C  
ATOM   3412  CG1 ILE A 369      17.078  24.456  32.192  1.00 78.06           C  
ANISOU 3412  CG1 ILE A 369    10053   9720   9887    544   -298    302       C  
ATOM   3413  CG2 ILE A 369      16.245  24.362  29.866  1.00 78.28           C  
ANISOU 3413  CG2 ILE A 369    10086   9707   9949    570   -318    297       C  
ATOM   3414  CD1 ILE A 369      16.255  23.288  32.678  1.00 80.60           C  
ANISOU 3414  CD1 ILE A 369    10365  10026  10232    584   -268    282       C  
ATOM   3415  N   TYR A 370      15.629  27.770  29.314  1.00 79.67           N  
ANISOU 3415  N   TYR A 370    10340   9794  10137    510   -386    280       N  
ATOM   3416  CA  TYR A 370      15.215  28.376  28.050  1.00 75.65           C  
ANISOU 3416  CA  TYR A 370     9846   9256   9642    513   -410    284       C  
ATOM   3417  C   TYR A 370      16.264  29.350  27.531  1.00 86.47           C  
ANISOU 3417  C   TYR A 370    11239  10638  10977    466   -436    308       C  
ATOM   3418  O   TYR A 370      16.497  29.440  26.321  1.00 92.05           O  
ANISOU 3418  O   TYR A 370    11942  11353  11679    460   -454    325       O  
ATOM   3419  CB  TYR A 370      13.877  29.104  28.207  1.00 64.73           C  
ANISOU 3419  CB  TYR A 370     8490   7811   8294    538   -415    256       C  
ATOM   3420  CG  TYR A 370      12.733  28.249  28.672  1.00 62.31           C  
ANISOU 3420  CG  TYR A 370     8161   7495   8017    580   -393    228       C  
ATOM   3421  CD1 TYR A 370      12.766  26.865  28.530  1.00 60.42           C  
ANISOU 3421  CD1 TYR A 370     7886   7291   7778    597   -371    229       C  
ATOM   3422  CD2 TYR A 370      11.621  28.825  29.271  1.00 69.89           C  
ANISOU 3422  CD2 TYR A 370     9140   8412   9001    601   -391    198       C  
ATOM   3423  CE1 TYR A 370      11.720  26.083  28.975  1.00 60.43           C  
ANISOU 3423  CE1 TYR A 370     7874   7285   7801    627   -348    200       C  
ATOM   3424  CE2 TYR A 370      10.578  28.059  29.718  1.00 71.21           C  
ANISOU 3424  CE2 TYR A 370     9287   8579   9190    634   -371    170       C  
ATOM   3425  CZ  TYR A 370      10.633  26.687  29.576  1.00 69.69           C  
ANISOU 3425  CZ  TYR A 370     9061   8422   8995    644   -350    170       C  
ATOM   3426  OH  TYR A 370       9.578  25.927  30.027  1.00 77.44           O  
ANISOU 3426  OH  TYR A 370    10028   9404   9992    669   -329    140       O  
ATOM   3427  N   CYS A 371      16.888  30.099  28.434  1.00 91.63           N  
ANISOU 3427  N   CYS A 371    11917  11296  11601    425   -436    309       N  
ATOM   3428  CA  CYS A 371      17.928  31.040  28.039  1.00101.92           C  
ANISOU 3428  CA  CYS A 371    13247  12616  12860    369   -458    330       C  
ATOM   3429  C   CYS A 371      19.102  30.321  27.385  1.00104.58           C  
ANISOU 3429  C   CYS A 371    13545  13029  13162    353   -462    359       C  
ATOM   3430  O   CYS A 371      19.576  30.732  26.320  1.00112.45           O  
ANISOU 3430  O   CYS A 371    14550  14035  14141    329   -486    376       O  
ATOM   3431  CB  CYS A 371      18.391  31.836  29.257  1.00110.34           C  
ANISOU 3431  CB  CYS A 371    14345  13684  13896    322   -449    322       C  
ATOM   3432  SG  CYS A 371      18.621  33.588  28.933  1.00121.78           S  
ANISOU 3432  SG  CYS A 371    15870  15084  15317    265   -470    323       S  
ATOM   3433  N   PHE A 372      19.583  29.241  28.000  1.00100.71           N  
ANISOU 3433  N   PHE A 372    13013  12592  12660    368   -439    367       N  
ATOM   3434  CA  PHE A 372      20.740  28.528  27.469  1.00100.88           C  
ANISOU 3434  CA  PHE A 372    12996  12691  12644    360   -440    396       C  
ATOM   3435  C   PHE A 372      20.405  27.650  26.275  1.00105.11           C  
ANISOU 3435  C   PHE A 372    13506  13224  13207    400   -439    402       C  
ATOM   3436  O   PHE A 372      21.283  26.917  25.806  1.00107.32           O  
ANISOU 3436  O   PHE A 372    13752  13563  13460    403   -435    424       O  
ATOM   3437  CB  PHE A 372      21.394  27.676  28.562  1.00 97.84           C  
ANISOU 3437  CB  PHE A 372    12576  12366  12233    369   -412    407       C  
ATOM   3438  CG  PHE A 372      22.262  28.468  29.486  1.00100.98           C  
ANISOU 3438  CG  PHE A 372    12985  12805  12578    312   -415    415       C  
ATOM   3439  CD1 PHE A 372      21.695  29.308  30.439  1.00 97.88           C  
ANISOU 3439  CD1 PHE A 372    12629  12366  12196    289   -411    391       C  
ATOM   3440  CD2 PHE A 372      23.646  28.401  29.390  1.00 97.32           C  
ANISOU 3440  CD2 PHE A 372    12494  12432  12051    278   -419    445       C  
ATOM   3441  CE1 PHE A 372      22.491  30.062  31.278  1.00 87.84           C  
ANISOU 3441  CE1 PHE A 372    11370  11134  10872    227   -410    396       C  
ATOM   3442  CE2 PHE A 372      24.447  29.158  30.237  1.00 90.33           C  
ANISOU 3442  CE2 PHE A 372    11617  11595  11109    216   -420    451       C  
ATOM   3443  CZ  PHE A 372      23.863  29.987  31.174  1.00 83.21           C  
ANISOU 3443  CZ  PHE A 372    10756  10642  10219    188   -414    426       C  
ATOM   3444  N   MET A 373      19.170  27.698  25.779  1.00104.72           N  
ANISOU 3444  N   MET A 373    13471  13112  13206    430   -442    381       N  
ATOM   3445  CA  MET A 373      18.769  26.850  24.664  1.00108.58           C  
ANISOU 3445  CA  MET A 373    13936  13602  13719    461   -437    383       C  
ATOM   3446  C   MET A 373      18.970  27.503  23.300  1.00118.14           C  
ANISOU 3446  C   MET A 373    15154  14809  14923    435   -469    396       C  
ATOM   3447  O   MET A 373      19.227  26.791  22.323  1.00118.28           O  
ANISOU 3447  O   MET A 373    15146  14856  14941    443   -467    408       O  
ATOM   3448  CB  MET A 373      17.306  26.424  24.823  1.00100.96           C  
ANISOU 3448  CB  MET A 373    12973  12585  12802    504   -420    355       C  
ATOM   3449  CG  MET A 373      17.129  25.162  25.646  1.00 96.62           C  
ANISOU 3449  CG  MET A 373    12401  12050  12259    538   -382    346       C  
ATOM   3450  SD  MET A 373      17.808  23.684  24.873  1.00 97.10           S  
ANISOU 3450  SD  MET A 373    12427  12160  12306    558   -357    366       S  
ATOM   3451  CE  MET A 373      18.623  22.897  26.268  1.00 96.77           C  
ANISOU 3451  CE  MET A 373    12372  12160  12236    573   -326    378       C  
ATOM   3452  N   ASN A 374      18.849  28.823  23.198  1.00124.54           N  
ANISOU 3452  N   ASN A 374    16006  15585  15730    404   -496    394       N  
ATOM   3453  CA  ASN A 374      19.194  29.526  21.959  1.00132.88           C  
ANISOU 3453  CA  ASN A 374    17074  16642  16772    372   -529    410       C  
ATOM   3454  C   ASN A 374      20.633  30.032  21.998  1.00140.92           C  
ANISOU 3454  C   ASN A 374    18099  17714  17730    314   -545    430       C  
ATOM   3455  O   ASN A 374      20.917  31.210  21.785  1.00149.05           O  
ANISOU 3455  O   ASN A 374    19170  18725  18736    269   -570    435       O  
ATOM   3456  CB  ASN A 374      18.203  30.660  21.669  1.00130.42           C  
ANISOU 3456  CB  ASN A 374    16807  16260  16486    375   -548    399       C  
ATOM   3457  CG  ASN A 374      18.210  31.759  22.728  1.00125.75           C  
ANISOU 3457  CG  ASN A 374    16268  15632  15881    353   -550    389       C  
ATOM   3458  OD1 ASN A 374      17.246  31.912  23.473  1.00127.75           O  
ANISOU 3458  OD1 ASN A 374    16536  15838  16164    385   -536    368       O  
ATOM   3459  ND2 ASN A 374      19.279  32.549  22.772  1.00119.89           N  
ANISOU 3459  ND2 ASN A 374    15553  14910  15090    293   -566    403       N  
ATOM   3460  N   LYS A 375      21.564  29.126  22.286  1.00134.95           N  
ANISOU 3460  N   LYS A 375    17302  17027  16945    315   -528    444       N  
ATOM   3461  CA  LYS A 375      22.984  29.455  22.242  1.00126.83           C  
ANISOU 3461  CA  LYS A 375    16267  16070  15852    262   -543    465       C  
ATOM   3462  C   LYS A 375      23.506  29.237  20.824  1.00121.00           C  
ANISOU 3462  C   LYS A 375    15506  15366  15101    247   -563    481       C  
ATOM   3463  O   LYS A 375      22.745  28.857  19.931  1.00115.29           O  
ANISOU 3463  O   LYS A 375    14775  14610  14420    277   -564    476       O  
ATOM   3464  CB  LYS A 375      23.774  28.613  23.252  1.00116.65           C  
ANISOU 3464  CB  LYS A 375    14941  14848  14532    274   -515    475       C  
ATOM   3465  CG  LYS A 375      24.622  29.439  24.221  1.00110.83           C  
ANISOU 3465  CG  LYS A 375    14222  14152  13738    218   -519    481       C  
ATOM   3466  CD  LYS A 375      23.772  30.425  25.007  1.00105.84           C  
ANISOU 3466  CD  LYS A 375    13643  13443  13129    204   -519    457       C  
ATOM   3467  CE  LYS A 375      24.225  31.852  24.758  1.00106.48           C  
ANISOU 3467  CE  LYS A 375    13777  13514  13168    130   -546    458       C  
ATOM   3468  NZ  LYS A 375      23.242  32.842  25.264  1.00104.95           N  
ANISOU 3468  NZ  LYS A 375    13644  13228  13004    126   -545    434       N  
TER    3469      LYS A 375                                                      
HETATM 3470  N   1OZ A1501       5.723  21.373  54.143  1.00 73.37           N  
ANISOU 3470  N   1OZ A1501     9383   9045   9450    308   -101   -275       N  
HETATM 3471  CA  1OZ A1501       6.262  21.979  55.339  1.00 75.44           C  
ANISOU 3471  CA  1OZ A1501     9628   9332   9705    252    -97   -274       C  
HETATM 3472  C   1OZ A1501       5.103  22.266  56.330  1.00 81.17           C  
ANISOU 3472  C   1OZ A1501    10348  10044  10448    224    -99   -340       C  
HETATM 3473  O   1OZ A1501       4.855  21.627  57.363  1.00 84.89           O  
ANISOU 3473  O   1OZ A1501    10804  10540  10912    195    -91   -357       O  
HETATM 3474  CAA 1OZ A1501       3.148  23.694  56.846  1.00 75.49           C  
ANISOU 3474  CAA 1OZ A1501     9639   9272   9771    214   -112   -447       C  
HETATM 3475  CAD 1OZ A1501       3.154  20.500  50.054  1.00 57.45           C  
ANISOU 3475  CAD 1OZ A1501     7414   6953   7463    459   -118   -321       C  
HETATM 3476  CAE 1OZ A1501       4.532  20.247  50.126  1.00 62.24           C  
ANISOU 3476  CAE 1OZ A1501     8018   7575   8054    450   -110   -264       C  
HETATM 3477  CAF 1OZ A1501       2.546  21.373  50.978  1.00 63.70           C  
ANISOU 3477  CAF 1OZ A1501     8197   7737   8269    435   -127   -364       C  
HETATM 3478  CAG 1OZ A1501       4.699  26.091  52.553  1.00 69.02           C  
ANISOU 3478  CAG 1OZ A1501     8902   8358   8966    326   -141   -338       C  
HETATM 3479  CAH 1OZ A1501       4.146  26.514  53.814  1.00 76.20           C  
ANISOU 3479  CAH 1OZ A1501     9805   9264   9883    288   -134   -384       C  
HETATM 3480  CAI 1OZ A1501      11.645  17.383  59.551  1.00 62.91           C  
ANISOU 3480  CAI 1OZ A1501     7901   8078   7922    188     -7      8       C  
HETATM 3481  CAJ 1OZ A1501      11.915  18.493  60.418  1.00 64.67           C  
ANISOU 3481  CAJ 1OZ A1501     8096   8336   8140    115    -14     -5       C  
HETATM 3482  CAK 1OZ A1501       5.286  20.871  51.127  1.00 67.09           C  
ANISOU 3482  CAK 1OZ A1501     8621   8204   8666    412   -111   -251       C  
HETATM 3483  CAL 1OZ A1501       3.293  21.998  51.978  1.00 61.05           C  
ANISOU 3483  CAL 1OZ A1501     7854   7408   7934    395   -126   -352       C  
HETATM 3484  CAM 1OZ A1501       5.122  24.771  52.386  1.00 63.30           C  
ANISOU 3484  CAM 1OZ A1501     8157   7669   8224    336   -136   -307       C  
HETATM 3485  CAN 1OZ A1501       4.010  25.601  54.908  1.00 76.34           C  
ANISOU 3485  CAN 1OZ A1501     9795   9320   9892    258   -125   -399       C  
HETATM 3486  CAO 1OZ A1501      10.806  17.535  58.480  1.00 59.07           C  
ANISOU 3486  CAO 1OZ A1501     7452   7524   7470    222    -18    -30       C  
HETATM 3487  CAP 1OZ A1501      11.353  19.736  60.196  1.00 54.41           C  
ANISOU 3487  CAP 1OZ A1501     6810   6994   6869     83    -28    -55       C  
HETATM 3488  CAQ 1OZ A1501       9.322  19.369  57.232  1.00 50.25           C  
ANISOU 3488  CAQ 1OZ A1501     6372   6306   6415    217    -51   -121       C  
HETATM 3489  CAU 1OZ A1501       8.231  21.697  56.759  1.00 61.77           C  
ANISOU 3489  CAU 1OZ A1501     7856   7690   7923    186    -78   -200       C  
HETATM 3490  CAV 1OZ A1501       5.539  22.369  53.119  1.00 77.42           C  
ANISOU 3490  CAV 1OZ A1501     9913   9523   9981    331   -115   -279       C  
HETATM 3491  CAX 1OZ A1501       4.670  21.732  52.036  1.00 69.63           C  
ANISOU 3491  CAX 1OZ A1501     8938   8516   9003    382   -118   -295       C  
HETATM 3492  CAY 1OZ A1501       9.154  20.720  57.521  1.00 50.70           C  
ANISOU 3492  CAY 1OZ A1501     6427   6350   6486    172    -62   -152       C  
HETATM 3493  CAZ 1OZ A1501       4.976  23.800  53.509  1.00 71.17           C  
ANISOU 3493  CAZ 1OZ A1501     9131   8701   9211    309   -124   -321       C  
HETATM 3494  CBA 1OZ A1501       4.454  24.216  54.718  1.00 73.51           C  
ANISOU 3494  CBA 1OZ A1501     9418   8997   9514    270   -121   -365       C  
HETATM 3495  CBB 1OZ A1501      10.220  18.852  58.220  1.00 51.15           C  
ANISOU 3495  CBB 1OZ A1501     6456   6482   6495    192    -37    -79       C  
HETATM 3496  CBC 1OZ A1501      10.491  19.898  59.040  1.00 61.81           C  
ANISOU 3496  CBC 1OZ A1501     7786   7859   7842    128    -41    -90       C  
HETATM 3497  NAS 1OZ A1501       7.212  21.101  56.003  1.00 69.77           N  
ANISOU 3497  NAS 1OZ A1501     8889   8664   8957    235    -83   -229       N  
HETATM 3498  NAT 1OZ A1501       9.815  21.022  58.583  1.00 61.47           N  
ANISOU 3498  NAT 1OZ A1501     7764   7763   7829    118    -55   -137       N  
HETATM 3499  NBE 1OZ A1501       4.265  23.373  55.939  1.00 75.18           N  
ANISOU 3499  NBE 1OZ A1501     9607   9243   9716    236   -111   -382       N  
HETATM 3500  OAB 1OZ A1501       8.325  22.826  56.873  1.00 57.72           O  
ANISOU 3500  OAB 1OZ A1501     7349   7166   7417    155    -83   -214       O  
CONECT  612 1246                                                                
CONECT 1246  612                                                                
CONECT 3470 3471 3490                                                           
CONECT 3471 3470 3472 3497                                                      
CONECT 3472 3471 3473 3499                                                      
CONECT 3473 3472                                                                
CONECT 3474 3499                                                                
CONECT 3475 3476 3477                                                           
CONECT 3476 3475 3482                                                           
CONECT 3477 3475 3483                                                           
CONECT 3478 3479 3484                                                           
CONECT 3479 3478 3485                                                           
CONECT 3480 3481 3486                                                           
CONECT 3481 3480 3487                                                           
CONECT 3482 3476 3491                                                           
CONECT 3483 3477 3491                                                           
CONECT 3484 3478 3493                                                           
CONECT 3485 3479 3494                                                           
CONECT 3486 3480 3495                                                           
CONECT 3487 3481 3496                                                           
CONECT 3488 3492 3495                                                           
CONECT 3489 3492 3497 3500                                                      
CONECT 3490 3470 3491 3493                                                      
CONECT 3491 3482 3483 3490                                                      
CONECT 3492 3488 3489 3498                                                      
CONECT 3493 3484 3490 3494                                                      
CONECT 3494 3485 3493 3499                                                      
CONECT 3495 3486 3488 3496                                                      
CONECT 3496 3487 3495 3498                                                      
CONECT 3497 3471 3489                                                           
CONECT 3498 3492 3496                                                           
CONECT 3499 3472 3474 3494                                                      
CONECT 3500 3489                                                                
MASTER      364    0    1   24    5    0    0    6 3499    1   33   42          
END