mCSM-lig

Predicted Affinity Change:

-2.056 log(affinity fold change) - Destabilizing

Mutation information:

Wild-type: D
Position: 30
Mutant-type: N
Chain: A
Ligand ID: 065
Distance to ligand: 2.814 Å
DUET stability change: -0.087 Kcal/mol

Example

PDB file used: 2Z4O.

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HEADER    HYDROLASE                               20-JUN-07   2Z4O              
TITLE     WILD TYPE HIV-1 PROTEASE WITH POTENT ANTIVIRAL INHIBITOR              
TITLE    2 GRL-98065                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEASE;                                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.4.23.16;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE   3 ORGANISM_TAXID: 11676;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET11A                                    
KEYWDS    HIV-1, WILD TYPE PROTEASE, PROTEASE INHIBITOR, HYDROLASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.F.WANG,Y.TIE,P.I.BOROSS,J.TOZSER,A.K.GHOSH,R.W.HARRISON,            
AUTHOR   2 I.T.WEBER                                                            
REVDAT   2   24-FEB-09 2Z4O    1       VERSN                                    
REVDAT   1   22-APR-08 2Z4O    0                                                
JRNL        AUTH   Y.F.WANG,Y.TIE,P.I.BOROSS,J.TOZSER,A.K.GHOSH,                
JRNL        AUTH 2 R.W.HARRISON,I.T.WEBER                                       
JRNL        TITL   POTENT NEW ANTIVIRAL COMPOUND SHOWS SIMILAR                  
JRNL        TITL 2 INHIBITION AND STRUCTURAL INTERACTIONS WITH DRUG             
JRNL        TITL 3 RESISTANT MUTANTS AND WILD TYPE HIV-1 PROTEASE.              
JRNL        REF    J.MED.CHEM.                   V.  50  4509 2007              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   17696515                                                     
JRNL        DOI    10.1021/JM070482Q                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.147                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.144                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.205                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 1553                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 30875                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.133                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.129                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.193                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 1343                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 26355                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1605                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 87                                            
REMARK   3   SOLVENT ATOMS      : 238                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1761.28                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 1631.00                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 22                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 17401                   
REMARK   3   NUMBER OF RESTRAINTS                     : 22495                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.009                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.029                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.027                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.014                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.025                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.011                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.002                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.033                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.079                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2Z4O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JUN-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB027516.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X26C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9561                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : DOUBLY FOCUSING TOROIDAL           
REMARK 200                                   MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31020                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1FG6                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM SODIUM ACETATE, 10% (W/V)           
REMARK 280  SODIUM CHLORIDE, 6% DIOXANE, 10% (V/V) DIMETHYLSULFOXIDE            
REMARK 280  (DMSO), PH 4.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       29.12500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.91600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.12500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.91600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9400 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  41   CD  -  NE  -  CZ  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    ARG A  41   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG A  57   CD  -  NE  -  CZ  ANGL. DEV. =  13.8 DEGREES          
REMARK 500    ARG B 141   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG B 187   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 500  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  60   O                                                      
REMARK 620 2 HOH A 532   O   172.1                                              
REMARK 620 3 HOH A 510   O    92.8  89.8                                        
REMARK 620 4 HOH A 515   O   101.9  86.0  74.3                                  
REMARK 620 5 HOH A 522   O    78.5  99.2 170.9 104.7                            
REMARK 620 6 HOH A 530   O    95.8  76.8  87.3 154.9  96.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 500                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 502                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 802                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 065 B 404                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2QCI   RELATED DB: PDB                                   
REMARK 900 MUTANT D30N WITH THE SAME INHIBITOR                                  
REMARK 900 RELATED ID: 2QD6   RELATED DB: PDB                                   
REMARK 900 MUTANT I50V WITH THE SAME INHIBITOR                                  
REMARK 900 RELATED ID: 2QD7   RELATED DB: PDB                                   
REMARK 900 MUTANT V82A WITH THE SAME INHIBITOR                                  
REMARK 900 RELATED ID: 2QD8   RELATED DB: PDB                                   
REMARK 900 MUTANT I84V WITH THE SAME INHIBITOR                                  
DBREF  2Z4O A    1    99  UNP    P03367   POL_HV1BR      501    599             
DBREF  2Z4O B  101   199  UNP    P03367   POL_HV1BR      501    599             
SEQADV 2Z4O LYS A    7  UNP  P03367    GLN   507 ENGINEERED                     
SEQADV 2Z4O ILE A   33  UNP  P03367    LEU   533 ENGINEERED                     
SEQADV 2Z4O ILE A   63  UNP  P03367    LEU   563 ENGINEERED                     
SEQADV 2Z4O ALA A   67  UNP  P03367    CYS   567 ENGINEERED                     
SEQADV 2Z4O ALA A   95  UNP  P03367    CYS   595 ENGINEERED                     
SEQADV 2Z4O LYS B  107  UNP  P03367    GLN   507 ENGINEERED                     
SEQADV 2Z4O ILE B  133  UNP  P03367    LEU   533 ENGINEERED                     
SEQADV 2Z4O ILE B  163  UNP  P03367    LEU   563 ENGINEERED                     
SEQADV 2Z4O ALA B  167  UNP  P03367    CYS   567 ENGINEERED                     
SEQADV 2Z4O ALA B  195  UNP  P03367    CYS   595 ENGINEERED                     
SEQRES   1 A   99  PRO GLN ILE THR LEU TRP LYS ARG PRO LEU VAL THR ILE          
SEQRES   2 A   99  LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR          
SEQRES   3 A   99  GLY ALA ASP ASP THR VAL ILE GLU GLU MET SER LEU PRO          
SEQRES   4 A   99  GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY          
SEQRES   5 A   99  PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE ILE ILE GLU          
SEQRES   6 A   99  ILE ALA GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY          
SEQRES   7 A   99  PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR          
SEQRES   8 A   99  GLN ILE GLY ALA THR LEU ASN PHE                              
SEQRES   1 B   99  PRO GLN ILE THR LEU TRP LYS ARG PRO LEU VAL THR ILE          
SEQRES   2 B   99  LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR          
SEQRES   3 B   99  GLY ALA ASP ASP THR VAL ILE GLU GLU MET SER LEU PRO          
SEQRES   4 B   99  GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY          
SEQRES   5 B   99  PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE ILE ILE GLU          
SEQRES   6 B   99  ILE ALA GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY          
SEQRES   7 B   99  PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR          
SEQRES   8 B   99  GLN ILE GLY ALA THR LEU ASN PHE                              
HET     NA  A 500       1                                                       
HET     CL  A 502       1                                                       
HET     CL  B 501       1                                                       
HET    ACT  B 802       4                                                       
HET    065  B 404      80                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ACT ACETATE ION                                                      
HETNAM     065 (3R,3AS,6AR)-HEXAHYDROFURO[2,3-B]FURAN-3-YL(2S,3R)-3-            
HETNAM   2 065  HYDROXY-4-(N-ISOBUTYLBENZO[D][1,3]DIOXOLE-5-                    
HETNAM   3 065  SULFONAMIDO)-1-PHENYLBUTAN-2-YLCARBAMATE                        
HETSYN     065 RL-98065, [(1R,5S,6R)-2,8-DIOXABICYCLO[3.3.0]OCT-6-              
HETSYN   2 065  YL]N-[(2S,3R)-4-[(3,4-METHYLENEDIOXYPHENYL)SULFONYL-            
HETSYN   3 065  (2-METHYLPROPYL)AMINO]-3-HYDROXY-1-PHENYL-BUTAN-2-YL]           
HETSYN   4 065  CARBAMATE                                                       
FORMUL   3   NA    NA 1+                                                        
FORMUL   4   CL    2(CL 1-)                                                     
FORMUL   6  ACT    C2 H3 O2 1-                                                  
FORMUL   7  065    C28 H36 N2 O9 S                                              
FORMUL   8  HOH   *238(H2 O)                                                    
HELIX    1   1 GLY A   86  THR A   91  1                                   6    
HELIX    2   2 GLY B  186  THR B  191  1                                   6    
SHEET    1   A 4 GLN A   2  ILE A   3  0                                        
SHEET    2   A 4 THR B 196  ASN B 198 -1  O  LEU B 197   N  ILE A   3           
SHEET    3   A 4 THR A  96  ASN A  98 -1  N  THR A  96   O  ASN B 198           
SHEET    4   A 4 GLN B 102  ILE B 103 -1  O  ILE B 103   N  LEU A  97           
SHEET    1   B 8 TRP A  42  GLY A  49  0                                        
SHEET    2   B 8 GLY A  52  ILE A  66 -1  O  VAL A  56   N  LYS A  45           
SHEET    3   B 8 HIS A  69  VAL A  77 -1  O  HIS A  69   N  ILE A  66           
SHEET    4   B 8 VAL A  32  ILE A  33  1  N  ILE A  33   O  LEU A  76           
SHEET    5   B 8 ILE A  84  ILE A  85 -1  O  ILE A  84   N  VAL A  32           
SHEET    6   B 8 GLN A  18  LEU A  24  1  N  LEU A  23   O  ILE A  85           
SHEET    7   B 8 LEU A  10  ILE A  15 -1  N  ILE A  13   O  LYS A  20           
SHEET    8   B 8 GLY A  52  ILE A  66 -1  O  GLU A  65   N  LYS A  14           
SHEET    1   C 8 LYS B 143  GLY B 149  0                                        
SHEET    2   C 8 GLY B 152  ILE B 166 -1  O  GLN B 158   N  LYS B 143           
SHEET    3   C 8 HIS B 169  VAL B 177 -1  O  HIS B 169   N  ILE B 166           
SHEET    4   C 8 VAL B 132  ILE B 133  1  N  ILE B 133   O  LEU B 176           
SHEET    5   C 8 ILE B 184  ILE B 185 -1  O  ILE B 184   N  VAL B 132           
SHEET    6   C 8 GLN B 118  LEU B 124  1  N  LEU B 123   O  ILE B 185           
SHEET    7   C 8 LEU B 110  ILE B 115 -1  N  ILE B 113   O  LYS B 120           
SHEET    8   C 8 GLY B 152  ILE B 166 -1  O  GLU B 165   N  LYS B 114           
LINK         O   ASP A  60                NA    NA A 500     1555   1555  2.44  
LINK        NA    NA A 500                 O   HOH A 532     1555   1555  2.59  
LINK        NA    NA A 500                 O   HOH A 510     1555   1555  2.27  
LINK        NA    NA A 500                 O   HOH A 515     1555   1555  2.31  
LINK        NA    NA A 500                 O   HOH A 522     1555   1555  2.51  
LINK        NA    NA A 500                 O   HOH A 530     1555   1555  2.34  
SITE     1 AC1  6 ASP A  60  HOH A 510  HOH A 515  HOH A 522                    
SITE     2 AC1  6 HOH A 530  HOH A 532                                          
SITE     1 AC2  5 THR A  74  ASN A  88  HOH A 566  HOH A 595                    
SITE     2 AC2  5 ARG B 141                                                     
SITE     1 AC3  7 PRO B 139  GLY B 140  ARG B 141  TYR B 159                    
SITE     2 AC3  7 ASP B 160  HOH B 857  HOH B 920                               
SITE     1 AC4 26 LEU A  23  ASP A  25  GLY A  27  ALA A  28                    
SITE     2 AC4 26 ASP A  29  ASP A  30  GLY A  48  GLY A  49                    
SITE     3 AC4 26 ILE A  50  PRO A  81  ILE A  84  ARG B 108                    
SITE     4 AC4 26 ASP B 125  GLY B 127  ALA B 128  ASP B 129                    
SITE     5 AC4 26 ASP B 130  GLY B 148  GLY B 149  ILE B 150                    
SITE     6 AC4 26 PRO B 181  ILE B 184  HOH B 811  HOH B 820                    
SITE     7 AC4 26 HOH B 907  HOH B 921                                          
CRYST1   58.250   85.832   45.967  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017167  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011651  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021755        0.00000                         
ATOM      1  N   PRO A   1       0.563  39.396  17.364  1.00 34.08           N  
ANISOU    1  N   PRO A   1     3702   5197   4048   -207    -17   1643       N  
ATOM      2  CA  PRO A   1      -0.408  38.506  18.009  1.00 31.55           C  
ANISOU    2  CA  PRO A   1     3279   4688   4022     42   -196   1511       C  
ATOM      3  C   PRO A   1       0.141  37.898  19.291  1.00 26.84           C  
ANISOU    3  C   PRO A   1     2787   3585   3826    643    178   1014       C  
ATOM      4  O   PRO A   1       1.310  38.099  19.592  1.00 24.63           O  
ANISOU    4  O   PRO A   1     2791   3116   3452    462    369   1111       O  
ATOM      5  CB  PRO A   1      -0.610  37.402  16.958  1.00 33.29           C  
ANISOU    5  CB  PRO A   1     3626   5192   3831    -58    -90   1328       C  
ATOM      6  CG  PRO A   1       0.716  37.339  16.260  1.00 35.73           C  
ANISOU    6  CG  PRO A   1     3916   5599   4060   -255    264   1263       C  
ATOM      7  CD  PRO A   1       1.098  38.797  16.116  1.00 36.44           C  
ANISOU    7  CD  PRO A   1     3992   5650   4205   -324    172   1409       C  
ATOM      8  N   GLN A   2      -0.703  37.177  20.010  1.00 22.39           N  
ANISOU    8  N   GLN A   2     2209   2628   3669    969     17    631       N  
ATOM      9  CA  GLN A   2      -0.306  36.297  21.097  1.00 22.17           C  
ANISOU    9  CA  GLN A   2     2608   2286   3531    805   -114    405       C  
ATOM     10  C   GLN A   2      -0.502  34.867  20.596  1.00 22.17           C  
ANISOU   10  C   GLN A   2     2429   2413   3583    670   -229    311       C  
ATOM     11  O   GLN A   2      -1.601  34.428  20.261  1.00 24.37           O  
ANISOU   11  O   GLN A   2     2656   3148   3456    903   -891   -204       O  
ATOM     12  CB  GLN A   2      -1.091  36.481  22.378  1.00 24.07           C  
ANISOU   12  CB  GLN A   2     3212   2304   3630    534    177    399       C  
ATOM     13  CG  GLN A   2      -0.754  35.457  23.454  1.00 24.61           C  
ANISOU   13  CG  GLN A   2     3435   2430   3484    752     78    295       C  
ATOM     14  CD  GLN A   2      -1.391  35.862  24.781  1.00 26.45           C  
ANISOU   14  CD  GLN A   2     3461   2922   3666    196    529    309       C  
ATOM     15  OE1 GLN A   2      -2.416  35.335  25.198  1.00 30.36           O  
ANISOU   15  OE1 GLN A   2     3687   3495   4353   -360    594     84       O  
ATOM     16  NE2 GLN A   2      -0.717  36.826  25.400  1.00 26.71           N  
ANISOU   16  NE2 GLN A   2     3485   2678   3984     11   1651   -196       N  
ATOM     17  N   ILE A   3       0.602  34.163  20.552  1.00 20.88           N  
ANISOU   17  N   ILE A   3     2337   2313   3283    557     92     94       N  
ATOM     18  CA  ILE A   3       0.610  32.798  20.019  1.00 21.88           C  
ANISOU   18  CA  ILE A   3     2807   2203   3302    431    -34    249       C  
ATOM     19  C   ILE A   3       0.800  31.785  21.123  1.00 21.17           C  
ANISOU   19  C   ILE A   3     2114   2432   3500    301   -144    464       C  
ATOM     20  O   ILE A   3       1.809  31.806  21.818  1.00 19.27           O  
ANISOU   20  O   ILE A   3     1804   2409   3107    604    219    -94       O  
ATOM     21  CB  ILE A   3       1.721  32.705  18.968  1.00 22.24           C  
ANISOU   21  CB  ILE A   3     3375   1948   3126    439    136    -32       C  
ATOM     22  CG1 ILE A   3       1.448  33.701  17.832  1.00 22.74           C  
ANISOU   22  CG1 ILE A   3     3914   1538   3189    195    182    -86       C  
ATOM     23  CG2 ILE A   3       1.918  31.302  18.452  1.00 23.22           C  
ANISOU   23  CG2 ILE A   3     3733   1918   3171    884   -585     33       C  
ATOM     24  CD1 ILE A   3       2.692  34.060  17.055  1.00 30.98           C  
ANISOU   24  CD1 ILE A   3     4597   3903   3271   -942    339    120       C  
ATOM     25  N   THR A   4      -0.175  30.901  21.289  1.00 20.66           N  
ANISOU   25  N   THR A   4     1855   2526   3469    408     82    338       N  
ATOM     26  CA  THR A   4      -0.027  29.909  22.340  1.00 19.89           C  
ANISOU   26  CA  THR A   4     1771   2494   3292    170     32    237       C  
ATOM     27  C   THR A   4       0.853  28.803  21.796  1.00 17.18           C  
ANISOU   27  C   THR A   4     1738   2228   2560    -11   -149    246       C  
ATOM     28  O   THR A   4       1.204  28.767  20.617  1.00 18.27           O  
ANISOU   28  O   THR A   4     2569   2103   2270    -46   -530    106       O  
ATOM     29  CB  THR A   4      -1.344  29.283  22.810  1.00 23.44           C  
ANISOU   29  CB  THR A   4     2040   3087   3778     -6    464    212       C  
ATOM     30  OG1 THR A   4      -1.993  28.731  21.659  1.00 29.36           O  
ANISOU   30  OG1 THR A   4     2316   3850   4988   -592    -41   -404       O  
ATOM     31  CG2 THR A   4      -2.273  30.328  23.414  1.00 28.40           C  
ANISOU   31  CG2 THR A   4     2028   4325   4438    660    384    -42       C  
ATOM     32  N   LEU A   5       1.186  27.906  22.694  1.00 15.60           N  
ANISOU   32  N   LEU A   5     1514   2161   2253   -203    -70    134       N  
ATOM     33  CA  LEU A   5       2.183  26.918  22.290  1.00 13.91           C  
ANISOU   33  CA  LEU A   5     1519   2093   1671   -210   -114    187       C  
ATOM     34  C   LEU A   5       1.656  25.504  22.348  1.00 13.62           C  
ANISOU   34  C   LEU A   5     1408   2096   1669   -161   -196    389       C  
ATOM     35  O   LEU A   5       2.405  24.531  22.399  1.00 14.15           O  
ANISOU   35  O   LEU A   5     1748   2179   1450     50      1    627       O  
ATOM     36  CB  LEU A   5       3.417  27.140  23.183  1.00 13.35           C  
ANISOU   36  CB  LEU A   5     1559   2059   1454   -292    -86    397       C  
ATOM     37  CG  LEU A   5       4.178  28.452  22.939  1.00 12.87           C  
ANISOU   37  CG  LEU A   5     1421   2083   1384   -265    162    332       C  
ATOM     38  CD1 LEU A   5       5.245  28.651  24.001  1.00 14.52           C  
ANISOU   38  CD1 LEU A   5     1480   2510   1528   -397    197   -156       C  
ATOM     39  CD2 LEU A   5       4.781  28.473  21.549  1.00 14.91           C  
ANISOU   39  CD2 LEU A   5     2019   2258   1387    -11    258    507       C  
ATOM     40  N   TRP A   6       0.333  25.394  22.324  1.00 14.68           N  
ANISOU   40  N   TRP A   6     1436   2261   1879   -241     40    182       N  
ATOM     41  CA  TRP A   6      -0.294  24.095  22.198  1.00 15.31           C  
ANISOU   41  CA  TRP A   6     1566   2267   1984   -324     78    174       C  
ATOM     42  C   TRP A   6       0.140  23.386  20.922  1.00 15.21           C  
ANISOU   42  C   TRP A   6     1779   2104   1895   -362    133    293       C  
ATOM     43  O   TRP A   6       0.251  22.157  20.870  1.00 17.05           O  
ANISOU   43  O   TRP A   6     2584   2161   1735   -170    384    448       O  
ATOM     44  CB  TRP A   6      -1.807  24.231  22.178  1.00 15.62           C  
ANISOU   44  CB  TRP A   6     1570   2376   1990   -370   -104    -89       C  
ATOM     45  CG  TRP A   6      -2.436  24.757  23.421  1.00 17.35           C  
ANISOU   45  CG  TRP A   6     1764   2699   2128   -151    200     98       C  
ATOM     46  CD1 TRP A   6      -3.131  25.934  23.493  1.00 20.17           C  
ANISOU   46  CD1 TRP A   6     2839   2688   2136    123    501    120       C  
ATOM     47  CD2 TRP A   6      -2.476  24.216  24.744  1.00 19.42           C  
ANISOU   47  CD2 TRP A   6     2321   3114   1944    305    -51    -18       C  
ATOM     48  NE1 TRP A   6      -3.597  26.161  24.762  1.00 22.89           N  
ANISOU   48  NE1 TRP A   6     3339   3189   2170    644    691    351       N  
ATOM     49  CE2 TRP A   6      -3.205  25.113  25.555  1.00 23.10           C  
ANISOU   49  CE2 TRP A   6     3270   3406   2101    871    361    241       C  
ATOM     50  CE3 TRP A   6      -1.976  23.064  25.351  1.00 19.70           C  
ANISOU   50  CE3 TRP A   6     2193   3400   1892    547     41     68       C  
ATOM     51  CZ2 TRP A   6      -3.436  24.889  26.912  1.00 24.86           C  
ANISOU   51  CZ2 TRP A   6     3676   3667   2104   1366    416    356       C  
ATOM     52  CZ3 TRP A   6      -2.209  22.852  26.691  1.00 22.00           C  
ANISOU   52  CZ3 TRP A   6     2858   3560   1941   1023    281    125       C  
ATOM     53  CH2 TRP A   6      -2.931  23.755  27.460  1.00 24.00           C  
ANISOU   53  CH2 TRP A   6     3445   3611   2061   1379    386    225       C  
ATOM     54  N   LYS A   7       0.376  24.165  19.884  1.00 14.48           N  
ANISOU   54  N   LYS A   7     1763   1917   1821   -473   -154    237       N  
ATOM     55  CA  LYS A   7       0.884  23.564  18.666  1.00 16.35           C  
ANISOU   55  CA  LYS A   7     1913   2642   1659   -568   -194    118       C  
ATOM     56  C   LYS A   7       2.122  24.313  18.220  1.00 14.54           C  
ANISOU   56  C   LYS A   7     1790   2015   1719   -224   -156    112       C  
ATOM     57  O   LYS A   7       2.502  25.304  18.810  1.00 14.25           O  
ANISOU   57  O   LYS A   7     1829   1914   1670   -158   -122    177       O  
ATOM     58  CB ALYS A   7      -0.171  23.610  17.564  0.51 19.51           C  
ANISOU   58  CB ALYS A   7     1937   3652   1824   -619   -271    196       C  
ATOM     59  CB BLYS A   7      -0.170  23.535  17.558  0.49 19.29           C  
ANISOU   59  CB BLYS A   7     1928   3594   1807   -590   -283    214       C  
ATOM     60  CG ALYS A   7      -1.609  23.448  18.042  0.51 21.99           C  
ANISOU   60  CG ALYS A   7     1941   4152   2263   -871   -269    258       C  
ATOM     61  CG BLYS A   7      -0.724  24.817  17.006  0.49 20.33           C  
ANISOU   61  CG BLYS A   7     1996   3871   1856   -346   -326    319       C  
ATOM     62  CD ALYS A   7      -2.127  22.070  17.651  0.51 26.20           C  
ANISOU   62  CD ALYS A   7     2491   4456   3006  -1288   -208    106       C  
ATOM     63  CD BLYS A   7      -1.771  24.530  15.924  0.49 22.57           C  
ANISOU   63  CD BLYS A   7     2251   4273   2054   -347   -534    260       C  
ATOM     64  CE ALYS A   7      -3.242  21.616  18.581  0.51 27.52           C  
ANISOU   64  CE ALYS A   7     2496   4705   3254  -1433   -265    413       C  
ATOM     65  CE BLYS A   7      -2.466  25.809  15.506  0.49 24.36           C  
ANISOU   65  CE BLYS A   7     2585   4582   2087   -216   -615    648       C  
ATOM     66  NZ ALYS A   7      -3.611  20.193  18.318  0.51 29.95           N  
ANISOU   66  NZ ALYS A   7     3127   4645   3610  -1586   -775    761       N  
ATOM     67  NZ BLYS A   7      -3.619  25.515  14.603  0.49 29.38           N  
ANISOU   67  NZ BLYS A   7     3224   5170   2771   -364  -1303    914       N  
ATOM     68  N   ARG A   8       2.752  23.828  17.162  1.00 15.26           N  
ANISOU   68  N   ARG A   8     2086   1926   1785   -335     11    149       N  
ATOM     69  CA  ARG A   8       3.957  24.489  16.678  1.00 14.42           C  
ANISOU   69  CA  ARG A   8     2014   1802   1665   -372    -54    -69       C  
ATOM     70  C   ARG A   8       3.646  25.924  16.255  1.00 13.42           C  
ANISOU   70  C   ARG A   8     1778   1820   1500   -274   -140    -22       C  
ATOM     71  O   ARG A   8       2.632  26.042  15.542  1.00 17.05           O  
ANISOU   71  O   ARG A   8     1774   2590   2114   -815   -370    725       O  
ATOM     72  CB AARG A   8       4.562  23.714  15.514  0.60 14.06           C  
ANISOU   72  CB AARG A   8     2017   1744   1584   -294   -135    -26       C  
ATOM     73  CB BARG A   8       4.566  23.722  15.509  0.40 14.24           C  
ANISOU   73  CB BARG A   8     2113   1729   1567   -288    -99      4       C  
ATOM     74  CG AARG A   8       5.077  22.324  15.848  0.60 14.94           C  
ANISOU   74  CG AARG A   8     2400   1711   1565   -295   -179    -20       C  
ATOM     75  CG BARG A   8       5.295  22.455  15.911  0.40 15.21           C  
ANISOU   75  CG BARG A   8     2465   1717   1596   -212   -179    -13       C  
ATOM     76  CD AARG A   8       6.016  21.837  14.749  0.60 15.79           C  
ANISOU   76  CD AARG A   8     2588   1759   1653    -48   -170    -59       C  
ATOM     77  CD BARG A   8       5.378  21.471  14.747  0.40 15.68           C  
ANISOU   77  CD BARG A   8     2579   1831   1548    -50   -210    -12       C  
ATOM     78  NE AARG A   8       6.678  20.597  15.150  0.60 16.77           N  
ANISOU   78  NE AARG A   8     2839   1982   1551    114   -330      8       N  
ATOM     79  NE BARG A   8       5.908  20.211  15.275  0.40 16.02           N  
ANISOU   79  NE BARG A   8     2773   1890   1424    111   -381   -119       N  
ATOM     80  CZ AARG A   8       7.676  20.088  14.439  0.60 16.73           C  
ANISOU   80  CZ AARG A   8     2861   2031   1463    318   -460     83       C  
ATOM     81  CZ BARG A   8       5.951  19.104  14.553  0.40 16.23           C  
ANISOU   81  CZ BARG A   8     2922   1989   1254    220   -619   -159       C  
ATOM     82  NH1AARG A   8       8.259  18.968  14.816  0.60 20.35           N  
ANISOU   82  NH1AARG A   8     3221   2442   2068    717  -1427   -133       N  
ATOM     83  NH1BARG A   8       6.442  18.011  15.094  0.40 17.39           N  
ANISOU   83  NH1BARG A   8     3004   2246   1357    815  -1087   -647       N  
ATOM     84  NH2AARG A   8       8.095  20.699  13.342  0.60 18.36           N  
ANISOU   84  NH2AARG A   8     3125   2902    948   -101   -589   -168       N  
ATOM     85  NH2BARG A   8       5.502  19.118  13.308  0.40 20.89           N  
ANISOU   85  NH2BARG A   8     4007   2692   1238    849   -811   -204       N  
ATOM     86  N   PRO A   9       4.409  26.932  16.642  1.00 13.54           N  
ANISOU   86  N   PRO A   9     1775   1812   1558   -230   -195     17       N  
ATOM     87  CA  PRO A   9       4.165  28.331  16.250  1.00 13.74           C  
ANISOU   87  CA  PRO A   9     1831   1774   1617   -251    -36     20       C  
ATOM     88  C   PRO A   9       4.724  28.615  14.867  1.00 14.10           C  
ANISOU   88  C   PRO A   9     1958   1829   1571   -196    -77     34       C  
ATOM     89  O   PRO A   9       5.751  29.248  14.634  1.00 13.14           O  
ANISOU   89  O   PRO A   9     1569   2082   1341     13   -212     99       O  
ATOM     90  CB  PRO A   9       4.930  29.145  17.272  1.00 13.62           C  
ANISOU   90  CB  PRO A   9     1761   1860   1554   -284    207   -106       C  
ATOM     91  CG  PRO A   9       6.087  28.275  17.625  1.00 14.43           C  
ANISOU   91  CG  PRO A   9     2067   1754   1663   -303   -223    -80       C  
ATOM     92  CD  PRO A   9       5.587  26.849  17.525  1.00 14.89           C  
ANISOU   92  CD  PRO A   9     2096   1849   1715   -342   -432    -47       C  
ATOM     93  N   LEU A  10       3.967  28.089  13.921  1.00 14.26           N  
ANISOU   93  N   LEU A  10     1924   1922   1572   -415   -120    318       N  
ATOM     94  CA  LEU A  10       4.265  28.262  12.521  1.00 15.42           C  
ANISOU   94  CA  LEU A  10     2197   2168   1494    221   -141    177       C  
ATOM     95  C   LEU A  10       3.686  29.545  11.987  1.00 14.80           C  
ANISOU   95  C   LEU A  10     1854   2383   1386    424    245    322       C  
ATOM     96  O   LEU A  10       2.562  29.928  12.351  1.00 16.31           O  
ANISOU   96  O   LEU A  10     1678   3109   1409    392    233    579       O  
ATOM     97  CB  LEU A  10       3.680  27.058  11.775  1.00 18.21           C  
ANISOU   97  CB  LEU A  10     2739   2410   1768     89   -415     25       C  
ATOM     98  CG  LEU A  10       4.329  25.698  12.021  1.00 20.19           C  
ANISOU   98  CG  LEU A  10     3016   2219   2437      4   -581    -18       C  
ATOM     99  CD1 LEU A  10       3.606  24.599  11.254  1.00 23.95           C  
ANISOU   99  CD1 LEU A  10     3332   2373   3396  -1125      3    103       C  
ATOM    100  CD2 LEU A  10       5.801  25.724  11.637  1.00 22.00           C  
ANISOU  100  CD2 LEU A  10     2559   2596   3205     93  -1371   -224       C  
ATOM    101  N   VAL A  11       4.437  30.204  11.137  1.00 14.63           N  
ANISOU  101  N   VAL A  11     1653   2520   1385    578    258    406       N  
ATOM    102  CA  VAL A  11       3.902  31.383  10.483  1.00 15.16           C  
ANISOU  102  CA  VAL A  11     1963   2446   1352    478     44    391       C  
ATOM    103  C   VAL A  11       4.338  31.414   9.032  1.00 15.77           C  
ANISOU  103  C   VAL A  11     2143   2458   1390    715     54    424       C  
ATOM    104  O   VAL A  11       5.243  30.705   8.616  1.00 14.73           O  
ANISOU  104  O   VAL A  11     2342   1883   1374    498     45    193       O  
ATOM    105  CB  VAL A  11       4.369  32.686  11.139  1.00 16.15           C  
ANISOU  105  CB  VAL A  11     2412   2492   1233    115     99    565       C  
ATOM    106  CG1 VAL A  11       3.913  32.779  12.582  1.00 19.93           C  
ANISOU  106  CG1 VAL A  11     2997   3081   1494    142    486     74       C  
ATOM    107  CG2 VAL A  11       5.884  32.759  11.045  1.00 18.72           C  
ANISOU  107  CG2 VAL A  11     2400   3638   1074     -2    -65   -246       C  
ATOM    108  N   THR A  12       3.638  32.276   8.296  1.00 16.03           N  
ANISOU  108  N   THR A  12     2194   2364   1534    552     94    631       N  
ATOM    109  CA  THR A  12       4.028  32.484   6.910  1.00 16.96           C  
ANISOU  109  CA  THR A  12     2410   2646   1387    258    -76    525       C  
ATOM    110  C   THR A  12       5.093  33.575   6.818  1.00 16.29           C  
ANISOU  110  C   THR A  12     2409   2424   1357    353     42    519       C  
ATOM    111  O   THR A  12       5.027  34.641   7.422  1.00 17.32           O  
ANISOU  111  O   THR A  12     2270   2619   1694    364    160    248       O  
ATOM    112  CB  THR A  12       2.821  32.859   6.046  1.00 19.86           C  
ANISOU  112  CB  THR A  12     2512   3437   1596    185   -228    669       C  
ATOM    113  OG1 THR A  12       1.844  31.820   6.144  1.00 22.12           O  
ANISOU  113  OG1 THR A  12     3014   3414   1976   -113   -816    603       O  
ATOM    114  CG2 THR A  12       3.246  32.954   4.589  1.00 23.99           C  
ANISOU  114  CG2 THR A  12     2681   4947   1486    479   -359    599       C  
ATOM    115  N   ILE A  13       6.112  33.279   6.026  1.00 16.65           N  
ANISOU  115  N   ILE A  13     2528   2341   1458    297    125    353       N  
ATOM    116  CA  ILE A  13       7.146  34.252   5.738  1.00 15.97           C  
ANISOU  116  CA  ILE A  13     2373   2399   1295    396     77    381       C  
ATOM    117  C   ILE A  13       7.269  34.484   4.238  1.00 15.69           C  
ANISOU  117  C   ILE A  13     2576   2173   1214    127   -218    307       C  
ATOM    118  O   ILE A  13       6.911  33.640   3.414  1.00 17.11           O  
ANISOU  118  O   ILE A  13     2682   2297   1522    -18   -251    154       O  
ATOM    119  CB  ILE A  13       8.494  33.768   6.322  1.00 16.39           C  
ANISOU  119  CB  ILE A  13     2565   2381   1283    393   -181    350       C  
ATOM    120  CG1 ILE A  13       9.068  32.586   5.558  1.00 16.82           C  
ANISOU  120  CG1 ILE A  13     2574   2273   1545    499   -212    402       C  
ATOM    121  CG2 ILE A  13       8.338  33.479   7.801  1.00 16.09           C  
ANISOU  121  CG2 ILE A  13     2657   1856   1602    824    291    899       C  
ATOM    122  CD1 ILE A  13      10.496  32.174   5.885  1.00 16.06           C  
ANISOU  122  CD1 ILE A  13     2315   2464   1324    213    -50    288       C  
ATOM    123  N   LYS A  14       7.787  35.637   3.875  1.00 15.02           N  
ANISOU  123  N   LYS A  14     2454   2087   1165    211   -191    260       N  
ATOM    124  CA  LYS A  14       8.178  35.911   2.508  1.00 16.18           C  
ANISOU  124  CA  LYS A  14     2477   2289   1382    320     89    340       C  
ATOM    125  C   LYS A  14       9.691  36.198   2.520  1.00 16.51           C  
ANISOU  125  C   LYS A  14     2535   2134   1604    252    133     43       C  
ATOM    126  O   LYS A  14      10.152  37.069   3.229  1.00 15.98           O  
ANISOU  126  O   LYS A  14     2752   1797   1522     39    352    255       O  
ATOM    127  CB  LYS A  14       7.429  37.066   1.873  1.00 20.21           C  
ANISOU  127  CB  LYS A  14     2938   2901   1841    403   -199    982       C  
ATOM    128  CG  LYS A  14       7.736  37.248   0.373  1.00 24.97           C  
ANISOU  128  CG  LYS A  14     3506   3909   2071    429    153   1414       C  
ATOM    129  CD  LYS A  14       6.698  38.151  -0.282  1.00 29.24           C  
ANISOU  129  CD  LYS A  14     4261   4466   2383    595    -47   2073       C  
ATOM    130  CE  LYS A  14       6.466  37.659  -1.709  1.00 33.26           C  
ANISOU  130  CE  LYS A  14     4832   5368   2435    974   -323   1918       C  
ATOM    131  NZ  LYS A  14       5.734  38.616  -2.584  1.00 42.32           N  
ANISOU  131  NZ  LYS A  14     5739   7033   3307   2181  -1359   1728       N  
ATOM    132  N   ILE A  15      10.390  35.408   1.701  1.00 15.37           N  
ANISOU  132  N   ILE A  15     2495   1966   1378    257    128    266       N  
ATOM    133  CA  ILE A  15      11.826  35.464   1.568  1.00 15.25           C  
ANISOU  133  CA  ILE A  15     2488   1939   1368    297    104    433       C  
ATOM    134  C   ILE A  15      12.184  35.154   0.120  1.00 15.72           C  
ANISOU  134  C   ILE A  15     2393   2185   1393     54    148    393       C  
ATOM    135  O   ILE A  15      11.741  34.167  -0.432  1.00 16.08           O  
ANISOU  135  O   ILE A  15     2119   2620   1370    -99    -25    224       O  
ATOM    136  CB  ILE A  15      12.566  34.480   2.487  1.00 16.04           C  
ANISOU  136  CB  ILE A  15     2652   1958   1486    373     54    421       C  
ATOM    137  CG1 ILE A  15      14.081  34.583   2.323  1.00 17.77           C  
ANISOU  137  CG1 ILE A  15     2615   2269   1869    508     53    581       C  
ATOM    138  CG2 ILE A  15      12.109  33.041   2.299  1.00 17.30           C  
ANISOU  138  CG2 ILE A  15     2976   1885   1713    413    294    415       C  
ATOM    139  CD1 ILE A  15      14.855  33.811   3.355  1.00 21.39           C  
ANISOU  139  CD1 ILE A  15     3092   3690   1346   1198    -73    329       C  
ATOM    140  N   GLY A  16      12.992  36.038  -0.454  1.00 17.14           N  
ANISOU  140  N   GLY A  16     2506   2511   1496   -142    130    479       N  
ATOM    141  CA  GLY A  16      13.487  35.762  -1.791  1.00 18.87           C  
ANISOU  141  CA  GLY A  16     2910   2806   1453   -488    236    398       C  
ATOM    142  C   GLY A  16      12.360  35.719  -2.797  1.00 19.63           C  
ANISOU  142  C   GLY A  16     3185   2783   1492   -527     69    457       C  
ATOM    143  O   GLY A  16      12.530  35.046  -3.823  1.00 23.29           O  
ANISOU  143  O   GLY A  16     3749   3558   1542   -141    -88    156       O  
ATOM    144  N   GLY A  17      11.263  36.407  -2.514  1.00 19.30           N  
ANISOU  144  N   GLY A  17     3486   2370   1479   -253   -345    542       N  
ATOM    145  CA  GLY A  17      10.087  36.422  -3.366  1.00 21.33           C  
ANISOU  145  CA  GLY A  17     3741   2626   1737   -136   -608    428       C  
ATOM    146  C   GLY A  17       9.235  35.182  -3.237  1.00 21.79           C  
ANISOU  146  C   GLY A  17     3576   2733   1971   -154   -909    494       C  
ATOM    147  O   GLY A  17       8.328  34.918  -3.996  1.00 28.48           O  
ANISOU  147  O   GLY A  17     3809   3563   3449   -525  -1753   1206       O  
ATOM    148  N   GLN A  18       9.487  34.342  -2.254  1.00 20.09           N  
ANISOU  148  N   GLN A  18     3340   2302   1992    157   -586    334       N  
ATOM    149  CA  GLN A  18       8.802  33.100  -2.024  1.00 18.66           C  
ANISOU  149  CA  GLN A  18     3162   2234   1695    149   -233   -122       C  
ATOM    150  C   GLN A  18       8.048  33.103  -0.705  1.00 18.78           C  
ANISOU  150  C   GLN A  18     2999   2389   1745    317   -210   -234       C  
ATOM    151  O   GLN A  18       8.581  33.625   0.259  1.00 18.17           O  
ANISOU  151  O   GLN A  18     2779   2303   1823   -104    157   -290       O  
ATOM    152  CB  GLN A  18       9.770  31.894  -1.953  1.00 19.38           C  
ANISOU  152  CB  GLN A  18     3239   2062   2061     96    -92   -598       C  
ATOM    153  CG  GLN A  18      10.472  31.611  -3.260  1.00 23.49           C  
ANISOU  153  CG  GLN A  18     3797   3016   2111    348    -34   -830       C  
ATOM    154  CD  GLN A  18      11.352  30.371  -3.246  1.00 24.61           C  
ANISOU  154  CD  GLN A  18     4154   2989   2206    493    127  -1004       C  
ATOM    155  OE1 GLN A  18      12.457  30.392  -3.808  1.00 29.86           O  
ANISOU  155  OE1 GLN A  18     3420   4507   3417    658   -342  -1059       O  
ATOM    156  NE2 GLN A  18      10.932  29.282  -2.639  1.00 28.08           N  
ANISOU  156  NE2 GLN A  18     4968   2871   2830   -175  -1118   -788       N  
ATOM    157  N   LEU A  19       6.860  32.523  -0.687  1.00 18.50           N  
ANISOU  157  N   LEU A  19     3040   2884   1105    164   -575     47       N  
ATOM    158  CA  LEU A  19       6.144  32.293   0.551  1.00 19.02           C  
ANISOU  158  CA  LEU A  19     3026   3156   1045     40   -629    114       C  
ATOM    159  C   LEU A  19       6.530  30.937   1.114  1.00 18.54           C  
ANISOU  159  C   LEU A  19     3096   2804   1144   -228   -576    -42       C  
ATOM    160  O   LEU A  19       6.522  29.972   0.351  1.00 22.54           O  
ANISOU  160  O   LEU A  19     4551   2817   1196  -1027   -350    -49       O  
ATOM    161  CB  LEU A  19       4.643  32.380   0.310  1.00 22.08           C  
ANISOU  161  CB  LEU A  19     3001   4001   1385    164   -603     28       C  
ATOM    162  CG  LEU A  19       4.244  33.793  -0.158  1.00 25.75           C  
ANISOU  162  CG  LEU A  19     3509   4270   2005    426  -1489    123       C  
ATOM    163  CD1 LEU A  19       2.770  33.894  -0.560  1.00 34.27           C  
ANISOU  163  CD1 LEU A  19     3783   5778   3462    890  -2097   -238       C  
ATOM    164  CD2 LEU A  19       4.520  34.843   0.910  1.00 26.95           C  
ANISOU  164  CD2 LEU A  19     4540   3781   1919    238  -1489    405       C  
ATOM    165  N   LYS A  20       6.849  30.924   2.412  1.00 18.08           N  
ANISOU  165  N   LYS A  20     3154   2591   1124     73   -483     18       N  
ATOM    166  CA  LYS A  20       7.202  29.703   3.091  1.00 17.54           C  
ANISOU  166  CA  LYS A  20     2751   2592   1321    127   -381     29       C  
ATOM    167  C   LYS A  20       6.548  29.743   4.468  1.00 16.50           C  
ANISOU  167  C   LYS A  20     2383   2423   1462    -24   -290    153       C  
ATOM    168  O   LYS A  20       6.178  30.772   5.013  1.00 18.83           O  
ANISOU  168  O   LYS A  20     3048   2304   1801      5    504    400       O  
ATOM    169  CB  LYS A  20       8.711  29.537   3.219  1.00 17.88           C  
ANISOU  169  CB  LYS A  20     2698   2680   1414     62    -42     76       C  
ATOM    170  CG  LYS A  20       9.443  29.360   1.899  1.00 19.55           C  
ANISOU  170  CG  LYS A  20     3173   2746   1511   -206    152   -161       C  
ATOM    171  CD  LYS A  20      10.911  29.046   2.119  1.00 20.49           C  
ANISOU  171  CD  LYS A  20     3031   3099   1655   -335    393   -554       C  
ATOM    172  CE  LYS A  20      11.659  28.652   0.866  1.00 22.72           C  
ANISOU  172  CE  LYS A  20     3520   3301   1813   -428    661   -626       C  
ATOM    173  NZ  LYS A  20      11.328  27.287   0.355  1.00 26.00           N  
ANISOU  173  NZ  LYS A  20     4392   3782   1706   -911    737  -1015       N  
ATOM    174  N   GLU A  21       6.413  28.565   5.020  1.00 16.45           N  
ANISOU  174  N   GLU A  21     2405   2273   1573   -145   -412    -15       N  
ATOM    175  CA  GLU A  21       6.003  28.364   6.395  1.00 16.92           C  
ANISOU  175  CA  GLU A  21     2415   2461   1552   -259   -517    227       C  
ATOM    176  C   GLU A  21       7.255  28.174   7.247  1.00 15.20           C  
ANISOU  176  C   GLU A  21     1976   2291   1508   -226   -208     41       C  
ATOM    177  O   GLU A  21       8.161  27.450   6.851  1.00 15.90           O  
ANISOU  177  O   GLU A  21     2379   2378   1285    -81   -362   -313       O  
ATOM    178  CB AGLU A  21       5.068  27.174   6.559  0.56 18.78           C  
ANISOU  178  CB AGLU A  21     2499   2877   1759   -578  -1005    560       C  
ATOM    179  CB BGLU A  21       5.080  27.161   6.500  0.44 18.83           C  
ANISOU  179  CB BGLU A  21     2513   2865   1774   -576   -954    517       C  
ATOM    180  CG AGLU A  21       3.671  27.386   6.002  0.56 20.36           C  
ANISOU  180  CG AGLU A  21     2700   3018   2017   -369  -1296    298       C  
ATOM    181  CG BGLU A  21       4.776  26.563   7.847  0.44 20.18           C  
ANISOU  181  CG BGLU A  21     2722   3118   1827   -849   -791    496       C  
ATOM    182  CD AGLU A  21       3.022  28.704   6.352  0.56 24.56           C  
ANISOU  182  CD AGLU A  21     3142   3502   2689    103  -1349    -72       C  
ATOM    183  CD BGLU A  21       4.034  25.242   7.860  0.44 22.23           C  
ANISOU  183  CD BGLU A  21     2582   3663   2201  -1297   -891    654       C  
ATOM    184  OE1AGLU A  21       2.638  28.868   7.528  0.56 30.03           O  
ANISOU  184  OE1AGLU A  21     4171   4289   2951   -144  -1071   -844       O  
ATOM    185  OE1BGLU A  21       4.658  24.154   7.811  0.44 22.63           O  
ANISOU  185  OE1BGLU A  21     2657   3181   2759  -1652  -1174   1050       O  
ATOM    186  OE2AGLU A  21       2.902  29.553   5.447  0.56 27.80           O  
ANISOU  186  OE2AGLU A  21     3100   3634   3827    628  -1278    518       O  
ATOM    187  OE2BGLU A  21       2.783  25.266   7.927  0.44 26.24           O  
ANISOU  187  OE2BGLU A  21     2480   4839   2652  -1265  -1823    781       O  
ATOM    188  N   ALA A  22       7.311  28.814   8.409  1.00 12.80           N  
ANISOU  188  N   ALA A  22     1584   2023   1257    165    -76    317       N  
ATOM    189  CA  ALA A  22       8.482  28.723   9.246  1.00 11.32           C  
ANISOU  189  CA  ALA A  22     1559   1573   1170     70     19    344       C  
ATOM    190  C   ALA A  22       8.050  28.727  10.717  1.00 12.37           C  
ANISOU  190  C   ALA A  22     1855   1712   1134    120     82    139       C  
ATOM    191  O   ALA A  22       6.980  29.222  11.079  1.00 15.37           O  
ANISOU  191  O   ALA A  22     2096   2565   1180    641     95    335       O  
ATOM    192  CB  ALA A  22       9.452  29.844   8.911  1.00 12.42           C  
ANISOU  192  CB  ALA A  22     2021   1423   1273    -76   -171    388       C  
ATOM    193  N   LEU A  23       8.931  28.149  11.512  1.00 11.34           N  
ANISOU  193  N   LEU A  23     1537   1782    991     82    372    192       N  
ATOM    194  CA  LEU A  23       8.748  27.984  12.937  1.00 11.81           C  
ANISOU  194  CA  LEU A  23     1644   1827   1018    576    424    230       C  
ATOM    195  C   LEU A  23       9.324  29.158  13.691  1.00 13.34           C  
ANISOU  195  C   LEU A  23     1785   2343    939    273    260    116       C  
ATOM    196  O   LEU A  23      10.512  29.444  13.466  1.00 14.99           O  
ANISOU  196  O   LEU A  23     1941   2714   1040    128    515   -112       O  
ATOM    197  CB  LEU A  23       9.426  26.658  13.279  1.00 14.09           C  
ANISOU  197  CB  LEU A  23     1559   2325   1470    967    359    395       C  
ATOM    198  CG  LEU A  23       9.243  26.045  14.636  1.00 15.28           C  
ANISOU  198  CG  LEU A  23     1623   2324   1861    846    160    762       C  
ATOM    199  CD1 LEU A  23       7.792  25.688  14.856  1.00 18.05           C  
ANISOU  199  CD1 LEU A  23     1863   2435   2561    355    315   1067       C  
ATOM    200  CD2 LEU A  23      10.114  24.802  14.790  1.00 17.12           C  
ANISOU  200  CD2 LEU A  23     2304   1868   2334    830   -356    256       C  
ATOM    201  N   LEU A  24       8.554  29.824  14.542  1.00 11.54           N  
ANISOU  201  N   LEU A  24     1358   2142    885    114    -11     31       N  
ATOM    202  CA  LEU A  24       9.128  30.856  15.411  1.00 12.27           C  
ANISOU  202  CA  LEU A  24     1469   2047   1145    158   -135     62       C  
ATOM    203  C   LEU A  24       9.872  30.166  16.547  1.00 11.37           C  
ANISOU  203  C   LEU A  24     1480   1970    872     27    -36     76       C  
ATOM    204  O   LEU A  24       9.247  29.571  17.415  1.00 14.31           O  
ANISOU  204  O   LEU A  24     1575   2689   1174   -407   -102    295       O  
ATOM    205  CB  LEU A  24       8.068  31.792  15.951  1.00 13.49           C  
ANISOU  205  CB  LEU A  24     1785   2308   1033    390   -178    -79       C  
ATOM    206  CG  LEU A  24       7.224  32.543  14.916  1.00 14.79           C  
ANISOU  206  CG  LEU A  24     1862   2486   1272    524   -281    -23       C  
ATOM    207  CD1 LEU A  24       6.148  33.325  15.651  1.00 21.80           C  
ANISOU  207  CD1 LEU A  24     2294   3704   2285   1340   -374   -519       C  
ATOM    208  CD2 LEU A  24       8.072  33.449  14.050  1.00 18.91           C  
ANISOU  208  CD2 LEU A  24     2913   2537   1733     62   -405    421       C  
ATOM    209  N   ASP A  25      11.198  30.240  16.520  1.00 10.18           N  
ANISOU  209  N   ASP A  25     1510   1647    712   -193   -204    144       N  
ATOM    210  CA  ASP A  25      11.993  29.379  17.377  1.00 10.49           C  
ANISOU  210  CA  ASP A  25     1539   1803    646    -77    -85    169       C  
ATOM    211  C   ASP A  25      12.954  30.102  18.311  1.00  9.80           C  
ANISOU  211  C   ASP A  25     1547   1501    675     83   -148    211       C  
ATOM    212  O   ASP A  25      14.052  30.502  17.939  1.00 11.68           O  
ANISOU  212  O   ASP A  25     1692   1780    965   -185     35   -140       O  
ATOM    213  CB  ASP A  25      12.793  28.459  16.457  1.00 11.27           C  
ANISOU  213  CB  ASP A  25     1575   1656   1049   -166    -59    -69       C  
ATOM    214  CG  ASP A  25      13.453  27.317  17.194  1.00 13.40           C  
ANISOU  214  CG  ASP A  25     2018   1686   1387    -32    -61     60       C  
ATOM    215  OD1 ASP A  25      13.374  27.337  18.449  1.00 14.80           O  
ANISOU  215  OD1 ASP A  25     2461   1788   1376   -299   -204    213       O  
ATOM    216  OD2 ASP A  25      14.035  26.432  16.535  1.00 15.45           O  
ANISOU  216  OD2 ASP A  25     2219   1686   1967     46    158     -3       O  
ATOM    217  N   THR A  26      12.527  30.263  19.572  1.00 10.34           N  
ANISOU  217  N   THR A  26     1688   1484    758    209    -39    -17       N  
ATOM    218  CA  THR A  26      13.351  30.945  20.546  1.00 10.19           C  
ANISOU  218  CA  THR A  26     1774   1392    708     80   -103    202       C  
ATOM    219  C   THR A  26      14.612  30.147  20.898  1.00  9.90           C  
ANISOU  219  C   THR A  26     1738   1166    859     -1   -174    -36       C  
ATOM    220  O   THR A  26      15.532  30.747  21.434  1.00 10.50           O  
ANISOU  220  O   THR A  26     1644   1323   1023   -142    -70   -195       O  
ATOM    221  CB  THR A  26      12.562  31.214  21.836  1.00  9.44           C  
ANISOU  221  CB  THR A  26     1647   1267    675    -23   -152    175       C  
ATOM    222  OG1 THR A  26      12.077  29.973  22.380  1.00 10.16           O  
ANISOU  222  OG1 THR A  26     1828   1062    970    -16    178    -31       O  
ATOM    223  CG2 THR A  26      11.342  32.056  21.530  1.00 11.12           C  
ANISOU  223  CG2 THR A  26     1641   1228   1357      2    -77    154       C  
ATOM    224  N   GLY A  27      14.651  28.860  20.610  1.00  9.29           N  
ANISOU  224  N   GLY A  27     1710   1160    660   -108    118    -61       N  
ATOM    225  CA  GLY A  27      15.827  28.043  20.874  1.00  9.65           C  
ANISOU  225  CA  GLY A  27     1796   1042    829    -72     94      3       C  
ATOM    226  C   GLY A  27      16.880  28.111  19.793  1.00 10.06           C  
ANISOU  226  C   GLY A  27     1705   1247    869     72     59    139       C  
ATOM    227  O   GLY A  27      17.965  27.532  19.941  1.00 12.93           O  
ANISOU  227  O   GLY A  27     1854   2219    841    464      1    214       O  
ATOM    228  N   ALA A  28      16.592  28.813  18.701  1.00  9.37           N  
ANISOU  228  N   ALA A  28     1479   1255    826     36     39     63       N  
ATOM    229  CA  ALA A  28      17.468  28.975  17.553  1.00  9.43           C  
ANISOU  229  CA  ALA A  28     1507   1247    828     64     93     58       C  
ATOM    230  C   ALA A  28      18.173  30.322  17.605  1.00  9.87           C  
ANISOU  230  C   ALA A  28     1600   1218    932     68     87    152       C  
ATOM    231  O   ALA A  28      17.511  31.364  17.589  1.00 11.18           O  
ANISOU  231  O   ALA A  28     1594   1277   1378    114   -163    -15       O  
ATOM    232  CB  ALA A  28      16.706  28.870  16.242  1.00 10.68           C  
ANISOU  232  CB  ALA A  28     1715   1489    854    157     22    -55       C  
ATOM    233  N   ASP A  29      19.505  30.340  17.676  1.00  9.79           N  
ANISOU  233  N   ASP A  29     1622    973   1123    108    -80    -63       N  
ATOM    234  CA  ASP A  29      20.205  31.604  17.583  1.00 10.02           C  
ANISOU  234  CA  ASP A  29     1804   1054    949    -55   -238   -134       C  
ATOM    235  C   ASP A  29      20.046  32.281  16.232  1.00 10.90           C  
ANISOU  235  C   ASP A  29     2084   1070    986    -78   -306    -95       C  
ATOM    236  O   ASP A  29      19.949  33.516  16.124  1.00 12.22           O  
ANISOU  236  O   ASP A  29     2499   1163    983    236    249    -29       O  
ATOM    237  CB  ASP A  29      21.712  31.411  17.792  1.00 11.23           C  
ANISOU  237  CB  ASP A  29     1808   1173   1285    -77   -232     42       C  
ATOM    238  CG  ASP A  29      22.117  30.829  19.130  1.00 11.34           C  
ANISOU  238  CG  ASP A  29     1721   1219   1371     88   -178    181       C  
ATOM    239  OD1 ASP A  29      21.374  30.907  20.133  1.00 12.23           O  
ANISOU  239  OD1 ASP A  29     1883   1382   1382    -94    -66    156       O  
ATOM    240  OD2 ASP A  29      23.234  30.289  19.139  1.00 15.99           O  
ANISOU  240  OD2 ASP A  29     2238   2222   1614    839   -170     48       O  
ATOM    241  N   ASP A  30      20.042  31.426  15.210  1.00 11.61           N  
ANISOU  241  N   ASP A  30     2260   1226    927   -236   -264   -126       N  
ATOM    242  CA  ASP A  30      20.044  31.826  13.823  1.00 12.18           C  
ANISOU  242  CA  ASP A  30     2006   1686    935      4   -219    -62       C  
ATOM    243  C   ASP A  30      18.796  31.351  13.079  1.00 11.23           C  
ANISOU  243  C   ASP A  30     2048   1318    902    -53   -188    -50       C  
ATOM    244  O   ASP A  30      18.102  30.434  13.479  1.00 12.44           O  
ANISOU  244  O   ASP A  30     2362   1275   1092   -126   -288     52       O  
ATOM    245  CB  ASP A  30      21.271  31.257  13.105  1.00 13.97           C  
ANISOU  245  CB  ASP A  30     2081   2110   1118    312   -148    158       C  
ATOM    246  CG  ASP A  30      22.564  31.502  13.824  1.00 15.07           C  
ANISOU  246  CG  ASP A  30     2065   2222   1438    296   -202    178       C  
ATOM    247  OD1 ASP A  30      22.681  32.596  14.399  1.00 19.22           O  
ANISOU  247  OD1 ASP A  30     2552   2887   1864    -40   -180   -482       O  
ATOM    248  OD2 ASP A  30      23.427  30.611  13.804  1.00 21.61           O  
ANISOU  248  OD2 ASP A  30     2463   3091   2656    953   -530    240       O  
ATOM    249  N   THR A  31      18.517  31.997  11.969  1.00 11.28           N  
ANISOU  249  N   THR A  31     2151   1220    914   -200   -307   -105       N  
ATOM    250  CA  THR A  31      17.443  31.682  11.050  1.00  9.94           C  
ANISOU  250  CA  THR A  31     1769   1143    865      4    -88   -225       C  
ATOM    251  C   THR A  31      17.969  30.722   9.995  1.00 10.50           C  
ANISOU  251  C   THR A  31     1804   1230    955    -20    -12   -275       C  
ATOM    252  O   THR A  31      19.008  31.012   9.359  1.00 11.43           O  
ANISOU  252  O   THR A  31     1750   1488   1107     89     73   -120       O  
ATOM    253  CB  THR A  31      16.931  33.013  10.484  1.00 10.43           C  
ANISOU  253  CB  THR A  31     1558   1263   1142     54    107     -6       C  
ATOM    254  OG1 THR A  31      16.286  33.741  11.552  1.00 11.21           O  
ANISOU  254  OG1 THR A  31     2025    990   1247    -43    324     29       O  
ATOM    255  CG2 THR A  31      15.918  32.782   9.390  1.00 10.91           C  
ANISOU  255  CG2 THR A  31     1744   1162   1242    -26    -38    105       C  
ATOM    256  N   VAL A  32      17.266  29.605   9.820  1.00 10.78           N  
ANISOU  256  N   VAL A  32     1825   1174   1095     54    -48   -334       N  
ATOM    257  CA  VAL A  32      17.728  28.553   8.927  1.00  9.84           C  
ANISOU  257  CA  VAL A  32     1470   1202   1067     22    -79   -319       C  
ATOM    258  C   VAL A  32      16.568  28.149   8.017  1.00  8.54           C  
ANISOU  258  C   VAL A  32     1332   1110    803   -127     71    -54       C  
ATOM    259  O   VAL A  32      15.524  27.722   8.506  1.00 11.00           O  
ANISOU  259  O   VAL A  32     1646   1518   1017   -500    268   -118       O  
ATOM    260  CB  VAL A  32      18.275  27.309   9.665  1.00 11.20           C  
ANISOU  260  CB  VAL A  32     1444   1465   1347    330   -230   -333       C  
ATOM    261  CG1 VAL A  32      19.118  26.497   8.692  1.00 11.38           C  
ANISOU  261  CG1 VAL A  32     1419   1656   1247    431     60     45       C  
ATOM    262  CG2 VAL A  32      19.079  27.664  10.899  1.00 13.36           C  
ANISOU  262  CG2 VAL A  32     1840   1973   1262    -87   -316    -55       C  
ATOM    263  N   ILE A  33      16.783  28.301   6.719  1.00  9.66           N  
ANISOU  263  N   ILE A  33     1443   1439    791   -187    230   -311       N  
ATOM    264  CA  ILE A  33      15.776  28.012   5.716  1.00 11.89           C  
ANISOU  264  CA  ILE A  33     1897   1707    914      1   -108   -306       C  
ATOM    265  C   ILE A  33      16.224  26.880   4.802  1.00 11.60           C  
ANISOU  265  C   ILE A  33     1720   1920    768   -105    -23   -398       C  
ATOM    266  O   ILE A  33      17.420  26.739   4.508  1.00 12.07           O  
ANISOU  266  O   ILE A  33     1768   2001    818   -148    170   -122       O  
ATOM    267  CB  ILE A  33      15.480  29.273   4.883  1.00 13.30           C  
ANISOU  267  CB  ILE A  33     2377   1737    938   -240   -180   -148       C  
ATOM    268  CG1 ILE A  33      15.112  30.454   5.800  1.00 14.40           C  
ANISOU  268  CG1 ILE A  33     2612   1672   1189     87     16     16       C  
ATOM    269  CG2 ILE A  33      14.426  29.030   3.850  1.00 16.62           C  
ANISOU  269  CG2 ILE A  33     2847   2127   1342   -412   -658    206       C  
ATOM    270  CD1 ILE A  33      13.901  30.177   6.650  1.00 14.60           C  
ANISOU  270  CD1 ILE A  33     2589   1691   1267    109     35     -2       C  
ATOM    271  N   GLU A  34      15.296  26.059   4.334  1.00 11.80           N  
ANISOU  271  N   GLU A  34     1788   1847    849   -121    -53   -325       N  
ATOM    272  CA  GLU A  34      15.558  24.981   3.399  1.00 12.67           C  
ANISOU  272  CA  GLU A  34     2084   1813    915   -335    212   -384       C  
ATOM    273  C   GLU A  34      16.140  25.550   2.110  1.00 12.45           C  
ANISOU  273  C   GLU A  34     2137   1633    959     89    173   -171       C  
ATOM    274  O   GLU A  34      15.986  26.747   1.856  1.00 14.66           O  
ANISOU  274  O   GLU A  34     2325   1789   1455    304   -260    139       O  
ATOM    275  CB  GLU A  34      14.265  24.188   3.145  1.00 16.19           C  
ANISOU  275  CB  GLU A  34     2188   2030   1933   -503    191   -659       C  
ATOM    276  CG  GLU A  34      13.210  25.057   2.464  1.00 22.06           C  
ANISOU  276  CG  GLU A  34     2368   2992   3023   -565   -520   -246       C  
ATOM    277  CD  GLU A  34      11.757  24.635   2.564  1.00 23.96           C  
ANISOU  277  CD  GLU A  34     2348   2908   3848   -487   -244     17       C  
ATOM    278  OE1 GLU A  34      11.483  23.486   3.005  1.00 32.51           O  
ANISOU  278  OE1 GLU A  34     3416   2762   6175   -831    213     71       O  
ATOM    279  OE2 GLU A  34      10.856  25.438   2.204  1.00 21.04           O  
ANISOU  279  OE2 GLU A  34     2484   3445   2064    120      5   -802       O  
ATOM    280  N   GLU A  35      16.781  24.645   1.358  1.00 12.89           N  
ANISOU  280  N   GLU A  35     2090   1891    919    106    222   -198       N  
ATOM    281  CA  GLU A  35      17.472  25.068   0.165  1.00 13.28           C  
ANISOU  281  CA  GLU A  35     2506   1665    876    315    262    -53       C  
ATOM    282  C   GLU A  35      16.605  25.946  -0.733  1.00 13.67           C  
ANISOU  282  C   GLU A  35     2178   1564   1453     79    143    136       C  
ATOM    283  O   GLU A  35      15.460  25.616  -1.080  1.00 14.53           O  
ANISOU  283  O   GLU A  35     2171   1808   1542    -47    227     24       O  
ATOM    284  CB  GLU A  35      17.937  23.845  -0.636  1.00 15.06           C  
ANISOU  284  CB  GLU A  35     2718   1884   1123    526    366   -213       C  
ATOM    285  CG  GLU A  35      19.120  23.153  -0.006  1.00 17.88           C  
ANISOU  285  CG  GLU A  35     2875   1952   1966    621    116   -207       C  
ATOM    286  CD  GLU A  35      20.391  23.986  -0.128  1.00 21.38           C  
ANISOU  286  CD  GLU A  35     3009   2545   2571    214   -326   -147       C  
ATOM    287  OE1 GLU A  35      20.339  25.038  -0.815  1.00 22.75           O  
ANISOU  287  OE1 GLU A  35     3297   2605   2744    -86   -153     -9       O  
ATOM    288  OE2 GLU A  35      21.395  23.552   0.466  1.00 24.20           O  
ANISOU  288  OE2 GLU A  35     3230   3266   2698    301   -610   -266       O  
ATOM    289  N   MET A  36      17.174  27.084  -1.098  1.00 12.68           N  
ANISOU  289  N   MET A  36     2282   1353   1185     66    -18   -147       N  
ATOM    290  CA  MET A  36      16.612  28.044  -2.003  1.00 13.30           C  
ANISOU  290  CA  MET A  36     2353   1567   1134   -223   -191     61       C  
ATOM    291  C   MET A  36      17.755  28.930  -2.491  1.00 14.38           C  
ANISOU  291  C   MET A  36     2511   1834   1117   -428   -189     51       C  
ATOM    292  O   MET A  36      18.807  28.953  -1.868  1.00 14.59           O  
ANISOU  292  O   MET A  36     2238   1935   1370   -194     -6   -137       O  
ATOM    293  CB  MET A  36      15.540  28.917  -1.358  1.00 13.09           C  
ANISOU  293  CB  MET A  36     2125   1455   1394    -81   -470    221       C  
ATOM    294  CG  MET A  36      16.096  29.830  -0.284  1.00 14.11           C  
ANISOU  294  CG  MET A  36     2499   1362   1501   -190   -236     -6       C  
ATOM    295  SD  MET A  36      14.760  30.801   0.451  1.00 17.91           S  
ANISOU  295  SD  MET A  36     3006   2141   1659    243     68     76       S  
ATOM    296  CE  MET A  36      14.251  31.792  -0.958  1.00 18.58           C  
ANISOU  296  CE  MET A  36     3012   2061   1986    343   -165    209       C  
ATOM    297  N   SER A  37      17.492  29.624  -3.589  1.00 15.97           N  
ANISOU  297  N   SER A  37     3106   1907   1053   -570   -153    105       N  
ATOM    298  CA  SER A  37      18.406  30.648  -4.049  1.00 16.61           C  
ANISOU  298  CA  SER A  37     3428   1930    955   -628    222   -135       C  
ATOM    299  C   SER A  37      18.145  31.961  -3.345  1.00 15.01           C  
ANISOU  299  C   SER A  37     3006   1843    856   -373     99     10       C  
ATOM    300  O   SER A  37      17.012  32.368  -3.095  1.00 16.90           O  
ANISOU  300  O   SER A  37     2919   1963   1540   -386    133    257       O  
ATOM    301  CB ASER A  37      18.245  30.774  -5.571  0.56 20.03           C  
ANISOU  301  CB ASER A  37     4299   2413    899   -737    463   -189       C  
ATOM    302  CB BSER A  37      18.254  30.787  -5.571  0.44 19.92           C  
ANISOU  302  CB BSER A  37     4249   2416    905   -807    436   -186       C  
ATOM    303  OG ASER A  37      19.010  31.842  -6.097  0.56 23.07           O  
ANISOU  303  OG ASER A  37     4575   3053   1137  -1043    593     92       O  
ATOM    304  OG BSER A  37      18.506  29.502  -6.111  0.44 26.04           O  
ANISOU  304  OG BSER A  37     5463   3004   1425   -328    255   -844       O  
ATOM    305  N   LEU A  38      19.223  32.651  -3.014  1.00 15.55           N  
ANISOU  305  N   LEU A  38     2853   1560   1494     18   -144   -187       N  
ATOM    306  CA  LEU A  38      19.169  34.024  -2.543  1.00 14.56           C  
ANISOU  306  CA  LEU A  38     2594   1548   1391    171    -65   -175       C  
ATOM    307  C   LEU A  38      20.254  34.807  -3.286  1.00 17.13           C  
ANISOU  307  C   LEU A  38     3077   1821   1609   -179   -160    197       C  
ATOM    308  O   LEU A  38      21.282  34.264  -3.660  1.00 16.32           O  
ANISOU  308  O   LEU A  38     2570   1874   1759   -457   -192    559       O  
ATOM    309  CB  LEU A  38      19.344  34.130  -1.037  1.00 14.50           C  
ANISOU  309  CB  LEU A  38     2571   1554   1384    191   -221   -102       C  
ATOM    310  CG  LEU A  38      18.206  33.604  -0.163  1.00 14.26           C  
ANISOU  310  CG  LEU A  38     2641   1417   1362    286   -161    -69       C  
ATOM    311  CD1 LEU A  38      18.572  33.621   1.329  1.00 15.81           C  
ANISOU  311  CD1 LEU A  38     2962   1659   1385    132   -231     13       C  
ATOM    312  CD2 LEU A  38      16.906  34.385  -0.347  1.00 17.06           C  
ANISOU  312  CD2 LEU A  38     2513   1906   2065    309   -237    117       C  
ATOM    313  N   PRO A  39      19.983  36.095  -3.488  1.00 20.95           N  
ANISOU  313  N   PRO A  39     3622   2030   2308     37    -33    630       N  
ATOM    314  CA  PRO A  39      20.963  36.909  -4.213  1.00 22.55           C  
ANISOU  314  CA  PRO A  39     3915   1985   2667   -145     93    637       C  
ATOM    315  C   PRO A  39      22.117  37.306  -3.319  1.00 22.43           C  
ANISOU  315  C   PRO A  39     3731   2246   2547   -177    160    912       C  
ATOM    316  O   PRO A  39      21.980  37.320  -2.096  1.00 20.52           O  
ANISOU  316  O   PRO A  39     3542   1578   2677   -306    500     -4       O  
ATOM    317  CB  PRO A  39      20.152  38.142  -4.607  1.00 24.56           C  
ANISOU  317  CB  PRO A  39     4118   2248   2967   -149   -235    997       C  
ATOM    318  CG  PRO A  39      18.992  38.198  -3.692  1.00 24.77           C  
ANISOU  318  CG  PRO A  39     3754   2329   3328    233   -332   1264       C  
ATOM    319  CD  PRO A  39      18.784  36.837  -3.067  1.00 22.58           C  
ANISOU  319  CD  PRO A  39     3494   2046   3037    229   -205    917       C  
ATOM    320  N   GLY A  40      23.236  37.627  -3.963  1.00 23.21           N  
ANISOU  320  N   GLY A  40     3766   2615   2439    -59    208    973       N  
ATOM    321  CA  GLY A  40      24.378  38.160  -3.269  1.00 23.26           C  
ANISOU  321  CA  GLY A  40     3700   2460   2676   -208    329   1015       C  
ATOM    322  C   GLY A  40      25.369  37.107  -2.807  1.00 22.67           C  
ANISOU  322  C   GLY A  40     3563   2492   2561   -295    274   1000       C  
ATOM    323  O   GLY A  40      25.319  35.932  -3.155  1.00 22.90           O  
ANISOU  323  O   GLY A  40     4146   2472   2082    -88    581    957       O  
ATOM    324  N   ARG A  41      26.286  37.636  -1.984  1.00 23.75           N  
ANISOU  324  N   ARG A  41     3491   2982   2552   -707    362   1228       N  
ATOM    325  CA  ARG A  41      27.408  36.817  -1.545  1.00 24.81           C  
ANISOU  325  CA  ARG A  41     3402   3420   2604   -681    344   1425       C  
ATOM    326  C   ARG A  41      26.971  35.925  -0.405  1.00 20.03           C  
ANISOU  326  C   ARG A  41     2892   2583   2134   -408    562    739       C  
ATOM    327  O   ARG A  41      26.036  36.189   0.342  1.00 18.41           O  
ANISOU  327  O   ARG A  41     3036   2010   1947    -50    326    464       O  
ATOM    328  CB  ARG A  41      28.588  37.686  -1.114  1.00 31.56           C  
ANISOU  328  CB  ARG A  41     3712   4710   3570  -1585    -72   2399       C  
ATOM    329  CG  ARG A  41      29.407  38.282  -2.251  1.00 42.19           C  
ANISOU  329  CG  ARG A  41     4908   6329   4793  -2189    632   3144       C  
ATOM    330  CD  ARG A  41      30.682  39.020  -1.833  1.00 50.47           C  
ANISOU  330  CD  ARG A  41     5473   7728   5974  -3333    825   3362       C  
ATOM    331  NE  ARG A  41      31.283  39.715  -2.967  1.00 57.59           N  
ANISOU  331  NE  ARG A  41     6418   8889   6575  -3708   1310   3799       N  
ATOM    332  CZ  ARG A  41      32.063  40.741  -3.189  1.00 59.91           C  
ANISOU  332  CZ  ARG A  41     7071   9173   6520  -4096   1416   3883       C  
ATOM    333  NH1 ARG A  41      32.587  41.533  -2.252  1.00 67.00           N  
ANISOU  333  NH1 ARG A  41     7700   9655   8104  -4207    744   3120       N  
ATOM    334  NH2 ARG A  41      32.392  41.056  -4.449  1.00 67.61           N  
ANISOU  334  NH2 ARG A  41     8835   9830   7022  -3362   1496   5279       N  
ATOM    335  N   TRP A  42      27.689  34.820  -0.269  1.00 18.40           N  
ANISOU  335  N   TRP A  42     2501   2747   1743   -334   1056    625       N  
ATOM    336  CA  TRP A  42      27.461  33.958   0.869  1.00 17.09           C  
ANISOU  336  CA  TRP A  42     2349   2477   1669   -302    905    554       C  
ATOM    337  C   TRP A  42      28.772  33.305   1.264  1.00 17.37           C  
ANISOU  337  C   TRP A  42     2424   2172   2005   -210    943    287       C  
ATOM    338  O   TRP A  42      29.750  33.318   0.516  1.00 19.34           O  
ANISOU  338  O   TRP A  42     2710   2566   2073    228   1120    273       O  
ATOM    339  CB  TRP A  42      26.389  32.896   0.551  1.00 16.17           C  
ANISOU  339  CB  TRP A  42     2495   2006   1644    -46    838    245       C  
ATOM    340  CG  TRP A  42      26.831  32.041  -0.595  1.00 19.67           C  
ANISOU  340  CG  TRP A  42     3017   2513   1944    427    997     51       C  
ATOM    341  CD1 TRP A  42      26.546  32.309  -1.906  1.00 22.08           C  
ANISOU  341  CD1 TRP A  42     3765   2744   1880    744    918   -233       C  
ATOM    342  CD2 TRP A  42      27.605  30.827  -0.571  1.00 20.32           C  
ANISOU  342  CD2 TRP A  42     3015   2285   2419    237    823   -133       C  
ATOM    343  NE1 TRP A  42      27.094  31.337  -2.694  1.00 23.53           N  
ANISOU  343  NE1 TRP A  42     3906   2809   2224    783    908   -433       N  
ATOM    344  CE2 TRP A  42      27.752  30.411  -1.906  1.00 22.28           C  
ANISOU  344  CE2 TRP A  42     3410   2472   2584    407    743   -411       C  
ATOM    345  CE3 TRP A  42      28.185  30.056   0.442  1.00 19.49           C  
ANISOU  345  CE3 TRP A  42     2550   2142   2714    147    713   -152       C  
ATOM    346  CZ2 TRP A  42      28.460  29.252  -2.244  1.00 22.64           C  
ANISOU  346  CZ2 TRP A  42     3199   2557   2845    372    735   -494       C  
ATOM    347  CZ3 TRP A  42      28.887  28.904   0.106  1.00 21.64           C  
ANISOU  347  CZ3 TRP A  42     2731   2486   3004    397    317   -566       C  
ATOM    348  CH2 TRP A  42      29.020  28.510  -1.237  1.00 22.51           C  
ANISOU  348  CH2 TRP A  42     2874   2605   3076    383    323   -705       C  
ATOM    349  N   LYS A  43      28.791  32.729   2.457  1.00 16.57           N  
ANISOU  349  N   LYS A  43     2306   1686   2305   -135    853    489       N  
ATOM    350  CA  LYS A  43      29.984  32.004   2.860  1.00 18.56           C  
ANISOU  350  CA  LYS A  43     2065   2084   2902   -185    850    571       C  
ATOM    351  C   LYS A  43      29.513  30.773   3.626  1.00 15.78           C  
ANISOU  351  C   LYS A  43     1907   1835   2253     27    607    368       C  
ATOM    352  O   LYS A  43      28.437  30.783   4.225  1.00 15.18           O  
ANISOU  352  O   LYS A  43     1863   1629   2275    107    546    608       O  
ATOM    353  CB  LYS A  43      30.911  32.885   3.680  1.00 20.45           C  
ANISOU  353  CB  LYS A  43     2282   2095   3393   -280    591    580       C  
ATOM    354  CG  LYS A  43      30.326  33.313   5.000  1.00 22.50           C  
ANISOU  354  CG  LYS A  43     2730   2307   3512   -536    613    160       C  
ATOM    355  CD  LYS A  43      31.305  34.265   5.692  1.00 28.19           C  
ANISOU  355  CD  LYS A  43     3291   3101   4319   -901    401   -295       C  
ATOM    356  CE  LYS A  43      30.479  35.266   6.476  1.00 32.34           C  
ANISOU  356  CE  LYS A  43     4080   3720   4488   -994    566  -1069       C  
ATOM    357  NZ  LYS A  43      31.246  36.462   6.926  1.00 39.84           N  
ANISOU  357  NZ  LYS A  43     4846   5010   5281  -1701    800  -2258       N  
ATOM    358  N   PRO A  44      30.303  29.715   3.606  1.00 16.71           N  
ANISOU  358  N   PRO A  44     2020   2110   2219    227    576    260       N  
ATOM    359  CA  PRO A  44      29.880  28.496   4.280  1.00 16.01           C  
ANISOU  359  CA  PRO A  44     1918   1894   2269    318    239    286       C  
ATOM    360  C   PRO A  44      29.989  28.604   5.798  1.00 15.52           C  
ANISOU  360  C   PRO A  44     2046   1527   2325     43     96    301       C  
ATOM    361  O   PRO A  44      30.781  29.333   6.373  1.00 16.03           O  
ANISOU  361  O   PRO A  44     2086   1559   2447   -112    202    306       O  
ATOM    362  CB  PRO A  44      30.871  27.462   3.743  1.00 18.48           C  
ANISOU  362  CB  PRO A  44     2131   2305   2587    562    451    331       C  
ATOM    363  CG  PRO A  44      32.060  28.215   3.294  1.00 19.54           C  
ANISOU  363  CG  PRO A  44     2275   2417   2733    496    673    242       C  
ATOM    364  CD  PRO A  44      31.613  29.603   2.945  1.00 18.56           C  
ANISOU  364  CD  PRO A  44     2060   2601   2390    504    580    547       C  
ATOM    365  N   LYS A  45      29.127  27.818   6.439  1.00 15.26           N  
ANISOU  365  N   LYS A  45     2168   1465   2166   -110     56    152       N  
ATOM    366  CA  LYS A  45      29.019  27.734   7.880  1.00 15.33           C  
ANISOU  366  CA  LYS A  45     2165   1475   2185    -14     65    139       C  
ATOM    367  C   LYS A  45      28.558  26.340   8.283  1.00 14.24           C  
ANISOU  367  C   LYS A  45     1926   1493   1993    -19   -141    148       C  
ATOM    368  O   LYS A  45      27.850  25.682   7.516  1.00 14.83           O  
ANISOU  368  O   LYS A  45     2339   1485   1811      5   -295    149       O  
ATOM    369  CB  LYS A  45      28.038  28.774   8.372  1.00 16.03           C  
ANISOU  369  CB  LYS A  45     2330   1551   2210    118   -147    -69       C  
ATOM    370  CG  LYS A  45      28.036  29.100   9.850  1.00 16.86           C  
ANISOU  370  CG  LYS A  45     2448   1621   2336    -32   -420   -404       C  
ATOM    371  CD  LYS A  45      26.904  30.082  10.153  1.00 19.02           C  
ANISOU  371  CD  LYS A  45     2755   2151   2319    315   -312   -487       C  
ATOM    372  CE  LYS A  45      26.767  30.446  11.607  1.00 22.20           C  
ANISOU  372  CE  LYS A  45     3146   2793   2497    175   -272   -900       C  
ATOM    373  NZ  LYS A  45      27.947  31.208  12.069  1.00 31.28           N  
ANISOU  373  NZ  LYS A  45     3866   4221   3798   -523   -163  -2337       N  
ATOM    374  N   MET A  46      28.965  25.923   9.475  1.00 13.68           N  
ANISOU  374  N   MET A  46     1816   1461   1920   -129   -205      1       N  
ATOM    375  CA  MET A  46      28.415  24.745  10.093  1.00 13.44           C  
ANISOU  375  CA  MET A  46     1991   1345   1770    -45   -137    -40       C  
ATOM    376  C   MET A  46      27.585  25.158  11.309  1.00 13.59           C  
ANISOU  376  C   MET A  46     2076   1166   1921    -85    -46   -182       C  
ATOM    377  O   MET A  46      28.068  25.954  12.116  1.00 15.08           O  
ANISOU  377  O   MET A  46     2237   1553   1937   -601    236   -240       O  
ATOM    378  CB AMET A  46      29.521  23.811  10.550  0.67 15.11           C  
ANISOU  378  CB AMET A  46     2115   1461   2167    151    -10    -15       C  
ATOM    379  CB BMET A  46      29.500  23.734  10.490  0.33 15.28           C  
ANISOU  379  CB BMET A  46     2051   1564   2192    131     37    111       C  
ATOM    380  CG AMET A  46      30.256  23.133   9.408  0.67 15.71           C  
ANISOU  380  CG AMET A  46     2244   1496   2229     87     98    -60       C  
ATOM    381  CG BMET A  46      30.496  23.356   9.427  0.33 15.81           C  
ANISOU  381  CG BMET A  46     2254   1563   2189    145     58    -94       C  
ATOM    382  SD AMET A  46      29.279  21.768   8.774  0.67 18.10           S  
ANISOU  382  SD AMET A  46     1948   1994   2935    519   -829   -624       S  
ATOM    383  SD BMET A  46      30.660  21.659   8.883  0.33 18.16           S  
ANISOU  383  SD BMET A  46     2655   1543   2703    326   -214   -139       S  
ATOM    384  CE AMET A  46      29.832  20.460   9.890  0.67 14.09           C  
ANISOU  384  CE AMET A  46     1140   1314   2901   -287   -972   -807       C  
ATOM    385  CE BMET A  46      30.622  20.718  10.405  0.33 12.39           C  
ANISOU  385  CE BMET A  46     1261   1154   2291   -625   -860   -596       C  
ATOM    386  N   ILE A  47      26.389  24.631  11.427  1.00 13.50           N  
ANISOU  386  N   ILE A  47     2212   1156   1760   -254     33   -357       N  
ATOM    387  CA  ILE A  47      25.544  24.855  12.599  1.00 13.49           C  
ANISOU  387  CA  ILE A  47     2177   1046   1903     -5     56   -445       C  
ATOM    388  C   ILE A  47      25.083  23.501  13.130  1.00 13.84           C  
ANISOU  388  C   ILE A  47     2250   1208   1802     87    214   -250       C  
ATOM    389  O   ILE A  47      24.841  22.540  12.413  1.00 13.26           O  
ANISOU  389  O   ILE A  47     2387    967   1685   -110     50     61       O  
ATOM    390  CB  ILE A  47      24.344  25.757  12.295  1.00 16.50           C  
ANISOU  390  CB  ILE A  47     2423   1451   2396    183    169    129       C  
ATOM    391  CG1 ILE A  47      23.485  25.219  11.151  1.00 17.99           C  
ANISOU  391  CG1 ILE A  47     2470   1802   2564    381   -189    271       C  
ATOM    392  CG2 ILE A  47      24.821  27.175  12.047  1.00 19.54           C  
ANISOU  392  CG2 ILE A  47     3030   1622   2774     67   -496    834       C  
ATOM    393  CD1 ILE A  47      22.137  25.915  11.086  1.00 20.96           C  
ANISOU  393  CD1 ILE A  47     2545   2383   3036    663    -71   -534       C  
ATOM    394  N   GLY A  48      24.988  23.467  14.468  1.00 14.86           N  
ANISOU  394  N   GLY A  48     2366   1476   1806    467    125   -264       N  
ATOM    395  CA  GLY A  48      24.759  22.225  15.154  1.00 15.30           C  
ANISOU  395  CA  GLY A  48     2233   1840   1740    294    177    -63       C  
ATOM    396  C   GLY A  48      23.566  22.245  16.063  1.00 16.11           C  
ANISOU  396  C   GLY A  48     1962   2102   2056    315    158   -294       C  
ATOM    397  O   GLY A  48      23.199  23.265  16.645  1.00 20.29           O  
ANISOU  397  O   GLY A  48     1782   2393   3532    283    365   -868       O  
ATOM    398  N   GLY A  49      22.958  21.079  16.174  1.00 17.05           N  
ANISOU  398  N   GLY A  49     2065   2321   2093    123    395   -516       N  
ATOM    399  CA  GLY A  49      21.753  20.977  16.954  1.00 18.69           C  
ANISOU  399  CA  GLY A  49     2488   2410   2203    -83    705   -779       C  
ATOM    400  C   GLY A  49      21.658  19.546  17.448  1.00 16.65           C  
ANISOU  400  C   GLY A  49     2121   2562   1645    319    560   -479       C  
ATOM    401  O   GLY A  49      22.719  18.922  17.487  1.00 20.06           O  
ANISOU  401  O   GLY A  49     1990   4143   1490    657   -184    372       O  
ATOM    402  N  AILE A  50      20.444  19.130  17.809  0.63 15.92           N  
ANISOU  402  N  AILE A  50     2075   2247   1727    234    357   -570       N  
ATOM    403  N  BILE A  50      20.431  19.136  17.752  0.37 15.81           N  
ANISOU  403  N  BILE A  50     2083   2199   1725    262    381   -587       N  
ATOM    404  CA AILE A  50      20.279  17.734  18.191  0.63 16.99           C  
ANISOU  404  CA AILE A  50     2375   2341   1741    273    331   -392       C  
ATOM    405  CA BILE A  50      20.341  17.899  18.521  0.37 17.36           C  
ANISOU  405  CA BILE A  50     2376   2346   1873    177    417   -434       C  
ATOM    406  C  AILE A  50      20.530  16.905  16.957  0.63 16.64           C  
ANISOU  406  C  AILE A  50     2563   1979   1779    476    482   -168       C  
ATOM    407  C  BILE A  50      21.090  16.724  17.881  0.37 17.22           C  
ANISOU  407  C  BILE A  50     2461   2268   1814    358    539   -133       C  
ATOM    408  O  AILE A  50      20.087  17.231  15.852  0.63 13.81           O  
ANISOU  408  O  AILE A  50     3110    695   1443     12   1030    152       O  
ATOM    409  O  BILE A  50      21.837  16.201  18.724  0.37 15.00           O  
ANISOU  409  O  BILE A  50     1610   2542   1548    -75    852    -13       O  
ATOM    410  CB  ILE A  50      18.881  17.502  18.788  1.00 17.36           C  
ANISOU  410  CB  ILE A  50     2438   1989   2170    146    552   -712       C  
ATOM    411  CG1 ILE A  50      18.684  17.823  20.267  1.00 15.75           C  
ANISOU  411  CG1 ILE A  50     2400   1621   1962   -239    471   -308       C  
ATOM    412  CG2 ILE A  50      18.465  16.076  18.546  1.00 26.52           C  
ANISOU  412  CG2 ILE A  50     3990   2676   3412   -848    970  -1518       C  
ATOM    413  CD1 ILE A  50      17.275  17.824  20.769  1.00 18.78           C  
ANISOU  413  CD1 ILE A  50     2507   2702   1926  -1081    618   -903       C  
ATOM    414  N  AGLY A  51      21.254  15.791  17.060  0.63 17.88           N  
ANISOU  414  N  AGLY A  51     2652   2292   1851    721    542      6       N  
ATOM    415  N  BGLY A  51      20.929  16.398  16.620  0.37 17.08           N  
ANISOU  415  N  BGLY A  51     2692   2073   1725    680    518    -25       N  
ATOM    416  CA AGLY A  51      21.547  15.086  15.836  0.63 17.22           C  
ANISOU  416  CA AGLY A  51     2604   2042   1899    706    803    144       C  
ATOM    417  CA BGLY A  51      21.544  15.265  15.964  0.37 17.28           C  
ANISOU  417  CA BGLY A  51     2641   2059   1867    674    777     82       C  
ATOM    418  C  AGLY A  51      22.876  15.530  15.254  0.63 18.34           C  
ANISOU  418  C  AGLY A  51     2752   2014   2203    504    876    184       C  
ATOM    419  C  BGLY A  51      22.856  15.531  15.263  0.37 18.26           C  
ANISOU  419  C  BGLY A  51     2733   2022   2184    515    890    182       C  
ATOM    420  O   GLY A  51      23.327  14.808  14.375  1.00 21.13           O  
ANISOU  420  O   GLY A  51     2898   2073   3059    221   1509   -142       O  
ATOM    421  N   GLY A  52      23.513  16.616  15.649  1.00 17.00           N  
ANISOU  421  N   GLY A  52     2682   1954   1821    654    431    420       N  
ATOM    422  CA  GLY A  52      24.759  17.005  15.012  1.00 15.98           C  
ANISOU  422  CA  GLY A  52     2517   1726   1828    688    157    591       C  
ATOM    423  C   GLY A  52      24.696  18.254  14.158  1.00 15.29           C  
ANISOU  423  C   GLY A  52     2468   1603   1741    662     27    460       C  
ATOM    424  O   GLY A  52      23.823  19.093  14.350  1.00 15.51           O  
ANISOU  424  O   GLY A  52     2170   1396   2327    434   -180    127       O  
ATOM    425  N   PHE A  53      25.648  18.359  13.213  1.00 15.67           N  
ANISOU  425  N   PHE A  53     2800   1509   1646    625    148    386       N  
ATOM    426  CA  PHE A  53      25.799  19.574  12.448  1.00 14.17           C  
ANISOU  426  CA  PHE A  53     2661   1251   1473    594    195     83       C  
ATOM    427  C   PHE A  53      25.383  19.442  10.998  1.00 14.29           C  
ANISOU  427  C   PHE A  53     2938   1139   1353    466    319     44       C  
ATOM    428  O   PHE A  53      25.461  18.349  10.443  1.00 19.13           O  
ANISOU  428  O   PHE A  53     4444   1219   1604    683    108    -46       O  
ATOM    429  CB  PHE A  53      27.268  19.996  12.427  1.00 15.13           C  
ANISOU  429  CB  PHE A  53     2538   1774   1435    690    389    216       C  
ATOM    430  CG  PHE A  53      27.725  20.609  13.734  1.00 15.35           C  
ANISOU  430  CG  PHE A  53     2287   1934   1610    790     60    259       C  
ATOM    431  CD1 PHE A  53      27.918  19.799  14.829  1.00 17.42           C  
ANISOU  431  CD1 PHE A  53     2785   2250   1586    982    128    352       C  
ATOM    432  CD2 PHE A  53      27.941  21.958  13.813  1.00 16.58           C  
ANISOU  432  CD2 PHE A  53     2448   2032   1821    517   -211    188       C  
ATOM    433  CE1 PHE A  53      28.334  20.373  16.007  1.00 18.52           C  
ANISOU  433  CE1 PHE A  53     3008   2372   1658    714    -39    437       C  
ATOM    434  CE2 PHE A  53      28.351  22.542  14.987  1.00 16.55           C  
ANISOU  434  CE2 PHE A  53     2429   2146   1715    576   -192    239       C  
ATOM    435  CZ  PHE A  53      28.545  21.736  16.077  1.00 18.31           C  
ANISOU  435  CZ  PHE A  53     2749   2456   1753    514    -22    424       C  
ATOM    436  N   ILE A  54      24.959  20.535  10.404  1.00 14.21           N  
ANISOU  436  N   ILE A  54     2909   1076   1415    182     30      8       N  
ATOM    437  CA  ILE A  54      24.752  20.606   8.964  1.00 13.87           C  
ANISOU  437  CA  ILE A  54     2511   1349   1409    106    125    146       C  
ATOM    438  C   ILE A  54      25.554  21.770   8.388  1.00 12.43           C  
ANISOU  438  C   ILE A  54     2050   1325   1347     78     48    -95       C  
ATOM    439  O   ILE A  54      25.826  22.779   9.049  1.00 13.03           O  
ANISOU  439  O   ILE A  54     1942   1469   1539    179   -306   -237       O  
ATOM    440  CB  ILE A  54      23.268  20.764   8.604  1.00 13.51           C  
ANISOU  440  CB  ILE A  54     2352   1607   1172   -287    323   -200       C  
ATOM    441  CG1 ILE A  54      22.620  22.043   9.127  1.00 12.57           C  
ANISOU  441  CG1 ILE A  54     2115   1646   1014    -96    235     41       C  
ATOM    442  CG2 ILE A  54      22.522  19.528   9.072  1.00 15.80           C  
ANISOU  442  CG2 ILE A  54     3011   1672   1320   -499     72     33       C  
ATOM    443  CD1 ILE A  54      21.260  22.350   8.527  1.00 18.98           C  
ANISOU  443  CD1 ILE A  54     2590   2901   1722    314   -278    350       C  
ATOM    444  N   LYS A  55      25.938  21.615   7.127  1.00 12.16           N  
ANISOU  444  N   LYS A  55     1974   1333   1315    259     45     34       N  
ATOM    445  CA  LYS A  55      26.566  22.706   6.415  1.00 13.27           C  
ANISOU  445  CA  LYS A  55     2050   1381   1611    391    262    150       C  
ATOM    446  C   LYS A  55      25.509  23.598   5.776  1.00 12.21           C  
ANISOU  446  C   LYS A  55     1964   1166   1508     80    -37     24       C  
ATOM    447  O   LYS A  55      24.576  23.092   5.158  1.00 13.47           O  
ANISOU  447  O   LYS A  55     2454   1301   1364   -371   -196    302       O  
ATOM    448  CB  LYS A  55      27.519  22.138   5.361  1.00 17.06           C  
ANISOU  448  CB  LYS A  55     2560   1929   1993    596    725    260       C  
ATOM    449  CG  LYS A  55      28.342  23.194   4.632  1.00 20.52           C  
ANISOU  449  CG  LYS A  55     3263   2381   2151    646   1065    776       C  
ATOM    450  CD  LYS A  55      29.147  22.473   3.559  1.00 25.86           C  
ANISOU  450  CD  LYS A  55     4115   3111   2602    781   1701    636       C  
ATOM    451  CE  LYS A  55      30.151  23.345   2.854  1.00 30.82           C  
ANISOU  451  CE  LYS A  55     4612   3927   3171    248   2275    223       C  
ATOM    452  NZ  LYS A  55      30.831  22.568   1.771  1.00 42.00           N  
ANISOU  452  NZ  LYS A  55     6025   6409   3523    326   3103   -546       N  
ATOM    453  N   VAL A  56      25.689  24.901   5.944  1.00 11.63           N  
ANISOU  453  N   VAL A  56     1797   1154   1469     58     60     49       N  
ATOM    454  CA  VAL A  56      24.788  25.904   5.401  1.00 11.44           C  
ANISOU  454  CA  VAL A  56     1885   1183   1280    157    248     32       C  
ATOM    455  C   VAL A  56      25.552  26.996   4.664  1.00 11.88           C  
ANISOU  455  C   VAL A  56     1794   1254   1467    201    323    113       C  
ATOM    456  O   VAL A  56      26.763  27.142   4.816  1.00 13.74           O  
ANISOU  456  O   VAL A  56     1814   1726   1682     59    197    179       O  
ATOM    457  CB  VAL A  56      23.943  26.527   6.536  1.00 11.82           C  
ANISOU  457  CB  VAL A  56     1753   1416   1320     98    240    -13       C  
ATOM    458  CG1 VAL A  56      23.069  25.451   7.160  1.00 13.31           C  
ANISOU  458  CG1 VAL A  56     2164   1803   1092    -64    188    304       C  
ATOM    459  CG2 VAL A  56      24.846  27.187   7.557  1.00 13.05           C  
ANISOU  459  CG2 VAL A  56     2479   1125   1356    249   -175    -11       C  
ATOM    460  N   ARG A  57      24.779  27.743   3.866  1.00 12.17           N  
ANISOU  460  N   ARG A  57     1842   1268   1513    230    357    166       N  
ATOM    461  CA  ARG A  57      25.288  28.936   3.207  1.00 11.99           C  
ANISOU  461  CA  ARG A  57     1775   1363   1416    103    275    185       C  
ATOM    462  C   ARG A  57      24.782  30.121   4.008  1.00 11.25           C  
ANISOU  462  C   ARG A  57     1684   1211   1378    101    321    383       C  
ATOM    463  O   ARG A  57      23.586  30.210   4.251  1.00 11.92           O  
ANISOU  463  O   ARG A  57     1602   1611   1316    220      0     84       O  
ATOM    464  CB  ARG A  57      24.864  29.055   1.749  1.00 13.89           C  
ANISOU  464  CB  ARG A  57     2022   1816   1441   -129    234    229       C  
ATOM    465  CG  ARG A  57      25.405  27.942   0.874  1.00 17.23           C  
ANISOU  465  CG  ARG A  57     2489   2530   1527   -126    431   -211       C  
ATOM    466  CD  ARG A  57      25.099  28.140  -0.591  1.00 19.48           C  
ANISOU  466  CD  ARG A  57     2505   3267   1628   -276     18   -238       C  
ATOM    467  NE  ARG A  57      23.756  28.499  -0.979  1.00 22.75           N  
ANISOU  467  NE  ARG A  57     2486   3583   2575   -337   -111    200       N  
ATOM    468  CZ  ARG A  57      22.595  27.885  -1.157  1.00 24.12           C  
ANISOU  468  CZ  ARG A  57     2613   3488   3062   -451   -236    230       C  
ATOM    469  NH1 ARG A  57      22.437  26.574  -0.968  1.00 25.97           N  
ANISOU  469  NH1 ARG A  57     3828   3745   2292   -904    806    861       N  
ATOM    470  NH2 ARG A  57      21.517  28.601  -1.546  1.00 22.94           N  
ANISOU  470  NH2 ARG A  57     2548   3993   2176    142   -226  -1294       N  
ATOM    471  N   GLN A  58      25.682  30.990   4.394  1.00 11.48           N  
ANISOU  471  N   GLN A  58     1646   1333   1382    171    288    201       N  
ATOM    472  CA  GLN A  58      25.360  32.188   5.156  1.00 12.78           C  
ANISOU  472  CA  GLN A  58     2103   1197   1555    339     33    226       C  
ATOM    473  C   GLN A  58      25.211  33.402   4.248  1.00 11.72           C  
ANISOU  473  C   GLN A  58     2119   1254   1081    156   -109     72       C  
ATOM    474  O   GLN A  58      26.213  33.834   3.674  1.00 14.18           O  
ANISOU  474  O   GLN A  58     2405   1737   1246    166    253    234       O  
ATOM    475  CB  GLN A  58      26.448  32.470   6.198  1.00 12.82           C  
ANISOU  475  CB  GLN A  58     2325    961   1584    414   -165    337       C  
ATOM    476  CG  GLN A  58      26.117  33.658   7.067  1.00 12.90           C  
ANISOU  476  CG  GLN A  58     2101   1327   1473    308    140    192       C  
ATOM    477  CD  GLN A  58      27.217  34.057   7.998  1.00 15.57           C  
ANISOU  477  CD  GLN A  58     2405   1795   1716    157    -70    -12       C  
ATOM    478  OE1 GLN A  58      27.953  33.174   8.444  1.00 18.11           O  
ANISOU  478  OE1 GLN A  58     2530   1896   2455    103   -626    -67       O  
ATOM    479  NE2 GLN A  58      27.326  35.339   8.280  1.00 17.64           N  
ANISOU  479  NE2 GLN A  58     2476   1806   2421    -51   -346    119       N  
ATOM    480  N   TYR A  59      23.985  33.918   4.139  1.00 12.16           N  
ANISOU  480  N   TYR A  59     2322   1099   1199    339    -43     41       N  
ATOM    481  CA  TYR A  59      23.687  35.146   3.406  1.00 11.76           C  
ANISOU  481  CA  TYR A  59     2243   1139   1087    192      5    159       C  
ATOM    482  C   TYR A  59      23.419  36.282   4.369  1.00 10.73           C  
ANISOU  482  C   TYR A  59     1952    955   1170      3    325    286       C  
ATOM    483  O   TYR A  59      22.578  36.100   5.257  1.00 12.15           O  
ANISOU  483  O   TYR A  59     1823   1338   1455   -204    414    177       O  
ATOM    484  CB  TYR A  59      22.478  34.948   2.526  1.00 11.30           C  
ANISOU  484  CB  TYR A  59     1946   1320   1026    212    220    212       C  
ATOM    485  CG  TYR A  59      22.625  33.948   1.404  1.00 11.97           C  
ANISOU  485  CG  TYR A  59     2100   1423   1024    189     97    124       C  
ATOM    486  CD1 TYR A  59      22.401  32.586   1.606  1.00 12.26           C  
ANISOU  486  CD1 TYR A  59     2082   1437   1141    111    -53     57       C  
ATOM    487  CD2 TYR A  59      22.985  34.337   0.124  1.00 14.19           C  
ANISOU  487  CD2 TYR A  59     2745   1589   1058    436    282    166       C  
ATOM    488  CE1 TYR A  59      22.535  31.670   0.580  1.00 14.24           C  
ANISOU  488  CE1 TYR A  59     2297   1602   1513     87    169   -186       C  
ATOM    489  CE2 TYR A  59      23.125  33.436  -0.924  1.00 16.03           C  
ANISOU  489  CE2 TYR A  59     2894   1944   1252    352    527    -79       C  
ATOM    490  CZ  TYR A  59      22.898  32.097  -0.689  1.00 16.09           C  
ANISOU  490  CZ  TYR A  59     2782   1851   1480    417    486   -305       C  
ATOM    491  OH  TYR A  59      23.025  31.171  -1.704  1.00 20.42           O  
ANISOU  491  OH  TYR A  59     3887   2308   1563    752   -161   -639       O  
ATOM    492  N   ASP A  60      24.083  37.406   4.237  1.00 12.91           N  
ANISOU  492  N   ASP A  60     2051   1195   1659   -319    395    144       N  
ATOM    493  CA  ASP A  60      23.832  38.513   5.180  1.00 14.22           C  
ANISOU  493  CA  ASP A  60     2346   1160   1895   -201      8     10       C  
ATOM    494  C   ASP A  60      22.907  39.542   4.545  1.00 14.60           C  
ANISOU  494  C   ASP A  60     2393   1230   1923   -144    -70    -41       C  
ATOM    495  O   ASP A  60      22.759  39.560   3.321  1.00 15.39           O  
ANISOU  495  O   ASP A  60     2667   1319   1861    127    126     82       O  
ATOM    496  CB  ASP A  60      25.150  39.143   5.616  1.00 16.65           C  
ANISOU  496  CB  ASP A  60     2432   1690   2206   -204   -232   -144       C  
ATOM    497  CG  ASP A  60      26.075  38.166   6.314  1.00 18.10           C  
ANISOU  497  CG  ASP A  60     2269   2241   2368    -11     18    166       C  
ATOM    498  OD1 ASP A  60      25.596  37.341   7.121  1.00 17.22           O  
ANISOU  498  OD1 ASP A  60     2550   1851   2143   -106   -119    -59       O  
ATOM    499  OD2 ASP A  60      27.301  38.198   6.074  1.00 23.21           O  
ANISOU  499  OD2 ASP A  60     2297   3310   3213     72    158    520       O  
ATOM    500  N   GLN A  61      22.287  40.395   5.348  1.00 14.27           N  
ANISOU  500  N   GLN A  61     2479   1222   1722   -113    -36     96       N  
ATOM    501  CA  GLN A  61      21.445  41.503   4.906  1.00 14.79           C  
ANISOU  501  CA  GLN A  61     2711   1181   1726    -22    113    163       C  
ATOM    502  C   GLN A  61      20.366  41.030   3.945  1.00 14.67           C  
ANISOU  502  C   GLN A  61     2746   1312   1516    153     27    324       C  
ATOM    503  O   GLN A  61      20.132  41.528   2.844  1.00 17.40           O  
ANISOU  503  O   GLN A  61     3445   1842   1324    286    204    273       O  
ATOM    504  CB  GLN A  61      22.295  42.618   4.261  1.00 17.70           C  
ANISOU  504  CB  GLN A  61     3052   1547   2126   -187    115    507       C  
ATOM    505  CG  GLN A  61      23.375  43.138   5.217  1.00 23.96           C  
ANISOU  505  CG  GLN A  61     3648   2010   3445   -805    -88   -356       C  
ATOM    506  CD  GLN A  61      24.224  44.198   4.555  1.00 29.19           C  
ANISOU  506  CD  GLN A  61     4439   2690   3961  -1432    474   -498       C  
ATOM    507  OE1 GLN A  61      24.665  44.060   3.414  1.00 37.33           O  
ANISOU  507  OE1 GLN A  61     6206   3748   4231  -1439   1264   -248       O  
ATOM    508  NE2 GLN A  61      24.449  45.279   5.292  1.00 38.28           N  
ANISOU  508  NE2 GLN A  61     5796   3391   5357  -2617    845  -1212       N  
ATOM    509  N   ILE A  62      19.659  39.998   4.389  1.00 13.76           N  
ANISOU  509  N   ILE A  62     2634   1212   1382     76     32    -41       N  
ATOM    510  CA  ILE A  62      18.498  39.515   3.679  1.00 13.00           C  
ANISOU  510  CA  ILE A  62     2626   1247   1066    327   -134    114       C  
ATOM    511  C   ILE A  62      17.229  40.021   4.320  1.00 15.04           C  
ANISOU  511  C   ILE A  62     2702   1737   1274    598   -349   -460       C  
ATOM    512  O   ILE A  62      17.039  39.943   5.554  1.00 16.29           O  
ANISOU  512  O   ILE A  62     2691   2163   1338    452   -149   -497       O  
ATOM    513  CB  ILE A  62      18.490  37.973   3.686  1.00 12.93           C  
ANISOU  513  CB  ILE A  62     2682   1239    991    281   -203   -239       C  
ATOM    514  CG1 ILE A  62      19.722  37.409   2.992  1.00 13.07           C  
ANISOU  514  CG1 ILE A  62     2770   1380    815    287   -155   -204       C  
ATOM    515  CG2 ILE A  62      17.208  37.414   3.110  1.00 14.13           C  
ANISOU  515  CG2 ILE A  62     2736   1395   1238    413   -446   -294       C  
ATOM    516  CD1 ILE A  62      19.947  37.850   1.571  1.00 15.46           C  
ANISOU  516  CD1 ILE A  62     2738   2108   1027    530   -114    245       C  
ATOM    517  N   ILE A  63      16.340  40.550   3.488  1.00 17.90           N  
ANISOU  517  N   ILE A  63     2641   2521   1639    644   -516   -366       N  
ATOM    518  CA  ILE A  63      15.067  41.004   4.052  1.00 19.79           C  
ANISOU  518  CA  ILE A  63     2558   3124   1838    664   -651   -650       C  
ATOM    519  C   ILE A  63      14.054  39.880   4.063  1.00 18.45           C  
ANISOU  519  C   ILE A  63     2355   3224   1431    674   -825   -682       C  
ATOM    520  O   ILE A  63      13.905  39.123   3.115  1.00 19.94           O  
ANISOU  520  O   ILE A  63     3341   2707   1526    742   -581   -611       O  
ATOM    521  CB  ILE A  63      14.577  42.196   3.238  1.00 22.57           C  
ANISOU  521  CB  ILE A  63     2630   3061   2885    913   -694   -492       C  
ATOM    522  CG1 ILE A  63      15.560  43.365   3.286  1.00 24.71           C  
ANISOU  522  CG1 ILE A  63     3074   3078   3235    700   -811   -420       C  
ATOM    523  CG2 ILE A  63      13.200  42.589   3.703  1.00 27.41           C  
ANISOU  523  CG2 ILE A  63     2925   3820   3668   1191   -152   -149       C  
ATOM    524  CD1 ILE A  63      15.326  44.356   2.171  1.00 28.93           C  
ANISOU  524  CD1 ILE A  63     3576   3160   4256    777  -1122    115       C  
ATOM    525  N   ILE A  64      13.353  39.767   5.173  1.00 19.82           N  
ANISOU  525  N   ILE A  64     2479   3297   1754    660   -501   -895       N  
ATOM    526  CA  ILE A  64      12.319  38.773   5.309  1.00 21.35           C  
ANISOU  526  CA  ILE A  64     2706   3256   2148    608   -334   -708       C  
ATOM    527  C   ILE A  64      11.057  39.429   5.854  1.00 21.14           C  
ANISOU  527  C   ILE A  64     2795   2916   2320    427    -83   -609       C  
ATOM    528  O   ILE A  64      11.201  40.338   6.670  1.00 27.70           O  
ANISOU  528  O   ILE A  64     3004   4365   3158    485    -75  -1789       O  
ATOM    529  CB  ILE A  64      12.734  37.642   6.261  1.00 25.44           C  
ANISOU  529  CB  ILE A  64     2849   3946   2872    816    -72     25       C  
ATOM    530  CG1 ILE A  64      13.870  36.766   5.786  1.00 28.21           C  
ANISOU  530  CG1 ILE A  64     3393   3949   3375   1215   -130     37       C  
ATOM    531  CG2 ILE A  64      11.519  36.781   6.570  1.00 33.52           C  
ANISOU  531  CG2 ILE A  64     3856   4970   3911    129    658    632       C  
ATOM    532  CD1 ILE A  64      14.125  35.515   6.599  1.00 33.92           C  
ANISOU  532  CD1 ILE A  64     4324   4979   3584   1780   -940    612       C  
ATOM    533  N   GLU A  65       9.885  39.007   5.436  1.00 18.07           N  
ANISOU  533  N   GLU A  65     2688   1968   2210    218    214    111       N  
ATOM    534  CA  GLU A  65       8.608  39.392   5.997  1.00 18.70           C  
ANISOU  534  CA  GLU A  65     2841   2302   1963    386    224    192       C  
ATOM    535  C   GLU A  65       8.078  38.245   6.844  1.00 18.06           C  
ANISOU  535  C   GLU A  65     2731   2306   1824     58     94     -4       C  
ATOM    536  O   GLU A  65       7.871  37.168   6.277  1.00 20.24           O  
ANISOU  536  O   GLU A  65     3408   2526   1757   -183    -18   -104       O  
ATOM    537  CB  GLU A  65       7.572  39.731   4.927  1.00 24.03           C  
ANISOU  537  CB  GLU A  65     3078   3608   2446    866     82    674       C  
ATOM    538  CG  GLU A  65       6.253  40.157   5.555  1.00 31.31           C  
ANISOU  538  CG  GLU A  65     3286   5492   3119   1511    247    845       C  
ATOM    539  CD  GLU A  65       5.392  40.872   4.538  1.00 38.26           C  
ANISOU  539  CD  GLU A  65     3890   6644   4004   2343      3   1187       C  
ATOM    540  OE1 GLU A  65       5.799  40.925   3.356  1.00 46.99           O  
ANISOU  540  OE1 GLU A  65     5652   8423   3780   3126   -104   1912       O  
ATOM    541  OE2 GLU A  65       4.328  41.368   4.939  1.00 47.64           O  
ANISOU  541  OE2 GLU A  65     4430   7879   5794   3279     -3    751       O  
ATOM    542  N   ILE A  66       7.898  38.510   8.118  1.00 17.43           N  
ANISOU  542  N   ILE A  66     2740   2012   1870    304    199     19       N  
ATOM    543  CA  ILE A  66       7.546  37.465   9.089  1.00 17.59           C  
ANISOU  543  CA  ILE A  66     2659   2139   1884     73    -41    111       C  
ATOM    544  C   ILE A  66       6.173  37.843   9.664  1.00 19.34           C  
ANISOU  544  C   ILE A  66     2801   2428   2120     97    201    267       C  
ATOM    545  O   ILE A  66       6.101  38.850  10.367  1.00 20.26           O  
ANISOU  545  O   ILE A  66     2568   3166   1965    185     98   -204       O  
ATOM    546  CB  ILE A  66       8.549  37.244  10.233  1.00 19.47           C  
ANISOU  546  CB  ILE A  66     2874   2513   2012   -266   -282    234       C  
ATOM    547  CG1 ILE A  66       9.962  36.879   9.742  1.00 19.54           C  
ANISOU  547  CG1 ILE A  66     2831   2636   1956    -69   -553    231       C  
ATOM    548  CG2 ILE A  66       8.085  36.203  11.261  1.00 19.83           C  
ANISOU  548  CG2 ILE A  66     3091   2594   1850   -973   -822    157       C  
ATOM    549  CD1 ILE A  66      11.094  37.233  10.686  1.00 20.20           C  
ANISOU  549  CD1 ILE A  66     3129   2028   2517    213  -1043    187       C  
ATOM    550  N   ALA A  67       5.200  37.004   9.309  1.00 19.03           N  
ANISOU  550  N   ALA A  67     2517   2541   2172    371   -126    232       N  
ATOM    551  CA  ALA A  67       3.824  37.225   9.684  1.00 20.21           C  
ANISOU  551  CA  ALA A  67     2684   2477   2518    333    201   -113       C  
ATOM    552  C   ALA A  67       3.487  38.687   9.422  1.00 20.94           C  
ANISOU  552  C   ALA A  67     2776   2521   2659    443    483     58       C  
ATOM    553  O   ALA A  67       2.851  39.297  10.293  1.00 23.07           O  
ANISOU  553  O   ALA A  67     2288   3045   3433    810    787     19       O  
ATOM    554  CB  ALA A  67       3.600  36.814  11.139  1.00 23.17           C  
ANISOU  554  CB  ALA A  67     3596   2475   2734    625    698     87       C  
ATOM    555  N   GLY A  68       3.906  39.228   8.279  1.00 21.97           N  
ANISOU  555  N   GLY A  68     2796   2784   2768    192    359    178       N  
ATOM    556  CA  GLY A  68       3.594  40.614   7.945  1.00 22.81           C  
ANISOU  556  CA  GLY A  68     2595   2991   3081    164    -92    559       C  
ATOM    557  C   GLY A  68       4.529  41.654   8.514  1.00 23.64           C  
ANISOU  557  C   GLY A  68     2836   2730   3416    252   -183    493       C  
ATOM    558  O   GLY A  68       4.359  42.879   8.344  1.00 27.89           O  
ANISOU  558  O   GLY A  68     3373   2706   4517    283    181    673       O  
ATOM    559  N   HIS A  69       5.570  41.200   9.221  1.00 24.02           N  
ANISOU  559  N   HIS A  69     2440   3271   3414    373    -62    161       N  
ATOM    560  CA  HIS A  69       6.518  42.138   9.803  1.00 23.22           C  
ANISOU  560  CA  HIS A  69     2531   2916   3376    614     50    -97       C  
ATOM    561  C   HIS A  69       7.850  42.031   9.062  1.00 22.22           C  
ANISOU  561  C   HIS A  69     2291   2856   3297    640   -171    161       C  
ATOM    562  O   HIS A  69       8.416  40.946   8.984  1.00 20.88           O  
ANISOU  562  O   HIS A  69     2343   2698   2892    491    -54     34       O  
ATOM    563  CB  HIS A  69       6.726  41.876  11.292  1.00 24.96           C  
ANISOU  563  CB  HIS A  69     3186   3003   3293    425     98   -257       C  
ATOM    564  CG  HIS A  69       5.588  42.177  12.196  1.00 28.50           C  
ANISOU  564  CG  HIS A  69     3794   3322   3714    297    738    -79       C  
ATOM    565  ND1 HIS A  69       4.427  41.436  12.227  1.00 30.32           N  
ANISOU  565  ND1 HIS A  69     3998   3607   3916     75   1001     41       N  
ATOM    566  CD2 HIS A  69       5.417  43.155  13.125  1.00 29.85           C  
ANISOU  566  CD2 HIS A  69     4130   3258   3952    346   1183    -84       C  
ATOM    567  CE1 HIS A  69       3.595  41.942  13.131  1.00 31.42           C  
ANISOU  567  CE1 HIS A  69     4298   3774   3867     50   1223    124       C  
ATOM    568  NE2 HIS A  69       4.176  42.990  13.690  1.00 30.96           N  
ANISOU  568  NE2 HIS A  69     4463   3459   3843    116   1412    216       N  
ATOM    569  N   LYS A  70       8.369  43.113   8.523  1.00 23.38           N  
ANISOU  569  N   LYS A  70     2300   2835   3749    823   -106    363       N  
ATOM    570  CA  LYS A  70       9.642  43.171   7.815  1.00 24.25           C  
ANISOU  570  CA  LYS A  70     2437   3160   3617    455    -19    102       C  
ATOM    571  C   LYS A  70      10.813  43.237   8.797  1.00 23.15           C  
ANISOU  571  C   LYS A  70     2289   3001   3506    521    123   -402       C  
ATOM    572  O   LYS A  70      10.866  43.936   9.813  1.00 26.06           O  
ANISOU  572  O   LYS A  70     1841   3418   4643    719    113  -1372       O  
ATOM    573  CB  LYS A  70       9.708  44.368   6.860  1.00 29.78           C  
ANISOU  573  CB  LYS A  70     3553   3876   3886   -226   -251    639       C  
ATOM    574  CG  LYS A  70       8.726  44.410   5.713  1.00 36.48           C  
ANISOU  574  CG  LYS A  70     4472   4754   4634   -189  -1065   1214       C  
ATOM    575  CD  LYS A  70       8.619  45.750   4.981  1.00 40.73           C  
ANISOU  575  CD  LYS A  70     5217   5050   5209   -360  -1301   1629       C  
ATOM    576  CE  LYS A  70       7.244  45.933   4.352  1.00 43.50           C  
ANISOU  576  CE  LYS A  70     5664   5394   5471    -89  -1759   1771       C  
ATOM    577  NZ  LYS A  70       6.785  47.351   4.220  1.00 47.57           N  
ANISOU  577  NZ  LYS A  70     6257   5597   6219    416  -1794   1407       N  
ATOM    578  N   ALA A  71      11.824  42.445   8.463  1.00 21.37           N  
ANISOU  578  N   ALA A  71     2304   2888   2928    389    -26   -733       N  
ATOM    579  CA  ALA A  71      13.056  42.364   9.214  1.00 19.88           C  
ANISOU  579  CA  ALA A  71     2204   2709   2641    427    145   -963       C  
ATOM    580  C   ALA A  71      14.182  42.156   8.218  1.00 19.04           C  
ANISOU  580  C   ALA A  71     2332   2620   2281    462     62   -981       C  
ATOM    581  O   ALA A  71      13.920  41.649   7.133  1.00 28.96           O  
ANISOU  581  O   ALA A  71     2448   5566   2989    391    -70  -2322       O  
ATOM    582  CB  ALA A  71      13.018  41.248  10.229  1.00 24.24           C  
ANISOU  582  CB  ALA A  71     2996   3853   2363    422    129   -455       C  
ATOM    583  N   ILE A  72      15.382  42.545   8.599  1.00 15.64           N  
ANISOU  583  N   ILE A  72     2268   1978   1695    566     81   -445       N  
ATOM    584  CA  ILE A  72      16.578  42.208   7.821  1.00 14.58           C  
ANISOU  584  CA  ILE A  72     2415   1774   1352    454    263     51       C  
ATOM    585  C   ILE A  72      17.614  41.553   8.710  1.00 13.34           C  
ANISOU  585  C   ILE A  72     2150   1608   1312    334    380     42       C  
ATOM    586  O   ILE A  72      17.763  41.906   9.893  1.00 13.80           O  
ANISOU  586  O   ILE A  72     2572   1147   1525    530     76   -200       O  
ATOM    587  CB  ILE A  72      17.167  43.459   7.143  1.00 17.02           C  
ANISOU  587  CB  ILE A  72     3208   1543   1716    513    279    136       C  
ATOM    588  CG1 ILE A  72      18.329  43.134   6.193  1.00 18.27           C  
ANISOU  588  CG1 ILE A  72     3402   1495   2044    173    727    387       C  
ATOM    589  CG2 ILE A  72      17.596  44.508   8.144  1.00 21.47           C  
ANISOU  589  CG2 ILE A  72     4648   1510   1997    231    236     29       C  
ATOM    590  CD1 ILE A  72      18.665  44.242   5.210  1.00 23.29           C  
ANISOU  590  CD1 ILE A  72     4947   1329   2575   -767    901    224       C  
ATOM    591  N   GLY A  73      18.339  40.585   8.139  1.00 12.74           N  
ANISOU  591  N   GLY A  73     2128   1568   1145    231    146   -131       N  
ATOM    592  CA  GLY A  73      19.392  39.951   8.901  1.00 11.90           C  
ANISOU  592  CA  GLY A  73     1996   1321   1205    100    161    -43       C  
ATOM    593  C   GLY A  73      19.991  38.828   8.083  1.00 11.28           C  
ANISOU  593  C   GLY A  73     1944   1243   1101    -10    110    -16       C  
ATOM    594  O   GLY A  73      19.755  38.690   6.895  1.00 12.69           O  
ANISOU  594  O   GLY A  73     2006   1528   1288    172   -109   -261       O  
ATOM    595  N   THR A  74      20.783  38.036   8.791  1.00 12.50           N  
ANISOU  595  N   THR A  74     2352   1221   1176    171    213    158       N  
ATOM    596  CA  THR A  74      21.478  36.910   8.224  1.00 11.80           C  
ANISOU  596  CA  THR A  74     1988   1271   1225      1    276     69       C  
ATOM    597  C   THR A  74      20.501  35.744   8.162  1.00 11.72           C  
ANISOU  597  C   THR A  74     1906   1354   1193     49    398    -44       C  
ATOM    598  O   THR A  74      19.709  35.484   9.085  1.00 11.88           O  
ANISOU  598  O   THR A  74     1668   1574   1273     65    432   -156       O  
ATOM    599  CB  THR A  74      22.730  36.590   9.064  1.00 13.19           C  
ANISOU  599  CB  THR A  74     1908   1597   1508     71    269     -4       C  
ATOM    600  OG1 THR A  74      23.658  37.691   8.941  1.00 14.04           O  
ANISOU  600  OG1 THR A  74     1961   1551   1821     36     86     -9       O  
ATOM    601  CG2 THR A  74      23.403  35.313   8.578  1.00 12.70           C  
ANISOU  601  CG2 THR A  74     2019   1535   1271    101    160     12       C  
ATOM    602  N   VAL A  75      20.570  35.043   7.030  1.00 11.37           N  
ANISOU  602  N   VAL A  75     1866   1364   1090     -6    359      6       N  
ATOM    603  CA  VAL A  75      19.791  33.854   6.816  1.00 10.46           C  
ANISOU  603  CA  VAL A  75     1808   1155   1013     76    227    245       C  
ATOM    604  C   VAL A  75      20.737  32.751   6.362  1.00 10.25           C  
ANISOU  604  C   VAL A  75     1603   1284   1007     37    116    101       C  
ATOM    605  O   VAL A  75      21.515  32.955   5.455  1.00 11.04           O  
ANISOU  605  O   VAL A  75     1654   1279   1261     87    241    193       O  
ATOM    606  CB  VAL A  75      18.703  34.045   5.762  1.00 10.58           C  
ANISOU  606  CB  VAL A  75     1628   1367   1024    171    312    225       C  
ATOM    607  CG1 VAL A  75      17.969  32.764   5.463  1.00 12.19           C  
ANISOU  607  CG1 VAL A  75     1896   1466   1268    182     46      4       C  
ATOM    608  CG2 VAL A  75      17.711  35.091   6.254  1.00 15.03           C  
ANISOU  608  CG2 VAL A  75     2195   1831   1686    640   -160   -473       C  
ATOM    609  N   LEU A  76      20.607  31.621   7.048  1.00  9.95           N  
ANISOU  609  N   LEU A  76     1525   1327    929    265    211    128       N  
ATOM    610  CA  LEU A  76      21.350  30.426   6.721  1.00  9.33           C  
ANISOU  610  CA  LEU A  76     1461   1296    787    144    380     -2       C  
ATOM    611  C   LEU A  76      20.495  29.518   5.859  1.00 10.69           C  
ANISOU  611  C   LEU A  76     1667   1504    890    -92    333      4       C  
ATOM    612  O   LEU A  76      19.344  29.335   6.200  1.00 12.50           O  
ANISOU  612  O   LEU A  76     1825   1986    937   -381    435    -11       O  
ATOM    613  CB  LEU A  76      21.759  29.733   8.002  1.00  9.82           C  
ANISOU  613  CB  LEU A  76     1523   1295    914    381    299    -22       C  
ATOM    614  CG  LEU A  76      22.447  30.621   9.048  1.00 10.54           C  
ANISOU  614  CG  LEU A  76     1676   1463    866    201    252     22       C  
ATOM    615  CD1 LEU A  76      22.809  29.774  10.271  1.00 11.54           C  
ANISOU  615  CD1 LEU A  76     2080   1258   1046   -196     42    112       C  
ATOM    616  CD2 LEU A  76      23.678  31.325   8.492  1.00 10.94           C  
ANISOU  616  CD2 LEU A  76     1721   1194   1243    241    142    319       C  
ATOM    617  N   VAL A  77      21.065  28.985   4.789  1.00 10.69           N  
ANISOU  617  N   VAL A  77     1930   1266    866   -160    349     11       N  
ATOM    618  CA  VAL A  77      20.324  28.154   3.855  1.00 10.91           C  
ANISOU  618  CA  VAL A  77     1966   1275    903   -101    253     46       C  
ATOM    619  C   VAL A  77      21.006  26.799   3.777  1.00 11.18           C  
ANISOU  619  C   VAL A  77     1917   1297   1033   -128    215    -41       C  
ATOM    620  O   VAL A  77      22.213  26.719   3.527  1.00 11.62           O  
ANISOU  620  O   VAL A  77     1879   1429   1108   -161    220   -213       O  
ATOM    621  CB  VAL A  77      20.253  28.776   2.459  1.00 11.20           C  
ANISOU  621  CB  VAL A  77     1959   1527    770    212    454    -26       C  
ATOM    622  CG1 VAL A  77      19.518  27.841   1.508  1.00 13.44           C  
ANISOU  622  CG1 VAL A  77     2613   1310   1185    192   -413    358       C  
ATOM    623  CG2 VAL A  77      19.576  30.139   2.493  1.00 13.04           C  
ANISOU  623  CG2 VAL A  77     2433   1504   1018    284    403    121       C  
ATOM    624  N   GLY A  78      20.205  25.749   4.005  1.00 10.93           N  
ANISOU  624  N   GLY A  78     1908   1298    947   -118     42    146       N  
ATOM    625  CA  GLY A  78      20.756  24.409   3.980  1.00 11.61           C  
ANISOU  625  CA  GLY A  78     2134   1321    956      8   -149    166       C  
ATOM    626  C   GLY A  78      19.701  23.363   4.298  1.00 11.67           C  
ANISOU  626  C   GLY A  78     2013   1167   1255     -6     -7   -228       C  
ATOM    627  O   GLY A  78      18.511  23.665   4.357  1.00 13.31           O  
ANISOU  627  O   GLY A  78     2105   1320   1632    208    122    221       O  
ATOM    628  N   PRO A  79      20.176  22.140   4.492  1.00 11.92           N  
ANISOU  628  N   PRO A  79     1842   1241   1448     28     23   -179       N  
ATOM    629  CA  PRO A  79      19.259  21.001   4.623  1.00 12.25           C  
ANISOU  629  CA  PRO A  79     1930   1161   1563     93    225     -5       C  
ATOM    630  C   PRO A  79      18.702  20.882   6.024  1.00 12.01           C  
ANISOU  630  C   PRO A  79     2113   1075   1374    -76     17   -211       C  
ATOM    631  O   PRO A  79      18.902  19.897   6.722  1.00 15.65           O  
ANISOU  631  O   PRO A  79     2846   1581   1519    418    384     96       O  
ATOM    632  CB  PRO A  79      20.154  19.802   4.297  1.00 13.70           C  
ANISOU  632  CB  PRO A  79     1988   1284   1932    122    346    -41       C  
ATOM    633  CG  PRO A  79      21.506  20.261   4.786  1.00 14.92           C  
ANISOU  633  CG  PRO A  79     2080   1604   1985    321    -32    -67       C  
ATOM    634  CD  PRO A  79      21.585  21.747   4.576  1.00 13.53           C  
ANISOU  634  CD  PRO A  79     1897   1592   1652     48   -326   -116       C  
ATOM    635  N   THR A  80      17.990  21.923   6.417  1.00 13.11           N  
ANISOU  635  N   THR A  80     2095   1390   1496     82    216   -126       N  
ATOM    636  CA  THR A  80      17.242  21.896   7.677  1.00 11.91           C  
ANISOU  636  CA  THR A  80     2010   1110   1406    241    121    229       C  
ATOM    637  C   THR A  80      15.918  21.187   7.420  1.00 12.67           C  
ANISOU  637  C   THR A  80     2122   1167   1525    131    130    204       C  
ATOM    638  O   THR A  80      15.256  21.340   6.380  1.00 15.20           O  
ANISOU  638  O   THR A  80     2357   1789   1629   -187    -78    328       O  
ATOM    639  CB  THR A  80      17.033  23.298   8.259  1.00 10.97           C  
ANISOU  639  CB  THR A  80     1641   1209   1319    316     83    164       C  
ATOM    640  OG1 THR A  80      16.214  23.180   9.421  1.00 13.28           O  
ANISOU  640  OG1 THR A  80     2107   1785   1154    228    116    140       O  
ATOM    641  CG2 THR A  80      16.280  24.199   7.297  1.00  9.79           C  
ANISOU  641  CG2 THR A  80     1400   1227   1094    353    122    -43       C  
ATOM    642  N   PRO A  81      15.492  20.360   8.371  1.00 14.36           N  
ANISOU  642  N   PRO A  81     2631   1260   1565   -195     90    201       N  
ATOM    643  CA  PRO A  81      14.220  19.653   8.166  1.00 16.06           C  
ANISOU  643  CA  PRO A  81     2813   1479   1809   -423    128    251       C  
ATOM    644  C   PRO A  81      13.008  20.565   8.297  1.00 15.39           C  
ANISOU  644  C   PRO A  81     2577   1544   1728   -582     79     57       C  
ATOM    645  O   PRO A  81      11.914  20.191   7.866  1.00 18.29           O  
ANISOU  645  O   PRO A  81     2892   1880   2176   -391   -365   -530       O  
ATOM    646  CB  PRO A  81      14.166  18.621   9.299  1.00 18.42           C  
ANISOU  646  CB  PRO A  81     3151   1759   2090   -562    102    532       C  
ATOM    647  CG  PRO A  81      15.249  18.979  10.232  1.00 19.42           C  
ANISOU  647  CG  PRO A  81     3371   1957   2050   -611    -35    749       C  
ATOM    648  CD  PRO A  81      16.150  20.019   9.641  1.00 16.03           C  
ANISOU  648  CD  PRO A  81     2816   1672   1602   -265    130    446       C  
ATOM    649  N   VAL A  82      13.173  21.730   8.876  1.00 14.96           N  
ANISOU  649  N   VAL A  82     2382   1740   1562   -603    239   -183       N  
ATOM    650  CA  VAL A  82      12.105  22.677   9.120  1.00 14.64           C  
ANISOU  650  CA  VAL A  82     2299   1785   1479   -598    275    -36       C  
ATOM    651  C   VAL A  82      12.600  24.079   8.880  1.00 13.47           C  
ANISOU  651  C   VAL A  82     2040   1793   1286   -512    186    126       C  
ATOM    652  O   VAL A  82      13.738  24.360   9.262  1.00 14.10           O  
ANISOU  652  O   VAL A  82     2009   1555   1794   -303     27    133       O  
ATOM    653  CB AVAL A  82      11.564  22.598  10.571  0.60 17.43           C  
ANISOU  653  CB AVAL A  82     2622   2106   1894   -608    807    256       C  
ATOM    654  CB BVAL A  82      11.622  22.558  10.573  0.40 17.18           C  
ANISOU  654  CB BVAL A  82     2604   2088   1835   -492    746    317       C  
ATOM    655  CG1AVAL A  82      10.387  23.547  10.757  0.60 17.43           C  
ANISOU  655  CG1AVAL A  82     2186   2197   2241   -874    975    321       C  
ATOM    656  CG1BVAL A  82      10.814  21.310  10.828  0.40 20.50           C  
ANISOU  656  CG1BVAL A  82     3039   2157   2594   -604   1002    405       C  
ATOM    657  CG2AVAL A  82      11.156  21.181  10.949  0.60 21.48           C  
ANISOU  657  CG2AVAL A  82     3218   2261   2685   -681    964    578       C  
ATOM    658  CG2BVAL A  82      12.908  22.622  11.385  0.40 18.32           C  
ANISOU  658  CG2BVAL A  82     3205   2523   1234   -468    461    142       C  
ATOM    659  N   ASN A  83      11.870  25.002   8.293  1.00 12.81           N  
ANISOU  659  N   ASN A  83     2015   1756   1096   -524    -88   -217       N  
ATOM    660  CA  ASN A  83      12.338  26.383   8.246  1.00 12.03           C  
ANISOU  660  CA  ASN A  83     2021   1629    923   -289    -18   -310       C  
ATOM    661  C   ASN A  83      12.226  26.999   9.625  1.00 10.98           C  
ANISOU  661  C   ASN A  83     1792   1622    757   -187     78   -124       C  
ATOM    662  O   ASN A  83      11.146  26.886  10.214  1.00 11.60           O  
ANISOU  662  O   ASN A  83     1835   1559   1013    -20    149    249       O  
ATOM    663  CB  ASN A  83      11.503  27.174   7.266  1.00 12.01           C  
ANISOU  663  CB  ASN A  83     1895   1908    762   -478     23   -143       C  
ATOM    664  CG  ASN A  83      11.576  26.680   5.832  1.00 12.86           C  
ANISOU  664  CG  ASN A  83     1713   2314    861   -416     75   -418       C  
ATOM    665  OD1 ASN A  83      12.660  26.341   5.362  1.00 16.53           O  
ANISOU  665  OD1 ASN A  83     1777   3424   1080   -160    138   -408       O  
ATOM    666  ND2 ASN A  83      10.445  26.635   5.141  1.00 14.47           N  
ANISOU  666  ND2 ASN A  83     1970   2678    849    225   -173   -363       N  
ATOM    667  N   ILE A  84      13.263  27.620  10.117  1.00 11.07           N  
ANISOU  667  N   ILE A  84     1805   1713    689   -105     29   -278       N  
ATOM    668  CA  ILE A  84      13.326  28.189  11.446  1.00 10.72           C  
ANISOU  668  CA  ILE A  84     1891   1509    673   -116    184   -156       C  
ATOM    669  C   ILE A  84      13.658  29.664  11.437  1.00 11.25           C  
ANISOU  669  C   ILE A  84     1641   1565   1068   -182    105   -301       C  
ATOM    670  O   ILE A  84      14.675  30.078  10.877  1.00 11.57           O  
ANISOU  670  O   ILE A  84     1728   1463   1207    147    203    290       O  
ATOM    671  CB  ILE A  84      14.418  27.460  12.256  1.00 14.10           C  
ANISOU  671  CB  ILE A  84     2647   1980    729   -170   -243    197       C  
ATOM    672  CG1 ILE A  84      13.947  26.029  12.555  1.00 14.51           C  
ANISOU  672  CG1 ILE A  84     2425   1734   1355    138   -408     42       C  
ATOM    673  CG2 ILE A  84      14.850  28.263  13.471  1.00 19.94           C  
ANISOU  673  CG2 ILE A  84     3618   2472   1487   -568   -958   -108       C  
ATOM    674  CD1 ILE A  84      15.158  25.100  12.489  1.00 24.25           C  
ANISOU  674  CD1 ILE A  84     3310   2723   3181   1014   1069    766       C  
ATOM    675  N   ILE A  85      12.786  30.428  12.065  1.00 10.94           N  
ANISOU  675  N   ILE A  85     1754   1522    882   -300    165   -362       N  
ATOM    676  CA  ILE A  85      13.052  31.824  12.366  1.00 11.31           C  
ANISOU  676  CA  ILE A  85     1894   1435    968   -189    -65   -166       C  
ATOM    677  C   ILE A  85      13.693  31.883  13.750  1.00 11.51           C  
ANISOU  677  C   ILE A  85     1910   1524    938   -213    -43   -332       C  
ATOM    678  O   ILE A  85      13.026  31.568  14.742  1.00 11.17           O  
ANISOU  678  O   ILE A  85     1617   1643    985    131    -41   -176       O  
ATOM    679  CB  ILE A  85      11.783  32.687  12.307  1.00 11.45           C  
ANISOU  679  CB  ILE A  85     1930   1618    803    -58    158   -120       C  
ATOM    680  CG1 ILE A  85      11.049  32.601  10.976  1.00 13.60           C  
ANISOU  680  CG1 ILE A  85     2162   2005    999    171   -110    -89       C  
ATOM    681  CG2 ILE A  85      12.097  34.131  12.623  1.00 14.58           C  
ANISOU  681  CG2 ILE A  85     1949   1574   2015     32   -410   -109       C  
ATOM    682  CD1 ILE A  85      11.967  32.848   9.776  1.00 15.58           C  
ANISOU  682  CD1 ILE A  85     1993   3146    781    392   -359    291       C  
ATOM    683  N   GLY A  86      14.971  32.276  13.777  1.00 10.77           N  
ANISOU  683  N   GLY A  86     1954   1225    912   -222    -81    -81       N  
ATOM    684  CA  GLY A  86      15.734  32.315  15.012  1.00 10.60           C  
ANISOU  684  CA  GLY A  86     1852   1212    964     67   -102   -275       C  
ATOM    685  C   GLY A  86      15.767  33.691  15.646  1.00 10.03           C  
ANISOU  685  C   GLY A  86     1817   1081    912      2    -95   -103       C  
ATOM    686  O   GLY A  86      15.169  34.659  15.142  1.00  9.91           O  
ANISOU  686  O   GLY A  86     1676   1225    864     97    -40    -80       O  
ATOM    687  N   ARG A  87      16.472  33.778  16.764  1.00  9.41           N  
ANISOU  687  N   ARG A  87     1769   1019    787    104      3   -145       N  
ATOM    688  CA  ARG A  87      16.433  35.006  17.561  1.00  9.99           C  
ANISOU  688  CA  ARG A  87     1857    960    979   -167    128   -170       C  
ATOM    689  C   ARG A  87      16.934  36.210  16.787  1.00 10.11           C  
ANISOU  689  C   ARG A  87     1731   1124    988   -213    135    -84       C  
ATOM    690  O   ARG A  87      16.441  37.311  17.034  1.00 11.62           O  
ANISOU  690  O   ARG A  87     2289   1075   1053   -113    347     40       O  
ATOM    691  CB  ARG A  87      17.243  34.813  18.847  1.00  9.71           C  
ANISOU  691  CB  ARG A  87     1923    806    959   -333     77   -204       C  
ATOM    692  CG  ARG A  87      16.580  33.812  19.790  1.00 10.22           C  
ANISOU  692  CG  ARG A  87     1944    929   1011   -474     44   -168       C  
ATOM    693  CD  ARG A  87      17.265  33.792  21.136  1.00 11.44           C  
ANISOU  693  CD  ARG A  87     1939   1411    999   -380     99     26       C  
ATOM    694  NE  ARG A  87      18.646  33.371  20.981  1.00 11.26           N  
ANISOU  694  NE  ARG A  87     2044   1233   1004   -210     66    -78       N  
ATOM    695  CZ  ARG A  87      19.734  34.133  20.929  1.00 11.13           C  
ANISOU  695  CZ  ARG A  87     1793   1183   1252    -39   -344   -200       C  
ATOM    696  NH1 ARG A  87      19.688  35.468  21.022  1.00 12.87           N  
ANISOU  696  NH1 ARG A  87     1780   1209   1902    -87   -319   -504       N  
ATOM    697  NH2 ARG A  87      20.927  33.562  20.780  1.00 12.40           N  
ANISOU  697  NH2 ARG A  87     1946   1418   1349    166    -77   -111       N  
ATOM    698  N   ASN A  88      17.873  36.026  15.873  1.00 10.81           N  
ANISOU  698  N   ASN A  88     1732   1372   1003     36    103    181       N  
ATOM    699  CA  ASN A  88      18.393  37.173  15.128  1.00 10.77           C  
ANISOU  699  CA  ASN A  88     1876   1378    838    -83    111    102       C  
ATOM    700  C   ASN A  88      17.286  37.933  14.409  1.00 11.12           C  
ANISOU  700  C   ASN A  88     1931   1104   1189    -35    102    109       C  
ATOM    701  O   ASN A  88      17.460  39.146  14.188  1.00 12.78           O  
ANISOU  701  O   ASN A  88     2365   1072   1421   -107     20    -24       O  
ATOM    702  CB  ASN A  88      19.458  36.692  14.147  1.00 10.05           C  
ANISOU  702  CB  ASN A  88     1862   1294    665    -20     -7    193       C  
ATOM    703  CG  ASN A  88      18.923  35.968  12.943  1.00 10.03           C  
ANISOU  703  CG  ASN A  88     1863   1217    733    105   -119    166       C  
ATOM    704  OD1 ASN A  88      18.209  34.989  13.082  1.00 11.96           O  
ANISOU  704  OD1 ASN A  88     1846   1514   1182    -84   -216    145       O  
ATOM    705  ND2 ASN A  88      19.263  36.442  11.751  1.00 12.55           N  
ANISOU  705  ND2 ASN A  88     2542   1521    704     25   -372    364       N  
ATOM    706  N   LEU A  89      16.193  37.259  14.056  1.00 10.99           N  
ANISOU  706  N   LEU A  89     1967    971   1238     71    -62     84       N  
ATOM    707  CA  LEU A  89      15.087  37.973  13.412  1.00 10.73           C  
ANISOU  707  CA  LEU A  89     2056    893   1126     38    -24    174       C  
ATOM    708  C   LEU A  89      13.893  38.131  14.357  1.00 10.77           C  
ANISOU  708  C   LEU A  89     1962    973   1155    103    -57    262       C  
ATOM    709  O   LEU A  89      13.122  39.103  14.187  1.00 12.46           O  
ANISOU  709  O   LEU A  89     2306   1177   1250    375     26    383       O  
ATOM    710  CB  LEU A  89      14.628  37.294  12.119  1.00 11.34           C  
ANISOU  710  CB  LEU A  89     2209    996   1104     11    -87    188       C  
ATOM    711  CG  LEU A  89      15.640  37.233  10.984  1.00 12.74           C  
ANISOU  711  CG  LEU A  89     2376   1219   1244    243     43    -12       C  
ATOM    712  CD1 LEU A  89      15.036  36.500   9.787  1.00 15.29           C  
ANISOU  712  CD1 LEU A  89     3149   1431   1228    216    -82   -117       C  
ATOM    713  CD2 LEU A  89      16.085  38.607  10.573  1.00 17.85           C  
ANISOU  713  CD2 LEU A  89     2935   1691   2159   -478    996   -187       C  
ATOM    714  N   LEU A  90      13.740  37.223  15.314  1.00 10.30           N  
ANISOU  714  N   LEU A  90     1945    950   1021     94    -92    202       N  
ATOM    715  CA  LEU A  90      12.628  37.442  16.256  1.00 10.41           C  
ANISOU  715  CA  LEU A  90     1902   1104    949     24   -144     22       C  
ATOM    716  C   LEU A  90      12.752  38.742  17.022  1.00 11.41           C  
ANISOU  716  C   LEU A  90     2027   1202   1105    -62    -25    -36       C  
ATOM    717  O   LEU A  90      11.759  39.389  17.347  1.00 12.34           O  
ANISOU  717  O   LEU A  90     2173   1004   1512    100   -115    -69       O  
ATOM    718  CB  LEU A  90      12.538  36.286  17.245  1.00 10.10           C  
ANISOU  718  CB  LEU A  90     1911   1166    759    199    -30    -48       C  
ATOM    719  CG  LEU A  90      12.262  34.913  16.619  1.00 11.09           C  
ANISOU  719  CG  LEU A  90     2223   1102    888     35    150     -5       C  
ATOM    720  CD1 LEU A  90      12.530  33.807  17.625  1.00 14.06           C  
ANISOU  720  CD1 LEU A  90     2646   1304   1394    -10    320    362       C  
ATOM    721  CD2 LEU A  90      10.835  34.867  16.105  1.00 14.24           C  
ANISOU  721  CD2 LEU A  90     2444   1323   1644   -290   -185    -97       C  
ATOM    722  N   THR A  91      13.991  39.139  17.321  1.00 10.90           N  
ANISOU  722  N   THR A  91     2092   1098    952   -216     -1    131       N  
ATOM    723  CA  THR A  91      14.176  40.382  18.033  1.00 11.85           C  
ANISOU  723  CA  THR A  91     2235   1156   1111   -125   -101      8       C  
ATOM    724  C   THR A  91      13.642  41.540  17.197  1.00 11.72           C  
ANISOU  724  C   THR A  91     2276   1170   1008    130   -154   -206       C  
ATOM    725  O   THR A  91      13.042  42.482  17.719  1.00 13.12           O  
ANISOU  725  O   THR A  91     2633   1049   1304     -8    319   -190       O  
ATOM    726  CB  THR A  91      15.654  40.685  18.372  1.00 11.31           C  
ANISOU  726  CB  THR A  91     2112   1057   1128    150    -84   -366       C  
ATOM    727  OG1 THR A  91      16.450  40.682  17.173  1.00 11.93           O  
ANISOU  727  OG1 THR A  91     2140   1364   1030     47   -141   -303       O  
ATOM    728  CG2 THR A  91      16.228  39.618  19.294  1.00 12.18           C  
ANISOU  728  CG2 THR A  91     2263   1154   1211    -42   -128   -155       C  
ATOM    729  N   GLN A  92      13.866  41.469  15.882  1.00 12.21           N  
ANISOU  729  N   GLN A  92     2393   1199   1048    291     66    -29       N  
ATOM    730  CA  GLN A  92      13.562  42.611  15.036  1.00 12.22           C  
ANISOU  730  CA  GLN A  92     2229   1146   1267    170    -37     73       C  
ATOM    731  C   GLN A  92      12.073  42.824  14.868  1.00 13.46           C  
ANISOU  731  C   GLN A  92     2225   1286   1602    211    161    274       C  
ATOM    732  O   GLN A  92      11.630  43.955  14.570  1.00 15.27           O  
ANISOU  732  O   GLN A  92     2200   1092   2509    212     33    -22       O  
ATOM    733  CB  GLN A  92      14.188  42.406  13.659  1.00 12.01           C  
ANISOU  733  CB  GLN A  92     1985   1338   1242   -171    -40    174       C  
ATOM    734  CG  GLN A  92      15.700  42.215  13.717  1.00 11.25           C  
ANISOU  734  CG  GLN A  92     2002   1188   1084   -153   -181    115       C  
ATOM    735  CD  GLN A  92      16.371  43.482  14.232  1.00 12.07           C  
ANISOU  735  CD  GLN A  92     2114   1201   1269   -205    -69    -29       C  
ATOM    736  OE1 GLN A  92      16.476  44.487  13.522  1.00 11.31           O  
ANISOU  736  OE1 GLN A  92     1879   1023   1396     61    325    -91       O  
ATOM    737  NE2 GLN A  92      16.805  43.373  15.477  1.00 11.83           N  
ANISOU  737  NE2 GLN A  92     2059   1027   1409    105   -257   -227       N  
ATOM    738  N   ILE A  93      11.290  41.748  15.049  1.00 12.90           N  
ANISOU  738  N   ILE A  93     2123   1306   1474    274    136    435       N  
ATOM    739  CA  ILE A  93       9.844  41.938  15.024  1.00 13.58           C  
ANISOU  739  CA  ILE A  93     2100   1407   1651    311     70     67       C  
ATOM    740  C   ILE A  93       9.267  42.153  16.417  1.00 14.31           C  
ANISOU  740  C   ILE A  93     2058   1684   1694    202    145     81       C  
ATOM    741  O   ILE A  93       8.049  42.220  16.569  1.00 15.84           O  
ANISOU  741  O   ILE A  93     2068   1968   1982    183    280    281       O  
ATOM    742  CB  ILE A  93       9.153  40.730  14.374  1.00 14.79           C  
ANISOU  742  CB  ILE A  93     2301   1460   1856    376   -241     29       C  
ATOM    743  CG1 ILE A  93       9.265  39.421  15.143  1.00 14.72           C  
ANISOU  743  CG1 ILE A  93     2326   1313   1954    425   -494    -88       C  
ATOM    744  CG2 ILE A  93       9.691  40.578  12.955  1.00 18.71           C  
ANISOU  744  CG2 ILE A  93     3276   2082   1749    307   -238   -178       C  
ATOM    745  CD1 ILE A  93       8.428  38.309  14.544  1.00 16.97           C  
ANISOU  745  CD1 ILE A  93     2404   1860   2182   -285   -356    204       C  
ATOM    746  N   GLY A  94      10.124  42.268  17.414  1.00 15.04           N  
ANISOU  746  N   GLY A  94     2228   1868   1620    279    133     66       N  
ATOM    747  CA  GLY A  94       9.723  42.534  18.771  1.00 14.04           C  
ANISOU  747  CA  GLY A  94     2399   1238   1699    287    120     46       C  
ATOM    748  C   GLY A  94       9.091  41.351  19.477  1.00 14.61           C  
ANISOU  748  C   GLY A  94     2269   1335   1947    277    474    -19       C  
ATOM    749  O   GLY A  94       8.226  41.557  20.344  1.00 19.54           O  
ANISOU  749  O   GLY A  94     3148   1848   2429    656   1128    116       O  
ATOM    750  N   ALA A  95       9.512  40.140  19.121  1.00 13.53           N  
ANISOU  750  N   ALA A  95     2006   1232   1904    175    363     40       N  
ATOM    751  CA  ALA A  95       8.908  38.987  19.759  1.00 13.29           C  
ANISOU  751  CA  ALA A  95     1920   1333   1797    428    672    140       C  
ATOM    752  C   ALA A  95       9.485  38.746  21.139  1.00 13.86           C  
ANISOU  752  C   ALA A  95     1995   1444   1827    216    497     58       C  
ATOM    753  O   ALA A  95      10.697  38.806  21.308  1.00 15.06           O  
ANISOU  753  O   ALA A  95     2050   1701   1970    -88    476     77       O  
ATOM    754  CB  ALA A  95       9.122  37.733  18.936  1.00 13.78           C  
ANISOU  754  CB  ALA A  95     2119   1253   1862      1    669     67       C  
ATOM    755  N   THR A  96       8.584  38.471  22.057  1.00 13.86           N  
ANISOU  755  N   THR A  96     1861   1658   1749    243    295    233       N  
ATOM    756  CA  THR A  96       8.943  38.096  23.402  1.00 13.98           C  
ANISOU  756  CA  THR A  96     1990   1623   1697    227    295    120       C  
ATOM    757  C   THR A  96       8.181  36.840  23.820  1.00 13.37           C  
ANISOU  757  C   THR A  96     2102   1333   1646    384    290     43       C  
ATOM    758  O   THR A  96       7.114  36.532  23.297  1.00 13.41           O  
ANISOU  758  O   THR A  96     2419   1312   1366     89    159    238       O  
ATOM    759  CB  THR A  96       8.629  39.202  24.424  1.00 16.30           C  
ANISOU  759  CB  THR A  96     2606   1562   2026     44     19   -172       C  
ATOM    760  OG1 THR A  96       7.237  39.533  24.316  1.00 18.38           O  
ANISOU  760  OG1 THR A  96     2652   2014   2318    368    700   -369       O  
ATOM    761  CG2 THR A  96       9.434  40.447  24.118  1.00 16.92           C  
ANISOU  761  CG2 THR A  96     2686   1341   2401    471    406    294       C  
ATOM    762  N   LEU A  97       8.778  36.148  24.778  1.00 13.19           N  
ANISOU  762  N   LEU A  97     1861   1467   1686    399    326     25       N  
ATOM    763  CA  LEU A  97       8.221  35.061  25.529  1.00 14.10           C  
ANISOU  763  CA  LEU A  97     1994   1583   1781    352    149    243       C  
ATOM    764  C   LEU A  97       7.620  35.573  26.830  1.00 15.04           C  
ANISOU  764  C   LEU A  97     2335   1672   1709    -25    274    135       C  
ATOM    765  O   LEU A  97       8.344  36.276  27.537  1.00 19.31           O  
ANISOU  765  O   LEU A  97     2805   2971   1563   -598     80     60       O  
ATOM    766  CB  LEU A  97       9.282  34.051  25.923  1.00 17.19           C  
ANISOU  766  CB  LEU A  97     2119   1581   2833    408   -234    281       C  
ATOM    767  CG  LEU A  97       9.534  32.879  25.026  1.00 19.44           C  
ANISOU  767  CG  LEU A  97     2078   2129   3178    844   -811   -232       C  
ATOM    768  CD1 LEU A  97      10.648  32.005  25.609  1.00 26.23           C  
ANISOU  768  CD1 LEU A  97     3859   2687   3422   1808  -2149  -1049       C  
ATOM    769  CD2 LEU A  97       8.283  32.034  24.825  1.00 18.78           C  
ANISOU  769  CD2 LEU A  97     2435   1484   3217    522    -27     17       C  
ATOM    770  N   ASN A  98       6.383  35.241  27.118  1.00 14.84           N  
ANISOU  770  N   ASN A  98     2436   1327   1876     31    488    -59       N  
ATOM    771  CA  ASN A  98       5.693  35.807  28.258  1.00 15.87           C  
ANISOU  771  CA  ASN A  98     2765   1524   1740    395    501    150       C  
ATOM    772  C   ASN A  98       5.024  34.711  29.060  1.00 15.92           C  
ANISOU  772  C   ASN A  98     2758   1701   1591    133    407     57       C  
ATOM    773  O   ASN A  98       4.386  33.843  28.488  1.00 16.45           O  
ANISOU  773  O   ASN A  98     2487   1921   1843    150    430   -123       O  
ATOM    774  CB  ASN A  98       4.661  36.813  27.764  1.00 17.60           C  
ANISOU  774  CB  ASN A  98     2844   1790   2054    581    510    168       C  
ATOM    775  CG  ASN A  98       5.341  38.036  27.174  1.00 19.15           C  
ANISOU  775  CG  ASN A  98     3496   1509   2273    641    436    237       C  
ATOM    776  OD1 ASN A  98       5.420  39.084  27.799  1.00 28.45           O  
ANISOU  776  OD1 ASN A  98     5465   2007   3338   -120   1037   -461       O  
ATOM    777  ND2 ASN A  98       5.838  37.894  25.972  1.00 20.01           N  
ANISOU  777  ND2 ASN A  98     4059   1262   2282    836    638    703       N  
ATOM    778  N   PHE A  99       5.193  34.788  30.371  1.00 18.12           N  
ANISOU  778  N   PHE A  99     3132   2200   1552    -58    618    -59       N  
ATOM    779  CA  PHE A  99       4.513  33.873  31.268  1.00 19.16           C  
ANISOU  779  CA  PHE A  99     3445   2119   1715    188    690    195       C  
ATOM    780  C   PHE A  99       4.513  34.517  32.652  1.00 21.68           C  
ANISOU  780  C   PHE A  99     4135   2355   1747    -77   1022     74       C  
ATOM    781  O   PHE A  99       3.985  33.900  33.580  1.00 25.93           O  
ANISOU  781  O   PHE A  99     5052   2866   1935   -362   1296    155       O  
ATOM    782  CB  PHE A  99       5.169  32.514  31.288  1.00 19.38           C  
ANISOU  782  CB  PHE A  99     3244   2333   1785    355    495    151       C  
ATOM    783  CG  PHE A  99       6.637  32.441  31.657  1.00 21.40           C  
ANISOU  783  CG  PHE A  99     3233   2621   2276    148    411    130       C  
ATOM    784  CD1 PHE A  99       7.623  32.640  30.716  1.00 23.93           C  
ANISOU  784  CD1 PHE A  99     3195   3048   2849   -235    403    969       C  
ATOM    785  CD2 PHE A  99       7.037  32.167  32.946  1.00 21.52           C  
ANISOU  785  CD2 PHE A  99     3075   2798   2303    466    320    -83       C  
ATOM    786  CE1 PHE A  99       8.956  32.563  31.081  1.00 24.56           C  
ANISOU  786  CE1 PHE A  99     3233   3162   2935    -90    359   1232       C  
ATOM    787  CE2 PHE A  99       8.369  32.098  33.320  1.00 21.90           C  
ANISOU  787  CE2 PHE A  99     2962   2862   2495    522    520     88       C  
ATOM    788  CZ  PHE A  99       9.349  32.302  32.381  1.00 23.35           C  
ANISOU  788  CZ  PHE A  99     3194   3006   2671    182    524    739       C  
ATOM    789  OXT PHE A  99       5.043  35.643  32.796  1.00 23.90           O  
ANISOU  789  OXT PHE A  99     4534   2648   1899   -394    661     -2       O  
TER     790      PHE A  99                                                      
ATOM    791  N   PRO B 101       7.232  36.819  33.624  1.00 29.14           N  
ANISOU  791  N   PRO B 101     5140   2903   3029   -270    580    341       N  
ATOM    792  CA  PRO B 101       8.085  37.831  33.013  1.00 28.11           C  
ANISOU  792  CA  PRO B 101     4803   2879   2997   -252    563    114       C  
ATOM    793  C   PRO B 101       7.848  37.932  31.515  1.00 25.17           C  
ANISOU  793  C   PRO B 101     4296   2460   2807    416   1169   -158       C  
ATOM    794  O   PRO B 101       7.177  37.126  30.891  1.00 23.49           O  
ANISOU  794  O   PRO B 101     4377   2374   2174    220   1484     96       O  
ATOM    795  CB  PRO B 101       9.505  37.297  33.276  1.00 31.10           C  
ANISOU  795  CB  PRO B 101     4973   3255   3588    -74    414    386       C  
ATOM    796  CG  PRO B 101       9.309  35.813  33.145  1.00 32.07           C  
ANISOU  796  CG  PRO B 101     5084   3192   3910     -9    366    799       C  
ATOM    797  CD  PRO B 101       8.006  35.578  33.867  1.00 31.94           C  
ANISOU  797  CD  PRO B 101     5282   3266   3587    -64    465    748       C  
ATOM    798  N   GLN B 102       8.431  38.971  30.956  1.00 23.94           N  
ANISOU  798  N   GLN B 102     4055   2387   2656    363   1413   -505       N  
ATOM    799  CA  GLN B 102       8.454  39.177  29.520  1.00 22.44           C  
ANISOU  799  CA  GLN B 102     3693   2163   2669    327   1252   -485       C  
ATOM    800  C   GLN B 102       9.919  39.053  29.100  1.00 21.45           C  
ANISOU  800  C   GLN B 102     3597   1926   2625   -109   1187   -579       C  
ATOM    801  O   GLN B 102      10.761  39.854  29.524  1.00 28.01           O  
ANISOU  801  O   GLN B 102     4306   2174   4161   -767   1830  -1382       O  
ATOM    802  CB  GLN B 102       7.824  40.516  29.152  1.00 24.93           C  
ANISOU  802  CB  GLN B 102     4359   2170   2945    531   1042   -607       C  
ATOM    803  CG  GLN B 102       8.028  40.815  27.680  1.00 29.16           C  
ANISOU  803  CG  GLN B 102     4974   2868   3239    457   1118    104       C  
ATOM    804  CD  GLN B 102       7.070  41.869  27.175  1.00 30.53           C  
ANISOU  804  CD  GLN B 102     5036   2774   3790    302    970    332       C  
ATOM    805  OE1 GLN B 102       7.479  42.979  26.855  1.00 37.76           O  
ANISOU  805  OE1 GLN B 102     6871   2709   4768    121   1083    514       O  
ATOM    806  NE2 GLN B 102       5.799  41.522  27.103  1.00 35.61           N  
ANISOU  806  NE2 GLN B 102     5075   4128   4327    222     88   -502       N  
ATOM    807  N   ILE B 103      10.214  38.040  28.285  1.00 17.00           N  
ANISOU  807  N   ILE B 103     2946   1553   1960    -48    868   -123       N  
ATOM    808  CA  ILE B 103      11.618  37.772  27.973  1.00 16.23           C  
ANISOU  808  CA  ILE B 103     2831   1793   1543      2    514     15       C  
ATOM    809  C   ILE B 103      11.907  38.143  26.534  1.00 14.23           C  
ANISOU  809  C   ILE B 103     2462   1530   1415    -39    354   -212       C  
ATOM    810  O   ILE B 103      11.311  37.590  25.610  1.00 15.07           O  
ANISOU  810  O   ILE B 103     2823   1223   1678     64     38   -255       O  
ATOM    811  CB  ILE B 103      11.963  36.294  28.255  1.00 16.39           C  
ANISOU  811  CB  ILE B 103     2585   1808   1837    -77    503    127       C  
ATOM    812  CG1 ILE B 103      11.775  35.945  29.740  1.00 17.27           C  
ANISOU  812  CG1 ILE B 103     2545   2058   1958   -286    376    391       C  
ATOM    813  CG2 ILE B 103      13.340  35.975  27.752  1.00 17.75           C  
ANISOU  813  CG2 ILE B 103     2630   2325   1791    169    330   -245       C  
ATOM    814  CD1 ILE B 103      11.818  34.491  30.104  1.00 23.39           C  
ANISOU  814  CD1 ILE B 103     3524   2321   3043    -29    486    976       C  
ATOM    815  N   THR B 104      12.825  39.089  26.367  1.00 13.45           N  
ANISOU  815  N   THR B 104     2431   1339   1340     63    291   -171       N  
ATOM    816  CA  THR B 104      13.255  39.418  25.015  1.00 13.28           C  
ANISOU  816  CA  THR B 104     2419   1395   1232    -12    288   -296       C  
ATOM    817  C   THR B 104      14.276  38.399  24.535  1.00 12.90           C  
ANISOU  817  C   THR B 104     2446   1188   1267    -30    306    -90       C  
ATOM    818  O   THR B 104      14.754  37.537  25.282  1.00 15.02           O  
ANISOU  818  O   THR B 104     2572   1706   1427    125    257    176       O  
ATOM    819  CB  THR B 104      13.842  40.834  24.966  1.00 13.17           C  
ANISOU  819  CB  THR B 104     2573   1279   1154    126    207   -149       C  
ATOM    820  OG1 THR B 104      14.910  40.939  25.911  1.00 14.82           O  
ANISOU  820  OG1 THR B 104     2911   1563   1156   -350     35     15       O  
ATOM    821  CG2 THR B 104      12.754  41.836  25.345  1.00 17.96           C  
ANISOU  821  CG2 THR B 104     2953   1486   2385    260    688   -307       C  
ATOM    822  N   LEU B 105      14.618  38.499  23.261  1.00 12.01           N  
ANISOU  822  N   LEU B 105     2265    979   1319     34    357    -85       N  
ATOM    823  CA  LEU B 105      15.423  37.430  22.665  1.00 11.12           C  
ANISOU  823  CA  LEU B 105     1876   1077   1272     31     17   -195       C  
ATOM    824  C   LEU B 105      16.774  37.863  22.133  1.00 10.93           C  
ANISOU  824  C   LEU B 105     2001    899   1254    -58    103   -219       C  
ATOM    825  O   LEU B 105      17.362  37.210  21.261  1.00 11.39           O  
ANISOU  825  O   LEU B 105     2162   1136   1030    -73    155   -172       O  
ATOM    826  CB  LEU B 105      14.535  36.815  21.568  1.00 11.88           C  
ANISOU  826  CB  LEU B 105     1941   1292   1281    -79    -12   -192       C  
ATOM    827  CG  LEU B 105      13.256  36.198  22.141  1.00 13.11           C  
ANISOU  827  CG  LEU B 105     1918   1669   1395   -158    -82    -53       C  
ATOM    828  CD1 LEU B 105      12.321  35.817  21.004  1.00 13.73           C  
ANISOU  828  CD1 LEU B 105     2077   1750   1390   -381   -147    139       C  
ATOM    829  CD2 LEU B 105      13.550  34.986  23.016  1.00 13.24           C  
ANISOU  829  CD2 LEU B 105     2152   2067    813     29    348     44       C  
ATOM    830  N   TRP B 106      17.287  38.955  22.664  1.00 11.55           N  
ANISOU  830  N   TRP B 106     2032    829   1527     30    -22   -186       N  
ATOM    831  CA  TRP B 106      18.587  39.482  22.276  1.00 12.48           C  
ANISOU  831  CA  TRP B 106     2073    926   1741   -100   -129    -56       C  
ATOM    832  C   TRP B 106      19.681  38.530  22.748  1.00 12.89           C  
ANISOU  832  C   TRP B 106     1994   1251   1652    -92    -31    330       C  
ATOM    833  O   TRP B 106      20.762  38.466  22.149  1.00 14.58           O  
ANISOU  833  O   TRP B 106     2055   1859   1626     69     30    409       O  
ATOM    834  CB  TRP B 106      18.792  40.902  22.832  1.00 13.29           C  
ANISOU  834  CB  TRP B 106     2199   1141   1710   -196   -115   -276       C  
ATOM    835  CG  TRP B 106      17.697  41.829  22.418  1.00 12.43           C  
ANISOU  835  CG  TRP B 106     2289    901   1533   -174    179   -105       C  
ATOM    836  CD1 TRP B 106      16.614  42.233  23.144  1.00 13.57           C  
ANISOU  836  CD1 TRP B 106     2664    810   1683      8    455     83       C  
ATOM    837  CD2 TRP B 106      17.591  42.474  21.136  1.00 12.50           C  
ANISOU  837  CD2 TRP B 106     2308   1025   1417   -129    140   -247       C  
ATOM    838  NE1 TRP B 106      15.844  43.089  22.391  1.00 14.09           N  
ANISOU  838  NE1 TRP B 106     2594   1067   1694    100    439     79       N  
ATOM    839  CE2 TRP B 106      16.416  43.257  21.159  1.00 13.21           C  
ANISOU  839  CE2 TRP B 106     2490   1276   1254    112     72   -336       C  
ATOM    840  CE3 TRP B 106      18.384  42.454  19.990  1.00 12.47           C  
ANISOU  840  CE3 TRP B 106     2202   1130   1407   -126     84   -168       C  
ATOM    841  CZ2 TRP B 106      15.997  44.028  20.077  1.00 13.66           C  
ANISOU  841  CZ2 TRP B 106     2323   1558   1308     89    118   -203       C  
ATOM    842  CZ3 TRP B 106      17.958  43.219  18.925  1.00 12.19           C  
ANISOU  842  CZ3 TRP B 106     2077   1222   1332   -107    -34   -275       C  
ATOM    843  CH2 TRP B 106      16.785  43.992  18.966  1.00 12.63           C  
ANISOU  843  CH2 TRP B 106     2164   1268   1366     -5    129   -243       C  
ATOM    844  N   LYS B 107      19.376  37.797  23.818  1.00 13.54           N  
ANISOU  844  N   LYS B 107     2192   1299   1653   -371   -108    306       N  
ATOM    845  CA  LYS B 107      20.244  36.731  24.300  1.00 14.38           C  
ANISOU  845  CA  LYS B 107     2562   1328   1572   -286   -278    367       C  
ATOM    846  C   LYS B 107      19.431  35.442  24.379  1.00 13.40           C  
ANISOU  846  C   LYS B 107     2244   1327   1521   -118    147    421       C  
ATOM    847  O   LYS B 107      18.197  35.489  24.307  1.00 12.27           O  
ANISOU  847  O   LYS B 107     2228   1267   1167     21    207   -157       O  
ATOM    848  CB  LYS B 107      20.844  37.053  25.649  1.00 17.93           C  
ANISOU  848  CB  LYS B 107     3590   1547   1676      1   -631    170       C  
ATOM    849  CG  LYS B 107      19.873  37.351  26.769  1.00 25.60           C  
ANISOU  849  CG  LYS B 107     4841   2851   2036     29    -73   -546       C  
ATOM    850  CD  LYS B 107      20.616  38.125  27.873  1.00 32.59           C  
ANISOU  850  CD  LYS B 107     6053   3731   2597   -194   -273  -1300       C  
ATOM    851  CE  LYS B 107      20.133  37.765  29.262  1.00 35.28           C  
ANISOU  851  CE  LYS B 107     6807   4221   2377   -279   -352  -1430       C  
ATOM    852  NZ  LYS B 107      21.097  38.134  30.364  1.00 43.14           N  
ANISOU  852  NZ  LYS B 107     8308   5247   2835   -952  -1018  -1601       N  
ATOM    853  N   ARG B 108      20.147  34.329  24.530  1.00 12.76           N  
ANISOU  853  N   ARG B 108     2208   1274   1368    -94     -5     52       N  
ATOM    854  CA  ARG B 108      19.416  33.080  24.712  1.00 11.47           C  
ANISOU  854  CA  ARG B 108     2043   1151   1163     14    -51   -113       C  
ATOM    855  C   ARG B 108      18.461  33.127  25.889  1.00 11.53           C  
ANISOU  855  C   ARG B 108     2068   1289   1026    179    -71     97       C  
ATOM    856  O   ARG B 108      18.909  33.592  26.946  1.00 12.32           O  
ANISOU  856  O   ARG B 108     2328   1446    908     46   -179    306       O  
ATOM    857  CB AARG B 108      20.422  31.944  24.911  0.60 13.08           C  
ANISOU  857  CB AARG B 108     2294   1339   1335    263    101      5       C  
ATOM    858  CB BARG B 108      20.420  31.934  24.900  0.40 13.09           C  
ANISOU  858  CB BARG B 108     2294   1346   1333    255    104     21       C  
ATOM    859  CG AARG B 108      21.158  31.577  23.617  0.60 14.46           C  
ANISOU  859  CG AARG B 108     2471   1601   1422    355    228     17       C  
ATOM    860  CG BARG B 108      21.127  31.598  23.590  0.40 14.37           C  
ANISOU  860  CG BARG B 108     2450   1579   1430    399    210      6       C  
ATOM    861  CD AARG B 108      21.747  30.186  23.760  0.60 15.69           C  
ANISOU  861  CD AARG B 108     2659   1790   1513    638    299     17       C  
ATOM    862  CD BARG B 108      22.208  30.551  23.806  0.40 15.24           C  
ANISOU  862  CD BARG B 108     2624   1696   1470    548    242     69       C  
ATOM    863  NE AARG B 108      22.382  29.651  22.587  0.60 17.48           N  
ANISOU  863  NE AARG B 108     3133   1859   1650    711    636    198       N  
ATOM    864  NE BARG B 108      23.053  30.410  22.640  0.40 15.76           N  
ANISOU  864  NE BARG B 108     2654   1817   1518    691    261    108       N  
ATOM    865  CZ AARG B 108      22.608  28.358  22.350  0.60 22.41           C  
ANISOU  865  CZ AARG B 108     4501   2023   1991    817   1113   -114       C  
ATOM    866  CZ BARG B 108      24.217  29.781  22.555  0.40 16.55           C  
ANISOU  866  CZ BARG B 108     2686   2000   1603    785    208     77       C  
ATOM    867  NH1AARG B 108      22.245  27.419  23.214  0.60 26.76           N  
ANISOU  867  NH1AARG B 108     6055   1651   2460   1239   1541     47       N  
ATOM    868  NH1BARG B 108      24.768  29.173  23.594  0.40 18.23           N  
ANISOU  868  NH1BARG B 108     2892   2733   1302   1243    165   -184       N  
ATOM    869  NH2AARG B 108      23.206  27.964  21.232  0.60 29.56           N  
ANISOU  869  NH2AARG B 108     5917   2923   2393    797   1727   -542       N  
ATOM    870  NH2BARG B 108      24.854  29.758  21.391  0.40 15.20           N  
ANISOU  870  NH2BARG B 108     2210   2317   1247    752   -265   -293       N  
ATOM    871  N   PRO B 109      17.213  32.700  25.762  1.00 11.95           N  
ANISOU  871  N   PRO B 109     2109   1418   1014    100     18    -34       N  
ATOM    872  CA  PRO B 109      16.303  32.667  26.916  1.00 12.12           C  
ANISOU  872  CA  PRO B 109     2241   1362   1001     -5     30    111       C  
ATOM    873  C   PRO B 109      16.562  31.471  27.817  1.00 11.22           C  
ANISOU  873  C   PRO B 109     2127   1095   1042   -161   -173    -81       C  
ATOM    874  O   PRO B 109      15.831  30.475  27.850  1.00 11.98           O  
ANISOU  874  O   PRO B 109     2134   1188   1230   -246   -159   -157       O  
ATOM    875  CB  PRO B 109      14.925  32.549  26.270  1.00 12.31           C  
ANISOU  875  CB  PRO B 109     2082   1348   1247    298    103     33       C  
ATOM    876  CG  PRO B 109      15.192  31.793  25.002  1.00 13.44           C  
ANISOU  876  CG  PRO B 109     2043   1778   1284    176    -82   -183       C  
ATOM    877  CD  PRO B 109      16.546  32.257  24.534  1.00 12.61           C  
ANISOU  877  CD  PRO B 109     2054   1662   1074    247    -32   -144       C  
ATOM    878  N   LEU B 110      17.657  31.646  28.558  1.00 11.47           N  
ANISOU  878  N   LEU B 110     2242   1145    973   -283   -227    -63       N  
ATOM    879  CA  LEU B 110      18.078  30.688  29.559  1.00 11.33           C  
ANISOU  879  CA  LEU B 110     2300   1080    924   -287   -223    -88       C  
ATOM    880  C   LEU B 110      17.435  30.984  30.914  1.00 12.63           C  
ANISOU  880  C   LEU B 110     2742   1009   1048    -23     16     49       C  
ATOM    881  O   LEU B 110      17.385  32.149  31.339  1.00 15.08           O  
ANISOU  881  O   LEU B 110     3876   1023    830   -157     87     16       O  
ATOM    882  CB  LEU B 110      19.602  30.687  29.731  1.00 13.59           C  
ANISOU  882  CB  LEU B 110     2310   1747   1108   -293   -279    352       C  
ATOM    883  CG  LEU B 110      20.426  30.356  28.493  1.00 15.69           C  
ANISOU  883  CG  LEU B 110     2157   2517   1287     77   -308    285       C  
ATOM    884  CD1 LEU B 110      21.912  30.544  28.726  1.00 22.79           C  
ANISOU  884  CD1 LEU B 110     2029   3668   2960     86   -235    570       C  
ATOM    885  CD2 LEU B 110      20.126  28.924  28.059  1.00 22.19           C  
ANISOU  885  CD2 LEU B 110     3929   2958   1542   -213    -60   -468       C  
ATOM    886  N   VAL B 111      16.978  29.872  31.516  1.00 11.69           N  
ANISOU  886  N   VAL B 111     2450   1016    974    -49    -95    -47       N  
ATOM    887  CA  VAL B 111      16.409  29.933  32.863  1.00 12.18           C  
ANISOU  887  CA  VAL B 111     2387   1268    972   -157   -117     48       C  
ATOM    888  C   VAL B 111      17.005  28.807  33.695  1.00 12.89           C  
ANISOU  888  C   VAL B 111     2624   1378    897     -9    -61    -14       C  
ATOM    889  O   VAL B 111      17.646  27.880  33.194  1.00 12.91           O  
ANISOU  889  O   VAL B 111     2993    994    917   -135   -199   -135       O  
ATOM    890  CB  VAL B 111      14.888  29.812  32.896  1.00 15.02           C  
ANISOU  890  CB  VAL B 111     2415   1831   1460   -124     30    369       C  
ATOM    891  CG1 VAL B 111      14.243  30.932  32.100  1.00 19.27           C  
ANISOU  891  CG1 VAL B 111     2733   2047   2542    608    -19    314       C  
ATOM    892  CG2 VAL B 111      14.506  28.443  32.361  1.00 15.73           C  
ANISOU  892  CG2 VAL B 111     2405   1899   1674   -570   -294    690       C  
ATOM    893  N   THR B 112      16.754  28.949  34.993  1.00 13.10           N  
ANISOU  893  N   THR B 112     2458   1645    875      6     36     72       N  
ATOM    894  CA  THR B 112      17.098  27.913  35.921  1.00 12.08           C  
ANISOU  894  CA  THR B 112     2487   1283    819    -27     63   -137       C  
ATOM    895  C   THR B 112      15.912  26.980  36.061  1.00 11.74           C  
ANISOU  895  C   THR B 112     2365   1319    775     32     59   -236       C  
ATOM    896  O   THR B 112      14.780  27.451  36.185  1.00 13.02           O  
ANISOU  896  O   THR B 112     2399   1496   1053    138     73   -278       O  
ATOM    897  CB  THR B 112      17.451  28.465  37.312  1.00 14.47           C  
ANISOU  897  CB  THR B 112     3096   1604    799   -469   -122    -44       C  
ATOM    898  OG1 THR B 112      18.606  29.301  37.239  1.00 16.31           O  
ANISOU  898  OG1 THR B 112     3308   1718   1170   -655   -247     69       O  
ATOM    899  CG2 THR B 112      17.806  27.318  38.258  1.00 16.69           C  
ANISOU  899  CG2 THR B 112     3292   1997   1052   -601   -254    336       C  
ATOM    900  N   ILE B 113      16.245  25.698  36.028  1.00 11.67           N  
ANISOU  900  N   ILE B 113     2177   1305    953    -37   -107     81       N  
ATOM    901  CA  ILE B 113      15.229  24.669  36.256  1.00 11.69           C  
ANISOU  901  CA  ILE B 113     2341   1470    631   -173    -15    112       C  
ATOM    902  C   ILE B 113      15.658  23.857  37.474  1.00 11.69           C  
ANISOU  902  C   ILE B 113     2262   1532    649   -245   -157     69       C  
ATOM    903  O   ILE B 113      16.835  23.851  37.824  1.00 14.62           O  
ANISOU  903  O   ILE B 113     2367   2157   1029   -352   -422    117       O  
ATOM    904  CB  ILE B 113      15.009  23.745  35.044  1.00 12.32           C  
ANISOU  904  CB  ILE B 113     2617   1463    601   -292    -67    139       C  
ATOM    905  CG1 ILE B 113      16.246  22.904  34.692  1.00 13.30           C  
ANISOU  905  CG1 ILE B 113     2841   1176   1037   -288    -73   -134       C  
ATOM    906  CG2 ILE B 113      14.533  24.510  33.822  1.00 14.45           C  
ANISOU  906  CG2 ILE B 113     2299   2451    740   -422   -246    472       C  
ATOM    907  CD1 ILE B 113      15.964  21.817  33.677  1.00 13.79           C  
ANISOU  907  CD1 ILE B 113     2719   1515   1008   -573    -98   -261       C  
ATOM    908  N   LYS B 114      14.719  23.175  38.112  1.00 11.63           N  
ANISOU  908  N   LYS B 114     2444   1485    491   -242    -72     42       N  
ATOM    909  CA  LYS B 114      15.045  22.283  39.204  1.00 12.50           C  
ANISOU  909  CA  LYS B 114     2707   1487    555   -329   -216     61       C  
ATOM    910  C   LYS B 114      14.396  20.936  38.918  1.00 12.41           C  
ANISOU  910  C   LYS B 114     2317   1388   1010   -186     34    -15       C  
ATOM    911  O   LYS B 114      13.177  20.877  38.728  1.00 13.18           O  
ANISOU  911  O   LYS B 114     2218   1513   1275   -177    149    153       O  
ATOM    912  CB ALYS B 114      14.575  22.767  40.575  0.64 12.93           C  
ANISOU  912  CB ALYS B 114     2868   1525    522   -400   -129    162       C  
ATOM    913  CB BLYS B 114      14.555  22.844  40.518  0.36 12.88           C  
ANISOU  913  CB BLYS B 114     2865   1500    530   -384   -112    151       C  
ATOM    914  CG ALYS B 114      15.171  21.949  41.708  0.64 13.16           C  
ANISOU  914  CG ALYS B 114     2903   1534    561   -340   -122    177       C  
ATOM    915  CG BLYS B 114      15.107  22.123  41.739  0.36 13.36           C  
ANISOU  915  CG BLYS B 114     2942   1572    560   -342   -131    177       C  
ATOM    916  CD ALYS B 114      15.000  22.624  43.064  0.64 14.15           C  
ANISOU  916  CD ALYS B 114     3078   1749    548   -337   -251     97       C  
ATOM    917  CD BLYS B 114      14.580  22.891  42.943  0.36 14.26           C  
ANISOU  917  CD BLYS B 114     3100   1771    547   -345   -104    111       C  
ATOM    918  CE ALYS B 114      13.533  22.763  43.437  0.64 15.41           C  
ANISOU  918  CE ALYS B 114     3148   2043    665   -126   -201   -231       C  
ATOM    919  CE BLYS B 114      14.928  22.206  44.247  0.36 14.72           C  
ANISOU  919  CE BLYS B 114     3209   1817    568   -267   -171     93       C  
ATOM    920  NZ ALYS B 114      13.325  23.460  44.744  0.64 14.45           N  
ANISOU  920  NZ ALYS B 114     2610   1860   1021   -234   -706   -666       N  
ATOM    921  NZ BLYS B 114      14.691  23.197  45.354  0.36 19.13           N  
ANISOU  921  NZ BLYS B 114     3725   2665    877   -810   -935   -774       N  
ATOM    922  N   ILE B 115      15.254  19.937  38.902  1.00 13.95           N  
ANISOU  922  N   ILE B 115     2340   1581   1380    -51   -209   -150       N  
ATOM    923  CA  ILE B 115      14.707  18.586  38.629  1.00 15.21           C  
ANISOU  923  CA  ILE B 115     2624   1490   1665    -11     -5   -282       C  
ATOM    924  C   ILE B 115      15.486  17.651  39.522  1.00 18.34           C  
ANISOU  924  C   ILE B 115     2707   1593   2667    127   -222    -22       C  
ATOM    925  O   ILE B 115      16.705  17.768  39.632  1.00 19.27           O  
ANISOU  925  O   ILE B 115     2600   1501   3220    457     89   -168       O  
ATOM    926  CB  ILE B 115      14.747  18.296  37.121  1.00 18.40           C  
ANISOU  926  CB  ILE B 115     3009   2066   1914    237    194   -888       C  
ATOM    927  CG1 ILE B 115      14.261  16.878  36.762  1.00 20.90           C  
ANISOU  927  CG1 ILE B 115     3599   2309   2032    -79    -62   -913       C  
ATOM    928  CG2 ILE B 115      16.108  18.540  36.529  1.00 20.41           C  
ANISOU  928  CG2 ILE B 115     3453   1808   2495    344    859   -927       C  
ATOM    929  CD1 ILE B 115      14.082  16.766  35.238  1.00 23.36           C  
ANISOU  929  CD1 ILE B 115     4332   2383   2159    363   -695   -914       C  
ATOM    930  N   GLY B 116      14.810  16.726  40.192  1.00 21.32           N  
ANISOU  930  N   GLY B 116     2895   1980   3228   -249   -964    667       N  
ATOM    931  CA  GLY B 116      15.528  15.866  41.133  1.00 24.47           C  
ANISOU  931  CA  GLY B 116     3267   2297   3731   -197  -1331    843       C  
ATOM    932  C   GLY B 116      16.312  16.599  42.195  1.00 24.75           C  
ANISOU  932  C   GLY B 116     3553   2409   3442   -448  -1351   1118       C  
ATOM    933  O   GLY B 116      17.374  16.155  42.654  1.00 29.96           O  
ANISOU  933  O   GLY B 116     4570   2504   4308   -173  -2422   1256       O  
ATOM    934  N   GLY B 117      15.843  17.759  42.649  1.00 23.03           N  
ANISOU  934  N   GLY B 117     3415   2434   2902   -761   -900   1107       N  
ATOM    935  CA  GLY B 117      16.561  18.485  43.690  1.00 22.83           C  
ANISOU  935  CA  GLY B 117     3372   2841   2460   -931   -714   1231       C  
ATOM    936  C   GLY B 117      17.776  19.276  43.236  1.00 21.03           C  
ANISOU  936  C   GLY B 117     2911   2969   2113   -662   -709    960       C  
ATOM    937  O   GLY B 117      18.450  19.951  44.029  1.00 21.65           O  
ANISOU  937  O   GLY B 117     3092   3041   2092   -752   -535    711       O  
ATOM    938  N   GLN B 118      18.077  19.213  41.940  1.00 19.14           N  
ANISOU  938  N   GLN B 118     2584   2550   2138   -226   -712    752       N  
ATOM    939  CA  GLN B 118      19.250  19.879  41.425  1.00 19.77           C  
ANISOU  939  CA  GLN B 118     2740   2216   2556    -61   -256    673       C  
ATOM    940  C   GLN B 118      18.895  20.984  40.451  1.00 16.35           C  
ANISOU  940  C   GLN B 118     2434   1994   1786    -19   -154    165       C  
ATOM    941  O   GLN B 118      17.990  20.861  39.654  1.00 16.53           O  
ANISOU  941  O   GLN B 118     2814   1783   1683   -211   -239    -48       O  
ATOM    942  CB AGLN B 118      20.138  18.900  40.657  0.67 23.19           C  
ANISOU  942  CB AGLN B 118     3126   2237   3448    277      6    777       C  
ATOM    943  CB BGLN B 118      20.174  18.857  40.747  0.33 23.22           C  
ANISOU  943  CB BGLN B 118     3191   2147   3485    236     42    821       C  
ATOM    944  CG AGLN B 118      20.094  17.463  41.148  0.67 26.18           C  
ANISOU  944  CG AGLN B 118     3783   2245   3918    235     25    840       C  
ATOM    945  CG BGLN B 118      21.073  18.066  41.671  0.33 25.05           C  
ANISOU  945  CG BGLN B 118     3598   2129   3790    293   -138    983       C  
ATOM    946  CD AGLN B 118      20.480  16.453  40.080  0.67 29.47           C  
ANISOU  946  CD AGLN B 118     4398   2241   4559    -55    592    547       C  
ATOM    947  CD BGLN B 118      21.279  18.546  43.083  0.33 26.45           C  
ANISOU  947  CD BGLN B 118     3932   2251   3868   -102   -508   1038       C  
ATOM    948  OE1AGLN B 118      21.474  16.590  39.362  0.67 34.31           O  
ANISOU  948  OE1AGLN B 118     4541   2949   5547    693   1196    767       O  
ATOM    949  OE1BGLN B 118      21.914  19.573  43.347  0.33 29.51           O  
ANISOU  949  OE1BGLN B 118     4692   2595   3927   -670  -1607   1869       O  
ATOM    950  NE2AGLN B 118      19.665  15.404  39.976  0.67 37.39           N  
ANISOU  950  NE2AGLN B 118     6649   2507   5050  -1105    611    553       N  
ATOM    951  NE2BGLN B 118      20.747  17.807  44.062  0.33 28.50           N  
ANISOU  951  NE2BGLN B 118     4271   2809   3749   -899    184    268       N  
ATOM    952  N   LEU B 119      19.648  22.061  40.544  1.00 14.11           N  
ANISOU  952  N   LEU B 119     2257   1956   1149    115   -202    101       N  
ATOM    953  CA  LEU B 119      19.476  23.176  39.639  1.00 12.49           C  
ANISOU  953  CA  LEU B 119     2033   1746    966    183   -198   -135       C  
ATOM    954  C   LEU B 119      20.281  22.922  38.374  1.00 13.03           C  
ANISOU  954  C   LEU B 119     2119   1795   1037    485   -181     -8       C  
ATOM    955  O   LEU B 119      21.416  22.480  38.391  1.00 17.10           O  
ANISOU  955  O   LEU B 119     2301   2817   1379    901   -151   -264       O  
ATOM    956  CB  LEU B 119      19.929  24.484  40.281  1.00 14.24           C  
ANISOU  956  CB  LEU B 119     2189   1892   1329     67   -134   -294       C  
ATOM    957  CG  LEU B 119      19.290  24.874  41.599  1.00 12.85           C  
ANISOU  957  CG  LEU B 119     1998   1593   1292     55   -254   -304       C  
ATOM    958  CD1 LEU B 119      19.787  26.235  42.046  1.00 15.14           C  
ANISOU  958  CD1 LEU B 119     2605   1526   1621   -212    -52   -255       C  
ATOM    959  CD2 LEU B 119      17.798  24.842  41.400  1.00 14.89           C  
ANISOU  959  CD2 LEU B 119     2039   2408   1209     50   -279   -392       C  
ATOM    960  N   LYS B 120      19.669  23.221  37.245  1.00 12.99           N  
ANISOU  960  N   LYS B 120     2056   1900    978   -171   -264     48       N  
ATOM    961  CA  LYS B 120      20.292  23.195  35.948  1.00 13.74           C  
ANISOU  961  CA  LYS B 120     2288   1869   1065   -298    -64     73       C  
ATOM    962  C   LYS B 120      19.867  24.417  35.146  1.00 13.44           C  
ANISOU  962  C   LYS B 120     2383   1694   1030   -227      7    -66       C  
ATOM    963  O   LYS B 120      18.870  25.052  35.472  1.00 14.71           O  
ANISOU  963  O   LYS B 120     2466   1346   1779   -373    361   -130       O  
ATOM    964  CB  LYS B 120      19.899  21.952  35.170  1.00 15.09           C  
ANISOU  964  CB  LYS B 120     2709   1702   1323   -214    222    -39       C  
ATOM    965  CG  LYS B 120      20.289  20.652  35.829  1.00 17.51           C  
ANISOU  965  CG  LYS B 120     2963   1868   1822   -217   -174    179       C  
ATOM    966  CD  LYS B 120      19.569  19.527  35.098  1.00 21.07           C  
ANISOU  966  CD  LYS B 120     3562   1702   2743   -137   -153   -291       C  
ATOM    967  CE  LYS B 120      19.724  18.250  35.909  1.00 24.18           C  
ANISOU  967  CE  LYS B 120     3842   1770   3575   -112   -310     -8       C  
ATOM    968  NZ  LYS B 120      21.105  17.709  35.715  1.00 34.24           N  
ANISOU  968  NZ  LYS B 120     3963   3210   5838    570   -577    704       N  
ATOM    969  N   GLU B 121      20.647  24.704  34.109  1.00 13.87           N  
ANISOU  969  N   GLU B 121     2478   1816    978    -23      8     63       N  
ATOM    970  CA  GLU B 121      20.287  25.772  33.179  1.00 13.84           C  
ANISOU  970  CA  GLU B 121     2701   1493   1064   -177   -246    -38       C  
ATOM    971  C   GLU B 121      19.610  25.172  31.975  1.00 12.90           C  
ANISOU  971  C   GLU B 121     2377   1426   1100    -51   -169   -122       C  
ATOM    972  O   GLU B 121      20.046  24.102  31.532  1.00 13.04           O  
ANISOU  972  O   GLU B 121     2460   1515    979     87   -202    -57       O  
ATOM    973  CB AGLU B 121      21.522  26.577  32.779  0.53 14.13           C  
ANISOU  973  CB AGLU B 121     2625   1633   1111   -231   -448     78       C  
ATOM    974  CB BGLU B 121      21.529  26.524  32.756  0.47 13.74           C  
ANISOU  974  CB BGLU B 121     2645   1545   1030   -214   -348    -35       C  
ATOM    975  CG AGLU B 121      22.101  27.259  34.018  0.53 17.10           C  
ANISOU  975  CG AGLU B 121     2783   2133   1580   -173   -459   -546       C  
ATOM    976  CG BGLU B 121      21.369  27.729  31.851  0.47 14.01           C  
ANISOU  976  CG BGLU B 121     2696   1670    956   -539   -711     24       C  
ATOM    977  CD AGLU B 121      21.089  28.139  34.736  0.53 21.38           C  
ANISOU  977  CD AGLU B 121     3145   3002   1978     56   -108   -833       C  
ATOM    978  CD BGLU B 121      22.749  28.281  31.499  0.47 16.82           C  
ANISOU  978  CD BGLU B 121     3049   1917   1425  -1045   -748     -1       C  
ATOM    979  OE1AGLU B 121      20.855  27.978  35.953  0.53 25.21           O  
ANISOU  979  OE1AGLU B 121     2894   4335   2350   -698    602   -549       O  
ATOM    980  OE1BGLU B 121      23.396  27.810  30.537  0.47 17.02           O  
ANISOU  980  OE1BGLU B 121     3217   1781   1469   -952   -188    750       O  
ATOM    981  OE2AGLU B 121      20.513  29.023  34.057  0.53 28.12           O  
ANISOU  981  OE2AGLU B 121     4224   3385   3076   1159    240   -580       O  
ATOM    982  OE2BGLU B 121      23.180  29.207  32.218  0.47 23.71           O  
ANISOU  982  OE2BGLU B 121     4210   2736   2062  -1747  -1276   -282       O  
ATOM    983  N   ALA B 122      18.590  25.832  31.473  1.00 11.81           N  
ANISOU  983  N   ALA B 122     2409   1283    794    -62     59     86       N  
ATOM    984  CA  ALA B 122      17.915  25.303  30.285  1.00 11.27           C  
ANISOU  984  CA  ALA B 122     2293   1103    885     33     21     46       C  
ATOM    985  C   ALA B 122      17.390  26.464  29.439  1.00 11.61           C  
ANISOU  985  C   ALA B 122     2558   1014    839    -30     20     62       C  
ATOM    986  O   ALA B 122      17.176  27.580  29.933  1.00 13.66           O  
ANISOU  986  O   ALA B 122     3211    944   1034    -81   -306    -32       O  
ATOM    987  CB  ALA B 122      16.787  24.373  30.635  1.00 11.97           C  
ANISOU  987  CB  ALA B 122     2524    651   1373     61    138    -62       C  
ATOM    988  N   LEU B 123      17.198  26.151  28.171  1.00 11.14           N  
ANISOU  988  N   LEU B 123     2376    952    904   -169    -73      4       N  
ATOM    989  CA  LEU B 123      16.761  27.072  27.139  1.00 11.85           C  
ANISOU  989  CA  LEU B 123     2575   1012    916   -283    -54    123       C  
ATOM    990  C   LEU B 123      15.270  26.996  26.917  1.00 12.50           C  
ANISOU  990  C   LEU B 123     2679    796   1275   -288   -472    -15       C  
ATOM    991  O   LEU B 123      14.763  25.902  26.631  1.00 15.17           O  
ANISOU  991  O   LEU B 123     2995    776   1994   -319   -594    -89       O  
ATOM    992  CB  LEU B 123      17.524  26.687  25.882  1.00 14.20           C  
ANISOU  992  CB  LEU B 123     3270   1177    949   -518    182    -98       C  
ATOM    993  CG  LEU B 123      17.399  27.505  24.627  1.00 14.94           C  
ANISOU  993  CG  LEU B 123     3555   1247    873   -299    242   -205       C  
ATOM    994  CD1 LEU B 123      17.891  28.912  24.864  1.00 17.81           C  
ANISOU  994  CD1 LEU B 123     3721    973   2071   -173    688    -12       C  
ATOM    995  CD2 LEU B 123      18.214  26.897  23.507  1.00 17.34           C  
ANISOU  995  CD2 LEU B 123     3636   2119    833   -221    181   -527       C  
ATOM    996  N   LEU B 124      14.523  28.073  27.041  1.00 12.41           N  
ANISOU  996  N   LEU B 124     2640    892   1182   -263   -234   -169       N  
ATOM    997  CA  LEU B 124      13.127  28.051  26.653  1.00 12.58           C  
ANISOU  997  CA  LEU B 124     2563    937   1280   -280    -92    -45       C  
ATOM    998  C   LEU B 124      13.045  28.040  25.138  1.00 12.56           C  
ANISOU  998  C   LEU B 124     2286   1250   1236   -365   -118    -71       C  
ATOM    999  O   LEU B 124      13.466  28.986  24.482  1.00 14.79           O  
ANISOU  999  O   LEU B 124     2909   1390   1322   -604   -409    138       O  
ATOM   1000  CB  LEU B 124      12.380  29.260  27.202  1.00 13.70           C  
ANISOU 1000  CB  LEU B 124     2807   1015   1384   -111   -221   -163       C  
ATOM   1001  CG  LEU B 124      12.482  29.436  28.722  1.00 14.25           C  
ANISOU 1001  CG  LEU B 124     3107    849   1457    174   -474   -225       C  
ATOM   1002  CD1 LEU B 124      11.786  30.736  29.112  1.00 16.85           C  
ANISOU 1002  CD1 LEU B 124     2664   1682   2058    570    135   -496       C  
ATOM   1003  CD2 LEU B 124      11.893  28.261  29.446  1.00 17.83           C  
ANISOU 1003  CD2 LEU B 124     3973   1654   1147   -660   -560   -148       C  
ATOM   1004  N   ASP B 125      12.500  26.955  24.621  1.00 11.92           N  
ANISOU 1004  N   ASP B 125     2004   1323   1202   -335    -92     -1       N  
ATOM   1005  CA  ASP B 125      12.572  26.671  23.192  1.00 12.09           C  
ANISOU 1005  CA  ASP B 125     2065   1380   1149   -442   -263     28       C  
ATOM   1006  C   ASP B 125      11.254  26.400  22.491  1.00 11.39           C  
ANISOU 1006  C   ASP B 125     1950   1074   1303   -401   -181     81       C  
ATOM   1007  O   ASP B 125      10.770  25.267  22.488  1.00 12.78           O  
ANISOU 1007  O   ASP B 125     2590   1021   1246   -469   -640     65       O  
ATOM   1008  CB  ASP B 125      13.463  25.439  23.037  1.00 12.04           C  
ANISOU 1008  CB  ASP B 125     2159   1710    707   -202   -484   -129       C  
ATOM   1009  CG  ASP B 125      13.890  25.182  21.603  1.00 14.89           C  
ANISOU 1009  CG  ASP B 125     2686   2133    837   -420   -160   -240       C  
ATOM   1010  OD1 ASP B 125      13.358  25.854  20.695  1.00 16.44           O  
ANISOU 1010  OD1 ASP B 125     2640   2849    758   -974   -387    134       O  
ATOM   1011  OD2 ASP B 125      14.760  24.302  21.444  1.00 16.66           O  
ANISOU 1011  OD2 ASP B 125     2739   2055   1536   -583    477   -337       O  
ATOM   1012  N   THR B 126      10.699  27.466  21.893  1.00 12.08           N  
ANISOU 1012  N   THR B 126     1900    995   1693   -353   -248      8       N  
ATOM   1013  CA  THR B 126       9.407  27.336  21.249  1.00 10.82           C  
ANISOU 1013  CA  THR B 126     1530   1079   1501    -31    145   -278       C  
ATOM   1014  C   THR B 126       9.482  26.453  20.011  1.00 10.78           C  
ANISOU 1014  C   THR B 126     1737   1198   1160    119     -5   -120       C  
ATOM   1015  O   THR B 126       8.442  26.002  19.540  1.00 12.42           O  
ANISOU 1015  O   THR B 126     1825   1708   1187    -88     -8   -200       O  
ATOM   1016  CB  THR B 126       8.824  28.691  20.814  1.00 10.90           C  
ANISOU 1016  CB  THR B 126     1767   1069   1305   -102    111   -164       C  
ATOM   1017  OG1 THR B 126       9.756  29.368  19.985  1.00 11.48           O  
ANISOU 1017  OG1 THR B 126     1537   1249   1577     53    231   -102       O  
ATOM   1018  CG2 THR B 126       8.595  29.547  22.056  1.00 11.43           C  
ANISOU 1018  CG2 THR B 126     1758   1203   1382    220     64   -248       C  
ATOM   1019  N   GLY B 127      10.661  26.193  19.489  1.00 10.05           N  
ANISOU 1019  N   GLY B 127     1817   1067    937   -115     92    -77       N  
ATOM   1020  CA  GLY B 127      10.804  25.288  18.357  1.00  9.12           C  
ANISOU 1020  CA  GLY B 127     1819    941    705   -171    -12     21       C  
ATOM   1021  C   GLY B 127      10.968  23.836  18.729  1.00 11.40           C  
ANISOU 1021  C   GLY B 127     2643    910    780   -307   -165    -18       C  
ATOM   1022  O   GLY B 127      11.138  22.977  17.849  1.00 11.93           O  
ANISOU 1022  O   GLY B 127     2654   1003    875    -26    -26    -36       O  
ATOM   1023  N   ALA B 128      10.932  23.491  20.002  1.00 10.70           N  
ANISOU 1023  N   ALA B 128     2578    655    833   -167   -167    -61       N  
ATOM   1024  CA  ALA B 128      10.983  22.138  20.512  1.00  9.61           C  
ANISOU 1024  CA  ALA B 128     1814    792   1046     53     38     98       C  
ATOM   1025  C   ALA B 128       9.610  21.631  20.928  1.00 10.32           C  
ANISOU 1025  C   ALA B 128     1693    915   1312     63      2     37       C  
ATOM   1026  O   ALA B 128       8.987  22.251  21.774  1.00 10.49           O  
ANISOU 1026  O   ALA B 128     1575   1111   1301    -10    -78   -137       O  
ATOM   1027  CB  ALA B 128      11.930  22.101  21.701  1.00 13.31           C  
ANISOU 1027  CB  ALA B 128     1998   1234   1827   -183   -504    453       C  
ATOM   1028  N   ASP B 129       9.137  20.520  20.348  1.00 10.05           N  
ANISOU 1028  N   ASP B 129     1569    852   1399    174    156     10       N  
ATOM   1029  CA  ASP B 129       7.872  19.970  20.764  1.00  9.98           C  
ANISOU 1029  CA  ASP B 129     1718   1008   1067    -29     20    116       C  
ATOM   1030  C   ASP B 129       7.981  19.458  22.199  1.00 10.93           C  
ANISOU 1030  C   ASP B 129     1933   1166   1054     -8    -93    109       C  
ATOM   1031  O   ASP B 129       7.050  19.572  22.958  1.00 12.27           O  
ANISOU 1031  O   ASP B 129     2229   1403   1031     38     90    108       O  
ATOM   1032  CB  ASP B 129       7.422  18.822  19.879  1.00 12.70           C  
ANISOU 1032  CB  ASP B 129     2045   1631   1149   -377    181   -222       C  
ATOM   1033  CG  ASP B 129       7.230  19.165  18.420  1.00 13.40           C  
ANISOU 1033  CG  ASP B 129     2394   1520   1178   -220     77   -288       C  
ATOM   1034  OD1 ASP B 129       7.074  20.324  18.024  1.00 14.18           O  
ANISOU 1034  OD1 ASP B 129     2488   1579   1322    -64    -35   -229       O  
ATOM   1035  OD2 ASP B 129       7.250  18.149  17.668  1.00 17.05           O  
ANISOU 1035  OD2 ASP B 129     3471   1610   1396   -182   -546   -442       O  
ATOM   1036  N   ASP B 130       9.134  18.911  22.490  1.00 11.15           N  
ANISOU 1036  N   ASP B 130     2037   1088   1113    -65   -182    129       N  
ATOM   1037  CA  ASP B 130       9.459  18.172  23.687  1.00 12.63           C  
ANISOU 1037  CA  ASP B 130     2397   1191   1211    -30   -436    149       C  
ATOM   1038  C   ASP B 130      10.622  18.786  24.447  1.00 11.95           C  
ANISOU 1038  C   ASP B 130     2249   1170   1123    -66   -262    182       C  
ATOM   1039  O   ASP B 130      11.483  19.477  23.920  1.00 14.30           O  
ANISOU 1039  O   ASP B 130     2460   1873   1099   -363    -12     98       O  
ATOM   1040  CB  ASP B 130       9.868  16.755  23.336  1.00 16.36           C  
ANISOU 1040  CB  ASP B 130     3515   1076   1625     18   -859    110       C  
ATOM   1041  CG  ASP B 130       8.871  16.054  22.446  1.00 19.06           C  
ANISOU 1041  CG  ASP B 130     4142   1246   1852   -202  -1201    112       C  
ATOM   1042  OD1 ASP B 130       7.657  16.130  22.712  1.00 22.77           O  
ANISOU 1042  OD1 ASP B 130     4064   1877   2709   -852  -1181     47       O  
ATOM   1043  OD2 ASP B 130       9.293  15.414  21.468  1.00 26.41           O  
ANISOU 1043  OD2 ASP B 130     5304   2085   2645   -443  -1014   -894       O  
ATOM   1044  N   THR B 131      10.612  18.493  25.724  1.00 11.91           N  
ANISOU 1044  N   THR B 131     1954   1413   1157   -125   -322    302       N  
ATOM   1045  CA  THR B 131      11.671  18.858  26.659  1.00 10.16           C  
ANISOU 1045  CA  THR B 131     1707    979   1173    -35   -130    -55       C  
ATOM   1046  C   THR B 131      12.742  17.789  26.687  1.00  9.72           C  
ANISOU 1046  C   THR B 131     1726    833   1134   -100    -28    165       C  
ATOM   1047  O   THR B 131      12.445  16.601  26.901  1.00 12.35           O  
ANISOU 1047  O   THR B 131     2089    885   1719   -165    -58    366       O  
ATOM   1048  CB  THR B 131      11.049  19.055  28.040  1.00  9.13           C  
ANISOU 1048  CB  THR B 131     1491    817   1162   -199    -53    228       C  
ATOM   1049  OG1 THR B 131      10.156  20.188  27.950  1.00 11.58           O  
ANISOU 1049  OG1 THR B 131     1625   1305   1470    212     98    294       O  
ATOM   1050  CG2 THR B 131      12.102  19.359  29.115  1.00 11.96           C  
ANISOU 1050  CG2 THR B 131     1552   1786   1208    212   -100   -258       C  
ATOM   1051  N   VAL B 132      13.971  18.212  26.467  1.00 10.21           N  
ANISOU 1051  N   VAL B 132     1704   1035   1143    -64    172    -80       N  
ATOM   1052  CA  VAL B 132      15.076  17.275  26.351  1.00 12.30           C  
ANISOU 1052  CA  VAL B 132     1763   1334   1576    103   -164   -268       C  
ATOM   1053  C   VAL B 132      16.222  17.748  27.257  1.00 11.41           C  
ANISOU 1053  C   VAL B 132     1835   1049   1451   -147   -118    -48       C  
ATOM   1054  O   VAL B 132      16.645  18.881  27.118  1.00 12.10           O  
ANISOU 1054  O   VAL B 132     1864   1070   1665   -153    274      9       O  
ATOM   1055  CB  VAL B 132      15.638  17.116  24.924  1.00 13.98           C  
ANISOU 1055  CB  VAL B 132     1895   1613   1803    328   -126   -960       C  
ATOM   1056  CG1 VAL B 132      16.545  15.891  24.922  1.00 15.78           C  
ANISOU 1056  CG1 VAL B 132     2575   1481   1941    540   -102   -513       C  
ATOM   1057  CG2 VAL B 132      14.567  16.987  23.871  1.00 16.97           C  
ANISOU 1057  CG2 VAL B 132     2472   2288   1686    200   -437   -370       C  
ATOM   1058  N   ILE B 133      16.684  16.883  28.136  1.00 12.36           N  
ANISOU 1058  N   ILE B 133     2134   1163   1400   -174   -237     -4       N  
ATOM   1059  CA  ILE B 133      17.730  17.162  29.101  1.00 13.66           C  
ANISOU 1059  CA  ILE B 133     2025   1447   1716     14   -348   -155       C  
ATOM   1060  C   ILE B 133      18.911  16.226  28.942  1.00 13.17           C  
ANISOU 1060  C   ILE B 133     1987   1442   1577    -55    -49   -241       C  
ATOM   1061  O   ILE B 133      18.798  15.064  28.548  1.00 13.49           O  
ANISOU 1061  O   ILE B 133     2169   1268   1687   -155   -116     -3       O  
ATOM   1062  CB  ILE B 133      17.114  17.036  30.508  1.00 16.12           C  
ANISOU 1062  CB  ILE B 133     2170   2441   1514    447   -351   -776       C  
ATOM   1063  CG1 ILE B 133      15.879  17.940  30.621  1.00 17.46           C  
ANISOU 1063  CG1 ILE B 133     2567   2141   1924    605   -299   -450       C  
ATOM   1064  CG2 ILE B 133      18.098  17.291  31.630  1.00 24.89           C  
ANISOU 1064  CG2 ILE B 133     3510   3858   2090   1094  -1348   -980       C  
ATOM   1065  CD1 ILE B 133      16.092  19.401  30.611  1.00 23.07           C  
ANISOU 1065  CD1 ILE B 133     3182   2193   3391    465    -25    252       C  
ATOM   1066  N   GLU B 134      20.071  16.777  29.263  1.00 13.53           N  
ANISOU 1066  N   GLU B 134     1961   1340   1840    -88    123   -334       N  
ATOM   1067  CA  GLU B 134      21.294  16.008  29.247  1.00 16.05           C  
ANISOU 1067  CA  GLU B 134     1867   1823   2409     17    331     81       C  
ATOM   1068  C   GLU B 134      21.211  14.875  30.251  1.00 16.13           C  
ANISOU 1068  C   GLU B 134     1977   1618   2534   -107     13     33       C  
ATOM   1069  O   GLU B 134      20.414  14.976  31.172  1.00 16.48           O  
ANISOU 1069  O   GLU B 134     2531   1689   2042    105    -32    161       O  
ATOM   1070  CB AGLU B 134      22.497  16.894  29.573  0.62 18.88           C  
ANISOU 1070  CB AGLU B 134     1914   2121   3140   -260    381    353       C  
ATOM   1071  CB BGLU B 134      22.481  16.937  29.541  0.38 18.98           C  
ANISOU 1071  CB BGLU B 134     1916   2177   3117   -265    384    380       C  
ATOM   1072  CG AGLU B 134      22.674  17.923  28.453  0.62 21.50           C  
ANISOU 1072  CG AGLU B 134     2206   2494   3468   -284    478    674       C  
ATOM   1073  CG BGLU B 134      22.585  18.083  28.536  0.38 21.67           C  
ANISOU 1073  CG BGLU B 134     2238   2499   3495   -297    553    711       C  
ATOM   1074  CD AGLU B 134      23.561  19.074  28.866  0.62 23.65           C  
ANISOU 1074  CD AGLU B 134     2471   2575   3939   -571    594    855       C  
ATOM   1075  CD BGLU B 134      23.554  19.177  28.905  0.38 23.22           C  
ANISOU 1075  CD BGLU B 134     2392   2556   3874   -480    570    853       C  
ATOM   1076  OE1AGLU B 134      23.849  19.182  30.082  0.62 25.46           O  
ANISOU 1076  OE1AGLU B 134     2536   2960   4178   -897    274    537       O  
ATOM   1077  OE1BGLU B 134      23.116  20.326  29.161  0.38 24.96           O  
ANISOU 1077  OE1BGLU B 134     2676   2565   4242   -535    739    665       O  
ATOM   1078  OE2AGLU B 134      23.926  19.815  27.921  0.62 29.32           O  
ANISOU 1078  OE2AGLU B 134     3292   3011   4839   -640    741   1599       O  
ATOM   1079  OE2BGLU B 134      24.778  18.907  28.941  0.38 25.69           O  
ANISOU 1079  OE2BGLU B 134     2383   2959   4419   -460    274    782       O  
ATOM   1080  N   GLU B 135      22.041  13.882  29.980  1.00 16.92           N  
ANISOU 1080  N   GLU B 135     2015   1720   2695    -50   -125    -33       N  
ATOM   1081  CA  GLU B 135      22.062  12.661  30.761  1.00 19.20           C  
ANISOU 1081  CA  GLU B 135     2476   1727   3093     -5   -370    105       C  
ATOM   1082  C   GLU B 135      21.989  12.970  32.247  1.00 19.39           C  
ANISOU 1082  C   GLU B 135     2840   1519   3008     48   -563    367       C  
ATOM   1083  O   GLU B 135      22.775  13.781  32.746  1.00 20.56           O  
ANISOU 1083  O   GLU B 135     3154   1959   2697   -335   -585    539       O  
ATOM   1084  CB  GLU B 135      23.332  11.863  30.492  1.00 21.12           C  
ANISOU 1084  CB  GLU B 135     2492   1813   3719     78   -305    255       C  
ATOM   1085  CG  GLU B 135      23.444  10.621  31.382  1.00 24.33           C  
ANISOU 1085  CG  GLU B 135     2676   2118   4450     16   -659    697       C  
ATOM   1086  CD  GLU B 135      22.321   9.634  31.113  1.00 28.72           C  
ANISOU 1086  CD  GLU B 135     3321   2401   5191   -604   -394    700       C  
ATOM   1087  OE1 GLU B 135      21.938   9.565  29.923  1.00 33.24           O  
ANISOU 1087  OE1 GLU B 135     3402   3523   5705  -1420  -1192   1046       O  
ATOM   1088  OE2 GLU B 135      21.855   8.965  32.064  1.00 33.63           O  
ANISOU 1088  OE2 GLU B 135     4262   3147   5368   -931    958    127       O  
ATOM   1089  N   MET B 136      21.043  12.332  32.887  1.00 19.28           N  
ANISOU 1089  N   MET B 136     2924   1560   2841    -36   -606    358       N  
ATOM   1090  CA  MET B 136      20.876  12.426  34.324  1.00 20.86           C  
ANISOU 1090  CA  MET B 136     3199   1907   2821   -158   -655    347       C  
ATOM   1091  C   MET B 136      20.039  11.236  34.765  1.00 21.09           C  
ANISOU 1091  C   MET B 136     3236   1988   2789   -116   -647    503       C  
ATOM   1092  O   MET B 136      19.462  10.509  33.961  1.00 21.32           O  
ANISOU 1092  O   MET B 136     3197   2024   2878   -297   -452    419       O  
ATOM   1093  CB  MET B 136      20.210  13.728  34.756  1.00 20.99           C  
ANISOU 1093  CB  MET B 136     3253   1998   2722   -192   -991    -45       C  
ATOM   1094  CG  MET B 136      18.752  13.832  34.326  1.00 22.46           C  
ANISOU 1094  CG  MET B 136     3281   2113   3139    -52  -1069    -29       C  
ATOM   1095  SD  MET B 136      17.917  15.256  35.072  1.00 27.26           S  
ANISOU 1095  SD  MET B 136     3874   2099   4386    125    316    486       S  
ATOM   1096  CE  MET B 136      17.822  14.700  36.775  1.00 39.89           C  
ANISOU 1096  CE  MET B 136     8426   1803   4927    598   2936    968       C  
ATOM   1097  N   SER B 137      20.000  11.074  36.082  1.00 21.27           N  
ANISOU 1097  N   SER B 137     3148   2107   2828    252   -733    723       N  
ATOM   1098  CA  SER B 137      19.198   9.989  36.627  1.00 22.04           C  
ANISOU 1098  CA  SER B 137     3162   2011   3200    468   -467    888       C  
ATOM   1099  C   SER B 137      17.814  10.503  36.991  1.00 21.11           C  
ANISOU 1099  C   SER B 137     3162   1767   3090    284   -540    309       C  
ATOM   1100  O   SER B 137      17.623  11.498  37.679  1.00 20.82           O  
ANISOU 1100  O   SER B 137     3342   1723   2846    289   -854    370       O  
ATOM   1101  CB ASER B 137      19.909   9.366  37.832  0.51 24.70           C  
ANISOU 1101  CB ASER B 137     3509   2536   3339    534   -474   1200       C  
ATOM   1102  CB BSER B 137      19.888   9.378  37.845  0.49 24.50           C  
ANISOU 1102  CB BSER B 137     3480   2529   3299    547   -427   1180       C  
ATOM   1103  OG ASER B 137      21.025   8.568  37.446  0.51 29.16           O  
ANISOU 1103  OG ASER B 137     4193   2817   4071   1283   -304   1776       O  
ATOM   1104  OG BSER B 137      18.977   8.997  38.859  0.49 26.89           O  
ANISOU 1104  OG BSER B 137     3910   3010   3299   -261   -472   1140       O  
ATOM   1105  N   LEU B 138      16.810   9.797  36.511  1.00 19.13           N  
ANISOU 1105  N   LEU B 138     3177   1497   2593    125   -176    417       N  
ATOM   1106  CA  LEU B 138      15.443  10.080  36.877  1.00 17.72           C  
ANISOU 1106  CA  LEU B 138     3239   1431   2063     42   -125     33       C  
ATOM   1107  C   LEU B 138      14.771   8.818  37.365  1.00 17.73           C  
ANISOU 1107  C   LEU B 138     3354   1475   1909    -67    -97    -17       C  
ATOM   1108  O   LEU B 138      15.122   7.719  36.947  1.00 17.80           O  
ANISOU 1108  O   LEU B 138     3106   1528   2131   -169   -255   -235       O  
ATOM   1109  CB  LEU B 138      14.677  10.634  35.684  1.00 15.88           C  
ANISOU 1109  CB  LEU B 138     2911   1145   1979   -199   -182   -159       C  
ATOM   1110  CG  LEU B 138      15.105  12.051  35.290  1.00 16.49           C  
ANISOU 1110  CG  LEU B 138     2950   1300   2015   -318    -65      3       C  
ATOM   1111  CD1 LEU B 138      14.360  12.493  34.043  1.00 17.50           C  
ANISOU 1111  CD1 LEU B 138     2771   1867   2013    309    307    255       C  
ATOM   1112  CD2 LEU B 138      14.864  13.076  36.387  1.00 19.86           C  
ANISOU 1112  CD2 LEU B 138     3410   1260   2876    127   -759   -504       C  
ATOM   1113  N   PRO B 139      13.809   8.977  38.252  1.00 19.19           N  
ANISOU 1113  N   PRO B 139     3700   1606   1987    -55    117    -36       N  
ATOM   1114  CA  PRO B 139      13.127   7.780  38.755  1.00 19.70           C  
ANISOU 1114  CA  PRO B 139     3699   1793   1992   -227    192   -112       C  
ATOM   1115  C   PRO B 139      12.108   7.181  37.804  1.00 19.50           C  
ANISOU 1115  C   PRO B 139     3620   1717   2072   -132     79    101       C  
ATOM   1116  O   PRO B 139      11.607   7.875  36.920  1.00 19.99           O  
ANISOU 1116  O   PRO B 139     3296   2267   2033   -181    371    476       O  
ATOM   1117  CB  PRO B 139      12.396   8.366  39.978  1.00 21.54           C  
ANISOU 1117  CB  PRO B 139     4038   1941   2207   -147    424   -150       C  
ATOM   1118  CG  PRO B 139      12.039   9.736  39.484  1.00 23.40           C  
ANISOU 1118  CG  PRO B 139     4191   2128   2572    197    619      6       C  
ATOM   1119  CD  PRO B 139      13.315  10.237  38.829  1.00 21.81           C  
ANISOU 1119  CD  PRO B 139     4172   1754   2361    145    467     -3       C  
ATOM   1120  N   GLY B 140      11.819   5.883  38.017  1.00 18.38           N  
ANISOU 1120  N   GLY B 140     3580   1656   1749   -155    443   -176       N  
ATOM   1121  CA  GLY B 140      10.754   5.226  37.303  1.00 17.10           C  
ANISOU 1121  CA  GLY B 140     3218   1661   1617     48    695   -350       C  
ATOM   1122  C   GLY B 140      11.219   4.529  36.049  1.00 16.25           C  
ANISOU 1122  C   GLY B 140     3048   1529   1596     91    650   -224       C  
ATOM   1123  O   GLY B 140      12.401   4.382  35.741  1.00 18.52           O  
ANISOU 1123  O   GLY B 140     3085   2135   1817   -322    954   -486       O  
ATOM   1124  N   ARG B 141      10.214   4.092  35.304  1.00 15.04           N  
ANISOU 1124  N   ARG B 141     3125   1090   1500    187    509    -36       N  
ATOM   1125  CA  ARG B 141      10.486   3.482  34.018  1.00 14.82           C  
ANISOU 1125  CA  ARG B 141     3026   1196   1410    228    511     55       C  
ATOM   1126  C   ARG B 141      10.594   4.528  32.931  1.00 14.71           C  
ANISOU 1126  C   ARG B 141     2940   1212   1436    548    330     87       C  
ATOM   1127  O   ARG B 141      10.075   5.625  33.064  1.00 19.95           O  
ANISOU 1127  O   ARG B 141     3671   1900   2010   1504    730    542       O  
ATOM   1128  CB  ARG B 141       9.372   2.477  33.665  1.00 16.46           C  
ANISOU 1128  CB  ARG B 141     3278   1518   1459    103    116     -7       C  
ATOM   1129  CG  ARG B 141       9.491   1.288  34.621  1.00 17.36           C  
ANISOU 1129  CG  ARG B 141     3337   1748   1513   -437    140    242       C  
ATOM   1130  CD  ARG B 141       8.604   0.129  34.369  1.00 15.81           C  
ANISOU 1130  CD  ARG B 141     2864   1591   1553    -31    340   -271       C  
ATOM   1131  NE  ARG B 141       8.740  -0.424  33.019  1.00 16.06           N  
ANISOU 1131  NE  ARG B 141     2563   2077   1462    683    -65   -243       N  
ATOM   1132  CZ  ARG B 141       9.607  -1.352  32.655  1.00 14.31           C  
ANISOU 1132  CZ  ARG B 141     2231   1936   1270    406    160    -68       C  
ATOM   1133  NH1 ARG B 141      10.469  -1.886  33.500  1.00 12.95           N  
ANISOU 1133  NH1 ARG B 141     2219   1074   1630      5    -21     85       N  
ATOM   1134  NH2 ARG B 141       9.562  -1.716  31.383  1.00 14.14           N  
ANISOU 1134  NH2 ARG B 141     2232   1750   1391   -191    158   -281       N  
ATOM   1135  N   TRP B 142      11.274   4.133  31.865  1.00 13.26           N  
ANISOU 1135  N   TRP B 142     2754   1021   1263    131    236    -13       N  
ATOM   1136  CA  TRP B 142      11.295   4.976  30.687  1.00 13.40           C  
ANISOU 1136  CA  TRP B 142     2728    947   1416    -81    193     38       C  
ATOM   1137  C   TRP B 142      10.876   4.188  29.442  1.00 13.97           C  
ANISOU 1137  C   TRP B 142     2963   1041   1302   -115    139     71       C  
ATOM   1138  O   TRP B 142      10.902   2.945  29.496  1.00 14.88           O  
ANISOU 1138  O   TRP B 142     3573   1046   1033   -331    -71    189       O  
ATOM   1139  CB  TRP B 142      12.674   5.562  30.466  1.00 14.18           C  
ANISOU 1139  CB  TRP B 142     2726    809   1854    -56    235      3       C  
ATOM   1140  CG  TRP B 142      13.822   4.624  30.345  1.00 13.44           C  
ANISOU 1140  CG  TRP B 142     2671    774   1661   -149    189    -42       C  
ATOM   1141  CD1 TRP B 142      14.500   4.014  31.369  1.00 13.39           C  
ANISOU 1141  CD1 TRP B 142     2335   1074   1680   -208    321    142       C  
ATOM   1142  CD2 TRP B 142      14.432   4.186  29.129  1.00 13.01           C  
ANISOU 1142  CD2 TRP B 142     2355    920   1670   -328    270      8       C  
ATOM   1143  NE1 TRP B 142      15.499   3.217  30.864  1.00 13.56           N  
ANISOU 1143  NE1 TRP B 142     2184   1240   1727   -231    171    -76       N  
ATOM   1144  CE2 TRP B 142      15.470   3.314  29.493  1.00 13.57           C  
ANISOU 1144  CE2 TRP B 142     2530    911   1716   -214    268    -25       C  
ATOM   1145  CE3 TRP B 142      14.188   4.458  27.773  1.00 13.93           C  
ANISOU 1145  CE3 TRP B 142     2763    857   1673   -101    280    -45       C  
ATOM   1146  CZ2 TRP B 142      16.269   2.707  28.536  1.00 14.16           C  
ANISOU 1146  CZ2 TRP B 142     2725    854   1800   -140    272   -120       C  
ATOM   1147  CZ3 TRP B 142      14.998   3.842  26.828  1.00 14.93           C  
ANISOU 1147  CZ3 TRP B 142     2884   1097   1690    -15    251   -167       C  
ATOM   1148  CH2 TRP B 142      16.023   2.978  27.223  1.00 14.78           C  
ANISOU 1148  CH2 TRP B 142     2938    905   1771    -23    396    -77       C  
ATOM   1149  N   LYS B 143      10.522   4.930  28.396  1.00 14.04           N  
ANISOU 1149  N   LYS B 143     3013    999   1323     55    308    136       N  
ATOM   1150  CA  LYS B 143      10.102   4.376  27.113  1.00 16.34           C  
ANISOU 1150  CA  LYS B 143     3298   1659   1250   -375    174    280       C  
ATOM   1151  C   LYS B 143      11.004   4.944  26.034  1.00 14.36           C  
ANISOU 1151  C   LYS B 143     3093   1159   1204   -280     67    107       C  
ATOM   1152  O   LYS B 143      11.573   6.011  26.245  1.00 13.97           O  
ANISOU 1152  O   LYS B 143     2508   1144   1657    -79     83    -44       O  
ATOM   1153  CB ALYS B 143       8.617   4.642  26.871  0.55 20.73           C  
ANISOU 1153  CB ALYS B 143     3158   2922   1796   -617    151     24       C  
ATOM   1154  CB BLYS B 143       8.674   4.733  26.767  0.45 20.34           C  
ANISOU 1154  CB BLYS B 143     3136   2822   1769   -636    109    159       C  
ATOM   1155  CG ALYS B 143       7.768   4.131  28.034  0.55 23.03           C  
ANISOU 1155  CG ALYS B 143     3334   3266   2152   -773    321    170       C  
ATOM   1156  CG BLYS B 143       7.528   4.232  27.605  0.45 23.22           C  
ANISOU 1156  CG BLYS B 143     3384   3215   2223   -845    349    163       C  
ATOM   1157  CD ALYS B 143       7.192   2.744  27.841  0.55 25.31           C  
ANISOU 1157  CD ALYS B 143     3608   3354   2656   -933    495    149       C  
ATOM   1158  CD BLYS B 143       6.265   5.082  27.417  0.45 24.83           C  
ANISOU 1158  CD BLYS B 143     3304   3461   2668   -757    560     67       C  
ATOM   1159  CE ALYS B 143       6.863   2.070  29.169  0.55 27.73           C  
ANISOU 1159  CE ALYS B 143     3868   3667   3003  -1086    769    397       C  
ATOM   1160  CE BLYS B 143       5.026   4.208  27.561  0.45 26.83           C  
ANISOU 1160  CE BLYS B 143     3406   3651   3139   -898    678    -50       C  
ATOM   1161  NZ ALYS B 143       5.472   1.541  29.191  0.55 32.99           N  
ANISOU 1161  NZ ALYS B 143     4290   4160   4087  -1697    887    394       N  
ATOM   1162  NZ BLYS B 143       3.838   4.914  28.121  0.45 27.96           N  
ANISOU 1162  NZ BLYS B 143     3242   3317   4063  -1281    574   -902       N  
ATOM   1163  N   PRO B 144      11.135   4.268  24.919  1.00 14.80           N  
ANISOU 1163  N   PRO B 144     3145   1170   1309   -188    152     40       N  
ATOM   1164  CA  PRO B 144      12.008   4.783  23.866  1.00 14.20           C  
ANISOU 1164  CA  PRO B 144     2872   1209   1315    -19    129    -37       C  
ATOM   1165  C   PRO B 144      11.312   5.862  23.050  1.00 13.83           C  
ANISOU 1165  C   PRO B 144     2412   1372   1471   -473   -214    196       C  
ATOM   1166  O   PRO B 144      10.101   5.853  22.875  1.00 16.44           O  
ANISOU 1166  O   PRO B 144     2398   1809   2040   -545   -245    143       O  
ATOM   1167  CB  PRO B 144      12.252   3.538  23.014  1.00 16.35           C  
ANISOU 1167  CB  PRO B 144     3505   1384   1322   -255    119   -257       C  
ATOM   1168  CG  PRO B 144      10.941   2.803  23.132  1.00 16.87           C  
ANISOU 1168  CG  PRO B 144     3648   1417   1343   -365     47    -57       C  
ATOM   1169  CD  PRO B 144      10.500   2.996  24.554  1.00 16.26           C  
ANISOU 1169  CD  PRO B 144     3612   1198   1368   -299    110     -7       C  
ATOM   1170  N   LYS B 145      12.128   6.795  22.558  1.00 15.25           N  
ANISOU 1170  N   LYS B 145     2426   1728   1640   -414     -6    426       N  
ATOM   1171  CA  LYS B 145      11.646   7.808  21.658  1.00 16.02           C  
ANISOU 1171  CA  LYS B 145     2783   1545   1761   -460    -22    422       C  
ATOM   1172  C   LYS B 145      12.799   8.243  20.781  1.00 15.98           C  
ANISOU 1172  C   LYS B 145     2864   1611   1595   -263     24    406       C  
ATOM   1173  O   LYS B 145      13.930   8.276  21.219  1.00 15.48           O  
ANISOU 1173  O   LYS B 145     2752   1686   1443   -278    249    -74       O  
ATOM   1174  CB ALYS B 145      11.079   9.053  22.357  0.61 17.06           C  
ANISOU 1174  CB ALYS B 145     2928   1651   1905   -398    274    456       C  
ATOM   1175  CB BLYS B 145      11.089   8.996  22.434  0.39 17.03           C  
ANISOU 1175  CB BLYS B 145     2964   1603   1904   -402    312    507       C  
ATOM   1176  CG ALYS B 145      10.169   9.853  21.432  0.61 17.80           C  
ANISOU 1176  CG ALYS B 145     3197   1439   2127   -419    365    809       C  
ATOM   1177  CG BLYS B 145      10.741  10.160  21.521  0.39 18.16           C  
ANISOU 1177  CG BLYS B 145     3185   1498   2219   -458    280    618       C  
ATOM   1178  CD ALYS B 145       9.571  11.102  22.042  0.61 19.48           C  
ANISOU 1178  CD ALYS B 145     3363   1538   2500   -393    288    620       C  
ATOM   1179  CD BLYS B 145       9.533  10.918  22.038  0.39 19.36           C  
ANISOU 1179  CD BLYS B 145     3260   1598   2497   -326    269    646       C  
ATOM   1180  CE ALYS B 145       8.551  11.765  21.132  0.61 20.54           C  
ANISOU 1180  CE ALYS B 145     3491   1577   2736   -167    224    554       C  
ATOM   1181  CE BLYS B 145       9.005  11.909  21.013  0.39 20.28           C  
ANISOU 1181  CE BLYS B 145     3461   1566   2679   -308    169    673       C  
ATOM   1182  NZ ALYS B 145       7.752  12.828  21.803  0.61 24.00           N  
ANISOU 1182  NZ ALYS B 145     4118   2098   2903    261    208    277       N  
ATOM   1183  NZ BLYS B 145       7.572  11.629  20.702  0.39 20.98           N  
ANISOU 1183  NZ BLYS B 145     3601   1473   2898   -127   -197    138       N  
ATOM   1184  N   MET B 146      12.469   8.562  19.574  1.00 18.24           N  
ANISOU 1184  N   MET B 146     3351   1927   1652     36     59    586       N  
ATOM   1185  CA  MET B 146      13.381   9.129  18.613  1.00 20.17           C  
ANISOU 1185  CA  MET B 146     3850   2031   1784    255    580    527       C  
ATOM   1186  C   MET B 146      12.931  10.549  18.336  1.00 18.11           C  
ANISOU 1186  C   MET B 146     3271   2041   1571    205    591    590       C  
ATOM   1187  O   MET B 146      11.753  10.733  18.063  1.00 19.99           O  
ANISOU 1187  O   MET B 146     3345   2251   1998      6    204    473       O  
ATOM   1188  CB AMET B 146      13.411   8.351  17.295  0.58 23.47           C  
ANISOU 1188  CB AMET B 146     4550   2328   2039    509    621    239       C  
ATOM   1189  CB BMET B 146      13.437   8.318  17.316  0.42 23.39           C  
ANISOU 1189  CB BMET B 146     4578   2286   2024    443    601    267       C  
ATOM   1190  CG AMET B 146      14.055   6.966  17.416  0.58 24.56           C  
ANISOU 1190  CG AMET B 146     4899   2236   2197    462    461    234       C  
ATOM   1191  CG BMET B 146      14.264   7.038  17.480  0.42 24.08           C  
ANISOU 1191  CG BMET B 146     4772   2277   2101    489    547    242       C  
ATOM   1192  SD AMET B 146      15.830   7.114  17.129  0.58 41.53           S  
ANISOU 1192  SD AMET B 146     4944   5598   5236   1559   1519   -918       S  
ATOM   1193  SD BMET B 146      14.915   6.501  15.894  0.42 40.77           S  
ANISOU 1193  SD BMET B 146     4906   6737   3846   1095    642  -2739       S  
ATOM   1194  CE AMET B 146      15.822   7.430  15.368  0.58 43.37           C  
ANISOU 1194  CE AMET B 146     5365   5711   5402   -241   2632   -373       C  
ATOM   1195  CE BMET B 146      16.499   7.335  15.879  0.42 42.54           C  
ANISOU 1195  CE BMET B 146     5455   5815   4892    777   2169   -438       C  
ATOM   1196  N   ILE B 147      13.868  11.476  18.421  1.00 18.20           N  
ANISOU 1196  N   ILE B 147     3060   2103   1753    305    427    648       N  
ATOM   1197  CA  ILE B 147      13.489  12.864  18.094  1.00 17.96           C  
ANISOU 1197  CA  ILE B 147     2778   2064   1982    206    564    743       C  
ATOM   1198  C   ILE B 147      14.450  13.351  17.030  1.00 19.71           C  
ANISOU 1198  C   ILE B 147     2816   2395   2279    350    740    919       C  
ATOM   1199  O   ILE B 147      15.595  12.940  16.968  1.00 25.69           O  
ANISOU 1199  O   ILE B 147     2803   3366   3590    505    987   1886       O  
ATOM   1200  CB  ILE B 147      13.506  13.803  19.290  1.00 17.13           C  
ANISOU 1200  CB  ILE B 147     2453   1945   2109   -140    444    685       C  
ATOM   1201  CG1 ILE B 147      14.859  13.866  19.996  1.00 18.55           C  
ANISOU 1201  CG1 ILE B 147     2498   2040   2511    138    298    810       C  
ATOM   1202  CG2 ILE B 147      12.378  13.398  20.221  1.00 18.48           C  
ANISOU 1202  CG2 ILE B 147     2661   2123   2238    -75    727    467       C  
ATOM   1203  CD1 ILE B 147      14.898  14.772  21.208  1.00 20.27           C  
ANISOU 1203  CD1 ILE B 147     2707   1528   3466   -398   -210    400       C  
ATOM   1204  N   GLY B 148      13.908  14.227  16.215  1.00 19.29           N  
ANISOU 1204  N   GLY B 148     3193   2103   2035    477    882    767       N  
ATOM   1205  CA  GLY B 148      14.619  14.687  15.037  1.00 19.91           C  
ANISOU 1205  CA  GLY B 148     3109   2170   2285   -154    907    720       C  
ATOM   1206  C   GLY B 148      14.939  16.153  15.160  1.00 18.77           C  
ANISOU 1206  C   GLY B 148     2730   2234   2167   -108    883    182       C  
ATOM   1207  O   GLY B 148      14.102  17.026  15.316  1.00 18.36           O  
ANISOU 1207  O   GLY B 148     2439   2431   2108    -91    274   -158       O  
ATOM   1208  N   GLY B 149      16.226  16.475  15.091  1.00 18.22           N  
ANISOU 1208  N   GLY B 149     2668   2257   1996     26    930   -326       N  
ATOM   1209  CA  GLY B 149      16.560  17.873  15.125  1.00 18.98           C  
ANISOU 1209  CA  GLY B 149     2615   2312   2285   -110    820   -546       C  
ATOM   1210  C   GLY B 149      17.304  18.243  13.861  1.00 16.87           C  
ANISOU 1210  C   GLY B 149     2819   1739   1854    -59    416   -446       C  
ATOM   1211  O   GLY B 149      17.305  17.534  12.841  1.00 16.94           O  
ANISOU 1211  O   GLY B 149     2842   1892   1703     23     -6   -399       O  
ATOM   1212  N  AILE B 150      17.994  19.377  13.926  0.63 16.76           N  
ANISOU 1212  N  AILE B 150     2684   1790   1893    -62    255   -422       N  
ATOM   1213  N  BILE B 150      17.930  19.410  13.928  0.37 16.60           N  
ANISOU 1213  N  BILE B 150     2655   1778   1874    -26    281   -433       N  
ATOM   1214  CA AILE B 150      18.603  19.913  12.715  0.63 15.88           C  
ANISOU 1214  CA AILE B 150     2692   1570   1772     13   -102   -113       C  
ATOM   1215  CA BILE B 150      18.837  19.823  12.875  0.37 16.14           C  
ANISOU 1215  CA BILE B 150     2806   1647   1677     82    129   -105       C  
ATOM   1216  C  AILE B 150      19.587  18.928  12.097  0.63 16.32           C  
ANISOU 1216  C  AILE B 150     2772   1639   1789    -68    336     47       C  
ATOM   1217  C  BILE B 150      20.012  18.874  13.018  0.37 16.61           C  
ANISOU 1217  C  BILE B 150     2749   1809   1754    117    389    -50       C  
ATOM   1218  O  AILE B 150      19.609  18.885  10.865  0.63 16.72           O  
ANISOU 1218  O  AILE B 150     3110   1446   1797   -265    453    232       O  
ATOM   1219  O  BILE B 150      20.527  18.713  14.135  0.37 15.79           O  
ANISOU 1219  O  BILE B 150     2356   1942   1703    171    626    224       O  
ATOM   1220  CB  ILE B 150      19.281  21.278  12.983  1.00 15.67           C  
ANISOU 1220  CB  ILE B 150     2432   1774   1747    -47   -254   -214       C  
ATOM   1221  CG1 ILE B 150      18.901  22.213  11.815  1.00 17.21           C  
ANISOU 1221  CG1 ILE B 150     3124   1960   1457   -423    407    145       C  
ATOM   1222  CG2 ILE B 150      20.773  21.317  13.173  1.00 28.32           C  
ANISOU 1222  CG2 ILE B 150     2611   2888   5262    316  -1299  -2033       C  
ATOM   1223  CD1 ILE B 150      19.222  23.647  12.097  1.00 20.24           C  
ANISOU 1223  CD1 ILE B 150     3771   1975   1943   -497   -146    153       C  
ATOM   1224  N  AGLY B 151      20.347  18.156  12.860  0.63 16.95           N  
ANISOU 1224  N  AGLY B 151     2913   1764   1765    256    468    -22       N  
ATOM   1225  N  BGLY B 151      20.435  18.237  11.930  0.37 17.50           N  
ANISOU 1225  N  BGLY B 151     3024   1769   1855     76    490    -95       N  
ATOM   1226  CA AGLY B 151      21.385  17.290  12.324  0.63 18.16           C  
ANISOU 1226  CA AGLY B 151     3045   1821   2033    225    678   -153       C  
ATOM   1227  CA BGLY B 151      21.499  17.266  12.137  0.37 18.32           C  
ANISOU 1227  CA BGLY B 151     3110   1807   2045    178    647   -118       C  
ATOM   1228  C  AGLY B 151      20.977  15.858  12.110  0.63 19.26           C  
ANISOU 1228  C  AGLY B 151     3232   1764   2324    223    907   -125       C  
ATOM   1229  C  BGLY B 151      20.968  15.855  12.071  0.37 19.28           C  
ANISOU 1229  C  BGLY B 151     3229   1767   2331    194    902   -191       C  
ATOM   1230  O   GLY B 151      21.735  15.009  11.633  1.00 22.34           O  
ANISOU 1230  O   GLY B 151     3276   1846   3368    140   1294   -280       O  
ATOM   1231  N   GLY B 152      19.754  15.516  12.448  1.00 17.95           N  
ANISOU 1231  N   GLY B 152     3340   1533   1949    270   1022   -189       N  
ATOM   1232  CA  GLY B 152      19.266  14.151  12.359  1.00 20.21           C  
ANISOU 1232  CA  GLY B 152     3768   1622   2290    103   1255    170       C  
ATOM   1233  C   GLY B 152      18.572  13.759  13.652  1.00 23.40           C  
ANISOU 1233  C   GLY B 152     3854   2342   2694    494   1495    732       C  
ATOM   1234  O   GLY B 152      18.290  14.589  14.483  1.00 19.55           O  
ANISOU 1234  O   GLY B 152     1994   3278   2156    618    785    431       O  
ATOM   1235  N   PHE B 153      18.328  12.461  13.744  1.00 27.95           N  
ANISOU 1235  N   PHE B 153     4515   2421   3683    585   1736   1423       N  
ATOM   1236  CA  PHE B 153      17.560  11.844  14.815  1.00 30.09           C  
ANISOU 1236  CA  PHE B 153     4550   3160   3723    438   1657   1716       C  
ATOM   1237  C   PHE B 153      18.457  11.281  15.895  1.00 32.32           C  
ANISOU 1237  C   PHE B 153     4435   3781   4065   1061   1946   2094       C  
ATOM   1238  O   PHE B 153      19.572  10.811  15.666  1.00 35.73           O  
ANISOU 1238  O   PHE B 153     5146   4372   4057   1820   2353   2083       O  
ATOM   1239  CB  PHE B 153      16.684  10.711  14.263  1.00 35.38           C  
ANISOU 1239  CB  PHE B 153     5047   3683   4711   -273   1992   1438       C  
ATOM   1240  CG  PHE B 153      15.474  11.286  13.552  1.00 37.37           C  
ANISOU 1240  CG  PHE B 153     5322   3877   5000   -347   1212    682       C  
ATOM   1241  CD1 PHE B 153      15.583  11.757  12.256  1.00 37.25           C  
ANISOU 1241  CD1 PHE B 153     5592   3949   4614   -462    683    250       C  
ATOM   1242  CD2 PHE B 153      14.254  11.344  14.208  1.00 37.89           C  
ANISOU 1242  CD2 PHE B 153     5090   4114   5194   -250   1003    181       C  
ATOM   1243  CE1 PHE B 153      14.478  12.289  11.610  1.00 37.66           C  
ANISOU 1243  CE1 PHE B 153     5543   3979   4787   -548    436   -117       C  
ATOM   1244  CE2 PHE B 153      13.146  11.878  13.558  1.00 38.16           C  
ANISOU 1244  CE2 PHE B 153     5272   4143   5086   -420    594   -146       C  
ATOM   1245  CZ  PHE B 153      13.255  12.354  12.258  1.00 38.20           C  
ANISOU 1245  CZ  PHE B 153     5480   4009   5027   -687    457   -226       C  
ATOM   1246  N   ILE B 154      17.961  11.320  17.121  1.00 30.56           N  
ANISOU 1246  N   ILE B 154     3627   3980   4005   1342   1710   2337       N  
ATOM   1247  CA  ILE B 154      18.700  10.680  18.197  1.00 29.40           C  
ANISOU 1247  CA  ILE B 154     2990   3813   4369   1273   1723   2472       C  
ATOM   1248  C   ILE B 154      17.681   9.873  18.996  1.00 26.26           C  
ANISOU 1248  C   ILE B 154     3014   2984   3982   1006   1415   1913       C  
ATOM   1249  O   ILE B 154      16.483  10.194  18.978  1.00 22.91           O  
ANISOU 1249  O   ILE B 154     2753   2080   3872    376    858   1601       O  
ATOM   1250  CB  ILE B 154      19.439  11.668  19.112  1.00 30.75           C  
ANISOU 1250  CB  ILE B 154     2688   3956   5040    587   1299   3036       C  
ATOM   1251  CG1 ILE B 154      18.510  12.639  19.827  1.00 28.98           C  
ANISOU 1251  CG1 ILE B 154     2659   3726   4626    -76    970   2192       C  
ATOM   1252  CG2 ILE B 154      20.521  12.422  18.347  1.00 39.71           C  
ANISOU 1252  CG2 ILE B 154     3561   5553   5975     46   2191   3048       C  
ATOM   1253  CD1 ILE B 154      19.008  13.454  20.986  1.00 30.17           C  
ANISOU 1253  CD1 ILE B 154     2291   3506   5664   -468   -128   2377       C  
ATOM   1254  N   LYS B 155      18.167   8.857  19.677  1.00 24.46           N  
ANISOU 1254  N   LYS B 155     3134   2602   3557   1167   1494   1434       N  
ATOM   1255  CA  LYS B 155      17.421   8.080  20.643  1.00 22.25           C  
ANISOU 1255  CA  LYS B 155     3369   2216   2868    658   1166    909       C  
ATOM   1256  C   LYS B 155      17.492   8.747  22.012  1.00 20.29           C  
ANISOU 1256  C   LYS B 155     2500   2087   3123    201    703    691       C  
ATOM   1257  O   LYS B 155      18.556   9.195  22.422  1.00 23.17           O  
ANISOU 1257  O   LYS B 155     2485   1978   4339    -79    572   1165       O  
ATOM   1258  CB  LYS B 155      17.953   6.653  20.773  1.00 26.27           C  
ANISOU 1258  CB  LYS B 155     4381   1969   3632    518    849    732       C  
ATOM   1259  CG  LYS B 155      17.616   5.724  19.626  1.00 32.56           C  
ANISOU 1259  CG  LYS B 155     5626   2409   4336     -1    761    238       C  
ATOM   1260  CD  LYS B 155      18.172   4.328  19.817  1.00 36.24           C  
ANISOU 1260  CD  LYS B 155     6373   2246   5150      0    607    -52       C  
ATOM   1261  CE  LYS B 155      17.191   3.247  19.369  1.00 41.36           C  
ANISOU 1261  CE  LYS B 155     7137   2648   5929   -647    616    -64       C  
ATOM   1262  NZ  LYS B 155      17.870   1.947  19.062  1.00 44.11           N  
ANISOU 1262  NZ  LYS B 155     7066   2637   7058  -1140   1671   -621       N  
ATOM   1263  N   VAL B 156      16.397   8.828  22.734  1.00 17.25           N  
ANISOU 1263  N   VAL B 156     2457   1409   2690    -70    512    313       N  
ATOM   1264  CA  VAL B 156      16.392   9.418  24.054  1.00 16.09           C  
ANISOU 1264  CA  VAL B 156     2312   1301   2501    204    -26    543       C  
ATOM   1265  C   VAL B 156      15.549   8.500  24.923  1.00 14.63           C  
ANISOU 1265  C   VAL B 156     2304   1066   2189    124   -104    245       C  
ATOM   1266  O   VAL B 156      14.852   7.627  24.396  1.00 15.44           O  
ANISOU 1266  O   VAL B 156     2519   1455   1891    -62      6    111       O  
ATOM   1267  CB  VAL B 156      15.828  10.845  24.070  1.00 15.93           C  
ANISOU 1267  CB  VAL B 156     2438   1225   2390    116     42    486       C  
ATOM   1268  CG1 VAL B 156      16.626  11.820  23.242  1.00 18.23           C  
ANISOU 1268  CG1 VAL B 156     2964   1455   2510   -192     14    596       C  
ATOM   1269  CG2 VAL B 156      14.394  10.828  23.536  1.00 15.81           C  
ANISOU 1269  CG2 VAL B 156     2348   1520   2140    521    220     40       C  
ATOM   1270  N   ARG B 157      15.661   8.743  26.208  1.00 13.98           N  
ANISOU 1270  N   ARG B 157     2174    908   2228     68   -153    141       N  
ATOM   1271  CA  ARG B 157      14.868   8.017  27.181  1.00 13.81           C  
ANISOU 1271  CA  ARG B 157     2148   1071   2028    -50   -309    102       C  
ATOM   1272  C   ARG B 157      13.696   8.898  27.593  1.00 13.30           C  
ANISOU 1272  C   ARG B 157     2317    980   1758    102   -189    378       C  
ATOM   1273  O   ARG B 157      13.924  10.001  28.046  1.00 14.96           O  
ANISOU 1273  O   ARG B 157     2528   1161   1994    100   -239    132       O  
ATOM   1274  CB  ARG B 157      15.719   7.621  28.376  1.00 14.10           C  
ANISOU 1274  CB  ARG B 157     2142   1140   2075     60   -344     47       C  
ATOM   1275  CG  ARG B 157      16.963   6.813  28.038  1.00 16.39           C  
ANISOU 1275  CG  ARG B 157     2192   1553   2482    234   -161    236       C  
ATOM   1276  CD  ARG B 157      17.481   6.063  29.248  1.00 17.48           C  
ANISOU 1276  CD  ARG B 157     2300   1463   2878    127   -526    332       C  
ATOM   1277  NE  ARG B 157      17.816   6.916  30.375  1.00 19.02           N  
ANISOU 1277  NE  ARG B 157     2524   1754   2947     89   -848    330       N  
ATOM   1278  CZ  ARG B 157      18.896   7.676  30.502  1.00 20.54           C  
ANISOU 1278  CZ  ARG B 157     2635   1734   3437     53  -1026    297       C  
ATOM   1279  NH1 ARG B 157      19.806   7.716  29.544  1.00 23.13           N  
ANISOU 1279  NH1 ARG B 157     2837   2041   3910   -318   -709    612       N  
ATOM   1280  NH2 ARG B 157      19.055   8.402  31.609  1.00 24.36           N  
ANISOU 1280  NH2 ARG B 157     3484   2021   3752    -90  -1401     69       N  
ATOM   1281  N   GLN B 158      12.479   8.407  27.432  1.00 12.99           N  
ANISOU 1281  N   GLN B 158     2299    890   1747    226   -125    357       N  
ATOM   1282  CA  GLN B 158      11.317   9.190  27.806  1.00 12.36           C  
ANISOU 1282  CA  GLN B 158     2253    993   1451    113   -165    194       C  
ATOM   1283  C   GLN B 158      10.803   8.820  29.187  1.00 13.22           C  
ANISOU 1283  C   GLN B 158     2531   1005   1486    -20   -140    150       C  
ATOM   1284  O   GLN B 158      10.402   7.670  29.371  1.00 13.48           O  
ANISOU 1284  O   GLN B 158     2259   1013   1851    -10    575   -102       O  
ATOM   1285  CB  GLN B 158      10.203   8.970  26.791  1.00 12.64           C  
ANISOU 1285  CB  GLN B 158     1944   1472   1385   -273     90    216       C  
ATOM   1286  CG  GLN B 158       8.957   9.737  27.162  1.00 13.21           C  
ANISOU 1286  CG  GLN B 158     2075   1650   1295    -76   -110    133       C  
ATOM   1287  CD  GLN B 158       7.845   9.618  26.145  1.00 13.96           C  
ANISOU 1287  CD  GLN B 158     2088   1826   1389   -159   -153    -75       C  
ATOM   1288  OE1 GLN B 158       8.066   9.501  24.947  1.00 19.13           O  
ANISOU 1288  OE1 GLN B 158     2488   3381   1398     20   -308   -275       O  
ATOM   1289  NE2 GLN B 158       6.605   9.649  26.586  1.00 20.14           N  
ANISOU 1289  NE2 GLN B 158     2071   3562   2020  -1171    -50   -282       N  
ATOM   1290  N   TYR B 159      10.820   9.777  30.094  1.00 13.79           N  
ANISOU 1290  N   TYR B 159     2605   1115   1517   -358    -17     53       N  
ATOM   1291  CA  TYR B 159      10.264   9.693  31.438  1.00 12.68           C  
ANISOU 1291  CA  TYR B 159     2453    907   1459   -253   -113    214       C  
ATOM   1292  C   TYR B 159       8.992  10.549  31.503  1.00 13.98           C  
ANISOU 1292  C   TYR B 159     2387   1272   1651   -162   -175    120       C  
ATOM   1293  O   TYR B 159       8.962  11.714  31.131  1.00 15.00           O  
ANISOU 1293  O   TYR B 159     2486   1162   2052     95    339     56       O  
ATOM   1294  CB  TYR B 159      11.256  10.129  32.515  1.00 14.13           C  
ANISOU 1294  CB  TYR B 159     2429   1383   1559   -141   -208    178       C  
ATOM   1295  CG  TYR B 159      12.502   9.287  32.608  1.00 14.05           C  
ANISOU 1295  CG  TYR B 159     2514   1183   1641   -106   -182    250       C  
ATOM   1296  CD1 TYR B 159      13.558   9.551  31.740  1.00 13.90           C  
ANISOU 1296  CD1 TYR B 159     2361   1046   1873   -198   -244    284       C  
ATOM   1297  CD2 TYR B 159      12.621   8.264  33.529  1.00 14.72           C  
ANISOU 1297  CD2 TYR B 159     2702   1221   1671   -271   -330    300       C  
ATOM   1298  CE1 TYR B 159      14.714   8.799  31.797  1.00 15.47           C  
ANISOU 1298  CE1 TYR B 159     2523   1302   2054    -15   -108    225       C  
ATOM   1299  CE2 TYR B 159      13.788   7.515  33.578  1.00 16.09           C  
ANISOU 1299  CE2 TYR B 159     3066   1161   1888    -50   -385    312       C  
ATOM   1300  CZ  TYR B 159      14.828   7.781  32.718  1.00 15.91           C  
ANISOU 1300  CZ  TYR B 159     2889   1037   2117    174   -294     65       C  
ATOM   1301  OH  TYR B 159      16.006   7.037  32.756  1.00 19.05           O  
ANISOU 1301  OH  TYR B 159     2943   1825   2469    449   -852   -173       O  
ATOM   1302  N   ASP B 160       7.909   9.945  31.991  1.00 15.59           N  
ANISOU 1302  N   ASP B 160     2312   1533   2080   -230   -331    381       N  
ATOM   1303  CA  ASP B 160       6.657  10.681  32.112  1.00 16.17           C  
ANISOU 1303  CA  ASP B 160     2260   1849   2035   -177   -377    267       C  
ATOM   1304  C   ASP B 160       6.395  11.120  33.545  1.00 16.32           C  
ANISOU 1304  C   ASP B 160     2375   1919   1906    -95   -300    518       C  
ATOM   1305  O   ASP B 160       6.878  10.516  34.494  1.00 17.03           O  
ANISOU 1305  O   ASP B 160     2634   1765   2071   -344   -214    881       O  
ATOM   1306  CB  ASP B 160       5.491   9.818  31.647  1.00 17.32           C  
ANISOU 1306  CB  ASP B 160     2328   1928   2325   -363   -275    292       C  
ATOM   1307  CG  ASP B 160       5.604   9.511  30.165  1.00 19.60           C  
ANISOU 1307  CG  ASP B 160     2933   2125   2390   -854   -304     53       C  
ATOM   1308  OD1 ASP B 160       6.042  10.370  29.390  1.00 20.73           O  
ANISOU 1308  OD1 ASP B 160     3237   2329   2312   -768    -84    121       O  
ATOM   1309  OD2 ASP B 160       5.237   8.376  29.783  1.00 25.61           O  
ANISOU 1309  OD2 ASP B 160     4705   2110   2916  -1002   -506    -56       O  
ATOM   1310  N   GLN B 161       5.614  12.183  33.676  1.00 15.27           N  
ANISOU 1310  N   GLN B 161     2279   1679   1843   -321     66    651       N  
ATOM   1311  CA  GLN B 161       5.100  12.660  34.956  1.00 16.43           C  
ANISOU 1311  CA  GLN B 161     2257   2098   1889   -614    237    516       C  
ATOM   1312  C   GLN B 161       6.224  12.986  35.935  1.00 17.24           C  
ANISOU 1312  C   GLN B 161     2475   2309   1766   -696    149    654       C  
ATOM   1313  O   GLN B 161       6.127  12.611  37.114  1.00 22.03           O  
ANISOU 1313  O   GLN B 161     3022   3241   2108  -1292   -164   1351       O  
ATOM   1314  CB  GLN B 161       4.123  11.613  35.528  1.00 20.72           C  
ANISOU 1314  CB  GLN B 161     2666   2619   2588  -1036    667    366       C  
ATOM   1315  CG  GLN B 161       2.823  12.261  36.012  1.00 24.97           C  
ANISOU 1315  CG  GLN B 161     2962   3083   3442  -1163   1286   -183       C  
ATOM   1316  CD  GLN B 161       1.785  11.240  36.452  1.00 24.99           C  
ANISOU 1316  CD  GLN B 161     3152   2860   3484  -1307   1513   -702       C  
ATOM   1317  OE1 GLN B 161       1.387  10.346  35.689  1.00 32.16           O  
ANISOU 1317  OE1 GLN B 161     4991   2899   4328  -1553   1028   -985       O  
ATOM   1318  NE2 GLN B 161       1.317  11.353  37.705  1.00 23.19           N  
ANISOU 1318  NE2 GLN B 161     3178   1913   3719     43   1866    -27       N  
ATOM   1319  N   ILE B 162       7.260  13.668  35.456  1.00 14.59           N  
ANISOU 1319  N   ILE B 162     2436   1736   1369   -583     81    293       N  
ATOM   1320  CA  ILE B 162       8.431  14.117  36.202  1.00 14.53           C  
ANISOU 1320  CA  ILE B 162     2521   1598   1404   -492     10    165       C  
ATOM   1321  C   ILE B 162       8.180  15.517  36.723  1.00 14.10           C  
ANISOU 1321  C   ILE B 162     2492   1618   1248   -410    213    207       C  
ATOM   1322  O   ILE B 162       7.735  16.421  35.996  1.00 14.51           O  
ANISOU 1322  O   ILE B 162     2243   1937   1333    -86    186    193       O  
ATOM   1323  CB  ILE B 162       9.674  14.087  35.309  1.00 13.44           C  
ANISOU 1323  CB  ILE B 162     2219   1428   1460   -137   -235    118       C  
ATOM   1324  CG1 ILE B 162      10.052  12.662  34.865  1.00 13.86           C  
ANISOU 1324  CG1 ILE B 162     2272   1525   1469    -23   -852    -71       C  
ATOM   1325  CG2 ILE B 162      10.839  14.761  35.968  1.00 12.17           C  
ANISOU 1325  CG2 ILE B 162     2071    996   1556    268   -406     90       C  
ATOM   1326  CD1 ILE B 162      10.347  11.660  35.938  1.00 15.52           C  
ANISOU 1326  CD1 ILE B 162     2869   1492   1536    121   -931    -77       C  
ATOM   1327  N   ILE B 163       8.463  15.707  37.994  1.00 15.08           N  
ANISOU 1327  N   ILE B 163     2589   1655   1485   -388   -221    125       N  
ATOM   1328  CA  ILE B 163       8.302  17.036  38.594  1.00 15.55           C  
ANISOU 1328  CA  ILE B 163     2681   1750   1476   -509     -9     33       C  
ATOM   1329  C   ILE B 163       9.502  17.891  38.235  1.00 14.84           C  
ANISOU 1329  C   ILE B 163     2403   1639   1597   -341   -250     92       C  
ATOM   1330  O   ILE B 163      10.648  17.518  38.447  1.00 15.31           O  
ANISOU 1330  O   ILE B 163     2551   1576   1690   -208   -203    482       O  
ATOM   1331  CB  ILE B 163       8.096  16.923  40.113  1.00 18.69           C  
ANISOU 1331  CB  ILE B 163     3486   2144   1470   -568     35     34       C  
ATOM   1332  CG1 ILE B 163       6.952  15.957  40.445  1.00 19.58           C  
ANISOU 1332  CG1 ILE B 163     3794   2223   1424   -647     67    459       C  
ATOM   1333  CG2 ILE B 163       7.938  18.317  40.721  1.00 26.72           C  
ANISOU 1333  CG2 ILE B 163     5304   2682   2164  -1223    389   -878       C  
ATOM   1334  CD1 ILE B 163       6.781  15.443  41.830  1.00 26.05           C  
ANISOU 1334  CD1 ILE B 163     4890   3338   1669   -555    264    953       C  
ATOM   1335  N   ILE B 164       9.183  19.052  37.679  1.00 13.08           N  
ANISOU 1335  N   ILE B 164     1897   1641   1430   -211    -89     29       N  
ATOM   1336  CA  ILE B 164      10.262  19.939  37.280  1.00 13.11           C  
ANISOU 1336  CA  ILE B 164     1869   1765   1349   -192    -71    170       C  
ATOM   1337  C   ILE B 164       9.832  21.376  37.466  1.00 13.18           C  
ANISOU 1337  C   ILE B 164     1873   1694   1439   -244   -246    338       C  
ATOM   1338  O   ILE B 164       8.740  21.701  37.077  1.00 17.89           O  
ANISOU 1338  O   ILE B 164     1955   1831   3012   -131   -653   -198       O  
ATOM   1339  CB  ILE B 164      10.688  19.639  35.823  1.00 13.63           C  
ANISOU 1339  CB  ILE B 164     2174   1885   1121   -274   -300    322       C  
ATOM   1340  CG1 ILE B 164      11.703  20.663  35.282  1.00 13.69           C  
ANISOU 1340  CG1 ILE B 164     2131   1860   1209   -257    -67    139       C  
ATOM   1341  CG2 ILE B 164       9.508  19.505  34.896  1.00 16.72           C  
ANISOU 1341  CG2 ILE B 164     2390   2434   1530   -593   -537    443       C  
ATOM   1342  CD1 ILE B 164      12.211  20.375  33.891  1.00 16.22           C  
ANISOU 1342  CD1 ILE B 164     2444   2361   1358   -160    158     77       C  
ATOM   1343  N   GLU B 165      10.710  22.179  38.057  1.00 13.16           N  
ANISOU 1343  N   GLU B 165     2006   1731   1264   -252   -280    304       N  
ATOM   1344  CA  GLU B 165      10.470  23.615  38.237  1.00 13.97           C  
ANISOU 1344  CA  GLU B 165     2276   1753   1278   -238   -351    253       C  
ATOM   1345  C   GLU B 165      11.153  24.351  37.093  1.00 14.16           C  
ANISOU 1345  C   GLU B 165     2119   1634   1628    -93   -213    368       C  
ATOM   1346  O   GLU B 165      12.314  24.027  36.803  1.00 15.78           O  
ANISOU 1346  O   GLU B 165     1920   2010   2067   -152   -341    781       O  
ATOM   1347  CB  GLU B 165      10.964  24.130  39.584  1.00 19.64           C  
ANISOU 1347  CB  GLU B 165     3347   2613   1502   -414   -422   -292       C  
ATOM   1348  CG  GLU B 165      10.365  25.409  40.136  1.00 27.99           C  
ANISOU 1348  CG  GLU B 165     4722   3406   2507    -43   -125  -1172       C  
ATOM   1349  CD  GLU B 165      10.785  25.763  41.551  1.00 32.59           C  
ANISOU 1349  CD  GLU B 165     5489   4511   2381   -979    341  -1534       C  
ATOM   1350  OE1 GLU B 165      11.846  26.396  41.808  1.00 41.21           O  
ANISOU 1350  OE1 GLU B 165     7126   5939   2593  -2682   -594   -467       O  
ATOM   1351  OE2 GLU B 165      10.050  25.422  42.523  1.00 41.21           O  
ANISOU 1351  OE2 GLU B 165     6099   6905   2655  -1365    465   -773       O  
ATOM   1352  N   ILE B 166      10.436  25.292  36.492  1.00 13.10           N  
ANISOU 1352  N   ILE B 166     2141   1438   1399    -15    -45    204       N  
ATOM   1353  CA  ILE B 166      10.996  26.074  35.392  1.00 12.05           C  
ANISOU 1353  CA  ILE B 166     2020   1208   1350     93     49     25       C  
ATOM   1354  C   ILE B 166      10.865  27.566  35.707  1.00 11.83           C  
ANISOU 1354  C   ILE B 166     1918   1266   1311    176    -45     19       C  
ATOM   1355  O   ILE B 166       9.752  28.059  35.736  1.00 13.87           O  
ANISOU 1355  O   ILE B 166     2118   1693   1458    552   -101   -133       O  
ATOM   1356  CB  ILE B 166      10.300  25.743  34.072  1.00 14.51           C  
ANISOU 1356  CB  ILE B 166     2801   1451   1262    187    -53   -135       C  
ATOM   1357  CG1 ILE B 166      10.356  24.246  33.749  1.00 15.19           C  
ANISOU 1357  CG1 ILE B 166     3214   1437   1121    224   -255    -11       C  
ATOM   1358  CG2 ILE B 166      10.874  26.596  32.959  1.00 14.31           C  
ANISOU 1358  CG2 ILE B 166     2565   1536   1338   -137   -415    -72       C  
ATOM   1359  CD1 ILE B 166       9.258  23.765  32.841  1.00 17.28           C  
ANISOU 1359  CD1 ILE B 166     2995   1517   2054   -137   -318    -86       C  
ATOM   1360  N   ALA B 167      11.990  28.227  35.936  1.00 13.77           N  
ANISOU 1360  N   ALA B 167     2174   1466   1592   -164    178   -246       N  
ATOM   1361  CA  ALA B 167      11.965  29.646  36.236  1.00 14.48           C  
ANISOU 1361  CA  ALA B 167     2257   1469   1775     50     10   -284       C  
ATOM   1362  C   ALA B 167      11.003  29.920  37.380  1.00 16.22           C  
ANISOU 1362  C   ALA B 167     2568   1687   1908    -20    185   -472       C  
ATOM   1363  O   ALA B 167      10.292  30.924  37.386  1.00 20.58           O  
ANISOU 1363  O   ALA B 167     3496   1938   2387    485    719   -457       O  
ATOM   1364  CB  ALA B 167      11.609  30.417  34.969  1.00 17.73           C  
ANISOU 1364  CB  ALA B 167     2325   2198   2213   1245    513    212       C  
ATOM   1365  N   GLY B 168      10.974  29.012  38.357  1.00 16.27           N  
ANISOU 1365  N   GLY B 168     2662   1824   1696   -181    167   -550       N  
ATOM   1366  CA  GLY B 168      10.106  29.183  39.516  1.00 19.05           C  
ANISOU 1366  CA  GLY B 168     3042   2296   1901   -228    412   -638       C  
ATOM   1367  C   GLY B 168       8.689  28.694  39.329  1.00 18.12           C  
ANISOU 1367  C   GLY B 168     2920   2348   1615   -113    556   -773       C  
ATOM   1368  O   GLY B 168       7.926  28.765  40.288  1.00 24.20           O  
ANISOU 1368  O   GLY B 168     3248   4204   1743   -393    764  -1204       O  
ATOM   1369  N   HIS B 169       8.339  28.212  38.150  1.00 16.67           N  
ANISOU 1369  N   HIS B 169     2941   1996   1398     79    359   -375       N  
ATOM   1370  CA  HIS B 169       6.998  27.680  37.882  1.00 17.91           C  
ANISOU 1370  CA  HIS B 169     2936   2159   1712    139    279   -575       C  
ATOM   1371  C   HIS B 169       7.005  26.151  37.925  1.00 19.36           C  
ANISOU 1371  C   HIS B 169     3165   2149   2042   -120    669   -584       C  
ATOM   1372  O   HIS B 169       7.882  25.512  37.330  1.00 17.07           O  
ANISOU 1372  O   HIS B 169     2581   2008   1899   -104    195   -559       O  
ATOM   1373  CB  HIS B 169       6.435  28.133  36.530  1.00 18.08           C  
ANISOU 1373  CB  HIS B 169     2763   2567   1540    552    394   -807       C  
ATOM   1374  CG  HIS B 169       6.251  29.619  36.517  1.00 19.86           C  
ANISOU 1374  CG  HIS B 169     3063   2567   1914    609    271   -451       C  
ATOM   1375  ND1 HIS B 169       5.012  30.211  36.489  1.00 21.92           N  
ANISOU 1375  ND1 HIS B 169     3184   2589   2556    679    -64    114       N  
ATOM   1376  CD2 HIS B 169       7.148  30.632  36.538  1.00 20.77           C  
ANISOU 1376  CD2 HIS B 169     3228   2535   2129    556    142    101       C  
ATOM   1377  CE1 HIS B 169       5.145  31.527  36.490  1.00 21.89           C  
ANISOU 1377  CE1 HIS B 169     3322   2580   2414    694    234   -136       C  
ATOM   1378  NE2 HIS B 169       6.431  31.812  36.520  1.00 21.61           N  
ANISOU 1378  NE2 HIS B 169     3363   2558   2291    610    365    -47       N  
ATOM   1379  N   LYS B 170       6.022  25.590  38.636  1.00 21.04           N  
ANISOU 1379  N   LYS B 170     3336   2555   2103   -313    810   -680       N  
ATOM   1380  CA  LYS B 170       5.961  24.130  38.769  1.00 21.78           C  
ANISOU 1380  CA  LYS B 170     3679   2654   1940   -522    638   -353       C  
ATOM   1381  C   LYS B 170       5.278  23.491  37.569  1.00 19.94           C  
ANISOU 1381  C   LYS B 170     2943   2281   2350   -242    386   -365       C  
ATOM   1382  O   LYS B 170       4.240  23.969  37.144  1.00 23.09           O  
ANISOU 1382  O   LYS B 170     2788   2070   3916    -31    190  -1182       O  
ATOM   1383  CB  LYS B 170       5.240  23.692  40.064  1.00 29.90           C  
ANISOU 1383  CB  LYS B 170     5030   4100   2232   -359   1042    445       C  
ATOM   1384  CG  LYS B 170       5.968  24.217  41.298  1.00 36.32           C  
ANISOU 1384  CG  LYS B 170     6202   5682   1918    -86    733    336       C  
ATOM   1385  CD  LYS B 170       5.636  23.371  42.527  1.00 43.77           C  
ANISOU 1385  CD  LYS B 170     7265   7165   2201   -175   1113    913       C  
ATOM   1386  CE  LYS B 170       6.149  24.034  43.802  1.00 47.94           C  
ANISOU 1386  CE  LYS B 170     8071   8122   2022   -299    817   1005       C  
ATOM   1387  NZ  LYS B 170       6.407  23.057  44.911  1.00 58.99           N  
ANISOU 1387  NZ  LYS B 170     9671  10142   2600    278    530   2052       N  
ATOM   1388  N   ALA B 171       5.916  22.427  37.086  1.00 16.36           N  
ANISOU 1388  N   ALA B 171     2076   1886   2255   -461   -128   -113       N  
ATOM   1389  CA  ALA B 171       5.394  21.609  36.010  1.00 13.89           C  
ANISOU 1389  CA  ALA B 171     1648   1728   1902   -414     91     82       C  
ATOM   1390  C   ALA B 171       5.568  20.147  36.387  1.00 13.38           C  
ANISOU 1390  C   ALA B 171     1434   1752   1896   -189    -33    -63       C  
ATOM   1391  O   ALA B 171       6.429  19.873  37.202  1.00 15.59           O  
ANISOU 1391  O   ALA B 171     1938   1861   2126   -391   -484    -21       O  
ATOM   1392  CB  ALA B 171       6.089  21.905  34.714  1.00 15.12           C  
ANISOU 1392  CB  ALA B 171     1442   1996   2308   -579    480    -33       C  
ATOM   1393  N   ILE B 172       4.751  19.296  35.796  1.00 12.57           N  
ANISOU 1393  N   ILE B 172     1518   1558   1701    -46   -131    -58       N  
ATOM   1394  CA  ILE B 172       4.874  17.847  35.967  1.00 12.09           C  
ANISOU 1394  CA  ILE B 172     1552   1595   1448    -92     69     84       C  
ATOM   1395  C   ILE B 172       4.547  17.244  34.617  1.00 11.65           C  
ANISOU 1395  C   ILE B 172     1620   1381   1423   -377    119    190       C  
ATOM   1396  O   ILE B 172       3.415  17.306  34.168  1.00 13.92           O  
ANISOU 1396  O   ILE B 172     1756   2135   1399   -178    -35    247       O  
ATOM   1397  CB  ILE B 172       3.960  17.255  37.033  1.00 13.40           C  
ANISOU 1397  CB  ILE B 172     1839   1737   1514   -221    310   -151       C  
ATOM   1398  CG1 ILE B 172       3.996  18.016  38.346  1.00 15.02           C  
ANISOU 1398  CG1 ILE B 172     1894   2263   1549   -754    284   -295       C  
ATOM   1399  CG2 ILE B 172       4.304  15.792  37.239  1.00 15.02           C  
ANISOU 1399  CG2 ILE B 172     1803   1769   2134   -216    487    254       C  
ATOM   1400  CD1 ILE B 172       3.030  17.497  39.382  1.00 17.27           C  
ANISOU 1400  CD1 ILE B 172     2688   2889    983  -1467    -38    -17       C  
ATOM   1401  N   GLY B 173       5.539  16.672  33.961  1.00 12.51           N  
ANISOU 1401  N   GLY B 173     1801   1450   1502   -200    -53    -62       N  
ATOM   1402  CA  GLY B 173       5.284  16.221  32.603  1.00 13.12           C  
ANISOU 1402  CA  GLY B 173     2007   1664   1315     11   -111    102       C  
ATOM   1403  C   GLY B 173       6.451  15.404  32.100  1.00 12.88           C  
ANISOU 1403  C   GLY B 173     1874   1736   1286   -110    -82     14       C  
ATOM   1404  O   GLY B 173       7.323  14.959  32.854  1.00 13.36           O  
ANISOU 1404  O   GLY B 173     1792   2027   1258    -32     71    120       O  
ATOM   1405  N   THR B 174       6.435  15.220  30.789  1.00 13.05           N  
ANISOU 1405  N   THR B 174     2154   1475   1329   -184   -137    -56       N  
ATOM   1406  CA  THR B 174       7.393  14.320  30.168  1.00 14.14           C  
ANISOU 1406  CA  THR B 174     2383   1609   1382   -117     71    -58       C  
ATOM   1407  C   THR B 174       8.737  15.003  29.930  1.00 13.35           C  
ANISOU 1407  C   THR B 174     2307   1310   1455     61      3     77       C  
ATOM   1408  O   THR B 174       8.834  16.128  29.414  1.00 12.68           O  
ANISOU 1408  O   THR B 174     2093   1431   1293    188   -166    206       O  
ATOM   1409  CB  THR B 174       6.847  13.804  28.835  1.00 13.64           C  
ANISOU 1409  CB  THR B 174     2311   1455   1416    151   -103      7       C  
ATOM   1410  OG1 THR B 174       5.658  13.035  29.111  1.00 16.54           O  
ANISOU 1410  OG1 THR B 174     2548   1971   1765   -255    -83   -191       O  
ATOM   1411  CG2 THR B 174       7.862  12.902  28.140  1.00 15.61           C  
ANISOU 1411  CG2 THR B 174     2587   1692   1650    294   -143   -269       C  
ATOM   1412  N   VAL B 175       9.771  14.277  30.323  1.00 12.94           N  
ANISOU 1412  N   VAL B 175     2414   1104   1399     72     13    193       N  
ATOM   1413  CA  VAL B 175      11.132  14.706  30.144  1.00 13.04           C  
ANISOU 1413  CA  VAL B 175     2369   1117   1470     88    -74    195       C  
ATOM   1414  C   VAL B 175      11.882  13.627  29.383  1.00 12.19           C  
ANISOU 1414  C   VAL B 175     2235    838   1559   -114    -33    250       C  
ATOM   1415  O   VAL B 175      11.857  12.477  29.789  1.00 13.04           O  
ANISOU 1415  O   VAL B 175     2048    930   1976   -150     10    455       O  
ATOM   1416  CB  VAL B 175      11.795  14.977  31.501  1.00 14.39           C  
ANISOU 1416  CB  VAL B 175     2689   1257   1521   -123   -137    131       C  
ATOM   1417  CG1 VAL B 175      13.258  15.340  31.329  1.00 15.77           C  
ANISOU 1417  CG1 VAL B 175     3030   1562   1399   -832    -46   -192       C  
ATOM   1418  CG2 VAL B 175      11.007  16.074  32.194  1.00 16.59           C  
ANISOU 1418  CG2 VAL B 175     3651   1245   1405     97     44    177       C  
ATOM   1419  N   LEU B 176      12.508  14.062  28.303  1.00 12.18           N  
ANISOU 1419  N   LEU B 176     2249    658   1723   -174     85    189       N  
ATOM   1420  CA  LEU B 176      13.373  13.204  27.506  1.00 11.03           C  
ANISOU 1420  CA  LEU B 176     1880    897   1416   -190   -313     20       C  
ATOM   1421  C   LEU B 176      14.820  13.429  27.950  1.00 12.78           C  
ANISOU 1421  C   LEU B 176     2024    896   1935   -114   -700     71       C  
ATOM   1422  O   LEU B 176      15.227  14.557  28.192  1.00 15.12           O  
ANISOU 1422  O   LEU B 176     2045    924   2776   -329   -588    108       O  
ATOM   1423  CB  LEU B 176      13.186  13.478  26.028  1.00 11.90           C  
ANISOU 1423  CB  LEU B 176     2058   1024   1438   -262   -442     87       C  
ATOM   1424  CG  LEU B 176      11.734  13.548  25.526  1.00 10.58           C  
ANISOU 1424  CG  LEU B 176     1886    854   1281   -102   -217    -59       C  
ATOM   1425  CD1 LEU B 176      11.718  13.905  24.043  1.00 10.96           C  
ANISOU 1425  CD1 LEU B 176     2212    521   1431     17   -404    184       C  
ATOM   1426  CD2 LEU B 176      10.957  12.258  25.779  1.00 12.75           C  
ANISOU 1426  CD2 LEU B 176     2082   1250   1512   -400   -185    277       C  
ATOM   1427  N   VAL B 177      15.528  12.308  28.037  1.00 12.54           N  
ANISOU 1427  N   VAL B 177     2123   1020   1621     46   -467    188       N  
ATOM   1428  CA  VAL B 177      16.922  12.350  28.476  1.00 12.79           C  
ANISOU 1428  CA  VAL B 177     1995   1088   1778    -20   -337    450       C  
ATOM   1429  C   VAL B 177      17.792  11.757  27.371  1.00 14.10           C  
ANISOU 1429  C   VAL B 177     2107   1279   1973     51   -408    124       C  
ATOM   1430  O   VAL B 177      17.600  10.644  26.902  1.00 15.79           O  
ANISOU 1430  O   VAL B 177     2038   1385   2575     55   -537   -132       O  
ATOM   1431  CB  VAL B 177      17.171  11.603  29.797  1.00 14.10           C  
ANISOU 1431  CB  VAL B 177     1911   1428   2018   -357   -529    738       C  
ATOM   1432  CG1 VAL B 177      18.660  11.605  30.200  1.00 17.89           C  
ANISOU 1432  CG1 VAL B 177     2118   1939   2740   -478  -1045    681       C  
ATOM   1433  CG2 VAL B 177      16.326  12.211  30.905  1.00 15.85           C  
ANISOU 1433  CG2 VAL B 177     2447   2054   1520   -396   -789    329       C  
ATOM   1434  N   GLY B 178      18.778  12.551  26.962  1.00 14.32           N  
ANISOU 1434  N   GLY B 178     2063   1221   2156    168    -48   -130       N  
ATOM   1435  CA  GLY B 178      19.692  12.091  25.930  1.00 16.39           C  
ANISOU 1435  CA  GLY B 178     2435   1303   2490    246    142   -399       C  
ATOM   1436  C   GLY B 178      20.722  13.136  25.527  1.00 17.28           C  
ANISOU 1436  C   GLY B 178     2168   1679   2720    162    379   -611       C  
ATOM   1437  O   GLY B 178      20.821  14.191  26.170  1.00 17.98           O  
ANISOU 1437  O   GLY B 178     2613   2121   2100   -532    533   -688       O  
ATOM   1438  N   PRO B 179      21.460  12.807  24.468  1.00 19.02           N  
ANISOU 1438  N   PRO B 179     2269   1888   3071    372    543   -777       N  
ATOM   1439  CA  PRO B 179      22.618  13.642  24.100  1.00 19.97           C  
ANISOU 1439  CA  PRO B 179     2363   2078   3146    389    759   -584       C  
ATOM   1440  C   PRO B 179      22.215  14.906  23.365  1.00 20.47           C  
ANISOU 1440  C   PRO B 179     2687   2300   2789    411    695   -450       C  
ATOM   1441  O   PRO B 179      22.552  15.122  22.212  1.00 24.33           O  
ANISOU 1441  O   PRO B 179     3721   2859   2664      0    649   -595       O  
ATOM   1442  CB  PRO B 179      23.414  12.733  23.174  1.00 21.96           C  
ANISOU 1442  CB  PRO B 179     2438   2577   3329    575    725   -882       C  
ATOM   1443  CG  PRO B 179      22.351  11.900  22.533  1.00 20.71           C  
ANISOU 1443  CG  PRO B 179     2198   2324   3345    996    523   -877       C  
ATOM   1444  CD  PRO B 179      21.293  11.661  23.560  1.00 19.06           C  
ANISOU 1444  CD  PRO B 179     2410   1811   3021    710    381   -735       C  
ATOM   1445  N   THR B 180      21.480  15.741  24.085  1.00 20.91           N  
ANISOU 1445  N   THR B 180     2865   2433   2648    865    149   -504       N  
ATOM   1446  CA  THR B 180      21.173  17.056  23.558  1.00 18.01           C  
ANISOU 1446  CA  THR B 180     2535   2481   1828    615    -23   -512       C  
ATOM   1447  C   THR B 180      22.315  18.017  23.888  1.00 19.21           C  
ANISOU 1447  C   THR B 180     2617   2880   1800    370     74   -406       C  
ATOM   1448  O   THR B 180      22.938  17.902  24.950  1.00 17.75           O  
ANISOU 1448  O   THR B 180     2376   2468   1901    587     55   -540       O  
ATOM   1449  CB  THR B 180      19.824  17.583  24.090  1.00 16.53           C  
ANISOU 1449  CB  THR B 180     2582   2095   1605    532    -79   -858       C  
ATOM   1450  OG1 THR B 180      19.687  18.942  23.644  1.00 17.14           O  
ANISOU 1450  OG1 THR B 180     2554   2184   1773    426    -12   -600       O  
ATOM   1451  CG2 THR B 180      19.761  17.615  25.599  1.00 18.56           C  
ANISOU 1451  CG2 THR B 180     2759   2722   1572    463   -112   -572       C  
ATOM   1452  N   PRO B 181      22.647  18.966  23.020  1.00 19.33           N  
ANISOU 1452  N   PRO B 181     2293   3049   2001    417     77   -262       N  
ATOM   1453  CA  PRO B 181      23.751  19.904  23.284  1.00 18.91           C  
ANISOU 1453  CA  PRO B 181     1912   3206   2067    525    237   -339       C  
ATOM   1454  C   PRO B 181      23.525  20.912  24.406  1.00 18.71           C  
ANISOU 1454  C   PRO B 181     1632   3382   2094    534    -84   -474       C  
ATOM   1455  O   PRO B 181      24.474  21.419  24.972  1.00 20.64           O  
ANISOU 1455  O   PRO B 181     1868   3442   2533    -96     20   -329       O  
ATOM   1456  CB APRO B 181      23.825  20.705  21.974  0.60 19.44           C  
ANISOU 1456  CB APRO B 181     2077   3186   2122    378    163   -285       C  
ATOM   1457  CB BPRO B 181      23.874  20.702  21.966  0.40 19.25           C  
ANISOU 1457  CB BPRO B 181     1981   3219   2115    386    103   -267       C  
ATOM   1458  CG APRO B 181      22.465  20.602  21.375  0.60 19.56           C  
ANISOU 1458  CG APRO B 181     2157   3199   2077    207    149   -115       C  
ATOM   1459  CG BPRO B 181      23.312  19.741  20.960  0.40 19.46           C  
ANISOU 1459  CG BPRO B 181     2149   3163   2080    328    123   -218       C  
ATOM   1460  CD APRO B 181      21.996  19.207  21.711  0.60 20.07           C  
ANISOU 1460  CD APRO B 181     2358   3166   2103    215      4    -66       C  
ATOM   1461  CD BPRO B 181      22.064  19.288  21.683  0.40 19.73           C  
ANISOU 1461  CD BPRO B 181     2275   3157   2065    202     77    -77       C  
ATOM   1462  N   VAL B 182      22.280  21.193  24.703  1.00 17.73           N  
ANISOU 1462  N   VAL B 182     1756   3077   1904    647     25   -268       N  
ATOM   1463  CA  VAL B 182      21.836  22.052  25.769  1.00 16.73           C  
ANISOU 1463  CA  VAL B 182     2112   2535   1709    415    218     -6       C  
ATOM   1464  C   VAL B 182      20.503  21.515  26.288  1.00 14.38           C  
ANISOU 1464  C   VAL B 182     1872   1948   1643    618     -4    -99       C  
ATOM   1465  O   VAL B 182      19.764  20.879  25.546  1.00 16.70           O  
ANISOU 1465  O   VAL B 182     2180   2396   1768    440    101   -476       O  
ATOM   1466  CB AVAL B 182      21.628  23.522  25.369  0.60 18.51           C  
ANISOU 1466  CB AVAL B 182     2275   2670   2090    438    673    324       C  
ATOM   1467  CB BVAL B 182      21.630  23.507  25.337  0.40 18.62           C  
ANISOU 1467  CB BVAL B 182     2290   2676   2108    442    651    321       C  
ATOM   1468  CG1AVAL B 182      22.914  24.125  24.814  0.60 19.65           C  
ANISOU 1468  CG1AVAL B 182     2001   2487   2979    794    933    246       C  
ATOM   1469  CG1BVAL B 182      20.519  23.568  24.298  0.40 20.65           C  
ANISOU 1469  CG1BVAL B 182     2231   2994   2621    634    469    749       C  
ATOM   1470  CG2AVAL B 182      20.483  23.606  24.374  0.60 21.04           C  
ANISOU 1470  CG2AVAL B 182     2188   3111   2695    544    514    929       C  
ATOM   1471  CG2BVAL B 182      21.313  24.389  26.534  0.40 20.95           C  
ANISOU 1471  CG2BVAL B 182     2980   2438   2543    608   1079    282       C  
ATOM   1472  N   ASN B 183      20.222  21.788  27.553  1.00 12.32           N  
ANISOU 1472  N   ASN B 183     1910   1341   1430    315   -127    281       N  
ATOM   1473  CA  ASN B 183      18.920  21.442  28.095  1.00 11.50           C  
ANISOU 1473  CA  ASN B 183     1830   1247   1292    187   -215   -120       C  
ATOM   1474  C   ASN B 183      17.886  22.348  27.447  1.00 10.63           C  
ANISOU 1474  C   ASN B 183     1768    962   1310    -39   -277   -132       C  
ATOM   1475  O   ASN B 183      18.070  23.565  27.428  1.00 11.28           O  
ANISOU 1475  O   ASN B 183     2206    947   1131   -149   -313   -194       O  
ATOM   1476  CB  ASN B 183      18.900  21.589  29.599  1.00 11.59           C  
ANISOU 1476  CB  ASN B 183     1903   1242   1259     79   -248   -148       C  
ATOM   1477  CG  ASN B 183      19.878  20.684  30.309  1.00 11.16           C  
ANISOU 1477  CG  ASN B 183     1720   1337   1182    107      9     -7       C  
ATOM   1478  OD1 ASN B 183      20.129  19.541  29.892  1.00 14.99           O  
ANISOU 1478  OD1 ASN B 183     2270   1211   2213    113   -695   -157       O  
ATOM   1479  ND2 ASN B 183      20.441  21.196  31.399  1.00 13.25           N  
ANISOU 1479  ND2 ASN B 183     2027   1731   1274    403   -242   -137       N  
ATOM   1480  N   ILE B 184      16.832  21.730  26.934  1.00 10.10           N  
ANISOU 1480  N   ILE B 184     1650   1131   1056   -190   -109     -7       N  
ATOM   1481  CA  ILE B 184      15.793  22.485  26.252  1.00 11.17           C  
ANISOU 1481  CA  ILE B 184     1792   1404   1047    -46   -195    -43       C  
ATOM   1482  C   ILE B 184      14.439  22.224  26.871  1.00 10.29           C  
ANISOU 1482  C   ILE B 184     1666   1015   1228   -115   -325   -332       C  
ATOM   1483  O   ILE B 184      14.033  21.088  27.081  1.00 11.07           O  
ANISOU 1483  O   ILE B 184     1800    962   1442     77   -143    -41       O  
ATOM   1484  CB AILE B 184      15.772  22.237  24.718  0.60 13.23           C  
ANISOU 1484  CB AILE B 184     2055   1888   1083     29   -319   -130       C  
ATOM   1485  CB BILE B 184      15.774  21.967  24.810  0.40 12.93           C  
ANISOU 1485  CB BILE B 184     2031   1793   1088     40   -279   -144       C  
ATOM   1486  CG1AILE B 184      15.586  20.825  24.221  0.60 13.15           C  
ANISOU 1486  CG1AILE B 184     2083   1952    961     50   -455   -196       C  
ATOM   1487  CG1BILE B 184      16.876  22.506  23.878  0.40 13.10           C  
ANISOU 1487  CG1BILE B 184     2019   1990    969     37   -231   -293       C  
ATOM   1488  CG2AILE B 184      17.070  22.834  24.142  0.60 12.38           C  
ANISOU 1488  CG2AILE B 184     1951   2157    595    -52   -331   -635       C  
ATOM   1489  CG2BILE B 184      14.405  22.193  24.169  0.40 12.87           C  
ANISOU 1489  CG2BILE B 184     2019   1855   1018     27   -246    -99       C  
ATOM   1490  CD1AILE B 184      15.563  20.734  22.704  0.60 13.12           C  
ANISOU 1490  CD1AILE B 184     2555   1523    906    253   -481    123       C  
ATOM   1491  CD1BILE B 184      17.330  21.400  22.929  0.40 11.04           C  
ANISOU 1491  CD1BILE B 184     2134   1317    743    -64   -356     91       C  
ATOM   1492  N   ILE B 185      13.725  23.292  27.179  1.00  9.99           N  
ANISOU 1492  N   ILE B 185     1657    887   1252   -159   -353   -221       N  
ATOM   1493  CA  ILE B 185      12.357  23.208  27.635  1.00 10.65           C  
ANISOU 1493  CA  ILE B 185     1685    935   1429      1   -257    -35       C  
ATOM   1494  C   ILE B 185      11.460  23.430  26.432  1.00 10.32           C  
ANISOU 1494  C   ILE B 185     1550   1034   1340     20   -124    -25       C  
ATOM   1495  O   ILE B 185      11.467  24.544  25.867  1.00 11.40           O  
ANISOU 1495  O   ILE B 185     1910    921   1501    237   -302   -108       O  
ATOM   1496  CB  ILE B 185      12.071  24.245  28.721  1.00 10.92           C  
ANISOU 1496  CB  ILE B 185     1927    947   1274    -15   -131     67       C  
ATOM   1497  CG1 ILE B 185      13.096  24.204  29.866  1.00 12.16           C  
ANISOU 1497  CG1 ILE B 185     2397   1012   1211    309   -280     38       C  
ATOM   1498  CG2 ILE B 185      10.639  24.117  29.228  1.00 12.28           C  
ANISOU 1498  CG2 ILE B 185     2214   1374   1077   -300    142     44       C  
ATOM   1499  CD1 ILE B 185      13.187  22.852  30.530  1.00 13.19           C  
ANISOU 1499  CD1 ILE B 185     2584   1072   1355    302     11    239       C  
ATOM   1500  N   GLY B 186      10.722  22.404  26.055  1.00 11.16           N  
ANISOU 1500  N   GLY B 186     1739   1253   1249   -190   -166     -8       N  
ATOM   1501  CA  GLY B 186       9.889  22.457  24.880  1.00 11.06           C  
ANISOU 1501  CA  GLY B 186     1722   1264   1217     61   -131   -173       C  
ATOM   1502  C   GLY B 186       8.452  22.751  25.194  1.00 10.31           C  
ANISOU 1502  C   GLY B 186     1803   1077   1037    107   -131   -152       C  
ATOM   1503  O   GLY B 186       8.105  22.973  26.344  1.00 10.58           O  
ANISOU 1503  O   GLY B 186     1913   1122    986   -182     51    133       O  
ATOM   1504  N   ARG B 187       7.621  22.752  24.148  1.00 10.60           N  
ANISOU 1504  N   ARG B 187     1844    964   1220     85   -302    -67       N  
ATOM   1505  CA  ARG B 187       6.252  23.232  24.309  1.00 10.68           C  
ANISOU 1505  CA  ARG B 187     1864    921   1274    120   -140    180       C  
ATOM   1506  C   ARG B 187       5.454  22.410  25.304  1.00 11.56           C  
ANISOU 1506  C   ARG B 187     2050   1155   1188   -169   -193    167       C  
ATOM   1507  O   ARG B 187       4.532  22.944  25.919  1.00 12.87           O  
ANISOU 1507  O   ARG B 187     1832   1568   1489   -119   -131    241       O  
ATOM   1508  CB  ARG B 187       5.558  23.251  22.930  1.00 10.30           C  
ANISOU 1508  CB  ARG B 187     1540   1225   1148    157     32    103       C  
ATOM   1509  CG  ARG B 187       6.193  24.271  21.999  1.00 10.75           C  
ANISOU 1509  CG  ARG B 187     1763   1010   1312    173   -222    248       C  
ATOM   1510  CD  ARG B 187       5.405  24.487  20.712  1.00 12.13           C  
ANISOU 1510  CD  ARG B 187     1774   1308   1527    -44   -399    448       C  
ATOM   1511  NE  ARG B 187       5.423  23.240  19.956  1.00 12.31           N  
ANISOU 1511  NE  ARG B 187     1844   1533   1300   -312   -291    356       N  
ATOM   1512  CZ  ARG B 187       4.466  22.328  19.942  1.00 13.14           C  
ANISOU 1512  CZ  ARG B 187     1797   2249    946   -594   -383   -144       C  
ATOM   1513  NH1 ARG B 187       3.330  22.422  20.619  1.00 14.44           N  
ANISOU 1513  NH1 ARG B 187     2092   2012   1383   -453     46    360       N  
ATOM   1514  NH2 ARG B 187       4.653  21.232  19.190  1.00 14.88           N  
ANISOU 1514  NH2 ARG B 187     2227   2098   1330   -609   -239   -144       N  
ATOM   1515  N   ASN B 188       5.787  21.128  25.477  1.00 11.63           N  
ANISOU 1515  N   ASN B 188     2096   1196   1127   -270   -228    236       N  
ATOM   1516  CA  ASN B 188       4.993  20.351  26.427  1.00 12.04           C  
ANISOU 1516  CA  ASN B 188     2095   1181   1300   -191    -70    236       C  
ATOM   1517  C   ASN B 188       5.066  20.932  27.837  1.00 12.08           C  
ANISOU 1517  C   ASN B 188     2060   1213   1319   -323    112    215       C  
ATOM   1518  O   ASN B 188       4.081  20.778  28.573  1.00 14.15           O  
ANISOU 1518  O   ASN B 188     1868   2140   1367   -362    -19    118       O  
ATOM   1519  CB  ASN B 188       5.455  18.906  26.442  1.00 11.38           C  
ANISOU 1519  CB  ASN B 188     1939   1204   1180   -148   -156    266       C  
ATOM   1520  CG  ASN B 188       6.792  18.720  27.115  1.00 11.34           C  
ANISOU 1520  CG  ASN B 188     1909   1355   1044   -209   -142    103       C  
ATOM   1521  OD1 ASN B 188       7.770  19.373  26.737  1.00 11.35           O  
ANISOU 1521  OD1 ASN B 188     1829   1480   1003    -37    151     99       O  
ATOM   1522  ND2 ASN B 188       6.768  17.809  28.098  1.00 12.96           N  
ANISOU 1522  ND2 ASN B 188     1565   1722   1638   -168   -210    570       N  
ATOM   1523  N   LEU B 189       6.153  21.576  28.232  1.00 11.35           N  
ANISOU 1523  N   LEU B 189     1995   1183   1134   -281    169    252       N  
ATOM   1524  CA  LEU B 189       6.175  22.218  29.541  1.00 10.70           C  
ANISOU 1524  CA  LEU B 189     1758   1254   1053      9     75    320       C  
ATOM   1525  C   LEU B 189       5.999  23.726  29.439  1.00 10.96           C  
ANISOU 1525  C   LEU B 189     1950   1237    978      5    145    283       C  
ATOM   1526  O   LEU B 189       5.536  24.331  30.407  1.00 13.00           O  
ANISOU 1526  O   LEU B 189     2375   1492   1072     63     39    -10       O  
ATOM   1527  CB  LEU B 189       7.472  21.862  30.264  1.00 13.15           C  
ANISOU 1527  CB  LEU B 189     2006   1343   1649    -43   -290    370       C  
ATOM   1528  CG  LEU B 189       7.677  20.342  30.421  1.00 13.25           C  
ANISOU 1528  CG  LEU B 189     2003   1362   1671    111   -208    393       C  
ATOM   1529  CD1 LEU B 189       8.972  20.112  31.206  1.00 14.98           C  
ANISOU 1529  CD1 LEU B 189     2404   1613   1675    232   -533    247       C  
ATOM   1530  CD2 LEU B 189       6.517  19.665  31.090  1.00 13.58           C  
ANISOU 1530  CD2 LEU B 189     2285   1086   1787    347    201    398       C  
ATOM   1531  N   LEU B 190       6.345  24.349  28.302  1.00 12.18           N  
ANISOU 1531  N   LEU B 190     2258   1412    958     56   -124    447       N  
ATOM   1532  CA  LEU B 190       6.074  25.774  28.182  1.00 11.34           C  
ANISOU 1532  CA  LEU B 190     1939   1296   1074   -289   -285    372       C  
ATOM   1533  C   LEU B 190       4.573  25.992  28.310  1.00 12.38           C  
ANISOU 1533  C   LEU B 190     1994   1400   1311   -117   -185    162       C  
ATOM   1534  O   LEU B 190       4.212  27.008  28.898  1.00 15.11           O  
ANISOU 1534  O   LEU B 190     2375   1678   1690   -288    241   -146       O  
ATOM   1535  CB  LEU B 190       6.601  26.327  26.870  1.00 11.60           C  
ANISOU 1535  CB  LEU B 190     1921   1486    999   -527   -515    423       C  
ATOM   1536  CG  LEU B 190       8.117  26.296  26.673  1.00 11.90           C  
ANISOU 1536  CG  LEU B 190     1924   1675    921   -665   -406    214       C  
ATOM   1537  CD1 LEU B 190       8.484  26.640  25.238  1.00 12.93           C  
ANISOU 1537  CD1 LEU B 190     2124   1853    936    -58   -345    396       C  
ATOM   1538  CD2 LEU B 190       8.821  27.245  27.649  1.00 13.50           C  
ANISOU 1538  CD2 LEU B 190     2149   1729   1253   -733   -492     22       C  
ATOM   1539  N   THR B 191       3.745  25.071  27.790  1.00 11.92           N  
ANISOU 1539  N   THR B 191     1845   1639   1047   -198    -83    164       N  
ATOM   1540  CA  THR B 191       2.315  25.290  27.974  1.00 13.00           C  
ANISOU 1540  CA  THR B 191     1889   1613   1438   -139    -65    317       C  
ATOM   1541  C   THR B 191       1.916  25.167  29.434  1.00 13.33           C  
ANISOU 1541  C   THR B 191     1888   1680   1496     -5    126    274       C  
ATOM   1542  O   THR B 191       1.010  25.853  29.911  1.00 16.83           O  
ANISOU 1542  O   THR B 191     2480   2126   1790    500     59    -21       O  
ATOM   1543  CB  THR B 191       1.497  24.298  27.129  1.00 12.59           C  
ANISOU 1543  CB  THR B 191     1839   1485   1458   -187   -182    544       C  
ATOM   1544  OG1 THR B 191       1.946  22.978  27.409  1.00 14.81           O  
ANISOU 1544  OG1 THR B 191     1999   1514   2113   -108   -717    520       O  
ATOM   1545  CG2 THR B 191       1.718  24.552  25.640  1.00 13.06           C  
ANISOU 1545  CG2 THR B 191     1970   1550   1444   -412     69    309       C  
ATOM   1546  N   GLN B 192       2.562  24.305  30.204  1.00 13.94           N  
ANISOU 1546  N   GLN B 192     2329   1687   1280    168     21     76       N  
ATOM   1547  CA  GLN B 192       2.197  24.176  31.605  1.00 15.02           C  
ANISOU 1547  CA  GLN B 192     2628   1659   1422    -81    277    286       C  
ATOM   1548  C   GLN B 192       2.550  25.391  32.450  1.00 15.22           C  
ANISOU 1548  C   GLN B 192     2842   1733   1206    -23    773    138       C  
ATOM   1549  O   GLN B 192       1.893  25.648  33.461  1.00 21.53           O  
ANISOU 1549  O   GLN B 192     3433   2665   2081    649   1481   -146       O  
ATOM   1550  CB  GLN B 192       2.926  22.994  32.225  1.00 14.55           C  
ANISOU 1550  CB  GLN B 192     2550   1693   1285    -79     44     81       C  
ATOM   1551  CG  GLN B 192       2.418  21.638  31.714  1.00 14.72           C  
ANISOU 1551  CG  GLN B 192     2401   1672   1521   -134   -187    171       C  
ATOM   1552  CD  GLN B 192       2.820  20.510  32.643  1.00 14.72           C  
ANISOU 1552  CD  GLN B 192     2036   1721   1834   -115   -485    197       C  
ATOM   1553  OE1 GLN B 192       3.112  20.729  33.817  1.00 14.16           O  
ANISOU 1553  OE1 GLN B 192     1838   1742   1800   -192   -438    322       O  
ATOM   1554  NE2 GLN B 192       2.836  19.287  32.132  1.00 15.37           N  
ANISOU 1554  NE2 GLN B 192     2221   1761   1857    114     46    184       N  
ATOM   1555  N   ILE B 193       3.593  26.141  32.039  1.00 16.30           N  
ANISOU 1555  N   ILE B 193     2890   1961   1343   -342    424     89       N  
ATOM   1556  CA  ILE B 193       3.929  27.351  32.790  1.00 16.78           C  
ANISOU 1556  CA  ILE B 193     2731   2032   1611    -82    158    -93       C  
ATOM   1557  C   ILE B 193       3.213  28.566  32.206  1.00 17.70           C  
ANISOU 1557  C   ILE B 193     2674   2113   1939    126    239   -226       C  
ATOM   1558  O   ILE B 193       3.352  29.694  32.672  1.00 19.71           O  
ANISOU 1558  O   ILE B 193     3234   2230   2025    472    616   -585       O  
ATOM   1559  CB  ILE B 193       5.448  27.587  32.820  1.00 15.96           C  
ANISOU 1559  CB  ILE B 193     2702   1808   1554     78    230   -312       C  
ATOM   1560  CG1 ILE B 193       6.063  27.905  31.457  1.00 16.88           C  
ANISOU 1560  CG1 ILE B 193     2576   2263   1576   -250    -39     73       C  
ATOM   1561  CG2 ILE B 193       6.166  26.408  33.469  1.00 17.58           C  
ANISOU 1561  CG2 ILE B 193     2780   2036   1865   -384   -290    190       C  
ATOM   1562  CD1 ILE B 193       7.527  28.333  31.522  1.00 18.91           C  
ANISOU 1562  CD1 ILE B 193     2642   2243   2299   -434    330   -839       C  
ATOM   1563  N   GLY B 194       2.413  28.416  31.159  1.00 16.65           N  
ANISOU 1563  N   GLY B 194     2136   2195   1998    154    384      2       N  
ATOM   1564  CA  GLY B 194       1.600  29.483  30.631  1.00 15.55           C  
ANISOU 1564  CA  GLY B 194     1968   2022   1916    247    699   -203       C  
ATOM   1565  C   GLY B 194       2.317  30.396  29.671  1.00 15.95           C  
ANISOU 1565  C   GLY B 194     2071   1859   2132    401    797   -133       C  
ATOM   1566  O   GLY B 194       1.908  31.550  29.566  1.00 17.48           O  
ANISOU 1566  O   GLY B 194     2204   1970   2467    654    737    -10       O  
ATOM   1567  N   ALA B 195       3.354  29.873  29.007  1.00 15.85           N  
ANISOU 1567  N   ALA B 195     2149   1888   1984    544    814     93       N  
ATOM   1568  CA  ALA B 195       4.130  30.723  28.107  1.00 14.56           C  
ANISOU 1568  CA  ALA B 195     1928   1821   1782    296    564   -116       C  
ATOM   1569  C   ALA B 195       3.477  30.899  26.747  1.00 15.19           C  
ANISOU 1569  C   ALA B 195     2286   1688   1798    -24    399   -103       C  
ATOM   1570  O   ALA B 195       2.901  29.983  26.174  1.00 16.09           O  
ANISOU 1570  O   ALA B 195     2752   1539   1821   -217    393     82       O  
ATOM   1571  CB  ALA B 195       5.511  30.139  27.902  1.00 16.55           C  
ANISOU 1571  CB  ALA B 195     2055   1658   2577    398    782    194       C  
ATOM   1572  N   THR B 196       3.588  32.111  26.249  1.00 14.20           N  
ANISOU 1572  N   THR B 196     2203   1601   1590   -218    199   -336       N  
ATOM   1573  CA  THR B 196       3.124  32.489  24.942  1.00 15.19           C  
ANISOU 1573  CA  THR B 196     2073   1910   1790    186    388     -2       C  
ATOM   1574  C   THR B 196       4.203  33.300  24.245  1.00 14.36           C  
ANISOU 1574  C   THR B 196     1773   1952   1730    221    210     -1       C  
ATOM   1575  O   THR B 196       5.013  33.904  24.936  1.00 15.47           O  
ANISOU 1575  O   THR B 196     2044   2084   1750    155     99    -33       O  
ATOM   1576  CB  THR B 196       1.837  33.334  24.991  1.00 16.35           C  
ANISOU 1576  CB  THR B 196     1946   2191   2074    154    515   -122       C  
ATOM   1577  OG1 THR B 196       2.045  34.551  25.706  1.00 17.74           O  
ANISOU 1577  OG1 THR B 196     2627   1957   2156    517    227      1       O  
ATOM   1578  CG2 THR B 196       0.762  32.561  25.751  1.00 21.17           C  
ANISOU 1578  CG2 THR B 196     2369   3492   2183   -611    934   -705       C  
ATOM   1579  N   LEU B 197       4.143  33.266  22.934  1.00 13.93           N  
ANISOU 1579  N   LEU B 197     1771   1821   1702    192    239     -9       N  
ATOM   1580  CA  LEU B 197       4.940  34.184  22.131  1.00 14.87           C  
ANISOU 1580  CA  LEU B 197     2234   1700   1717    -32    340   -172       C  
ATOM   1581  C   LEU B 197       4.153  35.410  21.777  1.00 14.70           C  
ANISOU 1581  C   LEU B 197     2038   1890   1659   -165     58     55       C  
ATOM   1582  O   LEU B 197       2.984  35.246  21.429  1.00 19.46           O  
ANISOU 1582  O   LEU B 197     2262   2440   2690   -492   -431    535       O  
ATOM   1583  CB  LEU B 197       5.348  33.543  20.818  1.00 17.92           C  
ANISOU 1583  CB  LEU B 197     2321   2588   1900   -171    613   -438       C  
ATOM   1584  CG  LEU B 197       6.628  32.756  20.789  1.00 18.93           C  
ANISOU 1584  CG  LEU B 197     2066   3074   2052   -201    481   -940       C  
ATOM   1585  CD1 LEU B 197       6.770  32.011  19.481  1.00 22.88           C  
ANISOU 1585  CD1 LEU B 197     3092   3921   1682    473    623   -789       C  
ATOM   1586  CD2 LEU B 197       7.796  33.720  21.009  1.00 22.38           C  
ANISOU 1586  CD2 LEU B 197     2315   3301   2888   -733   1240   -375       C  
ATOM   1587  N   ASN B 198       4.759  36.590  21.859  1.00 14.25           N  
ANISOU 1587  N   ASN B 198     1887   1741   1786    -19    264    171       N  
ATOM   1588  CA  ASN B 198       3.994  37.802  21.604  1.00 15.93           C  
ANISOU 1588  CA  ASN B 198     2268   2003   1781    264    365    507       C  
ATOM   1589  C   ASN B 198       4.787  38.764  20.731  1.00 16.34           C  
ANISOU 1589  C   ASN B 198     2062   2289   1857    291    358    700       C  
ATOM   1590  O   ASN B 198       5.971  39.006  20.976  1.00 17.45           O  
ANISOU 1590  O   ASN B 198     1935   2332   2362    393    525    155       O  
ATOM   1591  CB  ASN B 198       3.632  38.463  22.926  1.00 16.80           C  
ANISOU 1591  CB  ASN B 198     2377   2023   1983    516    645    487       C  
ATOM   1592  CG  ASN B 198       2.705  37.606  23.749  1.00 18.35           C  
ANISOU 1592  CG  ASN B 198     2463   2194   2314    314    909    256       C  
ATOM   1593  OD1 ASN B 198       1.505  37.809  23.781  1.00 24.67           O  
ANISOU 1593  OD1 ASN B 198     2370   3380   3626    147    895    245       O  
ATOM   1594  ND2 ASN B 198       3.264  36.621  24.427  1.00 20.54           N  
ANISOU 1594  ND2 ASN B 198     3450   1675   2681    803   1909    360       N  
ATOM   1595  N   PHE B 199       4.169  39.331  19.697  1.00 19.67           N  
ANISOU 1595  N   PHE B 199     2632   2848   1993    543    344    990       N  
ATOM   1596  CA  PHE B 199       4.822  40.428  18.985  1.00 22.72           C  
ANISOU 1596  CA  PHE B 199     3354   3078   2200    495    555   1255       C  
ATOM   1597  C   PHE B 199       3.713  41.324  18.421  1.00 26.01           C  
ANISOU 1597  C   PHE B 199     3890   3269   2722    926    685   1526       C  
ATOM   1598  O   PHE B 199       4.027  42.309  17.734  1.00 29.34           O  
ANISOU 1598  O   PHE B 199     4642   3063   3444    930    837   1633       O  
ATOM   1599  CB  PHE B 199       5.774  39.943  17.902  1.00 22.79           C  
ANISOU 1599  CB  PHE B 199     3412   3130   2118    538    605   1446       C  
ATOM   1600  CG  PHE B 199       5.104  39.043  16.877  1.00 24.62           C  
ANISOU 1600  CG  PHE B 199     3680   3236   2439    740    583   1053       C  
ATOM   1601  CD1 PHE B 199       4.894  37.707  17.146  1.00 26.71           C  
ANISOU 1601  CD1 PHE B 199     3898   3430   2822    261    432   1150       C  
ATOM   1602  CD2 PHE B 199       4.692  39.556  15.653  1.00 25.38           C  
ANISOU 1602  CD2 PHE B 199     3849   3211   2582    975    172    794       C  
ATOM   1603  CE1 PHE B 199       4.284  36.886  16.217  1.00 28.40           C  
ANISOU 1603  CE1 PHE B 199     3989   3740   3062   -137    229   1272       C  
ATOM   1604  CE2 PHE B 199       4.079  38.749  14.716  1.00 27.37           C  
ANISOU 1604  CE2 PHE B 199     4036   3415   2949    423     31    927       C  
ATOM   1605  CZ  PHE B 199       3.875  37.404  15.006  1.00 29.21           C  
ANISOU 1605  CZ  PHE B 199     4117   3743   3238   -199    -48   1297       C  
ATOM   1606  OXT PHE B 199       2.509  41.038  18.672  1.00 29.25           O  
ANISOU 1606  OXT PHE B 199     3696   3879   3538   1135    432   2144       O  
TER    1607      PHE B 199                                                      
HETATM 1608 NA    NA A 500      24.166  39.742   1.333  1.00 23.88          NA  
ANISOU 1608 NA    NA A 500     4096   2454   2522   -544    936    401      NA  
HETATM 1609 CL    CL A 502      21.473  38.938  11.843  1.00 19.01          CL  
ANISOU 1609 CL    CL A 502     3162   2187   1875     30    258    -53      CL  
HETATM 1610 CL    CL B 501      15.804   2.159  23.364  1.00 19.75          CL  
ANISOU 1610 CL    CL B 501     3318   2161   2027   -159    305    447      CL  
HETATM 1611  C   ACT B 802       8.607   7.730  34.744  0.50 23.16           C  
ANISOU 1611  C   ACT B 802     3275   2097   3428    752   1183    464       C  
HETATM 1612  O   ACT B 802       9.794   7.438  34.920  0.50 23.57           O  
ANISOU 1612  O   ACT B 802     3267   2646   3043    647    906    377       O  
HETATM 1613  OXT ACT B 802       7.989   8.347  35.616  0.50 26.45           O  
ANISOU 1613  OXT ACT B 802     4209   2108   3734    815   2158    904       O  
HETATM 1614  CH3 ACT B 802       7.890   7.331  33.448  0.50 23.09           C  
ANISOU 1614  CH3 ACT B 802     3104   1857   3812    404    704   1015       C  
HETATM 1615  C2 A065 B 404      20.815  27.584  14.949  0.60 11.36           C  
ANISOU 1615  C2 A065 B 404     1509   1135   1671    179    342    158       C  
HETATM 1616  C2 B065 B 404      12.204  18.096  20.375  0.40 11.15           C  
ANISOU 1616  C2 B065 B 404     1785   1181   1270   -177     67      3       C  
HETATM 1617  O39A065 B 404      21.742  28.579  14.780  0.60 12.09           O  
ANISOU 1617  O39A065 B 404     1565   1180   1849    106    218    251       O  
HETATM 1618  O39B065 B 404      11.149  17.289  20.674  0.40 11.90           O  
ANISOU 1618  O39B065 B 404     1862   1460   1201   -351    -12     35       O  
HETATM 1619  C40A065 B 404      22.923  28.122  15.326  0.60 12.77           C  
ANISOU 1619  C40A065 B 404     1587   1365   1900     42    175    485       C  
HETATM 1620  C40B065 B 404      10.687  16.788  19.481  0.40 12.00           C  
ANISOU 1620  C40B065 B 404     1903   1440   1216   -341    253   -221       C  
HETATM 1621  O41A065 B 404      22.760  26.834  15.770  0.60 12.17           O  
ANISOU 1621  O41A065 B 404     1517   1218   1890    191    354    286       O  
HETATM 1622  O41B065 B 404      11.673  16.936  18.551  0.40 11.63           O  
ANISOU 1622  O41B065 B 404     1784   1203   1431   -268    307   -219       O  
HETATM 1623  C3 A065 B 404      21.438  26.520  15.588  0.60 11.41           C  
ANISOU 1623  C3 A065 B 404     1523   1145   1666    179    321    190       C  
HETATM 1624  C3 B065 B 404      12.530  17.871  19.043  0.40 11.39           C  
ANISOU 1624  C3 B065 B 404     1803   1220   1304   -243    107    -93       C  
HETATM 1625  C4 A065 B 404      20.694  25.393  15.897  0.60 11.20           C  
ANISOU 1625  C4 A065 B 404     1450   1105   1700    285    409    165       C  
HETATM 1626  C4 B065 B 404      13.591  18.532  18.461  0.40 11.26           C  
ANISOU 1626  C4 B065 B 404     1782   1207   1290   -250     81    -56       C  
HETATM 1627  C5 A065 B 404      19.332  25.318  15.598  0.60 10.91           C  
ANISOU 1627  C5 A065 B 404     1515   1052   1580    200    281     64       C  
HETATM 1628  C5 B065 B 404      14.287  19.482  19.197  0.40 10.50           C  
ANISOU 1628  C5 B065 B 404     1595   1171   1224   -129    187   -143       C  
HETATM 1629  C6 A065 B 404      18.727  26.384  14.970  0.60 10.23           C  
ANISOU 1629  C6 A065 B 404     1418    973   1498    301    433    -49       C  
HETATM 1630  C6 B065 B 404      13.966  19.712  20.526  0.40 10.42           C  
ANISOU 1630  C6 B065 B 404     1496   1263   1200    -65    161    -44       C  
HETATM 1631  C7 A065 B 404      19.459  27.516  14.639  0.60 10.29           C  
ANISOU 1631  C7 A065 B 404     1466    982   1462    248    424    -91       C  
HETATM 1632  C7 B065 B 404      12.923  19.012  21.127  0.40 10.21           C  
ANISOU 1632  C7 B065 B 404     1626   1037   1215    -57    144     -3       C  
HETATM 1633  S8 A065 B 404      18.441  23.876  16.041  0.60 10.34           S  
ANISOU 1633  S8 A065 B 404     1849    998   1081      1    151   -140       S  
HETATM 1634  S8 B065 B 404      15.597  20.367  18.438  0.40 10.07           S  
ANISOU 1634  S8 B065 B 404     1564   1091   1172    -69    135    -13       S  
HETATM 1635  O9 A065 B 404      17.327  23.619  15.093  0.60 11.79           O  
ANISOU 1635  O9 A065 B 404     2413    862   1203     49   -192   -409       O  
HETATM 1636  O9 B065 B 404      16.611  20.763  19.457  0.40 11.98           O  
ANISOU 1636  O9 B065 B 404     1752   1381   1418   -310   -141    377       O  
HETATM 1637  O10A065 B 404      19.426  22.751  16.167  0.60 11.64           O  
ANISOU 1637  O10A065 B 404     2349    979   1094    265    148   -226       O  
HETATM 1638  O10B065 B 404      16.159  19.539  17.333  0.40 11.87           O  
ANISOU 1638  O10B065 B 404     1801   1364   1343    385    370    123       O  
HETATM 1639  N11A065 B 404      17.800  24.095  17.537  0.60  9.93           N  
ANISOU 1639  N11A065 B 404     1630   1089   1054    -77     77   -236       N  
HETATM 1640  N11B065 B 404      14.991  21.725  17.778  0.40  9.71           N  
ANISOU 1640  N11B065 B 404     1578   1030   1083    -27     -8   -207       N  
HETATM 1641  C12A065 B 404      18.745  24.482  18.568  0.60 10.23           C  
ANISOU 1641  C12A065 B 404     1679   1094   1113   -169     62   -169       C  
HETATM 1642  C12B065 B 404      13.821  21.438  16.952  0.40 10.43           C  
ANISOU 1642  C12B065 B 404     1704   1051   1208    -65   -104   -241       C  
HETATM 1643  C13A065 B 404      18.420  23.863  19.931  0.60  9.27           C  
ANISOU 1643  C13A065 B 404     1505    938   1078   -248    -41   -233       C  
HETATM 1644  C13B065 B 404      13.850  22.391  15.755  0.40 10.32           C  
ANISOU 1644  C13B065 B 404     1650   1015   1257    152   -127   -201       C  
HETATM 1645  C14A065 B 404      18.337  22.348  19.861  0.60  9.94           C  
ANISOU 1645  C14A065 B 404     1475    988   1313   -223   -164   -123       C  
HETATM 1646  C14B065 B 404      15.031  22.047  14.857  0.40 11.95           C  
ANISOU 1646  C14B065 B 404     1876   1342   1322    559     18    196       C  
HETATM 1647  C15A065 B 404      19.483  24.259  20.966  0.60 10.10           C  
ANISOU 1647  C15A065 B 404     1533    959   1346   -231   -261    -71       C  
HETATM 1648  C15B065 B 404      12.486  22.323  15.092  0.40 10.82           C  
ANISOU 1648  C15B065 B 404     1719    716   1676     16   -283   -158       C  
HETATM 1649  C16A065 B 404      16.561  24.869  17.534  0.60  9.64           C  
ANISOU 1649  C16A065 B 404     1715    888   1060    -91     40   -272       C  
HETATM 1650  C16B065 B 404      14.737  22.755  18.790  0.40  9.81           C  
ANISOU 1650  C16B065 B 404     1535   1110   1081   -122     95   -250       C  
HETATM 1651  C17A065 B 404      15.415  23.993  18.042  0.60  9.77           C  
ANISOU 1651  C17A065 B 404     1647   1030   1036    -74     89   -213       C  
HETATM 1652  C17B065 B 404      15.528  23.999  18.397  0.40  9.43           C  
ANISOU 1652  C17B065 B 404     1533   1051   1000    -64     23   -189       C  
HETATM 1653  O18A065 B 404      14.242  24.749  18.323  0.60 10.93           O  
ANISOU 1653  O18A065 B 404     1692   1393   1069    -45     16   -657       O  
HETATM 1654  O18B065 B 404      15.019  25.152  19.042  0.40 10.04           O  
ANISOU 1654  O18B065 B 404     1396   1124   1294    -60   -225   -401       O  
HETATM 1655  C19A065 B 404      15.105  22.831  17.099  0.60  8.98           C  
ANISOU 1655  C19A065 B 404     1471    943    997    -40     30   -165       C  
HETATM 1656  C19B065 B 404      17.019  23.812  18.629  0.40  9.09           C  
ANISOU 1656  C19B065 B 404     1537    894   1024    -86      1   -264       C  
HETATM 1657  N20A065 B 404      14.216  21.920  17.820  0.60  9.40           N  
ANISOU 1657  N20A065 B 404     1542    974   1056    -17    156   -211       N  
HETATM 1658  N20B065 B 404      17.756  24.895  17.995  0.40  9.08           N  
ANISOU 1658  N20B065 B 404     1519    890   1043    -25     32   -230       N  
HETATM 1659  C21A065 B 404      14.461  20.674  18.187  0.60  9.62           C  
ANISOU 1659  C21A065 B 404     1597   1040   1017     -2    103    -77       C  
HETATM 1660  C21B065 B 404      18.523  24.816  16.909  0.40  9.70           C  
ANISOU 1660  C21B065 B 404     1581    988   1117     45    114   -166       C  
HETATM 1661  O22A065 B 404      15.512  20.092  17.921  0.60 11.63           O  
ANISOU 1661  O22A065 B 404     1740   1154   1527    175    307    245       O  
HETATM 1662  O22B065 B 404      18.758  23.778  16.280  0.40 10.86           O  
ANISOU 1662  O22B065 B 404     1792   1147   1189   -519    400   -453       O  
HETATM 1663  O23A065 B 404      13.437  20.099  18.873  0.60 10.52           O  
ANISOU 1663  O23A065 B 404     1665   1102   1231   -117    146    -91       O  
HETATM 1664  O23B065 B 404      19.063  25.989  16.516  0.40 10.34           O  
ANISOU 1664  O23B065 B 404     1541    853   1534    345    432    -61       O  
HETATM 1665  C24A065 B 404      13.583  18.699  19.076  0.60 11.17           C  
ANISOU 1665  C24A065 B 404     1798   1120   1327   -182     97    -44       C  
HETATM 1666  C24B065 B 404      20.132  25.925  15.579  0.40 11.30           C  
ANISOU 1666  C24B065 B 404     1539   1163   1592    356    440     97       C  
HETATM 1667  C25A065 B 404      13.000  18.380  20.456  0.60 11.00           C  
ANISOU 1667  C25A065 B 404     1774   1073   1335   -143     88    -42       C  
HETATM 1668  C25B065 B 404      20.041  27.174  14.699  0.40 10.91           C  
ANISOU 1668  C25B065 B 404     1487   1072   1585    266    367     43       C  
HETATM 1669  O26A065 B 404      11.579  18.501  20.259  0.60 10.94           O  
ANISOU 1669  O26A065 B 404     1778   1183   1197   -134     27    -83       O  
HETATM 1670  O26B065 B 404      20.557  28.223  15.536  0.40 11.63           O  
ANISOU 1670  O26B065 B 404     1582   1179   1660    342    145     -8       O  
HETATM 1671  C27A065 B 404      11.292  18.012  18.955  0.60 11.58           C  
ANISOU 1671  C27A065 B 404     1828   1420   1152   -319    212   -139       C  
HETATM 1672  C27B065 B 404      21.604  27.681  16.339  0.40 11.75           C  
ANISOU 1672  C27B065 B 404     1597   1218   1649    372    221    125       C  
HETATM 1673  O28A065 B 404      10.405  18.888  18.263  0.60 12.54           O  
ANISOU 1673  O28A065 B 404     1827   2088    852   -101    233   -109       O  
HETATM 1674  O28B065 B 404      21.423  28.005  17.716  0.40 12.89           O  
ANISOU 1674  O28B065 B 404     1834   1458   1605    199    153    118       O  
HETATM 1675  C29A065 B 404      11.164  19.619  17.319  0.60 12.50           C  
ANISOU 1675  C29A065 B 404     1677   1881   1192   -136     82     84       C  
HETATM 1676  C29B065 B 404      21.965  26.916  18.484  0.40 14.23           C  
ANISOU 1676  C29B065 B 404     2166   1541   1700    174    146    257       C  
HETATM 1677  C30A065 B 404      12.251  18.625  16.870  0.60 12.22           C  
ANISOU 1677  C30A065 B 404     1698   1754   1192   -300    264    -65       C  
HETATM 1678  C30B065 B 404      21.611  25.671  17.673  0.40 13.83           C  
ANISOU 1678  C30B065 B 404     2100   1449   1707    139    187    327       C  
HETATM 1679  C31A065 B 404      12.599  17.937  18.186  0.60 11.38           C  
ANISOU 1679  C31A065 B 404     1789   1222   1313   -310    205    -87       C  
HETATM 1680  C31B065 B 404      21.488  26.173  16.237  0.40 11.70           C  
ANISOU 1680  C31B065 B 404     1569   1208   1670    237    377    258       C  
HETATM 1681  C32A065 B 404      14.399  23.265  15.821  0.60 10.19           C  
ANISOU 1681  C32A065 B 404     1692   1023   1155     11   -135    -73       C  
HETATM 1682  C32B065 B 404      17.362  23.674  20.110  0.40  8.27           C  
ANISOU 1682  C32B065 B 404     1473    648   1022   -202    -13   -333       C  
HETATM 1683  C33A065 B 404      12.691  21.703  14.775  0.60  9.47           C  
ANISOU 1683  C33A065 B 404     1648    954    996    188    -93   -261       C  
HETATM 1684  C33B065 B 404      19.583  24.581  20.845  0.40  9.06           C  
ANISOU 1684  C33B065 B 404     1477    712   1252   -170   -164   -263       C  
HETATM 1685  C34A065 B 404      12.337  20.589  14.015  0.60  9.75           C  
ANISOU 1685  C34A065 B 404     1822   1100    783    143    -54   -297       C  
HETATM 1686  C34B065 B 404      20.957  24.472  21.005  0.40  9.22           C  
ANISOU 1686  C34B065 B 404     1509    503   1490   -110   -225   -309       C  
HETATM 1687  C35A065 B 404      13.309  19.842  13.361  0.60 10.96           C  
ANISOU 1687  C35A065 B 404     1770   1748    647    305   -257   -617       C  
HETATM 1688  C35B065 B 404      21.611  23.335  20.572  0.40  9.36           C  
ANISOU 1688  C35B065 B 404     1478    473   1605   -180   -472   -516       C  
HETATM 1689  C36A065 B 404      14.638  20.232  13.514  0.60 12.15           C  
ANISOU 1689  C36A065 B 404     1756   1857   1005    318   -319   -553       C  
HETATM 1690  C36B065 B 404      20.891  22.278  20.025  0.40  9.49           C  
ANISOU 1690  C36B065 B 404     1312    798   1497   -310   -340   -631       C  
HETATM 1691  C37A065 B 404      14.988  21.323  14.293  0.60 10.76           C  
ANISOU 1691  C37A065 B 404     1574   1665    850    364   -426   -340       C  
HETATM 1692  C37B065 B 404      19.515  22.377  19.866  0.40  9.15           C  
ANISOU 1692  C37B065 B 404     1314    846   1318   -228   -284   -419       C  
HETATM 1693  C38A065 B 404      14.014  22.073  14.947  0.60  9.87           C  
ANISOU 1693  C38A065 B 404     1619   1021   1109    281   -306    -89       C  
HETATM 1694  C38B065 B 404      18.871  23.534  20.277  0.40  8.88           C  
ANISOU 1694  C38B065 B 404     1477    755   1140   -228    -59   -277       C  
HETATM 1695  O   HOH A 503      13.068  40.128  21.574  1.00 12.28           O  
ANISOU 1695  O   HOH A 503     1802   1348   1515    101    -41   -245       O  
HETATM 1696  O   HOH A 504      16.562  21.659   1.812  1.00 13.71           O  
ANISOU 1696  O   HOH A 504     2369   1550   1289   -290     56    103       O  
HETATM 1697  O   HOH A 505      18.256  30.728  21.663  1.00 13.19           O  
ANISOU 1697  O   HOH A 505     2011   1491   1510     77   -108    326       O  
HETATM 1698  O   HOH A 506      19.107  39.889  17.371  1.00 15.44           O  
ANISOU 1698  O   HOH A 506     2905   1473   1491    190    468    197       O  
HETATM 1699  O   HOH A 507      20.696  33.580  10.833  1.00 14.07           O  
ANISOU 1699  O   HOH A 507     1521   2045   1781    215    388    685       O  
HETATM 1700  O   HOH A 508      15.275  44.609  11.037  1.00 15.23           O  
ANISOU 1700  O   HOH A 508     2413   1785   1589    262    318    -26       O  
HETATM 1701  O   HOH A 509      12.689  42.613  20.508  1.00 14.29           O  
ANISOU 1701  O   HOH A 509     2120   1851   1460    307    233    121       O  
HETATM 1702  O   HOH A 510      25.712  38.302   2.159  1.00 21.11           O  
ANISOU 1702  O   HOH A 510     3024   2074   2922    738    628   1507       O  
HETATM 1703  O   HOH A 511      28.057  35.813   4.386  1.00 22.24           O  
ANISOU 1703  O   HOH A 511     2742   3258   2450    -38    439   -211       O  
HETATM 1704  O   HOH A 512      14.853  28.915  -5.198  1.00 19.98           O  
ANISOU 1704  O   HOH A 512     3106   2388   2098    725   -221    497       O  
HETATM 1705  O   HOH A 513      25.217  19.039   5.787  1.00 17.62           O  
ANISOU 1705  O   HOH A 513     2955   2119   1622   -610    484   -497       O  
HETATM 1706  O   HOH A 514      20.023  28.665  21.333  1.00 20.75           O  
ANISOU 1706  O   HOH A 514     3218   2467   2200    109   1035    255       O  
HETATM 1707  O   HOH A 515      23.769  37.724   0.280  1.00 21.83           O  
ANISOU 1707  O   HOH A 515     3572   2120   2603    263    243    397       O  
HETATM 1708  O   HOH A 516      23.087  40.265   8.042  1.00 20.74           O  
ANISOU 1708  O   HOH A 516     3296   2927   1657   -826   -339     -7       O  
HETATM 1709  O   HOH A 517       1.442  34.061   9.379  1.00 24.69           O  
ANISOU 1709  O   HOH A 517     2674   4497   2209   1015   -139    729       O  
HETATM 1710  O   HOH A 518       8.989  24.326   7.574  1.00 25.75           O  
ANISOU 1710  O   HOH A 518     3963   3974   1845  -1707   -863    500       O  
HETATM 1711  O   HOH A 519      14.283  38.336   0.572  1.00 20.98           O  
ANISOU 1711  O   HOH A 519     4023   2263   1686   -284   -248     18       O  
HETATM 1712  O   HOH A 520       1.825  21.107  16.021  1.00 22.99           O  
ANISOU 1712  O   HOH A 520     2388   3214   3135  -1077    193  -1219       O  
HETATM 1713  O   HOH A 521       7.230  26.119   3.253  1.00 22.29           O  
ANISOU 1713  O   HOH A 521     3945   2480   2044    514    -81   -418       O  
HETATM 1714  O   HOH A 522      22.213  41.187   0.700  1.00 25.03           O  
ANISOU 1714  O   HOH A 522     4564   2419   2529    957    474   1341       O  
HETATM 1715  O   HOH A 523       6.436  41.397  22.587  1.00 22.83           O  
ANISOU 1715  O   HOH A 523     3519   2139   3018    427    268    376       O  
HETATM 1716  O   HOH A 524       0.435  28.813  15.951  1.00 26.07           O  
ANISOU 1716  O   HOH A 524     3332   3904   2669    550   -453   -200       O  
HETATM 1717  O   HOH A 525      26.063  25.813  16.067  0.60 19.44           O  
ANISOU 1717  O   HOH A 525     4097   1924   1365   -293   -700   -937       O  
HETATM 1718  O   HOH A 526      15.521  20.607   4.055  1.00 24.97           O  
ANISOU 1718  O   HOH A 526     3786   3497   2206     37    401  -1013       O  
HETATM 1719  O   HOH A 527      21.467  45.811   7.975  1.00 38.58           O  
ANISOU 1719  O   HOH A 527     4113   5438   5107  -1099    844   -777       O  
HETATM 1720  O   HOH A 528       5.664  31.640  -3.148  1.00 31.70           O  
ANISOU 1720  O   HOH A 528     4333   5632   2079  -1441   -595   -226       O  
HETATM 1721  O   HOH A 529      23.697  34.527  -4.594  1.00 27.11           O  
ANISOU 1721  O   HOH A 529     3943   3343   3014   -282    985    406       O  
HETATM 1722  O   HOH A 530      25.506  41.478   2.149  1.00 29.44           O  
ANISOU 1722  O   HOH A 530     3461   3091   4634  -1065    535    239       O  
HETATM 1723  O   HOH A 531      12.748  45.388  11.823  1.00 23.55           O  
ANISOU 1723  O   HOH A 531     3230   3150   2567   -264    -53   1102       O  
HETATM 1724  O   HOH A 532      25.737  40.267  -0.663  1.00 25.81           O  
ANISOU 1724  O   HOH A 532     3742   2562   3502    299    258    189       O  
HETATM 1725  O   HOH A 533      19.467  37.691  18.933  1.00 26.65           O  
ANISOU 1725  O   HOH A 533     4190   3637   2298    394   -196   -434       O  
HETATM 1726  O   HOH A 534      20.884  35.501  17.623  1.00 24.88           O  
ANISOU 1726  O   HOH A 534     3736   2554   3162   -870  -1129    679       O  
HETATM 1727  O   HOH A 535      10.744  38.653  -0.610  1.00 25.35           O  
ANISOU 1727  O   HOH A 535     3922   2843   2866    986    443     81       O  
HETATM 1728  O   HOH A 536      16.707  38.294  -0.953  1.00 25.89           O  
ANISOU 1728  O   HOH A 536     3957   3285   2596    582    276    276       O  
HETATM 1729  O   HOH A 537       1.590  27.873  18.216  1.00 30.89           O  
ANISOU 1729  O   HOH A 537     4277   3807   3653   -146   1028    625       O  
HETATM 1730  O   HOH A 538       1.012  24.624  13.960  1.00 27.74           O  
ANISOU 1730  O   HOH A 538     3303   4466   2769   -787   -626    263       O  
HETATM 1731  O   HOH A 539      -1.415  27.056  20.036  1.00 27.33           O  
ANISOU 1731  O   HOH A 539     3061   4013   3309   -560   -967     96       O  
HETATM 1732  O   HOH A 540      25.362  33.989  11.515  1.00 40.66           O  
ANISOU 1732  O   HOH A 540     6001   5526   3922    -27    380   2218       O  
HETATM 1733  O   HOH A 541       4.466  21.028  11.472  1.00 27.08           O  
ANISOU 1733  O   HOH A 541     3814   3808   2669   -586   -119   -118       O  
HETATM 1734  O   HOH A 542      23.166  37.566  -6.788  1.00 37.85           O  
ANISOU 1734  O   HOH A 542     4633   5250   4498    570    944   1572       O  
HETATM 1735  O   HOH A 543      22.730  14.986  19.494  0.63 22.79           O  
ANISOU 1735  O   HOH A 543     4008   1898   2753     67    465    985       O  
HETATM 1736  O   HOH A 544      22.550  34.659  12.610  1.00 32.04           O  
ANISOU 1736  O   HOH A 544     4377   3763   4036   -327  -1401   1642       O  
HETATM 1737  O   HOH A 545       0.529  28.007  13.536  1.00 39.86           O  
ANISOU 1737  O   HOH A 545     3600   6311   5236    457   1167   1440       O  
HETATM 1738  O   HOH A 546       8.980  23.484   4.835  1.00 36.77           O  
ANISOU 1738  O   HOH A 546     4803   4101   5068  -2204   -425   -706       O  
HETATM 1739  O   HOH A 547      23.239  25.131   1.360  1.00 29.93           O  
ANISOU 1739  O   HOH A 547     4074   4447   2851   -828    213   -723       O  
HETATM 1740  O   HOH A 548      18.528  45.918   1.815  1.00 35.85           O  
ANISOU 1740  O   HOH A 548     5338   3791   4493    535   1381   1137       O  
HETATM 1741  O   HOH A 549       8.952  46.181  18.457  1.00 38.40           O  
ANISOU 1741  O   HOH A 549     5786   3190   5616    231   1519    829       O  
HETATM 1742  O   HOH A 550      -3.708  33.398  21.476  1.00 28.90           O  
ANISOU 1742  O   HOH A 550     2460   4860   3660  -1130  -1016   1185       O  
HETATM 1743  O   HOH A 551      25.710  30.983  15.163  1.00 34.24           O  
ANISOU 1743  O   HOH A 551     4087   5851   3070   -262   -399    482       O  
HETATM 1744  O   HOH A 552      29.095  38.130   7.631  1.00 33.88           O  
ANISOU 1744  O   HOH A 552     5060   3524   4287   -190  -1143    100       O  
HETATM 1745  O   HOH A 553       6.759  45.633   8.082  0.50 24.72           O  
ANISOU 1745  O   HOH A 553     2459   2763   4170    940    959    696       O  
HETATM 1746  O   HOH A 554       6.727  22.089  11.485  1.00 30.44           O  
ANISOU 1746  O   HOH A 554     4903   3198   3466   1399   1133    933       O  
HETATM 1747  O   HOH A 555      17.743  47.717   4.187  1.00 38.80           O  
ANISOU 1747  O   HOH A 555     6104   2967   5669   1006    859    648       O  
HETATM 1748  O   HOH A 556      33.464  30.496   6.189  1.00 34.42           O  
ANISOU 1748  O   HOH A 556     3414   5833   3831  -1010   -121   -950       O  
HETATM 1749  O   HOH A 557      23.967  31.985  -4.005  1.00 37.56           O  
ANISOU 1749  O   HOH A 557     5080   4643   4549   -339   1421   -560       O  
HETATM 1750  O   HOH A 558       7.353  22.947   8.707  0.44 18.21           O  
ANISOU 1750  O   HOH A 558     2294   2681   1942   -722   -637    310       O  
HETATM 1751  O   HOH A 559      -3.701  33.591  23.964  1.00 38.07           O  
ANISOU 1751  O   HOH A 559     4586   4440   5440    -13    574    604       O  
HETATM 1752  O   HOH A 560      35.073  30.927   4.300  1.00 37.47           O  
ANISOU 1752  O   HOH A 560     3702   5767   4768   -622    951    895       O  
HETATM 1753  O   HOH A 561      28.143  25.899   2.466  1.00 31.18           O  
ANISOU 1753  O   HOH A 561     3809   5180   2858    -31    125  -1143       O  
HETATM 1754  O   HOH A 562      30.451  29.982  12.688  1.00 40.33           O  
ANISOU 1754  O   HOH A 562     4904   6418   4001   2305  -1406  -1638       O  
HETATM 1755  O   HOH A 563      12.045  22.118   5.223  0.50 27.07           O  
ANISOU 1755  O   HOH A 563     3562   2961   3762   -590    627   -196       O  
HETATM 1756  O   HOH A 564      -3.844  28.223  14.255  1.00 38.95           O  
ANISOU 1756  O   HOH A 564     4852   4862   5086   2185   1372    158       O  
HETATM 1757  O   HOH A 565       8.782  28.367  -1.204  0.50 21.55           O  
ANISOU 1757  O   HOH A 565     3436   3929    822   -253   -176     -5       O  
HETATM 1758  O   HOH A 566      23.216  41.054  11.916  0.50 26.25           O  
ANISOU 1758  O   HOH A 566     3825   2223   3926   -246    180    -99       O  
HETATM 1759  O   HOH A 567      31.819  38.172   5.206  1.00 40.19           O  
ANISOU 1759  O   HOH A 567     5117   3581   6573   -960   -819    224       O  
HETATM 1760  O   HOH A 568       8.620  43.950  21.988  0.50 33.26           O  
ANISOU 1760  O   HOH A 568     4397   3703   4536   1301    901    199       O  
HETATM 1761  O   HOH A 569      25.469  24.248   1.118  1.00 42.45           O  
ANISOU 1761  O   HOH A 569     5855   4659   5615    678    110  -1771       O  
HETATM 1762  O   HOH A 570       4.414  39.084  30.301  1.00 39.93           O  
ANISOU 1762  O   HOH A 570     6030   4994   4147    419  -1231  -1336       O  
HETATM 1763  O   HOH A 571      18.359  34.526  -6.060  0.56 26.28           O  
ANISOU 1763  O   HOH A 571     4884   2961   2142    477   -324    195       O  
HETATM 1764  O   HOH A 572       2.140  21.738  13.300  1.00 39.47           O  
ANISOU 1764  O   HOH A 572     4784   4453   5761  -1800   -139   -415       O  
HETATM 1765  O   HOH A 573      19.101  43.430   1.687  0.50 29.65           O  
ANISOU 1765  O   HOH A 573     5216   3880   2167   1771   1630    603       O  
HETATM 1766  O   HOH A 574      16.826  41.142   0.695  1.00 37.23           O  
ANISOU 1766  O   HOH A 574     4710   5716   3721    328  -1283   2143       O  
HETATM 1767  O   HOH A 575       9.347  45.677  15.797  0.50 20.96           O  
ANISOU 1767  O   HOH A 575     3005   2013   2945    708   -139   -517       O  
HETATM 1768  O   HOH A 576      23.069  24.047  -3.129  1.00 39.02           O  
ANISOU 1768  O   HOH A 576     4847   5106   4872    361  -1313    -59       O  
HETATM 1769  O   HOH A 577       1.902  30.621  14.851  1.00 29.41           O  
ANISOU 1769  O   HOH A 577     4725   4297   2152    500   -115    136       O  
HETATM 1770  O   HOH A 578      27.945  16.356  13.272  1.00 34.69           O  
ANISOU 1770  O   HOH A 578     4131   3196   5854    831   1772    531       O  
HETATM 1771  O   HOH A 579      25.186  30.407  17.321  1.00 33.41           O  
ANISOU 1771  O   HOH A 579     3186   6388   3120    734   1491    733       O  
HETATM 1772  O   HOH A 580      28.065  41.818   0.234  1.00 36.92           O  
ANISOU 1772  O   HOH A 580     5844   5296   2889    -84   -505   -379       O  
HETATM 1773  O   HOH A 581      10.877  39.546   1.494  1.00 35.59           O  
ANISOU 1773  O   HOH A 581     4669   4210   4644   -808   -885   1544       O  
HETATM 1774  O   HOH A 582      22.213  12.206  13.836  0.50 32.31           O  
ANISOU 1774  O   HOH A 582     4121   3406   4749   1260  -1980    692       O  
HETATM 1775  O   HOH A 583      22.005  41.420  -3.710  1.00 39.73           O  
ANISOU 1775  O   HOH A 583     5699   2968   6430   -540    351    198       O  
HETATM 1776  O   HOH A 584      24.424  13.328  19.042  1.00 39.02           O  
ANISOU 1776  O   HOH A 584     4911   5473   4441    840   -470    426       O  
HETATM 1777  O   HOH A 585      27.619  17.358   9.061  0.50 34.02           O  
ANISOU 1777  O   HOH A 585     5043   3870   4013    626   2130  -1027       O  
HETATM 1778  O   HOH A 586      -2.636  30.860  19.529  1.00 45.01           O  
ANISOU 1778  O   HOH A 586     5466   4970   6666   -418   -393    790       O  
HETATM 1779  O   HOH A 587       3.400  29.296   3.180  0.56 33.62           O  
ANISOU 1779  O   HOH A 587     4318   4146   4309    870  -1265   1031       O  
HETATM 1780  O   HOH A 588      20.971  21.190   1.203  1.00 37.93           O  
ANISOU 1780  O   HOH A 588     5345   5911   3158   -216  -1337    867       O  
HETATM 1781  O   HOH A 589      24.766  21.575   2.956  0.50 25.00           O  
ANISOU 1781  O   HOH A 589     2073   4605   2822   -615    168  -1335       O  
HETATM 1782  O   HOH A 590      21.745  31.371  -4.391  0.50 26.59           O  
ANISOU 1782  O   HOH A 590     2924   4093   3086    365    251   1259       O  
HETATM 1783  O   HOH A 591      20.136  17.282   6.711  1.00 39.12           O  
ANISOU 1783  O   HOH A 591     6050   5048   3767  -1833    965   -159       O  
HETATM 1784  O   HOH A 592      21.936  28.928  -5.601  1.00 42.29           O  
ANISOU 1784  O   HOH A 592     5825   6005   4239   -441     88   -201       O  
HETATM 1785  O   HOH A 593       3.604  42.268  22.554  1.00 42.50           O  
ANISOU 1785  O   HOH A 593     5566   5282   5299   1181   1174   -277       O  
HETATM 1786  O   HOH A 594      23.612  35.242  -7.070  0.50 34.72           O  
ANISOU 1786  O   HOH A 594     4609   4452   4131   1153    391    528       O  
HETATM 1787  O   HOH A 595      23.035  36.832  13.189  0.50 20.84           O  
ANISOU 1787  O   HOH A 595     2791   2707   2420   -383   -332    359       O  
HETATM 1788  O   HOH A 596      11.468  17.370   7.485  0.50 28.75           O  
ANISOU 1788  O   HOH A 596     3239   2876   4810   -914   -781  -2436       O  
HETATM 1789  O   HOH A 597      27.299  30.561  -5.663  1.00 42.63           O  
ANISOU 1789  O   HOH A 597     6780   5639   3780   -657   -435   -830       O  
HETATM 1790  O   HOH A 598       0.942  36.090   7.765  1.00 40.93           O  
ANISOU 1790  O   HOH A 598     5124   5801   4627    847      0   1387       O  
HETATM 1791  O   HOH A 599       9.269  20.690   7.632  0.50 24.05           O  
ANISOU 1791  O   HOH A 599     2835   3001   3300   -555   -255  -1022       O  
HETATM 1792  O   HOH A 600      29.877  36.790   2.879  1.00 39.86           O  
ANISOU 1792  O   HOH A 600     4509   5148   5488   -145    523    153       O  
HETATM 1793  O   HOH A 601      33.247  24.576   2.633  1.00 35.28           O  
ANISOU 1793  O   HOH A 601     4535   4157   4713    451    646  -1232       O  
HETATM 1794  O   HOH A 602      25.458  37.575  11.137  1.00 40.37           O  
ANISOU 1794  O   HOH A 602     4737   6916   3688     45   -446  -1046       O  
HETATM 1795  O   HOH A 603      28.311  33.494  11.157  0.50 22.64           O  
ANISOU 1795  O   HOH A 603     3764   3155   1683   -419  -1027    241       O  
HETATM 1796  O   HOH A 604       1.427  38.319  27.476  0.50 27.93           O  
ANISOU 1796  O   HOH A 604     3289   3428   3897    381     68    453       O  
HETATM 1797  O   HOH A 605      24.552  42.094  -2.582  0.50 25.40           O  
ANISOU 1797  O   HOH A 605     4122   2410   3121    295    279    993       O  
HETATM 1798  O   HOH A 606      23.201  19.271   1.675  0.50 28.58           O  
ANISOU 1798  O   HOH A 606     3901   4240   2720   1018   1514   -712       O  
HETATM 1799  O   HOH A 607      -2.659  34.134  17.783  0.50 26.81           O  
ANISOU 1799  O   HOH A 607     3481   3818   2887   -235   -934   -402       O  
HETATM 1800  O   HOH A 608      24.703  33.739  16.060  1.00 41.39           O  
ANISOU 1800  O   HOH A 608     3891   5993   5841  -1042   -258   1017       O  
HETATM 1801  O   HOH A 609      11.297  34.087  -6.546  0.50 31.50           O  
ANISOU 1801  O   HOH A 609     4018   4327   3622    334   -682   -151       O  
HETATM 1802  O   HOH A 610      22.581  36.109  20.882  0.50 27.80           O  
ANISOU 1802  O   HOH A 610     2901   2702   4958   -853   1894  -1646       O  
HETATM 1803  O   HOH A 611      15.664  34.635  -4.346  0.50 26.80           O  
ANISOU 1803  O   HOH A 611     3806   4003   2375   1766  -1253    -60       O  
HETATM 1804  O   HOH A 612       8.969  21.446  13.883  0.40 11.11           O  
ANISOU 1804  O   HOH A 612     1534   1874    815   -791   -446   -701       O  
HETATM 1805  O   HOH A 613      -3.669  37.063  19.505  0.50 29.90           O  
ANISOU 1805  O   HOH A 613     2346   4110   4903    297  -1028    559       O  
HETATM 1806  O   HOH A 614      28.136  39.455   3.564  1.00 39.29           O  
ANISOU 1806  O   HOH A 614     4793   4180   5953  -1494     11   1620       O  
HETATM 1807  O   HOH A 615       4.676  37.467   5.689  0.50 21.87           O  
ANISOU 1807  O   HOH A 615     2051   2637   3623    888    291    787       O  
HETATM 1808  O   HOH A 616      30.010  34.072  -2.570  1.00 40.04           O  
ANISOU 1808  O   HOH A 616     6675   5963   2574  -1636    949   1276       O  
HETATM 1809  O   HOH B 803       4.183  16.450  29.144  1.00  9.52           O  
ANISOU 1809  O   HOH B 803     1609   1029    977   -213     81    377       O  
HETATM 1810  O   HOH B 804       7.459  23.823  18.193  1.00 12.25           O  
ANISOU 1810  O   HOH B 804     1818   1598   1239   -320   -257     16       O  
HETATM 1811  O   HOH B 805       9.332  16.087  26.670  1.00 14.35           O  
ANISOU 1811  O   HOH B 805     2332   1457   1664   -300    234     55       O  
HETATM 1812  O   HOH B 806       8.778  22.032  16.650  1.00 15.22           O  
ANISOU 1812  O   HOH B 806     2308   1810   1666   -145    -75    132       O  
HETATM 1813  O   HOH B 807      17.421  39.521  25.881  1.00 13.34           O  
ANISOU 1813  O   HOH B 807     2198   1586   1286   -235     59   -237       O  
HETATM 1814  O   HOH B 808      23.177  34.494  24.296  1.00 19.17           O  
ANISOU 1814  O   HOH B 808     1782   1946   3555    -74   -462   -119       O  
HETATM 1815  O   HOH B 809       1.665  15.320  34.923  1.00 15.75           O  
ANISOU 1815  O   HOH B 809     1705   2140   2138    108    404   -253       O  
HETATM 1816  O   HOH B 810      15.328  31.411  36.050  1.00 17.53           O  
ANISOU 1816  O   HOH B 810     3466   1736   1460    221   -268   -620       O  
HETATM 1817  O   HOH B 811      18.164  20.645  16.546  1.00 17.07           O  
ANISOU 1817  O   HOH B 811     2076   2209   2203    517    -79  -1545       O  
HETATM 1818  O   HOH B 812       2.426  18.672  29.247  1.00 18.82           O  
ANISOU 1818  O   HOH B 812     2661   2509   1979   -727    251   -213       O  
HETATM 1819  O   HOH B 813       4.095  13.128  31.414  1.00 17.86           O  
ANISOU 1819  O   HOH B 813     2748   2299   1738   -167   -353    608       O  
HETATM 1820  O   HOH B 814      16.531  35.974  26.295  1.00 17.20           O  
ANISOU 1820  O   HOH B 814     2579   2252   1704    435    331    579       O  
HETATM 1821  O   HOH B 815      16.256   5.040  34.460  1.00 20.04           O  
ANISOU 1821  O   HOH B 815     3495   1920   2200    -53   -460    576       O  
HETATM 1822  O   HOH B 816      23.206  23.057  33.744  1.00 18.43           O  
ANISOU 1822  O   HOH B 816     2361   2383   2258    658    574    -25       O  
HETATM 1823  O   HOH B 817       0.832  28.379  25.399  1.00 22.86           O  
ANISOU 1823  O   HOH B 817     3223   2380   3084    -70    873   -752       O  
HETATM 1824  O   HOH B 818      15.824  15.560  11.804  1.00 20.73           O  
ANISOU 1824  O   HOH B 818     3569   1891   2418   -375   -114     15       O  
HETATM 1825  O   HOH B 819      14.689   5.090  36.608  1.00 21.24           O  
ANISOU 1825  O   HOH B 819     2936   2295   2841    126   -486   -139       O  
HETATM 1826  O   HOH B 820      11.006  14.883  16.507  1.00 19.14           O  
ANISOU 1826  O   HOH B 820     3700   1407   2166    159    184   -391       O  
HETATM 1827  O   HOH B 821      12.196  16.081  39.950  1.00 21.58           O  
ANISOU 1827  O   HOH B 821     2889   2218   3092    434   -361    317       O  
HETATM 1828  O   HOH B 822      16.896  35.961  29.001  1.00 21.49           O  
ANISOU 1828  O   HOH B 822     3702   2451   2011    480   -520   -816       O  
HETATM 1829  O   HOH B 823      18.446  19.955  46.687  1.00 22.86           O  
ANISOU 1829  O   HOH B 823     3512   2690   2484    110    628    431       O  
HETATM 1830  O   HOH B 824      14.210   4.990  20.105  1.00 22.48           O  
ANISOU 1830  O   HOH B 824     4215   2158   2169   -433   -187    686       O  
HETATM 1831  O   HOH B 825      15.161   5.372  22.829  1.00 20.69           O  
ANISOU 1831  O   HOH B 825     3312   2179   2370     38    818   -123       O  
HETATM 1832  O   HOH B 826       8.082  -0.896  28.632  1.00 20.95           O  
ANISOU 1832  O   HOH B 826     2464   2810   2685    -21   -100    392       O  
HETATM 1833  O   HOH B 827       1.348  34.089  28.423  1.00 24.60           O  
ANISOU 1833  O   HOH B 827     2329   3771   3246     89    723    778       O  
HETATM 1834  O   HOH B 828       9.766   7.581  18.578  1.00 22.66           O  
ANISOU 1834  O   HOH B 828     3543   3004   2064   -230   -588     41       O  
HETATM 1835  O   HOH B 829      14.342  39.788  28.861  1.00 21.44           O  
ANISOU 1835  O   HOH B 829     3622   2753   1772   -415    -89     54       O  
HETATM 1836  O   HOH B 830      21.907  23.571  29.163  1.00 24.34           O  
ANISOU 1836  O   HOH B 830     3733   3171   2345  -1495   -511    173       O  
HETATM 1837  O   HOH B 831       8.541   1.436  30.068  0.50 12.65           O  
ANISOU 1837  O   HOH B 831     1716    837   2255      9    -31    413       O  
HETATM 1838  O   HOH B 832      13.196  18.864  42.622  1.00 23.68           O  
ANISOU 1838  O   HOH B 832     3276   2537   3187   -629   -371   1174       O  
HETATM 1839  O   HOH B 833      13.024   4.394  40.224  1.00 25.30           O  
ANISOU 1839  O   HOH B 833     4810   1857   2944   -762   -372    927       O  
HETATM 1840  O   HOH B 834       2.227  19.857  21.525  1.00 38.90           O  
ANISOU 1840  O   HOH B 834     3558   4442   6782   -879    860   1810       O  
HETATM 1841  O   HOH B 835      22.621  19.581  32.815  1.00 25.22           O  
ANISOU 1841  O   HOH B 835     3442   3523   2618    519    -38   1104       O  
HETATM 1842  O   HOH B 836       9.569  13.322  39.632  1.00 22.88           O  
ANISOU 1842  O   HOH B 836     3521   2168   3005    260   -669    555       O  
HETATM 1843  O   HOH B 837      12.453  13.392  39.606  1.00 24.60           O  
ANISOU 1843  O   HOH B 837     3713   2470   3163   -263   -411     10       O  
HETATM 1844  O   HOH B 838      21.677  22.139  42.801  1.00 27.15           O  
ANISOU 1844  O   HOH B 838     3037   3577   3701   -384  -1691    786       O  
HETATM 1845  O   HOH B 839       7.444  -0.067  37.607  1.00 22.61           O  
ANISOU 1845  O   HOH B 839     2923   3136   2531    351    347    532       O  
HETATM 1846  O   HOH B 840       2.300  31.829  33.888  1.00 32.96           O  
ANISOU 1846  O   HOH B 840     4796   3538   4190  -1094   1426   -850       O  
HETATM 1847  O   HOH B 841       4.272  27.455  40.133  1.00 27.79           O  
ANISOU 1847  O   HOH B 841     3261   3057   4242   -686   1459   -901       O  
HETATM 1848  O   HOH B 842      12.964  26.627  43.889  1.00 30.95           O  
ANISOU 1848  O   HOH B 842     3690   3724   4344   -479    566  -1144       O  
HETATM 1849  O   HOH B 843      13.268  16.030  11.656  1.00 28.10           O  
ANISOU 1849  O   HOH B 843     4902   2759   3017   -689    144    588       O  
HETATM 1850  O   HOH B 844      21.312  34.151  28.018  1.00 22.82           O  
ANISOU 1850  O   HOH B 844     3368   2342   2960   -779   -295    458       O  
HETATM 1851  O   HOH B 845      11.613   4.648  19.315  1.00 30.93           O  
ANISOU 1851  O   HOH B 845     5123   4479   2152   -392    223   -355       O  
HETATM 1852  O   HOH B 846      23.330  27.962  26.088  1.00 25.63           O  
ANISOU 1852  O   HOH B 846     4145   3217   2378    950    767     49       O  
HETATM 1853  O   HOH B 847      21.584  12.649  38.081  1.00 27.83           O  
ANISOU 1853  O   HOH B 847     4358   3204   3012   -177  -1559    620       O  
HETATM 1854  O   HOH B 848      23.857  13.968  27.761  1.00 28.91           O  
ANISOU 1854  O   HOH B 848     3992   3399   3595   1378   1040    649       O  
HETATM 1855  O   HOH B 849       7.033  15.485  18.470  1.00 36.83           O  
ANISOU 1855  O   HOH B 849     6308   3371   4315  -1193  -1136  -1310       O  
HETATM 1856  O   HOH B 850      18.689  34.252  30.348  1.00 32.29           O  
ANISOU 1856  O   HOH B 850     5186   2831   4252    -46   -502   -304       O  
HETATM 1857  O   HOH B 851       4.539  18.791  22.630  1.00 28.74           O  
ANISOU 1857  O   HOH B 851     3166   4642   3113    267   -300    131       O  
HETATM 1858  O   HOH B 852      13.149  26.967  38.809  1.00 24.94           O  
ANISOU 1858  O   HOH B 852     3739   1741   3997   -633   -315   -115       O  
HETATM 1859  O   HOH B 853       7.606   7.253  23.094  1.00 35.72           O  
ANISOU 1859  O   HOH B 853     4595   3061   5916   -783   1427   -557       O  
HETATM 1860  O   HOH B 854       0.932  20.801  25.953  1.00 29.60           O  
ANISOU 1860  O   HOH B 854     3526   4127   3594    573    243   -520       O  
HETATM 1861  O   HOH B 855       0.472  32.870  31.499  1.00 38.10           O  
ANISOU 1861  O   HOH B 855     4975   4599   4901   -996    256    380       O  
HETATM 1862  O   HOH B 856      23.321  15.463  35.484  0.50 31.13           O  
ANISOU 1862  O   HOH B 856     3688   4001   4138  -1164     76   -721       O  
HETATM 1863  O   HOH B 857       7.071   9.634  37.194  0.50 22.04           O  
ANISOU 1863  O   HOH B 857     3660   2379   2336   -889   -770    696       O  
HETATM 1864  O   HOH B 858      18.454  10.951  10.808  0.50 26.58           O  
ANISOU 1864  O   HOH B 858     4099   2406   3592   -274    485   -115       O  
HETATM 1865  O   HOH B 859      19.850   8.601  26.453  1.00 40.10           O  
ANISOU 1865  O   HOH B 859     5812   2691   6733    -55    586    401       O  
HETATM 1866  O   HOH B 860       7.493   4.337  36.208  1.00 33.51           O  
ANISOU 1866  O   HOH B 860     4092   5438   3202     65   1394   -860       O  
HETATM 1867  O   HOH B 861      14.506  30.609  38.801  1.00 32.79           O  
ANISOU 1867  O   HOH B 861     4008   6049   2402   -614    385   -630       O  
HETATM 1868  O   HOH B 862       7.208  12.418  24.208  1.00 34.16           O  
ANISOU 1868  O   HOH B 862     5811   3308   3862   -312   -484    219       O  
HETATM 1869  O   HOH B 863      18.348   7.000  34.973  1.00 43.00           O  
ANISOU 1869  O   HOH B 863     5875   6417   4045  -1666     -9  -1184       O  
HETATM 1870  O   HOH B 864       7.527  15.630  25.322  1.00 39.45           O  
ANISOU 1870  O   HOH B 864     6108   5328   3552  -1055    642   -292       O  
HETATM 1871  O   HOH B 865      14.072  12.627  41.088  1.00 36.42           O  
ANISOU 1871  O   HOH B 865     6314   2419   5104   -219   -848   -977       O  
HETATM 1872  O   HOH B 866      22.866  26.173  28.402  0.38 13.91           O  
ANISOU 1872  O   HOH B 866     2355   1023   1905   -185    304    -56       O  
HETATM 1873  O   HOH B 867      14.084  21.206  46.713  1.00 34.90           O  
ANISOU 1873  O   HOH B 867     4968   4270   4024    222   -950    -73       O  
HETATM 1874  O   HOH B 868       0.864   7.527  35.389  0.50 31.32           O  
ANISOU 1874  O   HOH B 868     4556   3164   4178   -144    432  -1453       O  
HETATM 1875  O   HOH B 869      24.223  15.892  26.001  1.00 31.82           O  
ANISOU 1875  O   HOH B 869     3555   4724   3813    277   -788    704       O  
HETATM 1876  O   HOH B 870      19.756  41.105  26.483  1.00 36.58           O  
ANISOU 1876  O   HOH B 870     6533   4368   2998     65  -2113   -671       O  
HETATM 1877  O   HOH B 871       3.515  41.679  25.481  0.50 27.90           O  
ANISOU 1877  O   HOH B 871     3667   3565   3368    526    436    -81       O  
HETATM 1878  O   HOH B 872      21.175  14.423   8.809  0.50 30.23           O  
ANISOU 1878  O   HOH B 872     3985   5011   2488   1252   -374   -984       O  
HETATM 1879  O   HOH B 873       6.407   0.486  31.559  0.50 27.87           O  
ANISOU 1879  O   HOH B 873     3351   3604   3633   1029  -1034   -277       O  
HETATM 1880  O   HOH B 874       2.036  10.992  31.511  1.00 40.81           O  
ANISOU 1880  O   HOH B 874     2624   6666   6216   -616   -486     88       O  
HETATM 1881  O   HOH B 875      14.272  42.373  28.813  1.00 39.39           O  
ANISOU 1881  O   HOH B 875     6814   4141   4009   -798     58   -272       O  
HETATM 1882  O   HOH B 876      15.660  34.121  30.430  1.00 31.11           O  
ANISOU 1882  O   HOH B 876     5548   3563   2710    985    608    369       O  
HETATM 1883  O   HOH B 877      10.942  24.278  45.117  1.00 35.75           O  
ANISOU 1883  O   HOH B 877     4905   5390   3289  -1054    715  -1733       O  
HETATM 1884  O   HOH B 878      24.824  30.170  26.403  1.00 35.55           O  
ANISOU 1884  O   HOH B 878     4299   6462   2745    921   -249    464       O  
HETATM 1885  O   HOH B 879      20.988  17.005  32.889  1.00 41.92           O  
ANISOU 1885  O   HOH B 879     6344   4842   4743   -408   1223   -466       O  
HETATM 1886  O   HOH B 880       0.567  40.403  22.770  1.00 39.91           O  
ANISOU 1886  O   HOH B 880     4344   4790   6029   2206   -206    205       O  
HETATM 1887  O   HOH B 881       3.518  26.138  36.152  1.00 37.44           O  
ANISOU 1887  O   HOH B 881     6512   2885   4827    794   -815   -191       O  
HETATM 1888  O   HOH B 882      11.362  42.580  28.701  0.50 27.96           O  
ANISOU 1888  O   HOH B 882     4410   3052   3163  -1293   1309  -1455       O  
HETATM 1889  O   HOH B 883      17.360  38.606  28.309  1.00 40.88           O  
ANISOU 1889  O   HOH B 883     5636   4833   5064    768  -1970    773       O  
HETATM 1890  O   HOH B 884      17.249  15.004   9.390  1.00 39.51           O  
ANISOU 1890  O   HOH B 884     5546   6055   3409   1642   -318  -1396       O  
HETATM 1891  O   HOH B 885      18.351  31.691  36.476  1.00 38.57           O  
ANISOU 1891  O   HOH B 885     5803   3310   5543  -1137  -1341    796       O  
HETATM 1892  O   HOH B 886      12.358  34.138  34.056  1.00 39.92           O  
ANISOU 1892  O   HOH B 886     5490   5207   4469     11    254   1331       O  
HETATM 1893  O   HOH B 887       6.405   2.393  30.867  0.50 23.11           O  
ANISOU 1893  O   HOH B 887     1968   3405   3407   -818    458   -282       O  
HETATM 1894  O   HOH B 888      13.070  39.491  31.294  0.50 25.83           O  
ANISOU 1894  O   HOH B 888     3751   3380   2683  -1133   -606   -966       O  
HETATM 1895  O   HOH B 889      19.596  32.074  33.896  0.53 31.17           O  
ANISOU 1895  O   HOH B 889     4070   4176   3597   -832  -1113   -647       O  
HETATM 1896  O   HOH B 890       7.587  34.108  37.156  1.00 36.33           O  
ANISOU 1896  O   HOH B 890     5436   3815   4552    -41    -61    105       O  
HETATM 1897  O   HOH B 891       9.897  13.028  42.483  0.50 33.77           O  
ANISOU 1897  O   HOH B 891     3849   4978   4003   -715     85    -85       O  
HETATM 1898  O   HOH B 892      19.297  16.298  44.820  0.50 27.89           O  
ANISOU 1898  O   HOH B 892     3427   3336   3835    552   -806   -171       O  
HETATM 1899  O   HOH B 893       9.954  40.675  32.798  1.00 37.92           O  
ANISOU 1899  O   HOH B 893     5738   4605   4065  -2050   -119    -37       O  
HETATM 1900  O   HOH B 894      22.143   6.001  32.043  1.00 51.61           O  
ANISOU 1900  O   HOH B 894     6136   6430   7045   -146   -666    -37       O  
HETATM 1901  O   HOH B 895      18.029  12.318   9.046  0.50 29.24           O  
ANISOU 1901  O   HOH B 895     4789   3231   3090    -14   -251  -1783       O  
HETATM 1902  O   HOH B 896      22.383  26.540  37.015  0.47 27.44           O  
ANISOU 1902  O   HOH B 896     4443   3375   2606    442  -1280   -807       O  
HETATM 1903  O   HOH B 897      19.576   4.612  31.923  0.50 29.47           O  
ANISOU 1903  O   HOH B 897     3833   3479   3884    384   -309    780       O  
HETATM 1904  O   HOH B 898      20.751   6.902  35.189  0.51 27.56           O  
ANISOU 1904  O   HOH B 898     3380   3093   3999   -750   -741    209       O  
HETATM 1905  O   HOH B 899       2.851  28.561  36.071  1.00 31.69           O  
ANISOU 1905  O   HOH B 899     4110   3643   4288    305    202   -650       O  
HETATM 1906  O   HOH B 900       5.751  15.109  21.064  0.50 28.81           O  
ANISOU 1906  O   HOH B 900     3867   4434   2645  -1969   -996    180       O  
HETATM 1907  O   HOH B 901      16.693  12.697  40.017  0.50 28.27           O  
ANISOU 1907  O   HOH B 901     4648   2923   3169   -182    -11  -1129       O  
HETATM 1908  O   HOH B 902       7.347  31.478  40.749  0.50 26.30           O  
ANISOU 1908  O   HOH B 902     4546   3115   2332  -1068    -67   -376       O  
HETATM 1909  O   HOH B 903       7.696   6.717  30.088  1.00 32.42           O  
ANISOU 1909  O   HOH B 903     4693   2485   5140   -473   1249    631       O  
HETATM 1910  O   HOH B 904       8.773  32.336  39.685  0.50 24.39           O  
ANISOU 1910  O   HOH B 904     2121   4048   3099    369    193   -160       O  
HETATM 1911  O   HOH B 905      11.614  16.043  43.101  1.00 42.19           O  
ANISOU 1911  O   HOH B 905     5886   5182   4963   -296    335   1257       O  
HETATM 1912  O   HOH B 906      14.444  33.447  34.733  1.00 38.42           O  
ANISOU 1912  O   HOH B 906     6236   4599   3762   1056   -739    387       O  
HETATM 1913  O   HOH B 907      24.652  27.651  18.084  0.60 29.85           O  
ANISOU 1913  O   HOH B 907     4303   3248   3790    340   -367  -2081       O  
HETATM 1914  O   HOH B 908      16.385   9.372  40.157  0.49 25.88           O  
ANISOU 1914  O   HOH B 908     2932   3773   3129    348    213   -819       O  
HETATM 1915  O   HOH B 909      21.108   8.209  19.124  1.00 35.92           O  
ANISOU 1915  O   HOH B 909     3243   5016   5391   1333   1379   2254       O  
HETATM 1916  O   HOH B 910      26.519  22.669  23.519  0.50 28.68           O  
ANISOU 1916  O   HOH B 910     4480   2936   3482   -765    655  -1273       O  
HETATM 1917  O   HOH B 911      21.833  40.606  20.112  0.50 31.42           O  
ANISOU 1917  O   HOH B 911     2749   5173   4015    654    578    798       O  
HETATM 1918  O   HOH B 912      14.245  34.803  32.464  0.50 29.92           O  
ANISOU 1918  O   HOH B 912     5192   3328   2847     38     41   -629       O  
HETATM 1919  O   HOH B 913      18.879   1.220  21.997  0.50 26.38           O  
ANISOU 1919  O   HOH B 913     3276   2702   4046   -457    944  -1166       O  
HETATM 1920  O   HOH B 914      11.598  20.249  41.119  1.00 31.28           O  
ANISOU 1920  O   HOH B 914     3980   5079   2825    448    140    291       O  
HETATM 1921  O   HOH B 915       8.935  21.350  41.550  0.50 24.42           O  
ANISOU 1921  O   HOH B 915     3857   2087   3334   -186   1253     30       O  
HETATM 1922  O   HOH B 916      10.187  33.450  36.059  1.00 44.78           O  
ANISOU 1922  O   HOH B 916     4989   5959   6066   1932    -40    238       O  
HETATM 1923  O   HOH B 917      23.959  32.865  26.917  0.50 34.40           O  
ANISOU 1923  O   HOH B 917     4676   4736   3658   -504    164   1676       O  
HETATM 1924  O   HOH B 918      22.227  10.302  27.284  1.00 37.86           O  
ANISOU 1924  O   HOH B 918     4678   5149   4557    864  -1503   -665       O  
HETATM 1925  O   HOH B 919      19.804   6.342  26.861  1.00 37.64           O  
ANISOU 1925  O   HOH B 919     3935   4161   6208    -88   -576    519       O  
HETATM 1926  O   HOH B 920       8.006   7.114  32.679  0.50 21.80           O  
ANISOU 1926  O   HOH B 920     3103   1816   3364    476    834    528       O  
HETATM 1927  O   HOH B 921      20.627  27.607  18.486  0.60 13.66           O  
ANISOU 1927  O   HOH B 921     1871   1860   1461   -160    127    251       O  
HETATM 1928  O   HOH B 922      19.787  10.805  11.768  0.50 26.05           O  
ANISOU 1928  O   HOH B 922     4009   2208   3682   -273    810    165       O  
HETATM 1929  O   HOH B 923      14.739   2.386  20.399  0.50 17.73           O  
ANISOU 1929  O   HOH B 923     4141   1039   1556   1431   -178   -284       O  
HETATM 1930  O   HOH B 924      15.731  43.510  26.495  0.50 18.95           O  
ANISOU 1930  O   HOH B 924     3191   2227   1782   -631     -8  -1057       O  
HETATM 1931  O   HOH B 925      11.817   1.436  19.720  0.50 24.60           O  
ANISOU 1931  O   HOH B 925     3444   3232   2670    259   -170    362       O  
HETATM 1932  O   HOH B 926       6.703  20.776  40.210  1.00 31.59           O  
ANISOU 1932  O   HOH B 926     4355   3869   3779    159   -176   -829       O  
CONECT  495 1608                                                                
CONECT 1608  495 1702 1707 1714                                                 
CONECT 1608 1722 1724                                                           
CONECT 1611 1612 1613 1614                                                      
CONECT 1612 1611                                                                
CONECT 1613 1611                                                                
CONECT 1614 1611                                                                
CONECT 1615 1617 1623 1631                                                      
CONECT 1616 1618 1624 1632                                                      
CONECT 1617 1615 1619                                                           
CONECT 1618 1616 1620                                                           
CONECT 1619 1617 1621                                                           
CONECT 1620 1618 1622                                                           
CONECT 1621 1619 1623                                                           
CONECT 1622 1620 1624                                                           
CONECT 1623 1615 1621 1625                                                      
CONECT 1624 1616 1622 1626                                                      
CONECT 1625 1623 1627                                                           
CONECT 1626 1624 1628                                                           
CONECT 1627 1625 1629 1633                                                      
CONECT 1628 1626 1630 1634                                                      
CONECT 1629 1627 1631                                                           
CONECT 1630 1628 1632                                                           
CONECT 1631 1615 1629                                                           
CONECT 1632 1616 1630                                                           
CONECT 1633 1627 1635 1637 1639                                                 
CONECT 1634 1628 1636 1638 1640                                                 
CONECT 1635 1633                                                                
CONECT 1636 1634                                                                
CONECT 1637 1633                                                                
CONECT 1638 1634                                                                
CONECT 1639 1633 1641 1649                                                      
CONECT 1640 1634 1642 1650                                                      
CONECT 1641 1639 1643                                                           
CONECT 1642 1640 1644                                                           
CONECT 1643 1641 1645 1647                                                      
CONECT 1644 1642 1646 1648                                                      
CONECT 1645 1643                                                                
CONECT 1646 1644                                                                
CONECT 1647 1643                                                                
CONECT 1648 1644                                                                
CONECT 1649 1639 1651                                                           
CONECT 1650 1640 1652                                                           
CONECT 1651 1649 1653 1655                                                      
CONECT 1652 1650 1654 1656                                                      
CONECT 1653 1651                                                                
CONECT 1654 1652                                                                
CONECT 1655 1651 1657 1681                                                      
CONECT 1656 1652 1658 1682                                                      
CONECT 1657 1655 1659                                                           
CONECT 1658 1656 1660                                                           
CONECT 1659 1657 1661 1663                                                      
CONECT 1660 1658 1662 1664                                                      
CONECT 1661 1659                                                                
CONECT 1662 1660                                                                
CONECT 1663 1659 1665                                                           
CONECT 1664 1660 1666                                                           
CONECT 1665 1663 1667 1679                                                      
CONECT 1666 1664 1668 1680                                                      
CONECT 1667 1665 1669                                                           
CONECT 1668 1666 1670                                                           
CONECT 1669 1667 1671                                                           
CONECT 1670 1668 1672                                                           
CONECT 1671 1669 1673 1679                                                      
CONECT 1672 1670 1674 1680                                                      
CONECT 1673 1671 1675                                                           
CONECT 1674 1672 1676                                                           
CONECT 1675 1673 1677                                                           
CONECT 1676 1674 1678                                                           
CONECT 1677 1675 1679                                                           
CONECT 1678 1676 1680                                                           
CONECT 1679 1665 1671 1677                                                      
CONECT 1680 1666 1672 1678                                                      
CONECT 1681 1655 1693                                                           
CONECT 1682 1656 1694                                                           
CONECT 1683 1685 1693                                                           
CONECT 1684 1686 1694                                                           
CONECT 1685 1683 1687                                                           
CONECT 1686 1684 1688                                                           
CONECT 1687 1685 1689                                                           
CONECT 1688 1686 1690                                                           
CONECT 1689 1687 1691                                                           
CONECT 1690 1688 1692                                                           
CONECT 1691 1689 1693                                                           
CONECT 1692 1690 1694                                                           
CONECT 1693 1681 1683 1691                                                      
CONECT 1694 1682 1684 1692                                                      
CONECT 1702 1608                                                                
CONECT 1707 1608                                                                
CONECT 1714 1608                                                                
CONECT 1722 1608                                                                
CONECT 1724 1608                                                                
MASTER      245    0    5    2   20    0   13    6 1930    2   92   16          
END

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Molecule Visualization

mCSM-lig - Protein-ligand Affinity Change Upon Mutation

Predicted Affinity Change:

Mutation information:

Example