HEADER    MEMBRANE PROTEIN                        19-JUL-21   7FEE              
TITLE     CRYSTAL STRUCTURE OF PROTEIN L                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CANNABINOID RECEPTOR 1,GLGA GLYCOGEN SYNTHASE;             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CB-R,CB1,CANN6,GLYCOGEN SYNTHASE;                           
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 OTHER_DETAILS: CANNABINOID RECEPTOR 1 INSERTED WITH GLGA GLYCOGEN    
COMPND   8 SYNTHASE                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, PYROCOCCUS ABYSSI GE5;            
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 272844;                                        
SOURCE   5 GENE: CNR1, CNR, PAB2292;                                            
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC                                  
KEYWDS    SIGNAL PROTEIN, MEMBRANE PROTEIN, GPCR                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.WANG,C.ZHAO,Z.SHAO                                                  
REVDAT   2   10-AUG-22 7FEE    1       JRNL                                     
REVDAT   1   15-JUN-22 7FEE    0                                                
JRNL        AUTH   X.YANG,X.WANG,Z.XU,C.WU,Y.ZHOU,Y.WANG,G.LIN,K.LI,M.WU,A.XIA, 
JRNL        AUTH 2 J.LIU,L.CHENG,J.ZOU,W.YAN,Z.SHAO,S.YANG                      
JRNL        TITL   MOLECULAR MECHANISM OF ALLOSTERIC MODULATION FOR THE         
JRNL        TITL 2 CANNABINOID RECEPTOR CB1.                                    
JRNL        REF    NAT.CHEM.BIOL.                V.  18   831 2022              
JRNL        REFN                   ESSN 1552-4469                               
JRNL        PMID   35637350                                                     
JRNL        DOI    10.1038/S41589-022-01038-Y                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.60                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 17234                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.295                           
REMARK   3   R VALUE            (WORKING SET) : 0.293                           
REMARK   3   FREE R VALUE                     : 0.319                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.270                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1597                            
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 42.6000 -  6.0000    1.00     1551   159  0.2454 0.2820        
REMARK   3     2  6.0000 -  4.7600    1.00     1449   148  0.2875 0.2948        
REMARK   3     3  4.7600 -  4.1600    1.00     1435   147  0.2628 0.2983        
REMARK   3     4  4.1600 -  3.7800    1.00     1423   145  0.2846 0.2998        
REMARK   3     5  3.7800 -  3.5100    1.00     1420   145  0.3353 0.3557        
REMARK   3     6  3.5100 -  3.3000    1.00     1402   142  0.3415 0.3697        
REMARK   3     7  3.3000 -  3.1400    1.00     1398   144  0.3495 0.3692        
REMARK   3     8  3.1400 -  3.0000    1.00     1407   143  0.3676 0.4191        
REMARK   3     9  3.0000 -  2.8900    1.00     1373   140  0.4114 0.4984        
REMARK   3    10  2.8900 -  2.7900    1.00     1381   141  0.4389 0.3990        
REMARK   3    11  2.7900 -  2.7000    0.99     1398   143  0.4668 0.4948        
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)     : 0.520            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.830           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 86.93                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 107.2                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   9.5811  14.4860  18.5805              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6793 T22:   0.5885                                     
REMARK   3      T33:   0.7068 T12:   0.1093                                     
REMARK   3      T13:   0.0066 T23:   0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8017 L22:   1.0940                                     
REMARK   3      L33:   3.5103 L12:  -0.1493                                     
REMARK   3      L13:   1.5675 L23:  -0.2173                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0487 S12:  -0.6682 S13:  -0.2358                       
REMARK   3      S21:   0.3296 S22:   0.1335 S23:  -0.2400                       
REMARK   3      S31:   0.2689 S32:   0.1431 S33:  -0.1589                       
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 7FEE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-AUG-21.                  
REMARK 100 THE DEPOSITION ID IS D_1300023348.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-OCT-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL32XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17318                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 32.70                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.79                     
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         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 5U09                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25-36% PEG 300, 100MM MES PH 6.0, 120    
REMARK 280  -190MM MAGNESIUM SULFATE, LIPIDIC CUBIC PHASE, TEMPERATURE 293K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.16500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       92.10000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.16500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       92.10000            
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     MET A    42                                                      
REMARK 465     LYS A    43                                                      
REMARK 465     THR A    44                                                      
REMARK 465     ILE A    45                                                      
REMARK 465     ILE A    46                                                      
REMARK 465     ALA A    47                                                      
REMARK 465     LEU A    48                                                      
REMARK 465     SER A    49                                                      
REMARK 465     TYR A    50                                                      
REMARK 465     ILE A    51                                                      
REMARK 465     PHE A    52                                                      
REMARK 465     CYS A    53                                                      
REMARK 465     LEU A    54                                                      
REMARK 465     VAL A    55                                                      
REMARK 465     PHE A    56                                                      
REMARK 465     ALA A    57                                                      
REMARK 465     ASP A    58                                                      
REMARK 465     TYR A    59                                                      
REMARK 465     LYS A    60                                                      
REMARK 465     ASP A    61                                                      
REMARK 465     ASP A    62                                                      
REMARK 465     ASP A    63                                                      
REMARK 465     ASP A    64                                                      
REMARK 465     ALA A    65                                                      
REMARK 465     MET A    66                                                      
REMARK 465     ASP A    67                                                      
REMARK 465     GLN A    68                                                      
REMARK 465     VAL A    69                                                      
REMARK 465     ASN A    70                                                      
REMARK 465     ILE A    71                                                      
REMARK 465     THR A    72                                                      
REMARK 465     GLU A    73                                                      
REMARK 465     PHE A    74                                                      
REMARK 465     TYR A    75                                                      
REMARK 465     ASN A    76                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     SER A    78                                                      
REMARK 465     LEU A    79                                                      
REMARK 465     SER A    80                                                      
REMARK 465     SER A    81                                                      
REMARK 465     PHE A    82                                                      
REMARK 465     GLU A    83                                                      
REMARK 465     ASN A    84                                                      
REMARK 465     LEU A    85                                                      
REMARK 465     TYR A    86                                                      
REMARK 465     PHE A    87                                                      
REMARK 465     GLN A    88                                                      
REMARK 465     GLY A    89                                                      
REMARK 465     LYS A    90                                                      
REMARK 465     GLU A    91                                                      
REMARK 465     ASN A    92                                                      
REMARK 465     GLU A    93                                                      
REMARK 465     GLU A    94                                                      
REMARK 465     ASN A    95                                                      
REMARK 465     ILE A    96                                                      
REMARK 465     SER A   414                                                      
REMARK 465     GLU A   415                                                      
REMARK 465     ASN A   416                                                      
REMARK 465     LEU A   417                                                      
REMARK 465     TYR A   418                                                      
REMARK 465     PHE A   419                                                      
REMARK 465     GLN A   420                                                      
REMARK 465     GLY 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 465     HIS A   427                                                      
REMARK 465     HIS A   428                                                      
REMARK 465     HIS A   429                                                      
REMARK 465     HIS A   430                                                      
REMARK 465     HIS A   431                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 220    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1016    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1019    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A1029    CG   SD   CE                                        
REMARK 470     ARG A1043    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A1107    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLU A  1056     OG   SER A  1059              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OH   TYR A  1011     OE2  GLU A  1078     1455     2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A 143       30.66    -94.26                                   
REMARK 500    LYS A 183       52.88   -114.16                                   
REMARK 500    TYR A 224      -43.45   -132.52                                   
REMARK 500    SER A 262     -163.20   -108.73                                   
REMARK 500    HIS A 270      -13.48     69.46                                   
REMARK 500    TRP A1007       56.48   -105.60                                   
REMARK 500    THR A1013       76.05   -114.26                                   
REMARK 500    PHE A1027      -64.30   -132.88                                   
REMARK 500    PHE A1041       41.44   -108.32                                   
REMARK 500    GLN A1045      -81.28   -125.05                                   
REMARK 500    PRO A1118       47.42    -91.61                                   
REMARK 500    GLU A1122       73.49   -157.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1317        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH A1318        DISTANCE =  6.87 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLA A 1213                                                       
REMARK 610     OLA A 1214                                                       
REMARK 610     OLA A 1215                                                       
REMARK 610     OLA A 1216                                                       
DBREF  7FEE A   67    82  UNP    P21554   CNR1_HUMAN      74     89             
DBREF  7FEE A   90   305  UNP    P21554   CNR1_HUMAN      90    305             
DBREF  7FEE A 1001  1196  UNP    Q9V2J8   Q9V2J8_PYRAB   218    413             
DBREF  7FEE A  333   414  UNP    P21554   CNR1_HUMAN     333    414             
SEQADV 7FEE MET A   42  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE LYS A   43  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE THR A   44  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE ILE A   45  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE ILE A   46  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE ALA A   47  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE LEU A   48  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE SER A   49  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE TYR A   50  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE ILE A   51  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE PHE A   52  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE CYS A   53  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE LEU A   54  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE VAL A   55  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE PHE A   56  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE ALA A   57  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE ASP A   58  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE TYR A   59  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE LYS A   60  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE ASP A   61  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE ASP A   62  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE ASP A   63  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE ASP A   64  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE ALA A   65  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE MET A   66  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE GLU A   83  UNP  P21554              LINKER                         
SEQADV 7FEE ASN A   84  UNP  P21554              LINKER                         
SEQADV 7FEE LEU A   85  UNP  P21554              LINKER                         
SEQADV 7FEE TYR A   86  UNP  P21554              LINKER                         
SEQADV 7FEE PHE A   87  UNP  P21554              LINKER                         
SEQADV 7FEE GLN A   88  UNP  P21554              LINKER                         
SEQADV 7FEE GLY A   89  UNP  P21554              LINKER                         
SEQADV 7FEE LYS A  203  UNP  P21554    SER   203 ENGINEERED MUTATION            
SEQADV 7FEE ALA A  210  UNP  P21554    THR   210 ENGINEERED MUTATION            
SEQADV 7FEE LYS A  273  UNP  P21554    GLU   273 ENGINEERED MUTATION            
SEQADV 7FEE VAL A  283  UNP  P21554    THR   283 ENGINEERED MUTATION            
SEQADV 7FEE GLU A  340  UNP  P21554    ARG   340 ENGINEERED MUTATION            
SEQADV 7FEE ASP A  393  UNP  P21554    ASN   393 ENGINEERED MUTATION            
SEQADV 7FEE GLU A  415  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE ASN A  416  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE LEU A  417  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE TYR A  418  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE PHE A  419  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE GLN A  420  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE GLY A  421  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE HIS A  422  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE HIS A  423  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE HIS A  424  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE HIS A  425  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE HIS A  426  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE HIS A  427  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE HIS A  428  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE HIS A  429  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE HIS A  430  UNP  P21554              EXPRESSION TAG                 
SEQADV 7FEE HIS A  431  UNP  P21554              EXPRESSION TAG                 
SEQRES   1 A  559  MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU          
SEQRES   2 A  559  VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA MET ASP          
SEQRES   3 A  559  GLN VAL ASN ILE THR GLU PHE TYR ASN LYS SER LEU SER          
SEQRES   4 A  559  SER PHE GLU ASN LEU TYR PHE GLN GLY LYS GLU ASN GLU          
SEQRES   5 A  559  GLU ASN ILE GLN CYS GLY GLU ASN PHE MET ASP ILE GLU          
SEQRES   6 A  559  CYS PHE MET VAL LEU ASN PRO SER GLN GLN LEU ALA ILE          
SEQRES   7 A  559  ALA VAL LEU SER LEU THR LEU GLY THR PHE THR VAL LEU          
SEQRES   8 A  559  GLU ASN LEU LEU VAL LEU CYS VAL ILE LEU HIS SER ARG          
SEQRES   9 A  559  SER LEU ARG CYS ARG PRO SER TYR HIS PHE ILE GLY SER          
SEQRES  10 A  559  LEU ALA VAL ALA ASP LEU LEU GLY SER VAL ILE PHE VAL          
SEQRES  11 A  559  TYR SER PHE ILE ASP PHE HIS VAL PHE HIS ARG LYS ASP          
SEQRES  12 A  559  SER ARG ASN VAL PHE LEU PHE LYS LEU GLY GLY VAL THR          
SEQRES  13 A  559  ALA SER PHE THR ALA LYS VAL GLY SER LEU PHE LEU ALA          
SEQRES  14 A  559  ALA ILE ASP ARG TYR ILE SER ILE HIS ARG PRO LEU ALA          
SEQRES  15 A  559  TYR LYS ARG ILE VAL THR ARG PRO LYS ALA VAL VAL ALA          
SEQRES  16 A  559  PHE CYS LEU MET TRP THR ILE ALA ILE VAL ILE ALA VAL          
SEQRES  17 A  559  LEU PRO LEU LEU GLY TRP ASN CYS GLU LYS LEU GLN SER          
SEQRES  18 A  559  VAL CYS SER ASP ILE PHE PRO HIS ILE ASP LYS THR TYR          
SEQRES  19 A  559  LEU MET PHE TRP ILE GLY VAL VAL SER VAL LEU LEU LEU          
SEQRES  20 A  559  PHE ILE VAL TYR ALA TYR MET TYR ILE LEU TRP LYS ALA          
SEQRES  21 A  559  HIS SER HIS ALA GLY ILE ASP CYS SER PHE TRP ASN GLU          
SEQRES  22 A  559  SER TYR LEU THR GLY SER ARG ASP GLU ARG LYS LYS SER          
SEQRES  23 A  559  LEU LEU SER LYS PHE GLY MET ASP GLU GLY VAL THR PHE          
SEQRES  24 A  559  MET PHE ILE GLY ARG PHE ASP ARG GLY GLN LYS GLY VAL          
SEQRES  25 A  559  ASP VAL LEU LEU LYS ALA ILE GLU ILE LEU SER SER LYS          
SEQRES  26 A  559  LYS GLU PHE GLN GLU MET ARG PHE ILE ILE ILE GLY LYS          
SEQRES  27 A  559  GLY ASP PRO GLU LEU GLU GLY TRP ALA ARG SER LEU GLU          
SEQRES  28 A  559  GLU LYS HIS GLY ASN VAL LYS VAL ILE THR GLU MET LEU          
SEQRES  29 A  559  SER ARG GLU PHE VAL ARG GLU LEU TYR GLY SER VAL ASP          
SEQRES  30 A  559  PHE VAL ILE ILE PRO SER TYR PHE GLU PRO PHE GLY LEU          
SEQRES  31 A  559  VAL ALA LEU GLU ALA MET CYS LEU GLY ALA ILE PRO ILE          
SEQRES  32 A  559  ALA SER ALA VAL GLY GLY LEU ARG ASP ILE ILE THR ASN          
SEQRES  33 A  559  GLU THR GLY ILE LEU VAL LYS ALA GLY ASP PRO GLY GLU          
SEQRES  34 A  559  LEU ALA ASN ALA ILE LEU LYS ALA LEU GLU LEU SER ARG          
SEQRES  35 A  559  SER ASP LEU SER LYS PHE ARG GLU ASN CYS LYS LYS ARG          
SEQRES  36 A  559  ALA MET SER PHE SER ASP GLN ALA ARG MET ASP ILE GLU          
SEQRES  37 A  559  LEU ALA LYS THR LEU VAL LEU ILE LEU VAL VAL LEU ILE          
SEQRES  38 A  559  ILE CYS TRP GLY PRO LEU LEU ALA ILE MET VAL TYR ASP          
SEQRES  39 A  559  VAL PHE GLY LYS MET ASN LYS LEU ILE LYS THR VAL PHE          
SEQRES  40 A  559  ALA PHE CYS SER MET LEU CYS LEU LEU ASN SER THR VAL          
SEQRES  41 A  559  ASP PRO ILE ILE TYR ALA LEU ARG SER LYS ASP LEU ARG          
SEQRES  42 A  559  HIS ALA PHE ARG SER MET PHE PRO SER GLU ASN LEU TYR          
SEQRES  43 A  559  PHE GLN GLY HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS          
HET    CLR  A1201      28                                                       
HET    CLR  A1202      28                                                       
HET    9GF  A1203      27                                                       
HET    7IC  A1204      26                                                       
HET    PEG  A1205       7                                                       
HET    PEG  A1206       7                                                       
HET    GOL  A1207       6                                                       
HET    GOL  A1208       6                                                       
HET    GOL  A1209       6                                                       
HET    GOL  A1210       6                                                       
HET    OLC  A1211      25                                                       
HET    OLC  A1212      25                                                       
HET    OLA  A1213       8                                                       
HET    OLA  A1214       7                                                       
HET    OLA  A1215       8                                                       
HET    OLA  A1216       7                                                       
HETNAM     CLR CHOLESTEROL                                                      
HETNAM     9GF 2-[(1R,2R,5R)-5-HYDROXY-2-(3-HYDROXYPROPYL)CYCLOHEXYL]-          
HETNAM   2 9GF  5-(2-METHYLOCTAN-2-YL)PHENOL                                    
HETNAM     7IC 6-METHYL-3-[(1S)-2-NITRO-1-THIOPHEN-2-YL-ETHYL]-2-               
HETNAM   2 7IC  PHENYL-1H-INDOLE                                                
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     GOL GLYCEROL                                                         
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     OLA OLEIC ACID                                                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   2  CLR    2(C27 H46 O)                                                 
FORMUL   4  9GF    C24 H40 O3                                                   
FORMUL   5  7IC    C21 H18 N2 O2 S                                              
FORMUL   6  PEG    2(C4 H10 O3)                                                 
FORMUL   8  GOL    4(C3 H8 O3)                                                  
FORMUL  12  OLC    2(C21 H40 O4)                                                
FORMUL  14  OLA    4(C18 H34 O2)                                                
FORMUL  18  HOH   *18(H2 O)                                                     
HELIX    1 AA1 ASP A  104  MET A  109  5                                   6    
HELIX    2 AA2 ASN A  112  HIS A  143  1                                  32    
HELIX    3 AA3 SER A  144  CYS A  149  1                                   6    
HELIX    4 AA4 ARG A  150  VAL A  179  1                                  30    
HELIX    5 AA5 SER A  185  ARG A  220  1                                  36    
HELIX    6 AA6 THR A  229  LEU A  250  1                                  22    
HELIX    7 AA7 ASN A  256  GLN A  261  1                                   6    
HELIX    8 AA8 ASP A  272  SER A  303  1                                  32    
HELIX    9 AA9 ASN A 1008  LEU A 1012  5                                   5    
HELIX   10 AB1 SER A 1015  PHE A 1027  1                                  13    
HELIX   11 AB2 GLY A 1047  SER A 1060  1                                  14    
HELIX   12 AB3 LYS A 1061  GLN A 1065  5                                   5    
HELIX   13 AB4 ASP A 1076  GLY A 1091  1                                  16    
HELIX   14 AB5 VAL A 1105  VAL A 1112  1                                   8    
HELIX   15 AB6 GLY A 1125  CYS A 1133  1                                   9    
HELIX   16 AB7 GLY A 1144  ILE A 1150  1                                   7    
HELIX   17 AB8 ASP A 1162  SER A 1179  1                                  18    
HELIX   18 AB9 LEU A 1181  GLU A 1186  1                                   6    
HELIX   19 AC1 GLU A 1186  PHE A  368  1                                  47    
HELIX   20 AC2 ASN A  372  SER A  383  1                                  12    
HELIX   21 AC3 MET A  384  SER A  401  1                                  18    
HELIX   22 AC4 SER A  401  PHE A  412  1                                  12    
SHEET    1 AA1 6 VAL A1093  ILE A1096  0                                        
SHEET    2 AA1 6 MET A1067  ILE A1072  1  N  ILE A1071   O  ILE A1096           
SHEET    3 AA1 6 VAL A1033  ILE A1038  1  N  PHE A1035   O  ARG A1068           
SHEET    4 AA1 6 PHE A1114  ILE A1117  1  O  PHE A1114   N  MET A1036           
SHEET    5 AA1 6 ILE A1137  SER A1141  1  O  ILE A1139   N  VAL A1115           
SHEET    6 AA1 6 ILE A1156  VAL A1158  1  O  ILE A1156   N  ALA A1140           
SSBOND   1 CYS A   98    CYS A  107                          1555   1555  2.01  
SSBOND   2 CYS A  257    CYS A  264                          1555   1555  2.03  
CRYST1   43.790   74.330  184.200  90.00  90.00  90.00 P 2 21 21     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022836  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013454  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005429        0.00000                         
ATOM      1  N   GLN A  97      -2.950  14.982 -32.269  1.00123.73           N  
ANISOU    1  N   GLN A  97    16139  17718  13156    441    828  -1231       N  
ATOM      2  CA  GLN A  97      -3.837  16.150 -32.509  1.00123.98           C  
ANISOU    2  CA  GLN A  97    16163  17742  13201    232    801   -902       C  
ATOM      3  C   GLN A  97      -3.562  17.190 -31.422  1.00123.71           C  
ANISOU    3  C   GLN A  97    16071  17529  13405    106    886   -620       C  
ATOM      4  O   GLN A  97      -4.225  18.244 -31.434  1.00123.38           O  
ANISOU    4  O   GLN A  97    16030  17429  13418    -50    858   -338       O  
ATOM      5  CB  GLN A  97      -5.300  15.708 -32.468  1.00124.35           C  
ANISOU    5  CB  GLN A  97    16349  17515  13383    188    611   -948       C  
ATOM      6  CG  GLN A  97      -6.202  16.456 -33.439  1.00127.50           C  
ANISOU    6  CG  GLN A  97    16745  18080  13619     64    545   -754       C  
ATOM      7  CD  GLN A  97      -6.137  15.887 -34.835  1.00132.87           C  
ANISOU    7  CD  GLN A  97    17434  19104  13946    150    506   -951       C  
ATOM      8  OE1 GLN A  97      -5.674  14.769 -35.051  1.00133.98           O  
ANISOU    8  OE1 GLN A  97    17617  19292  13996    317    484  -1279       O  
ATOM      9  NE2 GLN A  97      -6.618  16.654 -35.798  1.00135.01           N  
ANISOU    9  NE2 GLN A  97    17674  19615  14009     49    482   -757       N  
ATOM     10  N   CYS A  98      -2.610  16.893 -30.528  1.00130.51           N  
ANISOU   10  N   CYS A  98    16887  18304  14396    184    972   -706       N  
ATOM     11  CA  CYS A  98      -2.336  17.799 -29.382  1.00129.56           C  
ANISOU   11  CA  CYS A  98    16725  17985  14518     73   1035   -473       C  
ATOM     12  C   CYS A  98      -0.852  18.142 -29.256  1.00128.83           C  
ANISOU   12  C   CYS A  98    16482  18133  14335     88   1195   -435       C  
ATOM     13  O   CYS A  98      -0.250  17.749 -28.245  1.00127.79           O  
ANISOU   13  O   CYS A  98    16335  17840  14378    164   1230   -531       O  
ATOM     14  CB  CYS A  98      -2.870  17.204 -28.090  1.00128.83           C  
ANISOU   14  CB  CYS A  98    16733  17470  14747    113    955   -563       C  
ATOM     15  SG  CYS A  98      -4.376  18.045 -27.541  1.00129.01           S  
ANISOU   15  SG  CYS A  98    16832  17194  14992    -44    846   -315       S  
ATOM     16  N   GLY A  99      -0.285  18.832 -30.247  1.00117.44           N  
ANISOU   16  N   GLY A  99    14922  17080  12620     10   1283   -292       N  
ATOM     17  CA  GLY A  99       1.077  19.314 -30.167  1.00116.12           C  
ANISOU   17  CA  GLY A  99    14583  17181  12358    -26   1433   -200       C  
ATOM     18  C   GLY A  99       1.110  20.807 -29.921  1.00114.98           C  
ANISOU   18  C   GLY A  99    14402  16991  12293   -273   1455    184       C  
ATOM     19  O   GLY A  99       2.169  21.379 -29.649  1.00114.17           O  
ANISOU   19  O   GLY A  99    14166  17040  12172   -360   1557    316       O  
ATOM     20  N   GLU A 100      -0.055  21.445 -30.012  1.00118.87           N  
ANISOU   20  N   GLU A 100    15016  17271  12879   -385   1343    363       N  
ATOM     21  CA  GLU A 100      -0.155  22.884 -29.813  1.00117.63           C  
ANISOU   21  CA  GLU A 100    14864  17019  12813   -602   1324    721       C  
ATOM     22  C   GLU A 100       0.150  23.259 -28.368  1.00115.92           C  
ANISOU   22  C   GLU A 100    14664  16471  12908   -635   1328    771       C  
ATOM     23  O   GLU A 100      -0.057  22.474 -27.439  1.00116.09           O  
ANISOU   23  O   GLU A 100    14740  16241  13127   -502   1306    564       O  
ATOM     24  CB  GLU A 100      -1.554  23.390 -30.182  1.00117.83           C  
ANISOU   24  CB  GLU A 100    15021  16867  12881   -664   1183    865       C  
ATOM     25  CG  GLU A 100      -2.194  22.745 -31.405  1.00119.65           C  
ANISOU   25  CG  GLU A 100    15277  17325  12860   -590   1135    741       C  
ATOM     26  CD  GLU A 100      -2.824  21.399 -31.107  1.00121.15           C  
ANISOU   26  CD  GLU A 100    15548  17343  13141   -405   1070    405       C  
ATOM     27  OE1 GLU A 100      -2.091  20.391 -31.128  1.00121.98           O  
ANISOU   27  OE1 GLU A 100    15606  17580  13162   -262   1137    140       O  
ATOM     28  OE2 GLU A 100      -4.044  21.348 -30.842  1.00120.99           O  
ANISOU   28  OE2 GLU A 100    15636  17057  13277   -403    944    410       O  
ATOM     29  N   ASN A 101       0.653  24.482 -28.187  1.00110.06           N  
ANISOU   29  N   ASN A 101    13881  15732  12205   -827   1345   1057       N  
ATOM     30  CA  ASN A 101       0.827  25.018 -26.841  1.00107.78           C  
ANISOU   30  CA  ASN A 101    13632  15109  12213   -876   1321   1126       C  
ATOM     31  C   ASN A 101      -0.517  25.143 -26.137  1.00106.28           C  
ANISOU   31  C   ASN A 101    13606  14506  12269   -822   1191   1118       C  
ATOM     32  O   ASN A 101      -0.661  24.761 -24.969  1.00105.95           O  
ANISOU   32  O   ASN A 101    13607  14197  12453   -732   1176    986       O  
ATOM     33  CB  ASN A 101       1.537  26.371 -26.906  1.00106.51           C  
ANISOU   33  CB  ASN A 101    13418  15014  12036  -1114   1329   1448       C  
ATOM     34  CG  ASN A 101       1.738  26.994 -25.538  1.00104.56           C  
ANISOU   34  CG  ASN A 101    13223  14420  12085  -1170   1285   1511       C  
ATOM     35  OD1 ASN A 101       1.800  26.294 -24.527  1.00104.22           O  
ANISOU   35  OD1 ASN A 101    13189  14200  12208  -1029   1304   1300       O  
ATOM     36  ND2 ASN A 101       1.837  28.318 -25.499  1.00103.77           N  
ANISOU   36  ND2 ASN A 101    13168  14212  12048  -1376   1213   1805       N  
ATOM     37  N   PHE A 102      -1.519  25.673 -26.840  1.00104.06           N  
ANISOU   37  N   PHE A 102    13407  14196  11935   -873   1094   1263       N  
ATOM     38  CA  PHE A 102      -2.885  25.745 -26.323  1.00102.96           C  
ANISOU   38  CA  PHE A 102    13395  13733  11990   -804    970   1248       C  
ATOM     39  C   PHE A 102      -3.636  24.509 -26.806  1.00105.13           C  
ANISOU   39  C   PHE A 102    13687  14079  12177   -665    948   1013       C  
ATOM     40  O   PHE A 102      -4.458  24.550 -27.724  1.00105.95           O  
ANISOU   40  O   PHE A 102    13827  14277  12152   -671    875   1061       O  
ATOM     41  CB  PHE A 102      -3.555  27.039 -26.764  1.00101.64           C  
ANISOU   41  CB  PHE A 102    13306  13483  11831   -921    858   1537       C  
ATOM     42  CG  PHE A 102      -2.965  28.263 -26.133  1.00 99.63           C  
ANISOU   42  CG  PHE A 102    13076  13062  11715  -1056    835   1755       C  
ATOM     43  CD1 PHE A 102      -2.991  28.427 -24.760  1.00 98.40           C  
ANISOU   43  CD1 PHE A 102    12966  12596  11825  -1003    814   1689       C  
ATOM     44  CD2 PHE A 102      -2.365  29.239 -26.909  1.00 99.07           C  
ANISOU   44  CD2 PHE A 102    12986  13152  11504  -1247    825   2028       C  
ATOM     45  CE1 PHE A 102      -2.443  29.547 -24.171  1.00 96.61           C  
ANISOU   45  CE1 PHE A 102    12777  12201  11728  -1127    772   1868       C  
ATOM     46  CE2 PHE A 102      -1.813  30.363 -26.326  1.00 98.04           C  
ANISOU   46  CE2 PHE A 102    12895  12842  11515  -1394    778   2231       C  
ATOM     47  CZ  PHE A 102      -1.850  30.515 -24.956  1.00 96.49           C  
ANISOU   47  CZ  PHE A 102    12755  12317  11590  -1328    747   2139       C  
ATOM     48  N   MET A 103      -3.332  23.384 -26.166  1.00110.02           N  
ANISOU   48  N   MET A 103    14289  14644  12870   -541    996    758       N  
ATOM     49  CA  MET A 103      -3.921  22.108 -26.535  1.00111.83           C  
ANISOU   49  CA  MET A 103    14550  14906  13035   -417    957    515       C  
ATOM     50  C   MET A 103      -5.323  21.977 -25.951  1.00110.65           C  
ANISOU   50  C   MET A 103    14490  14473  13079   -389    837    503       C  
ATOM     51  O   MET A 103      -5.661  22.601 -24.939  1.00108.11           O  
ANISOU   51  O   MET A 103    14196  13911  12972   -410    811    607       O  
ATOM     52  CB  MET A 103      -3.038  20.957 -26.049  1.00112.44           C  
ANISOU   52  CB  MET A 103    14589  15004  13128   -294   1031    257       C  
ATOM     53  CG  MET A 103      -3.060  20.759 -24.542  1.00110.14           C  
ANISOU   53  CG  MET A 103    14330  14397  13119   -253   1024    207       C  
ATOM     54  SD  MET A 103      -1.756  19.674 -23.923  1.00111.23           S  
ANISOU   54  SD  MET A 103    14412  14576  13277   -118   1113    -33       S  
ATOM     55  CE  MET A 103      -1.250  18.823 -25.413  1.00113.63           C  
ANISOU   55  CE  MET A 103    14666  15249  13258    -18   1147   -225       C  
ATOM     56  N   ASP A 104      -6.144  21.164 -26.609  1.00112.02           N  
ANISOU   56  N   ASP A 104    14702  14698  13164   -340    759    372       N  
ATOM     57  CA  ASP A 104      -7.475  20.882 -26.097  1.00111.56           C  
ANISOU   57  CA  ASP A 104    14700  14418  13270   -322    644    348       C  
ATOM     58  C   ASP A 104      -7.377  20.120 -24.781  1.00110.37           C  
ANISOU   58  C   ASP A 104    14566  14033  13336   -261    658    207       C  
ATOM     59  O   ASP A 104      -6.453  19.330 -24.563  1.00110.71           O  
ANISOU   59  O   ASP A 104    14602  14100  13364   -197    720     41       O  
ATOM     60  CB  ASP A 104      -8.282  20.075 -27.114  1.00114.16           C  
ANISOU   60  CB  ASP A 104    15061  14868  13448   -303    546    224       C  
ATOM     61  CG  ASP A 104      -8.631  20.879 -28.347  1.00116.36           C  
ANISOU   61  CG  ASP A 104    15327  15365  13521   -367    508    391       C  
ATOM     62  OD1 ASP A 104      -8.349  22.095 -28.364  1.00115.50           O  
ANISOU   62  OD1 ASP A 104    15197  15277  13411   -434    542    625       O  
ATOM     63  OD2 ASP A 104      -9.184  20.293 -29.302  1.00118.82           O  
ANISOU   63  OD2 ASP A 104    15658  15819  13668   -355    429    293       O  
ATOM     64  N   ILE A 105      -8.346  20.366 -23.896  1.00106.01           N  
ANISOU   64  N   ILE A 105    14030  13270  12978   -272    594    278       N  
ATOM     65  CA  ILE A 105      -8.344  19.728 -22.585  1.00104.17           C  
ANISOU   65  CA  ILE A 105    13808  12828  12944   -231    603    182       C  
ATOM     66  C   ILE A 105      -8.612  18.233 -22.667  1.00105.61           C  
ANISOU   66  C   ILE A 105    14034  12972  13120   -196    539    -31       C  
ATOM     67  O   ILE A 105      -8.405  17.520 -21.677  1.00102.54           O  
ANISOU   67  O   ILE A 105    13666  12425  12872   -164    544   -124       O  
ATOM     68  CB  ILE A 105      -9.378  20.399 -21.656  1.00100.32           C  
ANISOU   68  CB  ILE A 105    13309  12175  12635   -245    554    315       C  
ATOM     69  CG1 ILE A 105      -8.860  20.458 -20.219  1.00 95.76           C  
ANISOU   69  CG1 ILE A 105    12722  11428  12233   -213    617    304       C  
ATOM     70  CG2 ILE A 105     -10.702  19.661 -21.695  1.00101.70           C  
ANISOU   70  CG2 ILE A 105    13484  12315  12843   -260    443    264       C  
ATOM     71  CD1 ILE A 105      -9.633  21.424 -19.351  1.00 92.81           C  
ANISOU   71  CD1 ILE A 105    12329  10936  11999   -202    589    440       C  
ATOM     72  N   GLU A 106      -9.071  17.737 -23.822  1.00111.15           N  
ANISOU   72  N   GLU A 106    14762  13806  13664   -206    463   -110       N  
ATOM     73  CA  GLU A 106      -9.311  16.304 -23.971  1.00111.25           C  
ANISOU   73  CA  GLU A 106    14841  13757  13671   -179    372   -326       C  
ATOM     74  C   GLU A 106      -8.018  15.509 -23.890  1.00109.79           C  
ANISOU   74  C   GLU A 106    14687  13580  13447    -76    435   -518       C  
ATOM     75  O   GLU A 106      -8.035  14.328 -23.525  1.00108.03           O  
ANISOU   75  O   GLU A 106    14538  13207  13301    -35    360   -690       O  
ATOM     76  CB  GLU A 106     -10.004  16.018 -25.302  1.00113.83           C  
ANISOU   76  CB  GLU A 106    15194  14241  13814   -207    268   -383       C  
ATOM     77  CG  GLU A 106     -10.968  17.095 -25.760  1.00115.46           C  
ANISOU   77  CG  GLU A 106    15349  14541  13981   -280    230   -171       C  
ATOM     78  CD  GLU A 106     -12.229  16.521 -26.375  1.00117.60           C  
ANISOU   78  CD  GLU A 106    15640  14834  14208   -338     70   -219       C  
ATOM     79  OE1 GLU A 106     -12.146  15.455 -27.024  1.00118.57           O  
ANISOU   79  OE1 GLU A 106    15832  14993  14227   -321     -7   -425       O  
ATOM     80  OE2 GLU A 106     -13.302  17.138 -26.217  1.00118.18           O  
ANISOU   80  OE2 GLU A 106    15660  14895  14349   -394     10    -58       O  
ATOM     81  N   CYS A 107      -6.892  16.133 -24.227  1.00106.26           N  
ANISOU   81  N   CYS A 107    14181  13310  12882    -34    560   -486       N  
ATOM     82  CA  CYS A 107      -5.618  15.432 -24.284  1.00105.84           C  
ANISOU   82  CA  CYS A 107    14125  13332  12757     87    627   -674       C  
ATOM     83  C   CYS A 107      -4.974  15.263 -22.914  1.00102.37           C  
ANISOU   83  C   CYS A 107    13677  12702  12517    127    679   -680       C  
ATOM     84  O   CYS A 107      -3.968  14.554 -22.803  1.00101.14           O  
ANISOU   84  O   CYS A 107    13522  12573  12333    248    715   -849       O  
ATOM     85  CB  CYS A 107      -4.683  16.174 -25.235  1.00108.24           C  
ANISOU   85  CB  CYS A 107    14337  13958  12830     97    743   -618       C  
ATOM     86  SG  CYS A 107      -5.491  16.547 -26.807  1.00112.03           S  
ANISOU   86  SG  CYS A 107    14823  14682  13061     33    681   -559       S  
ATOM     87  N   PHE A 108      -5.525  15.895 -21.876  1.00 99.92           N  
ANISOU   87  N   PHE A 108    13355  12216  12395     46    681   -510       N  
ATOM     88  CA  PHE A 108      -5.152  15.558 -20.510  1.00 95.79           C  
ANISOU   88  CA  PHE A 108    12842  11492  12063     79    699   -529       C  
ATOM     89  C   PHE A 108      -5.961  14.384 -19.975  1.00 93.47           C  
ANISOU   89  C   PHE A 108    12640  10978  11896     77    571   -628       C  
ATOM     90  O   PHE A 108      -5.566  13.778 -18.974  1.00 90.05           O  
ANISOU   90  O   PHE A 108    12236  10384  11594    122    565   -682       O  
ATOM     91  CB  PHE A 108      -5.330  16.772 -19.591  1.00 93.42           C  
ANISOU   91  CB  PHE A 108    12487  11119  11891      5    756   -316       C  
ATOM     92  CG  PHE A 108      -4.597  18.005 -20.052  1.00 95.34           C  
ANISOU   92  CG  PHE A 108    12655  11534  12034    -31    852   -184       C  
ATOM     93  CD1 PHE A 108      -3.289  18.242 -19.656  1.00 95.04           C  
ANISOU   93  CD1 PHE A 108    12558  11557  11994      0    950   -193       C  
ATOM     94  CD2 PHE A 108      -5.221  18.932 -20.870  1.00 98.14           C  
ANISOU   94  CD2 PHE A 108    13000  11991  12300   -109    832    -35       C  
ATOM     95  CE1 PHE A 108      -2.616  19.377 -20.076  1.00 97.10           C  
ANISOU   95  CE1 PHE A 108    12748  11977  12167    -71   1024    -47       C  
ATOM     96  CE2 PHE A 108      -4.553  20.068 -21.293  1.00 99.18           C  
ANISOU   96  CE2 PHE A 108    13078  12262  12346   -169    901    115       C  
ATOM     97  CZ  PHE A 108      -3.251  20.291 -20.894  1.00 98.24           C  
ANISOU   97  CZ  PHE A 108    12899  12202  12228   -162    996    113       C  
ATOM     98  N   MET A 109      -7.082  14.055 -20.621  1.00 96.07           N  
ANISOU   98  N   MET A 109    13014  11302  12188     12    459   -639       N  
ATOM     99  CA  MET A 109      -7.912  12.907 -20.252  1.00 95.42           C  
ANISOU   99  CA  MET A 109    13020  11023  12214    -29    314   -719       C  
ATOM    100  C   MET A 109      -7.283  11.663 -20.873  1.00 95.56           C  
ANISOU  100  C   MET A 109    13142  11016  12151     79    238   -973       C  
ATOM    101  O   MET A 109      -7.678  11.178 -21.936  1.00 98.18           O  
ANISOU  101  O   MET A 109    13532  11415  12358     80    141  -1093       O  
ATOM    102  CB  MET A 109      -9.345  13.116 -20.718  1.00 97.36           C  
ANISOU  102  CB  MET A 109    13252  11296  12444   -152    217   -622       C  
ATOM    103  CG  MET A 109      -9.875  14.516 -20.446  1.00 97.90           C  
ANISOU  103  CG  MET A 109    13214  11446  12538   -207    292   -396       C  
ATOM    104  SD  MET A 109     -11.530  14.779 -21.105  1.00101.13           S  
ANISOU  104  SD  MET A 109    13585  11932  12909   -320    172   -291       S  
ATOM    105  CE  MET A 109     -11.898  16.409 -20.461  1.00 98.97           C  
ANISOU  105  CE  MET A 109    13200  11700  12703   -319    264    -51       C  
ATOM    106  N   VAL A 110      -6.284  11.132 -20.170  1.00 93.67           N  
ANISOU  106  N   VAL A 110    12931  10675  11984    187    270  -1068       N  
ATOM    107  CA  VAL A 110      -5.317  10.206 -20.744  1.00 94.54           C  
ANISOU  107  CA  VAL A 110    13111  10814  11996    356    239  -1320       C  
ATOM    108  C   VAL A 110      -5.622   8.747 -20.397  1.00 92.90           C  
ANISOU  108  C   VAL A 110    13068  10323  11908    380     50  -1477       C  
ATOM    109  O   VAL A 110      -4.840   7.856 -20.744  1.00 92.73           O  
ANISOU  109  O   VAL A 110    13131  10270  11833    551     -6  -1710       O  
ATOM    110  CB  VAL A 110      -3.896  10.605 -20.312  1.00 93.10           C  
ANISOU  110  CB  VAL A 110    12838  10741  11795    485    392  -1333       C  
ATOM    111  CG1 VAL A 110      -3.568  10.034 -18.938  1.00 89.81           C  
ANISOU  111  CG1 VAL A 110    12466  10077  11581    517    361  -1327       C  
ATOM    112  CG2 VAL A 110      -2.877  10.171 -21.347  1.00 95.15           C  
ANISOU  112  CG2 VAL A 110    13089  11211  11851    669    421  -1561       C  
ATOM    113  N   LEU A 111      -6.757   8.478 -19.756  1.00 91.70           N  
ANISOU  113  N   LEU A 111    12962   9971  11909    213    -60  -1353       N  
ATOM    114  CA  LEU A 111      -7.065   7.163 -19.212  1.00 90.03           C  
ANISOU  114  CA  LEU A 111    12906   9458  11844    187   -248  -1437       C  
ATOM    115  C   LEU A 111      -8.187   6.498 -20.004  1.00 92.09           C  
ANISOU  115  C   LEU A 111    13267   9645  12076     65   -441  -1503       C  
ATOM    116  O   LEU A 111      -9.140   7.161 -20.430  1.00 94.16           O  
ANISOU  116  O   LEU A 111    13447  10044  12286    -73   -429  -1374       O  
ATOM    117  CB  LEU A 111      -7.464   7.284 -17.738  1.00 86.93           C  
ANISOU  117  CB  LEU A 111    12478   8906  11647     62   -233  -1222       C  
ATOM    118  CG  LEU A 111      -6.381   7.863 -16.826  1.00 84.64           C  
ANISOU  118  CG  LEU A 111    12101   8659  11400    171    -69  -1161       C  
ATOM    119  CD1 LEU A 111      -6.986   8.213 -15.487  1.00 82.52           C  
ANISOU  119  CD1 LEU A 111    11772   8301  11282     32    -41   -931       C  
ATOM    120  CD2 LEU A 111      -5.234   6.883 -16.662  1.00 82.95           C  
ANISOU  120  CD2 LEU A 111    11993   8315  11210    361   -124  -1359       C  
ATOM    121  N   ASN A 112      -8.065   5.163 -20.199  1.00 95.67           N  
ANISOU  121  N   ASN A 112    13908   9870  12570    122   -639  -1712       N  
ATOM    122  CA  ASN A 112      -9.020   4.319 -20.909  1.00 97.24           C  
ANISOU  122  CA  ASN A 112    14242   9944  12760      8   -869  -1814       C  
ATOM    123  C   ASN A 112     -10.060   3.765 -19.937  1.00 96.44           C  
ANISOU  123  C   ASN A 112    14191   9586  12868   -237  -1020  -1631       C  
ATOM    124  O   ASN A 112      -9.793   3.646 -18.739  1.00 94.39           O  
ANISOU  124  O   ASN A 112    13924   9182  12757   -257   -987  -1505       O  
ATOM    125  CB  ASN A 112      -8.269   3.201 -21.663  1.00 97.61           C  
ANISOU  125  CB  ASN A 112    14480   9874  12732    217  -1018  -2157       C  
ATOM    126  CG  ASN A 112      -7.917   1.981 -20.792  1.00 95.72           C  
ANISOU  126  CG  ASN A 112    14428   9254  12688    262  -1194  -2236       C  
ATOM    127  OD1 ASN A 112      -8.755   1.410 -20.091  1.00 95.32           O  
ANISOU  127  OD1 ASN A 112    14460   8943  12814     48  -1355  -2097       O  
ATOM    128  ND2 ASN A 112      -6.654   1.571 -20.859  1.00 95.04           N  
ANISOU  128  ND2 ASN A 112    14403   9148  12559    544  -1169  -2456       N  
ATOM    129  N   PRO A 113     -11.259   3.394 -20.420  1.00 97.36           N  
ANISOU  129  N   PRO A 113    14348   9655  12988   -437  -1194  -1604       N  
ATOM    130  CA  PRO A 113     -12.374   3.140 -19.478  1.00 96.68           C  
ANISOU  130  CA  PRO A 113    14233   9427  13074   -713  -1295  -1361       C  
ATOM    131  C   PRO A 113     -12.076   2.113 -18.392  1.00 94.47           C  
ANISOU  131  C   PRO A 113    14096   8813  12984   -751  -1423  -1334       C  
ATOM    132  O   PRO A 113     -12.498   2.299 -17.242  1.00 93.34           O  
ANISOU  132  O   PRO A 113    13860   8641  12962   -901  -1376  -1085       O  
ATOM    133  CB  PRO A 113     -13.528   2.687 -20.389  1.00 99.50           C  
ANISOU  133  CB  PRO A 113    14641   9778  13386   -899  -1503  -1403       C  
ATOM    134  CG  PRO A 113     -12.988   2.546 -21.750  1.00101.61           C  
ANISOU  134  CG  PRO A 113    15004  10135  13469   -710  -1539  -1694       C  
ATOM    135  CD  PRO A 113     -11.609   3.090 -21.820  1.00100.27           C  
ANISOU  135  CD  PRO A 113    14795  10103  13200   -423  -1324  -1805       C  
ATOM    136  N   SER A 114     -11.353   1.039 -18.713  1.00 94.05           N  
ANISOU  136  N   SER A 114    14268   8513  12954   -605  -1589  -1584       N  
ATOM    137  CA  SER A 114     -10.951   0.090 -17.678  1.00 92.57           C  
ANISOU  137  CA  SER A 114    14232   7992  12948   -611  -1718  -1555       C  
ATOM    138  C   SER A 114      -9.988   0.734 -16.688  1.00 89.96           C  
ANISOU  138  C   SER A 114    13785   7751  12646   -457  -1487  -1455       C  
ATOM    139  O   SER A 114     -10.030   0.441 -15.486  1.00 88.56           O  
ANISOU  139  O   SER A 114    13620   7414  12616   -556  -1513  -1271       O  
ATOM    140  CB  SER A 114     -10.322  -1.143 -18.322  1.00 93.24           C  
ANISOU  140  CB  SER A 114    14593   7792  13041   -436  -1956  -1879       C  
ATOM    141  OG  SER A 114      -9.389  -0.757 -19.310  1.00 94.73           O  
ANISOU  141  OG  SER A 114    14757   8196  13039   -134  -1829  -2144       O  
ATOM    142  N   GLN A 115      -9.115   1.620 -17.175  1.00 88.12           N  
ANISOU  142  N   GLN A 115    13433   7783  12265   -229  -1266  -1562       N  
ATOM    143  CA  GLN A 115      -8.236   2.364 -16.279  1.00 86.25           C  
ANISOU  143  CA  GLN A 115    13064   7662  12046   -106  -1044  -1457       C  
ATOM    144  C   GLN A 115      -9.026   3.333 -15.405  1.00 85.30           C  
ANISOU  144  C   GLN A 115    12750   7689  11972   -307   -901  -1146       C  
ATOM    145  O   GLN A 115      -8.710   3.510 -14.224  1.00 83.40           O  
ANISOU  145  O   GLN A 115    12456   7408  11822   -312   -822   -998       O  
ATOM    146  CB  GLN A 115      -7.178   3.117 -17.087  1.00 86.69           C  
ANISOU  146  CB  GLN A 115    13024   7990  11923    145   -854  -1626       C  
ATOM    147  CG  GLN A 115      -6.048   2.251 -17.618  1.00 87.21           C  
ANISOU  147  CG  GLN A 115    13236   7960  11939    421   -940  -1935       C  
ATOM    148  CD  GLN A 115      -5.118   3.025 -18.529  1.00 88.65           C  
ANISOU  148  CD  GLN A 115    13290   8483  11909    635   -746  -2082       C  
ATOM    149  OE1 GLN A 115      -5.549   3.924 -19.252  1.00 90.04           O  
ANISOU  149  OE1 GLN A 115    13341   8920  11949    558   -632  -2018       O  
ATOM    150  NE2 GLN A 115      -3.836   2.682 -18.501  1.00 87.87           N  
ANISOU  150  NE2 GLN A 115    13212   8400  11775    902   -712  -2267       N  
ATOM    151  N   GLN A 116     -10.057   3.971 -15.965  1.00 86.31           N  
ANISOU  151  N   GLN A 116    12767   7999  12028   -457   -872  -1051       N  
ATOM    152  CA  GLN A 116     -10.857   4.914 -15.187  1.00 86.12           C  
ANISOU  152  CA  GLN A 116    12552   8134  12035   -614   -743   -780       C  
ATOM    153  C   GLN A 116     -11.599   4.205 -14.060  1.00 85.37           C  
ANISOU  153  C   GLN A 116    12484   7858  12093   -826   -868   -589       C  
ATOM    154  O   GLN A 116     -11.626   4.687 -12.922  1.00 83.94           O  
ANISOU  154  O   GLN A 116    12190   7737  11966   -863   -752   -404       O  
ATOM    155  CB  GLN A 116     -11.841   5.643 -16.101  1.00 89.12           C  
ANISOU  155  CB  GLN A 116    12817   8737  12305   -711   -719   -733       C  
ATOM    156  CG  GLN A 116     -11.343   5.858 -17.518  1.00 91.06           C  
ANISOU  156  CG  GLN A 116    13102   9112  12387   -558   -700   -947       C  
ATOM    157  CD  GLN A 116     -12.200   6.834 -18.303  1.00 93.45           C  
ANISOU  157  CD  GLN A 116    13265   9670  12571   -631   -640   -860       C  
ATOM    158  OE1 GLN A 116     -13.423   6.861 -18.159  1.00 94.42           O  
ANISOU  158  OE1 GLN A 116    13319   9821  12735   -823   -717   -713       O  
ATOM    159  NE2 GLN A 116     -11.563   7.620 -19.166  1.00 95.22           N  
ANISOU  159  NE2 GLN A 116    13443  10097  12641   -481   -512   -944       N  
ATOM    160  N   LEU A 117     -12.198   3.047 -14.355  1.00 87.87           N  
ANISOU  160  N   LEU A 117    12954   7959  12474   -977  -1114   -630       N  
ATOM    161  CA  LEU A 117     -12.916   2.311 -13.317  1.00 87.31           C  
ANISOU  161  CA  LEU A 117    12911   7719  12542  -1217  -1252   -422       C  
ATOM    162  C   LEU A 117     -11.985   1.928 -12.173  1.00 85.03           C  
ANISOU  162  C   LEU A 117    12696   7259  12351  -1121  -1229   -380       C  
ATOM    163  O   LEU A 117     -12.367   2.009 -11.000  1.00 84.29           O  
ANISOU  163  O   LEU A 117    12513   7191  12324  -1261  -1191   -142       O  
ATOM    164  CB  LEU A 117     -13.582   1.066 -13.908  1.00 88.83           C  
ANISOU  164  CB  LEU A 117    13290   7664  12796  -1400  -1553   -490       C  
ATOM    165  CG  LEU A 117     -14.912   0.610 -13.293  1.00 89.47           C  
ANISOU  165  CG  LEU A 117    13314   7713  12967  -1759  -1696   -224       C  
ATOM    166  CD1 LEU A 117     -15.668  -0.284 -14.265  1.00 91.48           C  
ANISOU  166  CD1 LEU A 117    13712   7809  13236  -1939  -1974   -323       C  
ATOM    167  CD2 LEU A 117     -14.697  -0.111 -11.969  1.00 87.91           C  
ANISOU  167  CD2 LEU A 117    13194   7299  12908  -1861  -1773    -48       C  
ATOM    168  N   ALA A 118     -10.751   1.529 -12.492  1.00 82.58           N  
ANISOU  168  N   ALA A 118    12535   6804  12037   -871  -1250   -610       N  
ATOM    169  CA  ALA A 118      -9.800   1.160 -11.448  1.00 80.59           C  
ANISOU  169  CA  ALA A 118    12351   6396  11873   -754  -1239   -582       C  
ATOM    170  C   ALA A 118      -9.390   2.375 -10.624  1.00 79.63           C  
ANISOU  170  C   ALA A 118    12018   6532  11706   -674   -967   -450       C  
ATOM    171  O   ALA A 118      -9.369   2.326  -9.389  1.00 78.38           O  
ANISOU  171  O   ALA A 118    11824   6339  11620   -742   -942   -265       O  
ATOM    172  CB  ALA A 118      -8.573   0.491 -12.066  1.00 80.28           C  
ANISOU  172  CB  ALA A 118    12497   6181  11825   -473  -1323   -881       C  
ATOM    173  N   ILE A 119      -9.052   3.478 -11.296  1.00 83.38           N  
ANISOU  173  N   ILE A 119    12359   7265  12057   -534   -773   -540       N  
ATOM    174  CA  ILE A 119      -8.669   4.689 -10.577  1.00 81.83           C  
ANISOU  174  CA  ILE A 119    11978   7291  11821   -464   -538   -428       C  
ATOM    175  C   ILE A 119      -9.848   5.239  -9.787  1.00 82.09           C  
ANISOU  175  C   ILE A 119    11859   7458  11873   -675   -484   -171       C  
ATOM    176  O   ILE A 119      -9.685   5.706  -8.653  1.00 80.89           O  
ANISOU  176  O   ILE A 119    11614   7377  11744   -672   -376    -32       O  
ATOM    177  CB  ILE A 119      -8.090   5.733 -11.550  1.00 82.66           C  
ANISOU  177  CB  ILE A 119    11990   7625  11792   -298   -371   -564       C  
ATOM    178  CG1 ILE A 119      -6.581   5.530 -11.687  1.00 82.20           C  
ANISOU  178  CG1 ILE A 119    11992   7530  11711    -50   -330   -753       C  
ATOM    179  CG2 ILE A 119      -8.427   7.149 -11.110  1.00 82.77           C  
ANISOU  179  CG2 ILE A 119    11805   7883  11762   -334   -175   -401       C  
ATOM    180  CD1 ILE A 119      -5.918   6.504 -12.611  1.00 82.58           C  
ANISOU  180  CD1 ILE A 119    11938   7822  11616     92   -168   -864       C  
ATOM    181  N   ALA A 120     -11.049   5.189 -10.367  1.00 80.38           N  
ANISOU  181  N   ALA A 120    11606   7301  11635   -851   -562   -112       N  
ATOM    182  CA  ALA A 120     -12.236   5.664  -9.666  1.00 81.06           C  
ANISOU  182  CA  ALA A 120    11523   7552  11724  -1042   -517    125       C  
ATOM    183  C   ALA A 120     -12.431   4.910  -8.357  1.00 80.59           C  
ANISOU  183  C   ALA A 120    11489   7371  11759  -1184   -596    307       C  
ATOM    184  O   ALA A 120     -12.380   5.504  -7.274  1.00 80.03           O  
ANISOU  184  O   ALA A 120    11295   7434  11680  -1168   -463    444       O  
ATOM    185  CB  ALA A 120     -13.472   5.526 -10.558  1.00 84.11           C  
ANISOU  185  CB  ALA A 120    11873   8009  12077  -1217   -626    150       C  
ATOM    186  N   VAL A 121     -12.627   3.587  -8.440  1.00 81.87           N  
ANISOU  186  N   VAL A 121    11826   7274  12009  -1324   -825    308       N  
ATOM    187  CA  VAL A 121     -12.905   2.790  -7.245  1.00 81.73           C  
ANISOU  187  CA  VAL A 121    11844   7131  12079  -1503   -930    518       C  
ATOM    188  C   VAL A 121     -11.810   2.974  -6.204  1.00 79.82           C  
ANISOU  188  C   VAL A 121    11614   6859  11855  -1333   -822    533       C  
ATOM    189  O   VAL A 121     -12.095   3.103  -5.010  1.00 79.96           O  
ANISOU  189  O   VAL A 121    11530   6978  11873  -1431   -766    745       O  
ATOM    190  CB  VAL A 121     -13.106   1.307  -7.614  1.00 82.39           C  
ANISOU  190  CB  VAL A 121    12163   6873  12269  -1660  -1227    490       C  
ATOM    191  CG1 VAL A 121     -11.835   0.694  -8.181  1.00 81.50           C  
ANISOU  191  CG1 VAL A 121    12285   6484  12198  -1413  -1319    220       C  
ATOM    192  CG2 VAL A 121     -13.581   0.523  -6.399  1.00 82.54           C  
ANISOU  192  CG2 VAL A 121    12203   6786  12371  -1907  -1350    766       C  
ATOM    193  N   LEU A 122     -10.547   3.041  -6.640  1.00 77.10           N  
ANISOU  193  N   LEU A 122    11373   6415  11507  -1071   -782    309       N  
ATOM    194  CA  LEU A 122      -9.450   3.263  -5.703  1.00 75.25           C  
ANISOU  194  CA  LEU A 122    11135   6173  11284   -899   -681    311       C  
ATOM    195  C   LEU A 122      -9.531   4.650  -5.081  1.00 74.69           C  
ANISOU  195  C   LEU A 122    10839   6414  11128   -852   -439    403       C  
ATOM    196  O   LEU A 122      -9.260   4.819  -3.887  1.00 73.64           O  
ANISOU  196  O   LEU A 122    10650   6331  10998   -843   -375    529       O  
ATOM    197  CB  LEU A 122      -8.106   3.065  -6.406  1.00 73.68           C  
ANISOU  197  CB  LEU A 122    11063   5847  11086   -628   -689     43       C  
ATOM    198  CG  LEU A 122      -6.912   2.658  -5.537  1.00 72.64           C  
ANISOU  198  CG  LEU A 122    11010   5580  11009   -465   -704     21       C  
ATOM    199  CD1 LEU A 122      -7.362   1.850  -4.328  1.00 73.32           C  
ANISOU  199  CD1 LEU A 122    11161   5515  11182   -651   -838    259       C  
ATOM    200  CD2 LEU A 122      -5.895   1.879  -6.354  1.00 72.77           C  
ANISOU  200  CD2 LEU A 122    11207   5390  11054   -245   -824   -242       C  
ATOM    201  N   SER A 123      -9.914   5.653  -5.872  1.00 75.91           N  
ANISOU  201  N   SER A 123    10870   6772  11201   -817   -318    341       N  
ATOM    202  CA  SER A 123     -10.055   7.003  -5.337  1.00 75.75           C  
ANISOU  202  CA  SER A 123    10656   7017  11107   -763   -115    416       C  
ATOM    203  C   SER A 123     -11.179   7.069  -4.311  1.00 77.30           C  
ANISOU  203  C   SER A 123    10721   7358  11292   -947   -105    652       C  
ATOM    204  O   SER A 123     -11.031   7.685  -3.249  1.00 76.65           O  
ANISOU  204  O   SER A 123    10535   7413  11176   -899     12    739       O  
ATOM    205  CB  SER A 123     -10.301   7.996  -6.474  1.00 76.29           C  
ANISOU  205  CB  SER A 123    10645   7243  11100   -696    -23    314       C  
ATOM    206  OG  SER A 123      -9.230   7.990  -7.402  1.00 75.87           O  
ANISOU  206  OG  SER A 123    10687   7113  11028   -529    -13    109       O  
ATOM    207  N   LEU A 124     -12.310   6.425  -4.604  1.00 80.07           N  
ANISOU  207  N   LEU A 124    11065   7698  11660  -1162   -232    756       N  
ATOM    208  CA  LEU A 124     -13.457   6.509  -3.704  1.00 81.82           C  
ANISOU  208  CA  LEU A 124    11120   8120  11846  -1349   -214    990       C  
ATOM    209  C   LEU A 124     -13.195   5.790  -2.386  1.00 81.30           C  
ANISOU  209  C   LEU A 124    11096   7980  11815  -1432   -262   1152       C  
ATOM    210  O   LEU A 124     -13.459   6.344  -1.313  1.00 82.57           O  
ANISOU  210  O   LEU A 124    11102   8363  11906  -1435   -145   1286       O  
ATOM    211  CB  LEU A 124     -14.716   5.963  -4.379  1.00 84.70           C  
ANISOU  211  CB  LEU A 124    11453   8510  12220  -1584   -350   1073       C  
ATOM    212  CG  LEU A 124     -15.442   6.945  -5.303  1.00 85.90           C  
ANISOU  212  CG  LEU A 124    11460   8881  12296  -1540   -268   1011       C  
ATOM    213  CD1 LEU A 124     -15.021   6.769  -6.762  1.00 85.44           C  
ANISOU  213  CD1 LEU A 124    11550   8658  12254  -1461   -345    797       C  
ATOM    214  CD2 LEU A 124     -16.953   6.818  -5.139  1.00 89.17           C  
ANISOU  214  CD2 LEU A 124    11693   9512  12675  -1780   -318   1209       C  
ATOM    215  N   THR A 125     -12.689   4.554  -2.439  1.00 80.59           N  
ANISOU  215  N   THR A 125    11217   7580  11823  -1492   -445   1140       N  
ATOM    216  CA  THR A 125     -12.476   3.811  -1.200  1.00 80.22           C  
ANISOU  216  CA  THR A 125    11223   7447  11810  -1589   -517   1322       C  
ATOM    217  C   THR A 125     -11.357   4.438  -0.380  1.00 78.91           C  
ANISOU  217  C   THR A 125    11038   7336  11610  -1359   -371   1263       C  
ATOM    218  O   THR A 125     -11.488   4.610   0.838  1.00 79.96           O  
ANISOU  218  O   THR A 125    11070   7626  11686  -1404   -306   1434       O  
ATOM    219  CB  THR A 125     -12.169   2.336  -1.480  1.00 79.64           C  
ANISOU  219  CB  THR A 125    11408   6987  11864  -1689   -777   1316       C  
ATOM    220  OG1 THR A 125     -11.839   1.685  -0.250  1.00 79.52           O  
ANISOU  220  OG1 THR A 125    11456   6879  11880  -1758   -847   1500       O  
ATOM    221  CG2 THR A 125     -10.980   2.186  -2.410  1.00 78.41           C  
ANISOU  221  CG2 THR A 125    11435   6596  11763  -1432   -813   1021       C  
ATOM    222  N   LEU A 126     -10.246   4.794  -1.032  1.00 76.93           N  
ANISOU  222  N   LEU A 126    10871   6980  11379  -1115   -320   1024       N  
ATOM    223  CA  LEU A 126      -9.160   5.442  -0.311  1.00 75.95           C  
ANISOU  223  CA  LEU A 126    10714   6919  11222   -909   -189    962       C  
ATOM    224  C   LEU A 126      -9.617   6.779   0.246  1.00 76.95           C  
ANISOU  224  C   LEU A 126    10625   7374  11240   -874      9   1016       C  
ATOM    225  O   LEU A 126      -9.384   7.079   1.421  1.00 77.65           O  
ANISOU  225  O   LEU A 126    10643   7580  11278   -843     80   1108       O  
ATOM    226  CB  LEU A 126      -7.945   5.619  -1.223  1.00 74.40           C  
ANISOU  226  CB  LEU A 126    10615   6596  11055   -676   -168    703       C  
ATOM    227  CG  LEU A 126      -6.816   4.599  -1.057  1.00 73.21           C  
ANISOU  227  CG  LEU A 126    10651   6179  10988   -564   -302    626       C  
ATOM    228  CD1 LEU A 126      -5.556   5.068  -1.768  1.00 71.72           C  
ANISOU  228  CD1 LEU A 126    10478   5986  10787   -308   -222    381       C  
ATOM    229  CD2 LEU A 126      -6.538   4.335   0.417  1.00 73.21           C  
ANISOU  229  CD2 LEU A 126    10643   6184  10990   -592   -315    801       C  
ATOM    230  N   GLY A 127     -10.306   7.577  -0.573  1.00 75.63           N  
ANISOU  230  N   GLY A 127    10354   7355  11030   -874     86    958       N  
ATOM    231  CA  GLY A 127     -10.793   8.864  -0.105  1.00 75.92           C  
ANISOU  231  CA  GLY A 127    10198   7679  10969   -816    251    991       C  
ATOM    232  C   GLY A 127     -11.778   8.740   1.041  1.00 78.44           C  
ANISOU  232  C   GLY A 127    10379   8207  11219   -965    265   1212       C  
ATOM    233  O   GLY A 127     -11.719   9.506   2.006  1.00 79.22           O  
ANISOU  233  O   GLY A 127    10364   8501  11235   -876    382   1244       O  
ATOM    234  N   THR A 128     -12.699   7.775   0.951  1.00 80.10           N  
ANISOU  234  N   THR A 128    10590   8392  11451  -1198    139   1368       N  
ATOM    235  CA  THR A 128     -13.627   7.530   2.050  1.00 82.09           C  
ANISOU  235  CA  THR A 128    10696   8871  11624  -1374    145   1611       C  
ATOM    236  C   THR A 128     -12.876   7.225   3.341  1.00 81.84           C  
ANISOU  236  C   THR A 128    10709   8819  11568  -1341    153   1699       C  
ATOM    237  O   THR A 128     -13.288   7.653   4.425  1.00 83.52           O  
ANISOU  237  O   THR A 128    10761   9313  11660  -1351    250   1824       O  
ATOM    238  CB  THR A 128     -14.577   6.383   1.691  1.00 82.66           C  
ANISOU  238  CB  THR A 128    10794   8868  11746  -1668    -28   1778       C  
ATOM    239  OG1 THR A 128     -15.311   6.721   0.506  1.00 83.36           O  
ANISOU  239  OG1 THR A 128    10825   9007  11842  -1695    -37   1694       O  
ATOM    240  CG2 THR A 128     -15.559   6.117   2.819  1.00 84.05           C  
ANISOU  240  CG2 THR A 128    10792   9323  11822  -1880    -19   2059       C  
ATOM    241  N   PHE A 129     -11.752   6.511   3.238  1.00 79.97           N  
ANISOU  241  N   PHE A 129    10683   8271  11432  -1281     52   1624       N  
ATOM    242  CA  PHE A 129     -10.962   6.200   4.424  1.00 79.41           C  
ANISOU  242  CA  PHE A 129    10664   8168  11342  -1235     44   1704       C  
ATOM    243  C   PHE A 129     -10.367   7.460   5.045  1.00 80.24           C  
ANISOU  243  C   PHE A 129    10661   8474  11353  -1008    226   1589       C  
ATOM    244  O   PHE A 129     -10.382   7.619   6.272  1.00 81.92           O  
ANISOU  244  O   PHE A 129    10790   8873  11464  -1011    280   1709       O  
ATOM    245  CB  PHE A 129      -9.857   5.202   4.071  1.00 77.66           C  
ANISOU  245  CB  PHE A 129    10687   7565  11254  -1180   -114   1620       C  
ATOM    246  CG  PHE A 129     -10.342   3.792   3.863  1.00 78.16           C  
ANISOU  246  CG  PHE A 129    10896   7390  11412  -1415   -338   1772       C  
ATOM    247  CD1 PHE A 129     -11.681   3.466   4.012  1.00 80.59           C  
ANISOU  247  CD1 PHE A 129    11099   7842  11680  -1693   -385   1994       C  
ATOM    248  CD2 PHE A 129      -9.448   2.789   3.525  1.00 76.95           C  
ANISOU  248  CD2 PHE A 129    10983   6866  11387  -1356   -515   1692       C  
ATOM    249  CE1 PHE A 129     -12.119   2.167   3.822  1.00 80.72           C  
ANISOU  249  CE1 PHE A 129    11261   7616  11793  -1939   -615   2145       C  
ATOM    250  CE2 PHE A 129      -9.880   1.490   3.334  1.00 77.47           C  
ANISOU  250  CE2 PHE A 129    11213   6669  11554  -1570   -752   1822       C  
ATOM    251  CZ  PHE A 129     -11.215   1.179   3.482  1.00 78.95           C  
ANISOU  251  CZ  PHE A 129    11308   6981  11710  -1878   -808   2056       C  
ATOM    252  N   THR A 130      -9.868   8.369   4.203  1.00 79.17           N  
ANISOU  252  N   THR A 130    10528   8309  11241   -823    311   1364       N  
ATOM    253  CA  THR A 130      -9.253   9.627   4.703  1.00 79.24           C  
ANISOU  253  CA  THR A 130    10457   8470  11179   -617    460   1240       C  
ATOM    254  C   THR A 130     -10.319  10.475   5.388  1.00 82.15           C  
ANISOU  254  C   THR A 130    10624   9178  11412   -631    573   1323       C  
ATOM    255  O   THR A 130     -10.045  11.000   6.472  1.00 83.56           O  
ANISOU  255  O   THR A 130    10736   9517  11496   -541    648   1332       O  
ATOM    256  CB  THR A 130      -8.655  10.462   3.567  1.00 76.73           C  
ANISOU  256  CB  THR A 130    10176   8066  10914   -459    516   1016       C  
ATOM    257  OG1 THR A 130      -9.655  11.304   2.995  1.00 78.76           O  
ANISOU  257  OG1 THR A 130    10312   8487  11125   -467    587    997       O  
ATOM    258  CG2 THR A 130      -8.004   9.636   2.483  1.00 74.29           C  
ANISOU  258  CG2 THR A 130    10028   7481  10717   -458    409    918       C  
ATOM    259  N   VAL A 131     -11.480  10.609   4.758  1.00 80.51           N  
ANISOU  259  N   VAL A 131    10317   9085  11187   -726    580   1367       N  
ATOM    260  CA  VAL A 131     -12.562  11.415   5.320  1.00 83.77           C  
ANISOU  260  CA  VAL A 131    10517   9847  11464   -713    685   1430       C  
ATOM    261  C   VAL A 131     -12.899  10.924   6.722  1.00 85.75           C  
ANISOU  261  C   VAL A 131    10676  10308  11597   -816    691   1631       C  
ATOM    262  O   VAL A 131     -12.774  11.662   7.706  1.00 87.24           O  
ANISOU  262  O   VAL A 131    10772  10709  11665   -682    790   1603       O  
ATOM    263  CB  VAL A 131     -13.790  11.387   4.393  1.00 84.22           C  
ANISOU  263  CB  VAL A 131    10478   9995  11529   -829    661   1476       C  
ATOM    264  CG1 VAL A 131     -14.961  12.118   5.032  1.00 86.62           C  
ANISOU  264  CG1 VAL A 131    10535  10696  11680   -805    762   1552       C  
ATOM    265  CG2 VAL A 131     -13.446  12.001   3.045  1.00 82.49           C  
ANISOU  265  CG2 VAL A 131    10341   9606  11397   -710    664   1281       C  
ATOM    266  N   LEU A 132     -13.263   9.642   6.834  1.00 86.21           N  
ANISOU  266  N   LEU A 132    10776  10293  11687  -1058    572   1836       N  
ATOM    267  CA  LEU A 132     -13.679   9.080   8.117  1.00 87.72           C  
ANISOU  267  CA  LEU A 132    10872  10702  11755  -1204    565   2076       C  
ATOM    268  C   LEU A 132     -12.606   9.248   9.188  1.00 87.86           C  
ANISOU  268  C   LEU A 132    10954  10711  11719  -1062    600   2043       C  
ATOM    269  O   LEU A 132     -12.912   9.611  10.330  1.00 89.87           O  
ANISOU  269  O   LEU A 132    11063  11284  11802  -1035    687   2129       O  
ATOM    270  CB  LEU A 132     -14.027   7.601   7.948  1.00 87.56           C  
ANISOU  270  CB  LEU A 132    10947  10504  11818  -1504    388   2302       C  
ATOM    271  CG  LEU A 132     -15.235   7.272   7.070  1.00 87.99           C  
ANISOU  271  CG  LEU A 132    10915  10611  11905  -1708    329   2388       C  
ATOM    272  CD1 LEU A 132     -15.119   5.859   6.521  1.00 86.62           C  
ANISOU  272  CD1 LEU A 132    10949  10075  11888  -1942    108   2498       C  
ATOM    273  CD2 LEU A 132     -16.533   7.449   7.841  1.00 89.73           C  
ANISOU  273  CD2 LEU A 132    10853  11295  11944  -1853    408   2604       C  
ATOM    274  N   GLU A 133     -11.344   8.978   8.847  1.00 86.32           N  
ANISOU  274  N   GLU A 133    10964  10179  11655   -964    531   1914       N  
ATOM    275  CA  GLU A 133     -10.285   9.049   9.850  1.00 85.56           C  
ANISOU  275  CA  GLU A 133    10928  10067  11514   -841    543   1892       C  
ATOM    276  C   GLU A 133     -10.024  10.483  10.294  1.00 87.07           C  
ANISOU  276  C   GLU A 133    11013  10472  11599   -607    695   1708       C  
ATOM    277  O   GLU A 133      -9.867  10.747  11.492  1.00 89.11           O  
ANISOU  277  O   GLU A 133    11203  10940  11716   -551    745   1754       O  
ATOM    278  CB  GLU A 133      -8.999   8.428   9.308  1.00 83.65           C  
ANISOU  278  CB  GLU A 133    10909   9436  11438   -775    430   1786       C  
ATOM    279  CG  GLU A 133      -9.009   6.920   9.249  1.00 83.51           C  
ANISOU  279  CG  GLU A 133    11039   9176  11516   -971    245   1971       C  
ATOM    280  CD  GLU A 133      -7.817   6.376   8.497  1.00 80.01           C  
ANISOU  280  CD  GLU A 133    10805   8355  11238   -858    133   1815       C  
ATOM    281  OE1 GLU A 133      -7.202   7.150   7.734  1.00 78.56           O  
ANISOU  281  OE1 GLU A 133    10630   8118  11100   -675    209   1576       O  
ATOM    282  OE2 GLU A 133      -7.491   5.181   8.670  1.00 80.78           O  
ANISOU  282  OE2 GLU A 133    11059   8218  11417   -948    -36   1935       O  
ATOM    283  N   ASN A 134      -9.976  11.423   9.347  1.00 83.35           N  
ANISOU  283  N   ASN A 134    10536   9945  11188   -471    756   1500       N  
ATOM    284  CA  ASN A 134      -9.550  12.779   9.679  1.00 84.57           C  
ANISOU  284  CA  ASN A 134    10641  10214  11278   -247    861   1307       C  
ATOM    285  C   ASN A 134     -10.634  13.554  10.419  1.00 87.88           C  
ANISOU  285  C   ASN A 134    10861  11013  11517   -197    964   1337       C  
ATOM    286  O   ASN A 134     -10.321  14.365  11.299  1.00 90.02           O  
ANISOU  286  O   ASN A 134    11087  11440  11677    -39   1026   1241       O  
ATOM    287  CB  ASN A 134      -9.118  13.520   8.415  1.00 82.30           C  
ANISOU  287  CB  ASN A 134    10425   9729  11115   -136    875   1102       C  
ATOM    288  CG  ASN A 134      -7.666  13.267   8.060  1.00 79.49           C  
ANISOU  288  CG  ASN A 134    10229   9094  10878    -75    819    994       C  
ATOM    289  OD1 ASN A 134      -6.757  13.753   8.734  1.00 78.10           O  
ANISOU  289  OD1 ASN A 134    10075   8926  10673     43    839    909       O  
ATOM    290  ND2 ASN A 134      -7.440  12.498   7.004  1.00 76.74           N  
ANISOU  290  ND2 ASN A 134     9986   8515  10656   -149    742    990       N  
ATOM    291  N   LEU A 135     -11.911  13.330  10.086  1.00 90.36           N  
ANISOU  291  N   LEU A 135    11046  11496  11791   -319    976   1457       N  
ATOM    292  CA  LEU A 135     -12.963  13.944  10.892  1.00 92.49           C  
ANISOU  292  CA  LEU A 135    11096  12181  11863   -264   1074   1499       C  
ATOM    293  C   LEU A 135     -12.981  13.354  12.293  1.00 93.46           C  
ANISOU  293  C   LEU A 135    11151  12538  11823   -346   1083   1680       C  
ATOM    294  O   LEU A 135     -13.335  14.045  13.256  1.00 94.93           O  
ANISOU  294  O   LEU A 135    11191  13061  11816   -215   1175   1645       O  
ATOM    295  CB  LEU A 135     -14.346  13.781  10.252  1.00 93.47           C  
ANISOU  295  CB  LEU A 135    11066  12479  11970   -388   1083   1606       C  
ATOM    296  CG  LEU A 135     -14.885  12.431   9.778  1.00 93.14           C  
ANISOU  296  CG  LEU A 135    11037  12352  12002   -693    980   1839       C  
ATOM    297  CD1 LEU A 135     -15.738  11.797  10.864  1.00 93.87           C  
ANISOU  297  CD1 LEU A 135    10946  12804  11915   -873    998   2104       C  
ATOM    298  CD2 LEU A 135     -15.724  12.643   8.526  1.00 92.72           C  
ANISOU  298  CD2 LEU A 135    10927  12277  12026   -730    966   1798       C  
ATOM    299  N   LEU A 136     -12.617  12.076  12.425  1.00 90.39           N  
ANISOU  299  N   LEU A 136    10869  11979  11498   -554    979   1873       N  
ATOM    300  CA  LEU A 136     -12.488  11.477  13.749  1.00 91.25           C  
ANISOU  300  CA  LEU A 136    10942  12274  11457   -640    968   2065       C  
ATOM    301  C   LEU A 136     -11.357  12.128  14.532  1.00 92.59           C  
ANISOU  301  C   LEU A 136    11185  12424  11572   -422    999   1898       C  
ATOM    302  O   LEU A 136     -11.496  12.396  15.732  1.00 93.84           O  
ANISOU  302  O   LEU A 136    11231  12903  11521   -365   1061   1944       O  
ATOM    303  CB  LEU A 136     -12.257   9.973  13.621  1.00 89.88           C  
ANISOU  303  CB  LEU A 136    10908  11846  11396   -900    815   2301       C  
ATOM    304  CG  LEU A 136     -12.296   9.174  14.924  1.00 91.18           C  
ANISOU  304  CG  LEU A 136    11035  12200  11407  -1052    777   2574       C  
ATOM    305  CD1 LEU A 136     -13.613   9.393  15.656  1.00 92.56           C  
ANISOU  305  CD1 LEU A 136    10933  12896  11340  -1145    883   2743       C  
ATOM    306  CD2 LEU A 136     -12.068   7.698  14.651  1.00 89.70           C  
ANISOU  306  CD2 LEU A 136    11025  11686  11370  -1305    590   2798       C  
ATOM    307  N   VAL A 137     -10.228  12.392  13.869  1.00 92.15           N  
ANISOU  307  N   VAL A 137    11306  12016  11689   -302    955   1702       N  
ATOM    308  CA  VAL A 137      -9.123  13.090  14.520  1.00 93.08           C  
ANISOU  308  CA  VAL A 137    11488  12108  11771   -105    974   1529       C  
ATOM    309  C   VAL A 137      -9.573  14.469  14.982  1.00 94.98           C  
ANISOU  309  C   VAL A 137    11594  12635  11859     98   1088   1351       C  
ATOM    310  O   VAL A 137      -9.319  14.879  16.121  1.00 96.13           O  
ANISOU  310  O   VAL A 137    11693  12995  11838    207   1122   1312       O  
ATOM    311  CB  VAL A 137      -7.914  13.184  13.571  1.00 90.49           C  
ANISOU  311  CB  VAL A 137    11340  11385  11657    -29    912   1355       C  
ATOM    312  CG1 VAL A 137      -6.853  14.108  14.147  1.00 91.96           C  
ANISOU  312  CG1 VAL A 137    11565  11568  11808    168    934   1158       C  
ATOM    313  CG2 VAL A 137      -7.333  11.806  13.304  1.00 89.20           C  
ANISOU  313  CG2 VAL A 137    11320  10949  11623   -175    784   1501       C  
ATOM    314  N   LEU A 138     -10.264  15.200  14.106  1.00 91.74           N  
ANISOU  314  N   LEU A 138    11126  12232  11498    164   1137   1235       N  
ATOM    315  CA  LEU A 138     -10.694  16.551  14.446  1.00 92.37           C  
ANISOU  315  CA  LEU A 138    11103  12538  11457    388   1221   1043       C  
ATOM    316  C   LEU A 138     -11.733  16.539  15.560  1.00 93.69           C  
ANISOU  316  C   LEU A 138    11059  13176  11363    397   1299   1156       C  
ATOM    317  O   LEU A 138     -11.686  17.379  16.465  1.00 94.21           O  
ANISOU  317  O   LEU A 138    11065  13466  11263    592   1349   1014       O  
ATOM    318  CB  LEU A 138     -11.238  17.249  13.201  1.00 91.12           C  
ANISOU  318  CB  LEU A 138    10937  12267  11419    451   1236    921       C  
ATOM    319  CG  LEU A 138     -10.173  17.698  12.197  1.00 88.85           C  
ANISOU  319  CG  LEU A 138    10834  11584  11339    507   1181    754       C  
ATOM    320  CD1 LEU A 138     -10.807  18.096  10.873  1.00 87.88           C  
ANISOU  320  CD1 LEU A 138    10704  11356  11329    509   1183    704       C  
ATOM    321  CD2 LEU A 138      -9.343  18.841  12.764  1.00 87.28           C  
ANISOU  321  CD2 LEU A 138    10700  11354  11109    713   1183    535       C  
ATOM    322  N   CYS A 139     -12.670  15.587  15.520  1.00 97.53           N  
ANISOU  322  N   CYS A 139    11425  13832  11800    181   1304   1410       N  
ATOM    323  CA  CYS A 139     -13.705  15.525  16.549  1.00 98.52           C  
ANISOU  323  CA  CYS A 139    11315  14461  11657    163   1387   1548       C  
ATOM    324  C   CYS A 139     -13.106  15.280  17.927  1.00 99.25           C  
ANISOU  324  C   CYS A 139    11414  14729  11570    179   1391   1613       C  
ATOM    325  O   CYS A 139     -13.535  15.888  18.916  1.00100.21           O  
ANISOU  325  O   CYS A 139    11379  15255  11442    332   1476   1552       O  
ATOM    326  CB  CYS A 139     -14.721  14.436  16.209  1.00 98.20           C  
ANISOU  326  CB  CYS A 139    11154  14542  11617   -129   1369   1846       C  
ATOM    327  SG  CYS A 139     -15.983  14.181  17.482  1.00100.89           S  
ANISOU  327  SG  CYS A 139    11171  15553  11608   -215   1471   2083       S  
ATOM    328  N   VAL A 140     -12.117  14.387  18.013  1.00 95.74           N  
ANISOU  328  N   VAL A 140    11145  13996  11237     38   1292   1729       N  
ATOM    329  CA  VAL A 140     -11.452  14.126  19.287  1.00 96.73           C  
ANISOU  329  CA  VAL A 140    11293  14258  11201     53   1276   1797       C  
ATOM    330  C   VAL A 140     -10.782  15.393  19.801  1.00 97.03           C  
ANISOU  330  C   VAL A 140    11366  14339  11163    353   1314   1484       C  
ATOM    331  O   VAL A 140     -10.888  15.739  20.984  1.00 97.76           O  
ANISOU  331  O   VAL A 140    11355  14787  11001    461   1366   1462       O  
ATOM    332  CB  VAL A 140     -10.441  12.973  19.139  1.00 96.28           C  
ANISOU  332  CB  VAL A 140    11440  13828  11315   -121   1140   1955       C  
ATOM    333  CG1 VAL A 140      -9.538  12.896  20.356  1.00 96.68           C  
ANISOU  333  CG1 VAL A 140    11541  13966  11226    -53   1110   1968       C  
ATOM    334  CG2 VAL A 140     -11.164  11.654  18.928  1.00 95.81           C  
ANISOU  334  CG2 VAL A 140    11349  13768  11286   -433   1078   2294       C  
ATOM    335  N   ILE A 141     -10.096  16.113  18.913  1.00 96.31           N  
ANISOU  335  N   ILE A 141    11418  13894  11280    483   1280   1239       N  
ATOM    336  CA  ILE A 141      -9.393  17.326  19.320  1.00 96.29           C  
ANISOU  336  CA  ILE A 141    11475  13872  11238    738   1284    944       C  
ATOM    337  C   ILE A 141     -10.384  18.445  19.621  1.00 95.74           C  
ANISOU  337  C   ILE A 141    11250  14134  10993    952   1376    771       C  
ATOM    338  O   ILE A 141     -10.292  19.116  20.656  1.00 95.99           O  
ANISOU  338  O   ILE A 141    11236  14414  10821   1135   1401    629       O  
ATOM    339  CB  ILE A 141      -8.382  17.747  18.238  1.00 94.69           C  
ANISOU  339  CB  ILE A 141    11462  13203  11311    781   1214    765       C  
ATOM    340  CG1 ILE A 141      -7.289  16.689  18.078  1.00 95.15           C  
ANISOU  340  CG1 ILE A 141    11664  12975  11515    626   1120    898       C  
ATOM    341  CG2 ILE A 141      -7.777  19.104  18.566  1.00 92.82           C  
ANISOU  341  CG2 ILE A 141    11285  12934  11047   1020   1202    464       C  
ATOM    342  CD1 ILE A 141      -6.259  17.039  17.027  1.00 93.17           C  
ANISOU  342  CD1 ILE A 141    11568  12322  11508    661   1061    736       C  
ATOM    343  N   LEU A 142     -11.352  18.657  18.724  1.00 99.31           N  
ANISOU  343  N   LEU A 142    11617  14601  11514    947   1417    772       N  
ATOM    344  CA  LEU A 142     -12.230  19.818  18.838  1.00 98.52           C  
ANISOU  344  CA  LEU A 142    11389  14758  11286   1194   1485    571       C  
ATOM    345  C   LEU A 142     -13.115  19.740  20.076  1.00 99.71           C  
ANISOU  345  C   LEU A 142    11307  15475  11101   1255   1578    649       C  
ATOM    346  O   LEU A 142     -13.373  20.761  20.723  1.00 99.66           O  
ANISOU  346  O   LEU A 142    11235  15712  10920   1530   1615    419       O  
ATOM    347  CB  LEU A 142     -13.090  19.957  17.582  1.00 97.74           C  
ANISOU  347  CB  LEU A 142    11238  14567  11333   1163   1499    584       C  
ATOM    348  CG  LEU A 142     -12.418  20.464  16.303  1.00 96.17           C  
ANISOU  348  CG  LEU A 142    11238  13883  11419   1188   1424    437       C  
ATOM    349  CD1 LEU A 142     -13.407  21.248  15.451  1.00 95.23           C  
ANISOU  349  CD1 LEU A 142    11038  13801  11343   1317   1447    334       C  
ATOM    350  CD2 LEU A 142     -11.195  21.304  16.616  1.00 94.42           C  
ANISOU  350  CD2 LEU A 142    11197  13426  11251   1344   1361    203       C  
ATOM    351  N   HIS A 143     -13.593  18.543  20.423  1.00102.45           N  
ANISOU  351  N   HIS A 143    11531  16047  11348   1002   1608    971       N  
ATOM    352  CA  HIS A 143     -14.525  18.377  21.533  1.00103.44           C  
ANISOU  352  CA  HIS A 143    11400  16765  11136   1017   1708   1097       C  
ATOM    353  C   HIS A 143     -13.831  18.031  22.846  1.00104.41           C  
ANISOU  353  C   HIS A 143    11549  17065  11057   1003   1698   1165       C  
ATOM    354  O   HIS A 143     -14.414  17.331  23.685  1.00105.35           O  
ANISOU  354  O   HIS A 143    11487  17608  10932    864   1756   1417       O  
ATOM    355  CB  HIS A 143     -15.572  17.317  21.191  1.00104.47           C  
ANISOU  355  CB  HIS A 143    11352  17095  11247    724   1743   1438       C  
ATOM    356  CG  HIS A 143     -16.827  17.428  22.001  1.00105.75           C  
ANISOU  356  CG  HIS A 143    11188  17917  11075    775   1868   1528       C  
ATOM    357  ND1 HIS A 143     -17.359  18.640  22.386  1.00105.78           N  
ANISOU  357  ND1 HIS A 143    11052  18249  10892   1128   1950   1244       N  
ATOM    358  CD2 HIS A 143     -17.646  16.479  22.513  1.00106.32           C  
ANISOU  358  CD2 HIS A 143    11039  18401  10956    519   1919   1873       C  
ATOM    359  CE1 HIS A 143     -18.457  18.433  23.092  1.00106.12           C  
ANISOU  359  CE1 HIS A 143    10782  18908  10630   1107   2062   1397       C  
ATOM    360  NE2 HIS A 143     -18.652  17.130  23.185  1.00106.86           N  
ANISOU  360  NE2 HIS A 143    10815  19074  10713    722   2048   1793       N  
ATOM    361  N   SER A 144     -12.603  18.496  23.053  1.00102.50           N  
ANISOU  361  N   SER A 144    11517  16526  10901   1130   1622    961       N  
ATOM    362  CA  SER A 144     -11.914  18.287  24.320  1.00103.26           C  
ANISOU  362  CA  SER A 144    11639  16800  10793   1149   1602    993       C  
ATOM    363  C   SER A 144     -11.128  19.542  24.660  1.00102.89           C  
ANISOU  363  C   SER A 144    11720  16638  10735   1451   1560    610       C  
ATOM    364  O   SER A 144     -10.245  19.950  23.900  1.00102.37           O  
ANISOU  364  O   SER A 144    11858  16102  10938   1485   1472    446       O  
ATOM    365  CB  SER A 144     -10.993  17.067  24.265  1.00103.86           C  
ANISOU  365  CB  SER A 144    11871  16571  11020    877   1502   1251       C  
ATOM    366  OG  SER A 144     -10.475  16.776  25.551  1.00105.48           O  
ANISOU  366  OG  SER A 144    12070  17012  10995    880   1485   1329       O  
ATOM    367  N   ARG A 145     -11.458  20.145  25.804  1.00108.09           N  
ANISOU  367  N   ARG A 145    12255  17741  11073   1664   1616    471       N  
ATOM    368  CA  ARG A 145     -10.797  21.371  26.237  1.00107.50           C  
ANISOU  368  CA  ARG A 145    12302  17587  10958   1960   1558     91       C  
ATOM    369  C   ARG A 145      -9.309  21.151  26.480  1.00108.24           C  
ANISOU  369  C   ARG A 145    12612  17341  11174   1882   1436     72       C  
ATOM    370  O   ARG A 145      -8.482  22.003  26.135  1.00107.28           O  
ANISOU  370  O   ARG A 145    12669  16868  11226   2009   1341   -196       O  
ATOM    371  CB  ARG A 145     -11.471  21.886  27.505  1.00108.06           C  
ANISOU  371  CB  ARG A 145    12186  18251  10621   2194   1640    -35       C  
ATOM    372  CG  ARG A 145     -11.140  23.311  27.893  1.00107.71           C  
ANISOU  372  CG  ARG A 145    12242  18172  10511   2553   1579   -477       C  
ATOM    373  CD  ARG A 145     -12.014  23.751  29.057  1.00108.80           C  
ANISOU  373  CD  ARG A 145    12162  18956  10223   2806   1676   -602       C  
ATOM    374  NE  ARG A 145     -11.345  23.562  30.340  1.00110.86           N  
ANISOU  374  NE  ARG A 145    12441  19460  10222   2825   1648   -608       N  
ATOM    375  CZ  ARG A 145     -11.287  22.414  31.004  1.00111.97           C  
ANISOU  375  CZ  ARG A 145    12478  19874  10189   2581   1695   -258       C  
ATOM    376  NH1 ARG A 145     -11.873  21.318  30.547  1.00111.38           N  
ANISOU  376  NH1 ARG A 145    12279  19867  10174   2285   1767    131       N  
ATOM    377  NH2 ARG A 145     -10.636  22.369  32.162  1.00112.96           N  
ANISOU  377  NH2 ARG A 145    12636  20211  10074   2629   1654   -296       N  
ATOM    378  N   SER A 146      -8.949  20.013  27.080  1.00103.86           N  
ANISOU  378  N   SER A 146    12039  16892  10531   1668   1425    365       N  
ATOM    379  CA  SER A 146      -7.552  19.740  27.397  1.00104.07           C  
ANISOU  379  CA  SER A 146    12246  16648  10649   1607   1305    361       C  
ATOM    380  C   SER A 146      -6.707  19.501  26.153  1.00104.14           C  
ANISOU  380  C   SER A 146    12439  16077  11051   1478   1216    371       C  
ATOM    381  O   SER A 146      -5.478  19.605  26.228  1.00105.06           O  
ANISOU  381  O   SER A 146    12706  15928  11282   1486   1111    277       O  
ATOM    382  CB  SER A 146      -7.453  18.532  28.331  1.00105.51           C  
ANISOU  382  CB  SER A 146    12362  17092  10636   1415   1304    699       C  
ATOM    383  OG  SER A 146      -8.114  17.404  27.784  1.00105.36           O  
ANISOU  383  OG  SER A 146    12272  17060  10701   1153   1341   1049       O  
ATOM    384  N   LEU A 147      -7.332  19.186  25.019  1.00103.45           N  
ANISOU  384  N   LEU A 147    12330  15818  11158   1363   1255    479       N  
ATOM    385  CA  LEU A 147      -6.610  18.934  23.777  1.00102.70           C  
ANISOU  385  CA  LEU A 147    12395  15215  11413   1247   1183    487       C  
ATOM    386  C   LEU A 147      -6.473  20.196  22.930  1.00100.55           C  
ANISOU  386  C   LEU A 147    12206  14686  11311   1415   1164    180       C  
ATOM    387  O   LEU A 147      -5.361  20.573  22.548  1.00 99.38           O  
ANISOU  387  O   LEU A 147    12210  14204  11345   1433   1075     40       O  
ATOM    388  CB  LEU A 147      -7.315  17.834  22.974  1.00102.32           C  
ANISOU  388  CB  LEU A 147    12296  15101  11482   1015   1214    778       C  
ATOM    389  CG  LEU A 147      -6.979  16.367  23.275  1.00102.60           C  
ANISOU  389  CG  LEU A 147    12361  15098  11524    775   1157   1109       C  
ATOM    390  CD1 LEU A 147      -5.482  16.155  23.333  1.00102.57           C  
ANISOU  390  CD1 LEU A 147    12533  14778  11661    779   1039   1055       C  
ATOM    391  CD2 LEU A 147      -7.628  15.891  24.562  1.00104.07           C  
ANISOU  391  CD2 LEU A 147    12392  15767  11384    722   1208   1316       C  
ATOM    392  N   ARG A 148      -7.594  20.863  22.640  1.00 98.83           N  
ANISOU  392  N   ARG A 148    11884  14634  11034   1536   1240     82       N  
ATOM    393  CA  ARG A 148      -7.598  22.034  21.770  1.00 96.37           C  
ANISOU  393  CA  ARG A 148    11658  14069  10891   1688   1211   -177       C  
ATOM    394  C   ARG A 148      -6.846  23.222  22.357  1.00 96.06           C  
ANISOU  394  C   ARG A 148    11730  13961  10809   1899   1128   -489       C  
ATOM    395  O   ARG A 148      -6.588  24.186  21.630  1.00 93.94           O  
ANISOU  395  O   ARG A 148    11577  13403  10715   1992   1065   -691       O  
ATOM    396  CB  ARG A 148      -9.040  22.443  21.458  1.00 95.32           C  
ANISOU  396  CB  ARG A 148    11370  14175  10673   1796   1302   -203       C  
ATOM    397  CG  ARG A 148      -9.827  22.903  22.675  1.00 96.66           C  
ANISOU  397  CG  ARG A 148    11377  14845  10506   2004   1370   -303       C  
ATOM    398  CD  ARG A 148     -11.325  22.743  22.468  1.00 96.74           C  
ANISOU  398  CD  ARG A 148    11161  15201  10393   2023   1484   -193       C  
ATOM    399  NE  ARG A 148     -12.088  23.282  23.587  1.00 97.27           N  
ANISOU  399  NE  ARG A 148    11054  15783  10122   2262   1556   -322       N  
ATOM    400  CZ  ARG A 148     -13.372  23.035  23.809  1.00 98.23           C  
ANISOU  400  CZ  ARG A 148    10919  16367  10038   2283   1673   -203       C  
ATOM    401  NH1 ARG A 148     -14.074  22.252  23.007  1.00 98.28           N  
ANISOU  401  NH1 ARG A 148    10817  16376  10149   2061   1722     57       N  
ATOM    402  NH2 ARG A 148     -13.965  23.584  24.865  1.00 99.25           N  
ANISOU  402  NH2 ARG A 148    10886  16986   9839   2533   1738   -352       N  
ATOM    403  N   CYS A 149      -6.448  23.154  23.627  1.00104.16           N  
ANISOU  403  N   CYS A 149    12735  15228  11613   1959   1110   -520       N  
ATOM    404  CA  CYS A 149      -5.761  24.305  24.278  1.00103.48           C  
ANISOU  404  CA  CYS A 149    12758  15095  11464   2163   1011   -837       C  
ATOM    405  C   CYS A 149      -4.253  24.229  24.020  1.00103.19           C  
ANISOU  405  C   CYS A 149    12890  14683  11635   2039    890   -856       C  
ATOM    406  O   CYS A 149      -3.580  25.252  24.210  1.00102.22           O  
ANISOU  406  O   CYS A 149    12886  14403  11549   2158    782  -1115       O  
ATOM    407  CB  CYS A 149      -6.022  24.315  25.777  1.00105.44           C  
ANISOU  407  CB  CYS A 149    12902  15807  11354   2297   1041   -885       C  
ATOM    408  SG  CYS A 149      -5.742  25.924  26.561  1.00106.05           S  
ANISOU  408  SG  CYS A 149    13082  15917  11296   2626    932  -1337       S  
ATOM    409  N   ARG A 150      -3.750  23.066  23.600  1.00100.65           N  
ANISOU  409  N   ARG A 150    12574  14226  11443   1812    897   -596       N  
ATOM    410  CA  ARG A 150      -2.325  22.879  23.362  1.00100.12           C  
ANISOU  410  CA  ARG A 150    12631  13854  11556   1704    791   -597       C  
ATOM    411  C   ARG A 150      -1.989  23.191  21.910  1.00 96.52           C  
ANISOU  411  C   ARG A 150    12267  13001  11406   1628    764   -633       C  
ATOM    412  O   ARG A 150      -2.635  22.652  21.004  1.00 95.27           O  
ANISOU  412  O   ARG A 150    12070  12775  11355   1535    834   -483       O  
ATOM    413  CB  ARG A 150      -1.912  21.451  23.688  1.00102.85           C  
ANISOU  413  CB  ARG A 150    12941  14260  11876   1532    795   -311       C  
ATOM    414  CG  ARG A 150      -1.467  21.239  25.126  1.00104.82           C  
ANISOU  414  CG  ARG A 150    13163  14784  11878   1579    753   -300       C  
ATOM    415  CD  ARG A 150      -0.456  22.289  25.552  1.00105.51           C  
ANISOU  415  CD  ARG A 150    13348  14772  11971   1696    636   -580       C  
ATOM    416  NE  ARG A 150      -0.182  22.242  26.983  1.00108.80           N  
ANISOU  416  NE  ARG A 150    13732  15498  12110   1773    595   -609       N  
ATOM    417  CZ  ARG A 150       0.363  23.233  27.673  1.00108.50           C  
ANISOU  417  CZ  ARG A 150    13753  15497  11975   1912    500   -878       C  
ATOM    418  NH1 ARG A 150       0.707  24.372  27.094  1.00106.00           N  
ANISOU  418  NH1 ARG A 150    13541  14909  11827   1979    424  -1135       N  
ATOM    419  NH2 ARG A 150       0.575  23.077  28.977  1.00110.02           N  
ANISOU  419  NH2 ARG A 150    13907  16002  11894   1975    466   -884       N  
ATOM    420  N   PRO A 151      -1.000  24.050  21.648  1.00 94.23           N  
ANISOU  420  N   PRO A 151    12092  12456  11253   1651    657   -822       N  
ATOM    421  CA  PRO A 151      -0.568  24.277  20.258  1.00 91.17           C  
ANISOU  421  CA  PRO A 151    11781  11716  11142   1551    632   -823       C  
ATOM    422  C   PRO A 151      -0.013  23.034  19.580  1.00 90.28           C  
ANISOU  422  C   PRO A 151    11655  11477  11170   1369    655   -597       C  
ATOM    423  O   PRO A 151       0.180  23.056  18.357  1.00 87.70           O  
ANISOU  423  O   PRO A 151    11366  10910  11045   1286    659   -572       O  
ATOM    424  CB  PRO A 151       0.507  25.366  20.390  1.00 90.28           C  
ANISOU  424  CB  PRO A 151    11781  11418  11106   1584    497  -1043       C  
ATOM    425  CG  PRO A 151       0.889  25.382  21.837  1.00 92.88           C  
ANISOU  425  CG  PRO A 151    12094  11977  11220   1667    443  -1121       C  
ATOM    426  CD  PRO A 151      -0.326  24.954  22.594  1.00 94.68           C  
ANISOU  426  CD  PRO A 151    12214  12554  11206   1769    549  -1051       C  
ATOM    427  N   SER A 152       0.256  21.959  20.326  1.00 93.54           N  
ANISOU  427  N   SER A 152    12021  12042  11479   1314    659   -436       N  
ATOM    428  CA  SER A 152       0.653  20.705  19.696  1.00 93.19           C  
ANISOU  428  CA  SER A 152    11975  11868  11564   1169    666   -225       C  
ATOM    429  C   SER A 152      -0.477  20.118  18.864  1.00 92.42           C  
ANISOU  429  C   SER A 152    11838  11759  11519   1100    755    -77       C  
ATOM    430  O   SER A 152      -0.221  19.468  17.843  1.00 90.90           O  
ANISOU  430  O   SER A 152    11677  11361  11499    998    753     17       O  
ATOM    431  CB  SER A 152       1.099  19.697  20.755  1.00 97.29           C  
ANISOU  431  CB  SER A 152    12466  12546  11952   1138    629    -73       C  
ATOM    432  OG  SER A 152       1.458  18.463  20.158  1.00 97.67           O  
ANISOU  432  OG  SER A 152    12534  12444  12133   1021    614    120       O  
ATOM    433  N   TYR A 153      -1.725  20.332  19.280  1.00 94.69           N  
ANISOU  433  N   TYR A 153    12048  12281  11649   1159    828    -63       N  
ATOM    434  CA  TYR A 153      -2.873  19.780  18.575  1.00 94.89           C  
ANISOU  434  CA  TYR A 153    12012  12337  11703   1081    906     86       C  
ATOM    435  C   TYR A 153      -3.537  20.776  17.640  1.00 91.80           C  
ANISOU  435  C   TYR A 153    11625  11854  11401   1153    941    -55       C  
ATOM    436  O   TYR A 153      -4.341  20.369  16.795  1.00 91.44           O  
ANISOU  436  O   TYR A 153    11542  11776  11425   1077    990     52       O  
ATOM    437  CB  TYR A 153      -3.884  19.237  19.585  1.00 98.45           C  
ANISOU  437  CB  TYR A 153    12340  13151  11915   1074    968    239       C  
ATOM    438  CG  TYR A 153      -3.279  18.087  20.338  1.00101.40           C  
ANISOU  438  CG  TYR A 153    12726  13575  12226    967    919    435       C  
ATOM    439  CD1 TYR A 153      -2.948  16.916  19.680  1.00102.21           C  
ANISOU  439  CD1 TYR A 153    12885  13460  12488    809    876    624       C  
ATOM    440  CD2 TYR A 153      -2.982  18.186  21.690  1.00103.31           C  
ANISOU  440  CD2 TYR A 153    12936  14066  12252   1039    898    420       C  
ATOM    441  CE1 TYR A 153      -2.364  15.871  20.344  1.00103.22           C  
ANISOU  441  CE1 TYR A 153    13045  13599  12576    728    806    803       C  
ATOM    442  CE2 TYR A 153      -2.396  17.133  22.367  1.00105.60           C  
ANISOU  442  CE2 TYR A 153    13247  14390  12487    944    838    615       C  
ATOM    443  CZ  TYR A 153      -2.098  15.973  21.686  1.00104.99           C  
ANISOU  443  CZ  TYR A 153    13232  14073  12585    790    788    812       C  
ATOM    444  OH  TYR A 153      -1.516  14.911  22.337  1.00105.50           O  
ANISOU  444  OH  TYR A 153    13335  14141  12610    709    705   1010       O  
ATOM    445  N   HIS A 154      -3.219  22.065  17.772  1.00 90.45           N  
ANISOU  445  N   HIS A 154    11508  11628  11232   1293    900   -290       N  
ATOM    446  CA  HIS A 154      -3.433  22.981  16.661  1.00 87.13           C  
ANISOU  446  CA  HIS A 154    11143  10998  10965   1331    891   -411       C  
ATOM    447  C   HIS A 154      -2.622  22.544  15.449  1.00 84.57           C  
ANISOU  447  C   HIS A 154    10890  10377  10864   1183    864   -340       C  
ATOM    448  O   HIS A 154      -3.063  22.714  14.307  1.00 82.73           O  
ANISOU  448  O   HIS A 154    10671  10011  10752   1148    886   -325       O  
ATOM    449  CB  HIS A 154      -3.053  24.404  17.071  1.00 86.55           C  
ANISOU  449  CB  HIS A 154    11147  10866  10871   1487    813   -667       C  
ATOM    450  CG  HIS A 154      -4.188  25.193  17.642  1.00 87.85           C  
ANISOU  450  CG  HIS A 154    11257  11252  10872   1686    841   -798       C  
ATOM    451  ND1 HIS A 154      -4.489  25.197  18.987  1.00 90.00           N  
ANISOU  451  ND1 HIS A 154    11457  11840  10900   1807    860   -851       N  
ATOM    452  CD2 HIS A 154      -5.091  26.012  17.052  1.00 86.19           C  
ANISOU  452  CD2 HIS A 154    11046  11010  10694   1804    850   -894       C  
ATOM    453  CE1 HIS A 154      -5.530  25.982  19.200  1.00 89.58           C  
ANISOU  453  CE1 HIS A 154    11353  11954  10731   2004    885   -988       C  
ATOM    454  NE2 HIS A 154      -5.914  26.489  18.043  1.00 88.09           N  
ANISOU  454  NE2 HIS A 154    11208  11547  10714   2011    875  -1017       N  
ATOM    455  N   PHE A 155      -1.441  21.965  15.686  1.00 80.40           N  
ANISOU  455  N   PHE A 155    10399   9770  10381   1107    814   -298       N  
ATOM    456  CA  PHE A 155      -0.605  21.458  14.605  1.00 77.85           C  
ANISOU  456  CA  PHE A 155    10122   9213  10243    990    793   -238       C  
ATOM    457  C   PHE A 155      -1.139  20.140  14.058  1.00 78.30           C  
ANISOU  457  C   PHE A 155    10148   9266  10336    885    838    -43       C  
ATOM    458  O   PHE A 155      -1.146  19.930  12.840  1.00 76.18           O  
ANISOU  458  O   PHE A 155     9906   8834  10205    818    850    -15       O  
ATOM    459  CB  PHE A 155       0.835  21.294  15.096  1.00 78.15           C  
ANISOU  459  CB  PHE A 155    10190   9199  10305    970    717   -271       C  
ATOM    460  CG  PHE A 155       1.670  20.380  14.246  1.00 75.75           C  
ANISOU  460  CG  PHE A 155     9900   8740  10142    873    703   -179       C  
ATOM    461  CD1 PHE A 155       2.150  20.803  13.018  1.00 72.67           C  
ANISOU  461  CD1 PHE A 155     9538   8171   9903    825    700   -233       C  
ATOM    462  CD2 PHE A 155       1.990  19.104  14.681  1.00 77.67           C  
ANISOU  462  CD2 PHE A 155    10130   9024  10359    840    683    -41       C  
ATOM    463  CE1 PHE A 155       2.928  19.967  12.234  1.00 71.95           C  
ANISOU  463  CE1 PHE A 155     9445   7974   9918    764    692   -172       C  
ATOM    464  CE2 PHE A 155       2.769  18.262  13.901  1.00 75.76           C  
ANISOU  464  CE2 PHE A 155     9905   8636  10243    789    657     16       C  
ATOM    465  CZ  PHE A 155       3.238  18.696  12.677  1.00 72.91           C  
ANISOU  465  CZ  PHE A 155     9558   8128  10018    761    668    -61       C  
ATOM    466  N   ILE A 156      -1.581  19.241  14.941  1.00 81.80           N  
ANISOU  466  N   ILE A 156    10541   9887  10653    861    852     98       N  
ATOM    467  CA  ILE A 156      -2.225  18.011  14.488  1.00 82.95           C  
ANISOU  467  CA  ILE A 156    10668  10020  10829    742    873    295       C  
ATOM    468  C   ILE A 156      -3.543  18.330  13.798  1.00 83.05           C  
ANISOU  468  C   ILE A 156    10626  10087  10842    731    939    309       C  
ATOM    469  O   ILE A 156      -3.861  17.776  12.738  1.00 81.19           O  
ANISOU  469  O   ILE A 156    10410   9719  10720    638    942    383       O  
ATOM    470  CB  ILE A 156      -2.428  17.042  15.666  1.00 88.01           C  
ANISOU  470  CB  ILE A 156    11268  10849  11323    696    858    470       C  
ATOM    471  CG1 ILE A 156      -1.090  16.707  16.321  1.00 87.89           C  
ANISOU  471  CG1 ILE A 156    11307  10776  11312    719    778    459       C  
ATOM    472  CG2 ILE A 156      -3.123  15.774  15.197  1.00 88.46           C  
ANISOU  472  CG2 ILE A 156    11322  10864  11425    546    852    686       C  
ATOM    473  CD1 ILE A 156      -0.123  16.011  15.400  1.00 83.52           C  
ANISOU  473  CD1 ILE A 156    10833   9955  10948    672    717    474       C  
ATOM    474  N   GLY A 157      -4.331  19.230  14.390  1.00 86.49           N  
ANISOU  474  N   GLY A 157    10990  10728  11142    840    984    226       N  
ATOM    475  CA  GLY A 157      -5.565  19.649  13.750  1.00 86.07           C  
ANISOU  475  CA  GLY A 157    10871  10745  11085    861   1040    221       C  
ATOM    476  C   GLY A 157      -5.325  20.283  12.394  1.00 82.37           C  
ANISOU  476  C   GLY A 157    10480  10023  10795    866   1022    119       C  
ATOM    477  O   GLY A 157      -6.083  20.052  11.450  1.00 81.76           O  
ANISOU  477  O   GLY A 157    10376   9909  10779    805   1046    184       O  
ATOM    478  N   SER A 158      -4.255  21.074  12.274  1.00 79.82           N  
ANISOU  478  N   SER A 158    10246   9532  10548    923    973    -30       N  
ATOM    479  CA  SER A 158      -3.914  21.685  10.992  1.00 75.62           C  
ANISOU  479  CA  SER A 158     9787   8771  10175    904    951   -103       C  
ATOM    480  C   SER A 158      -3.673  20.625   9.924  1.00 73.94           C  
ANISOU  480  C   SER A 158     9596   8419  10079    764    955     17       C  
ATOM    481  O   SER A 158      -4.257  20.680   8.835  1.00 73.21           O  
ANISOU  481  O   SER A 158     9504   8259  10054    727    972     40       O  
ATOM    482  CB  SER A 158      -2.685  22.581  11.146  1.00 74.53           C  
ANISOU  482  CB  SER A 158     9730   8496  10092    944    886   -247       C  
ATOM    483  OG  SER A 158      -2.541  23.445  10.030  1.00 71.99           O  
ANISOU  483  OG  SER A 158     9469   7992   9893    934    861   -314       O  
ATOM    484  N   LEU A 159      -2.811  19.648  10.221  1.00 74.38           N  
ANISOU  484  N   LEU A 159     9674   8432  10153    700    927     83       N  
ATOM    485  CA  LEU A 159      -2.540  18.578   9.265  1.00 72.34           C  
ANISOU  485  CA  LEU A 159     9450   8036   9999    597    913    171       C  
ATOM    486  C   LEU A 159      -3.811  17.817   8.913  1.00 74.14           C  
ANISOU  486  C   LEU A 159     9638   8324  10207    518    936    303       C  
ATOM    487  O   LEU A 159      -3.998  17.402   7.763  1.00 72.52           O  
ANISOU  487  O   LEU A 159     9463   8001  10092    452    929    328       O  
ATOM    488  CB  LEU A 159      -1.494  17.617   9.829  1.00 72.30           C  
ANISOU  488  CB  LEU A 159     9476   7991  10004    576    862    220       C  
ATOM    489  CG  LEU A 159      -0.140  18.182  10.254  1.00 71.81           C  
ANISOU  489  CG  LEU A 159     9433   7896   9958    637    826    108       C  
ATOM    490  CD1 LEU A 159       0.750  17.063  10.766  1.00 72.61           C  
ANISOU  490  CD1 LEU A 159     9553   7971  10066    628    768    177       C  
ATOM    491  CD2 LEU A 159       0.520  18.906   9.098  1.00 68.45           C  
ANISOU  491  CD2 LEU A 159     9031   7337   9641    629    829      5       C  
ATOM    492  N   ALA A 160      -4.693  17.620   9.895  1.00 77.43           N  
ANISOU  492  N   ALA A 160     9978   8944  10496    517    960    390       N  
ATOM    493  CA  ALA A 160      -5.945  16.914   9.643  1.00 80.49           C  
ANISOU  493  CA  ALA A 160    10303   9426  10854    416    976    536       C  
ATOM    494  C   ALA A 160      -6.785  17.643   8.602  1.00 79.53           C  
ANISOU  494  C   ALA A 160    10148   9298  10772    438   1010    478       C  
ATOM    495  O   ALA A 160      -7.286  17.031   7.651  1.00 78.90           O  
ANISOU  495  O   ALA A 160    10076   9144  10760    335    993    549       O  
ATOM    496  CB  ALA A 160      -6.723  16.748  10.948  1.00 86.24           C  
ANISOU  496  CB  ALA A 160    10923  10437  11408    415   1008    640       C  
ATOM    497  N   VAL A 161      -6.943  18.959   8.764  1.00 80.37           N  
ANISOU  497  N   VAL A 161    10228   9471  10838    578   1041    343       N  
ATOM    498  CA  VAL A 161      -7.729  19.743   7.815  1.00 79.22           C  
ANISOU  498  CA  VAL A 161    10058   9314  10728    622   1058    289       C  
ATOM    499  C   VAL A 161      -7.022  19.834   6.470  1.00 75.12           C  
ANISOU  499  C   VAL A 161     9642   8546  10355    575   1026    242       C  
ATOM    500  O   VAL A 161      -7.664  19.775   5.414  1.00 74.84           O  
ANISOU  500  O   VAL A 161     9596   8474  10366    528   1025    273       O  
ATOM    501  CB  VAL A 161      -8.025  21.139   8.392  1.00 79.18           C  
ANISOU  501  CB  VAL A 161    10022   9414  10647    807   1073    147       C  
ATOM    502  CG1 VAL A 161      -9.059  21.854   7.547  1.00 78.86           C  
ANISOU  502  CG1 VAL A 161     9938   9399  10625    871   1081    118       C  
ATOM    503  CG2 VAL A 161      -8.522  21.023   9.820  1.00 82.84           C  
ANISOU  503  CG2 VAL A 161    10382  10157  10938    873   1110    173       C  
ATOM    504  N   ALA A 162      -5.696  19.991   6.482  1.00 72.42           N  
ANISOU  504  N   ALA A 162     9386   8058  10074    585    999    168       N  
ATOM    505  CA  ALA A 162      -4.949  20.032   5.228  1.00 68.54           C  
ANISOU  505  CA  ALA A 162     8968   7379   9695    536    979    132       C  
ATOM    506  C   ALA A 162      -5.121  18.735   4.449  1.00 68.24           C  
ANISOU  506  C   ALA A 162     8943   7283   9701    423    965    225       C  
ATOM    507  O   ALA A 162      -5.285  18.753   3.223  1.00 67.30           O  
ANISOU  507  O   ALA A 162     8848   7086   9636    383    961    218       O  
ATOM    508  CB  ALA A 162      -3.470  20.304   5.502  1.00 67.16           C  
ANISOU  508  CB  ALA A 162     8849   7110   9560    555    954     54       C  
ATOM    509  N   ASP A 163      -5.093  17.599   5.147  1.00 70.11           N  
ANISOU  509  N   ASP A 163     9176   7550   9913    368    945    314       N  
ATOM    510  CA  ASP A 163      -5.375  16.320   4.505  1.00 70.25           C  
ANISOU  510  CA  ASP A 163     9226   7490   9977    258    903    402       C  
ATOM    511  C   ASP A 163      -6.826  16.245   4.050  1.00 72.90           C  
ANISOU  511  C   ASP A 163     9496   7918  10284    189    911    480       C  
ATOM    512  O   ASP A 163      -7.113  15.869   2.907  1.00 71.84           O  
ANISOU  512  O   ASP A 163     9394   7698  10204    125    883    483       O  
ATOM    513  CB  ASP A 163      -5.059  15.174   5.465  1.00 72.62           C  
ANISOU  513  CB  ASP A 163     9550   7785  10259    211    854    500       C  
ATOM    514  CG  ASP A 163      -3.577  14.898   5.574  1.00 70.57           C  
ANISOU  514  CG  ASP A 163     9361   7400  10051    269    820    428       C  
ATOM    515  OD1 ASP A 163      -2.812  15.458   4.763  1.00 67.30           O  
ANISOU  515  OD1 ASP A 163     8971   6911   9690    321    836    311       O  
ATOM    516  OD2 ASP A 163      -3.177  14.126   6.470  1.00 71.71           O  
ANISOU  516  OD2 ASP A 163     9529   7540  10177    260    772    498       O  
ATOM    517  N   LEU A 164      -7.756  16.613   4.933  1.00 75.91           N  
ANISOU  517  N   LEU A 164     9773   8500  10568    208    949    538       N  
ATOM    518  CA  LEU A 164      -9.177  16.427   4.652  1.00 78.83           C  
ANISOU  518  CA  LEU A 164    10046   9010  10896    134    955    634       C  
ATOM    519  C   LEU A 164      -9.644  17.326   3.513  1.00 78.06           C  
ANISOU  519  C   LEU A 164     9935   8891  10832    188    970    555       C  
ATOM    520  O   LEU A 164     -10.327  16.871   2.587  1.00 78.43           O  
ANISOU  520  O   LEU A 164     9971   8920  10910     94    938    606       O  
ATOM    521  CB  LEU A 164      -9.989  16.691   5.920  1.00 84.45           C  
ANISOU  521  CB  LEU A 164    10621   9995  11469    169   1004    703       C  
ATOM    522  CG  LEU A 164     -11.512  16.622   5.833  1.00 87.89           C  
ANISOU  522  CG  LEU A 164    10905  10660  11831    109   1024    807       C  
ATOM    523  CD1 LEU A 164     -11.975  15.182   5.712  1.00 87.22           C  
ANISOU  523  CD1 LEU A 164    10813  10561  11765   -117    961    993       C  
ATOM    524  CD2 LEU A 164     -12.127  17.282   7.056  1.00 90.63           C  
ANISOU  524  CD2 LEU A 164    11104  11313  12018    224   1094    809       C  
ATOM    525  N   LEU A 165      -9.288  18.611   3.565  1.00 78.86           N  
ANISOU  525  N   LEU A 165    10049   8986  10929    334   1001    434       N  
ATOM    526  CA  LEU A 165      -9.765  19.553   2.557  1.00 78.06           C  
ANISOU  526  CA  LEU A 165     9943   8861  10855    394   1001    377       C  
ATOM    527  C   LEU A 165      -9.146  19.281   1.192  1.00 74.92           C  
ANISOU  527  C   LEU A 165     9644   8274  10547    321    968    353       C  
ATOM    528  O   LEU A 165      -9.829  19.375   0.167  1.00 75.34           O  
ANISOU  528  O   LEU A 165     9682   8330  10614    290    950    373       O  
ATOM    529  CB  LEU A 165      -9.478  20.983   3.010  1.00 76.29           C  
ANISOU  529  CB  LEU A 165     9734   8639  10613    561   1014    259       C  
ATOM    530  CG  LEU A 165     -10.691  21.727   3.561  1.00 79.39           C  
ANISOU  530  CG  LEU A 165    10011   9239  10916    690   1035    245       C  
ATOM    531  CD1 LEU A 165     -11.774  21.771   2.508  1.00 81.33           C  
ANISOU  531  CD1 LEU A 165    10194   9535  11173    666   1021    297       C  
ATOM    532  CD2 LEU A 165     -11.206  21.030   4.809  1.00 83.56           C  
ANISOU  532  CD2 LEU A 165    10422   9998  11328    671   1075    320       C  
ATOM    533  N   GLY A 166      -7.860  18.932   1.154  1.00 69.19           N  
ANISOU  533  N   GLY A 166     9008   7409   9871    302    958    309       N  
ATOM    534  CA  GLY A 166      -7.206  18.716  -0.127  1.00 66.63           C  
ANISOU  534  CA  GLY A 166     8761   6950   9607    256    937    271       C  
ATOM    535  C   GLY A 166      -7.673  17.449  -0.817  1.00 67.88           C  
ANISOU  535  C   GLY A 166     8934   7077   9779    144    894    327       C  
ATOM    536  O   GLY A 166      -7.957  17.449  -2.018  1.00 67.25           O  
ANISOU  536  O   GLY A 166     8874   6967   9710    109    874    315       O  
ATOM    537  N   SER A 167      -7.764  16.351  -0.064  1.00 70.86           N  
ANISOU  537  N   SER A 167     9312   7455  10155     81    863    395       N  
ATOM    538  CA  SER A 167      -8.119  15.069  -0.664  1.00 71.52           C  
ANISOU  538  CA  SER A 167     9441   7464  10270    -37    789    444       C  
ATOM    539  C   SER A 167      -9.549  15.073  -1.189  1.00 73.90           C  
ANISOU  539  C   SER A 167     9667   7869  10543   -120    769    517       C  
ATOM    540  O   SER A 167      -9.817  14.542  -2.273  1.00 73.93           O  
ANISOU  540  O   SER A 167     9715   7804  10572   -191    711    503       O  
ATOM    541  CB  SER A 167      -7.923  13.946   0.354  1.00 72.59           C  
ANISOU  541  CB  SER A 167     9605   7560  10414    -99    740    526       C  
ATOM    542  OG  SER A 167      -6.548  13.733   0.617  1.00 70.03           O  
ANISOU  542  OG  SER A 167     9360   7123  10126    -21    734    450       O  
ATOM    543  N   VAL A 168     -10.480  15.667  -0.437  1.00 74.41           N  
ANISOU  543  N   VAL A 168     9608   8118  10546   -101    812    586       N  
ATOM    544  CA  VAL A 168     -11.883  15.683  -0.849  1.00 77.45           C  
ANISOU  544  CA  VAL A 168     9886   8645  10895   -172    794    664       C  
ATOM    545  C   VAL A 168     -12.048  16.469  -2.144  1.00 76.67           C  
ANISOU  545  C   VAL A 168     9802   8520  10809   -117    793    589       C  
ATOM    546  O   VAL A 168     -12.709  16.018  -3.088  1.00 78.15           O  
ANISOU  546  O   VAL A 168     9984   8708  11003   -211    735    617       O  
ATOM    547  CB  VAL A 168     -12.766  16.259   0.272  1.00 81.05           C  
ANISOU  547  CB  VAL A 168    10184   9349  11263   -121    853    733       C  
ATOM    548  CG1 VAL A 168     -14.118  16.686  -0.281  1.00 84.56           C  
ANISOU  548  CG1 VAL A 168    10494   9971  11663   -128    849    776       C  
ATOM    549  CG2 VAL A 168     -12.940  15.246   1.389  1.00 81.95           C  
ANISOU  549  CG2 VAL A 168    10257   9539  11339   -238    837    864       C  
ATOM    550  N   ILE A 169     -11.463  17.667  -2.200  1.00 74.20           N  
ANISOU  550  N   ILE A 169     9514   8183  10496     26    844    502       N  
ATOM    551  CA  ILE A 169     -11.533  18.470  -3.416  1.00 73.45           C  
ANISOU  551  CA  ILE A 169     9446   8053  10408     71    835    453       C  
ATOM    552  C   ILE A 169     -10.847  17.748  -4.566  1.00 72.00           C  
ANISOU  552  C   ILE A 169     9369   7732  10256     -7    794    409       C  
ATOM    553  O   ILE A 169     -11.314  17.787  -5.711  1.00 73.01           O  
ANISOU  553  O   ILE A 169     9502   7870  10369    -42    758    409       O  
ATOM    554  CB  ILE A 169     -10.921  19.862  -3.177  1.00 71.99           C  
ANISOU  554  CB  ILE A 169     9289   7834  10229    215    875    384       C  
ATOM    555  CG1 ILE A 169     -11.687  20.602  -2.081  1.00 74.30           C  
ANISOU  555  CG1 ILE A 169     9482   8273  10477    327    902    395       C  
ATOM    556  CG2 ILE A 169     -10.918  20.674  -4.464  1.00 70.77           C  
ANISOU  556  CG2 ILE A 169     9179   7629  10082    240    852    363       C  
ATOM    557  CD1 ILE A 169     -10.981  21.847  -1.597  1.00 71.22           C  
ANISOU  557  CD1 ILE A 169     9147   7813  10102    466    918    310       C  
ATOM    558  N   PHE A 170      -9.736  17.066  -4.280  1.00 70.39           N  
ANISOU  558  N   PHE A 170     9247   7413  10085    -19    796    364       N  
ATOM    559  CA  PHE A 170      -9.019  16.357  -5.334  1.00 68.71           C  
ANISOU  559  CA  PHE A 170     9129   7090   9887    -56    758    294       C  
ATOM    560  C   PHE A 170      -9.871  15.238  -5.922  1.00 70.87           C  
ANISOU  560  C   PHE A 170     9417   7349  10162   -175    669    326       C  
ATOM    561  O   PHE A 170     -10.119  15.208  -7.131  1.00 72.44           O  
ANISOU  561  O   PHE A 170     9640   7549  10334   -201    633    290       O  
ATOM    562  CB  PHE A 170      -7.694  15.810  -4.799  1.00 66.82           C  
ANISOU  562  CB  PHE A 170     8959   6749   9682    -19    768    233       C  
ATOM    563  CG  PHE A 170      -7.010  14.856  -5.740  1.00 65.80           C  
ANISOU  563  CG  PHE A 170     8919   6521   9560    -30    717    146       C  
ATOM    564  CD1 PHE A 170      -6.239  15.326  -6.792  1.00 64.75           C  
ANISOU  564  CD1 PHE A 170     8808   6403   9391     22    750     60       C  
ATOM    565  CD2 PHE A 170      -7.139  13.487  -5.572  1.00 66.66           C  
ANISOU  565  CD2 PHE A 170     9095   6528   9706    -89    627    148       C  
ATOM    566  CE1 PHE A 170      -5.614  14.449  -7.659  1.00 66.22           C  
ANISOU  566  CE1 PHE A 170     9064   6535   9560     41    708    -43       C  
ATOM    567  CE2 PHE A 170      -6.517  12.604  -6.437  1.00 67.49           C  
ANISOU  567  CE2 PHE A 170     9296   6531   9815    -67    564     38       C  
ATOM    568  CZ  PHE A 170      -5.753  13.086  -7.480  1.00 67.04           C  
ANISOU  568  CZ  PHE A 170     9245   6522   9706     12    612    -70       C  
ATOM    569  N   VAL A 171     -10.346  14.319  -5.073  1.00 71.99           N  
ANISOU  569  N   VAL A 171     9545   7481  10328   -262    622    404       N  
ATOM    570  CA  VAL A 171     -11.034  13.126  -5.569  1.00 74.08           C  
ANISOU  570  CA  VAL A 171     9848   7689  10611   -405    508    439       C  
ATOM    571  C   VAL A 171     -12.269  13.506  -6.379  1.00 76.63           C  
ANISOU  571  C   VAL A 171    10085   8140  10891   -467    482    482       C  
ATOM    572  O   VAL A 171     -12.576  12.876  -7.399  1.00 77.85           O  
ANISOU  572  O   VAL A 171    10296   8241  11045   -547    391    445       O  
ATOM    573  CB  VAL A 171     -11.387  12.179  -4.404  1.00 74.63           C  
ANISOU  573  CB  VAL A 171     9907   7739  10711   -516    455    558       C  
ATOM    574  CG1 VAL A 171     -12.275  12.871  -3.383  1.00 77.53           C  
ANISOU  574  CG1 VAL A 171    10109   8321  11027   -524    527    682       C  
ATOM    575  CG2 VAL A 171     -12.064  10.921  -4.929  1.00 76.35           C  
ANISOU  575  CG2 VAL A 171    10185   7862  10963   -692    307    602       C  
ATOM    576  N   TYR A 172     -12.992  14.539  -5.944  1.00 80.03           N  
ANISOU  576  N   TYR A 172    10380   8744  11282   -417    551    549       N  
ATOM    577  CA  TYR A 172     -14.170  14.978  -6.684  1.00 83.43           C  
ANISOU  577  CA  TYR A 172    10714   9316  11671   -449    523    592       C  
ATOM    578  C   TYR A 172     -13.782  15.503  -8.059  1.00 82.54           C  
ANISOU  578  C   TYR A 172    10673   9155  11535   -387    516    498       C  
ATOM    579  O   TYR A 172     -14.360  15.105  -9.075  1.00 85.02           O  
ANISOU  579  O   TYR A 172    10995   9485  11824   -469    436    492       O  
ATOM    580  CB  TYR A 172     -14.922  16.045  -5.887  1.00 85.57           C  
ANISOU  580  CB  TYR A 172    10828   9785  11901   -356    597    659       C  
ATOM    581  CG  TYR A 172     -15.719  17.021  -6.730  1.00 87.57           C  
ANISOU  581  CG  TYR A 172    11003  10157  12112   -285    591    660       C  
ATOM    582  CD1 TYR A 172     -16.810  16.597  -7.480  1.00 90.49           C  
ANISOU  582  CD1 TYR A 172    11297  10628  12456   -397    510    717       C  
ATOM    583  CD2 TYR A 172     -15.388  18.370  -6.763  1.00 86.77           C  
ANISOU  583  CD2 TYR A 172    10909  10058  12001   -111    649    611       C  
ATOM    584  CE1 TYR A 172     -17.542  17.489  -8.247  1.00 93.37           C  
ANISOU  584  CE1 TYR A 172    11588  11109  12780   -320    494    724       C  
ATOM    585  CE2 TYR A 172     -16.115  19.270  -7.526  1.00 89.06           C  
ANISOU  585  CE2 TYR A 172    11144  10437  12260    -35    624    624       C  
ATOM    586  CZ  TYR A 172     -17.191  18.824  -8.265  1.00 92.96           C  
ANISOU  586  CZ  TYR A 172    11554  11047  12721   -131    551    681       C  
ATOM    587  OH  TYR A 172     -17.918  19.713  -9.025  1.00 95.29           O  
ANISOU  587  OH  TYR A 172    11789  11436  12980    -44    516    699       O  
ATOM    588  N   SER A 173     -12.786  16.389  -8.109  1.00 77.38           N  
ANISOU  588  N   SER A 173    10069   8452  10879   -258    592    431       N  
ATOM    589  CA  SER A 173     -12.408  17.001  -9.377  1.00 77.34           C  
ANISOU  589  CA  SER A 173    10117   8434  10833   -211    593    374       C  
ATOM    590  C   SER A 173     -11.578  16.051 -10.233  1.00 76.77           C  
ANISOU  590  C   SER A 173    10163   8258  10750   -253    553    273       C  
ATOM    591  O   SER A 173     -11.677  16.075 -11.464  1.00 79.04           O  
ANISOU  591  O   SER A 173    10480   8574  10976   -268    515    234       O  
ATOM    592  CB  SER A 173     -11.644  18.298  -9.124  1.00 75.56           C  
ANISOU  592  CB  SER A 173     9902   8197  10610    -87    674    360       C  
ATOM    593  OG  SER A 173     -10.685  18.131  -8.094  1.00 72.77           O  
ANISOU  593  OG  SER A 173     9581   7768  10301    -52    725    326       O  
ATOM    594  N   PHE A 174     -10.758  15.207  -9.602  1.00 76.96           N  
ANISOU  594  N   PHE A 174    10253   8169  10820   -255    552    223       N  
ATOM    595  CA  PHE A 174      -9.857  14.344 -10.361  1.00 76.61           C  
ANISOU  595  CA  PHE A 174    10321   8028  10762   -245    512     98       C  
ATOM    596  C   PHE A 174     -10.633  13.351 -11.218  1.00 79.60           C  
ANISOU  596  C   PHE A 174    10746   8378  11120   -347    387     67       C  
ATOM    597  O   PHE A 174     -10.369  13.210 -12.417  1.00 80.76           O  
ANISOU  597  O   PHE A 174    10948   8540  11196   -326    357    -32       O  
ATOM    598  CB  PHE A 174      -8.903  13.610  -9.417  1.00 73.91           C  
ANISOU  598  CB  PHE A 174    10037   7563  10483   -209    517     57       C  
ATOM    599  CG  PHE A 174      -7.974  12.656 -10.112  1.00 74.52           C  
ANISOU  599  CG  PHE A 174    10226   7541  10548   -161    464    -91       C  
ATOM    600  CD1 PHE A 174      -6.834  13.119 -10.749  1.00 74.43           C  
ANISOU  600  CD1 PHE A 174    10220   7584  10475    -53    538   -189       C  
ATOM    601  CD2 PHE A 174      -8.238  11.297 -10.126  1.00 75.40           C  
ANISOU  601  CD2 PHE A 174    10433   7511  10703   -223    333   -131       C  
ATOM    602  CE1 PHE A 174      -5.977  12.243 -11.391  1.00 75.11           C  
ANISOU  602  CE1 PHE A 174    10390   7618  10531     23    495   -344       C  
ATOM    603  CE2 PHE A 174      -7.385  10.418 -10.768  1.00 75.58           C  
ANISOU  603  CE2 PHE A 174    10571   7434  10714   -142    269   -294       C  
ATOM    604  CZ  PHE A 174      -6.253  10.891 -11.400  1.00 76.01           C  
ANISOU  604  CZ  PHE A 174    10612   7575  10691     -3    358   -411       C  
ATOM    605  N   ILE A 175     -11.600  12.653 -10.620  1.00 80.98           N  
ANISOU  605  N   ILE A 175    10896   8526  11347   -468    307    153       N  
ATOM    606  CA  ILE A 175     -12.331  11.650 -11.385  1.00 83.50           C  
ANISOU  606  CA  ILE A 175    11270   8796  11660   -593    161    125       C  
ATOM    607  C   ILE A 175     -13.428  12.289 -12.233  1.00 86.15           C  
ANISOU  607  C   ILE A 175    11512   9295  11927   -643    142    177       C  
ATOM    608  O   ILE A 175     -13.774  11.763 -13.296  1.00 88.66           O  
ANISOU  608  O   ILE A 175    11885   9603  12200   -703     37    107       O  
ATOM    609  CB  ILE A 175     -12.888  10.557 -10.455  1.00 84.05           C  
ANISOU  609  CB  ILE A 175    11357   8765  11815   -741     58    216       C  
ATOM    610  CG1 ILE A 175     -14.044  11.090  -9.606  1.00 85.03           C  
ANISOU  610  CG1 ILE A 175    11306   9060  11941   -828     98    400       C  
ATOM    611  CG2 ILE A 175     -11.780   9.996  -9.572  1.00 81.33           C  
ANISOU  611  CG2 ILE A 175    11107   8260  11536   -673     72    179       C  
ATOM    612  CD1 ILE A 175     -14.594  10.077  -8.629  1.00 84.85           C  
ANISOU  612  CD1 ILE A 175    11275   8982  11982  -1000      9    529       C  
ATOM    613  N   ASP A 176     -13.989  13.421 -11.797  1.00 84.24           N  
ANISOU  613  N   ASP A 176    11132   9206  11671   -604    229    288       N  
ATOM    614  CA  ASP A 176     -14.918  14.150 -12.656  1.00 87.42           C  
ANISOU  614  CA  ASP A 176    11447   9763  12003   -611    209    332       C  
ATOM    615  C   ASP A 176     -14.235  14.576 -13.948  1.00 88.05           C  
ANISOU  615  C   ASP A 176    11607   9849  11998   -531    224    230       C  
ATOM    616  O   ASP A 176     -14.844  14.550 -15.023  1.00 90.67           O  
ANISOU  616  O   ASP A 176    11934  10259  12257   -575    148    217       O  
ATOM    617  CB  ASP A 176     -15.477  15.370 -11.922  1.00 87.49           C  
ANISOU  617  CB  ASP A 176    11313   9915  12016   -531    297    444       C  
ATOM    618  CG  ASP A 176     -16.799  15.843 -12.495  1.00 91.56           C  
ANISOU  618  CG  ASP A 176    11703  10605  12480   -561    242    523       C  
ATOM    619  OD1 ASP A 176     -17.612  14.988 -12.906  1.00 94.56           O  
ANISOU  619  OD1 ASP A 176    12055  11021  12850   -707    131    543       O  
ATOM    620  OD2 ASP A 176     -17.025  17.071 -12.534  1.00 91.93           O  
ANISOU  620  OD2 ASP A 176    11683  10746  12502   -437    296    564       O  
ATOM    621  N   PHE A 177     -12.962  14.963 -13.859  1.00 86.32           N  
ANISOU  621  N   PHE A 177    11451   9571  11774   -421    317    165       N  
ATOM    622  CA  PHE A 177     -12.195  15.288 -15.055  1.00 86.55           C  
ANISOU  622  CA  PHE A 177    11543   9638  11703   -359    340     79       C  
ATOM    623  C   PHE A 177     -11.884  14.035 -15.865  1.00 88.30           C  
ANISOU  623  C   PHE A 177    11874   9796  11879   -392    247    -70       C  
ATOM    624  O   PHE A 177     -12.026  14.026 -17.093  1.00 91.69           O  
ANISOU  624  O   PHE A 177    12330  10311  12197   -397    201   -129       O  
ATOM    625  CB  PHE A 177     -10.904  16.010 -14.662  1.00 83.96           C  
ANISOU  625  CB  PHE A 177    11230   9288  11382   -254    462     64       C  
ATOM    626  CG  PHE A 177     -10.088  16.482 -15.833  1.00 85.45           C  
ANISOU  626  CG  PHE A 177    11452   9564  11453   -207    502     11       C  
ATOM    627  CD1 PHE A 177      -9.170  15.637 -16.438  1.00 86.56           C  
ANISOU  627  CD1 PHE A 177    11664   9696  11528   -172    496   -138       C  
ATOM    628  CD2 PHE A 177     -10.230  17.769 -16.322  1.00 85.98           C  
ANISOU  628  CD2 PHE A 177    11476   9729  11464   -190    540    114       C  
ATOM    629  CE1 PHE A 177      -8.419  16.062 -17.515  1.00 88.94           C  
ANISOU  629  CE1 PHE A 177    11970  10132  11692   -131    545   -179       C  
ATOM    630  CE2 PHE A 177      -9.478  18.202 -17.399  1.00 88.09           C  
ANISOU  630  CE2 PHE A 177    11764  10100  11606   -173    576     97       C  
ATOM    631  CZ  PHE A 177      -8.572  17.347 -17.996  1.00 89.95           C  
ANISOU  631  CZ  PHE A 177    12047  10372  11757   -147    588    -48       C  
ATOM    632  N   HIS A 178     -11.459  12.963 -15.194  1.00 85.49           N  
ANISOU  632  N   HIS A 178    11592   9287  11604   -405    206   -140       N  
ATOM    633  CA  HIS A 178     -10.921  11.815 -15.914  1.00 86.47           C  
ANISOU  633  CA  HIS A 178    11845   9318  11690   -385    114   -317       C  
ATOM    634  C   HIS A 178     -12.007  10.826 -16.330  1.00 88.43           C  
ANISOU  634  C   HIS A 178    12145   9503  11952   -525    -63   -338       C  
ATOM    635  O   HIS A 178     -11.955  10.288 -17.442  1.00 90.28           O  
ANISOU  635  O   HIS A 178    12463   9741  12097   -514   -153   -482       O  
ATOM    636  CB  HIS A 178      -9.853  11.120 -15.068  1.00 83.15           C  
ANISOU  636  CB  HIS A 178    11500   8741  11352   -309    130   -394       C  
ATOM    637  CG  HIS A 178      -8.463  11.614 -15.327  1.00 82.63           C  
ANISOU  637  CG  HIS A 178    11431   8747  11217   -155    252   -483       C  
ATOM    638  ND1 HIS A 178      -7.608  12.002 -14.318  1.00 80.00           N  
ANISOU  638  ND1 HIS A 178    11060   8388  10948    -87    353   -443       N  
ATOM    639  CD2 HIS A 178      -7.780  11.785 -16.484  1.00 84.65           C  
ANISOU  639  CD2 HIS A 178    11700   9129  11333    -66    287   -604       C  
ATOM    640  CE1 HIS A 178      -6.458  12.388 -14.841  1.00 80.14           C  
ANISOU  640  CE1 HIS A 178    11063   8509  10879     26    443   -529       C  
ATOM    641  NE2 HIS A 178      -6.537  12.266 -16.154  1.00 82.82           N  
ANISOU  641  NE2 HIS A 178    11426   8953  11088     42    411   -623       N  
ATOM    642  N   VAL A 179     -12.988  10.580 -15.460  1.00 88.30           N  
ANISOU  642  N   VAL A 179    12071   9445  12035   -662   -119   -198       N  
ATOM    643  CA  VAL A 179     -14.014   9.537 -15.766  1.00 91.36           C  
ANISOU  643  CA  VAL A 179    12504   9758  12451   -836   -310   -200       C  
ATOM    644  C   VAL A 179     -15.294  10.172 -16.319  1.00 93.68           C  
ANISOU  644  C   VAL A 179    12664  10248  12683   -932   -336    -91       C  
ATOM    645  O   VAL A 179     -15.908   9.554 -17.200  1.00 96.08           O  
ANISOU  645  O   VAL A 179    13015  10547  12943  -1032   -486   -154       O  
ATOM    646  CB  VAL A 179     -14.280   8.596 -14.573  1.00 89.66           C  
ANISOU  646  CB  VAL A 179    12320   9372  12373   -964   -394   -112       C  
ATOM    647  CG1 VAL A 179     -15.410   7.620 -14.859  1.00 89.03           C  
ANISOU  647  CG1 VAL A 179    12272   9226  12328  -1186   -600    -76       C  
ATOM    648  CG2 VAL A 179     -13.042   7.856 -14.094  1.00 90.81           C  
ANISOU  648  CG2 VAL A 179    12616   9305  12582   -860   -402   -225       C  
ATOM    649  N   PHE A 180     -15.674  11.354 -15.836  1.00 94.20           N  
ANISOU  649  N   PHE A 180    12573  10476  12743   -891   -210     55       N  
ATOM    650  CA  PHE A 180     -16.852  12.020 -16.373  1.00 97.54           C  
ANISOU  650  CA  PHE A 180    12861  11095  13105   -944   -239    153       C  
ATOM    651  C   PHE A 180     -16.507  13.048 -17.439  1.00 99.64           C  
ANISOU  651  C   PHE A 180    13125  11484  13249   -814   -172    113       C  
ATOM    652  O   PHE A 180     -17.420  13.588 -18.073  1.00102.09           O  
ANISOU  652  O   PHE A 180    13343  11952  13494   -840   -214    181       O  
ATOM    653  CB  PHE A 180     -17.657  12.689 -15.253  1.00 97.82           C  
ANISOU  653  CB  PHE A 180    12717  11254  13198   -963   -169    334       C  
ATOM    654  CG  PHE A 180     -18.517  11.735 -14.467  1.00 98.27           C  
ANISOU  654  CG  PHE A 180    12713  11293  13331  -1156   -267    432       C  
ATOM    655  CD1 PHE A 180     -18.620  10.404 -14.838  1.00 98.24           C  
ANISOU  655  CD1 PHE A 180    12831  11137  13359  -1319   -435    367       C  
ATOM    656  CD2 PHE A 180     -19.235  12.174 -13.367  1.00 98.69           C  
ANISOU  656  CD2 PHE A 180    12589  11491  13418  -1179   -202    591       C  
ATOM    657  CE1 PHE A 180     -19.412   9.526 -14.119  1.00 97.74           C  
ANISOU  657  CE1 PHE A 180    12716  11050  13370  -1532   -542    488       C  
ATOM    658  CE2 PHE A 180     -20.031  11.301 -12.644  1.00 98.72           C  
ANISOU  658  CE2 PHE A 180    12516  11519  13473  -1381   -288    709       C  
ATOM    659  CZ  PHE A 180     -20.119   9.976 -13.021  1.00 97.70           C  
ANISOU  659  CZ  PHE A 180    12514  11223  13387  -1575   -462    672       C  
ATOM    660  N   HIS A 181     -15.217  13.327 -17.644  1.00 95.90           N  
ANISOU  660  N   HIS A 181    12741  10958  12739   -682    -75     18       N  
ATOM    661  CA  HIS A 181     -14.744  14.195 -18.722  1.00 97.03           C  
ANISOU  661  CA  HIS A 181    12896  11223  12750   -585    -18    -11       C  
ATOM    662  C   HIS A 181     -15.350  15.594 -18.612  1.00 98.33           C  
ANISOU  662  C   HIS A 181    12936  11521  12905   -541     44    153       C  
ATOM    663  O   HIS A 181     -15.965  16.108 -19.548  1.00101.30           O  
ANISOU  663  O   HIS A 181    13275  12030  13186   -546     -5    198       O  
ATOM    664  CB  HIS A 181     -15.033  13.569 -20.088  1.00100.49           C  
ANISOU  664  CB  HIS A 181    13401  11719  13062   -633   -142   -125       C  
ATOM    665  CG  HIS A 181     -14.445  12.203 -20.260  1.00100.02           C  
ANISOU  665  CG  HIS A 181    13485  11508  13009   -647   -228   -316       C  
ATOM    666  ND1 HIS A 181     -13.090  11.985 -20.391  1.00 99.25           N  
ANISOU  666  ND1 HIS A 181    13479  11361  12872   -520   -154   -456       N  
ATOM    667  CD2 HIS A 181     -15.028  10.982 -20.316  1.00100.64           C  
ANISOU  667  CD2 HIS A 181    13637  11467  13134   -767   -398   -393       C  
ATOM    668  CE1 HIS A 181     -12.864  10.691 -20.523  1.00 98.83           C  
ANISOU  668  CE1 HIS A 181    13555  11157  12839   -532   -275   -626       C  
ATOM    669  NE2 HIS A 181     -14.024  10.059 -20.481  1.00 99.12           N  
ANISOU  669  NE2 HIS A 181    13597  11130  12935   -690   -432   -589       N  
ATOM    670  N   ARG A 182     -15.160  16.215 -17.451  1.00 97.97           N  
ANISOU  670  N   ARG A 182    12836  11433  12956   -484    140    235       N  
ATOM    671  CA  ARG A 182     -15.728  17.532 -17.201  1.00 97.65           C  
ANISOU  671  CA  ARG A 182    12694  11486  12924   -413    182    370       C  
ATOM    672  C   ARG A 182     -15.034  18.592 -18.049  1.00 97.95           C  
ANISOU  672  C   ARG A 182    12778  11564  12873   -331    232    391       C  
ATOM    673  O   ARG A 182     -13.812  18.576 -18.222  1.00 96.26           O  
ANISOU  673  O   ARG A 182    12645  11299  12629   -301    301    325       O  
ATOM    674  CB  ARG A 182     -15.622  17.884 -15.716  1.00 94.65           C  
ANISOU  674  CB  ARG A 182    12259  11046  12658   -360    264    423       C  
ATOM    675  CG  ARG A 182     -16.131  19.272 -15.366  1.00 94.28           C  
ANISOU  675  CG  ARG A 182    12125  11070  12625   -249    298    531       C  
ATOM    676  CD  ARG A 182     -17.651  19.325 -15.339  1.00 97.93           C  
ANISOU  676  CD  ARG A 182    12444  11683  13082   -270    221    612       C  
ATOM    677  NE  ARG A 182     -18.245  18.087 -14.852  1.00 99.72           N  
ANISOU  677  NE  ARG A 182    12613  11933  13343   -408    172    605       N  
ATOM    678  CZ  ARG A 182     -19.478  17.688 -15.136  1.00102.79           C  
ANISOU  678  CZ  ARG A 182    12886  12463  13706   -502     76    660       C  
ATOM    679  NH1 ARG A 182     -20.277  18.409 -15.907  1.00105.64           N  
ANISOU  679  NH1 ARG A 182    13169  12964  14004   -451     21    715       N  
ATOM    680  NH2 ARG A 182     -19.922  16.540 -14.632  1.00103.26           N  
ANISOU  680  NH2 ARG A 182    12905  12525  13805   -659     23    672       N  
ATOM    681  N   LYS A 183     -15.830  19.522 -18.575  1.00101.01           N  
ANISOU  681  N   LYS A 183    13106  12057  13215   -297    190    497       N  
ATOM    682  CA  LYS A 183     -15.343  20.549 -19.485  1.00100.93           C  
ANISOU  682  CA  LYS A 183    13144  12094  13112   -246    207    557       C  
ATOM    683  C   LYS A 183     -15.454  21.934 -18.859  1.00 98.78           C  
ANISOU  683  C   LYS A 183    12842  11777  12912   -142    237    678       C  
ATOM    684  O   LYS A 183     -16.029  22.845 -19.463  1.00100.03           O  
ANISOU  684  O   LYS A 183    12984  11998  13027    -96    176    783       O  
ATOM    685  CB  LYS A 183     -16.128  20.497 -20.799  1.00105.56           C  
ANISOU  685  CB  LYS A 183    13715  12827  13567   -289    101    584       C  
ATOM    686  CG  LYS A 183     -15.688  19.397 -21.751  1.00108.39           C  
ANISOU  686  CG  LYS A 183    14146  13232  13807   -366     68    446       C  
ATOM    687  CD  LYS A 183     -14.177  19.329 -21.874  1.00106.81           C  
ANISOU  687  CD  LYS A 183    14032  12990  13560   -338    173    368       C  
ATOM    688  CE  LYS A 183     -13.741  19.134 -23.323  1.00111.49           C  
ANISOU  688  CE  LYS A 183    14678  13734  13950   -357    151    308       C  
ATOM    689  NZ  LYS A 183     -13.629  17.690 -23.674  1.00113.46           N  
ANISOU  689  NZ  LYS A 183    14984  13976  14150   -390     94    107       N  
ATOM    690  N   ASP A 184     -14.908  22.107 -17.659  1.00 96.89           N  
ANISOU  690  N   ASP A 184    12607  11423  12782    -96    315    658       N  
ATOM    691  CA  ASP A 184     -15.042  23.376 -16.959  1.00 94.58           C  
ANISOU  691  CA  ASP A 184    12302  11068  12567     17    325    741       C  
ATOM    692  C   ASP A 184     -14.181  24.452 -17.612  1.00 93.59           C  
ANISOU  692  C   ASP A 184    12271  10889  12401     30    332    817       C  
ATOM    693  O   ASP A 184     -13.161  24.166 -18.247  1.00 93.66           O  
ANISOU  693  O   ASP A 184    12341  10911  12334    -47    377    791       O  
ATOM    694  CB  ASP A 184     -14.659  23.216 -15.489  1.00 91.53           C  
ANISOU  694  CB  ASP A 184    11898  10586  12292     57    399    686       C  
ATOM    695  CG  ASP A 184     -15.805  22.701 -14.643  1.00 92.95           C  
ANISOU  695  CG  ASP A 184    11956  10843  12518     75    379    679       C  
ATOM    696  OD1 ASP A 184     -16.973  22.953 -15.010  1.00 95.83           O  
ANISOU  696  OD1 ASP A 184    12232  11325  12854    107    306    738       O  
ATOM    697  OD2 ASP A 184     -15.541  22.045 -13.614  1.00 91.69           O  
ANISOU  697  OD2 ASP A 184    11776  10646  12414     54    433    627       O  
ATOM    698  N   SER A 185     -14.602  25.706 -17.448  1.00 91.18           N  
ANISOU  698  N   SER A 185    11974  10529  12140    130    278    916       N  
ATOM    699  CA  SER A 185     -13.881  26.825 -18.036  1.00 90.78           C  
ANISOU  699  CA  SER A 185    12025  10403  12064    122    255   1023       C  
ATOM    700  C   SER A 185     -12.516  26.983 -17.366  1.00 87.85           C  
ANISOU  700  C   SER A 185    11716   9912  11749     82    341    987       C  
ATOM    701  O   SER A 185     -12.154  26.255 -16.436  1.00 86.48           O  
ANISOU  701  O   SER A 185    11512   9711  11635     82    417    876       O  
ATOM    702  CB  SER A 185     -14.696  28.113 -17.923  1.00 90.69           C  
ANISOU  702  CB  SER A 185    12029  10318  12109    255    147   1128       C  
ATOM    703  OG  SER A 185     -14.647  28.650 -16.613  1.00 87.60           O  
ANISOU  703  OG  SER A 185    11646   9791  11849    370    160   1081       O  
ATOM    704  N   ARG A 186     -11.746  27.957 -17.852  1.00 87.45           N  
ANISOU  704  N   ARG A 186    11752   9796  11678     35    320   1098       N  
ATOM    705  CA  ARG A 186     -10.394  28.152 -17.341  1.00 85.61           C  
ANISOU  705  CA  ARG A 186    11565   9477  11487    -30    392   1082       C  
ATOM    706  C   ARG A 186     -10.408  28.611 -15.888  1.00 82.88           C  
ANISOU  706  C   ARG A 186    11234   8964  11294     71    389   1023       C  
ATOM    707  O   ARG A 186      -9.549  28.208 -15.096  1.00 80.75           O  
ANISOU  707  O   ARG A 186    10954   8658  11068     44    469    937       O  
ATOM    708  CB  ARG A 186      -9.652  29.157 -18.218  1.00 86.71           C  
ANISOU  708  CB  ARG A 186    11784   9598  11566   -133    352   1247       C  
ATOM    709  CG  ARG A 186      -8.322  29.616 -17.660  1.00 84.52           C  
ANISOU  709  CG  ARG A 186    11547   9224  11345   -215    398   1263       C  
ATOM    710  CD  ARG A 186      -7.810  30.807 -18.441  1.00 86.65           C  
ANISOU  710  CD  ARG A 186    11900   9447  11575   -331    321   1469       C  
ATOM    711  NE  ARG A 186      -8.790  31.886 -18.478  1.00 87.06           N  
ANISOU  711  NE  ARG A 186    12042   9338  11701   -239    167   1578       N  
ATOM    712  CZ  ARG A 186      -9.046  32.635 -19.542  1.00 88.68           C  
ANISOU  712  CZ  ARG A 186    12310   9553  11832   -296     66   1767       C  
ATOM    713  NH1 ARG A 186      -8.427  32.435 -20.694  1.00 90.39           N  
ANISOU  713  NH1 ARG A 186    12501   9963  11880   -458    110   1878       N  
ATOM    714  NH2 ARG A 186      -9.952  33.604 -19.450  1.00 88.48           N  
ANISOU  714  NH2 ARG A 186    12372   9353  11894   -176    -89   1847       N  
ATOM    715  N   ASN A 187     -11.380  29.445 -15.515  1.00 81.61           N  
ANISOU  715  N   ASN A 187    11090   8713  11203    205    293   1058       N  
ATOM    716  CA  ASN A 187     -11.420  29.966 -14.152  1.00 79.32           C  
ANISOU  716  CA  ASN A 187    10820   8281  11039    326    280    985       C  
ATOM    717  C   ASN A 187     -11.845  28.890 -13.158  1.00 78.58           C  
ANISOU  717  C   ASN A 187    10615   8280  10964    384    364    846       C  
ATOM    718  O   ASN A 187     -11.153  28.645 -12.163  1.00 77.06           O  
ANISOU  718  O   ASN A 187    10422   8034  10822    380    429    763       O  
ATOM    719  CB  ASN A 187     -12.356  31.174 -14.078  1.00 80.13           C  
ANISOU  719  CB  ASN A 187    10974   8273  11200    487    142   1044       C  
ATOM    720  CG  ASN A 187     -11.714  32.445 -14.606  1.00 80.42           C  
ANISOU  720  CG  ASN A 187    11163   8126  11268    431     35   1182       C  
ATOM    721  OD1 ASN A 187     -10.497  32.613 -14.539  1.00 79.14           O  
ANISOU  721  OD1 ASN A 187    11063   7888  11120    292     69   1209       O  
ATOM    722  ND2 ASN A 187     -12.534  33.349 -15.130  1.00 82.53           N  
ANISOU  722  ND2 ASN A 187    11488   8322  11546    533   -107   1280       N  
ATOM    723  N   VAL A 188     -12.978  28.230 -13.413  1.00 79.27           N  
ANISOU  723  N   VAL A 188    10602   8513  11005    421    356    834       N  
ATOM    724  CA  VAL A 188     -13.508  27.271 -12.446  1.00 79.08           C  
ANISOU  724  CA  VAL A 188    10466   8583  10998    457    418    737       C  
ATOM    725  C   VAL A 188     -12.575  26.074 -12.307  1.00 77.08           C  
ANISOU  725  C   VAL A 188    10211   8349  10726    324    513    670       C  
ATOM    726  O   VAL A 188     -12.406  25.531 -11.208  1.00 76.02           O  
ANISOU  726  O   VAL A 188    10040   8212  10634    340    570    597       O  
ATOM    727  CB  VAL A 188     -14.938  26.849 -12.838  1.00 81.68           C  
ANISOU  727  CB  VAL A 188    10677   9079  11279    495    372    761       C  
ATOM    728  CG1 VAL A 188     -15.017  26.542 -14.316  1.00 84.54           C  
ANISOU  728  CG1 VAL A 188    11059   9510  11551    385    331    826       C  
ATOM    729  CG2 VAL A 188     -15.404  25.655 -12.013  1.00 81.79           C  
ANISOU  729  CG2 VAL A 188    10571   9211  11293    461    433    694       C  
ATOM    730  N   PHE A 189     -11.943  25.649 -13.404  1.00 78.03           N  
ANISOU  730  N   PHE A 189    10373   8500  10775    205    527    691       N  
ATOM    731  CA  PHE A 189     -10.942  24.592 -13.298  1.00 77.13           C  
ANISOU  731  CA  PHE A 189    10268   8394  10644    115    606    610       C  
ATOM    732  C   PHE A 189      -9.767  25.046 -12.442  1.00 74.00           C  
ANISOU  732  C   PHE A 189     9918   7888  10312    123    656    582       C  
ATOM    733  O   PHE A 189      -9.346  24.343 -11.517  1.00 71.84           O  
ANISOU  733  O   PHE A 189     9622   7594  10078    127    709    503       O  
ATOM    734  CB  PHE A 189     -10.458  24.161 -14.682  1.00 78.88           C  
ANISOU  734  CB  PHE A 189    10519   8697  10754     17    609    620       C  
ATOM    735  CG  PHE A 189      -9.328  23.172 -14.634  1.00 79.02           C  
ANISOU  735  CG  PHE A 189    10549   8727  10748    -38    682    520       C  
ATOM    736  CD1 PHE A 189      -9.584  21.817 -14.506  1.00 79.31           C  
ANISOU  736  CD1 PHE A 189    10564   8790  10779    -57    684    423       C  
ATOM    737  CD2 PHE A 189      -8.009  23.597 -14.691  1.00 78.23           C  
ANISOU  737  CD2 PHE A 189    10480   8609  10634    -70    736    527       C  
ATOM    738  CE1 PHE A 189      -8.549  20.905 -14.449  1.00 78.38           C  
ANISOU  738  CE1 PHE A 189    10469   8666  10646    -75    733    319       C  
ATOM    739  CE2 PHE A 189      -6.972  22.690 -14.632  1.00 77.68           C  
ANISOU  739  CE2 PHE A 189    10404   8573  10538    -91    801    426       C  
ATOM    740  CZ  PHE A 189      -7.244  21.343 -14.508  1.00 77.39           C  
ANISOU  740  CZ  PHE A 189    10358   8546  10500    -78    796    315       C  
ATOM    741  N   LEU A 190      -9.219  26.227 -12.744  1.00 73.61           N  
ANISOU  741  N   LEU A 190     9935   7761  10272    115    626    658       N  
ATOM    742  CA  LEU A 190      -8.121  26.758 -11.945  1.00 71.43           C  
ANISOU  742  CA  LEU A 190     9701   7377  10061    105    652    639       C  
ATOM    743  C   LEU A 190      -8.552  27.006 -10.507  1.00 69.55           C  
ANISOU  743  C   LEU A 190     9451   7062   9913    224    642    573       C  
ATOM    744  O   LEU A 190      -7.719  26.977  -9.594  1.00 67.74           O  
ANISOU  744  O   LEU A 190     9232   6775   9729    221    679    514       O  
ATOM    745  CB  LEU A 190      -7.588  28.046 -12.573  1.00 72.32           C  
ANISOU  745  CB  LEU A 190     9896   7408  10174     48    591    757       C  
ATOM    746  CG  LEU A 190      -6.602  27.873 -13.729  1.00 73.21           C  
ANISOU  746  CG  LEU A 190    10009   7625  10184    -99    632    822       C  
ATOM    747  CD1 LEU A 190      -6.033  29.217 -14.146  1.00 74.15           C  
ANISOU  747  CD1 LEU A 190    10208   7652  10316   -185    562    970       C  
ATOM    748  CD2 LEU A 190      -5.491  26.909 -13.348  1.00 72.60           C  
ANISOU  748  CD2 LEU A 190     9877   7620  10089   -143    735    720       C  
ATOM    749  N   PHE A 191      -9.846  27.248 -10.284  1.00 72.76           N  
ANISOU  749  N   PHE A 191     9822   7492  10331    336    593    578       N  
ATOM    750  CA  PHE A 191     -10.337  27.418  -8.922  1.00 71.83           C  
ANISOU  750  CA  PHE A 191     9669   7358  10267    466    594    506       C  
ATOM    751  C   PHE A 191     -10.316  26.098  -8.162  1.00 71.27           C  
ANISOU  751  C   PHE A 191     9514   7383  10180    435    676    438       C  
ATOM    752  O   PHE A 191      -9.910  26.055  -6.995  1.00 70.68           O  
ANISOU  752  O   PHE A 191     9435   7282  10138    477    709    375       O  
ATOM    753  CB  PHE A 191     -11.746  28.009  -8.942  1.00 73.86           C  
ANISOU  753  CB  PHE A 191     9881   7661  10521    610    522    528       C  
ATOM    754  CG  PHE A 191     -12.413  28.032  -7.598  1.00 74.30           C  
ANISOU  754  CG  PHE A 191     9859   7778  10592    758    538    446       C  
ATOM    755  CD1 PHE A 191     -12.128  29.037  -6.689  1.00 73.57           C  
ANISOU  755  CD1 PHE A 191     9834   7567  10552    886    498    381       C  
ATOM    756  CD2 PHE A 191     -13.336  27.060  -7.247  1.00 75.38           C  
ANISOU  756  CD2 PHE A 191     9855   8104  10682    764    585    437       C  
ATOM    757  CE1 PHE A 191     -12.742  29.066  -5.449  1.00 73.56           C  
ANISOU  757  CE1 PHE A 191     9753   7659  10537   1041    517    292       C  
ATOM    758  CE2 PHE A 191     -13.955  27.085  -6.010  1.00 76.07           C  
ANISOU  758  CE2 PHE A 191     9848   8297  10757    893    609    377       C  
ATOM    759  CZ  PHE A 191     -13.656  28.089  -5.110  1.00 75.27           C  
ANISOU  759  CZ  PHE A 191     9808   8101  10689   1044    582    296       C  
ATOM    760  N   LYS A 192     -10.749  25.011  -8.806  1.00 72.58           N  
ANISOU  760  N   LYS A 192     9625   7655  10297    355    696    454       N  
ATOM    761  CA  LYS A 192     -10.746  23.707  -8.148  1.00 72.32           C  
ANISOU  761  CA  LYS A 192     9536   7683  10260    306    747    409       C  
ATOM    762  C   LYS A 192      -9.324  23.220  -7.903  1.00 69.97           C  
ANISOU  762  C   LYS A 192     9294   7311   9979    245    797    357       C  
ATOM    763  O   LYS A 192      -9.006  22.726  -6.815  1.00 68.55           O  
ANISOU  763  O   LYS A 192     9096   7125   9826    259    831    316       O  
ATOM    764  CB  LYS A 192     -11.521  22.690  -8.985  1.00 74.48           C  
ANISOU  764  CB  LYS A 192     9762   8052  10486    222    723    435       C  
ATOM    765  CG  LYS A 192     -13.023  22.873  -8.956  1.00 77.09           C  
ANISOU  765  CG  LYS A 192     9990   8504  10795    273    679    484       C  
ATOM    766  CD  LYS A 192     -13.689  22.094 -10.076  1.00 80.62           C  
ANISOU  766  CD  LYS A 192    10410   9031  11192    171    630    515       C  
ATOM    767  CE  LYS A 192     -15.200  22.226 -10.012  1.00 84.25           C  
ANISOU  767  CE  LYS A 192    10738   9646  11629    211    582    573       C  
ATOM    768  NZ  LYS A 192     -15.846  21.761 -11.269  1.00 87.03           N  
ANISOU  768  NZ  LYS A 192    11070  10070  11925    120    512    606       N  
ATOM    769  N   LEU A 193      -8.456  23.339  -8.911  1.00 68.59           N  
ANISOU  769  N   LEU A 193     9174   7107   9778    180    802    364       N  
ATOM    770  CA  LEU A 193      -7.056  22.980  -8.718  1.00 66.55           C  
ANISOU  770  CA  LEU A 193     8945   6812   9528    139    850    313       C  
ATOM    771  C   LEU A 193      -6.415  23.827  -7.630  1.00 65.31           C  
ANISOU  771  C   LEU A 193     8808   6577   9431    185    857    297       C  
ATOM    772  O   LEU A 193      -5.567  23.334  -6.878  1.00 63.96           O  
ANISOU  772  O   LEU A 193     8630   6391   9280    182    893    243       O  
ATOM    773  CB  LEU A 193      -6.285  23.128 -10.031  1.00 68.25           C  
ANISOU  773  CB  LEU A 193     9189   7062   9680     67    860    334       C  
ATOM    774  CG  LEU A 193      -4.803  22.750  -9.986  1.00 67.46           C  
ANISOU  774  CG  LEU A 193     9087   6976   9568     32    914    280       C  
ATOM    775  CD1 LEU A 193      -4.632  21.279  -9.636  1.00 66.63           C  
ANISOU  775  CD1 LEU A 193     8967   6884   9464     53    934    185       C  
ATOM    776  CD2 LEU A 193      -4.117  23.077 -11.305  1.00 69.61           C  
ANISOU  776  CD2 LEU A 193     9362   7338   9751    -39    930    319       C  
ATOM    777  N   GLY A 194      -6.815  25.096  -7.523  1.00 66.65           N  
ANISOU  777  N   GLY A 194     9009   6688   9628    237    808    337       N  
ATOM    778  CA  GLY A 194      -6.266  25.951  -6.483  1.00 65.72           C  
ANISOU  778  CA  GLY A 194     8927   6477   9567    286    790    304       C  
ATOM    779  C   GLY A 194      -6.536  25.425  -5.087  1.00 65.01           C  
ANISOU  779  C   GLY A 194     8791   6420   9489    365    818    234       C  
ATOM    780  O   GLY A 194      -5.666  25.475  -4.214  1.00 64.07           O  
ANISOU  780  O   GLY A 194     8685   6264   9395    368    831    183       O  
ATOM    781  N   GLY A 195      -7.744  24.907  -4.855  1.00 66.04           N  
ANISOU  781  N   GLY A 195     8856   6643   9592    419    824    240       N  
ATOM    782  CA  GLY A 195      -8.049  24.324  -3.559  1.00 66.49           C  
ANISOU  782  CA  GLY A 195     8854   6772   9638    472    856    201       C  
ATOM    783  C   GLY A 195      -7.165  23.141  -3.220  1.00 65.16           C  
ANISOU  783  C   GLY A 195     8681   6607   9470    392    899    183       C  
ATOM    784  O   GLY A 195      -6.879  22.889  -2.046  1.00 64.94           O  
ANISOU  784  O   GLY A 195     8635   6599   9439    426    918    151       O  
ATOM    785  N   VAL A 196      -6.718  22.405  -4.238  1.00 66.01           N  
ANISOU  785  N   VAL A 196     8809   6700   9573    301    908    197       N  
ATOM    786  CA  VAL A 196      -5.803  21.293  -4.013  1.00 65.24           C  
ANISOU  786  CA  VAL A 196     8719   6587   9481    254    932    164       C  
ATOM    787  C   VAL A 196      -4.389  21.799  -3.741  1.00 64.11           C  
ANISOU  787  C   VAL A 196     8605   6393   9361    258    947    120       C  
ATOM    788  O   VAL A 196      -3.657  21.208  -2.937  1.00 63.76           O  
ANISOU  788  O   VAL A 196     8554   6344   9329    269    960     85       O  
ATOM    789  CB  VAL A 196      -5.844  20.331  -5.214  1.00 65.19           C  
ANISOU  789  CB  VAL A 196     8728   6590   9452    186    923    165       C  
ATOM    790  CG1 VAL A 196      -4.717  19.310  -5.140  1.00 64.04           C  
ANISOU  790  CG1 VAL A 196     8607   6411   9315    173    933    107       C  
ATOM    791  CG2 VAL A 196      -7.197  19.639  -5.291  1.00 66.57           C  
ANISOU  791  CG2 VAL A 196     8869   6814   9612    155    891    212       C  
ATOM    792  N   THR A 197      -3.981  22.897  -4.383  1.00 63.66           N  
ANISOU  792  N   THR A 197     8576   6302   9310    238    935    134       N  
ATOM    793  CA  THR A 197      -2.642  23.424  -4.146  1.00 63.25           C  
ANISOU  793  CA  THR A 197     8536   6217   9280    209    939    110       C  
ATOM    794  C   THR A 197      -2.543  24.123  -2.793  1.00 63.06           C  
ANISOU  794  C   THR A 197     8525   6144   9290    269    912     73       C  
ATOM    795  O   THR A 197      -1.571  23.913  -2.061  1.00 63.11           O  
ANISOU  795  O   THR A 197     8517   6153   9307    265    919     31       O  
ATOM    796  CB  THR A 197      -2.231  24.373  -5.276  1.00 64.16           C  
ANISOU  796  CB  THR A 197     8676   6316   9385    134    922    165       C  
ATOM    797  OG1 THR A 197      -2.987  25.583  -5.189  1.00 65.84           O  
ANISOU  797  OG1 THR A 197     8942   6447   9628    166    861    203       O  
ATOM    798  CG2 THR A 197      -2.475  23.732  -6.628  1.00 64.65           C  
ANISOU  798  CG2 THR A 197     8724   6455   9387     90    947    193       C  
ATOM    799  N   ALA A 198      -3.541  24.941  -2.436  1.00 64.40           N  
ANISOU  799  N   ALA A 198     8720   6282   9468    341    873     77       N  
ATOM    800  CA  ALA A 198      -3.528  25.604  -1.133  1.00 64.00           C  
ANISOU  800  CA  ALA A 198     8688   6199   9431    426    839     14       C  
ATOM    801  C   ALA A 198      -3.446  24.594   0.003  1.00 63.72           C  
ANISOU  801  C   ALA A 198     8600   6250   9363    463    880    -20       C  
ATOM    802  O   ALA A 198      -2.743  24.817   0.996  1.00 63.59           O  
ANISOU  802  O   ALA A 198     8592   6223   9348    488    863    -76       O  
ATOM    803  CB  ALA A 198      -4.774  26.473  -0.966  1.00 64.51           C  
ANISOU  803  CB  ALA A 198     8772   6248   9490    540    793      5       C  
ATOM    804  N   SER A 199      -4.158  23.474  -0.130  1.00 63.01           N  
ANISOU  804  N   SER A 199     8460   6242   9240    454    919     22       N  
ATOM    805  CA  SER A 199      -4.186  22.486   0.941  1.00 63.23           C  
ANISOU  805  CA  SER A 199     8445   6345   9233    471    942     22       C  
ATOM    806  C   SER A 199      -2.816  21.855   1.153  1.00 62.32           C  
ANISOU  806  C   SER A 199     8342   6197   9140    428    946     -1       C  
ATOM    807  O   SER A 199      -2.407  21.618   2.296  1.00 62.49           O  
ANISOU  807  O   SER A 199     8352   6252   9141    463    942    -23       O  
ATOM    808  CB  SER A 199      -5.228  21.414   0.631  1.00 64.52           C  
ANISOU  808  CB  SER A 199     8564   6580   9370    433    959     94       C  
ATOM    809  OG  SER A 199      -6.542  21.927   0.760  1.00 66.22           O  
ANISOU  809  OG  SER A 199     8731   6882   9548    491    958    117       O  
ATOM    810  N   PHE A 200      -2.087  21.581   0.069  1.00 61.40           N  
ANISOU  810  N   PHE A 200     8240   6039   9052    365    953      0       N  
ATOM    811  CA  PHE A 200      -0.787  20.932   0.218  1.00 61.05           C  
ANISOU  811  CA  PHE A 200     8184   5992   9020    351    957    -31       C  
ATOM    812  C   PHE A 200       0.240  21.876   0.835  1.00 61.53           C  
ANISOU  812  C   PHE A 200     8241   6042   9096    353    937    -76       C  
ATOM    813  O   PHE A 200       0.917  21.516   1.805  1.00 62.13           O  
ANISOU  813  O   PHE A 200     8298   6141   9166    383    924   -104       O  
ATOM    814  CB  PHE A 200      -0.281  20.406  -1.122  1.00 61.52           C  
ANISOU  814  CB  PHE A 200     8241   6052   9083    306    974    -36       C  
ATOM    815  CG  PHE A 200       1.087  19.795  -1.036  1.00 62.22           C  
ANISOU  815  CG  PHE A 200     8299   6165   9176    321    978    -84       C  
ATOM    816  CD1 PHE A 200       1.298  18.637  -0.304  1.00 62.10           C  
ANISOU  816  CD1 PHE A 200     8289   6140   9167    373    956    -97       C  
ATOM    817  CD2 PHE A 200       2.169  20.398  -1.654  1.00 63.76           C  
ANISOU  817  CD2 PHE A 200     8453   6408   9366    283    995   -105       C  
ATOM    818  CE1 PHE A 200       2.561  18.080  -0.208  1.00 62.47           C  
ANISOU  818  CE1 PHE A 200     8302   6216   9219    417    948   -148       C  
ATOM    819  CE2 PHE A 200       3.433  19.846  -1.561  1.00 65.39           C  
ANISOU  819  CE2 PHE A 200     8601   6677   9567    312   1001   -153       C  
ATOM    820  CZ  PHE A 200       3.628  18.685  -0.837  1.00 64.24           C  
ANISOU  820  CZ  PHE A 200     8463   6513   9432    395    976   -184       C  
ATOM    821  N   THR A 201       0.389  23.081   0.275  1.00 62.94           N  
ANISOU  821  N   THR A 201     8443   6177   9296    311    919    -75       N  
ATOM    822  CA  THR A 201       1.344  24.036   0.836  1.00 63.79           C  
ANISOU  822  CA  THR A 201     8557   6254   9428    284    875   -112       C  
ATOM    823  C   THR A 201       1.028  24.370   2.286  1.00 63.99           C  
ANISOU  823  C   THR A 201     8603   6272   9436    367    838   -167       C  
ATOM    824  O   THR A 201       1.937  24.703   3.055  1.00 65.31           O  
ANISOU  824  O   THR A 201     8765   6439   9610    358    798   -215       O  
ATOM    825  CB  THR A 201       1.384  25.320   0.003  1.00 64.58           C  
ANISOU  825  CB  THR A 201     8701   6277   9560    208    835    -78       C  
ATOM    826  OG1 THR A 201       0.347  26.212   0.441  1.00 65.31           O  
ANISOU  826  OG1 THR A 201     8864   6287   9663    280    784    -98       O  
ATOM    827  CG2 THR A 201       1.237  25.023  -1.469  1.00 64.57           C  
ANISOU  827  CG2 THR A 201     8683   6309   9542    145    878    -12       C  
ATOM    828  N   ALA A 202      -0.247  24.300   2.674  1.00 61.99           N  
ANISOU  828  N   ALA A 202     8364   6040   9150    449    848   -164       N  
ATOM    829  CA  ALA A 202      -0.598  24.477   4.077  1.00 63.43           C  
ANISOU  829  CA  ALA A 202     8547   6272   9283    545    827   -219       C  
ATOM    830  C   ALA A 202       0.053  23.404   4.939  1.00 63.37           C  
ANISOU  830  C   ALA A 202     8494   6344   9239    548    844   -214       C  
ATOM    831  O   ALA A 202       0.461  23.669   6.076  1.00 65.06           O  
ANISOU  831  O   ALA A 202     8709   6594   9415    594    810   -271       O  
ATOM    832  CB  ALA A 202      -2.116  24.454   4.245  1.00 62.86           C  
ANISOU  832  CB  ALA A 202     8459   6266   9159    630    851   -202       C  
ATOM    833  N   LYS A 203       0.163  22.184   4.410  1.00 63.13           N  
ANISOU  833  N   LYS A 203     8434   6334   9218    507    882   -150       N  
ATOM    834  CA  LYS A 203       0.823  21.115   5.150  1.00 64.40           C  
ANISOU  834  CA  LYS A 203     8569   6542   9358    518    877   -134       C  
ATOM    835  C   LYS A 203       2.328  21.342   5.228  1.00 65.37           C  
ANISOU  835  C   LYS A 203     8672   6652   9512    496    847   -186       C  
ATOM    836  O   LYS A 203       2.943  21.103   6.275  1.00 66.55           O  
ANISOU  836  O   LYS A 203     8804   6850   9632    530    815   -206       O  
ATOM    837  CB  LYS A 203       0.520  19.764   4.507  1.00 63.31           C  
ANISOU  837  CB  LYS A 203     8429   6392   9235    490    897    -64       C  
ATOM    838  CG  LYS A 203       0.526  18.623   5.497  1.00 65.14           C  
ANISOU  838  CG  LYS A 203     8657   6664   9431    513    875     -9       C  
ATOM    839  CD  LYS A 203       0.280  17.288   4.833  1.00 65.20           C  
ANISOU  839  CD  LYS A 203     8691   6612   9471    479    861     53       C  
ATOM    840  CE  LYS A 203       0.091  16.216   5.887  1.00 66.21           C  
ANISOU  840  CE  LYS A 203     8832   6760   9564    481    819    142       C  
ATOM    841  NZ  LYS A 203       0.933  15.012   5.632  1.00 66.20           N  
ANISOU  841  NZ  LYS A 203     8874   6662   9616    501    759    147       N  
ATOM    842  N   VAL A 204       2.942  21.793   4.131  1.00 63.20           N  
ANISOU  842  N   VAL A 204     8388   6338   9287    431    854   -197       N  
ATOM    843  CA  VAL A 204       4.367  22.109   4.163  1.00 64.46           C  
ANISOU  843  CA  VAL A 204     8501   6523   9469    390    826   -234       C  
ATOM    844  C   VAL A 204       4.629  23.246   5.143  1.00 66.32           C  
ANISOU  844  C   VAL A 204     8760   6740   9699    383    761   -289       C  
ATOM    845  O   VAL A 204       5.651  23.264   5.841  1.00 68.12           O  
ANISOU  845  O   VAL A 204     8945   7015   9920    377    719   -325       O  
ATOM    846  CB  VAL A 204       4.874  22.445   2.748  1.00 65.39           C  
ANISOU  846  CB  VAL A 204     8588   6640   9617    303    852   -214       C  
ATOM    847  CG1 VAL A 204       6.367  22.728   2.773  1.00 67.29           C  
ANISOU  847  CG1 VAL A 204     8745   6953   9869    244    829   -236       C  
ATOM    848  CG2 VAL A 204       4.556  21.308   1.786  1.00 63.99           C  
ANISOU  848  CG2 VAL A 204     8400   6482   9430    330    905   -188       C  
ATOM    849  N   GLY A 205       3.704  24.206   5.220  1.00 65.37           N  
ANISOU  849  N   GLY A 205     8708   6550   9578    397    740   -308       N  
ATOM    850  CA  GLY A 205       3.827  25.270   6.199  1.00 66.27           C  
ANISOU  850  CA  GLY A 205     8870   6629   9682    419    660   -388       C  
ATOM    851  C   GLY A 205       3.496  24.834   7.609  1.00 67.75           C  
ANISOU  851  C   GLY A 205     9052   6905   9784    529    653   -431       C  
ATOM    852  O   GLY A 205       4.095  25.332   8.567  1.00 69.59           O  
ANISOU  852  O   GLY A 205     9295   7153   9991    544    583   -508       O  
ATOM    853  N   SER A 206       2.538  23.916   7.763  1.00 68.05           N  
ANISOU  853  N   SER A 206     9072   7015   9770    593    717   -376       N  
ATOM    854  CA  SER A 206       2.261  23.363   9.085  1.00 69.73           C  
ANISOU  854  CA  SER A 206     9263   7349   9882    675    717   -381       C  
ATOM    855  C   SER A 206       3.452  22.567   9.600  1.00 70.30           C  
ANISOU  855  C   SER A 206     9293   7470   9949    654    691   -362       C  
ATOM    856  O   SER A 206       3.796  22.649  10.785  1.00 72.47           O  
ANISOU  856  O   SER A 206     9561   7825  10150    701    647   -406       O  
ATOM    857  CB  SER A 206       1.006  22.492   9.041  1.00 69.58           C  
ANISOU  857  CB  SER A 206     9221   7404   9811    706    784   -289       C  
ATOM    858  OG  SER A 206      -0.086  23.195   8.475  1.00 68.70           O  
ANISOU  858  OG  SER A 206     9130   7266   9706    734    805   -303       O  
ATOM    859  N   LEU A 207       4.089  21.787   8.722  1.00 69.76           N  
ANISOU  859  N   LEU A 207     9192   7367   9947    601    714   -307       N  
ATOM    860  CA  LEU A 207       5.371  21.178   9.063  1.00 71.24           C  
ANISOU  860  CA  LEU A 207     9328   7597  10142    600    677   -308       C  
ATOM    861  C   LEU A 207       6.408  22.247   9.384  1.00 73.01           C  
ANISOU  861  C   LEU A 207     9531   7826  10383    556    611   -395       C  
ATOM    862  O   LEU A 207       7.247  22.066  10.275  1.00 75.44           O  
ANISOU  862  O   LEU A 207     9801   8208  10656    579    555   -420       O  
ATOM    863  CB  LEU A 207       5.860  20.299   7.910  1.00 69.46           C  
ANISOU  863  CB  LEU A 207     9068   7341   9983    576    711   -266       C  
ATOM    864  CG  LEU A 207       5.637  18.785   7.960  1.00 69.57           C  
ANISOU  864  CG  LEU A 207     9091   7351   9989    630    716   -192       C  
ATOM    865  CD1 LEU A 207       4.188  18.449   8.254  1.00 69.44           C  
ANISOU  865  CD1 LEU A 207     9130   7325   9930    633    741   -120       C  
ATOM    866  CD2 LEU A 207       6.087  18.138   6.652  1.00 68.19           C  
ANISOU  866  CD2 LEU A 207     8896   7135   9878    627    740   -195       C  
ATOM    867  N   PHE A 208       6.353  23.375   8.673  1.00 71.89           N  
ANISOU  867  N   PHE A 208     9419   7602  10294    483    601   -430       N  
ATOM    868  CA  PHE A 208       7.349  24.426   8.851  1.00 73.99           C  
ANISOU  868  CA  PHE A 208     9674   7848  10593    400    518   -495       C  
ATOM    869  C   PHE A 208       7.201  25.115  10.203  1.00 75.74           C  
ANISOU  869  C   PHE A 208     9951   8078  10751    456    434   -590       C  
ATOM    870  O   PHE A 208       8.201  25.389  10.877  1.00 78.24           O  
ANISOU  870  O   PHE A 208    10234   8438  11056    422    353   -642       O  
ATOM    871  CB  PHE A 208       7.234  25.438   7.713  1.00 73.14           C  
ANISOU  871  CB  PHE A 208     9604   7627  10560    292    512   -481       C  
ATOM    872  CG  PHE A 208       8.356  26.426   7.666  1.00 76.26           C  
ANISOU  872  CG  PHE A 208     9977   7995  11003    156    419   -508       C  
ATOM    873  CD1 PHE A 208       9.670  26.009   7.766  1.00 78.56           C  
ANISOU  873  CD1 PHE A 208    10146   8409  11296     98    404   -496       C  
ATOM    874  CD2 PHE A 208       8.098  27.775   7.518  1.00 76.56           C  
ANISOU  874  CD2 PHE A 208    10117   7885  11090     82    333   -540       C  
ATOM    875  CE1 PHE A 208      10.702  26.923   7.722  1.00 81.15           C  
ANISOU  875  CE1 PHE A 208    10433   8734  11665    -58    312   -505       C  
ATOM    876  CE2 PHE A 208       9.129  28.694   7.476  1.00 79.05           C  
ANISOU  876  CE2 PHE A 208    10421   8158  11458    -79    226   -546       C  
ATOM    877  CZ  PHE A 208      10.432  28.267   7.578  1.00 81.63           C  
ANISOU  877  CZ  PHE A 208    10605   8630  11778   -162    219   -523       C  
ATOM    878  N   LEU A 209       5.963  25.407  10.616  1.00 74.40           N  
ANISOU  878  N   LEU A 209     9857   7887  10526    550    449   -624       N  
ATOM    879  CA  LEU A 209       5.749  26.042  11.914  1.00 75.97           C  
ANISOU  879  CA  LEU A 209    10106   8123  10636    635    374   -738       C  
ATOM    880  C   LEU A 209       6.205  25.139  13.052  1.00 78.09           C  
ANISOU  880  C   LEU A 209    10314   8552  10803    692    368   -725       C  
ATOM    881  O   LEU A 209       6.757  25.616  14.051  1.00 80.27           O  
ANISOU  881  O   LEU A 209    10602   8875  11020    712    277   -820       O  
ATOM    882  CB  LEU A 209       4.275  26.410  12.087  1.00 75.04           C  
ANISOU  882  CB  LEU A 209    10051   8004  10459    754    408   -775       C  
ATOM    883  CG  LEU A 209       3.676  27.379  11.068  1.00 73.46           C  
ANISOU  883  CG  LEU A 209     9925   7639  10348    731    393   -792       C  
ATOM    884  CD1 LEU A 209       2.214  27.050  10.834  1.00 71.98           C  
ANISOU  884  CD1 LEU A 209     9730   7507  10110    834    483   -750       C  
ATOM    885  CD2 LEU A 209       3.841  28.817  11.534  1.00 73.92           C  
ANISOU  885  CD2 LEU A 209    10092   7572  10423    755    254   -943       C  
ATOM    886  N   ALA A 210       5.981  23.829  12.922  1.00 77.80           N  
ANISOU  886  N   ALA A 210    10224   8592  10745    716    449   -605       N  
ATOM    887  CA  ALA A 210       6.438  22.901  13.952  1.00 80.34           C  
ANISOU  887  CA  ALA A 210    10498   9049  10977    764    429   -563       C  
ATOM    888  C   ALA A 210       7.958  22.881  14.041  1.00 81.53           C  
ANISOU  888  C   ALA A 210    10589   9214  11174    708    354   -589       C  
ATOM    889  O   ALA A 210       8.522  22.747  15.133  1.00 84.14           O  
ANISOU  889  O   ALA A 210    10897   9651  11422    747    285   -617       O  
ATOM    890  CB  ALA A 210       5.898  21.499  13.675  1.00 78.52           C  
ANISOU  890  CB  ALA A 210    10245   8850  10739    784    504   -417       C  
ATOM    891  N   ALA A 211       8.641  23.011  12.900  1.00 82.18           N  
ANISOU  891  N   ALA A 211    10631   9219  11375    618    365   -574       N  
ATOM    892  CA  ALA A 211      10.100  23.025  12.913  1.00 84.38           C  
ANISOU  892  CA  ALA A 211    10818   9550  11692    559    299   -593       C  
ATOM    893  C   ALA A 211      10.630  24.255  13.635  1.00 87.47           C  
ANISOU  893  C   ALA A 211    11230   9939  12065    500    184   -707       C  
ATOM    894  O   ALA A 211      11.609  24.171  14.386  1.00 90.53           O  
ANISOU  894  O   ALA A 211    11552  10427  12417    494    102   -738       O  
ATOM    895  CB  ALA A 211      10.639  22.964  11.485  1.00 82.80           C  
ANISOU  895  CB  ALA A 211    10552   9311  11599    471    348   -550       C  
ATOM    896  N   ILE A 212       9.991  25.408  13.424  1.00 90.03           N  
ANISOU  896  N   ILE A 212    11652  10140  12415    460    159   -776       N  
ATOM    897  CA  ILE A 212      10.374  26.614  14.149  1.00 92.21           C  
ANISOU  897  CA  ILE A 212    11986  10373  12677    414     23   -905       C  
ATOM    898  C   ILE A 212      10.066  26.463  15.633  1.00 93.75           C  
ANISOU  898  C   ILE A 212    12216  10683  12724    548    -23   -986       C  
ATOM    899  O   ILE A 212      10.884  26.818  16.490  1.00 96.71           O  
ANISOU  899  O   ILE A 212    12574  11118  13054    524   -140  -1068       O  
ATOM    900  CB  ILE A 212       9.673  27.843  13.539  1.00 90.42           C  
ANISOU  900  CB  ILE A 212    11882   9955  12520    367    -10   -960       C  
ATOM    901  CG1 ILE A 212      10.521  28.431  12.412  1.00 91.02           C  
ANISOU  901  CG1 ILE A 212    11920   9937  12728    168    -46   -903       C  
ATOM    902  CG2 ILE A 212       9.405  28.902  14.595  1.00 91.54           C  
ANISOU  902  CG2 ILE A 212    12142  10038  12601    426   -142  -1129       C  
ATOM    903  CD1 ILE A 212      11.789  29.097  12.900  1.00 95.05           C  
ANISOU  903  CD1 ILE A 212    12391  10461  13262     30   -195   -959       C  
ATOM    904  N   ASP A 213       8.889  25.918  15.958  1.00 85.69           N  
ANISOU  904  N   ASP A 213    11230   9717  11610    680     66   -956       N  
ATOM    905  CA  ASP A 213       8.497  25.753  17.354  1.00 87.62           C  
ANISOU  905  CA  ASP A 213    11494  10114  11682    807     38  -1016       C  
ATOM    906  C   ASP A 213       9.513  24.919  18.125  1.00 89.87           C  
ANISOU  906  C   ASP A 213    11692  10550  11905    808     -7   -965       C  
ATOM    907  O   ASP A 213       9.848  25.238  19.271  1.00 93.06           O  
ANISOU  907  O   ASP A 213    12107  11060  12192    852   -102  -1061       O  
ATOM    908  CB  ASP A 213       7.112  25.111  17.431  1.00 86.08           C  
ANISOU  908  CB  ASP A 213    11311   9996  11400    916    159   -940       C  
ATOM    909  CG  ASP A 213       6.741  24.696  18.838  1.00 88.60           C  
ANISOU  909  CG  ASP A 213    11617  10532  11515   1032    153   -950       C  
ATOM    910  OD1 ASP A 213       6.676  25.575  19.721  1.00 90.45           O  
ANISOU  910  OD1 ASP A 213    11902  10822  11644   1105     72  -1112       O  
ATOM    911  OD2 ASP A 213       6.518  23.488  19.061  1.00 89.44           O  
ANISOU  911  OD2 ASP A 213    11668  10753  11561   1048    220   -794       O  
ATOM    912  N   ARG A 214      10.018  23.847  17.510  1.00 87.55           N  
ANISOU  912  N   ARG A 214    11314  10270  11683    773     48   -825       N  
ATOM    913  CA  ARG A 214      11.005  23.011  18.184  1.00 90.05           C  
ANISOU  913  CA  ARG A 214    11546  10718  11950    796     -7   -772       C  
ATOM    914  C   ARG A 214      12.377  23.673  18.196  1.00 92.41           C  
ANISOU  914  C   ARG A 214    11778  11024  12310    699   -123   -854       C  
ATOM    915  O   ARG A 214      13.139  23.510  19.157  1.00 95.85           O  
ANISOU  915  O   ARG A 214    12164  11590  12664    724   -218   -879       O  
ATOM    916  CB  ARG A 214      11.074  21.638  17.516  1.00 87.81           C  
ANISOU  916  CB  ARG A 214    11209  10429  11728    820     71   -613       C  
ATOM    917  CG  ARG A 214       9.835  20.769  17.706  1.00 86.53           C  
ANISOU  917  CG  ARG A 214    11100  10284  11492    893    155   -499       C  
ATOM    918  CD  ARG A 214       9.767  20.173  19.107  1.00 90.44           C  
ANISOU  918  CD  ARG A 214    11597  10946  11820    971    106   -443       C  
ATOM    919  NE  ARG A 214       9.283  21.130  20.095  1.00 92.08           N  
ANISOU  919  NE  ARG A 214    11846  11259  11882   1006     75   -562       N  
ATOM    920  CZ  ARG A 214       9.249  20.905  21.401  1.00 95.36           C  
ANISOU  920  CZ  ARG A 214    12259  11858  12116   1073     26   -549       C  
ATOM    921  NH1 ARG A 214       9.659  19.758  21.916  1.00 97.80           N  
ANISOU  921  NH1 ARG A 214    12534  12254  12373   1099     -7   -401       N  
ATOM    922  NH2 ARG A 214       8.796  21.858  22.211  1.00 97.03           N  
ANISOU  922  NH2 ARG A 214    12510  12171  12188   1124     -2   -692       N  
ATOM    923  N   TYR A 215      12.709  24.413  17.135  1.00 95.76           N  
ANISOU  923  N   TYR A 215    12191  11325  12870    574   -122   -881       N  
ATOM    924  CA  TYR A 215      13.989  25.112  17.080  1.00 99.74           C  
ANISOU  924  CA  TYR A 215    12616  11845  13434    441   -237   -939       C  
ATOM    925  C   TYR A 215      14.175  26.011  18.295  1.00102.50           C  
ANISOU  925  C   TYR A 215    13030  12223  13693    436   -385  -1085       C  
ATOM    926  O   TYR A 215      15.199  25.945  18.982  1.00105.96           O  
ANISOU  926  O   TYR A 215    13384  12787  14090    409   -491  -1112       O  
ATOM    927  CB  TYR A 215      14.092  25.923  15.784  1.00 98.51           C  
ANISOU  927  CB  TYR A 215    12463  11547  13419    286   -217   -930       C  
ATOM    928  CG  TYR A 215      15.027  25.330  14.749  1.00 99.63           C  
ANISOU  928  CG  TYR A 215    12443  11763  13646    212   -161   -828       C  
ATOM    929  CD1 TYR A 215      15.259  23.965  14.693  1.00 99.36           C  
ANISOU  929  CD1 TYR A 215    12319  11847  13588    336    -90   -746       C  
ATOM    930  CD2 TYR A 215      15.679  26.140  13.829  1.00101.71           C  
ANISOU  930  CD2 TYR A 215    12647  11989  14008     23   -189   -812       C  
ATOM    931  CE1 TYR A 215      16.115  23.418  13.748  1.00100.84           C  
ANISOU  931  CE1 TYR A 215    12353  12123  13838    307    -42   -682       C  
ATOM    932  CE2 TYR A 215      16.538  25.603  12.881  1.00103.79           C  
ANISOU  932  CE2 TYR A 215    12738  12376  14322    -31   -127   -725       C  
ATOM    933  CZ  TYR A 215      16.751  24.242  12.845  1.00103.57           C  
ANISOU  933  CZ  TYR A 215    12616  12475  14259    128    -51   -676       C  
ATOM    934  OH  TYR A 215      17.602  23.705  11.904  1.00105.32           O  
ANISOU  934  OH  TYR A 215    12663  12837  14517    112      8   -618       O  
ATOM    935  N   ILE A 216      13.178  26.846  18.593  1.00103.33           N  
ANISOU  935  N   ILE A 216    13284  12222  13756    479   -402  -1191       N  
ATOM    936  CA  ILE A 216      13.312  27.774  19.708  1.00105.33           C  
ANISOU  936  CA  ILE A 216    13618  12485  13916    492   -557  -1364       C  
ATOM    937  C   ILE A 216      13.197  27.070  21.056  1.00107.41           C  
ANISOU  937  C   ILE A 216    13864  12963  13985    644   -568  -1380       C  
ATOM    938  O   ILE A 216      13.659  27.608  22.069  1.00109.86           O  
ANISOU  938  O   ILE A 216    14199  13343  14198    651   -711  -1513       O  
ATOM    939  CB  ILE A 216      12.281  28.909  19.577  1.00102.95           C  
ANISOU  939  CB  ILE A 216    13487  12000  13629    525   -584  -1494       C  
ATOM    940  CG1 ILE A 216      10.955  28.516  20.215  1.00101.32           C  
ANISOU  940  CG1 ILE A 216    13342  11890  13266    735   -486  -1519       C  
ATOM    941  CG2 ILE A 216      12.071  29.269  18.117  1.00100.04           C  
ANISOU  941  CG2 ILE A 216    13137  11438  13436    409   -522  -1412       C  
ATOM    942  CD1 ILE A 216      10.009  29.663  20.308  1.00 99.61           C  
ANISOU  942  CD1 ILE A 216    13280  11536  13033    817   -537  -1686       C  
ATOM    943  N   SER A 217      12.597  25.878  21.101  1.00101.74           N  
ANISOU  943  N   SER A 217    13108  12350  13200    755   -434  -1240       N  
ATOM    944  CA  SER A 217      12.624  25.093  22.332  1.00104.50           C  
ANISOU  944  CA  SER A 217    13425  12916  13364    870   -453  -1206       C  
ATOM    945  C   SER A 217      14.038  24.628  22.652  1.00107.76           C  
ANISOU  945  C   SER A 217    13716  13436  13790    819   -552  -1163       C  
ATOM    946  O   SER A 217      14.433  24.575  23.822  1.00110.01           O  
ANISOU  946  O   SER A 217    13988  13883  13926    871   -653  -1213       O  
ATOM    947  CB  SER A 217      11.684  23.893  22.220  1.00102.15           C  
ANISOU  947  CB  SER A 217    13119  12681  13013    964   -305  -1032       C  
ATOM    948  OG  SER A 217      11.663  23.156  23.430  1.00105.40           O  
ANISOU  948  OG  SER A 217    13508  13304  13235   1058   -331   -972       O  
ATOM    949  N   ILE A 218      14.814  24.286  21.622  1.00105.21           N  
ANISOU  949  N   ILE A 218    13294  13050  13631    727   -526  -1076       N  
ATOM    950  CA  ILE A 218      16.180  23.820  21.839  1.00108.40           C  
ANISOU  950  CA  ILE A 218    13553  13580  14052    695   -616  -1036       C  
ATOM    951  C   ILE A 218      17.110  24.994  22.130  1.00111.38           C  
ANISOU  951  C   ILE A 218    13902  13963  14453    557   -777  -1180       C  
ATOM    952  O   ILE A 218      17.975  24.915  23.012  1.00113.03           O  
ANISOU  952  O   ILE A 218    14038  14328  14580    561   -904  -1214       O  
ATOM    953  CB  ILE A 218      16.663  23.005  20.622  1.00106.05           C  
ANISOU  953  CB  ILE A 218    13142  13250  13903    673   -526   -904       C  
ATOM    954  CG1 ILE A 218      15.842  21.721  20.413  1.00101.03           C  
ANISOU  954  CG1 ILE A 218    12544  12595  13247    806   -403   -760       C  
ATOM    955  CG2 ILE A 218      18.135  22.668  20.761  1.00108.34           C  
ANISOU  955  CG2 ILE A 218    13256  13691  14216    649   -623   -885       C  
ATOM    956  CD1 ILE A 218      15.247  21.110  21.667  1.00102.66           C  
ANISOU  956  CD1 ILE A 218    12818  12910  13277    929   -424   -711       C  
ATOM    957  N   HIS A 219      16.943  26.105  21.405  1.00116.30           N  
ANISOU  957  N   HIS A 219    14590  14411  15189    422   -792  -1261       N  
ATOM    958  CA  HIS A 219      17.880  27.219  21.511  1.00117.23           C  
ANISOU  958  CA  HIS A 219    14683  14498  15362    244   -963  -1372       C  
ATOM    959  C   HIS A 219      17.589  28.117  22.710  1.00117.36           C  
ANISOU  959  C   HIS A 219    14841  14499  15251    277  -1113  -1564       C  
ATOM    960  O   HIS A 219      18.517  28.718  23.264  1.00119.32           O  
ANISOU  960  O   HIS A 219    15054  14797  15487    167  -1291  -1658       O  
ATOM    961  CB  HIS A 219      17.870  28.038  20.216  1.00115.76           C  
ANISOU  961  CB  HIS A 219    14516  14114  15351     65   -939  -1354       C  
ATOM    962  CG  HIS A 219      18.448  27.313  19.040  1.00116.74           C  
ANISOU  962  CG  HIS A 219    14470  14300  15586      5   -823  -1194       C  
ATOM    963  ND1 HIS A 219      19.806  27.186  18.839  1.00119.20           N  
ANISOU  963  ND1 HIS A 219    14579  14769  15942   -115   -887  -1145       N  
ATOM    964  CD2 HIS A 219      17.855  26.672  18.004  1.00115.28           C  
ANISOU  964  CD2 HIS A 219    14279  14061  15462     60   -651  -1083       C  
ATOM    965  CE1 HIS A 219      20.024  26.497  17.734  1.00119.20           C  
ANISOU  965  CE1 HIS A 219    14453  14820  16017   -113   -753  -1020       C  
ATOM    966  NE2 HIS A 219      18.857  26.174  17.207  1.00117.45           N  
ANISOU  966  NE2 HIS A 219    14358  14460  15809    -10   -613   -984       N  
ATOM    967  N   ARG A 220      16.327  28.228  23.121  1.00109.47           N  
ANISOU  967  N   ARG A 220    13994  13450  14148    430  -1051  -1632       N  
ATOM    968  CA  ARG A 220      15.944  28.980  24.317  1.00109.43           C  
ANISOU  968  CA  ARG A 220    14123  13472  13985    517  -1179  -1835       C  
ATOM    969  C   ARG A 220      15.023  28.115  25.169  1.00110.17           C  
ANISOU  969  C   ARG A 220    14236  13754  13869    738  -1070  -1798       C  
ATOM    970  O   ARG A 220      13.813  28.359  25.244  1.00108.03           O  
ANISOU  970  O   ARG A 220    14076  13443  13528    859   -991  -1857       O  
ATOM    971  CB  ARG A 220      15.269  30.301  23.945  1.00107.15           C  
ANISOU  971  CB  ARG A 220    14014  12927  13773    481  -1242  -1995       C  
ATOM    972  N   PRO A 221      15.572  27.093  25.838  1.00115.70           N  
ANISOU  972  N   PRO A 221    14823  14678  14460    791  -1069  -1689       N  
ATOM    973  CA  PRO A 221      14.702  26.173  26.596  1.00115.98           C  
ANISOU  973  CA  PRO A 221    14870  14901  14296    970   -964  -1601       C  
ATOM    974  C   PRO A 221      13.906  26.866  27.683  1.00115.89           C  
ANISOU  974  C   PRO A 221    14977  14990  14065   1099  -1014  -1790       C  
ATOM    975  O   PRO A 221      12.745  26.516  27.930  1.00115.08           O  
ANISOU  975  O   PRO A 221    14912  14980  13832   1230   -888  -1748       O  
ATOM    976  CB  PRO A 221      15.686  25.162  27.204  1.00118.21           C  
ANISOU  976  CB  PRO A 221    15022  15383  14508    982  -1020  -1471       C  
ATOM    977  CG  PRO A 221      16.971  25.340  26.503  1.00118.82           C  
ANISOU  977  CG  PRO A 221    14989  15384  14775    829  -1103  -1459       C  
ATOM    978  CD  PRO A 221      16.976  26.649  25.785  1.00117.72           C  
ANISOU  978  CD  PRO A 221    14920  15024  14783    688  -1154  -1607       C  
ATOM    979  N   LEU A 222      14.507  27.856  28.337  1.00123.19           N  
ANISOU  979  N   LEU A 222    15955  15913  14940   1065  -1203  -2005       N  
ATOM    980  CA  LEU A 222      13.903  28.428  29.533  1.00123.19           C  
ANISOU  980  CA  LEU A 222    16057  16060  14691   1218  -1274  -2209       C  
ATOM    981  C   LEU A 222      12.698  29.289  29.185  1.00120.96           C  
ANISOU  981  C   LEU A 222    15914  15627  14420   1312  -1219  -2361       C  
ATOM    982  O   LEU A 222      11.708  29.311  29.925  1.00121.08           O  
ANISOU  982  O   LEU A 222    15974  15820  14212   1499  -1161  -2443       O  
ATOM    983  CB  LEU A 222      14.940  29.238  30.305  1.00125.15           C  
ANISOU  983  CB  LEU A 222    16332  16329  14889   1151  -1518  -2412       C  
ATOM    984  CG  LEU A 222      16.123  28.544  30.988  1.00128.04           C  
ANISOU  984  CG  LEU A 222    16563  16908  15178   1099  -1617  -2318       C  
ATOM    985  CD1 LEU A 222      16.894  27.546  30.123  1.00128.22           C  
ANISOU  985  CD1 LEU A 222    16423  16907  15388    984  -1539  -2056       C  
ATOM    986  CD2 LEU A 222      17.042  29.618  31.437  1.00129.88           C  
ANISOU  986  CD2 LEU A 222    16842  17081  15424    989  -1867  -2546       C  
ATOM    987  N   ALA A 223      12.764  30.004  28.069  1.00115.81           N  
ANISOU  987  N   ALA A 223    15320  14668  14014   1191  -1239  -2393       N  
ATOM    988  CA  ALA A 223      11.632  30.768  27.556  1.00112.93           C  
ANISOU  988  CA  ALA A 223    15084  14129  13697   1281  -1187  -2507       C  
ATOM    989  C   ALA A 223      11.023  29.970  26.408  1.00111.15           C  
ANISOU  989  C   ALA A 223    14787  13839  13607   1250   -972  -2266       C  
ATOM    990  O   ALA A 223      11.509  30.023  25.275  1.00110.16           O  
ANISOU  990  O   ALA A 223    14636  13505  13714   1083   -961  -2162       O  
ATOM    991  CB  ALA A 223      12.071  32.158  27.110  1.00111.91           C  
ANISOU  991  CB  ALA A 223    15094  13681  13746   1163  -1381  -2700       C  
ATOM    992  N   TYR A 224       9.973  29.206  26.712  1.00109.52           N  
ANISOU  992  N   TYR A 224    14538  13833  13241   1402   -807  -2170       N  
ATOM    993  CA  TYR A 224       9.212  28.494  25.692  1.00107.10           C  
ANISOU  993  CA  TYR A 224    14182  13471  13042   1387   -616  -1965       C  
ATOM    994  C   TYR A 224       7.714  28.684  25.862  1.00105.68           C  
ANISOU  994  C   TYR A 224    14042  13385  12726   1569   -505  -2025       C  
ATOM    995  O   TYR A 224       7.009  28.906  24.876  1.00103.61           O  
ANISOU  995  O   TYR A 224    13809  12959  12599   1564   -424  -1992       O  
ATOM    996  CB  TYR A 224       9.553  26.990  25.709  1.00109.25           C  
ANISOU  996  CB  TYR A 224    14318  13902  13290   1338   -513  -1697       C  
ATOM    997  CG  TYR A 224       8.794  26.191  24.671  1.00106.08           C  
ANISOU  997  CG  TYR A 224    13874  13432  12999   1313   -336  -1492       C  
ATOM    998  CD1 TYR A 224       9.184  26.206  23.335  1.00103.95           C  
ANISOU  998  CD1 TYR A 224    13595  12925  12977   1180   -309  -1417       C  
ATOM    999  CD2 TYR A 224       7.690  25.425  25.021  1.00106.24           C  
ANISOU  999  CD2 TYR A 224    13859  13643  12865   1411   -203  -1369       C  
ATOM   1000  CE1 TYR A 224       8.500  25.481  22.384  1.00101.33           C  
ANISOU 1000  CE1 TYR A 224    13232  12532  12736   1160   -162  -1248       C  
ATOM   1001  CE2 TYR A 224       6.999  24.697  24.073  1.00104.46           C  
ANISOU 1001  CE2 TYR A 224    13600  13346  12744   1371    -62  -1187       C  
ATOM   1002  CZ  TYR A 224       7.409  24.729  22.757  1.00102.02           C  
ANISOU 1002  CZ  TYR A 224    13296  12785  12682   1253    -46  -1138       C  
ATOM   1003  OH  TYR A 224       6.720  24.002  21.814  1.00100.22           O  
ANISOU 1003  OH  TYR A 224    13043  12489  12548   1218     82   -973       O  
ATOM   1004  N   LYS A 225       7.210  28.602  27.094  1.00108.79           N  
ANISOU 1004  N   LYS A 225    14424  14069  12842   1733   -501  -2109       N  
ATOM   1005  CA  LYS A 225       5.790  28.850  27.332  1.00107.63           C  
ANISOU 1005  CA  LYS A 225    14288  14070  12536   1925   -399  -2185       C  
ATOM   1006  C   LYS A 225       5.427  30.311  27.084  1.00105.75           C  
ANISOU 1006  C   LYS A 225    14197  13615  12367   2031   -508  -2472       C  
ATOM   1007  O   LYS A 225       4.292  30.612  26.691  1.00104.12           O  
ANISOU 1007  O   LYS A 225    14005  13403  12153   2157   -421  -2512       O  
ATOM   1008  CB  LYS A 225       5.418  28.449  28.761  1.00110.78           C  
ANISOU 1008  CB  LYS A 225    14623  14878  12591   2075   -373  -2211       C  
ATOM   1009  CG  LYS A 225       3.943  28.176  28.983  1.00110.47           C  
ANISOU 1009  CG  LYS A 225    14510  15106  12357   2234   -206  -2165       C  
ATOM   1010  CD  LYS A 225       3.717  27.534  30.344  1.00112.74           C  
ANISOU 1010  CD  LYS A 225    14701  15839  12296   2326   -165  -2106       C  
ATOM   1011  CE  LYS A 225       2.254  27.197  30.556  1.00111.99           C  
ANISOU 1011  CE  LYS A 225    14496  16061  11994   2455     12  -2025       C  
ATOM   1012  NZ  LYS A 225       2.014  26.525  31.860  1.00114.71           N  
ANISOU 1012  NZ  LYS A 225    14731  16873  11980   2518     61  -1927       N  
ATOM   1013  N   ARG A 226       6.396  31.204  27.282  1.00105.39           N  
ANISOU 1013  N   ARG A 226    14262  13380  12401   1972   -714  -2663       N  
ATOM   1014  CA  ARG A 226       6.125  32.656  27.122  1.00104.06           C  
ANISOU 1014  CA  ARG A 226    14272  12960  12307   2069   -867  -2951       C  
ATOM   1015  C   ARG A 226       6.242  33.067  25.652  1.00101.56           C  
ANISOU 1015  C   ARG A 226    14017  12263  12310   1906   -877  -2862       C  
ATOM   1016  O   ARG A 226       5.552  34.021  25.270  1.00100.43           O  
ANISOU 1016  O   ARG A 226    14001  11927  12232   2019   -934  -3020       O  
ATOM   1017  CB  ARG A 226       7.084  33.478  27.986  1.00106.07           C  
ANISOU 1017  CB  ARG A 226    14636  13157  12508   2057  -1112  -3197       C  
ATOM   1018  CG  ARG A 226       6.412  34.231  29.124  1.00106.68           C  
ANISOU 1018  CG  ARG A 226    14808  13403  12323   2343  -1200  -3519       C  
ATOM   1019  CD  ARG A 226       5.928  33.308  30.224  1.00108.60           C  
ANISOU 1019  CD  ARG A 226    14904  14133  12227   2496  -1056  -3456       C  
ATOM   1020  NE  ARG A 226       5.287  34.037  31.307  1.00110.08           N  
ANISOU 1020  NE  ARG A 226    15165  14528  12134   2787  -1132  -3778       N  
ATOM   1021  CZ  ARG A 226       4.855  33.481  32.432  1.00112.15           C  
ANISOU 1021  CZ  ARG A 226    15315  15248  12047   2949  -1041  -3785       C  
ATOM   1022  NH1 ARG A 226       5.001  32.182  32.625  1.00113.82           N  
ANISOU 1022  NH1 ARG A 226    15353  15726  12168   2830   -885  -3469       N  
ATOM   1023  NH2 ARG A 226       4.284  34.225  33.361  1.00113.22           N  
ANISOU 1023  NH2 ARG A 226    15519  15579  11922   3233  -1115  -4108       N  
ATOM   1024  N   ILE A 227       7.098  32.405  24.871  1.00100.79           N  
ANISOU 1024  N   ILE A 227    13836  12069  12393   1665   -835  -2628       N  
ATOM   1025  CA  ILE A 227       7.295  32.812  23.484  1.00 98.46           C  
ANISOU 1025  CA  ILE A 227    13588  11445  12376   1496   -848  -2539       C  
ATOM   1026  C   ILE A 227       6.325  32.082  22.562  1.00 96.18           C  
ANISOU 1026  C   ILE A 227    13219  11188  12137   1523   -633  -2338       C  
ATOM   1027  O   ILE A 227       5.782  32.675  21.623  1.00 94.74           O  
ANISOU 1027  O   ILE A 227    13113  10785  12098   1521   -630  -2345       O  
ATOM   1028  CB  ILE A 227       8.764  32.600  23.073  1.00 99.61           C  
ANISOU 1028  CB  ILE A 227    13676  11490  12681   1228   -926  -2417       C  
ATOM   1029  CG1 ILE A 227       8.959  32.873  21.581  1.00 97.89           C  
ANISOU 1029  CG1 ILE A 227    13474  10997  12723   1040   -908  -2282       C  
ATOM   1030  CG2 ILE A 227       9.230  31.208  23.436  1.00102.34           C  
ANISOU 1030  CG2 ILE A 227    13846  12107  12932   1193   -805  -2222       C  
ATOM   1031  CD1 ILE A 227      10.312  33.460  21.242  1.00 99.21           C  
ANISOU 1031  CD1 ILE A 227    13655  10987  13052    788  -1080  -2280       C  
ATOM   1032  N   VAL A 228       6.072  30.798  22.816  1.00 93.91           N  
ANISOU 1032  N   VAL A 228    12785  11165  11732   1544   -466  -2154       N  
ATOM   1033  CA  VAL A 228       5.058  30.070  22.062  1.00 91.78           C  
ANISOU 1033  CA  VAL A 228    12442  10946  11486   1572   -276  -1975       C  
ATOM   1034  C   VAL A 228       3.764  30.064  22.863  1.00 92.29           C  
ANISOU 1034  C   VAL A 228    12483  11266  11316   1807   -196  -2059       C  
ATOM   1035  O   VAL A 228       3.298  29.006  23.301  1.00 93.99           O  
ANISOU 1035  O   VAL A 228    12578  11754  11381   1838    -63  -1905       O  
ATOM   1036  CB  VAL A 228       5.495  28.630  21.735  1.00 92.28           C  
ANISOU 1036  CB  VAL A 228    12368  11113  11582   1439   -155  -1705       C  
ATOM   1037  CG1 VAL A 228       4.680  28.078  20.566  1.00 89.62           C  
ANISOU 1037  CG1 VAL A 228    11989  10707  11355   1403     -5  -1532       C  
ATOM   1038  CG2 VAL A 228       6.970  28.572  21.437  1.00 92.97           C  
ANISOU 1038  CG2 VAL A 228    12439  11073  11811   1255   -252  -1663       C  
ATOM   1039  N   THR A 229       3.184  31.242  23.074  1.00 93.18           N  
ANISOU 1039  N   THR A 229    12709  11302  11392   1975   -286  -2302       N  
ATOM   1040  CA  THR A 229       1.852  31.309  23.652  1.00 93.48           C  
ANISOU 1040  CA  THR A 229    12704  11597  11215   2221   -197  -2390       C  
ATOM   1041  C   THR A 229       0.857  30.606  22.740  1.00 91.53           C  
ANISOU 1041  C   THR A 229    12353  11398  11025   2199    -13  -2176       C  
ATOM   1042  O   THR A 229       1.060  30.501  21.527  1.00 89.75           O  
ANISOU 1042  O   THR A 229    12148  10923  11029   2042      7  -2043       O  
ATOM   1043  CB  THR A 229       1.419  32.761  23.858  1.00 92.93           C  
ANISOU 1043  CB  THR A 229    12791  11385  11132   2429   -345  -2707       C  
ATOM   1044  OG1 THR A 229       0.813  33.253  22.654  1.00 90.80           O  
ANISOU 1044  OG1 THR A 229    12580  10860  11060   2429   -332  -2680       O  
ATOM   1045  CG2 THR A 229       2.601  33.635  24.222  1.00 94.07           C  
ANISOU 1045  CG2 THR A 229    13091  11298  11354   2357   -577  -2897       C  
ATOM   1046  N   ARG A 230      -0.225  30.112  23.334  1.00 91.92           N  
ANISOU 1046  N   ARG A 230    12281  11794  10849   2347    119  -2138       N  
ATOM   1047  CA  ARG A 230      -1.307  29.570  22.516  1.00 90.77           C  
ANISOU 1047  CA  ARG A 230    12034  11710  10743   2339    274  -1961       C  
ATOM   1048  C   ARG A 230      -1.854  30.599  21.532  1.00 87.94           C  
ANISOU 1048  C   ARG A 230    11774  11084  10555   2421    223  -2082       C  
ATOM   1049  O   ARG A 230      -2.027  30.253  20.351  1.00 86.14           O  
ANISOU 1049  O   ARG A 230    11529  10690  10510   2286    286  -1911       O  
ATOM   1050  CB  ARG A 230      -2.421  29.010  23.402  1.00 92.51           C  
ANISOU 1050  CB  ARG A 230    12093  12385  10673   2486    410  -1913       C  
ATOM   1051  CG  ARG A 230      -3.770  29.146  22.737  1.00 92.24           C  
ANISOU 1051  CG  ARG A 230    11981  12422  10644   2590    512  -1885       C  
ATOM   1052  CD  ARG A 230      -4.866  28.317  23.344  1.00 94.23           C  
ANISOU 1052  CD  ARG A 230    12027  13134  10643   2647    674  -1738       C  
ATOM   1053  NE  ARG A 230      -6.049  28.457  22.507  1.00 94.14           N  
ANISOU 1053  NE  ARG A 230    11939  13145  10685   2713    757  -1698       N  
ATOM   1054  CZ  ARG A 230      -7.196  27.823  22.695  1.00 95.61           C  
ANISOU 1054  CZ  ARG A 230    11927  13703  10700   2742    901  -1551       C  
ATOM   1055  NH1 ARG A 230      -7.381  27.017  23.727  1.00 97.59           N  
ANISOU 1055  NH1 ARG A 230    12035  14349  10696   2711    984  -1421       N  
ATOM   1056  NH2 ARG A 230      -8.188  28.016  21.832  1.00 93.68           N  
ANISOU 1056  NH2 ARG A 230    11618  13445  10533   2793    956  -1524       N  
ATOM   1057  N   PRO A 231      -2.140  31.853  21.921  1.00 85.86           N  
ANISOU 1057  N   PRO A 231    11625  10756  10243   2643    100  -2371       N  
ATOM   1058  CA  PRO A 231      -2.599  32.821  20.907  1.00 83.88           C  
ANISOU 1058  CA  PRO A 231    11489  10203  10179   2711     27  -2461       C  
ATOM   1059  C   PRO A 231      -1.584  33.067  19.804  1.00 82.29           C  
ANISOU 1059  C   PRO A 231    11410   9584  10271   2460    -69  -2368       C  
ATOM   1060  O   PRO A 231      -1.973  33.170  18.634  1.00 80.26           O  
ANISOU 1060  O   PRO A 231    11170   9145  10181   2399    -40  -2262       O  
ATOM   1061  CB  PRO A 231      -2.880  34.092  21.728  1.00 84.31           C  
ANISOU 1061  CB  PRO A 231    11670  10247  10117   3003   -129  -2814       C  
ATOM   1062  CG  PRO A 231      -2.208  33.881  23.042  1.00 86.86           C  
ANISOU 1062  CG  PRO A 231    11978  10785  10239   3024   -169  -2914       C  
ATOM   1063  CD  PRO A 231      -2.252  32.412  23.282  1.00 88.13           C  
ANISOU 1063  CD  PRO A 231    11935  11271  10281   2877     26  -2630       C  
ATOM   1064  N   LYS A 232      -0.293  33.158  20.138  1.00 82.96           N  
ANISOU 1064  N   LYS A 232    11569   9541  10412   2308   -183  -2397       N  
ATOM   1065  CA  LYS A 232       0.723  33.336  19.104  1.00 81.48           C  
ANISOU 1065  CA  LYS A 232    11461   9015  10481   2050   -261  -2287       C  
ATOM   1066  C   LYS A 232       0.711  32.175  18.120  1.00 80.82           C  
ANISOU 1066  C   LYS A 232    11247   8971  10491   1865    -91  -1993       C  
ATOM   1067  O   LYS A 232       0.876  32.374  16.912  1.00 79.07           O  
ANISOU 1067  O   LYS A 232    11068   8512  10464   1727   -101  -1891       O  
ATOM   1068  CB  LYS A 232       2.107  33.487  19.736  1.00 84.04           C  
ANISOU 1068  CB  LYS A 232    11839   9275  10819   1915   -397  -2352       C  
ATOM   1069  CG  LYS A 232       3.233  33.711  18.731  1.00 83.63           C  
ANISOU 1069  CG  LYS A 232    11841   8923  11012   1637   -482  -2237       C  
ATOM   1070  CD  LYS A 232       4.051  32.449  18.498  1.00 83.74           C  
ANISOU 1070  CD  LYS A 232    11701   9068  11048   1439   -364  -2006       C  
ATOM   1071  CE  LYS A 232       5.136  32.683  17.462  1.00 83.60           C  
ANISOU 1071  CE  LYS A 232    11706   8809  11249   1179   -432  -1896       C  
ATOM   1072  NZ  LYS A 232       5.924  31.448  17.201  1.00 83.52           N  
ANISOU 1072  NZ  LYS A 232    11540   8939  11256   1027   -320  -1694       N  
ATOM   1073  N   ALA A 233       0.517  30.952  18.619  1.00 81.66           N  
ANISOU 1073  N   ALA A 233    11200   9372  10455   1856     55  -1854       N  
ATOM   1074  CA  ALA A 233       0.447  29.796  17.733  1.00 80.36           C  
ANISOU 1074  CA  ALA A 233    10927   9233  10372   1698    198  -1593       C  
ATOM   1075  C   ALA A 233      -0.808  29.835  16.870  1.00 78.86           C  
ANISOU 1075  C   ALA A 233    10708   9036  10219   1766    288  -1533       C  
ATOM   1076  O   ALA A 233      -0.772  29.440  15.700  1.00 77.49           O  
ANISOU 1076  O   ALA A 233    10519   8729  10195   1625    340  -1377       O  
ATOM   1077  CB  ALA A 233       0.500  28.505  18.549  1.00 82.37           C  
ANISOU 1077  CB  ALA A 233    11051   9780  10467   1675    300  -1456       C  
ATOM   1078  N   VAL A 234      -1.923  30.317  17.426  1.00 80.80           N  
ANISOU 1078  N   VAL A 234    10937   9445  10320   1993    303  -1663       N  
ATOM   1079  CA  VAL A 234      -3.175  30.358  16.673  1.00 80.04           C  
ANISOU 1079  CA  VAL A 234    10788   9381  10241   2076    384  -1609       C  
ATOM   1080  C   VAL A 234      -3.034  31.256  15.451  1.00 78.34           C  
ANISOU 1080  C   VAL A 234    10707   8812  10248   2026    289  -1635       C  
ATOM   1081  O   VAL A 234      -3.389  30.871  14.330  1.00 77.25           O  
ANISOU 1081  O   VAL A 234    10531   8600  10219   1924    358  -1476       O  
ATOM   1082  CB  VAL A 234      -4.335  30.815  17.575  1.00 81.43           C  
ANISOU 1082  CB  VAL A 234    10907   9832  10203   2360    406  -1773       C  
ATOM   1083  CG1 VAL A 234      -5.525  31.246  16.729  1.00 80.11           C  
ANISOU 1083  CG1 VAL A 234    10715   9636  10086   2480    436  -1775       C  
ATOM   1084  CG2 VAL A 234      -4.737  29.698  18.524  1.00 83.28           C  
ANISOU 1084  CG2 VAL A 234    10962  10472  10208   2365    543  -1655       C  
ATOM   1085  N   VAL A 235      -2.509  32.468  15.646  1.00 78.29           N  
ANISOU 1085  N   VAL A 235    10864   8576  10306   2086    116  -1830       N  
ATOM   1086  CA  VAL A 235      -2.372  33.382  14.517  1.00 76.70           C  
ANISOU 1086  CA  VAL A 235    10804   8026  10311   2024      4  -1834       C  
ATOM   1087  C   VAL A 235      -1.218  32.960  13.618  1.00 75.84           C  
ANISOU 1087  C   VAL A 235    10704   7741  10370   1723      6  -1652       C  
ATOM   1088  O   VAL A 235      -1.275  33.161  12.400  1.00 75.23           O  
ANISOU 1088  O   VAL A 235    10665   7480  10440   1616      1  -1540       O  
ATOM   1089  CB  VAL A 235      -2.221  34.837  15.004  1.00 77.47           C  
ANISOU 1089  CB  VAL A 235    11094   7906  10434   2177   -210  -2094       C  
ATOM   1090  CG1 VAL A 235      -1.956  35.768  13.830  1.00 76.72           C  
ANISOU 1090  CG1 VAL A 235    11162   7423  10566   2067   -350  -2059       C  
ATOM   1091  CG2 VAL A 235      -3.442  35.288  15.800  1.00 79.63           C  
ANISOU 1091  CG2 VAL A 235    11351   8374  10531   2522   -210  -2298       C  
ATOM   1092  N   ALA A 236      -0.166  32.357  14.182  1.00 75.12           N  
ANISOU 1092  N   ALA A 236    10567   7727  10248   1592     15  -1616       N  
ATOM   1093  CA  ALA A 236       0.919  31.850  13.347  1.00 74.58           C  
ANISOU 1093  CA  ALA A 236    10471   7550  10315   1332     34  -1448       C  
ATOM   1094  C   ALA A 236       0.401  30.803  12.373  1.00 73.43           C  
ANISOU 1094  C   ALA A 236    10212   7489  10198   1261    196  -1244       C  
ATOM   1095  O   ALA A 236       0.834  30.748  11.216  1.00 72.15           O  
ANISOU 1095  O   ALA A 236    10059   7187  10170   1099    205  -1124       O  
ATOM   1096  CB  ALA A 236       2.035  31.271  14.217  1.00 76.61           C  
ANISOU 1096  CB  ALA A 236    10672   7925  10512   1247     22  -1449       C  
ATOM   1097  N   PHE A 237      -0.537  29.969  12.828  1.00 74.85           N  
ANISOU 1097  N   PHE A 237    10285   7912  10243   1373    319  -1202       N  
ATOM   1098  CA  PHE A 237      -1.227  29.051  11.930  1.00 73.87           C  
ANISOU 1098  CA  PHE A 237    10070   7856  10143   1317    450  -1028       C  
ATOM   1099  C   PHE A 237      -2.201  29.794  11.024  1.00 72.43           C  
ANISOU 1099  C   PHE A 237     9935   7561  10026   1389    434  -1040       C  
ATOM   1100  O   PHE A 237      -2.337  29.456   9.842  1.00 70.81           O  
ANISOU 1100  O   PHE A 237     9711   7279   9913   1280    482   -908       O  
ATOM   1101  CB  PHE A 237      -1.968  27.988  12.743  1.00 75.32           C  
ANISOU 1101  CB  PHE A 237    10124   8332  10160   1390    564   -964       C  
ATOM   1102  CG  PHE A 237      -1.113  26.825  13.154  1.00 76.17           C  
ANISOU 1102  CG  PHE A 237    10171   8529  10241   1269    604   -853       C  
ATOM   1103  CD1 PHE A 237      -0.764  25.851  12.237  1.00 74.80           C  
ANISOU 1103  CD1 PHE A 237     9961   8296  10164   1118    661   -692       C  
ATOM   1104  CD2 PHE A 237      -0.666  26.700  14.459  1.00 77.96           C  
ANISOU 1104  CD2 PHE A 237    10382   8902  10339   1324    574   -918       C  
ATOM   1105  CE1 PHE A 237       0.020  24.777  12.612  1.00 76.23           C  
ANISOU 1105  CE1 PHE A 237    10097   8540  10327   1036    679   -601       C  
ATOM   1106  CE2 PHE A 237       0.118  25.629  14.840  1.00 79.29           C  
ANISOU 1106  CE2 PHE A 237    10499   9143  10485   1227    595   -807       C  
ATOM   1107  CZ  PHE A 237       0.462  24.668  13.915  1.00 78.21           C  
ANISOU 1107  CZ  PHE A 237    10333   8925  10459   1090    643   -650       C  
ATOM   1108  N   CYS A 238      -2.882  30.812  11.560  1.00 76.79           N  
ANISOU 1108  N   CYS A 238    10549   8105  10522   1590    358  -1207       N  
ATOM   1109  CA  CYS A 238      -3.961  31.466  10.824  1.00 76.06           C  
ANISOU 1109  CA  CYS A 238    10486   7942  10470   1707    340  -1224       C  
ATOM   1110  C   CYS A 238      -3.453  32.081   9.524  1.00 74.45           C  
ANISOU 1110  C   CYS A 238    10397   7436  10453   1559    258  -1154       C  
ATOM   1111  O   CYS A 238      -3.943  31.754   8.438  1.00 74.08           O  
ANISOU 1111  O   CYS A 238    10311   7375  10463   1494    319  -1019       O  
ATOM   1112  CB  CYS A 238      -4.627  32.525  11.708  1.00 77.00           C  
ANISOU 1112  CB  CYS A 238    10668   8089  10497   1980    246  -1451       C  
ATOM   1113  SG  CYS A 238      -5.629  33.756  10.831  1.00 76.58           S  
ANISOU 1113  SG  CYS A 238    10723   7836  10539   2154    139  -1524       S  
ATOM   1114  N   LEU A 239      -2.419  32.919   9.657  1.00 71.37           N  
ANISOU 1114  N   LEU A 239    10142   6827  10150   1483    116  -1232       N  
ATOM   1115  CA  LEU A 239      -1.838  33.644   8.498  1.00 70.69           C  
ANISOU 1115  CA  LEU A 239    10172   6456  10233   1317     15  -1153       C  
ATOM   1116  C   LEU A 239      -1.116  32.670   7.579  1.00 70.30           C  
ANISOU 1116  C   LEU A 239    10026   6450  10234   1076    124   -954       C  
ATOM   1117  O   LEU A 239      -1.132  32.882   6.366  1.00 69.71           O  
ANISOU 1117  O   LEU A 239     9981   6255  10251    966    117   -835       O  
ATOM   1118  CB  LEU A 239      -0.833  34.651   9.054  1.00 72.21           C  
ANISOU 1118  CB  LEU A 239    10510   6440  10487   1264   -168  -1277       C  
ATOM   1119  CG  LEU A 239      -1.376  35.615  10.105  1.00 73.38           C  
ANISOU 1119  CG  LEU A 239    10773   6534  10574   1518   -303  -1520       C  
ATOM   1120  CD1 LEU A 239      -0.244  36.391  10.759  1.00 74.90           C  
ANISOU 1120  CD1 LEU A 239    11098   6544  10817   1430   -484  -1642       C  
ATOM   1121  CD2 LEU A 239      -2.395  36.564   9.495  1.00 71.50           C  
ANISOU 1121  CD2 LEU A 239    10649   6120  10398   1680   -398  -1565       C  
ATOM   1122  N   MET A 240      -0.450  31.680   8.152  1.00 70.81           N  
ANISOU 1122  N   MET A 240     9987   6679  10237   1007    209   -927       N  
ATOM   1123  CA  MET A 240       0.207  30.663   7.337  1.00 69.67           C  
ANISOU 1123  CA  MET A 240     9747   6595  10128    824    311   -765       C  
ATOM   1124  C   MET A 240      -0.791  30.036   6.375  1.00 68.37           C  
ANISOU 1124  C   MET A 240     9523   6497   9959    840    418   -652       C  
ATOM   1125  O   MET A 240      -0.487  29.836   5.193  1.00 67.72           O  
ANISOU 1125  O   MET A 240     9429   6359   9943    703    447   -536       O  
ATOM   1126  CB  MET A 240       0.857  29.608   8.243  1.00 70.65           C  
ANISOU 1126  CB  MET A 240     9773   6898  10174    806    377   -766       C  
ATOM   1127  CG  MET A 240       1.590  28.424   7.577  1.00 69.44           C  
ANISOU 1127  CG  MET A 240     9519   6819  10044    663    472   -630       C  
ATOM   1128  SD  MET A 240       0.664  27.260   6.554  1.00 68.13           S  
ANISOU 1128  SD  MET A 240     9278   6740   9869    657    607   -493       S  
ATOM   1129  CE  MET A 240      -0.480  26.574   7.766  1.00 68.83           C  
ANISOU 1129  CE  MET A 240     9310   7019   9822    817    665   -519       C  
ATOM   1130  N   TRP A 241      -2.001  29.747   6.861  1.00 66.08           N  
ANISOU 1130  N   TRP A 241     9185   6346   9578   1004    473   -685       N  
ATOM   1131  CA  TRP A 241      -3.050  29.225   5.996  1.00 65.60           C  
ANISOU 1131  CA  TRP A 241     9062   6355   9510   1018    555   -584       C  
ATOM   1132  C   TRP A 241      -3.463  30.244   4.939  1.00 64.91           C  
ANISOU 1132  C   TRP A 241     9064   6090   9508   1024    479   -566       C  
ATOM   1133  O   TRP A 241      -3.778  29.861   3.808  1.00 64.23           O  
ANISOU 1133  O   TRP A 241     8948   6003   9454    944    526   -450       O  
ATOM   1134  CB  TRP A 241      -4.256  28.804   6.839  1.00 66.59           C  
ANISOU 1134  CB  TRP A 241     9096   6698   9508   1183    619   -620       C  
ATOM   1135  CG  TRP A 241      -4.288  27.334   7.176  1.00 66.66           C  
ANISOU 1135  CG  TRP A 241     8986   6896   9444   1113    729   -519       C  
ATOM   1136  CD1 TRP A 241      -3.922  26.754   8.359  1.00 67.73           C  
ANISOU 1136  CD1 TRP A 241     9076   7169   9488   1131    754   -541       C  
ATOM   1137  CD2 TRP A 241      -4.727  26.265   6.326  1.00 65.84           C  
ANISOU 1137  CD2 TRP A 241     8811   6849   9354   1011    808   -377       C  
ATOM   1138  NE1 TRP A 241      -4.100  25.391   8.294  1.00 68.07           N  
ANISOU 1138  NE1 TRP A 241     9032   7334   9498   1041    837   -407       N  
ATOM   1139  CE2 TRP A 241      -4.594  25.066   7.057  1.00 66.25           C  
ANISOU 1139  CE2 TRP A 241     8788   7048   9335    967    867   -315       C  
ATOM   1140  CE3 TRP A 241      -5.219  26.206   5.018  1.00 65.62           C  
ANISOU 1140  CE3 TRP A 241     8784   6758   9389    952    821   -298       C  
ATOM   1141  CZ2 TRP A 241      -4.932  23.824   6.522  1.00 66.91           C  
ANISOU 1141  CZ2 TRP A 241     8813   7186   9424    862    924   -183       C  
ATOM   1142  CZ3 TRP A 241      -5.557  24.970   4.490  1.00 64.67           C  
ANISOU 1142  CZ3 TRP A 241     8595   6717   9261    853    887   -182       C  
ATOM   1143  CH2 TRP A 241      -5.410  23.798   5.240  1.00 65.88           C  
ANISOU 1143  CH2 TRP A 241     8688   6985   9357    808    931   -128       C  
ATOM   1144  N   THR A 242      -3.458  31.539   5.278  1.00 67.26           N  
ANISOU 1144  N   THR A 242     9485   6228   9844   1119    345   -681       N  
ATOM   1145  CA  THR A 242      -3.836  32.560   4.301  1.00 67.27           C  
ANISOU 1145  CA  THR A 242     9594   6030   9934   1128    245   -650       C  
ATOM   1146  C   THR A 242      -2.786  32.698   3.205  1.00 66.99           C  
ANISOU 1146  C   THR A 242     9606   5847   9998    883    215   -517       C  
ATOM   1147  O   THR A 242      -3.122  32.748   2.016  1.00 67.14           O  
ANISOU 1147  O   THR A 242     9632   5824  10054    818    225   -397       O  
ATOM   1148  CB  THR A 242      -4.055  33.912   4.981  1.00 68.01           C  
ANISOU 1148  CB  THR A 242     9833   5955  10053   1299     79   -816       C  
ATOM   1149  OG1 THR A 242      -2.788  34.535   5.223  1.00 68.58           O  
ANISOU 1149  OG1 THR A 242    10017   5838  10202   1159    -38   -850       O  
ATOM   1150  CG2 THR A 242      -4.803  33.752   6.287  1.00 68.92           C  
ANISOU 1150  CG2 THR A 242     9883   6267  10037   1539    115   -976       C  
ATOM   1151  N   ILE A 243      -1.509  32.788   3.589  1.00 65.97           N  
ANISOU 1151  N   ILE A 243     9501   5664   9901    746    176   -533       N  
ATOM   1152  CA  ILE A 243      -0.439  32.861   2.597  1.00 65.23           C  
ANISOU 1152  CA  ILE A 243     9414   5494   9878    504    163   -398       C  
ATOM   1153  C   ILE A 243      -0.489  31.643   1.686  1.00 64.29           C  
ANISOU 1153  C   ILE A 243     9163   5547   9716    423    319   -274       C  
ATOM   1154  O   ILE A 243      -0.210  31.730   0.483  1.00 64.51           O  
ANISOU 1154  O   ILE A 243     9192   5545   9775    282    326   -147       O  
ATOM   1155  CB  ILE A 243       0.928  32.997   3.295  1.00 66.56           C  
ANISOU 1155  CB  ILE A 243     9583   5639  10067    379    109   -443       C  
ATOM   1156  CG1 ILE A 243       1.090  34.392   3.900  1.00 67.49           C  
ANISOU 1156  CG1 ILE A 243     9869   5522  10252    408    -90   -551       C  
ATOM   1157  CG2 ILE A 243       2.068  32.704   2.328  1.00 66.94           C  
ANISOU 1157  CG2 ILE A 243     9563   5724  10149    134    147   -295       C  
ATOM   1158  CD1 ILE A 243       1.961  34.414   5.139  1.00 69.40           C  
ANISOU 1158  CD1 ILE A 243    10107   5792  10472    398   -144   -675       C  
ATOM   1159  N   ALA A 244      -0.874  30.494   2.242  1.00 64.96           N  
ANISOU 1159  N   ALA A 244     9142   5817   9723    510    434   -306       N  
ATOM   1160  CA  ALA A 244      -1.032  29.281   1.450  1.00 64.21           C  
ANISOU 1160  CA  ALA A 244     8945   5862   9592    454    559   -211       C  
ATOM   1161  C   ALA A 244      -2.065  29.473   0.343  1.00 64.65           C  
ANISOU 1161  C   ALA A 244     9019   5894   9653    474    564   -135       C  
ATOM   1162  O   ALA A 244      -1.788  29.220  -0.834  1.00 64.54           O  
ANISOU 1162  O   ALA A 244     8985   5891   9645    355    596    -35       O  
ATOM   1163  CB  ALA A 244      -1.423  28.119   2.364  1.00 63.51           C  
ANISOU 1163  CB  ALA A 244     8767   5937   9427    546    646   -252       C  
ATOM   1164  N   ILE A 245      -3.267  29.935   0.707  1.00 65.90           N  
ANISOU 1164  N   ILE A 245     9204   6040   9794    637    529   -186       N  
ATOM   1165  CA  ILE A 245      -4.344  30.040  -0.275  1.00 66.24           C  
ANISOU 1165  CA  ILE A 245     9244   6090   9833    676    531   -116       C  
ATOM   1166  C   ILE A 245      -4.067  31.156  -1.273  1.00 66.48           C  
ANISOU 1166  C   ILE A 245     9387   5937   9935    595    426    -42       C  
ATOM   1167  O   ILE A 245      -4.537  31.103  -2.416  1.00 67.34           O  
ANISOU 1167  O   ILE A 245     9489   6058  10038    552    436     60       O  
ATOM   1168  CB  ILE A 245      -5.711  30.226   0.422  1.00 66.88           C  
ANISOU 1168  CB  ILE A 245     9295   6249   9867    889    522   -193       C  
ATOM   1169  CG1 ILE A 245      -6.116  28.986   1.233  1.00 65.10           C  
ANISOU 1169  CG1 ILE A 245     8939   6243   9554    927    634   -212       C  
ATOM   1170  CG2 ILE A 245      -6.785  30.599  -0.589  1.00 68.18           C  
ANISOU 1170  CG2 ILE A 245     9466   6401  10040    943    490   -125       C  
ATOM   1171  CD1 ILE A 245      -7.316  29.198   2.152  1.00 66.45           C  
ANISOU 1171  CD1 ILE A 245     9049   6549   9649   1133    636   -293       C  
ATOM   1172  N   VAL A 246      -3.309  32.180  -0.870  1.00 66.62           N  
ANISOU 1172  N   VAL A 246     9514   5783  10018    560    313    -80       N  
ATOM   1173  CA  VAL A 246      -2.980  33.267  -1.788  1.00 67.87           C  
ANISOU 1173  CA  VAL A 246     9790   5748  10248    449    193     19       C  
ATOM   1174  C   VAL A 246      -2.138  32.741  -2.942  1.00 68.48           C  
ANISOU 1174  C   VAL A 246     9805   5909  10307    224    267    168       C  
ATOM   1175  O   VAL A 246      -2.373  33.072  -4.111  1.00 69.67           O  
ANISOU 1175  O   VAL A 246     9987   6026  10458    149    239    296       O  
ATOM   1176  CB  VAL A 246      -2.268  34.407  -1.038  1.00 68.80           C  
ANISOU 1176  CB  VAL A 246    10043   5652  10445    428     37    -53       C  
ATOM   1177  CG1 VAL A 246      -1.236  35.078  -1.937  1.00 69.28           C  
ANISOU 1177  CG1 VAL A 246    10173   5580  10570    177    -46     98       C  
ATOM   1178  CG2 VAL A 246      -3.285  35.422  -0.545  1.00 67.93           C  
ANISOU 1178  CG2 VAL A 246    10059   5380  10372    655   -101   -162       C  
ATOM   1179  N   ILE A 247      -1.148  31.902  -2.628  1.00 66.00           N  
ANISOU 1179  N   ILE A 247     9394   5722   9961    129    359    149       N  
ATOM   1180  CA  ILE A 247      -0.350  31.260  -3.668  1.00 67.09           C  
ANISOU 1180  CA  ILE A 247     9444   5991  10056    -43    446    259       C  
ATOM   1181  C   ILE A 247      -1.251  30.456  -4.598  1.00 65.99           C  
ANISOU 1181  C   ILE A 247     9248   5974   9851      4    533    306       C  
ATOM   1182  O   ILE A 247      -1.033  30.407  -5.816  1.00 67.55           O  
ANISOU 1182  O   ILE A 247     9426   6231  10009   -112    556    418       O  
ATOM   1183  CB  ILE A 247       0.744  30.387  -3.022  1.00 67.57           C  
ANISOU 1183  CB  ILE A 247     9400   6181  10091    -90    526    198       C  
ATOM   1184  CG1 ILE A 247       1.917  31.255  -2.558  1.00 68.26           C  
ANISOU 1184  CG1 ILE A 247     9524   6177  10236   -220    432    203       C  
ATOM   1185  CG2 ILE A 247       1.223  29.307  -3.978  1.00 67.22           C  
ANISOU 1185  CG2 ILE A 247     9239   6326   9974   -168    646    255       C  
ATOM   1186  CD1 ILE A 247       2.455  30.882  -1.189  1.00 67.22           C  
ANISOU 1186  CD1 ILE A 247     9355   6079  10108   -157    437     74       C  
ATOM   1187  N   ALA A 248      -2.301  29.846  -4.043  1.00 66.94           N  
ANISOU 1187  N   ALA A 248     9337   6147   9948    164    573    227       N  
ATOM   1188  CA  ALA A 248      -3.204  29.012  -4.826  1.00 66.51           C  
ANISOU 1188  CA  ALA A 248     9225   6210   9835    198    641    263       C  
ATOM   1189  C   ALA A 248      -4.112  29.817  -5.744  1.00 67.56           C  
ANISOU 1189  C   ALA A 248     9420   6275   9973    221    567    348       C  
ATOM   1190  O   ALA A 248      -4.625  29.266  -6.724  1.00 68.09           O  
ANISOU 1190  O   ALA A 248     9446   6441   9986    196    607    406       O  
ATOM   1191  CB  ALA A 248      -4.060  28.164  -3.895  1.00 66.14           C  
ANISOU 1191  CB  ALA A 248     9116   6251   9764    333    692    177       C  
ATOM   1192  N   VAL A 249      -4.334  31.098  -5.444  1.00 68.31           N  
ANISOU 1192  N   VAL A 249     9623   6198  10133    277    446    348       N  
ATOM   1193  CA  VAL A 249      -5.282  31.919  -6.188  1.00 69.71           C  
ANISOU 1193  CA  VAL A 249     9871   6291  10326    338    352    422       C  
ATOM   1194  C   VAL A 249      -4.609  32.740  -7.280  1.00 70.67           C  
ANISOU 1194  C   VAL A 249    10078   6308  10464    166    274    576       C  
ATOM   1195  O   VAL A 249      -5.297  33.461  -8.018  1.00 72.13           O  
ANISOU 1195  O   VAL A 249    10336   6410  10660    196    180    667       O  
ATOM   1196  CB  VAL A 249      -6.076  32.829  -5.226  1.00 69.07           C  
ANISOU 1196  CB  VAL A 249     9866   6075  10301    545    244    321       C  
ATOM   1197  CG1 VAL A 249      -5.311  34.117  -4.940  1.00 69.31           C  
ANISOU 1197  CG1 VAL A 249    10052   5859  10423    497     96    325       C  
ATOM   1198  CG2 VAL A 249      -7.473  33.110  -5.766  1.00 70.09           C  
ANISOU 1198  CG2 VAL A 249     9993   6224  10414    693    195    352       C  
ATOM   1199  N   LEU A 250      -3.281  32.639  -7.420  1.00 69.00           N  
ANISOU 1199  N   LEU A 250     9847   6122  10247    -19    309    621       N  
ATOM   1200  CA  LEU A 250      -2.590  33.439  -8.431  1.00 70.46           C  
ANISOU 1200  CA  LEU A 250    10095   6243  10433   -215    237    794       C  
ATOM   1201  C   LEU A 250      -2.986  33.056  -9.854  1.00 71.74           C  
ANISOU 1201  C   LEU A 250    10211   6552  10495   -276    286    920       C  
ATOM   1202  O   LEU A 250      -3.272  33.966 -10.653  1.00 72.91           O  
ANISOU 1202  O   LEU A 250    10453   6597  10651   -331    176   1065       O  
ATOM   1203  CB  LEU A 250      -1.076  33.357  -8.215  1.00 71.21           C  
ANISOU 1203  CB  LEU A 250    10140   6389  10529   -401    274    813       C  
ATOM   1204  CG  LEU A 250      -0.497  33.986  -6.944  1.00 70.80           C  
ANISOU 1204  CG  LEU A 250    10155   6169  10576   -393    185    719       C  
ATOM   1205  CD1 LEU A 250       0.904  34.516  -7.201  1.00 72.75           C  
ANISOU 1205  CD1 LEU A 250    10395   6408  10838   -649    142    836       C  
ATOM   1206  CD2 LEU A 250      -1.388  35.102  -6.413  1.00 70.06           C  
ANISOU 1206  CD2 LEU A 250    10230   5811  10580   -246     17    673       C  
ATOM   1207  N   PRO A 251      -3.026  31.772 -10.247  1.00 72.30           N  
ANISOU 1207  N   PRO A 251    10154   6849  10467   -268    429    874       N  
ATOM   1208  CA  PRO A 251      -3.481  31.461 -11.615  1.00 73.86           C  
ANISOU 1208  CA  PRO A 251    10321   7184  10559   -313    457    976       C  
ATOM   1209  C   PRO A 251      -4.894  31.935 -11.899  1.00 74.43           C  
ANISOU 1209  C   PRO A 251    10458   7172  10650   -181    364   1008       C  
ATOM   1210  O   PRO A 251      -5.171  32.440 -12.995  1.00 76.21           O  
ANISOU 1210  O   PRO A 251    10727   7405  10824   -244    303   1154       O  
ATOM   1211  CB  PRO A 251      -3.376  29.930 -11.676  1.00 73.61           C  
ANISOU 1211  CB  PRO A 251    10163   7364  10444   -283    601    862       C  
ATOM   1212  CG  PRO A 251      -2.344  29.595 -10.675  1.00 71.90           C  
ANISOU 1212  CG  PRO A 251     9903   7146  10271   -302    655    768       C  
ATOM   1213  CD  PRO A 251      -2.578  30.553  -9.549  1.00 70.86           C  
ANISOU 1213  CD  PRO A 251     9863   6801  10262   -230    554    734       C  
ATOM   1214  N   LEU A 252      -5.796  31.774 -10.928  1.00 74.39           N  
ANISOU 1214  N   LEU A 252    10448   7112  10706      6    353    880       N  
ATOM   1215  CA  LEU A 252      -7.166  32.256 -11.073  1.00 74.66           C  
ANISOU 1215  CA  LEU A 252    10518   7090  10759    162    262    895       C  
ATOM   1216  C   LEU A 252      -7.205  33.736 -11.426  1.00 75.83           C  
ANISOU 1216  C   LEU A 252    10818   7022  10972    154     94   1018       C  
ATOM   1217  O   LEU A 252      -8.018  34.165 -12.252  1.00 77.84           O  
ANISOU 1217  O   LEU A 252    11109   7264  11203    199     12   1118       O  
ATOM   1218  CB  LEU A 252      -7.938  32.000  -9.778  1.00 74.16           C  
ANISOU 1218  CB  LEU A 252    10412   7020  10745    360    277    736       C  
ATOM   1219  CG  LEU A 252      -9.461  32.125  -9.808  1.00 74.84           C  
ANISOU 1219  CG  LEU A 252    10463   7149  10823    548    225    717       C  
ATOM   1220  CD1 LEU A 252     -10.038  31.368 -10.988  1.00 76.31           C  
ANISOU 1220  CD1 LEU A 252    10571   7511  10914    485    266    794       C  
ATOM   1221  CD2 LEU A 252     -10.063  31.631  -8.499  1.00 73.97           C  
ANISOU 1221  CD2 LEU A 252    10264   7117  10724    708    280    565       C  
ATOM   1222  N   LEU A 253      -6.332  34.529 -10.813  1.00 75.42           N  
ANISOU 1222  N   LEU A 253    10862   6787  11006     92     23   1019       N  
ATOM   1223  CA  LEU A 253      -6.312  35.970 -11.010  1.00 75.89           C  
ANISOU 1223  CA  LEU A 253    11096   6585  11152     76   -170   1130       C  
ATOM   1224  C   LEU A 253      -5.505  36.403 -12.225  1.00 77.01           C  
ANISOU 1224  C   LEU A 253    11285   6730  11247   -182   -208   1359       C  
ATOM   1225  O   LEU A 253      -5.377  37.609 -12.463  1.00 77.71           O  
ANISOU 1225  O   LEU A 253    11532   6584  11410   -244   -386   1491       O  
ATOM   1226  CB  LEU A 253      -5.762  36.664  -9.763  1.00 75.10           C  
ANISOU 1226  CB  LEU A 253    11095   6269  11171    115   -256   1020       C  
ATOM   1227  CG  LEU A 253      -6.632  36.500  -8.521  1.00 73.69           C  
ANISOU 1227  CG  LEU A 253    10890   6080  11028    393   -249    802       C  
ATOM   1228  CD1 LEU A 253      -5.850  36.867  -7.271  1.00 72.04           C  
ANISOU 1228  CD1 LEU A 253    10743   5734  10897    398   -290    670       C  
ATOM   1229  CD2 LEU A 253      -7.895  37.336  -8.645  1.00 74.14           C  
ANISOU 1229  CD2 LEU A 253    11039   6004  11128    621   -398    795       C  
ATOM   1230  N   GLY A 254      -4.949  35.467 -12.990  1.00 77.75           N  
ANISOU 1230  N   GLY A 254    11246   7083  11212   -333    -57   1412       N  
ATOM   1231  CA  GLY A 254      -4.318  35.837 -14.240  1.00 78.90           C  
ANISOU 1231  CA  GLY A 254    11409   7298  11272   -563    -80   1638       C  
ATOM   1232  C   GLY A 254      -2.953  35.244 -14.518  1.00 79.89           C  
ANISOU 1232  C   GLY A 254    11414   7637  11305   -778     55   1673       C  
ATOM   1233  O   GLY A 254      -2.421  35.428 -15.615  1.00 81.29           O  
ANISOU 1233  O   GLY A 254    11567   7947  11371   -970     64   1861       O  
ATOM   1234  N   TRP A 255      -2.363  34.534 -13.556  1.00 77.50           N  
ANISOU 1234  N   TRP A 255    11024   7391  11030   -744    161   1502       N  
ATOM   1235  CA  TRP A 255      -1.040  33.942 -13.769  1.00 78.31           C  
ANISOU 1235  CA  TRP A 255    10995   7715  11046   -917    287   1517       C  
ATOM   1236  C   TRP A 255      -1.218  32.544 -14.355  1.00 79.36           C  
ANISOU 1236  C   TRP A 255    10984   8134  11034   -848    452   1423       C  
ATOM   1237  O   TRP A 255      -1.127  31.521 -13.672  1.00 77.59           O  
ANISOU 1237  O   TRP A 255    10678   7987  10816   -740    554   1242       O  
ATOM   1238  CB  TRP A 255      -0.231  33.918 -12.479  1.00 77.51           C  
ANISOU 1238  CB  TRP A 255    10876   7530  11045   -918    297   1391       C  
ATOM   1239  CG  TRP A 255       1.211  33.533 -12.693  1.00 79.25           C  
ANISOU 1239  CG  TRP A 255    10957   7969  11185  -1106    398   1432       C  
ATOM   1240  CD1 TRP A 255       1.782  33.090 -13.855  1.00 81.27           C  
ANISOU 1240  CD1 TRP A 255    11091   8512  11277  -1236    499   1537       C  
ATOM   1241  CD2 TRP A 255       2.262  33.569 -11.722  1.00 79.36           C  
ANISOU 1241  CD2 TRP A 255    10924   7964  11265  -1172    404   1363       C  
ATOM   1242  NE1 TRP A 255       3.118  32.841 -13.662  1.00 82.88           N  
ANISOU 1242  NE1 TRP A 255    11161   8888  11441  -1368    573   1535       N  
ATOM   1243  CE2 TRP A 255       3.439  33.128 -12.361  1.00 81.73           C  
ANISOU 1243  CE2 TRP A 255    11058   8554  11440  -1338    513   1435       C  
ATOM   1244  CE3 TRP A 255       2.323  33.930 -10.373  1.00 77.59           C  
ANISOU 1244  CE3 TRP A 255    10774   7527  11181  -1098    325   1240       C  
ATOM   1245  CZ2 TRP A 255       4.660  33.038 -11.697  1.00 82.09           C  
ANISOU 1245  CZ2 TRP A 255    11002   8680  11507  -1436    542   1397       C  
ATOM   1246  CZ3 TRP A 255       3.535  33.839  -9.717  1.00 78.06           C  
ANISOU 1246  CZ3 TRP A 255    10747   7652  11260  -1205    348   1202       C  
ATOM   1247  CH2 TRP A 255       4.687  33.397 -10.378  1.00 80.24           C  
ANISOU 1247  CH2 TRP A 255    10850   8217  11421  -1375    454   1285       C  
ATOM   1248  N   ASN A 256      -1.447  32.510 -15.664  1.00 78.40           N  
ANISOU 1248  N   ASN A 256    10843   8167  10776   -919    464   1553       N  
ATOM   1249  CA  ASN A 256      -1.647  31.260 -16.381  1.00 80.07           C  
ANISOU 1249  CA  ASN A 256    10943   8642  10839   -860    593   1463       C  
ATOM   1250  C   ASN A 256      -1.375  31.507 -17.859  1.00 82.65           C  
ANISOU 1250  C   ASN A 256    11239   9176  10988  -1013    601   1649       C  
ATOM   1251  O   ASN A 256      -1.283  32.651 -18.310  1.00 82.91           O  
ANISOU 1251  O   ASN A 256    11354   9122  11028  -1152    493   1864       O  
ATOM   1252  CB  ASN A 256      -3.057  30.716 -16.142  1.00 78.96           C  
ANISOU 1252  CB  ASN A 256    10832   8431  10737   -659    574   1340       C  
ATOM   1253  CG  ASN A 256      -4.126  31.738 -16.430  1.00 78.41           C  
ANISOU 1253  CG  ASN A 256    10881   8190  10720   -614    428   1463       C  
ATOM   1254  OD1 ASN A 256      -4.388  32.066 -17.586  1.00 80.15           O  
ANISOU 1254  OD1 ASN A 256    11123   8496  10836   -686    386   1613       O  
ATOM   1255  ND2 ASN A 256      -4.746  32.260 -15.376  1.00 76.60           N  
ANISOU 1255  ND2 ASN A 256    10730   7730  10645   -482    343   1398       N  
ATOM   1256  N   CYS A 257      -1.248  30.413 -18.615  1.00 86.35           N  
ANISOU 1256  N   CYS A 257    11596   9923  11289   -985    719   1564       N  
ATOM   1257  CA  CYS A 257      -0.791  30.528 -19.996  1.00 88.53           C  
ANISOU 1257  CA  CYS A 257    11812  10471  11355  -1129    755   1718       C  
ATOM   1258  C   CYS A 257      -1.841  31.122 -20.925  1.00 89.23           C  
ANISOU 1258  C   CYS A 257    11994  10524  11385  -1138    648   1875       C  
ATOM   1259  O   CYS A 257      -1.485  31.595 -22.008  1.00 90.42           O  
ANISOU 1259  O   CYS A 257    12125  10853  11376  -1293    639   2072       O  
ATOM   1260  CB  CYS A 257      -0.343  29.165 -20.529  1.00 91.43           C  
ANISOU 1260  CB  CYS A 257    12039  11151  11547  -1062    902   1547       C  
ATOM   1261  SG  CYS A 257      -1.569  27.845 -20.415  1.00 91.58           S  
ANISOU 1261  SG  CYS A 257    12083  11133  11582   -831    914   1300       S  
ATOM   1262  N   GLU A 258      -3.118  31.116 -20.538  1.00 89.59           N  
ANISOU 1262  N   GLU A 258    12128  10369  11544   -978    566   1804       N  
ATOM   1263  CA  GLU A 258      -4.147  31.665 -21.417  1.00 90.02           C  
ANISOU 1263  CA  GLU A 258    12260  10400  11542   -967    454   1949       C  
ATOM   1264  C   GLU A 258      -4.221  33.187 -21.317  1.00 89.11           C  
ANISOU 1264  C   GLU A 258    12285  10035  11540  -1055    291   2178       C  
ATOM   1265  O   GLU A 258      -4.133  33.889 -22.329  1.00 90.22           O  
ANISOU 1265  O   GLU A 258    12466  10244  11570  -1195    221   2411       O  
ATOM   1266  CB  GLU A 258      -5.508  31.038 -21.105  1.00 90.05           C  
ANISOU 1266  CB  GLU A 258    12278  10329  11609   -761    424   1789       C  
ATOM   1267  CG  GLU A 258      -5.505  29.520 -21.044  1.00 91.07           C  
ANISOU 1267  CG  GLU A 258    12302  10634  11668   -677    550   1556       C  
ATOM   1268  CD  GLU A 258      -6.897  28.928 -21.185  1.00 91.65           C  
ANISOU 1268  CD  GLU A 258    12376  10703  11743   -541    501   1463       C  
ATOM   1269  OE1 GLU A 258      -7.830  29.669 -21.561  1.00 92.25           O  
ANISOU 1269  OE1 GLU A 258    12512  10707  11833   -510    384   1588       O  
ATOM   1270  OE2 GLU A 258      -7.056  27.717 -20.925  1.00 92.04           O  
ANISOU 1270  OE2 GLU A 258    12366  10822  11782   -470    569   1271       O  
ATOM   1271  N   LYS A 259      -4.398  33.716 -20.102  1.00 90.47           N  
ANISOU 1271  N   LYS A 259    12540   9908  11925   -970    215   2113       N  
ATOM   1272  CA  LYS A 259      -4.425  35.166 -19.923  1.00 89.51           C  
ANISOU 1272  CA  LYS A 259    12578   9502  11931  -1038     33   2302       C  
ATOM   1273  C   LYS A 259      -3.121  35.819 -20.365  1.00 90.27           C  
ANISOU 1273  C   LYS A 259    12674   9657  11968  -1319     24   2517       C  
ATOM   1274  O   LYS A 259      -3.124  36.975 -20.800  1.00 90.45           O  
ANISOU 1274  O   LYS A 259    12826   9520  12019  -1447   -137   2759       O  
ATOM   1275  CB  LYS A 259      -4.700  35.524 -18.461  1.00 87.13           C  
ANISOU 1275  CB  LYS A 259    12356   8898  11852   -885    -35   2149       C  
ATOM   1276  CG  LYS A 259      -6.163  35.504 -18.026  1.00 87.16           C  
ANISOU 1276  CG  LYS A 259    12405   8771  11942   -619   -108   2027       C  
ATOM   1277  CD  LYS A 259      -6.423  34.335 -17.095  1.00 85.85           C  
ANISOU 1277  CD  LYS A 259    12122   8694  11802   -465     30   1764       C  
ATOM   1278  CE  LYS A 259      -7.865  34.260 -16.630  1.00 85.11           C  
ANISOU 1278  CE  LYS A 259    12035   8529  11776   -219    -27   1652       C  
ATOM   1279  NZ  LYS A 259      -7.943  33.605 -15.294  1.00 82.73           N  
ANISOU 1279  NZ  LYS A 259    11667   8209  11557    -89     57   1432       N  
ATOM   1280  N   LEU A 260      -2.004  35.099 -20.258  1.00 88.64           N  
ANISOU 1280  N   LEU A 260    12320   9680  11679  -1421    185   2441       N  
ATOM   1281  CA  LEU A 260      -0.677  35.631 -20.537  1.00 89.35           C  
ANISOU 1281  CA  LEU A 260    12365   9874  11711  -1695    195   2629       C  
ATOM   1282  C   LEU A 260      -0.156  35.289 -21.925  1.00 91.55           C  
ANISOU 1282  C   LEU A 260    12512  10554  11720  -1855    298   2780       C  
ATOM   1283  O   LEU A 260       0.821  35.906 -22.365  1.00 92.07           O  
ANISOU 1283  O   LEU A 260    12538  10736  11708  -2115    286   3005       O  
ATOM   1284  CB  LEU A 260       0.319  35.121 -19.486  1.00 89.12           C  
ANISOU 1284  CB  LEU A 260    12232   9875  11755  -1701    301   2454       C  
ATOM   1285  CG  LEU A 260       0.649  36.063 -18.328  1.00 87.43           C  
ANISOU 1285  CG  LEU A 260    12139   9316  11763  -1751    164   2465       C  
ATOM   1286  CD1 LEU A 260      -0.598  36.763 -17.838  1.00 85.63           C  
ANISOU 1286  CD1 LEU A 260    12112   8718  11705  -1571    -10   2434       C  
ATOM   1287  CD2 LEU A 260       1.279  35.272 -17.185  1.00 85.94           C  
ANISOU 1287  CD2 LEU A 260    11844   9166  11642  -1664    280   2222       C  
ATOM   1288  N   GLN A 261      -0.780  34.340 -22.621  1.00 91.95           N  
ANISOU 1288  N   GLN A 261    12491  10830  11615  -1715    392   2665       N  
ATOM   1289  CA  GLN A 261      -0.255  33.810 -23.878  1.00 94.07           C  
ANISOU 1289  CA  GLN A 261    12615  11529  11598  -1821    514   2739       C  
ATOM   1290  C   GLN A 261       1.194  33.358 -23.708  1.00 94.63           C  
ANISOU 1290  C   GLN A 261    12505  11868  11581  -1937    666   2690       C  
ATOM   1291  O   GLN A 261       2.093  33.743 -24.459  1.00 95.76           O  
ANISOU 1291  O   GLN A 261    12551  12280  11554  -2162    704   2900       O  
ATOM   1292  CB  GLN A 261      -0.392  34.828 -25.012  1.00 94.54           C  
ANISOU 1292  CB  GLN A 261    12745  11643  11532  -2016    399   3080       C  
ATOM   1293  CG  GLN A 261      -1.828  35.135 -25.435  1.00 94.67           C  
ANISOU 1293  CG  GLN A 261    12908  11486  11578  -1881    259   3128       C  
ATOM   1294  CD  GLN A 261      -2.665  33.892 -25.708  1.00 95.92           C  
ANISOU 1294  CD  GLN A 261    12999  11805  11641  -1651    351   2871       C  
ATOM   1295  OE1 GLN A 261      -3.161  33.243 -24.787  1.00 94.65           O  
ANISOU 1295  OE1 GLN A 261    12842  11491  11631  -1453    379   2616       O  
ATOM   1296  NE2 GLN A 261      -2.821  33.555 -26.983  1.00 97.64           N  
ANISOU 1296  NE2 GLN A 261    13155  12343  11600  -1689    389   2944       N  
ATOM   1297  N   SER A 262       1.416  32.538 -22.682  1.00 91.70           N  
ANISOU 1297  N   SER A 262    12080  11436  11325  -1780    750   2420       N  
ATOM   1298  CA  SER A 262       2.695  31.912 -22.408  1.00 93.23           C  
ANISOU 1298  CA  SER A 262    12092  11882  11449  -1821    896   2315       C  
ATOM   1299  C   SER A 262       2.591  30.416 -22.721  1.00 95.21           C  
ANISOU 1299  C   SER A 262    12232  12385  11559  -1610   1040   2041       C  
ATOM   1300  O   SER A 262       1.664  29.979 -23.417  1.00 95.70           O  
ANISOU 1300  O   SER A 262    12341  12493  11528  -1500   1028   1988       O  
ATOM   1301  CB  SER A 262       3.101  32.204 -20.960  1.00 91.78           C  
ANISOU 1301  CB  SER A 262    11948  11412  11511  -1814    851   2235       C  
ATOM   1302  OG  SER A 262       2.030  31.949 -20.071  1.00 89.39           O  
ANISOU 1302  OG  SER A 262    11777  10790  11396  -1596    789   2054       O  
ATOM   1303  N   VAL A 263       3.537  29.632 -22.214  1.00 97.61           N  
ANISOU 1303  N   VAL A 263    12395  12844  11849  -1550   1158   1865       N  
ATOM   1304  CA  VAL A 263       3.580  28.200 -22.491  1.00 99.42           C  
ANISOU 1304  CA  VAL A 263    12529  13296  11950  -1344   1276   1596       C  
ATOM   1305  C   VAL A 263       2.734  27.460 -21.460  1.00 98.49           C  
ANISOU 1305  C   VAL A 263    12519  12866  12036  -1127   1238   1361       C  
ATOM   1306  O   VAL A 263       2.816  27.732 -20.256  1.00 96.39           O  
ANISOU 1306  O   VAL A 263    12302  12341  11980  -1116   1196   1332       O  
ATOM   1307  CB  VAL A 263       5.033  27.687 -22.520  1.00100.67           C  
ANISOU 1307  CB  VAL A 263    12473  13798  11977  -1362   1413   1521       C  
ATOM   1308  CG1 VAL A 263       5.705  27.830 -21.161  1.00100.25           C  
ANISOU 1308  CG1 VAL A 263    12399  13557  12135  -1372   1404   1470       C  
ATOM   1309  CG2 VAL A 263       5.077  26.242 -22.991  1.00102.86           C  
ANISOU 1309  CG2 VAL A 263    12670  14316  12097  -1132   1514   1242       C  
ATOM   1310  N   CYS A 264       1.894  26.544 -21.937  1.00 98.06           N  
ANISOU 1310  N   CYS A 264    12503  12844  11911   -969   1243   1203       N  
ATOM   1311  CA  CYS A 264       1.006  25.782 -21.074  1.00 96.18           C  
ANISOU 1311  CA  CYS A 264    12358  12343  11843   -791   1201   1007       C  
ATOM   1312  C   CYS A 264       1.676  24.494 -20.618  1.00 97.02           C  
ANISOU 1312  C   CYS A 264    12383  12538  11942   -641   1286    755       C  
ATOM   1313  O   CYS A 264       2.509  23.917 -21.322  1.00 99.63           O  
ANISOU 1313  O   CYS A 264    12595  13173  12085   -611   1375    675       O  
ATOM   1314  CB  CYS A 264      -0.306  25.446 -21.787  1.00 97.13           C  
ANISOU 1314  CB  CYS A 264    12565  12433  11908   -719   1137    976       C  
ATOM   1315  SG  CYS A 264      -1.372  26.847 -22.173  1.00 95.58           S  
ANISOU 1315  SG  CYS A 264    12488  12070  11757   -830   1003   1243       S  
ATOM   1316  N   SER A 265       1.301  24.048 -19.424  1.00 94.18           N  
ANISOU 1316  N   SER A 265    12087  11916  11779   -536   1252    632       N  
ATOM   1317  CA  SER A 265       1.798  22.786 -18.903  1.00 94.33           C  
ANISOU 1317  CA  SER A 265    12062  11961  11819   -383   1302    402       C  
ATOM   1318  C   SER A 265       1.101  21.618 -19.589  1.00 96.43           C  
ANISOU 1318  C   SER A 265    12373  12273  11993   -252   1283    229       C  
ATOM   1319  O   SER A 265      -0.066  21.704 -19.983  1.00 96.78           O  
ANISOU 1319  O   SER A 265    12506  12226  12041   -265   1212    267       O  
ATOM   1320  CB  SER A 265       1.585  22.706 -17.392  1.00 91.06           C  
ANISOU 1320  CB  SER A 265    11707  11257  11634   -330   1261    352       C  
ATOM   1321  OG  SER A 265       1.595  21.359 -16.949  1.00 91.70           O  
ANISOU 1321  OG  SER A 265    11798  11294  11749   -172   1267    141       O  
ATOM   1322  N   ASP A 266       1.837  20.519 -19.737  1.00 97.27           N  
ANISOU 1322  N   ASP A 266    12418  12523  12016   -121   1333     30       N  
ATOM   1323  CA  ASP A 266       1.290  19.300 -20.316  1.00 98.20           C  
ANISOU 1323  CA  ASP A 266    12598  12656  12059     16   1293   -170       C  
ATOM   1324  C   ASP A 266       0.643  18.393 -19.280  1.00 94.90           C  
ANISOU 1324  C   ASP A 266    12286  11936  11835    111   1214   -297       C  
ATOM   1325  O   ASP A 266      -0.101  17.480 -19.653  1.00 94.92           O  
ANISOU 1325  O   ASP A 266    12374  11872  11819    182   1140   -428       O  
ATOM   1326  CB  ASP A 266       2.386  18.534 -21.063  1.00100.29           C  
ANISOU 1326  CB  ASP A 266    12756  13225  12123    139   1367   -343       C  
ATOM   1327  CG  ASP A 266       3.069  19.381 -22.120  1.00102.02           C  
ANISOU 1327  CG  ASP A 266    12842  13805  12116     31   1457   -202       C  
ATOM   1328  OD1 ASP A 266       2.397  19.766 -23.102  1.00103.50           O  
ANISOU 1328  OD1 ASP A 266    13063  14089  12173    -46   1432   -111       O  
ATOM   1329  OD2 ASP A 266       4.275  19.667 -21.967  1.00102.13           O  
ANISOU 1329  OD2 ASP A 266    12708  14020  12075     11   1547   -169       O  
ATOM   1330  N   ILE A 267       0.908  18.619 -17.998  1.00 95.02           N  
ANISOU 1330  N   ILE A 267    12299  11776  12028    102   1218   -256       N  
ATOM   1331  CA  ILE A 267       0.236  17.887 -16.932  1.00 91.02           C  
ANISOU 1331  CA  ILE A 267    11887  10996  11700    161   1143   -328       C  
ATOM   1332  C   ILE A 267      -1.046  18.587 -16.510  1.00 88.84           C  
ANISOU 1332  C   ILE A 267    11679  10541  11537     65   1084   -182       C  
ATOM   1333  O   ILE A 267      -2.113  17.970 -16.438  1.00 87.30           O  
ANISOU 1333  O   ILE A 267    11559  10218  11392     79   1006   -223       O  
ATOM   1334  CB  ILE A 267       1.192  17.713 -15.734  1.00 88.47           C  
ANISOU 1334  CB  ILE A 267    11521  10605  11490    217   1175   -366       C  
ATOM   1335  CG1 ILE A 267       2.400  16.854 -16.122  1.00 90.20           C  
ANISOU 1335  CG1 ILE A 267    11666  11005  11601    356   1220   -539       C  
ATOM   1336  CG2 ILE A 267       0.443  17.132 -14.548  1.00 84.15           C  
ANISOU 1336  CG2 ILE A 267    11066   9787  11119    247   1100   -389       C  
ATOM   1337  CD1 ILE A 267       3.143  16.260 -14.942  1.00 87.43           C  
ANISOU 1337  CD1 ILE A 267    11301  10550  11370    457   1213   -620       C  
ATOM   1338  N   PHE A 268      -0.959  19.888 -16.238  1.00 87.27           N  
ANISOU 1338  N   PHE A 268    11450  10334  11376    -32   1110    -13       N  
ATOM   1339  CA  PHE A 268      -2.058  20.648 -15.663  1.00 83.92           C  
ANISOU 1339  CA  PHE A 268    11080   9738  11068    -85   1053    109       C  
ATOM   1340  C   PHE A 268      -2.646  21.582 -16.708  1.00 86.26           C  
ANISOU 1340  C   PHE A 268    11387  10113  11274   -167   1027    249       C  
ATOM   1341  O   PHE A 268      -1.911  22.398 -17.286  1.00 87.97           O  
ANISOU 1341  O   PHE A 268    11562  10458  11405   -245   1065    351       O  
ATOM   1342  CB  PHE A 268      -1.572  21.438 -14.451  1.00 80.17           C  
ANISOU 1342  CB  PHE A 268    10591   9150  10721   -108   1069    178       C  
ATOM   1343  CG  PHE A 268      -0.903  20.590 -13.407  1.00 78.35           C  
ANISOU 1343  CG  PHE A 268    10343   8859  10568    -29   1091     60       C  
ATOM   1344  CD1 PHE A 268      -1.590  19.562 -12.782  1.00 75.31           C  
ANISOU 1344  CD1 PHE A 268    10007   8351  10256     40   1047    -27       C  
ATOM   1345  CD2 PHE A 268       0.421  20.809 -13.065  1.00 79.68           C  
ANISOU 1345  CD2 PHE A 268    10439   9103  10730    -35   1146     49       C  
ATOM   1346  CE1 PHE A 268      -0.973  18.779 -11.821  1.00 73.44           C  
ANISOU 1346  CE1 PHE A 268     9765   8051  10088    110   1052   -116       C  
ATOM   1347  CE2 PHE A 268       1.045  20.029 -12.109  1.00 77.57           C  
ANISOU 1347  CE2 PHE A 268    10155   8787  10531     49   1155    -55       C  
ATOM   1348  CZ  PHE A 268       0.346  19.012 -11.487  1.00 74.16           C  
ANISOU 1348  CZ  PHE A 268     9788   8215  10172    126   1106   -135       C  
ATOM   1349  N   PRO A 269      -3.942  21.489 -16.996  1.00 84.65           N  
ANISOU 1349  N   PRO A 269    11232   9852  11079   -162    955    270       N  
ATOM   1350  CA  PRO A 269      -4.552  22.415 -17.956  1.00 86.87           C  
ANISOU 1350  CA  PRO A 269    11527  10200  11278   -228    914    414       C  
ATOM   1351  C   PRO A 269      -4.463  23.862 -17.485  1.00 84.34           C  
ANISOU 1351  C   PRO A 269    11224   9779  11042   -284    896    583       C  
ATOM   1352  O   PRO A 269      -4.543  24.154 -16.290  1.00 80.78           O  
ANISOU 1352  O   PRO A 269    10789   9165  10739   -250    885    578       O  
ATOM   1353  CB  PRO A 269      -6.006  21.937 -18.032  1.00 86.58           C  
ANISOU 1353  CB  PRO A 269    11525  10100  11273   -195    831    387       C  
ATOM   1354  CG  PRO A 269      -5.940  20.490 -17.675  1.00 86.31           C  
ANISOU 1354  CG  PRO A 269    11497  10035  11261   -139    833    209       C  
ATOM   1355  CD  PRO A 269      -4.826  20.357 -16.672  1.00 83.62           C  
ANISOU 1355  CD  PRO A 269    11137   9633  11003   -106    901    156       C  
ATOM   1356  N   HIS A 270      -4.265  24.763 -18.452  1.00 85.96           N  
ANISOU 1356  N   HIS A 270    11433  10084  11145   -372    883    732       N  
ATOM   1357  CA  HIS A 270      -4.308  26.214 -18.270  1.00 84.59           C  
ANISOU 1357  CA  HIS A 270    11308   9793  11041   -440    824    916       C  
ATOM   1358  C   HIS A 270      -3.147  26.771 -17.452  1.00 82.98           C  
ANISOU 1358  C   HIS A 270    11090   9520  10919   -499    859    945       C  
ATOM   1359  O   HIS A 270      -2.928  27.985 -17.448  1.00 82.41           O  
ANISOU 1359  O   HIS A 270    11065   9359  10887   -589    800   1104       O  
ATOM   1360  CB  HIS A 270      -5.631  26.643 -17.623  1.00 82.35           C  
ANISOU 1360  CB  HIS A 270    11084   9315  10891   -352    730    936       C  
ATOM   1361  CG  HIS A 270      -6.830  25.918 -18.151  1.00 83.66           C  
ANISOU 1361  CG  HIS A 270    11239   9544  11004   -290    692    881       C  
ATOM   1362  ND1 HIS A 270      -7.069  25.757 -19.498  1.00 87.12           N  
ANISOU 1362  ND1 HIS A 270    11671  10152  11279   -336    674    927       N  
ATOM   1363  CD2 HIS A 270      -7.865  25.322 -17.512  1.00 82.43           C  
ANISOU 1363  CD2 HIS A 270    11070   9323  10928   -200    663    792       C  
ATOM   1364  CE1 HIS A 270      -8.195  25.087 -19.667  1.00 88.37           C  
ANISOU 1364  CE1 HIS A 270    11819  10329  11430   -277    625    859       C  
ATOM   1365  NE2 HIS A 270      -8.698  24.811 -18.477  1.00 85.72           N  
ANISOU 1365  NE2 HIS A 270    11472   9856  11242   -203    619    785       N  
ATOM   1366  N   ILE A 271      -2.392  25.917 -16.770  1.00 82.66           N  
ANISOU 1366  N   ILE A 271    10992   9511  10906   -455    937    799       N  
ATOM   1367  CA  ILE A 271      -1.366  26.385 -15.843  1.00 81.54           C  
ANISOU 1367  CA  ILE A 271    10829   9298  10855   -500    958    810       C  
ATOM   1368  C   ILE A 271      -0.130  26.820 -16.618  1.00 83.88           C  
ANISOU 1368  C   ILE A 271    11049   9792  11028   -646   1008    917       C  
ATOM   1369  O   ILE A 271       0.337  26.113 -17.520  1.00 87.22           O  
ANISOU 1369  O   ILE A 271    11390  10461  11287   -648   1083    871       O  
ATOM   1370  CB  ILE A 271      -1.027  25.295 -14.813  1.00 79.98           C  
ANISOU 1370  CB  ILE A 271    10591   9072  10726   -393   1013    625       C  
ATOM   1371  CG1 ILE A 271      -2.033  25.332 -13.665  1.00 75.34           C  
ANISOU 1371  CG1 ILE A 271    10069   8269  10287   -298    955    579       C  
ATOM   1372  CG2 ILE A 271       0.384  25.471 -14.276  1.00 80.32           C  
ANISOU 1372  CG2 ILE A 271    10564   9167  10787   -451   1062    619       C  
ATOM   1373  CD1 ILE A 271      -1.903  26.559 -12.792  1.00 73.94           C  
ANISOU 1373  CD1 ILE A 271     9944   7921  10228   -328    895    657       C  
ATOM   1374  N   ASP A 272       0.401  27.990 -16.269  1.00 82.62           N  
ANISOU 1374  N   ASP A 272    10916   9536  10939   -771    958   1061       N  
ATOM   1375  CA  ASP A 272       1.643  28.468 -16.858  1.00 85.93           C  
ANISOU 1375  CA  ASP A 272    11245  10151  11254   -947    999   1190       C  
ATOM   1376  C   ASP A 272       2.829  27.687 -16.302  1.00 86.09           C  
ANISOU 1376  C   ASP A 272    11132  10318  11258   -917   1099   1053       C  
ATOM   1377  O   ASP A 272       2.914  27.433 -15.097  1.00 84.30           O  
ANISOU 1377  O   ASP A 272    10924   9934  11172   -833   1089    937       O  
ATOM   1378  CB  ASP A 272       1.817  29.961 -16.575  1.00 85.01           C  
ANISOU 1378  CB  ASP A 272    11215   9844  11241  -1109    883   1390       C  
ATOM   1379  CG  ASP A 272       2.782  30.635 -17.530  1.00 87.10           C  
ANISOU 1379  CG  ASP A 272    11403  10321  11369  -1343    896   1606       C  
ATOM   1380  OD1 ASP A 272       3.686  29.955 -18.057  1.00 89.63           O  
ANISOU 1380  OD1 ASP A 272    11561  10964  11531  -1375   1019   1568       O  
ATOM   1381  OD2 ASP A 272       2.640  31.856 -17.747  1.00 87.04           O  
ANISOU 1381  OD2 ASP A 272    11498  10162  11411  -1494    773   1818       O  
ATOM   1382  N   LYS A 273       3.755  27.314 -17.191  1.00 89.01           N  
ANISOU 1382  N   LYS A 273    11360  11015  11445   -978   1195   1069       N  
ATOM   1383  CA  LYS A 273       4.944  26.589 -16.753  1.00 91.12           C  
ANISOU 1383  CA  LYS A 273    11479  11459  11682   -932   1287    940       C  
ATOM   1384  C   LYS A 273       5.805  27.429 -15.819  1.00 89.72           C  
ANISOU 1384  C   LYS A 273    11272  11191  11627  -1067   1248   1029       C  
ATOM   1385  O   LYS A 273       6.500  26.878 -14.957  1.00 89.97           O  
ANISOU 1385  O   LYS A 273    11229  11241  11716   -990   1285    897       O  
ATOM   1386  CB  LYS A 273       5.766  26.137 -17.960  1.00 94.27           C  
ANISOU 1386  CB  LYS A 273    11711  12270  11836   -960   1396    944       C  
ATOM   1387  CG  LYS A 273       5.131  25.019 -18.771  1.00 96.27           C  
ANISOU 1387  CG  LYS A 273    11980  12640  11958   -784   1438    780       C  
ATOM   1388  CD  LYS A 273       6.180  24.041 -19.282  1.00 98.67           C  
ANISOU 1388  CD  LYS A 273    12107  13305  12078   -678   1554    625       C  
ATOM   1389  CE  LYS A 273       5.534  22.791 -19.859  1.00 99.03           C  
ANISOU 1389  CE  LYS A 273    12203  13391  12033   -469   1564    406       C  
ATOM   1390  NZ  LYS A 273       6.523  21.705 -20.098  1.00100.71           N  
ANISOU 1390  NZ  LYS A 273    12272  13883  12108   -298   1652    194       N  
ATOM   1391  N   THR A 274       5.777  28.756 -15.969  1.00 91.93           N  
ANISOU 1391  N   THR A 274    11618  11361  11950  -1270   1157   1251       N  
ATOM   1392  CA  THR A 274       6.578  29.600 -15.088  1.00 91.33           C  
ANISOU 1392  CA  THR A 274    11532  11172  11997  -1419   1092   1332       C  
ATOM   1393  C   THR A 274       5.981  29.663 -13.686  1.00 88.24           C  
ANISOU 1393  C   THR A 274    11278  10432  11816  -1289   1009   1204       C  
ATOM   1394  O   THR A 274       6.720  29.719 -12.696  1.00 87.86           O  
ANISOU 1394  O   THR A 274    11187  10341  11856  -1307    994   1146       O  
ATOM   1395  CB  THR A 274       6.740  31.003 -15.683  1.00 91.07           C  
ANISOU 1395  CB  THR A 274    11550  11097  11954  -1690    992   1616       C  
ATOM   1396  OG1 THR A 274       7.664  31.756 -14.887  1.00 91.40           O  
ANISOU 1396  OG1 THR A 274    11567  11059  12104  -1862    922   1691       O  
ATOM   1397  CG2 THR A 274       5.412  31.744 -15.752  1.00 88.77           C  
ANISOU 1397  CG2 THR A 274    11483  10480  11766  -1660    858   1693       C  
ATOM   1398  N   TYR A 275       4.649  29.645 -13.574  1.00 86.01           N  
ANISOU 1398  N   TYR A 275    11148   9929  11602  -1155    953   1157       N  
ATOM   1399  CA  TYR A 275       4.043  29.518 -12.254  1.00 82.20           C  
ANISOU 1399  CA  TYR A 275    10764   9187  11282  -1002    900   1013       C  
ATOM   1400  C   TYR A 275       4.331  28.150 -11.657  1.00 82.17           C  
ANISOU 1400  C   TYR A 275    10666   9291  11263   -837   1001    810       C  
ATOM   1401  O   TYR A 275       4.516  28.031 -10.440  1.00 80.82           O  
ANISOU 1401  O   TYR A 275    10509   9001  11198   -770    978    711       O  
ATOM   1402  CB  TYR A 275       2.535  29.756 -12.325  1.00 80.61           C  
ANISOU 1402  CB  TYR A 275    10710   8783  11135   -889    829   1012       C  
ATOM   1403  CG  TYR A 275       1.817  29.392 -11.042  1.00 77.21           C  
ANISOU 1403  CG  TYR A 275    10344   8168  10826   -706    805    851       C  
ATOM   1404  CD1 TYR A 275       1.796  30.266  -9.962  1.00 75.38           C  
ANISOU 1404  CD1 TYR A 275    10203   7712  10727   -702    703    839       C  
ATOM   1405  CD2 TYR A 275       1.172  28.169 -10.905  1.00 76.05           C  
ANISOU 1405  CD2 TYR A 275    10164   8079  10650   -544    876    711       C  
ATOM   1406  CE1 TYR A 275       1.149  29.935  -8.786  1.00 72.53           C  
ANISOU 1406  CE1 TYR A 275     9882   7229  10446   -531    690    694       C  
ATOM   1407  CE2 TYR A 275       0.525  27.829  -9.731  1.00 73.28           C  
ANISOU 1407  CE2 TYR A 275     9855   7596  10392   -401    858    592       C  
ATOM   1408  CZ  TYR A 275       0.514  28.717  -8.677  1.00 71.59           C  
ANISOU 1408  CZ  TYR A 275     9714   7199  10288   -389    775    584       C  
ATOM   1409  OH  TYR A 275      -0.131  28.385  -7.508  1.00 68.63           O  
ANISOU 1409  OH  TYR A 275     9364   6736   9975   -242    766    467       O  
ATOM   1410  N   LEU A 276       4.367  27.113 -12.495  1.00 85.27           N  
ANISOU 1410  N   LEU A 276    10975   9901  11524   -764   1098    744       N  
ATOM   1411  CA  LEU A 276       4.772  25.793 -12.028  1.00 85.85           C  
ANISOU 1411  CA  LEU A 276    10967  10070  11581   -610   1173    558       C  
ATOM   1412  C   LEU A 276       6.195  25.833 -11.485  1.00 87.83           C  
ANISOU 1412  C   LEU A 276    11087  10450  11835   -668   1204    544       C  
ATOM   1413  O   LEU A 276       6.467  25.338 -10.386  1.00 86.92           O  
ANISOU 1413  O   LEU A 276    10963  10259  11804   -570   1199    430       O  
ATOM   1414  CB  LEU A 276       4.652  24.782 -13.169  1.00 88.49           C  
ANISOU 1414  CB  LEU A 276    11247  10615  11762   -528   1249    486       C  
ATOM   1415  CG  LEU A 276       5.011  23.324 -12.882  1.00 90.27           C  
ANISOU 1415  CG  LEU A 276    11414  10922  11963   -348   1304    284       C  
ATOM   1416  CD1 LEU A 276       4.224  22.782 -11.697  1.00 86.10           C  
ANISOU 1416  CD1 LEU A 276    10991  10140  11582   -228   1252    187       C  
ATOM   1417  CD2 LEU A 276       4.787  22.477 -14.129  1.00 93.02           C  
ANISOU 1417  CD2 LEU A 276    11738  11452  12152   -271   1351    207       C  
ATOM   1418  N   MET A 277       7.115  26.437 -12.246  1.00 89.65           N  
ANISOU 1418  N   MET A 277    11204  10895  11965   -839   1233    675       N  
ATOM   1419  CA  MET A 277       8.485  26.642 -11.781  1.00 91.43           C  
ANISOU 1419  CA  MET A 277    11280  11270  12188   -933   1251    694       C  
ATOM   1420  C   MET A 277       8.511  27.263 -10.391  1.00 89.08           C  
ANISOU 1420  C   MET A 277    11069  10710  12068   -965   1151    686       C  
ATOM   1421  O   MET A 277       9.186  26.766  -9.482  1.00 89.50           O  
ANISOU 1421  O   MET A 277    11048  10793  12164   -890   1162    577       O  
ATOM   1422  CB  MET A 277       9.236  27.543 -12.762  1.00 93.53           C  
ANISOU 1422  CB  MET A 277    11438  11761  12339  -1179   1264    902       C  
ATOM   1423  CG  MET A 277      10.092  26.826 -13.779  1.00 96.41           C  
ANISOU 1423  CG  MET A 277    11590  12550  12491  -1156   1395    876       C  
ATOM   1424  SD  MET A 277      10.361  27.833 -15.252  1.00 98.44           S  
ANISOU 1424  SD  MET A 277    11771  13063  12570  -1433   1412   1153       S  
ATOM   1425  CE  MET A 277      10.369  29.479 -14.543  1.00 95.29           C  
ANISOU 1425  CE  MET A 277    11503  12344  12358  -1715   1244   1381       C  
ATOM   1426  N   PHE A 278       7.772  28.360 -10.217  1.00 87.09           N  
ANISOU 1426  N   PHE A 278    10977  10200  11913  -1061   1042    794       N  
ATOM   1427  CA  PHE A 278       7.793  29.088  -8.954  1.00 84.99           C  
ANISOU 1427  CA  PHE A 278    10806   9686  11802  -1091    929    778       C  
ATOM   1428  C   PHE A 278       7.250  28.243  -7.809  1.00 82.96           C  
ANISOU 1428  C   PHE A 278    10602   9301  11619   -865    938    588       C  
ATOM   1429  O   PHE A 278       7.729  28.344  -6.674  1.00 82.88           O  
ANISOU 1429  O   PHE A 278    10587   9220  11685   -851    893    521       O  
ATOM   1430  CB  PHE A 278       6.991  30.382  -9.093  1.00 83.21           C  
ANISOU 1430  CB  PHE A 278    10761   9197  11658  -1194    797    909       C  
ATOM   1431  CG  PHE A 278       6.519  30.950  -7.785  1.00 81.01           C  
ANISOU 1431  CG  PHE A 278    10629   8619  11531  -1122    678    826       C  
ATOM   1432  CD1 PHE A 278       7.388  31.651  -6.967  1.00 81.98           C  
ANISOU 1432  CD1 PHE A 278    10751   8667  11732  -1248    585    837       C  
ATOM   1433  CD2 PHE A 278       5.204  30.788  -7.376  1.00 78.04           C  
ANISOU 1433  CD2 PHE A 278    10383   8062  11207   -929    655    732       C  
ATOM   1434  CE1 PHE A 278       6.958  32.178  -5.764  1.00 79.76           C  
ANISOU 1434  CE1 PHE A 278    10610   8125  11572  -1165    469    738       C  
ATOM   1435  CE2 PHE A 278       4.767  31.312  -6.172  1.00 75.72           C  
ANISOU 1435  CE2 PHE A 278    10209   7536  11026   -842    553    642       C  
ATOM   1436  CZ  PHE A 278       5.646  32.008  -5.365  1.00 76.17           C  
ANISOU 1436  CZ  PHE A 278    10278   7510  11153   -951    459    636       C  
ATOM   1437  N   TRP A 279       6.252  27.401  -8.084  1.00 78.15           N  
ANISOU 1437  N   TRP A 279    10042   8671  10981   -700    988    510       N  
ATOM   1438  CA  TRP A 279       5.577  26.698  -6.998  1.00 74.65           C  
ANISOU 1438  CA  TRP A 279     9663   8094  10608   -517    981    369       C  
ATOM   1439  C   TRP A 279       6.435  25.570  -6.443  1.00 76.16           C  
ANISOU 1439  C   TRP A 279     9739   8422  10775   -420   1043    251       C  
ATOM   1440  O   TRP A 279       6.524  25.393  -5.221  1.00 74.88           O  
ANISOU 1440  O   TRP A 279     9597   8171  10681   -348   1008    175       O  
ATOM   1441  CB  TRP A 279       4.231  26.152  -7.459  1.00 73.19           C  
ANISOU 1441  CB  TRP A 279     9556   7849  10402   -401   1000    342       C  
ATOM   1442  CG  TRP A 279       3.508  25.536  -6.317  1.00 69.43           C  
ANISOU 1442  CG  TRP A 279     9136   7253   9992   -250    987    234       C  
ATOM   1443  CD1 TRP A 279       2.906  26.194  -5.286  1.00 66.47           C  
ANISOU 1443  CD1 TRP A 279     8848   6708   9699   -210    915    218       C  
ATOM   1444  CD2 TRP A 279       3.350  24.136  -6.047  1.00 67.67           C  
ANISOU 1444  CD2 TRP A 279     8882   7082   9749   -122   1037    131       C  
ATOM   1445  NE1 TRP A 279       2.361  25.295  -4.406  1.00 64.19           N  
ANISOU 1445  NE1 TRP A 279     8566   6397   9426    -77    934    127       N  
ATOM   1446  CE2 TRP A 279       2.619  24.025  -4.847  1.00 63.76           C  
ANISOU 1446  CE2 TRP A 279     8448   6458   9318    -34   1000     84       C  
ATOM   1447  CE3 TRP A 279       3.742  22.968  -6.710  1.00 69.77           C  
ANISOU 1447  CE3 TRP A 279     9081   7485   9942    -68   1098     71       C  
ATOM   1448  CZ2 TRP A 279       2.273  22.794  -4.293  1.00 63.77           C  
ANISOU 1448  CZ2 TRP A 279     8447   6461   9321     74   1020     13       C  
ATOM   1449  CZ3 TRP A 279       3.396  21.744  -6.157  1.00 67.22           C  
ANISOU 1449  CZ3 TRP A 279     8778   7125   9638     55   1101    -21       C  
ATOM   1450  CH2 TRP A 279       2.669  21.668  -4.961  1.00 64.53           C  
ANISOU 1450  CH2 TRP A 279     8500   6651   9368    109   1061    -33       C  
ATOM   1451  N   ILE A 280       7.041  24.771  -7.327  1.00 81.68           N  
ANISOU 1451  N   ILE A 280    10321   9344  11370   -397   1126    227       N  
ATOM   1452  CA  ILE A 280       7.940  23.710  -6.879  1.00 83.63           C  
ANISOU 1452  CA  ILE A 280    10456   9726  11593   -283   1170    111       C  
ATOM   1453  C   ILE A 280       9.017  24.283  -5.969  1.00 84.80           C  
ANISOU 1453  C   ILE A 280    10524   9905  11790   -365   1131    127       C  
ATOM   1454  O   ILE A 280       9.217  23.815  -4.843  1.00 84.06           O  
ANISOU 1454  O   ILE A 280    10435   9749  11754   -266   1102     42       O  
ATOM   1455  CB  ILE A 280       8.560  22.974  -8.083  1.00 88.17           C  
ANISOU 1455  CB  ILE A 280    10903  10568  12030   -244   1258     77       C  
ATOM   1456  CG1 ILE A 280       7.541  22.791  -9.217  1.00 87.50           C  
ANISOU 1456  CG1 ILE A 280    10897  10472  11876   -228   1281     95       C  
ATOM   1457  CG2 ILE A 280       9.223  21.668  -7.644  1.00 88.14           C  
ANISOU 1457  CG2 ILE A 280    10821  10657  12011    -56   1285    -77       C  
ATOM   1458  CD1 ILE A 280       6.569  21.652  -9.016  1.00 84.12           C  
ANISOU 1458  CD1 ILE A 280    10575   9906  11481    -57   1266    -24       C  
ATOM   1459  N   GLY A 281       9.712  25.319  -6.443  1.00 87.88           N  
ANISOU 1459  N   GLY A 281    10843  10394  12155   -564   1117    250       N  
ATOM   1460  CA  GLY A 281      10.815  25.878  -5.679  1.00 89.44           C  
ANISOU 1460  CA  GLY A 281    10946  10644  12391   -675   1067    274       C  
ATOM   1461  C   GLY A 281      10.424  26.309  -4.279  1.00 86.77           C  
ANISOU 1461  C   GLY A 281    10738  10053  12177   -647    965    226       C  
ATOM   1462  O   GLY A 281      11.172  26.092  -3.324  1.00 87.39           O  
ANISOU 1462  O   GLY A 281    10748  10173  12284   -616    937    162       O  
ATOM   1463  N   VAL A 282       9.242  26.913  -4.132  1.00 84.22           N  
ANISOU 1463  N   VAL A 282    10595   9486  11917   -642    906    249       N  
ATOM   1464  CA  VAL A 282       8.851  27.444  -2.829  1.00 81.10           C  
ANISOU 1464  CA  VAL A 282    10321   8875  11619   -607    806    193       C  
ATOM   1465  C   VAL A 282       8.613  26.315  -1.834  1.00 78.93           C  
ANISOU 1465  C   VAL A 282    10045   8599  11347   -404    837     61       C  
ATOM   1466  O   VAL A 282       9.029  26.397  -0.672  1.00 79.57           O  
ANISOU 1466  O   VAL A 282    10123   8647  11462   -378    780     -1       O  
ATOM   1467  CB  VAL A 282       7.623  28.362  -2.971  1.00 77.76           C  
ANISOU 1467  CB  VAL A 282    10078   8219  11250   -618    735    238       C  
ATOM   1468  CG1 VAL A 282       6.806  28.377  -1.689  1.00 74.95           C  
ANISOU 1468  CG1 VAL A 282     9837   7691  10951   -466    680    126       C  
ATOM   1469  CG2 VAL A 282       8.069  29.771  -3.328  1.00 79.81           C  
ANISOU 1469  CG2 VAL A 282    10380   8393  11553   -839    629    362       C  
ATOM   1470  N   VAL A 283       7.958  25.238  -2.268  1.00 77.82           N  
ANISOU 1470  N   VAL A 283     9910   8493  11165   -268    915     23       N  
ATOM   1471  CA  VAL A 283       7.776  24.106  -1.368  1.00 76.49           C  
ANISOU 1471  CA  VAL A 283     9745   8318  10999   -100    930    -74       C  
ATOM   1472  C   VAL A 283       9.013  23.214  -1.350  1.00 79.37           C  
ANISOU 1472  C   VAL A 283     9963   8868  11324    -51    967   -122       C  
ATOM   1473  O   VAL A 283       9.256  22.512  -0.363  1.00 78.69           O  
ANISOU 1473  O   VAL A 283     9867   8779  11252     58    945   -186       O  
ATOM   1474  CB  VAL A 283       6.512  23.310  -1.739  1.00 72.62           C  
ANISOU 1474  CB  VAL A 283     9337   7761  10496      8    970    -88       C  
ATOM   1475  CG1 VAL A 283       5.343  24.252  -1.973  1.00 71.27           C  
ANISOU 1475  CG1 VAL A 283     9278   7450  10351    -35    938    -34       C  
ATOM   1476  CG2 VAL A 283       6.760  22.441  -2.963  1.00 74.05           C  
ANISOU 1476  CG2 VAL A 283     9451   8073  10611     36   1040    -97       C  
ATOM   1477  N   SER A 284       9.819  23.227  -2.417  1.00 84.32           N  
ANISOU 1477  N   SER A 284    10468   9679  11891   -119   1018    -89       N  
ATOM   1478  CA  SER A 284      11.039  22.426  -2.414  1.00 87.50           C  
ANISOU 1478  CA  SER A 284    10708  10292  12247    -46   1051   -148       C  
ATOM   1479  C   SER A 284      12.044  22.964  -1.405  1.00 90.61           C  
ANISOU 1479  C   SER A 284    11017  10735  12674   -117    988   -146       C  
ATOM   1480  O   SER A 284      12.733  22.189  -0.732  1.00 91.35           O  
ANISOU 1480  O   SER A 284    11032  10912  12764      3    976   -218       O  
ATOM   1481  CB  SER A 284      11.659  22.382  -3.811  1.00 91.89           C  
ANISOU 1481  CB  SER A 284    11128  11085  12703    -98   1130   -117       C  
ATOM   1482  OG  SER A 284      11.159  21.286  -4.560  1.00 89.59           O  
ANISOU 1482  OG  SER A 284    10867  10816  12358     57   1184   -191       O  
ATOM   1483  N   VAL A 285      12.139  24.290  -1.277  1.00 91.05           N  
ANISOU 1483  N   VAL A 285    11099  10729  12768   -310    928    -64       N  
ATOM   1484  CA  VAL A 285      13.090  24.867  -0.333  1.00 93.66           C  
ANISOU 1484  CA  VAL A 285    11356  11097  13132   -401    847    -65       C  
ATOM   1485  C   VAL A 285      12.595  24.701   1.100  1.00 90.11           C  
ANISOU 1485  C   VAL A 285    11027  10474  12736   -287    775   -147       C  
ATOM   1486  O   VAL A 285      13.388  24.450   2.015  1.00 92.44           O  
ANISOU 1486  O   VAL A 285    11244  10846  13033   -249    729   -196       O  
ATOM   1487  CB  VAL A 285      13.375  26.344  -0.676  1.00 93.79           C  
ANISOU 1487  CB  VAL A 285    11379  11078  13178   -664    779     51       C  
ATOM   1488  CG1 VAL A 285      14.045  26.457  -2.040  1.00 96.53           C  
ANISOU 1488  CG1 VAL A 285    11567  11667  13443   -797    855    155       C  
ATOM   1489  CG2 VAL A 285      12.108  27.188  -0.615  1.00 89.48           C  
ANISOU 1489  CG2 VAL A 285    11056  10244  12696   -697    718     79       C  
ATOM   1490  N   LEU A 286      11.284  24.834   1.322  1.00 84.46           N  
ANISOU 1490  N   LEU A 286    10489   9551  12051   -227    765   -158       N  
ATOM   1491  CA  LEU A 286      10.732  24.580   2.649  1.00 81.52           C  
ANISOU 1491  CA  LEU A 286    10214   9062  11698   -105    714   -230       C  
ATOM   1492  C   LEU A 286      10.929  23.124   3.042  1.00 80.89           C  
ANISOU 1492  C   LEU A 286    10080   9069  11585     69    755   -280       C  
ATOM   1493  O   LEU A 286      11.477  22.824   4.108  1.00 81.96           O  
ANISOU 1493  O   LEU A 286    10181   9246  11715    128    703   -323       O  
ATOM   1494  CB  LEU A 286       9.247  24.943   2.689  1.00 76.82           C  
ANISOU 1494  CB  LEU A 286     9786   8280  11123    -63    711   -227       C  
ATOM   1495  CG  LEU A 286       8.835  26.411   2.602  1.00 76.40           C  
ANISOU 1495  CG  LEU A 286     9837   8075  11115   -182    633   -200       C  
ATOM   1496  CD1 LEU A 286       7.321  26.520   2.595  1.00 73.52           C  
ANISOU 1496  CD1 LEU A 286     9607   7572  10755    -85    645   -209       C  
ATOM   1497  CD2 LEU A 286       9.427  27.200   3.756  1.00 78.14           C  
ANISOU 1497  CD2 LEU A 286    10079   8248  11362   -231    516   -257       C  
ATOM   1498  N   LEU A 287      10.492  22.204   2.178  1.00 78.25           N  
ANISOU 1498  N   LEU A 287     9749   8754  11229    153    830   -275       N  
ATOM   1499  CA  LEU A 287      10.622  20.782   2.471  1.00 76.67           C  
ANISOU 1499  CA  LEU A 287     9528   8592  11011    321    843   -320       C  
ATOM   1500  C   LEU A 287      12.081  20.383   2.654  1.00 80.30           C  
ANISOU 1500  C   LEU A 287     9826   9233  11450    363    827   -358       C  
ATOM   1501  O   LEU A 287      12.398  19.531   3.492  1.00 79.88           O  
ANISOU 1501  O   LEU A 287     9763   9190  11396    493    785   -393       O  
ATOM   1502  CB  LEU A 287       9.974  19.961   1.355  1.00 74.64           C  
ANISOU 1502  CB  LEU A 287     9310   8314  10738    386    907   -322       C  
ATOM   1503  CG  LEU A 287       8.589  19.389   1.662  1.00 70.49           C  
ANISOU 1503  CG  LEU A 287     8929   7625  10228    449    900   -307       C  
ATOM   1504  CD1 LEU A 287       8.076  18.551   0.497  1.00 69.50           C  
ANISOU 1504  CD1 LEU A 287     8836   7484  10088    499    942   -319       C  
ATOM   1505  CD2 LEU A 287       8.623  18.575   2.945  1.00 70.18           C  
ANISOU 1505  CD2 LEU A 287     8921   7546  10196    553    843   -318       C  
ATOM   1506  N   LEU A 288      12.986  20.991   1.882  1.00 86.41           N  
ANISOU 1506  N   LEU A 288    10461  10169  12201    253    854   -338       N  
ATOM   1507  CA  LEU A 288      14.407  20.695   2.041  1.00 90.20           C  
ANISOU 1507  CA  LEU A 288    10751  10870  12651    287    840   -370       C  
ATOM   1508  C   LEU A 288      14.905  21.140   3.409  1.00 91.51           C  
ANISOU 1508  C   LEU A 288    10902  11024  12844    250    744   -379       C  
ATOM   1509  O   LEU A 288      15.570  20.377   4.119  1.00 91.60           O  
ANISOU 1509  O   LEU A 288    10842  11118  12844    382    703   -425       O  
ATOM   1510  CB  LEU A 288      15.219  21.364   0.931  1.00 95.11           C  
ANISOU 1510  CB  LEU A 288    11206  11705  13226    138    894   -323       C  
ATOM   1511  CG  LEU A 288      16.591  20.754   0.626  1.00 97.44           C  
ANISOU 1511  CG  LEU A 288    11262  12304  13457    223    922   -367       C  
ATOM   1512  CD1 LEU A 288      16.464  19.579  -0.332  1.00 95.05           C  
ANISOU 1512  CD1 LEU A 288    10940  12079  13097    423    998   -443       C  
ATOM   1513  CD2 LEU A 288      17.539  21.808   0.067  1.00101.99           C  
ANISOU 1513  CD2 LEU A 288    11649  13111  13991     -7    937   -281       C  
ATOM   1514  N   PHE A 289      14.590  22.378   3.799  1.00 90.38           N  
ANISOU 1514  N   PHE A 289    10834  10771  12733     81    692   -341       N  
ATOM   1515  CA  PHE A 289      15.001  22.855   5.114  1.00 92.35           C  
ANISOU 1515  CA  PHE A 289    11089  11001  12998     47    586   -369       C  
ATOM   1516  C   PHE A 289      14.325  22.060   6.224  1.00 88.60           C  
ANISOU 1516  C   PHE A 289    10733  10418  12514    221    556   -412       C  
ATOM   1517  O   PHE A 289      14.957  21.733   7.236  1.00 89.84           O  
ANISOU 1517  O   PHE A 289    10838  10647  12652    287    488   -445       O  
ATOM   1518  CB  PHE A 289      14.684  24.340   5.271  1.00 92.42           C  
ANISOU 1518  CB  PHE A 289    11193  10876  13047   -149    517   -342       C  
ATOM   1519  CG  PHE A 289      14.656  24.793   6.701  1.00 92.63           C  
ANISOU 1519  CG  PHE A 289    11297  10817  13079   -142    402   -402       C  
ATOM   1520  CD1 PHE A 289      15.836  25.003   7.394  1.00 97.81           C  
ANISOU 1520  CD1 PHE A 289    11828  11609  13727   -203    314   -427       C  
ATOM   1521  CD2 PHE A 289      13.454  24.979   7.363  1.00 88.38           C  
ANISOU 1521  CD2 PHE A 289    10943  10097  12541    -64    382   -442       C  
ATOM   1522  CE1 PHE A 289      15.819  25.409   8.714  1.00 97.95           C  
ANISOU 1522  CE1 PHE A 289    11922  11562  13734   -191    200   -496       C  
ATOM   1523  CE2 PHE A 289      13.433  25.380   8.686  1.00 88.88           C  
ANISOU 1523  CE2 PHE A 289    11072  10116  12583    -38    280   -513       C  
ATOM   1524  CZ  PHE A 289      14.616  25.598   9.360  1.00 93.87           C  
ANISOU 1524  CZ  PHE A 289    11596  10865  13204   -102    186   -544       C  
ATOM   1525  N   ILE A 290      13.033  21.759   6.061  1.00 83.42           N  
ANISOU 1525  N   ILE A 290    10228   9606  11864    285    602   -400       N  
ATOM   1526  CA  ILE A 290      12.319  20.969   7.061  1.00 80.12           C  
ANISOU 1526  CA  ILE A 290     9911   9108  11423    424    579   -411       C  
ATOM   1527  C   ILE A 290      13.014  19.630   7.267  1.00 81.09           C  
ANISOU 1527  C   ILE A 290     9958   9324  11531    576    568   -419       C  
ATOM   1528  O   ILE A 290      13.118  19.133   8.396  1.00 81.32           O  
ANISOU 1528  O   ILE A 290    10008   9359  11533    662    504   -420       O  
ATOM   1529  CB  ILE A 290      10.843  20.795   6.652  1.00 76.44           C  
ANISOU 1529  CB  ILE A 290     9584   8497  10963    449    637   -379       C  
ATOM   1530  CG1 ILE A 290      10.064  22.094   6.879  1.00 75.61           C  
ANISOU 1530  CG1 ILE A 290     9574   8289  10865    354    616   -386       C  
ATOM   1531  CG2 ILE A 290      10.193  19.656   7.423  1.00 73.87           C  
ANISOU 1531  CG2 ILE A 290     9330   8127  10609    580    626   -356       C  
ATOM   1532  CD1 ILE A 290       8.897  22.287   5.930  1.00 72.68           C  
ANISOU 1532  CD1 ILE A 290     9285   7816  10512    332    679   -350       C  
ATOM   1533  N   VAL A 291      13.519  19.037   6.183  1.00 82.01           N  
ANISOU 1533  N   VAL A 291     9984   9520  11655    622    620   -429       N  
ATOM   1534  CA  VAL A 291      14.278  17.794   6.288  1.00 82.48           C  
ANISOU 1534  CA  VAL A 291     9969   9663  11705    796    593   -459       C  
ATOM   1535  C   VAL A 291      15.515  17.999   7.155  1.00 85.98           C  
ANISOU 1535  C   VAL A 291    10274  10266  12130    805    517   -482       C  
ATOM   1536  O   VAL A 291      15.812  17.192   8.044  1.00 85.78           O  
ANISOU 1536  O   VAL A 291    10255  10246  12093    940    444   -484       O  
ATOM   1537  CB  VAL A 291      14.643  17.272   4.886  1.00 82.10           C  
ANISOU 1537  CB  VAL A 291     9837   9705  11652    857    663   -497       C  
ATOM   1538  CG1 VAL A 291      15.821  16.313   4.956  1.00 83.59           C  
ANISOU 1538  CG1 VAL A 291     9890  10047  11825   1039    623   -557       C  
ATOM   1539  CG2 VAL A 291      13.442  16.592   4.248  1.00 79.47           C  
ANISOU 1539  CG2 VAL A 291     9660   9198  11336    909    701   -488       C  
ATOM   1540  N   TYR A 292      16.249  19.089   6.918  1.00 90.54           N  
ANISOU 1540  N   TYR A 292    10725  10974  12703    648    519   -486       N  
ATOM   1541  CA  TYR A 292      17.406  19.390   7.755  1.00 94.05           C  
ANISOU 1541  CA  TYR A 292    11028  11578  13128    623    433   -504       C  
ATOM   1542  C   TYR A 292      16.986  19.652   9.195  1.00 93.90           C  
ANISOU 1542  C   TYR A 292    11129  11454  13095    618    343   -503       C  
ATOM   1543  O   TYR A 292      17.603  19.142  10.137  1.00 95.02           O  
ANISOU 1543  O   TYR A 292    11218  11676  13207    719    262   -516       O  
ATOM   1544  CB  TYR A 292      18.174  20.592   7.207  1.00 98.20           C  
ANISOU 1544  CB  TYR A 292    11408  12247  13657    407    439   -488       C  
ATOM   1545  CG  TYR A 292      19.271  21.050   8.146  1.00101.90           C  
ANISOU 1545  CG  TYR A 292    11741  12866  14110    339    331   -504       C  
ATOM   1546  CD1 TYR A 292      20.487  20.385   8.196  1.00102.86           C  
ANISOU 1546  CD1 TYR A 292    11647  13234  14201    448    308   -527       C  
ATOM   1547  CD2 TYR A 292      19.079  22.128   9.001  1.00104.01           C  
ANISOU 1547  CD2 TYR A 292    12097  13033  14391    183    239   -507       C  
ATOM   1548  CE1 TYR A 292      21.488  20.788   9.058  1.00105.41           C  
ANISOU 1548  CE1 TYR A 292    11833  13712  14507    381    200   -538       C  
ATOM   1549  CE2 TYR A 292      20.075  22.537   9.870  1.00107.40           C  
ANISOU 1549  CE2 TYR A 292    12409  13596  14803    113    123   -530       C  
ATOM   1550  CZ  TYR A 292      21.278  21.864   9.893  1.00108.25           C  
ANISOU 1550  CZ  TYR A 292    12289  13960  14880    202    105   -538       C  
ATOM   1551  OH  TYR A 292      22.275  22.266  10.752  1.00111.26           O  
ANISOU 1551  OH  TYR A 292    12539  14494  15241    126    -18   -557       O  
ATOM   1552  N   ALA A 293      15.938  20.458   9.381  1.00 89.73           N  
ANISOU 1552  N   ALA A 293    10756  10762  12575    515    351   -493       N  
ATOM   1553  CA  ALA A 293      15.494  20.807  10.726  1.00 89.48           C  
ANISOU 1553  CA  ALA A 293    10832  10662  12504    519    272   -511       C  
ATOM   1554  C   ALA A 293      15.106  19.565  11.516  1.00 87.59           C  
ANISOU 1554  C   ALA A 293    10658  10399  12221    698    254   -480       C  
ATOM   1555  O   ALA A 293      15.613  19.335  12.620  1.00 89.58           O  
ANISOU 1555  O   ALA A 293    10882  10731  12422    756    166   -487       O  
ATOM   1556  CB  ALA A 293      14.323  21.788  10.651  1.00 88.48           C  
ANISOU 1556  CB  ALA A 293    10860  10370  12388    423    294   -519       C  
ATOM   1557  N   TYR A 294      14.221  18.737  10.953  1.00 86.33           N  
ANISOU 1557  N   TYR A 294    10589  10131  12080    776    324   -435       N  
ATOM   1558  CA  TYR A 294      13.699  17.592  11.694  1.00 84.90           C  
ANISOU 1558  CA  TYR A 294    10497   9897  11864    909    293   -376       C  
ATOM   1559  C   TYR A 294      14.800  16.613  12.081  1.00 86.45           C  
ANISOU 1559  C   TYR A 294    10601  10191  12055   1046    214   -370       C  
ATOM   1560  O   TYR A 294      14.726  15.990  13.147  1.00 86.83           O  
ANISOU 1560  O   TYR A 294    10700  10239  12052   1127    139   -317       O  
ATOM   1561  CB  TYR A 294      12.614  16.889  10.877  1.00 80.90           C  
ANISOU 1561  CB  TYR A 294    10097   9249  11392    938    365   -326       C  
ATOM   1562  CG  TYR A 294      11.287  17.617  10.878  1.00 80.02           C  
ANISOU 1562  CG  TYR A 294    10094   9048  11263    845    421   -308       C  
ATOM   1563  CD1 TYR A 294      11.151  18.849  11.502  1.00 80.74           C  
ANISOU 1563  CD1 TYR A 294    10195   9169  11314    763    404   -355       C  
ATOM   1564  CD2 TYR A 294      10.170  17.071  10.258  1.00 77.60           C  
ANISOU 1564  CD2 TYR A 294     9879   8627  10977    849    478   -254       C  
ATOM   1565  CE1 TYR A 294       9.947  19.519  11.509  1.00 79.11           C  
ANISOU 1565  CE1 TYR A 294    10080   8890  11087    715    447   -355       C  
ATOM   1566  CE2 TYR A 294       8.958  17.735  10.257  1.00 75.41           C  
ANISOU 1566  CE2 TYR A 294     9677   8297  10677    780    528   -239       C  
ATOM   1567  CZ  TYR A 294       8.853  18.959  10.885  1.00 76.05           C  
ANISOU 1567  CZ  TYR A 294     9761   8419  10717    727    514   -293       C  
ATOM   1568  OH  TYR A 294       7.649  19.627  10.892  1.00 75.25           O  
ANISOU 1568  OH  TYR A 294     9729   8274  10589    695    556   -295       O  
ATOM   1569  N   MET A 295      15.828  16.467  11.243  1.00 88.12           N  
ANISOU 1569  N   MET A 295    10669  10504  12308   1082    227   -418       N  
ATOM   1570  CA  MET A 295      16.966  15.635  11.622  1.00 89.39           C  
ANISOU 1570  CA  MET A 295    10717  10786  12461   1235    142   -430       C  
ATOM   1571  C   MET A 295      17.735  16.258  12.780  1.00 92.69           C  
ANISOU 1571  C   MET A 295    11047  11346  12823   1189     49   -443       C  
ATOM   1572  O   MET A 295      18.225  15.545  13.664  1.00 93.63           O  
ANISOU 1572  O   MET A 295    11149  11517  12908   1316    -50   -416       O  
ATOM   1573  CB  MET A 295      17.886  15.421  10.420  1.00 90.22           C  
ANISOU 1573  CB  MET A 295    10658  11020  12602   1295    188   -495       C  
ATOM   1574  CG  MET A 295      17.365  14.420   9.401  1.00 87.52           C  
ANISOU 1574  CG  MET A 295    10398  10556  12301   1418    238   -505       C  
ATOM   1575  SD  MET A 295      17.030  12.801  10.123  1.00 87.48           S  
ANISOU 1575  SD  MET A 295    10550  10375  12314   1636    122   -449       S  
ATOM   1576  CE  MET A 295      17.075  11.754   8.669  1.00 85.73           C  
ANISOU 1576  CE  MET A 295    10343  10086  12144   1809    153   -531       C  
ATOM   1577  N   TYR A 296      17.844  17.588  12.793  1.00 94.02           N  
ANISOU 1577  N   TYR A 296    11173  11567  12984   1005     63   -484       N  
ATOM   1578  CA  TYR A 296      18.542  18.269  13.878  1.00 97.53           C  
ANISOU 1578  CA  TYR A 296    11548  12134  13376    940    -42   -513       C  
ATOM   1579  C   TYR A 296      17.760  18.180  15.183  1.00 97.82           C  
ANISOU 1579  C   TYR A 296    11739  12096  13332    975   -100   -484       C  
ATOM   1580  O   TYR A 296      18.355  18.041  16.257  1.00100.05           O  
ANISOU 1580  O   TYR A 296    11978  12490  13548   1025   -207   -485       O  
ATOM   1581  CB  TYR A 296      18.800  19.726  13.489  1.00100.25           C  
ANISOU 1581  CB  TYR A 296    11834  12511  13746    719    -34   -564       C  
ATOM   1582  CG  TYR A 296      19.326  20.603  14.603  1.00103.81           C  
ANISOU 1582  CG  TYR A 296    12256  13040  14146    618   -159   -612       C  
ATOM   1583  CD1 TYR A 296      20.690  20.721  14.830  1.00106.77           C  
ANISOU 1583  CD1 TYR A 296    12429  13624  14514    585   -246   -634       C  
ATOM   1584  CD2 TYR A 296      18.462  21.317  15.425  1.00104.53           C  
ANISOU 1584  CD2 TYR A 296    12516  13012  14190    564   -197   -648       C  
ATOM   1585  CE1 TYR A 296      21.180  21.522  15.843  1.00109.93           C  
ANISOU 1585  CE1 TYR A 296    12808  14094  14868    481   -378   -686       C  
ATOM   1586  CE2 TYR A 296      18.943  22.121  16.441  1.00108.23           C  
ANISOU 1586  CE2 TYR A 296    12971  13546  14603    483   -326   -718       C  
ATOM   1587  CZ  TYR A 296      20.302  22.220  16.645  1.00111.02           C  
ANISOU 1587  CZ  TYR A 296    13136  14088  14959    432   -422   -734       C  
ATOM   1588  OH  TYR A 296      20.786  23.020  17.655  1.00114.23           O  
ANISOU 1588  OH  TYR A 296    13535  14556  15310    339   -568   -810       O  
ATOM   1589  N   ILE A 297      16.428  18.272  15.113  1.00 91.17           N  
ANISOU 1589  N   ILE A 297    11063  11098  12481    950    -30   -455       N  
ATOM   1590  CA  ILE A 297      15.609  18.104  16.312  1.00 91.33           C  
ANISOU 1590  CA  ILE A 297    11210  11092  12400    991    -67   -414       C  
ATOM   1591  C   ILE A 297      15.790  16.703  16.880  1.00 91.13           C  
ANISOU 1591  C   ILE A 297    11197  11087  12340   1147   -126   -313       C  
ATOM   1592  O   ILE A 297      15.920  16.521  18.097  1.00 92.88           O  
ANISOU 1592  O   ILE A 297    11435  11395  12458   1192   -214   -279       O  
ATOM   1593  CB  ILE A 297      14.126  18.401  16.008  1.00 88.90           C  
ANISOU 1593  CB  ILE A 297    11046  10646  12087    943     29   -394       C  
ATOM   1594  CG1 ILE A 297      13.815  19.892  16.151  1.00 89.22           C  
ANISOU 1594  CG1 ILE A 297    11121  10671  12108    823     28   -497       C  
ATOM   1595  CG2 ILE A 297      13.208  17.592  16.910  1.00 88.00           C  
ANISOU 1595  CG2 ILE A 297    11038  10523  11877   1021     22   -292       C  
ATOM   1596  CD1 ILE A 297      14.405  20.748  15.086  1.00 90.38           C  
ANISOU 1596  CD1 ILE A 297    11195  10786  12358    701     47   -557       C  
ATOM   1597  N   LEU A 298      15.817  15.695  16.006  1.00 90.28           N  
ANISOU 1597  N   LEU A 298    11092  10897  12315   1236    -93   -266       N  
ATOM   1598  CA  LEU A 298      15.931  14.316  16.469  1.00 90.14           C  
ANISOU 1598  CA  LEU A 298    11118  10844  12285   1388   -172   -163       C  
ATOM   1599  C   LEU A 298      17.310  14.038  17.055  1.00 92.89           C  
ANISOU 1599  C   LEU A 298    11332  11349  12612   1494   -292   -185       C  
ATOM   1600  O   LEU A 298      17.435  13.286  18.029  1.00 93.70           O  
ANISOU 1600  O   LEU A 298    11477  11471  12653   1591   -397    -94       O  
ATOM   1601  CB  LEU A 298      15.621  13.356  15.321  1.00 86.95           C  
ANISOU 1601  CB  LEU A 298    10768  10286  11984   1465   -128   -137       C  
ATOM   1602  CG  LEU A 298      15.682  11.859  15.620  1.00 87.39           C  
ANISOU 1602  CG  LEU A 298    10907  10239  12059   1626   -232    -33       C  
ATOM   1603  CD1 LEU A 298      14.453  11.418  16.395  1.00 87.28           C  
ANISOU 1603  CD1 LEU A 298    11060  10121  11980   1567   -249    120       C  
ATOM   1604  CD2 LEU A 298      15.813  11.066  14.330  1.00 85.02           C  
ANISOU 1604  CD2 LEU A 298    10618   9816  11871   1731   -212    -78       C  
ATOM   1605  N   TRP A 299      18.357  14.639  16.483  1.00100.53           N  
ANISOU 1605  N   TRP A 299    12126  12446  13624   1469   -284   -290       N  
ATOM   1606  CA  TRP A 299      19.697  14.476  17.038  1.00102.71           C  
ANISOU 1606  CA  TRP A 299    12240  12910  13874   1558   -399   -316       C  
ATOM   1607  C   TRP A 299      19.809  15.150  18.400  1.00105.26           C  
ANISOU 1607  C   TRP A 299    12568  13344  14082   1482   -488   -316       C  
ATOM   1608  O   TRP A 299      20.357  14.574  19.347  1.00106.47           O  
ANISOU 1608  O   TRP A 299    12693  13589  14170   1593   -610   -266       O  
ATOM   1609  CB  TRP A 299      20.739  15.041  16.072  1.00104.06           C  
ANISOU 1609  CB  TRP A 299    12199  13235  14105   1515   -360   -417       C  
ATOM   1610  CG  TRP A 299      22.107  14.440  16.235  1.00105.71           C  
ANISOU 1610  CG  TRP A 299    12215  13638  14313   1676   -460   -439       C  
ATOM   1611  CD1 TRP A 299      22.665  13.963  17.387  1.00107.11           C  
ANISOU 1611  CD1 TRP A 299    12366  13905  14427   1790   -603   -398       C  
ATOM   1612  CD2 TRP A 299      23.095  14.269  15.212  1.00106.20           C  
ANISOU 1612  CD2 TRP A 299    12066  13860  14426   1753   -426   -508       C  
ATOM   1613  NE1 TRP A 299      23.935  13.499  17.142  1.00108.02           N  
ANISOU 1613  NE1 TRP A 299    12268  14213  14563   1943   -666   -440       N  
ATOM   1614  CE2 TRP A 299      24.223  13.676  15.814  1.00107.54           C  
ANISOU 1614  CE2 TRP A 299    12081  14211  14566   1928   -554   -513       C  
ATOM   1615  CE3 TRP A 299      23.134  14.556  13.844  1.00105.68           C  
ANISOU 1615  CE3 TRP A 299    11917  13827  14412   1699   -299   -563       C  
ATOM   1616  CZ2 TRP A 299      25.376  13.365  15.096  1.00108.25           C  
ANISOU 1616  CZ2 TRP A 299    11925  14527  14678   2061   -554   -582       C  
ATOM   1617  CZ3 TRP A 299      24.280  14.246  13.133  1.00105.84           C  
ANISOU 1617  CZ3 TRP A 299    11694  14081  14441   1819   -293   -626       C  
ATOM   1618  CH2 TRP A 299      25.384  13.657  13.760  1.00107.05           C  
ANISOU 1618  CH2 TRP A 299    11685  14425  14565   2005   -417   -640       C  
ATOM   1619  N   LYS A 300      19.293  16.377  18.515  1.00 99.42           N  
ANISOU 1619  N   LYS A 300    11870  12594  13312   1304   -440   -378       N  
ATOM   1620  CA  LYS A 300      19.386  17.106  19.775  1.00101.99           C  
ANISOU 1620  CA  LYS A 300    12209  13025  13519   1239   -532   -413       C  
ATOM   1621  C   LYS A 300      18.537  16.465  20.865  1.00101.86           C  
ANISOU 1621  C   LYS A 300    12343  12980  13380   1319   -565   -311       C  
ATOM   1622  O   LYS A 300      18.905  16.517  22.045  1.00104.11           O  
ANISOU 1622  O   LYS A 300    12612  13401  13542   1347   -676   -306       O  
ATOM   1623  CB  LYS A 300      18.972  18.563  19.571  1.00103.20           C  
ANISOU 1623  CB  LYS A 300    12399  13136  13678   1051   -489   -521       C  
ATOM   1624  CG  LYS A 300      19.967  19.576  20.114  1.00106.99           C  
ANISOU 1624  CG  LYS A 300    12765  13761  14126    939   -606   -624       C  
ATOM   1625  CD  LYS A 300      21.324  19.445  19.441  1.00107.26           C  
ANISOU 1625  CD  LYS A 300    12575  13935  14244    925   -637   -633       C  
ATOM   1626  CE  LYS A 300      22.303  20.479  19.970  1.00111.39           C  
ANISOU 1626  CE  LYS A 300    12975  14607  14740    775   -767   -722       C  
ATOM   1627  NZ  LYS A 300      23.621  20.402  19.285  1.00112.04           N  
ANISOU 1627  NZ  LYS A 300    12805  14873  14893    740   -789   -719       N  
ATOM   1628  N   ALA A 301      17.403  15.864  20.499  1.00101.33           N  
ANISOU 1628  N   ALA A 301    12412  12757  13331   1343   -476   -221       N  
ATOM   1629  CA  ALA A 301      16.570  15.206  21.500  1.00101.73           C  
ANISOU 1629  CA  ALA A 301    12588  12806  13257   1393   -504    -91       C  
ATOM   1630  C   ALA A 301      17.265  13.979  22.076  1.00101.71           C  
ANISOU 1630  C   ALA A 301    12567  12847  13232   1539   -630     32       C  
ATOM   1631  O   ALA A 301      17.217  13.744  23.289  1.00103.55           O  
ANISOU 1631  O   ALA A 301    12835  13190  13319   1570   -717    114       O  
ATOM   1632  CB  ALA A 301      15.219  14.827  20.895  1.00 99.51           C  
ANISOU 1632  CB  ALA A 301    12438  12358  13012   1361   -387     -9       C  
ATOM   1633  N   HIS A 302      17.926  13.193  21.224  1.00100.48           N  
ANISOU 1633  N   HIS A 302    12355  12612  13210   1644   -649     43       N  
ATOM   1634  CA  HIS A 302      18.633  12.004  21.683  1.00100.95           C  
ANISOU 1634  CA  HIS A 302    12403  12684  13269   1815   -789    147       C  
ATOM   1635  C   HIS A 302      19.885  12.335  22.486  1.00103.15           C  
ANISOU 1635  C   HIS A 302    12529  13187  13477   1866   -914     91       C  
ATOM   1636  O   HIS A 302      20.476  11.425  23.078  1.00104.02           O  
ANISOU 1636  O   HIS A 302    12629  13334  13560   2015  -1052    185       O  
ATOM   1637  CB  HIS A 302      18.996  11.122  20.487  1.00 98.66           C  
ANISOU 1637  CB  HIS A 302    12096  12251  13141   1945   -781    135       C  
ATOM   1638  CG  HIS A 302      17.894  10.201  20.062  1.00 97.23           C  
ANISOU 1638  CG  HIS A 302    12102  11828  13014   1956   -749    256       C  
ATOM   1639  ND1 HIS A 302      17.245   9.358  20.940  1.00 98.21           N  
ANISOU 1639  ND1 HIS A 302    12378  11870  13066   1969   -834    448       N  
ATOM   1640  CD2 HIS A 302      17.315  10.002  18.854  1.00 94.87           C  
ANISOU 1640  CD2 HIS A 302    11861  11358  12827   1936   -650    221       C  
ATOM   1641  CE1 HIS A 302      16.321   8.674  20.289  1.00 96.13           C  
ANISOU 1641  CE1 HIS A 302    12258  11386  12880   1945   -797    528       C  
ATOM   1642  NE2 HIS A 302      16.343   9.046  19.022  1.00 94.06           N  
ANISOU 1642  NE2 HIS A 302    11944  11064  12730   1933   -686    383       N  
ATOM   1643  N   SER A 303      20.303  13.602  22.521  1.00105.95           N  
ANISOU 1643  N   SER A 303    12768  13682  13804   1741   -888    -55       N  
ATOM   1644  CA  SER A 303      21.435  14.000  23.348  1.00107.97           C  
ANISOU 1644  CA  SER A 303    12879  14163  13983   1756  -1020   -112       C  
ATOM   1645  C   SER A 303      21.110  13.968  24.835  1.00109.56           C  
ANISOU 1645  C   SER A 303    13168  14465  13995   1758  -1116    -34       C  
ATOM   1646  O   SER A 303      22.027  14.071  25.657  1.00111.41           O  
ANISOU 1646  O   SER A 303    13298  14888  14146   1798  -1252    -54       O  
ATOM   1647  CB  SER A 303      21.911  15.398  22.950  1.00109.03           C  
ANISOU 1647  CB  SER A 303    12886  14393  14148   1586   -982   -281       C  
ATOM   1648  OG  SER A 303      22.302  15.434  21.588  1.00108.31           O  
ANISOU 1648  OG  SER A 303    12688  14259  14208   1575   -894   -336       O  
ATOM   1649  N   HIS A 304      19.835  13.841  25.195  1.00106.58           N  
ANISOU 1649  N   HIS A 304    12965  13996  13534   1714  -1048     55       N  
ATOM   1650  CA  HIS A 304      19.400  13.676  26.572  1.00108.21           C  
ANISOU 1650  CA  HIS A 304    13257  14323  13534   1724  -1122    157       C  
ATOM   1651  C   HIS A 304      18.679  12.340  26.707  1.00107.55           C  
ANISOU 1651  C   HIS A 304    13311  14113  13440   1801  -1131    389       C  
ATOM   1652  O   HIS A 304      18.275  11.730  25.714  1.00105.98           O  
ANISOU 1652  O   HIS A 304    13170  13707  13391   1820  -1062    440       O  
ATOM   1653  CB  HIS A 304      18.479  14.823  27.007  1.00109.61           C  
ANISOU 1653  CB  HIS A 304    13502  14562  13584   1591  -1039     55       C  
ATOM   1654  CG  HIS A 304      18.980  16.182  26.622  1.00110.69           C  
ANISOU 1654  CG  HIS A 304    13549  14731  13776   1485  -1025   -172       C  
ATOM   1655  ND1 HIS A 304      19.723  16.971  27.473  1.00112.63           N  
ANISOU 1655  ND1 HIS A 304    13722  15161  13913   1451  -1146   -295       N  
ATOM   1656  CD2 HIS A 304      18.843  16.891  25.476  1.00110.16           C  
ANISOU 1656  CD2 HIS A 304    13463  14530  13862   1390   -921   -285       C  
ATOM   1657  CE1 HIS A 304      20.023  18.107  26.869  1.00113.11           C  
ANISOU 1657  CE1 HIS A 304    13729  15179  14068   1329  -1125   -470       C  
ATOM   1658  NE2 HIS A 304      19.501  18.084  25.656  1.00112.02           N  
ANISOU 1658  NE2 HIS A 304    13621  14853  14087   1290   -987   -460       N  
ATOM   1659  N   ALA A 305      18.516  11.886  27.948  1.00109.11           N  
ANISOU 1659  N   ALA A 305    13566  14438  13452   1833  -1230    537       N  
ATOM   1660  CA  ALA A 305      17.900  10.589  28.190  1.00108.83           C  
ANISOU 1660  CA  ALA A 305    13666  14288  13398   1880  -1272    795       C  
ATOM   1661  C   ALA A 305      17.132  10.615  29.503  1.00110.39           C  
ANISOU 1661  C   ALA A 305    13937  14673  13334   1816  -1289    935       C  
ATOM   1662  O   ALA A 305      17.346  11.477  30.359  1.00112.11           O  
ANISOU 1662  O   ALA A 305    14095  15128  13375   1790  -1311    826       O  
ATOM   1663  CB  ALA A 305      18.940   9.464  28.212  1.00108.07           C  
ANISOU 1663  CB  ALA A 305    13546  14125  13389   2055  -1446    901       C  
ATOM   1664  N   GLY A1001      16.226   9.643  29.646  1.00109.75           N  
ANISOU 1664  N   GLY A1001    13987  14492  13220   1785  -1286   1183       N  
ATOM   1665  CA  GLY A1001      15.463   9.486  30.865  1.00111.54           C  
ANISOU 1665  CA  GLY A1001    14274  14921  13184   1718  -1301   1368       C  
ATOM   1666  C   GLY A1001      15.345   8.022  31.236  1.00111.35           C  
ANISOU 1666  C   GLY A1001    14365  14788  13154   1745  -1437   1695       C  
ATOM   1667  O   GLY A1001      15.771   7.134  30.493  1.00110.91           O  
ANISOU 1667  O   GLY A1001    14363  14464  13314   1828  -1519   1758       O  
ATOM   1668  N   ILE A1002      14.751   7.784  32.403  1.00113.47           N  
ANISOU 1668  N   ILE A1002    14677  15272  13165   1676  -1468   1905       N  
ATOM   1669  CA  ILE A1002      14.635   6.443  32.958  1.00115.28           C  
ANISOU 1669  CA  ILE A1002    15024  15430  13349   1672  -1622   2257       C  
ATOM   1670  C   ILE A1002      13.163   6.073  33.076  1.00115.73           C  
ANISOU 1670  C   ILE A1002    15168  15502  13302   1487  -1522   2491       C  
ATOM   1671  O   ILE A1002      12.273   6.928  33.061  1.00115.09           O  
ANISOU 1671  O   ILE A1002    15031  15590  13107   1387  -1339   2382       O  
ATOM   1672  CB  ILE A1002      15.329   6.321  34.330  1.00116.27           C  
ANISOU 1672  CB  ILE A1002    15116  15828  13234   1741  -1784   2367       C  
ATOM   1673  CG1 ILE A1002      14.790   7.379  35.296  1.00117.16           C  
ANISOU 1673  CG1 ILE A1002    15149  16339  13029   1661  -1673   2274       C  
ATOM   1674  CG2 ILE A1002      16.832   6.452  34.179  1.00115.50           C  
ANISOU 1674  CG2 ILE A1002    14929  15696  13262   1925  -1918   2183       C  
ATOM   1675  CD1 ILE A1002      13.897   6.819  36.385  1.00118.59           C  
ANISOU 1675  CD1 ILE A1002    15390  16750  12920   1546  -1690   2603       C  
ATOM   1676  N   ASP A1003      12.916   4.772  33.194  1.00125.02           N  
ANISOU 1676  N   ASP A1003    16480  16498  14522   1442  -1656   2822       N  
ATOM   1677  CA  ASP A1003      11.584   4.264  33.496  1.00125.11           C  
ANISOU 1677  CA  ASP A1003    16568  16563  14406   1236  -1601   3117       C  
ATOM   1678  C   ASP A1003      11.343   4.414  34.993  1.00126.96           C  
ANISOU 1678  C   ASP A1003    16753  17220  14267   1174  -1622   3297       C  
ATOM   1679  O   ASP A1003      11.990   3.742  35.803  1.00127.81           O  
ANISOU 1679  O   ASP A1003    16909  17368  14284   1230  -1815   3499       O  
ATOM   1680  CB  ASP A1003      11.453   2.809  33.059  1.00124.62           C  
ANISOU 1680  CB  ASP A1003    16686  16122  14540   1191  -1769   3412       C  
ATOM   1681  CG  ASP A1003      10.136   2.192  33.481  1.00124.72           C  
ANISOU 1681  CG  ASP A1003    16773  16206  14410    941  -1747   3773       C  
ATOM   1682  OD1 ASP A1003       9.126   2.926  33.542  1.00124.55           O  
ANISOU 1682  OD1 ASP A1003    16652  16436  14234    806  -1540   3723       O  
ATOM   1683  OD2 ASP A1003      10.111   0.975  33.758  1.00124.99           O  
ANISOU 1683  OD2 ASP A1003    16960  16049  14482    877  -1945   4113       O  
ATOM   1684  N   CYS A1004      10.413   5.295  35.363  1.00124.47           N  
ANISOU 1684  N   CYS A1004    16338  17233  13724   1074  -1430   3220       N  
ATOM   1685  CA  CYS A1004      10.173   5.584  36.772  1.00125.87           C  
ANISOU 1685  CA  CYS A1004    16445  17871  13511   1039  -1426   3336       C  
ATOM   1686  C   CYS A1004       9.443   4.460  37.495  1.00126.53           C  
ANISOU 1686  C   CYS A1004    16606  18048  13421    861  -1508   3811       C  
ATOM   1687  O   CYS A1004       9.372   4.487  38.729  1.00127.32           O  
ANISOU 1687  O   CYS A1004    16659  18534  13184    834  -1542   3967       O  
ATOM   1688  CB  CYS A1004       9.381   6.885  36.910  1.00125.54           C  
ANISOU 1688  CB  CYS A1004    16271  18156  13274   1019  -1198   3079       C  
ATOM   1689  SG  CYS A1004      10.233   8.344  36.271  1.00124.94           S  
ANISOU 1689  SG  CYS A1004    16109  18012  13350   1198  -1126   2541       S  
ATOM   1690  N   SER A1005       8.894   3.503  36.744  1.00129.50           N  
ANISOU 1690  N   SER A1005    17100  18089  14014    729  -1546   4040       N  
ATOM   1691  CA  SER A1005       8.217   2.346  37.382  1.00129.76           C  
ANISOU 1691  CA  SER A1005    17227  18164  13912    521  -1657   4534       C  
ATOM   1692  C   SER A1005       9.236   1.575  38.221  1.00130.91           C  
ANISOU 1692  C   SER A1005    17466  18276  13998    612  -1918   4751       C  
ATOM   1693  O   SER A1005       8.932   1.293  39.393  1.00131.65           O  
ANISOU 1693  O   SER A1005    17541  18712  13769    504  -1967   5051       O  
ATOM   1694  CB  SER A1005       7.559   1.462  36.364  1.00128.75           C  
ANISOU 1694  CB  SER A1005    17230  17626  14064    367  -1689   4713       C  
ATOM   1695  OG  SER A1005       6.986   0.322  36.986  1.00129.75           O  
ANISOU 1695  OG  SER A1005    17462  17761  14078    145  -1831   5208       O  
ATOM   1696  N   PHE A1006      10.402   1.267  37.645  1.00130.10           N  
ANISOU 1696  N   PHE A1006    17446  17806  14182    812  -2077   4603       N  
ATOM   1697  CA  PHE A1006      11.422   0.526  38.376  1.00130.84           C  
ANISOU 1697  CA  PHE A1006    17625  17847  14243    931  -2341   4792       C  
ATOM   1698  C   PHE A1006      12.057   1.390  39.457  1.00131.75           C  
ANISOU 1698  C   PHE A1006    17592  18414  14052   1051  -2324   4638       C  
ATOM   1699  O   PHE A1006      12.409   0.892  40.532  1.00132.91           O  
ANISOU 1699  O   PHE A1006    17773  18743  13984   1055  -2492   4902       O  
ATOM   1700  CB  PHE A1006      12.484   0.005  37.410  1.00130.35           C  
ANISOU 1700  CB  PHE A1006    17664  17299  14565   1142  -2505   4640       C  
ATOM   1701  CG  PHE A1006      12.298  -1.435  37.020  1.00130.60           C  
ANISOU 1701  CG  PHE A1006    17923  16884  14815   1073  -2719   4976       C  
ATOM   1702  CD1 PHE A1006      11.080  -2.068  37.207  1.00130.63           C  
ANISOU 1702  CD1 PHE A1006    18022  16877  14734    785  -2712   5346       C  
ATOM   1703  CD2 PHE A1006      13.342  -2.156  36.464  1.00130.90           C  
ANISOU 1703  CD2 PHE A1006    18080  16517  15141   1299  -2940   4919       C  
ATOM   1704  CE1 PHE A1006      10.907  -3.392  36.848  1.00130.46           C  
ANISOU 1704  CE1 PHE A1006    18233  16411  14926    702  -2938   5657       C  
ATOM   1705  CE2 PHE A1006      13.176  -3.480  36.103  1.00130.61           C  
ANISOU 1705  CE2 PHE A1006    18279  16035  15313   1255  -3164   5206       C  
ATOM   1706  CZ  PHE A1006      11.956  -4.099  36.296  1.00130.31           C  
ANISOU 1706  CZ  PHE A1006    18358  15952  15202    946  -3172   5579       C  
ATOM   1707  N   TRP A1007      12.199   2.684  39.196  1.00123.89           N  
ANISOU 1707  N   TRP A1007    16445  17598  13031   1142  -2137   4219       N  
ATOM   1708  CA  TRP A1007      12.821   3.608  40.146  1.00124.60           C  
ANISOU 1708  CA  TRP A1007    16401  18092  12849   1258  -2130   4016       C  
ATOM   1709  C   TRP A1007      11.760   4.484  40.810  1.00125.07           C  
ANISOU 1709  C   TRP A1007    16345  18619  12558   1138  -1917   3965       C  
ATOM   1710  O   TRP A1007      11.798   5.716  40.774  1.00124.55           O  
ANISOU 1710  O   TRP A1007    16162  18745  12417   1215  -1774   3592       O  
ATOM   1711  CB  TRP A1007      13.886   4.447  39.444  1.00123.31           C  
ANISOU 1711  CB  TRP A1007    16156  17791  12907   1455  -2117   3574       C  
ATOM   1712  CG  TRP A1007      14.789   3.632  38.579  1.00122.29           C  
ANISOU 1712  CG  TRP A1007    16113  17214  13137   1586  -2282   3584       C  
ATOM   1713  CD1 TRP A1007      14.693   3.450  37.230  1.00121.28           C  
ANISOU 1713  CD1 TRP A1007    16034  16698  13350   1600  -2222   3463       C  
ATOM   1714  CD2 TRP A1007      15.922   2.870  39.007  1.00123.27           C  
ANISOU 1714  CD2 TRP A1007    16283  17250  13304   1742  -2541   3716       C  
ATOM   1715  NE1 TRP A1007      15.701   2.627  36.790  1.00120.86           N  
ANISOU 1715  NE1 TRP A1007    16050  16330  13542   1768  -2423   3495       N  
ATOM   1716  CE2 TRP A1007      16.469   2.257  37.863  1.00122.58           C  
ANISOU 1716  CE2 TRP A1007    16266  16720  13590   1863  -2624   3651       C  
ATOM   1717  CE3 TRP A1007      16.528   2.650  40.248  1.00124.84           C  
ANISOU 1717  CE3 TRP A1007    16465  17717  13251   1804  -2717   3878       C  
ATOM   1718  CZ2 TRP A1007      17.596   1.438  37.922  1.00123.37           C  
ANISOU 1718  CZ2 TRP A1007    16416  16636  13825   2062  -2876   3732       C  
ATOM   1719  CZ3 TRP A1007      17.645   1.837  40.305  1.00125.23           C  
ANISOU 1719  CZ3 TRP A1007    16567  17573  13442   1986  -2973   3976       C  
ATOM   1720  CH2 TRP A1007      18.168   1.241  39.149  1.00124.22           C  
ANISOU 1720  CH2 TRP A1007    16504  17001  13694   2122  -3050   3898       C  
ATOM   1721  N   ASN A1008      10.798   3.808  41.428  1.00128.75           N  
ANISOU 1721  N   ASN A1008    16848  19269  12803    948  -1909   4356       N  
ATOM   1722  CA  ASN A1008       9.746   4.455  42.193  1.00129.08           C  
ANISOU 1722  CA  ASN A1008    16766  19817  12460    839  -1721   4374       C  
ATOM   1723  C   ASN A1008      10.042   4.308  43.679  1.00131.08           C  
ANISOU 1723  C   ASN A1008    16985  20511  12306    850  -1836   4576       C  
ATOM   1724  O   ASN A1008      10.549   3.273  44.122  1.00131.23           O  
ANISOU 1724  O   ASN A1008    17112  20422  12328    826  -2056   4917       O  
ATOM   1725  CB  ASN A1008       8.380   3.851  41.865  1.00128.19           C  
ANISOU 1725  CB  ASN A1008    16677  19684  12343    593  -1611   4682       C  
ATOM   1726  CG  ASN A1008       7.244   4.806  42.149  1.00128.73           C  
ANISOU 1726  CG  ASN A1008    16580  20207  12124    532  -1352   4541       C  
ATOM   1727  OD1 ASN A1008       7.306   5.600  43.088  1.00129.47           O  
ANISOU 1727  OD1 ASN A1008    16560  20757  11874    625  -1293   4383       O  
ATOM   1728  ND2 ASN A1008       6.197   4.737  41.339  1.00128.16           N  
ANISOU 1728  ND2 ASN A1008    16492  20020  12183    389  -1203   4583       N  
ATOM   1729  N   GLU A1009       9.727   5.353  44.445  1.00138.55           N  
ANISOU 1729  N   GLU A1009    17790  21954  12898    899  -1696   4359       N  
ATOM   1730  CA  GLU A1009       9.986   5.333  45.879  1.00139.75           C  
ANISOU 1730  CA  GLU A1009    17894  22582  12621    923  -1790   4508       C  
ATOM   1731  C   GLU A1009       9.009   4.438  46.630  1.00140.43           C  
ANISOU 1731  C   GLU A1009    17984  22963  12408    694  -1785   5027       C  
ATOM   1732  O   GLU A1009       9.321   3.998  47.742  1.00141.36           O  
ANISOU 1732  O   GLU A1009    18110  23378  12224    677  -1925   5294       O  
ATOM   1733  CB  GLU A1009       9.930   6.757  46.435  1.00140.05           C  
ANISOU 1733  CB  GLU A1009    17789  23056  12368   1062  -1650   4078       C  
ATOM   1734  CG  GLU A1009      10.345   6.896  47.890  1.00141.72           C  
ANISOU 1734  CG  GLU A1009    17947  23769  12131   1128  -1756   4140       C  
ATOM   1735  CD  GLU A1009       9.162   6.978  48.842  1.00142.88           C  
ANISOU 1735  CD  GLU A1009    17986  24514  11788   1015  -1605   4333       C  
ATOM   1736  OE1 GLU A1009       8.053   6.538  48.474  1.00143.15           O  
ANISOU 1736  OE1 GLU A1009    18001  24554  11837    835  -1468   4579       O  
ATOM   1737  OE2 GLU A1009       9.346   7.476  49.971  1.00143.99           O  
ANISOU 1737  OE2 GLU A1009    18049  25144  11515   1107  -1628   4241       O  
ATOM   1738  N   SER A1010       7.846   4.146  46.039  1.00141.82           N  
ANISOU 1738  N   SER A1010    18151  23073  12661    503  -1635   5193       N  
ATOM   1739  CA  SER A1010       6.794   3.416  46.739  1.00142.17           C  
ANISOU 1739  CA  SER A1010    18161  23463  12395    250  -1601   5681       C  
ATOM   1740  C   SER A1010       7.268   2.082  47.301  1.00142.72           C  
ANISOU 1740  C   SER A1010    18381  23397  12449    131  -1874   6196       C  
ATOM   1741  O   SER A1010       6.641   1.551  48.224  1.00143.27           O  
ANISOU 1741  O   SER A1010    18412  23862  12162    -63  -1887   6619       O  
ATOM   1742  CB  SER A1010       5.611   3.178  45.798  1.00140.89           C  
ANISOU 1742  CB  SER A1010    17984  23128  12421     51  -1441   5788       C  
ATOM   1743  OG  SER A1010       5.224   4.376  45.146  1.00140.24           O  
ANISOU 1743  OG  SER A1010    17785  23093  12408    179  -1213   5309       O  
ATOM   1744  N   TYR A1011       8.364   1.537  46.781  1.00130.15           N  
ANISOU 1744  N   TYR A1011    16954  21274  11223    249  -2097   6175       N  
ATOM   1745  CA  TYR A1011       8.815   0.205  47.158  1.00129.94           C  
ANISOU 1745  CA  TYR A1011    17102  21017  11251    157  -2385   6659       C  
ATOM   1746  C   TYR A1011       9.635   0.184  48.442  1.00131.70           C  
ANISOU 1746  C   TYR A1011    17308  21592  11138    268  -2551   6764       C  
ATOM   1747  O   TYR A1011      10.071  -0.896  48.855  1.00132.18           O  
ANISOU 1747  O   TYR A1011    17520  21455  11246    214  -2798   7133       O  
ATOM   1748  CB  TYR A1011       9.634  -0.407  46.021  1.00128.90           C  
ANISOU 1748  CB  TYR A1011    17154  20167  11657    272  -2564   6576       C  
ATOM   1749  CG  TYR A1011       8.902  -0.466  44.700  1.00127.10           C  
ANISOU 1749  CG  TYR A1011    16962  19554  11775    170  -2429   6475       C  
ATOM   1750  CD1 TYR A1011       7.515  -0.548  44.647  1.00126.53           C  
ANISOU 1750  CD1 TYR A1011    16828  19683  11566   -101  -2255   6689       C  
ATOM   1751  CD2 TYR A1011       9.599  -0.419  43.506  1.00126.28           C  
ANISOU 1751  CD2 TYR A1011    16940  18924  12118    346  -2473   6162       C  
ATOM   1752  CE1 TYR A1011       6.851  -0.595  43.435  1.00124.85           C  
ANISOU 1752  CE1 TYR A1011    16645  19128  11666   -195  -2142   6593       C  
ATOM   1753  CE2 TYR A1011       8.948  -0.466  42.294  1.00125.07           C  
ANISOU 1753  CE2 TYR A1011    16821  18433  12265    259  -2356   6062       C  
ATOM   1754  CZ  TYR A1011       7.576  -0.553  42.262  1.00124.13           C  
ANISOU 1754  CZ  TYR A1011    16651  18497  12015    -11  -2196   6276       C  
ATOM   1755  OH  TYR A1011       6.937  -0.597  41.048  1.00122.02           O  
ANISOU 1755  OH  TYR A1011    16417  17901  12046    -97  -2091   6173       O  
ATOM   1756  N   LEU A1012       9.866   1.331  49.076  1.00138.17           N  
ANISOU 1756  N   LEU A1012    17965  22877  11658    428  -2428   6405       N  
ATOM   1757  CA  LEU A1012      10.577   1.338  50.346  1.00139.43           C  
ANISOU 1757  CA  LEU A1012    18097  23421  11457    522  -2584   6503       C  
ATOM   1758  C   LEU A1012       9.718   0.693  51.426  1.00142.23           C  
ANISOU 1758  C   LEU A1012    18437  24081  11524    274  -2530   6860       C  
ATOM   1759  O   LEU A1012       8.555   1.062  51.612  1.00142.38           O  
ANISOU 1759  O   LEU A1012    18321  24439  11339    124  -2282   6844       O  
ATOM   1760  CB  LEU A1012      10.952   2.762  50.750  1.00139.80           C  
ANISOU 1760  CB  LEU A1012    17981  23856  11280    739  -2454   5968       C  
ATOM   1761  CG  LEU A1012      11.860   2.865  51.980  1.00140.32           C  
ANISOU 1761  CG  LEU A1012    18021  24286  11009    872  -2636   5988       C  
ATOM   1762  CD1 LEU A1012      13.132   2.052  51.783  1.00140.67           C  
ANISOU 1762  CD1 LEU A1012    18212  23876  11362    986  -2944   6117       C  
ATOM   1763  CD2 LEU A1012      12.191   4.316  52.295  1.00140.35           C  
ANISOU 1763  CD2 LEU A1012    17880  24627  10819   1074  -2519   5423       C  
ATOM   1764  N   THR A1013      10.293  -0.274  52.135  1.00146.17           N  
ANISOU 1764  N   THR A1013    19064  24445  12028    239  -2757   7155       N  
ATOM   1765  CA  THR A1013       9.602  -1.004  53.196  1.00150.33           C  
ANISOU 1765  CA  THR A1013    19590  25210  12319      1  -2736   7507       C  
ATOM   1766  C   THR A1013      10.288  -0.665  54.515  1.00153.40           C  
ANISOU 1766  C   THR A1013    19914  26030  12341    133  -2814   7435       C  
ATOM   1767  O   THR A1013      11.045  -1.464  55.067  1.00156.73           O  
ANISOU 1767  O   THR A1013    20469  26288  12792    159  -3057   7662       O  
ATOM   1768  CB  THR A1013       9.605  -2.509  52.924  1.00152.47           C  
ANISOU 1768  CB  THR A1013    20088  24936  12908   -173  -2946   7939       C  
ATOM   1769  OG1 THR A1013      10.911  -2.914  52.499  1.00151.60           O  
ANISOU 1769  OG1 THR A1013    20149  24362  13089     50  -3228   7905       O  
ATOM   1770  CG2 THR A1013       8.600  -2.853  51.832  1.00150.53           C  
ANISOU 1770  CG2 THR A1013    19876  24374  12946   -378  -2825   8034       C  
ATOM   1771  N   GLY A1014      10.014   0.532  55.028  1.00154.18           N  
ANISOU 1771  N   GLY A1014    19813  26679  12091    228  -2613   7100       N  
ATOM   1772  CA  GLY A1014      10.646   1.006  56.248  1.00157.26           C  
ANISOU 1772  CA  GLY A1014    20129  27500  12122    368  -2673   6961       C  
ATOM   1773  C   GLY A1014      10.923   2.501  56.216  1.00155.07           C  
ANISOU 1773  C   GLY A1014    19703  27554  11664    607  -2549   6416       C  
ATOM   1774  O   GLY A1014      10.897   3.121  55.147  1.00151.05           O  
ANISOU 1774  O   GLY A1014    19174  26860  11359    703  -2469   6147       O  
ATOM   1775  N   SER A1015      11.195   3.095  57.375  1.00160.74           N  
ANISOU 1775  N   SER A1015    20323  28749  12004    708  -2543   6237       N  
ATOM   1776  CA  SER A1015      11.451   4.524  57.448  1.00159.10           C  
ANISOU 1776  CA  SER A1015    19989  28850  11611    934  -2445   5691       C  
ATOM   1777  C   SER A1015      12.764   4.866  56.749  1.00155.49           C  
ANISOU 1777  C   SER A1015    19605  28059  11416   1153  -2653   5437       C  
ATOM   1778  O   SER A1015      13.536   3.991  56.348  1.00154.88           O  
ANISOU 1778  O   SER A1015    19659  27558  11629   1157  -2878   5682       O  
ATOM   1779  CB  SER A1015      11.483   4.987  58.903  1.00162.96           C  
ANISOU 1779  CB  SER A1015    20374  29897  11646    988  -2421   5571       C  
ATOM   1780  OG  SER A1015      11.667   6.389  58.978  1.00161.72           O  
ANISOU 1780  OG  SER A1015    20114  30011  11323   1205  -2334   5014       O  
ATOM   1781  N   ARG A1016      13.012   6.170  56.605  1.00147.02           N  
ANISOU 1781  N   ARG A1016    18438  27178  10245   1346  -2582   4921       N  
ATOM   1782  CA  ARG A1016      14.232   6.616  55.945  1.00144.25           C  
ANISOU 1782  CA  ARG A1016    18119  26561  10128   1548  -2768   4638       C  
ATOM   1783  C   ARG A1016      15.463   6.263  56.767  1.00146.63           C  
ANISOU 1783  C   ARG A1016    18459  26884  10370   1637  -3043   4705       C  
ATOM   1784  O   ARG A1016      16.468   5.801  56.217  1.00145.22           O  
ANISOU 1784  O   ARG A1016    18345  26340  10490   1724  -3263   4778       O  
ATOM   1785  CB  ARG A1016      14.169   8.121  55.690  1.00142.07           C  
ANISOU 1785  CB  ARG A1016    17744  26492   9744   1714  -2641   4057       C  
ATOM   1786  N   ASP A1017      15.406   6.476  58.083  1.00152.97           N  
ANISOU 1786  N   ASP A1017    19211  28121  10790   1630  -3036   4674       N  
ATOM   1787  CA  ASP A1017      16.559   6.183  58.927  1.00155.82           C  
ANISOU 1787  CA  ASP A1017    19603  28535  11067   1714  -3297   4728       C  
ATOM   1788  C   ASP A1017      16.689   4.691  59.208  1.00158.29           C  
ANISOU 1788  C   ASP A1017    20042  28617  11485   1583  -3454   5293       C  
ATOM   1789  O   ASP A1017      17.804   4.160  59.246  1.00158.89           O  
ANISOU 1789  O   ASP A1017    20186  28461  11723   1676  -3720   5399       O  
ATOM   1790  CB  ASP A1017      16.461   6.963  60.238  1.00159.22           C  
ANISOU 1790  CB  ASP A1017    19940  29509  11045   1761  -3240   4481       C  
ATOM   1791  CG  ASP A1017      15.080   6.893  60.855  1.00161.55           C  
ANISOU 1791  CG  ASP A1017    20175  30163  11044   1608  -2983   4633       C  
ATOM   1792  OD1 ASP A1017      14.827   5.957  61.644  1.00164.93           O  
ANISOU 1792  OD1 ASP A1017    20635  30705  11325   1466  -3018   5051       O  
ATOM   1793  OD2 ASP A1017      14.248   7.773  60.553  1.00160.08           O  
ANISOU 1793  OD2 ASP A1017    19901  30148  10774   1635  -2750   4331       O  
ATOM   1794  N   GLU A1018      15.564   3.996  59.399  1.00159.71           N  
ANISOU 1794  N   GLU A1018    20251  28845  11586   1368  -3304   5651       N  
ATOM   1795  CA  GLU A1018      15.626   2.584  59.765  1.00162.67           C  
ANISOU 1795  CA  GLU A1018    20764  29003  12040   1225  -3464   6184       C  
ATOM   1796  C   GLU A1018      16.054   1.718  58.586  1.00160.04           C  
ANISOU 1796  C   GLU A1018    20579  28034  12194   1234  -3623   6391       C  
ATOM   1797  O   GLU A1018      16.888   0.819  58.745  1.00161.66           O  
ANISOU 1797  O   GLU A1018    20912  27959  12554   1281  -3887   6637       O  
ATOM   1798  CB  GLU A1018      14.277   2.118  60.310  1.00166.00           C  
ANISOU 1798  CB  GLU A1018    21157  29673  12241    973  -3260   6496       C  
ATOM   1799  CG  GLU A1018      14.299   0.703  60.865  1.00170.16           C  
ANISOU 1799  CG  GLU A1018    21828  30028  12796    808  -3430   7039       C  
ATOM   1800  CD  GLU A1018      15.335   0.523  61.959  1.00173.58           C  
ANISOU 1800  CD  GLU A1018    22296  30628  13027    924  -3665   7083       C  
ATOM   1801  OE1 GLU A1018      15.265   1.249  62.973  1.00175.65           O  
ANISOU 1801  OE1 GLU A1018    22428  31419  12892    968  -3581   6887       O  
ATOM   1802  OE2 GLU A1018      16.220  -0.344  61.804  1.00174.08           O  
ANISOU 1802  OE2 GLU A1018    22518  30292  13333    984  -3940   7302       O  
ATOM   1803  N   ARG A1019      15.490   1.964  57.399  1.00155.35           N  
ANISOU 1803  N   ARG A1019    19974  27204  11849   1202  -3472   6289       N  
ATOM   1804  CA  ARG A1019      15.923   1.224  56.216  1.00152.66           C  
ANISOU 1804  CA  ARG A1019    19765  26256  11982   1237  -3621   6437       C  
ATOM   1805  C   ARG A1019      17.410   1.421  55.955  1.00151.17           C  
ANISOU 1805  C   ARG A1019    19574  25884  11978   1502  -3870   6221       C  
ATOM   1806  O   ARG A1019      18.065   0.541  55.387  1.00150.51           O  
ANISOU 1806  O   ARG A1019    19616  25331  12241   1572  -4082   6410       O  
ATOM   1807  CB  ARG A1019      15.109   1.650  54.994  1.00147.41           C  
ANISOU 1807  CB  ARG A1019    19063  25425  11522   1181  -3405   6299       C  
ATOM   1808  N   LYS A1020      17.946   2.545  56.424  1.00153.77           N  
ANISOU 1808  N   LYS A1020    19761  26589  12076   1652  -3854   5820       N  
ATOM   1809  CA  LYS A1020      19.403   2.789  56.291  1.00153.31           C  
ANISOU 1809  CA  LYS A1020    19664  26421  12167   1892  -4096   5595       C  
ATOM   1810  C   LYS A1020      20.115   1.858  57.268  1.00157.88           C  
ANISOU 1810  C   LYS A1020    20335  26984  12668   1911  -4351   5897       C  
ATOM   1811  O   LYS A1020      20.919   1.031  56.808  1.00158.06           O  
ANISOU 1811  O   LYS A1020    20449  26596  13009   2018  -4581   6063       O  
ATOM   1812  CB  LYS A1020      19.697   4.242  56.673  1.00152.58           C  
ANISOU 1812  CB  LYS A1020    19405  26754  11815   2008  -4017   5084       C  
ATOM   1813  CG  LYS A1020      21.077   4.763  56.303  1.00151.31           C  
ANISOU 1813  CG  LYS A1020    19159  26498  11835   2233  -4215   4758       C  
ATOM   1814  CD  LYS A1020      21.392   6.087  56.959  1.00151.54           C  
ANISOU 1814  CD  LYS A1020    19057  26952  11569   2309  -4184   4287       C  
ATOM   1815  CE  LYS A1020      20.257   7.082  56.846  1.00149.82           C  
ANISOU 1815  CE  LYS A1020    18794  26971  11160   2234  -3891   4009       C  
ATOM   1816  NZ  LYS A1020      20.542   8.324  57.603  1.00150.77           N  
ANISOU 1816  NZ  LYS A1020    18819  27489  10977   2314  -3888   3551       N  
ATOM   1817  N   LYS A1021      19.785   1.962  58.556  1.00160.50           N  
ANISOU 1817  N   LYS A1021    20647  27746  12592   1818  -4308   5968       N  
ATOM   1818  CA  LYS A1021      20.455   1.178  59.591  1.00165.02           C  
ANISOU 1818  CA  LYS A1021    21299  28362  13037   1840  -4546   6235       C  
ATOM   1819  C   LYS A1021      20.596  -0.291  59.210  1.00166.37           C  
ANISOU 1819  C   LYS A1021    21670  28019  13523   1804  -4736   6686       C  
ATOM   1820  O   LYS A1021      21.676  -0.877  59.338  1.00168.08           O  
ANISOU 1820  O   LYS A1021    21954  28021  13887   1960  -5016   6776       O  
ATOM   1821  CB  LYS A1021      19.695   1.283  60.916  1.00168.88           C  
ANISOU 1821  CB  LYS A1021    21759  29351  13056   1684  -4417   6353       C  
ATOM   1822  CG  LYS A1021      19.432   2.684  61.433  1.00168.37           C  
ANISOU 1822  CG  LYS A1021    21519  29809  12644   1724  -4227   5908       C  
ATOM   1823  CD  LYS A1021      18.419   2.630  62.569  1.00171.99           C  
ANISOU 1823  CD  LYS A1021    21945  30723  12680   1553  -4055   6080       C  
ATOM   1824  CE  LYS A1021      17.847   3.998  62.892  1.00171.36           C  
ANISOU 1824  CE  LYS A1021    21702  31115  12292   1590  -3812   5631       C  
ATOM   1825  NZ  LYS A1021      16.757   3.900  63.902  1.00175.03           N  
ANISOU 1825  NZ  LYS A1021    22110  32028  12368   1431  -3620   5807       N  
ATOM   1826  N   SER A1022      19.508  -0.898  58.731  1.00166.82           N  
ANISOU 1826  N   SER A1022    21826  27863  13694   1605  -4592   6957       N  
ATOM   1827  CA  SER A1022      19.502  -2.335  58.472  1.00168.83           C  
ANISOU 1827  CA  SER A1022    22300  27625  14222   1543  -4769   7391       C  
ATOM   1828  C   SER A1022      20.471  -2.703  57.354  1.00166.21           C  
ANISOU 1828  C   SER A1022    22039  26757  14357   1766  -4976   7307       C  
ATOM   1829  O   SER A1022      21.220  -3.680  57.463  1.00168.65           O  
ANISOU 1829  O   SER A1022    22495  26742  14841   1882  -5249   7520       O  
ATOM   1830  CB  SER A1022      18.085  -2.797  58.133  1.00168.79           C  
ANISOU 1830  CB  SER A1022    22365  27519  14251   1262  -4557   7650       C  
ATOM   1831  OG  SER A1022      17.147  -2.270  59.055  1.00170.94           O  
ANISOU 1831  OG  SER A1022    22512  28345  14093   1080  -4324   7656       O  
ATOM   1832  N   LEU A1023      20.466  -1.934  56.262  1.00160.57           N  
ANISOU 1832  N   LEU A1023    21214  25948  13848   1845  -4849   6989       N  
ATOM   1833  CA  LEU A1023      21.383  -2.212  55.161  1.00157.76           C  
ANISOU 1833  CA  LEU A1023    20886  25123  13931   2070  -5024   6881       C  
ATOM   1834  C   LEU A1023      22.831  -2.023  55.596  1.00158.87           C  
ANISOU 1834  C   LEU A1023    20940  25364  14060   2333  -5270   6703       C  
ATOM   1835  O   LEU A1023      23.700  -2.845  55.280  1.00159.92           O  
ANISOU 1835  O   LEU A1023    21167  25116  14479   2517  -5525   6806       O  
ATOM   1836  CB  LEU A1023      21.054  -1.321  53.964  1.00152.37           C  
ANISOU 1836  CB  LEU A1023    20075  24389  13428   2094  -4817   6567       C  
ATOM   1837  CG  LEU A1023      19.749  -1.645  53.232  1.00150.46           C  
ANISOU 1837  CG  LEU A1023    19930  23919  13318   1866  -4613   6742       C  
ATOM   1838  CD1 LEU A1023      19.803  -1.107  51.814  1.00145.93           C  
ANISOU 1838  CD1 LEU A1023    19288  23060  13099   1962  -4494   6428       C  
ATOM   1839  CD2 LEU A1023      19.480  -3.140  53.231  1.00153.37           C  
ANISOU 1839  CD2 LEU A1023    20553  23835  13885   1759  -4767   7178       C  
ATOM   1840  N   LEU A1024      23.113  -0.931  56.314  1.00150.56           N  
ANISOU 1840  N   LEU A1024    19703  24821  12682   2363  -5202   6411       N  
ATOM   1841  CA  LEU A1024      24.420  -0.788  56.949  1.00152.19           C  
ANISOU 1841  CA  LEU A1024    19826  25179  12821   2565  -5441   6274       C  
ATOM   1842  C   LEU A1024      24.682  -1.918  57.930  1.00158.60           C  
ANISOU 1842  C   LEU A1024    20810  25922  13529   2552  -5669   6662       C  
ATOM   1843  O   LEU A1024      25.823  -2.372  58.071  1.00160.69           O  
ANISOU 1843  O   LEU A1024    21086  26041  13926   2758  -5944   6678       O  
ATOM   1844  CB  LEU A1024      24.536   0.562  57.657  1.00151.28           C  
ANISOU 1844  CB  LEU A1024    19513  25624  12343   2558  -5324   5898       C  
ATOM   1845  CG  LEU A1024      24.972   1.750  56.807  1.00146.97           C  
ANISOU 1845  CG  LEU A1024    18771  25142  11930   2684  -5235   5415       C  
ATOM   1846  CD1 LEU A1024      23.747   2.417  56.199  1.00143.64           C  
ANISOU 1846  CD1 LEU A1024    18330  24786  11462   2538  -4922   5287       C  
ATOM   1847  CD2 LEU A1024      25.777   2.737  57.628  1.00147.48           C  
ANISOU 1847  CD2 LEU A1024    18673  25629  11735   2766  -5309   5065       C  
ATOM   1848  N   SER A1025      23.637  -2.388  58.610  1.00175.09           N  
ANISOU 1848  N   SER A1025    23023  28123  15380   2317  -5559   6975       N  
ATOM   1849  CA  SER A1025      23.814  -3.435  59.606  1.00180.33           C  
ANISOU 1849  CA  SER A1025    23852  28755  15909   2289  -5762   7355       C  
ATOM   1850  C   SER A1025      24.300  -4.735  58.988  1.00181.44           C  
ANISOU 1850  C   SER A1025    24204  28288  16449   2423  -6013   7614       C  
ATOM   1851  O   SER A1025      24.919  -5.543  59.682  1.00185.63           O  
ANISOU 1851  O   SER A1025    24854  28736  16939   2520  -6265   7839       O  
ATOM   1852  CB  SER A1025      22.510  -3.680  60.368  1.00182.85           C  
ANISOU 1852  CB  SER A1025    24240  29323  15911   1990  -5566   7645       C  
ATOM   1853  OG  SER A1025      22.228  -2.612  61.257  1.00183.47           O  
ANISOU 1853  OG  SER A1025    24140  30011  15558   1917  -5393   7424       O  
ATOM   1854  N   LYS A1026      24.027  -4.966  57.702  1.00169.83           N  
ANISOU 1854  N   LYS A1026    22786  26383  15357   2446  -5953   7579       N  
ATOM   1855  CA  LYS A1026      24.460  -6.213  57.077  1.00170.37           C  
ANISOU 1855  CA  LYS A1026    23068  25852  15812   2600  -6185   7788       C  
ATOM   1856  C   LYS A1026      25.980  -6.332  57.079  1.00171.24           C  
ANISOU 1856  C   LYS A1026    23124  25866  16073   2948  -6481   7627       C  
ATOM   1857  O   LYS A1026      26.524  -7.436  57.204  1.00174.63           O  
ANISOU 1857  O   LYS A1026    23736  25962  16652   3114  -6737   7845       O  
ATOM   1858  CB  LYS A1026      23.908  -6.311  55.653  1.00166.36           C  
ANISOU 1858  CB  LYS A1026    22605  24925  15680   2571  -6052   7719       C  
ATOM   1859  CG  LYS A1026      23.901  -7.725  55.087  1.00167.69           C  
ANISOU 1859  CG  LYS A1026    23044  24472  16200   2643  -6223   7992       C  
ATOM   1860  CD  LYS A1026      22.976  -8.639  55.878  1.00171.87           C  
ANISOU 1860  CD  LYS A1026    23777  24977  16551   2374  -6209   8430       C  
ATOM   1861  CE  LYS A1026      22.950 -10.042  55.292  1.00173.27           C  
ANISOU 1861  CE  LYS A1026    24222  24524  17088   2437  -6373   8683       C  
ATOM   1862  NZ  LYS A1026      22.090 -10.970  56.078  1.00177.47           N  
ANISOU 1862  NZ  LYS A1026    24941  25029  17461   2155  -6379   9129       N  
ATOM   1863  N   PHE A1027      26.638  -5.172  57.052  1.00168.46           N  
ANISOU 1863  N   PHE A1027    22509  25855  15642   3051  -6440   7247       N  
ATOM   1864  CA  PHE A1027      28.119  -5.166  57.111  1.00169.37           C  
ANISOU 1864  CA  PHE A1027    22516  25955  15882   3359  -6711   7066       C  
ATOM   1865  C   PHE A1027      28.578  -4.137  58.139  1.00170.63           C  
ANISOU 1865  C   PHE A1027    22461  26703  15667   3329  -6694   6851       C  
ATOM   1866  O   PHE A1027      29.155  -4.554  59.156  1.00174.76           O  
ANISOU 1866  O   PHE A1027    23034  27358  16009   3392  -6908   6998       O  
ATOM   1867  CB  PHE A1027      28.713  -4.863  55.735  1.00165.03           C  
ANISOU 1867  CB  PHE A1027    21829  25134  15742   3567  -6709   6764       C  
ATOM   1868  CG  PHE A1027      30.219  -4.811  55.697  1.00166.15           C  
ANISOU 1868  CG  PHE A1027    21808  25284  16036   3870  -6962   6555       C  
ATOM   1869  CD1 PHE A1027      30.972  -5.970  55.796  1.00169.37           C  
ANISOU 1869  CD1 PHE A1027    22374  25348  16631   4101  -7277   6744       C  
ATOM   1870  CD2 PHE A1027      30.886  -3.605  55.555  1.00163.46           C  
ANISOU 1870  CD2 PHE A1027    21154  25300  15655   3932  -6882   6154       C  
ATOM   1871  CE1 PHE A1027      32.356  -5.922  55.759  1.00170.11           C  
ANISOU 1871  CE1 PHE A1027    22288  25469  16879   4365  -7511   6554       C  
ATOM   1872  CE2 PHE A1027      32.270  -3.559  55.521  1.00164.46           C  
ANISOU 1872  CE2 PHE A1027    21099  25459  15930   4182  -7097   5965       C  
ATOM   1873  CZ  PHE A1027      33.003  -4.717  55.621  1.00167.43           C  
ANISOU 1873  CZ  PHE A1027    21602  25509  16503   4389  -7408   6174       C  
ATOM   1874  N   GLY A1028      28.305  -2.849  57.901  1.00173.53           N  
ANISOU 1874  N   GLY A1028    22613  27405  15914   3243  -6452   6508       N  
ATOM   1875  CA  GLY A1028      28.839  -1.824  58.786  1.00174.91           C  
ANISOU 1875  CA  GLY A1028    22587  28103  15767   3246  -6450   6236       C  
ATOM   1876  C   GLY A1028      28.374  -1.970  60.222  1.00179.41           C  
ANISOU 1876  C   GLY A1028    23249  29024  15895   3081  -6452   6461       C  
ATOM   1877  O   GLY A1028      29.160  -1.797  61.156  1.00183.05           O  
ANISOU 1877  O   GLY A1028    23639  29762  16150   3155  -6618   6404       O  
ATOM   1878  N   MET A1029      27.094  -2.296  60.415  1.00182.58           N  
ANISOU 1878  N   MET A1029    23794  29432  16145   2852  -6263   6720       N  
ATOM   1879  CA  MET A1029      26.509  -2.468  61.747  1.00186.95           C  
ANISOU 1879  CA  MET A1029    24422  30340  16269   2675  -6225   6955       C  
ATOM   1880  C   MET A1029      26.663  -1.203  62.588  1.00188.18           C  
ANISOU 1880  C   MET A1029    24378  31082  16041   2650  -6123   6613       C  
ATOM   1881  O   MET A1029      26.918  -1.261  63.792  1.00192.17           O  
ANISOU 1881  O   MET A1029    24888  31904  16225   2633  -6226   6703       O  
ATOM   1882  CB  MET A1029      27.107  -3.680  62.467  1.00191.42           C  
ANISOU 1882  CB  MET A1029    25166  30732  16833   2761  -6531   7324       C  
ATOM   1883  N   ASP A1030      26.508  -0.049  61.945  1.00184.60           N  
ANISOU 1883  N   ASP A1030    23756  30762  15622   2655  -5927   6205       N  
ATOM   1884  CA  ASP A1030      26.607   1.231  62.629  1.00184.45           C  
ANISOU 1884  CA  ASP A1030    23564  31252  15267   2643  -5826   5820       C  
ATOM   1885  C   ASP A1030      25.723   2.242  61.916  1.00179.73           C  
ANISOU 1885  C   ASP A1030    22877  30749  14663   2558  -5518   5513       C  
ATOM   1886  O   ASP A1030      25.306   2.036  60.773  1.00176.40           O  
ANISOU 1886  O   ASP A1030    22490  29988  14546   2545  -5418   5550       O  
ATOM   1887  CB  ASP A1030      28.057   1.726  62.691  1.00184.30           C  
ANISOU 1887  CB  ASP A1030    23397  31292  15337   2843  -6054   5515       C  
ATOM   1888  CG  ASP A1030      28.828   1.435  61.419  1.00181.42           C  
ANISOU 1888  CG  ASP A1030    22989  30484  15457   3015  -6174   5444       C  
ATOM   1889  OD1 ASP A1030      28.207   1.409  60.336  1.00177.56           O  
ANISOU 1889  OD1 ASP A1030    22529  29727  15210   2982  -6011   5436       O  
ATOM   1890  OD2 ASP A1030      30.058   1.232  61.504  1.00182.84           O  
ANISOU 1890  OD2 ASP A1030    23097  30599  15775   3187  -6429   5391       O  
ATOM   1891  N   GLU A1031      25.436   3.339  62.609  1.00171.46           N  
ANISOU 1891  N   GLU A1031    21722  30160  13263   2511  -5378   5200       N  
ATOM   1892  CA  GLU A1031      24.622   4.422  62.066  1.00167.15           C  
ANISOU 1892  CA  GLU A1031    21093  29748  12668   2456  -5100   4854       C  
ATOM   1893  C   GLU A1031      25.534   5.582  61.690  1.00164.67           C  
ANISOU 1893  C   GLU A1031    20626  29496  12446   2597  -5167   4335       C  
ATOM   1894  O   GLU A1031      26.164   6.195  62.559  1.00166.45           O  
ANISOU 1894  O   GLU A1031    20777  30027  12441   2645  -5275   4102       O  
ATOM   1895  CB  GLU A1031      23.554   4.868  63.063  1.00169.12           C  
ANISOU 1895  CB  GLU A1031    21337  30453  12467   2318  -4884   4835       C  
ATOM   1896  CG  GLU A1031      22.527   3.801  63.398  1.00171.16           C  
ANISOU 1896  CG  GLU A1031    21720  30684  12628   2140  -4783   5335       C  
ATOM   1897  CD  GLU A1031      21.361   4.351  64.197  1.00172.48           C  
ANISOU 1897  CD  GLU A1031    21834  31321  12380   2012  -4519   5270       C  
ATOM   1898  OE1 GLU A1031      21.107   5.571  64.116  1.00170.63           O  
ANISOU 1898  OE1 GLU A1031    21490  31324  12018   2064  -4362   4820       O  
ATOM   1899  OE2 GLU A1031      20.695   3.563  64.902  1.00175.64           O  
ANISOU 1899  OE2 GLU A1031    22299  31850  12587   1864  -4473   5662       O  
ATOM   1900  N   GLY A1032      25.601   5.879  60.397  1.00163.81           N  
ANISOU 1900  N   GLY A1032    20470  29094  12677   2652  -5107   4157       N  
ATOM   1901  CA  GLY A1032      26.374   7.006  59.918  1.00160.98           C  
ANISOU 1901  CA  GLY A1032    19964  28768  12432   2757  -5153   3662       C  
ATOM   1902  C   GLY A1032      25.983   7.337  58.499  1.00155.81           C  
ANISOU 1902  C   GLY A1032    19284  27830  12087   2770  -5002   3509       C  
ATOM   1903  O   GLY A1032      25.329   6.545  57.812  1.00154.44           O  
ANISOU 1903  O   GLY A1032    19202  27379  12098   2726  -4907   3815       O  
ATOM   1904  N   VAL A1033      26.386   8.530  58.063  1.00150.09           N  
ANISOU 1904  N   VAL A1033    18439  27167  11420   2822  -4988   3027       N  
ATOM   1905  CA  VAL A1033      26.099   8.959  56.700  1.00146.51           C  
ANISOU 1905  CA  VAL A1033    17980  26300  11386   2785  -4791   2789       C  
ATOM   1906  C   VAL A1033      26.841   8.054  55.728  1.00145.96           C  
ANISOU 1906  C   VAL A1033    17903  25759  11796   2863  -4894   2971       C  
ATOM   1907  O   VAL A1033      28.028   7.750  55.915  1.00146.74           O  
ANISOU 1907  O   VAL A1033    17914  25868  11972   2986  -5145   2999       O  
ATOM   1908  CB  VAL A1033      26.483  10.432  56.505  1.00145.63           C  
ANISOU 1908  CB  VAL A1033    17769  26250  11314   2778  -4757   2214       C  
ATOM   1909  CG1 VAL A1033      25.441  11.327  57.150  1.00145.32           C  
ANISOU 1909  CG1 VAL A1033    17774  26562  10879   2713  -4586   2000       C  
ATOM   1910  CG2 VAL A1033      27.862  10.705  57.087  1.00146.58           C  
ANISOU 1910  CG2 VAL A1033    17762  26568  11366   2868  -5053   2061       C  
ATOM   1911  N   THR A1034      26.142   7.606  54.690  1.00144.17           N  
ANISOU 1911  N   THR A1034    17763  25132  11883   2806  -4706   3091       N  
ATOM   1912  CA  THR A1034      26.683   6.634  53.750  1.00143.78           C  
ANISOU 1912  CA  THR A1034    17736  24626  12270   2894  -4791   3285       C  
ATOM   1913  C   THR A1034      26.754   7.243  52.358  1.00141.79           C  
ANISOU 1913  C   THR A1034    17425  24000  12447   2877  -4618   2943       C  
ATOM   1914  O   THR A1034      25.780   7.836  51.882  1.00141.10           O  
ANISOU 1914  O   THR A1034    17384  23841  12387   2754  -4365   2786       O  
ATOM   1915  CB  THR A1034      25.839   5.360  53.725  1.00143.80           C  
ANISOU 1915  CB  THR A1034    17915  24446  12277   2843  -4766   3788       C  
ATOM   1916  OG1 THR A1034      25.468   5.007  55.063  1.00145.54           O  
ANISOU 1916  OG1 THR A1034    18191  25084  12023   2796  -4861   4096       O  
ATOM   1917  CG2 THR A1034      26.640   4.224  53.124  1.00143.58           C  
ANISOU 1917  CG2 THR A1034    17923  24022  12610   2993  -4965   4021       C  
ATOM   1918  N   PHE A1035      27.909   7.094  51.713  1.00139.50           N  
ANISOU 1918  N   PHE A1035    17025  23498  12482   3005  -4757   2834       N  
ATOM   1919  CA  PHE A1035      28.145   7.586  50.363  1.00138.16           C  
ANISOU 1919  CA  PHE A1035    16778  22993  12725   2999  -4620   2538       C  
ATOM   1920  C   PHE A1035      28.333   6.388  49.443  1.00137.67           C  
ANISOU 1920  C   PHE A1035    16775  22509  13025   3113  -4659   2788       C  
ATOM   1921  O   PHE A1035      29.289   5.621  49.603  1.00138.49           O  
ANISOU 1921  O   PHE A1035    16829  22585  13206   3287  -4896   2945       O  
ATOM   1922  CB  PHE A1035      29.370   8.499  50.320  1.00138.17           C  
ANISOU 1922  CB  PHE A1035    16568  23137  12794   3043  -4742   2172       C  
ATOM   1923  CG  PHE A1035      29.405   9.516  51.422  1.00139.03           C  
ANISOU 1923  CG  PHE A1035    16630  23675  12518   2968  -4798   1954       C  
ATOM   1924  CD1 PHE A1035      28.739  10.722  51.293  1.00138.27           C  
ANISOU 1924  CD1 PHE A1035    16553  23634  12350   2826  -4610   1623       C  
ATOM   1925  CD2 PHE A1035      30.106   9.265  52.590  1.00140.71           C  
ANISOU 1925  CD2 PHE A1035    16789  24236  12439   3052  -5054   2072       C  
ATOM   1926  CE1 PHE A1035      28.769  11.659  52.306  1.00139.75           C  
ANISOU 1926  CE1 PHE A1035    16715  24202  12181   2777  -4679   1393       C  
ATOM   1927  CE2 PHE A1035      30.141  10.198  53.608  1.00141.49           C  
ANISOU 1927  CE2 PHE A1035    16853  24737  12170   2991  -5117   1851       C  
ATOM   1928  CZ  PHE A1035      29.472  11.397  53.465  1.00141.22           C  
ANISOU 1928  CZ  PHE A1035    16847  24742  12069   2857  -4932   1501       C  
ATOM   1929  N   MET A1036      27.430   6.234  48.481  1.00130.64           N  
ANISOU 1929  N   MET A1036    15990  21293  12353   3030  -4439   2809       N  
ATOM   1930  CA  MET A1036      27.435   5.090  47.582  1.00129.69           C  
ANISOU 1930  CA  MET A1036    15963  20749  12565   3128  -4466   3035       C  
ATOM   1931  C   MET A1036      28.020   5.480  46.232  1.00128.41           C  
ANISOU 1931  C   MET A1036    15675  20318  12798   3190  -4379   2727       C  
ATOM   1932  O   MET A1036      27.825   6.602  45.757  1.00128.45           O  
ANISOU 1932  O   MET A1036    15597  20358  12849   3071  -4196   2398       O  
ATOM   1933  CB  MET A1036      26.019   4.538  47.400  1.00129.84           C  
ANISOU 1933  CB  MET A1036    16190  20583  12561   2984  -4300   3299       C  
ATOM   1934  CG  MET A1036      25.958   3.179  46.719  1.00129.09           C  
ANISOU 1934  CG  MET A1036    16241  20056  12752   3077  -4389   3602       C  
ATOM   1935  SD  MET A1036      24.688   3.096  45.441  1.00128.40           S  
ANISOU 1935  SD  MET A1036    16284  19573  12928   2923  -4106   3586       S  
ATOM   1936  CE  MET A1036      23.200   3.172  46.436  1.00129.35           C  
ANISOU 1936  CE  MET A1036    16528  19976  12641   2672  -3970   3849       C  
ATOM   1937  N   PHE A1037      28.750   4.549  45.627  1.00132.15           N  
ANISOU 1937  N   PHE A1037    16134  20531  13544   3385  -4521   2836       N  
ATOM   1938  CA  PHE A1037      29.258   4.690  44.270  1.00130.89           C  
ANISOU 1938  CA  PHE A1037    15864  20109  13760   3467  -4437   2598       C  
ATOM   1939  C   PHE A1037      28.808   3.485  43.462  1.00130.25           C  
ANISOU 1939  C   PHE A1037    15961  19595  13934   3558  -4433   2830       C  
ATOM   1940  O   PHE A1037      28.930   2.345  43.921  1.00131.43           O  
ANISOU 1940  O   PHE A1037    16236  19643  14059   3690  -4640   3150       O  
ATOM   1941  CB  PHE A1037      30.787   4.805  44.250  1.00131.26           C  
ANISOU 1941  CB  PHE A1037    15668  20309  13897   3658  -4632   2437       C  
ATOM   1942  CG  PHE A1037      31.396   4.625  42.883  1.00130.24           C  
ANISOU 1942  CG  PHE A1037    15419  19924  14141   3797  -4584   2269       C  
ATOM   1943  CD1 PHE A1037      31.552   5.708  42.032  1.00129.26           C  
ANISOU 1943  CD1 PHE A1037    15134  19822  14157   3679  -4397   1928       C  
ATOM   1944  CD2 PHE A1037      31.828   3.378  42.456  1.00129.97           C  
ANISOU 1944  CD2 PHE A1037    15437  19636  14310   4052  -4736   2451       C  
ATOM   1945  CE1 PHE A1037      32.114   5.548  40.778  1.00127.86           C  
ANISOU 1945  CE1 PHE A1037    14830  19457  14293   3802  -4345   1783       C  
ATOM   1946  CE2 PHE A1037      32.388   3.212  41.203  1.00128.97           C  
ANISOU 1946  CE2 PHE A1037    15190  19313  14500   4203  -4688   2277       C  
ATOM   1947  CZ  PHE A1037      32.533   4.299  40.364  1.00127.74           C  
ANISOU 1947  CZ  PHE A1037    14854  19223  14459   4073  -4483   1947       C  
ATOM   1948  N   ILE A1038      28.291   3.734  42.263  1.00128.75           N  
ANISOU 1948  N   ILE A1038    15792  19139  13987   3488  -4215   2669       N  
ATOM   1949  CA  ILE A1038      27.850   2.647  41.399  1.00128.44           C  
ANISOU 1949  CA  ILE A1038    15926  18671  14204   3568  -4210   2846       C  
ATOM   1950  C   ILE A1038      28.280   2.943  39.966  1.00126.84           C  
ANISOU 1950  C   ILE A1038    15597  18269  14329   3648  -4084   2551       C  
ATOM   1951  O   ILE A1038      27.569   3.606  39.201  1.00125.39           O  
ANISOU 1951  O   ILE A1038    15423  17990  14231   3484  -3840   2381       O  
ATOM   1952  CB  ILE A1038      26.331   2.420  41.530  1.00128.67           C  
ANISOU 1952  CB  ILE A1038    16185  18572  14131   3344  -4061   3067       C  
ATOM   1953  CG1 ILE A1038      25.836   1.400  40.498  1.00128.21           C  
ANISOU 1953  CG1 ILE A1038    16305  18042  14365   3395  -4048   3206       C  
ATOM   1954  CG2 ILE A1038      25.570   3.743  41.489  1.00127.89           C  
ANISOU 1954  CG2 ILE A1038    16023  18670  13901   3109  -3792   2826       C  
ATOM   1955  CD1 ILE A1038      24.712   0.524  41.003  1.00129.13           C  
ANISOU 1955  CD1 ILE A1038    16678  18019  14368   3252  -4085   3607       C  
ATOM   1956  N   GLY A1039      29.458   2.471  39.607  1.00124.79           N  
ANISOU 1956  N   GLY A1039    15206  17972  14237   3909  -4251   2487       N  
ATOM   1957  CA  GLY A1039      29.988   2.657  38.272  1.00123.57           C  
ANISOU 1957  CA  GLY A1039    14904  17678  14369   4017  -4151   2223       C  
ATOM   1958  C   GLY A1039      31.000   1.577  37.965  1.00123.47           C  
ANISOU 1958  C   GLY A1039    14847  17533  14533   4366  -4381   2282       C  
ATOM   1959  O   GLY A1039      30.909   0.456  38.470  1.00124.96           O  
ANISOU 1959  O   GLY A1039    15224  17551  14705   4505  -4588   2569       O  
ATOM   1960  N   ARG A1040      31.975   1.919  37.131  1.00125.57           N  
ANISOU 1960  N   ARG A1040    14858  17887  14965   4510  -4352   2013       N  
ATOM   1961  CA  ARG A1040      33.022   0.996  36.721  1.00126.02           C  
ANISOU 1961  CA  ARG A1040    14821  17866  15194   4880  -4551   2006       C  
ATOM   1962  C   ARG A1040      34.381   1.559  37.115  1.00126.82           C  
ANISOU 1962  C   ARG A1040    14577  18390  15218   4990  -4666   1845       C  
ATOM   1963  O   ARG A1040      34.509   2.723  37.500  1.00126.77           O  
ANISOU 1963  O   ARG A1040    14407  18694  15064   4761  -4571   1702       O  
ATOM   1964  CB  ARG A1040      32.956   0.731  35.214  1.00124.06           C  
ANISOU 1964  CB  ARG A1040    14565  17348  15226   4994  -4412   1832       C  
ATOM   1965  CG  ARG A1040      33.482   1.874  34.384  1.00123.80           C  
ANISOU 1965  CG  ARG A1040    14225  17558  15256   4899  -4207   1501       C  
ATOM   1966  CD  ARG A1040      33.296   1.637  32.904  1.00122.37           C  
ANISOU 1966  CD  ARG A1040    14050  17129  15315   4987  -4051   1344       C  
ATOM   1967  NE  ARG A1040      32.158   2.381  32.389  1.00121.18           N  
ANISOU 1967  NE  ARG A1040    14017  16852  15174   4664  -3781   1282       N  
ATOM   1968  CZ  ARG A1040      31.820   2.420  31.109  1.00120.04           C  
ANISOU 1968  CZ  ARG A1040    13883  16521  15207   4658  -3602   1136       C  
ATOM   1969  NH1 ARG A1040      32.531   1.788  30.188  1.00119.08           N  
ANISOU 1969  NH1 ARG A1040    13654  16332  15257   4957  -3650   1017       N  
ATOM   1970  NH2 ARG A1040      30.757   3.126  30.741  1.00119.45           N  
ANISOU 1970  NH2 ARG A1040    13917  16346  15122   4360  -3371   1097       N  
ATOM   1971  N   PHE A1041      35.405   0.715  37.009  1.00126.99           N  
ANISOU 1971  N   PHE A1041    14489  18418  15342   5352  -4887   1863       N  
ATOM   1972  CA  PHE A1041      36.726   1.004  37.557  1.00128.15           C  
ANISOU 1972  CA  PHE A1041    14320  18973  15398   5499  -5059   1776       C  
ATOM   1973  C   PHE A1041      37.758   1.304  36.474  1.00127.37           C  
ANISOU 1973  C   PHE A1041    13874  19046  15476   5667  -4992   1486       C  
ATOM   1974  O   PHE A1041      38.906   0.864  36.547  1.00129.49           O  
ANISOU 1974  O   PHE A1041    13920  19505  15777   5977  -5188   1452       O  
ATOM   1975  CB  PHE A1041      37.200  -0.141  38.449  1.00130.56           C  
ANISOU 1975  CB  PHE A1041    14726  19240  15641   5797  -5395   2037       C  
ATOM   1976  CG  PHE A1041      36.345  -0.349  39.665  1.00131.41           C  
ANISOU 1976  CG  PHE A1041    15118  19291  15521   5613  -5481   2343       C  
ATOM   1977  CD1 PHE A1041      35.072  -0.881  39.558  1.00131.04           C  
ANISOU 1977  CD1 PHE A1041    15425  18860  15504   5480  -5402   2547       C  
ATOM   1978  CD2 PHE A1041      36.814   0.000  40.920  1.00132.93           C  
ANISOU 1978  CD2 PHE A1041    15210  19844  15453   5561  -5641   2429       C  
ATOM   1979  CE1 PHE A1041      34.288  -1.060  40.676  1.00131.97           C  
ANISOU 1979  CE1 PHE A1041    15776  18978  15389   5296  -5470   2843       C  
ATOM   1980  CE2 PHE A1041      36.028  -0.183  42.044  1.00133.61           C  
ANISOU 1980  CE2 PHE A1041    15543  19925  15299   5393  -5711   2714       C  
ATOM   1981  CZ  PHE A1041      34.764  -0.717  41.918  1.00132.97           C  
ANISOU 1981  CZ  PHE A1041    15799  19481  15244   5259  -5620   2927       C  
ATOM   1982  N   ASP A1042      37.363   2.066  35.460  1.00123.67           N  
ANISOU 1982  N   ASP A1042    13342  18536  15112   5465  -4715   1280       N  
ATOM   1983  CA  ASP A1042      38.330   2.542  34.489  1.00123.17           C  
ANISOU 1983  CA  ASP A1042    12914  18714  15171   5553  -4627   1013       C  
ATOM   1984  C   ASP A1042      39.024   3.792  35.018  1.00124.66           C  
ANISOU 1984  C   ASP A1042    12796  19361  15210   5316  -4618    881       C  
ATOM   1985  O   ASP A1042      38.501   4.513  35.872  1.00125.24           O  
ANISOU 1985  O   ASP A1042    12973  19505  15108   5021  -4596    931       O  
ATOM   1986  CB  ASP A1042      37.653   2.845  33.156  1.00121.96           C  
ANISOU 1986  CB  ASP A1042    12816  18340  15184   5427  -4345    863       C  
ATOM   1987  CG  ASP A1042      36.296   3.487  33.330  1.00121.02           C  
ANISOU 1987  CG  ASP A1042    12965  18024  14994   5046  -4154    921       C  
ATOM   1988  OD1 ASP A1042      35.965   3.884  34.467  1.00121.99           O  
ANISOU 1988  OD1 ASP A1042    13181  18248  14921   4856  -4216   1037       O  
ATOM   1989  OD2 ASP A1042      35.559   3.594  32.330  1.00119.90           O  
ANISOU 1989  OD2 ASP A1042    12933  17644  14980   4948  -3945    845       O  
ATOM   1990  N   ARG A1043      40.221   4.041  34.501  1.00128.03           N  
ANISOU 1990  N   ARG A1043    12835  20111  15701   5448  -4643    704       N  
ATOM   1991  CA  ARG A1043      40.995   5.220  34.861  1.00128.77           C  
ANISOU 1991  CA  ARG A1043    12601  20645  15682   5214  -4649    567       C  
ATOM   1992  C   ARG A1043      40.758   6.300  33.814  1.00127.56           C  
ANISOU 1992  C   ARG A1043    12326  20521  15619   4911  -4372    365       C  
ATOM   1993  O   ARG A1043      41.067   6.105  32.633  1.00126.44           O  
ANISOU 1993  O   ARG A1043    12029  20376  15638   5045  -4253    250       O  
ATOM   1994  CB  ARG A1043      42.483   4.886  34.967  1.00129.26           C  
ANISOU 1994  CB  ARG A1043    12275  21093  15745   5511  -4856    515       C  
ATOM   1995  N   GLY A1044      40.204   7.429  34.245  1.00127.35           N  
ANISOU 1995  N   GLY A1044    12378  20526  15484   4516  -4279    323       N  
ATOM   1996  CA  GLY A1044      39.981   8.552  33.360  1.00127.04           C  
ANISOU 1996  CA  GLY A1044    12240  20508  15521   4199  -4047    148       C  
ATOM   1997  C   GLY A1044      38.599   8.648  32.756  1.00125.13           C  
ANISOU 1997  C   GLY A1044    12327  19863  15353   4046  -3816    162       C  
ATOM   1998  O   GLY A1044      38.391   9.482  31.866  1.00123.99           O  
ANISOU 1998  O   GLY A1044    12113  19703  15296   3818  -3619     26       O  
ATOM   1999  N   GLN A1045      37.647   7.829  33.203  1.00128.73           N  
ANISOU 1999  N   GLN A1045    13134  20002  15776   4152  -3840    334       N  
ATOM   2000  CA  GLN A1045      36.290   7.908  32.676  1.00127.58           C  
ANISOU 2000  CA  GLN A1045    13292  19493  15691   3997  -3629    358       C  
ATOM   2001  C   GLN A1045      35.277   8.100  33.798  1.00128.16           C  
ANISOU 2001  C   GLN A1045    13657  19456  15580   3821  -3652    489       C  
ATOM   2002  O   GLN A1045      34.839   9.226  34.058  1.00128.54           O  
ANISOU 2002  O   GLN A1045    13733  19569  15537   3521  -3557    392       O  
ATOM   2003  CB  GLN A1045      35.945   6.657  31.863  1.00126.39           C  
ANISOU 2003  CB  GLN A1045    13293  19025  15703   4282  -3598    439       C  
ATOM   2004  CG  GLN A1045      36.794   6.463  30.614  1.00125.55           C  
ANISOU 2004  CG  GLN A1045    12915  19020  15768   4472  -3537    283       C  
ATOM   2005  CD  GLN A1045      36.306   5.317  29.743  1.00124.22           C  
ANISOU 2005  CD  GLN A1045    12940  18499  15760   4733  -3495    325       C  
ATOM   2006  OE1 GLN A1045      35.186   4.831  29.904  1.00124.04           O  
ANISOU 2006  OE1 GLN A1045    13263  18123  15745   4692  -3468    465       O  
ATOM   2007  NE2 GLN A1045      37.149   4.878  28.818  1.00123.68           N  
ANISOU 2007  NE2 GLN A1045    12642  18539  15811   5002  -3497    201       N  
ATOM   2008  N   LYS A1046      34.897   7.010  34.471  1.00122.43           N  
ANISOU 2008  N   LYS A1046    13154  18571  14793   4009  -3785    711       N  
ATOM   2009  CA  LYS A1046      33.871   7.085  35.505  1.00122.74           C  
ANISOU 2009  CA  LYS A1046    13466  18530  14638   3851  -3794    864       C  
ATOM   2010  C   LYS A1046      34.372   7.719  36.797  1.00124.25           C  
ANISOU 2010  C   LYS A1046    13557  19064  14589   3753  -3952    854       C  
ATOM   2011  O   LYS A1046      33.559   8.219  37.582  1.00124.50           O  
ANISOU 2011  O   LYS A1046    13756  19116  14430   3557  -3914    893       O  
ATOM   2012  CB  LYS A1046      33.306   5.692  35.792  1.00123.11           C  
ANISOU 2012  CB  LYS A1046    13781  18301  14694   4054  -3897   1138       C  
ATOM   2013  CG  LYS A1046      31.909   5.479  35.231  1.00122.06           C  
ANISOU 2013  CG  LYS A1046    13930  17814  14634   3927  -3704   1215       C  
ATOM   2014  CD  LYS A1046      31.842   5.810  33.748  1.00120.19           C  
ANISOU 2014  CD  LYS A1046    13609  17432  14624   3897  -3496   1014       C  
ATOM   2015  CE  LYS A1046      30.445   5.575  33.198  1.00118.92           C  
ANISOU 2015  CE  LYS A1046    13724  16927  14532   3773  -3319   1093       C  
ATOM   2016  NZ  LYS A1046      29.988   4.175  33.419  1.00119.00           N  
ANISOU 2016  NZ  LYS A1046    13984  16654  14578   3947  -3453   1357       N  
ATOM   2017  N   GLY A1047      35.678   7.706  37.042  1.00126.82           N  
ANISOU 2017  N   GLY A1047    13605  19676  14904   3891  -4133    796       N  
ATOM   2018  CA  GLY A1047      36.241   8.449  38.151  1.00127.28           C  
ANISOU 2018  CA  GLY A1047    13534  20081  14744   3771  -4283    742       C  
ATOM   2019  C   GLY A1047      36.369   7.706  39.459  1.00128.41           C  
ANISOU 2019  C   GLY A1047    13777  20334  14677   3923  -4521    964       C  
ATOM   2020  O   GLY A1047      36.430   8.351  40.512  1.00129.32           O  
ANISOU 2020  O   GLY A1047    13882  20695  14559   3779  -4616    939       O  
ATOM   2021  N   VAL A1048      36.418   6.371  39.436  1.00122.90           N  
ANISOU 2021  N   VAL A1048    13186  19461  14051   4212  -4637   1181       N  
ATOM   2022  CA  VAL A1048      36.708   5.637  40.662  1.00124.49           C  
ANISOU 2022  CA  VAL A1048    13454  19787  14058   4373  -4898   1411       C  
ATOM   2023  C   VAL A1048      38.128   5.919  41.135  1.00125.79           C  
ANISOU 2023  C   VAL A1048    13288  20351  14156   4479  -5112   1311       C  
ATOM   2024  O   VAL A1048      38.445   5.701  42.310  1.00127.27           O  
ANISOU 2024  O   VAL A1048    13485  20747  14125   4537  -5330   1448       O  
ATOM   2025  CB  VAL A1048      36.496   4.126  40.462  1.00124.51           C  
ANISOU 2025  CB  VAL A1048    13656  19471  14182   4666  -5004   1669       C  
ATOM   2026  CG1 VAL A1048      37.678   3.529  39.728  1.00124.56           C  
ANISOU 2026  CG1 VAL A1048    13423  19506  14400   4994  -5122   1589       C  
ATOM   2027  CG2 VAL A1048      36.266   3.432  41.797  1.00126.11           C  
ANISOU 2027  CG2 VAL A1048    14051  19718  14147   4729  -5223   1974       C  
ATOM   2028  N   ASP A1049      38.941   6.411  40.212  1.00134.81           N  
ANISOU 2028  N   ASP A1049    14134  21612  15474   4487  -5046   1083       N  
ATOM   2029  CA  ASP A1049      40.319   6.796  40.570  1.00135.95           C  
ANISOU 2029  CA  ASP A1049    13915  22174  15564   4546  -5234    969       C  
ATOM   2030  C   ASP A1049      40.217   7.991  41.508  1.00136.94           C  
ANISOU 2030  C   ASP A1049    14024  22555  15453   4224  -5261    864       C  
ATOM   2031  O   ASP A1049      40.796   7.946  42.605  1.00138.39           O  
ANISOU 2031  O   ASP A1049    14131  23018  15434   4276  -5496    930       O  
ATOM   2032  CB  ASP A1049      41.023   7.225  39.289  1.00135.19           C  
ANISOU 2032  CB  ASP A1049    13510  22158  15696   4544  -5105    747       C  
ATOM   2033  CG  ASP A1049      41.305   6.053  38.378  1.00136.74           C  
ANISOU 2033  CG  ASP A1049    13679  22168  16108   4912  -5107    807       C  
ATOM   2034  OD1 ASP A1049      41.214   4.909  38.867  1.00138.11           O  
ANISOU 2034  OD1 ASP A1049    14030  22190  16257   5192  -5277   1020       O  
ATOM   2035  OD2 ASP A1049      41.631   6.287  37.206  1.00136.57           O  
ANISOU 2035  OD2 ASP A1049    13463  22159  16270   4921  -4955    642       O  
ATOM   2036  N   VAL A1050      39.495   9.017  41.073  1.00129.62           N  
ANISOU 2036  N   VAL A1050    13174  21524  14550   3914  -5038    699       N  
ATOM   2037  CA  VAL A1050      39.343  10.232  41.868  1.00130.29           C  
ANISOU 2037  CA  VAL A1050    13266  21810  14427   3610  -5060    555       C  
ATOM   2038  C   VAL A1050      38.763   9.897  43.234  1.00130.87           C  
ANISOU 2038  C   VAL A1050    13582  21937  14207   3634  -5188    733       C  
ATOM   2039  O   VAL A1050      39.134  10.496  44.251  1.00132.04           O  
ANISOU 2039  O   VAL A1050    13664  22380  14124   3529  -5349    666       O  
ATOM   2040  CB  VAL A1050      38.474  11.255  41.111  1.00129.35           C  
ANISOU 2040  CB  VAL A1050    13257  21488  14403   3314  -4794    373       C  
ATOM   2041  CG1 VAL A1050      37.991  12.357  42.040  1.00130.71           C  
ANISOU 2041  CG1 VAL A1050    13548  21779  14336   3045  -4816    246       C  
ATOM   2042  CG2 VAL A1050      39.250  11.846  39.952  1.00128.60           C  
ANISOU 2042  CG2 VAL A1050    12869  21455  14540   3224  -4711    183       C  
ATOM   2043  N   LEU A1051      37.898   8.884  43.283  1.00130.97           N  
ANISOU 2043  N   LEU A1051    13865  21682  14216   3778  -5136    975       N  
ATOM   2044  CA  LEU A1051      37.235   8.527  44.566  1.00131.53           C  
ANISOU 2044  CA  LEU A1051    14175  21814  13985   3779  -5238   1183       C  
ATOM   2045  C   LEU A1051      38.253   7.834  45.472  1.00132.74           C  
ANISOU 2045  C   LEU A1051    14201  22232  14004   4007  -5551   1341       C  
ATOM   2046  O   LEU A1051      38.283   8.144  46.675  1.00133.30           O  
ANISOU 2046  O   LEU A1051    14302  22573  13774   3936  -5695   1373       O  
ATOM   2047  CB  LEU A1051      36.058   7.593  44.276  1.00130.22           C  
ANISOU 2047  CB  LEU A1051    14318  21283  13877   3844  -5104   1426       C  
ATOM   2048  CG  LEU A1051      35.294   7.059  45.486  1.00130.10           C  
ANISOU 2048  CG  LEU A1051    14553  21317  13564   3843  -5191   1702       C  
ATOM   2049  CD1 LEU A1051      34.645   8.204  46.244  1.00132.24           C  
ANISOU 2049  CD1 LEU A1051    14891  21800  13555   3579  -5103   1551       C  
ATOM   2050  CD2 LEU A1051      34.242   6.042  45.077  1.00130.00           C  
ANISOU 2050  CD2 LEU A1051    14815  20927  13650   3899  -5081   1966       C  
ATOM   2051  N   LEU A1052      39.052   6.927  44.913  1.00133.34           N  
ANISOU 2051  N   LEU A1052    14138  22241  14286   4288  -5658   1427       N  
ATOM   2052  CA  LEU A1052      39.989   6.174  45.744  1.00134.64           C  
ANISOU 2052  CA  LEU A1052    14192  22631  14335   4544  -5968   1597       C  
ATOM   2053  C   LEU A1052      41.059   7.072  46.354  1.00135.44           C  
ANISOU 2053  C   LEU A1052    13987  23182  14291   4451  -6134   1403       C  
ATOM   2054  O   LEU A1052      41.525   6.809  47.469  1.00137.82           O  
ANISOU 2054  O   LEU A1052    14260  23745  14361   4544  -6384   1530       O  
ATOM   2055  CB  LEU A1052      40.632   5.050  44.929  1.00135.27           C  
ANISOU 2055  CB  LEU A1052    14178  22535  14683   4896  -6048   1692       C  
ATOM   2056  CG  LEU A1052      39.788   3.789  44.720  1.00134.95           C  
ANISOU 2056  CG  LEU A1052    14468  22072  14736   5073  -6034   1976       C  
ATOM   2057  CD1 LEU A1052      40.460   2.840  43.737  1.00134.67           C  
ANISOU 2057  CD1 LEU A1052    14325  21847  14995   5426  -6098   1982       C  
ATOM   2058  CD2 LEU A1052      39.527   3.093  46.047  1.00136.57           C  
ANISOU 2058  CD2 LEU A1052    14884  22334  14674   5143  -6259   2299       C  
ATOM   2059  N   LYS A1053      41.411   8.149  45.651  1.00139.08           N  
ANISOU 2059  N   LYS A1053    14233  23735  14878   4247  -6006   1108       N  
ATOM   2060  CA  LYS A1053      42.400   9.114  46.193  1.00140.98           C  
ANISOU 2060  CA  LYS A1053    14183  24392  14991   4100  -6168    908       C  
ATOM   2061  C   LYS A1053      41.718   9.946  47.277  1.00141.23           C  
ANISOU 2061  C   LYS A1053    14406  24542  14712   3842  -6183    848       C  
ATOM   2062  O   LYS A1053      42.347  10.183  48.320  1.00143.30           O  
ANISOU 2062  O   LYS A1053    14561  25147  14741   3833  -6422    835       O  
ATOM   2063  CB  LYS A1053      42.939  10.004  45.071  1.00140.79           C  
ANISOU 2063  CB  LYS A1053    13885  24407  15202   3929  -6031    638       C  
ATOM   2064  CG  LYS A1053      44.097  10.914  45.455  1.00142.55           C  
ANISOU 2064  CG  LYS A1053    13764  25050  15348   3775  -6216    447       C  
ATOM   2065  CD  LYS A1053      45.305  10.162  45.976  1.00144.97           C  
ANISOU 2065  CD  LYS A1053    13806  25676  15600   4063  -6505    565       C  
ATOM   2066  CE  LYS A1053      45.908   9.217  44.957  1.00145.14           C  
ANISOU 2066  CE  LYS A1053    13666  25571  15909   4349  -6438    638       C  
ATOM   2067  NZ  LYS A1053      47.005   8.408  45.539  1.00149.34           N  
ANISOU 2067  NZ  LYS A1053    14066  26232  16445   4569  -6626    769       N  
ATOM   2068  N   ALA A1054      40.483  10.377  47.028  1.00140.01           N  
ANISOU 2068  N   ALA A1054    14518  24131  14550   3653  -5941    799       N  
ATOM   2069  CA  ALA A1054      39.731  11.132  48.029  1.00140.60           C  
ANISOU 2069  CA  ALA A1054    14789  24316  14316   3444  -5937    728       C  
ATOM   2070  C   ALA A1054      39.701  10.400  49.367  1.00141.69           C  
ANISOU 2070  C   ALA A1054    15042  24658  14134   3597  -6152    977       C  
ATOM   2071  O   ALA A1054      40.248  10.884  50.363  1.00143.38           O  
ANISOU 2071  O   ALA A1054    15161  25220  14098   3542  -6359    896       O  
ATOM   2072  CB  ALA A1054      38.309  11.399  47.529  1.00139.73           C  
ANISOU 2072  CB  ALA A1054    14962  23880  14252   3299  -5641    704       C  
ATOM   2073  N   ILE A1055      39.105   9.202  49.391  1.00137.57           N  
ANISOU 2073  N   ILE A1055    14724  23926  13621   3787  -6123   1294       N  
ATOM   2074  CA  ILE A1055      38.871   8.467  50.637  1.00138.84           C  
ANISOU 2074  CA  ILE A1055    15043  24243  13465   3903  -6301   1582       C  
ATOM   2075  C   ILE A1055      40.131   8.404  51.497  1.00142.14           C  
ANISOU 2075  C   ILE A1055    15232  25052  13724   4024  -6629   1591       C  
ATOM   2076  O   ILE A1055      40.061   8.466  52.732  1.00144.71           O  
ANISOU 2076  O   ILE A1055    15639  25630  13713   3984  -6769   1674       O  
ATOM   2077  CB  ILE A1055      38.331   7.058  50.320  1.00138.39           C  
ANISOU 2077  CB  ILE A1055    15190  23860  13532   4110  -6272   1942       C  
ATOM   2078  CG1 ILE A1055      36.879   7.143  49.845  1.00136.79           C  
ANISOU 2078  CG1 ILE A1055    15257  23349  13368   3948  -5974   1975       C  
ATOM   2079  CG2 ILE A1055      38.443   6.140  51.533  1.00141.04           C  
ANISOU 2079  CG2 ILE A1055    15631  24369  13588   4271  -6528   2284       C  
ATOM   2080  CD1 ILE A1055      36.164   5.809  49.805  1.00136.38           C  
ANISOU 2080  CD1 ILE A1055    15456  23007  13357   4087  -5970   2362       C  
ATOM   2081  N   GLU A1056      41.303   8.313  50.862  1.00145.13           N  
ANISOU 2081  N   GLU A1056    15313  25484  14344   4153  -6734   1495       N  
ATOM   2082  CA  GLU A1056      42.544   8.183  51.621  1.00149.17           C  
ANISOU 2082  CA  GLU A1056    15638  26230  14808   4201  -6962   1506       C  
ATOM   2083  C   GLU A1056      42.824   9.421  52.466  1.00151.08           C  
ANISOU 2083  C   GLU A1056    15795  26808  14801   3941  -7045   1254       C  
ATOM   2084  O   GLU A1056      43.336   9.310  53.586  1.00154.79           O  
ANISOU 2084  O   GLU A1056    16261  27486  15065   3940  -7230   1326       O  
ATOM   2085  CB  GLU A1056      43.715   7.908  50.679  1.00149.80           C  
ANISOU 2085  CB  GLU A1056    15411  26277  15228   4350  -6995   1427       C  
ATOM   2086  CG  GLU A1056      43.571   6.632  49.871  1.00149.20           C  
ANISOU 2086  CG  GLU A1056    15421  25856  15411   4640  -6941   1648       C  
ATOM   2087  CD  GLU A1056      44.379   5.485  50.446  1.00153.86           C  
ANISOU 2087  CD  GLU A1056    16000  26427  16032   4888  -7153   1889       C  
ATOM   2088  OE1 GLU A1056      44.955   5.653  51.541  1.00157.30           O  
ANISOU 2088  OE1 GLU A1056    16379  27127  16261   4832  -7337   1914       O  
ATOM   2089  OE2 GLU A1056      44.438   4.417  49.803  1.00154.15           O  
ANISOU 2089  OE2 GLU A1056    16094  26175  16303   5141  -7146   2045       O  
ATOM   2090  N   ILE A1057      42.501  10.610  51.955  1.00150.17           N  
ANISOU 2090  N   ILE A1057    15621  26733  14702   3716  -6925    951       N  
ATOM   2091  CA  ILE A1057      42.799  11.811  52.729  1.00151.97           C  
ANISOU 2091  CA  ILE A1057    15787  27236  14717   3463  -7025    686       C  
ATOM   2092  C   ILE A1057      41.733  12.098  53.782  1.00152.05           C  
ANISOU 2092  C   ILE A1057    16096  27322  14353   3367  -6998    705       C  
ATOM   2093  O   ILE A1057      42.014  12.818  54.747  1.00154.61           O  
ANISOU 2093  O   ILE A1057    16419  27884  14442   3219  -7125    548       O  
ATOM   2094  CB  ILE A1057      43.006  13.035  51.818  1.00149.72           C  
ANISOU 2094  CB  ILE A1057    15318  26959  14611   3234  -6949    339       C  
ATOM   2095  CG1 ILE A1057      41.701  13.454  51.138  1.00145.69           C  
ANISOU 2095  CG1 ILE A1057    15063  26104  14189   3092  -6639    255       C  
ATOM   2096  CG2 ILE A1057      44.093  12.749  50.785  1.00150.09           C  
ANISOU 2096  CG2 ILE A1057    15039  26978  15008   3319  -6957    332       C  
ATOM   2097  CD1 ILE A1057      41.900  14.300  49.896  1.00144.91           C  
ANISOU 2097  CD1 ILE A1057    14821  25824  14413   2891  -6478     10       C  
ATOM   2098  N   LEU A1058      40.520  11.550  53.647  1.00147.63           N  
ANISOU 2098  N   LEU A1058    15791  26578  13722   3446  -6835    894       N  
ATOM   2099  CA  LEU A1058      39.570  11.646  54.754  1.00148.49           C  
ANISOU 2099  CA  LEU A1058    16165  26805  13450   3380  -6807    966       C  
ATOM   2100  C   LEU A1058      39.900  10.682  55.890  1.00152.56           C  
ANISOU 2100  C   LEU A1058    16756  27439  13773   3506  -6972   1279       C  
ATOM   2101  O   LEU A1058      39.399  10.868  57.003  1.00154.40           O  
ANISOU 2101  O   LEU A1058    17152  27858  13656   3430  -6993   1309       O  
ATOM   2102  CB  LEU A1058      38.129  11.387  54.296  1.00145.06           C  
ANISOU 2102  CB  LEU A1058    15992  26098  13024   3362  -6531   1085       C  
ATOM   2103  CG  LEU A1058      37.419  12.207  53.215  1.00142.65           C  
ANISOU 2103  CG  LEU A1058    15752  25482  12968   3178  -6237    831       C  
ATOM   2104  CD1 LEU A1058      37.707  13.696  53.397  1.00143.33           C  
ANISOU 2104  CD1 LEU A1058    15750  25731  12978   2958  -6281    411       C  
ATOM   2105  CD2 LEU A1058      37.719  11.727  51.807  1.00141.73           C  
ANISOU 2105  CD2 LEU A1058    15531  25018  13302   3250  -6114    878       C  
ATOM   2106  N   SER A1059      40.729   9.664  55.639  1.00153.97           N  
ANISOU 2106  N   SER A1059    16821  27514  14168   3703  -7091   1503       N  
ATOM   2107  CA  SER A1059      40.939   8.619  56.637  1.00157.28           C  
ANISOU 2107  CA  SER A1059    17346  27983  14428   3838  -7251   1840       C  
ATOM   2108  C   SER A1059      41.669   9.138  57.869  1.00161.58           C  
ANISOU 2108  C   SER A1059    17814  28872  14709   3747  -7452   1728       C  
ATOM   2109  O   SER A1059      41.398   8.679  58.985  1.00164.37           O  
ANISOU 2109  O   SER A1059    18332  29348  14775   3763  -7536   1941       O  
ATOM   2110  CB  SER A1059      41.707   7.449  56.022  1.00158.35           C  
ANISOU 2110  CB  SER A1059    17380  27901  14885   4088  -7349   2066       C  
ATOM   2111  OG  SER A1059      42.641   7.896  55.059  1.00157.45           O  
ANISOU 2111  OG  SER A1059    16971  27781  15074   4108  -7352   1820       O  
ATOM   2112  N   SER A1060      42.595  10.084  57.695  1.00163.05           N  
ANISOU 2112  N   SER A1060    17752  29217  14984   3638  -7536   1405       N  
ATOM   2113  CA  SER A1060      43.316  10.617  58.846  1.00166.31           C  
ANISOU 2113  CA  SER A1060    18090  29945  15153   3541  -7739   1283       C  
ATOM   2114  C   SER A1060      42.410  11.451  59.744  1.00166.65           C  
ANISOU 2114  C   SER A1060    18341  30159  14818   3360  -7676   1128       C  
ATOM   2115  O   SER A1060      42.629  11.511  60.961  1.00170.50           O  
ANISOU 2115  O   SER A1060    18883  30888  15010   3332  -7823   1155       O  
ATOM   2116  CB  SER A1060      44.508  11.451  58.378  1.00166.96           C  
ANISOU 2116  CB  SER A1060    17857  30139  15443   3436  -7845    982       C  
ATOM   2117  OG  SER A1060      44.092  12.492  57.510  1.00163.88           O  
ANISOU 2117  OG  SER A1060    17431  29659  15175   3254  -7686    679       O  
ATOM   2118  N   LYS A1061      41.390  12.086  59.172  1.00163.18           N  
ANISOU 2118  N   LYS A1061    18020  29603  14378   3251  -7459    960       N  
ATOM   2119  CA  LYS A1061      40.525  12.974  59.933  1.00163.88           C  
ANISOU 2119  CA  LYS A1061    18293  29848  14126   3095  -7383    757       C  
ATOM   2120  C   LYS A1061      39.706  12.199  60.960  1.00165.85           C  
ANISOU 2120  C   LYS A1061    18781  30196  14040   3171  -7346   1067       C  
ATOM   2121  O   LYS A1061      39.404  11.015  60.789  1.00165.29           O  
ANISOU 2121  O   LYS A1061    18792  29971  14038   3314  -7306   1444       O  
ATOM   2122  CB  LYS A1061      39.588  13.738  58.997  1.00160.28           C  
ANISOU 2122  CB  LYS A1061    17911  29218  13771   2990  -7154    525       C  
ATOM   2123  CG  LYS A1061      40.155  13.993  57.610  1.00157.54           C  
ANISOU 2123  CG  LYS A1061    17351  28668  13841   2970  -7125    385       C  
ATOM   2124  CD  LYS A1061      40.745  15.390  57.496  1.00157.78           C  
ANISOU 2124  CD  LYS A1061    17244  28781  13923   2748  -7215    -44       C  
ATOM   2125  CE  LYS A1061      41.647  15.511  56.280  1.00156.33           C  
ANISOU 2125  CE  LYS A1061    16784  28469  14147   2719  -7239   -127       C  
ATOM   2126  NZ  LYS A1061      42.472  16.748  56.300  1.00158.36           N  
ANISOU 2126  NZ  LYS A1061    16875  28830  14463   2478  -7385   -480       N  
ATOM   2127  N   LYS A1062      39.343  12.892  62.044  1.00164.65           N  
ANISOU 2127  N   LYS A1062    18743  30297  13519   3063  -7364    903       N  
ATOM   2128  CA  LYS A1062      38.510  12.281  63.073  1.00166.77           C  
ANISOU 2128  CA  LYS A1062    19225  30708  13432   3104  -7309   1172       C  
ATOM   2129  C   LYS A1062      37.080  12.088  62.591  1.00164.27           C  
ANISOU 2129  C   LYS A1062    19093  30244  13079   3096  -7027   1283       C  
ATOM   2130  O   LYS A1062      36.413  11.129  62.994  1.00164.95           O  
ANISOU 2130  O   LYS A1062    19328  30325  13020   3155  -6960   1655       O  
ATOM   2131  CB  LYS A1062      38.520  13.142  64.336  1.00169.82           C  
ANISOU 2131  CB  LYS A1062    19667  31425  13430   3003  -7394    928       C  
ATOM   2132  CG  LYS A1062      39.862  13.775  64.646  1.00171.74           C  
ANISOU 2132  CG  LYS A1062    19719  31804  13731   2947  -7652    678       C  
ATOM   2133  CD  LYS A1062      39.721  14.884  65.675  1.00174.22           C  
ANISOU 2133  CD  LYS A1062    20111  32384  13700   2823  -7707    339       C  
ATOM   2134  CE  LYS A1062      39.319  14.338  67.035  1.00178.07           C  
ANISOU 2134  CE  LYS A1062    20748  33144  13767   2883  -7734    569       C  
ATOM   2135  NZ  LYS A1062      40.409  13.541  67.658  1.00181.77           N  
ANISOU 2135  NZ  LYS A1062    21108  33732  14224   2968  -7990    824       N  
ATOM   2136  N   GLU A1063      36.595  12.988  61.733  1.00168.04           N  
ANISOU 2136  N   GLU A1063    19564  30598  13688   3011  -6869    973       N  
ATOM   2137  CA  GLU A1063      35.229  12.935  61.227  1.00165.22           C  
ANISOU 2137  CA  GLU A1063    19366  30112  13298   2996  -6597   1035       C  
ATOM   2138  C   GLU A1063      34.989  11.764  60.284  1.00162.79           C  
ANISOU 2138  C   GLU A1063    19074  29507  13273   3104  -6514   1408       C  
ATOM   2139  O   GLU A1063      33.839  11.539  59.890  1.00160.86           O  
ANISOU 2139  O   GLU A1063    18967  29149  13002   3091  -6296   1531       O  
ATOM   2140  CB  GLU A1063      34.873  14.248  60.515  1.00162.38           C  
ANISOU 2140  CB  GLU A1063    18991  29676  13031   2885  -6479    581       C  
ATOM   2141  CG  GLU A1063      35.368  15.533  61.192  1.00165.35           C  
ANISOU 2141  CG  GLU A1063    19330  30250  13245   2770  -6613    143       C  
ATOM   2142  CD  GLU A1063      36.857  15.786  61.010  1.00166.99           C  
ANISOU 2142  CD  GLU A1063    19317  30448  13682   2734  -6865     10       C  
ATOM   2143  OE1 GLU A1063      37.653  15.254  61.810  1.00170.66           O  
ANISOU 2143  OE1 GLU A1063    19716  31081  14047   2786  -7054    183       O  
ATOM   2144  OE2 GLU A1063      37.229  16.515  60.064  1.00164.36           O  
ANISOU 2144  OE2 GLU A1063    18870  29948  13632   2645  -6874   -259       O  
ATOM   2145  N   PHE A1064      36.039  11.025  59.919  1.00160.75           N  
ANISOU 2145  N   PHE A1064    18678  29115  13284   3216  -6686   1580       N  
ATOM   2146  CA  PHE A1064      35.878   9.876  59.035  1.00158.64           C  
ANISOU 2146  CA  PHE A1064    18439  28534  13303   3345  -6633   1920       C  
ATOM   2147  C   PHE A1064      34.981   8.821  59.666  1.00160.26           C  
ANISOU 2147  C   PHE A1064    18868  28723  13303   3369  -6571   2354       C  
ATOM   2148  O   PHE A1064      34.197   8.169  58.968  1.00158.16           O  
ANISOU 2148  O   PHE A1064    18714  28204  13176   3397  -6425   2584       O  
ATOM   2149  CB  PHE A1064      37.265   9.317  58.679  1.00159.66           C  
ANISOU 2149  CB  PHE A1064    18371  28561  13731   3484  -6851   1989       C  
ATOM   2150  CG  PHE A1064      37.253   8.050  57.849  1.00158.11           C  
ANISOU 2150  CG  PHE A1064    18211  28023  13841   3657  -6841   2329       C  
ATOM   2151  CD1 PHE A1064      36.898   6.819  58.382  1.00160.60           C  
ANISOU 2151  CD1 PHE A1064    18710  28240  14071   3741  -6896   2764       C  
ATOM   2152  CD2 PHE A1064      37.579   8.114  56.506  1.00155.47           C  
ANISOU 2152  CD2 PHE A1064    17736  27448  13887   3728  -6779   2201       C  
ATOM   2153  CE1 PHE A1064      36.901   5.682  57.601  1.00159.75           C  
ANISOU 2153  CE1 PHE A1064    18659  27775  14266   3899  -6909   3050       C  
ATOM   2154  CE2 PHE A1064      37.581   6.979  55.715  1.00154.88           C  
ANISOU 2154  CE2 PHE A1064    17702  27041  14103   3904  -6773   2475       C  
ATOM   2155  CZ  PHE A1064      37.237   5.758  56.266  1.00157.09           C  
ANISOU 2155  CZ  PHE A1064    18184  27197  14307   3992  -6845   2896       C  
ATOM   2156  N   GLN A1065      35.081   8.642  60.985  1.00165.30           N  
ANISOU 2156  N   GLN A1065    19572  29626  13609   3345  -6686   2476       N  
ATOM   2157  CA  GLN A1065      34.310   7.597  61.649  1.00167.50           C  
ANISOU 2157  CA  GLN A1065    20053  29901  13689   3345  -6651   2915       C  
ATOM   2158  C   GLN A1065      32.809   7.807  61.486  1.00165.33           C  
ANISOU 2158  C   GLN A1065    19932  29627  13258   3228  -6363   2948       C  
ATOM   2159  O   GLN A1065      32.045   6.835  61.469  1.00165.45           O  
ANISOU 2159  O   GLN A1065    20102  29496  13264   3216  -6284   3338       O  
ATOM   2160  CB  GLN A1065      34.685   7.528  63.130  1.00172.46           C  
ANISOU 2160  CB  GLN A1065    20710  30861  13957   3326  -6818   2993       C  
ATOM   2161  CG  GLN A1065      34.219   6.258  63.821  1.00175.66           C  
ANISOU 2161  CG  GLN A1065    21300  31232  14212   3342  -6861   3499       C  
ATOM   2162  CD  GLN A1065      34.632   5.003  63.074  1.00175.29           C  
ANISOU 2162  CD  GLN A1065    21286  30782  14534   3482  -6983   3840       C  
ATOM   2163  OE1 GLN A1065      33.793   4.177  62.712  1.00174.30           O  
ANISOU 2163  OE1 GLN A1065    21327  30414  14486   3463  -6880   4161       O  
ATOM   2164  NE2 GLN A1065      35.931   4.853  62.838  1.00176.04           N  
ANISOU 2164  NE2 GLN A1065    21222  30800  14867   3625  -7209   3765       N  
ATOM   2165  N   GLU A1066      32.366   9.060  61.363  1.00165.85           N  
ANISOU 2165  N   GLU A1066    19960  29845  13209   3136  -6210   2541       N  
ATOM   2166  CA  GLU A1066      30.961   9.309  61.059  1.00163.68           C  
ANISOU 2166  CA  GLU A1066    19806  29558  12827   3045  -5927   2538       C  
ATOM   2167  C   GLU A1066      30.604   8.848  59.652  1.00159.82           C  
ANISOU 2167  C   GLU A1066    19329  28684  12711   3082  -5810   2660       C  
ATOM   2168  O   GLU A1066      29.442   8.524  59.381  1.00158.13           O  
ANISOU 2168  O   GLU A1066    19240  28390  12454   3019  -5604   2849       O  
ATOM   2169  CB  GLU A1066      30.637  10.795  61.219  1.00163.00           C  
ANISOU 2169  CB  GLU A1066    19684  29691  12556   2967  -5817   2036       C  
ATOM   2170  CG  GLU A1066      31.262  11.445  62.440  1.00166.86           C  
ANISOU 2170  CG  GLU A1066    20131  30519  12750   2949  -5975   1809       C  
ATOM   2171  CD  GLU A1066      30.960  12.928  62.517  1.00166.21           C  
ANISOU 2171  CD  GLU A1066    20038  30584  12530   2882  -5888   1286       C  
ATOM   2172  OE1 GLU A1066      29.951  13.361  61.921  1.00163.77           O  
ANISOU 2172  OE1 GLU A1066    19793  30194  12237   2848  -5661   1160       O  
ATOM   2173  OE2 GLU A1066      31.730  13.662  63.171  1.00169.32           O  
ANISOU 2173  OE2 GLU A1066    20368  31157  12808   2866  -6058    998       O  
ATOM   2174  N   MET A1067      31.584   8.806  58.753  1.00154.26           N  
ANISOU 2174  N   MET A1067    18488  27753  12372   3183  -5936   2557       N  
ATOM   2175  CA  MET A1067      31.336   8.465  57.361  1.00150.14           C  
ANISOU 2175  CA  MET A1067    17958  26871  12216   3238  -5831   2618       C  
ATOM   2176  C   MET A1067      31.356   6.958  57.142  1.00151.24           C  
ANISOU 2176  C   MET A1067    18200  26723  12543   3335  -5905   3102       C  
ATOM   2177  O   MET A1067      32.024   6.207  57.857  1.00154.48           O  
ANISOU 2177  O   MET A1067    18625  27161  12910   3404  -6109   3333       O  
ATOM   2178  CB  MET A1067      32.378   9.114  56.452  1.00147.91           C  
ANISOU 2178  CB  MET A1067    17483  26420  12296   3277  -5889   2261       C  
ATOM   2179  CG  MET A1067      32.833  10.484  56.891  1.00148.22           C  
ANISOU 2179  CG  MET A1067    17402  26749  12165   3193  -5951   1808       C  
ATOM   2180  SD  MET A1067      33.848  11.251  55.619  1.00145.96           S  
ANISOU 2180  SD  MET A1067    16906  26181  12371   3158  -5950   1422       S  
ATOM   2181  CE  MET A1067      33.454  12.975  55.876  1.00145.26           C  
ANISOU 2181  CE  MET A1067    16832  26261  12099   2963  -5858    905       C  
ATOM   2182  N   ARG A1068      30.618   6.527  56.124  1.00154.41           N  
ANISOU 2182  N   ARG A1068    18695  26769  13206   3317  -5725   3227       N  
ATOM   2183  CA  ARG A1068      30.628   5.145  55.672  1.00154.78           C  
ANISOU 2183  CA  ARG A1068    18849  26464  13495   3420  -5805   3641       C  
ATOM   2184  C   ARG A1068      30.425   5.155  54.165  1.00151.71           C  
ANISOU 2184  C   ARG A1068    18467  25589  13589   3411  -5607   3488       C  
ATOM   2185  O   ARG A1068      29.699   6.000  53.638  1.00150.55           O  
ANISOU 2185  O   ARG A1068    18327  25381  13492   3266  -5347   3224       O  
ATOM   2186  CB  ARG A1068      29.547   4.316  56.373  1.00156.70           C  
ANISOU 2186  CB  ARG A1068    19310  26745  13485   3310  -5754   4080       C  
ATOM   2187  CG  ARG A1068      30.015   3.658  57.666  1.00161.64           C  
ANISOU 2187  CG  ARG A1068    20002  27527  13887   3316  -5964   4335       C  
ATOM   2188  CD  ARG A1068      29.513   4.412  58.891  1.00163.93           C  
ANISOU 2188  CD  ARG A1068    20298  28281  13706   3164  -5876   4222       C  
ATOM   2189  NE  ARG A1068      30.312   4.127  60.077  1.00168.54           N  
ANISOU 2189  NE  ARG A1068    20873  29079  14087   3207  -6106   4318       N  
ATOM   2190  CZ  ARG A1068      30.006   4.528  61.304  1.00171.58           C  
ANISOU 2190  CZ  ARG A1068    21282  29858  14054   3104  -6080   4291       C  
ATOM   2191  NH1 ARG A1068      28.917   5.239  61.548  1.00170.70           N  
ANISOU 2191  NH1 ARG A1068    21199  29982  13676   2961  -5831   4158       N  
ATOM   2192  NH2 ARG A1068      30.813   4.208  62.312  1.00175.68           N  
ANISOU 2192  NH2 ARG A1068    21791  30543  14415   3158  -6310   4390       N  
ATOM   2193  N   PHE A1069      31.088   4.234  53.476  1.00140.10           N  
ANISOU 2193  N   PHE A1069    16989  23781  12463   3582  -5740   3641       N  
ATOM   2194  CA  PHE A1069      31.110   4.227  52.023  1.00137.80           C  
ANISOU 2194  CA  PHE A1069    16673  23057  12629   3611  -5586   3468       C  
ATOM   2195  C   PHE A1069      30.804   2.827  51.510  1.00137.27           C  
ANISOU 2195  C   PHE A1069    16787  22575  12794   3711  -5643   3850       C  
ATOM   2196  O   PHE A1069      31.131   1.830  52.157  1.00139.00           O  
ANISOU 2196  O   PHE A1069    17088  22807  12918   3839  -5892   4202       O  
ATOM   2197  CB  PHE A1069      32.473   4.694  51.461  1.00137.06           C  
ANISOU 2197  CB  PHE A1069    16325  22969  12781   3752  -5694   3145       C  
ATOM   2198  CG  PHE A1069      32.978   6.006  52.033  1.00136.93           C  
ANISOU 2198  CG  PHE A1069    16126  23352  12549   3656  -5714   2785       C  
ATOM   2199  CD1 PHE A1069      33.427   6.100  53.346  1.00139.62           C  
ANISOU 2199  CD1 PHE A1069    16421  24111  12516   3684  -5933   2856       C  
ATOM   2200  CD2 PHE A1069      33.083   7.120  51.221  1.00135.19           C  
ANISOU 2200  CD2 PHE A1069    15778  23072  12515   3543  -5541   2378       C  
ATOM   2201  CE1 PHE A1069      33.903   7.307  53.847  1.00140.43           C  
ANISOU 2201  CE1 PHE A1069    16367  24557  12431   3592  -5973   2506       C  
ATOM   2202  CE2 PHE A1069      33.560   8.319  51.711  1.00135.57           C  
ANISOU 2202  CE2 PHE A1069    15678  23441  12391   3442  -5587   2047       C  
ATOM   2203  CZ  PHE A1069      33.973   8.414  53.027  1.00137.91           C  
ANISOU 2203  CZ  PHE A1069    15939  24145  12316   3468  -5807   2100       C  
ATOM   2204  N   ILE A1070      30.161   2.756  50.344  1.00139.35           N  
ANISOU 2204  N   ILE A1070    17128  22458  13362   3651  -5427   3780       N  
ATOM   2205  CA  ILE A1070      29.912   1.488  49.661  1.00139.47           C  
ANISOU 2205  CA  ILE A1070    17318  22018  13658   3750  -5483   4076       C  
ATOM   2206  C   ILE A1070      30.264   1.680  48.190  1.00137.67           C  
ANISOU 2206  C   ILE A1070    16995  21454  13859   3837  -5356   3777       C  
ATOM   2207  O   ILE A1070      29.616   2.467  47.492  1.00136.19           O  
ANISOU 2207  O   ILE A1070    16790  21196  13760   3674  -5084   3535       O  
ATOM   2208  CB  ILE A1070      28.461   0.994  49.807  1.00139.41           C  
ANISOU 2208  CB  ILE A1070    17555  21880  13535   3544  -5345   4394       C  
ATOM   2209  CG1 ILE A1070      27.955   1.128  51.244  1.00140.60           C  
ANISOU 2209  CG1 ILE A1070    17756  22471  13196   3402  -5388   4621       C  
ATOM   2210  CG2 ILE A1070      28.338  -0.454  49.369  1.00140.10           C  
ANISOU 2210  CG2 ILE A1070    17849  21516  13866   3651  -5500   4763       C  
ATOM   2211  CD1 ILE A1070      26.448   1.235  51.336  1.00140.40           C  
ANISOU 2211  CD1 ILE A1070    17870  22477  13001   3140  -5144   4767       C  
ATOM   2212  N   ILE A1071      31.282   0.962  47.717  1.00137.92           N  
ANISOU 2212  N   ILE A1071    16963  21293  14148   4105  -5554   3795       N  
ATOM   2213  CA  ILE A1071      31.703   1.006  46.320  1.00136.26           C  
ANISOU 2213  CA  ILE A1071    16652  20791  14331   4226  -5457   3536       C  
ATOM   2214  C   ILE A1071      31.188  -0.241  45.616  1.00136.23           C  
ANISOU 2214  C   ILE A1071    16887  20295  14581   4323  -5493   3790       C  
ATOM   2215  O   ILE A1071      31.198  -1.338  46.186  1.00138.07           O  
ANISOU 2215  O   ILE A1071    17292  20404  14763   4435  -5730   4152       O  
ATOM   2216  CB  ILE A1071      33.235   1.122  46.202  1.00136.61           C  
ANISOU 2216  CB  ILE A1071    16423  20998  14484   4478  -5643   3335       C  
ATOM   2217  CG1 ILE A1071      33.742   2.324  47.001  1.00137.30           C  
ANISOU 2217  CG1 ILE A1071    16292  21571  14306   4356  -5647   3106       C  
ATOM   2218  CG2 ILE A1071      33.651   1.235  44.745  1.00134.70           C  
ANISOU 2218  CG2 ILE A1071    16048  20515  14616   4591  -5517   3058       C  
ATOM   2219  CD1 ILE A1071      35.177   2.705  46.693  1.00136.82           C  
ANISOU 2219  CD1 ILE A1071    15912  21700  14375   4531  -5769   2842       C  
ATOM   2220  N   ILE A1072      30.712  -0.073  44.380  1.00133.88           N  
ANISOU 2220  N   ILE A1072    16612  19704  14551   4269  -5271   3609       N  
ATOM   2221  CA  ILE A1072      30.118  -1.161  43.612  1.00133.78           C  
ANISOU 2221  CA  ILE A1072    16837  19206  14787   4329  -5286   3806       C  
ATOM   2222  C   ILE A1072      30.602  -1.070  42.168  1.00131.99           C  
ANISOU 2222  C   ILE A1072    16490  18743  14917   4487  -5182   3493       C  
ATOM   2223  O   ILE A1072      30.827   0.022  41.638  1.00130.85           O  
ANISOU 2223  O   ILE A1072    16133  18772  14810   4404  -4981   3149       O  
ATOM   2224  CB  ILE A1072      28.562  -1.148  43.668  1.00133.14           C  
ANISOU 2224  CB  ILE A1072    16980  19003  14603   4017  -5086   3991       C  
ATOM   2225  CG1 ILE A1072      28.020  -1.242  45.103  1.00134.07           C  
ANISOU 2225  CG1 ILE A1072    17202  19406  14332   3849  -5168   4317       C  
ATOM   2226  CG2 ILE A1072      27.965  -2.261  42.830  1.00133.25           C  
ANISOU 2226  CG2 ILE A1072    17239  18498  14890   4059  -5118   4184       C  
ATOM   2227  CD1 ILE A1072      27.844   0.082  45.814  1.00134.21           C  
ANISOU 2227  CD1 ILE A1072    17057  19904  14034   3661  -5001   4110       C  
ATOM   2228  N   GLY A1073      30.775  -2.238  41.532  1.00131.75           N  
ANISOU 2228  N   GLY A1073    16603  18313  15143   4720  -5336   3616       N  
ATOM   2229  CA  GLY A1073      31.089  -2.357  40.123  1.00130.03           C  
ANISOU 2229  CA  GLY A1073    16318  17833  15255   4888  -5246   3357       C  
ATOM   2230  C   GLY A1073      32.239  -3.312  39.896  1.00130.39           C  
ANISOU 2230  C   GLY A1073    16316  17745  15480   5304  -5530   3366       C  
ATOM   2231  O   GLY A1073      32.733  -3.961  40.822  1.00132.05           O  
ANISOU 2231  O   GLY A1073    16578  18016  15578   5462  -5812   3603       O  
ATOM   2232  N   LYS A1074      32.694  -3.374  38.647  1.00135.15           N  
ANISOU 2232  N   LYS A1074    16808  18191  16353   5500  -5456   3094       N  
ATOM   2233  CA  LYS A1074      33.836  -4.249  38.297  1.00135.95           C  
ANISOU 2233  CA  LYS A1074    16831  18188  16635   5947  -5711   3043       C  
ATOM   2234  C   LYS A1074      34.704  -3.480  37.302  1.00134.52           C  
ANISOU 2234  C   LYS A1074    16291  18239  16582   6067  -5544   2630       C  
ATOM   2235  O   LYS A1074      34.149  -2.664  36.547  1.00132.55           O  
ANISOU 2235  O   LYS A1074    15986  18000  16379   5829  -5247   2431       O  
ATOM   2236  CB  LYS A1074      33.324  -5.566  37.708  1.00136.57           C  
ANISOU 2236  CB  LYS A1074    17240  17704  16946   6098  -5836   3211       C  
ATOM   2237  CG  LYS A1074      32.140  -5.437  36.761  1.00134.45           C  
ANISOU 2237  CG  LYS A1074    17152  17129  16803   5874  -5596   3153       C  
ATOM   2238  CD  LYS A1074      31.658  -6.766  36.227  1.00136.00           C  
ANISOU 2238  CD  LYS A1074    17673  16769  17232   5971  -5715   3313       C  
ATOM   2239  CE  LYS A1074      31.241  -7.726  37.319  1.00139.25           C  
ANISOU 2239  CE  LYS A1074    18359  16999  17553   5857  -5917   3749       C  
ATOM   2240  NZ  LYS A1074      30.780  -9.018  36.759  1.00141.66           N  
ANISOU 2240  NZ  LYS A1074    18957  16769  18099   5880  -5972   3876       N  
ATOM   2241  N   GLY A1075      36.016  -3.709  37.332  1.00130.42           N  
ANISOU 2241  N   GLY A1075    15525  17924  16105   6403  -5726   2518       N  
ATOM   2242  CA  GLY A1075      36.906  -3.013  36.418  1.00129.33           C  
ANISOU 2242  CA  GLY A1075    15014  18058  16069   6514  -5581   2151       C  
ATOM   2243  C   GLY A1075      38.390  -3.335  36.466  1.00133.21           C  
ANISOU 2243  C   GLY A1075    15213  18772  16627   6764  -5691   2032       C  
ATOM   2244  O   GLY A1075      38.788  -4.481  36.691  1.00136.56           O  
ANISOU 2244  O   GLY A1075    15763  18971  17151   6968  -5863   2172       O  
ATOM   2245  N   ASP A1076      39.209  -2.302  36.258  1.00141.06           N  
ANISOU 2245  N   ASP A1076    15811  20223  17563   6735  -5594   1778       N  
ATOM   2246  CA  ASP A1076      40.636  -2.468  35.996  1.00144.15           C  
ANISOU 2246  CA  ASP A1076    15867  20864  18038   6961  -5639   1605       C  
ATOM   2247  C   ASP A1076      41.339  -3.155  37.164  1.00148.32           C  
ANISOU 2247  C   ASP A1076    16413  21460  18481   7090  -5905   1812       C  
ATOM   2248  O   ASP A1076      41.233  -2.686  38.306  1.00148.57           O  
ANISOU 2248  O   ASP A1076    16449  21709  18290   6919  -6010   1961       O  
ATOM   2249  CB  ASP A1076      41.265  -1.099  35.731  1.00142.71           C  
ANISOU 2249  CB  ASP A1076    15262  21191  17770   6810  -5495   1346       C  
ATOM   2250  CG  ASP A1076      42.780  -1.127  35.766  1.00146.58           C  
ANISOU 2250  CG  ASP A1076    15377  22037  18279   6980  -5569   1214       C  
ATOM   2251  OD1 ASP A1076      43.385  -2.007  35.121  1.00149.38           O  
ANISOU 2251  OD1 ASP A1076    15698  22256  18803   7263  -5583   1145       O  
ATOM   2252  OD2 ASP A1076      43.368  -0.261  36.447  1.00146.92           O  
ANISOU 2252  OD2 ASP A1076    15158  22504  18159   6826  -5615   1174       O  
ATOM   2253  N   PRO A1077      42.089  -4.236  36.919  1.00144.69           N  
ANISOU 2253  N   PRO A1077    15952  20841  18181   7395  -6020   1816       N  
ATOM   2254  CA  PRO A1077      42.674  -5.004  38.033  1.00148.77           C  
ANISOU 2254  CA  PRO A1077    16525  21367  18633   7531  -6291   2046       C  
ATOM   2255  C   PRO A1077      43.669  -4.234  38.885  1.00150.33           C  
ANISOU 2255  C   PRO A1077    16379  22095  18645   7473  -6378   2000       C  
ATOM   2256  O   PRO A1077      43.917  -4.640  40.028  1.00153.38           O  
ANISOU 2256  O   PRO A1077    16840  22525  18911   7496  -6601   2230       O  
ATOM   2257  CB  PRO A1077      43.349  -6.188  37.326  1.00152.08           C  
ANISOU 2257  CB  PRO A1077    16961  21540  19283   7893  -6356   1974       C  
ATOM   2258  CG  PRO A1077      43.537  -5.739  35.912  1.00149.79           C  
ANISOU 2258  CG  PRO A1077    16464  21327  19124   7946  -6105   1635       C  
ATOM   2259  CD  PRO A1077      42.354  -4.870  35.618  1.00145.19           C  
ANISOU 2259  CD  PRO A1077    15999  20684  18484   7635  -5914   1619       C  
ATOM   2260  N   GLU A1078      44.247  -3.143  38.382  1.00145.06           N  
ANISOU 2260  N   GLU A1078    15337  21831  17946   7380  -6218   1722       N  
ATOM   2261  CA  GLU A1078      45.264  -2.449  39.164  1.00146.58           C  
ANISOU 2261  CA  GLU A1078    15194  22521  17977   7312  -6314   1671       C  
ATOM   2262  C   GLU A1078      44.649  -1.704  40.345  1.00145.48           C  
ANISOU 2262  C   GLU A1078    15159  22544  17574   7009  -6383   1825       C  
ATOM   2263  O   GLU A1078      45.249  -1.642  41.425  1.00147.53           O  
ANISOU 2263  O   GLU A1078    15326  23053  17675   6989  -6569   1929       O  
ATOM   2264  CB  GLU A1078      46.058  -1.492  38.275  1.00145.06           C  
ANISOU 2264  CB  GLU A1078    14569  22718  17829   7259  -6127   1349       C  
ATOM   2265  CG  GLU A1078      47.127  -0.731  39.035  1.00147.04           C  
ANISOU 2265  CG  GLU A1078    14461  23485  17924   7152  -6227   1289       C  
ATOM   2266  CD  GLU A1078      48.228  -1.638  39.544  1.00152.51           C  
ANISOU 2266  CD  GLU A1078    15054  24246  18646   7446  -6445   1372       C  
ATOM   2267  OE1 GLU A1078      48.486  -2.684  38.914  1.00154.12           O  
ANISOU 2267  OE1 GLU A1078    15329  24199  19032   7761  -6459   1362       O  
ATOM   2268  OE2 GLU A1078      48.809  -1.324  40.602  1.00154.56           O  
ANISOU 2268  OE2 GLU A1078    15181  24802  18743   7365  -6613   1447       O  
ATOM   2269  N   LEU A1079      43.431  -1.183  40.137  1.00154.37           N  
ANISOU 2269  N   LEU A1079    16488  23522  18645   6784  -6235   1839       N  
ATOM   2270  CA  LEU A1079      42.787  -0.302  41.150  1.00152.71           C  
ANISOU 2270  CA  LEU A1079    16353  23516  18154   6479  -6257   1930       C  
ATOM   2271  C   LEU A1079      41.611  -0.992  41.850  1.00152.46           C  
ANISOU 2271  C   LEU A1079    16763  23144  18020   6427  -6343   2255       C  
ATOM   2272  O   LEU A1079      41.149  -0.458  42.868  1.00151.96           O  
ANISOU 2272  O   LEU A1079    16781  23267  17687   6212  -6393   2371       O  
ATOM   2273  CB  LEU A1079      42.267   0.939  40.417  1.00148.45           C  
ANISOU 2273  CB  LEU A1079    15689  23119  17597   6238  -6017   1694       C  
ATOM   2274  CG  LEU A1079      43.265   2.072  40.183  1.00148.57           C  
ANISOU 2274  CG  LEU A1079    15260  23602  17587   6111  -5954   1418       C  
ATOM   2275  CD1 LEU A1079      44.163   1.792  38.990  1.00149.34           C  
ANISOU 2275  CD1 LEU A1079    15092  23719  17931   6314  -5857   1227       C  
ATOM   2276  CD2 LEU A1079      42.535   3.390  39.989  1.00144.62           C  
ANISOU 2276  CD2 LEU A1079    14738  23222  16990   5751  -5762   1267       C  
ATOM   2277  N   GLU A1080      41.126  -2.107  41.296  1.00149.05           N  
ANISOU 2277  N   GLU A1080    16603  22243  17787   6596  -6350   2389       N  
ATOM   2278  CA  GLU A1080      40.012  -2.856  41.937  1.00149.29           C  
ANISOU 2278  CA  GLU A1080    17057  21930  17736   6520  -6441   2737       C  
ATOM   2279  C   GLU A1080      40.528  -3.412  43.263  1.00153.72           C  
ANISOU 2279  C   GLU A1080    17659  22607  18140   6566  -6706   2998       C  
ATOM   2280  O   GLU A1080      39.786  -3.353  44.257  1.00154.36           O  
ANISOU 2280  O   GLU A1080    17948  22722  17981   6373  -6773   3247       O  
ATOM   2281  CB  GLU A1080      39.439  -3.926  41.004  1.00149.01           C  
ANISOU 2281  CB  GLU A1080    17292  21353  17970   6665  -6402   2810       C  
ATOM   2282  CG  GLU A1080      40.340  -5.125  40.780  1.00153.07           C  
ANISOU 2282  CG  GLU A1080    17795  21663  18702   6986  -6560   2846       C  
ATOM   2283  CD  GLU A1080      39.703  -6.240  39.972  1.00153.23           C  
ANISOU 2283  CD  GLU A1080    18127  21126  18969   7105  -6543   2933       C  
ATOM   2284  OE1 GLU A1080      38.537  -6.079  39.562  1.00150.38           O  
ANISOU 2284  OE1 GLU A1080    17989  20528  18619   6922  -6406   2975       O  
ATOM   2285  OE2 GLU A1080      40.373  -7.268  39.756  1.00157.06           O  
ANISOU 2285  OE2 GLU A1080    18630  21415  19629   7379  -6671   2952       O  
ATOM   2286  N   GLY A1081      41.749  -3.939  43.270  1.00153.49           N  
ANISOU 2286  N   GLY A1081    17434  22653  18231   6815  -6848   2947       N  
ATOM   2287  CA  GLY A1081      42.366  -4.397  44.501  1.00157.20           C  
ANISOU 2287  CA  GLY A1081    17899  23271  18558   6871  -7107   3171       C  
ATOM   2288  C   GLY A1081      42.709  -3.252  45.429  1.00156.91           C  
ANISOU 2288  C   GLY A1081    17644  23748  18226   6661  -7129   3091       C  
ATOM   2289  O   GLY A1081      42.722  -3.423  46.652  1.00159.50           O  
ANISOU 2289  O   GLY A1081    18065  24202  18336   6586  -7312   3325       O  
ATOM   2290  N   TRP A1082      42.996  -2.076  44.863  1.00155.35           N  
ANISOU 2290  N   TRP A1082    17157  23854  18017   6549  -6948   2761       N  
ATOM   2291  CA  TRP A1082      43.168  -0.867  45.661  1.00154.52           C  
ANISOU 2291  CA  TRP A1082    16869  24210  17633   6299  -6944   2654       C  
ATOM   2292  C   TRP A1082      41.958  -0.639  46.559  1.00153.00           C  
ANISOU 2292  C   TRP A1082    16976  23999  17160   6055  -6940   2867       C  
ATOM   2293  O   TRP A1082      42.102  -0.299  47.739  1.00154.50           O  
ANISOU 2293  O   TRP A1082    17153  24474  17076   5924  -7066   2956       O  
ATOM   2294  CB  TRP A1082      43.403   0.322  44.720  1.00151.04           C  
ANISOU 2294  CB  TRP A1082    16128  24000  17262   6178  -6725   2288       C  
ATOM   2295  CG  TRP A1082      43.642   1.678  45.349  1.00150.54           C  
ANISOU 2295  CG  TRP A1082    15848  24395  16955   5899  -6709   2117       C  
ATOM   2296  CD1 TRP A1082      43.527   2.021  46.666  1.00151.98           C  
ANISOU 2296  CD1 TRP A1082    16101  24808  16835   5734  -6843   2233       C  
ATOM   2297  CD2 TRP A1082      44.050   2.870  44.662  1.00148.58           C  
ANISOU 2297  CD2 TRP A1082    15281  24419  16752   5738  -6558   1793       C  
ATOM   2298  NE1 TRP A1082      43.829   3.351  46.839  1.00150.55           N  
ANISOU 2298  NE1 TRP A1082    15681  25005  16516   5488  -6790   1981       N  
ATOM   2299  CE2 TRP A1082      44.155   3.893  45.624  1.00148.43           C  
ANISOU 2299  CE2 TRP A1082    15172  24762  16464   5475  -6623   1720       C  
ATOM   2300  CE3 TRP A1082      44.334   3.169  43.326  1.00146.74           C  
ANISOU 2300  CE3 TRP A1082    14836  24161  16758   5777  -6378   1563       C  
ATOM   2301  CZ2 TRP A1082      44.532   5.194  45.293  1.00146.89           C  
ANISOU 2301  CZ2 TRP A1082    14693  24869  16251   5237  -6531   1431       C  
ATOM   2302  CZ3 TRP A1082      44.708   4.461  42.999  1.00144.98           C  
ANISOU 2302  CZ3 TRP A1082    14315  24264  16506   5534  -6277   1298       C  
ATOM   2303  CH2 TRP A1082      44.804   5.457  43.978  1.00145.16           C  
ANISOU 2303  CH2 TRP A1082    14265  24611  16277   5261  -6362   1236       C  
ATOM   2304  N   ALA A1083      40.753  -0.848  46.025  1.00146.61           N  
ANISOU 2304  N   ALA A1083    16438  22864  16402   5991  -6795   2956       N  
ATOM   2305  CA  ALA A1083      39.551  -0.727  46.843  1.00145.51           C  
ANISOU 2305  CA  ALA A1083    16586  22711  15988   5766  -6775   3186       C  
ATOM   2306  C   ALA A1083      39.453  -1.869  47.849  1.00149.72           C  
ANISOU 2306  C   ALA A1083    17369  23085  16431   5825  -7009   3584       C  
ATOM   2307  O   ALA A1083      39.160  -1.646  49.030  1.00150.81           O  
ANISOU 2307  O   ALA A1083    17593  23455  16255   5656  -7090   3750       O  
ATOM   2308  CB  ALA A1083      38.309  -0.685  45.952  1.00141.30           C  
ANISOU 2308  CB  ALA A1083    16266  21873  15548   5683  -6559   3185       C  
ATOM   2309  N   ARG A1084      39.697  -3.104  47.401  1.00158.41           N  
ANISOU 2309  N   ARG A1084    18590  23796  17803   6057  -7122   3740       N  
ATOM   2310  CA  ARG A1084      39.639  -4.246  48.308  1.00162.57           C  
ANISOU 2310  CA  ARG A1084    19352  24142  18277   6108  -7366   4140       C  
ATOM   2311  C   ARG A1084      40.784  -4.253  49.310  1.00166.09           C  
ANISOU 2311  C   ARG A1084    19604  24916  18589   6188  -7593   4169       C  
ATOM   2312  O   ARG A1084      40.645  -4.846  50.386  1.00169.17           O  
ANISOU 2312  O   ARG A1084    20169  25301  18807   6138  -7792   4500       O  
ATOM   2313  CB  ARG A1084      39.624  -5.558  47.521  1.00164.64           C  
ANISOU 2313  CB  ARG A1084    19787  23886  18882   6335  -7429   4281       C  
ATOM   2314  CG  ARG A1084      38.259  -6.221  47.503  1.00163.85           C  
ANISOU 2314  CG  ARG A1084    20077  23398  18781   6182  -7394   4602       C  
ATOM   2315  CD  ARG A1084      38.176  -7.354  46.503  1.00164.04           C  
ANISOU 2315  CD  ARG A1084    20260  22900  19167   6385  -7398   4654       C  
ATOM   2316  NE  ARG A1084      36.863  -7.986  46.533  1.00163.70           N  
ANISOU 2316  NE  ARG A1084    20583  22501  19116   6202  -7365   4980       N  
ATOM   2317  CZ  ARG A1084      36.311  -8.618  45.506  1.00162.54           C  
ANISOU 2317  CZ  ARG A1084    20621  21900  19236   6258  -7268   4966       C  
ATOM   2318  NH1 ARG A1084      36.940  -8.735  44.348  1.00161.63           N  
ANISOU 2318  NH1 ARG A1084    20373  21623  19415   6505  -7196   4641       N  
ATOM   2319  NH2 ARG A1084      35.093  -9.135  45.641  1.00162.54           N  
ANISOU 2319  NH2 ARG A1084    20943  21624  19192   6051  -7232   5278       N  
ATOM   2320  N   SER A1085      41.913  -3.619  48.986  1.00161.30           N  
ANISOU 2320  N   SER A1085    18635  24599  18052   6298  -7574   3843       N  
ATOM   2321  CA  SER A1085      42.931  -3.382  50.000  1.00164.95           C  
ANISOU 2321  CA  SER A1085    18893  25442  18339   6316  -7768   3838       C  
ATOM   2322  C   SER A1085      42.456  -2.389  51.050  1.00163.88           C  
ANISOU 2322  C   SER A1085    18775  25677  17813   6015  -7741   3837       C  
ATOM   2323  O   SER A1085      43.032  -2.335  52.140  1.00166.88           O  
ANISOU 2323  O   SER A1085    19090  26329  17987   5989  -7928   3920       O  
ATOM   2324  CB  SER A1085      44.223  -2.878  49.354  1.00165.24           C  
ANISOU 2324  CB  SER A1085    18521  25723  18541   6469  -7737   3487       C  
ATOM   2325  OG  SER A1085      44.129  -1.499  49.041  1.00161.36           O  
ANISOU 2325  OG  SER A1085    17823  25538  17947   6255  -7535   3173       O  
ATOM   2326  N   LEU A1086      41.417  -1.611  50.744  1.00159.82           N  
ANISOU 2326  N   LEU A1086    18351  25184  17190   5796  -7509   3735       N  
ATOM   2327  CA  LEU A1086      40.856  -0.636  51.667  1.00158.65           C  
ANISOU 2327  CA  LEU A1086    18231  25383  16665   5513  -7448   3704       C  
ATOM   2328  C   LEU A1086      39.555  -1.101  52.310  1.00158.72           C  
ANISOU 2328  C   LEU A1086    18606  25242  16459   5356  -7430   4045       C  
ATOM   2329  O   LEU A1086      39.079  -0.445  53.244  1.00158.88           O  
ANISOU 2329  O   LEU A1086    18674  25566  16129   5136  -7395   4060       O  
ATOM   2330  CB  LEU A1086      40.620   0.697  50.946  1.00154.25           C  
ANISOU 2330  CB  LEU A1086    17489  25015  16102   5355  -7198   3329       C  
ATOM   2331  CG  LEU A1086      41.733   1.750  50.992  1.00154.59           C  
ANISOU 2331  CG  LEU A1086    17162  25455  16121   5308  -7220   2984       C  
ATOM   2332  CD1 LEU A1086      41.850   2.347  52.380  1.00156.23           C  
ANISOU 2332  CD1 LEU A1086    17359  26043  15956   5126  -7336   2997       C  
ATOM   2333  CD2 LEU A1086      43.069   1.176  50.544  1.00157.18           C  
ANISOU 2333  CD2 LEU A1086    17250  25749  16723   5570  -7358   2928       C  
ATOM   2334  N   GLU A1087      38.964  -2.202  51.831  1.00159.29           N  
ANISOU 2334  N   GLU A1087    18933  24863  16728   5449  -7449   4312       N  
ATOM   2335  CA  GLU A1087      37.768  -2.736  52.477  1.00159.91           C  
ANISOU 2335  CA  GLU A1087    19355  24799  16606   5275  -7455   4679       C  
ATOM   2336  C   GLU A1087      38.093  -3.277  53.861  1.00165.23           C  
ANISOU 2336  C   GLU A1087    20127  25615  17039   5251  -7716   4966       C  
ATOM   2337  O   GLU A1087      37.328  -3.073  54.813  1.00165.79           O  
ANISOU 2337  O   GLU A1087    20357  25873  16762   5032  -7689   5133       O  
ATOM   2338  CB  GLU A1087      37.134  -3.832  51.618  1.00159.36           C  
ANISOU 2338  CB  GLU A1087    19535  24182  16834   5364  -7447   4903       C  
ATOM   2339  CG  GLU A1087      35.872  -4.416  52.239  1.00160.10           C  
ANISOU 2339  CG  GLU A1087    19984  24113  16733   5150  -7457   5305       C  
ATOM   2340  CD  GLU A1087      35.255  -5.517  51.406  1.00159.90           C  
ANISOU 2340  CD  GLU A1087    20210  23527  17015   5206  -7474   5540       C  
ATOM   2341  OE1 GLU A1087      35.878  -5.932  50.407  1.00160.31           O  
ANISOU 2341  OE1 GLU A1087    20164  23314  17433   5445  -7486   5399       O  
ATOM   2342  OE2 GLU A1087      34.139  -5.963  51.746  1.00159.38           O  
ANISOU 2342  OE2 GLU A1087    20441  23295  16819   5004  -7462   5851       O  
ATOM   2343  N   GLU A1088      39.227  -3.964  53.991  1.00173.27           N  
ANISOU 2343  N   GLU A1088    21043  26562  18228   5480  -7964   5022       N  
ATOM   2344  CA  GLU A1088      39.670  -4.480  55.270  1.00178.09           C  
ANISOU 2344  CA  GLU A1088    21727  27308  18632   5484  -8239   5279       C  
ATOM   2345  C   GLU A1088      40.703  -3.591  55.954  1.00179.53           C  
ANISOU 2345  C   GLU A1088    21609  27981  18622   5489  -8305   5022       C  
ATOM   2346  O   GLU A1088      41.048  -3.865  57.104  1.00183.47           O  
ANISOU 2346  O   GLU A1088    22160  28653  18898   5472  -8520   5205       O  
ATOM   2347  CB  GLU A1088      40.253  -5.888  55.108  1.00182.25           C  
ANISOU 2347  CB  GLU A1088    22344  27448  19456   5727  -8504   5556       C  
ATOM   2348  CG  GLU A1088      39.232  -6.926  54.710  1.00182.43           C  
ANISOU 2348  CG  GLU A1088    22705  26975  19636   5680  -8511   5901       C  
ATOM   2349  CD  GLU A1088      39.079  -8.010  55.753  1.00187.73           C  
ANISOU 2349  CD  GLU A1088    23653  27484  20193   5634  -8817   6369       C  
ATOM   2350  OE1 GLU A1088      40.046  -8.251  56.506  1.00192.18           O  
ANISOU 2350  OE1 GLU A1088    24109  28218  20695   5755  -9058   6431       O  
ATOM   2351  OE2 GLU A1088      37.988  -8.614  55.829  1.00187.81           O  
ANISOU 2351  OE2 GLU A1088    24006  27186  20167   5471  -8832   6668       O  
ATOM   2352  N   LYS A1089      41.215  -2.541  55.300  1.00170.95           N  
ANISOU 2352  N   LYS A1089    20218  27121  17614   5498  -8142   4610       N  
ATOM   2353  CA  LYS A1089      42.180  -1.715  56.010  1.00172.30           C  
ANISOU 2353  CA  LYS A1089    20120  27747  17599   5467  -8229   4387       C  
ATOM   2354  C   LYS A1089      41.475  -0.732  56.946  1.00171.80           C  
ANISOU 2354  C   LYS A1089    20119  28044  17114   5177  -8122   4323       C  
ATOM   2355  O   LYS A1089      41.929  -0.530  58.080  1.00174.91           O  
ANISOU 2355  O   LYS A1089    20473  28746  17240   5123  -8279   4353       O  
ATOM   2356  CB  LYS A1089      43.102  -1.007  55.010  1.00169.88           C  
ANISOU 2356  CB  LYS A1089    19455  27552  17541   5568  -8131   3988       C  
ATOM   2357  CG  LYS A1089      44.322  -0.218  55.572  1.00171.65           C  
ANISOU 2357  CG  LYS A1089    19352  28216  17652   5553  -8249   3744       C  
ATOM   2358  CD  LYS A1089      44.913  -0.645  56.956  1.00177.90           C  
ANISOU 2358  CD  LYS A1089    20175  29209  18210   5582  -8536   3958       C  
ATOM   2359  CE  LYS A1089      45.247  -2.140  57.111  1.00181.17           C  
ANISOU 2359  CE  LYS A1089    20735  29310  18791   5834  -8777   4315       C  
ATOM   2360  NZ  LYS A1089      45.799  -2.387  58.471  1.00185.14           N  
ANISOU 2360  NZ  LYS A1089    21255  30050  19038   5834  -9048   4494       N  
ATOM   2361  N   HIS A1090      40.347  -0.143  56.529  1.00171.71           N  
ANISOU 2361  N   HIS A1090    20213  28003  17024   4996  -7860   4238       N  
ATOM   2362  CA  HIS A1090      39.593   0.733  57.426  1.00171.30           C  
ANISOU 2362  CA  HIS A1090    20235  28287  16563   4735  -7745   4181       C  
ATOM   2363  C   HIS A1090      38.326   0.089  57.977  1.00171.82           C  
ANISOU 2363  C   HIS A1090    20642  28222  16419   4608  -7693   4547       C  
ATOM   2364  O   HIS A1090      37.978   0.322  59.137  1.00174.33           O  
ANISOU 2364  O   HIS A1090    21051  28824  16362   4458  -7716   4636       O  
ATOM   2365  CB  HIS A1090      39.277   2.047  56.707  1.00167.25           C  
ANISOU 2365  CB  HIS A1090    19563  27922  16062   4596  -7490   3783       C  
ATOM   2366  CG  HIS A1090      40.503   2.858  56.426  1.00167.17           C  
ANISOU 2366  CG  HIS A1090    19215  28131  16172   4641  -7551   3420       C  
ATOM   2367  ND1 HIS A1090      41.538   2.376  55.656  1.00167.71           N  
ANISOU 2367  ND1 HIS A1090    19094  28041  16588   4862  -7653   3373       N  
ATOM   2368  CD2 HIS A1090      40.889   4.083  56.851  1.00166.89           C  
ANISOU 2368  CD2 HIS A1090    18997  28462  15952   4484  -7540   3098       C  
ATOM   2369  CE1 HIS A1090      42.504   3.274  55.605  1.00167.97           C  
ANISOU 2369  CE1 HIS A1090    18826  28353  16643   4825  -7689   3052       C  
ATOM   2370  NE2 HIS A1090      42.134   4.321  56.321  1.00167.59           N  
ANISOU 2370  NE2 HIS A1090    18786  28608  16283   4589  -7634   2882       N  
ATOM   2371  N   GLY A1091      37.643  -0.749  57.198  1.00166.51           N  
ANISOU 2371  N   GLY A1091    20161  27129  15975   4660  -7630   4766       N  
ATOM   2372  CA  GLY A1091      36.646  -1.650  57.743  1.00168.20           C  
ANISOU 2372  CA  GLY A1091    20707  27160  16042   4561  -7655   5183       C  
ATOM   2373  C   GLY A1091      35.224  -1.136  57.777  1.00165.44           C  
ANISOU 2373  C   GLY A1091    20495  26900  15464   4307  -7370   5206       C  
ATOM   2374  O   GLY A1091      34.320  -1.884  58.181  1.00166.97           O  
ANISOU 2374  O   GLY A1091    20957  26947  15536   4197  -7362   5559       O  
ATOM   2375  N   ASN A1092      34.989   0.111  57.374  1.00167.52           N  
ANISOU 2375  N   ASN A1092    20584  27401  15664   4205  -7139   4842       N  
ATOM   2376  CA  ASN A1092      33.638   0.651  57.331  1.00165.05           C  
ANISOU 2376  CA  ASN A1092    20379  27182  15150   3979  -6859   4835       C  
ATOM   2377  C   ASN A1092      33.129   0.793  55.904  1.00160.55           C  
ANISOU 2377  C   ASN A1092    19797  26317  14890   4003  -6659   4715       C  
ATOM   2378  O   ASN A1092      32.169   1.531  55.667  1.00157.47           O  
ANISOU 2378  O   ASN A1092    19419  26041  14371   3837  -6409   4590       O  
ATOM   2379  CB  ASN A1092      33.564   1.998  58.050  1.00164.99           C  
ANISOU 2379  CB  ASN A1092    20231  27668  14790   3828  -6745   4511       C  
ATOM   2380  CG  ASN A1092      34.465   3.047  57.430  1.00162.41           C  
ANISOU 2380  CG  ASN A1092    19626  27462  14621   3903  -6738   4050       C  
ATOM   2381  OD1 ASN A1092      35.439   2.733  56.747  1.00162.38           O  
ANISOU 2381  OD1 ASN A1092    19488  27270  14941   4088  -6867   3983       O  
ATOM   2382  ND2 ASN A1092      34.109   4.312  57.630  1.00160.81           N  
ANISOU 2382  ND2 ASN A1092    19338  27566  14196   3753  -6581   3720       N  
ATOM   2383  N   VAL A1093      33.750   0.099  54.951  1.00156.23           N  
ANISOU 2383  N   VAL A1093    19225  25395  14742   4217  -6765   4740       N  
ATOM   2384  CA  VAL A1093      33.420   0.233  53.539  1.00151.22           C  
ANISOU 2384  CA  VAL A1093    18559  24477  14421   4276  -6591   4591       C  
ATOM   2385  C   VAL A1093      33.244  -1.156  52.940  1.00152.03           C  
ANISOU 2385  C   VAL A1093    18875  24059  14830   4406  -6696   4915       C  
ATOM   2386  O   VAL A1093      34.067  -2.048  53.176  1.00155.68           O  
ANISOU 2386  O   VAL A1093    19370  24351  15431   4583  -6954   5068       O  
ATOM   2387  CB  VAL A1093      34.500   1.031  52.780  1.00149.45           C  
ANISOU 2387  CB  VAL A1093    18030  24346  14409   4425  -6590   4160       C  
ATOM   2388  CG1 VAL A1093      34.511   2.474  53.245  1.00148.40           C  
ANISOU 2388  CG1 VAL A1093    17722  24666  13997   4257  -6479   3820       C  
ATOM   2389  CG2 VAL A1093      35.876   0.417  52.989  1.00152.58           C  
ANISOU 2389  CG2 VAL A1093    18304  24701  14968   4649  -6863   4181       C  
ATOM   2390  N   LYS A1094      32.160  -1.345  52.188  1.00149.83           N  
ANISOU 2390  N   LYS A1094    18752  23520  14658   4313  -6508   5018       N  
ATOM   2391  CA  LYS A1094      31.946  -2.556  51.401  1.00150.24           C  
ANISOU 2391  CA  LYS A1094    19009  23028  15047   4431  -6589   5258       C  
ATOM   2392  C   LYS A1094      32.162  -2.227  49.932  1.00146.51           C  
ANISOU 2392  C   LYS A1094    18421  22289  14958   4547  -6424   4909       C  
ATOM   2393  O   LYS A1094      31.339  -1.546  49.314  1.00143.31           O  
ANISOU 2393  O   LYS A1094    18021  21822  14608   4334  -6119   4713       O  
ATOM   2394  CB  LYS A1094      30.551  -3.140  51.613  1.00150.92           C  
ANISOU 2394  CB  LYS A1094    19387  22931  15024   4186  -6496   5631       C  
ATOM   2395  CG  LYS A1094      30.490  -4.635  51.311  1.00153.34           C  
ANISOU 2395  CG  LYS A1094    19976  22680  15607   4287  -6707   5961       C  
ATOM   2396  CD  LYS A1094      29.089  -5.203  51.454  1.00153.74           C  
ANISOU 2396  CD  LYS A1094    20317  22531  15566   4015  -6595   6302       C  
ATOM   2397  CE  LYS A1094      29.073  -6.696  51.144  1.00156.17           C  
ANISOU 2397  CE  LYS A1094    20934  22268  16134   4157  -6795   6571       C  
ATOM   2398  NZ  LYS A1094      27.810  -7.146  50.496  1.00154.98           N  
ANISOU 2398  NZ  LYS A1094    20991  21782  16112   3944  -6609   6748       N  
ATOM   2399  N   VAL A1095      33.261  -2.698  49.382  1.00147.70           N  
ANISOU 2399  N   VAL A1095    18463  22275  15380   4862  -6609   4809       N  
ATOM   2400  CA  VAL A1095      33.456  -2.661  47.941  1.00144.47           C  
ANISOU 2400  CA  VAL A1095    17984  21537  15369   4978  -6468   4522       C  
ATOM   2401  C   VAL A1095      32.861  -3.933  47.353  1.00144.62           C  
ANISOU 2401  C   VAL A1095    18305  21011  15633   5060  -6548   4808       C  
ATOM   2402  O   VAL A1095      33.009  -5.029  47.910  1.00148.92           O  
ANISOU 2402  O   VAL A1095    19021  21366  16196   5135  -6799   5151       O  
ATOM   2403  CB  VAL A1095      34.945  -2.481  47.583  1.00145.54           C  
ANISOU 2403  CB  VAL A1095    17819  21816  15665   5284  -6609   4240       C  
ATOM   2404  CG1 VAL A1095      35.569  -1.424  48.480  1.00145.96           C  
ANISOU 2404  CG1 VAL A1095    17615  22421  15422   5195  -6630   4062       C  
ATOM   2405  CG2 VAL A1095      35.708  -3.783  47.711  1.00149.92           C  
ANISOU 2405  CG2 VAL A1095    18447  22086  16432   5511  -6876   4449       C  
ATOM   2406  N   ILE A1096      32.130  -3.780  46.254  1.00139.23           N  
ANISOU 2406  N   ILE A1096    17693  20031  15178   4943  -6296   4656       N  
ATOM   2407  CA  ILE A1096      31.393  -4.876  45.636  1.00139.49           C  
ANISOU 2407  CA  ILE A1096    18027  19533  15438   4958  -6341   4899       C  
ATOM   2408  C   ILE A1096      31.891  -5.029  44.210  1.00137.48           C  
ANISOU 2408  C   ILE A1096    17694  18967  15577   5195  -6285   4589       C  
ATOM   2409  O   ILE A1096      31.764  -4.104  43.399  1.00134.85           O  
ANISOU 2409  O   ILE A1096    17195  18708  15335   5088  -6001   4240       O  
ATOM   2410  CB  ILE A1096      29.876  -4.634  45.662  1.00138.58           C  
ANISOU 2410  CB  ILE A1096    18095  19354  15205   4571  -6091   5044       C  
ATOM   2411  CG1 ILE A1096      29.340  -4.746  47.088  1.00140.19           C  
ANISOU 2411  CG1 ILE A1096    18409  19846  15012   4365  -6182   5423       C  
ATOM   2412  CG2 ILE A1096      29.177  -5.645  44.787  1.00138.37           C  
ANISOU 2412  CG2 ILE A1096    18344  18762  15468   4575  -6115   5215       C  
ATOM   2413  CD1 ILE A1096      29.928  -5.896  47.861  1.00144.36           C  
ANISOU 2413  CD1 ILE A1096    19078  20280  15492   4571  -6575   5806       C  
ATOM   2414  N   THR A1097      32.457  -6.194  43.906  1.00140.56           N  
ANISOU 2414  N   THR A1097    18182  19012  16213   5468  -6514   4705       N  
ATOM   2415  CA  THR A1097      32.991  -6.439  42.575  1.00139.42           C  
ANISOU 2415  CA  THR A1097    17947  18593  16435   5702  -6446   4401       C  
ATOM   2416  C   THR A1097      31.982  -7.089  41.641  1.00138.70           C  
ANISOU 2416  C   THR A1097    18136  17989  16575   5618  -6350   4473       C  
ATOM   2417  O   THR A1097      32.077  -6.902  40.424  1.00137.07           O  
ANISOU 2417  O   THR A1097    17856  17621  16602   5729  -6209   4167       O  
ATOM   2418  CB  THR A1097      34.257  -7.295  42.668  1.00143.99           C  
ANISOU 2418  CB  THR A1097    18412  19113  17185   6002  -6643   4398       C  
ATOM   2419  OG1 THR A1097      35.124  -6.745  43.667  1.00146.16           O  
ANISOU 2419  OG1 THR A1097    18447  19861  17227   6034  -6756   4380       O  
ATOM   2420  CG2 THR A1097      34.991  -7.333  41.335  1.00142.74           C  
ANISOU 2420  CG2 THR A1097    18077  18818  17339   6265  -6549   4016       C  
ATOM   2421  N   GLU A1098      31.007  -7.822  42.163  1.00146.34           N  
ANISOU 2421  N   GLU A1098    19407  18721  17473   5405  -6407   4866       N  
ATOM   2422  CA  GLU A1098      30.071  -8.511  41.288  1.00146.17           C  
ANISOU 2422  CA  GLU A1098    19647  18207  17682   5304  -6321   4935       C  
ATOM   2423  C   GLU A1098      28.813  -7.669  41.070  1.00142.70           C  
ANISOU 2423  C   GLU A1098    19294  17814  17113   4985  -6124   4936       C  
ATOM   2424  O   GLU A1098      28.500  -6.755  41.838  1.00142.43           O  
ANISOU 2424  O   GLU A1098    19137  18198  16781   4749  -5982   4955       O  
ATOM   2425  CB  GLU A1098      29.729  -9.898  41.856  1.00150.77           C  
ANISOU 2425  CB  GLU A1098    20515  18475  18297   5253  -6479   5346       C  
ATOM   2426  CG  GLU A1098      28.700 -10.742  41.071  1.00151.08           C  
ANISOU 2426  CG  GLU A1098    20857  17991  18556   5110  -6410   5450       C  
ATOM   2427  CD  GLU A1098      29.125 -11.132  39.656  1.00150.55           C  
ANISOU 2427  CD  GLU A1098    20776  17567  18858   5358  -6367   5107       C  
ATOM   2428  OE1 GLU A1098      30.053 -10.524  39.084  1.00148.97           O  
ANISOU 2428  OE1 GLU A1098    20308  17550  18743   5603  -6320   4742       O  
ATOM   2429  OE2 GLU A1098      28.501 -12.055  39.096  1.00151.63           O  
ANISOU 2429  OE2 GLU A1098    21170  17253  19189   5296  -6374   5193       O  
ATOM   2430  N   MET A1099      28.125  -7.992  39.972  1.00147.35           N  
ANISOU 2430  N   MET A1099    20032  18005  17949   4925  -6003   4857       N  
ATOM   2431  CA  MET A1099      26.938  -7.212  39.566  1.00145.17           C  
ANISOU 2431  CA  MET A1099    19770  17775  17614   4572  -5691   4788       C  
ATOM   2432  C   MET A1099      25.768  -7.419  40.510  1.00146.49           C  
ANISOU 2432  C   MET A1099    20134  17989  17537   4206  -5687   5213       C  
ATOM   2433  O   MET A1099      25.792  -8.384  41.295  1.00148.42           O  
ANISOU 2433  O   MET A1099    20567  18110  17716   4224  -5944   5589       O  
ATOM   2434  CB  MET A1099      26.497  -7.578  38.145  1.00143.31           C  
ANISOU 2434  CB  MET A1099    19657  17092  17702   4613  -5600   4616       C  
ATOM   2435  CG  MET A1099      27.499  -7.191  37.071  1.00142.26           C  
ANISOU 2435  CG  MET A1099    19290  16982  17782   4925  -5521   4159       C  
ATOM   2436  SD  MET A1099      27.846  -5.416  37.004  1.00143.69           S  
ANISOU 2436  SD  MET A1099    19059  17743  17795   4788  -5164   3763       S  
ATOM   2437  CE  MET A1099      26.258  -4.794  36.453  1.00140.00           C  
ANISOU 2437  CE  MET A1099    18693  17191  17310   4363  -4818   3748       C  
ATOM   2438  N   LEU A1100      24.780  -6.550  40.390  1.00133.83           N  
ANISOU 2438  N   LEU A1100    18466  16575  15808   3880  -5367   5133       N  
ATOM   2439  CA  LEU A1100      23.580  -6.560  41.213  1.00134.05           C  
ANISOU 2439  CA  LEU A1100    18620  16740  15574   3510  -5294   5488       C  
ATOM   2440  C   LEU A1100      22.378  -6.290  40.321  1.00132.75           C  
ANISOU 2440  C   LEU A1100    18517  16403  15518   3252  -5025   5409       C  
ATOM   2441  O   LEU A1100      22.456  -5.469  39.403  1.00131.96           O  
ANISOU 2441  O   LEU A1100    18255  16338  15547   3287  -4787   5011       O  
ATOM   2442  CB  LEU A1100      23.658  -5.503  42.322  1.00134.94           C  
ANISOU 2442  CB  LEU A1100    18516  17456  15299   3382  -5163   5447       C  
ATOM   2443  CG  LEU A1100      24.644  -5.704  43.477  1.00137.46           C  
ANISOU 2443  CG  LEU A1100    18774  18042  15412   3558  -5423   5596       C  
ATOM   2444  CD1 LEU A1100      24.627  -7.140  43.980  1.00138.57           C  
ANISOU 2444  CD1 LEU A1100    19197  17866  15587   3612  -5776   6078       C  
ATOM   2445  CD2 LEU A1100      26.045  -5.266  43.097  1.00137.22           C  
ANISOU 2445  CD2 LEU A1100    18510  18108  15518   3893  -5476   5210       C  
ATOM   2446  N   SER A1101      21.272  -6.983  40.588  1.00134.74           N  
ANISOU 2446  N   SER A1101    18998  16481  15716   2982  -5071   5802       N  
ATOM   2447  CA  SER A1101      20.078  -6.804  39.773  1.00133.30           C  
ANISOU 2447  CA  SER A1101    18876  16139  15632   2724  -4836   5761       C  
ATOM   2448  C   SER A1101      19.535  -5.388  39.923  1.00133.24           C  
ANISOU 2448  C   SER A1101    18625  16610  15390   2529  -4471   5521       C  
ATOM   2449  O   SER A1101      19.495  -4.832  41.024  1.00133.89           O  
ANISOU 2449  O   SER A1101    18591  17148  15135   2433  -4422   5609       O  
ATOM   2450  CB  SER A1101      19.010  -7.830  40.157  1.00133.07           C  
ANISOU 2450  CB  SER A1101    19119  15880  15560   2440  -4977   6271       C  
ATOM   2451  OG  SER A1101      18.692  -7.753  41.534  1.00134.43           O  
ANISOU 2451  OG  SER A1101    19266  16458  15352   2246  -5008   6614       O  
ATOM   2452  N   ARG A1102      19.120  -4.804  38.794  1.00137.18           N  
ANISOU 2452  N   ARG A1102    19056  16998  16069   2486  -4227   5207       N  
ATOM   2453  CA  ARG A1102      18.634  -3.428  38.773  1.00136.89           C  
ANISOU 2453  CA  ARG A1102    18802  17351  15859   2336  -3892   4934       C  
ATOM   2454  C   ARG A1102      17.441  -3.211  39.696  1.00137.12           C  
ANISOU 2454  C   ARG A1102    18842  17703  15554   2013  -3770   5219       C  
ATOM   2455  O   ARG A1102      17.182  -2.071  40.097  1.00136.86           O  
ANISOU 2455  O   ARG A1102    18625  18090  15285   1929  -3548   5030       O  
ATOM   2456  CB  ARG A1102      18.267  -3.036  37.342  1.00135.57           C  
ANISOU 2456  CB  ARG A1102    18607  16940  15962   2326  -3684   4621       C  
ATOM   2457  CG  ARG A1102      17.523  -4.132  36.601  1.00134.47           C  
ANISOU 2457  CG  ARG A1102    18715  16321  16056   2230  -3777   4838       C  
ATOM   2458  CD  ARG A1102      17.004  -3.668  35.254  1.00132.57           C  
ANISOU 2458  CD  ARG A1102    18439  15899  16032   2182  -3550   4544       C  
ATOM   2459  NE  ARG A1102      15.973  -4.568  34.752  1.00131.32           N  
ANISOU 2459  NE  ARG A1102    18506  15376  16014   1990  -3604   4793       N  
ATOM   2460  CZ  ARG A1102      16.203  -5.591  33.941  1.00130.29           C  
ANISOU 2460  CZ  ARG A1102    18573  14750  16181   2122  -3803   4818       C  
ATOM   2461  NH1 ARG A1102      17.423  -5.873  33.512  1.00129.96           N  
ANISOU 2461  NH1 ARG A1102    18523  14530  16326   2470  -3956   4605       N  
ATOM   2462  NH2 ARG A1102      15.185  -6.354  33.554  1.00129.48           N  
ANISOU 2462  NH2 ARG A1102    18678  14333  16186   1903  -3858   5055       N  
ATOM   2463  N   GLU A1103      16.710  -4.271  40.037  1.00136.45           N  
ANISOU 2463  N   GLU A1103    18966  17438  15440   1830  -3917   5667       N  
ATOM   2464  CA  GLU A1103      15.605  -4.181  40.980  1.00136.21           C  
ANISOU 2464  CA  GLU A1103    18931  17756  15066   1518  -3820   5990       C  
ATOM   2465  C   GLU A1103      16.037  -4.391  42.424  1.00137.62           C  
ANISOU 2465  C   GLU A1103    19098  18278  14913   1531  -3994   6273       C  
ATOM   2466  O   GLU A1103      15.225  -4.187  43.332  1.00137.95           O  
ANISOU 2466  O   GLU A1103    19093  18717  14606   1297  -3898   6513       O  
ATOM   2467  CB  GLU A1103      14.517  -5.199  40.619  1.00135.26           C  
ANISOU 2467  CB  GLU A1103    19027  17302  15064   1259  -3885   6365       C  
ATOM   2468  CG  GLU A1103      15.040  -6.605  40.381  1.00135.35           C  
ANISOU 2468  CG  GLU A1103    19306  16775  15346   1372  -4246   6625       C  
ATOM   2469  CD  GLU A1103      15.404  -6.852  38.930  1.00134.11           C  
ANISOU 2469  CD  GLU A1103    19231  16108  15618   1566  -4270   6315       C  
ATOM   2470  OE1 GLU A1103      15.144  -5.965  38.090  1.00133.27           O  
ANISOU 2470  OE1 GLU A1103    18977  16064  15594   1566  -3997   5944       O  
ATOM   2471  OE2 GLU A1103      15.951  -7.932  38.630  1.00133.96           O  
ANISOU 2471  OE2 GLU A1103    19426  15629  15845   1728  -4570   6441       O  
ATOM   2472  N   PHE A1104      17.303  -4.745  42.649  1.00134.02           N  
ANISOU 2472  N   PHE A1104    18663  17715  14542   1810  -4238   6233       N  
ATOM   2473  CA  PHE A1104      17.813  -4.879  44.040  1.00135.37           C  
ANISOU 2473  CA  PHE A1104    18809  18242  14385   1847  -4413   6478       C  
ATOM   2474  C   PHE A1104      18.346  -3.526  44.498  1.00135.41           C  
ANISOU 2474  C   PHE A1104    18547  18745  14158   1952  -4239   6091       C  
ATOM   2475  O   PHE A1104      18.273  -3.219  45.702  1.00135.93           O  
ANISOU 2475  O   PHE A1104    18537  19274  13835   1876  -4245   6237       O  
ATOM   2476  CB  PHE A1104      18.947  -5.905  44.072  1.00136.21           C  
ANISOU 2476  CB  PHE A1104    19059  17999  14694   2117  -4780   6614       C  
ATOM   2477  CG  PHE A1104      19.886  -5.796  45.245  1.00138.14           C  
ANISOU 2477  CG  PHE A1104    19216  18598  14674   2272  -4956   6687       C  
ATOM   2478  CD1 PHE A1104      19.518  -6.263  46.496  1.00139.94           C  
ANISOU 2478  CD1 PHE A1104    19524  19081  14566   2102  -5075   7123       C  
ATOM   2479  CD2 PHE A1104      21.144  -5.236  45.097  1.00138.22           C  
ANISOU 2479  CD2 PHE A1104    19053  18698  14766   2579  -4995   6307       C  
ATOM   2480  CE1 PHE A1104      20.382  -6.162  47.574  1.00142.16           C  
ANISOU 2480  CE1 PHE A1104    19728  19687  14600   2248  -5218   7144       C  
ATOM   2481  CE2 PHE A1104      22.007  -5.136  46.175  1.00140.25           C  
ANISOU 2481  CE2 PHE A1104    19222  19292  14777   2716  -5169   6372       C  
ATOM   2482  CZ  PHE A1104      21.626  -5.600  47.412  1.00141.52           C  
ANISOU 2482  CZ  PHE A1104    19473  19702  14597   2557  -5304   6820       C  
ATOM   2483  N   VAL A1105      18.813  -2.717  43.552  1.00135.17           N  
ANISOU 2483  N   VAL A1105    18381  18629  14349   2104  -4085   5614       N  
ATOM   2484  CA  VAL A1105      19.468  -1.458  43.894  1.00134.77           C  
ANISOU 2484  CA  VAL A1105    18094  18980  14133   2214  -3965   5228       C  
ATOM   2485  C   VAL A1105      18.493  -0.305  44.077  1.00133.61           C  
ANISOU 2485  C   VAL A1105    17819  19203  13742   2012  -3654   5051       C  
ATOM   2486  O   VAL A1105      18.912   0.781  44.507  1.00133.32           O  
ANISOU 2486  O   VAL A1105    17609  19525  13523   2074  -3566   4750       O  
ATOM   2487  CB  VAL A1105      20.523  -1.122  42.821  1.00133.45           C  
ANISOU 2487  CB  VAL A1105    17828  18566  14311   2467  -3970   4816       C  
ATOM   2488  CG1 VAL A1105      19.884  -0.402  41.656  1.00131.77           C  
ANISOU 2488  CG1 VAL A1105    17561  18217  14288   2375  -3686   4509       C  
ATOM   2489  CG2 VAL A1105      21.648  -0.286  43.413  1.00133.37           C  
ANISOU 2489  CG2 VAL A1105    17612  18911  14153   2633  -4019   4549       C  
ATOM   2490  N   ARG A1106      17.208  -0.498  43.772  1.00137.24           N  
ANISOU 2490  N   ARG A1106    18360  19591  14192   1779  -3497   5220       N  
ATOM   2491  CA  ARG A1106      16.231   0.553  44.038  1.00136.78           C  
ANISOU 2491  CA  ARG A1106    18176  19922  13872   1610  -3213   5072       C  
ATOM   2492  C   ARG A1106      16.157   0.862  45.527  1.00137.94           C  
ANISOU 2492  C   ARG A1106    18246  20622  13543   1559  -3240   5218       C  
ATOM   2493  O   ARG A1106      16.082   2.030  45.926  1.00137.98           O  
ANISOU 2493  O   ARG A1106    18097  21013  13318   1576  -3080   4916       O  
ATOM   2494  CB  ARG A1106      14.857   0.148  43.504  1.00135.80           C  
ANISOU 2494  CB  ARG A1106    18142  19646  13809   1366  -3066   5284       C  
ATOM   2495  CG  ARG A1106      14.420  -1.246  43.916  1.00136.34           C  
ANISOU 2495  CG  ARG A1106    18401  19553  13848   1210  -3266   5838       C  
ATOM   2496  CD  ARG A1106      12.913  -1.395  43.845  1.00135.99           C  
ANISOU 2496  CD  ARG A1106    18378  19602  13691    905  -3091   6078       C  
ATOM   2497  NE  ARG A1106      12.400  -1.271  42.486  1.00134.00           N  
ANISOU 2497  NE  ARG A1106    18150  18988  13774    865  -2942   5873       N  
ATOM   2498  CZ  ARG A1106      11.914  -2.278  41.773  1.00133.32           C  
ANISOU 2498  CZ  ARG A1106    18240  18466  13947    735  -3035   6121       C  
ATOM   2499  NH1 ARG A1106      11.860  -3.508  42.259  1.00134.20           N  
ANISOU 2499  NH1 ARG A1106    18535  18409  14046    623  -3287   6596       N  
ATOM   2500  NH2 ARG A1106      11.461  -2.044  40.545  1.00131.82           N  
ANISOU 2500  NH2 ARG A1106    18054  17997  14035    710  -2885   5891       N  
ATOM   2501  N   GLU A1107      16.183  -0.175  46.367  1.00133.49           N  
ANISOU 2501  N   GLU A1107    17799  20100  12820   1500  -3457   5679       N  
ATOM   2502  CA  GLU A1107      16.209   0.043  47.808  1.00134.48           C  
ANISOU 2502  CA  GLU A1107    17853  20767  12475   1466  -3508   5838       C  
ATOM   2503  C   GLU A1107      17.545   0.615  48.261  1.00135.48           C  
ANISOU 2503  C   GLU A1107    17872  21060  12544   1712  -3640   5550       C  
ATOM   2504  O   GLU A1107      17.607   1.307  49.283  1.00136.53           O  
ANISOU 2504  O   GLU A1107    17891  21694  12292   1718  -3609   5466       O  
ATOM   2505  CB  GLU A1107      15.915  -1.264  48.544  1.00136.03           C  
ANISOU 2505  CB  GLU A1107    18212  20944  12529   1323  -3724   6442       C  
ATOM   2506  N   LEU A1108      18.622   0.340  47.520  1.00133.78           N  
ANISOU 2506  N   LEU A1108    17682  20453  12696   1920  -3793   5390       N  
ATOM   2507  CA  LEU A1108      19.921   0.906  47.872  1.00134.19           C  
ANISOU 2507  CA  LEU A1108    17603  20668  12715   2143  -3919   5106       C  
ATOM   2508  C   LEU A1108      19.936   2.418  47.690  1.00133.78           C  
ANISOU 2508  C   LEU A1108    17369  20870  12593   2156  -3692   4599       C  
ATOM   2509  O   LEU A1108      20.475   3.144  48.533  1.00134.52           O  
ANISOU 2509  O   LEU A1108    17343  21350  12419   2222  -3737   4424       O  
ATOM   2510  CB  LEU A1108      21.029   0.263  47.038  1.00133.48           C  
ANISOU 2510  CB  LEU A1108    17554  20123  13039   2368  -4117   5044       C  
ATOM   2511  CG  LEU A1108      21.678  -1.012  47.575  1.00134.44           C  
ANISOU 2511  CG  LEU A1108    17810  20094  13176   2486  -4456   5440       C  
ATOM   2512  CD1 LEU A1108      22.764  -1.494  46.626  1.00134.38           C  
ANISOU 2512  CD1 LEU A1108    17811  19659  13588   2752  -4619   5286       C  
ATOM   2513  CD2 LEU A1108      22.241  -0.782  48.967  1.00136.11           C  
ANISOU 2513  CD2 LEU A1108    17938  20786  12993   2535  -4606   5530       C  
ATOM   2514  N   TYR A1109      19.357   2.911  46.594  1.00133.58           N  
ANISOU 2514  N   TYR A1109    17329  20620  12807   2093  -3466   4359       N  
ATOM   2515  CA  TYR A1109      19.359   4.349  46.346  1.00133.04           C  
ANISOU 2515  CA  TYR A1109    17110  20735  12703   2103  -3269   3884       C  
ATOM   2516  C   TYR A1109      18.510   5.089  47.370  1.00133.96           C  
ANISOU 2516  C   TYR A1109    17173  21356  12371   1985  -3132   3862       C  
ATOM   2517  O   TYR A1109      18.842   6.210  47.767  1.00134.16           O  
ANISOU 2517  O   TYR A1109    17082  21664  12228   2041  -3090   3514       O  
ATOM   2518  CB  TYR A1109      18.855   4.644  44.933  1.00131.77           C  
ANISOU 2518  CB  TYR A1109    16961  20213  12891   2056  -3066   3674       C  
ATOM   2519  CG  TYR A1109      19.842   4.336  43.832  1.00130.86           C  
ANISOU 2519  CG  TYR A1109    16839  19682  13200   2210  -3161   3529       C  
ATOM   2520  CD1 TYR A1109      21.085   4.953  43.788  1.00130.77           C  
ANISOU 2520  CD1 TYR A1109    16688  19738  13263   2367  -3254   3227       C  
ATOM   2521  CD2 TYR A1109      19.528   3.427  42.834  1.00129.93           C  
ANISOU 2521  CD2 TYR A1109    16846  19125  13397   2199  -3161   3688       C  
ATOM   2522  CE1 TYR A1109      21.987   4.670  42.777  1.00129.87           C  
ANISOU 2522  CE1 TYR A1109    16537  19296  13512   2514  -3328   3097       C  
ATOM   2523  CE2 TYR A1109      20.420   3.139  41.823  1.00129.17           C  
ANISOU 2523  CE2 TYR A1109    16734  18683  13663   2364  -3241   3538       C  
ATOM   2524  CZ  TYR A1109      21.646   3.760  41.797  1.00129.21           C  
ANISOU 2524  CZ  TYR A1109    16578  18795  13721   2525  -3316   3247       C  
ATOM   2525  OH  TYR A1109      22.530   3.465  40.784  1.00128.34           O  
ANISOU 2525  OH  TYR A1109    16424  18390  13950   2696  -3385   3102       O  
ATOM   2526  N   GLY A1110      17.415   4.476  47.812  1.00142.50           N  
ANISOU 2526  N   GLY A1110    18335  22564  13244   1822  -3069   4227       N  
ATOM   2527  CA  GLY A1110      16.523   5.161  48.733  1.00142.82           C  
ANISOU 2527  CA  GLY A1110    18304  23120  12841   1723  -2914   4202       C  
ATOM   2528  C   GLY A1110      17.082   5.268  50.141  1.00144.06           C  
ANISOU 2528  C   GLY A1110    18411  23742  12584   1789  -3075   4272       C  
ATOM   2529  O   GLY A1110      16.984   6.318  50.780  1.00144.29           O  
ANISOU 2529  O   GLY A1110    18337  24176  12310   1826  -2991   3983       O  
ATOM   2530  N   SER A1111      17.690   4.189  50.641  1.00137.27           N  
ANISOU 2530  N   SER A1111    17630  22821  11703   1817  -3325   4647       N  
ATOM   2531  CA  SER A1111      18.171   4.182  52.019  1.00138.22           C  
ANISOU 2531  CA  SER A1111    17711  23401  11406   1868  -3493   4770       C  
ATOM   2532  C   SER A1111      19.460   4.981  52.165  1.00138.61           C  
ANISOU 2532  C   SER A1111    17655  23518  11493   2065  -3621   4365       C  
ATOM   2533  O   SER A1111      19.651   5.687  53.162  1.00139.39           O  
ANISOU 2533  O   SER A1111    17668  24080  11214   2105  -3649   4206       O  
ATOM   2534  CB  SER A1111      18.371   2.739  52.487  1.00139.02           C  
ANISOU 2534  CB  SER A1111    17946  23395  11482   1829  -3736   5332       C  
ATOM   2535  OG  SER A1111      18.780   1.915  51.410  1.00138.54           O  
ANISOU 2535  OG  SER A1111    17996  22732  11910   1881  -3841   5428       O  
ATOM   2536  N   VAL A1112      20.349   4.891  51.176  1.00141.03           N  
ANISOU 2536  N   VAL A1112    17958  23385  12242   2183  -3704   4189       N  
ATOM   2537  CA  VAL A1112      21.659   5.521  51.273  1.00141.17           C  
ANISOU 2537  CA  VAL A1112    17860  23456  12322   2351  -3854   3856       C  
ATOM   2538  C   VAL A1112      21.507   7.037  51.276  1.00140.46           C  
ANISOU 2538  C   VAL A1112    17656  23597  12116   2338  -3684   3357       C  
ATOM   2539  O   VAL A1112      20.657   7.601  50.572  1.00139.38           O  
ANISOU 2539  O   VAL A1112    17527  23344  12087   2253  -3445   3174       O  
ATOM   2540  CB  VAL A1112      22.562   5.033  50.126  1.00140.41           C  
ANISOU 2540  CB  VAL A1112    17767  22856  12727   2475  -3957   3799       C  
ATOM   2541  CG1 VAL A1112      23.705   5.999  49.876  1.00139.90           C  
ANISOU 2541  CG1 VAL A1112    17539  22828  12787   2598  -4016   3354       C  
ATOM   2542  CG2 VAL A1112      23.100   3.642  50.438  1.00141.05           C  
ANISOU 2542  CG2 VAL A1112    17947  22783  12862   2565  -4225   4233       C  
ATOM   2543  N   ASP A1113      22.337   7.717  52.072  1.00140.25           N  
ANISOU 2543  N   ASP A1113    17531  23889  11870   2425  -3825   3130       N  
ATOM   2544  CA  ASP A1113      22.195   9.189  52.231  1.00139.99           C  
ANISOU 2544  CA  ASP A1113    17414  24091  11684   2413  -3705   2651       C  
ATOM   2545  C   ASP A1113      22.732   9.956  51.031  1.00139.01           C  
ANISOU 2545  C   ASP A1113    17226  23613  11980   2436  -3646   2259       C  
ATOM   2546  O   ASP A1113      22.115  10.971  50.679  1.00138.41           O  
ANISOU 2546  O   ASP A1113    17143  23540  11907   2379  -3460   1943       O  
ATOM   2547  CB  ASP A1113      22.953   9.685  53.463  1.00141.32           C  
ANISOU 2547  CB  ASP A1113    17506  24701  11487   2489  -3903   2517       C  
ATOM   2548  CG  ASP A1113      22.141   9.617  54.743  1.00142.76           C  
ANISOU 2548  CG  ASP A1113    17723  25392  11127   2447  -3873   2702       C  
ATOM   2549  OD1 ASP A1113      20.899   9.652  54.650  1.00142.68           O  
ANISOU 2549  OD1 ASP A1113    17762  25449  11001   2353  -3647   2779       O  
ATOM   2550  OD2 ASP A1113      22.756   9.525  55.821  1.00143.90           O  
ANISOU 2550  OD2 ASP A1113    17832  25885  10958   2510  -4077   2771       O  
ATOM   2551  N   PHE A1114      23.809   9.483  50.411  1.00138.12           N  
ANISOU 2551  N   PHE A1114    17064  23213  12202   2519  -3796   2286       N  
ATOM   2552  CA  PHE A1114      24.453  10.264  49.366  1.00136.66           C  
ANISOU 2552  CA  PHE A1114    16786  22768  12371   2531  -3759   1916       C  
ATOM   2553  C   PHE A1114      25.055   9.345  48.312  1.00135.93           C  
ANISOU 2553  C   PHE A1114    16683  22265  12699   2606  -3813   2073       C  
ATOM   2554  O   PHE A1114      25.496   8.234  48.612  1.00136.44           O  
ANISOU 2554  O   PHE A1114    16778  22294  12771   2702  -3987   2395       O  
ATOM   2555  CB  PHE A1114      25.550  11.163  49.945  1.00137.43           C  
ANISOU 2555  CB  PHE A1114    16749  23115  12352   2576  -3939   1604       C  
ATOM   2556  CG  PHE A1114      25.149  12.606  50.091  1.00137.75           C  
ANISOU 2556  CG  PHE A1114    16777  23308  12252   2494  -3830   1190       C  
ATOM   2557  CD1 PHE A1114      24.351  13.018  51.141  1.00138.60           C  
ANISOU 2557  CD1 PHE A1114    16947  23784  11930   2473  -3783   1156       C  
ATOM   2558  CD2 PHE A1114      25.607  13.556  49.201  1.00137.16           C  
ANISOU 2558  CD2 PHE A1114    16629  23020  12467   2447  -3792    833       C  
ATOM   2559  CE1 PHE A1114      23.999  14.356  51.282  1.00138.70           C  
ANISOU 2559  CE1 PHE A1114    16965  23919  11817   2431  -3706    746       C  
ATOM   2560  CE2 PHE A1114      25.259  14.890  49.334  1.00137.59           C  
ANISOU 2560  CE2 PHE A1114    16698  23172  12409   2377  -3725    451       C  
ATOM   2561  CZ  PHE A1114      24.456  15.284  50.381  1.00138.20           C  
ANISOU 2561  CZ  PHE A1114    16852  23590  12067   2383  -3688    396       C  
ATOM   2562  N   VAL A1115      25.069   9.825  47.068  1.00130.09           N  
ANISOU 2562  N   VAL A1115    15905  21217  12304   2573  -3672   1838       N  
ATOM   2563  CA  VAL A1115      25.732   9.155  45.952  1.00128.85           C  
ANISOU 2563  CA  VAL A1115    15709  20697  12553   2662  -3710   1893       C  
ATOM   2564  C   VAL A1115      26.713  10.126  45.311  1.00128.38           C  
ANISOU 2564  C   VAL A1115    15473  20605  12700   2666  -3729   1517       C  
ATOM   2565  O   VAL A1115      26.376  11.292  45.077  1.00128.51           O  
ANISOU 2565  O   VAL A1115    15469  20654  12707   2548  -3596   1217       O  
ATOM   2566  CB  VAL A1115      24.733   8.633  44.900  1.00127.80           C  
ANISOU 2566  CB  VAL A1115    15702  20200  12656   2604  -3507   2022       C  
ATOM   2567  CG1 VAL A1115      25.398   7.589  44.003  1.00127.14           C  
ANISOU 2567  CG1 VAL A1115    15614  19775  12920   2741  -3602   2166       C  
ATOM   2568  CG2 VAL A1115      23.515   8.029  45.577  1.00128.26           C  
ANISOU 2568  CG2 VAL A1115    15920  20353  12459   2520  -3440   2341       C  
ATOM   2569  N   ILE A1116      27.917   9.642  45.017  1.00126.00           N  
ANISOU 2569  N   ILE A1116    15044  20243  12587   2801  -3901   1542       N  
ATOM   2570  CA  ILE A1116      28.975  10.447  44.417  1.00126.04           C  
ANISOU 2570  CA  ILE A1116    14847  20255  12788   2798  -3943   1232       C  
ATOM   2571  C   ILE A1116      29.167  10.005  42.971  1.00124.67           C  
ANISOU 2571  C   ILE A1116    14632  19730  13008   2856  -3843   1226       C  
ATOM   2572  O   ILE A1116      29.343   8.812  42.694  1.00124.48           O  
ANISOU 2572  O   ILE A1116    14649  19533  13113   3014  -3914   1468       O  
ATOM   2573  CB  ILE A1116      30.286  10.342  45.220  1.00127.51           C  
ANISOU 2573  CB  ILE A1116    14867  20724  12858   2911  -4221   1233       C  
ATOM   2574  CG1 ILE A1116      31.422  11.108  44.529  1.00127.56           C  
ANISOU 2574  CG1 ILE A1116    14632  20751  13083   2888  -4267    941       C  
ATOM   2575  CG2 ILE A1116      30.649   8.886  45.485  1.00127.75           C  
ANISOU 2575  CG2 ILE A1116    14936  20698  12907   3116  -4390   1587       C  
ATOM   2576  CD1 ILE A1116      31.061  12.514  44.097  1.00127.52           C  
ANISOU 2576  CD1 ILE A1116    14613  20721  13117   2674  -4112    609       C  
ATOM   2577  N   ILE A1117      29.110  10.964  42.052  1.00122.06           N  
ANISOU 2577  N   ILE A1117    14233  19288  12858   2733  -3686    951       N  
ATOM   2578  CA  ILE A1117      29.357  10.711  40.635  1.00120.74           C  
ANISOU 2578  CA  ILE A1117    13998  18835  13042   2775  -3581    902       C  
ATOM   2579  C   ILE A1117      30.570  11.534  40.213  1.00120.92           C  
ANISOU 2579  C   ILE A1117    13765  18986  13193   2742  -3651    641       C  
ATOM   2580  O   ILE A1117      30.415  12.663  39.725  1.00120.61           O  
ANISOU 2580  O   ILE A1117    13685  18922  13218   2563  -3532    398       O  
ATOM   2581  CB  ILE A1117      28.125  11.046  39.779  1.00119.36           C  
ANISOU 2581  CB  ILE A1117    13969  18401  12981   2641  -3318    847       C  
ATOM   2582  CG1 ILE A1117      26.897  10.292  40.293  1.00119.38           C  
ANISOU 2582  CG1 ILE A1117    14202  18333  12826   2639  -3256   1115       C  
ATOM   2583  CG2 ILE A1117      28.379  10.695  38.323  1.00117.98           C  
ANISOU 2583  CG2 ILE A1117    13731  17947  13147   2699  -3219    811       C  
ATOM   2584  CD1 ILE A1117      25.847  11.188  40.916  1.00119.63           C  
ANISOU 2584  CD1 ILE A1117    14336  18507  12610   2478  -3131   1019       C  
ATOM   2585  N   PRO A1118      31.794  11.022  40.396  1.00123.01           N  
ANISOU 2585  N   PRO A1118    13847  19398  13495   2903  -3852    690       N  
ATOM   2586  CA  PRO A1118      33.006  11.769  40.037  1.00124.06           C  
ANISOU 2586  CA  PRO A1118    13699  19703  13734   2857  -3931    466       C  
ATOM   2587  C   PRO A1118      33.482  11.487  38.613  1.00123.48           C  
ANISOU 2587  C   PRO A1118    13479  19458  13978   2932  -3832    417       C  
ATOM   2588  O   PRO A1118      34.668  11.240  38.369  1.00123.70           O  
ANISOU 2588  O   PRO A1118    13260  19638  14103   3058  -3958    390       O  
ATOM   2589  CB  PRO A1118      34.016  11.285  41.077  1.00124.57           C  
ANISOU 2589  CB  PRO A1118    13635  20060  13637   3012  -4207    568       C  
ATOM   2590  CG  PRO A1118      33.607   9.861  41.338  1.00124.47           C  
ANISOU 2590  CG  PRO A1118    13794  19898  13600   3233  -4258    882       C  
ATOM   2591  CD  PRO A1118      32.115   9.758  41.082  1.00123.82           C  
ANISOU 2591  CD  PRO A1118    13990  19547  13510   3128  -4041    969       C  
ATOM   2592  N   SER A1119      32.558  11.529  37.658  1.00123.36           N  
ANISOU 2592  N   SER A1119    13603  19154  14114   2860  -3606    400       N  
ATOM   2593  CA  SER A1119      32.868  11.156  36.288  1.00122.47           C  
ANISOU 2593  CA  SER A1119    13384  18871  14280   2949  -3498    367       C  
ATOM   2594  C   SER A1119      33.595  12.283  35.558  1.00122.79           C  
ANISOU 2594  C   SER A1119    13178  19039  14438   2775  -3445    124       C  
ATOM   2595  O   SER A1119      33.527  13.456  35.936  1.00123.53           O  
ANISOU 2595  O   SER A1119    13258  19243  14436   2540  -3445    -31       O  
ATOM   2596  CB  SER A1119      31.590  10.789  35.531  1.00121.00           C  
ANISOU 2596  CB  SER A1119    13439  18335  14201   2924  -3285    442       C  
ATOM   2597  OG  SER A1119      30.875   9.764  36.197  1.00121.84           O  
ANISOU 2597  OG  SER A1119    13774  18322  14199   3042  -3339    691       O  
ATOM   2598  N   TYR A1120      34.310  11.904  34.499  1.00122.70           N  
ANISOU 2598  N   TYR A1120    12970  19018  14631   2895  -3410     94       N  
ATOM   2599  CA  TYR A1120      34.907  12.870  33.585  1.00122.48           C  
ANISOU 2599  CA  TYR A1120    12708  19092  14736   2717  -3325    -98       C  
ATOM   2600  C   TYR A1120      34.011  13.157  32.391  1.00121.01           C  
ANISOU 2600  C   TYR A1120    12647  18624  14708   2600  -3074   -151       C  
ATOM   2601  O   TYR A1120      34.053  14.265  31.842  1.00121.09           O  
ANISOU 2601  O   TYR A1120    12573  18658  14779   2353  -2983   -300       O  
ATOM   2602  CB  TYR A1120      36.261  12.366  33.078  1.00122.53           C  
ANISOU 2602  CB  TYR A1120    12381  19324  14850   2911  -3420   -110       C  
ATOM   2603  CG  TYR A1120      37.332  12.218  34.138  1.00124.41           C  
ANISOU 2603  CG  TYR A1120    12428  19895  14950   3012  -3679    -82       C  
ATOM   2604  CD1 TYR A1120      37.477  11.035  34.851  1.00124.64           C  
ANISOU 2604  CD1 TYR A1120    12529  19925  14902   3311  -3839     92       C  
ATOM   2605  CD2 TYR A1120      38.211  13.259  34.410  1.00125.20           C  
ANISOU 2605  CD2 TYR A1120    12273  20301  14998   2799  -3779   -220       C  
ATOM   2606  CE1 TYR A1120      38.462  10.898  35.813  1.00125.89           C  
ANISOU 2606  CE1 TYR A1120    12507  20398  14928   3412  -4085    124       C  
ATOM   2607  CE2 TYR A1120      39.197  13.132  35.370  1.00126.92           C  
ANISOU 2607  CE2 TYR A1120    12301  20838  15083   2885  -4024   -197       C  
ATOM   2608  CZ  TYR A1120      39.318  11.950  36.069  1.00127.19           C  
ANISOU 2608  CZ  TYR A1120    12406  20883  15035   3201  -4173    -27       C  
ATOM   2609  OH  TYR A1120      40.301  11.821  37.022  1.00127.67           O  
ANISOU 2609  OH  TYR A1120    12277  21272  14959   3295  -4426      1       O  
ATOM   2610  N   PHE A1121      33.209  12.177  31.977  1.00120.20           N  
ANISOU 2610  N   PHE A1121    12746  18250  14675   2766  -2977    -23       N  
ATOM   2611  CA  PHE A1121      32.272  12.315  30.873  1.00118.98           C  
ANISOU 2611  CA  PHE A1121    12730  17818  14659   2678  -2749    -56       C  
ATOM   2612  C   PHE A1121      30.935  11.735  31.300  1.00118.63           C  
ANISOU 2612  C   PHE A1121    13018  17511  14544   2707  -2692     93       C  
ATOM   2613  O   PHE A1121      30.872  10.592  31.763  1.00119.47           O  
ANISOU 2613  O   PHE A1121    13226  17551  14614   2920  -2797    267       O  
ATOM   2614  CB  PHE A1121      32.763  11.591  29.610  1.00117.53           C  
ANISOU 2614  CB  PHE A1121    12407  17579  14670   2868  -2679    -66       C  
ATOM   2615  CG  PHE A1121      34.213  11.833  29.281  1.00118.22           C  
ANISOU 2615  CG  PHE A1121    12124  17991  14804   2915  -2762   -167       C  
ATOM   2616  CD1 PHE A1121      35.200  11.037  29.837  1.00119.14           C  
ANISOU 2616  CD1 PHE A1121    12082  18308  14879   3175  -2960   -105       C  
ATOM   2617  CD2 PHE A1121      34.586  12.829  28.390  1.00118.40           C  
ANISOU 2617  CD2 PHE A1121    11947  18129  14910   2700  -2646   -309       C  
ATOM   2618  CE1 PHE A1121      36.531  11.243  29.537  1.00119.77           C  
ANISOU 2618  CE1 PHE A1121    11791  18725  14991   3225  -3034   -195       C  
ATOM   2619  CE2 PHE A1121      35.922  13.038  28.082  1.00119.20           C  
ANISOU 2619  CE2 PHE A1121    11680  18570  15042   2724  -2718   -382       C  
ATOM   2620  CZ  PHE A1121      36.895  12.241  28.657  1.00119.94           C  
ANISOU 2620  CZ  PHE A1121    11598  18888  15087   2992  -2908   -331       C  
ATOM   2621  N   GLU A1122      29.870  12.519  31.143  1.00117.02           N  
ANISOU 2621  N   GLU A1122    12979  17165  14320   2492  -2537     34       N  
ATOM   2622  CA  GLU A1122      28.518  12.090  31.504  1.00117.53           C  
ANISOU 2622  CA  GLU A1122    13333  17019  14306   2485  -2460    170       C  
ATOM   2623  C   GLU A1122      27.508  12.922  30.725  1.00116.40           C  
ANISOU 2623  C   GLU A1122    13297  16697  14232   2286  -2247     65       C  
ATOM   2624  O   GLU A1122      26.858  13.824  31.266  1.00116.97           O  
ANISOU 2624  O   GLU A1122    13465  16800  14179   2119  -2207     -9       O  
ATOM   2625  CB  GLU A1122      28.298  12.215  33.009  1.00118.82           C  
ANISOU 2625  CB  GLU A1122    13588  17346  14212   2456  -2588    242       C  
ATOM   2626  CG  GLU A1122      27.173  11.347  33.554  1.00118.88           C  
ANISOU 2626  CG  GLU A1122    13847  17210  14112   2513  -2566    464       C  
ATOM   2627  CD  GLU A1122      27.642   9.958  33.916  1.00119.56           C  
ANISOU 2627  CD  GLU A1122    13953  17274  14201   2748  -2733    685       C  
ATOM   2628  OE1 GLU A1122      28.863   9.776  34.076  1.00119.23           O  
ANISOU 2628  OE1 GLU A1122    13722  17398  14180   2879  -2890    653       O  
ATOM   2629  OE2 GLU A1122      26.797   9.048  34.042  1.00119.81           O  
ANISOU 2629  OE2 GLU A1122    14186  17121  14215   2798  -2719    896       O  
ATOM   2630  N   PRO A1123      27.373  12.659  29.424  1.00111.47           N  
ANISOU 2630  N   PRO A1123    12656  15892  13806   2313  -2113     44       N  
ATOM   2631  CA  PRO A1123      26.321  13.339  28.657  1.00111.15           C  
ANISOU 2631  CA  PRO A1123    12737  15664  13832   2141  -1915    -29       C  
ATOM   2632  C   PRO A1123      24.927  13.002  29.149  1.00110.97           C  
ANISOU 2632  C   PRO A1123    12970  15487  13706   2119  -1848     99       C  
ATOM   2633  O   PRO A1123      24.018  13.838  29.045  1.00110.38           O  
ANISOU 2633  O   PRO A1123    12996  15346  13598   1959  -1725     22       O  
ATOM   2634  CB  PRO A1123      26.556  12.841  27.227  1.00109.36           C  
ANISOU 2634  CB  PRO A1123    12435  15301  13817   2227  -1816    -47       C  
ATOM   2635  CG  PRO A1123      27.297  11.548  27.374  1.00109.04           C  
ANISOU 2635  CG  PRO A1123    12336  15289  13806   2494  -1954     66       C  
ATOM   2636  CD  PRO A1123      28.136  11.700  28.611  1.00110.81           C  
ANISOU 2636  CD  PRO A1123    12449  15774  13878   2524  -2144     79       C  
ATOM   2637  N   PHE A1124      24.778  11.805  29.720  1.00116.14           N  
ANISOU 2637  N   PHE A1124    13723  16101  14302   2276  -1940    299       N  
ATOM   2638  CA  PHE A1124      23.477  11.388  30.296  1.00115.99           C  
ANISOU 2638  CA  PHE A1124    13930  15980  14160   2238  -1892    465       C  
ATOM   2639  C   PHE A1124      23.716  10.945  31.741  1.00117.87           C  
ANISOU 2639  C   PHE A1124    14198  16408  14180   2308  -2066    611       C  
ATOM   2640  O   PHE A1124      24.406   9.930  31.937  1.00118.32           O  
ANISOU 2640  O   PHE A1124    14228  16458  14269   2482  -2216    745       O  
ATOM   2641  CB  PHE A1124      22.896  10.202  29.524  1.00114.44           C  
ANISOU 2641  CB  PHE A1124    13865  15507  14110   2331  -1845    624       C  
ATOM   2642  CG  PHE A1124      23.082  10.209  28.029  1.00112.61           C  
ANISOU 2642  CG  PHE A1124    13570  15105  14111   2354  -1734    505       C  
ATOM   2643  CD1 PHE A1124      22.186  10.866  27.205  1.00109.88           C  
ANISOU 2643  CD1 PHE A1124    13283  14634  13834   2204  -1546    416       C  
ATOM   2644  CD2 PHE A1124      24.134   9.525  27.444  1.00113.42           C  
ANISOU 2644  CD2 PHE A1124    13552  15190  14353   2544  -1822    482       C  
ATOM   2645  CE1 PHE A1124      22.351  10.855  25.830  1.00108.17           C  
ANISOU 2645  CE1 PHE A1124    13008  14281  13810   2223  -1447    316       C  
ATOM   2646  CE2 PHE A1124      24.300   9.519  26.069  1.00112.04           C  
ANISOU 2646  CE2 PHE A1124    13309  14897  14363   2576  -1714    367       C  
ATOM   2647  CZ  PHE A1124      23.408  10.185  25.264  1.00109.30           C  
ANISOU 2647  CZ  PHE A1124    13026  14429  14073   2406  -1526    290       C  
ATOM   2648  N   GLY A1125      23.172  11.674  32.713  1.00113.53           N  
ANISOU 2648  N   GLY A1125    13702  16027  13408   2193  -2055    581       N  
ATOM   2649  CA  GLY A1125      23.322  11.320  34.109  1.00114.88           C  
ANISOU 2649  CA  GLY A1125    13901  16412  13334   2246  -2210    720       C  
ATOM   2650  C   GLY A1125      22.293  10.298  34.543  1.00114.61           C  
ANISOU 2650  C   GLY A1125    14055  16292  13201   2262  -2197   1005       C  
ATOM   2651  O   GLY A1125      21.523  10.539  35.477  1.00114.80           O  
ANISOU 2651  O   GLY A1125    14159  16479  12981   2184  -2173   1073       O  
ATOM   2652  N   LEU A1126      22.273   9.148  33.862  1.00116.80           N  
ANISOU 2652  N   LEU A1126    14399  16319  13661   2361  -2220   1172       N  
ATOM   2653  CA  LEU A1126      21.268   8.130  34.151  1.00116.49           C  
ANISOU 2653  CA  LEU A1126    14548  16151  13561   2343  -2220   1465       C  
ATOM   2654  C   LEU A1126      21.405   7.600  35.572  1.00118.14           C  
ANISOU 2654  C   LEU A1126    14801  16572  13514   2382  -2392   1691       C  
ATOM   2655  O   LEU A1126      20.400   7.373  36.257  1.00118.51           O  
ANISOU 2655  O   LEU A1126    14966  16696  13367   2278  -2354   1886       O  
ATOM   2656  CB  LEU A1126      21.375   6.986  33.142  1.00115.19           C  
ANISOU 2656  CB  LEU A1126    14458  15650  13659   2457  -2257   1577       C  
ATOM   2657  CG  LEU A1126      20.080   6.579  32.435  1.00114.75           C  
ANISOU 2657  CG  LEU A1126    14563  15340  13695   2344  -2115   1688       C  
ATOM   2658  CD1 LEU A1126      19.373   7.797  31.854  1.00113.50           C  
ANISOU 2658  CD1 LEU A1126    14360  15222  13545   2187  -1886   1465       C  
ATOM   2659  CD2 LEU A1126      20.353   5.544  31.358  1.00113.75           C  
ANISOU 2659  CD2 LEU A1126    14503  14877  13841   2479  -2174   1734       C  
ATOM   2660  N   VAL A1127      22.640   7.397  36.034  1.00116.63           N  
ANISOU 2660  N   VAL A1127    14503  16504  13307   2528  -2584   1678       N  
ATOM   2661  CA  VAL A1127      22.854   6.915  37.395  1.00117.29           C  
ANISOU 2661  CA  VAL A1127    14622  16807  13138   2574  -2765   1894       C  
ATOM   2662  C   VAL A1127      22.386   7.951  38.409  1.00118.46           C  
ANISOU 2662  C   VAL A1127    14743  17294  12973   2438  -2700   1801       C  
ATOM   2663  O   VAL A1127      21.786   7.609  39.435  1.00119.84           O  
ANISOU 2663  O   VAL A1127    15008  17639  12886   2389  -2740   2023       O  
ATOM   2664  CB  VAL A1127      24.333   6.536  37.599  1.00118.46           C  
ANISOU 2664  CB  VAL A1127    14639  17024  13347   2777  -2990   1873       C  
ATOM   2665  CG1 VAL A1127      25.246   7.622  37.048  1.00118.34           C  
ANISOU 2665  CG1 VAL A1127    14406  17118  13439   2781  -2945   1526       C  
ATOM   2666  CG2 VAL A1127      24.623   6.286  39.072  1.00120.20           C  
ANISOU 2666  CG2 VAL A1127    14869  17529  13272   2811  -3178   2054       C  
ATOM   2667  N   ALA A1128      22.642   9.233  38.137  1.00120.12           N  
ANISOU 2667  N   ALA A1128    14831  17610  13198   2375  -2607   1473       N  
ATOM   2668  CA  ALA A1128      22.164  10.283  39.029  1.00120.65           C  
ANISOU 2668  CA  ALA A1128    14890  17970  12980   2266  -2551   1336       C  
ATOM   2669  C   ALA A1128      20.642  10.333  39.055  1.00120.65           C  
ANISOU 2669  C   ALA A1128    15023  17953  12866   2145  -2363   1431       C  
ATOM   2670  O   ALA A1128      20.042  10.498  40.122  1.00121.47           O  
ANISOU 2670  O   ALA A1128    15168  18330  12655   2100  -2359   1508       O  
ATOM   2671  CB  ALA A1128      22.740  11.635  38.610  1.00119.96           C  
ANISOU 2671  CB  ALA A1128    14671  17931  12976   2215  -2511    964       C  
ATOM   2672  N   LEU A1129      20.001  10.177  37.893  1.00118.85           N  
ANISOU 2672  N   LEU A1129    14850  17432  12875   2095  -2207   1428       N  
ATOM   2673  CA  LEU A1129      18.542  10.198  37.833  1.00118.81           C  
ANISOU 2673  CA  LEU A1129    14949  17414  12778   1977  -2028   1523       C  
ATOM   2674  C   LEU A1129      17.936   9.114  38.716  1.00119.94           C  
ANISOU 2674  C   LEU A1129    15194  17663  12713   1954  -2094   1902       C  
ATOM   2675  O   LEU A1129      16.993   9.368  39.475  1.00120.63           O  
ANISOU 2675  O   LEU A1129    15310  18003  12522   1869  -2009   1975       O  
ATOM   2676  CB  LEU A1129      18.075  10.029  36.386  1.00116.77           C  
ANISOU 2676  CB  LEU A1129    14733  16805  12831   1937  -1885   1489       C  
ATOM   2677  CG  LEU A1129      18.255  11.209  35.430  1.00115.81           C  
ANISOU 2677  CG  LEU A1129    14532  16585  12886   1904  -1765   1146       C  
ATOM   2678  CD1 LEU A1129      17.650  10.884  34.074  1.00114.08           C  
ANISOU 2678  CD1 LEU A1129    14368  16043  12932   1862  -1626   1166       C  
ATOM   2679  CD2 LEU A1129      17.632  12.468  36.008  1.00116.78           C  
ANISOU 2679  CD2 LEU A1129    14641  16942  12789   1831  -1668    940       C  
ATOM   2680  N   GLU A1130      18.471   7.893  38.631  1.00120.66           N  
ANISOU 2680  N   GLU A1130    15341  17573  12930   2032  -2253   2153       N  
ATOM   2681  CA  GLU A1130      17.920   6.783  39.402  1.00121.57           C  
ANISOU 2681  CA  GLU A1130    15575  17740  12877   1988  -2342   2554       C  
ATOM   2682  C   GLU A1130      18.092   6.996  40.901  1.00123.21           C  
ANISOU 2682  C   GLU A1130    15744  18370  12701   1994  -2443   2636       C  
ATOM   2683  O   GLU A1130      17.290   6.490  41.694  1.00124.24           O  
ANISOU 2683  O   GLU A1130    15945  18678  12583   1899  -2442   2929       O  
ATOM   2684  CB  GLU A1130      18.578   5.472  38.970  1.00121.55           C  
ANISOU 2684  CB  GLU A1130    15656  17412  13113   2100  -2531   2775       C  
ATOM   2685  CG  GLU A1130      18.379   5.137  37.500  1.00119.49           C  
ANISOU 2685  CG  GLU A1130    15449  16739  13212   2107  -2446   2706       C  
ATOM   2686  CD  GLU A1130      19.434   4.185  36.970  1.00119.43           C  
ANISOU 2686  CD  GLU A1130    15471  16445  13463   2300  -2643   2758       C  
ATOM   2687  OE1 GLU A1130      20.421   3.927  37.692  1.00120.37           O  
ANISOU 2687  OE1 GLU A1130    15540  16694  13499   2438  -2839   2809       O  
ATOM   2688  OE2 GLU A1130      19.278   3.694  35.832  1.00118.23           O  
ANISOU 2688  OE2 GLU A1130    15388  15948  13587   2328  -2609   2739       O  
ATOM   2689  N   ALA A1131      19.121   7.741  41.308  1.00124.62           N  
ANISOU 2689  N   ALA A1131    15803  18732  12813   2093  -2534   2388       N  
ATOM   2690  CA  ALA A1131      19.341   7.989  42.729  1.00126.12           C  
ANISOU 2690  CA  ALA A1131    15955  19337  12628   2109  -2642   2435       C  
ATOM   2691  C   ALA A1131      18.384   9.044  43.272  1.00126.85           C  
ANISOU 2691  C   ALA A1131    16022  19747  12428   2012  -2467   2265       C  
ATOM   2692  O   ALA A1131      17.839   8.883  44.370  1.00128.03           O  
ANISOU 2692  O   ALA A1131    16193  20231  12220   1969  -2478   2449       O  
ATOM   2693  CB  ALA A1131      20.790   8.410  42.971  1.00126.28           C  
ANISOU 2693  CB  ALA A1131    15853  19447  12682   2242  -2820   2222       C  
ATOM   2694  N   MET A1132      18.256  10.144  42.530  1.00125.08           N  
ANISOU 2694  N   MET A1132    15745  19435  12344   1993  -2321   1906       N  
ATOM   2695  CA  MET A1132      17.378  11.250  42.972  1.00125.47           C  
ANISOU 2695  CA  MET A1132    15776  19758  12140   1939  -2165   1688       C  
ATOM   2696  C   MET A1132      15.944  10.729  42.949  1.00125.60           C  
ANISOU 2696  C   MET A1132    15862  19811  12048   1832  -1998   1943       C  
ATOM   2697  O   MET A1132      15.130  11.182  43.770  1.00125.80           O  
ANISOU 2697  O   MET A1132    15870  20196  11732   1804  -1909   1925       O  
ATOM   2698  CB  MET A1132      17.527  12.440  42.022  1.00124.53           C  
ANISOU 2698  CB  MET A1132    15611  19453  12251   1936  -2063   1283       C  
ATOM   2699  CG  MET A1132      18.944  12.951  41.919  1.00124.53           C  
ANISOU 2699  CG  MET A1132    15524  19405  12387   2002  -2225   1048       C  
ATOM   2700  SD  MET A1132      19.007  14.668  41.370  1.00124.12           S  
ANISOU 2700  SD  MET A1132    15428  19297  12435   1964  -2142    560       S  
ATOM   2701  CE  MET A1132      17.977  14.582  39.908  1.00122.78           C  
ANISOU 2701  CE  MET A1132    15320  18769  12563   1890  -1904    585       C  
ATOM   2702  N   CYS A1133      15.669   9.764  42.066  1.00132.19           N  
ANISOU 2702  N   CYS A1133    16768  20306  13154   1779  -1971   2180       N  
ATOM   2703  CA  CYS A1133      14.304   9.184  41.945  1.00131.74           C  
ANISOU 2703  CA  CYS A1133    16772  20252  13029   1645  -1827   2451       C  
ATOM   2704  C   CYS A1133      14.019   8.286  43.145  1.00132.56           C  
ANISOU 2704  C   CYS A1133    16912  20647  12810   1589  -1927   2850       C  
ATOM   2705  O   CYS A1133      12.867   7.862  43.293  1.00132.81           O  
ANISOU 2705  O   CYS A1133    16969  20789  12703   1454  -1816   3101       O  
ATOM   2706  CB  CYS A1133      14.135   8.389  40.656  1.00130.60           C  
ANISOU 2706  CB  CYS A1133    16708  19643  13273   1595  -1799   2582       C  
ATOM   2707  SG  CYS A1133      14.251   9.404  39.161  1.00129.11           S  
ANISOU 2707  SG  CYS A1133    16477  19140  13440   1627  -1649   2161       S  
ATOM   2708  N   LEU A1134      15.044   7.934  43.916  1.00128.59           N  
ANISOU 2708  N   LEU A1134    16406  20248  12203   1679  -2140   2937       N  
ATOM   2709  CA  LEU A1134      14.774   7.195  45.173  1.00130.00           C  
ANISOU 2709  CA  LEU A1134    16614  20761  12021   1622  -2241   3317       C  
ATOM   2710  C   LEU A1134      15.153   8.046  46.390  1.00130.93           C  
ANISOU 2710  C   LEU A1134    16639  21361  11748   1705  -2288   3125       C  
ATOM   2711  O   LEU A1134      15.087   7.522  47.507  1.00132.48           O  
ANISOU 2711  O   LEU A1134    16844  21881  11612   1677  -2388   3412       O  
ATOM   2712  CB  LEU A1134      15.441   5.823  45.105  1.00129.89           C  
ANISOU 2712  CB  LEU A1134    16707  20459  12187   1640  -2469   3679       C  
ATOM   2713  CG  LEU A1134      14.747   4.876  44.129  1.00129.21           C  
ANISOU 2713  CG  LEU A1134    16739  19965  12390   1522  -2425   3933       C  
ATOM   2714  CD1 LEU A1134      15.744   4.067  43.324  1.00128.75           C  
ANISOU 2714  CD1 LEU A1134    16766  19428  12725   1642  -2611   3972       C  
ATOM   2715  CD2 LEU A1134      13.750   3.978  44.840  1.00129.73           C  
ANISOU 2715  CD2 LEU A1134    16878  20208  12207   1332  -2434   4413       C  
ATOM   2716  N   GLY A1135      15.475   9.327  46.189  1.00127.92           N  
ANISOU 2716  N   GLY A1135    16180  21032  11392   1791  -2221   2662       N  
ATOM   2717  CA  GLY A1135      15.736  10.233  47.327  1.00128.49           C  
ANISOU 2717  CA  GLY A1135    16178  21559  11084   1869  -2266   2432       C  
ATOM   2718  C   GLY A1135      17.189  10.353  47.751  1.00129.27           C  
ANISOU 2718  C   GLY A1135    16240  21675  11200   1986  -2505   2309       C  
ATOM   2719  O   GLY A1135      17.461  11.171  48.638  1.00129.93           O  
ANISOU 2719  O   GLY A1135    16268  22112  10988   2048  -2559   2078       O  
ATOM   2720  N   ALA A1136      18.106   9.599  47.148  1.00128.90           N  
ANISOU 2720  N   ALA A1136    16217  21279  11481   2027  -2652   2435       N  
ATOM   2721  CA  ALA A1136      19.531   9.811  47.487  1.00128.74           C  
ANISOU 2721  CA  ALA A1136    16126  21298  11490   2147  -2876   2282       C  
ATOM   2722  C   ALA A1136      19.941  11.210  47.028  1.00128.67           C  
ANISOU 2722  C   ALA A1136    16037  21253  11599   2173  -2822   1781       C  
ATOM   2723  O   ALA A1136      19.631  11.564  45.881  1.00127.85           O  
ANISOU 2723  O   ALA A1136    15941  20840  11797   2132  -2672   1622       O  
ATOM   2724  CB  ALA A1136      20.370   8.774  46.811  1.00128.57           C  
ANISOU 2724  CB  ALA A1136    16129  20908  11813   2210  -3024   2483       C  
ATOM   2725  N   ILE A1137      20.641  11.957  47.882  1.00129.65           N  
ANISOU 2725  N   ILE A1137    16091  21671  11498   2230  -2957   1553       N  
ATOM   2726  CA  ILE A1137      21.116  13.319  47.502  1.00129.14           C  
ANISOU 2726  CA  ILE A1137    15961  21557  11547   2234  -2950   1080       C  
ATOM   2727  C   ILE A1137      22.415  13.139  46.729  1.00128.72           C  
ANISOU 2727  C   ILE A1137    15825  21223  11861   2271  -3089   1023       C  
ATOM   2728  O   ILE A1137      23.297  12.426  47.215  1.00129.62           O  
ANISOU 2728  O   ILE A1137    15892  21420  11936   2346  -3289   1206       O  
ATOM   2729  CB  ILE A1137      21.273  14.232  48.731  1.00130.53           C  
ANISOU 2729  CB  ILE A1137    16110  22160  11327   2270  -3049    837       C  
ATOM   2730  CG1 ILE A1137      20.013  14.232  49.600  1.00131.38           C  
ANISOU 2730  CG1 ILE A1137    16278  22623  11019   2263  -2916    940       C  
ATOM   2731  CG2 ILE A1137      21.652  15.642  48.309  1.00130.38           C  
ANISOU 2731  CG2 ILE A1137    16056  22043  11441   2250  -3054    359       C  
ATOM   2732  CD1 ILE A1137      20.157  13.490  50.907  1.00131.68           C  
ANISOU 2732  CD1 ILE A1137    16311  23059  10663   2301  -3059   1236       C  
ATOM   2733  N   PRO A1138      22.562  13.728  45.531  1.00128.80           N  
ANISOU 2733  N   PRO A1138    15804  20919  12215   2227  -2992    791       N  
ATOM   2734  CA  PRO A1138      23.738  13.478  44.726  1.00128.09           C  
ANISOU 2734  CA  PRO A1138    15611  20595  12463   2263  -3101    764       C  
ATOM   2735  C   PRO A1138      24.869  14.503  44.776  1.00128.70           C  
ANISOU 2735  C   PRO A1138    15556  20754  12590   2244  -3245    433       C  
ATOM   2736  O   PRO A1138      24.641  15.671  44.550  1.00129.39           O  
ANISOU 2736  O   PRO A1138    15650  20818  12694   2159  -3176    124       O  
ATOM   2737  CB  PRO A1138      23.133  13.508  43.321  1.00126.55           C  
ANISOU 2737  CB  PRO A1138    15456  20026  12599   2203  -2891    727       C  
ATOM   2738  CG  PRO A1138      22.013  14.528  43.403  1.00126.41           C  
ANISOU 2738  CG  PRO A1138    15515  20076  12437   2118  -2716    516       C  
ATOM   2739  CD  PRO A1138      21.574  14.561  44.851  1.00128.41           C  
ANISOU 2739  CD  PRO A1138    15811  20731  12247   2148  -2772    580       C  
ATOM   2740  N   ILE A1139      26.073  14.044  45.124  1.00128.13           N  
ANISOU 2740  N   ILE A1139    15367  20785  12532   2324  -3461    510       N  
ATOM   2741  CA  ILE A1139      27.264  14.933  45.011  1.00128.67           C  
ANISOU 2741  CA  ILE A1139    15275  20914  12701   2284  -3609    221       C  
ATOM   2742  C   ILE A1139      27.857  14.493  43.683  1.00128.07           C  
ANISOU 2742  C   ILE A1139    15096  20538  13028   2305  -3565    266       C  
ATOM   2743  O   ILE A1139      28.058  13.287  43.521  1.00127.95           O  
ANISOU 2743  O   ILE A1139    15077  20438  13098   2432  -3604    543       O  
ATOM   2744  CB  ILE A1139      28.275  14.721  46.153  1.00129.86           C  
ANISOU 2744  CB  ILE A1139    15326  21393  12624   2361  -3878    269       C  
ATOM   2745  CG1 ILE A1139      27.850  15.441  47.430  1.00131.07           C  
ANISOU 2745  CG1 ILE A1139    15555  21878  12368   2329  -3939    127       C  
ATOM   2746  CG2 ILE A1139      29.657  15.188  45.734  1.00130.33           C  
ANISOU 2746  CG2 ILE A1139    15175  21455  12889   2335  -4034     82       C  
ATOM   2747  CD1 ILE A1139      28.777  15.191  48.590  1.00133.67           C  
ANISOU 2747  CD1 ILE A1139    15795  22550  12444   2405  -4207    190       C  
ATOM   2748  N   ALA A1140      28.059  15.408  42.745  1.00126.66           N  
ANISOU 2748  N   ALA A1140    14851  20195  13080   2189  -3485     12       N  
ATOM   2749  CA  ALA A1140      28.513  14.940  41.419  1.00125.60           C  
ANISOU 2749  CA  ALA A1140    14617  19798  13306   2217  -3413     66       C  
ATOM   2750  C   ALA A1140      29.460  15.920  40.744  1.00126.01           C  
ANISOU 2750  C   ALA A1140    14487  19836  13554   2097  -3459   -196       C  
ATOM   2751  O   ALA A1140      29.523  17.081  41.168  1.00127.12           O  
ANISOU 2751  O   ALA A1140    14628  20085  13585   1959  -3516   -438       O  
ATOM   2752  CB  ALA A1140      27.318  14.698  40.544  1.00124.22           C  
ANISOU 2752  CB  ALA A1140    14594  19335  13269   2189  -3168    140       C  
ATOM   2753  N   SER A1141      30.182  15.434  39.740  1.00132.80           N  
ANISOU 2753  N   SER A1141    15196  20576  14685   2152  -3446   -141       N  
ATOM   2754  CA  SER A1141      31.094  16.306  38.962  1.00132.99           C  
ANISOU 2754  CA  SER A1141    15018  20603  14909   2016  -3471   -353       C  
ATOM   2755  C   SER A1141      30.277  17.263  38.089  1.00132.50           C  
ANISOU 2755  C   SER A1141    15061  20303  14980   1834  -3274   -521       C  
ATOM   2756  O   SER A1141      29.171  16.886  37.685  1.00131.62           O  
ANISOU 2756  O   SER A1141    15124  19984  14903   1870  -3091   -427       O  
ATOM   2757  CB  SER A1141      32.032  15.468  38.143  1.00132.40           C  
ANISOU 2757  CB  SER A1141    14741  20510  15055   2151  -3497   -243       C  
ATOM   2758  OG  SER A1141      32.408  16.152  36.962  1.00132.25           O  
ANISOU 2758  OG  SER A1141    14581  20395  15272   2011  -3400   -393       O  
ATOM   2759  N   ALA A1142      30.806  18.457  37.813  1.00124.92           N  
ANISOU 2759  N   ALA A1142    13999  19371  14095   1636  -3326   -749       N  
ATOM   2760  CA  ALA A1142      30.102  19.422  36.941  1.00124.03           C  
ANISOU 2760  CA  ALA A1142    13986  19015  14124   1459  -3164   -904       C  
ATOM   2761  C   ALA A1142      30.411  19.085  35.485  1.00123.21           C  
ANISOU 2761  C   ALA A1142    13752  18749  14313   1450  -3028   -839       C  
ATOM   2762  O   ALA A1142      31.096  19.886  34.830  1.00123.93           O  
ANISOU 2762  O   ALA A1142    13693  18844  14552   1274  -3055   -964       O  
ATOM   2763  CB  ALA A1142      30.551  20.817  37.273  1.00125.10           C  
ANISOU 2763  CB  ALA A1142    14088  19223  14221   1241  -3307  -1159       C  
ATOM   2764  N   VAL A1143      29.921  17.941  35.007  1.00123.23           N  
ANISOU 2764  N   VAL A1143    13814  18622  14385   1626  -2895   -646       N  
ATOM   2765  CA  VAL A1143      30.238  17.505  33.617  1.00121.94           C  
ANISOU 2765  CA  VAL A1143    13526  18326  14482   1657  -2771   -591       C  
ATOM   2766  C   VAL A1143      28.965  17.093  32.872  1.00120.42           C  
ANISOU 2766  C   VAL A1143    13536  17843  14375   1697  -2548   -509       C  
ATOM   2767  O   VAL A1143      28.196  16.292  33.425  1.00119.98           O  
ANISOU 2767  O   VAL A1143    13647  17736  14203   1827  -2524   -361       O  
ATOM   2768  CB  VAL A1143      31.285  16.375  33.623  1.00120.95           C  
ANISOU 2768  CB  VAL A1143    13204  18356  14396   1872  -2881   -452       C  
ATOM   2769  CG1 VAL A1143      31.163  15.490  32.397  1.00120.17           C  
ANISOU 2769  CG1 VAL A1143    13082  18076  14502   2010  -2733   -351       C  
ATOM   2770  CG2 VAL A1143      32.700  16.915  33.756  1.00122.25           C  
ANISOU 2770  CG2 VAL A1143    13077  18797  14574   1790  -3053   -556       C  
ATOM   2771  N   GLY A1144      28.744  17.633  31.672  1.00120.17           N  
ANISOU 2771  N   GLY A1144    13487  17642  14530   1572  -2399   -590       N  
ATOM   2772  CA  GLY A1144      27.617  17.180  30.836  1.00118.62           C  
ANISOU 2772  CA  GLY A1144    13458  17180  14433   1614  -2194   -510       C  
ATOM   2773  C   GLY A1144      26.277  17.273  31.523  1.00119.29           C  
ANISOU 2773  C   GLY A1144    13795  17170  14361   1607  -2128   -483       C  
ATOM   2774  O   GLY A1144      25.959  18.348  32.050  1.00120.85           O  
ANISOU 2774  O   GLY A1144    14063  17405  14451   1473  -2156   -634       O  
ATOM   2775  N   GLY A1145      25.520  16.176  31.514  1.00117.47           N  
ANISOU 2775  N   GLY A1145    13693  16827  14113   1747  -2053   -298       N  
ATOM   2776  CA  GLY A1145      24.166  16.174  32.090  1.00117.12           C  
ANISOU 2776  CA  GLY A1145    13865  16723  13914   1734  -1967   -241       C  
ATOM   2777  C   GLY A1145      24.175  16.479  33.569  1.00118.87           C  
ANISOU 2777  C   GLY A1145    14125  17180  13861   1739  -2101   -265       C  
ATOM   2778  O   GLY A1145      23.280  17.177  34.019  1.00119.54           O  
ANISOU 2778  O   GLY A1145    14333  17281  13804   1670  -2043   -355       O  
ATOM   2779  N   LEU A1146      25.152  15.952  34.296  1.00116.86           N  
ANISOU 2779  N   LEU A1146    13763  17116  13522   1836  -2280   -192       N  
ATOM   2780  CA  LEU A1146      25.255  16.238  35.745  1.00118.12           C  
ANISOU 2780  CA  LEU A1146    13948  17534  13397   1845  -2427   -218       C  
ATOM   2781  C   LEU A1146      25.061  17.738  35.980  1.00119.06           C  
ANISOU 2781  C   LEU A1146    14096  17701  13442   1687  -2429   -494       C  
ATOM   2782  O   LEU A1146      24.327  18.088  36.913  1.00119.08           O  
ANISOU 2782  O   LEU A1146    14222  17822  13203   1688  -2433   -538       O  
ATOM   2783  CB  LEU A1146      26.617  15.749  36.239  1.00118.26           C  
ANISOU 2783  CB  LEU A1146    13792  17748  13392   1942  -2637   -163       C  
ATOM   2784  CG  LEU A1146      26.893  14.263  36.031  1.00116.52           C  
ANISOU 2784  CG  LEU A1146    13555  17463  13256   2131  -2672     95       C  
ATOM   2785  CD1 LEU A1146      28.339  13.931  36.358  1.00118.24           C  
ANISOU 2785  CD1 LEU A1146    13567  17877  13484   2238  -2881    107       C  
ATOM   2786  CD2 LEU A1146      25.946  13.417  36.864  1.00116.55           C  
ANISOU 2786  CD2 LEU A1146    13746  17476  13062   2206  -2666    329       C  
ATOM   2787  N   ARG A1147      25.686  18.586  35.159  1.00128.09           N  
ANISOU 2787  N   ARG A1147    15132  18757  14779   1559  -2434   -669       N  
ATOM   2788  CA  ARG A1147      25.520  20.029  35.296  1.00128.90           C  
ANISOU 2788  CA  ARG A1147    15286  18845  14844   1399  -2462   -930       C  
ATOM   2789  C   ARG A1147      24.117  20.467  34.896  1.00128.39           C  
ANISOU 2789  C   ARG A1147    15410  18586  14785   1368  -2275   -984       C  
ATOM   2790  O   ARG A1147      23.545  21.375  35.511  1.00129.19           O  
ANISOU 2790  O   ARG A1147    15630  18725  14733   1329  -2300  -1162       O  
ATOM   2791  CB  ARG A1147      26.560  20.753  34.446  1.00129.55           C  
ANISOU 2791  CB  ARG A1147    15202  18874  15149   1242  -2523  -1057       C  
ATOM   2792  CG  ARG A1147      26.526  22.263  34.551  1.00131.22           C  
ANISOU 2792  CG  ARG A1147    15473  19031  15352   1052  -2598  -1318       C  
ATOM   2793  CD  ARG A1147      27.723  22.850  33.826  1.00131.73           C  
ANISOU 2793  CD  ARG A1147    15339  19095  15618    871  -2693  -1391       C  
ATOM   2794  NE  ARG A1147      27.814  22.313  32.473  1.00130.79           N  
ANISOU 2794  NE  ARG A1147    15120  18840  15733    873  -2529  -1259       N  
ATOM   2795  CZ  ARG A1147      28.843  22.495  31.656  1.00131.25           C  
ANISOU 2795  CZ  ARG A1147    14961  18940  15968    752  -2562  -1255       C  
ATOM   2796  NH1 ARG A1147      29.878  23.244  32.002  1.00132.78           N  
ANISOU 2796  NH1 ARG A1147    15008  19287  16154    588  -2756  -1364       N  
ATOM   2797  NH2 ARG A1147      28.831  21.915  30.459  1.00129.58           N  
ANISOU 2797  NH2 ARG A1147    14669  18630  15935    792  -2399  -1138       N  
ATOM   2798  N   ASP A1148      23.550  19.842  33.862  1.00123.83           N  
ANISOU 2798  N   ASP A1148    14862  17809  14381   1397  -2096   -846       N  
ATOM   2799  CA  ASP A1148      22.219  20.232  33.408  1.00123.24           C  
ANISOU 2799  CA  ASP A1148    14946  17558  14322   1369  -1919   -887       C  
ATOM   2800  C   ASP A1148      21.140  19.725  34.358  1.00122.93           C  
ANISOU 2800  C   ASP A1148    15037  17643  14029   1478  -1865   -780       C  
ATOM   2801  O   ASP A1148      20.149  20.421  34.608  1.00123.74           O  
ANISOU 2801  O   ASP A1148    15259  17741  14016   1467  -1791   -901       O  
ATOM   2802  CB  ASP A1148      21.972  19.714  31.992  1.00121.53           C  
ANISOU 2802  CB  ASP A1148    14711  17104  14361   1357  -1756   -775       C  
ATOM   2803  CG  ASP A1148      23.115  20.033  31.046  1.00122.39           C  
ANISOU 2803  CG  ASP A1148    14654  17152  14696   1261  -1801   -838       C  
ATOM   2804  OD1 ASP A1148      23.734  21.106  31.202  1.00124.30           O  
ANISOU 2804  OD1 ASP A1148    14843  17441  14945   1130  -1914  -1018       O  
ATOM   2805  OD2 ASP A1148      23.393  19.210  30.146  1.00120.86           O  
ANISOU 2805  OD2 ASP A1148    14382  16874  14667   1313  -1729   -708       O  
ATOM   2806  N   ILE A1149      21.319  18.524  34.903  1.00119.98           N  
ANISOU 2806  N   ILE A1149    14638  17393  13557   1587  -1907   -549       N  
ATOM   2807  CA  ILE A1149      20.306  17.940  35.779  1.00120.34           C  
ANISOU 2807  CA  ILE A1149    14792  17578  13354   1665  -1855   -395       C  
ATOM   2808  C   ILE A1149      20.382  18.544  37.176  1.00121.84           C  
ANISOU 2808  C   ILE A1149    15000  18063  13229   1690  -1982   -523       C  
ATOM   2809  O   ILE A1149      19.414  19.132  37.671  1.00122.41           O  
ANISOU 2809  O   ILE A1149    15168  18233  13109   1698  -1911   -629       O  
ATOM   2810  CB  ILE A1149      20.450  16.407  35.825  1.00119.76           C  
ANISOU 2810  CB  ILE A1149    14706  17497  13300   1757  -1875    -74       C  
ATOM   2811  CG1 ILE A1149      20.438  15.823  34.410  1.00118.07           C  
ANISOU 2811  CG1 ILE A1149    14479  16986  13397   1750  -1768     15       C  
ATOM   2812  CG2 ILE A1149      19.343  15.791  36.669  1.00120.42           C  
ANISOU 2812  CG2 ILE A1149    14899  17725  13130   1795  -1816    125       C  
ATOM   2813  CD1 ILE A1149      20.737  14.340  34.356  1.00116.84           C  
ANISOU 2813  CD1 ILE A1149    14322  16770  13302   1857  -1827    295       C  
ATOM   2814  N   ILE A1150      21.530  18.406  37.830  1.00122.31           N  
ANISOU 2814  N   ILE A1150    14963  18289  13220   1717  -2174   -525       N  
ATOM   2815  CA  ILE A1150      21.668  18.819  39.222  1.00123.31           C  
ANISOU 2815  CA  ILE A1150    15104  18724  13023   1754  -2315   -623       C  
ATOM   2816  C   ILE A1150      21.990  20.305  39.283  1.00124.37           C  
ANISOU 2816  C   ILE A1150    15244  18850  13162   1665  -2400   -980       C  
ATOM   2817  O   ILE A1150      22.947  20.775  38.656  1.00124.82           O  
ANISOU 2817  O   ILE A1150    15205  18783  13439   1570  -2486  -1095       O  
ATOM   2818  CB  ILE A1150      22.748  17.988  39.932  1.00124.16           C  
ANISOU 2818  CB  ILE A1150    15108  19021  13045   1825  -2504   -457       C  
ATOM   2819  CG1 ILE A1150      22.527  16.499  39.666  1.00123.77           C  
ANISOU 2819  CG1 ILE A1150    15072  18891  13065   1908  -2446   -102       C  
ATOM   2820  CG2 ILE A1150      22.731  18.264  41.426  1.00125.20           C  
ANISOU 2820  CG2 ILE A1150    15270  19503  12799   1874  -2636   -518       C  
ATOM   2821  CD1 ILE A1150      23.669  15.625  40.118  1.00122.35           C  
ANISOU 2821  CD1 ILE A1150    14787  18827  12873   2001  -2639     67       C  
ATOM   2822  N   THR A1151      21.191  21.046  40.041  1.00128.82           N  
ANISOU 2822  N   THR A1151    15917  19553  13476   1694  -2386  -1155       N  
ATOM   2823  CA  THR A1151      21.429  22.451  40.326  1.00129.97           C  
ANISOU 2823  CA  THR A1151    16106  19701  13575   1635  -2508  -1510       C  
ATOM   2824  C   THR A1151      21.759  22.608  41.809  1.00131.21           C  
ANISOU 2824  C   THR A1151    16266  20211  13377   1707  -2689  -1602       C  
ATOM   2825  O   THR A1151      21.934  21.624  42.536  1.00131.44           O  
ANISOU 2825  O   THR A1151    16245  20476  13221   1788  -2725  -1370       O  
ATOM   2826  CB  THR A1151      20.219  23.292  39.910  1.00129.96           C  
ANISOU 2826  CB  THR A1151    16244  19548  13589   1640  -2358  -1690       C  
ATOM   2827  OG1 THR A1151      20.550  24.684  39.988  1.00130.49           O  
ANISOU 2827  OG1 THR A1151    16371  19526  13683   1570  -2503  -2040       O  
ATOM   2828  CG2 THR A1151      19.024  23.000  40.811  1.00129.70           C  
ANISOU 2828  CG2 THR A1151    16290  19775  13214   1783  -2250  -1637       C  
ATOM   2829  N   ASN A1152      21.847  23.861  42.261  1.00134.32           N  
ANISOU 2829  N   ASN A1152    16730  20633  13671   1679  -2818  -1944       N  
ATOM   2830  CA  ASN A1152      22.201  24.119  43.653  1.00135.31           C  
ANISOU 2830  CA  ASN A1152    16865  21095  13451   1746  -3009  -2077       C  
ATOM   2831  C   ASN A1152      21.148  23.570  44.608  1.00135.59           C  
ANISOU 2831  C   ASN A1152    16963  21446  13110   1909  -2897  -1961       C  
ATOM   2832  O   ASN A1152      21.482  23.029  45.669  1.00136.31           O  
ANISOU 2832  O   ASN A1152    17008  21865  12918   1978  -3004  -1851       O  
ATOM   2833  CB  ASN A1152      22.391  25.619  43.873  1.00136.04           C  
ANISOU 2833  CB  ASN A1152    17053  21111  13525   1687  -3175  -2495       C  
ATOM   2834  CG  ASN A1152      23.313  25.923  45.036  1.00137.69           C  
ANISOU 2834  CG  ASN A1152    17226  21594  13496   1687  -3447  -2646       C  
ATOM   2835  OD1 ASN A1152      23.850  25.015  45.670  1.00138.79           O  
ANISOU 2835  OD1 ASN A1152    17257  21993  13486   1734  -3511  -2428       O  
ATOM   2836  ND2 ASN A1152      23.497  27.206  45.326  1.00138.25           N  
ANISOU 2836  ND2 ASN A1152    17398  21598  13532   1635  -3626  -3020       N  
ATOM   2837  N   GLU A1153      19.869  23.688  44.245  1.00137.58           N  
ANISOU 2837  N   GLU A1153    17305  21627  13344   1966  -2684  -1968       N  
ATOM   2838  CA  GLU A1153      18.785  23.279  45.130  1.00137.85           C  
ANISOU 2838  CA  GLU A1153    17378  21997  13003   2107  -2564  -1872       C  
ATOM   2839  C   GLU A1153      18.664  21.767  45.275  1.00137.78           C  
ANISOU 2839  C   GLU A1153    17293  22127  12931   2117  -2474  -1421       C  
ATOM   2840  O   GLU A1153      17.899  21.306  46.130  1.00138.03           O  
ANISOU 2840  O   GLU A1153    17334  22492  12619   2205  -2400  -1282       O  
ATOM   2841  CB  GLU A1153      17.458  23.851  44.627  1.00137.15           C  
ANISOU 2841  CB  GLU A1153    17382  21799  12930   2163  -2362  -2007       C  
ATOM   2842  CG  GLU A1153      17.489  25.345  44.336  1.00137.47           C  
ANISOU 2842  CG  GLU A1153    17529  21623  13080   2159  -2455  -2441       C  
ATOM   2843  CD  GLU A1153      17.293  26.184  45.584  1.00138.98           C  
ANISOU 2843  CD  GLU A1153    17797  22124  12884   2300  -2587  -2769       C  
ATOM   2844  OE1 GLU A1153      16.130  26.373  45.997  1.00138.84           O  
ANISOU 2844  OE1 GLU A1153    17828  22316  12608   2456  -2452  -2853       O  
ATOM   2845  OE2 GLU A1153      18.301  26.657  46.151  1.00139.81           O  
ANISOU 2845  OE2 GLU A1153    17908  22280  12935   2261  -2831  -2952       O  
ATOM   2846  N   THR A1154      19.391  20.986  44.476  1.00133.51           N  
ANISOU 2846  N   THR A1154    16678  21348  12701   2033  -2488  -1188       N  
ATOM   2847  CA  THR A1154      19.266  19.534  44.507  1.00132.75           C  
ANISOU 2847  CA  THR A1154    16540  21310  12590   2047  -2423   -762       C  
ATOM   2848  C   THR A1154      20.515  18.809  44.982  1.00132.89           C  
ANISOU 2848  C   THR A1154    16467  21429  12598   2055  -2629   -592       C  
ATOM   2849  O   THR A1154      20.395  17.755  45.609  1.00132.93           O  
ANISOU 2849  O   THR A1154    16462  21625  12419   2102  -2645   -277       O  
ATOM   2850  CB  THR A1154      18.891  19.000  43.119  1.00131.38           C  
ANISOU 2850  CB  THR A1154    16370  20765  12784   1983  -2252   -592       C  
ATOM   2851  OG1 THR A1154      19.538  19.784  42.110  1.00130.82           O  
ANISOU 2851  OG1 THR A1154    16276  20382  13047   1904  -2285   -822       O  
ATOM   2852  CG2 THR A1154      17.383  19.054  42.915  1.00130.94           C  
ANISOU 2852  CG2 THR A1154    16388  20723  12640   1999  -2024   -557       C  
ATOM   2853  N   GLY A1155      21.704  19.334  44.703  1.00129.54           N  
ANISOU 2853  N   GLY A1155    15969  20888  12362   2005  -2794   -776       N  
ATOM   2854  CA  GLY A1155      22.912  18.646  45.110  1.00129.08           C  
ANISOU 2854  CA  GLY A1155    15801  20939  12303   2028  -2992   -619       C  
ATOM   2855  C   GLY A1155      24.109  19.569  45.087  1.00129.29           C  
ANISOU 2855  C   GLY A1155    15740  20948  12436   1959  -3191   -906       C  
ATOM   2856  O   GLY A1155      24.010  20.752  44.756  1.00129.49           O  
ANISOU 2856  O   GLY A1155    15807  20849  12543   1879  -3188  -1222       O  
ATOM   2857  N   ILE A1156      25.254  19.002  45.445  1.00131.82           N  
ANISOU 2857  N   ILE A1156    15935  21391  12758   1986  -3381   -782       N  
ATOM   2858  CA  ILE A1156      26.518  19.728  45.498  1.00132.26           C  
ANISOU 2858  CA  ILE A1156    15868  21482  12902   1908  -3597  -1006       C  
ATOM   2859  C   ILE A1156      27.372  19.330  44.301  1.00131.63           C  
ANISOU 2859  C   ILE A1156    15641  21157  13217   1859  -3590   -908       C  
ATOM   2860  O   ILE A1156      27.509  18.141  43.990  1.00130.90           O  
ANISOU 2860  O   ILE A1156    15500  21014  13223   1954  -3549   -614       O  
ATOM   2861  CB  ILE A1156      27.245  19.480  46.835  1.00133.21           C  
ANISOU 2861  CB  ILE A1156    15927  21980  12708   1979  -3837   -968       C  
ATOM   2862  CG1 ILE A1156      26.250  19.532  48.001  1.00134.56           C  
ANISOU 2862  CG1 ILE A1156    16240  22437  12451   2064  -3800   -972       C  
ATOM   2863  CG2 ILE A1156      28.382  20.465  47.023  1.00134.01           C  
ANISOU 2863  CG2 ILE A1156    15920  22149  12849   1871  -4070  -1258       C  
ATOM   2864  CD1 ILE A1156      26.680  18.767  49.238  1.00135.69           C  
ANISOU 2864  CD1 ILE A1156    16339  22951  12265   2167  -3971   -766       C  
ATOM   2865  N   LEU A1157      27.917  20.329  43.611  1.00128.69           N  
ANISOU 2865  N   LEU A1157    15202  20630  13064   1712  -3631  -1156       N  
ATOM   2866  CA  LEU A1157      28.666  20.146  42.375  1.00127.65           C  
ANISOU 2866  CA  LEU A1157    14917  20289  13297   1645  -3599  -1103       C  
ATOM   2867  C   LEU A1157      30.140  20.443  42.616  1.00129.14           C  
ANISOU 2867  C   LEU A1157    14893  20650  13523   1575  -3845  -1192       C  
ATOM   2868  O   LEU A1157      30.485  21.411  43.299  1.00129.84           O  
ANISOU 2868  O   LEU A1157    14988  20873  13472   1473  -4017  -1429       O  
ATOM   2869  CB  LEU A1157      28.128  21.054  41.262  1.00125.67           C  
ANISOU 2869  CB  LEU A1157    14735  19730  13283   1500  -3442  -1279       C  
ATOM   2870  CG  LEU A1157      27.088  20.465  40.300  1.00125.27           C  
ANISOU 2870  CG  LEU A1157    14783  19424  13390   1551  -3176  -1118       C  
ATOM   2871  CD1 LEU A1157      27.571  19.167  39.666  1.00125.05           C  
ANISOU 2871  CD1 LEU A1157    14632  19341  13538   1655  -3132   -839       C  
ATOM   2872  CD2 LEU A1157      25.767  20.250  41.018  1.00125.79           C  
ANISOU 2872  CD2 LEU A1157    15041  19561  13195   1650  -3062  -1062       C  
ATOM   2873  N   VAL A1158      31.010  19.602  42.059  1.00131.68           N  
ANISOU 2873  N   VAL A1158    15025  20978  14031   1638  -3872  -1009       N  
ATOM   2874  CA  VAL A1158      32.450  19.687  42.289  1.00132.66           C  
ANISOU 2874  CA  VAL A1158    14904  21316  14184   1601  -4103  -1047       C  
ATOM   2875  C   VAL A1158      33.175  19.466  40.969  1.00132.72           C  
ANISOU 2875  C   VAL A1158    14705  21193  14529   1562  -4035   -993       C  
ATOM   2876  O   VAL A1158      32.774  18.621  40.162  1.00131.83           O  
ANISOU 2876  O   VAL A1158    14617  20900  14572   1679  -3859   -819       O  
ATOM   2877  CB  VAL A1158      32.906  18.665  43.353  1.00133.37           C  
ANISOU 2877  CB  VAL A1158    14940  21686  14049   1799  -4265   -845       C  
ATOM   2878  CG1 VAL A1158      34.417  18.618  43.445  1.00134.91           C  
ANISOU 2878  CG1 VAL A1158    14849  22104  14307   1790  -4491   -858       C  
ATOM   2879  CG2 VAL A1158      32.317  19.025  44.700  1.00134.21           C  
ANISOU 2879  CG2 VAL A1158    15219  21988  13787   1813  -4352   -925       C  
ATOM   2880  N   LYS A1159      34.241  20.234  40.749  1.00137.03           N  
ANISOU 2880  N   LYS A1159    15043  21844  15178   1390  -4180  -1145       N  
ATOM   2881  CA  LYS A1159      35.012  20.115  39.519  1.00137.19           C  
ANISOU 2881  CA  LYS A1159    14827  21809  15489   1335  -4121  -1104       C  
ATOM   2882  C   LYS A1159      35.658  18.739  39.416  1.00136.73           C  
ANISOU 2882  C   LYS A1159    14596  21884  15472   1594  -4146   -870       C  
ATOM   2883  O   LYS A1159      36.224  18.222  40.383  1.00137.36           O  
ANISOU 2883  O   LYS A1159    14602  22211  15378   1729  -4334   -792       O  
ATOM   2884  CB  LYS A1159      36.081  21.206  39.458  1.00138.62           C  
ANISOU 2884  CB  LYS A1159    14797  22136  15734   1076  -4303  -1290       C  
ATOM   2885  CG  LYS A1159      35.773  22.310  38.461  1.00139.02           C  
ANISOU 2885  CG  LYS A1159    14896  21939  15986    808  -4192  -1441       C  
ATOM   2886  CD  LYS A1159      36.233  23.665  38.971  1.00140.65           C  
ANISOU 2886  CD  LYS A1159    15094  22209  16136    524  -4411  -1677       C  
ATOM   2887  CE  LYS A1159      35.535  24.795  38.230  1.00140.27           C  
ANISOU 2887  CE  LYS A1159    15223  21839  16235    289  -4310  -1832       C  
ATOM   2888  NZ  LYS A1159      35.945  24.862  36.800  1.00138.94           N  
ANISOU 2888  NZ  LYS A1159    14867  21574  16350    152  -4177  -1750       N  
ATOM   2889  N   ALA A1160      35.571  18.148  38.228  1.00136.73           N  
ANISOU 2889  N   ALA A1160    14539  21712  15701   1676  -3966   -767       N  
ATOM   2890  CA  ALA A1160      36.096  16.809  38.011  1.00135.67           C  
ANISOU 2890  CA  ALA A1160    14272  21648  15629   1955  -3983   -564       C  
ATOM   2891  C   ALA A1160      37.620  16.811  38.023  1.00136.54           C  
ANISOU 2891  C   ALA A1160    14019  22078  15781   1969  -4173   -589       C  
ATOM   2892  O   ALA A1160      38.269  17.802  37.678  1.00137.80           O  
ANISOU 2892  O   ALA A1160    13991  22349  16017   1728  -4220   -744       O  
ATOM   2893  CB  ALA A1160      35.591  16.246  36.683  1.00134.03           C  
ANISOU 2893  CB  ALA A1160    14106  21169  15652   2038  -3746   -484       C  
ATOM   2894  N   GLY A1161      38.192  15.678  38.429  1.00131.51           N  
ANISOU 2894  N   GLY A1161    13281  21593  15095   2252  -4295   -425       N  
ATOM   2895  CA  GLY A1161      39.627  15.502  38.434  1.00131.91           C  
ANISOU 2895  CA  GLY A1161    12967  21972  15181   2326  -4475   -428       C  
ATOM   2896  C   GLY A1161      40.341  15.995  39.671  1.00134.38           C  
ANISOU 2896  C   GLY A1161    13172  22605  15281   2240  -4744   -493       C  
ATOM   2897  O   GLY A1161      41.549  15.761  39.801  1.00135.68           O  
ANISOU 2897  O   GLY A1161    13022  23078  15451   2325  -4918   -477       O  
ATOM   2898  N   ASP A1162      39.648  16.672  40.582  1.00138.29           N  
ANISOU 2898  N   ASP A1162    13906  23058  15579   2085  -4789   -577       N  
ATOM   2899  CA  ASP A1162      40.253  17.123  41.830  1.00140.06           C  
ANISOU 2899  CA  ASP A1162    14060  23586  15571   2013  -5057   -651       C  
ATOM   2900  C   ASP A1162      39.686  16.310  42.984  1.00140.26           C  
ANISOU 2900  C   ASP A1162    14310  23641  15340   2232  -5135   -491       C  
ATOM   2901  O   ASP A1162      38.541  16.549  43.402  1.00140.01           O  
ANISOU 2901  O   ASP A1162    14583  23444  15171   2179  -5035   -510       O  
ATOM   2902  CB  ASP A1162      40.005  18.616  42.050  1.00140.81           C  
ANISOU 2902  CB  ASP A1162    14241  23649  15611   1663  -5089   -903       C  
ATOM   2903  CG  ASP A1162      41.031  19.247  42.974  1.00142.71           C  
ANISOU 2903  CG  ASP A1162    14291  24234  15696   1528  -5389  -1026       C  
ATOM   2904  OD1 ASP A1162      41.465  18.575  43.932  1.00143.17           O  
ANISOU 2904  OD1 ASP A1162    14296  24540  15564   1721  -5572   -919       O  
ATOM   2905  OD2 ASP A1162      41.404  20.417  42.744  1.00143.69           O  
ANISOU 2905  OD2 ASP A1162    14326  24378  15891   1219  -5458  -1223       O  
ATOM   2906  N   PRO A1163      40.430  15.345  43.516  1.00143.08           N  
ANISOU 2906  N   PRO A1163    14527  24217  15621   2481  -5312   -321       N  
ATOM   2907  CA  PRO A1163      39.913  14.526  44.621  1.00142.98           C  
ANISOU 2907  CA  PRO A1163    14730  24240  15356   2679  -5401   -129       C  
ATOM   2908  C   PRO A1163      39.861  15.283  45.939  1.00144.19           C  
ANISOU 2908  C   PRO A1163    14965  24629  15191   2538  -5579   -248       C  
ATOM   2909  O   PRO A1163      39.040  14.975  46.811  1.00144.32           O  
ANISOU 2909  O   PRO A1163    15232  24641  14963   2606  -5579   -143       O  
ATOM   2910  CB  PRO A1163      40.908  13.358  44.684  1.00143.14           C  
ANISOU 2910  CB  PRO A1163    14536  24427  15422   2984  -5569     69       C  
ATOM   2911  CG  PRO A1163      41.621  13.381  43.360  1.00142.52           C  
ANISOU 2911  CG  PRO A1163    14184  24314  15655   2993  -5475     -5       C  
ATOM   2912  CD  PRO A1163      41.715  14.835  43.020  1.00143.29           C  
ANISOU 2912  CD  PRO A1163    14193  24448  15802   2627  -5421   -270       C  
ATOM   2913  N   GLY A1164      40.751  16.264  46.104  1.00138.23           N  
ANISOU 2913  N   GLY A1164    13993  24101  14425   2337  -5741   -464       N  
ATOM   2914  CA  GLY A1164      40.683  17.114  47.281  1.00138.69           C  
ANISOU 2914  CA  GLY A1164    14145  24360  14192   2182  -5915   -630       C  
ATOM   2915  C   GLY A1164      39.401  17.920  47.328  1.00138.75           C  
ANISOU 2915  C   GLY A1164    14467  24134  14119   2018  -5740   -787       C  
ATOM   2916  O   GLY A1164      38.786  18.069  48.387  1.00139.23           O  
ANISOU 2916  O   GLY A1164    14733  24294  13874   2035  -5798   -815       O  
ATOM   2917  N   GLU A1165      38.978  18.447  46.177  1.00142.79           N  
ANISOU 2917  N   GLU A1165    15013  24350  14891   1869  -5526   -891       N  
ATOM   2918  CA  GLU A1165      37.687  19.121  46.095  1.00142.30           C  
ANISOU 2918  CA  GLU A1165    15251  24036  14781   1752  -5340  -1023       C  
ATOM   2919  C   GLU A1165      36.548  18.152  46.380  1.00141.25           C  
ANISOU 2919  C   GLU A1165    15363  23791  14515   1964  -5176   -798       C  
ATOM   2920  O   GLU A1165      35.539  18.526  46.992  1.00141.19           O  
ANISOU 2920  O   GLU A1165    15598  23759  14289   1937  -5111   -872       O  
ATOM   2921  CB  GLU A1165      37.524  19.759  44.715  1.00141.68           C  
ANISOU 2921  CB  GLU A1165    15141  23662  15029   1570  -5150  -1138       C  
ATOM   2922  CG  GLU A1165      38.328  21.032  44.515  1.00143.13           C  
ANISOU 2922  CG  GLU A1165    15167  23908  15309   1274  -5301  -1394       C  
ATOM   2923  CD  GLU A1165      37.751  22.212  45.271  1.00144.46           C  
ANISOU 2923  CD  GLU A1165    15562  24042  15283   1101  -5389  -1664       C  
ATOM   2924  OE1 GLU A1165      36.561  22.153  45.647  1.00144.00           O  
ANISOU 2924  OE1 GLU A1165    15786  23862  15067   1198  -5256  -1672       O  
ATOM   2925  OE2 GLU A1165      38.483  23.201  45.485  1.00145.42           O  
ANISOU 2925  OE2 GLU A1165    15581  24265  15409    871  -5599  -1872       O  
ATOM   2926  N   LEU A1166      36.690  16.899  45.941  1.00137.92           N  
ANISOU 2926  N   LEU A1166    14879  23305  14218   2176  -5115   -522       N  
ATOM   2927  CA  LEU A1166      35.718  15.874  46.304  1.00137.41           C  
ANISOU 2927  CA  LEU A1166    15036  23153  14020   2361  -5008   -265       C  
ATOM   2928  C   LEU A1166      35.749  15.602  47.802  1.00138.42           C  
ANISOU 2928  C   LEU A1166    15231  23595  13767   2452  -5206   -174       C  
ATOM   2929  O   LEU A1166      34.699  15.409  48.427  1.00138.35           O  
ANISOU 2929  O   LEU A1166    15452  23589  13525   2484  -5122    -82       O  
ATOM   2930  CB  LEU A1166      35.990  14.592  45.516  1.00136.69           C  
ANISOU 2930  CB  LEU A1166    14867  22907  14162   2572  -4950     -3       C  
ATOM   2931  CG  LEU A1166      35.254  13.319  45.946  1.00135.74           C  
ANISOU 2931  CG  LEU A1166    14945  22707  13922   2776  -4917    323       C  
ATOM   2932  CD1 LEU A1166      33.755  13.553  46.053  1.00135.06           C  
ANISOU 2932  CD1 LEU A1166    15142  22459  13714   2680  -4703    332       C  
ATOM   2933  CD2 LEU A1166      35.553  12.179  44.985  1.00134.25           C  
ANISOU 2933  CD2 LEU A1166    14692  22301  14018   2974  -4870    522       C  
ATOM   2934  N   ALA A1167      36.945  15.586  48.397  1.00143.60           N  
ANISOU 2934  N   ALA A1167    15676  24546  14339   2491  -5472   -192       N  
ATOM   2935  CA  ALA A1167      37.048  15.402  49.840  1.00144.67           C  
ANISOU 2935  CA  ALA A1167    15862  25011  14093   2566  -5681   -121       C  
ATOM   2936  C   ALA A1167      36.321  16.512  50.588  1.00145.35           C  
ANISOU 2936  C   ALA A1167    16125  25198  13904   2401  -5668   -374       C  
ATOM   2937  O   ALA A1167      35.745  16.278  51.657  1.00145.98           O  
ANISOU 2937  O   ALA A1167    16359  25470  13634   2473  -5709   -283       O  
ATOM   2938  CB  ALA A1167      38.515  15.345  50.258  1.00145.44           C  
ANISOU 2938  CB  ALA A1167    15675  25413  14171   2613  -5977   -138       C  
ATOM   2939  N   ASN A1168      36.336  17.729  50.039  1.00145.31           N  
ANISOU 2939  N   ASN A1168    16099  25068  14042   2186  -5618   -694       N  
ATOM   2940  CA  ASN A1168      35.589  18.823  50.650  1.00145.70           C  
ANISOU 2940  CA  ASN A1168    16340  25161  13859   2054  -5605   -970       C  
ATOM   2941  C   ASN A1168      34.090  18.660  50.438  1.00144.86           C  
ANISOU 2941  C   ASN A1168    16491  24849  13701   2097  -5323   -901       C  
ATOM   2942  O   ASN A1168      33.295  19.099  51.276  1.00145.28           O  
ANISOU 2942  O   ASN A1168    16721  25038  13440   2099  -5308  -1016       O  
ATOM   2943  CB  ASN A1168      36.059  20.163  50.083  1.00146.34           C  
ANISOU 2943  CB  ASN A1168    16341  25125  14135   1806  -5662  -1320       C  
ATOM   2944  CG  ASN A1168      37.548  20.382  50.258  1.00147.39           C  
ANISOU 2944  CG  ASN A1168    16193  25484  14324   1726  -5944  -1388       C  
ATOM   2945  OD1 ASN A1168      38.174  19.797  51.142  1.00147.93           O  
ANISOU 2945  OD1 ASN A1168    16159  25863  14184   1853  -6145  -1259       O  
ATOM   2946  ND2 ASN A1168      38.124  21.226  49.410  1.00147.91           N  
ANISOU 2946  ND2 ASN A1168    16122  25408  14669   1506  -5966  -1577       N  
ATOM   2947  N   ALA A1169      33.690  18.035  49.327  1.00135.42           N  
ANISOU 2947  N   ALA A1169    15307  23346  12798   2137  -5102   -723       N  
ATOM   2948  CA  ALA A1169      32.272  17.866  49.026  1.00133.82           C  
ANISOU 2948  CA  ALA A1169    15328  22942  12576   2160  -4832   -648       C  
ATOM   2949  C   ALA A1169      31.580  17.020  50.084  1.00134.42           C  
ANISOU 2949  C   ALA A1169    15539  23236  12298   2307  -4830   -392       C  
ATOM   2950  O   ALA A1169      30.529  17.401  50.612  1.00134.73           O  
ANISOU 2950  O   ALA A1169    15751  23356  12086   2293  -4722   -467       O  
ATOM   2951  CB  ALA A1169      32.102  17.235  47.647  1.00132.31           C  
ANISOU 2951  CB  ALA A1169    15107  22398  12765   2182  -4631   -485       C  
ATOM   2952  N   ILE A1170      32.152  15.854  50.400  1.00144.86           N  
ANISOU 2952  N   ILE A1170    16781  24668  13592   2452  -4952    -78       N  
ATOM   2953  CA  ILE A1170      31.585  15.007  51.446  1.00145.53           C  
ANISOU 2953  CA  ILE A1170    16987  24977  13332   2571  -4982    208       C  
ATOM   2954  C   ILE A1170      31.850  15.554  52.838  1.00146.74           C  
ANISOU 2954  C   ILE A1170    17138  25554  13062   2568  -5187     70       C  
ATOM   2955  O   ILE A1170      31.264  15.060  53.809  1.00147.08           O  
ANISOU 2955  O   ILE A1170    17290  25842  12750   2640  -5198    268       O  
ATOM   2956  CB  ILE A1170      32.117  13.568  51.319  1.00145.39           C  
ANISOU 2956  CB  ILE A1170    16908  24900  13433   2735  -5074    600       C  
ATOM   2957  CG1 ILE A1170      33.644  13.556  51.317  1.00146.30           C  
ANISOU 2957  CG1 ILE A1170    16782  25133  13672   2790  -5327    537       C  
ATOM   2958  CG2 ILE A1170      31.588  12.919  50.047  1.00143.99           C  
ANISOU 2958  CG2 ILE A1170    16790  24309  13613   2756  -4855    756       C  
ATOM   2959  CD1 ILE A1170      34.220  12.172  51.458  1.00146.53           C  
ANISOU 2959  CD1 ILE A1170    16757  25171  13745   2996  -5474    904       C  
ATOM   2960  N   LEU A1171      32.723  16.558  52.965  1.00140.35           N  
ANISOU 2960  N   LEU A1171    16205  24850  12271   2475  -5358   -259       N  
ATOM   2961  CA  LEU A1171      32.818  17.315  54.209  1.00141.35           C  
ANISOU 2961  CA  LEU A1171    16364  25346  11997   2448  -5535   -481       C  
ATOM   2962  C   LEU A1171      31.742  18.391  54.275  1.00141.57           C  
ANISOU 2962  C   LEU A1171    16569  25331  11891   2360  -5376   -790       C  
ATOM   2963  O   LEU A1171      31.118  18.586  55.325  1.00142.19           O  
ANISOU 2963  O   LEU A1171    16764  25708  11555   2411  -5391   -841       O  
ATOM   2964  CB  LEU A1171      34.211  17.931  54.347  1.00141.34           C  
ANISOU 2964  CB  LEU A1171    16160  25473  12071   2372  -5814   -704       C  
ATOM   2965  CG  LEU A1171      35.282  17.077  55.028  1.00141.78           C  
ANISOU 2965  CG  LEU A1171    16050  25808  12010   2497  -6075   -466       C  
ATOM   2966  CD1 LEU A1171      36.392  17.952  55.585  1.00144.33           C  
ANISOU 2966  CD1 LEU A1171    16216  26383  12240   2398  -6370   -756       C  
ATOM   2967  CD2 LEU A1171      34.660  16.256  56.141  1.00142.55           C  
ANISOU 2967  CD2 LEU A1171    16283  26181  11698   2643  -6092   -181       C  
ATOM   2968  N   LYS A1172      31.462  19.031  53.139  1.00145.10           N  
ANISOU 2968  N   LYS A1172    17037  25416  12676   2248  -5212   -977       N  
ATOM   2969  CA  LYS A1172      30.328  19.988  53.106  1.00145.00           C  
ANISOU 2969  CA  LYS A1172    17208  25322  12562   2195  -5045  -1252       C  
ATOM   2970  C   LYS A1172      29.062  19.147  53.263  1.00144.91           C  
ANISOU 2970  C   LYS A1172    17330  25350  12379   2305  -4808   -963       C  
ATOM   2971  O   LYS A1172      28.091  19.653  53.841  1.00145.50           O  
ANISOU 2971  O   LYS A1172    17542  25583  12157   2336  -4716  -1111       O  
ATOM   2972  CB  LYS A1172      30.345  20.792  51.804  1.00143.85           C  
ANISOU 2972  CB  LYS A1172    17056  24766  12835   2048  -4936  -1475       C  
ATOM   2973  CG  LYS A1172      29.244  21.832  51.657  1.00143.67           C  
ANISOU 2973  CG  LYS A1172    17221  24610  12758   2005  -4785  -1774       C  
ATOM   2974  CD  LYS A1172      29.447  22.732  50.460  1.00143.38           C  
ANISOU 2974  CD  LYS A1172    17173  24184  13123   1838  -4742  -2004       C  
ATOM   2975  CE  LYS A1172      30.774  23.460  50.496  1.00144.25           C  
ANISOU 2975  CE  LYS A1172    17145  24312  13350   1686  -5022  -2219       C  
ATOM   2976  NZ  LYS A1172      30.943  24.349  49.322  1.00143.55           N  
ANISOU 2976  NZ  LYS A1172    17049  23850  13642   1495  -4983  -2412       N  
ATOM   2977  N   ALA A1173      29.091  17.896  52.790  1.00144.05           N  
ANISOU 2977  N   ALA A1173    17178  25114  12441   2366  -4728   -566       N  
ATOM   2978  CA  ALA A1173      27.955  17.005  52.978  1.00143.25           C  
ANISOU 2978  CA  ALA A1173    17196  25055  12178   2441  -4536   -244       C  
ATOM   2979  C   ALA A1173      27.874  16.448  54.392  1.00144.43           C  
ANISOU 2979  C   ALA A1173    17371  25654  11854   2534  -4664    -39       C  
ATOM   2980  O   ALA A1173      26.859  15.837  54.738  1.00144.72           O  
ANISOU 2980  O   ALA A1173    17506  25805  11675   2570  -4516    215       O  
ATOM   2981  CB  ALA A1173      28.014  15.850  51.976  1.00141.66           C  
ANISOU 2981  CB  ALA A1173    16964  24529  12331   2467  -4435    105       C  
ATOM   2982  N   LEU A1174      28.912  16.635  55.209  1.00140.07           N  
ANISOU 2982  N   LEU A1174    16723  25371  11126   2562  -4938   -128       N  
ATOM   2983  CA  LEU A1174      28.884  16.212  56.604  1.00141.14           C  
ANISOU 2983  CA  LEU A1174    16880  25970  10778   2648  -5079     41       C  
ATOM   2984  C   LEU A1174      28.283  17.285  57.506  1.00142.40           C  
ANISOU 2984  C   LEU A1174    17125  26457  10523   2645  -5075   -306       C  
ATOM   2985  O   LEU A1174      27.452  16.982  58.367  1.00142.61           O  
ANISOU 2985  O   LEU A1174    17232  26815  10140   2705  -5001   -156       O  
ATOM   2986  CB  LEU A1174      30.294  15.854  57.084  1.00141.08           C  
ANISOU 2986  CB  LEU A1174    16721  26122  10759   2696  -5392    120       C  
ATOM   2987  CG  LEU A1174      30.342  15.006  58.358  1.00143.07           C  
ANISOU 2987  CG  LEU A1174    16989  26792  10579   2800  -5543    446       C  
ATOM   2988  CD1 LEU A1174      29.420  13.800  58.243  1.00142.46           C  
ANISOU 2988  CD1 LEU A1174    17019  26634  10477   2839  -5367    918       C  
ATOM   2989  CD2 LEU A1174      31.762  14.578  58.689  1.00145.19           C  
ANISOU 2989  CD2 LEU A1174    17109  27125  10934   2846  -5827    545       C  
ATOM   2990  N   GLU A1175      28.700  18.541  57.325  1.00161.82           N  
ANISOU 2990  N   GLU A1175    19569  28836  13078   2576  -5163   -769       N  
ATOM   2991  CA  GLU A1175      28.098  19.634  58.078  1.00162.37           C  
ANISOU 2991  CA  GLU A1175    19744  29158  12790   2595  -5165  -1152       C  
ATOM   2992  C   GLU A1175      26.667  19.909  57.638  1.00161.41           C  
ANISOU 2992  C   GLU A1175    19754  28914  12659   2611  -4856  -1213       C  
ATOM   2993  O   GLU A1175      25.891  20.479  58.412  1.00162.07           O  
ANISOU 2993  O   GLU A1175    19928  29299  12351   2685  -4808  -1419       O  
ATOM   2994  CB  GLU A1175      28.940  20.903  57.937  1.00162.93           C  
ANISOU 2994  CB  GLU A1175    19786  29114  13006   2502  -5370  -1627       C  
ATOM   2995  CG  GLU A1175      29.453  21.157  56.531  1.00162.11           C  
ANISOU 2995  CG  GLU A1175    19613  28512  13470   2368  -5326  -1692       C  
ATOM   2996  CD  GLU A1175      29.725  22.625  56.269  1.00162.46           C  
ANISOU 2996  CD  GLU A1175    19703  28383  13642   2248  -5437  -2191       C  
ATOM   2997  OE1 GLU A1175      29.985  23.365  57.240  1.00163.81           O  
ANISOU 2997  OE1 GLU A1175    19914  28825  13501   2261  -5650  -2488       O  
ATOM   2998  OE2 GLU A1175      29.676  23.040  55.092  1.00161.73           O  
ANISOU 2998  OE2 GLU A1175    19614  27879  13959   2137  -5324  -2285       O  
ATOM   2999  N   LEU A1176      26.305  19.521  56.415  1.00148.24           N  
ANISOU 2999  N   LEU A1176    18090  26834  11403   2554  -4649  -1049       N  
ATOM   3000  CA  LEU A1176      24.932  19.639  55.944  1.00147.22           C  
ANISOU 3000  CA  LEU A1176    18066  26591  11281   2567  -4352  -1051       C  
ATOM   3001  C   LEU A1176      24.078  18.434  56.311  1.00146.92           C  
ANISOU 3001  C   LEU A1176    18046  26758  11018   2618  -4191   -585       C  
ATOM   3002  O   LEU A1176      22.848  18.553  56.350  1.00146.40           O  
ANISOU 3002  O   LEU A1176    18051  26790  10782   2647  -3969   -587       O  
ATOM   3003  CB  LEU A1176      24.907  19.832  54.424  1.00145.79           C  
ANISOU 3003  CB  LEU A1176    17883  25869  11641   2469  -4209  -1102       C  
ATOM   3004  CG  LEU A1176      24.784  21.263  53.894  1.00145.36           C  
ANISOU 3004  CG  LEU A1176    17896  25581  11752   2413  -4199  -1588       C  
ATOM   3005  CD1 LEU A1176      25.943  22.126  54.368  1.00146.95           C  
ANISOU 3005  CD1 LEU A1176    18054  25858  11921   2364  -4503  -1917       C  
ATOM   3006  CD2 LEU A1176      24.696  21.266  52.374  1.00143.74           C  
ANISOU 3006  CD2 LEU A1176    17682  24871  12060   2313  -4039  -1551       C  
ATOM   3007  N   SER A1177      24.698  17.282  56.582  1.00146.43           N  
ANISOU 3007  N   SER A1177    17919  26767  10951   2627  -4310   -181       N  
ATOM   3008  CA  SER A1177      23.932  16.092  56.936  1.00146.10           C  
ANISOU 3008  CA  SER A1177    17910  26893  10710   2647  -4191    300       C  
ATOM   3009  C   SER A1177      23.334  16.196  58.332  1.00146.97           C  
ANISOU 3009  C   SER A1177    18046  27585  10209   2714  -4203    316       C  
ATOM   3010  O   SER A1177      22.248  15.658  58.579  1.00147.12           O  
ANISOU 3010  O   SER A1177    18104  27790  10004   2708  -4016    587       O  
ATOM   3011  CB  SER A1177      24.814  14.849  56.837  1.00145.80           C  
ANISOU 3011  CB  SER A1177    17814  26733  10851   2653  -4350    718       C  
ATOM   3012  OG  SER A1177      25.902  14.925  57.742  1.00146.86           O  
ANISOU 3012  OG  SER A1177    17874  27149  10776   2708  -4638    663       O  
ATOM   3013  N   ARG A1178      24.028  16.888  59.239  1.00152.59           N  
ANISOU 3013  N   ARG A1178    18735  28560  10683   2757  -4403     30       N  
ATOM   3014  CA  ARG A1178      23.541  16.977  60.644  1.00156.33           C  
ANISOU 3014  CA  ARG A1178    19245  29427  10726   2774  -4347     35       C  
ATOM   3015  C   ARG A1178      22.253  17.800  60.674  1.00155.87           C  
ANISOU 3015  C   ARG A1178    19249  29481  10493   2810  -4096   -241       C  
ATOM   3016  O   ARG A1178      21.312  17.390  61.378  1.00157.79           O  
ANISOU 3016  O   ARG A1178    19503  30005  10447   2812  -3915    -27       O  
ATOM   3017  CB  ARG A1178      24.631  17.510  61.579  1.00159.77           C  
ANISOU 3017  CB  ARG A1178    19652  30019  11034   2789  -4601   -208       C  
ATOM   3018  CG  ARG A1178      25.546  18.557  60.962  1.00158.64           C  
ANISOU 3018  CG  ARG A1178    19482  29638  11157   2774  -4785   -659       C  
ATOM   3019  CD  ARG A1178      26.665  18.898  61.924  1.00162.38           C  
ANISOU 3019  CD  ARG A1178    19915  30273  11508   2764  -5050   -817       C  
ATOM   3020  NE  ARG A1178      27.331  17.694  62.400  1.00163.91           N  
ANISOU 3020  NE  ARG A1178    20041  30571  11666   2763  -5175   -366       N  
ATOM   3021  CZ  ARG A1178      28.483  17.233  61.929  1.00163.27           C  
ANISOU 3021  CZ  ARG A1178    19855  30314  11865   2745  -5379   -234       C  
ATOM   3022  NH1 ARG A1178      29.118  17.888  60.973  1.00160.96           N  
ANISOU 3022  NH1 ARG A1178    19497  29760  11902   2705  -5475   -515       N  
ATOM   3023  NH2 ARG A1178      29.005  16.127  62.427  1.00164.87           N  
ANISOU 3023  NH2 ARG A1178    20016  30606  12021   2768  -5490    175       N  
ATOM   3024  N   SER A1179      22.212  18.909  59.935  1.00149.14           N  
ANISOU 3024  N   SER A1179    18430  28415   9821   2837  -4090   -693       N  
ATOM   3025  CA  SER A1179      20.994  19.697  59.840  1.00148.25           C  
ANISOU 3025  CA  SER A1179    18379  28358   9591   2897  -3858   -967       C  
ATOM   3026  C   SER A1179      19.982  18.986  58.950  1.00145.50           C  
ANISOU 3026  C   SER A1179    18026  27899   9356   2868  -3614   -647       C  
ATOM   3027  O   SER A1179      20.345  18.207  58.063  1.00143.64           O  
ANISOU 3027  O   SER A1179    17767  27361   9448   2791  -3632   -352       O  
ATOM   3028  CB  SER A1179      21.293  21.094  59.292  1.00146.86           C  
ANISOU 3028  CB  SER A1179    18264  27929   9607   2928  -3953  -1539       C  
ATOM   3029  OG  SER A1179      21.948  21.023  58.038  1.00143.99           O  
ANISOU 3029  OG  SER A1179    17879  27142   9687   2847  -4035  -1527       O  
ATOM   3030  N   ASP A1180      18.701  19.257  59.198  1.00147.88           N  
ANISOU 3030  N   ASP A1180    18346  28391   9451   2915  -3363   -705       N  
ATOM   3031  CA  ASP A1180      17.637  18.576  58.471  1.00145.98           C  
ANISOU 3031  CA  ASP A1180    18090  28093   9281   2869  -3117   -385       C  
ATOM   3032  C   ASP A1180      17.755  18.845  56.978  1.00143.41           C  
ANISOU 3032  C   ASP A1180    17802  27212   9474   2817  -3073   -506       C  
ATOM   3033  O   ASP A1180      17.615  19.987  56.527  1.00143.00           O  
ANISOU 3033  O   ASP A1180    17802  26967   9564   2872  -3048   -960       O  
ATOM   3034  CB  ASP A1180      16.270  19.023  58.985  1.00147.42           C  
ANISOU 3034  CB  ASP A1180    18258  28567   9187   2937  -2854   -507       C  
ATOM   3035  CG  ASP A1180      15.124  18.345  58.255  1.00145.34           C  
ANISOU 3035  CG  ASP A1180    17963  28265   8995   2869  -2596   -176       C  
ATOM   3036  OD1 ASP A1180      15.314  17.210  57.769  1.00144.38           O  
ANISOU 3036  OD1 ASP A1180    17832  27996   9031   2746  -2616    289       O  
ATOM   3037  OD2 ASP A1180      14.033  18.947  58.166  1.00145.40           O  
ANISOU 3037  OD2 ASP A1180    17954  28378   8915   2941  -2383   -379       O  
ATOM   3038  N   LEU A1181      18.015  17.786  56.215  1.00138.01           N  
ANISOU 3038  N   LEU A1181    17102  26190   9146   2693  -3047    -96       N  
ATOM   3039  CA  LEU A1181      18.164  17.871  54.770  1.00136.99           C  
ANISOU 3039  CA  LEU A1181    16998  25464   9588   2612  -2971   -149       C  
ATOM   3040  C   LEU A1181      17.042  17.153  54.031  1.00136.02           C  
ANISOU 3040  C   LEU A1181    16880  25192   9608   2537  -2712    171       C  
ATOM   3041  O   LEU A1181      17.165  16.901  52.826  1.00135.35           O  
ANISOU 3041  O   LEU A1181    16813  24623   9990   2456  -2650    240       O  
ATOM   3042  CB  LEU A1181      19.529  17.324  54.336  1.00136.75           C  
ANISOU 3042  CB  LEU A1181    16938  25111   9909   2547  -3178     -6       C  
ATOM   3043  CG  LEU A1181      19.922  15.848  54.495  1.00136.52           C  
ANISOU 3043  CG  LEU A1181    16880  25083   9907   2500  -3256    530       C  
ATOM   3044  CD1 LEU A1181      21.290  15.624  53.873  1.00136.49           C  
ANISOU 3044  CD1 LEU A1181    16834  24722  10305   2479  -3450    527       C  
ATOM   3045  CD2 LEU A1181      19.936  15.376  55.946  1.00137.55           C  
ANISOU 3045  CD2 LEU A1181    16990  25762   9511   2549  -3373    748       C  
ATOM   3046  N   SER A1182      15.948  16.818  54.724  1.00133.39           N  
ANISOU 3046  N   SER A1182    16523  25287   8873   2554  -2561    367       N  
ATOM   3047  CA  SER A1182      14.780  16.268  54.043  1.00132.60           C  
ANISOU 3047  CA  SER A1182    16416  25080   8885   2470  -2311    633       C  
ATOM   3048  C   SER A1182      14.038  17.345  53.264  1.00132.15           C  
ANISOU 3048  C   SER A1182    16380  24838   8991   2526  -2135    235       C  
ATOM   3049  O   SER A1182      13.379  17.043  52.262  1.00130.39           O  
ANISOU 3049  O   SER A1182    16165  24318   9061   2445  -1963    371       O  
ATOM   3050  CB  SER A1182      13.849  15.598  55.052  1.00131.71           C  
ANISOU 3050  CB  SER A1182    16245  25527   8270   2451  -2208    983       C  
ATOM   3051  OG  SER A1182      13.572  16.461  56.141  1.00131.67           O  
ANISOU 3051  OG  SER A1182    16204  26058   7767   2600  -2214    672       O  
ATOM   3052  N   LYS A1183      14.126  18.601  53.712  1.00143.51           N  
ANISOU 3052  N   LYS A1183    17839  26442  10246   2670  -2192   -259       N  
ATOM   3053  CA  LYS A1183      13.653  19.721  52.908  1.00143.12           C  
ANISOU 3053  CA  LYS A1183    17838  26125  10417   2735  -2087   -678       C  
ATOM   3054  C   LYS A1183      14.362  19.783  51.563  1.00142.67           C  
ANISOU 3054  C   LYS A1183    17830  25423  10955   2627  -2132   -721       C  
ATOM   3055  O   LYS A1183      13.802  20.312  50.598  1.00142.29           O  
ANISOU 3055  O   LYS A1183    17817  25074  11175   2624  -1996   -889       O  
ATOM   3056  CB  LYS A1183      13.858  21.032  53.672  1.00143.79           C  
ANISOU 3056  CB  LYS A1183    17967  26441  10225   2908  -2213  -1209       C  
ATOM   3057  CG  LYS A1183      13.143  22.236  53.081  1.00142.87           C  
ANISOU 3057  CG  LYS A1183    17913  26147  10224   3019  -2107  -1649       C  
ATOM   3058  CD  LYS A1183      11.660  22.218  53.405  1.00142.44           C  
ANISOU 3058  CD  LYS A1183    17793  26500   9828   3131  -1860  -1605       C  
ATOM   3059  CE  LYS A1183      11.430  22.302  54.907  1.00142.98           C  
ANISOU 3059  CE  LYS A1183    17808  27251   9268   3279  -1901  -1672       C  
ATOM   3060  NZ  LYS A1183      11.817  23.629  55.462  1.00144.03           N  
ANISOU 3060  NZ  LYS A1183    18028  27395   9300   3451  -2063  -2242       N  
ATOM   3061  N   PHE A1184      15.557  19.199  51.472  1.00141.95           N  
ANISOU 3061  N   PHE A1184    17731  25142  11063   2544  -2315   -550       N  
ATOM   3062  CA  PHE A1184      16.284  19.174  50.176  1.00141.25           C  
ANISOU 3062  CA  PHE A1184    17661  24483  11525   2444  -2352   -567       C  
ATOM   3063  C   PHE A1184      16.190  17.780  49.556  1.00140.77           C  
ANISOU 3063  C   PHE A1184    17576  24221  11689   2335  -2273    -76       C  
ATOM   3064  O   PHE A1184      16.324  17.663  48.328  1.00140.00           O  
ANISOU 3064  O   PHE A1184    17493  23678  12023   2263  -2213    -54       O  
ATOM   3065  CB  PHE A1184      17.741  19.595  50.365  1.00142.02           C  
ANISOU 3065  CB  PHE A1184    17748  24481  11731   2437  -2619   -769       C  
ATOM   3066  CG  PHE A1184      18.054  20.991  49.894  1.00142.33           C  
ANISOU 3066  CG  PHE A1184    17840  24280  11959   2446  -2686  -1256       C  
ATOM   3067  CD1 PHE A1184      17.167  22.032  50.115  1.00141.93           C  
ANISOU 3067  CD1 PHE A1184    17859  24346  11721   2546  -2602  -1599       C  
ATOM   3068  CD2 PHE A1184      19.241  21.267  49.234  1.00142.52           C  
ANISOU 3068  CD2 PHE A1184    17841  23967  12342   2354  -2844  -1367       C  
ATOM   3069  CE1 PHE A1184      17.456  23.316  49.681  1.00141.97           C  
ANISOU 3069  CE1 PHE A1184    17940  24090  11914   2548  -2693  -2037       C  
ATOM   3070  CE2 PHE A1184      19.531  22.552  48.803  1.00142.69           C  
ANISOU 3070  CE2 PHE A1184    17918  23757  12539   2328  -2923  -1785       C  
ATOM   3071  CZ  PHE A1184      18.638  23.574  49.026  1.00142.40           C  
ANISOU 3071  CZ  PHE A1184    17981  23794  12332   2422  -2857  -2116       C  
ATOM   3072  N   ARG A1185      15.944  16.755  50.370  1.00134.62           N  
ANISOU 3072  N   ARG A1185    16770  23759  10621   2322  -2281    310       N  
ATOM   3073  CA  ARG A1185      15.925  15.362  49.852  1.00133.86           C  
ANISOU 3073  CA  ARG A1185    16677  23444  10739   2217  -2254    793       C  
ATOM   3074  C   ARG A1185      14.834  15.224  48.790  1.00133.04           C  
ANISOU 3074  C   ARG A1185    16597  23084  10869   2144  -2015    871       C  
ATOM   3075  O   ARG A1185      14.991  14.390  47.885  1.00132.07           O  
ANISOU 3075  O   ARG A1185    16500  22587  11095   2061  -2003   1117       O  
ATOM   3076  CB  ARG A1185      15.674  14.383  51.002  1.00134.62           C  
ANISOU 3076  CB  ARG A1185    16756  23959  10435   2200  -2303   1200       C  
ATOM   3077  CG  ARG A1185      16.543  13.134  50.967  1.00134.78           C  
ANISOU 3077  CG  ARG A1185    16793  23794  10621   2153  -2479   1594       C  
ATOM   3078  CD  ARG A1185      16.484  12.305  52.238  1.00135.50           C  
ANISOU 3078  CD  ARG A1185    16877  24318  10290   2142  -2582   1969       C  
ATOM   3079  NE  ARG A1185      17.537  11.299  52.306  1.00135.72           N  
ANISOU 3079  NE  ARG A1185    16927  24169  10470   2143  -2809   2266       N  
ATOM   3080  CZ  ARG A1185      17.401  10.028  51.945  1.00134.95           C  
ANISOU 3080  CZ  ARG A1185    16891  23836  10547   2062  -2834   2716       C  
ATOM   3081  NH1 ARG A1185      16.242   9.587  51.488  1.00133.55           N  
ANISOU 3081  NH1 ARG A1185    16751  23578  10413   1942  -2643   2937       N  
ATOM   3082  NH2 ARG A1185      18.423   9.199  52.048  1.00135.20           N  
ANISOU 3082  NH2 ARG A1185    16946  23712  10710   2104  -3065   2940       N  
ATOM   3083  N   GLU A1186      13.767  16.011  48.905  1.00138.35           N  
ANISOU 3083  N   GLU A1186    17259  23961  11347   2187  -1842    658       N  
ATOM   3084  CA  GLU A1186      12.662  15.892  47.967  1.00137.29           C  
ANISOU 3084  CA  GLU A1186    17130  23635  11398   2121  -1618    738       C  
ATOM   3085  C   GLU A1186      12.820  16.776  46.739  1.00136.60           C  
ANISOU 3085  C   GLU A1186    17081  23103  11718   2134  -1570    393       C  
ATOM   3086  O   GLU A1186      12.131  16.542  45.740  1.00135.80           O  
ANISOU 3086  O   GLU A1186    16992  22741  11865   2064  -1415    488       O  
ATOM   3087  CB  GLU A1186      11.332  16.173  48.691  1.00137.34           C  
ANISOU 3087  CB  GLU A1186    17081  24126  10976   2167  -1442    734       C  
ATOM   3088  CG  GLU A1186      11.092  17.597  49.233  1.00138.14           C  
ANISOU 3088  CG  GLU A1186    17173  24496  10818   2342  -1426    234       C  
ATOM   3089  CD  GLU A1186      10.977  18.683  48.170  1.00137.83           C  
ANISOU 3089  CD  GLU A1186    17186  24068  11114   2393  -1366   -169       C  
ATOM   3090  OE1 GLU A1186      10.468  18.394  47.061  1.00137.19           O  
ANISOU 3090  OE1 GLU A1186    17113  23659  11354   2305  -1230    -48       O  
ATOM   3091  OE2 GLU A1186      11.360  19.836  48.453  1.00139.35           O  
ANISOU 3091  OE2 GLU A1186    17419  24285  11241   2517  -1464   -604       O  
ATOM   3092  N   ASN A1187      13.695  17.784  46.786  1.00136.38           N  
ANISOU 3092  N   ASN A1187    17074  22987  11758   2206  -1709      8       N  
ATOM   3093  CA  ASN A1187      14.034  18.512  45.567  1.00135.93           C  
ANISOU 3093  CA  ASN A1187    17054  22472  12121   2180  -1697   -258       C  
ATOM   3094  C   ASN A1187      14.557  17.557  44.502  1.00134.75           C  
ANISOU 3094  C   ASN A1187    16902  21918  12379   2071  -1703     15       C  
ATOM   3095  O   ASN A1187      14.281  17.729  43.310  1.00133.52           O  
ANISOU 3095  O   ASN A1187    16769  21412  12551   2020  -1593    -40       O  
ATOM   3096  CB  ASN A1187      15.068  19.609  45.855  1.00136.70           C  
ANISOU 3096  CB  ASN A1187    17170  22538  12231   2232  -1891   -655       C  
ATOM   3097  CG  ASN A1187      14.519  20.738  46.722  1.00137.54           C  
ANISOU 3097  CG  ASN A1187    17310  22965  11986   2364  -1894  -1015       C  
ATOM   3098  OD1 ASN A1187      15.144  21.790  46.850  1.00138.21           O  
ANISOU 3098  OD1 ASN A1187    17437  22977  12099   2401  -2043  -1385       O  
ATOM   3099  ND2 ASN A1187      13.346  20.530  47.307  1.00137.37           N  
ANISOU 3099  ND2 ASN A1187    17265  23300  11630   2434  -1739   -914       N  
ATOM   3100  N   CYS A1188      15.306  16.534  44.923  1.00130.13           N  
ANISOU 3100  N   CYS A1188    16293  21381  11768   2049  -1839    308       N  
ATOM   3101  CA  CYS A1188      15.736  15.484  44.009  1.00129.39           C  
ANISOU 3101  CA  CYS A1188    16205  20934  12023   1980  -1854    587       C  
ATOM   3102  C   CYS A1188      14.577  14.575  43.617  1.00128.47           C  
ANISOU 3102  C   CYS A1188    16122  20762  11928   1904  -1684    917       C  
ATOM   3103  O   CYS A1188      14.602  13.969  42.540  1.00127.97           O  
ANISOU 3103  O   CYS A1188    16085  20333  12203   1847  -1642   1054       O  
ATOM   3104  CB  CYS A1188      16.856  14.668  44.656  1.00130.18           C  
ANISOU 3104  CB  CYS A1188    16277  21117  12070   2008  -2072    795       C  
ATOM   3105  SG  CYS A1188      17.980  15.636  45.692  1.00130.19           S  
ANISOU 3105  SG  CYS A1188    16224  21396  11847   2089  -2292    471       S  
ATOM   3106  N   LYS A1189      13.556  14.472  44.473  1.00131.10           N  
ANISOU 3106  N   LYS A1189    16447  21471  11895   1899  -1590   1044       N  
ATOM   3107  CA  LYS A1189      12.437  13.576  44.194  1.00130.61           C  
ANISOU 3107  CA  LYS A1189    16400  21401  11825   1796  -1443   1391       C  
ATOM   3108  C   LYS A1189      11.649  14.030  42.972  1.00129.59           C  
ANISOU 3108  C   LYS A1189    16283  20991  11965   1757  -1256   1243       C  
ATOM   3109  O   LYS A1189      11.191  13.201  42.176  1.00128.96           O  
ANISOU 3109  O   LYS A1189    16236  20661  12104   1656  -1186   1495       O  
ATOM   3110  CB  LYS A1189      11.522  13.490  45.416  1.00131.13           C  
ANISOU 3110  CB  LYS A1189    16419  22001  11402   1793  -1374   1540       C  
ATOM   3111  CG  LYS A1189      10.644  12.259  45.445  1.00131.23           C  
ANISOU 3111  CG  LYS A1189    16439  22071  11352   1645  -1300   2023       C  
ATOM   3112  CD  LYS A1189      11.463  11.014  45.718  1.00131.98           C  
ANISOU 3112  CD  LYS A1189    16594  22039  11515   1591  -1499   2399       C  
ATOM   3113  CE  LYS A1189      10.830   9.805  45.066  1.00131.89           C  
ANISOU 3113  CE  LYS A1189    16643  21769  11701   1428  -1458   2812       C  
ATOM   3114  NZ  LYS A1189      11.131   9.737  43.613  1.00130.74           N  
ANISOU 3114  NZ  LYS A1189    16556  21070  12048   1425  -1441   2691       N  
ATOM   3115  N   LYS A1190      11.484  15.340  42.804  1.00124.68           N  
ANISOU 3115  N   LYS A1190    15646  20393  11333   1838  -1191    834       N  
ATOM   3116  CA  LYS A1190      10.675  15.884  41.722  1.00123.48           C  
ANISOU 3116  CA  LYS A1190    15506  20013  11400   1817  -1019    679       C  
ATOM   3117  C   LYS A1190      11.500  16.417  40.562  1.00123.02           C  
ANISOU 3117  C   LYS A1190    15483  19505  11754   1815  -1067    442       C  
ATOM   3118  O   LYS A1190      11.026  16.390  39.421  1.00122.17           O  
ANISOU 3118  O   LYS A1190    15396  19105  11918   1760   -950    447       O  
ATOM   3119  CB  LYS A1190       9.767  16.995  42.260  1.00123.57           C  
ANISOU 3119  CB  LYS A1190    15483  20349  11119   1921   -907    394       C  
ATOM   3120  CG  LYS A1190       9.042  16.589  43.532  1.00124.85           C  
ANISOU 3120  CG  LYS A1190    15581  21047  10811   1939   -862    594       C  
ATOM   3121  CD  LYS A1190       8.238  17.727  44.131  1.00125.02           C  
ANISOU 3121  CD  LYS A1190    15558  21429  10513   2089   -766    266       C  
ATOM   3122  CE  LYS A1190       7.560  17.284  45.421  1.00125.40           C  
ANISOU 3122  CE  LYS A1190    15517  22070  10059   2108   -716    478       C  
ATOM   3123  NZ  LYS A1190       7.861  15.860  45.751  1.00125.58           N  
ANISOU 3123  NZ  LYS A1190    15534  22130  10049   1951   -786    975       N  
ATOM   3124  N   ARG A1191      12.717  16.900  40.819  1.00125.43           N  
ANISOU 3124  N   ARG A1191    15786  19769  12101   1863  -1238    243       N  
ATOM   3125  CA  ARG A1191      13.596  17.294  39.723  1.00124.87           C  
ANISOU 3125  CA  ARG A1191    15725  19305  12415   1835  -1292     70       C  
ATOM   3126  C   ARG A1191      13.913  16.104  38.827  1.00123.99           C  
ANISOU 3126  C   ARG A1191    15617  18895  12598   1766  -1290    361       C  
ATOM   3127  O   ARG A1191      13.952  16.233  37.598  1.00122.74           O  
ANISOU 3127  O   ARG A1191    15469  18407  12758   1723  -1223    295       O  
ATOM   3128  CB  ARG A1191      14.883  17.911  40.273  1.00125.36           C  
ANISOU 3128  CB  ARG A1191    15760  19429  12441   1876  -1494   -151       C  
ATOM   3129  CG  ARG A1191      15.953  18.202  39.229  1.00124.81           C  
ANISOU 3129  CG  ARG A1191    15665  19011  12746   1825  -1570   -280       C  
ATOM   3130  CD  ARG A1191      15.402  19.007  38.066  1.00124.18           C  
ANISOU 3130  CD  ARG A1191    15623  18653  12908   1779  -1435   -472       C  
ATOM   3131  NE  ARG A1191      16.406  19.892  37.489  1.00124.34           N  
ANISOU 3131  NE  ARG A1191    15619  18473  13152   1729  -1541   -723       N  
ATOM   3132  CZ  ARG A1191      16.434  20.256  36.214  1.00123.83           C  
ANISOU 3132  CZ  ARG A1191    15559  18095  13396   1656  -1468   -799       C  
ATOM   3133  NH1 ARG A1191      15.523  19.832  35.355  1.00122.96           N  
ANISOU 3133  NH1 ARG A1191    15483  17822  13416   1637  -1293   -667       N  
ATOM   3134  NH2 ARG A1191      17.403  21.062  35.790  1.00124.32           N  
ANISOU 3134  NH2 ARG A1191    15585  18017  13632   1587  -1580  -1002       N  
ATOM   3135  N   ALA A1192      14.130  14.931  39.425  1.00125.52           N  
ANISOU 3135  N   ALA A1192    15811  19198  12685   1762  -1373    685       N  
ATOM   3136  CA  ALA A1192      14.444  13.743  38.638  1.00124.73           C  
ANISOU 3136  CA  ALA A1192    15735  18800  12855   1723  -1402    954       C  
ATOM   3137  C   ALA A1192      13.247  13.300  37.806  1.00124.13           C  
ANISOU 3137  C   ALA A1192    15709  18554  12902   1639  -1226   1107       C  
ATOM   3138  O   ALA A1192      13.373  13.049  36.602  1.00123.63           O  
ANISOU 3138  O   ALA A1192    15667  18147  13161   1611  -1187   1103       O  
ATOM   3139  CB  ALA A1192      14.906  12.612  39.554  1.00125.52           C  
ANISOU 3139  CB  ALA A1192    15847  19048  12798   1746  -1558   1273       C  
ATOM   3140  N   MET A1193      12.072  13.199  38.433  1.00124.43           N  
ANISOU 3140  N   MET A1193    15752  18855  12672   1595  -1119   1243       N  
ATOM   3141  CA  MET A1193      10.895  12.713  37.723  1.00123.58           C  
ANISOU 3141  CA  MET A1193    15673  18624  12657   1495   -964   1420       C  
ATOM   3142  C   MET A1193      10.368  13.718  36.707  1.00122.37           C  
ANISOU 3142  C   MET A1193    15510  18304  12681   1498   -813   1131       C  
ATOM   3143  O   MET A1193       9.606  13.332  35.816  1.00121.36           O  
ANISOU 3143  O   MET A1193    15407  17982  12721   1418   -702   1241       O  
ATOM   3144  CB  MET A1193       9.793  12.350  38.718  1.00124.33           C  
ANISOU 3144  CB  MET A1193    15744  19104  12391   1436   -891   1658       C  
ATOM   3145  CG  MET A1193       9.687  10.860  38.992  1.00124.27           C  
ANISOU 3145  CG  MET A1193    15790  19064  12365   1330   -977   2115       C  
ATOM   3146  SD  MET A1193       8.085  10.375  39.659  1.00125.09           S  
ANISOU 3146  SD  MET A1193    15849  19542  12137   1181   -836   2443       S  
ATOM   3147  CE  MET A1193       8.541   9.917  41.330  1.00126.32           C  
ANISOU 3147  CE  MET A1193    15986  20130  11879   1199   -988   2677       C  
ATOM   3148  N   SER A1194      10.751  14.990  36.817  1.00118.07           N  
ANISOU 3148  N   SER A1194    14939  17818  12104   1580   -821    772       N  
ATOM   3149  CA  SER A1194      10.334  15.990  35.840  1.00117.08           C  
ANISOU 3149  CA  SER A1194    14819  17504  12161   1585   -706    501       C  
ATOM   3150  C   SER A1194      11.343  16.141  34.709  1.00116.40           C  
ANISOU 3150  C   SER A1194    14747  17040  12439   1569   -766    378       C  
ATOM   3151  O   SER A1194      10.951  16.295  33.547  1.00115.25           O  
ANISOU 3151  O   SER A1194    14621  16640  12530   1525   -664    331       O  
ATOM   3152  CB  SER A1194      10.111  17.340  36.526  1.00118.24           C  
ANISOU 3152  CB  SER A1194    14951  17891  12083   1681   -696    172       C  
ATOM   3153  OG  SER A1194      11.323  18.064  36.636  1.00118.92           O  
ANISOU 3153  OG  SER A1194    15042  17897  12244   1722   -845    -75       O  
ATOM   3154  N   PHE A1195      12.640  16.104  35.029  1.00117.19           N  
ANISOU 3154  N   PHE A1195    14823  17128  12574   1604   -929    329       N  
ATOM   3155  CA  PHE A1195      13.661  16.129  33.987  1.00115.87           C  
ANISOU 3155  CA  PHE A1195    14636  16657  12731   1587   -986    245       C  
ATOM   3156  C   PHE A1195      13.544  14.914  33.077  1.00114.42           C  
ANISOU 3156  C   PHE A1195    14479  16225  12769   1552   -948    497       C  
ATOM   3157  O   PHE A1195      13.683  15.029  31.854  1.00113.27           O  
ANISOU 3157  O   PHE A1195    14332  15813  12891   1523   -891    422       O  
ATOM   3158  CB  PHE A1195      15.052  16.193  34.621  1.00116.34           C  
ANISOU 3158  CB  PHE A1195    14638  16813  12754   1635  -1176    179       C  
ATOM   3159  CG  PHE A1195      16.169  16.368  33.629  1.00116.20           C  
ANISOU 3159  CG  PHE A1195    14560  16557  13034   1618  -1235     67       C  
ATOM   3160  CD1 PHE A1195      16.726  15.272  32.988  1.00114.92           C  
ANISOU 3160  CD1 PHE A1195    14375  16222  13067   1643  -1271    254       C  
ATOM   3161  CD2 PHE A1195      16.671  17.627  33.347  1.00116.71           C  
ANISOU 3161  CD2 PHE A1195    14590  16582  13175   1579  -1265   -224       C  
ATOM   3162  CE1 PHE A1195      17.753  15.430  32.078  1.00114.15           C  
ANISOU 3162  CE1 PHE A1195    14194  15961  13216   1641  -1314    146       C  
ATOM   3163  CE2 PHE A1195      17.700  17.792  32.439  1.00115.57           C  
ANISOU 3163  CE2 PHE A1195    14365  16263  13284   1542  -1314   -304       C  
ATOM   3164  CZ  PHE A1195      18.241  16.693  31.803  1.00114.54           C  
ANISOU 3164  CZ  PHE A1195    14186  16008  13326   1579  -1327   -122       C  
ATOM   3165  N   SER A1196      13.291  13.740  33.660  1.00114.66           N  
ANISOU 3165  N   SER A1196    14543  16338  12685   1551   -991    799       N  
ATOM   3166  CA  SER A1196      13.171  12.525  32.862  1.00113.43           C  
ANISOU 3166  CA  SER A1196    14441  15922  12737   1522   -989   1038       C  
ATOM   3167  C   SER A1196      11.994  12.607  31.899  1.00112.88           C  
ANISOU 3167  C   SER A1196    14411  15695  12784   1439   -816   1045       C  
ATOM   3168  O   SER A1196      12.078  12.128  30.762  1.00111.50           O  
ANISOU 3168  O   SER A1196    14267  15229  12870   1423   -794   1075       O  
ATOM   3169  CB  SER A1196      13.029  11.310  33.778  1.00114.41           C  
ANISOU 3169  CB  SER A1196    14614  16161  12695   1516  -1090   1379       C  
ATOM   3170  OG  SER A1196      12.773  10.134  33.030  1.00113.24           O  
ANISOU 3170  OG  SER A1196    14547  15734  12745   1478  -1104   1612       O  
ATOM   3171  N   ASP A 333      10.889  13.215  32.333  1.00117.52           N  
ANISOU 3171  N   ASP A 333    14990  16490  13172   1398   -695   1005       N  
ATOM   3172  CA  ASP A 333       9.700  13.285  31.495  1.00116.51           C  
ANISOU 3172  CA  ASP A 333    14884  16254  13131   1322   -535   1025       C  
ATOM   3173  C   ASP A 333       9.779  14.376  30.438  1.00116.01           C  
ANISOU 3173  C   ASP A 333    14805  16010  13265   1337   -453    729       C  
ATOM   3174  O   ASP A 333       9.016  14.329  29.469  1.00115.27           O  
ANISOU 3174  O   ASP A 333    14733  15750  13314   1281   -342    745       O  
ATOM   3175  CB  ASP A 333       8.455  13.489  32.359  1.00117.42           C  
ANISOU 3175  CB  ASP A 333    14971  16700  12944   1288   -434   1105       C  
ATOM   3176  CG  ASP A 333       8.229  12.346  33.324  1.00118.60           C  
ANISOU 3176  CG  ASP A 333    15135  17035  12892   1232   -503   1453       C  
ATOM   3177  OD1 ASP A 333       9.052  11.406  33.330  1.00117.92           O  
ANISOU 3177  OD1 ASP A 333    15100  16788  12916   1233   -645   1624       O  
ATOM   3178  OD2 ASP A 333       7.230  12.380  34.072  1.00119.52           O  
ANISOU 3178  OD2 ASP A 333    15208  17467  12737   1189   -420   1564       O  
ATOM   3179  N   GLN A 334      10.669  15.357  30.598  1.00115.38           N  
ANISOU 3179  N   GLN A 334    14691  15957  13193   1397   -517    472       N  
ATOM   3180  CA  GLN A 334      10.899  16.311  29.518  1.00115.06           C  
ANISOU 3180  CA  GLN A 334    14644  15707  13368   1386   -469    230       C  
ATOM   3181  C   GLN A 334      11.852  15.739  28.477  1.00113.60           C  
ANISOU 3181  C   GLN A 334    14445  15256  13461   1373   -518    266       C  
ATOM   3182  O   GLN A 334      11.693  15.992  27.277  1.00112.43           O  
ANISOU 3182  O   GLN A 334    14305  14897  13518   1334   -439    193       O  
ATOM   3183  CB  GLN A 334      11.439  17.630  30.076  1.00116.06           C  
ANISOU 3183  CB  GLN A 334    14747  15953  13399   1428   -534    -55       C  
ATOM   3184  CG  GLN A 334      11.857  18.633  29.007  1.00115.81           C  
ANISOU 3184  CG  GLN A 334    14713  15694  13597   1390   -521   -282       C  
ATOM   3185  CD  GLN A 334      10.693  19.448  28.474  1.00116.98           C  
ANISOU 3185  CD  GLN A 334    14908  15780  13761   1381   -392   -400       C  
ATOM   3186  OE1 GLN A 334       9.537  19.203  28.818  1.00117.54           O  
ANISOU 3186  OE1 GLN A 334    14993  15984  13681   1406   -296   -310       O  
ATOM   3187  NE2 GLN A 334      10.995  20.422  27.624  1.00116.71           N  
ANISOU 3187  NE2 GLN A 334    14887  15553  13904   1341   -395   -591       N  
ATOM   3188  N   ALA A 335      12.840  14.960  28.919  1.00109.24           N  
ANISOU 3188  N   ALA A 335    13869  14730  12907   1421   -652    377       N  
ATOM   3189  CA  ALA A 335      13.735  14.294  27.980  1.00107.61           C  
ANISOU 3189  CA  ALA A 335    13639  14305  12943   1446   -703    415       C  
ATOM   3190  C   ALA A 335      13.007  13.188  27.226  1.00105.52           C  
ANISOU 3190  C   ALA A 335    13450  13842  12800   1423   -644    616       C  
ATOM   3191  O   ALA A 335      13.135  13.070  26.002  1.00103.57           O  
ANISOU 3191  O   ALA A 335    13203  13380  12770   1416   -595    566       O  
ATOM   3192  CB  ALA A 335      14.951  13.737  28.721  1.00107.81           C  
ANISOU 3192  CB  ALA A 335    13613  14429  12921   1532   -876    478       C  
ATOM   3193  N   ARG A 336      12.232  12.369  27.944  1.00108.90           N  
ANISOU 3193  N   ARG A 336    13944  14349  13082   1398   -655    851       N  
ATOM   3194  CA  ARG A 336      11.486  11.295  27.296  1.00107.55           C  
ANISOU 3194  CA  ARG A 336    13860  13981  13023   1347   -624   1058       C  
ATOM   3195  C   ARG A 336      10.413  11.847  26.367  1.00106.66           C  
ANISOU 3195  C   ARG A 336    13759  13779  12988   1262   -458    974       C  
ATOM   3196  O   ARG A 336      10.160  11.279  25.298  1.00104.03           O  
ANISOU 3196  O   ARG A 336    13475  13209  12844   1235   -429   1021       O  
ATOM   3197  CB  ARG A 336      10.859  10.378  28.345  1.00108.75           C  
ANISOU 3197  CB  ARG A 336    14072  14264  12984   1300   -682   1352       C  
ATOM   3198  CG  ARG A 336      11.662   9.120  28.630  1.00108.43           C  
ANISOU 3198  CG  ARG A 336    14092  14108  13000   1368   -866   1554       C  
ATOM   3199  CD  ARG A 336      11.396   8.608  30.035  1.00110.89           C  
ANISOU 3199  CD  ARG A 336    14430  14654  13050   1333   -951   1803       C  
ATOM   3200  NE  ARG A 336      10.305   7.641  30.067  1.00111.09           N  
ANISOU 3200  NE  ARG A 336    14551  14610  13047   1200   -945   2104       N  
ATOM   3201  CZ  ARG A 336      10.434   6.355  29.771  1.00111.26           C  
ANISOU 3201  CZ  ARG A 336    14692  14368  13214   1192  -1081   2331       C  
ATOM   3202  NH1 ARG A 336      11.603   5.839  29.425  1.00110.55           N  
ANISOU 3202  NH1 ARG A 336    14634  14068  13300   1343  -1229   2282       N  
ATOM   3203  NH2 ARG A 336       9.366   5.564  29.831  1.00111.19           N  
ANISOU 3203  NH2 ARG A 336    14770  14308  13171   1032  -1080   2612       N  
ATOM   3204  N   MET A 337       9.764  12.944  26.762  1.00116.15           N  
ANISOU 3204  N   MET A 337    14920  15170  14040   1234   -359    841       N  
ATOM   3205  CA  MET A 337       8.795  13.592  25.883  1.00115.31           C  
ANISOU 3205  CA  MET A 337    14816  14988  14007   1176   -213    739       C  
ATOM   3206  C   MET A 337       9.453  14.003  24.572  1.00113.02           C  
ANISOU 3206  C   MET A 337    14515  14460  13969   1190   -194    564       C  
ATOM   3207  O   MET A 337       9.096  13.502  23.500  1.00110.67           O  
ANISOU 3207  O   MET A 337    14254  13959  13837   1152   -146    618       O  
ATOM   3208  CB  MET A 337       8.182  14.808  26.581  1.00117.33           C  
ANISOU 3208  CB  MET A 337    15032  15487  14063   1192   -139    580       C  
ATOM   3209  CG  MET A 337       6.693  14.998  26.341  1.00118.30           C  
ANISOU 3209  CG  MET A 337    15153  15675  14119   1137      1    623       C  
ATOM   3210  SD  MET A 337       5.945  16.112  27.550  1.00123.74           S  
ANISOU 3210  SD  MET A 337    15788  16736  14491   1206     59    480       S  
ATOM   3211  CE  MET A 337       5.458  14.959  28.831  1.00121.86           C  
ANISOU 3211  CE  MET A 337    15527  16793  13981   1159     32    803       C  
ATOM   3212  N   ASP A 338      10.449  14.894  24.654  1.00105.14           N  
ANISOU 3212  N   ASP A 338    13461  13497  12991   1235   -241    362       N  
ATOM   3213  CA  ASP A 338      11.087  15.454  23.465  1.00102.61           C  
ANISOU 3213  CA  ASP A 338    13105  13003  12877   1225   -218    199       C  
ATOM   3214  C   ASP A 338      11.549  14.380  22.491  1.00 99.44           C  
ANISOU 3214  C   ASP A 338    12713  12404  12665   1248   -240    296       C  
ATOM   3215  O   ASP A 338      11.555  14.607  21.276  1.00 96.26           O  
ANISOU 3215  O   ASP A 338    12302  11851  12422   1222   -173    216       O  
ATOM   3216  CB  ASP A 338      12.273  16.327  23.875  1.00104.38           C  
ANISOU 3216  CB  ASP A 338    13255  13319  13084   1249   -307     23       C  
ATOM   3217  CG  ASP A 338      11.842  17.643  24.486  1.00106.62           C  
ANISOU 3217  CG  ASP A 338    13550  13727  13233   1228   -289   -148       C  
ATOM   3218  OD1 ASP A 338      10.729  17.699  25.050  1.00107.56           O  
ANISOU 3218  OD1 ASP A 338    13715  13954  13198   1237   -227   -105       O  
ATOM   3219  OD2 ASP A 338      12.617  18.619  24.408  1.00107.43           O  
ANISOU 3219  OD2 ASP A 338    13613  13825  13380   1203   -346   -328       O  
ATOM   3220  N   ILE A 339      11.949  13.212  23.002  1.00100.57           N  
ANISOU 3220  N   ILE A 339    12880  12546  12785   1309   -345    462       N  
ATOM   3221  CA  ILE A 339      12.276  12.096  22.121  1.00 97.99           C  
ANISOU 3221  CA  ILE A 339    12589  12012  12631   1360   -384    547       C  
ATOM   3222  C   ILE A 339      11.082  11.750  21.244  1.00 95.60           C  
ANISOU 3222  C   ILE A 339    12370  11548  12407   1281   -285    617       C  
ATOM   3223  O   ILE A 339      11.217  11.580  20.027  1.00 92.75           O  
ANISOU 3223  O   ILE A 339    12013  11018  12211   1294   -249    551       O  
ATOM   3224  CB  ILE A 339      12.742  10.880  22.943  1.00 99.38           C  
ANISOU 3224  CB  ILE A 339    12809  12192  12758   1443   -537    735       C  
ATOM   3225  CG1 ILE A 339      14.048  11.192  23.670  1.00100.44           C  
ANISOU 3225  CG1 ILE A 339    12842  12487  12834   1534   -647    652       C  
ATOM   3226  CG2 ILE A 339      12.909   9.661  22.045  1.00 97.14           C  
ANISOU 3226  CG2 ILE A 339    12599  11658  12653   1511   -596    819       C  
ATOM   3227  CD1 ILE A 339      15.247  11.227  22.764  1.00 99.76           C  
ANISOU 3227  CD1 ILE A 339    12657  12333  12915   1627   -678    508       C  
ATOM   3228  N   GLU A 340       9.890  11.674  21.839  1.00 99.18           N  
ANISOU 3228  N   GLU A 340    12875  12079  12729   1196   -238    748       N  
ATOM   3229  CA  GLU A 340       8.716  11.225  21.096  1.00 97.06           C  
ANISOU 3229  CA  GLU A 340    12677  11676  12525   1106   -162    846       C  
ATOM   3230  C   GLU A 340       8.299  12.236  20.034  1.00 94.84           C  
ANISOU 3230  C   GLU A 340    12360  11346  12330   1066    -30    666       C  
ATOM   3231  O   GLU A 340       8.037  11.858  18.888  1.00 92.27           O  
ANISOU 3231  O   GLU A 340    12072  10835  12150   1044      3    662       O  
ATOM   3232  CB  GLU A 340       7.566  10.932  22.058  1.00 99.67           C  
ANISOU 3232  CB  GLU A 340    13037  12161  12671   1013   -143   1043       C  
ATOM   3233  CG  GLU A 340       7.803   9.706  22.931  1.00101.42           C  
ANISOU 3233  CG  GLU A 340    13324  12382  12828   1017   -286   1287       C  
ATOM   3234  CD  GLU A 340       8.351   8.524  22.149  1.00 99.16           C  
ANISOU 3234  CD  GLU A 340    13133  11798  12747   1066   -403   1359       C  
ATOM   3235  OE1 GLU A 340       7.546   7.786  21.544  1.00 98.62           O  
ANISOU 3235  OE1 GLU A 340    13150  11556  12763    976   -405   1485       O  
ATOM   3236  OE2 GLU A 340       9.586   8.331  22.144  1.00 98.65           O  
ANISOU 3236  OE2 GLU A 340    13052  11678  12752   1201   -502   1280       O  
ATOM   3237  N   LEU A 341       8.227  13.525  20.391  1.00 93.09           N  
ANISOU 3237  N   LEU A 341    12077  11278  12016   1061     33    514       N  
ATOM   3238  CA  LEU A 341       7.907  14.541  19.387  1.00 91.24           C  
ANISOU 3238  CA  LEU A 341    11820  10975  11870   1028    136    350       C  
ATOM   3239  C   LEU A 341       8.835  14.446  18.182  1.00 87.84           C  
ANISOU 3239  C   LEU A 341    11369  10378  11629   1053    123    259       C  
ATOM   3240  O   LEU A 341       8.386  14.543  17.035  1.00 85.32           O  
ANISOU 3240  O   LEU A 341    11067   9932  11418   1013    196    225       O  
ATOM   3241  CB  LEU A 341       7.974  15.956  19.977  1.00 92.71           C  
ANISOU 3241  CB  LEU A 341    11962  11311  11952   1039    157    178       C  
ATOM   3242  CG  LEU A 341       7.100  16.471  21.129  1.00 96.63           C  
ANISOU 3242  CG  LEU A 341    12456  12024  12233   1049    186    180       C  
ATOM   3243  CD1 LEU A 341       5.623  16.291  20.793  1.00 95.85           C  
ANISOU 3243  CD1 LEU A 341    12376  11938  12104    999    291    274       C  
ATOM   3244  CD2 LEU A 341       7.447  15.899  22.496  1.00101.11           C  
ANISOU 3244  CD2 LEU A 341    13014  12775  12627   1087    100    288       C  
ATOM   3245  N   ALA A 342      10.132  14.245  18.424  1.00 90.43           N  
ANISOU 3245  N   ALA A 342    11647  10729  11984   1124     32    220       N  
ATOM   3246  CA  ALA A 342      11.082  14.148  17.322  1.00 87.73           C  
ANISOU 3246  CA  ALA A 342    11251  10287  11795   1163     25    130       C  
ATOM   3247  C   ALA A 342      10.820  12.923  16.454  1.00 85.87           C  
ANISOU 3247  C   ALA A 342    11084   9875  11669   1199     18    220       C  
ATOM   3248  O   ALA A 342      11.157  12.927  15.266  1.00 83.90           O  
ANISOU 3248  O   ALA A 342    10805   9539  11534   1216     57    136       O  
ATOM   3249  CB  ALA A 342      12.510  14.120  17.864  1.00 89.92           C  
ANISOU 3249  CB  ALA A 342    11437  10669  12061   1244    -80     80       C  
ATOM   3250  N   LYS A 343      10.221  11.871  17.019  1.00 90.20           N  
ANISOU 3250  N   LYS A 343    11726  10369  12177   1205    -41    393       N  
ATOM   3251  CA  LYS A 343       9.951  10.667  16.237  1.00 88.40           C  
ANISOU 3251  CA  LYS A 343    11591   9937  12060   1232    -81    475       C  
ATOM   3252  C   LYS A 343       8.680  10.804  15.406  1.00 86.45           C  
ANISOU 3252  C   LYS A 343    11399   9599  11850   1119     21    493       C  
ATOM   3253  O   LYS A 343       8.694  10.551  14.196  1.00 84.04           O  
ANISOU 3253  O   LYS A 343    11114   9158  11660   1136     45    425       O  
ATOM   3254  CB  LYS A 343       9.862   9.443  17.153  1.00 90.36           C  
ANISOU 3254  CB  LYS A 343    11934  10132  12267   1262   -216    675       C  
ATOM   3255  CG  LYS A 343      11.048   9.271  18.085  1.00 92.79           C  
ANISOU 3255  CG  LYS A 343    12190  10544  12522   1380   -331    679       C  
ATOM   3256  CD  LYS A 343      12.214   8.584  17.394  1.00 91.61           C  
ANISOU 3256  CD  LYS A 343    12021  10280  12506   1549   -422    596       C  
ATOM   3257  CE  LYS A 343      13.074   7.830  18.396  1.00 94.16           C  
ANISOU 3257  CE  LYS A 343    12353  10635  12788   1676   -590    692       C  
ATOM   3258  NZ  LYS A 343      12.653   6.408  18.535  1.00 95.38           N  
ANISOU 3258  NZ  LYS A 343    12680  10566  12993   1706   -729    885       N  
ATOM   3259  N   THR A 344       7.566  11.195  16.036  1.00 84.77           N  
ANISOU 3259  N   THR A 344    11200   9484  11525   1012     79    580       N  
ATOM   3260  CA  THR A 344       6.331  11.389  15.281  1.00 82.76           C  
ANISOU 3260  CA  THR A 344    10975   9175  11296    908    174    597       C  
ATOM   3261  C   THR A 344       6.519  12.402  14.161  1.00 80.27           C  
ANISOU 3261  C   THR A 344    10603   8839  11057    912    269    411       C  
ATOM   3262  O   THR A 344       5.901  12.274  13.098  1.00 77.87           O  
ANISOU 3262  O   THR A 344    10332   8425  10830    866    317    400       O  
ATOM   3263  CB  THR A 344       5.194  11.845  16.199  1.00 85.39           C  
ANISOU 3263  CB  THR A 344    11288   9685  11472    820    233    691       C  
ATOM   3264  OG1 THR A 344       5.173  13.276  16.261  1.00 86.43           O  
ANISOU 3264  OG1 THR A 344    11344   9947  11548    834    322    528       O  
ATOM   3265  CG2 THR A 344       5.364  11.292  17.598  1.00 88.63           C  
ANISOU 3265  CG2 THR A 344    11709  10217  11750    829    148    841       C  
ATOM   3266  N   LEU A 345       7.367  13.410  14.378  1.00 82.43           N  
ANISOU 3266  N   LEU A 345    10796   9217  11308    952    286    276       N  
ATOM   3267  CA  LEU A 345       7.641  14.400  13.342  1.00 79.86           C  
ANISOU 3267  CA  LEU A 345    10418   8872  11054    933    360    125       C  
ATOM   3268  C   LEU A 345       8.226  13.745  12.097  1.00 78.07           C  
ANISOU 3268  C   LEU A 345    10191   8522  10950    978    351     84       C  
ATOM   3269  O   LEU A 345       7.667  13.854  11.000  1.00 75.99           O  
ANISOU 3269  O   LEU A 345     9949   8180  10744    933    415     57       O  
ATOM   3270  CB  LEU A 345       8.592  15.471  13.881  1.00 81.00           C  
ANISOU 3270  CB  LEU A 345    10481   9138  11159    948    342      9       C  
ATOM   3271  CG  LEU A 345       7.982  16.635  14.661  1.00 82.55           C  
ANISOU 3271  CG  LEU A 345    10677   9437  11250    906    372    -40       C  
ATOM   3272  CD1 LEU A 345       8.967  17.788  14.725  1.00 83.69           C  
ANISOU 3272  CD1 LEU A 345    10758   9633  11407    891    343   -183       C  
ATOM   3273  CD2 LEU A 345       6.670  17.080  14.034  1.00 80.89           C  
ANISOU 3273  CD2 LEU A 345    10509   9178  11048    850    463    -36       C  
ATOM   3274  N   VAL A 346       9.358  13.053  12.252  1.00 77.97           N  
ANISOU 3274  N   VAL A 346    10148   8508  10967   1082    268     72       N  
ATOM   3275  CA  VAL A 346      10.017  12.457  11.095  1.00 76.96           C  
ANISOU 3275  CA  VAL A 346    10002   8302  10936   1163    258      1       C  
ATOM   3276  C   VAL A 346       9.140  11.379  10.469  1.00 75.28           C  
ANISOU 3276  C   VAL A 346     9915   7908  10779   1163    236     72       C  
ATOM   3277  O   VAL A 346       9.167  11.187   9.250  1.00 74.07           O  
ANISOU 3277  O   VAL A 346     9766   7686  10690   1188    268     -5       O  
ATOM   3278  CB  VAL A 346      11.408  11.913  11.474  1.00 78.55           C  
ANISOU 3278  CB  VAL A 346    10133   8563  11150   1307    162    -34       C  
ATOM   3279  CG1 VAL A 346      12.262  13.014  12.078  1.00 79.94           C  
ANISOU 3279  CG1 VAL A 346    10177   8925  11271   1278    171   -102       C  
ATOM   3280  CG2 VAL A 346      11.295  10.735  12.428  1.00 79.18           C  
ANISOU 3280  CG2 VAL A 346    10313   8560  11214   1379     36     98       C  
ATOM   3281  N   LEU A 347       8.344  10.669  11.274  1.00 75.53           N  
ANISOU 3281  N   LEU A 347    10048   7872  10780   1123    174    223       N  
ATOM   3282  CA  LEU A 347       7.400   9.705  10.715  1.00 74.67           C  
ANISOU 3282  CA  LEU A 347    10063   7583  10726   1079    138    307       C  
ATOM   3283  C   LEU A 347       6.444  10.381   9.740  1.00 72.83           C  
ANISOU 3283  C   LEU A 347     9822   7346  10504    970    254    263       C  
ATOM   3284  O   LEU A 347       6.205   9.881   8.636  1.00 71.46           O  
ANISOU 3284  O   LEU A 347     9703   7047  10403    978    247    219       O  
ATOM   3285  CB  LEU A 347       6.619   9.012  11.833  1.00 76.85           C  
ANISOU 3285  CB  LEU A 347    10426   7829  10945   1001     61    512       C  
ATOM   3286  CG  LEU A 347       6.978   7.555  12.130  1.00 77.36           C  
ANISOU 3286  CG  LEU A 347    10610   7716  11068   1077   -111    617       C  
ATOM   3287  CD1 LEU A 347       8.484   7.365  12.219  1.00 78.24           C  
ANISOU 3287  CD1 LEU A 347    10671   7843  11212   1272   -182    507       C  
ATOM   3288  CD2 LEU A 347       6.288   7.086  13.400  1.00 79.61           C  
ANISOU 3288  CD2 LEU A 347    10953   8030  11263    970   -178    849       C  
ATOM   3289  N   ILE A 348       5.898  11.532  10.132  1.00 71.43           N  
ANISOU 3289  N   ILE A 348     9582   7307  10252    884    349    263       N  
ATOM   3290  CA  ILE A 348       5.021  12.281   9.242  1.00 69.80           C  
ANISOU 3290  CA  ILE A 348     9361   7105  10054    798    450    220       C  
ATOM   3291  C   ILE A 348       5.790  12.784   8.026  1.00 68.32           C  
ANISOU 3291  C   ILE A 348     9121   6913   9926    843    498     71       C  
ATOM   3292  O   ILE A 348       5.233  12.877   6.925  1.00 66.23           O  
ANISOU 3292  O   ILE A 348     8875   6594   9695    800    545     40       O  
ATOM   3293  CB  ILE A 348       4.357  13.434  10.018  1.00 70.31           C  
ANISOU 3293  CB  ILE A 348     9374   7317  10022    736    521    234       C  
ATOM   3294  CG1 ILE A 348       3.499  12.889  11.162  1.00 73.33           C  
ANISOU 3294  CG1 ILE A 348     9787   7757  10316    686    488    395       C  
ATOM   3295  CG2 ILE A 348       3.510  14.297   9.099  1.00 68.47           C  
ANISOU 3295  CG2 ILE A 348     9126   7086   9804    672    611    184       C  
ATOM   3296  CD1 ILE A 348       3.133  13.934  12.196  1.00 75.39           C  
ANISOU 3296  CD1 ILE A 348     9987   8207  10452    680    540    382       C  
ATOM   3297  N   LEU A 349       7.079  13.097   8.190  1.00 72.02           N  
ANISOU 3297  N   LEU A 349     9509   7459  10396    920    485    -13       N  
ATOM   3298  CA  LEU A 349       7.837  13.671   7.083  1.00 70.73           C  
ANISOU 3298  CA  LEU A 349     9264   7344  10265    938    540   -133       C  
ATOM   3299  C   LEU A 349       8.105  12.617   6.013  1.00 70.17           C  
ANISOU 3299  C   LEU A 349     9228   7185  10249   1027    511   -183       C  
ATOM   3300  O   LEU A 349       7.819  12.841   4.831  1.00 69.09           O  
ANISOU 3300  O   LEU A 349     9087   7039  10126    995    571   -236       O  
ATOM   3301  CB  LEU A 349       9.151  14.271   7.591  1.00 72.41           C  
ANISOU 3301  CB  LEU A 349     9361   7694  10458    978    526   -196       C  
ATOM   3302  CG  LEU A 349      10.206  14.759   6.585  1.00 73.62           C  
ANISOU 3302  CG  LEU A 349     9392   7951  10629    991    570   -298       C  
ATOM   3303  CD1 LEU A 349       9.574  15.553   5.418  1.00 72.04           C  
ANISOU 3303  CD1 LEU A 349     9196   7739  10437    883    662   -317       C  
ATOM   3304  CD2 LEU A 349      11.310  15.551   7.299  1.00 75.95           C  
ANISOU 3304  CD2 LEU A 349     9566   8395  10898    975    546   -332       C  
ATOM   3305  N   VAL A 350       8.627  11.448   6.414  1.00 70.42           N  
ANISOU 3305  N   VAL A 350     9304   7146  10308   1149    407   -171       N  
ATOM   3306  CA  VAL A 350       9.033  10.436   5.436  1.00 70.67           C  
ANISOU 3306  CA  VAL A 350     9372   7091  10389   1278    357   -256       C  
ATOM   3307  C   VAL A 350       7.843   9.953   4.616  1.00 69.18           C  
ANISOU 3307  C   VAL A 350     9306   6747  10230   1209    355   -233       C  
ATOM   3308  O   VAL A 350       7.964   9.734   3.407  1.00 69.24           O  
ANISOU 3308  O   VAL A 350     9315   6742  10251   1262    376   -340       O  
ATOM   3309  CB  VAL A 350       9.778   9.265   6.117  1.00 71.54           C  
ANISOU 3309  CB  VAL A 350     9528   7122  10531   1442    216   -245       C  
ATOM   3310  CG1 VAL A 350      10.819   9.776   7.092  1.00 73.61           C  
ANISOU 3310  CG1 VAL A 350     9666   7550  10753   1489    207   -245       C  
ATOM   3311  CG2 VAL A 350       8.815   8.324   6.833  1.00 72.26           C  
ANISOU 3311  CG2 VAL A 350     9790   7014  10651   1389    107    -92       C  
ATOM   3312  N   VAL A 351       6.673   9.801   5.244  1.00 70.47           N  
ANISOU 3312  N   VAL A 351     9562   6821  10392   1084    332    -93       N  
ATOM   3313  CA  VAL A 351       5.500   9.363   4.496  1.00 70.25           C  
ANISOU 3313  CA  VAL A 351     9636   6664  10392    994    321    -59       C  
ATOM   3314  C   VAL A 351       5.047  10.445   3.527  1.00 68.79           C  
ANISOU 3314  C   VAL A 351     9380   6580  10176    911    449   -118       C  
ATOM   3315  O   VAL A 351       4.538  10.146   2.442  1.00 67.83           O  
ANISOU 3315  O   VAL A 351     9309   6390  10072    891    450   -164       O  
ATOM   3316  CB  VAL A 351       4.367   8.947   5.449  1.00 69.84           C  
ANISOU 3316  CB  VAL A 351     9666   6536  10332    864    266    126       C  
ATOM   3317  CG1 VAL A 351       3.324   8.177   4.692  1.00 70.39           C  
ANISOU 3317  CG1 VAL A 351     9850   6447  10449    778    208    165       C  
ATOM   3318  CG2 VAL A 351       4.910   8.086   6.566  1.00 71.67           C  
ANISOU 3318  CG2 VAL A 351     9955   6701  10576    932    143    214       C  
ATOM   3319  N   LEU A 352       5.233  11.715   3.893  1.00 66.05           N  
ANISOU 3319  N   LEU A 352     8928   6385   9782    862    544   -119       N  
ATOM   3320  CA  LEU A 352       4.931  12.791   2.956  1.00 64.55           C  
ANISOU 3320  CA  LEU A 352     8681   6277   9570    791    647   -167       C  
ATOM   3321  C   LEU A 352       5.918  12.800   1.794  1.00 66.20           C  
ANISOU 3321  C   LEU A 352     8827   6549   9776    872    677   -294       C  
ATOM   3322  O   LEU A 352       5.533  13.082   0.654  1.00 65.55           O  
ANISOU 3322  O   LEU A 352     8745   6484   9679    831    727   -332       O  
ATOM   3323  CB  LEU A 352       4.935  14.143   3.673  1.00 65.35           C  
ANISOU 3323  CB  LEU A 352     8708   6491   9631    726    709   -142       C  
ATOM   3324  CG  LEU A 352       4.660  15.356   2.779  1.00 64.61           C  
ANISOU 3324  CG  LEU A 352     8570   6456   9523    649    793   -174       C  
ATOM   3325  CD1 LEU A 352       3.516  16.208   3.316  1.00 63.69           C  
ANISOU 3325  CD1 LEU A 352     8473   6345   9382    571    820   -109       C  
ATOM   3326  CD2 LEU A 352       5.919  16.194   2.589  1.00 65.38           C  
ANISOU 3326  CD2 LEU A 352     8565   6664   9611    656    823   -241       C  
ATOM   3327  N   ILE A 353       7.191  12.487   2.059  1.00 68.00           N  
ANISOU 3327  N   ILE A 353     8991   6841  10006    991    646   -359       N  
ATOM   3328  CA  ILE A 353       8.198  12.531   0.998  1.00 69.28           C  
ANISOU 3328  CA  ILE A 353     9055   7127  10140   1077    687   -480       C  
ATOM   3329  C   ILE A 353       7.946  11.435  -0.031  1.00 69.60           C  
ANISOU 3329  C   ILE A 353     9182   7071  10190   1172    642   -564       C  
ATOM   3330  O   ILE A 353       7.879  11.704  -1.235  1.00 69.63           O  
ANISOU 3330  O   ILE A 353     9153   7153  10150   1158    704   -629       O  
ATOM   3331  CB  ILE A 353       9.624  12.440   1.576  1.00 71.01           C  
ANISOU 3331  CB  ILE A 353     9159   7472  10352   1194    660   -531       C  
ATOM   3332  CG1 ILE A 353      10.192  13.831   1.855  1.00 72.07           C  
ANISOU 3332  CG1 ILE A 353     9154   7777  10451   1081    732   -507       C  
ATOM   3333  CG2 ILE A 353      10.559  11.741   0.609  1.00 72.21           C  
ANISOU 3333  CG2 ILE A 353     9243   7714  10479   1365    654   -669       C  
ATOM   3334  CD1 ILE A 353      11.452  13.807   2.702  1.00 74.99           C  
ANISOU 3334  CD1 ILE A 353     9410   8268  10816   1162    689   -531       C  
ATOM   3335  N   ILE A 354       7.807  10.184   0.417  1.00 69.73           N  
ANISOU 3335  N   ILE A 354     9319   6913  10261   1269    519   -562       N  
ATOM   3336  CA  ILE A 354       7.663   9.092  -0.540  1.00 70.41           C  
ANISOU 3336  CA  ILE A 354     9508   6882  10365   1379    445   -668       C  
ATOM   3337  C   ILE A 354       6.297   9.087  -1.206  1.00 69.03           C  
ANISOU 3337  C   ILE A 354     9437   6598  10195   1237    450   -624       C  
ATOM   3338  O   ILE A 354       6.102   8.374  -2.196  1.00 69.37           O  
ANISOU 3338  O   ILE A 354     9558   6565  10235   1303    399   -728       O  
ATOM   3339  CB  ILE A 354       7.929   7.719   0.112  1.00 71.28           C  
ANISOU 3339  CB  ILE A 354     9743   6792  10546   1524    277   -676       C  
ATOM   3340  CG1 ILE A 354       7.214   7.609   1.459  1.00 70.30           C  
ANISOU 3340  CG1 ILE A 354     9701   6542  10468   1395    217   -485       C  
ATOM   3341  CG2 ILE A 354       9.428   7.486   0.270  1.00 72.86           C  
ANISOU 3341  CG2 ILE A 354     9833   7120  10730   1741    257   -790       C  
ATOM   3342  CD1 ILE A 354       7.634   6.409   2.286  1.00 69.91           C  
ANISOU 3342  CD1 ILE A 354     9762   6320  10483   1522     48   -452       C  
ATOM   3343  N   CYS A 355       5.347   9.867  -0.690  1.00 68.17           N  
ANISOU 3343  N   CYS A 355     9324   6492  10086   1055    503   -483       N  
ATOM   3344  CA  CYS A 355       4.065  10.021  -1.367  1.00 67.34           C  
ANISOU 3344  CA  CYS A 355     9280   6333   9974    921    520   -439       C  
ATOM   3345  C   CYS A 355       4.117  11.144  -2.395  1.00 67.11           C  
ANISOU 3345  C   CYS A 355     9148   6476   9874    874    645   -487       C  
ATOM   3346  O   CYS A 355       3.647  10.981  -3.526  1.00 68.07           O  
ANISOU 3346  O   CYS A 355     9305   6592   9966    858    647   -543       O  
ATOM   3347  CB  CYS A 355       2.957  10.283  -0.348  1.00 66.59           C  
ANISOU 3347  CB  CYS A 355     9216   6187   9900    769    514   -269       C  
ATOM   3348  SG  CYS A 355       2.154   8.797   0.280  1.00 67.48           S  
ANISOU 3348  SG  CYS A 355     9491   6066  10083    724    348   -163       S  
ATOM   3349  N   TRP A 356       4.703  12.284  -2.025  1.00 66.21           N  
ANISOU 3349  N   TRP A 356     8914   6512   9730    843    735   -459       N  
ATOM   3350  CA  TRP A 356       4.719  13.459  -2.885  1.00 66.87           C  
ANISOU 3350  CA  TRP A 356     8913   6741   9755    765    837   -463       C  
ATOM   3351  C   TRP A 356       6.028  13.647  -3.640  1.00 69.20           C  
ANISOU 3351  C   TRP A 356     9089   7216   9987    848    891   -564       C  
ATOM   3352  O   TRP A 356       6.049  14.386  -4.631  1.00 70.88           O  
ANISOU 3352  O   TRP A 356     9242   7555  10135    785    963   -567       O  
ATOM   3353  CB  TRP A 356       4.423  14.719  -2.062  1.00 66.23           C  
ANISOU 3353  CB  TRP A 356     8788   6695   9683    653    885   -359       C  
ATOM   3354  CG  TRP A 356       2.959  14.940  -1.834  1.00 64.43           C  
ANISOU 3354  CG  TRP A 356     8630   6377   9472    557    875   -267       C  
ATOM   3355  CD1 TRP A 356       2.183  14.370  -0.868  1.00 63.64           C  
ANISOU 3355  CD1 TRP A 356     8594   6183   9406    539    821   -194       C  
ATOM   3356  CD2 TRP A 356       2.092  15.785  -2.600  1.00 64.05           C  
ANISOU 3356  CD2 TRP A 356     8581   6355   9398    468    919   -228       C  
ATOM   3357  NE1 TRP A 356       0.887  14.814  -0.980  1.00 63.83           N  
ANISOU 3357  NE1 TRP A 356     8636   6195   9420    449    836   -121       N  
ATOM   3358  CE2 TRP A 356       0.806  15.683  -2.037  1.00 63.61           C  
ANISOU 3358  CE2 TRP A 356     8576   6230   9363    414    891   -146       C  
ATOM   3359  CE3 TRP A 356       2.281  16.619  -3.705  1.00 65.78           C  
ANISOU 3359  CE3 TRP A 356     8757   6665   9572    425    974   -242       C  
ATOM   3360  CZ2 TRP A 356      -0.287  16.383  -2.543  1.00 63.18           C  
ANISOU 3360  CZ2 TRP A 356     8523   6190   9290    344    914    -95       C  
ATOM   3361  CZ3 TRP A 356       1.195  17.315  -4.205  1.00 65.22           C  
ANISOU 3361  CZ3 TRP A 356     8710   6584   9489    347    987   -180       C  
ATOM   3362  CH2 TRP A 356      -0.072  17.192  -3.625  1.00 63.74           C  
ANISOU 3362  CH2 TRP A 356     8567   6322   9328    319    956   -116       C  
ATOM   3363  N   GLY A 357       7.111  13.014  -3.196  1.00 69.01           N  
ANISOU 3363  N   GLY A 357     9019   7229   9973    986    854   -636       N  
ATOM   3364  CA  GLY A 357       8.360  13.020  -3.923  1.00 71.71           C  
ANISOU 3364  CA  GLY A 357     9224   7780  10241   1090    902   -743       C  
ATOM   3365  C   GLY A 357       8.220  12.581  -5.369  1.00 73.16           C  
ANISOU 3365  C   GLY A 357     9422   8030  10347   1152    922   -850       C  
ATOM   3366  O   GLY A 357       8.709  13.250  -6.284  1.00 75.58           O  
ANISOU 3366  O   GLY A 357     9605   8559  10554   1117   1014   -868       O  
ATOM   3367  N   PRO A 358       7.566  11.435  -5.608  1.00 70.25           N  
ANISOU 3367  N   PRO A 358     9205   7475  10011   1237    828   -919       N  
ATOM   3368  CA  PRO A 358       7.280  11.053  -7.002  1.00 71.82           C  
ANISOU 3368  CA  PRO A 358     9437   7725  10126   1286    834  -1032       C  
ATOM   3369  C   PRO A 358       6.464  12.089  -7.752  1.00 72.61           C  
ANISOU 3369  C   PRO A 358     9519   7900  10168   1100    917   -937       C  
ATOM   3370  O   PRO A 358       6.704  12.317  -8.943  1.00 74.89           O  
ANISOU 3370  O   PRO A 358     9742   8377  10338   1116    979  -1002       O  
ATOM   3371  CB  PRO A 358       6.516   9.729  -6.856  1.00 70.69           C  
ANISOU 3371  CB  PRO A 358     9494   7300  10065   1356    684  -1086       C  
ATOM   3372  CG  PRO A 358       6.932   9.189  -5.539  1.00 68.75           C  
ANISOU 3372  CG  PRO A 358     9284   6918   9920   1427    601  -1047       C  
ATOM   3373  CD  PRO A 358       7.216  10.364  -4.657  1.00 69.30           C  
ANISOU 3373  CD  PRO A 358     9229   7105   9997   1304    695   -908       C  
ATOM   3374  N   LEU A 359       5.502  12.729  -7.086  1.00 72.57           N  
ANISOU 3374  N   LEU A 359     9568   7770  10235    935    916   -785       N  
ATOM   3375  CA  LEU A 359       4.671  13.720  -7.762  1.00 73.04           C  
ANISOU 3375  CA  LEU A 359     9621   7882  10251    778    976   -692       C  
ATOM   3376  C   LEU A 359       5.466  14.982  -8.068  1.00 75.06           C  
ANISOU 3376  C   LEU A 359     9729   8355  10437    703   1080   -634       C  
ATOM   3377  O   LEU A 359       5.385  15.524  -9.176  1.00 77.92           O  
ANISOU 3377  O   LEU A 359    10047   8857  10700    642   1135   -619       O  
ATOM   3378  CB  LEU A 359       3.440  14.035  -6.912  1.00 70.15           C  
ANISOU 3378  CB  LEU A 359     9338   7340   9974    656    939   -560       C  
ATOM   3379  CG  LEU A 359       2.470  12.881  -6.634  1.00 69.04           C  
ANISOU 3379  CG  LEU A 359     9336   6997   9900    668    831   -568       C  
ATOM   3380  CD1 LEU A 359       1.057  13.404  -6.436  1.00 68.44           C  
ANISOU 3380  CD1 LEU A 359     9298   6854   9853    524    826   -440       C  
ATOM   3381  CD2 LEU A 359       2.490  11.842  -7.752  1.00 70.42           C  
ANISOU 3381  CD2 LEU A 359     9579   7151  10027    761    771   -712       C  
ATOM   3382  N   LEU A 360       6.251  15.461  -7.099  1.00 73.70           N  
ANISOU 3382  N   LEU A 360     9479   8216  10309    691   1097   -591       N  
ATOM   3383  CA  LEU A 360       7.102  16.620  -7.339  1.00 76.89           C  
ANISOU 3383  CA  LEU A 360     9741   8818  10656    596   1173   -528       C  
ATOM   3384  C   LEU A 360       8.200  16.323  -8.350  1.00 80.40           C  
ANISOU 3384  C   LEU A 360    10048   9528  10973    680   1232   -623       C  
ATOM   3385  O   LEU A 360       8.809  17.259  -8.879  1.00 83.74           O  
ANISOU 3385  O   LEU A 360    10343  10157  11317    570   1301   -551       O  
ATOM   3386  CB  LEU A 360       7.716  17.104  -6.024  1.00 76.47           C  
ANISOU 3386  CB  LEU A 360     9639   8736  10680    566   1156   -478       C  
ATOM   3387  CG  LEU A 360       6.948  18.196  -5.275  1.00 74.46           C  
ANISOU 3387  CG  LEU A 360     9450   8344  10498    423   1138   -356       C  
ATOM   3388  CD1 LEU A 360       6.716  19.402  -6.176  1.00 76.38           C  
ANISOU 3388  CD1 LEU A 360     9670   8657  10693    271   1179   -261       C  
ATOM   3389  CD2 LEU A 360       5.634  17.661  -4.711  1.00 70.83           C  
ANISOU 3389  CD2 LEU A 360     9133   7674  10104    451   1084   -342       C  
ATOM   3390  N   ALA A 361       8.466  15.045  -8.627  1.00 77.24           N  
ANISOU 3390  N   ALA A 361     9669   9133  10544    875   1197   -780       N  
ATOM   3391  CA  ALA A 361       9.448  14.686  -9.640  1.00 80.17           C  
ANISOU 3391  CA  ALA A 361     9904   9787  10772    998   1254   -902       C  
ATOM   3392  C   ALA A 361       8.851  14.738 -11.041  1.00 81.96           C  
ANISOU 3392  C   ALA A 361    10159  10110  10872    966   1290   -926       C  
ATOM   3393  O   ALA A 361       9.510  15.202 -11.978  1.00 85.43           O  
ANISOU 3393  O   ALA A 361    10449  10853  11159    939   1379   -923       O  
ATOM   3394  CB  ALA A 361      10.015  13.296  -9.348  1.00 78.65           C  
ANISOU 3394  CB  ALA A 361     9733   9550  10599   1257   1182  -1086       C  
ATOM   3395  N   ILE A 362       7.609  14.274 -11.207  1.00 82.92           N  
ANISOU 3395  N   ILE A 362    10461  10001  11044    956   1220   -939       N  
ATOM   3396  CA  ILE A 362       6.994  14.285 -12.532  1.00 84.23           C  
ANISOU 3396  CA  ILE A 362    10661  10257  11086    928   1238   -968       C  
ATOM   3397  C   ILE A 362       6.691  15.713 -12.977  1.00 86.15           C  
ANISOU 3397  C   ILE A 362    10845  10612  11278    706   1313   -776       C  
ATOM   3398  O   ILE A 362       6.711  16.015 -14.178  1.00 89.79           O  
ANISOU 3398  O   ILE A 362    11250  11285  11581    669   1366   -770       O  
ATOM   3399  CB  ILE A 362       5.730  13.403 -12.542  1.00 82.15           C  
ANISOU 3399  CB  ILE A 362    10599   9714  10899    957   1125  -1026       C  
ATOM   3400  CG1 ILE A 362       6.074  11.983 -12.080  1.00 80.40           C  
ANISOU 3400  CG1 ILE A 362    10461   9346  10743   1166   1022  -1201       C  
ATOM   3401  CG2 ILE A 362       5.109  13.376 -13.939  1.00 84.01           C  
ANISOU 3401  CG2 ILE A 362    10868  10055  10995    934   1131  -1071       C  
ATOM   3402  CD1 ILE A 362       5.150  10.899 -12.611  1.00 79.78           C  
ANISOU 3402  CD1 ILE A 362    10562   9075  10676   1229    899  -1321       C  
ATOM   3403  N   MET A 363       6.418  16.617 -12.032  1.00 86.48           N  
ANISOU 3403  N   MET A 363    10902  10513  11441    561   1306   -618       N  
ATOM   3404  CA  MET A 363       6.195  18.013 -12.400  1.00 88.84           C  
ANISOU 3404  CA  MET A 363    11164  10882  11708    361   1349   -435       C  
ATOM   3405  C   MET A 363       7.499  18.696 -12.793  1.00 92.47           C  
ANISOU 3405  C   MET A 363    11436  11640  12059    294   1433   -380       C  
ATOM   3406  O   MET A 363       7.532  19.477 -13.750  1.00 95.64           O  
ANISOU 3406  O   MET A 363    11780  12214  12343    165   1480   -270       O  
ATOM   3407  CB  MET A 363       5.523  18.767 -11.254  1.00 85.44           C  
ANISOU 3407  CB  MET A 363    10818  10207  11439    255   1300   -311       C  
ATOM   3408  CG  MET A 363       4.356  18.039 -10.622  1.00 80.92           C  
ANISOU 3408  CG  MET A 363    10393   9380  10975    317   1224   -354       C  
ATOM   3409  SD  MET A 363       3.658  18.938  -9.226  1.00 77.27           S  
ANISOU 3409  SD  MET A 363     9996   8700  10664    226   1181   -229       S  
ATOM   3410  CE  MET A 363       2.920  17.586  -8.313  1.00 73.28           C  
ANISOU 3410  CE  MET A 363     9593   7999  10250    338   1110   -311       C  
ATOM   3411  N   VAL A 364       8.581  18.429 -12.056  1.00 88.04           N  
ANISOU 3411  N   VAL A 364    10768  11154  11529    367   1447   -438       N  
ATOM   3412  CA  VAL A 364       9.891  18.945 -12.446  1.00 91.48           C  
ANISOU 3412  CA  VAL A 364    10990  11921  11847    306   1527   -393       C  
ATOM   3413  C   VAL A 364      10.285  18.398 -13.809  1.00 93.92           C  
ANISOU 3413  C   VAL A 364    11195  12546  11945    407   1599   -494       C  
ATOM   3414  O   VAL A 364      10.904  19.101 -14.620  1.00 96.63           O  
ANISOU 3414  O   VAL A 364    11382  13197  12137    282   1677   -390       O  
ATOM   3415  CB  VAL A 364      10.938  18.607 -11.365  1.00 90.63           C  
ANISOU 3415  CB  VAL A 364    10781  11843  11813    397   1515   -459       C  
ATOM   3416  CG1 VAL A 364      12.352  18.730 -11.916  1.00 93.62           C  
ANISOU 3416  CG1 VAL A 364    10902  12633  12038    401   1602   -469       C  
ATOM   3417  CG2 VAL A 364      10.757  19.508 -10.156  1.00 89.51           C  
ANISOU 3417  CG2 VAL A 364    10698  11479  11832    244   1459   -328       C  
ATOM   3418  N   TYR A 365       9.822  17.190 -14.124  1.00 98.94           N  
ANISOU 3418  N   TYR A 365    11931  13103  12559    616   1562   -684       N  
ATOM   3419  CA  TYR A 365      10.083  16.624 -15.473  1.00100.65           C  
ANISOU 3419  CA  TYR A 365    12073  13612  12558    739   1617   -815       C  
ATOM   3420  C   TYR A 365       9.212  17.377 -16.479  1.00102.45           C  
ANISOU 3420  C   TYR A 365    12358  13877  12690    563   1636   -676       C  
ATOM   3421  O   TYR A 365       9.522  17.354 -17.680  1.00104.34           O  
ANISOU 3421  O   TYR A 365    12496  14437  12710    584   1705   -709       O  
ATOM   3422  CB  TYR A 365       9.840  15.113 -15.465  1.00 98.53           C  
ANISOU 3422  CB  TYR A 365    11924  13203  12311   1015   1540  -1072       C  
ATOM   3423  CG  TYR A 365       9.871  14.419 -16.802  1.00 99.78           C  
ANISOU 3423  CG  TYR A 365    12064  13590  12259   1173   1562  -1251       C  
ATOM   3424  CD1 TYR A 365      11.067  14.136 -17.440  1.00102.73           C  
ANISOU 3424  CD1 TYR A 365    12228  14371  12435   1330   1648  -1379       C  
ATOM   3425  CD2 TYR A 365       8.700  14.018 -17.421  1.00 99.27           C  
ANISOU 3425  CD2 TYR A 365    12182  13354  12181   1176   1491  -1305       C  
ATOM   3426  CE1 TYR A 365      11.095  13.489 -18.665  1.00104.12           C  
ANISOU 3426  CE1 TYR A 365    12386  14778  12395   1500   1666  -1568       C  
ATOM   3427  CE2 TYR A 365       8.710  13.372 -18.645  1.00100.03           C  
ANISOU 3427  CE2 TYR A 365    12274  13657  12075   1326   1497  -1488       C  
ATOM   3428  CZ  TYR A 365       9.913  13.104 -19.270  1.00102.49           C  
ANISOU 3428  CZ  TYR A 365    12386  14376  12181   1498   1586  -1629       C  
ATOM   3429  OH  TYR A 365       9.925  12.463 -20.475  1.00102.66           O  
ANISOU 3429  OH  TYR A 365    12403  14622  11981   1669   1590  -1833       O  
ATOM   3430  N   ASP A 366       8.165  18.047 -15.993  1.00 94.92           N  
ANISOU 3430  N   ASP A 366    11555  12624  11886    404   1575   -525       N  
ATOM   3431  CA  ASP A 366       7.335  18.834 -16.903  1.00 95.99           C  
ANISOU 3431  CA  ASP A 366    11746  12785  11942    242   1578   -377       C  
ATOM   3432  C   ASP A 366       7.874  20.240 -17.088  1.00 97.57           C  
ANISOU 3432  C   ASP A 366    11830  13147  12095      5   1629   -137       C  
ATOM   3433  O   ASP A 366       7.769  20.809 -18.182  1.00 98.80           O  
ANISOU 3433  O   ASP A 366    11945  13505  12091   -110   1666    -20       O  
ATOM   3434  CB  ASP A 366       5.889  18.900 -16.401  1.00 93.84           C  
ANISOU 3434  CB  ASP A 366    11678  12140  11836    200   1479   -332       C  
ATOM   3435  CG  ASP A 366       5.014  19.826 -17.242  1.00 95.66           C  
ANISOU 3435  CG  ASP A 366    11963  12379  12003     38   1466   -161       C  
ATOM   3436  OD1 ASP A 366       5.118  19.778 -18.488  1.00 97.80           O  
ANISOU 3436  OD1 ASP A 366    12180  12907  12074     35   1509   -168       O  
ATOM   3437  OD2 ASP A 366       4.204  20.583 -16.669  1.00 93.79           O  
ANISOU 3437  OD2 ASP A 366    11825  11904  11907    -69   1408    -26       O  
ATOM   3438  N   VAL A 367       8.435  20.815 -16.025  1.00 98.95           N  
ANISOU 3438  N   VAL A 367    11962  13228  12408    -80   1618    -53       N  
ATOM   3439  CA  VAL A 367       8.915  22.192 -16.081  1.00 99.79           C  
ANISOU 3439  CA  VAL A 367    11987  13425  12503   -333   1631    185       C  
ATOM   3440  C   VAL A 367       9.893  22.360 -17.238  1.00102.25           C  
ANISOU 3440  C   VAL A 367    12088  14193  12569   -401   1734    243       C  
ATOM   3441  O   VAL A 367       9.773  23.283 -18.053  1.00102.54           O  
ANISOU 3441  O   VAL A 367    12105  14351  12503   -601   1744    447       O  
ATOM   3442  CB  VAL A 367       9.541  22.582 -14.731  1.00 99.11           C  
ANISOU 3442  CB  VAL A 367    11870  13199  12587   -384   1596    216       C  
ATOM   3443  CG1 VAL A 367      10.621  23.619 -14.921  1.00100.30           C  
ANISOU 3443  CG1 VAL A 367    11851  13589  12671   -611   1629    401       C  
ATOM   3444  CG2 VAL A 367       8.463  23.065 -13.772  1.00 95.74           C  
ANISOU 3444  CG2 VAL A 367    11648  12359  12368   -423   1492    266       C  
ATOM   3445  N   PHE A 368      10.858  21.449 -17.342  1.00106.60           N  
ANISOU 3445  N   PHE A 368    12474  15019  13011   -224   1807     67       N  
ATOM   3446  CA  PHE A 368      11.732  21.348 -18.506  1.00107.43           C  
ANISOU 3446  CA  PHE A 368    12359  15619  12842   -220   1919     66       C  
ATOM   3447  C   PHE A 368      11.638  19.919 -19.029  1.00107.44           C  
ANISOU 3447  C   PHE A 368    12370  15727  12726     97   1945   -231       C  
ATOM   3448  O   PHE A 368      12.119  18.981 -18.386  1.00107.20           O  
ANISOU 3448  O   PHE A 368    12311  15660  12759    322   1934   -437       O  
ATOM   3449  CB  PHE A 368      13.175  21.741 -18.168  1.00107.67           C  
ANISOU 3449  CB  PHE A 368    12130  15954  12825   -313   1984    141       C  
ATOM   3450  CG  PHE A 368      13.638  21.299 -16.802  1.00106.89           C  
ANISOU 3450  CG  PHE A 368    12029  15664  12922   -192   1938     20       C  
ATOM   3451  CD1 PHE A 368      14.202  20.049 -16.614  1.00106.30           C  
ANISOU 3451  CD1 PHE A 368    11872  15710  12808    112   1965   -241       C  
ATOM   3452  CD2 PHE A 368      13.533  22.146 -15.710  1.00106.79           C  
ANISOU 3452  CD2 PHE A 368    12100  15354  13123   -373   1855    165       C  
ATOM   3453  CE1 PHE A 368      14.634  19.643 -15.364  1.00106.11           C  
ANISOU 3453  CE1 PHE A 368    11847  15516  12955    223   1912   -335       C  
ATOM   3454  CE2 PHE A 368      13.962  21.745 -14.455  1.00106.35           C  
ANISOU 3454  CE2 PHE A 368    12038  15145  13226   -264   1809     58       C  
ATOM   3455  CZ  PHE A 368      14.515  20.493 -14.283  1.00106.40           C  
ANISOU 3455  CZ  PHE A 368    11958  15279  13191     28   1839   -180       C  
ATOM   3456  N   GLY A 369      10.999  19.752 -20.181  1.00112.70           N  
ANISOU 3456  N   GLY A 369    13092  16504  13225    120   1959   -254       N  
ATOM   3457  CA  GLY A 369      10.729  18.455 -20.759  1.00112.33           C  
ANISOU 3457  CA  GLY A 369    13101  16508  13070    406   1951   -540       C  
ATOM   3458  C   GLY A 369       9.307  18.388 -21.270  1.00113.22           C  
ANISOU 3458  C   GLY A 369    13439  16375  13203    377   1871   -534       C  
ATOM   3459  O   GLY A 369       8.558  19.368 -21.233  1.00113.29           O  
ANISOU 3459  O   GLY A 369    13543  16208  13294    154   1832   -305       O  
ATOM   3460  N   LYS A 370       8.907  17.210 -21.748  1.00116.47           N  
ANISOU 3460  N   LYS A 370    13944  16764  13545    614   1829   -794       N  
ATOM   3461  CA  LYS A 370       7.601  17.041 -22.374  1.00117.00           C  
ANISOU 3461  CA  LYS A 370    14202  16656  13597    594   1748   -811       C  
ATOM   3462  C   LYS A 370       6.975  15.718 -21.943  1.00115.37           C  
ANISOU 3462  C   LYS A 370    14182  16127  13527    814   1629  -1071       C  
ATOM   3463  O   LYS A 370       7.671  14.712 -21.785  1.00114.21           O  
ANISOU 3463  O   LYS A 370    14001  16038  13358   1052   1623  -1310       O  
ATOM   3464  CB  LYS A 370       7.716  17.116 -23.904  1.00119.04           C  
ANISOU 3464  CB  LYS A 370    14366  17335  13530    599   1816   -827       C  
ATOM   3465  CG  LYS A 370       6.401  16.879 -24.605  1.00119.47           C  
ANISOU 3465  CG  LYS A 370    14608  17235  13550    591   1721   -862       C  
ATOM   3466  CD  LYS A 370       5.605  18.162 -24.735  1.00119.95           C  
ANISOU 3466  CD  LYS A 370    14723  17193  13661    309   1701   -542       C  
ATOM   3467  CE  LYS A 370       4.243  17.887 -25.336  1.00120.42           C  
ANISOU 3467  CE  LYS A 370    14961  17088  13706    311   1593   -580       C  
ATOM   3468  NZ  LYS A 370       3.589  19.127 -25.812  1.00121.18           N  
ANISOU 3468  NZ  LYS A 370    15078  17198  13767     73   1580   -281       N  
ATOM   3469  N   MET A 371       5.660  15.729 -21.766  1.00108.10           N  
ANISOU 3469  N   MET A 371    13456  14872  12746    730   1523  -1017       N  
ATOM   3470  CA  MET A 371       5.001  14.517 -21.239  1.00105.20           C  
ANISOU 3470  CA  MET A 371    13272  14165  12534    884   1392  -1220       C  
ATOM   3471  C   MET A 371       4.422  13.677 -22.363  1.00105.47           C  
ANISOU 3471  C   MET A 371    13404  14261  12410   1002   1320  -1418       C  
ATOM   3472  O   MET A 371       3.504  14.162 -23.033  1.00107.52           O  
ANISOU 3472  O   MET A 371    13719  14528  12607    864   1295  -1307       O  
ATOM   3473  CB  MET A 371       3.873  14.914 -20.282  1.00103.23           C  
ANISOU 3473  CB  MET A 371    13164  13525  12534    726   1309  -1055       C  
ATOM   3474  CG  MET A 371       3.948  14.239 -18.933  1.00 99.52           C  
ANISOU 3474  CG  MET A 371    12770  12752  12292    810   1242  -1123       C  
ATOM   3475  SD  MET A 371       5.457  14.712 -18.072  1.00 99.60           S  
ANISOU 3475  SD  MET A 371    12597  12909  12337    833   1348  -1070       S  
ATOM   3476  CE  MET A 371       5.556  16.429 -18.558  1.00103.40           C  
ANISOU 3476  CE  MET A 371    12952  13612  12725    574   1453   -783       C  
ATOM   3477  N   ASN A 372       5.009  12.515 -22.632  1.00101.72           N  
ANISOU 3477  N   ASN A 372    12939  13857  11853   1257   1286  -1707       N  
ATOM   3478  CA  ASN A 372       4.375  11.566 -23.526  1.00102.00           C  
ANISOU 3478  CA  ASN A 372    13114  13861  11779   1385   1174  -1935       C  
ATOM   3479  C   ASN A 372       3.071  11.071 -22.901  1.00100.05           C  
ANISOU 3479  C   ASN A 372    13093  13150  11772   1302   1006  -1919       C  
ATOM   3480  O   ASN A 372       2.775  11.320 -21.727  1.00 98.27           O  
ANISOU 3480  O   ASN A 372    12907  12649  11783   1193    984  -1766       O  
ATOM   3481  CB  ASN A 372       5.313  10.396 -23.830  1.00100.78           C  
ANISOU 3481  CB  ASN A 372    12942  13839  11510   1707   1150  -2271       C  
ATOM   3482  CG  ASN A 372       5.887   9.761 -22.580  1.00 98.26           C  
ANISOU 3482  CG  ASN A 372    12655  13265  11413   1841   1099  -2347       C  
ATOM   3483  OD1 ASN A 372       5.155   9.427 -21.653  1.00 96.91           O  
ANISOU 3483  OD1 ASN A 372    12651  12678  11494   1767    979  -2291       O  
ATOM   3484  ND2 ASN A 372       7.204   9.594 -22.549  1.00 97.96           N  
ANISOU 3484  ND2 ASN A 372    12446  13503  11272   2036   1189  -2464       N  
ATOM   3485  N   LYS A 373       2.278  10.363 -23.705  1.00100.56           N  
ANISOU 3485  N   LYS A 373    13298  13151  11759   1347    882  -2077       N  
ATOM   3486  CA  LYS A 373       1.037   9.798 -23.189  1.00 98.79           C  
ANISOU 3486  CA  LYS A 373    13274  12517  11745   1255    708  -2066       C  
ATOM   3487  C   LYS A 373       1.296   8.841 -22.031  1.00 96.17           C  
ANISOU 3487  C   LYS A 373    13048  11853  11640   1366    608  -2168       C  
ATOM   3488  O   LYS A 373       0.426   8.654 -21.172  1.00 94.62           O  
ANISOU 3488  O   LYS A 373    12965  11325  11662   1235    507  -2056       O  
ATOM   3489  CB  LYS A 373       0.276   9.099 -24.317  1.00100.59           C  
ANISOU 3489  CB  LYS A 373    13631  12753  11835   1297    574  -2252       C  
ATOM   3490  CG  LYS A 373      -1.111   8.635 -23.930  1.00 99.20           C  
ANISOU 3490  CG  LYS A 373    13634  12206  11851   1148    393  -2204       C  
ATOM   3491  CD  LYS A 373      -2.092   8.750 -25.083  1.00102.07           C  
ANISOU 3491  CD  LYS A 373    14044  12678  12059   1052    321  -2215       C  
ATOM   3492  CE  LYS A 373      -3.396   8.035 -24.759  1.00102.24           C  
ANISOU 3492  CE  LYS A 373    14242  12344  12261    926    112  -2218       C  
ATOM   3493  NZ  LYS A 373      -4.576   8.937 -24.889  1.00102.34           N  
ANISOU 3493  NZ  LYS A 373    14209  12383  12293    688    118  -1963       N  
ATOM   3494  N   LEU A 374       2.494   8.252 -21.970  1.00 96.66           N  
ANISOU 3494  N   LEU A 374    13062  12018  11647   1609    633  -2366       N  
ATOM   3495  CA  LEU A 374       2.799   7.317 -20.893  1.00 94.36           C  
ANISOU 3495  CA  LEU A 374    12878  11410  11564   1733    522  -2460       C  
ATOM   3496  C   LEU A 374       3.021   8.044 -19.570  1.00 92.17           C  
ANISOU 3496  C   LEU A 374    12513  11036  11471   1600    610  -2209       C  
ATOM   3497  O   LEU A 374       2.401   7.701 -18.556  1.00 90.09           O  
ANISOU 3497  O   LEU A 374    12371  10431  11427   1509    506  -2117       O  
ATOM   3498  CB  LEU A 374       4.018   6.467 -21.250  1.00 94.40           C  
ANISOU 3498  CB  LEU A 374    12854  11565  11449   2066    511  -2761       C  
ATOM   3499  CG  LEU A 374       4.221   5.303 -20.277  1.00 91.77           C  
ANISOU 3499  CG  LEU A 374    12684  10853  11330   2222    340  -2890       C  
ATOM   3500  CD1 LEU A 374       3.148   4.240 -20.481  1.00 90.71           C  
ANISOU 3500  CD1 LEU A 374    12825  10345  11295   2203     95  -3017       C  
ATOM   3501  CD2 LEU A 374       5.612   4.704 -20.416  1.00 91.08           C  
ANISOU 3501  CD2 LEU A 374    12513  10953  11139   2570    361  -3146       C  
ATOM   3502  N   ILE A 375       3.905   9.047 -19.555  1.00 89.07           N  
ANISOU 3502  N   ILE A 375    11908  10951  10984   1577    793  -2093       N  
ATOM   3503  CA  ILE A 375       4.183   9.754 -18.308  1.00 87.38           C  
ANISOU 3503  CA  ILE A 375    11615  10652  10935   1460    864  -1879       C  
ATOM   3504  C   ILE A 375       2.931  10.461 -17.804  1.00 86.56           C  
ANISOU 3504  C   ILE A 375    11578  10342  10968   1198    842  -1635       C  
ATOM   3505  O   ILE A 375       2.755  10.644 -16.593  1.00 84.20           O  
ANISOU 3505  O   ILE A 375    11300   9838  10853   1117    828  -1501       O  
ATOM   3506  CB  ILE A 375       5.363  10.729 -18.477  1.00 88.90           C  
ANISOU 3506  CB  ILE A 375    11565  11220  10991   1457   1047  -1797       C  
ATOM   3507  CG1 ILE A 375       6.589   9.987 -19.020  1.00 90.15           C  
ANISOU 3507  CG1 ILE A 375    11626  11638  10988   1741   1074  -2053       C  
ATOM   3508  CG2 ILE A 375       5.704  11.408 -17.152  1.00 87.70           C  
ANISOU 3508  CG2 ILE A 375    11345  10964  11012   1346   1097  -1603       C  
ATOM   3509  CD1 ILE A 375       7.226   9.033 -18.033  1.00 88.00           C  
ANISOU 3509  CD1 ILE A 375    11403  11166  10866   1946    987  -2190       C  
ATOM   3510  N   LYS A 376       2.032  10.852 -18.711  1.00 90.33           N  
ANISOU 3510  N   LYS A 376    12085  10886  11350   1078    835  -1582       N  
ATOM   3511  CA  LYS A 376       0.737  11.365 -18.277  1.00 89.76           C  
ANISOU 3511  CA  LYS A 376    12081  10616  11406    867    789  -1383       C  
ATOM   3512  C   LYS A 376      -0.077  10.282 -17.577  1.00 87.05           C  
ANISOU 3512  C   LYS A 376    11910   9925  11241    865    623  -1437       C  
ATOM   3513  O   LYS A 376      -0.744  10.549 -16.571  1.00 84.43           O  
ANISOU 3513  O   LYS A 376    11602   9407  11070    735    600  -1271       O  
ATOM   3514  CB  LYS A 376      -0.037  11.928 -19.469  1.00 92.12           C  
ANISOU 3514  CB  LYS A 376    12372  11074  11554    761    799  -1327       C  
ATOM   3515  CG  LYS A 376       0.411  13.308 -19.925  1.00 94.44           C  
ANISOU 3515  CG  LYS A 376    12512  11650  11723    664    948  -1153       C  
ATOM   3516  CD  LYS A 376      -0.596  13.905 -20.896  1.00 97.82           C  
ANISOU 3516  CD  LYS A 376    12959  12166  12044    535    927  -1049       C  
ATOM   3517  CE  LYS A 376       0.037  14.975 -21.767  1.00101.43           C  
ANISOU 3517  CE  LYS A 376    13277  12959  12302    477   1053   -931       C  
ATOM   3518  NZ  LYS A 376       1.007  14.400 -22.738  1.00102.20           N  
ANISOU 3518  NZ  LYS A 376    13306  13358  12169    633   1104  -1128       N  
ATOM   3519  N   THR A 377      -0.031   9.050 -18.094  1.00 89.89           N  
ANISOU 3519  N   THR A 377    12391  10197  11565   1007    495  -1668       N  
ATOM   3520  CA  THR A 377      -0.835   7.975 -17.520  1.00 88.05           C  
ANISOU 3520  CA  THR A 377    12339   9617  11498    974    308  -1705       C  
ATOM   3521  C   THR A 377      -0.300   7.552 -16.159  1.00 85.05           C  
ANISOU 3521  C   THR A 377    11985   9038  11294   1028    282  -1667       C  
ATOM   3522  O   THR A 377      -1.070   7.384 -15.207  1.00 82.97           O  
ANISOU 3522  O   THR A 377    11787   8545  11192    889    208  -1521       O  
ATOM   3523  CB  THR A 377      -0.877   6.768 -18.459  1.00 89.20           C  
ANISOU 3523  CB  THR A 377    12634   9693  11566   1117    149  -1977       C  
ATOM   3524  OG1 THR A 377       0.390   6.613 -19.104  1.00 90.37           O  
ANISOU 3524  OG1 THR A 377    12710  10078  11549   1360    223  -2185       O  
ATOM   3525  CG2 THR A 377      -1.962   6.931 -19.510  1.00 90.98           C  
ANISOU 3525  CG2 THR A 377    12898   9984  11686    987     95  -1972       C  
ATOM   3526  N   VAL A 378       1.017   7.353 -16.049  1.00 83.80           N  
ANISOU 3526  N   VAL A 378    11764   8985  11091   1232    338  -1795       N  
ATOM   3527  CA  VAL A 378       1.578   6.933 -14.768  1.00 81.66           C  
ANISOU 3527  CA  VAL A 378    11516   8536  10977   1298    302  -1761       C  
ATOM   3528  C   VAL A 378       1.384   8.026 -13.727  1.00 80.09           C  
ANISOU 3528  C   VAL A 378    11205   8360  10864   1122    419  -1500       C  
ATOM   3529  O   VAL A 378       1.073   7.745 -12.564  1.00 78.16           O  
ANISOU 3529  O   VAL A 378    11022   7901  10775   1056    355  -1388       O  
ATOM   3530  CB  VAL A 378       3.061   6.535 -14.918  1.00 82.49           C  
ANISOU 3530  CB  VAL A 378    11550   8789  11002   1573    339  -1960       C  
ATOM   3531  CG1 VAL A 378       3.823   7.574 -15.695  1.00 84.66           C  
ANISOU 3531  CG1 VAL A 378    11611   9472  11083   1598    534  -1958       C  
ATOM   3532  CG2 VAL A 378       3.704   6.309 -13.555  1.00 80.93           C  
ANISOU 3532  CG2 VAL A 378    11343   8451  10955   1632    321  -1892       C  
ATOM   3533  N   PHE A 379       1.530   9.292 -14.130  1.00 81.88           N  
ANISOU 3533  N   PHE A 379    11278   8845  10988   1037    579  -1395       N  
ATOM   3534  CA  PHE A 379       1.243  10.386 -13.207  1.00 79.92           C  
ANISOU 3534  CA  PHE A 379    10947   8597  10821    875    667  -1165       C  
ATOM   3535  C   PHE A 379      -0.222  10.397 -12.794  1.00 78.36           C  
ANISOU 3535  C   PHE A 379    10838   8211  10726    699    590  -1025       C  
ATOM   3536  O   PHE A 379      -0.545  10.784 -11.664  1.00 76.15           O  
ANISOU 3536  O   PHE A 379    10540   7840  10554    610    604   -874       O  
ATOM   3537  CB  PHE A 379       1.623  11.730 -13.827  1.00 81.82           C  
ANISOU 3537  CB  PHE A 379    11034   9118  10937    808    819  -1077       C  
ATOM   3538  CG  PHE A 379       1.339  12.900 -12.933  1.00 79.96           C  
ANISOU 3538  CG  PHE A 379    10734   8861  10785    658    887   -866       C  
ATOM   3539  CD1 PHE A 379       2.234  13.261 -11.942  1.00 78.42           C  
ANISOU 3539  CD1 PHE A 379    10463   8682  10652    685    940   -822       C  
ATOM   3540  CD2 PHE A 379       0.169  13.628 -13.071  1.00 79.49           C  
ANISOU 3540  CD2 PHE A 379    10695   8766  10741    506    885   -725       C  
ATOM   3541  CE1 PHE A 379       1.974  14.331 -11.111  1.00 76.80           C  
ANISOU 3541  CE1 PHE A 379    10216   8446  10519    562    986   -654       C  
ATOM   3542  CE2 PHE A 379      -0.100  14.695 -12.238  1.00 77.50           C  
ANISOU 3542  CE2 PHE A 379    10398   8485  10565    403    932   -558       C  
ATOM   3543  CZ  PHE A 379       0.807  15.051 -11.260  1.00 76.21           C  
ANISOU 3543  CZ  PHE A 379    10172   8326  10459    430    981   -529       C  
ATOM   3544  N   ALA A 380      -1.121   9.988 -13.692  1.00 78.80           N  
ANISOU 3544  N   ALA A 380    10975   8232  10735    649    507  -1075       N  
ATOM   3545  CA  ALA A 380      -2.524   9.841 -13.321  1.00 78.19           C  
ANISOU 3545  CA  ALA A 380    10965   7993  10749    483    417   -950       C  
ATOM   3546  C   ALA A 380      -2.689   8.777 -12.243  1.00 76.91           C  
ANISOU 3546  C   ALA A 380    10913   7572  10737    477    291   -937       C  
ATOM   3547  O   ALA A 380      -3.329   9.012 -11.212  1.00 75.52           O  
ANISOU 3547  O   ALA A 380    10717   7319  10657    355    290   -766       O  
ATOM   3548  CB  ALA A 380      -3.360   9.497 -14.554  1.00 80.71           C  
ANISOU 3548  CB  ALA A 380    11350   8333  10982    435    332  -1026       C  
ATOM   3549  N   PHE A 381      -2.111   7.594 -12.467  1.00 77.85           N  
ANISOU 3549  N   PHE A 381    11150   7560  10870    615    174  -1116       N  
ATOM   3550  CA  PHE A 381      -2.154   6.540 -11.457  1.00 75.85           C  
ANISOU 3550  CA  PHE A 381    11020   7038  10761    616     33  -1094       C  
ATOM   3551  C   PHE A 381      -1.329   6.911 -10.230  1.00 74.09           C  
ANISOU 3551  C   PHE A 381    10717   6834  10599    672    120  -1004       C  
ATOM   3552  O   PHE A 381      -1.684   6.545  -9.104  1.00 72.89           O  
ANISOU 3552  O   PHE A 381    10611   6523  10559    588     54   -870       O  
ATOM   3553  CB  PHE A 381      -1.659   5.222 -12.055  1.00 77.19           C  
ANISOU 3553  CB  PHE A 381    11352   7044  10932    784   -133  -1330       C  
ATOM   3554  CG  PHE A 381      -2.679   4.509 -12.900  1.00 78.71           C  
ANISOU 3554  CG  PHE A 381    11684   7103  11118    688   -298  -1400       C  
ATOM   3555  CD1 PHE A 381      -3.689   3.762 -12.317  1.00 78.34           C  
ANISOU 3555  CD1 PHE A 381    11762   6798  11205    504   -469  -1279       C  
ATOM   3556  CD2 PHE A 381      -2.628   4.593 -14.282  1.00 81.25           C  
ANISOU 3556  CD2 PHE A 381    12004   7577  11290    767   -286  -1578       C  
ATOM   3557  CE1 PHE A 381      -4.625   3.104 -13.098  1.00 80.16           C  
ANISOU 3557  CE1 PHE A 381    12118   6906  11435    393   -638  -1340       C  
ATOM   3558  CE2 PHE A 381      -3.563   3.942 -15.067  1.00 82.58           C  
ANISOU 3558  CE2 PHE A 381    12303   7627  11447    676   -451  -1654       C  
ATOM   3559  CZ  PHE A 381      -4.564   3.199 -14.474  1.00 81.67           C  
ANISOU 3559  CZ  PHE A 381    12315   7236  11481    484   -632  -1537       C  
ATOM   3560  N   CYS A 382      -0.216   7.625 -10.425  1.00 75.95           N  
ANISOU 3560  N   CYS A 382    10826   7280  10752    802    261  -1068       N  
ATOM   3561  CA  CYS A 382       0.601   8.034  -9.287  1.00 73.87           C  
ANISOU 3561  CA  CYS A 382    10478   7051  10539    847    337   -989       C  
ATOM   3562  C   CYS A 382      -0.088   9.085  -8.428  1.00 72.13           C  
ANISOU 3562  C   CYS A 382    10172   6878  10356    672    425   -772       C  
ATOM   3563  O   CYS A 382       0.278   9.249  -7.260  1.00 70.41           O  
ANISOU 3563  O   CYS A 382     9920   6633  10199    675    447   -685       O  
ATOM   3564  CB  CYS A 382       1.957   8.565  -9.757  1.00 75.47           C  
ANISOU 3564  CB  CYS A 382    10546   7491  10636   1005    459  -1103       C  
ATOM   3565  SG  CYS A 382       3.220   7.293  -9.998  1.00 77.27           S  
ANISOU 3565  SG  CYS A 382    10833   7675  10852   1295    362  -1349       S  
ATOM   3566  N   SER A 383      -1.079   9.795  -8.975  1.00 71.66           N  
ANISOU 3566  N   SER A 383    10080   6896  10254    536    469   -693       N  
ATOM   3567  CA  SER A 383      -1.799  10.796  -8.198  1.00 69.40           C  
ANISOU 3567  CA  SER A 383     9715   6656   9996    402    540   -511       C  
ATOM   3568  C   SER A 383      -2.582  10.184  -7.044  1.00 68.58           C  
ANISOU 3568  C   SER A 383     9668   6398   9991    310    454   -388       C  
ATOM   3569  O   SER A 383      -2.987  10.912  -6.132  1.00 67.47           O  
ANISOU 3569  O   SER A 383     9456   6310   9868    240    514   -254       O  
ATOM   3570  CB  SER A 383      -2.741  11.588  -9.105  1.00 70.83           C  
ANISOU 3570  CB  SER A 383     9855   6945  10111    302    581   -462       C  
ATOM   3571  OG  SER A 383      -2.014  12.445  -9.970  1.00 71.29           O  
ANISOU 3571  OG  SER A 383     9838   7180  10071    354    682   -515       O  
ATOM   3572  N   MET A 384      -2.803   8.867  -7.061  1.00 71.01           N  
ANISOU 3572  N   MET A 384    10106   6521  10354    306    306   -428       N  
ATOM   3573  CA  MET A 384      -3.465   8.207  -5.943  1.00 70.59           C  
ANISOU 3573  CA  MET A 384    10106   6327  10387    196    212   -285       C  
ATOM   3574  C   MET A 384      -2.647   8.286  -4.661  1.00 69.78           C  
ANISOU 3574  C   MET A 384     9973   6219  10320    265    247   -228       C  
ATOM   3575  O   MET A 384      -3.208   8.126  -3.571  1.00 69.77           O  
ANISOU 3575  O   MET A 384     9968   6184  10358    163    218    -70       O  
ATOM   3576  CB  MET A 384      -3.746   6.741  -6.286  1.00 71.75           C  
ANISOU 3576  CB  MET A 384    10425   6241  10597    171     15   -340       C  
ATOM   3577  CG  MET A 384      -4.383   6.518  -7.650  1.00 74.17           C  
ANISOU 3577  CG  MET A 384    10782   6540  10859    127    -46   -441       C  
ATOM   3578  SD  MET A 384      -6.151   6.860  -7.710  1.00 76.96           S  
ANISOU 3578  SD  MET A 384    11073   6962  11208   -129    -62   -259       S  
ATOM   3579  CE  MET A 384      -6.609   6.547  -6.008  1.00 74.88           C  
ANISOU 3579  CE  MET A 384    10789   6635  11027   -263    -94    -24       C  
ATOM   3580  N   LEU A 385      -1.336   8.532  -4.767  1.00 69.02           N  
ANISOU 3580  N   LEU A 385     9841   6183  10199    432    307   -349       N  
ATOM   3581  CA  LEU A 385      -0.490   8.591  -3.579  1.00 67.71           C  
ANISOU 3581  CA  LEU A 385     9641   6022  10063    504    328   -306       C  
ATOM   3582  C   LEU A 385      -0.914   9.709  -2.636  1.00 66.79           C  
ANISOU 3582  C   LEU A 385     9413   6040   9924    411    436   -162       C  
ATOM   3583  O   LEU A 385      -0.772   9.576  -1.415  1.00 66.63           O  
ANISOU 3583  O   LEU A 385     9387   5999   9928    404    418    -69       O  
ATOM   3584  CB  LEU A 385       0.976   8.771  -3.978  1.00 68.19           C  
ANISOU 3584  CB  LEU A 385     9648   6173  10087    691    382   -463       C  
ATOM   3585  CG  LEU A 385       1.625   7.690  -4.845  1.00 68.97           C  
ANISOU 3585  CG  LEU A 385     9841   6176  10188    851    281   -647       C  
ATOM   3586  CD1 LEU A 385       2.981   8.159  -5.351  1.00 69.83           C  
ANISOU 3586  CD1 LEU A 385     9831   6480  10222   1020    379   -790       C  
ATOM   3587  CD2 LEU A 385       1.757   6.387  -4.073  1.00 68.48           C  
ANISOU 3587  CD2 LEU A 385     9923   5874  10223    908    109   -631       C  
ATOM   3588  N   CYS A 386      -1.473  10.779  -3.189  1.00 67.28           N  
ANISOU 3588  N   CYS A 386     9395   6234   9935    348    533   -147       N  
ATOM   3589  CA  CYS A 386      -1.906  11.926  -2.351  1.00 66.33           C  
ANISOU 3589  CA  CYS A 386     9177   6235   9791    290    624    -39       C  
ATOM   3590  C   CYS A 386      -3.053  11.469  -1.451  1.00 67.66           C  
ANISOU 3590  C   CYS A 386     9360   6371   9978    175    571    110       C  
ATOM   3591  O   CYS A 386      -3.188  12.022  -0.350  1.00 68.65           O  
ANISOU 3591  O   CYS A 386     9422   6580  10081    165    618    191       O  
ATOM   3592  CB  CYS A 386      -2.285  13.125  -3.211  1.00 66.48           C  
ANISOU 3592  CB  CYS A 386     9128   6372   9759    262    712    -55       C  
ATOM   3593  SG  CYS A 386      -3.994  13.127  -3.802  1.00 67.32           S  
ANISOU 3593  SG  CYS A 386     9235   6491   9850    133    682     27       S  
ATOM   3594  N   LEU A 387      -3.838  10.492  -1.902  1.00 67.82           N  
ANISOU 3594  N   LEU A 387     9455   6286  10026     86    470    144       N  
ATOM   3595  CA  LEU A 387      -4.903   9.947  -1.072  1.00 69.40           C  
ANISOU 3595  CA  LEU A 387     9658   6474  10238    -54    409    310       C  
ATOM   3596  C   LEU A 387      -4.391   8.900  -0.093  1.00 70.01           C  
ANISOU 3596  C   LEU A 387     9819   6420  10362    -50    309    375       C  
ATOM   3597  O   LEU A 387      -5.011   8.687   0.955  1.00 70.93           O  
ANISOU 3597  O   LEU A 387     9905   6583  10463   -153    290    540       O  
ATOM   3598  CB  LEU A 387      -6.007   9.342  -1.945  1.00 71.00           C  
ANISOU 3598  CB  LEU A 387     9902   6619  10456   -187    322    341       C  
ATOM   3599  CG  LEU A 387      -6.677  10.285  -2.948  1.00 70.56           C  
ANISOU 3599  CG  LEU A 387     9767   6695  10350   -203    397    299       C  
ATOM   3600  CD1 LEU A 387      -7.894   9.628  -3.582  1.00 73.19           C  
ANISOU 3600  CD1 LEU A 387    10123   6994  10693   -360    295    359       C  
ATOM   3601  CD2 LEU A 387      -7.059  11.596  -2.280  1.00 70.60           C  
ANISOU 3601  CD2 LEU A 387     9631   6896  10298   -183    525    365       C  
ATOM   3602  N   LEU A 388      -3.274   8.241  -0.413  1.00 69.14           N  
ANISOU 3602  N   LEU A 388     9806   6163  10299     75    243    254       N  
ATOM   3603  CA  LEU A 388      -2.646   7.334   0.542  1.00 69.06           C  
ANISOU 3603  CA  LEU A 388     9879   6025  10336    114    141    310       C  
ATOM   3604  C   LEU A 388      -2.046   8.105   1.710  1.00 68.50           C  
ANISOU 3604  C   LEU A 388     9709   6102  10217    177    238    356       C  
ATOM   3605  O   LEU A 388      -2.220   7.726   2.875  1.00 70.45           O  
ANISOU 3605  O   LEU A 388     9964   6349  10455    119    193    504       O  
ATOM   3606  CB  LEU A 388      -1.572   6.500  -0.153  1.00 68.40           C  
ANISOU 3606  CB  LEU A 388     9914   5766  10309    275     43    140       C  
ATOM   3607  CG  LEU A 388      -0.854   5.477   0.729  1.00 68.94           C  
ANISOU 3607  CG  LEU A 388    10089   5667  10438    349    -93    184       C  
ATOM   3608  CD1 LEU A 388      -1.846   4.554   1.425  1.00 69.44           C  
ANISOU 3608  CD1 LEU A 388    10251   5587  10548    155   -235    396       C  
ATOM   3609  CD2 LEU A 388       0.151   4.684  -0.087  1.00 68.67           C  
ANISOU 3609  CD2 LEU A 388    10164   5472  10454    546   -194    -18       C  
ATOM   3610  N   ASN A 389      -1.327   9.189   1.411  1.00 66.08           N  
ANISOU 3610  N   ASN A 389     9309   5927   9871    286    362    235       N  
ATOM   3611  CA  ASN A 389      -0.735  10.024   2.452  1.00 66.41           C  
ANISOU 3611  CA  ASN A 389     9259   6106   9867    341    443    255       C  
ATOM   3612  C   ASN A 389      -1.794  10.535   3.421  1.00 67.50           C  
ANISOU 3612  C   ASN A 389     9328   6376   9943    229    490    404       C  
ATOM   3613  O   ASN A 389      -1.590  10.545   4.640  1.00 68.65           O  
ANISOU 3613  O   ASN A 389     9449   6586  10050    238    487    484       O  
ATOM   3614  CB  ASN A 389       0.007  11.196   1.809  1.00 64.86           C  
ANISOU 3614  CB  ASN A 389     8979   6023   9644    426    554    117       C  
ATOM   3615  CG  ASN A 389       0.986  11.861   2.751  1.00 63.66           C  
ANISOU 3615  CG  ASN A 389     8756   5967   9464    502    598     98       C  
ATOM   3616  OD1 ASN A 389       1.192  11.406   3.876  1.00 65.65           O  
ANISOU 3616  OD1 ASN A 389     9025   6209   9711    515    547    173       O  
ATOM   3617  ND2 ASN A 389       1.595  12.951   2.295  1.00 64.04           N  
ANISOU 3617  ND2 ASN A 389     8727   6113   9491    539    682      6       N  
ATOM   3618  N   SER A 390      -2.942  10.960   2.890  1.00 69.61           N  
ANISOU 3618  N   SER A 390     9553   6710  10187    135    533    438       N  
ATOM   3619  CA  SER A 390      -3.997  11.485   3.746  1.00 70.69           C  
ANISOU 3619  CA  SER A 390     9597   7014  10247     55    586    562       C  
ATOM   3620  C   SER A 390      -4.577  10.403   4.647  1.00 73.08           C  
ANISOU 3620  C   SER A 390     9929   7300  10537    -64    499    746       C  
ATOM   3621  O   SER A 390      -5.125  10.712   5.711  1.00 75.43           O  
ANISOU 3621  O   SER A 390    10140   7773  10745   -105    542    858       O  
ATOM   3622  CB  SER A 390      -5.098  12.113   2.892  1.00 70.96           C  
ANISOU 3622  CB  SER A 390     9571   7129  10263     -4    638    556       C  
ATOM   3623  OG  SER A 390      -6.205  12.491   3.686  1.00 74.94           O  
ANISOU 3623  OG  SER A 390     9969   7817  10685    -68    681    674       O  
ATOM   3624  N   THR A 391      -4.461   9.135   4.249  1.00 71.34           N  
ANISOU 3624  N   THR A 391     9833   6875  10397   -121    367    781       N  
ATOM   3625  CA  THR A 391      -5.035   8.037   5.017  1.00 73.06           C  
ANISOU 3625  CA  THR A 391    10101   7042  10617   -270    254    984       C  
ATOM   3626  C   THR A 391      -4.100   7.506   6.094  1.00 73.48           C  
ANISOU 3626  C   THR A 391    10213   7036  10669   -207    190   1042       C  
ATOM   3627  O   THR A 391      -4.572   6.997   7.118  1.00 74.78           O  
ANISOU 3627  O   THR A 391    10369   7260  10783   -325    141   1243       O  
ATOM   3628  CB  THR A 391      -5.419   6.880   4.090  1.00 72.68           C  
ANISOU 3628  CB  THR A 391    10186   6761  10668   -377    103   1001       C  
ATOM   3629  OG1 THR A 391      -5.859   7.393   2.827  1.00 71.85           O  
ANISOU 3629  OG1 THR A 391    10051   6676  10574   -373    154    876       O  
ATOM   3630  CG2 THR A 391      -6.527   6.059   4.711  1.00 74.74           C  
ANISOU 3630  CG2 THR A 391    10449   7035  10913   -612      7   1250       C  
ATOM   3631  N   VAL A 392      -2.790   7.600   5.889  1.00 72.00           N  
ANISOU 3631  N   VAL A 392    10075   6755  10528    -28    186    883       N  
ATOM   3632  CA  VAL A 392      -1.848   7.039   6.849  1.00 71.85           C  
ANISOU 3632  CA  VAL A 392    10113   6672  10513     50    107    931       C  
ATOM   3633  C   VAL A 392      -1.507   8.027   7.962  1.00 72.97           C  
ANISOU 3633  C   VAL A 392    10131   7049  10544    112    218    941       C  
ATOM   3634  O   VAL A 392      -1.158   7.608   9.070  1.00 74.84           O  
ANISOU 3634  O   VAL A 392    10387   7309  10739    116    160   1056       O  
ATOM   3635  CB  VAL A 392      -0.578   6.570   6.126  1.00 70.71           C  
ANISOU 3635  CB  VAL A 392    10064   6336  10465    227     34    753       C  
ATOM   3636  CG1 VAL A 392      -0.865   5.317   5.316  1.00 70.74           C  
ANISOU 3636  CG1 VAL A 392    10231   6072  10574    180   -129    757       C  
ATOM   3637  CG2 VAL A 392      -0.073   7.669   5.224  1.00 69.54           C  
ANISOU 3637  CG2 VAL A 392     9825   6293  10305    339    170    547       C  
ATOM   3638  N   ASP A 393      -1.593   9.328   7.689  1.00 72.48           N  
ANISOU 3638  N   ASP A 393     9956   7150  10431    162    361    821       N  
ATOM   3639  CA  ASP A 393      -1.339  10.339   8.715  1.00 73.33           C  
ANISOU 3639  CA  ASP A 393     9961   7468  10433    222    451    806       C  
ATOM   3640  C   ASP A 393      -2.177  10.151   9.974  1.00 77.18           C  
ANISOU 3640  C   ASP A 393    10398   8126  10800    122    451    999       C  
ATOM   3641  O   ASP A 393      -1.607  10.207  11.076  1.00 78.82           O  
ANISOU 3641  O   ASP A 393    10590   8426  10933    175    438   1035       O  
ATOM   3642  CB  ASP A 393      -1.558  11.736   8.119  1.00 73.24           C  
ANISOU 3642  CB  ASP A 393     9862   7568  10399    267    577    663       C  
ATOM   3643  CG  ASP A 393      -0.302  12.308   7.506  1.00 70.08           C  
ANISOU 3643  CG  ASP A 393     9465   7105  10056    388    598    484       C  
ATOM   3644  OD1 ASP A 393       0.790  11.762   7.768  1.00 70.52           O  
ANISOU 3644  OD1 ASP A 393     9560   7088  10147    463    534    457       O  
ATOM   3645  OD2 ASP A 393      -0.410  13.296   6.754  1.00 68.42           O  
ANISOU 3645  OD2 ASP A 393     9213   6930   9855    404    674    381       O  
ATOM   3646  N   PRO A 394      -3.498   9.935   9.904  1.00 76.08           N  
ANISOU 3646  N   PRO A 394    10218   8068  10621    -24    464   1133       N  
ATOM   3647  CA  PRO A 394      -4.248   9.692  11.148  1.00 79.02           C  
ANISOU 3647  CA  PRO A 394    10519   8650  10853   -128    468   1337       C  
ATOM   3648  C   PRO A 394      -3.795   8.444  11.884  1.00 80.60           C  
ANISOU 3648  C   PRO A 394    10823   8736  11067   -193    328   1514       C  
ATOM   3649  O   PRO A 394      -3.924   8.377  13.113  1.00 83.36           O  
ANISOU 3649  O   PRO A 394    11118   9274  11280   -227    332   1657       O  
ATOM   3650  CB  PRO A 394      -5.703   9.574  10.673  1.00 80.68           C  
ANISOU 3650  CB  PRO A 394    10660   8953  11043   -287    493   1446       C  
ATOM   3651  CG  PRO A 394      -5.735  10.174   9.317  1.00 78.63           C  
ANISOU 3651  CG  PRO A 394    10410   8586  10881   -225    538   1260       C  
ATOM   3652  CD  PRO A 394      -4.386   9.962   8.728  1.00 74.46           C  
ANISOU 3652  CD  PRO A 394    10006   7811  10474   -105    482   1109       C  
ATOM   3653  N   ILE A 395      -3.268   7.451  11.166  1.00 80.17           N  
ANISOU 3653  N   ILE A 395    10920   8377  11164   -200    195   1505       N  
ATOM   3654  CA  ILE A 395      -2.741   6.260  11.822  1.00 80.29           C  
ANISOU 3654  CA  ILE A 395    11059   8234  11212   -233     34   1662       C  
ATOM   3655  C   ILE A 395      -1.497   6.608  12.628  1.00 80.99           C  
ANISOU 3655  C   ILE A 395    11140   8377  11255    -55     40   1581       C  
ATOM   3656  O   ILE A 395      -1.253   6.036  13.696  1.00 83.09           O  
ANISOU 3656  O   ILE A 395    11438   8674  11456    -83    -43   1749       O  
ATOM   3657  CB  ILE A 395      -2.460   5.158  10.783  1.00 78.69           C  
ANISOU 3657  CB  ILE A 395    11036   7673  11191   -243   -126   1629       C  
ATOM   3658  CG1 ILE A 395      -3.739   4.802  10.021  1.00 78.96           C  
ANISOU 3658  CG1 ILE A 395    11078   7661  11263   -443   -150   1715       C  
ATOM   3659  CG2 ILE A 395      -1.883   3.917  11.453  1.00 78.55           C  
ANISOU 3659  CG2 ILE A 395    11171   7451  11222   -253   -322   1786       C  
ATOM   3660  CD1 ILE A 395      -4.947   4.588  10.916  1.00 81.32           C  
ANISOU 3660  CD1 ILE A 395    11288   8171  11440   -677   -145   1997       C  
ATOM   3661  N   ILE A 396      -0.695   7.555  12.136  1.00 80.05           N  
ANISOU 3661  N   ILE A 396    10972   8279  11164    115    130   1337       N  
ATOM   3662  CA  ILE A 396       0.467   8.006  12.898  1.00 80.93           C  
ANISOU 3662  CA  ILE A 396    11051   8472  11226    268    138   1253       C  
ATOM   3663  C   ILE A 396       0.023   8.644  14.209  1.00 84.18           C  
ANISOU 3663  C   ILE A 396    11354   9183  11449    232    213   1348       C  
ATOM   3664  O   ILE A 396       0.541   8.316  15.283  1.00 85.94           O  
ANISOU 3664  O   ILE A 396    11588   9472  11592    260    148   1445       O  
ATOM   3665  CB  ILE A 396       1.326   8.973  12.061  1.00 78.88           C  
ANISOU 3665  CB  ILE A 396    10744   8199  11028    416    221    990       C  
ATOM   3666  CG1 ILE A 396       1.928   8.253  10.852  1.00 76.05           C  
ANISOU 3666  CG1 ILE A 396    10483   7588  10827    483    143    888       C  
ATOM   3667  CG2 ILE A 396       2.430   9.581  12.911  1.00 78.99           C  
ANISOU 3667  CG2 ILE A 396    10699   8337  10978    542    232    908       C  
ATOM   3668  CD1 ILE A 396       2.376   9.184   9.748  1.00 73.33           C  
ANISOU 3668  CD1 ILE A 396    10076   7257  10528    565    244    669       C  
ATOM   3669  N   TYR A 397      -0.950   9.560  14.145  1.00 83.78           N  
ANISOU 3669  N   TYR A 397    11195   9328  11311    184    344   1315       N  
ATOM   3670  CA  TYR A 397      -1.451  10.180  15.369  1.00 86.99           C  
ANISOU 3670  CA  TYR A 397    11490  10047  11517    175    418   1381       C  
ATOM   3671  C   TYR A 397      -2.030   9.136  16.315  1.00 88.64           C  
ANISOU 3671  C   TYR A 397    11709  10347  11622     27    343   1670       C  
ATOM   3672  O   TYR A 397      -1.838   9.216  17.534  1.00 91.01           O  
ANISOU 3672  O   TYR A 397    11965  10851  11762     49    340   1751       O  
ATOM   3673  CB  TYR A 397      -2.515  11.238  15.062  1.00 87.69           C  
ANISOU 3673  CB  TYR A 397    11461  10323  11535    166    555   1297       C  
ATOM   3674  CG  TYR A 397      -2.305  12.085  13.822  1.00 85.34           C  
ANISOU 3674  CG  TYR A 397    11169   9892  11363    247    613   1075       C  
ATOM   3675  CD1 TYR A 397      -1.044  12.539  13.457  1.00 82.35           C  
ANISOU 3675  CD1 TYR A 397    10836   9379  11075    370    596    895       C  
ATOM   3676  CD2 TYR A 397      -3.387  12.464  13.036  1.00 84.40           C  
ANISOU 3676  CD2 TYR A 397    10998   9811  11260    192    681   1060       C  
ATOM   3677  CE1 TYR A 397      -0.865  13.322  12.329  1.00 79.48           C  
ANISOU 3677  CE1 TYR A 397    10472   8917  10811    419    647    722       C  
ATOM   3678  CE2 TYR A 397      -3.217  13.245  11.910  1.00 81.26           C  
ANISOU 3678  CE2 TYR A 397    10610   9299  10965    258    726    880       C  
ATOM   3679  CZ  TYR A 397      -1.956  13.671  11.560  1.00 78.82           C  
ANISOU 3679  CZ  TYR A 397    10353   8855  10740    364    709    719       C  
ATOM   3680  OH  TYR A 397      -1.788  14.450  10.437  1.00 76.09           O  
ANISOU 3680  OH  TYR A 397    10013   8415  10483    406    751    568       O  
ATOM   3681  N   ALA A 398      -2.744   8.148  15.769  1.00 88.91           N  
ANISOU 3681  N   ALA A 398    11805  10236  11739   -138    270   1838       N  
ATOM   3682  CA  ALA A 398      -3.386   7.142  16.609  1.00 90.19           C  
ANISOU 3682  CA  ALA A 398    11979  10480  11809   -326    186   2150       C  
ATOM   3683  C   ALA A 398      -2.359   6.321  17.379  1.00 90.61           C  
ANISOU 3683  C   ALA A 398    12150  10407  11871   -286     39   2260       C  
ATOM   3684  O   ALA A 398      -2.561   6.006  18.558  1.00 93.50           O  
ANISOU 3684  O   ALA A 398    12480  10972  12073   -366     11   2474       O  
ATOM   3685  CB  ALA A 398      -4.269   6.233  15.754  1.00 88.91           C  
ANISOU 3685  CB  ALA A 398    11882  10134  11766   -526    107   2295       C  
ATOM   3686  N   LEU A 399      -1.249   5.965  16.732  1.00 88.89           N  
ANISOU 3686  N   LEU A 399    12062   9879  11831   -153    -58   2119       N  
ATOM   3687  CA  LEU A 399      -0.233   5.160  17.401  1.00 89.91           C  
ANISOU 3687  CA  LEU A 399    12304   9874  11983    -85   -215   2211       C  
ATOM   3688  C   LEU A 399       0.700   6.011  18.254  1.00 91.58           C  
ANISOU 3688  C   LEU A 399    12431  10290  12075     90   -154   2080       C  
ATOM   3689  O   LEU A 399       1.088   5.598  19.353  1.00 93.21           O  
ANISOU 3689  O   LEU A 399    12656  10583  12174     93   -238   2235       O  
ATOM   3690  CB  LEU A 399       0.582   4.374  16.372  1.00 87.23           C  
ANISOU 3690  CB  LEU A 399    12129   9141  11875     13   -356   2102       C  
ATOM   3691  CG  LEU A 399      -0.198   3.471  15.422  1.00 85.69           C  
ANISOU 3691  CG  LEU A 399    12053   8686  11821   -139   -452   2190       C  
ATOM   3692  CD1 LEU A 399       0.638   3.147  14.193  1.00 82.63           C  
ANISOU 3692  CD1 LEU A 399    11781   7984  11633     28   -527   1959       C  
ATOM   3693  CD2 LEU A 399      -0.619   2.205  16.140  1.00 86.08           C  
ANISOU 3693  CD2 LEU A 399    12225   8620  11861   -325   -639   2523       C  
ATOM   3694  N   ARG A 400       1.067   7.196  17.774  1.00 90.18           N  
ANISOU 3694  N   ARG A 400    12165  10189  11909    224    -24   1807       N  
ATOM   3695  CA  ARG A 400       2.140   7.980  18.371  1.00 91.16           C  
ANISOU 3695  CA  ARG A 400    12231  10439  11967    391      1   1645       C  
ATOM   3696  C   ARG A 400       1.659   8.990  19.407  1.00 94.14           C  
ANISOU 3696  C   ARG A 400    12476  11175  12117    388    117   1632       C  
ATOM   3697  O   ARG A 400       2.461   9.812  19.862  1.00 95.74           O  
ANISOU 3697  O   ARG A 400    12628  11490  12260    517    141   1467       O  
ATOM   3698  CB  ARG A 400       2.927   8.708  17.279  1.00 88.48           C  
ANISOU 3698  CB  ARG A 400    11875   9971  11771    526     54   1361       C  
ATOM   3699  CG  ARG A 400       3.504   7.800  16.204  1.00 85.61           C  
ANISOU 3699  CG  ARG A 400    11624   9292  11611    574    -50   1322       C  
ATOM   3700  CD  ARG A 400       4.769   7.128  16.694  1.00 87.08           C  
ANISOU 3700  CD  ARG A 400    11866   9386  11833    706   -193   1337       C  
ATOM   3701  NE  ARG A 400       5.659   8.081  17.344  1.00 88.19           N  
ANISOU 3701  NE  ARG A 400    11898   9724  11884    817   -147   1202       N  
ATOM   3702  CZ  ARG A 400       6.453   7.787  18.364  1.00 90.23           C  
ANISOU 3702  CZ  ARG A 400    12157  10055  12070    893   -246   1268       C  
ATOM   3703  NH1 ARG A 400       6.508   6.565  18.865  1.00 91.11           N  
ANISOU 3703  NH1 ARG A 400    12377  10048  12192    881   -400   1476       N  
ATOM   3704  NH2 ARG A 400       7.205   8.745  18.899  1.00 91.12           N  
ANISOU 3704  NH2 ARG A 400    12165  10355  12100    976   -205   1128       N  
ATOM   3705  N   SER A 401       0.385   8.953  19.796  1.00 93.76           N  
ANISOU 3705  N   SER A 401    12367  11325  11934    250    182   1793       N  
ATOM   3706  CA  SER A 401      -0.150   9.927  20.749  1.00 96.42           C  
ANISOU 3706  CA  SER A 401    12568  12033  12035    277    298   1755       C  
ATOM   3707  C   SER A 401      -1.028   9.196  21.761  1.00 98.07           C  
ANISOU 3707  C   SER A 401    12735  12479  12050    121    279   2063       C  
ATOM   3708  O   SER A 401      -2.184   8.872  21.473  1.00 97.58           O  
ANISOU 3708  O   SER A 401    12628  12481  11967    -34    322   2213       O  
ATOM   3709  CB  SER A 401      -0.926  11.027  20.037  1.00 96.51           C  
ANISOU 3709  CB  SER A 401    12492  12124  12055    306    442   1568       C  
ATOM   3710  OG  SER A 401      -1.003  12.195  20.838  1.00 98.72           O  
ANISOU 3710  OG  SER A 401    12671  12690  12148    421    529   1418       O  
ATOM   3711  N   LYS A 402      -0.469   8.943  22.946  1.00100.31           N  
ANISOU 3711  N   LYS A 402    13022  12910  12179    151    212   2169       N  
ATOM   3712  CA  LYS A 402      -1.250   8.412  24.056  1.00101.49           C  
ANISOU 3712  CA  LYS A 402    13108  13362  12091      8    208   2463       C  
ATOM   3713  C   LYS A 402      -2.385   9.349  24.449  1.00103.14           C  
ANISOU 3713  C   LYS A 402    13135  13980  12075      8    383   2407       C  
ATOM   3714  O   LYS A 402      -3.395   8.893  24.996  1.00103.23           O  
ANISOU 3714  O   LYS A 402    13056  14256  11912   -155    415   2663       O  
ATOM   3715  CB  LYS A 402      -0.320   8.152  25.248  1.00103.07           C  
ANISOU 3715  CB  LYS A 402    13340  13669  12151     77    107   2543       C  
ATOM   3716  CG  LYS A 402      -1.003   7.781  26.556  1.00104.52           C  
ANISOU 3716  CG  LYS A 402    13440  14242  12033    -48    115   2831       C  
ATOM   3717  CD  LYS A 402      -0.043   7.927  27.731  1.00106.52           C  
ANISOU 3717  CD  LYS A 402    13698  14662  12112     75     46   2816       C  
ATOM   3718  CE  LYS A 402       0.922   6.753  27.820  1.00106.47           C  
ANISOU 3718  CE  LYS A 402    13858  14349  12247     51   -165   3004       C  
ATOM   3719  NZ  LYS A 402       0.386   5.653  28.668  1.00107.30           N  
ANISOU 3719  NZ  LYS A 402    13987  14586  12195   -155   -260   3428       N  
ATOM   3720  N   ASP A 403      -2.252  10.645  24.159  1.00104.48           N  
ANISOU 3720  N   ASP A 403    13246  14206  12245    186    488   2082       N  
ATOM   3721  CA  ASP A 403      -3.290  11.602  24.529  1.00104.53           C  
ANISOU 3721  CA  ASP A 403    13087  14589  12039    237    640   1988       C  
ATOM   3722  C   ASP A 403      -4.517  11.465  23.632  1.00103.75           C  
ANISOU 3722  C   ASP A 403    12921  14483  12016    112    717   2064       C  
ATOM   3723  O   ASP A 403      -5.652  11.455  24.122  1.00103.67           O  
ANISOU 3723  O   ASP A 403    12758  14832  11801     32    803   2206       O  
ATOM   3724  CB  ASP A 403      -2.732  13.022  24.474  1.00106.43           C  
ANISOU 3724  CB  ASP A 403    13319  14839  12281    469    692   1614       C  
ATOM   3725  CG  ASP A 403      -1.994  13.408  25.741  1.00107.71           C  
ANISOU 3725  CG  ASP A 403    13471  15220  12236    591    655   1539       C  
ATOM   3726  OD1 ASP A 403      -2.367  12.910  26.826  1.00107.17           O  
ANISOU 3726  OD1 ASP A 403    13334  15468  11920    526    655   1751       O  
ATOM   3727  OD2 ASP A 403      -1.034  14.202  25.653  1.00108.44           O  
ANISOU 3727  OD2 ASP A 403    13621  15177  12405    737    618   1279       O  
ATOM   3728  N   LEU A 404      -4.311  11.371  22.311  1.00100.66           N  
ANISOU 3728  N   LEU A 404    12627  13716  11904     97    687   1969       N  
ATOM   3729  CA  LEU A 404      -5.428  11.085  21.410  1.00 99.60           C  
ANISOU 3729  CA  LEU A 404    12443  13546  11855    -45    731   2064       C  
ATOM   3730  C   LEU A 404      -6.157   9.821  21.828  1.00 99.44           C  
ANISOU 3730  C   LEU A 404    12397  13628  11757   -300    672   2441       C  
ATOM   3731  O   LEU A 404      -7.392   9.775  21.830  1.00 98.92           O  
ANISOU 3731  O   LEU A 404    12186  13818  11582   -425    749   2576       O  
ATOM   3732  CB  LEU A 404      -4.946  10.926  19.966  1.00 97.90           C  
ANISOU 3732  CB  LEU A 404    12364  12890  11945    -42    675   1940       C  
ATOM   3733  CG  LEU A 404      -4.870  12.121  19.017  1.00 97.38           C  
ANISOU 3733  CG  LEU A 404    12286  12723  11990    114    756   1633       C  
ATOM   3734  CD1 LEU A 404      -6.225  12.805  18.870  1.00 97.64           C  
ANISOU 3734  CD1 LEU A 404    12161  13027  11911    114    880   1607       C  
ATOM   3735  CD2 LEU A 404      -3.812  13.083  19.453  1.00 97.90           C  
ANISOU 3735  CD2 LEU A 404    12380  12789  12027    314    761   1391       C  
ATOM   3736  N   ARG A 405      -5.399   8.782  22.180  1.00 98.70           N  
ANISOU 3736  N   ARG A 405    12443  13338  11723   -384    525   2625       N  
ATOM   3737  CA  ARG A 405      -5.992   7.489  22.489  1.00 97.39           C  
ANISOU 3737  CA  ARG A 405    12297  13184  11524   -654    426   3006       C  
ATOM   3738  C   ARG A 405      -6.924   7.591  23.687  1.00 99.27           C  
ANISOU 3738  C   ARG A 405    12336  13952  11430   -751    519   3216       C  
ATOM   3739  O   ARG A 405      -8.082   7.164  23.623  1.00 99.10           O  
ANISOU 3739  O   ARG A 405    12200  14114  11337   -967    548   3444       O  
ATOM   3740  CB  ARG A 405      -4.884   6.466  22.741  1.00 97.54           C  
ANISOU 3740  CB  ARG A 405    12517  12884  11660   -676    233   3138       C  
ATOM   3741  CG  ARG A 405      -4.856   5.325  21.740  1.00 95.88           C  
ANISOU 3741  CG  ARG A 405    12484  12226  11719   -827     72   3261       C  
ATOM   3742  CD  ARG A 405      -3.585   4.504  21.855  1.00 95.46           C  
ANISOU 3742  CD  ARG A 405    12638  11822  11809   -755   -120   3295       C  
ATOM   3743  NE  ARG A 405      -2.393   5.242  21.456  1.00 94.51           N  
ANISOU 3743  NE  ARG A 405    12559  11553  11796   -479    -92   2952       N  
ATOM   3744  CZ  ARG A 405      -1.302   5.355  22.201  1.00 95.20           C  
ANISOU 3744  CZ  ARG A 405    12680  11663  11827   -324   -145   2896       C  
ATOM   3745  NH1 ARG A 405      -1.225   4.805  23.403  1.00 96.58           N  
ANISOU 3745  NH1 ARG A 405    12862  12003  11832   -397   -226   3151       N  
ATOM   3746  NH2 ARG A 405      -0.259   6.031  21.727  1.00 95.14           N  
ANISOU 3746  NH2 ARG A 405    12692  11525  11930   -103   -121   2590       N  
ATOM   3747  N   HIS A 406      -6.441   8.174  24.787  1.00102.69           N  
ANISOU 3747  N   HIS A 406    12711  14665  11642   -595    566   3136       N  
ATOM   3748  CA  HIS A 406      -7.260   8.281  25.990  1.00103.81           C  
ANISOU 3748  CA  HIS A 406    12655  15359  11430   -662    658   3322       C  
ATOM   3749  C   HIS A 406      -8.473   9.178  25.773  1.00103.92           C  
ANISOU 3749  C   HIS A 406    12444  15731  11309   -613    842   3198       C  
ATOM   3750  O   HIS A 406      -9.531   8.940  26.367  1.00104.67           O  
ANISOU 3750  O   HIS A 406    12349  16257  11166   -764    915   3434       O  
ATOM   3751  CB  HIS A 406      -6.418   8.799  27.156  1.00105.06           C  
ANISOU 3751  CB  HIS A 406    12809  15731  11377   -470    663   3210       C  
ATOM   3752  CG  HIS A 406      -5.304   7.880  27.552  1.00106.02           C  
ANISOU 3752  CG  HIS A 406    13119  15583  11583   -517    479   3372       C  
ATOM   3753  ND1 HIS A 406      -4.504   8.111  28.650  1.00107.88           N  
ANISOU 3753  ND1 HIS A 406    13363  15997  11629   -386    446   3336       N  
ATOM   3754  CD2 HIS A 406      -4.856   6.730  26.995  1.00105.06           C  
ANISOU 3754  CD2 HIS A 406    13185  15023  11711   -663    305   3561       C  
ATOM   3755  CE1 HIS A 406      -3.613   7.141  28.754  1.00107.58           C  
ANISOU 3755  CE1 HIS A 406    13502  15652  11723   -449    263   3509       C  
ATOM   3756  NE2 HIS A 406      -3.804   6.291  27.761  1.00105.89           N  
ANISOU 3756  NE2 HIS A 406    13403  15052  11777   -607    172   3641       N  
ATOM   3757  N   ALA A 407      -8.344  10.206  24.933  1.00102.29           N  
ANISOU 3757  N   ALA A 407    12249  15369  11246   -404    913   2841       N  
ATOM   3758  CA  ALA A 407      -9.485  11.067  24.645  1.00102.56           C  
ANISOU 3758  CA  ALA A 407    12085  15707  11177   -329   1067   2710       C  
ATOM   3759  C   ALA A 407     -10.542  10.319  23.842  1.00101.33           C  
ANISOU 3759  C   ALA A 407    11864  15510  11125   -588   1060   2945       C  
ATOM   3760  O   ALA A 407     -11.725  10.320  24.201  1.00101.55           O  
ANISOU 3760  O   ALA A 407    11666  15975  10944   -687   1157   3099       O  
ATOM   3761  CB  ALA A 407      -9.024  12.320  23.901  1.00102.38           C  
ANISOU 3761  CB  ALA A 407    12124  15472  11305    -55   1113   2291       C  
ATOM   3762  N   PHE A 408     -10.129   9.667  22.752  1.00103.18           N  
ANISOU 3762  N   PHE A 408    12286  15243  11675   -699    941   2969       N  
ATOM   3763  CA  PHE A 408     -11.066   8.868  21.970  1.00102.24           C  
ANISOU 3763  CA  PHE A 408    12134  15043  11670   -965    900   3192       C  
ATOM   3764  C   PHE A 408     -11.628   7.719  22.797  1.00102.54           C  
ANISOU 3764  C   PHE A 408    12104  15306  11550  -1275    834   3628       C  
ATOM   3765  O   PHE A 408     -12.819   7.398  22.699  1.00102.31           O  
ANISOU 3765  O   PHE A 408    11903  15534  11436  -1489    872   3841       O  
ATOM   3766  CB  PHE A 408     -10.375   8.342  20.708  1.00100.57           C  
ANISOU 3766  CB  PHE A 408    12164  14236  11812  -1002    764   3113       C  
ATOM   3767  CG  PHE A 408     -11.209   7.377  19.903  1.00 99.61           C  
ANISOU 3767  CG  PHE A 408    12056  13965  11828  -1292    677   3343       C  
ATOM   3768  CD1 PHE A 408     -11.189   6.017  20.179  1.00 98.67           C  
ANISOU 3768  CD1 PHE A 408    12047  13690  11753  -1569    511   3684       C  
ATOM   3769  CD2 PHE A 408     -11.998   7.828  18.857  1.00 99.14           C  
ANISOU 3769  CD2 PHE A 408    11911  13899  11860  -1290    742   3219       C  
ATOM   3770  CE1 PHE A 408     -11.948   5.132  19.440  1.00 97.76           C  
ANISOU 3770  CE1 PHE A 408    11960  13412  11772  -1850    406   3888       C  
ATOM   3771  CE2 PHE A 408     -12.759   6.945  18.112  1.00 98.19           C  
ANISOU 3771  CE2 PHE A 408    11804  13642  11863  -1565    648   3421       C  
ATOM   3772  CZ  PHE A 408     -12.733   5.595  18.405  1.00 97.66           C  
ANISOU 3772  CZ  PHE A 408    11851  13413  11842  -1851    476   3751       C  
ATOM   3773  N   ARG A 409     -10.786   7.092  23.622  1.00106.45           N  
ANISOU 3773  N   ARG A 409    12729  15719  11999  -1312    727   3780       N  
ATOM   3774  CA  ARG A 409     -11.239   5.940  24.395  1.00106.25           C  
ANISOU 3774  CA  ARG A 409    12671  15861  11837  -1629    636   4228       C  
ATOM   3775  C   ARG A 409     -12.335   6.336  25.376  1.00107.62           C  
ANISOU 3775  C   ARG A 409    12530  16728  11633  -1686    800   4379       C  
ATOM   3776  O   ARG A 409     -13.300   5.588  25.576  1.00107.62           O  
ANISOU 3776  O   ARG A 409    12400  16959  11530  -2001    780   4739       O  
ATOM   3777  CB  ARG A 409     -10.055   5.296  25.123  1.00106.75           C  
ANISOU 3777  CB  ARG A 409    12938  15709  11913  -1614    484   4341       C  
ATOM   3778  CG  ARG A 409     -10.437   4.243  26.144  1.00108.47           C  
ANISOU 3778  CG  ARG A 409    13120  16155  11938  -1915    391   4813       C  
ATOM   3779  CD  ARG A 409     -10.445   2.881  25.469  1.00107.83           C  
ANISOU 3779  CD  ARG A 409    13252  15588  12129  -2209    161   5090       C  
ATOM   3780  NE  ARG A 409     -10.623   1.763  26.388  1.00108.93           N  
ANISOU 3780  NE  ARG A 409    13425  15826  12136  -2513     16   5565       N  
ATOM   3781  CZ  ARG A 409     -11.707   1.536  27.118  1.00109.67           C  
ANISOU 3781  CZ  ARG A 409    13290  16426  11953  -2779     84   5907       C  
ATOM   3782  NH1 ARG A 409     -12.742   2.361  27.102  1.00109.43           N  
ANISOU 3782  NH1 ARG A 409    12958  16892  11728  -2754    305   5815       N  
ATOM   3783  NH2 ARG A 409     -11.760   0.446  27.877  1.00110.15           N  
ANISOU 3783  NH2 ARG A 409    13420  16507  11926  -3077    -80   6362       N  
ATOM   3784  N   SER A 410     -12.215   7.518  25.984  1.00103.09           N  
ANISOU 3784  N   SER A 410    11823  16504  10843  -1385    958   4101       N  
ATOM   3785  CA  SER A 410     -13.230   7.964  26.932  1.00103.59           C  
ANISOU 3785  CA  SER A 410    11575  17266  10520  -1384   1124   4197       C  
ATOM   3786  C   SER A 410     -14.509   8.405  26.233  1.00103.31           C  
ANISOU 3786  C   SER A 410    11311  17470  10471  -1412   1249   4146       C  
ATOM   3787  O   SER A 410     -15.590   8.341  26.829  1.00103.80           O  
ANISOU 3787  O   SER A 410    11091  18100  10249  -1540   1353   4358       O  
ATOM   3788  CB  SER A 410     -12.676   9.095  27.795  1.00104.34           C  
ANISOU 3788  CB  SER A 410    11619  17636  10388  -1026   1231   3882       C  
ATOM   3789  OG  SER A 410     -12.955  10.361  27.223  1.00103.83           O  
ANISOU 3789  OG  SER A 410    11473  17619  10358   -735   1357   3481       O  
ATOM   3790  N   MET A 411     -14.412   8.857  24.980  1.00104.73           N  
ANISOU 3790  N   MET A 411    11592  17258  10941  -1294   1239   3875       N  
ATOM   3791  CA  MET A 411     -15.609   9.254  24.246  1.00104.52           C  
ANISOU 3791  CA  MET A 411    11359  17434  10920  -1316   1338   3828       C  
ATOM   3792  C   MET A 411     -16.413   8.045  23.785  1.00104.37           C  
ANISOU 3792  C   MET A 411    11299  17363  10993  -1738   1241   4222       C  
ATOM   3793  O   MET A 411     -17.645   8.117  23.702  1.00104.45           O  
ANISOU 3793  O   MET A 411    11038  17782  10867  -1856   1332   4344       O  
ATOM   3794  CB  MET A 411     -15.225  10.124  23.048  1.00103.79           C  
ANISOU 3794  CB  MET A 411    11399  16936  11100  -1064   1346   3430       C  
ATOM   3795  CG  MET A 411     -14.631  11.470  23.425  1.00104.08           C  
ANISOU 3795  CG  MET A 411    11447  17053  11044   -659   1441   3030       C  
ATOM   3796  SD  MET A 411     -13.983  12.382  22.010  1.00104.12           S  
ANISOU 3796  SD  MET A 411    11655  16511  11394   -415   1412   2617       S  
ATOM   3797  CE  MET A 411     -13.396  13.871  22.812  1.00103.88           C  
ANISOU 3797  CE  MET A 411    11615  16668  11187      2   1500   2225       C  
ATOM   3798  N   PHE A 412     -15.742   6.932  23.485  1.00105.74           N  
ANISOU 3798  N   PHE A 412    11737  17042  11397  -1963   1045   4418       N  
ATOM   3799  CA  PHE A 412     -16.387   5.716  22.990  1.00104.89           C  
ANISOU 3799  CA  PHE A 412    11653  16781  11420  -2377    903   4781       C  
ATOM   3800  C   PHE A 412     -16.041   4.559  23.917  1.00105.64           C  
ANISOU 3800  C   PHE A 412    11851  16853  11433  -2652    757   5182       C  
ATOM   3801  O   PHE A 412     -15.076   3.819  23.669  1.00106.21           O  
ANISOU 3801  O   PHE A 412    12233  16383  11740  -2699    567   5220       O  
ATOM   3802  CB  PHE A 412     -15.956   5.415  21.555  1.00102.98           C  
ANISOU 3802  CB  PHE A 412    11669  15887  11571  -2386    764   4620       C  
ATOM   3803  CG  PHE A 412     -16.303   6.501  20.577  1.00102.89           C  
ANISOU 3803  CG  PHE A 412    11571  15875  11648  -2143    888   4259       C  
ATOM   3804  CD1 PHE A 412     -17.536   6.514  19.943  1.00103.03           C  
ANISOU 3804  CD1 PHE A 412    11388  16099  11661  -2299    929   4338       C  
ATOM   3805  CD2 PHE A 412     -15.398   7.510  20.292  1.00103.39           C  
ANISOU 3805  CD2 PHE A 412    11751  15735  11796  -1770    951   3856       C  
ATOM   3806  CE1 PHE A 412     -17.857   7.513  19.043  1.00103.13           C  
ANISOU 3806  CE1 PHE A 412    11327  16106  11752  -2067   1029   4019       C  
ATOM   3807  CE2 PHE A 412     -15.714   8.513  19.393  1.00102.94           C  
ANISOU 3807  CE2 PHE A 412    11630  15661  11821  -1558   1047   3549       C  
ATOM   3808  CZ  PHE A 412     -16.945   8.514  18.767  1.00102.83           C  
ANISOU 3808  CZ  PHE A 412    11424  15845  11800  -1696   1086   3629       C  
ATOM   3809  N   PRO A 413     -16.801   4.363  25.006  1.00108.97           N  
ANISOU 3809  N   PRO A 413    12018  17869  11517  -2833    835   5497       N  
ATOM   3810  CA  PRO A 413     -16.584   3.241  25.926  1.00109.62           C  
ANISOU 3810  CA  PRO A 413    12190  17941  11521  -3104    676   5879       C  
ATOM   3811  C   PRO A 413     -16.865   1.896  25.264  1.00108.85           C  
ANISOU 3811  C   PRO A 413    12275  17359  11723  -3454    412   6094       C  
ATOM   3812  O   PRO A 413     -16.326   0.885  25.712  1.00108.88           O  
ANISOU 3812  O   PRO A 413    12489  17073  11808  -3607    208   6298       O  
ATOM   3813  CB  PRO A 413     -17.583   3.507  27.060  1.00110.99           C  
ANISOU 3813  CB  PRO A 413    12009  18836  11328  -3119    806   5958       C  
ATOM   3814  CG  PRO A 413     -18.590   4.439  26.489  1.00110.60           C  
ANISOU 3814  CG  PRO A 413    11681  19136  11206  -2990    993   5748       C  
ATOM   3815  CD  PRO A 413     -17.880   5.256  25.460  1.00109.71           C  
ANISOU 3815  CD  PRO A 413    11722  18677  11286  -2730   1070   5440       C  
TER    3816      PRO A 413                                                      
HETATM 3817  C1  CLR A1201       5.589  35.542  14.796  1.00 86.32           C  
ANISOU 3817  C1  CLR A1201    12403   8291  12101    839   -772  -1880       C  
HETATM 3818  C2  CLR A1201       5.290  36.312  16.084  1.00 87.56           C  
ANISOU 3818  C2  CLR A1201    12692   8430  12147   1047   -926  -2158       C  
HETATM 3819  C3  CLR A1201       4.912  37.747  15.808  1.00 87.77           C  
ANISOU 3819  C3  CLR A1201    12949   8114  12287   1101  -1136  -2300       C  
HETATM 3820  C4  CLR A1201       3.735  37.792  14.854  1.00 85.28           C  
ANISOU 3820  C4  CLR A1201    12649   7733  12019   1216  -1038  -2217       C  
HETATM 3821  C5  CLR A1201       4.027  37.032  13.580  1.00 83.98           C  
ANISOU 3821  C5  CLR A1201    12352   7601  11956    989   -881  -1928       C  
HETATM 3822  C6  CLR A1201       3.960  37.626  12.399  1.00 82.63           C  
ANISOU 3822  C6  CLR A1201    12265   7187  11942    862   -940  -1809       C  
HETATM 3823  C7  CLR A1201       4.048  36.928  11.080  1.00 81.09           C  
ANISOU 3823  C7  CLR A1201    11947   7045  11819    684   -781  -1547       C  
HETATM 3824  C8  CLR A1201       4.082  35.410  11.217  1.00 81.96           C  
ANISOU 3824  C8  CLR A1201    11836   7489  11815    696   -544  -1444       C  
HETATM 3825  C9  CLR A1201       4.955  34.998  12.415  1.00 83.24           C  
ANISOU 3825  C9  CLR A1201    11932   7813  11884    682   -566  -1535       C  
HETATM 3826  C10 CLR A1201       4.441  35.578  13.762  1.00 83.71           C  
ANISOU 3826  C10 CLR A1201    12095   7886  11825    922   -674  -1790       C  
HETATM 3827  C11 CLR A1201       5.146  33.475  12.472  1.00 83.81           C  
ANISOU 3827  C11 CLR A1201    11801   8177  11868    666   -361  -1404       C  
HETATM 3828  C12 CLR A1201       5.637  32.872  11.151  1.00 82.79           C  
ANISOU 3828  C12 CLR A1201    11569   8052  11835    468   -256  -1187       C  
HETATM 3829  C13 CLR A1201       4.720  33.241   9.981  1.00 81.27           C  
ANISOU 3829  C13 CLR A1201    11439   7723  11717    480   -223  -1106       C  
HETATM 3830  C14 CLR A1201       4.651  34.779   9.955  1.00 81.16           C  
ANISOU 3830  C14 CLR A1201    11620   7421  11795    467   -433  -1208       C  
HETATM 3831  C15 CLR A1201       4.002  35.093   8.613  1.00 78.43           C  
ANISOU 3831  C15 CLR A1201    11321   6941  11538    426   -408  -1078       C  
HETATM 3832  C16 CLR A1201       4.653  34.070   7.666  1.00 78.61           C  
ANISOU 3832  C16 CLR A1201    11176   7119  11573    241   -253   -878       C  
HETATM 3833  C17 CLR A1201       5.260  32.947   8.550  1.00 80.27           C  
ANISOU 3833  C17 CLR A1201    11240   7574  11685    267   -155   -907       C  
HETATM 3834  C18 CLR A1201       3.330  32.609  10.152  1.00 78.86           C  
ANISOU 3834  C18 CLR A1201    11096   7556  11312    702    -90  -1122       C  
HETATM 3835  C19 CLR A1201       3.230  34.797  14.302  1.00 82.97           C  
ANISOU 3835  C19 CLR A1201    11908   8056  11560   1179   -506  -1826       C  
HETATM 3836  C20 CLR A1201       5.058  31.552   7.932  1.00 78.67           C  
ANISOU 3836  C20 CLR A1201    10884   7570  11436    275     43   -776       C  
HETATM 3837  C21 CLR A1201       5.982  30.489   8.520  1.00 80.13           C  
ANISOU 3837  C21 CLR A1201    10931   7952  11562    245    108   -762       C  
HETATM 3838  C22 CLR A1201       5.211  31.610   6.406  1.00 77.41           C  
ANISOU 3838  C22 CLR A1201    10702   7353  11356    117     85   -618       C  
HETATM 3839  C23 CLR A1201       4.586  30.461   5.659  1.00 75.80           C  
ANISOU 3839  C23 CLR A1201    10405   7284  11110    170    252   -523       C  
HETATM 3840  C24 CLR A1201       4.958  30.436   4.201  1.00 75.56           C  
ANISOU 3840  C24 CLR A1201    10334   7246  11131      9    295   -379       C  
HETATM 3841  C25 CLR A1201       4.062  29.586   3.307  1.00 73.58           C  
ANISOU 3841  C25 CLR A1201    10040   7071  10847     71    423   -304       C  
HETATM 3842  C26 CLR A1201       4.638  29.464   1.907  1.00 74.56           C  
ANISOU 3842  C26 CLR A1201    10103   7236  10990    -88    470   -175       C  
HETATM 3843  C27 CLR A1201       3.822  28.211   3.904  1.00 72.63           C  
ANISOU 3843  C27 CLR A1201     9832   7111  10654    188    529   -333       C  
HETATM 3844  O1  CLR A1201       4.571  38.404  17.035  1.00 89.94           O  
ANISOU 3844  O1  CLR A1201    13346   8390  12437   1339  -1278  -2591       O  
HETATM 3845  C1  CLR A1202     -12.703  26.305  12.384  1.00 96.27           C  
ANISOU 3845  C1  CLR A1202    11695  12846  12036   2053   1165   -543       C  
HETATM 3846  C2  CLR A1202     -11.933  26.951  13.539  1.00 95.86           C  
ANISOU 3846  C2  CLR A1202    11735  12795  11894   2205   1121   -733       C  
HETATM 3847  C3  CLR A1202     -11.516  25.933  14.572  1.00 97.08           C  
ANISOU 3847  C3  CLR A1202    11820  13155  11910   2072   1183   -613       C  
HETATM 3848  C4  CLR A1202     -10.693  24.843  13.913  1.00 96.59           C  
ANISOU 3848  C4  CLR A1202    11835  12858  12008   1776   1179   -414       C  
HETATM 3849  C5  CLR A1202     -11.431  24.205  12.756  1.00 97.61           C  
ANISOU 3849  C5  CLR A1202    11895  12955  12236   1626   1213   -241       C  
HETATM 3850  C6  CLR A1202     -11.634  22.897  12.710  1.00 99.14           C  
ANISOU 3850  C6  CLR A1202    12007  13248  12414   1406   1260    -13       C  
HETATM 3851  C7  CLR A1202     -12.154  22.149  11.523  1.00 99.77           C  
ANISOU 3851  C7  CLR A1202    12056  13238  12613   1221   1265    152       C  
HETATM 3852  C8  CLR A1202     -12.348  23.040  10.299  1.00 98.14           C  
ANISOU 3852  C8  CLR A1202    11920  12818  12550   1306   1222     44       C  
HETATM 3853  C9  CLR A1202     -12.906  24.408  10.730  1.00 97.80           C  
ANISOU 3853  C9  CLR A1202    11839  12904  12416   1599   1214   -158       C  
HETATM 3854  C10 CLR A1202     -11.937  25.161  11.683  1.00 96.32           C  
ANISOU 3854  C10 CLR A1202    11771  12637  12189   1743   1170   -343       C  
HETATM 3855  C11 CLR A1202     -13.320  25.262   9.522  1.00 95.85           C  
ANISOU 3855  C11 CLR A1202    11644  12476  12297   1688   1160   -231       C  
HETATM 3856  C12 CLR A1202     -14.256  24.527   8.558  1.00 97.29           C  
ANISOU 3856  C12 CLR A1202    11710  12742  12515   1542   1189    -57       C  
HETATM 3857  C13 CLR A1202     -13.629  23.224   8.056  1.00 97.95           C  
ANISOU 3857  C13 CLR A1202    11852  12671  12694   1248   1192    118       C  
HETATM 3858  C14 CLR A1202     -13.304  22.387   9.309  1.00 99.33           C  
ANISOU 3858  C14 CLR A1202    11974  13020  12748   1167   1238    199       C  
HETATM 3859  C15 CLR A1202     -12.969  21.003   8.762  1.00 99.23           C  
ANISOU 3859  C15 CLR A1202    12002  12875  12827    890   1223    388       C  
HETATM 3860  C16 CLR A1202     -13.905  20.847   7.549  1.00 99.93           C  
ANISOU 3860  C16 CLR A1202    12028  12958  12982    815   1210    461       C  
HETATM 3861  C17 CLR A1202     -14.568  22.230   7.309  1.00 99.87           C  
ANISOU 3861  C17 CLR A1202    11972  13025  12948   1060   1210    307       C  
HETATM 3862  C18 CLR A1202     -12.379  23.516   7.209  1.00 94.71           C  
ANISOU 3862  C18 CLR A1202    11657  11865  12462   1192   1127     54       C  
HETATM 3863  C19 CLR A1202     -10.721  25.733  10.931  1.00 92.81           C  
ANISOU 3863  C19 CLR A1202    11549  11769  11946   1701   1077   -432       C  
HETATM 3864  C20 CLR A1202     -14.941  22.453   5.831  1.00 99.09           C  
ANISOU 3864  C20 CLR A1202    11911  12765  12973   1026   1163    317       C  
HETATM 3865  C21 CLR A1202     -15.918  23.608   5.629  1.00 99.14           C  
ANISOU 3865  C21 CLR A1202    11826  12909  12935   1258   1153    216       C  
HETATM 3866  C22 CLR A1202     -15.522  21.160   5.238  1.00100.75           C  
ANISOU 3866  C22 CLR A1202    12041  13037  13202    776   1161    510       C  
HETATM 3867  C23 CLR A1202     -16.249  21.319   3.923  1.00100.78           C  
ANISOU 3867  C23 CLR A1202    12018  13000  13275    749   1120    534       C  
HETATM 3868  C24 CLR A1202     -15.387  21.036   2.718  1.00 98.51           C  
ANISOU 3868  C24 CLR A1202    11917  12374  13137    628   1062    527       C  
HETATM 3869  C25 CLR A1202     -15.992  21.425   1.370  1.00 98.23           C  
ANISOU 3869  C25 CLR A1202    11879  12286  13159    636   1013    526       C  
HETATM 3870  C26 CLR A1202     -15.142  20.923   0.214  1.00 96.25           C  
ANISOU 3870  C26 CLR A1202    11795  11754  13023    490    966    532       C  
HETATM 3871  C27 CLR A1202     -16.186  22.929   1.268  1.00 96.41           C  
ANISOU 3871  C27 CLR A1202    11663  12045  12925    886    998    397       C  
HETATM 3872  O1  CLR A1202     -10.749  26.577  15.597  1.00 96.33           O  
ANISOU 3872  O1  CLR A1202    11819  13050  11731   2213   1127   -803       O  
HETATM 3873  CAA 9GF A1203      -0.524  22.959  -9.727  1.00 71.88           C  
ANISOU 3873  CAA 9GF A1203     9552   7668  10091    -66   1045    209       C  
HETATM 3874  CAB 9GF A1203       0.240  22.469  -8.497  1.00 71.15           C  
ANISOU 3874  CAB 9GF A1203     9431   7542  10060    -14   1060    130       C  
HETATM 3875  CAC 9GF A1203       0.295  20.944  -8.418  1.00 70.66           C  
ANISOU 3875  CAC 9GF A1203     9358   7507   9982     71   1076     21       C  
HETATM 3876  CAD 9GF A1203      -0.389  20.398  -7.164  1.00 67.31           C  
ANISOU 3876  CAD 9GF A1203     8972   6966   9638    132   1042     -4       C  
HETATM 3877  CAE 9GF A1203      -0.387  18.869  -7.126  1.00 67.52           C  
ANISOU 3877  CAE 9GF A1203     9015   6979   9661    196   1028    -88       C  
HETATM 3878  CAF 9GF A1203      -1.794  18.283  -7.278  1.00 66.63           C  
ANISOU 3878  CAF 9GF A1203     8953   6806   9558    184    981    -67       C  
HETATM 3879  CAG 9GF A1203      -1.832  16.814  -7.713  1.00 67.41           C  
ANISOU 3879  CAG 9GF A1203     9095   6875   9642    218    937   -150       C  
HETATM 3880  CAH 9GF A1203      -2.424  15.972  -6.587  1.00 64.91           C  
ANISOU 3880  CAH 9GF A1203     8816   6450   9397    221    882   -126       C  
HETATM 3881  CAI 9GF A1203      -0.434  16.300  -8.048  1.00 68.73           C  
ANISOU 3881  CAI 9GF A1203     9241   7099   9774    293    960   -256       C  
HETATM 3882  CAJ 9GF A1203      -2.693  16.669  -8.967  1.00 69.55           C  
ANISOU 3882  CAJ 9GF A1203     9392   7179   9853    176    910   -151       C  
HETATM 3883  CAK 9GF A1203      -3.510  17.708  -9.388  1.00 69.29           C  
ANISOU 3883  CAK 9GF A1203     9340   7189   9797    119    920    -62       C  
HETATM 3884  CAL 9GF A1203      -4.279  17.566 -10.533  1.00 71.44           C  
ANISOU 3884  CAL 9GF A1203     9631   7507  10007     82    886    -59       C  
HETATM 3885  CAM 9GF A1203      -4.239  16.380 -11.252  1.00 73.06           C  
ANISOU 3885  CAM 9GF A1203     9882   7707  10169     98    839   -162       C  
HETATM 3886  CAN 9GF A1203      -5.077  16.180 -12.528  1.00 75.65           C  
ANISOU 3886  CAN 9GF A1203    10236   8094  10415     55    788   -175       C  
HETATM 3887  CAO 9GF A1203      -4.150  16.416 -13.725  1.00 77.76           C  
ANISOU 3887  CAO 9GF A1203    10486   8507  10552     89    837   -240       C  
HETATM 3888  CAP 9GF A1203      -4.886  16.290 -15.058  1.00 81.42           C  
ANISOU 3888  CAP 9GF A1203    10973   9059  10905     53    788   -258       C  
HETATM 3889  CAR 9GF A1203      -6.098  17.229 -15.115  1.00 81.94           C  
ANISOU 3889  CAR 9GF A1203    11014   9130  10988    -24    764   -107       C  
HETATM 3890  CAS 9GF A1203      -7.034  17.045 -13.919  1.00 78.94           C  
ANISOU 3890  CAS 9GF A1203    10631   8622  10741    -51    722    -47       C  
HETATM 3891  CAT 9GF A1203      -6.316  17.096 -12.566  1.00 76.38           C  
ANISOU 3891  CAT 9GF A1203    10294   8211  10517    -10    772    -43       C  
HETATM 3892  CAU 9GF A1203      -7.339  16.657 -11.504  1.00 74.84           C  
ANISOU 3892  CAU 9GF A1203    10090   7930  10416    -45    722     10       C  
HETATM 3893  CAV 9GF A1203      -8.325  17.773 -11.157  1.00 74.10           C  
ANISOU 3893  CAV 9GF A1203     9931   7881  10341    -57    732    132       C  
HETATM 3894  CAW 9GF A1203      -7.724  18.785 -10.184  1.00 71.53           C  
ANISOU 3894  CAW 9GF A1203     9582   7533  10064      0    798    170       C  
HETATM 3895  CAY 9GF A1203      -3.419  15.346 -10.833  1.00 72.26           C  
ANISOU 3895  CAY 9GF A1203     9814   7543  10097    166    822   -265       C  
HETATM 3896  CBA 9GF A1203      -2.648  15.491  -9.693  1.00 70.35           C  
ANISOU 3896  CBA 9GF A1203     9546   7263   9921    206    859   -252       C  
HETATM 3897  OAQ 9GF A1203      -4.004  16.621 -16.104  1.00 84.94           O  
ANISOU 3897  OAQ 9GF A1203    11386   9682  11207     81    847   -297       O  
HETATM 3898  OAX 9GF A1203      -8.755  19.574  -9.660  1.00 72.12           O  
ANISOU 3898  OAX 9GF A1203     9604   7633  10165     19    787    252       O  
HETATM 3899  OAZ 9GF A1203      -3.372  14.151 -11.566  1.00 74.50           O  
ANISOU 3899  OAZ 9GF A1203    10166   7795  10343    204    751   -391       O  
HETATM 3900  C10 7IC A1204     -12.159  25.355  -2.613  1.00 76.37           C  
ANISOU 3900  C10 7IC A1204     9844   8399  10776    814    805    228       C  
HETATM 3901  C4  7IC A1204     -12.299  27.010   0.058  1.00 77.53           C  
ANISOU 3901  C4  7IC A1204     9972   8622  10863   1190    793     16       C  
HETATM 3902  C5  7IC A1204     -11.018  26.934  -0.776  1.00 75.07           C  
ANISOU 3902  C5  7IC A1204     9800   8085  10638   1027    775     48       C  
HETATM 3903  C6  7IC A1204     -11.231  26.370  -2.192  1.00 74.77           C  
ANISOU 3903  C6  7IC A1204     9756   8034  10618    888    774    151       C  
HETATM 3904  C7  7IC A1204     -10.536  26.731  -3.356  1.00 73.47           C  
ANISOU 3904  C7  7IC A1204     9698   7711  10507    797    735    190       C  
HETATM 3905  C9  7IC A1204     -11.981  25.177  -3.960  1.00 75.95           C  
ANISOU 3905  C9  7IC A1204     9842   8267  10747    704    779    286       C  
HETATM 3906  C11 7IC A1204     -13.143  24.572  -1.951  1.00 79.26           C  
ANISOU 3906  C11 7IC A1204    10060   8983  11074    816    846    263       C  
HETATM 3907  C12 7IC A1204     -13.912  23.646  -2.652  1.00 82.28           C  
ANISOU 3907  C12 7IC A1204    10358   9471  11432    695    845    353       C  
HETATM 3908  C13 7IC A1204     -13.719  23.475  -4.024  1.00 81.20           C  
ANISOU 3908  C13 7IC A1204    10292   9231  11331    594    806    389       C  
HETATM 3909  C14 7IC A1204     -12.761  24.232  -4.681  1.00 77.95           C  
ANISOU 3909  C14 7IC A1204    10016   8633  10967    605    781    356       C  
HETATM 3910  C15 7IC A1204     -14.557  22.462  -4.802  1.00 84.05           C  
ANISOU 3910  C15 7IC A1204    10574   9697  11665    458    784    468       C  
HETATM 3911  C16 7IC A1204      -9.420  27.768  -3.544  1.00 71.45           C  
ANISOU 3911  C16 7IC A1204     9581   7252  10315    782    679    167       C  
HETATM 3912  C17 7IC A1204      -9.331  28.418  -4.766  1.00 71.37           C  
ANISOU 3912  C17 7IC A1204     9645   7140  10332    732    618    240       C  
HETATM 3913  C18 7IC A1204      -8.340  29.359  -4.994  1.00 70.94           C  
ANISOU 3913  C18 7IC A1204     9712   6909  10334    681    556    252       C  
HETATM 3914  C19 7IC A1204      -7.423  29.653  -3.998  1.00 69.91           C  
ANISOU 3914  C19 7IC A1204     9627   6697  10239    683    550    176       C  
HETATM 3915  C20 7IC A1204      -7.502  29.005  -2.777  1.00 68.95           C  
ANISOU 3915  C20 7IC A1204     9433   6677  10086    750    612     88       C  
HETATM 3916  C21 7IC A1204      -8.492  28.062  -2.556  1.00 70.15           C  
ANISOU 3916  C21 7IC A1204     9467   7011  10177    797    679     92       C  
HETATM 3917  C22 7IC A1204      -9.993  26.047  -0.067  1.00 73.74           C  
ANISOU 3917  C22 7IC A1204     9640   7912  10464    917    833     39       C  
HETATM 3918  C23 7IC A1204      -9.563  24.770  -0.463  1.00 72.07           C  
ANISOU 3918  C23 7IC A1204     9411   7714  10258    750    879    109       C  
HETATM 3919  C24 7IC A1204      -8.587  24.160   0.388  1.00 71.51           C  
ANISOU 3919  C24 7IC A1204     9358   7628  10185    700    912     84       C  
HETATM 3920  C25 7IC A1204      -8.221  24.954   1.485  1.00 71.93           C  
ANISOU 3920  C25 7IC A1204     9437   7671  10223    813    896     -5       C  
HETATM 3921  N2  7IC A1204     -13.095  28.185  -0.256  1.00 79.27           N  
ANISOU 3921  N2  7IC A1204    10203   8823  11091   1376    716    -29       N  
HETATM 3922  N8  7IC A1204     -11.005  26.019  -4.364  1.00 74.18           N  
ANISOU 3922  N8  7IC A1204     9744   7867  10574    701    745    265       N  
HETATM 3923  O1  7IC A1204     -14.356  27.781  -0.722  1.00 82.48           O1-
ANISOU 3923  O1  7IC A1204    10463   9430  11445   1393    732     43       O1-
HETATM 3924  O3  7IC A1204     -12.459  28.969  -1.232  1.00 77.82           O  
ANISOU 3924  O3  7IC A1204    10177   8390  11001   1337    633    -13       O  
HETATM 3925  S26 7IC A1204      -9.127  26.374   1.348  1.00 73.63           S  
ANISOU 3925  S26 7IC A1204     9667   7873  10436    985    835    -64       S  
HETATM 3926  C1  PEG A1205       4.462  27.613  16.152  1.00 79.88           C  
ANISOU 3926  C1  PEG A1205    10740   8914  10695   1050    187  -1157       C  
HETATM 3927  O1  PEG A1205       4.950  28.715  16.899  1.00 81.42           O  
ANISOU 3927  O1  PEG A1205    11020   9055  10863   1082     39  -1344       O  
HETATM 3928  C2  PEG A1205       3.491  26.798  16.949  1.00 81.41           C  
ANISOU 3928  C2  PEG A1205    10872   9345  10714   1176    283  -1105       C  
HETATM 3929  O2  PEG A1205       3.381  25.501  16.383  1.00 81.06           O  
ANISOU 3929  O2  PEG A1205    10748   9346  10705   1103    391   -904       O  
HETATM 3930  C3  PEG A1205       3.364  24.473  17.363  1.00 83.09           C  
ANISOU 3930  C3  PEG A1205    10940   9814  10818   1136    423   -814       C  
HETATM 3931  C4  PEG A1205       3.609  23.147  16.709  1.00 82.56           C  
ANISOU 3931  C4  PEG A1205    10820   9719  10831   1039    484   -619       C  
HETATM 3932  O4  PEG A1205       3.721  22.111  17.669  1.00 85.66           O  
ANISOU 3932  O4  PEG A1205    11166  10282  11098   1056    486   -508       O  
HETATM 3933  C1  PEG A1206       1.819  13.275  22.053  1.00103.75           C  
ANISOU 3933  C1  PEG A1206    13360  13316  12744    713    397   1074       C  
HETATM 3934  O1  PEG A1206       1.980  12.411  23.164  1.00104.74           O  
ANISOU 3934  O1  PEG A1206    13495  13581  12722    675    317   1289       O  
HETATM 3935  C2  PEG A1206       2.667  12.839  20.896  1.00100.03           C  
ANISOU 3935  C2  PEG A1206    12970  12505  12533    717    335   1023       C  
HETATM 3936  O2  PEG A1206       2.310  13.578  19.738  1.00 97.74           O  
ANISOU 3936  O2  PEG A1206    12670  12096  12370    722    420    863       O  
HETATM 3937  C3  PEG A1206       2.398  14.984  19.925  1.00 98.78           C  
ANISOU 3937  C3  PEG A1206    12752  12341  12438    812    476    638       C  
HETATM 3938  C4  PEG A1206       2.110  15.685  18.633  1.00 95.67           C  
ANISOU 3938  C4  PEG A1206    12365  11789  12198    810    543    497       C  
HETATM 3939  O4  PEG A1206       3.289  15.883  17.871  1.00 91.65           O  
ANISOU 3939  O4  PEG A1206    11889  11079  11855    839    496    375       O  
HETATM 3940  C1  GOL A1207       2.872  20.831  24.466  1.00108.75           C  
ANISOU 3940  C1  GOL A1207    13915  14522  12884   1382    412   -373       C  
HETATM 3941  O1  GOL A1207       1.708  20.067  24.520  1.00109.82           O  
ANISOU 3941  O1  GOL A1207    13984  14825  12919   1347    517   -174       O  
HETATM 3942  C2  GOL A1207       2.767  21.710  23.202  1.00104.37           C  
ANISOU 3942  C2  GOL A1207    13411  13694  12550   1378    429   -522       C  
HETATM 3943  O2  GOL A1207       1.749  22.636  23.293  1.00103.22           O  
ANISOU 3943  O2  GOL A1207    13261  13647  12311   1492    479   -671       O  
HETATM 3944  C3  GOL A1207       4.141  22.383  23.058  1.00103.47           C  
ANISOU 3944  C3  GOL A1207    13358  13389  12566   1360    306   -684       C  
HETATM 3945  O3  GOL A1207       4.005  23.313  22.033  1.00 99.97           O  
ANISOU 3945  O3  GOL A1207    12968  12724  12292   1352    309   -817       O  
HETATM 3946  C1  GOL A1208      -1.073   1.305 -16.768  1.00 88.76           C  
ANISOU 3946  C1  GOL A1208    13430   8217  12078   1441   -761  -2503       C  
HETATM 3947  O1  GOL A1208      -1.130   1.567 -18.136  1.00 91.51           O  
ANISOU 3947  O1  GOL A1208    13737   8813  12218   1508   -716  -2675       O  
HETATM 3948  C2  GOL A1208      -0.214   2.414 -16.122  1.00 87.78           C  
ANISOU 3948  C2  GOL A1208    13067   8367  11921   1480   -501  -2353       C  
HETATM 3949  O2  GOL A1208       0.255   2.044 -14.869  1.00 86.08           O  
ANISOU 3949  O2  GOL A1208    12886   7956  11867   1520   -543  -2264       O  
HETATM 3950  C3  GOL A1208       0.930   2.675 -17.133  1.00 89.93           C  
ANISOU 3950  C3  GOL A1208    13217   8981  11973   1751   -372  -2589       C  
HETATM 3951  O3  GOL A1208       1.380   1.431 -17.572  1.00 90.54           O  
ANISOU 3951  O3  GOL A1208    13469   8893  12040   2006   -562  -2891       O  
HETATM 3952  C1  GOL A1209      -3.736  -2.262 -18.335  1.00 90.05           C  
ANISOU 3952  C1  GOL A1209    14403   7367  12445   1202  -1703  -2921       C  
HETATM 3953  O1  GOL A1209      -4.130  -1.965 -17.034  1.00 88.14           O  
ANISOU 3953  O1  GOL A1209    14094   7023  12374    973  -1652  -2583       O  
HETATM 3954  C2  GOL A1209      -3.930  -0.977 -19.171  1.00 91.29           C  
ANISOU 3954  C2  GOL A1209    14316   7985  12385   1150  -1444  -2872       C  
HETATM 3955  O2  GOL A1209      -3.467   0.147 -18.510  1.00 90.24           O  
ANISOU 3955  O2  GOL A1209    13945   8108  12235   1134  -1168  -2659       O  
HETATM 3956  C3  GOL A1209      -3.146  -1.239 -20.476  1.00 93.00           C  
ANISOU 3956  C3  GOL A1209    14566   8393  12379   1468  -1449  -3248       C  
HETATM 3957  O3  GOL A1209      -1.794  -1.159 -20.152  1.00 92.13           O  
ANISOU 3957  O3  GOL A1209    14368   8407  12230   1758  -1318  -3350       O  
HETATM 3958  C1  GOL A1210      24.599  21.636  24.123  1.00122.15           C  
ANISOU 3958  C1  GOL A1210    14168  16514  15730    702  -1352   -918       C  
HETATM 3959  O1  GOL A1210      24.643  20.706  25.156  1.00121.92           O  
ANISOU 3959  O1  GOL A1210    14156  16599  15568    890  -1420   -852       O  
HETATM 3960  C2  GOL A1210      26.038  22.158  23.939  1.00123.23           C  
ANISOU 3960  C2  GOL A1210    14056  16843  15922    554  -1473   -961       C  
HETATM 3961  O2  GOL A1210      26.271  22.600  22.648  1.00123.02           O  
ANISOU 3961  O2  GOL A1210    13931  16769  16041    406  -1382   -951       O  
HETATM 3962  C3  GOL A1210      26.180  23.288  24.978  1.00124.55           C  
ANISOU 3962  C3  GOL A1210    14291  17037  15996    402  -1648  -1098       C  
HETATM 3963  O3  GOL A1210      26.606  22.689  26.159  1.00124.88           O  
ANISOU 3963  O3  GOL A1210    14292  17265  15891    544  -1772  -1085       O  
HETATM 3964  C18 OLC A1211     -10.183  27.204   5.146  1.00 72.71           C  
ANISOU 3964  C18 OLC A1211     9392   8180  10053   1427    866   -322       C  
HETATM 3965  C10 OLC A1211      -5.830  23.945  13.374  1.00 81.62           C  
ANISOU 3965  C10 OLC A1211    10419  10038  10553   1339    977   -394       C  
HETATM 3966  C9  OLC A1211      -6.277  23.240  14.445  1.00 85.45           C  
ANISOU 3966  C9  OLC A1211    10798  10811  10859   1345   1029   -305       C  
HETATM 3967  C17 OLC A1211      -9.889  26.762   6.608  1.00 74.90           C  
ANISOU 3967  C17 OLC A1211     9615   8628  10217   1461    912   -364       C  
HETATM 3968  C11 OLC A1211      -6.997  24.422  12.460  1.00 81.00           C  
ANISOU 3968  C11 OLC A1211    10299   9962  10514   1397   1004   -400       C  
HETATM 3969  C8  OLC A1211      -7.410  22.606  15.321  1.00 88.83           C  
ANISOU 3969  C8  OLC A1211    11057  11622  11073   1362   1112   -182       C  
HETATM 3970  C24 OLC A1211     -12.564  26.633  25.077  1.00 98.84           C  
ANISOU 3970  C24 OLC A1211    11288  16338   9928   3214   1475  -1267       C  
HETATM 3971  C16 OLC A1211      -8.417  27.093   6.973  1.00 73.28           C  
ANISOU 3971  C16 OLC A1211     9549   8219  10074   1412    858   -442       C  
HETATM 3972  C12 OLC A1211      -6.492  25.512  11.449  1.00 76.96           C  
ANISOU 3972  C12 OLC A1211     9925   9144  10174   1425    925   -521       C  
HETATM 3973  C7  OLC A1211      -7.009  22.690  16.825  1.00 90.02           C  
ANISOU 3973  C7  OLC A1211    11185  11992  11025   1452   1103   -244       C  
HETATM 3974  C15 OLC A1211      -7.832  25.892   7.776  1.00 73.02           C  
ANISOU 3974  C15 OLC A1211     9463   8305   9978   1295    920   -367       C  
HETATM 3975  C13 OLC A1211      -6.926  25.100  10.001  1.00 75.77           C  
ANISOU 3975  C13 OLC A1211     9765   8876  10149   1305    951   -395       C  
HETATM 3976  C6  OLC A1211      -8.271  22.955  17.711  1.00 92.87           C  
ANISOU 3976  C6  OLC A1211    11377  12777  11132   1602   1180   -266       C  
HETATM 3977  C14 OLC A1211      -7.354  26.358   9.180  1.00 73.71           C  
ANISOU 3977  C14 OLC A1211     9570   8467   9968   1415    893   -499       C  
HETATM 3978  C5  OLC A1211      -8.478  24.495  17.878  1.00 90.80           C  
ANISOU 3978  C5  OLC A1211    11158  12512  10831   1876   1141   -565       C  
HETATM 3979  C4  OLC A1211      -9.833  24.776  18.603  1.00 92.52           C  
ANISOU 3979  C4  OLC A1211    11182  13176  10794   2063   1225   -606       C  
HETATM 3980  C3  OLC A1211      -9.591  25.718  19.821  1.00 92.97           C  
ANISOU 3980  C3  OLC A1211    11267  13401  10657   2317   1183   -866       C  
HETATM 3981  C2  OLC A1211     -10.955  26.065  20.483  1.00 94.11           C  
ANISOU 3981  C2  OLC A1211    11204  14021  10533   2544   1272   -938       C  
HETATM 3982  C21 OLC A1211     -11.032  28.069  23.719  1.00 95.84           C  
ANISOU 3982  C21 OLC A1211    11381  14954  10079   3272   1210  -1610       C  
HETATM 3983  C1  OLC A1211     -10.725  26.521  21.945  1.00 95.64           C  
ANISOU 3983  C1  OLC A1211    11380  14504  10454   2746   1258  -1125       C  
HETATM 3984  C22 OLC A1211     -12.097  28.069  24.830  1.00 97.48           C  
ANISOU 3984  C22 OLC A1211    11340  15801   9895   3490   1326  -1661       C  
HETATM 3985  O19 OLC A1211      -9.823  26.063  22.569  1.00 96.61           O  
ANISOU 3985  O19 OLC A1211    11566  14602  10539   2633   1228  -1070       O  
HETATM 3986  O25 OLC A1211     -13.155  26.544  26.350  1.00100.48           O  
ANISOU 3986  O25 OLC A1211    11289  17147   9740   3363   1568  -1290       O  
HETATM 3987  O23 OLC A1211     -11.554  28.587  26.009  1.00 98.94           O  
ANISOU 3987  O23 OLC A1211    11592  16129   9871   3675   1263  -1895       O  
HETATM 3988  O20 OLC A1211     -11.570  27.488  22.544  1.00 95.40           O  
ANISOU 3988  O20 OLC A1211    11259  14775  10213   3084   1272  -1377       O  
HETATM 3989  C18 OLC A1212      -7.702   5.898  13.265  1.00 87.58           C  
ANISOU 3989  C18 OLC A1212    11570   9980  11727   -999    160   2440       C  
HETATM 3990  C10 OLC A1212      -8.020   5.152  19.486  1.00 96.85           C  
ANISOU 3990  C10 OLC A1212    12405  12398  11996  -1273    197   3394       C  
HETATM 3991  C9  OLC A1212      -7.247   4.061  19.714  1.00 96.35           C  
ANISOU 3991  C9  OLC A1212    12545  12023  12040  -1339      1   3554       C  
HETATM 3992  C17 OLC A1212      -7.428   7.392  12.936  1.00 88.33           C  
ANISOU 3992  C17 OLC A1212    11559  10220  11783   -760    337   2144       C  
HETATM 3993  C11 OLC A1212      -7.217   6.342  18.883  1.00 95.93           C  
ANISOU 3993  C11 OLC A1212    12300  12185  11964   -959    302   2981       C  
HETATM 3994  C8  OLC A1212      -7.020   2.592  20.197  1.00 96.06           C  
ANISOU 3994  C8  OLC A1212    12687  11754  12058  -1549   -234   3899       C  
HETATM 3995  C24 OLC A1212      -1.885   2.430  30.692  1.00109.33           C  
ANISOU 3995  C24 OLC A1212    14284  15238  12021   -981   -524   4822       C  
HETATM 3996  C16 OLC A1212      -8.221   8.288  13.923  1.00 90.80           C  
ANISOU 3996  C16 OLC A1212    11652  10984  11864   -744    490   2194       C  
HETATM 3997  C12 OLC A1212      -8.129   7.108  17.861  1.00 95.27           C  
ANISOU 3997  C12 OLC A1212    12099  12175  11926   -945    427   2817       C  
HETATM 3998  C7  OLC A1212      -7.495   2.440  21.674  1.00 97.31           C  
ANISOU 3998  C7  OLC A1212    12705  12350  11918  -1700   -203   4220       C  
HETATM 3999  C15 OLC A1212      -7.297   8.669  15.117  1.00 92.44           C  
ANISOU 3999  C15 OLC A1212    11858  11314  11950   -592    517   2154       C  
HETATM 4000  C13 OLC A1212      -7.566   8.551  17.632  1.00 96.04           C  
ANISOU 4000  C13 OLC A1212    12150  12326  12016   -649    561   2453       C  
HETATM 4001  C6  OLC A1212      -6.337   1.857  22.551  1.00 98.68           C  
ANISOU 4001  C6  OLC A1212    13040  12378  12077  -1620   -355   4327       C  
HETATM 4002  C14 OLC A1212      -8.174   9.129  16.316  1.00 94.58           C  
ANISOU 4002  C14 OLC A1212    11927  12053  11956   -623    627   2280       C  
HETATM 4003  C5  OLC A1212      -6.682   2.036  24.066  1.00101.14           C  
ANISOU 4003  C5  OLC A1212    13180  13210  12040  -1697   -276   4569       C  
HETATM 4004  C4  OLC A1212      -6.279   3.472  24.537  1.00101.59           C  
ANISOU 4004  C4  OLC A1212    13074  13611  11913  -1391    -65   4237       C  
HETATM 4005  C3  OLC A1212      -5.230   3.366  25.685  1.00103.29           C  
ANISOU 4005  C3  OLC A1212    13354  13898  11993  -1265   -140   4289       C  
HETATM 4006  C2  OLC A1212      -3.839   3.052  25.072  1.00101.98           C  
ANISOU 4006  C2  OLC A1212    13422  13216  12110  -1074   -296   4095       C  
HETATM 4007  C21 OLC A1212      -1.921   3.324  28.353  1.00107.02           C  
ANISOU 4007  C21 OLC A1212    14022  14445  12196   -799   -387   4250       C  
HETATM 4008  C1  OLC A1212      -2.727   3.257  26.129  1.00102.90           C  
ANISOU 4008  C1  OLC A1212    13562  13445  12089   -888   -340   4054       C  
HETATM 4009  C22 OLC A1212      -2.358   3.582  29.803  1.00108.80           C  
ANISOU 4009  C22 OLC A1212    14084  15232  12021   -859   -308   4442       C  
HETATM 4010  O19 OLC A1212      -1.594   3.366  25.784  1.00101.96           O  
ANISOU 4010  O19 OLC A1212    13554  13054  12132   -681   -409   3835       O  
HETATM 4011  O25 OLC A1212      -1.524   2.935  31.953  1.00110.77           O  
ANISOU 4011  O25 OLC A1212    14363  15842  11884   -871   -477   4819       O  
HETATM 4012  O23 OLC A1212      -1.787   4.775  30.253  1.00109.57           O  
ANISOU 4012  O23 OLC A1212    14082  15574  11974   -597   -190   4109       O  
HETATM 4013  O20 OLC A1212      -3.056   3.309  27.506  1.00105.54           O  
ANISOU 4013  O20 OLC A1212    13773  14235  12091   -965   -300   4279       O  
HETATM 4014  C11 OLA A1213     -18.945   2.375  -9.344  1.00 92.91           C  
ANISOU 4014  C11 OLA A1213    12771   9136  13393  -2609  -1349   1004       C  
HETATM 4015  C12 OLA A1213     -18.355   2.903  -8.041  1.00 91.36           C  
ANISOU 4015  C12 OLA A1213    12487   9038  13188  -2480  -1152   1116       C  
HETATM 4016  C13 OLA A1213     -18.272   1.797  -6.996  1.00 90.65           C  
ANISOU 4016  C13 OLA A1213    12508   8739  13196  -2679  -1296   1299       C  
HETATM 4017  C14 OLA A1213     -18.209   2.365  -5.581  1.00 91.12           C  
ANISOU 4017  C14 OLA A1213    12389   9024  13207  -2649  -1107   1495       C  
HETATM 4018  C15 OLA A1213     -16.768   2.384  -5.086  1.00 89.14           C  
ANISOU 4018  C15 OLA A1213    12298   8579  12992  -2392  -1033   1373       C  
HETATM 4019  C16 OLA A1213     -16.626   1.738  -3.712  1.00 88.35           C  
ANISOU 4019  C16 OLA A1213    12225   8413  12932  -2525  -1080   1602       C  
HETATM 4020  C17 OLA A1213     -17.394   2.507  -2.643  1.00 89.37           C  
ANISOU 4020  C17 OLA A1213    12056   8954  12947  -2603   -898   1834       C  
HETATM 4021  C18 OLA A1213     -16.839   2.192  -1.259  1.00 88.36           C  
ANISOU 4021  C18 OLA A1213    11956   8797  12820  -2610   -873   1996       C  
HETATM 4022  C12 OLA A1214     -20.078  14.423 -10.818  1.00 98.45           C  
ANISOU 4022  C12 OLA A1214    12160  11864  13384   -928     94    840       C  
HETATM 4023  C13 OLA A1214     -19.537  13.550  -9.692  1.00 96.22           C  
ANISOU 4023  C13 OLA A1214    11935  11462  13164  -1015    110    871       C  
HETATM 4024  C14 OLA A1214     -18.050  13.272  -9.875  1.00 92.57           C  
ANISOU 4024  C14 OLA A1214    11694  10736  12743   -940    134    736       C  
HETATM 4025  C15 OLA A1214     -17.575  12.224  -8.877  1.00 90.53           C  
ANISOU 4025  C15 OLA A1214    11509  10337  12551  -1042    109    772       C  
HETATM 4026  C16 OLA A1214     -17.832  12.679  -7.446  1.00 90.90           C  
ANISOU 4026  C16 OLA A1214    11412  10538  12588  -1003    213    888       C  
HETATM 4027  C17 OLA A1214     -17.146  11.751  -6.451  1.00 87.89           C  
ANISOU 4027  C17 OLA A1214    11125  10006  12263  -1076    197    924       C  
HETATM 4028  C18 OLA A1214     -17.353  12.230  -5.020  1.00 88.26           C  
ANISOU 4028  C18 OLA A1214    11028  10234  12273  -1027    306   1032       C  
HETATM 4029  C11 OLA A1215       9.566  35.021 -17.055  1.00 96.93           C  
ANISOU 4029  C11 OLA A1215    12173  12042  12612  -2861    705   2612       C  
HETATM 4030  C12 OLA A1215       8.997  34.558 -15.719  1.00 95.47           C  
ANISOU 4030  C12 OLA A1215    12109  11538  12626  -2583    676   2319       C  
HETATM 4031  C13 OLA A1215       8.307  35.710 -14.998  1.00 93.24           C  
ANISOU 4031  C13 OLA A1215    12100  10753  12573  -2622    450   2377       C  
HETATM 4032  C14 OLA A1215       7.629  35.241 -13.716  1.00 91.23           C  
ANISOU 4032  C14 OLA A1215    11955  10227  12481  -2329    433   2088       C  
HETATM 4033  C15 OLA A1215       8.528  35.439 -12.501  1.00 91.14           C  
ANISOU 4033  C15 OLA A1215    11906  10132  12592  -2395    379   2003       C  
HETATM 4034  C16 OLA A1215       7.794  35.055 -11.222  1.00 88.62           C  
ANISOU 4034  C16 OLA A1215    11706   9551  12415  -2110    352   1736       C  
HETATM 4035  C17 OLA A1215       8.470  35.656  -9.996  1.00 88.19           C  
ANISOU 4035  C17 OLA A1215    11695   9308  12505  -2197    226   1682       C  
HETATM 4036  C18 OLA A1215       7.720  35.281  -8.724  1.00 85.84           C  
ANISOU 4036  C18 OLA A1215    11507   8789  12320  -1909    205   1423       C  
HETATM 4037  C12 OLA A1216      -8.219  31.319  10.195  1.00 75.84           C  
ANISOU 4037  C12 OLA A1216    10156   8434  10225   2176    533  -1182       C  
HETATM 4038  C13 OLA A1216      -8.347  30.331   9.040  1.00 75.07           C  
ANISOU 4038  C13 OLA A1216     9984   8333  10206   1959    624   -955       C  
HETATM 4039  C14 OLA A1216      -8.010  30.983   7.702  1.00 73.67           C  
ANISOU 4039  C14 OLA A1216     9940   7842  10208   1868    536   -909       C  
HETATM 4040  C15 OLA A1216      -8.597  32.387   7.603  1.00 74.51           C  
ANISOU 4040  C15 OLA A1216    10153   7809  10349   2095    403  -1057       C  
HETATM 4041  C16 OLA A1216      -9.150  32.657   6.208  1.00 73.37           C  
ANISOU 4041  C16 OLA A1216    10034   7536  10309   2059    374   -947       C  
HETATM 4042  C17 OLA A1216      -8.149  33.421   5.349  1.00 71.63           C  
ANISOU 4042  C17 OLA A1216    10005   6956  10254   1910    246   -910       C  
HETATM 4043  C18 OLA A1216      -8.769  33.851   4.025  1.00 71.74           C  
ANISOU 4043  C18 OLA A1216    10058   6847  10352   1906    195   -807       C  
HETATM 4044  O   HOH A1301      22.943  22.663  47.491  1.00126.11           O  
ANISOU 4044  O   HOH A1301    15605  21090  11220   2029  -3370  -1825       O  
HETATM 4045  O   HOH A1302       2.363  13.037   6.063  1.00 64.95           O  
ANISOU 4045  O   HOH A1302     8791   6370   9518    592    621    169       O  
HETATM 4046  O   HOH A1303      33.543   7.053  28.913  1.00110.56           O  
ANISOU 4046  O   HOH A1303    11656  16310  14042   3979  -2981    273       O  
HETATM 4047  O   HOH A1304      -4.234  23.805 -21.374  1.00 94.01           O  
ANISOU 4047  O   HOH A1304    12399  11592  11727   -419    911    698       O  
HETATM 4048  O   HOH A1305      16.060  22.695  55.675  1.00134.99           O  
ANISOU 4048  O   HOH A1305    16944  25703   8643   3093  -2825  -1985       O  
HETATM 4049  O   HOH A1306      24.773  18.812  16.653  1.00106.32           O  
ANISOU 4049  O   HOH A1306    11727  14335  14335    948   -584   -641       O  
HETATM 4050  O   HOH A1307      44.030   8.452  38.990  1.00130.09           O  
ANISOU 4050  O   HOH A1307    11883  22458  15088   4522  -5337    398       O  
HETATM 4051  O   HOH A1308      -6.759  31.051 -24.974  1.00 95.16           O  
ANISOU 4051  O   HOH A1308    12910  11542  11705   -891    324   2123       O  
HETATM 4052  O   HOH A1309     -12.309  29.943 -21.221  1.00 99.77           O  
ANISOU 4052  O   HOH A1309    13450  11500  12959    -85     76   1551       O  
HETATM 4053  O   HOH A1310      16.446   4.960  19.346  1.00 93.11           O  
ANISOU 4053  O   HOH A1310    12230  10357  12792   2326  -1149    772       O  
HETATM 4054  O   HOH A1311      23.799   3.488  34.087  1.00113.63           O  
ANISOU 4054  O   HOH A1311    14361  15203  13610   3086  -2976   2109       O  
HETATM 4055  O   HOH A1312      38.177  -9.878  50.588  1.00167.50           O  
ANISOU 4055  O   HOH A1312    21174  23429  19040   6220  -8184   6092       O  
HETATM 4056  O   HOH A1313      37.448 -11.860  49.285  1.00176.31           O  
ANISOU 4056  O   HOH A1313    22706  23665  20620   6470  -8122   6326       O  
HETATM 4057  O   HOH A1314      25.972  -6.322  64.868  1.00185.32           O  
ANISOU 4057  O   HOH A1314    24903  29965  15546   2436  -6752   8502       O  
HETATM 4058  O   HOH A1315      26.818  24.176  16.689  1.00111.22           O  
ANISOU 4058  O   HOH A1315    12030  15197  15031   -218   -897   -763       O  
HETATM 4059  O   HOH A1316      32.736 -13.151  33.349  1.00146.43           O  
ANISOU 4059  O   HOH A1316    19873  16030  19733   6949  -6230   3234       O  
HETATM 4060  O   HOH A1317       6.653  37.517 -19.653  1.00 93.12           O  
ANISOU 4060  O   HOH A1317    12286  10996  12099  -3077    304   3279       O  
HETATM 4061  O   HOH A1318      26.943  -1.051  26.848  1.00109.01           O  
ANISOU 4061  O   HOH A1318    13788  13063  14567   4626  -3299   1367       O  
CONECT   15   86                                                                
CONECT   86   15                                                                
CONECT 1261 1315                                                                
CONECT 1315 1261                                                                
CONECT 3817 3818 3826                                                           
CONECT 3818 3817 3819                                                           
CONECT 3819 3818 3820 3844                                                      
CONECT 3820 3819 3821                                                           
CONECT 3821 3820 3822 3826                                                      
CONECT 3822 3821 3823                                                           
CONECT 3823 3822 3824                                                           
CONECT 3824 3823 3825 3830                                                      
CONECT 3825 3824 3826 3827                                                      
CONECT 3826 3817 3821 3825 3835                                                 
CONECT 3827 3825 3828                                                           
CONECT 3828 3827 3829                                                           
CONECT 3829 3828 3830 3833 3834                                                 
CONECT 3830 3824 3829 3831                                                      
CONECT 3831 3830 3832                                                           
CONECT 3832 3831 3833                                                           
CONECT 3833 3829 3832 3836                                                      
CONECT 3834 3829                                                                
CONECT 3835 3826                                                                
CONECT 3836 3833 3837 3838                                                      
CONECT 3837 3836                                                                
CONECT 3838 3836 3839                                                           
CONECT 3839 3838 3840                                                           
CONECT 3840 3839 3841                                                           
CONECT 3841 3840 3842 3843                                                      
CONECT 3842 3841                                                                
CONECT 3843 3841                                                                
CONECT 3844 3819                                                                
CONECT 3845 3846 3854                                                           
CONECT 3846 3845 3847                                                           
CONECT 3847 3846 3848 3872                                                      
CONECT 3848 3847 3849                                                           
CONECT 3849 3848 3850 3854                                                      
CONECT 3850 3849 3851                                                           
CONECT 3851 3850 3852                                                           
CONECT 3852 3851 3853 3858                                                      
CONECT 3853 3852 3854 3855                                                      
CONECT 3854 3845 3849 3853 3863                                                 
CONECT 3855 3853 3856                                                           
CONECT 3856 3855 3857                                                           
CONECT 3857 3856 3858 3861 3862                                                 
CONECT 3858 3852 3857 3859                                                      
CONECT 3859 3858 3860                                                           
CONECT 3860 3859 3861                                                           
CONECT 3861 3857 3860 3864                                                      
CONECT 3862 3857                                                                
CONECT 3863 3854                                                                
CONECT 3864 3861 3865 3866                                                      
CONECT 3865 3864                                                                
CONECT 3866 3864 3867                                                           
CONECT 3867 3866 3868                                                           
CONECT 3868 3867 3869                                                           
CONECT 3869 3868 3870 3871                                                      
CONECT 3870 3869                                                                
CONECT 3871 3869                                                                
CONECT 3872 3847                                                                
CONECT 3873 3874                                                                
CONECT 3874 3873 3875                                                           
CONECT 3875 3874 3876                                                           
CONECT 3876 3875 3877                                                           
CONECT 3877 3876 3878                                                           
CONECT 3878 3877 3879                                                           
CONECT 3879 3878 3880 3881 3882                                                 
CONECT 3880 3879                                                                
CONECT 3881 3879                                                                
CONECT 3882 3879 3883 3896                                                      
CONECT 3883 3882 3884                                                           
CONECT 3884 3883 3885                                                           
CONECT 3885 3884 3886 3895                                                      
CONECT 3886 3885 3887 3891                                                      
CONECT 3887 3886 3888                                                           
CONECT 3888 3887 3889 3897                                                      
CONECT 3889 3888 3890                                                           
CONECT 3890 3889 3891                                                           
CONECT 3891 3886 3890 3892                                                      
CONECT 3892 3891 3893                                                           
CONECT 3893 3892 3894                                                           
CONECT 3894 3893 3898                                                           
CONECT 3895 3885 3896 3899                                                      
CONECT 3896 3882 3895                                                           
CONECT 3897 3888                                                                
CONECT 3898 3894                                                                
CONECT 3899 3895                                                                
CONECT 3900 3903 3905 3906                                                      
CONECT 3901 3902 3921                                                           
CONECT 3902 3901 3903 3917                                                      
CONECT 3903 3900 3902 3904                                                      
CONECT 3904 3903 3911 3922                                                      
CONECT 3905 3900 3909 3922                                                      
CONECT 3906 3900 3907                                                           
CONECT 3907 3906 3908                                                           
CONECT 3908 3907 3909 3910                                                      
CONECT 3909 3905 3908                                                           
CONECT 3910 3908                                                                
CONECT 3911 3904 3912 3916                                                      
CONECT 3912 3911 3913                                                           
CONECT 3913 3912 3914                                                           
CONECT 3914 3913 3915                                                           
CONECT 3915 3914 3916                                                           
CONECT 3916 3911 3915                                                           
CONECT 3917 3902 3918 3925                                                      
CONECT 3918 3917 3919                                                           
CONECT 3919 3918 3920                                                           
CONECT 3920 3919 3925                                                           
CONECT 3921 3901 3923 3924                                                      
CONECT 3922 3904 3905                                                           
CONECT 3923 3921                                                                
CONECT 3924 3921                                                                
CONECT 3925 3917 3920                                                           
CONECT 3926 3927 3928                                                           
CONECT 3927 3926                                                                
CONECT 3928 3926 3929                                                           
CONECT 3929 3928 3930                                                           
CONECT 3930 3929 3931                                                           
CONECT 3931 3930 3932                                                           
CONECT 3932 3931                                                                
CONECT 3933 3934 3935                                                           
CONECT 3934 3933                                                                
CONECT 3935 3933 3936                                                           
CONECT 3936 3935 3937                                                           
CONECT 3937 3936 3938                                                           
CONECT 3938 3937 3939                                                           
CONECT 3939 3938                                                                
CONECT 3940 3941 3942                                                           
CONECT 3941 3940                                                                
CONECT 3942 3940 3943 3944                                                      
CONECT 3943 3942                                                                
CONECT 3944 3942 3945                                                           
CONECT 3945 3944                                                                
CONECT 3946 3947 3948                                                           
CONECT 3947 3946                                                                
CONECT 3948 3946 3949 3950                                                      
CONECT 3949 3948                                                                
CONECT 3950 3948 3951                                                           
CONECT 3951 3950                                                                
CONECT 3952 3953 3954                                                           
CONECT 3953 3952                                                                
CONECT 3954 3952 3955 3956                                                      
CONECT 3955 3954                                                                
CONECT 3956 3954 3957                                                           
CONECT 3957 3956                                                                
CONECT 3958 3959 3960                                                           
CONECT 3959 3958                                                                
CONECT 3960 3958 3961 3962                                                      
CONECT 3961 3960                                                                
CONECT 3962 3960 3963                                                           
CONECT 3963 3962                                                                
CONECT 3964 3967                                                                
CONECT 3965 3966 3968                                                           
CONECT 3966 3965 3969                                                           
CONECT 3967 3964 3971                                                           
CONECT 3968 3965 3972                                                           
CONECT 3969 3966 3973                                                           
CONECT 3970 3984 3986                                                           
CONECT 3971 3967 3974                                                           
CONECT 3972 3968 3975                                                           
CONECT 3973 3969 3976                                                           
CONECT 3974 3971 3977                                                           
CONECT 3975 3972 3977                                                           
CONECT 3976 3973 3978                                                           
CONECT 3977 3974 3975                                                           
CONECT 3978 3976 3979                                                           
CONECT 3979 3978 3980                                                           
CONECT 3980 3979 3981                                                           
CONECT 3981 3980 3983                                                           
CONECT 3982 3984 3988                                                           
CONECT 3983 3981 3985 3988                                                      
CONECT 3984 3970 3982 3987                                                      
CONECT 3985 3983                                                                
CONECT 3986 3970                                                                
CONECT 3987 3984                                                                
CONECT 3988 3982 3983                                                           
CONECT 3989 3992                                                                
CONECT 3990 3991 3993                                                           
CONECT 3991 3990 3994                                                           
CONECT 3992 3989 3996                                                           
CONECT 3993 3990 3997                                                           
CONECT 3994 3991 3998                                                           
CONECT 3995 4009 4011                                                           
CONECT 3996 3992 3999                                                           
CONECT 3997 3993 4000                                                           
CONECT 3998 3994 4001                                                           
CONECT 3999 3996 4002                                                           
CONECT 4000 3997 4002                                                           
CONECT 4001 3998 4003                                                           
CONECT 4002 3999 4000                                                           
CONECT 4003 4001 4004                                                           
CONECT 4004 4003 4005                                                           
CONECT 4005 4004 4006                                                           
CONECT 4006 4005 4008                                                           
CONECT 4007 4009 4013                                                           
CONECT 4008 4006 4010 4013                                                      
CONECT 4009 3995 4007 4012                                                      
CONECT 4010 4008                                                                
CONECT 4011 3995                                                                
CONECT 4012 4009                                                                
CONECT 4013 4007 4008                                                           
CONECT 4014 4015                                                                
CONECT 4015 4014 4016                                                           
CONECT 4016 4015 4017                                                           
CONECT 4017 4016 4018                                                           
CONECT 4018 4017 4019                                                           
CONECT 4019 4018 4020                                                           
CONECT 4020 4019 4021                                                           
CONECT 4021 4020                                                                
CONECT 4022 4023                                                                
CONECT 4023 4022 4024                                                           
CONECT 4024 4023 4025                                                           
CONECT 4025 4024 4026                                                           
CONECT 4026 4025 4027                                                           
CONECT 4027 4026 4028                                                           
CONECT 4028 4027                                                                
CONECT 4029 4030                                                                
CONECT 4030 4029 4031                                                           
CONECT 4031 4030 4032                                                           
CONECT 4032 4031 4033                                                           
CONECT 4033 4032 4034                                                           
CONECT 4034 4033 4035                                                           
CONECT 4035 4034 4036                                                           
CONECT 4036 4035                                                                
CONECT 4037 4038                                                                
CONECT 4038 4037 4039                                                           
CONECT 4039 4038 4040                                                           
CONECT 4040 4039 4041                                                           
CONECT 4041 4040 4042                                                           
CONECT 4042 4041 4043                                                           
CONECT 4043 4042                                                                
MASTER      386    0   16   22    6    0    0    6 4060    1  231   43          
END