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***  HEME PROTEIN 25-FEB-98 1A6G  ***

elNémo ID: 22100401053527177

Job options:

ID        	=	 22100401053527177
JOBID     	=	 HEME PROTEIN 25-FEB-98 1A6G
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    HEME PROTEIN                            25-FEB-98   1A6G              
TITLE     CARBONMONOXY-MYOGLOBIN, ATOMIC RESOLUTION                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MYOGLOBIN;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PHYSETER CATODON;                               
SOURCE   3 ORGANISM_COMMON: SPERM WHALE;                                        
SOURCE   4 ORGANISM_TAXID: 9755                                                 
KEYWDS    HEME PROTEIN, MODEL COMPOUNDS, OXYGEN STORAGE, LIGAND                 
KEYWDS   2 BINDING GEOMETRY, CONFORMATIONAL SUBSTATES                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.VOJTECHOVSKY,K.CHU,J.BERENDZEN,R.M.SWEET,I.SCHLICHTING              
REVDAT   3   24-FEB-09 1A6G    1       VERSN                                    
REVDAT   2   14-JUN-05 1A6G    1       AUTHOR JRNL                              
REVDAT   1   21-OCT-98 1A6G    0                                                
JRNL        AUTH   J.VOJTECHOVSKY,K.CHU,J.BERENDZEN,R.M.SWEET,                  
JRNL        AUTH 2 I.SCHLICHTING                                                
JRNL        TITL   CRYSTAL STRUCTURES OF MYOGLOBIN-LIGAND COMPLEXES             
JRNL        TITL 2 AT NEAR-ATOMIC RESOLUTION.                                   
JRNL        REF    BIOPHYS.J.                    V.  77  2153 1999              
JRNL        REFN                   ISSN 0006-3495                               
JRNL        PMID   10512835                                                     
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.15 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) : 1.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.0                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.128                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.127                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.160                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2084                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 41538                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.119                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.118                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.150                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 1784                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 35480                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1363                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 55                                            
REMARK   3   SOLVENT ATOMS      : 187                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1415.90                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 1263.10                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 26                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 12713                   
REMARK   3   NUMBER OF RESTRAINTS                     : 19055                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.015                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.033                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.023                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.094                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.115                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL                    
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.005                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.044                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.083                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS & KRETSINGER                                    
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: HEME - PARAMETERS BASED ON CSD                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NO GEOMETRIC RESTRAINTS APPLIED TO        
REMARK   3  IRON AND THE PLANAR ATOMS OF THE HEME. DATA CUTOFF -3.0             
REMARK   3  (SIGMA(I)) BAYESIAN DIFFERENCE REFINEMENT WAS USED AT THE           
REMARK   3  FINAL STEP. SEE TERWILLIGER AND BERENDZEN, ACTA CRYST. D52:         
REMARK   3  1004-1011. THE SOLVENT MOLECULES 129,130,132,139 AND 146 CAN        
REMARK   3  BE MODELED FOR ONE ALTERNATIVE PROTEIN CONFORMATION.                
REMARK   4                                                                      
REMARK   4 1A6G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JAN-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE AREA DETECTOR          
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42857                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.150                              
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     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05900                            
REMARK 200   FOR THE DATA SET  : 20.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 63.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.29900                            
REMARK 200   FOR SHELL         : 4.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: SHELXL-97                                             
REMARK 200 STARTING MODEL: 1MBC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM            
REMARK 280  AMMONIUM SULPHATE, 50MM POTASSIUM PHOSPHATE, PH 6.0                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       15.31500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    ASP A  20   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP A  27   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG A  31   CD  -  NE  -  CZ  ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ARG A  31   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A  45   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    TYR A 103   CB  -  CG  -  CD1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    GLU A 109   CB  -  CG  -  CD  ANGL. DEV. =  22.5 DEGREES          
REMARK 500    GLU A 109   OE1 -  CD  -  OE2 ANGL. DEV. = -11.7 DEGREES          
REMARK 500    GLU A 109   CG  -  CD  -  OE1 ANGL. DEV. =  12.7 DEGREES          
REMARK 500    ARG A 118   CD  -  NE  -  CZ  ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ARG A 118   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP A 126   CB  -  CG  -  OD1 ANGL. DEV. =  10.0 DEGREES          
REMARK 500    TYR A 146   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    TYR A 146   CB  -  CG  -  CD1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    TYR A 146   CB  -  CG  -  CD1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  20       64.06   -154.34                                   
REMARK 500    PHE A 123       45.06   -143.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1116        DISTANCE =  5.76 ANGSTROMS                       
REMARK 525    HOH A1165        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH A1174        DISTANCE =  5.29 ANGSTROMS                       
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                             HEM A 154  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  93   NE2                                                    
REMARK 620 2 CMO A 157   C   174.3                                              
REMARK 620 3 CMO A 157   O   171.2   3.3                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 155                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 156                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 154                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO A 157                 
DBREF  1A6G A    1   151  UNP    P02185   MYG_PHYCA        2    152             
SEQRES   1 A  151  VAL LEU SER GLU GLY GLU TRP GLN LEU VAL LEU HIS VAL          
SEQRES   2 A  151  TRP ALA LYS VAL GLU ALA ASP VAL ALA GLY HIS GLY GLN          
SEQRES   3 A  151  ASP ILE LEU ILE ARG LEU PHE LYS SER HIS PRO GLU THR          
SEQRES   4 A  151  LEU GLU LYS PHE ASP ARG PHE LYS HIS LEU LYS THR GLU          
SEQRES   5 A  151  ALA GLU MET LYS ALA SER GLU ASP LEU LYS LYS HIS GLY          
SEQRES   6 A  151  VAL THR VAL LEU THR ALA LEU GLY ALA ILE LEU LYS LYS          
SEQRES   7 A  151  LYS GLY HIS HIS GLU ALA GLU LEU LYS PRO LEU ALA GLN          
SEQRES   8 A  151  SER HIS ALA THR LYS HIS LYS ILE PRO ILE LYS TYR LEU          
SEQRES   9 A  151  GLU PHE ILE SER GLU ALA ILE ILE HIS VAL LEU HIS SER          
SEQRES  10 A  151  ARG HIS PRO GLY ASN PHE GLY ALA ASP ALA GLN GLY ALA          
SEQRES  11 A  151  MET ASN LYS ALA LEU GLU LEU PHE ARG LYS ASP ILE ALA          
SEQRES  12 A  151  ALA LYS TYR LYS GLU LEU GLY TYR                              
HET    SO4  A 155       5                                                       
HET    SO4  A 156       5                                                       
HET    HEM  A 154      43                                                       
HET    CMO  A 157       2                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     CMO CARBON MONOXIDE                                                  
HETSYN     HEM HEME                                                             
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4  HEM    C34 H32 FE N4 O4                                             
FORMUL   5  CMO    C O                                                          
FORMUL   6  HOH   *184(H2 O)                                                    
HELIX    1   A SER A    3  GLU A   18  1                                  16    
HELIX    2   B ASP A   20  SER A   35  1                                  16    
HELIX    3   C HIS A   36  LYS A   42  1                                   7    
HELIX    4   D THR A   51  ALA A   57  1                                   7    
HELIX    5   E SER A   58  LYS A   77  1                                  20    
HELIX    6   F LEU A   86  THR A   95  1                                  10    
HELIX    7   G PRO A  100  ARG A  118  1                                  19    
HELIX    8   H GLY A  124  LEU A  149  1                                  26    
LINK        FE   HEM A 154                 NE2 HIS A  93     1555   1555  2.06  
LINK        FE   HEM A 154                 C   CMO A 157     1555   1555  1.82  
LINK        FE   HEM A 154                 O   CMO A 157     1555   1555  2.91  
SITE     1 AC1  8 ALA A  57  SER A  58  GLU A  59  ASP A  60                    
SITE     2 AC1  8 HOH A1007  HOH A1026  HOH A1038  HOH A1086                    
SITE     1 AC2  5 GLN A  26  LYS A  62  HOH A1043  HOH A1045                    
SITE     2 AC2  5 HOH A1063                                                     
SITE     1 AC3 22 THR A  39  LYS A  42  PHE A  43  ARG A  45                    
SITE     2 AC3 22 HIS A  64  THR A  67  VAL A  68  LEU A  89                    
SITE     3 AC3 22 SER A  92  HIS A  93  HIS A  97  ILE A  99                    
SITE     4 AC3 22 TYR A 103  PHE A 138  CMO A 157  HOH A1024                    
SITE     5 AC3 22 HOH A1033  HOH A1059  HOH A1088  HOH A1092                    
SITE     6 AC3 22 HOH A1102  HOH A1118                                          
SITE     1 AC4  4 PHE A  43  HIS A  64  VAL A  68  HEM A 154                    
CRYST1   63.800   30.630   34.420  90.00 105.80  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015674  0.000000  0.004435        0.00000                         
SCALE2      0.000000  0.032648  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.030194        0.00000                         
ATOM      1  N   VAL A   1      -4.040  15.048  13.602  1.00 37.04           N  
ANISOU    1  N   VAL A   1     4226   5590   4259   -553  -1578    468       N  
ATOM      2  CA  VAL A   1      -3.621  15.574  14.908  1.00 25.44           C  
ANISOU    2  CA  VAL A   1     1866   3610   4188   -352   -557    429       C  
ATOM      3  C   VAL A   1      -2.766  14.564  15.637  1.00 24.20           C  
ANISOU    3  C   VAL A   1     1759   3383   4054   -620   -491    670       C  
ATOM      4  O   VAL A   1      -3.155  13.399  15.760  1.00 27.65           O  
ANISOU    4  O   VAL A   1     2426   3194   4886   -751  -1043    132       O  
ATOM      5  CB  VAL A   1      -4.863  15.869  15.757  1.00 32.48           C  
ANISOU    5  CB  VAL A   1     1625   5454   5261   -119   -158   1285       C  
ATOM      6  CG1 VAL A   1      -4.402  15.954  17.205  1.00 38.33           C  
ANISOU    6  CG1 VAL A   1     3074   6411   5079   1179    167   -873       C  
ATOM      7  CG2 VAL A   1      -5.600  17.125  15.353  1.00 45.60           C  
ANISOU    7  CG2 VAL A   1     3094   6062   8170   1583  -1370   -361       C  
ATOM      8  N   LEU A   2      -1.588  14.922  16.125  1.00 17.99           N  
ANISOU    8  N   LEU A   2     1322   2782   2731   -197    358    163       N  
ATOM      9  CA  LEU A   2      -0.767  13.985  16.878  1.00 16.85           C  
ANISOU    9  CA  LEU A   2     1223   3092   2089   -172    334    -91       C  
ATOM     10  C   LEU A   2      -1.326  13.777  18.289  1.00 16.94           C  
ANISOU   10  C   LEU A   2     1301   2920   2216   -697    432   -219       C  
ATOM     11  O   LEU A   2      -1.795  14.765  18.873  1.00 19.44           O  
ANISOU   11  O   LEU A   2     1931   3174   2283   -138    755    -25       O  
ATOM     12  CB  LEU A   2       0.694  14.436  17.007  1.00 15.72           C  
ANISOU   12  CB  LEU A   2     1427   2719   1827   -483    326     89       C  
ATOM     13  CG  LEU A   2       1.598  14.164  15.773  1.00 14.99           C  
ANISOU   13  CG  LEU A   2     1475   2616   1605   -658    295      5       C  
ATOM     14  CD1 LEU A   2       1.269  15.130  14.656  1.00 15.12           C  
ANISOU   14  CD1 LEU A   2     1615   2470   1661   -419    274   -124       C  
ATOM     15  CD2 LEU A   2       3.080  14.254  16.161  1.00 14.37           C  
ANISOU   15  CD2 LEU A   2     1473   2168   1817   -524    210   -199       C  
ATOM     16  N   SER A   3      -1.218  12.546  18.763  1.00 16.86           N  
ANISOU   16  N   SER A   3     1362   2899   2147   -841    301   -272       N  
ATOM     17  CA  SER A   3      -1.535  12.277  20.163  1.00 16.55           C  
ANISOU   17  CA  SER A   3     1360   2737   2192   -557    407   -243       C  
ATOM     18  C   SER A   3      -0.447  12.807  21.083  1.00 14.85           C  
ANISOU   18  C   SER A   3     1268   2493   1881   -325    495     -6       C  
ATOM     19  O   SER A   3       0.700  13.067  20.651  1.00 14.97           O  
ANISOU   19  O   SER A   3     1270   2413   2005   -474    479    -89       O  
ATOM     20  CB  SER A   3      -1.723  10.786  20.393  1.00 19.61           C  
ANISOU   20  CB  SER A   3     1829   2843   2779   -859    702   -127       C  
ATOM     21  OG  SER A   3      -0.446  10.166  20.255  1.00 18.94           O  
ANISOU   21  OG  SER A   3     2027   2415   2755   -771    647   -250       O  
ATOM     22  N   GLU A   4      -0.757  12.861  22.363  1.00 15.78           N  
ANISOU   22  N   GLU A   4     1581   2442   1974   -430    572   -122       N  
ATOM     23  CA  GLU A   4       0.275  13.242  23.326  1.00 15.57           C  
ANISOU   23  CA  GLU A   4     1617   2478   1821   -433    633   -205       C  
ATOM     24  C   GLU A   4       1.448  12.252  23.299  1.00 15.42           C  
ANISOU   24  C   GLU A   4     1566   2319   1974   -527    618     74       C  
ATOM     25  O   GLU A   4       2.646  12.626  23.387  1.00 14.63           O  
ANISOU   25  O   GLU A   4     1659   2442   1459   -546    368   -220       O  
ATOM     26  CB AGLU A   4      -0.330  13.353  24.732  0.53 18.37           C  
ANISOU   26  CB AGLU A   4     1797   3304   1879   -418    706   -180       C  
ATOM     27  CB BGLU A   4      -0.381  13.255  24.715  0.47 17.67           C  
ANISOU   27  CB BGLU A   4     1376   3431   1905   -596    626   -127       C  
ATOM     28  CG AGLU A   4      -1.131  14.620  24.961  0.53 17.56           C  
ANISOU   28  CG AGLU A   4     1665   3311   1694   -575    556   -615       C  
ATOM     29  CG BGLU A   4       0.653  13.342  25.810  0.47 18.45           C  
ANISOU   29  CG BGLU A   4     1301   3910   1800   -404    729   -646       C  
ATOM     30  CD AGLU A   4      -0.355  15.901  25.090  0.53 16.66           C  
ANISOU   30  CD AGLU A   4     1368   3344   1616   -539    210   -416       C  
ATOM     31  CD BGLU A   4       1.596  14.517  25.704  0.47 16.28           C  
ANISOU   31  CD BGLU A   4     1306   3252   1629      5    361   -636       C  
ATOM     32  OE1AGLU A   4       0.878  15.849  25.215  0.53 17.28           O  
ANISOU   32  OE1AGLU A   4     1477   3531   1558   -467   -100     13       O  
ATOM     33  OE1BGLU A   4       1.210  15.634  25.321  0.47 19.03           O  
ANISOU   33  OE1BGLU A   4     1340   3705   2187    105   -440   -254       O  
ATOM     34  OE2AGLU A   4      -0.975  16.982  25.077  0.53 17.32           O  
ANISOU   34  OE2AGLU A   4     1557   3303   1720   -499   -161   -258       O  
ATOM     35  OE2BGLU A   4       2.801  14.251  26.005  0.47 17.00           O  
ANISOU   35  OE2BGLU A   4     1702   2518   2239   -388   -725   -108       O  
ATOM     36  N   GLY A   5       1.170  10.966  23.156  1.00 16.78           N  
ANISOU   36  N   GLY A   5     1715   2328   2332   -473    467     64       N  
ATOM     37  CA  GLY A   5       2.197   9.970  23.084  1.00 15.89           C  
ANISOU   37  CA  GLY A   5     1865   2284   1890   -327    346    584       C  
ATOM     38  C   GLY A   5       3.120  10.174  21.877  1.00 14.88           C  
ANISOU   38  C   GLY A   5     1827   1995   1831   -320    373    326       C  
ATOM     39  O   GLY A   5       4.325   9.996  21.971  1.00 15.95           O  
ANISOU   39  O   GLY A   5     1830   2322   1910   -154    327    508       O  
ATOM     40  N   GLU A   6       2.533  10.524  20.769  1.00 14.11           N  
ANISOU   40  N   GLU A   6     1720   2038   1605   -532    243   -111       N  
ATOM     41  CA  GLU A   6       3.298  10.796  19.564  1.00 13.02           C  
ANISOU   41  CA  GLU A   6     1460   1924   1561   -350    198   -147       C  
ATOM     42  C   GLU A   6       4.196  12.027  19.762  1.00 11.53           C  
ANISOU   42  C   GLU A   6     1354   1757   1270   -228    122    -55       C  
ATOM     43  O   GLU A   6       5.393  12.004  19.395  1.00 11.96           O  
ANISOU   43  O   GLU A   6     1172   2014   1359   -159     -1   -133       O  
ATOM     44  CB  GLU A   6       2.374  10.937  18.352  1.00 13.94           C  
ANISOU   44  CB  GLU A   6     1433   2223   1639   -556     65   -197       C  
ATOM     45  CG  GLU A   6       1.797   9.608  17.905  1.00 14.64           C  
ANISOU   45  CG  GLU A   6     1670   2166   1725   -496    109   -279       C  
ATOM     46  CD  GLU A   6       0.617   9.694  16.963  1.00 15.85           C  
ANISOU   46  CD  GLU A   6     1478   2171   2372   -555     -5   -458       C  
ATOM     47  OE1 GLU A   6      -0.103  10.717  16.873  1.00 17.12           O  
ANISOU   47  OE1 GLU A   6     1639   2375   2493   -389    -64   -283       O  
ATOM     48  OE2 GLU A   6       0.388   8.728  16.213  1.00 18.46           O  
ANISOU   48  OE2 GLU A   6     1679   2702   2632   -525   -198   -829       O  
ATOM     49  N   TRP A   7       3.647  13.097  20.331  1.00 11.39           N  
ANISOU   49  N   TRP A   7     1193   1733   1401   -235    148    -26       N  
ATOM     50  CA  TRP A   7       4.471  14.270  20.609  1.00 10.81           C  
ANISOU   50  CA  TRP A   7     1342   1604   1162   -151     64    -56       C  
ATOM     51  C   TRP A   7       5.631  13.931  21.542  1.00 10.85           C  
ANISOU   51  C   TRP A   7     1302   1861    960   -153    184    -55       C  
ATOM     52  O   TRP A   7       6.730  14.463  21.356  1.00 11.28           O  
ANISOU   52  O   TRP A   7     1168   1843   1273    -67    140     38       O  
ATOM     53  CB  TRP A   7       3.673  15.420  21.217  1.00 11.10           C  
ANISOU   53  CB  TRP A   7     1181   1855   1180   -144    192   -127       C  
ATOM     54  CG  TRP A   7       2.828  16.141  20.200  1.00 11.13           C  
ANISOU   54  CG  TRP A   7     1116   1796   1317   -133    155    -95       C  
ATOM     55  CD1 TRP A   7       1.446  16.305  20.214  1.00 12.43           C  
ANISOU   55  CD1 TRP A   7     1145   2095   1485   -132    212     24       C  
ATOM     56  CD2 TRP A   7       3.252  16.844  19.016  1.00 10.93           C  
ANISOU   56  CD2 TRP A   7     1063   1549   1539    -85    159     73       C  
ATOM     57  NE1 TRP A   7       1.064  17.008  19.136  1.00 12.79           N  
ANISOU   57  NE1 TRP A   7     1019   2276   1564    -50     47      0       N  
ATOM     58  CE2 TRP A   7       2.146  17.378  18.367  1.00 11.98           C  
ANISOU   58  CE2 TRP A   7      977   1972   1602   -220    -32     89       C  
ATOM     59  CE3 TRP A   7       4.541  17.104  18.464  1.00 10.24           C  
ANISOU   59  CE3 TRP A   7     1022   1446   1424   -101    111   -153       C  
ATOM     60  CZ2 TRP A   7       2.219  18.085  17.194  1.00 13.14           C  
ANISOU   60  CZ2 TRP A   7     1215   2016   1761     93      8    180       C  
ATOM     61  CZ3 TRP A   7       4.611  17.815  17.276  1.00 12.12           C  
ANISOU   61  CZ3 TRP A   7     1174   1847   1584    -23    164    131       C  
ATOM     62  CH2 TRP A   7       3.451  18.311  16.650  1.00 12.47           C  
ANISOU   62  CH2 TRP A   7     1373   1843   1522   -121      4    180       C  
ATOM     63  N   GLN A   8       5.407  13.073  22.534  1.00 11.53           N  
ANISOU   63  N   GLN A   8     1277   1932   1170   -144    139    101       N  
ATOM     64  CA  GLN A   8       6.484  12.685  23.453  1.00 12.28           C  
ANISOU   64  CA  GLN A   8     1378   2160   1129     -3    127     96       C  
ATOM     65  C   GLN A   8       7.596  12.033  22.668  1.00 11.21           C  
ANISOU   65  C   GLN A   8     1505   1624   1130     -2    126    269       C  
ATOM     66  O   GLN A   8       8.785  12.277  22.943  1.00 11.66           O  
ANISOU   66  O   GLN A   8     1491   1774   1165     73    -22    107       O  
ATOM     67  CB AGLN A   8       5.948  11.719  24.501  0.47 15.46           C  
ANISOU   67  CB AGLN A   8     2142   2522   1212    323    500    347       C  
ATOM     68  CB BGLN A   8       6.002  11.843  24.620  0.53 15.66           C  
ANISOU   68  CB BGLN A   8     2000   2612   1340    408    463    420       C  
ATOM     69  CG AGLN A   8       6.968  11.152  25.440  0.47 19.92           C  
ANISOU   69  CG AGLN A   8     2830   2935   1803   -101   -168    809       C  
ATOM     70  CG BGLN A   8       7.046  11.901  25.734  0.53 18.29           C  
ANISOU   70  CG BGLN A   8     2762   2747   1439     39     87    712       C  
ATOM     71  CD AGLN A   8       7.912  10.075  24.986  0.47 20.81           C  
ANISOU   71  CD AGLN A   8     2188   2851   2869     35   -694   1009       C  
ATOM     72  CD BGLN A   8       6.455  11.354  27.016  0.53 20.00           C  
ANISOU   72  CD BGLN A   8     3317   2861   1422  -1010    -57    448       C  
ATOM     73  OE1AGLN A   8       7.610   9.249  24.131  0.47 28.28           O  
ANISOU   73  OE1AGLN A   8     4475   2437   3832     58   -387    405       O  
ATOM     74  OE1BGLN A   8       5.538  10.514  26.976  0.53 27.73           O  
ANISOU   74  OE1BGLN A   8     5150   3342   2045  -2252   -333    632       O  
ATOM     75  NE2AGLN A   8       9.129   9.989  25.527  0.47 30.94           N  
ANISOU   75  NE2AGLN A   8     1930   4781   5045   -562   -840   3330       N  
ATOM     76  NE2BGLN A   8       6.961  11.804  28.148  0.53 21.97           N  
ANISOU   76  NE2BGLN A   8     4425   2531   1392  -1488     63    378       N  
ATOM     77  N   LEU A   9       7.271  11.148  21.744  1.00 11.63           N  
ANISOU   77  N   LEU A   9     1410   1650   1359   -112    110    160       N  
ATOM     78  CA  LEU A   9       8.299  10.476  20.936  1.00 11.80           C  
ANISOU   78  CA  LEU A   9     1487   1538   1458    -15    176    234       C  
ATOM     79  C   LEU A   9       9.086  11.506  20.093  1.00 10.37           C  
ANISOU   79  C   LEU A   9     1268   1494   1180     27      1    135       C  
ATOM     80  O   LEU A   9      10.305  11.372  20.005  1.00 10.91           O  
ANISOU   80  O   LEU A   9     1234   1525   1385    222    106    218       O  
ATOM     81  CB  LEU A   9       7.694   9.429  20.041  1.00 12.66           C  
ANISOU   81  CB  LEU A   9     1807   1453   1551   -117    236    161       C  
ATOM     82  CG  LEU A   9       7.122   8.192  20.711  1.00 14.53           C  
ANISOU   82  CG  LEU A   9     1845   1756   1921   -278    332    367       C  
ATOM     83  CD1 LEU A   9       6.298   7.367  19.752  1.00 17.69           C  
ANISOU   83  CD1 LEU A   9     2742   1742   2238   -639    282    132       C  
ATOM     84  CD2 LEU A   9       8.225   7.371  21.344  1.00 21.53           C  
ANISOU   84  CD2 LEU A   9     2774   1858   3546   -189   -331    958       C  
ATOM     85  N   VAL A  10       8.391  12.449  19.505  1.00  9.52           N  
ANISOU   85  N   VAL A  10     1041   1497   1081     13     32    103       N  
ATOM     86  CA  VAL A  10       9.015  13.482  18.685  1.00  9.43           C  
ANISOU   86  CA  VAL A  10     1167   1305   1111    -48      8    -39       C  
ATOM     87  C   VAL A  10       9.968  14.291  19.534  1.00  9.12           C  
ANISOU   87  C   VAL A  10     1026   1384   1055    103    -15     21       C  
ATOM     88  O   VAL A  10      11.120  14.545  19.138  1.00 10.12           O  
ANISOU   88  O   VAL A  10      965   1703   1177     95    -52    -77       O  
ATOM     89  CB  VAL A  10       7.906  14.373  18.077  1.00  9.92           C  
ANISOU   89  CB  VAL A  10     1172   1644    953    -27    -99    149       C  
ATOM     90  CG1 VAL A  10       8.493  15.623  17.459  1.00 10.24           C  
ANISOU   90  CG1 VAL A  10     1244   1625   1021    -48    -51    110       C  
ATOM     91  CG2 VAL A  10       7.114  13.606  17.040  1.00 11.44           C  
ANISOU   91  CG2 VAL A  10     1399   1772   1174   -249   -216    224       C  
ATOM     92  N   LEU A  11       9.503  14.790  20.685  1.00 10.12           N  
ANISOU   92  N   LEU A  11     1119   1685   1041   -139    -25    -70       N  
ATOM     93  CA  LEU A  11      10.328  15.707  21.498  1.00 10.16           C  
ANISOU   93  CA  LEU A  11     1144   1575   1143    -20   -137    -57       C  
ATOM     94  C   LEU A  11      11.428  14.981  22.241  1.00 10.31           C  
ANISOU   94  C   LEU A  11     1335   1564   1018     58   -161   -100       C  
ATOM     95  O   LEU A  11      12.427  15.615  22.577  1.00 11.25           O  
ANISOU   95  O   LEU A  11     1163   1828   1282     84   -226   -127       O  
ATOM     96  CB  LEU A  11       9.398  16.534  22.397  1.00 10.74           C  
ANISOU   96  CB  LEU A  11     1383   1431   1267      8   -140   -124       C  
ATOM     97  CG  LEU A  11       8.450  17.442  21.610  1.00 10.96           C  
ANISOU   97  CG  LEU A  11     1357   1578   1229     71    -97     -1       C  
ATOM     98  CD1 LEU A  11       7.584  18.191  22.602  1.00 14.87           C  
ANISOU   98  CD1 LEU A  11     2060   2010   1578    464    144   -149       C  
ATOM     99  CD2 LEU A  11       9.222  18.387  20.687  1.00 13.37           C  
ANISOU   99  CD2 LEU A  11     1528   1592   1960    131    -31    421       C  
ATOM    100  N   HIS A  12      11.260  13.681  22.482  1.00 10.72           N  
ANISOU  100  N   HIS A  12     1317   1660   1094     58   -221     -8       N  
ATOM    101  CA  HIS A  12      12.326  12.927  23.122  1.00 11.55           C  
ANISOU  101  CA  HIS A  12     1314   1893   1180    153   -169    142       C  
ATOM    102  C   HIS A  12      13.530  12.844  22.194  1.00 11.86           C  
ANISOU  102  C   HIS A  12     1257   1938   1310    351   -190      8       C  
ATOM    103  O   HIS A  12      14.647  13.103  22.630  1.00 12.68           O  
ANISOU  103  O   HIS A  12     1315   2087   1417    243   -153    -60       O  
ATOM    104  CB  HIS A  12      11.834  11.528  23.498  1.00 12.69           C  
ANISOU  104  CB  HIS A  12     1738   1769   1315    217    -22    169       C  
ATOM    105  CG  HIS A  12      12.831  10.775  24.275  1.00 13.14           C  
ANISOU  105  CG  HIS A  12     1662   1722   1608    308   -157    -29       C  
ATOM    106  ND1 HIS A  12      13.090  11.027  25.591  1.00 15.34           N  
ANISOU  106  ND1 HIS A  12     2007   2115   1706    437   -495     65       N  
ATOM    107  CD2 HIS A  12      13.640   9.768  23.869  1.00 15.32           C  
ANISOU  107  CD2 HIS A  12     1879   1924   2019    496    402    336       C  
ATOM    108  CE1 HIS A  12      14.053  10.155  25.989  1.00 18.96           C  
ANISOU  108  CE1 HIS A  12     2555   2263   2384    654   -647    419       C  
ATOM    109  NE2 HIS A  12      14.374   9.414  24.956  1.00 19.97           N  
ANISOU  109  NE2 HIS A  12     2216   2846   2526   1010    -29    422       N  
ATOM    110  N   VAL A  13      13.315  12.526  20.927  1.00 11.70           N  
ANISOU  110  N   VAL A  13     1227   1904   1312    200     -7     93       N  
ATOM    111  CA  VAL A  13      14.432  12.517  19.996  1.00 11.61           C  
ANISOU  111  CA  VAL A  13     1383   1723   1304    184     62    224       C  
ATOM    112  C   VAL A  13      14.900  13.918  19.728  1.00 10.43           C  
ANISOU  112  C   VAL A  13     1067   1691   1207    218    -90     37       C  
ATOM    113  O   VAL A  13      16.130  14.164  19.591  1.00 11.81           O  
ANISOU  113  O   VAL A  13     1088   1788   1612    138    -99     63       O  
ATOM    114  CB  VAL A  13      14.153  11.716  18.748  1.00 11.68           C  
ANISOU  114  CB  VAL A  13     1286   1656   1495     20    147     47       C  
ATOM    115  CG1 VAL A  13      13.149  12.342  17.827  1.00 13.20           C  
ANISOU  115  CG1 VAL A  13     1759   1998   1261    321    -64   -147       C  
ATOM    116  CG2 VAL A  13      15.469  11.421  17.989  1.00 13.89           C  
ANISOU  116  CG2 VAL A  13     1630   1919   1730    226    287   -108       C  
ATOM    117  N   TRP A  14      14.024  14.893  19.641  1.00 10.48           N  
ANISOU  117  N   TRP A  14     1050   1624   1306     75   -105    128       N  
ATOM    118  CA  TRP A  14      14.474  16.240  19.371  1.00 10.41           C  
ANISOU  118  CA  TRP A  14      975   1652   1329    129    -89    261       C  
ATOM    119  C   TRP A  14      15.395  16.780  20.467  1.00 11.11           C  
ANISOU  119  C   TRP A  14     1125   1614   1483     64    -60    123       C  
ATOM    120  O   TRP A  14      16.336  17.538  20.183  1.00 12.48           O  
ANISOU  120  O   TRP A  14     1168   2000   1574   -124   -111    162       O  
ATOM    121  CB  TRP A  14      13.258  17.213  19.153  1.00 10.90           C  
ANISOU  121  CB  TRP A  14     1121   1633   1388    174     -5    166       C  
ATOM    122  CG  TRP A  14      13.782  18.435  18.497  1.00 12.41           C  
ANISOU  122  CG  TRP A  14     1086   1641   1988     68   -244    371       C  
ATOM    123  CD1 TRP A  14      14.115  19.610  19.092  1.00 17.58           C  
ANISOU  123  CD1 TRP A  14     2048   1587   3044     48   -678    236       C  
ATOM    124  CD2 TRP A  14      14.155  18.535  17.120  1.00 14.08           C  
ANISOU  124  CD2 TRP A  14      977   2325   2050    -28   -205    936       C  
ATOM    125  NE1 TRP A  14      14.634  20.421  18.135  1.00 20.98           N  
ANISOU  125  NE1 TRP A  14     1723   1917   4332   -448   -761    939       N  
ATOM    126  CE2 TRP A  14      14.671  19.835  16.922  1.00 19.19           C  
ANISOU  126  CE2 TRP A  14      973   2680   3638   -222   -212   1561       C  
ATOM    127  CE3 TRP A  14      14.062  17.665  16.024  1.00 16.19           C  
ANISOU  127  CE3 TRP A  14     1362   3244   1546    462   -119    856       C  
ATOM    128  CZ2 TRP A  14      15.110  20.305  15.685  1.00 24.22           C  
ANISOU  128  CZ2 TRP A  14     1239   3520   4443    -23     98   2550       C  
ATOM    129  CZ3 TRP A  14      14.514  18.127  14.777  1.00 21.38           C  
ANISOU  129  CZ3 TRP A  14     1609   4618   1897    559    129   1329       C  
ATOM    130  CH2 TRP A  14      15.009  19.417  14.645  1.00 25.56           C  
ANISOU  130  CH2 TRP A  14     1399   4868   3445    592    404   2435       C  
ATOM    131  N   ALA A  15      15.152  16.390  21.735  1.00 11.40           N  
ANISOU  131  N   ALA A  15     1082   1911   1338     -9   -112     22       N  
ATOM    132  CA  ALA A  15      16.042  16.829  22.822  1.00 12.98           C  
ANISOU  132  CA  ALA A  15     1292   2175   1464    245   -152   -254       C  
ATOM    133  C   ALA A  15      17.431  16.296  22.603  1.00 12.64           C  
ANISOU  133  C   ALA A  15     1212   2154   1436    156   -206   -263       C  
ATOM    134  O   ALA A  15      18.441  16.909  23.043  1.00 15.17           O  
ANISOU  134  O   ALA A  15     1353   2315   2096    307   -452   -549       O  
ATOM    135  CB  ALA A  15      15.484  16.337  24.169  1.00 17.46           C  
ANISOU  135  CB  ALA A  15     1614   3743   1275    257    -52   -147       C  
ATOM    136  N   LYS A  16      17.597  15.126  21.972  1.00 12.26           N  
ANISOU  136  N   LYS A  16     1159   1896   1602    221   -368    -38       N  
ATOM    137  CA  LYS A  16      18.893  14.608  21.581  1.00 14.10           C  
ANISOU  137  CA  LYS A  16     1434   2241   1682    527   -135     77       C  
ATOM    138  C   LYS A  16      19.509  15.450  20.479  1.00 13.65           C  
ANISOU  138  C   LYS A  16     1081   2339   1768     44   -379      4       C  
ATOM    139  O   LYS A  16      20.721  15.693  20.458  1.00 18.88           O  
ANISOU  139  O   LYS A  16     1065   3359   2750     84   -591    766       O  
ATOM    140  CB  LYS A  16      18.815  13.169  21.079  1.00 13.87           C  
ANISOU  140  CB  LYS A  16     1106   2202   1962    318     22    -21       C  
ATOM    141  CG  LYS A  16      18.110  12.134  21.955  1.00 15.48           C  
ANISOU  141  CG  LYS A  16     1479   2408   1995    433    106    255       C  
ATOM    142  CD  LYS A  16      18.830  11.957  23.254  1.00 15.39           C  
ANISOU  142  CD  LYS A  16     1671   2229   1948    274     31     42       C  
ATOM    143  CE  LYS A  16      18.193  10.864  24.114  1.00 17.49           C  
ANISOU  143  CE  LYS A  16     2095   2829   1720     87    119    243       C  
ATOM    144  NZ  LYS A  16      18.940  10.630  25.363  1.00 21.13           N  
ANISOU  144  NZ  LYS A  16     2632   2724   2671    142   -696    730       N  
ATOM    145  N   VAL A  17      18.761  15.910  19.526  1.00 13.66           N  
ANISOU  145  N   VAL A  17      843   2180   2168    132   -160    487       N  
ATOM    146  CA  VAL A  17      19.240  16.728  18.420  1.00 15.60           C  
ANISOU  146  CA  VAL A  17     1105   2452   2370      3    -65    683       C  
ATOM    147  C   VAL A  17      19.853  17.986  18.991  1.00 16.21           C  
ANISOU  147  C   VAL A  17      993   2648   2520   -138   -202    799       C  
ATOM    148  O   VAL A  17      20.860  18.510  18.520  1.00 18.31           O  
ANISOU  148  O   VAL A  17     1212   2806   2941   -328    -63   1153       O  
ATOM    149  CB  VAL A  17      18.102  17.069  17.402  1.00 15.28           C  
ANISOU  149  CB  VAL A  17      943   3128   1734    101    169    559       C  
ATOM    150  CG1 VAL A  17      18.517  18.159  16.446  1.00 15.70           C  
ANISOU  150  CG1 VAL A  17      948   3122   1897    260    198    658       C  
ATOM    151  CG2 VAL A  17      17.611  15.833  16.678  1.00 18.46           C  
ANISOU  151  CG2 VAL A  17     1229   3270   2515     -7   -137    387       C  
ATOM    152  N   GLU A  18      19.152  18.565  19.969  1.00 17.11           N  
ANISOU  152  N   GLU A  18     1526   2627   2348   -433   -164    529       N  
ATOM    153  CA  GLU A  18      19.590  19.833  20.545  1.00 20.98           C  
ANISOU  153  CA  GLU A  18     2007   2744   3221   -592   -528    366       C  
ATOM    154  C   GLU A  18      20.893  19.733  21.297  1.00 20.04           C  
ANISOU  154  C   GLU A  18     2694   2986   1935   -999   -791   1030       C  
ATOM    155  O   GLU A  18      21.514  20.796  21.568  1.00 25.47           O  
ANISOU  155  O   GLU A  18     3164   3428   3085  -1311  -1123    403       O  
ATOM    156  CB  GLU A  18      18.410  20.388  21.361  1.00 22.50           C  
ANISOU  156  CB  GLU A  18     2874   2642   3033   -538   -341    -59       C  
ATOM    157  CG  GLU A  18      17.380  20.893  20.320  1.00 23.35           C  
ANISOU  157  CG  GLU A  18     2331   3214   3326     12   -265   -559       C  
ATOM    158  CD  GLU A  18      16.304  21.710  21.012  1.00 27.47           C  
ANISOU  158  CD  GLU A  18     3327   3478   3634    320   -227  -1313       C  
ATOM    159  OE1 GLU A  18      16.260  21.471  22.222  1.00 31.77           O  
ANISOU  159  OE1 GLU A  18     4314   4032   3726  -1403    782  -1277       O  
ATOM    160  OE2 GLU A  18      15.620  22.495  20.325  1.00 30.10           O  
ANISOU  160  OE2 GLU A  18     2543   2586   6308   -151    129   -236       O  
ATOM    161  N   ALA A  19      21.399  18.537  21.553  1.00 21.01           N  
ANISOU  161  N   ALA A  19     2341   3304   2339   -748   -769    912       N  
ATOM    162  CA  ALA A  19      22.757  18.513  22.119  1.00 21.06           C  
ANISOU  162  CA  ALA A  19     2576   3231   2197   -933   -926    988       C  
ATOM    163  C   ALA A  19      23.800  18.845  21.054  1.00 21.69           C  
ANISOU  163  C   ALA A  19     2305   3637   2301  -1010  -1017    980       C  
ATOM    164  O   ALA A  19      24.980  19.066  21.374  1.00 22.64           O  
ANISOU  164  O   ALA A  19     2295   3335   2970   -884  -1298   1162       O  
ATOM    165  CB  ALA A  19      22.996  17.111  22.668  1.00 25.94           C  
ANISOU  165  CB  ALA A  19     2076   3340   4440  -1379  -1348   1715       C  
ATOM    166  N   ASP A  20      23.545  18.855  19.780  1.00 20.00           N  
ANISOU  166  N   ASP A  20     2210   3140   2249   -859   -822   1140       N  
ATOM    167  CA  ASP A  20      24.475  19.098  18.673  1.00 18.20           C  
ANISOU  167  CA  ASP A  20     2032   2537   2347   -824   -923   1030       C  
ATOM    168  C   ASP A  20      23.695  19.632  17.487  1.00 14.89           C  
ANISOU  168  C   ASP A  20      839   2951   1866   -526   -455    658       C  
ATOM    169  O   ASP A  20      23.602  19.024  16.429  1.00 16.45           O  
ANISOU  169  O   ASP A  20     1302   3046   1904   -564    -41    588       O  
ATOM    170  CB  ASP A  20      25.276  17.838  18.293  1.00 19.49           C  
ANISOU  170  CB  ASP A  20     2055   2608   2741   -637   -858   1250       C  
ATOM    171  CG  ASP A  20      26.240  18.097  17.145  1.00 23.45           C  
ANISOU  171  CG  ASP A  20     2113   3604   3194   -853   -466    771       C  
ATOM    172  OD1 ASP A  20      26.640  19.233  16.787  1.00 19.05           O  
ANISOU  172  OD1 ASP A  20     1288   3714   2236   -681   -460    738       O  
ATOM    173  OD2 ASP A  20      26.757  17.111  16.529  1.00 29.45           O  
ANISOU  173  OD2 ASP A  20     3909   3779   3503  -1376    227     62       O  
ATOM    174  N   VAL A  21      23.117  20.832  17.708  1.00 15.87           N  
ANISOU  174  N   VAL A  21     1305   2891   1832   -441   -333    720       N  
ATOM    175  CA  VAL A  21      22.270  21.438  16.677  1.00 13.79           C  
ANISOU  175  CA  VAL A  21     1265   2402   1573   -398   -227    325       C  
ATOM    176  C   VAL A  21      23.079  21.544  15.375  1.00 13.05           C  
ANISOU  176  C   VAL A  21      898   2350   1708   -104   -234    515       C  
ATOM    177  O   VAL A  21      22.647  21.190  14.279  1.00 13.80           O  
ANISOU  177  O   VAL A  21     1046   2576   1623   -238    -32    415       O  
ATOM    178  CB  VAL A  21      21.585  22.748  17.139  1.00 14.92           C  
ANISOU  178  CB  VAL A  21     1349   2617   1704   -298    -66    211       C  
ATOM    179  CG1 VAL A  21      20.779  23.356  16.002  1.00 17.04           C  
ANISOU  179  CG1 VAL A  21     1630   3213   1631    446    108     76       C  
ATOM    180  CG2 VAL A  21      20.648  22.514  18.313  1.00 17.53           C  
ANISOU  180  CG2 VAL A  21     1706   3267   1689   -513     73     73       C  
ATOM    181  N   ALA A  22      24.289  22.127  15.472  1.00 15.67           N  
ANISOU  181  N   ALA A  22     1159   3075   1719   -436   -171    465       N  
ATOM    182  CA  ALA A  22      25.039  22.445  14.244  1.00 14.76           C  
ANISOU  182  CA  ALA A  22     1199   2549   1862   -537    -74    353       C  
ATOM    183  C   ALA A  22      25.466  21.196  13.456  1.00 15.02           C  
ANISOU  183  C   ALA A  22     1398   2556   1751   -356   -290    380       C  
ATOM    184  O   ALA A  22      25.348  21.152  12.175  1.00 15.33           O  
ANISOU  184  O   ALA A  22     1279   2708   1837   -374   -128    338       O  
ATOM    185  CB  ALA A  22      26.292  23.263  14.552  1.00 16.59           C  
ANISOU  185  CB  ALA A  22     1333   2774   2197   -668   -383    403       C  
ATOM    186  N   GLY A  23      25.841  20.129  14.134  1.00 16.30           N  
ANISOU  186  N   GLY A  23     1012   2808   2374   -181    -11    649       N  
ATOM    187  CA  GLY A  23      26.193  18.902  13.364  1.00 15.97           C  
ANISOU  187  CA  GLY A  23     1051   2798   2218    -56   -176    656       C  
ATOM    188  C   GLY A  23      25.009  18.277  12.610  1.00 14.67           C  
ANISOU  188  C   GLY A  23      990   2936   1646     63     79    612       C  
ATOM    189  O   GLY A  23      25.103  17.787  11.480  1.00 15.07           O  
ANISOU  189  O   GLY A  23     1227   2759   1741     78     33    550       O  
ATOM    190  N   HIS A  24      23.895  18.305  13.360  1.00 14.65           N  
ANISOU  190  N   HIS A  24      941   3055   1570    176    -11    813       N  
ATOM    191  CA  HIS A  24      22.708  17.789  12.671  1.00 12.89           C  
ANISOU  191  CA  HIS A  24      987   2459   1453    209    119    663       C  
ATOM    192  C   HIS A  24      22.325  18.665  11.467  1.00 11.61           C  
ANISOU  192  C   HIS A  24      994   2101   1316      2     75    472       C  
ATOM    193  O   HIS A  24      21.912  18.139  10.440  1.00 11.97           O  
ANISOU  193  O   HIS A  24     1186   1969   1392    -73     78    460       O  
ATOM    194  CB  HIS A  24      21.519  17.770  13.633  1.00 11.32           C  
ANISOU  194  CB  HIS A  24     1082   1958   1262     79     83    426       C  
ATOM    195  CG  HIS A  24      21.586  16.701  14.673  1.00 11.53           C  
ANISOU  195  CG  HIS A  24     1119   1976   1285    186    -19    482       C  
ATOM    196  ND1 HIS A  24      22.358  16.754  15.791  1.00 12.55           N  
ANISOU  196  ND1 HIS A  24     1246   2234   1289    206     -2    430       N  
ATOM    197  CD2 HIS A  24      20.945  15.524  14.745  1.00 13.55           C  
ANISOU  197  CD2 HIS A  24     1799   1808   1543     99   -155    396       C  
ATOM    198  CE1 HIS A  24      22.168  15.635  16.512  1.00 14.08           C  
ANISOU  198  CE1 HIS A  24     1495   2283   1571    358    -51    626       C  
ATOM    199  NE2 HIS A  24      21.291  14.848  15.890  1.00 15.01           N  
ANISOU  199  NE2 HIS A  24     2124   2239   1342    -59    -20    614       N  
ATOM    200  N   GLY A  25      22.428  20.002  11.637  1.00 11.31           N  
ANISOU  200  N   GLY A  25      890   2100   1307   -101    -63    487       N  
ATOM    201  CA  GLY A  25      21.995  20.882  10.561  1.00 11.79           C  
ANISOU  201  CA  GLY A  25     1063   2029   1385    -92   -199    460       C  
ATOM    202  C   GLY A  25      22.814  20.698   9.315  1.00 11.31           C  
ANISOU  202  C   GLY A  25     1226   1830   1241   -465   -201    288       C  
ATOM    203  O   GLY A  25      22.312  20.670   8.197  1.00 11.35           O  
ANISOU  203  O   GLY A  25     1354   1656   1303   -458   -326    322       O  
ATOM    204  N   GLN A  26      24.128  20.509   9.503  1.00 14.84           N  
ANISOU  204  N   GLN A  26     1139   3320   1178   -735   -155    291       N  
ATOM    205  CA  GLN A  26      25.058  20.246   8.398  1.00 16.26           C  
ANISOU  205  CA  GLN A  26     1098   3710   1370   -884    -51    289       C  
ATOM    206  C   GLN A  26      24.677  18.967   7.717  1.00 14.88           C  
ANISOU  206  C   GLN A  26      770   3522   1363   -466    -87    236       C  
ATOM    207  O   GLN A  26      24.546  18.950   6.459  1.00 18.11           O  
ANISOU  207  O   GLN A  26      965   4639   1276   -691     -4    113       O  
ATOM    208  CB AGLN A  26      26.455  19.848   8.947  0.58 16.02           C  
ANISOU  208  CB AGLN A  26     1065   3306   1715   -913   -122    498       C  
ATOM    209  CB BGLN A  26      26.508  20.456   8.835  0.42 18.66           C  
ANISOU  209  CB BGLN A  26     1115   4309   1667  -1165   -102    426       C  
ATOM    210  CG AGLN A  26      27.247  21.069   9.288  0.58 13.30           C  
ANISOU  210  CG AGLN A  26      919   2464   1669   -375   -243    930       C  
ATOM    211  CG BGLN A  26      27.504  19.714   7.943  0.42 21.12           C  
ANISOU  211  CG BGLN A  26     1361   4093   2571   -236   -119    815       C  
ATOM    212  CD AGLN A  26      28.532  20.773  10.018  0.58 13.08           C  
ANISOU  212  CD AGLN A  26     1059   2237   1673   -291   -478    411       C  
ATOM    213  CD BGLN A  26      28.802  19.620   8.749  0.42 22.37           C  
ANISOU  213  CD BGLN A  26     1449   4357   2692   -639   -240   1316       C  
ATOM    214  OE1AGLN A  26      28.522  20.107  11.052  0.58 16.10           O  
ANISOU  214  OE1AGLN A  26     1436   2767   1912   -179   -696    801       O  
ATOM    215  OE1BGLN A  26      29.070  18.724   9.545  0.42 28.37           O  
ANISOU  215  OE1BGLN A  26     2505   5020   3252  -2020  -1456   2150       O  
ATOM    216  NE2AGLN A  26      29.649  21.263   9.501  0.58 14.12           N  
ANISOU  216  NE2AGLN A  26     1053   2066   2245   -535   -573    318       N  
ATOM    217  NE2BGLN A  26      29.572  20.680   8.533  0.42 22.95           N  
ANISOU  217  NE2BGLN A  26     2743   3454   2521   -782  -1349   1039       N  
ATOM    218  N   ASP A  27      24.470  17.868   8.457  1.00 15.51           N  
ANISOU  218  N   ASP A  27      787   3339   1768     14    -82    300       N  
ATOM    219  CA  ASP A  27      24.165  16.575   7.829  1.00 15.32           C  
ANISOU  219  CA  ASP A  27     1021   3310   1489    335    -13    169       C  
ATOM    220  C   ASP A  27      22.873  16.701   7.073  1.00 12.44           C  
ANISOU  220  C   ASP A  27     1015   2319   1393    201     96    256       C  
ATOM    221  O   ASP A  27      22.810  16.132   6.013  1.00 12.90           O  
ANISOU  221  O   ASP A  27     1142   2412   1350    376     33     97       O  
ATOM    222  CB  ASP A  27      24.082  15.433   8.871  1.00 17.41           C  
ANISOU  222  CB  ASP A  27     1344   3195   2075    388   -484    396       C  
ATOM    223  CG  ASP A  27      25.311  15.028   9.658  1.00 18.05           C  
ANISOU  223  CG  ASP A  27     1503   2380   2973    335   -834    116       C  
ATOM    224  OD1 ASP A  27      26.376  15.582   9.321  1.00 25.44           O  
ANISOU  224  OD1 ASP A  27     1194   3264   5207    164   -892    476       O  
ATOM    225  OD2 ASP A  27      25.315  14.266  10.622  1.00 26.66           O  
ANISOU  225  OD2 ASP A  27     2513   3129   4487    271  -1699   1326       O  
ATOM    226  N   ILE A  28      21.889  17.409   7.651  1.00 10.44           N  
ANISOU  226  N   ILE A  28      937   1847   1183     10    -73    119       N  
ATOM    227  CA  ILE A  28      20.588  17.446   6.987  1.00  9.91           C  
ANISOU  227  CA  ILE A  28      866   1639   1259    -19    -62    197       C  
ATOM    228  C   ILE A  28      20.664  18.256   5.696  1.00  8.94           C  
ANISOU  228  C   ILE A  28      816   1534   1047   -100    -65     43       C  
ATOM    229  O   ILE A  28      20.133  17.793   4.683  1.00  9.39           O  
ANISOU  229  O   ILE A  28      905   1522   1142   -217     10     30       O  
ATOM    230  CB  ILE A  28      19.559  18.011   7.981  1.00  9.90           C  
ANISOU  230  CB  ILE A  28      913   1680   1170   -169     13    199       C  
ATOM    231  CG1 ILE A  28      19.275  16.960   9.061  1.00  9.74           C  
ANISOU  231  CG1 ILE A  28     1062   1358   1281   -101    103     93       C  
ATOM    232  CG2 ILE A  28      18.279  18.459   7.291  1.00 10.04           C  
ANISOU  232  CG2 ILE A  28      881   1533   1399    -26    -67     30       C  
ATOM    233  CD1 ILE A  28      18.559  17.456  10.284  1.00 10.32           C  
ANISOU  233  CD1 ILE A  28     1099   1576   1246   -168     15    -23       C  
ATOM    234  N   LEU A  29      21.280  19.431   5.711  1.00  9.48           N  
ANISOU  234  N   LEU A  29      863   1685   1053   -218    -79     62       N  
ATOM    235  CA  LEU A  29      21.353  20.203   4.479  1.00  9.17           C  
ANISOU  235  CA  LEU A  29      872   1716    897   -165   -179     87       C  
ATOM    236  C   LEU A  29      22.176  19.510   3.442  1.00  9.25           C  
ANISOU  236  C   LEU A  29     1041   1409   1064   -259    -16    177       C  
ATOM    237  O   LEU A  29      21.840  19.548   2.251  1.00  9.72           O  
ANISOU  237  O   LEU A  29     1129   1545   1021   -255     -4     17       O  
ATOM    238  CB  LEU A  29      21.840  21.640   4.742  1.00  9.92           C  
ANISOU  238  CB  LEU A  29     1040   1671   1059   -249    -93    -36       C  
ATOM    239  CG  LEU A  29      20.904  22.528   5.547  1.00 10.71           C  
ANISOU  239  CG  LEU A  29     1262   1691   1115   -307    -97    -98       C  
ATOM    240  CD1 LEU A  29      21.502  23.872   5.855  1.00 12.14           C  
ANISOU  240  CD1 LEU A  29     1653   1631   1329   -262    -84   -114       C  
ATOM    241  CD2 LEU A  29      19.561  22.749   4.817  1.00 12.40           C  
ANISOU  241  CD2 LEU A  29     1299   1805   1605     45   -204   -319       C  
ATOM    242  N   ILE A  30      23.290  18.881   3.847  1.00  9.96           N  
ANISOU  242  N   ILE A  30      951   1782   1049   -206     20    111       N  
ATOM    243  CA  ILE A  30      24.103  18.146   2.874  1.00 10.74           C  
ANISOU  243  CA  ILE A  30     1002   1901   1178    -97   -121     26       C  
ATOM    244  C   ILE A  30      23.337  17.002   2.222  1.00 10.75           C  
ANISOU  244  C   ILE A  30      951   1750   1385      1      0    -27       C  
ATOM    245  O   ILE A  30      23.361  16.801   1.024  1.00 10.60           O  
ANISOU  245  O   ILE A  30      940   1742   1346     20    -29    -19       O  
ATOM    246  CB  ILE A  30      25.437  17.716   3.487  1.00 11.79           C  
ANISOU  246  CB  ILE A  30      961   2176   1342    -78    -29    159       C  
ATOM    247  CG1 ILE A  30      26.286  18.935   3.827  1.00 14.66           C  
ANISOU  247  CG1 ILE A  30      969   2844   1755   -528    -29     18       C  
ATOM    248  CG2 ILE A  30      26.159  16.719   2.582  1.00 14.81           C  
ANISOU  248  CG2 ILE A  30     1084   3143   1402    212    -71   -267       C  
ATOM    249  CD1 ILE A  30      27.548  18.631   4.600  1.00 17.42           C  
ANISOU  249  CD1 ILE A  30     1077   3510   2030   -188   -177   -242       C  
ATOM    250  N   ARG A  31      22.586  16.258   3.068  1.00 10.66           N  
ANISOU  250  N   ARG A  31     1010   1725   1316     -2      8   -103       N  
ATOM    251  CA  ARG A  31      21.806  15.175   2.507  1.00 10.61           C  
ANISOU  251  CA  ARG A  31     1207   1408   1417     61    -29     66       C  
ATOM    252  C   ARG A  31      20.772  15.716   1.535  1.00 10.11           C  
ANISOU  252  C   ARG A  31      965   1638   1236      6     59    -92       C  
ATOM    253  O   ARG A  31      20.555  15.160   0.450  1.00 11.28           O  
ANISOU  253  O   ARG A  31     1145   1806   1335    -71     29   -202       O  
ATOM    254  CB AARG A  31      21.065  14.463   3.673  0.56 13.07           C  
ANISOU  254  CB AARG A  31     1355   1827   1784     -9      9    456       C  
ATOM    255  CB BARG A  31      21.084  14.365   3.608  0.44 12.64           C  
ANISOU  255  CB BARG A  31     1432   1714   1655     -7     28    279       C  
ATOM    256  CG AARG A  31      19.987  13.476   3.257  0.56 15.51           C  
ANISOU  256  CG AARG A  31     1386   1768   2741    -85    307    230       C  
ATOM    257  CG BARG A  31      20.411  13.142   3.000  0.44 15.71           C  
ANISOU  257  CG BARG A  31     1976   1648   2346   -305     37    307       C  
ATOM    258  CD AARG A  31      20.619  12.294   2.565  0.56 19.44           C  
ANISOU  258  CD AARG A  31     2057   2271   3059   -212    632   -368       C  
ATOM    259  CD BARG A  31      19.895  12.194   4.078  0.44 18.26           C  
ANISOU  259  CD BARG A  31     2320   2266   2352   -620    290    363       C  
ATOM    260  NE AARG A  31      19.621  11.236   2.277  0.56 23.73           N  
ANISOU  260  NE AARG A  31     2754   1995   4265   -266   -254   -182       N  
ATOM    261  NE BARG A  31      18.894  11.300   3.545  0.44 24.48           N  
ANISOU  261  NE BARG A  31     3169   2159   3974  -1139    -68    469       N  
ATOM    262  CZ AARG A  31      20.007   9.974   2.504  0.56 29.63           C  
ANISOU  262  CZ AARG A  31     4105   2176   4977   -386   -932    479       C  
ATOM    263  CZ BARG A  31      18.978  10.196   2.850  0.44 30.10           C  
ANISOU  263  CZ BARG A  31     4333   2501   4601   -968   -837    -45       C  
ATOM    264  NH1AARG A  31      21.233   9.767   2.973  0.56 29.37           N  
ANISOU  264  NH1AARG A  31     4916   2550   3693     18  -1505    903       N  
ATOM    265  NH1BARG A  31      20.163   9.691   2.529  0.44 31.58           N  
ANISOU  265  NH1BARG A  31     4747   2779   4472  -1052   -462  -1071       N  
ATOM    266  NH2AARG A  31      19.244   8.920   2.278  0.56 31.52           N  
ANISOU  266  NH2AARG A  31     4508   1857   5613    -54   -208   -998       N  
ATOM    267  NH2BARG A  31      17.855   9.578   2.480  0.44 36.49           N  
ANISOU  267  NH2BARG A  31     4697   3790   5376   -737  -2187   -761       N  
ATOM    268  N   LEU A  32      20.100  16.821   1.889  1.00  9.89           N  
ANISOU  268  N   LEU A  32      881   1651   1226     -5     -5    -88       N  
ATOM    269  CA  LEU A  32      19.131  17.461   1.022  1.00  9.70           C  
ANISOU  269  CA  LEU A  32      878   1615   1193    -92    -61    -52       C  
ATOM    270  C   LEU A  32      19.757  17.827  -0.336  1.00  9.46           C  
ANISOU  270  C   LEU A  32      872   1511   1211    -54    -12   -139       C  
ATOM    271  O   LEU A  32      19.225  17.531  -1.410  1.00 10.27           O  
ANISOU  271  O   LEU A  32     1021   1756   1126    -53     51   -166       O  
ATOM    272  CB  LEU A  32      18.573  18.698   1.704  1.00  9.68           C  
ANISOU  272  CB  LEU A  32      896   1749   1033    -32    -10    -56       C  
ATOM    273  CG  LEU A  32      17.602  19.543   0.874  1.00 10.37           C  
ANISOU  273  CG  LEU A  32      900   1773   1266    -20     -9     -8       C  
ATOM    274  CD1 LEU A  32      16.292  18.775   0.654  1.00 11.80           C  
ANISOU  274  CD1 LEU A  32      811   2227   1447    -95    -58     13       C  
ATOM    275  CD2 LEU A  32      17.327  20.845   1.588  1.00 11.27           C  
ANISOU  275  CD2 LEU A  32     1011   1925   1345    199      7    -27       C  
ATOM    276  N   PHE A  33      20.919  18.511  -0.265  1.00  9.26           N  
ANISOU  276  N   PHE A  33      832   1481   1206     46     45    -99       N  
ATOM    277  CA  PHE A  33      21.562  18.987  -1.475  1.00  9.92           C  
ANISOU  277  CA  PHE A  33      860   1730   1179     32     80    -57       C  
ATOM    278  C   PHE A  33      22.049  17.852  -2.370  1.00 10.12           C  
ANISOU  278  C   PHE A  33      820   1848   1178    143    113    -32       C  
ATOM    279  O   PHE A  33      22.042  17.968  -3.610  1.00 12.20           O  
ANISOU  279  O   PHE A  33     1330   2171   1136    426    164    -47       O  
ATOM    280  CB  PHE A  33      22.718  19.883  -1.092  1.00 10.45           C  
ANISOU  280  CB  PHE A  33      793   1922   1255      4     57     -8       C  
ATOM    281  CG  PHE A  33      22.352  21.188  -0.389  1.00 10.10           C  
ANISOU  281  CG  PHE A  33     1018   1713   1108   -104    -86    157       C  
ATOM    282  CD1 PHE A  33      21.089  21.738  -0.483  1.00 10.04           C  
ANISOU  282  CD1 PHE A  33     1026   1592   1198   -127     88     34       C  
ATOM    283  CD2 PHE A  33      23.318  21.815   0.371  1.00 11.83           C  
ANISOU  283  CD2 PHE A  33     1413   1665   1415   -343   -374    355       C  
ATOM    284  CE1 PHE A  33      20.823  22.945   0.150  1.00 11.94           C  
ANISOU  284  CE1 PHE A  33     1550   1599   1387   -106    153    -57       C  
ATOM    285  CE2 PHE A  33      23.038  22.987   0.995  1.00 13.47           C  
ANISOU  285  CE2 PHE A  33     1896   1745   1477   -518   -247    179       C  
ATOM    286  CZ  PHE A  33      21.779  23.592   0.912  1.00 13.09           C  
ANISOU  286  CZ  PHE A  33     2142   1546   1285   -289    -34    -49       C  
ATOM    287  N   LYS A  34      22.560  16.788  -1.761  1.00 10.57           N  
ANISOU  287  N   LYS A  34     1001   1780   1236    150    -26   -126       N  
ATOM    288  CA  LYS A  34      23.062  15.633  -2.528  1.00 12.15           C  
ANISOU  288  CA  LYS A  34     1220   1921   1474    242     38   -212       C  
ATOM    289  C   LYS A  34      21.930  14.846  -3.144  1.00 11.68           C  
ANISOU  289  C   LYS A  34     1341   1804   1294    279    -10   -258       C  
ATOM    290  O   LYS A  34      21.970  14.414  -4.279  1.00 13.88           O  
ANISOU  290  O   LYS A  34     1561   2309   1403    404     54   -524       O  
ATOM    291  CB  LYS A  34      23.961  14.775  -1.668  1.00 15.03           C  
ANISOU  291  CB  LYS A  34     1717   2020   1974    656   -358   -516       C  
ATOM    292  CG  LYS A  34      25.283  15.344  -1.264  1.00 17.53           C  
ANISOU  292  CG  LYS A  34     1485   3088   2090    736   -228   -821       C  
ATOM    293  CD  LYS A  34      25.924  14.346  -0.298  1.00 26.99           C  
ANISOU  293  CD  LYS A  34     3094   3349   3810   1574  -1721  -1016       C  
ATOM    294  CE  LYS A  34      26.179  12.962  -0.870  1.00 29.72           C  
ANISOU  294  CE  LYS A  34     3272   2913   5108    814  -1544  -1024       C  
ATOM    295  NZ  LYS A  34      27.612  12.894  -1.259  1.00 35.25           N  
ANISOU  295  NZ  LYS A  34     3812   3063   6519   1053   -459  -1771       N  
ATOM    296  N   SER A  35      20.866  14.627  -2.361  1.00 11.47           N  
ANISOU  296  N   SER A  35     1424   1684   1251    130    -20   -213       N  
ATOM    297  CA  SER A  35      19.739  13.821  -2.821  1.00 12.92           C  
ANISOU  297  CA  SER A  35     1519   1734   1656     91   -183   -140       C  
ATOM    298  C   SER A  35      18.856  14.570  -3.806  1.00 11.58           C  
ANISOU  298  C   SER A  35     1394   1682   1323      3    -61   -407       C  
ATOM    299  O   SER A  35      18.209  13.942  -4.663  1.00 12.84           O  
ANISOU  299  O   SER A  35     1778   1727   1374     -6   -200   -343       O  
ATOM    300  CB  SER A  35      18.906  13.382  -1.619  1.00 13.93           C  
ANISOU  300  CB  SER A  35     1605   2005   1681   -139   -235      0       C  
ATOM    301  OG  SER A  35      19.541  12.395  -0.833  1.00 19.15           O  
ANISOU  301  OG  SER A  35     2408   2632   2236     95   -267    602       O  
ATOM    302  N   HIS A  36      18.795  15.870  -3.721  1.00 10.78           N  
ANISOU  302  N   HIS A  36     1347   1667   1081    114    -48   -221       N  
ATOM    303  CA  HIS A  36      17.898  16.698  -4.509  1.00 11.64           C  
ANISOU  303  CA  HIS A  36     1238   2107   1076    114   -167    -76       C  
ATOM    304  C   HIS A  36      18.635  17.958  -4.925  1.00 11.16           C  
ANISOU  304  C   HIS A  36     1239   1853   1150    253    -74   -147       C  
ATOM    305  O   HIS A  36      18.441  19.015  -4.362  1.00 11.68           O  
ANISOU  305  O   HIS A  36     1408   2020   1009    266    -35   -194       O  
ATOM    306  CB  HIS A  36      16.602  17.044  -3.740  1.00 12.16           C  
ANISOU  306  CB  HIS A  36     1367   2174   1078    282    -56    -57       C  
ATOM    307  CG  HIS A  36      15.908  15.823  -3.232  1.00 13.59           C  
ANISOU  307  CG  HIS A  36     1438   2295   1430    187    129    -83       C  
ATOM    308  ND1 HIS A  36      15.076  15.040  -4.001  1.00 14.97           N  
ANISOU  308  ND1 HIS A  36     1504   2498   1686      1    277   -310       N  
ATOM    309  CD2 HIS A  36      15.967  15.226  -2.006  1.00 14.12           C  
ANISOU  309  CD2 HIS A  36     1424   2293   1647    312    183    184       C  
ATOM    310  CE1 HIS A  36      14.635  14.026  -3.250  1.00 16.01           C  
ANISOU  310  CE1 HIS A  36     1388   2721   1974    -41    392   -112       C  
ATOM    311  NE2 HIS A  36      15.156  14.123  -2.061  1.00 16.25           N  
ANISOU  311  NE2 HIS A  36     1908   2382   1885     58    409    -60       N  
ATOM    312  N   PRO A  37      19.509  17.898  -5.934  1.00 11.07           N  
ANISOU  312  N   PRO A  37     1046   1948   1211    118   -105   -283       N  
ATOM    313  CA  PRO A  37      20.349  19.061  -6.275  1.00 11.54           C  
ANISOU  313  CA  PRO A  37     1239   1996   1150     88    -63   -281       C  
ATOM    314  C   PRO A  37      19.621  20.302  -6.669  1.00 12.20           C  
ANISOU  314  C   PRO A  37     1319   2048   1270     38    176      0       C  
ATOM    315  O   PRO A  37      20.192  21.404  -6.567  1.00 12.89           O  
ANISOU  315  O   PRO A  37     1352   2032   1514     47    242    -91       O  
ATOM    316  CB  PRO A  37      21.242  18.507  -7.394  1.00 13.76           C  
ANISOU  316  CB  PRO A  37     1403   2119   1707    -19    318   -480       C  
ATOM    317  CG  PRO A  37      21.280  16.988  -7.173  1.00 13.89           C  
ANISOU  317  CG  PRO A  37     1324   2135   1820    186    101   -439       C  
ATOM    318  CD  PRO A  37      19.876  16.671  -6.685  1.00 12.29           C  
ANISOU  318  CD  PRO A  37     1329   1982   1356    127     38   -313       C  
ATOM    319  N   GLU A  38      18.369  20.217  -7.127  1.00 11.76           N  
ANISOU  319  N   GLU A  38     1475   1874   1118    181    -75      2       N  
ATOM    320  CA  GLU A  38      17.573  21.412  -7.388  1.00 12.59           C  
ANISOU  320  CA  GLU A  38     1657   1919   1209    120   -149    124       C  
ATOM    321  C   GLU A  38      17.394  22.260  -6.140  1.00 12.54           C  
ANISOU  321  C   GLU A  38     1539   1857   1368    385   -285     14       C  
ATOM    322  O   GLU A  38      17.244  23.494  -6.318  1.00 15.08           O  
ANISOU  322  O   GLU A  38     2330   1918   1480    390   -284    126       O  
ATOM    323  CB  GLU A  38      16.216  21.034  -7.967  1.00 14.52           C  
ANISOU  323  CB  GLU A  38     1740   2147   1628    438   -512   -195       C  
ATOM    324  CG  GLU A  38      15.251  20.293  -7.099  1.00 14.79           C  
ANISOU  324  CG  GLU A  38     1192   2445   1983    363   -269   -604       C  
ATOM    325  CD  GLU A  38      15.402  18.787  -7.067  1.00 12.96           C  
ANISOU  325  CD  GLU A  38     1243   2522   1160    139   -263   -117       C  
ATOM    326  OE1 GLU A  38      16.553  18.262  -7.094  1.00 13.04           O  
ANISOU  326  OE1 GLU A  38     1316   2391   1247    279   -228   -202       O  
ATOM    327  OE2 GLU A  38      14.353  18.129  -6.971  1.00 14.64           O  
ANISOU  327  OE2 GLU A  38     1326   2685   1550     58   -146   -226       O  
ATOM    328  N   THR A  39      17.482  21.681  -4.979  1.00 11.02           N  
ANISOU  328  N   THR A  39     1025   1916   1247    167   -138    -55       N  
ATOM    329  CA  THR A  39      17.327  22.447  -3.767  1.00 10.84           C  
ANISOU  329  CA  THR A  39     1085   1692   1343    110     -1    -69       C  
ATOM    330  C   THR A  39      18.486  23.428  -3.527  1.00 11.03           C  
ANISOU  330  C   THR A  39     1178   1666   1347     -6    -23    114       C  
ATOM    331  O   THR A  39      18.320  24.537  -3.059  1.00 11.69           O  
ANISOU  331  O   THR A  39     1267   1744   1432     -1     96    -24       O  
ATOM    332  CB  THR A  39      17.087  21.547  -2.543  1.00 10.75           C  
ANISOU  332  CB  THR A  39     1040   1727   1319     52    143   -108       C  
ATOM    333  OG1 THR A  39      18.239  20.735  -2.267  1.00 10.84           O  
ANISOU  333  OG1 THR A  39     1091   1794   1235      5    -99     -8       O  
ATOM    334  CG2 THR A  39      15.825  20.710  -2.709  1.00 11.97           C  
ANISOU  334  CG2 THR A  39     1113   1929   1506   -139     60   -160       C  
ATOM    335  N   LEU A  40      19.698  22.939  -3.873  1.00 12.58           N  
ANISOU  335  N   LEU A  40     1091   2019   1671    -53    -43   -263       N  
ATOM    336  CA  LEU A  40      20.906  23.739  -3.662  1.00 12.74           C  
ANISOU  336  CA  LEU A  40     1095   2068   1678    -80     27   -250       C  
ATOM    337  C   LEU A  40      20.808  24.987  -4.496  1.00 12.54           C  
ANISOU  337  C   LEU A  40      846   2376   1544   -116    100    -32       C  
ATOM    338  O   LEU A  40      21.250  26.101  -4.082  1.00 13.73           O  
ANISOU  338  O   LEU A  40     1379   2267   1571   -321     27    185       O  
ATOM    339  CB  LEU A  40      22.119  22.866  -4.045  1.00 13.26           C  
ANISOU  339  CB  LEU A  40     1133   2166   1740    -51    -65   -413       C  
ATOM    340  CG  LEU A  40      23.477  23.546  -3.965  1.00 13.19           C  
ANISOU  340  CG  LEU A  40     1110   2307   1594   -187     37    161       C  
ATOM    341  CD1 LEU A  40      23.727  24.031  -2.568  1.00 18.11           C  
ANISOU  341  CD1 LEU A  40     1486   3602   1792  -1078     76   -405       C  
ATOM    342  CD2 LEU A  40      24.565  22.594  -4.462  1.00 19.64           C  
ANISOU  342  CD2 LEU A  40     1231   3416   2814    266    107   -421       C  
ATOM    343  N   GLU A  41      20.210  24.889  -5.673  1.00 15.05           N  
ANISOU  343  N   GLU A  41     1374   2902   1442   -497    101     36       N  
ATOM    344  CA  GLU A  41      20.122  25.985  -6.601  1.00 17.96           C  
ANISOU  344  CA  GLU A  41     1541   3588   1693   -232    -12    463       C  
ATOM    345  C   GLU A  41      19.278  27.125  -6.079  1.00 16.77           C  
ANISOU  345  C   GLU A  41     1613   3122   1637   -394   -100    582       C  
ATOM    346  O   GLU A  41      19.411  28.240  -6.526  1.00 20.22           O  
ANISOU  346  O   GLU A  41     2362   3400   1922   -456    246   1048       O  
ATOM    347  CB AGLU A  41      19.555  25.404  -7.903  0.54 18.88           C  
ANISOU  347  CB AGLU A  41     2193   3341   1641   -472    -23    494       C  
ATOM    348  CB BGLU A  41      19.644  25.490  -7.974  0.46 18.78           C  
ANISOU  348  CB BGLU A  41     2247   3109   1780   -392   -207    493       C  
ATOM    349  CG AGLU A  41      19.355  26.286  -9.087  0.54 21.99           C  
ANISOU  349  CG AGLU A  41     2376   4221   1757   -250    -40    842       C  
ATOM    350  CG BGLU A  41      20.089  26.400  -9.096  0.46 20.68           C  
ANISOU  350  CG BGLU A  41     2345   3788   1724    172    554    572       C  
ATOM    351  CD AGLU A  41      20.586  26.549  -9.917  0.54 24.00           C  
ANISOU  351  CD AGLU A  41     2957   3950   2211   -289    513    994       C  
ATOM    352  CD BGLU A  41      21.587  26.583  -9.232  0.46 24.35           C  
ANISOU  352  CD BGLU A  41     2469   4567   2216   -461    482    338       C  
ATOM    353  OE1AGLU A  41      21.708  26.469  -9.360  0.54 22.53           O  
ANISOU  353  OE1AGLU A  41     2639   4293   1626   -398    978    726       O  
ATOM    354  OE1BGLU A  41      22.381  25.838  -8.630  0.46 27.28           O  
ANISOU  354  OE1BGLU A  41     2279   4854   3232    313    451   -234       O  
ATOM    355  OE2AGLU A  41      20.442  26.855 -11.136  0.54 21.33           O  
ANISOU  355  OE2AGLU A  41     3163   3005   1938   -558    405    294       O  
ATOM    356  OE2BGLU A  41      21.901  27.522 -10.003  0.46 28.89           O  
ANISOU  356  OE2BGLU A  41     3664   4950   2364  -1376    849    200       O  
ATOM    357  N   LYS A  42      18.395  26.865  -5.091  1.00 15.63           N  
ANISOU  357  N   LYS A  42     1174   2885   1878    -53   -141    932       N  
ATOM    358  CA  LYS A  42      17.614  27.899  -4.447  1.00 15.69           C  
ANISOU  358  CA  LYS A  42     1179   2887   1896     93   -160   1130       C  
ATOM    359  C   LYS A  42      18.410  28.797  -3.504  1.00 15.56           C  
ANISOU  359  C   LYS A  42     1130   2638   2145    245    -71    964       C  
ATOM    360  O   LYS A  42      17.910  29.831  -3.034  1.00 17.53           O  
ANISOU  360  O   LYS A  42     1248   2412   2999    315   -138   1003       O  
ATOM    361  CB  LYS A  42      16.407  27.296  -3.693  1.00 17.00           C  
ANISOU  361  CB  LYS A  42     1291   2893   2277     -3      5   1082       C  
ATOM    362  CG  LYS A  42      15.344  26.658  -4.544  1.00 18.44           C  
ANISOU  362  CG  LYS A  42     1165   3253   2588     -3    -31    920       C  
ATOM    363  CD  LYS A  42      14.532  27.707  -5.300  1.00 21.35           C  
ANISOU  363  CD  LYS A  42     1425   3532   3157   -298   -502   1293       C  
ATOM    364  CE  LYS A  42      13.510  27.042  -6.206  1.00 22.84           C  
ANISOU  364  CE  LYS A  42     1794   3767   3117    -83   -619    845       C  
ATOM    365  NZ  LYS A  42      12.571  28.017  -6.821  1.00 23.31           N  
ANISOU  365  NZ  LYS A  42     1834   4551   2470    -20   -515   1255       N  
ATOM    366  N   PHE A  43      19.628  28.411  -3.168  1.00 13.55           N  
ANISOU  366  N   PHE A  43     1111   2289   1750    176    -19    692       N  
ATOM    367  CA  PHE A  43      20.491  29.155  -2.266  1.00 12.82           C  
ANISOU  367  CA  PHE A  43     1228   2079   1563    378    136    395       C  
ATOM    368  C   PHE A  43      21.588  29.873  -3.018  1.00 13.05           C  
ANISOU  368  C   PHE A  43     1271   1872   1817    207    -52    489       C  
ATOM    369  O   PHE A  43      22.623  29.246  -3.287  1.00 12.13           O  
ANISOU  369  O   PHE A  43     1072   1840   1695    -36    -99    400       O  
ATOM    370  CB APHE A  43      21.138  28.326  -1.148  0.54 13.33           C  
ANISOU  370  CB APHE A  43     1095   2283   1688    229      6    504       C  
ATOM    371  CB BPHE A  43      21.107  28.204  -1.235  0.46 12.43           C  
ANISOU  371  CB BPHE A  43     1285   1918   1520    308     29    285       C  
ATOM    372  CG APHE A  43      20.164  27.778  -0.102  0.54 11.73           C  
ANISOU  372  CG APHE A  43      932   2235   1291    262   -176    359       C  
ATOM    373  CG BPHE A  43      20.126  27.442  -0.348  0.46 10.59           C  
ANISOU  373  CG BPHE A  43     1177   1391   1456    379    -31     65       C  
ATOM    374  CD1APHE A  43      19.528  26.591  -0.346  0.54 12.33           C  
ANISOU  374  CD1APHE A  43     1096   2169   1419    270    268    116       C  
ATOM    375  CD1BPHE A  43      19.524  26.263  -0.766  0.46 10.91           C  
ANISOU  375  CD1BPHE A  43     1269   1490   1385    435     21   -132       C  
ATOM    376  CD2APHE A  43      19.963  28.454   1.063  0.54 13.16           C  
ANISOU  376  CD2APHE A  43     1322   2021   1658    260    -39    163       C  
ATOM    377  CD2BPHE A  43      19.884  27.949   0.902  0.46 11.05           C  
ANISOU  377  CD2BPHE A  43     1067   1744   1386   -211   -145    -95       C  
ATOM    378  CE1APHE A  43      18.682  26.025   0.592  0.54 12.53           C  
ANISOU  378  CE1APHE A  43     1037   2084   1639    456    489     94       C  
ATOM    379  CE1BPHE A  43      18.684  25.566   0.121  0.46 13.29           C  
ANISOU  379  CE1BPHE A  43     1461   1859   1731     -7     -7    -36       C  
ATOM    380  CE2APHE A  43      19.094  27.900   2.007  0.54 13.14           C  
ANISOU  380  CE2APHE A  43     1211   2508   1274    314   -144     87       C  
ATOM    381  CE2BPHE A  43      19.044  27.272   1.787  0.46 10.84           C  
ANISOU  381  CE2BPHE A  43      897   1694   1530     93    -84    168       C  
ATOM    382  CZ APHE A  43      18.455  26.706   1.748  0.54 12.26           C  
ANISOU  382  CZ APHE A  43      714   2323   1622    485    393    113       C  
ATOM    383  CZ BPHE A  43      18.461  26.093   1.368  0.46 11.15           C  
ANISOU  383  CZ BPHE A  43     1072   1528   1635     94    148    168       C  
ATOM    384  N   ASP A  44      21.437  31.147  -3.318  1.00 15.77           N  
ANISOU  384  N   ASP A  44     1567   2043   2384    322     75    783       N  
ATOM    385  CA  ASP A  44      22.544  31.869  -3.932  1.00 16.47           C  
ANISOU  385  CA  ASP A  44     1672   1969   2616    180    163    714       C  
ATOM    386  C  AASP A  44      23.758  31.742  -3.013  0.62 18.30           C  
ANISOU  386  C  AASP A  44     1864   2132   2956   -265    -85    975       C  
ATOM    387  C  BASP A  44      23.871  31.755  -3.195  0.38 18.75           C  
ANISOU  387  C  BASP A  44     2012   1899   3212   -390   -423    792       C  
ATOM    388  O  AASP A  44      24.926  31.718  -3.371  0.62 21.31           O  
ANISOU  388  O  AASP A  44     1788   2706   3601   -153    -12   1547       O  
ATOM    389  O  BASP A  44      24.888  31.692  -3.888  0.38 17.70           O  
ANISOU  389  O  BASP A  44     1658   2205   2862   -512   -760   1253       O  
ATOM    390  CB  ASP A  44      22.143  33.330  -4.128  1.00 22.20           C  
ANISOU  390  CB  ASP A  44     2754   1991   3691    126   -200   1068       C  
ATOM    391  CG  ASP A  44      21.166  33.573  -5.248  1.00 27.77           C  
ANISOU  391  CG  ASP A  44     3558   2501   4490    214   -877   1628       C  
ATOM    392  OD1 ASP A  44      20.889  32.667  -6.057  1.00 28.61           O  
ANISOU  392  OD1 ASP A  44     3727   3698   3446    899   -782   1151       O  
ATOM    393  OD2 ASP A  44      20.767  34.754  -5.305  1.00 35.69           O  
ANISOU  393  OD2 ASP A  44     4278   2879   6403    845  -1295   1598       O  
ATOM    394  N  AARG A  45      23.412  31.660  -1.733  0.62 16.64           N  
ANISOU  394  N  AARG A  45     2103   1404   2815     37   -219    380       N  
ATOM    395  N  BARG A  45      23.874  31.742  -1.873  0.38 16.77           N  
ANISOU  395  N  BARG A  45     1635   1512   3224    -71   -469    -81       N  
ATOM    396  CA AARG A  45      24.341  31.598  -0.631  0.62 15.97           C  
ANISOU  396  CA AARG A  45     1881   1308   2880   -541   -157    244       C  
ATOM    397  CA BARG A  45      25.113  31.653  -1.116  0.38 17.04           C  
ANISOU  397  CA BARG A  45     1579   1508   3388   -550   -546    -59       C  
ATOM    398  C  AARG A  45      25.232  30.357  -0.688  0.62 15.73           C  
ANISOU  398  C  AARG A  45     1583   1486   2906   -501   -473    431       C  
ATOM    399  C  BARG A  45      25.789  30.293  -1.141  0.38 14.13           C  
ANISOU  399  C  BARG A  45     1024   1600   2744   -595    -60    600       C  
ATOM    400  O  AARG A  45      26.356  30.433  -0.147  0.62 17.06           O  
ANISOU  400  O  AARG A  45     1646   2177   2660   -660   -440    558       O  
ATOM    401  O  BARG A  45      26.976  30.147  -0.823  0.38 17.78           O  
ANISOU  401  O  BARG A  45     1530   1736   3489   -694  -1102    550       O  
ATOM    402  CB AARG A  45      23.578  31.610   0.690  0.62 18.40           C  
ANISOU  402  CB AARG A  45     2253   1956   2783   -460    -76    261       C  
ATOM    403  CB BARG A  45      24.855  31.998   0.354  0.38 18.43           C  
ANISOU  403  CB BARG A  45     1840   1880   3281    -53   -630     81       C  
ATOM    404  CG AARG A  45      24.339  31.969   1.925  0.62 17.49           C  
ANISOU  404  CG AARG A  45     1380   2348   2917   -485     87    304       C  
ATOM    405  CG BARG A  45      23.918  31.058   1.078  0.38 16.97           C  
ANISOU  405  CG BARG A  45     1362   1968   3116    114   -792    174       C  
ATOM    406  CD AARG A  45      23.391  32.292   3.091  0.62 16.95           C  
ANISOU  406  CD AARG A  45     1802   1676   2962    129    -81    -41       C  
ATOM    407  CD BARG A  45      23.612  31.615   2.472  0.38 19.89           C  
ANISOU  407  CD BARG A  45     1973   2278   3308    313   -483    101       C  
ATOM    408  NE AARG A  45      24.080  32.172   4.360  0.62 17.21           N  
ANISOU  408  NE AARG A  45     1245   2257   3039    344    -54   -142       N  
ATOM    409  NE BARG A  45      23.115  32.990   2.347  0.38 23.31           N  
ANISOU  409  NE BARG A  45     2655   2715   3485   1121   -370    116       N  
ATOM    410  CZ AARG A  45      23.462  32.261   5.544  0.62 19.15           C  
ANISOU  410  CZ AARG A  45     1182   3107   2988    252   -140   -373       C  
ATOM    411  CZ BARG A  45      23.529  34.017   3.069  0.38 26.09           C  
ANISOU  411  CZ BARG A  45     3599   1963   4352    767   -806    637       C  
ATOM    412  NH1AARG A  45      22.177  32.489   5.690  0.62 25.59           N  
ANISOU  412  NH1AARG A  45     1495   4972   3256   1158    104   -193       N  
ATOM    413  NH1BARG A  45      24.459  33.809   3.991  0.38 24.55           N  
ANISOU  413  NH1BARG A  45     2276   2187   4867    571   -586    -56       N  
ATOM    414  NH2AARG A  45      24.195  32.127   6.654  0.62 27.38           N  
ANISOU  414  NH2AARG A  45     1130   6242   3030     99   -103    -53       N  
ATOM    415  NH2BARG A  45      23.040  35.233   2.906  0.38 29.85           N  
ANISOU  415  NH2BARG A  45     3533   2527   5281   1687    125    374       N  
ATOM    416  N  APHE A  46      24.811  29.238  -1.314  0.62 14.05           N  
ANISOU  416  N  APHE A  46     1534   1362   2443   -293   -128    408       N  
ATOM    417  N  BPHE A  46      24.958  29.283  -1.457  0.38 13.32           N  
ANISOU  417  N  BPHE A  46     1291   1374   2398   -322   -678    323       N  
ATOM    418  CA  PHE A  46      25.500  27.952  -1.293  1.00 13.73           C  
ANISOU  418  CA  PHE A  46     1094   1576   2548   -154    -60    502       C  
ATOM    419  C   PHE A  46      25.742  27.338  -2.662  1.00 14.20           C  
ANISOU  419  C   PHE A  46     1113   1648   2634    -60   -134    398       C  
ATOM    420  O   PHE A  46      26.415  26.282  -2.756  1.00 15.60           O  
ANISOU  420  O   PHE A  46     1145   1685   3097    -18    137    487       O  
ATOM    421  CB  PHE A  46      24.719  26.983  -0.408  1.00 14.08           C  
ANISOU  421  CB  PHE A  46     1094   1436   2820    -80   -100    584       C  
ATOM    422  CG  PHE A  46      24.523  27.495   1.008  1.00 15.24           C  
ANISOU  422  CG  PHE A  46     1140   2109   2540    -88   -166    918       C  
ATOM    423  CD1 PHE A  46      25.610  27.940   1.750  1.00 14.61           C  
ANISOU  423  CD1 PHE A  46     1167   1520   2865   -128     55    309       C  
ATOM    424  CD2 PHE A  46      23.285  27.487   1.615  1.00 17.37           C  
ANISOU  424  CD2 PHE A  46     1106   3182   2313    -41   -169   1247       C  
ATOM    425  CE1 PHE A  46      25.451  28.424   3.026  1.00 15.97           C  
ANISOU  425  CE1 PHE A  46     1588   1860   2620   -134    155    560       C  
ATOM    426  CE2 PHE A  46      23.164  27.975   2.897  1.00 18.23           C  
ANISOU  426  CE2 PHE A  46     1622   3096   2208   -177     -1   1381       C  
ATOM    427  CZ  PHE A  46      24.207  28.434   3.646  1.00 16.95           C  
ANISOU  427  CZ  PHE A  46     1580   2503   2357    121     92    996       C  
ATOM    428  N   LYS A  47      25.235  27.900  -3.703  1.00 15.98           N  
ANISOU  428  N   LYS A  47     1961   1530   2579    206   -533    -41       N  
ATOM    429  CA  LYS A  47      25.263  27.151  -4.946  1.00 18.99           C  
ANISOU  429  CA  LYS A  47     2253   2185   2777    292   -590   -278       C  
ATOM    430  C   LYS A  47      26.678  27.100  -5.532  1.00 18.19           C  
ANISOU  430  C   LYS A  47     2563   2934   1415   -221   -504     -8       C  
ATOM    431  O   LYS A  47      26.970  26.269  -6.432  1.00 20.28           O  
ANISOU  431  O   LYS A  47     2956   2904   1847   -116   -278   -151       O  
ATOM    432  CB ALYS A  47      24.111  27.621  -5.790  0.75 20.36           C  
ANISOU  432  CB ALYS A  47     2476   3073   2186   -418   -477    650       C  
ATOM    433  CB BLYS A  47      24.274  27.743  -5.944  0.25 20.95           C  
ANISOU  433  CB BLYS A  47     2819   2835   2304    233   -461    236       C  
ATOM    434  CG ALYS A  47      24.297  29.022  -6.352  0.75 21.50           C  
ANISOU  434  CG ALYS A  47     3394   2860   1916    379    199    519       C  
ATOM    435  CG BLYS A  47      24.514  29.207  -6.276  0.25 23.29           C  
ANISOU  435  CG BLYS A  47     3746   3017   2086    152   -142    585       C  
ATOM    436  CD ALYS A  47      23.122  29.567  -7.123  0.75 24.25           C  
ANISOU  436  CD ALYS A  47     3616   3102   2495    389   -262    447       C  
ATOM    437  CD BLYS A  47      23.733  29.675  -7.494  0.25 24.11           C  
ANISOU  437  CD BLYS A  47     3793   3430   1937    257     -3    643       C  
ATOM    438  CE ALYS A  47      23.513  30.639  -8.111  0.75 29.05           C  
ANISOU  438  CE ALYS A  47     4373   3767   2898    654   -328   1195       C  
ATOM    439  CE BLYS A  47      23.292  31.123  -7.367  0.25 22.67           C  
ANISOU  439  CE BLYS A  47     4004   3478   1134    358     79    714       C  
ATOM    440  NZ ALYS A  47      22.328  31.225  -8.838  0.75 41.18           N  
ANISOU  440  NZ ALYS A  47     4927   5281   5437    941   -967   2569       N  
ATOM    441  NZ BLYS A  47      23.604  31.932  -8.578  0.25 35.68           N  
ANISOU  441  NZ BLYS A  47     5721   4723   3114  -1247   -658   2497       N  
ATOM    442  N   HIS A  48      27.682  27.770  -4.952  1.00 16.85           N  
ANISOU  442  N   HIS A  48     2373   1899   2131   -159   -228    340       N  
ATOM    443  CA  HIS A  48      29.072  27.559  -5.338  1.00 17.73           C  
ANISOU  443  CA  HIS A  48     2509   2033   2192   -406    163    601       C  
ATOM    444  C   HIS A  48      29.684  26.250  -4.862  1.00 16.71           C  
ANISOU  444  C   HIS A  48     2432   1861   2054    -62    749    201       C  
ATOM    445  O   HIS A  48      30.769  25.831  -5.257  1.00 21.26           O  
ANISOU  445  O   HIS A  48     2694   2127   3257   -196   1593    156       O  
ATOM    446  CB  HIS A  48      30.001  28.675  -4.821  1.00 16.57           C  
ANISOU  446  CB  HIS A  48     2324   1905   2068   -181    130    462       C  
ATOM    447  CG  HIS A  48      30.169  28.708  -3.333  1.00 15.78           C  
ANISOU  447  CG  HIS A  48     2085   1828   2083   -255    175    673       C  
ATOM    448  ND1 HIS A  48      29.282  29.318  -2.500  1.00 17.25           N  
ANISOU  448  ND1 HIS A  48     2813   1644   2098    147    -35    264       N  
ATOM    449  CD2 HIS A  48      31.204  28.172  -2.577  1.00 15.91           C  
ANISOU  449  CD2 HIS A  48     1888   1916   2242   -489    -42    457       C  
ATOM    450  CE1 HIS A  48      29.755  29.157  -1.249  1.00 18.79           C  
ANISOU  450  CE1 HIS A  48     3176   1815   2148    250   -195    215       C  
ATOM    451  NE2 HIS A  48      30.899  28.464  -1.274  1.00 16.64           N  
ANISOU  451  NE2 HIS A  48     2233   1882   2207   -517   -139    370       N  
ATOM    452  N   LEU A  49      29.015  25.583  -3.914  1.00 14.19           N  
ANISOU  452  N   LEU A  49     1350   1743   2298    142    343    461       N  
ATOM    453  CA  LEU A  49      29.475  24.308  -3.385  1.00 12.89           C  
ANISOU  453  CA  LEU A  49     1231   1541   2125    -61     71    133       C  
ATOM    454  C   LEU A  49      29.195  23.164  -4.348  1.00 14.41           C  
ANISOU  454  C   LEU A  49     1285   1778   2412   -392    328   -101       C  
ATOM    455  O   LEU A  49      28.066  22.956  -4.728  1.00 19.22           O  
ANISOU  455  O   LEU A  49     1466   2836   3003   -331     18   -584       O  
ATOM    456  CB  LEU A  49      28.811  24.113  -2.038  1.00 14.04           C  
ANISOU  456  CB  LEU A  49     1488   1748   2098    -85    121    235       C  
ATOM    457  CG  LEU A  49      29.054  25.182  -0.977  1.00 12.75           C  
ANISOU  457  CG  LEU A  49     1333   1533   1979    285    195    369       C  
ATOM    458  CD1 LEU A  49      28.113  25.040   0.203  1.00 14.16           C  
ANISOU  458  CD1 LEU A  49     1461   2188   1733     86     60    581       C  
ATOM    459  CD2 LEU A  49      30.518  25.165  -0.485  1.00 13.83           C  
ANISOU  459  CD2 LEU A  49     1447   1998   1810     49    -28    347       C  
ATOM    460  N   LYS A  50      30.237  22.443  -4.776  1.00 13.87           N  
ANISOU  460  N   LYS A  50     1706   1415   2149    159   -149    235       N  
ATOM    461  CA  LYS A  50      30.156  21.459  -5.826  1.00 15.89           C  
ANISOU  461  CA  LYS A  50     1977   1647   2413    457   -372     16       C  
ATOM    462  C   LYS A  50      30.431  20.034  -5.338  1.00 15.89           C  
ANISOU  462  C   LYS A  50     1859   1465   2715    140   -726     62       C  
ATOM    463  O   LYS A  50      30.207  19.074  -6.116  1.00 17.37           O  
ANISOU  463  O   LYS A  50     2258   1838   2505     -4   -522    -77       O  
ATOM    464  CB  LYS A  50      31.204  21.783  -6.904  1.00 21.90           C  
ANISOU  464  CB  LYS A  50     3905   2164   2254     46    377    -63       C  
ATOM    465  CG  LYS A  50      31.183  23.074  -7.680  1.00 27.59           C  
ANISOU  465  CG  LYS A  50     4615   2644   3224     87    465    604       C  
ATOM    466  CD  LYS A  50      29.785  23.573  -7.963  1.00 34.02           C  
ANISOU  466  CD  LYS A  50     5284   3314   4327    770   -414    553       C  
ATOM    467  CE  LYS A  50      29.928  24.978  -8.551  1.00 36.68           C  
ANISOU  467  CE  LYS A  50     5671   3511   4757    730   -505    828       C  
ATOM    468  NZ  LYS A  50      28.606  25.526  -8.999  1.00 43.52           N  
ANISOU  468  NZ  LYS A  50     5512   5512   5512      0      0      0       N  
ATOM    469  N   THR A  51      31.024  19.876  -4.148  1.00 11.54           N  
ANISOU  469  N   THR A  51     1169   1324   1890    156    310     71       N  
ATOM    470  CA  THR A  51      31.362  18.570  -3.563  1.00 10.95           C  
ANISOU  470  CA  THR A  51     1204   1145   1811     62    183    -19       C  
ATOM    471  C   THR A  51      30.855  18.521  -2.114  1.00  9.82           C  
ANISOU  471  C   THR A  51      865   1152   1712    150     19   -162       C  
ATOM    472  O   THR A  51      30.716  19.519  -1.456  1.00 10.16           O  
ANISOU  472  O   THR A  51      973   1072   1815     34     10   -172       O  
ATOM    473  CB  THR A  51      32.869  18.274  -3.568  1.00 11.67           C  
ANISOU  473  CB  THR A  51     1152   1316   1967    174    320   -231       C  
ATOM    474  OG1 THR A  51      33.483  19.095  -2.601  1.00 11.72           O  
ANISOU  474  OG1 THR A  51     1059   1472   1922    137    190    -74       O  
ATOM    475  CG2 THR A  51      33.473  18.511  -4.924  1.00 12.90           C  
ANISOU  475  CG2 THR A  51     1293   1673   1937     40    271    -90       C  
ATOM    476  N   GLU A  52      30.673  17.263  -1.661  1.00 10.29           N  
ANISOU  476  N   GLU A  52     1081   1152   1677    122    107    -77       N  
ATOM    477  CA  GLU A  52      30.337  17.093  -0.264  1.00 10.06           C  
ANISOU  477  CA  GLU A  52     1072   1030   1721    152    149   -283       C  
ATOM    478  C   GLU A  52      31.414  17.639   0.662  1.00  9.66           C  
ANISOU  478  C   GLU A  52     1053    998   1619     -2     47    181       C  
ATOM    479  O   GLU A  52      31.101  18.227   1.718  1.00 10.85           O  
ANISOU  479  O   GLU A  52     1093   1241   1788    -20     55   -138       O  
ATOM    480  CB  GLU A  52      30.070  15.611   0.017  1.00 10.90           C  
ANISOU  480  CB  GLU A  52     1122   1215   1803     -2    222   -128       C  
ATOM    481  CG  GLU A  52      29.656  15.306   1.395  1.00 12.75           C  
ANISOU  481  CG  GLU A  52     1581   1430   1832     58    562   -202       C  
ATOM    482  CD  GLU A  52      29.114  13.905   1.625  1.00 14.66           C  
ANISOU  482  CD  GLU A  52     1753   1449   2366     55    762    -24       C  
ATOM    483  OE1 GLU A  52      29.077  13.103   0.694  1.00 17.72           O  
ANISOU  483  OE1 GLU A  52     2440   1489   2805   -260    920   -316       O  
ATOM    484  OE2 GLU A  52      28.718  13.652   2.779  1.00 20.63           O  
ANISOU  484  OE2 GLU A  52     3248   2028   2562   -475   1084     66       O  
ATOM    485  N   ALA A  53      32.692  17.444   0.351  1.00 10.41           N  
ANISOU  485  N   ALA A  53     1095   1104   1757     42    -20    -75       N  
ATOM    486  CA  ALA A  53      33.751  17.996   1.213  1.00 10.97           C  
ANISOU  486  CA  ALA A  53     1115   1190   1864     70    -90    -32       C  
ATOM    487  C   ALA A  53      33.652  19.510   1.249  1.00 10.34           C  
ANISOU  487  C   ALA A  53      839   1166   1924      6    -67     -3       C  
ATOM    488  O   ALA A  53      33.831  20.082   2.339  1.00 11.22           O  
ANISOU  488  O   ALA A  53     1014   1306   1943     68   -194   -126       O  
ATOM    489  CB  ALA A  53      35.130  17.607   0.647  1.00 13.40           C  
ANISOU  489  CB  ALA A  53     1086   1545   2461    372   -218   -238       C  
ATOM    490  N   GLU A  54      33.360  20.187   0.158  1.00 10.47           N  
ANISOU  490  N   GLU A  54      869   1170   1938    -30    -26     26       N  
ATOM    491  CA  GLU A  54      33.228  21.636   0.201  1.00 10.16           C  
ANISOU  491  CA  GLU A  54      918   1144   1799     19    -38      7       C  
ATOM    492  C   GLU A  54      32.022  22.019   1.093  1.00  9.41           C  
ANISOU  492  C   GLU A  54      882   1085   1608    -25   -140     12       C  
ATOM    493  O   GLU A  54      32.115  22.970   1.885  1.00 10.11           O  
ANISOU  493  O   GLU A  54      922   1132   1788   -137      4    -79       O  
ATOM    494  CB  GLU A  54      33.000  22.213  -1.195  1.00 10.77           C  
ANISOU  494  CB  GLU A  54     1039   1264   1790    -20    175     72       C  
ATOM    495  CG  GLU A  54      34.239  22.189  -2.057  1.00 12.59           C  
ANISOU  495  CG  GLU A  54     1260   1294   2229   -302    383    -87       C  
ATOM    496  CD  GLU A  54      34.009  22.528  -3.477  1.00 14.67           C  
ANISOU  496  CD  GLU A  54     1609   1867   2097   -182    575    -11       C  
ATOM    497  OE1 GLU A  54      32.863  22.791  -3.888  1.00 19.99           O  
ANISOU  497  OE1 GLU A  54     1716   3943   1937      1    344    119       O  
ATOM    498  OE2 GLU A  54      34.966  22.585  -4.286  1.00 21.92           O  
ANISOU  498  OE2 GLU A  54     2123   3336   2867     42   1266    178       O  
ATOM    499  N   MET A  55      30.915  21.282   0.982  1.00  9.30           N  
ANISOU  499  N   MET A  55      803   1096   1636     47    -43   -106       N  
ATOM    500  CA  MET A  55      29.776  21.550   1.849  1.00  9.20           C  
ANISOU  500  CA  MET A  55      900   1139   1454      4    -38   -162       C  
ATOM    501  C   MET A  55      30.129  21.393   3.304  1.00  9.34           C  
ANISOU  501  C   MET A  55      720   1271   1557    -47   -112    -96       C  
ATOM    502  O   MET A  55      29.751  22.231   4.150  1.00 10.11           O  
ANISOU  502  O   MET A  55      980   1441   1422    -84   -131   -104       O  
ATOM    503  CB  MET A  55      28.607  20.635   1.466  1.00  8.86           C  
ANISOU  503  CB  MET A  55      896   1241   1228   -145     35    -11       C  
ATOM    504  CG  MET A  55      28.086  20.866   0.071  1.00  9.30           C  
ANISOU  504  CG  MET A  55      754   1342   1439    -46    -13    108       C  
ATOM    505  SD  MET A  55      26.859  19.577  -0.350  1.00 11.61           S  
ANISOU  505  SD  MET A  55      985   1856   1572   -202   -135   -219       S  
ATOM    506  CE  MET A  55      26.639  19.933  -2.085  1.00 14.79           C  
ANISOU  506  CE  MET A  55     1313   2748   1560    -95   -222   -242       C  
ATOM    507  N   LYS A  56      30.823  20.319   3.652  1.00  9.80           N  
ANISOU  507  N   LYS A  56     1023   1185   1514   -162   -125    -43       N  
ATOM    508  CA  LYS A  56      31.191  20.030   5.050  1.00 11.48           C  
ANISOU  508  CA  LYS A  56     1292   1519   1551   -154   -221     85       C  
ATOM    509  C   LYS A  56      32.146  21.095   5.590  1.00 10.99           C  
ANISOU  509  C   LYS A  56     1034   1485   1656     20   -294     19       C  
ATOM    510  O   LYS A  56      32.175  21.304   6.785  1.00 14.39           O  
ANISOU  510  O   LYS A  56     1600   2277   1591   -598   -397     60       O  
ATOM    511  CB ALYS A  56      31.789  18.618   5.149  0.54 13.08           C  
ANISOU  511  CB ALYS A  56     1785   1519   1664    -13   -559    -45       C  
ATOM    512  CB BLYS A  56      31.794  18.627   5.156  0.46 12.95           C  
ANISOU  512  CB BLYS A  56     1706   1476   1740    -81   -408     74       C  
ATOM    513  CG ALYS A  56      30.815  17.477   5.379  0.54 18.02           C  
ANISOU  513  CG ALYS A  56     2140   1515   3190    -79   -277    126       C  
ATOM    514  CG BLYS A  56      30.872  17.488   4.766  0.46 18.42           C  
ANISOU  514  CG BLYS A  56     2233   1599   3167   -437   -181   -144       C  
ATOM    515  CD ALYS A  56      31.382  16.117   5.028  0.54 21.45           C  
ANISOU  515  CD ALYS A  56     3076   1523   3552     33    -47     36       C  
ATOM    516  CD BLYS A  56      31.057  16.261   5.636  0.46 24.84           C  
ANISOU  516  CD BLYS A  56     3539   2172   3725  -1109   -236    692       C  
ATOM    517  CE ALYS A  56      30.458  15.010   5.520  0.54 22.26           C  
ANISOU  517  CE ALYS A  56     2868   1394   4196    291    469    -59       C  
ATOM    518  CE BLYS A  56      31.170  16.590   7.120  0.46 30.01           C  
ANISOU  518  CE BLYS A  56     5033   2570   3800   -182  -1010    555       C  
ATOM    519  NZ ALYS A  56      29.228  14.919   4.711  0.54 29.13           N  
ANISOU  519  NZ ALYS A  56     3105   5000   2961  -1174    943   -112       N  
ATOM    520  NZ BLYS A  56      30.794  18.021   7.334  0.46 39.03           N  
ANISOU  520  NZ BLYS A  56     8089   2249   4489   -534  -3857   -126       N  
ATOM    521  N   ALA A  57      32.941  21.726   4.739  1.00 10.73           N  
ANISOU  521  N   ALA A  57      998   1405   1674    -66   -339     10       N  
ATOM    522  CA  ALA A  57      33.947  22.727   5.129  1.00 11.18           C  
ANISOU  522  CA  ALA A  57     1017   1556   1675    -59   -369   -173       C  
ATOM    523  C   ALA A  57      33.329  24.119   5.220  1.00  9.95           C  
ANISOU  523  C   ALA A  57      962   1429   1391   -120   -192    -65       C  
ATOM    524  O   ALA A  57      34.070  25.046   5.557  1.00 12.75           O  
ANISOU  524  O   ALA A  57     1167   1575   2104   -257   -376   -212       O  
ATOM    525  CB  ALA A  57      35.102  22.737   4.160  1.00 13.36           C  
ANISOU  525  CB  ALA A  57      809   1668   2600    -26    -93   -339       C  
ATOM    526  N   SER A  58      32.084  24.339   4.827  1.00  9.60           N  
ANISOU  526  N   SER A  58      971   1227   1451   -177    -63    -15       N  
ATOM    527  CA  SER A  58      31.515  25.673   4.818  1.00  9.06           C  
ANISOU  527  CA  SER A  58     1095   1139   1207   -182    -13    -31       C  
ATOM    528  C   SER A  58      30.922  26.062   6.157  1.00  9.36           C  
ANISOU  528  C   SER A  58     1212   1265   1080   -245     89    191       C  
ATOM    529  O   SER A  58      29.912  25.459   6.605  1.00 10.03           O  
ANISOU  529  O   SER A  58     1173   1301   1337   -282    138    -92       O  
ATOM    530  CB  SER A  58      30.414  25.772   3.747  1.00  9.04           C  
ANISOU  530  CB  SER A  58     1052   1192   1192   -119     25     42       C  
ATOM    531  OG  SER A  58      29.719  26.978   3.843  1.00  9.63           O  
ANISOU  531  OG  SER A  58     1144   1235   1280    -71    104     29       O  
ATOM    532  N   GLU A  59      31.519  27.017   6.808  1.00 10.81           N  
ANISOU  532  N   GLU A  59     1181   1602   1324   -424    145   -137       N  
ATOM    533  CA  GLU A  59      30.993  27.500   8.094  1.00 11.28           C  
ANISOU  533  CA  GLU A  59     1391   1412   1481   -434    200   -102       C  
ATOM    534  C   GLU A  59      29.668  28.203   7.887  1.00 11.21           C  
ANISOU  534  C   GLU A  59     1380   1317   1563   -482    289   -179       C  
ATOM    535  O   GLU A  59      28.743  28.083   8.729  1.00 12.60           O  
ANISOU  535  O   GLU A  59     1408   1728   1651   -609    436   -382       O  
ATOM    536  CB  GLU A  59      32.022  28.438   8.786  1.00 13.59           C  
ANISOU  536  CB  GLU A  59     1528   2105   1532   -711    206   -383       C  
ATOM    537  CG  GLU A  59      31.602  28.733  10.204  1.00 13.11           C  
ANISOU  537  CG  GLU A  59     1334   2101   1547   -509     83   -341       C  
ATOM    538  CD  GLU A  59      31.625  27.584  11.162  1.00 13.58           C  
ANISOU  538  CD  GLU A  59     1662   2006   1494   -674     84   -355       C  
ATOM    539  OE1 GLU A  59      32.131  26.520  10.787  1.00 14.47           O  
ANISOU  539  OE1 GLU A  59     1965   2083   1449   -470     17   -308       O  
ATOM    540  OE2 GLU A  59      31.186  27.789  12.326  1.00 16.13           O  
ANISOU  540  OE2 GLU A  59     1983   2698   1448   -554    174   -421       O  
ATOM    541  N   ASP A  60      29.490  28.897   6.779  1.00 11.22           N  
ANISOU  541  N   ASP A  60     1319   1330   1613   -293    300   -208       N  
ATOM    542  CA  ASP A  60      28.219  29.557   6.488  1.00 12.76           C  
ANISOU  542  CA  ASP A  60     1425   1170   2254   -245    386    -44       C  
ATOM    543  C   ASP A  60      27.090  28.518   6.368  1.00 10.87           C  
ANISOU  543  C   ASP A  60     1129   1346   1656   -100    313    -98       C  
ATOM    544  O   ASP A  60      25.980  28.751   6.861  1.00 11.53           O  
ANISOU  544  O   ASP A  60     1173   1279   1929     62    386     73       O  
ATOM    545  CB  ASP A  60      28.378  30.360   5.210  1.00 14.24           C  
ANISOU  545  CB  ASP A  60     1127   1518   2766   -223    134    445       C  
ATOM    546  CG  ASP A  60      27.286  31.412   5.264  1.00 16.48           C  
ANISOU  546  CG  ASP A  60     1296   1637   3328   -108    -75    285       C  
ATOM    547  OD1 ASP A  60      27.081  32.116   6.308  1.00 20.58           O  
ANISOU  547  OD1 ASP A  60     2050   1825   3944    114    152    -98       O  
ATOM    548  OD2 ASP A  60      26.671  31.519   4.236  1.00 26.18           O  
ANISOU  548  OD2 ASP A  60     2721   1802   5424    418  -2606   -695       O  
ATOM    549  N   LEU A  61      27.353  27.385   5.753  1.00  9.95           N  
ANISOU  549  N   LEU A  61      975   1219   1586   -148    225    -16       N  
ATOM    550  CA  LEU A  61      26.346  26.319   5.644  1.00  9.18           C  
ANISOU  550  CA  LEU A  61      812   1251   1427    -36     59     62       C  
ATOM    551  C   LEU A  61      26.006  25.808   7.021  1.00  8.92           C  
ANISOU  551  C   LEU A  61      937   1104   1349   -110      0      1       C  
ATOM    552  O   LEU A  61      24.824  25.588   7.369  1.00  9.15           O  
ANISOU  552  O   LEU A  61      895   1325   1256   -166     37     11       O  
ATOM    553  CB ALEU A  61      26.819  25.227   4.682  0.67  9.16           C  
ANISOU  553  CB ALEU A  61      810   1267   1404   -107    -15     -6       C  
ATOM    554  CB BLEU A  61      26.877  25.193   4.746  0.33  9.12           C  
ANISOU  554  CB BLEU A  61      980   1138   1346    -93     65    105       C  
ATOM    555  CG ALEU A  61      25.747  24.105   4.468  0.67  9.70           C  
ANISOU  555  CG ALEU A  61      837   1394   1456   -193    -71     44       C  
ATOM    556  CG BLEU A  61      25.907  24.026   4.469  0.33  9.14           C  
ANISOU  556  CG BLEU A  61     1101   1424    949   -252    180    -16       C  
ATOM    557  CD1ALEU A  61      24.470  24.755   3.932  0.67 10.82           C  
ANISOU  557  CD1ALEU A  61      953   1694   1466    -18   -282   -184       C  
ATOM    558  CD1BLEU A  61      26.155  23.439   3.086  0.33  8.70           C  
ANISOU  558  CD1BLEU A  61      704   1574   1026     84    147    -94       C  
ATOM    559  CD2ALEU A  61      26.344  23.055   3.570  0.67 11.40           C  
ANISOU  559  CD2ALEU A  61     1225   1079   2029     26   -386     -6       C  
ATOM    560  CD2BLEU A  61      25.972  22.960   5.552  0.33  7.26           C  
ANISOU  560  CD2BLEU A  61      855    973    930   -163    117   -265       C  
ATOM    561  N   LYS A  62      27.017  25.597   7.888  1.00  9.06           N  
ANISOU  561  N   LYS A  62      832   1274   1338   -120     38    -11       N  
ATOM    562  CA  LYS A  62      26.798  25.132   9.240  1.00  9.11           C  
ANISOU  562  CA  LYS A  62      944   1205   1311   -165      2     45       C  
ATOM    563  C   LYS A  62      25.950  26.134  10.000  1.00 10.01           C  
ANISOU  563  C   LYS A  62     1147   1353   1306   -154    102    -90       C  
ATOM    564  O   LYS A  62      25.004  25.742  10.750  1.00 10.81           O  
ANISOU  564  O   LYS A  62     1156   1619   1333   -199    132     39       O  
ATOM    565  CB  LYS A  62      28.151  24.911   9.910  1.00 10.68           C  
ANISOU  565  CB  LYS A  62      993   1662   1401   -179    -47     43       C  
ATOM    566  CG  LYS A  62      28.083  24.308  11.276  1.00 11.87           C  
ANISOU  566  CG  LYS A  62     1253   1867   1389   -223   -226    171       C  
ATOM    567  CD  LYS A  62      29.497  23.924  11.775  1.00 14.09           C  
ANISOU  567  CD  LYS A  62     1235   2424   1693   -330   -352    273       C  
ATOM    568  CE  LYS A  62      29.468  23.319  13.154  1.00 13.75           C  
ANISOU  568  CE  LYS A  62     1413   2007   1805     68   -114    329       C  
ATOM    569  NZ  LYS A  62      30.831  22.899  13.552  1.00 15.00           N  
ANISOU  569  NZ  LYS A  62     1295   2269   2136   -112   -350    280       N  
ATOM    570  N   LYS A  63      26.188  27.420   9.871  1.00 10.70           N  
ANISOU  570  N   LYS A  63     1208   1345   1512   -279    199   -187       N  
ATOM    571  CA  LYS A  63      25.405  28.461  10.531  1.00 11.67           C  
ANISOU  571  CA  LYS A  63     1416   1318   1701   -194    221   -122       C  
ATOM    572  C   LYS A  63      23.984  28.378  10.075  1.00 10.89           C  
ANISOU  572  C   LYS A  63     1344   1302   1493   -107    377    123       C  
ATOM    573  O   LYS A  63      23.025  28.493  10.853  1.00 13.38           O  
ANISOU  573  O   LYS A  63     1527   1671   1885   -158    606    -92       O  
ATOM    574  CB ALYS A  63      25.920  29.861  10.162  0.61 14.44           C  
ANISOU  574  CB ALYS A  63     1988   1242   2257   -411    100   -284       C  
ATOM    575  CB BLYS A  63      26.130  29.798  10.288  0.39 13.80           C  
ANISOU  575  CB BLYS A  63     1623   1301   2319   -287    345   -395       C  
ATOM    576  CG ALYS A  63      27.127  30.171  11.027  0.61 15.69           C  
ANISOU  576  CG ALYS A  63     1656   1603   2703   -327    199   -655       C  
ATOM    577  CG BLYS A  63      25.636  30.859  11.248  0.39 14.61           C  
ANISOU  577  CG BLYS A  63     1765   1398   2389    142    -59   -443       C  
ATOM    578  CD ALYS A  63      27.664  31.486  10.514  0.61 19.08           C  
ANISOU  578  CD ALYS A  63     2141   2073   3037   -770   -330   -130       C  
ATOM    579  CD BLYS A  63      26.555  32.058  11.267  0.39 16.43           C  
ANISOU  579  CD BLYS A  63     2405   1256   2582     22     75   -555       C  
ATOM    580  CE ALYS A  63      26.630  32.579  10.471  0.61 20.11           C  
ANISOU  580  CE ALYS A  63     2901   1998   2743   -461   -413    312       C  
ATOM    581  CE BLYS A  63      26.429  32.865   9.994  0.39 21.92           C  
ANISOU  581  CE BLYS A  63     3255   1555   3517   -307   -659    164       C  
ATOM    582  NZ ALYS A  63      26.084  33.142  11.714  0.61 30.41           N  
ANISOU  582  NZ ALYS A  63     4316   3451   3787    595   -558  -1126       N  
ATOM    583  NZ BLYS A  63      27.347  34.027   9.969  0.39 20.78           N  
ANISOU  583  NZ BLYS A  63     2233   2908   2756   -723   -965    727       N  
ATOM    584  N   HIS A  64      23.733  28.181   8.782  1.00 11.68           N  
ANISOU  584  N   HIS A  64     1272   1562   1606    171    201    181       N  
ATOM    585  CA  HIS A  64      22.374  28.110   8.299  1.00 11.33           C  
ANISOU  585  CA  HIS A  64     1313   1419   1573    238    240    194       C  
ATOM    586  C   HIS A  64      21.655  26.866   8.751  1.00 11.87           C  
ANISOU  586  C   HIS A  64     1117   1670   1724    222    313    451       C  
ATOM    587  O   HIS A  64      20.447  26.887   9.070  1.00 11.90           O  
ANISOU  587  O   HIS A  64     1073   1976   1472    224    262    317       O  
ATOM    588  CB AHIS A  64      22.298  28.325   6.791  0.59 12.35           C  
ANISOU  588  CB AHIS A  64     1564   1564   1564      0      0      0       C  
ATOM    589  CB BHIS A  64      22.384  28.112   6.750  0.20 10.55           C  
ANISOU  589  CB BHIS A  64     1336   1336   1336      0      0      0       C  
ATOM    590  CB CHIS A  64      22.234  28.050   6.755  0.20 11.01           C  
ANISOU  590  CB CHIS A  64     1394   1394   1394      0      0      0       C  
ATOM    591  CG AHIS A  64      20.904  28.794   6.477  0.59 11.11           C  
ANISOU  591  CG AHIS A  64     1407   1407   1407      0      0      0       C  
ATOM    592  CG BHIS A  64      21.008  28.371   6.227  0.20 10.36           C  
ANISOU  592  CG BHIS A  64     1312   1312   1312      0      0      0       C  
ATOM    593  CG CHIS A  64      22.119  29.370   6.078  0.20  6.70           C  
ANISOU  593  CG CHIS A  64      849    849    849      0      0      0       C  
ATOM    594  ND1AHIS A  64      20.427  29.941   7.008  0.59 12.92           N  
ANISOU  594  ND1AHIS A  64     1636   1636   1636      0      0      0       N  
ATOM    595  ND1BHIS A  64      20.419  29.551   6.629  0.20 14.31           N  
ANISOU  595  ND1BHIS A  64     1812   1812   1812      0      0      0       N  
ATOM    596  ND1CHIS A  64      23.271  30.114   6.051  0.20  8.07           N  
ANISOU  596  ND1CHIS A  64     1022   1022   1022      0      0      0       N  
ATOM    597  CD2AHIS A  64      19.953  28.189   5.763  0.59 12.01           C  
ANISOU  597  CD2AHIS A  64     1521   1521   1521      0      0      0       C  
ATOM    598  CD2BHIS A  64      20.153  27.674   5.457  0.20 15.56           C  
ANISOU  598  CD2BHIS A  64     1971   1971   1971      0      0      0       C  
ATOM    599  CD2CHIS A  64      21.166  30.093   5.468  0.20  9.77           C  
ANISOU  599  CD2CHIS A  64     1237   1237   1237      0      0      0       C  
ATOM    600  CE1AHIS A  64      19.187  30.040   6.553  0.59 15.01           C  
ANISOU  600  CE1AHIS A  64     1901   1901   1901      0      0      0       C  
ATOM    601  CE1BHIS A  64      19.228  29.570   6.078  0.20 14.91           C  
ANISOU  601  CE1BHIS A  64     1888   1888   1888      0      0      0       C  
ATOM    602  CE1CHIS A  64      23.010  31.254   5.453  0.20  9.58           C  
ANISOU  602  CE1CHIS A  64     1213   1213   1213      0      0      0       C  
ATOM    603  NE2AHIS A  64      18.865  28.973   5.809  0.59 12.78           N  
ANISOU  603  NE2AHIS A  64     1619   1619   1619      0      0      0       N  
ATOM    604  NE2BHIS A  64      19.025  28.457   5.357  0.20 11.81           N  
ANISOU  604  NE2BHIS A  64     1496   1496   1496      0      0      0       N  
ATOM    605  NE2CHIS A  64      21.717  31.269   5.043  0.20  9.49           N  
ANISOU  605  NE2CHIS A  64     1202   1202   1202      0      0      0       N  
ATOM    606  N   GLY A  65      22.373  25.752   8.908  1.00 10.02           N  
ANISOU  606  N   GLY A  65      906   1447   1453     -9     11     67       N  
ATOM    607  CA  GLY A  65      21.779  24.567   9.483  1.00  9.96           C  
ANISOU  607  CA  GLY A  65     1025   1492   1269    -39     38     76       C  
ATOM    608  C   GLY A  65      21.276  24.829  10.887  1.00  9.50           C  
ANISOU  608  C   GLY A  65      817   1598   1195     60    -83    -48       C  
ATOM    609  O   GLY A  65      20.198  24.366  11.265  1.00  9.76           O  
ANISOU  609  O   GLY A  65      864   1609   1237    -30    -54    -14       O  
ATOM    610  N   VAL A  66      22.008  25.601  11.679  1.00 10.40           N  
ANISOU  610  N   VAL A  66      948   1689   1316   -119     42    -97       N  
ATOM    611  CA  VAL A  66      21.526  26.009  13.005  1.00 10.51           C  
ANISOU  611  CA  VAL A  66     1029   1671   1292   -147     44   -107       C  
ATOM    612  C   VAL A  66      20.282  26.853  12.905  1.00 10.64           C  
ANISOU  612  C   VAL A  66     1062   1735   1245   -105     44   -171       C  
ATOM    613  O   VAL A  66      19.315  26.629  13.648  1.00 11.09           O  
ANISOU  613  O   VAL A  66      958   1920   1335   -189     62   -239       O  
ATOM    614  CB  VAL A  66      22.633  26.744  13.793  1.00 12.44           C  
ANISOU  614  CB  VAL A  66     1068   2309   1350   -322    -67   -204       C  
ATOM    615  CG1 VAL A  66      22.087  27.339  15.068  1.00 14.48           C  
ANISOU  615  CG1 VAL A  66     1396   2608   1499   -363   -107   -481       C  
ATOM    616  CG2 VAL A  66      23.786  25.793  14.073  1.00 14.23           C  
ANISOU  616  CG2 VAL A  66     1196   2735   1475   -162   -126    -93       C  
ATOM    617  N   THR A  67      20.238  27.798  11.988  1.00 11.15           N  
ANISOU  617  N   THR A  67     1197   1502   1540    -57    216   -133       N  
ATOM    618  CA  THR A  67      19.046  28.637  11.797  1.00 11.47           C  
ANISOU  618  CA  THR A  67     1242   1427   1691    -55    262   -159       C  
ATOM    619  C   THR A  67      17.829  27.749  11.508  1.00 10.44           C  
ANISOU  619  C   THR A  67     1202   1345   1420    118    153   -100       C  
ATOM    620  O   THR A  67      16.726  27.930  12.105  1.00 11.50           O  
ANISOU  620  O   THR A  67     1196   1594   1580    -80    289   -298       O  
ATOM    621  CB  THR A  67      19.281  29.629  10.664  1.00 12.66           C  
ANISOU  621  CB  THR A  67     1252   1713   1843   -100     92     71       C  
ATOM    622  OG1 THR A  67      20.333  30.510  11.132  1.00 15.58           O  
ANISOU  622  OG1 THR A  67     1810   1719   2390   -543    331   -167       O  
ATOM    623  CG2 THR A  67      18.042  30.466  10.381  1.00 15.26           C  
ANISOU  623  CG2 THR A  67     1664   1756   2378    240    406    276       C  
ATOM    624  N   VAL A  68      17.977  26.830  10.612  1.00  9.77           N  
ANISOU  624  N   VAL A  68      917   1388   1409    129     94    -30       N  
ATOM    625  CA  VAL A  68      16.861  25.949  10.204  1.00  9.20           C  
ANISOU  625  CA  VAL A  68     1020   1319   1157    209    -15    -39       C  
ATOM    626  C   VAL A  68      16.366  25.107  11.358  1.00  8.96           C  
ANISOU  626  C   VAL A  68      964   1300   1141    109   -104    -47       C  
ATOM    627  O   VAL A  68      15.178  25.065  11.657  1.00  9.41           O  
ANISOU  627  O   VAL A  68      980   1368   1228     44   -119    -82       O  
ATOM    628  CB  VAL A  68      17.276  25.088   9.007  1.00 10.09           C  
ANISOU  628  CB  VAL A  68     1196   1573   1066    438   -107    -87       C  
ATOM    629  CG1 VAL A  68      16.221  24.019   8.719  1.00 12.86           C  
ANISOU  629  CG1 VAL A  68     1315   1911   1659    314   -322   -464       C  
ATOM    630  CG2 VAL A  68      17.559  25.942   7.764  1.00 13.59           C  
ANISOU  630  CG2 VAL A  68     1583   2400   1180    846    152    270       C  
ATOM    631  N   LEU A  69      17.290  24.433  12.050  1.00  9.06           N  
ANISOU  631  N   LEU A  69      944   1479   1019     17   -133    -51       N  
ATOM    632  CA  LEU A  69      16.856  23.493  13.095  1.00  9.51           C  
ANISOU  632  CA  LEU A  69      949   1495   1170    -15   -177     48       C  
ATOM    633  C   LEU A  69      16.362  24.236  14.296  1.00  9.72           C  
ANISOU  633  C   LEU A  69      901   1637   1155    -49   -112      4       C  
ATOM    634  O   LEU A  69      15.511  23.758  15.034  1.00 10.70           O  
ANISOU  634  O   LEU A  69      924   1725   1416    -12     -1    102       O  
ATOM    635  CB  LEU A  69      17.952  22.543  13.462  1.00 10.11           C  
ANISOU  635  CB  LEU A  69      960   1539   1343    -27   -103     97       C  
ATOM    636  CG  LEU A  69      18.349  21.562  12.358  1.00 10.57           C  
ANISOU  636  CG  LEU A  69     1041   1306   1672     33    -92     48       C  
ATOM    637  CD1 LEU A  69      19.293  20.517  12.959  1.00 12.67           C  
ANISOU  637  CD1 LEU A  69     1408   1499   1907    163   -106    252       C  
ATOM    638  CD2 LEU A  69      17.195  20.869  11.668  1.00 13.64           C  
ANISOU  638  CD2 LEU A  69     1247   1856   2080    115   -146   -505       C  
ATOM    639  N   THR A  70      16.869  25.437  14.579  1.00 10.28           N  
ANISOU  639  N   THR A  70      948   1792   1165   -202     46    -92       N  
ATOM    640  CA  THR A  70      16.359  26.242  15.683  1.00 11.77           C  
ANISOU  640  CA  THR A  70     1123   2103   1244   -344     57   -343       C  
ATOM    641  C   THR A  70      14.902  26.598  15.445  1.00 10.77           C  
ANISOU  641  C   THR A  70     1089   1660   1343   -371     82   -294       C  
ATOM    642  O   THR A  70      14.058  26.473  16.355  1.00 11.60           O  
ANISOU  642  O   THR A  70     1118   1872   1418   -193    201   -300       O  
ATOM    643  CB  THR A  70      17.206  27.513  15.840  1.00 14.93           C  
ANISOU  643  CB  THR A  70     1235   2793   1643   -783    201  -1007       C  
ATOM    644  OG1 THR A  70      18.533  27.120  16.208  1.00 17.90           O  
ANISOU  644  OG1 THR A  70     1303   3792   1705   -699    126  -1018       O  
ATOM    645  CG2 THR A  70      16.666  28.393  16.937  1.00 21.52           C  
ANISOU  645  CG2 THR A  70     1774   3498   2905  -1144    832  -1962       C  
ATOM    646  N   ALA A  71      14.589  27.026  14.214  1.00 10.21           N  
ANISOU  646  N   ALA A  71     1133   1362   1383   -150    213   -271       N  
ATOM    647  CA  ALA A  71      13.174  27.327  13.853  1.00 10.42           C  
ANISOU  647  CA  ALA A  71     1209   1081   1671      9    188   -173       C  
ATOM    648  C   ALA A  71      12.328  26.087  13.936  1.00  9.53           C  
ANISOU  648  C   ALA A  71     1057   1233   1332    -53    -14   -100       C  
ATOM    649  O   ALA A  71      11.196  26.157  14.486  1.00 10.18           O  
ANISOU  649  O   ALA A  71     1066   1258   1543     -7    118   -118       O  
ATOM    650  CB  ALA A  71      13.145  27.960  12.490  1.00 11.32           C  
ANISOU  650  CB  ALA A  71     1314   1211   1776    -61    107    -13       C  
ATOM    651  N   LEU A  72      12.800  24.949  13.423  1.00  9.22           N  
ANISOU  651  N   LEU A  72     1008   1191   1306    -27     18   -156       N  
ATOM    652  CA  LEU A  72      11.982  23.727  13.483  1.00  9.53           C  
ANISOU  652  CA  LEU A  72     1258   1192   1172    -37   -118   -134       C  
ATOM    653  C   LEU A  72      11.758  23.297  14.891  1.00  9.11           C  
ANISOU  653  C   LEU A  72     1005   1272   1183    -84     11   -216       C  
ATOM    654  O   LEU A  72      10.646  22.876  15.242  1.00 10.14           O  
ANISOU  654  O   LEU A  72     1010   1473   1370    -95     31   -201       O  
ATOM    655  CB  LEU A  72      12.656  22.649  12.620  1.00  9.64           C  
ANISOU  655  CB  LEU A  72     1190   1213   1259     -9     40   -146       C  
ATOM    656  CG  LEU A  72      11.883  21.343  12.564  1.00 10.19           C  
ANISOU  656  CG  LEU A  72     1333   1345   1195   -146    -62   -181       C  
ATOM    657  CD1 LEU A  72      10.450  21.537  12.020  1.00 12.54           C  
ANISOU  657  CD1 LEU A  72     1446   1564   1755   -226   -333   -149       C  
ATOM    658  CD2 LEU A  72      12.641  20.326  11.753  1.00 11.96           C  
ANISOU  658  CD2 LEU A  72     1728   1162   1653   -139    163   -133       C  
ATOM    659  N   GLY A  73      12.754  23.340  15.763  1.00  9.77           N  
ANISOU  659  N   GLY A  73     1021   1463   1228    -56     -3   -131       N  
ATOM    660  CA  GLY A  73      12.624  22.946  17.134  1.00 10.68           C  
ANISOU  660  CA  GLY A  73     1152   1720   1188    103   -119   -165       C  
ATOM    661  C   GLY A  73      11.543  23.798  17.823  1.00  9.99           C  
ANISOU  661  C   GLY A  73     1069   1581   1146     -1    -18   -142       C  
ATOM    662  O   GLY A  73      10.724  23.286  18.608  1.00 10.98           O  
ANISOU  662  O   GLY A  73     1127   1899   1145    -83    -83      8       O  
ATOM    663  N   ALA A  74      11.540  25.112  17.578  1.00 10.48           N  
ANISOU  663  N   ALA A  74     1142   1548   1291   -110    -25   -266       N  
ATOM    664  CA  ALA A  74      10.531  26.009  18.215  1.00 11.52           C  
ANISOU  664  CA  ALA A  74     1192   1598   1587     -8   -133   -372       C  
ATOM    665  C   ALA A  74       9.142  25.599  17.770  1.00 11.32           C  
ANISOU  665  C   ALA A  74     1157   1623   1522     12     28   -419       C  
ATOM    666  O   ALA A  74       8.210  25.625  18.548  1.00 13.35           O  
ANISOU  666  O   ALA A  74     1204   2333   1535     -2     61   -484       O  
ATOM    667  CB  ALA A  74      10.825  27.452  17.937  1.00 13.16           C  
ANISOU  667  CB  ALA A  74     1397   1621   1981    -61     -6   -469       C  
ATOM    668  N   ILE A  75       8.990  25.219  16.506  1.00 10.13           N  
ANISOU  668  N   ILE A  75      985   1486   1377    -48     77   -124       N  
ATOM    669  CA  ILE A  75       7.700  24.710  15.995  1.00 10.02           C  
ANISOU  669  CA  ILE A  75      919   1456   1433    -32     71   -122       C  
ATOM    670  C   ILE A  75       7.323  23.421  16.651  1.00 10.05           C  
ANISOU  670  C   ILE A  75     1039   1451   1327    -41     23   -109       C  
ATOM    671  O   ILE A  75       6.179  23.292  17.129  1.00 10.80           O  
ANISOU  671  O   ILE A  75     1037   1593   1473      2     47     73       O  
ATOM    672  CB  ILE A  75       7.775  24.573  14.469  1.00 10.57           C  
ANISOU  672  CB  ILE A  75     1055   1511   1449    -53    -66     58       C  
ATOM    673  CG1 ILE A  75       7.794  25.923  13.765  1.00 11.55           C  
ANISOU  673  CG1 ILE A  75     1271   1525   1592     12   -153     47       C  
ATOM    674  CG2 ILE A  75       6.630  23.696  13.907  1.00 11.26           C  
ANISOU  674  CG2 ILE A  75     1214   1558   1505    -70   -213     36       C  
ATOM    675  CD1 ILE A  75       8.272  25.902  12.331  1.00 15.30           C  
ANISOU  675  CD1 ILE A  75     2160   2216   1437   -928   -176    182       C  
ATOM    676  N   LEU A  76       8.246  22.434  16.670  1.00  9.59           N  
ANISOU  676  N   LEU A  76     1055   1399   1189    -58    -58     -1       N  
ATOM    677  CA  LEU A  76       7.850  21.150  17.234  1.00  9.83           C  
ANISOU  677  CA  LEU A  76     1012   1473   1251     33    -70    101       C  
ATOM    678  C   LEU A  76       7.452  21.256  18.685  1.00  9.78           C  
ANISOU  678  C   LEU A  76     1124   1329   1262     37    -26     73       C  
ATOM    679  O   LEU A  76       6.528  20.556  19.126  1.00 11.15           O  
ANISOU  679  O   LEU A  76     1379   1453   1405    -84    109     60       O  
ATOM    680  CB  LEU A  76       9.008  20.144  17.069  1.00  9.42           C  
ANISOU  680  CB  LEU A  76      985   1350   1246    -63    -81     22       C  
ATOM    681  CG  LEU A  76       9.373  19.771  15.631  1.00 10.02           C  
ANISOU  681  CG  LEU A  76     1105   1439   1262    -65    -77   -101       C  
ATOM    682  CD1 LEU A  76      10.620  18.911  15.629  1.00 11.34           C  
ANISOU  682  CD1 LEU A  76     1264   1507   1537    117    -24    -33       C  
ATOM    683  CD2 LEU A  76       8.227  19.029  14.972  1.00 12.29           C  
ANISOU  683  CD2 LEU A  76     1270   1919   1481   -184    -88   -199       C  
ATOM    684  N   LYS A  77       8.117  22.116  19.457  1.00 11.06           N  
ANISOU  684  N   LYS A  77     1296   1746   1161   -107     36     39       N  
ATOM    685  CA  LYS A  77       7.799  22.240  20.882  1.00 11.84           C  
ANISOU  685  CA  LYS A  77     1558   1757   1183      3     52    -41       C  
ATOM    686  C   LYS A  77       6.455  22.883  21.163  1.00 12.51           C  
ANISOU  686  C   LYS A  77     1604   1836   1314     28    166    -46       C  
ATOM    687  O   LYS A  77       5.938  22.739  22.260  1.00 14.72           O  
ANISOU  687  O   LYS A  77     1923   2205   1466    205    419    119       O  
ATOM    688  CB  LYS A  77       8.893  23.024  21.617  1.00 13.36           C  
ANISOU  688  CB  LYS A  77     1729   2090   1257    -98   -130   -101       C  
ATOM    689  CG  LYS A  77      10.172  22.203  21.656  1.00 14.51           C  
ANISOU  689  CG  LYS A  77     1784   2237   1492    -27   -218   -191       C  
ATOM    690  CD  LYS A  77      11.324  23.045  22.124  1.00 16.76           C  
ANISOU  690  CD  LYS A  77     1689   2760   1919      7   -150   -532       C  
ATOM    691  CE  LYS A  77      12.652  22.399  21.874  1.00 17.78           C  
ANISOU  691  CE  LYS A  77     1710   3013   2034    186    -70   -123       C  
ATOM    692  NZ  LYS A  77      13.784  23.229  22.342  1.00 26.52           N  
ANISOU  692  NZ  LYS A  77     1803   5323   2948   -217   -199  -1391       N  
ATOM    693  N   LYS A  78       5.831  23.480  20.152  1.00 12.13           N  
ANISOU  693  N   LYS A  78     1351   1925   1331     18     52   -129       N  
ATOM    694  CA  LYS A  78       4.451  23.987  20.224  1.00 13.75           C  
ANISOU  694  CA  LYS A  78     1418   1817   1988    131    174   -204       C  
ATOM    695  C   LYS A  78       3.452  22.863  20.004  1.00 13.48           C  
ANISOU  695  C   LYS A  78     1300   1933   1889    278   -175   -432       C  
ATOM    696  O   LYS A  78       2.221  23.114  20.213  1.00 15.28           O  
ANISOU  696  O   LYS A  78     1303   1911   2593    209    146   -330       O  
ATOM    697  CB  LYS A  78       4.204  25.132  19.277  1.00 16.19           C  
ANISOU  697  CB  LYS A  78     1736   2091   2323    487    368     66       C  
ATOM    698  CG  LYS A  78       4.981  26.416  19.563  1.00 20.39           C  
ANISOU  698  CG  LYS A  78     1525   2385   3838    -87    378    905       C  
ATOM    699  CD  LYS A  78       4.614  26.967  20.944  1.00 32.14           C  
ANISOU  699  CD  LYS A  78     4738   3264   4208  -1208   -519   -892       C  
ATOM    700  CE  LYS A  78       4.973  28.437  20.954  1.00 41.82           C  
ANISOU  700  CE  LYS A  78     7114   2644   6133   -192   -329    -56       C  
ATOM    701  NZ  LYS A  78       3.818  29.266  21.364  1.00 47.59           N  
ANISOU  701  NZ  LYS A  78     8037   3334   6711   -991   2342   -905       N  
ATOM    702  N   LYS A  79       3.847  21.689  19.612  1.00 12.98           N  
ANISOU  702  N   LYS A  79     1246   1756   1931    168     37   -145       N  
ATOM    703  CA  LYS A  79       2.941  20.542  19.545  1.00 13.05           C  
ANISOU  703  CA  LYS A  79     1251   1819   1890     79     15   -154       C  
ATOM    704  C   LYS A  79       1.695  20.882  18.730  1.00 14.09           C  
ANISOU  704  C   LYS A  79     1293   2000   2060     84    -14      6       C  
ATOM    705  O   LYS A  79       0.549  20.585  19.144  1.00 15.99           O  
ANISOU  705  O   LYS A  79     1178   2295   2604     92    -11     45       O  
ATOM    706  CB  LYS A  79       2.622  19.969  20.918  1.00 13.50           C  
ANISOU  706  CB  LYS A  79     1339   2084   1707     -1    -62   -208       C  
ATOM    707  CG  LYS A  79       3.868  19.494  21.666  1.00 14.37           C  
ANISOU  707  CG  LYS A  79     1334   2423   1704   -107    -10    -88       C  
ATOM    708  CD  LYS A  79       3.648  19.270  23.139  1.00 15.83           C  
ANISOU  708  CD  LYS A  79     1357   2945   1714    -24   -131     24       C  
ATOM    709  CE  LYS A  79       2.712  18.181  23.470  1.00 16.36           C  
ANISOU  709  CE  LYS A  79     1916   2762   1537   -200   -116     -4       C  
ATOM    710  NZ  LYS A  79       2.425  18.131  24.921  1.00 16.29           N  
ANISOU  710  NZ  LYS A  79     1329   3216   1646     49    147   -213       N  
ATOM    711  N   GLY A  80       1.927  21.450  17.522  1.00 13.64           N  
ANISOU  711  N   GLY A  80     1588   1536   2057    -64   -185   -108       N  
ATOM    712  CA  GLY A  80       0.760  21.738  16.706  1.00 15.77           C  
ANISOU  712  CA  GLY A  80     1553   2118   2320     -2   -231     20       C  
ATOM    713  C   GLY A  80       0.178  23.108  16.891  1.00 15.97           C  
ANISOU  713  C   GLY A  80     1717   1972   2378     -4    -37    249       C  
ATOM    714  O   GLY A  80      -0.443  23.562  15.931  1.00 18.47           O  
ANISOU  714  O   GLY A  80     1986   2520   2513     56    -99    588       O  
ATOM    715  N   HIS A  81       0.356  23.712  18.070  1.00 17.09           N  
ANISOU  715  N   HIS A  81     1860   2051   2583    239   -151     13       N  
ATOM    716  CA  HIS A  81      -0.154  25.068  18.250  1.00 16.36           C  
ANISOU  716  CA  HIS A  81     1666   2239   2311    483    176    173       C  
ATOM    717  C   HIS A  81       0.886  26.090  17.799  1.00 15.81           C  
ANISOU  717  C   HIS A  81     1739   1961   2307    448    149    -52       C  
ATOM    718  O   HIS A  81       1.397  26.881  18.582  1.00 18.13           O  
ANISOU  718  O   HIS A  81     1552   2779   2560    340    397   -556       O  
ATOM    719  CB  HIS A  81      -0.440  25.364  19.724  1.00 19.96           C  
ANISOU  719  CB  HIS A  81     2465   2722   2396    316    430     30       C  
ATOM    720  CG  HIS A  81      -1.449  24.402  20.245  1.00 27.44           C  
ANISOU  720  CG  HIS A  81     3338   3576   3511   -154   1515     66       C  
ATOM    721  ND1 HIS A  81      -2.785  24.699  20.101  1.00 35.01           N  
ANISOU  721  ND1 HIS A  81     3140   4218   5942   -113   2203    324       N  
ATOM    722  CD2 HIS A  81      -1.286  23.227  20.885  1.00 34.47           C  
ANISOU  722  CD2 HIS A  81     4090   4324   4681  -1020    775   1181       C  
ATOM    723  CE1 HIS A  81      -3.429  23.707  20.653  1.00 39.65           C  
ANISOU  723  CE1 HIS A  81     3785   5317   5963   -647   2303    879       C  
ATOM    724  NE2 HIS A  81      -2.576  22.786  21.146  1.00 39.64           N  
ANISOU  724  NE2 HIS A  81     4360   5055   5645  -1089   1665   1130       N  
ATOM    725  N   HIS A  82       1.225  26.007  16.503  1.00 16.43           N  
ANISOU  725  N   HIS A  82     1461   2544   2240     76     28   -111       N  
ATOM    726  CA  HIS A  82       2.426  26.675  15.951  1.00 16.04           C  
ANISOU  726  CA  HIS A  82     1592   2000   2502    134    253   -370       C  
ATOM    727  C   HIS A  82       2.089  27.723  14.940  1.00 16.68           C  
ANISOU  727  C   HIS A  82     1659   2063   2615    275    446   -299       C  
ATOM    728  O   HIS A  82       2.903  28.121  14.112  1.00 17.77           O  
ANISOU  728  O   HIS A  82     2023   1869   2859    130    837   -391       O  
ATOM    729  CB  HIS A  82       3.349  25.591  15.365  1.00 15.64           C  
ANISOU  729  CB  HIS A  82     1687   2027   2227    206     -5   -420       C  
ATOM    730  CG  HIS A  82       2.691  24.693  14.364  1.00 13.73           C  
ANISOU  730  CG  HIS A  82     1418   1914   1884     23    122   -111       C  
ATOM    731  ND1 HIS A  82       3.055  23.377  14.233  1.00 13.49           N  
ANISOU  731  ND1 HIS A  82     1307   1726   2094   -298   -184     92       N  
ATOM    732  CD2 HIS A  82       1.725  24.959  13.432  1.00 15.58           C  
ANISOU  732  CD2 HIS A  82     1731   2237   1953    333     -8   -168       C  
ATOM    733  CE1 HIS A  82       2.332  22.876  13.259  1.00 13.36           C  
ANISOU  733  CE1 HIS A  82     1433   1762   1883   -298   -167    198       C  
ATOM    734  NE2 HIS A  82       1.496  23.788  12.760  1.00 13.92           N  
ANISOU  734  NE2 HIS A  82     1515   2158   1616     79     10    113       N  
ATOM    735  N   GLU A  83       0.881  28.288  14.959  1.00 18.00           N  
ANISOU  735  N   GLU A  83     1669   2600   2568    407    518    116       N  
ATOM    736  CA  GLU A  83       0.476  29.282  13.947  1.00 21.21           C  
ANISOU  736  CA  GLU A  83     2194   2799   3067    648    638    448       C  
ATOM    737  C   GLU A  83       1.419  30.469  13.882  1.00 21.66           C  
ANISOU  737  C   GLU A  83     2724   2401   3105    665   1272      4       C  
ATOM    738  O   GLU A  83       1.742  30.873  12.754  1.00 22.16           O  
ANISOU  738  O   GLU A  83     2659   2681   3079    504   1026    112       O  
ATOM    739  CB  GLU A  83      -0.959  29.717  14.205  1.00 26.16           C  
ANISOU  739  CB  GLU A  83     2129   4343   3468   1059    552   1036       C  
ATOM    740  CG  GLU A  83      -1.903  28.790  14.875  1.00 32.33           C  
ANISOU  740  CG  GLU A  83     2477   5722   4085    480   1015   1185       C  
ATOM    741  CD  GLU A  83      -1.749  28.071  16.173  1.00 34.58           C  
ANISOU  741  CD  GLU A  83     2606   6416   4115    -37   1178   1548       C  
ATOM    742  OE1 GLU A  83      -1.144  28.513  17.177  1.00 41.23           O  
ANISOU  742  OE1 GLU A  83     3552   7694   4420   1217    313    927       O  
ATOM    743  OE2 GLU A  83      -2.307  26.938  16.228  1.00 48.18           O  
ANISOU  743  OE2 GLU A  83     5234   5901   7170    -94   -185   2514       O  
ATOM    744  N   ALA A  84       1.789  30.987  15.060  1.00 21.53           N  
ANISOU  744  N   ALA A  84     2972   2138   3072    540   1574    -16       N  
ATOM    745  CA  ALA A  84       2.614  32.196  15.098  1.00 23.60           C  
ANISOU  745  CA  ALA A  84     3304   2100   3565    456   1423    -83       C  
ATOM    746  C   ALA A  84       4.027  31.958  14.539  1.00 22.05           C  
ANISOU  746  C   ALA A  84     3327   1545   3506      2   1480   -636       C  
ATOM    747  O   ALA A  84       4.645  32.800  13.932  1.00 30.38           O  
ANISOU  747  O   ALA A  84     3937   1636   5968    -36   2421   -127       O  
ATOM    748  CB  ALA A  84       2.752  32.777  16.488  1.00 27.67           C  
ANISOU  748  CB  ALA A  84     3558   2878   4077    419   1729   -981       C  
ATOM    749  N   GLU A  85       4.521  30.753  14.807  1.00 18.98           N  
ANISOU  749  N   GLU A  85     2451   1813   2948   -109    661   -409       N  
ATOM    750  CA  GLU A  85       5.848  30.434  14.271  1.00 20.81           C  
ANISOU  750  CA  GLU A  85     2347   1877   3683   -331    813   -643       C  
ATOM    751  C   GLU A  85       5.726  30.174  12.790  1.00 21.38           C  
ANISOU  751  C   GLU A  85     1720   2404   4000    -90    845  -1407       C  
ATOM    752  O   GLU A  85       6.619  30.535  11.954  1.00 17.13           O  
ANISOU  752  O   GLU A  85     1651   1910   2948    -67   -325   -183       O  
ATOM    753  CB  GLU A  85       6.356  29.250  15.112  1.00 24.68           C  
ANISOU  753  CB  GLU A  85     1955   2107   5313   -348    399    -95       C  
ATOM    754  CG  GLU A  85       6.701  29.492  16.572  1.00 30.68           C  
ANISOU  754  CG  GLU A  85     2501   3705   5453    554   -556    461       C  
ATOM    755  CD  GLU A  85       5.556  29.609  17.540  1.00 28.87           C  
ANISOU  755  CD  GLU A  85     3212   2962   4797    506   -476   -415       C  
ATOM    756  OE1 GLU A  85       4.421  29.228  17.130  1.00 26.23           O  
ANISOU  756  OE1 GLU A  85     2860   3555   3553    582    111   -452       O  
ATOM    757  OE2 GLU A  85       5.690  30.069  18.691  1.00 33.33           O  
ANISOU  757  OE2 GLU A  85     4312   3132   5221    150   -980   -824       O  
ATOM    758  N   LEU A  86       4.708  29.498  12.275  1.00 21.23           N  
ANISOU  758  N   LEU A  86     2154   2066   3845   -419   1067  -1176       N  
ATOM    759  CA  LEU A  86       4.734  29.157  10.860  1.00 23.29           C  
ANISOU  759  CA  LEU A  86     2014   2651   4183   -900   1236  -1835       C  
ATOM    760  C   LEU A  86       4.427  30.327   9.953  1.00 21.95           C  
ANISOU  760  C   LEU A  86     1647   3484   3208   -776    614  -1876       C  
ATOM    761  O   LEU A  86       4.912  30.273   8.807  1.00 26.15           O  
ANISOU  761  O   LEU A  86     2678   3541   3717  -1233   1520  -2128       O  
ATOM    762  CB  LEU A  86       3.671  28.134  10.520  1.00 28.34           C  
ANISOU  762  CB  LEU A  86     1881   3429   5457  -1050    668  -2026       C  
ATOM    763  CG  LEU A  86       3.966  26.714  10.949  1.00 33.36           C  
ANISOU  763  CG  LEU A  86     2733   3277   6665  -1981    849  -1335       C  
ATOM    764  CD1 LEU A  86       3.113  25.661  10.249  1.00 32.74           C  
ANISOU  764  CD1 LEU A  86     5466   3820   3152  -2465   1275  -1703       C  
ATOM    765  CD2 LEU A  86       5.435  26.364  10.887  1.00 37.33           C  
ANISOU  765  CD2 LEU A  86     3530   2681   7973   -478   1774  -1102       C  
ATOM    766  N   LYS A  87       3.607  31.294  10.357  1.00 22.88           N  
ANISOU  766  N   LYS A  87     1365   5026   2302    498   -110  -1329       N  
ATOM    767  CA  LYS A  87       3.262  32.355   9.402  1.00 26.47           C  
ANISOU  767  CA  LYS A  87     2164   5749   2143    883   -169  -1163       C  
ATOM    768  C   LYS A  87       4.463  33.004   8.766  1.00 23.39           C  
ANISOU  768  C   LYS A  87     2095   4812   1980   1008   -560   -995       C  
ATOM    769  O   LYS A  87       4.487  33.116   7.549  1.00 23.83           O  
ANISOU  769  O   LYS A  87     1693   5352   2011    926   -573   -872       O  
ATOM    770  CB  LYS A  87       2.508  33.473  10.154  1.00 30.88           C  
ANISOU  770  CB  LYS A  87     2579   6372   2782   1991   -107   -757       C  
ATOM    771  CG  LYS A  87       1.867  34.574   9.322  1.00 36.73           C  
ANISOU  771  CG  LYS A  87     3219   7008   3729   2209   -766   -385       C  
ATOM    772  CD  LYS A  87       0.874  35.317  10.226  1.00 40.17           C  
ANISOU  772  CD  LYS A  87     3573   7044   4647   2770   -805   -595       C  
ATOM    773  CE  LYS A  87       0.639  36.733   9.742  1.00 46.38           C  
ANISOU  773  CE  LYS A  87     4907   7177   5538   3020  -1684   -425       C  
ATOM    774  NZ  LYS A  87      -0.775  37.137   9.928  1.00 55.11           N  
ANISOU  774  NZ  LYS A  87     5624   7712   7603   3930  -1009   -380       N  
ATOM    775  N   PRO A  88       5.416  33.464   9.562  1.00 21.72           N  
ANISOU  775  N   PRO A  88     2432   3802   2019   1239   -798  -1012       N  
ATOM    776  CA  PRO A  88       6.484  34.193   8.889  1.00 19.75           C  
ANISOU  776  CA  PRO A  88     2797   2382   2326   1141  -1168   -837       C  
ATOM    777  C   PRO A  88       7.340  33.290   7.991  1.00 15.38           C  
ANISOU  777  C   PRO A  88     1578   1840   2427    467  -1019   -556       C  
ATOM    778  O   PRO A  88       7.832  33.709   6.970  1.00 16.28           O  
ANISOU  778  O   PRO A  88     2046   1672   2467    501  -1040   -282       O  
ATOM    779  CB  PRO A  88       7.343  34.771   9.992  1.00 23.65           C  
ANISOU  779  CB  PRO A  88     4088   2372   2524    727  -1599   -793       C  
ATOM    780  CG  PRO A  88       6.902  34.110  11.216  1.00 25.99           C  
ANISOU  780  CG  PRO A  88     5063   2165   2647   -158  -1911   -564       C  
ATOM    781  CD  PRO A  88       5.492  33.614  11.043  1.00 24.05           C  
ANISOU  781  CD  PRO A  88     3250   3858   2031   1644  -1070   -806       C  
ATOM    782  N   LEU A  89       7.520  32.043   8.402  1.00 14.33           N  
ANISOU  782  N   LEU A  89     1436   1804   2205    184   -787   -451       N  
ATOM    783  CA  LEU A  89       8.294  31.073   7.656  1.00 13.22           C  
ANISOU  783  CA  LEU A  89     1102   1694   2228    239   -642    -98       C  
ATOM    784  C   LEU A  89       7.614  30.756   6.349  1.00 12.72           C  
ANISOU  784  C   LEU A  89     1042   1665   2128     72   -358   -298       C  
ATOM    785  O   LEU A  89       8.238  30.711   5.295  1.00 12.34           O  
ANISOU  785  O   LEU A  89      944   1516   2228    -74   -271   -111       O  
ATOM    786  CB  LEU A  89       8.395  29.790   8.511  1.00 14.18           C  
ANISOU  786  CB  LEU A  89     1347   1843   2196     32    -56     88       C  
ATOM    787  CG  LEU A  89       9.238  28.704   7.872  1.00 15.34           C  
ANISOU  787  CG  LEU A  89     1535   1786   2506    299     11    370       C  
ATOM    788  CD1 LEU A  89      10.699  29.095   7.919  1.00 18.98           C  
ANISOU  788  CD1 LEU A  89     1430   2289   3492    451     71    683       C  
ATOM    789  CD2 LEU A  89       8.987  27.371   8.572  1.00 22.56           C  
ANISOU  789  CD2 LEU A  89     2299   1929   4343    456    595    912       C  
ATOM    790  N   ALA A  90       6.280  30.489   6.385  1.00 13.80           N  
ANISOU  790  N   ALA A  90     1069   2043   2132    -35   -158   -661       N  
ATOM    791  CA  ALA A  90       5.591  30.235   5.137  1.00 15.64           C  
ANISOU  791  CA  ALA A  90      958   2672   2312    -26   -133  -1082       C  
ATOM    792  C   ALA A  90       5.639  31.446   4.230  1.00 17.12           C  
ANISOU  792  C   ALA A  90     1413   2797   2294     40  -1009  -1012       C  
ATOM    793  O   ALA A  90       5.793  31.307   3.038  1.00 16.60           O  
ANISOU  793  O   ALA A  90     1051   2879   2376    122   -543   -825       O  
ATOM    794  CB  ALA A  90       4.116  29.882   5.491  1.00 22.15           C  
ANISOU  794  CB  ALA A  90     1126   4244   3044   -642    132  -2017       C  
ATOM    795  N   GLN A  91       5.467  32.643   4.794  1.00 16.51           N  
ANISOU  795  N   GLN A  91     1213   2758   2301    481   -720   -796       N  
ATOM    796  CA  GLN A  91       5.462  33.832   3.963  1.00 19.36           C  
ANISOU  796  CA  GLN A  91     1871   3086   2401   1001   -958   -513       C  
ATOM    797  C   GLN A  91       6.826  33.982   3.291  1.00 16.41           C  
ANISOU  797  C   GLN A  91     1875   2054   2306    643  -1033   -312       C  
ATOM    798  O   GLN A  91       6.873  34.251   2.102  1.00 17.03           O  
ANISOU  798  O   GLN A  91     2096   2013   2362    545  -1125   -156       O  
ATOM    799  CB AGLN A  91       5.150  35.071   4.785  0.71 21.46           C  
ANISOU  799  CB AGLN A  91     2853   2952   2350   1201   -666   -291       C  
ATOM    800  CB BGLN A  91       5.194  35.093   4.780  0.29 21.36           C  
ANISOU  800  CB BGLN A  91     2446   2854   2816    762   -450   -471       C  
ATOM    801  CG AGLN A  91       3.722  34.996   5.318  0.71 25.71           C  
ANISOU  801  CG AGLN A  91     2705   3932   3131   1757   -622   -514       C  
ATOM    802  CG BGLN A  91       3.786  35.643   4.734  0.29 25.50           C  
ANISOU  802  CG BGLN A  91     2848   3543   3297   1423   -862  -1140       C  
ATOM    803  CD AGLN A  91       3.446  36.195   6.211  0.71 28.58           C  
ANISOU  803  CD AGLN A  91     2899   4242   3720    990   -179  -1091       C  
ATOM    804  CD BGLN A  91       3.479  36.552   3.582  0.29 22.22           C  
ANISOU  804  CD BGLN A  91     2844   3471   2128   1359  -1373  -2029       C  
ATOM    805  OE1AGLN A  91       4.351  36.718   6.867  0.71 42.23           O  
ANISOU  805  OE1AGLN A  91     4863   4674   6507   1173  -2473  -1699       O  
ATOM    806  OE1BGLN A  91       2.552  37.372   3.597  0.29 35.37           O  
ANISOU  806  OE1BGLN A  91     5029   5426   2986   3443   -899  -1194       O  
ATOM    807  NE2AGLN A  91       2.194  36.579   6.159  0.71 29.23           N  
ANISOU  807  NE2AGLN A  91     3096   3536   4475   1245    467   -610       N  
ATOM    808  NE2BGLN A  91       4.195  36.420   2.463  0.29 26.53           N  
ANISOU  808  NE2BGLN A  91     2631   3858   3592    -77    -44  -1455       N  
ATOM    809  N   SER A  92       7.933  33.836   4.041  1.00 15.28           N  
ANISOU  809  N   SER A  92     1841   1685   2279    515   -931   -278       N  
ATOM    810  CA  SER A  92       9.237  34.065   3.397  1.00 16.66           C  
ANISOU  810  CA  SER A  92     1796   1630   2902    248   -949    -40       C  
ATOM    811  C   SER A  92       9.529  32.995   2.369  1.00 13.56           C  
ANISOU  811  C   SER A  92     1206   1594   2352    -15   -710    213       C  
ATOM    812  O   SER A  92      10.099  33.199   1.289  1.00 15.60           O  
ANISOU  812  O   SER A  92     1474   1789   2665    -95   -528    515       O  
ATOM    813  CB  SER A  92      10.381  34.142   4.422  1.00 16.77           C  
ANISOU  813  CB  SER A  92     2028   1603   2740    132   -988   -192       C  
ATOM    814  OG  SER A  92      10.575  32.907   4.968  1.00 15.77           O  
ANISOU  814  OG  SER A  92     1564   1795   2631    -87   -897     82       O  
ATOM    815  N   HIS A  93       9.182  31.708   2.732  1.00 12.47           N  
ANISOU  815  N   HIS A  93     1064   1569   2104     52   -450    126       N  
ATOM    816  CA  HIS A  93       9.545  30.610   1.845  1.00 11.57           C  
ANISOU  816  CA  HIS A  93     1004   1611   1780    -17   -325    275       C  
ATOM    817  C   HIS A  93       8.725  30.598   0.563  1.00 11.77           C  
ANISOU  817  C   HIS A  93     1221   1530   1720     25   -359    367       C  
ATOM    818  O   HIS A  93       9.209  30.262  -0.516  1.00 13.57           O  
ANISOU  818  O   HIS A  93     1475   1899   1781    302   -249    259       O  
ATOM    819  CB  HIS A  93       9.563  29.266   2.603  1.00 10.62           C  
ANISOU  819  CB  HIS A  93      993   1566   1477     32   -279    164       C  
ATOM    820  CG  HIS A  93      10.793  29.144   3.477  1.00 10.28           C  
ANISOU  820  CG  HIS A  93      890   1617   1400    109   -182     94       C  
ATOM    821  ND1 HIS A  93      11.018  29.971   4.542  1.00 12.24           N  
ANISOU  821  ND1 HIS A  93     1003   1897   1752    103   -336   -237       N  
ATOM    822  CD2 HIS A  93      11.903  28.341   3.405  1.00 10.52           C  
ANISOU  822  CD2 HIS A  93      979   1578   1439    199   -235    148       C  
ATOM    823  CE1 HIS A  93      12.244  29.623   5.051  1.00 13.47           C  
ANISOU  823  CE1 HIS A  93     1306   2037   1774    313   -631   -164       C  
ATOM    824  NE2 HIS A  93      12.785  28.643   4.387  1.00 10.91           N  
ANISOU  824  NE2 HIS A  93      980   1837   1329    -64   -208    177       N  
ATOM    825  N   ALA A  94       7.447  31.043   0.672  1.00 11.58           N  
ANISOU  825  N   ALA A  94     1206   1602   1593     97   -409    114       N  
ATOM    826  CA  ALA A  94       6.619  31.122  -0.535  1.00 12.85           C  
ANISOU  826  CA  ALA A  94     1332   1808   1741     20   -529    305       C  
ATOM    827  C   ALA A  94       7.034  32.313  -1.392  1.00 14.23           C  
ANISOU  827  C   ALA A  94     1455   1983   1968    -49   -479    506       C  
ATOM    828  O   ALA A  94       7.238  32.165  -2.597  1.00 18.84           O  
ANISOU  828  O   ALA A  94     2681   2471   2007    205     -7    567       O  
ATOM    829  CB  ALA A  94       5.124  31.275  -0.153  1.00 14.87           C  
ANISOU  829  CB  ALA A  94     1234   2271   2144   -196   -668    531       C  
ATOM    830  N   THR A  95       7.128  33.492  -0.815  1.00 14.68           N  
ANISOU  830  N   THR A  95     1546   1921   2110    -96   -605    601       N  
ATOM    831  CA  THR A  95       7.151  34.706  -1.610  1.00 17.03           C  
ANISOU  831  CA  THR A  95     1612   1985   2875    -14   -508    922       C  
ATOM    832  C   THR A  95       8.544  35.247  -1.831  1.00 19.91           C  
ANISOU  832  C   THR A  95     1749   2364   3451   -101   -497   1423       C  
ATOM    833  O   THR A  95       8.757  35.990  -2.767  1.00 22.73           O  
ANISOU  833  O   THR A  95     2211   3125   3298   -285   -355   1554       O  
ATOM    834  CB  THR A  95       6.325  35.842  -0.985  1.00 18.40           C  
ANISOU  834  CB  THR A  95     1907   2027   3056     17   -650    672       C  
ATOM    835  OG1 THR A  95       6.957  36.423   0.145  1.00 21.49           O  
ANISOU  835  OG1 THR A  95     2562   2294   3309    -12   -904    526       O  
ATOM    836  CG2 THR A  95       4.939  35.383  -0.574  1.00 17.70           C  
ANISOU  836  CG2 THR A  95     1899   1851   2975    305   -398    615       C  
ATOM    837  N   LYS A  96       9.508  34.991  -0.952  1.00 19.35           N  
ANISOU  837  N   LYS A  96     1685   2083   3584   -234   -597   1276       N  
ATOM    838  CA  LYS A  96      10.848  35.503  -1.145  1.00 19.67           C  
ANISOU  838  CA  LYS A  96     1924   1807   3741   -390   -566    989       C  
ATOM    839  C   LYS A  96      11.788  34.436  -1.622  1.00 19.26           C  
ANISOU  839  C   LYS A  96     1782   2358   3176   -164   -522   1036       C  
ATOM    840  O   LYS A  96      12.490  34.599  -2.616  1.00 23.05           O  
ANISOU  840  O   LYS A  96     2135   3006   3618   -203   -129   1456       O  
ATOM    841  CB ALYS A  96      11.390  36.055   0.178  0.62 21.97           C  
ANISOU  841  CB ALYS A  96     2095   2026   4227   -183   -794    518       C  
ATOM    842  CB BLYS A  96      11.434  36.153   0.116  0.38 23.82           C  
ANISOU  842  CB BLYS A  96     2430   2179   4442   -288   -957    372       C  
ATOM    843  CG ALYS A  96      12.713  36.780  -0.040  0.62 26.51           C  
ANISOU  843  CG ALYS A  96     2600   2901   4573   -955   -821    510       C  
ATOM    844  CG BLYS A  96      12.916  36.018   0.357  0.38 26.40           C  
ANISOU  844  CG BLYS A  96     2353   2995   4684   -639   -985    240       C  
ATOM    845  CD ALYS A  96      13.508  36.696   1.244  0.62 30.25           C  
ANISOU  845  CD ALYS A  96     3002   3608   4885  -1154  -1255    207       C  
ATOM    846  CD BLYS A  96      13.808  37.149  -0.076  0.38 29.14           C  
ANISOU  846  CD BLYS A  96     2900   3599   4573  -1145   -868    331       C  
ATOM    847  CE ALYS A  96      13.235  37.900   2.127  0.62 30.21           C  
ANISOU  847  CE ALYS A  96     4056   3464   3958   -854   -679    814       C  
ATOM    848  CE BLYS A  96      13.043  38.349  -0.598  0.38 31.58           C  
ANISOU  848  CE BLYS A  96     4143   3411   4445  -1235  -1056    631       C  
ATOM    849  NZ ALYS A  96      13.323  39.128   1.280  0.62 37.99           N  
ANISOU  849  NZ ALYS A  96     6815   3571   4050  -1562   -699    837       N  
ATOM    850  NZ BLYS A  96      13.516  39.599   0.073  0.38 33.75           N  
ANISOU  850  NZ BLYS A  96     7541   3407   1874  -1640     19    745       N  
ATOM    851  N   HIS A  97      11.800  33.300  -0.935  1.00 15.36           N  
ANISOU  851  N   HIS A  97     1270   2078   2488    -26   -443    547       N  
ATOM    852  CA  HIS A  97      12.767  32.258  -1.281  1.00 15.31           C  
ANISOU  852  CA  HIS A  97     1384   2301   2133      6   -379    454       C  
ATOM    853  C   HIS A  97      12.278  31.345  -2.385  1.00 15.70           C  
ANISOU  853  C   HIS A  97     1506   2277   2181    111   -401    515       C  
ATOM    854  O   HIS A  97      13.062  30.696  -3.039  1.00 17.32           O  
ANISOU  854  O   HIS A  97     1767   2652   2161     -7    -62    322       O  
ATOM    855  CB  HIS A  97      13.111  31.437  -0.054  1.00 14.57           C  
ANISOU  855  CB  HIS A  97     1433   1912   2192     -6   -308    389       C  
ATOM    856  CG  HIS A  97      13.529  32.267   1.117  1.00 14.55           C  
ANISOU  856  CG  HIS A  97     1319   1930   2277    -35   -623    492       C  
ATOM    857  ND1 HIS A  97      14.409  33.313   1.018  1.00 15.85           N  
ANISOU  857  ND1 HIS A  97     1339   2150   2532   -193   -444    410       N  
ATOM    858  CD2 HIS A  97      13.190  32.116   2.397  1.00 14.66           C  
ANISOU  858  CD2 HIS A  97     1194   2180   2196   -102   -751    542       C  
ATOM    859  CE1 HIS A  97      14.554  33.792   2.242  1.00 16.08           C  
ANISOU  859  CE1 HIS A  97     1767   1803   2539    -81   -668    493       C  
ATOM    860  NE2 HIS A  97      13.804  33.077   3.119  1.00 15.58           N  
ANISOU  860  NE2 HIS A  97     1309   2297   2311    -31   -732    415       N  
ATOM    861  N   LYS A  98      10.973  31.371  -2.657  1.00 16.26           N  
ANISOU  861  N   LYS A  98     1636   2469   2074      6   -620    337       N  
ATOM    862  CA  LYS A  98      10.347  30.647  -3.766  1.00 19.18           C  
ANISOU  862  CA  LYS A  98     2494   2706   2087    -51   -888    225       C  
ATOM    863  C   LYS A  98      10.635  29.143  -3.661  1.00 16.54           C  
ANISOU  863  C   LYS A  98     1541   2734   2010    189   -597    108       C  
ATOM    864  O   LYS A  98      11.054  28.446  -4.582  1.00 19.10           O  
ANISOU  864  O   LYS A  98     2066   3242   1947    295   -565     10       O  
ATOM    865  CB  LYS A  98      10.797  31.264  -5.095  1.00 24.20           C  
ANISOU  865  CB  LYS A  98     3895   3184   2116    191   -710    470       C  
ATOM    866  CG  LYS A  98      10.587  32.755  -5.243  1.00 31.23           C  
ANISOU  866  CG  LYS A  98     5572   3063   3231   -388  -1126    856       C  
ATOM    867  CD  LYS A  98       9.657  33.186  -6.351  1.00 37.79           C  
ANISOU  867  CD  LYS A  98     6321   3189   4847    -87  -2041   1430       C  
ATOM    868  CE  LYS A  98       9.241  34.658  -6.058  1.00 40.51           C  
ANISOU  868  CE  LYS A  98     6468   3387   5536     -8  -2032   1008       C  
ATOM    869  NZ  LYS A  98       9.489  34.729  -4.563  1.00 49.81           N  
ANISOU  869  NZ  LYS A  98     7207   5754   5964    853  -2992   -315       N  
ATOM    870  N   ILE A  99      10.272  28.578  -2.522  1.00 15.93           N  
ANISOU  870  N   ILE A  99     1400   2549   2105    479   -493    110       N  
ATOM    871  CA  ILE A  99      10.504  27.164  -2.228  1.00 14.64           C  
ANISOU  871  CA  ILE A  99     1188   2392   1983    368   -416   -142       C  
ATOM    872  C   ILE A  99       9.207  26.396  -2.452  1.00 15.83           C  
ANISOU  872  C   ILE A  99     1230   2670   2114    352   -523   -480       C  
ATOM    873  O   ILE A  99       8.256  26.604  -1.677  1.00 20.25           O  
ANISOU  873  O   ILE A  99      988   3568   3139    227   -406  -1224       O  
ATOM    874  CB  ILE A  99      11.002  26.948  -0.783  1.00 13.11           C  
ANISOU  874  CB  ILE A  99     1013   2007   1963    125   -248      0       C  
ATOM    875  CG1 ILE A  99      12.229  27.837  -0.523  1.00 12.93           C  
ANISOU  875  CG1 ILE A  99     1071   2099   1742     52   -289    190       C  
ATOM    876  CG2 ILE A  99      11.280  25.476  -0.485  1.00 14.68           C  
ANISOU  876  CG2 ILE A  99     1157   2020   2403    176      7    156       C  
ATOM    877  CD1 ILE A  99      13.328  27.717  -1.535  1.00 14.71           C  
ANISOU  877  CD1 ILE A  99     1251   2364   1974    172     -1    720       C  
ATOM    878  N   PRO A 100       9.109  25.450  -3.368  1.00 15.59           N  
ANISOU  878  N   PRO A 100     1339   2289   2296    531   -670   -348       N  
ATOM    879  CA  PRO A 100       7.906  24.619  -3.470  1.00 17.61           C  
ANISOU  879  CA  PRO A 100     1570   2447   2674    335   -742   -431       C  
ATOM    880  C   PRO A 100       7.675  23.706  -2.269  1.00 17.72           C  
ANISOU  880  C   PRO A 100     1182   2926   2626    259   -477   -333       C  
ATOM    881  O   PRO A 100       8.612  23.274  -1.649  1.00 16.21           O  
ANISOU  881  O   PRO A 100     1081   2493   2587    285   -360   -441       O  
ATOM    882  CB  PRO A 100       8.151  23.802  -4.714  1.00 22.19           C  
ANISOU  882  CB  PRO A 100     2610   3384   2440   -142   -774   -713       C  
ATOM    883  CG  PRO A 100       9.291  24.380  -5.449  1.00 21.56           C  
ANISOU  883  CG  PRO A 100     2347   2839   3005    242   -376  -1081       C  
ATOM    884  CD  PRO A 100      10.085  25.128  -4.393  1.00 17.11           C  
ANISOU  884  CD  PRO A 100     1793   2668   2041    629   -498   -321       C  
ATOM    885  N   ILE A 101       6.378  23.447  -1.987  1.00 17.88           N  
ANISOU  885  N   ILE A 101     1058   2633   3101     98   -695   -635       N  
ATOM    886  CA  ILE A 101       6.081  22.491  -0.872  1.00 18.81           C  
ANISOU  886  CA  ILE A 101     1163   3177   2806      3   -200   -757       C  
ATOM    887  C   ILE A 101       6.830  21.205  -1.041  1.00 14.79           C  
ANISOU  887  C   ILE A 101      861   2995   1763   -232   -101   -363       C  
ATOM    888  O   ILE A 101       7.278  20.531  -0.067  1.00 15.85           O  
ANISOU  888  O   ILE A 101     1056   3271   1696   -194   -137   -479       O  
ATOM    889  CB  ILE A 101       4.572  22.239  -0.716  1.00 19.64           C  
ANISOU  889  CB  ILE A 101     1077   3643   2740     23   -342   -659       C  
ATOM    890  CG1 ILE A 101       3.861  23.521  -0.384  1.00 18.42           C  
ANISOU  890  CG1 ILE A 101      923   3677   2398   -128   -227   -722       C  
ATOM    891  CG2 ILE A 101       4.278  21.220   0.395  1.00 21.95           C  
ANISOU  891  CG2 ILE A 101     1222   3909   3209   -129   -265   -266       C  
ATOM    892  CD1 ILE A 101       4.247  23.981   1.003  1.00 19.47           C  
ANISOU  892  CD1 ILE A 101     1515   3669   2212   -231   -388   -419       C  
ATOM    893  N   LYS A 102       7.018  20.730  -2.322  1.00 15.46           N  
ANISOU  893  N   LYS A 102     1158   2950   1767    -94   -145   -352       N  
ATOM    894  CA  LYS A 102       7.727  19.483  -2.544  1.00 14.26           C  
ANISOU  894  CA  LYS A 102     1413   2663   1343   -233   -228   -141       C  
ATOM    895  C   LYS A 102       9.115  19.496  -1.905  1.00 12.54           C  
ANISOU  895  C   LYS A 102     1305   2293   1165   -235   -185   -196       C  
ATOM    896  O   LYS A 102       9.617  18.499  -1.381  1.00 13.09           O  
ANISOU  896  O   LYS A 102     1483   2159   1331   -350    -53    -79       O  
ATOM    897  CB  LYS A 102       7.835  19.248  -4.035  1.00 16.30           C  
ANISOU  897  CB  LYS A 102     1930   2847   1417    -72   -587   -452       C  
ATOM    898  CG  LYS A 102       8.344  17.857  -4.321  1.00 18.12           C  
ANISOU  898  CG  LYS A 102     2183   2895   1805    178   -471   -413       C  
ATOM    899  CD  LYS A 102       7.276  16.824  -4.049  1.00 23.45           C  
ANISOU  899  CD  LYS A 102     2615   2910   3387   -234   -657   -881       C  
ATOM    900  CE  LYS A 102       7.740  15.442  -4.445  1.00 23.89           C  
ANISOU  900  CE  LYS A 102     2717   2889   3470   -111    381   -352       C  
ATOM    901  NZ  LYS A 102       6.758  14.395  -4.008  1.00 23.79           N  
ANISOU  901  NZ  LYS A 102     3257   3199   2583   -917   -269   -678       N  
ATOM    902  N   TYR A 103       9.790  20.676  -1.932  1.00 12.29           N  
ANISOU  902  N   TYR A 103     1140   2172   1359    -57    -54    -68       N  
ATOM    903  CA  TYR A 103      11.127  20.695  -1.347  1.00 12.06           C  
ANISOU  903  CA  TYR A 103     1020   2197   1367    -83      4    114       C  
ATOM    904  C   TYR A 103      11.053  20.578   0.173  1.00 10.50           C  
ANISOU  904  C   TYR A 103      936   1712   1340    -35    -88     43       C  
ATOM    905  O   TYR A 103      12.020  20.119   0.791  1.00 10.68           O  
ANISOU  905  O   TYR A 103     1005   1718   1334    -86    -29    103       O  
ATOM    906  CB  TYR A 103      11.815  21.993  -1.760  1.00 12.58           C  
ANISOU  906  CB  TYR A 103     1136   2093   1549    -26    -61    256       C  
ATOM    907  CG  TYR A 103      12.203  22.152  -3.205  1.00 13.79           C  
ANISOU  907  CG  TYR A 103      998   2654   1589    369     38    606       C  
ATOM    908  CD1 TYR A 103      11.689  21.450  -4.236  1.00 18.05           C  
ANISOU  908  CD1 TYR A 103     1856   3201   1802    109    725   -294       C  
ATOM    909  CD2 TYR A 103      13.069  23.170  -3.578  1.00 15.54           C  
ANISOU  909  CD2 TYR A 103     1256   2632   2018    412    233    769       C  
ATOM    910  CE1 TYR A 103      12.009  21.616  -5.560  1.00 20.46           C  
ANISOU  910  CE1 TYR A 103     2749   3282   1743    895    567     31       C  
ATOM    911  CE2 TYR A 103      13.460  23.432  -4.856  1.00 18.69           C  
ANISOU  911  CE2 TYR A 103     1887   2884   2331    809    701   1184       C  
ATOM    912  CZ  TYR A 103      12.915  22.640  -5.845  1.00 19.82           C  
ANISOU  912  CZ  TYR A 103     2405   3270   1854   1356    734    897       C  
ATOM    913  OH  TYR A 103      13.279  22.908  -7.137  1.00 26.35           O  
ANISOU  913  OH  TYR A 103     3916   4030   2063   2084   1236   1317       O  
ATOM    914  N   LEU A 104       9.943  20.999   0.784  1.00 10.39           N  
ANISOU  914  N   LEU A 104     1080   1610   1258     52   -118     21       N  
ATOM    915  CA  LEU A 104       9.722  20.741   2.206  1.00 10.40           C  
ANISOU  915  CA  LEU A 104      891   1777   1282    -98   -104    -43       C  
ATOM    916  C   LEU A 104       9.577  19.264   2.492  1.00 10.38           C  
ANISOU  916  C   LEU A 104      818   1792   1333   -139    -47    -10       C  
ATOM    917  O   LEU A 104      10.001  18.770   3.540  1.00 10.77           O  
ANISOU  917  O   LEU A 104      981   1769   1343   -142      6     17       O  
ATOM    918  CB  LEU A 104       8.549  21.553   2.738  1.00 11.72           C  
ANISOU  918  CB  LEU A 104     1154   1845   1455     50    -49   -126       C  
ATOM    919  CG  LEU A 104       8.689  23.065   2.608  1.00 12.75           C  
ANISOU  919  CG  LEU A 104     1297   1802   1747     94    -86     -9       C  
ATOM    920  CD1 LEU A 104       7.499  23.763   3.240  1.00 16.99           C  
ANISOU  920  CD1 LEU A 104     1658   2237   2561    556   -381   -603       C  
ATOM    921  CD2 LEU A 104       9.947  23.597   3.262  1.00 16.50           C  
ANISOU  921  CD2 LEU A 104     1605   2065   2597    -78   -268   -552       C  
ATOM    922  N   GLU A 105       8.965  18.518   1.581  1.00 10.08           N  
ANISOU  922  N   GLU A 105      816   1696   1317    -52    -15     61       N  
ATOM    923  CA  GLU A 105       8.926  17.081   1.682  1.00 10.24           C  
ANISOU  923  CA  GLU A 105      869   1768   1254    -44   -138    -72       C  
ATOM    924  C   GLU A 105      10.357  16.489   1.628  1.00  9.84           C  
ANISOU  924  C   GLU A 105      859   1627   1253   -119   -197    -41       C  
ATOM    925  O   GLU A 105      10.736  15.647   2.447  1.00 10.25           O  
ANISOU  925  O   GLU A 105      861   1694   1338    -68    -90    -38       O  
ATOM    926  CB  GLU A 105       8.031  16.483   0.600  1.00 11.80           C  
ANISOU  926  CB  GLU A 105      864   1965   1654    -77   -335   -152       C  
ATOM    927  CG  GLU A 105       7.941  14.964   0.733  1.00 14.62           C  
ANISOU  927  CG  GLU A 105     1362   1968   2225   -208   -413   -262       C  
ATOM    928  CD  GLU A 105       7.210  14.336  -0.430  1.00 17.40           C  
ANISOU  928  CD  GLU A 105     1409   2335   2867     -3   -759   -822       C  
ATOM    929  OE1 GLU A 105       6.685  15.021  -1.322  1.00 18.29           O  
ANISOU  929  OE1 GLU A 105     1808   2718   2424    159   -561   -909       O  
ATOM    930  OE2 GLU A 105       7.074  13.086  -0.449  1.00 26.16           O  
ANISOU  930  OE2 GLU A 105     3143   2408   4389   -404  -1637   -762       O  
ATOM    931  N   PHE A 106      11.170  17.026   0.717  1.00  9.83           N  
ANISOU  931  N   PHE A 106      808   1631   1297    -73    -84   -172       N  
ATOM    932  CA  PHE A 106      12.550  16.507   0.628  1.00  9.88           C  
ANISOU  932  CA  PHE A 106      904   1688   1163    -70    -94    -17       C  
ATOM    933  C   PHE A 106      13.347  16.778   1.910  1.00  9.05           C  
ANISOU  933  C   PHE A 106      855   1474   1110   -127    -64    -37       C  
ATOM    934  O   PHE A 106      14.089  15.923   2.375  1.00  9.85           O  
ANISOU  934  O   PHE A 106      956   1599   1187    -52     -6    -34       O  
ATOM    935  CB  PHE A 106      13.294  17.203  -0.540  1.00 10.43           C  
ANISOU  935  CB  PHE A 106     1061   1885   1017     15    -18    -70       C  
ATOM    936  CG  PHE A 106      12.704  16.915  -1.922  1.00 11.26           C  
ANISOU  936  CG  PHE A 106     1050   2146   1080    -12     46   -204       C  
ATOM    937  CD1 PHE A 106      11.961  15.779  -2.198  1.00 13.06           C  
ANISOU  937  CD1 PHE A 106     1423   2334   1204   -178   -109   -328       C  
ATOM    938  CD2 PHE A 106      12.941  17.861  -2.928  1.00 12.60           C  
ANISOU  938  CD2 PHE A 106     1302   2364   1121    142    -36     -4       C  
ATOM    939  CE1 PHE A 106      11.479  15.585  -3.482  1.00 16.60           C  
ANISOU  939  CE1 PHE A 106     1526   3561   1221   -578    -30   -530       C  
ATOM    940  CE2 PHE A 106      12.452  17.662  -4.205  1.00 15.60           C  
ANISOU  940  CE2 PHE A 106     1447   3250   1232    165   -179     98       C  
ATOM    941  CZ  PHE A 106      11.722  16.516  -4.460  1.00 17.95           C  
ANISOU  941  CZ  PHE A 106     1753   4090    978   -463     13   -397       C  
ATOM    942  N   ILE A 107      13.237  17.974   2.489  1.00  8.80           N  
ANISOU  942  N   ILE A 107      789   1503   1050   -104     37     14       N  
ATOM    943  CA  ILE A 107      13.991  18.239   3.705  1.00  9.02           C  
ANISOU  943  CA  ILE A 107      879   1462   1085   -107    -53     29       C  
ATOM    944  C   ILE A 107      13.464  17.387   4.859  1.00  8.89           C  
ANISOU  944  C   ILE A 107      986   1295   1097    -95    -76     20       C  
ATOM    945  O   ILE A 107      14.225  16.967   5.726  1.00  9.51           O  
ANISOU  945  O   ILE A 107      949   1544   1122   -111   -108     47       O  
ATOM    946  CB  ILE A 107      14.105  19.724   4.061  1.00  8.72           C  
ANISOU  946  CB  ILE A 107      888   1370   1055    -85    -92    113       C  
ATOM    947  CG1 ILE A 107      15.318  19.972   4.984  1.00  9.36           C  
ANISOU  947  CG1 ILE A 107     1043   1430   1084   -166    -97     48       C  
ATOM    948  CG2 ILE A 107      12.832  20.293   4.675  1.00 10.46           C  
ANISOU  948  CG2 ILE A 107     1028   1527   1421   -112    153    -66       C  
ATOM    949  CD1 ILE A 107      15.603  21.403   5.278  1.00 10.16           C  
ANISOU  949  CD1 ILE A 107     1143   1526   1192   -261     -5    -94       C  
ATOM    950  N   SER A 108      12.141  17.117   4.873  1.00  9.14           N  
ANISOU  950  N   SER A 108      884   1442   1145    -96    -49     69       N  
ATOM    951  CA  SER A 108      11.596  16.230   5.893  1.00 10.03           C  
ANISOU  951  CA  SER A 108     1020   1679   1110    -76     21    152       C  
ATOM    952  C   SER A 108      12.207  14.835   5.821  1.00  9.58           C  
ANISOU  952  C   SER A 108      803   1603   1232   -193   -127    181       C  
ATOM    953  O   SER A 108      12.561  14.256   6.824  1.00 10.55           O  
ANISOU  953  O   SER A 108      971   1758   1280    -59   -105    210       O  
ATOM    954  CB  SER A 108      10.075  16.165   5.728  1.00 10.62           C  
ANISOU  954  CB  SER A 108      967   1748   1322    -29     57    299       C  
ATOM    955  OG  SER A 108       9.457  17.384   5.983  1.00 12.37           O  
ANISOU  955  OG  SER A 108     1181   1914   1605    136    333    433       O  
ATOM    956  N   GLU A 109      12.387  14.329   4.591  1.00 10.05           N  
ANISOU  956  N   GLU A 109     1097   1422   1300   -251   -152    108       N  
ATOM    957  CA  GLU A 109      13.065  13.022   4.412  1.00 11.01           C  
ANISOU  957  CA  GLU A 109     1211   1489   1481   -232   -218    -57       C  
ATOM    958  C   GLU A 109      14.485  13.072   4.924  1.00 10.55           C  
ANISOU  958  C   GLU A 109     1123   1403   1483    -64    -91   -110       C  
ATOM    959  O   GLU A 109      14.962  12.135   5.574  1.00 11.39           O  
ANISOU  959  O   GLU A 109     1284   1439   1606      5    -96    -53       O  
ATOM    960  CB AGLU A 109      13.164  12.552   2.937  0.75 16.35           C  
ANISOU  960  CB AGLU A 109     2505   1974   1732    -76   -753   -598       C  
ATOM    961  CB BGLU A 109      12.900  12.645   2.947  0.25  8.78           C  
ANISOU  961  CB BGLU A 109      773   1157   1404   -188    -37    259       C  
ATOM    962  CG AGLU A 109      14.051  11.385   2.624  0.75 30.81           C  
ANISOU  962  CG AGLU A 109     4483   3920   3305   1361    325  -1439       C  
ATOM    963  CG BGLU A 109      11.528  12.323   2.456  0.25  9.07           C  
ANISOU  963  CG BGLU A 109     1253    810   1383   -688   -207    -97       C  
ATOM    964  CD AGLU A 109      15.481  11.170   2.335  0.75 37.10           C  
ANISOU  964  CD AGLU A 109     4478   3734   5883   1882    367   -307       C  
ATOM    965  CD BGLU A 109      11.153  12.442   1.003  0.25 20.19           C  
ANISOU  965  CD BGLU A 109     3526   2502   1642  -1334  -1196      0       C  
ATOM    966  OE1AGLU A 109      16.423  11.994   2.140  0.75 45.07           O  
ANISOU  966  OE1AGLU A 109     4517   5074   7534   1604    650    937       O  
ATOM    967  OE1BGLU A 109      11.894  12.862   0.084  0.25 24.06           O  
ANISOU  967  OE1BGLU A 109     6095   1672   1375   -867   -400    369       O  
ATOM    968  OE2AGLU A 109      15.885   9.949   2.216  0.75 46.57           O  
ANISOU  968  OE2AGLU A 109     5287   3944   8462   2117  -1360  -2564       O  
ATOM    969  OE2BGLU A 109       9.974  12.087   0.726  0.25 27.98           O  
ANISOU  969  OE2BGLU A 109     4098   2692   3840  -1129  -2766   -369       O  
ATOM    970  N   ALA A 110      15.198  14.164   4.658  1.00  9.63           N  
ANISOU  970  N   ALA A 110      989   1434   1237     22     16   -133       N  
ATOM    971  CA  ALA A 110      16.567  14.290   5.136  1.00  9.88           C  
ANISOU  971  CA  ALA A 110      918   1467   1368    122     15   -124       C  
ATOM    972  C   ALA A 110      16.660  14.343   6.646  1.00  9.94           C  
ANISOU  972  C   ALA A 110      955   1464   1360      6    -65     18       C  
ATOM    973  O   ALA A 110      17.553  13.725   7.255  1.00 10.67           O  
ANISOU  973  O   ALA A 110     1014   1555   1486     66   -139     16       O  
ATOM    974  CB  ALA A 110      17.230  15.545   4.548  1.00 10.90           C  
ANISOU  974  CB  ALA A 110     1066   1668   1408   -117     11     14       C  
ATOM    975  N   ILE A 111      15.733  15.070   7.273  1.00  9.44           N  
ANISOU  975  N   ILE A 111      945   1484   1159    -26    -70     31       N  
ATOM    976  CA  ILE A 111      15.661  15.112   8.722  1.00  9.46           C  
ANISOU  976  CA  ILE A 111      854   1582   1159     29   -127    204       C  
ATOM    977  C   ILE A 111      15.487  13.708   9.311  1.00 10.14           C  
ANISOU  977  C   ILE A 111      761   1716   1377     29   -112    356       C  
ATOM    978  O   ILE A 111      16.200  13.314  10.223  1.00 10.87           O  
ANISOU  978  O   ILE A 111      983   1651   1497     64   -231    293       O  
ATOM    979  CB  ILE A 111      14.533  16.056   9.204  1.00  9.53           C  
ANISOU  979  CB  ILE A 111      970   1552   1098    -11   -119     -1       C  
ATOM    980  CG1 ILE A 111      14.897  17.505   8.811  1.00  9.70           C  
ANISOU  980  CG1 ILE A 111      980   1485   1219    -49   -123    -87       C  
ATOM    981  CG2 ILE A 111      14.249  15.879  10.686  1.00 11.08           C  
ANISOU  981  CG2 ILE A 111     1201   1828   1179    105     19     64       C  
ATOM    982  CD1 ILE A 111      13.677  18.431   8.790  1.00 10.13           C  
ANISOU  982  CD1 ILE A 111      927   1529   1392      0    -18    -77       C  
ATOM    983  N   ILE A 112      14.502  12.990   8.775  1.00 10.75           N  
ANISOU  983  N   ILE A 112      969   1646   1470     12   -177    141       N  
ATOM    984  CA  ILE A 112      14.231  11.651   9.312  1.00 11.11           C  
ANISOU  984  CA  ILE A 112     1029   1699   1495     -9   -211    168       C  
ATOM    985  C   ILE A 112      15.427  10.770   9.142  1.00 11.68           C  
ANISOU  985  C   ILE A 112     1131   1607   1700      6    -77    198       C  
ATOM    986  O   ILE A 112      15.805   9.998  10.032  1.00 13.05           O  
ANISOU  986  O   ILE A 112     1225   1680   2054    -34   -281    370       O  
ATOM    987  CB  ILE A 112      12.944  11.097   8.639  1.00 12.66           C  
ANISOU  987  CB  ILE A 112     1155   1797   1860   -264   -262    407       C  
ATOM    988  CG1 ILE A 112      11.737  11.884   9.089  1.00 16.46           C  
ANISOU  988  CG1 ILE A 112     1002   2669   2585      6   -162    659       C  
ATOM    989  CG2 ILE A 112      12.803   9.609   8.861  1.00 17.58           C  
ANISOU  989  CG2 ILE A 112     1718   1933   3030   -533   -811    742       C  
ATOM    990  CD1 ILE A 112      10.447  11.713   8.349  1.00 20.17           C  
ANISOU  990  CD1 ILE A 112     1375   2472   3815   -214   -764    508       C  
ATOM    991  N   HIS A 113      16.082  10.824   7.965  1.00 11.61           N  
ANISOU  991  N   HIS A 113     1178   1553   1680     27   -121   -102       N  
ATOM    992  CA  HIS A 113      17.286   9.978   7.783  1.00 12.60           C  
ANISOU  992  CA  HIS A 113     1432   1653   1704    180   -108   -162       C  
ATOM    993  C   HIS A 113      18.377  10.307   8.781  1.00 12.19           C  
ANISOU  993  C   HIS A 113     1232   1576   1822     59   -110     92       C  
ATOM    994  O   HIS A 113      18.996   9.360   9.329  1.00 13.97           O  
ANISOU  994  O   HIS A 113     1397   1565   2345    277   -233     74       O  
ATOM    995  CB  HIS A 113      17.763  10.198   6.352  1.00 14.13           C  
ANISOU  995  CB  HIS A 113     1621   1991   1757    180      5   -329       C  
ATOM    996  CG  HIS A 113      18.875   9.268   6.007  1.00 21.95           C  
ANISOU  996  CG  HIS A 113     2219   3367   2754    770    574   -660       C  
ATOM    997  ND1 HIS A 113      20.199   9.406   6.317  1.00 29.81           N  
ANISOU  997  ND1 HIS A 113     2092   5528   3707   1427    398  -1134       N  
ATOM    998  CD2 HIS A 113      18.717   8.080   5.336  1.00 26.61           C  
ANISOU  998  CD2 HIS A 113     3733   3552   2828   1854     39  -1082       C  
ATOM    999  CE1 HIS A 113      20.816   8.352   5.855  1.00 30.99           C  
ANISOU  999  CE1 HIS A 113     3012   5453   3311   2004   1063   -141       C  
ATOM   1000  NE2 HIS A 113      19.954   7.511   5.253  1.00 32.50           N  
ANISOU 1000  NE2 HIS A 113     4159   4078   4110   2399    457   -274       N  
ATOM   1001  N   VAL A 114      18.688  11.579   8.964  1.00 11.78           N  
ANISOU 1001  N   VAL A 114     1094   1526   1855    114   -121    106       N  
ATOM   1002  CA  VAL A 114      19.779  11.936   9.884  1.00 11.27           C  
ANISOU 1002  CA  VAL A 114      946   1572   1765    138    -23     57       C  
ATOM   1003  C   VAL A 114      19.423  11.558  11.332  1.00 11.04           C  
ANISOU 1003  C   VAL A 114     1020   1333   1842     11    -77    189       C  
ATOM   1004  O   VAL A 114      20.288  11.064  12.071  1.00 12.20           O  
ANISOU 1004  O   VAL A 114     1017   1511   2109    162   -169    301       O  
ATOM   1005  CB  VAL A 114      20.112  13.408   9.715  1.00 11.19           C  
ANISOU 1005  CB  VAL A 114     1044   1581   1626     44     22    160       C  
ATOM   1006  CG1 VAL A 114      21.034  13.924  10.794  1.00 12.37           C  
ANISOU 1006  CG1 VAL A 114     1194   1653   1854     25   -260     88       C  
ATOM   1007  CG2 VAL A 114      20.756  13.657   8.326  1.00 12.20           C  
ANISOU 1007  CG2 VAL A 114     1246   1679   1711    277    140    116       C  
ATOM   1008  N   LEU A 115      18.177  11.759  11.733  1.00 11.99           N  
ANISOU 1008  N   LEU A 115     1073   1957   1525    283    -88    137       N  
ATOM   1009  CA  LEU A 115      17.800  11.368  13.093  1.00 11.75           C  
ANISOU 1009  CA  LEU A 115     1196   1781   1489    271   -137    138       C  
ATOM   1010  C   LEU A 115      17.949   9.888  13.296  1.00 11.88           C  
ANISOU 1010  C   LEU A 115     1035   1762   1716    149   -280    203       C  
ATOM   1011  O   LEU A 115      18.373   9.432  14.350  1.00 12.84           O  
ANISOU 1011  O   LEU A 115     1083   1926   1868    141   -272    334       O  
ATOM   1012  CB ALEU A 115      16.414  11.914  13.465  0.55 11.83           C  
ANISOU 1012  CB ALEU A 115     1031   1671   1795    104    -45    153       C  
ATOM   1013  CB BLEU A 115      16.333  11.723  13.408  0.45 12.14           C  
ANISOU 1013  CB BLEU A 115     1091   1651   1871     98    -15    347       C  
ATOM   1014  CG ALEU A 115      16.460  13.302  14.114  0.55 10.14           C  
ANISOU 1014  CG ALEU A 115     1291   1806    757    302   -145    290       C  
ATOM   1015  CG BLEU A 115      16.030  13.207  13.517  0.45 10.43           C  
ANISOU 1015  CG BLEU A 115     1016   1583   1362    102     -6    669       C  
ATOM   1016  CD1ALEU A 115      17.146  14.313  13.235  0.55 10.84           C  
ANISOU 1016  CD1ALEU A 115     1201   1745   1172   -131   -232    179       C  
ATOM   1017  CD1BLEU A 115      14.520  13.425  13.609  0.45 14.71           C  
ANISOU 1017  CD1BLEU A 115     1137   2655   1798    486    507    880       C  
ATOM   1018  CD2ALEU A 115      15.004  13.750  14.340  0.55 11.76           C  
ANISOU 1018  CD2ALEU A 115     1187   1805   1478    199    -47    158       C  
ATOM   1019  CD2BLEU A 115      16.745  13.812  14.716  0.45 15.65           C  
ANISOU 1019  CD2BLEU A 115     2323   1925   1699    364   -493    155       C  
ATOM   1020  N   HIS A 116      17.630   9.079  12.261  1.00 12.24           N  
ANISOU 1020  N   HIS A 116     1215   1667   1767    -96   -259    340       N  
ATOM   1021  CA  HIS A 116      17.779   7.634  12.381  1.00 12.91           C  
ANISOU 1021  CA  HIS A 116     1245   1686   1973   -210   -164    191       C  
ATOM   1022  C   HIS A 116      19.266   7.275  12.505  1.00 12.62           C  
ANISOU 1022  C   HIS A 116     1386   1473   1936    -66   -320     39       C  
ATOM   1023  O   HIS A 116      19.603   6.385  13.297  1.00 15.44           O  
ANISOU 1023  O   HIS A 116     1755   1738   2372    116   -367    307       O  
ATOM   1024  CB AHIS A 116      17.069   7.010  11.180  0.57 14.84           C  
ANISOU 1024  CB AHIS A 116     1257   2084   2297   -342   -248    -24       C  
ATOM   1025  CB BHIS A 116      17.092   6.881  11.253  0.43 19.10           C  
ANISOU 1025  CB BHIS A 116     2119   1966   3174     89  -1352   -155       C  
ATOM   1026  CG AHIS A 116      17.192   5.521  11.182  0.57 20.98           C  
ANISOU 1026  CG AHIS A 116     2468   2088   3415   -326   -779   -448       C  
ATOM   1027  CG BHIS A 116      16.705   5.487  11.660  0.43 18.97           C  
ANISOU 1027  CG BHIS A 116     2470   1540   3196    435  -1034   -667       C  
ATOM   1028  ND1AHIS A 116      18.154   4.822  10.516  0.57 24.69           N  
ANISOU 1028  ND1AHIS A 116     3275   1992   4115   -266   -376   -915       N  
ATOM   1029  ND1BHIS A 116      15.875   4.756  10.864  0.43 23.65           N  
ANISOU 1029  ND1BHIS A 116     3438   1920   3629   -163  -1448   -509       N  
ATOM   1030  CD2AHIS A 116      16.384   4.633  11.815  0.57 20.98           C  
ANISOU 1030  CD2AHIS A 116     2598   1594   3780   -189  -1033   -153       C  
ATOM   1031  CD2BHIS A 116      17.036   4.723  12.723  0.43 22.72           C  
ANISOU 1031  CD2BHIS A 116     3149   1532   3951   -101  -1628   -180       C  
ATOM   1032  CE1AHIS A 116      17.939   3.543  10.748  0.57 23.35           C  
ANISOU 1032  CE1AHIS A 116     3206   2072   3594   -420   -754   -839       C  
ATOM   1033  CE1BHIS A 116      15.714   3.583  11.440  0.43 22.47           C  
ANISOU 1033  CE1BHIS A 116     2515   2090   3931   -141  -1345   -285       C  
ATOM   1034  NE2AHIS A 116      16.863   3.382  11.536  0.57 22.52           N  
ANISOU 1034  NE2AHIS A 116     2519   1971   4068    218   -993   -253       N  
ATOM   1035  NE2BHIS A 116      16.406   3.510  12.586  0.43 19.35           N  
ANISOU 1035  NE2BHIS A 116     2073   1570   3711    209  -1050   -616       N  
ATOM   1036  N   SER A 117      20.148   7.912  11.720  1.00 13.27           N  
ANISOU 1036  N   SER A 117     1209   1735   2099     64    -53    -33       N  
ATOM   1037  CA  SER A 117      21.551   7.625  11.788  1.00 15.72           C  
ANISOU 1037  CA  SER A 117     1315   1921   2738    252    -52   -149       C  
ATOM   1038  C   SER A 117      22.176   8.003  13.122  1.00 14.59           C  
ANISOU 1038  C   SER A 117     1046   1551   2948    171   -276    233       C  
ATOM   1039  O   SER A 117      23.007   7.270  13.651  1.00 17.98           O  
ANISOU 1039  O   SER A 117     1423   1851   3559    326   -446    480       O  
ATOM   1040  CB ASER A 117      22.310   8.426  10.711  0.48 18.32           C  
ANISOU 1040  CB ASER A 117     1547   2674   2740    140    663   -503       C  
ATOM   1041  CB BSER A 117      22.255   8.444  10.684  0.52 18.75           C  
ANISOU 1041  CB BSER A 117     1615   2785   2725    172    736   -440       C  
ATOM   1042  OG ASER A 117      21.998   8.016   9.400  0.48 16.26           O  
ANISOU 1042  OG ASER A 117     1146   2214   2820    220    399   -351       O  
ATOM   1043  OG BSER A 117      23.625   8.142  10.763  0.52 24.50           O  
ANISOU 1043  OG BSER A 117     1716   4085   3508    568    871   -546       O  
ATOM   1044  N   ARG A 118      21.783   9.160  13.668  1.00 13.42           N  
ANISOU 1044  N   ARG A 118     1266   1754   2078    175   -239    333       N  
ATOM   1045  CA  ARG A 118      22.383   9.653  14.887  1.00 13.72           C  
ANISOU 1045  CA  ARG A 118     1026   2046   2143    -23   -294    388       C  
ATOM   1046  C   ARG A 118      21.762   9.150  16.210  1.00 12.68           C  
ANISOU 1046  C   ARG A 118     1061   1740   2016    101   -347    337       C  
ATOM   1047  O   ARG A 118      22.438   9.140  17.201  1.00 14.08           O  
ANISOU 1047  O   ARG A 118     1203   1896   2251   -122   -485    492       O  
ATOM   1048  CB AARG A 118      22.277  11.193  14.886  0.66 14.06           C  
ANISOU 1048  CB AARG A 118     1531   1996   1814    -62   -211    353       C  
ATOM   1049  CB BARG A 118      22.464  11.191  14.834  0.34 13.63           C  
ANISOU 1049  CB BARG A 118      639   2051   2488   -338   -687    519       C  
ATOM   1050  CG AARG A 118      23.352  11.762  13.929  0.66 15.85           C  
ANISOU 1050  CG AARG A 118     1136   2513   2372   -178   -406    727       C  
ATOM   1051  CG BARG A 118      23.129  11.688  13.542  0.34 16.87           C  
ANISOU 1051  CG BARG A 118     1222   2538   2649    -54   -645   1080       C  
ATOM   1052  CD AARG A 118      23.186  13.242  13.866  0.66 21.01           C  
ANISOU 1052  CD AARG A 118     2108   2438   3437   -615   -719    958       C  
ATOM   1053  CD BARG A 118      23.448  13.172  13.566  0.34 19.34           C  
ANISOU 1053  CD BARG A 118     1366   2722   3262   -636   -422    994       C  
ATOM   1054  NE AARG A 118      24.288  13.951  13.298  0.66 18.32           N  
ANISOU 1054  NE AARG A 118     1668   2167   3127    -63   -305    412       N  
ATOM   1055  NE BARG A 118      24.176  13.493  14.785  0.34 21.93           N  
ANISOU 1055  NE BARG A 118     1919   3047   3366   -276   -521    436       N  
ATOM   1056  CZ AARG A 118      25.281  14.601  13.838  0.66 18.22           C  
ANISOU 1056  CZ AARG A 118     1622   3062   2240   -468   -126    647       C  
ATOM   1057  CZ BARG A 118      25.056  14.460  14.983  0.34 17.11           C  
ANISOU 1057  CZ BARG A 118      661   2875   2964    452    268   -593       C  
ATOM   1058  NH1AARG A 118      25.457  14.693  15.141  0.66 20.71           N  
ANISOU 1058  NH1AARG A 118     2854   2896   2118  -1056   -193   1393       N  
ATOM   1059  NH1BARG A 118      25.293  15.263  13.952  0.34 26.98           N  
ANISOU 1059  NH1BARG A 118     2566   3539   4146   -867   -379    494       N  
ATOM   1060  NH2AARG A 118      26.185  15.210  13.070  0.66 19.07           N  
ANISOU 1060  NH2AARG A 118     1884   3622   1741   -647   -148    569       N  
ATOM   1061  NH2BARG A 118      25.645  14.634  16.149  0.34 24.33           N  
ANISOU 1061  NH2BARG A 118     1769   3540   3934   1185  -1082   -749       N  
ATOM   1062  N   HIS A 119      20.488   8.723  16.159  1.00 13.03           N  
ANISOU 1062  N   HIS A 119     1019   2064   1868     57   -149    285       N  
ATOM   1063  CA  HIS A 119      19.749   8.411  17.377  1.00 12.27           C  
ANISOU 1063  CA  HIS A 119     1153   1759   1750    131   -131    219       C  
ATOM   1064  C   HIS A 119      18.920   7.160  17.274  1.00 12.17           C  
ANISOU 1064  C   HIS A 119     1272   1736   1616    110    -33    103       C  
ATOM   1065  O   HIS A 119      17.743   7.160  17.649  1.00 12.79           O  
ANISOU 1065  O   HIS A 119     1184   1931   1744     48   -155    198       O  
ATOM   1066  CB  HIS A 119      18.842   9.573  17.832  1.00 12.67           C  
ANISOU 1066  CB  HIS A 119     1179   1760   1875    142   -209    115       C  
ATOM   1067  CG  HIS A 119      19.570  10.869  17.838  1.00 11.56           C  
ANISOU 1067  CG  HIS A 119     1267   1832   1294    131     14    216       C  
ATOM   1068  ND1 HIS A 119      20.632  11.179  18.644  1.00 12.16           N  
ANISOU 1068  ND1 HIS A 119     1468   1668   1485    -36   -166    224       N  
ATOM   1069  CD2 HIS A 119      19.478  11.937  17.012  1.00 14.19           C  
ANISOU 1069  CD2 HIS A 119     1622   2120   1650   -144   -210    567       C  
ATOM   1070  CE1 HIS A 119      21.080  12.392  18.354  1.00 13.11           C  
ANISOU 1070  CE1 HIS A 119     1672   1842   1466   -102    -56    364       C  
ATOM   1071  NE2 HIS A 119      20.379  12.841  17.322  1.00 14.56           N  
ANISOU 1071  NE2 HIS A 119     1694   2015   1821    -58   -289    479       N  
ATOM   1072  N   PRO A 120      19.543   6.069  16.812  1.00 13.75           N  
ANISOU 1072  N   PRO A 120     1280   1719   2226     85     41     72       N  
ATOM   1073  CA  PRO A 120      18.715   4.887  16.544  1.00 13.94           C  
ANISOU 1073  CA  PRO A 120     1557   1852   1888    -28    -65   -204       C  
ATOM   1074  C   PRO A 120      17.948   4.384  17.756  1.00 13.13           C  
ANISOU 1074  C   PRO A 120     1265   1581   2144    181   -195    164       C  
ATOM   1075  O   PRO A 120      16.797   3.970  17.622  1.00 14.17           O  
ANISOU 1075  O   PRO A 120     1458   1792   2133    -40    -71    -42       O  
ATOM   1076  CB  PRO A 120      19.683   3.825  16.054  1.00 16.94           C  
ANISOU 1076  CB  PRO A 120     1804   2111   2522    106     97   -509       C  
ATOM   1077  CG  PRO A 120      21.023   4.268  16.614  1.00 17.02           C  
ANISOU 1077  CG  PRO A 120     1700   1718   3050    269   -133     17       C  
ATOM   1078  CD  PRO A 120      20.941   5.760  16.521  1.00 14.59           C  
ANISOU 1078  CD  PRO A 120     1502   1732   2311    211    397    226       C  
ATOM   1079  N   GLY A 121      18.515   4.414  18.945  1.00 13.54           N  
ANISOU 1079  N   GLY A 121     1535   1559   2050     50   -206    323       N  
ATOM   1080  CA  GLY A 121      17.839   3.911  20.114  1.00 15.79           C  
ANISOU 1080  CA  GLY A 121     1952   1767   2282    231     67    524       C  
ATOM   1081  C   GLY A 121      16.669   4.738  20.583  1.00 15.01           C  
ANISOU 1081  C   GLY A 121     1957   1590   2156    -43     83    108       C  
ATOM   1082  O   GLY A 121      15.797   4.245  21.302  1.00 18.96           O  
ANISOU 1082  O   GLY A 121     2313   2035   2857   -139    590    245       O  
ATOM   1083  N   ASN A 122      16.534   5.960  20.104  1.00 13.12           N  
ANISOU 1083  N   ASN A 122     1474   1719   1793     41     -8     76       N  
ATOM   1084  CA  ASN A 122      15.447   6.877  20.366  1.00 13.31           C  
ANISOU 1084  CA  ASN A 122     1616   1565   1875    -68    168     35       C  
ATOM   1085  C   ASN A 122      14.677   7.180  19.102  1.00 13.78           C  
ANISOU 1085  C   ASN A 122     1310   1730   2195    -16    -22    102       C  
ATOM   1086  O   ASN A 122      13.861   8.131  19.055  1.00 16.00           O  
ANISOU 1086  O   ASN A 122     1347   1798   2935     77    113    202       O  
ATOM   1087  CB  ASN A 122      15.899   8.133  21.094  1.00 15.30           C  
ANISOU 1087  CB  ASN A 122     1799   1871   2144   -238    326   -323       C  
ATOM   1088  CG  ASN A 122      16.342   7.774  22.507  1.00 16.95           C  
ANISOU 1088  CG  ASN A 122     2420   1982   2039    -47    164   -465       C  
ATOM   1089  OD1 ASN A 122      15.613   7.439  23.390  1.00 20.34           O  
ANISOU 1089  OD1 ASN A 122     2924   2633   2170    258    642   -296       O  
ATOM   1090  ND2 ASN A 122      17.650   7.829  22.620  1.00 22.94           N  
ANISOU 1090  ND2 ASN A 122     2510   3970   2236   -406   -168   -449       N  
ATOM   1091  N   PHE A 123      14.890   6.396  18.075  1.00 13.44           N  
ANISOU 1091  N   PHE A 123     1532   1468   2105    -76   -281    210       N  
ATOM   1092  CA  PHE A 123      14.298   6.603  16.781  1.00 13.60           C  
ANISOU 1092  CA  PHE A 123     1515   1459   2195   -213   -385    330       C  
ATOM   1093  C   PHE A 123      13.951   5.304  16.104  1.00 13.35           C  
ANISOU 1093  C   PHE A 123     1340   1479   2255     -7   -494    290       C  
ATOM   1094  O   PHE A 123      14.211   5.084  14.919  1.00 14.66           O  
ANISOU 1094  O   PHE A 123     1572   1706   2293   -214   -388    103       O  
ATOM   1095  CB  PHE A 123      15.174   7.524  15.883  1.00 13.26           C  
ANISOU 1095  CB  PHE A 123     1398   1652   1989   -136   -277    178       C  
ATOM   1096  CG  PHE A 123      14.318   8.325  14.903  1.00 11.94           C  
ANISOU 1096  CG  PHE A 123     1249   1401   1887   -269   -202    207       C  
ATOM   1097  CD1 PHE A 123      13.409   9.267  15.371  1.00 13.65           C  
ANISOU 1097  CD1 PHE A 123     1630   1649   1907      6   -283     48       C  
ATOM   1098  CD2 PHE A 123      14.465   8.187  13.510  1.00 13.95           C  
ANISOU 1098  CD2 PHE A 123     1185   2200   1916    -38    -65    273       C  
ATOM   1099  CE1 PHE A 123      12.666  10.030  14.473  1.00 13.68           C  
ANISOU 1099  CE1 PHE A 123     1442   1889   1866    -59   -273    196       C  
ATOM   1100  CE2 PHE A 123      13.738   8.965  12.627  1.00 14.49           C  
ANISOU 1100  CE2 PHE A 123     1391   2261   1854    -20   -230    182       C  
ATOM   1101  CZ  PHE A 123      12.849   9.891  13.112  1.00 13.95           C  
ANISOU 1101  CZ  PHE A 123     1334   2080   1887   -113   -103    322       C  
ATOM   1102  N   GLY A 124      13.338   4.398  16.890  1.00 13.49           N  
ANISOU 1102  N   GLY A 124     1534   1314   2279    -82   -590    266       N  
ATOM   1103  CA  GLY A 124      12.698   3.189  16.372  1.00 16.32           C  
ANISOU 1103  CA  GLY A 124     1601   1330   3271   -151   -975    170       C  
ATOM   1104  C   GLY A 124      11.448   3.551  15.578  1.00 14.17           C  
ANISOU 1104  C   GLY A 124     1641   1195   2550     35   -667   -117       C  
ATOM   1105  O   GLY A 124      11.139   4.748  15.371  1.00 13.56           O  
ANISOU 1105  O   GLY A 124     1285   1266   2601    -98   -519    103       O  
ATOM   1106  N   ALA A 125      10.748   2.523  15.109  1.00 16.63           N  
ANISOU 1106  N   ALA A 125     1163   1346   3809   -120   -881      6       N  
ATOM   1107  CA  ALA A 125       9.669   2.773  14.167  1.00 14.94           C  
ANISOU 1107  CA  ALA A 125     1355   1321   3001     35   -606   -314       C  
ATOM   1108  C   ALA A 125       8.579   3.620  14.781  1.00 13.54           C  
ANISOU 1108  C   ALA A 125     1064   1212   2868   -200   -485    -72       C  
ATOM   1109  O   ALA A 125       8.000   4.452  14.085  1.00 14.19           O  
ANISOU 1109  O   ALA A 125     1268   1342   2779    -55   -467    -50       O  
ATOM   1110  CB  ALA A 125       9.114   1.415  13.737  1.00 18.53           C  
ANISOU 1110  CB  ALA A 125     1524   1321   4197     96  -1034   -498       C  
ATOM   1111  N   ASP A 126       8.249   3.442  16.059  1.00 14.91           N  
ANISOU 1111  N   ASP A 126     1425   1167   3074    -59   -215    303       N  
ATOM   1112  CA  ASP A 126       7.216   4.303  16.643  1.00 16.03           C  
ANISOU 1112  CA  ASP A 126     1499   1380   3212    -75    136    265       C  
ATOM   1113  C   ASP A 126       7.583   5.766  16.565  1.00 12.47           C  
ANISOU 1113  C   ASP A 126     1227   1372   2138    -52      8    127       C  
ATOM   1114  O   ASP A 126       6.789   6.614  16.182  1.00 12.62           O  
ANISOU 1114  O   ASP A 126     1228   1351   2217    -74    -77     55       O  
ATOM   1115  CB AASP A 126       7.004   3.777  18.065  0.72 18.92           C  
ANISOU 1115  CB AASP A 126     2310   1327   3553    193    440    672       C  
ATOM   1116  CB BASP A 126       6.920   3.914  18.105  0.28 19.70           C  
ANISOU 1116  CB BASP A 126     2156   1700   3628    286    589    909       C  
ATOM   1117  CG AASP A 126       8.237   3.756  18.920  0.72 22.36           C  
ANISOU 1117  CG AASP A 126     2451   2231   3815   1006    248   1538       C  
ATOM   1118  CG BASP A 126       6.321   2.534  18.244  0.28 23.27           C  
ANISOU 1118  CG BASP A 126     2844   2212   3786   -462    395    889       C  
ATOM   1119  OD1AASP A 126       9.455   3.823  18.551  0.72 23.95           O  
ANISOU 1119  OD1AASP A 126     2410   3129   3562    741    105   1661       O  
ATOM   1120  OD1BASP A 126       6.193   1.844  17.212  0.28 28.37           O  
ANISOU 1120  OD1BASP A 126     4519   2156   4104   -249   -808    842       O  
ATOM   1121  OD2AASP A 126       8.039   3.608  20.139  0.72 28.06           O  
ANISOU 1121  OD2AASP A 126     2478   4235   3949   -297    172   1958       O  
ATOM   1122  OD2BASP A 126       6.006   2.072  19.372  0.28 28.41           O  
ANISOU 1122  OD2BASP A 126     4287   2113   4396    157   1148   1456       O  
ATOM   1123  N   ALA A 127       8.836   6.075  16.940  1.00 12.30           N  
ANISOU 1123  N   ALA A 127     1427   1251   1995     24   -188    119       N  
ATOM   1124  CA  ALA A 127       9.297   7.451  16.904  1.00 11.53           C  
ANISOU 1124  CA  ALA A 127     1498   1252   1629   -171   -211    101       C  
ATOM   1125  C   ALA A 127       9.432   7.944  15.459  1.00 10.45           C  
ANISOU 1125  C   ALA A 127     1065   1274   1630   -174   -203    -60       C  
ATOM   1126  O   ALA A 127       9.149   9.130  15.202  1.00 10.97           O  
ANISOU 1126  O   ALA A 127     1283   1284   1601    -83   -263     44       O  
ATOM   1127  CB  ALA A 127      10.629   7.578  17.600  1.00 12.58           C  
ANISOU 1127  CB  ALA A 127     1668   1437   1675    -85   -330     19       C  
ATOM   1128  N   GLN A 128       9.860   7.095  14.541  1.00 11.46           N  
ANISOU 1128  N   GLN A 128     1184   1457   1713     15   -271   -188       N  
ATOM   1129  CA  GLN A 128       9.903   7.525  13.137  1.00 11.64           C  
ANISOU 1129  CA  GLN A 128     1361   1327   1734    185   -289   -171       C  
ATOM   1130  C   GLN A 128       8.522   7.886  12.602  1.00 11.28           C  
ANISOU 1130  C   GLN A 128     1422   1215   1650     69   -272   -211       C  
ATOM   1131  O   GLN A 128       8.343   8.872  11.896  1.00 11.47           O  
ANISOU 1131  O   GLN A 128     1297   1553   1508    211   -126    -57       O  
ATOM   1132  CB AGLN A 128      10.387   6.334  12.307  0.52 12.73           C  
ANISOU 1132  CB AGLN A 128     1312   1642   1881     85    -15   -311       C  
ATOM   1133  CB BGLN A 128      10.596   6.407  12.340  0.48 13.26           C  
ANISOU 1133  CB BGLN A 128     1507   1730   1802    274   -281   -402       C  
ATOM   1134  CG AGLN A 128      11.826   5.983  12.486  0.52 13.10           C  
ANISOU 1134  CG AGLN A 128     1357   1976   1643    280    -64   -468       C  
ATOM   1135  CG BGLN A 128      10.648   6.672  10.868  0.48 16.68           C  
ANISOU 1135  CG BGLN A 128     2105   2537   1695    357   -457   -484       C  
ATOM   1136  CD AGLN A 128      12.196   4.622  11.917  0.52 13.63           C  
ANISOU 1136  CD AGLN A 128     1638   1986   1554    337    -55   -439       C  
ATOM   1137  CD BGLN A 128      11.207   5.647   9.922  0.48 20.10           C  
ANISOU 1137  CD BGLN A 128     2716   3281   1640   1312   -450   -362       C  
ATOM   1138  OE1AGLN A 128      11.732   4.307  10.840  0.52 19.67           O  
ANISOU 1138  OE1AGLN A 128     3062   2664   1747   1558   -794   -909       O  
ATOM   1139  OE1BGLN A 128      11.292   5.909   8.718  0.48 20.80           O  
ANISOU 1139  OE1BGLN A 128     2745   3278   1881    677    407    -99       O  
ATOM   1140  NE2AGLN A 128      12.960   3.799  12.642  0.52 11.49           N  
ANISOU 1140  NE2AGLN A 128      995   1745   1627    -72   -314   -585       N  
ATOM   1141  NE2BGLN A 128      11.601   4.492  10.462  0.48 15.93           N  
ANISOU 1141  NE2BGLN A 128     1383   2433   2237    135   -175   -301       N  
ATOM   1142  N   GLY A 129       7.527   7.049  12.941  1.00 11.30           N  
ANISOU 1142  N   GLY A 129     1382   1355   1555    116   -224    -82       N  
ATOM   1143  CA  GLY A 129       6.192   7.370  12.517  1.00 11.56           C  
ANISOU 1143  CA  GLY A 129     1449   1418   1527     98   -277     -7       C  
ATOM   1144  C   GLY A 129       5.674   8.670  13.110  1.00 10.76           C  
ANISOU 1144  C   GLY A 129     1026   1546   1517      1    -99   -152       C  
ATOM   1145  O   GLY A 129       5.012   9.454  12.418  1.00 11.56           O  
ANISOU 1145  O   GLY A 129     1235   1488   1670     69   -273   -251       O  
ATOM   1146  N   ALA A 130       5.945   8.882  14.393  1.00 10.35           N  
ANISOU 1146  N   ALA A 130     1208   1212   1514    -75     15     11       N  
ATOM   1147  CA  ALA A 130       5.495  10.113  15.042  1.00 10.18           C  
ANISOU 1147  CA  ALA A 130     1254   1160   1452   -181    -91    -62       C  
ATOM   1148  C   ALA A 130       6.167  11.338  14.414  1.00  9.15           C  
ANISOU 1148  C   ALA A 130     1083   1230   1164    -61    -60   -139       C  
ATOM   1149  O   ALA A 130       5.520  12.343  14.179  1.00  9.50           O  
ANISOU 1149  O   ALA A 130     1154   1168   1289     -7    -24      3       O  
ATOM   1150  CB  ALA A 130       5.788  10.056  16.542  1.00 11.03           C  
ANISOU 1150  CB  ALA A 130     1402   1377   1413   -102     68     32       C  
ATOM   1151  N   MET A 131       7.490  11.254  14.141  1.00  9.56           N  
ANISOU 1151  N   MET A 131     1049   1169   1415     94   -126     62       N  
ATOM   1152  CA  MET A 131       8.183  12.369  13.501  1.00  9.75           C  
ANISOU 1152  CA  MET A 131     1100   1290   1315    -79    -90      7       C  
ATOM   1153  C   MET A 131       7.660  12.599  12.100  1.00  9.55           C  
ANISOU 1153  C   MET A 131      945   1352   1330    -50     -3     13       C  
ATOM   1154  O   MET A 131       7.511  13.753  11.670  1.00 10.19           O  
ANISOU 1154  O   MET A 131     1085   1386   1402      9     26     97       O  
ATOM   1155  CB  MET A 131       9.694  12.112  13.516  1.00 10.23           C  
ANISOU 1155  CB  MET A 131     1084   1435   1368     41   -187      2       C  
ATOM   1156  CG  MET A 131      10.499  13.288  12.959  1.00 11.37           C  
ANISOU 1156  CG  MET A 131     1098   1744   1478     32     36    -15       C  
ATOM   1157  SD  MET A 131      10.360  14.839  13.849  1.00 11.81           S  
ANISOU 1157  SD  MET A 131     1272   1586   1629   -158     71    -32       S  
ATOM   1158  CE  MET A 131      11.380  14.477  15.268  1.00 13.84           C  
ANISOU 1158  CE  MET A 131     1509   2183   1568    116     -3    -95       C  
ATOM   1159  N   ASN A 132       7.377  11.529  11.352  1.00 10.34           N  
ANISOU 1159  N   ASN A 132     1311   1344   1271    184   -125     37       N  
ATOM   1160  CA  ASN A 132       6.778  11.664  10.041  1.00 11.77           C  
ANISOU 1160  CA  ASN A 132     1661   1665   1148    468   -197   -106       C  
ATOM   1161  C   ASN A 132       5.469  12.466  10.157  1.00 10.34           C  
ANISOU 1161  C   ASN A 132     1374   1252   1301     94   -149    -18       C  
ATOM   1162  O   ASN A 132       5.208  13.364   9.391  1.00 10.73           O  
ANISOU 1162  O   ASN A 132     1359   1469   1249    170   -143     29       O  
ATOM   1163  CB  ASN A 132       6.519  10.332   9.407  1.00 15.12           C  
ANISOU 1163  CB  ASN A 132     2305   1726   1714    750   -361   -496       C  
ATOM   1164  CG  ASN A 132       6.107  10.633   7.954  1.00 16.94           C  
ANISOU 1164  CG  ASN A 132     2663   1800   1973    486   -941   -573       C  
ATOM   1165  OD1 ASN A 132       6.639  11.303   7.078  1.00 27.09           O  
ANISOU 1165  OD1 ASN A 132     5065   2572   2656   -525  -1714    830       O  
ATOM   1166  ND2 ASN A 132       4.866  10.133   7.816  1.00 29.41           N  
ANISOU 1166  ND2 ASN A 132     3682   3376   4115   -760  -2022   -614       N  
ATOM   1167  N   LYS A 133       4.651  12.114  11.145  1.00 10.53           N  
ANISOU 1167  N   LYS A 133     1274   1345   1382     57   -260    115       N  
ATOM   1168  CA  LYS A 133       3.355  12.820  11.354  1.00 10.26           C  
ANISOU 1168  CA  LYS A 133     1143   1362   1392    -80   -307     -7       C  
ATOM   1169  C   LYS A 133       3.570  14.282  11.707  1.00  9.13           C  
ANISOU 1169  C   LYS A 133      908   1340   1220     15   -150     41       C  
ATOM   1170  O   LYS A 133       2.849  15.144  11.242  1.00  9.56           O  
ANISOU 1170  O   LYS A 133      871   1370   1391    -63   -193     80       O  
ATOM   1171  CB ALYS A 133       2.475  12.188  12.409  0.64 11.86           C  
ANISOU 1171  CB ALYS A 133     1380   1462   1665   -228   -184     74       C  
ATOM   1172  CB BLYS A 133       2.636  12.046  12.442  0.36 12.30           C  
ANISOU 1172  CB BLYS A 133     1514   1468   1694   -305    -73    -53       C  
ATOM   1173  CG ALYS A 133       1.826  10.866  12.082  0.64 12.79           C  
ANISOU 1173  CG ALYS A 133     1390   1527   1941   -295   -193   -167       C  
ATOM   1174  CG BLYS A 133       1.140  12.271  12.360  0.36 11.76           C  
ANISOU 1174  CG BLYS A 133     1538   1236   1695   -146      0     60       C  
ATOM   1175  CD ALYS A 133       0.926  10.352  13.218  0.64 16.29           C  
ANISOU 1175  CD ALYS A 133     2202   1797   2190   -617   -171    351       C  
ATOM   1176  CD BLYS A 133       0.407  11.497  13.416  0.36 16.46           C  
ANISOU 1176  CD BLYS A 133     2141   2088   2026   -386    543    122       C  
ATOM   1177  CE ALYS A 133       0.031   9.192  12.829  0.64 25.55           C  
ANISOU 1177  CE ALYS A 133     3066   2993   3650  -1789   -289    342       C  
ATOM   1178  CE BLYS A 133      -0.985  12.067  13.681  0.36 19.60           C  
ANISOU 1178  CE BLYS A 133     1507   3009   2931   -717    217    388       C  
ATOM   1179  NZ ALYS A 133      -1.063   9.027  13.842  0.64 31.16           N  
ANISOU 1179  NZ ALYS A 133     2119   4865   4854  -1615   -229    672       N  
ATOM   1180  NZ BLYS A 133      -1.655  11.093  14.579  0.36 22.79           N  
ANISOU 1180  NZ BLYS A 133     1663   4288   2708  -1472   -159    742       N  
ATOM   1181  N   ALA A 134       4.572  14.564  12.550  1.00  8.65           N  
ANISOU 1181  N   ALA A 134      837   1310   1138     20    -49    -29       N  
ATOM   1182  CA  ALA A 134       4.881  15.948  12.934  1.00  8.73           C  
ANISOU 1182  CA  ALA A 134      909   1332   1075      6      3    -99       C  
ATOM   1183  C   ALA A 134       5.306  16.781  11.735  1.00  8.34           C  
ANISOU 1183  C   ALA A 134      778   1285   1106    -45   -100    -63       C  
ATOM   1184  O   ALA A 134       4.926  17.930  11.580  1.00  9.03           O  
ANISOU 1184  O   ALA A 134      972   1362   1098     70   -123      1       O  
ATOM   1185  CB  ALA A 134       5.931  16.011  14.034  1.00  9.31           C  
ANISOU 1185  CB  ALA A 134     1171   1321   1045    -33    -81   -119       C  
ATOM   1186  N   LEU A 135       6.159  16.196  10.887  1.00  8.31           N  
ANISOU 1186  N   LEU A 135      921   1213   1025     11    -92     21       N  
ATOM   1187  CA  LEU A 135       6.641  16.896   9.695  1.00  8.89           C  
ANISOU 1187  CA  LEU A 135      952   1248   1180    -30    -34     33       C  
ATOM   1188  C   LEU A 135       5.562  17.011   8.648  1.00  8.48           C  
ANISOU 1188  C   LEU A 135      911   1254   1056     87      3    -32       C  
ATOM   1189  O   LEU A 135       5.480  17.988   7.922  1.00  9.85           O  
ANISOU 1189  O   LEU A 135     1064   1411   1269     90   -111     92       O  
ATOM   1190  CB  LEU A 135       7.902  16.274   9.144  1.00  9.50           C  
ANISOU 1190  CB  LEU A 135      882   1538   1191      2    -83    164       C  
ATOM   1191  CG  LEU A 135       9.104  16.314  10.166  1.00 10.39           C  
ANISOU 1191  CG  LEU A 135      827   1749   1370   -100   -182    136       C  
ATOM   1192  CD1 LEU A 135      10.266  15.541   9.637  1.00 12.19           C  
ANISOU 1192  CD1 LEU A 135      844   2312   1476     97   -144    352       C  
ATOM   1193  CD2 LEU A 135       9.445  17.753  10.494  1.00 16.58           C  
ANISOU 1193  CD2 LEU A 135     1440   1777   3083   -136  -1090     72       C  
ATOM   1194  N   GLU A 136       4.658  16.019   8.557  1.00  9.08           N  
ANISOU 1194  N   GLU A 136     1098   1257   1096     21   -219      0       N  
ATOM   1195  CA  GLU A 136       3.472  16.117   7.707  1.00  9.92           C  
ANISOU 1195  CA  GLU A 136     1106   1522   1142     73   -252     59       C  
ATOM   1196  C   GLU A 136       2.593  17.267   8.169  1.00 10.00           C  
ANISOU 1196  C   GLU A 136     1044   1521   1235      4   -272    -72       C  
ATOM   1197  O   GLU A 136       2.082  18.051   7.322  1.00 10.40           O  
ANISOU 1197  O   GLU A 136     1109   1562   1280     64   -308   -101       O  
ATOM   1198  CB AGLU A 136       2.687  14.819   7.756  0.52 11.02           C  
ANISOU 1198  CB AGLU A 136     1328   1608   1250    -74   -371   -302       C  
ATOM   1199  CB BGLU A 136       2.717  14.797   7.660  0.48 11.38           C  
ANISOU 1199  CB BGLU A 136     1071   1569   1683     51   -363   -169       C  
ATOM   1200  CG AGLU A 136       3.307  13.703   6.992  0.52 14.25           C  
ANISOU 1200  CG AGLU A 136     2090   1797   1526    181   -566   -550       C  
ATOM   1201  CG BGLU A 136       3.347  13.871   6.660  0.48 13.45           C  
ANISOU 1201  CG BGLU A 136     1650   1811   1648   -158   -224   -380       C  
ATOM   1202  CD AGLU A 136       2.647  12.358   7.227  0.52 21.79           C  
ANISOU 1202  CD AGLU A 136     3145   1908   3225   -562   -785  -1140       C  
ATOM   1203  CD BGLU A 136       2.391  12.846   6.093  0.48 16.75           C  
ANISOU 1203  CD BGLU A 136     2122   1925   2318   -498   -132   -571       C  
ATOM   1204  OE1AGLU A 136       1.727  12.227   8.050  0.52 23.43           O  
ANISOU 1204  OE1AGLU A 136     3498   1686   3718   -696   -523    -83       O  
ATOM   1205  OE1BGLU A 136       1.270  12.653   6.603  0.48 17.03           O  
ANISOU 1205  OE1BGLU A 136     2090   1959   2421   -581   -139   -573       O  
ATOM   1206  OE2AGLU A 136       3.086  11.403   6.543  0.52 38.20           O  
ANISOU 1206  OE2AGLU A 136     5628   2486   6400   -797    621  -2489       O  
ATOM   1207  OE2BGLU A 136       2.740  12.225   5.065  0.48 22.82           O  
ANISOU 1207  OE2BGLU A 136     2371   2538   3760  -1080    595  -1739       O  
ATOM   1208  N   LEU A 137       2.396  17.433   9.465  1.00  9.40           N  
ANISOU 1208  N   LEU A 137      851   1434   1285     72   -261   -109       N  
ATOM   1209  CA  LEU A 137       1.570  18.532   9.997  1.00  9.81           C  
ANISOU 1209  CA  LEU A 137      923   1435   1371     57   -144    -10       C  
ATOM   1210  C   LEU A 137       2.166  19.884   9.623  1.00  9.24           C  
ANISOU 1210  C   LEU A 137     1026   1364   1120    133    -92    -82       C  
ATOM   1211  O   LEU A 137       1.495  20.796   9.179  1.00 10.12           O  
ANISOU 1211  O   LEU A 137     1030   1371   1446    107    -93     25       O  
ATOM   1212  CB  LEU A 137       1.404  18.367  11.473  1.00 10.52           C  
ANISOU 1212  CB  LEU A 137     1118   1515   1364    -81     14     24       C  
ATOM   1213  CG  LEU A 137       0.598  19.473  12.171  1.00 12.09           C  
ANISOU 1213  CG  LEU A 137     1308   1655   1632    162    -11   -103       C  
ATOM   1214  CD1 LEU A 137      -0.851  19.520  11.651  1.00 17.22           C  
ANISOU 1214  CD1 LEU A 137     1417   2682   2446    501    -91   -380       C  
ATOM   1215  CD2 LEU A 137       0.678  19.343  13.672  1.00 15.37           C  
ANISOU 1215  CD2 LEU A 137     2116   2100   1623    201    159   -224       C  
ATOM   1216  N   PHE A 138       3.492  19.985   9.802  1.00  9.66           N  
ANISOU 1216  N   PHE A 138     1017   1334   1321     35   -221     30       N  
ATOM   1217  CA  PHE A 138       4.262  21.154   9.396  1.00  9.83           C  
ANISOU 1217  CA  PHE A 138     1112   1260   1363      7   -307    -13       C  
ATOM   1218  C   PHE A 138       3.969  21.485   7.931  1.00  9.60           C  
ANISOU 1218  C   PHE A 138      869   1419   1359     36   -131     25       C  
ATOM   1219  O   PHE A 138       3.633  22.612   7.579  1.00 10.58           O  
ANISOU 1219  O   PHE A 138     1108   1407   1505     17   -237    179       O  
ATOM   1220  CB APHE A 138       5.724  20.797   9.652  0.58 10.55           C  
ANISOU 1220  CB APHE A 138     1066   1672   1272    -41   -193    112       C  
ATOM   1221  CB BPHE A 138       5.743  20.947   9.701  0.42  9.94           C  
ANISOU 1221  CB BPHE A 138     1091   1259   1427     -9   -346   -255       C  
ATOM   1222  CG APHE A 138       6.821  21.715   9.154  0.58 10.20           C  
ANISOU 1222  CG APHE A 138     1164   1317   1394    152    -77    219       C  
ATOM   1223  CG BPHE A 138       6.621  21.985   9.011  0.42 10.45           C  
ANISOU 1223  CG BPHE A 138     1025   1528   1416    -29   -527     55       C  
ATOM   1224  CD1APHE A 138       7.151  22.880   9.799  0.58 12.03           C  
ANISOU 1224  CD1APHE A 138     1345   1550   1674    -21     57    -38       C  
ATOM   1225  CD1BPHE A 138       6.690  23.288   9.461  0.42 12.41           C  
ANISOU 1225  CD1BPHE A 138     1452   1548   1716   -321    -68    -49       C  
ATOM   1226  CD2APHE A 138       7.502  21.407   8.007  0.58 12.16           C  
ANISOU 1226  CD2APHE A 138     1148   1617   1855    -28    179   -205       C  
ATOM   1227  CD2BPHE A 138       7.351  21.601   7.910  0.42 12.80           C  
ANISOU 1227  CD2BPHE A 138     1184   1598   2080   -132    -33   -166       C  
ATOM   1228  CE1APHE A 138       8.149  23.713   9.320  0.58 12.35           C  
ANISOU 1228  CE1APHE A 138     1489   1266   1939     76    189    110       C  
ATOM   1229  CE1BPHE A 138       7.502  24.200   8.805  0.42 12.81           C  
ANISOU 1229  CE1BPHE A 138     1622   1620   1625   -141     57    245       C  
ATOM   1230  CE2APHE A 138       8.528  22.188   7.503  0.58 12.59           C  
ANISOU 1230  CE2APHE A 138      973   1903   1907    -15    127   -208       C  
ATOM   1231  CE2BPHE A 138       8.166  22.492   7.243  0.42 15.00           C  
ANISOU 1231  CE2BPHE A 138     1517   1713   2469    -31    385    -56       C  
ATOM   1232  CZ APHE A 138       8.827  23.364   8.177  0.58 13.24           C  
ANISOU 1232  CZ APHE A 138     1037   1562   2431     37    319   -153       C  
ATOM   1233  CZ BPHE A 138       8.233  23.790   7.721  0.42 14.01           C  
ANISOU 1233  CZ BPHE A 138     1444   1748   2132   -262    196    -73       C  
ATOM   1234  N   ARG A 139       4.144  20.500   7.047  1.00  9.69           N  
ANISOU 1234  N   ARG A 139      865   1552   1265    221   -147     52       N  
ATOM   1235  CA  ARG A 139       3.916  20.676   5.609  1.00 11.13           C  
ANISOU 1235  CA  ARG A 139     1212   1786   1233    195   -113    135       C  
ATOM   1236  C   ARG A 139       2.470  21.077   5.306  1.00 10.88           C  
ANISOU 1236  C   ARG A 139     1268   1679   1186    151   -285     53       C  
ATOM   1237  O   ARG A 139       2.220  21.955   4.456  1.00 11.13           O  
ANISOU 1237  O   ARG A 139     1261   1720   1247    359   -179     49       O  
ATOM   1238  CB  ARG A 139       4.310  19.430   4.800  1.00 11.13           C  
ANISOU 1238  CB  ARG A 139     1210   1785   1233     97    -73    143       C  
ATOM   1239  CG  ARG A 139       5.775  19.196   4.782  1.00 12.77           C  
ANISOU 1239  CG  ARG A 139     1345   1999   1507    278     -1    -92       C  
ATOM   1240  CD  ARG A 139       6.129  18.316   3.623  1.00 13.63           C  
ANISOU 1240  CD  ARG A 139     1427   1974   1777     18    259   -261       C  
ATOM   1241  NE  ARG A 139       5.498  16.987   3.518  1.00 12.03           N  
ANISOU 1241  NE  ARG A 139     1040   2007   1525     67    199   -104       N  
ATOM   1242  CZ  ARG A 139       5.828  15.982   4.267  1.00 12.08           C  
ANISOU 1242  CZ  ARG A 139     1175   1836   1580    194   -144   -325       C  
ATOM   1243  NH1 ARG A 139       6.774  16.057   5.227  1.00 13.24           N  
ANISOU 1243  NH1 ARG A 139     1298   2173   1558   -149   -218   -380       N  
ATOM   1244  NH2 ARG A 139       5.277  14.819   4.058  1.00 15.78           N  
ANISOU 1244  NH2 ARG A 139     1710   1833   2452     26   -817   -366       N  
ATOM   1245  N   LYS A 140       1.523  20.420   5.952  1.00 10.56           N  
ANISOU 1245  N   LYS A 140     1142   1467   1402    213   -314    -71       N  
ATOM   1246  CA  LYS A 140       0.083  20.690   5.710  1.00 11.52           C  
ANISOU 1246  CA  LYS A 140     1164   1491   1723     88   -510   -218       C  
ATOM   1247  C   LYS A 140      -0.195  22.144   6.009  1.00 10.16           C  
ANISOU 1247  C   LYS A 140      939   1467   1455    131   -289    -98       C  
ATOM   1248  O   LYS A 140      -0.898  22.836   5.259  1.00 11.04           O  
ANISOU 1248  O   LYS A 140     1051   1557   1586    109   -382     53       O  
ATOM   1249  CB  LYS A 140      -0.762  19.749   6.614  1.00 13.46           C  
ANISOU 1249  CB  LYS A 140     1298   1553   2264     57   -316     47       C  
ATOM   1250  CG  LYS A 140      -2.250  20.088   6.674  1.00 16.17           C  
ANISOU 1250  CG  LYS A 140     1151   2036   2957   -202   -648    390       C  
ATOM   1251  CD  LYS A 140      -3.053  19.293   7.676  1.00 21.81           C  
ANISOU 1251  CD  LYS A 140     1447   2869   3972   -639   -350    836       C  
ATOM   1252  CE  LYS A 140      -4.528  19.658   7.850  1.00 28.56           C  
ANISOU 1252  CE  LYS A 140     1831   4919   4101    -78    329    353       C  
ATOM   1253  NZ  LYS A 140      -5.225  18.793   8.847  1.00 42.09           N  
ANISOU 1253  NZ  LYS A 140     3108   7607   5276   -252   1789   1233       N  
ATOM   1254  N   ASP A 141       0.308  22.592   7.164  1.00 10.09           N  
ANISOU 1254  N   ASP A 141      997   1441   1394    167   -224    -70       N  
ATOM   1255  CA  ASP A 141      -0.017  23.940   7.589  1.00 10.96           C  
ANISOU 1255  CA  ASP A 141     1157   1413   1595    210   -148   -153       C  
ATOM   1256  C   ASP A 141       0.682  25.009   6.771  1.00 11.38           C  
ANISOU 1256  C   ASP A 141     1350   1463   1513    290   -194    -32       C  
ATOM   1257  O   ASP A 141       0.133  26.054   6.455  1.00 12.50           O  
ANISOU 1257  O   ASP A 141     1479   1346   1924    275   -209    -56       O  
ATOM   1258  CB  ASP A 141       0.193  24.058   9.107  1.00 11.07           C  
ANISOU 1258  CB  ASP A 141     1274   1430   1502    227   -174   -181       C  
ATOM   1259  CG  ASP A 141      -0.836  23.309   9.966  1.00 12.03           C  
ANISOU 1259  CG  ASP A 141     1339   1602   1630    239   -156    -57       C  
ATOM   1260  OD1 ASP A 141      -1.846  22.840   9.397  1.00 15.00           O  
ANISOU 1260  OD1 ASP A 141     1251   2534   1917    -26   -113    -13       O  
ATOM   1261  OD2 ASP A 141      -0.584  23.249  11.200  1.00 14.62           O  
ANISOU 1261  OD2 ASP A 141     1664   2326   1567    -61    -26     27       O  
ATOM   1262  N   ILE A 142       1.929  24.736   6.364  1.00 10.86           N  
ANISOU 1262  N   ILE A 142     1139   1433   1553     41   -272    -59       N  
ATOM   1263  CA  ILE A 142       2.619  25.659   5.457  1.00 11.47           C  
ANISOU 1263  CA  ILE A 142     1204   1610   1545    167   -313    178       C  
ATOM   1264  C   ILE A 142       1.881  25.690   4.132  1.00 11.06           C  
ANISOU 1264  C   ILE A 142      934   1606   1663     31   -388    114       C  
ATOM   1265  O   ILE A 142       1.698  26.764   3.541  1.00 11.65           O  
ANISOU 1265  O   ILE A 142     1011   1663   1752    124   -406    209       O  
ATOM   1266  CB AILE A 142       4.091  25.163   5.279  0.58 12.09           C  
ANISOU 1266  CB AILE A 142     1012   1772   1809   -107   -530    528       C  
ATOM   1267  CB BILE A 142       4.134  25.359   5.325  0.42 12.74           C  
ANISOU 1267  CB BILE A 142     1109   2032   1699    -57   -474    610       C  
ATOM   1268  CG1AILE A 142       4.903  25.326   6.550  0.58 13.38           C  
ANISOU 1268  CG1AILE A 142     1563   1416   2106   -333   -916    516       C  
ATOM   1269  CG1BILE A 142       4.897  25.683   6.608  0.42 12.00           C  
ANISOU 1269  CG1BILE A 142     1082   1794   1684    -61   -155    -93       C  
ATOM   1270  CG2AILE A 142       4.669  25.861   4.044  0.58 19.36           C  
ANISOU 1270  CG2AILE A 142     1503   3675   2177    561    148   1243       C  
ATOM   1271  CG2BILE A 142       4.727  26.071   4.106  0.42  9.79           C  
ANISOU 1271  CG2BILE A 142     1125    752   1841   -369   -353    165       C  
ATOM   1272  CD1AILE A 142       5.372  26.736   6.822  0.58 25.31           C  
ANISOU 1272  CD1AILE A 142     3677   1749   4190   -675  -1496   -240       C  
ATOM   1273  CD1BILE A 142       6.263  25.055   6.662  0.42 12.52           C  
ANISOU 1273  CD1BILE A 142      948   1916   1892   -231   -380    552       C  
ATOM   1274  N   ALA A 143       1.473  24.531   3.610  1.00 11.50           N  
ANISOU 1274  N   ALA A 143     1018   1708   1643     49   -364     74       N  
ATOM   1275  CA  ALA A 143       0.812  24.455   2.314  1.00 11.66           C  
ANISOU 1275  CA  ALA A 143     1269   1677   1483    177   -403     63       C  
ATOM   1276  C   ALA A 143      -0.479  25.266   2.314  1.00 11.71           C  
ANISOU 1276  C   ALA A 143      957   1715   1777    -84   -468    146       C  
ATOM   1277  O   ALA A 143      -0.816  25.911   1.320  1.00 12.31           O  
ANISOU 1277  O   ALA A 143     1106   1741   1829      9   -511    206       O  
ATOM   1278  CB  ALA A 143       0.524  22.976   1.967  1.00 12.40           C  
ANISOU 1278  CB  ALA A 143     1435   1829   1450     51   -373    -10       C  
ATOM   1279  N   ALA A 144      -1.193  25.293   3.420  1.00 11.92           N  
ANISOU 1279  N   ALA A 144      919   1758   1851    -75   -419    153       N  
ATOM   1280  CA  ALA A 144      -2.437  26.095   3.481  1.00 12.72           C  
ANISOU 1280  CA  ALA A 144      987   1776   2069    -29   -398    221       C  
ATOM   1281  C   ALA A 144      -2.123  27.566   3.369  1.00 12.34           C  
ANISOU 1281  C   ALA A 144      982   1761   1947     70   -474     14       C  
ATOM   1282  O   ALA A 144      -2.876  28.297   2.747  1.00 13.85           O  
ANISOU 1282  O   ALA A 144     1132   1965   2165     95   -494    318       O  
ATOM   1283  CB  ALA A 144      -3.178  25.755   4.763  1.00 13.80           C  
ANISOU 1283  CB  ALA A 144     1304   1909   2032    151   -241    132       C  
ATOM   1284  N   LYS A 145      -1.037  28.020   3.983  1.00 11.72           N  
ANISOU 1284  N   LYS A 145     1127   1571   1756     80   -393     31       N  
ATOM   1285  CA  LYS A 145      -0.594  29.371   3.860  1.00 12.69           C  
ANISOU 1285  CA  LYS A 145     1041   1639   2142     38   -322    193       C  
ATOM   1286  C   LYS A 145      -0.152  29.688   2.448  1.00 12.60           C  
ANISOU 1286  C   LYS A 145      907   1772   2108    148   -483    351       C  
ATOM   1287  O   LYS A 145      -0.433  30.742   1.848  1.00 14.84           O  
ANISOU 1287  O   LYS A 145     1248   1731   2657    115   -398    570       O  
ATOM   1288  CB  LYS A 145       0.450  29.701   4.902  1.00 13.27           C  
ANISOU 1288  CB  LYS A 145     1370   1515   2155   -221   -394    332       C  
ATOM   1289  CG  LYS A 145      -0.043  29.672   6.343  1.00 22.71           C  
ANISOU 1289  CG  LYS A 145     3923   2629   2077   -769   -160   -262       C  
ATOM   1290  CD  LYS A 145      -0.963  30.799   6.763  1.00 34.44           C  
ANISOU 1290  CD  LYS A 145     4399   5264   3422    417    850  -1166       C  
ATOM   1291  CE  LYS A 145      -1.882  30.408   7.907  1.00 40.87           C  
ANISOU 1291  CE  LYS A 145     4690   6025   4813    552   1328    175       C  
ATOM   1292  NZ  LYS A 145      -2.949  29.491   7.374  1.00 34.07           N  
ANISOU 1292  NZ  LYS A 145     3622   4483   4842   1747    430   1431       N  
ATOM   1293  N   TYR A 146       0.626  28.777   1.838  1.00 12.06           N  
ANISOU 1293  N   TYR A 146     1027   1600   1954    -42   -478    314       N  
ATOM   1294  CA  TYR A 146       1.007  28.924   0.449  1.00 12.60           C  
ANISOU 1294  CA  TYR A 146     1192   1668   1928     44   -473    351       C  
ATOM   1295  C   TYR A 146      -0.270  29.110  -0.405  1.00 13.12           C  
ANISOU 1295  C   TYR A 146     1113   1939   1934    187   -348    411       C  
ATOM   1296  O   TYR A 146      -0.271  29.932  -1.319  1.00 14.89           O  
ANISOU 1296  O   TYR A 146     1227   2212   2219    199   -386    738       O  
ATOM   1297  CB ATYR A 146       1.743  27.692  -0.049  0.45 13.05           C  
ANISOU 1297  CB ATYR A 146     1146   1819   1992     89   -614    191       C  
ATOM   1298  CB BTYR A 146       1.775  27.742  -0.103  0.55 13.09           C  
ANISOU 1298  CB BTYR A 146     1100   1798   2074     71   -377    365       C  
ATOM   1299  CG ATYR A 146       3.240  27.641   0.249  0.45 12.35           C  
ANISOU 1299  CG ATYR A 146     1106   1717   1868     49   -538    174       C  
ATOM   1300  CG BTYR A 146       3.290  27.723   0.093  0.55 11.00           C  
ANISOU 1300  CG BTYR A 146     1130   1357   1693     -4   -387    626       C  
ATOM   1301  CD1ATYR A 146       3.861  28.232   1.316  0.45 11.22           C  
ANISOU 1301  CD1ATYR A 146      923   1701   1639   -108   -215    198       C  
ATOM   1302  CD1BTYR A 146       3.929  27.951   1.285  0.55 13.39           C  
ANISOU 1302  CD1BTYR A 146     1440   1788   1859   -158   -512    295       C  
ATOM   1303  CD2ATYR A 146       4.045  26.934  -0.641  0.45 14.37           C  
ANISOU 1303  CD2ATYR A 146     1242   2043   2176    242   -802   -360       C  
ATOM   1304  CD2BTYR A 146       4.095  27.447  -1.019  0.55 12.15           C  
ANISOU 1304  CD2BTYR A 146     1176   1422   2019    234   -376     88       C  
ATOM   1305  CE1ATYR A 146       5.220  28.162   1.537  0.45 11.10           C  
ANISOU 1305  CE1ATYR A 146      857   1684   1678   -333   -135    176       C  
ATOM   1306  CE1BTYR A 146       5.302  27.928   1.419  0.55 13.70           C  
ANISOU 1306  CE1BTYR A 146     1458   1679   2068     -3   -676    186       C  
ATOM   1307  CE2ATYR A 146       5.411  26.828  -0.456  0.45 13.07           C  
ANISOU 1307  CE2ATYR A 146     1246   1651   2069    356   -782   -143       C  
ATOM   1308  CE2BTYR A 146       5.475  27.388  -0.892  0.55 11.38           C  
ANISOU 1308  CE2BTYR A 146     1128   1257   1940    -58   -365    565       C  
ATOM   1309  CZ ATYR A 146       5.970  27.441   0.629  0.45 10.61           C  
ANISOU 1309  CZ ATYR A 146      883   1412   1736     55   -462    233       C  
ATOM   1310  CZ BTYR A 146       6.063  27.628   0.309  0.55 13.53           C  
ANISOU 1310  CZ BTYR A 146     1351   1569   2220   -238   -526    213       C  
ATOM   1311  OH ATYR A 146       7.335  27.343   0.843  0.45 13.19           O  
ANISOU 1311  OH ATYR A 146      869   2149   1992    184   -561    189       O  
ATOM   1312  OH BTYR A 146       7.446  27.589   0.442  0.55 14.34           O  
ANISOU 1312  OH BTYR A 146     1392   1706   2351    -72   -703    370       O  
ATOM   1313  N   LYS A 147      -1.274  28.298  -0.187  1.00 14.52           N  
ANISOU 1313  N   LYS A 147     1141   2447   1930    -21   -497    612       N  
ATOM   1314  CA  LYS A 147      -2.485  28.358  -1.037  1.00 15.53           C  
ANISOU 1314  CA  LYS A 147     1452   2368   2081   -111   -797    392       C  
ATOM   1315  C   LYS A 147      -3.127  29.720  -0.917  1.00 15.29           C  
ANISOU 1315  C   LYS A 147     1129   2505   2176    -84   -563    735       C  
ATOM   1316  O   LYS A 147      -3.530  30.298  -1.913  1.00 18.83           O  
ANISOU 1316  O   LYS A 147     1568   3026   2561    168  -1012    739       O  
ATOM   1317  CB  LYS A 147      -3.445  27.209  -0.621  1.00 17.68           C  
ANISOU 1317  CB  LYS A 147     1464   2588   2665   -250   -870    649       C  
ATOM   1318  CG  LYS A 147      -4.692  27.151  -1.488  1.00 20.84           C  
ANISOU 1318  CG  LYS A 147     1823   3233   2864   -546  -1132    652       C  
ATOM   1319  CD  LYS A 147      -5.658  26.049  -1.118  1.00 26.01           C  
ANISOU 1319  CD  LYS A 147     2105   4115   3663  -1251  -1042    591       C  
ATOM   1320  CE  LYS A 147      -6.916  26.274  -1.990  1.00 29.89           C  
ANISOU 1320  CE  LYS A 147     1622   5422   4315   -748   -859    140       C  
ATOM   1321  NZ  LYS A 147      -6.913  25.368  -3.151  1.00 40.98           N  
ANISOU 1321  NZ  LYS A 147     4311   7104   4155  -1110  -1827   -398       N  
ATOM   1322  N   GLU A 148      -3.228  30.251   0.298  1.00 15.97           N  
ANISOU 1322  N   GLU A 148     1234   2523   2311    410   -395    672       N  
ATOM   1323  CA  GLU A 148      -3.773  31.559   0.518  1.00 18.85           C  
ANISOU 1323  CA  GLU A 148     1525   2789   2849    759   -148    805       C  
ATOM   1324  C   GLU A 148      -3.062  32.568  -0.374  1.00 20.30           C  
ANISOU 1324  C   GLU A 148     1876   2616   3220    767   -279   1083       C  
ATOM   1325  O   GLU A 148      -3.673  33.423  -1.031  1.00 27.02           O  
ANISOU 1325  O   GLU A 148     2609   3898   3760   1902    439   1846       O  
ATOM   1326  CB  GLU A 148      -3.637  31.929   1.998  1.00 19.71           C  
ANISOU 1326  CB  GLU A 148     1820   2705   2964    879    -52    478       C  
ATOM   1327  CG  GLU A 148      -4.007  33.320   2.367  1.00 21.40           C  
ANISOU 1327  CG  GLU A 148     1693   2626   3812    802     76    419       C  
ATOM   1328  CD  GLU A 148      -3.640  33.651   3.809  1.00 24.37           C  
ANISOU 1328  CD  GLU A 148     1801   3314   4146    565    138   -425       C  
ATOM   1329  OE1 GLU A 148      -3.426  32.788   4.677  1.00 30.09           O  
ANISOU 1329  OE1 GLU A 148     4099   4163   3170   1186    -57   -645       O  
ATOM   1330  OE2 GLU A 148      -3.549  34.875   4.026  1.00 39.55           O  
ANISOU 1330  OE2 GLU A 148     5308   3571   6149   -527   -369   -882       O  
ATOM   1331  N   LEU A 149      -1.730  32.490  -0.387  1.00 16.35           N  
ANISOU 1331  N   LEU A 149     1752   2077   2385    374   -396    536       N  
ATOM   1332  CA  LEU A 149      -0.948  33.457  -1.110  1.00 17.64           C  
ANISOU 1332  CA  LEU A 149     2285   2078   2341    129   -288    262       C  
ATOM   1333  C   LEU A 149      -0.804  33.187  -2.609  1.00 16.43           C  
ANISOU 1333  C   LEU A 149     2088   1905   2248    245   -390    485       C  
ATOM   1334  O   LEU A 149      -0.216  33.996  -3.322  1.00 22.71           O  
ANISOU 1334  O   LEU A 149     3435   2614   2581   -485   -197    713       O  
ATOM   1335  CB  LEU A 149       0.459  33.434  -0.476  1.00 17.49           C  
ANISOU 1335  CB  LEU A 149     2187   2471   1985   -330    -63    358       C  
ATOM   1336  CG  LEU A 149       0.491  33.989   0.938  1.00 18.66           C  
ANISOU 1336  CG  LEU A 149     2651   2384   2054   -453    -85    246       C  
ATOM   1337  CD1 LEU A 149       1.849  33.775   1.586  1.00 22.62           C  
ANISOU 1337  CD1 LEU A 149     2294   4197   2102  -1003     -9   -485       C  
ATOM   1338  CD2 LEU A 149       0.160  35.490   1.012  1.00 33.31           C  
ANISOU 1338  CD2 LEU A 149     6692   2391   3572     26   -864   -252       C  
ATOM   1339  N   GLY A 150      -1.328  32.057  -3.055  1.00 16.42           N  
ANISOU 1339  N   GLY A 150     1977   2054   2206    250   -804    530       N  
ATOM   1340  CA  GLY A 150      -1.229  31.841  -4.479  1.00 16.21           C  
ANISOU 1340  CA  GLY A 150     1752   2180   2227     76   -742    534       C  
ATOM   1341  C   GLY A 150       0.017  31.079  -4.923  1.00 16.63           C  
ANISOU 1341  C   GLY A 150     1663   2464   2193     65   -643    629       C  
ATOM   1342  O   GLY A 150       0.374  31.193  -6.101  1.00 18.70           O  
ANISOU 1342  O   GLY A 150     1942   3074   2089    179   -670    460       O  
ATOM   1343  N   TYR A 151       0.653  30.312  -4.047  1.00 16.85           N  
ANISOU 1343  N   TYR A 151     1636   2919   1846    394   -544    292       N  
ATOM   1344  CA  TYR A 151       1.820  29.502  -4.301  1.00 18.99           C  
ANISOU 1344  CA  TYR A 151     1815   3073   2328    594   -707    183       C  
ATOM   1345  C   TYR A 151       1.569  28.024  -4.029  1.00 21.97           C  
ANISOU 1345  C   TYR A 151     2345   2947   3055    505  -1328     -9       C  
ATOM   1346  O   TYR A 151       2.507  27.204  -4.111  1.00 29.51           O  
ANISOU 1346  O   TYR A 151     3760   3299   4154   1384  -1164   -393       O  
ATOM   1347  CB ATYR A 151       2.981  30.105  -3.474  0.39 17.88           C  
ANISOU 1347  CB ATYR A 151     1685   2919   2190    440   -562    434       C  
ATOM   1348  CB BTYR A 151       2.937  30.013  -3.369  0.61 17.94           C  
ANISOU 1348  CB BTYR A 151     1637   2906   2273    286   -612    695       C  
ATOM   1349  CG ATYR A 151       4.332  29.626  -3.944  0.39 20.60           C  
ANISOU 1349  CG ATYR A 151     1762   3428   2638    685   -510    569       C  
ATOM   1350  CG BTYR A 151       3.449  31.415  -3.623  0.61 17.88           C  
ANISOU 1350  CG BTYR A 151     1508   3029   2257    322   -576    951       C  
ATOM   1351  CD1ATYR A 151       4.822  29.805  -5.232  0.39 22.54           C  
ANISOU 1351  CD1ATYR A 151     1396   4192   2975    421   -213    780       C  
ATOM   1352  CD1BTYR A 151       2.694  32.479  -3.133  0.61 16.97           C  
ANISOU 1352  CD1BTYR A 151     1818   2883   1746    -89   -497    518       C  
ATOM   1353  CD2ATYR A 151       5.163  28.956  -3.054  0.39 21.98           C  
ANISOU 1353  CD2ATYR A 151     2267   3502   2580   1043  -1219   -388       C  
ATOM   1354  CD2BTYR A 151       4.629  31.655  -4.338  0.61 20.66           C  
ANISOU 1354  CD2BTYR A 151     1940   3057   2852    458   -128   1191       C  
ATOM   1355  CE1ATYR A 151       6.065  29.343  -5.616  0.39 24.48           C  
ANISOU 1355  CE1ATYR A 151     1609   4026   3665    608    -50    694       C  
ATOM   1356  CE1BTYR A 151       3.095  33.818  -3.320  0.61 16.82           C  
ANISOU 1356  CE1BTYR A 151     1484   2993   1916   -260   -691    394       C  
ATOM   1357  CE2ATYR A 151       6.414  28.491  -3.432  0.39 27.65           C  
ANISOU 1357  CE2ATYR A 151     3355   3950   3199   2451  -1032   -610       C  
ATOM   1358  CE2BTYR A 151       5.027  32.987  -4.540  0.61 18.18           C  
ANISOU 1358  CE2BTYR A 151     1695   3159   2052     92   -483    761       C  
ATOM   1359  CZ ATYR A 151       6.870  28.686  -4.714  0.39 28.72           C  
ANISOU 1359  CZ ATYR A 151     2721   4504   3688   1927   -574   -354       C  
ATOM   1360  CZ BTYR A 151       4.249  34.022  -4.050  0.61 17.43           C  
ANISOU 1360  CZ BTYR A 151     1489   3023   2111   -128   -566    527       C  
ATOM   1361  OH ATYR A 151       8.097  28.257  -5.183  0.39 31.66           O  
ANISOU 1361  OH ATYR A 151     1611   5972   4447   1088  -1046   -905       O  
ATOM   1362  OH BTYR A 151       4.692  35.340  -4.228  0.61 20.07           O  
ANISOU 1362  OH BTYR A 151     1854   3121   2651   -535   -508    182       O  
ATOM   1363  OXT TYR A 151       0.376  27.646  -3.769  1.00 27.51           O  
ANISOU 1363  OXT TYR A 151     3153   3860   3439   -279   -654    617       O  
TER    1364      TYR A 151                                                      
HETATM 1365  S   SO4 A 155      32.505  29.531   4.228  0.95  9.99           S  
ANISOU 1365  S   SO4 A 155     1029   1234   1531   -154      7    141       S  
HETATM 1366  O1  SO4 A 155      31.596  28.933   3.208  0.95 11.68           O  
ANISOU 1366  O1  SO4 A 155     1558   1477   1402   -355    -70    144       O  
HETATM 1367  O2  SO4 A 155      33.285  30.579   3.607  0.95 11.88           O  
ANISOU 1367  O2  SO4 A 155     1283   1494   1738   -302    130    359       O  
HETATM 1368  O3  SO4 A 155      33.337  28.522   4.855  0.95 13.09           O  
ANISOU 1368  O3  SO4 A 155     1306   1323   2346   -179   -238    418       O  
HETATM 1369  O4  SO4 A 155      31.646  30.090   5.286  0.95 11.95           O  
ANISOU 1369  O4  SO4 A 155     1361   1517   1661   -349    193   -104       O  
HETATM 1370  S   SO4 A 156      32.880  20.174  12.118  0.73 13.85           S  
ANISOU 1370  S   SO4 A 156     1293   2155   1813    113   -355   -200       S  
HETATM 1371  O1  SO4 A 156      33.511  20.931  13.206  0.73 14.27           O  
ANISOU 1371  O1  SO4 A 156     1522   2287   1614    152   -530   -106       O  
HETATM 1372  O2  SO4 A 156      33.797  20.004  10.998  0.73 19.78           O  
ANISOU 1372  O2  SO4 A 156     2059   3527   1928     80     22   -757       O  
HETATM 1373  O3  SO4 A 156      31.705  20.911  11.678  0.73 19.38           O  
ANISOU 1373  O3  SO4 A 156     1975   2734   2655    811  -1191   -653       O  
HETATM 1374  O4  SO4 A 156      32.499  18.883  12.681  0.73 20.24           O  
ANISOU 1374  O4  SO4 A 156     2190   2590   2910   -515  -1054    507       O  
HETATM 1375 FE   HEM A 154      14.633  27.800   4.742  1.00 11.45          FE  
ANISOU 1375 FE   HEM A 154      881   2005   1465    130   -154    395      FE  
HETATM 1376  CHA HEM A 154      15.982  30.876   5.035  1.00 13.00           C  
ANISOU 1376  CHA HEM A 154     1011   2001   1926    -78   -105    265       C  
HETATM 1377  CHB HEM A 154      13.859  27.797   8.082  1.00 11.37           C  
ANISOU 1377  CHB HEM A 154      826   1981   1515   -106   -181     46       C  
HETATM 1378  CHC HEM A 154      13.333  24.699   4.461  1.00 11.20           C  
ANISOU 1378  CHC HEM A 154     1164   1791   1301    328   -108    181       C  
HETATM 1379  CHD HEM A 154      15.457  27.772   1.469  1.00 12.53           C  
ANISOU 1379  CHD HEM A 154      989   1970   1802    316    -67    350       C  
HETATM 1380  NA  HEM A 154      14.899  29.068   6.263  1.00 11.65           N  
ANISOU 1380  NA  HEM A 154      953   1834   1639     61   -269    300       N  
HETATM 1381  C1A HEM A 154      15.422  30.325   6.188  1.00 12.60           C  
ANISOU 1381  C1A HEM A 154     1142   1997   1648   -201   -534    338       C  
HETATM 1382  C2A HEM A 154      15.366  30.961   7.489  1.00 12.95           C  
ANISOU 1382  C2A HEM A 154     1126   1975   1820   -342   -416    301       C  
HETATM 1383  C3A HEM A 154      14.809  30.050   8.337  1.00 13.08           C  
ANISOU 1383  C3A HEM A 154     1165   2155   1649   -433   -387    224       C  
HETATM 1384  C4A HEM A 154      14.506  28.948   7.597  1.00 12.11           C  
ANISOU 1384  C4A HEM A 154      956   2095   1551   -242   -374    165       C  
HETATM 1385  CMA HEM A 154      14.492  30.266   9.839  1.00 14.56           C  
ANISOU 1385  CMA HEM A 154     1346   2490   1695   -412   -239    -90       C  
HETATM 1386  CAA HEM A 154      15.740  32.409   7.822  1.00 14.61           C  
ANISOU 1386  CAA HEM A 154     1542   1974   2034   -275   -447    115       C  
HETATM 1387  CBA HEM A 154      14.479  33.295   8.021  1.00 15.34           C  
ANISOU 1387  CBA HEM A 154     1538   2046   2245   -281   -444     24       C  
HETATM 1388  CGA HEM A 154      13.598  33.317   6.814  1.00 15.15           C  
ANISOU 1388  CGA HEM A 154     1459   2183   2114   -147   -334     26       C  
HETATM 1389  O1A HEM A 154      12.422  32.879   6.900  1.00 18.91           O  
ANISOU 1389  O1A HEM A 154     1728   2959   2499   -719   -622    185       O  
HETATM 1390  O2A HEM A 154      14.082  33.765   5.740  1.00 16.42           O  
ANISOU 1390  O2A HEM A 154     1849   2000   2392   -261   -503    400       O  
HETATM 1391  NB  HEM A 154      13.754  26.474   5.981  1.00 10.57           N  
ANISOU 1391  NB  HEM A 154      890   1804   1321    155   -212    206       N  
HETATM 1392  C1B HEM A 154      13.521  26.642   7.379  1.00 10.67           C  
ANISOU 1392  C1B HEM A 154      735   1915   1404     57   -318    121       C  
HETATM 1393  C2B HEM A 154      12.876  25.492   7.903  1.00 10.58           C  
ANISOU 1393  C2B HEM A 154      707   1906   1408     -4   -102     13       C  
HETATM 1394  C3B HEM A 154      12.732  24.643   6.900  1.00 10.36           C  
ANISOU 1394  C3B HEM A 154      970   1685   1282    173    -90    191       C  
HETATM 1395  C4B HEM A 154      13.286  25.256   5.694  1.00 10.32           C  
ANISOU 1395  C4B HEM A 154      833   1736   1351    177   -146    271       C  
HETATM 1396  CMB HEM A 154      12.416  25.358   9.356  1.00 12.06           C  
ANISOU 1396  CMB HEM A 154     1075   2217   1289   -113   -197     -2       C  
HETATM 1397  CAB HEM A 154      12.192  23.231   6.941  1.00 11.40           C  
ANISOU 1397  CAB HEM A 154     1222   1695   1414      3      7     77       C  
HETATM 1398  CBB HEM A 154      12.298  22.383   7.924  1.00 12.61           C  
ANISOU 1398  CBB HEM A 154     1597   1789   1407   -160    -63    188       C  
HETATM 1399  NC  HEM A 154      14.397  26.546   3.282  1.00 10.88           N  
ANISOU 1399  NC  HEM A 154      888   2007   1238    326   -210    234       N  
HETATM 1400  C1C HEM A 154      13.905  25.194   3.289  1.00 11.66           C  
ANISOU 1400  C1C HEM A 154     1112   1819   1500    447     67    275       C  
HETATM 1401  C2C HEM A 154      14.088  24.503   2.063  1.00 11.66           C  
ANISOU 1401  C2C HEM A 154     1003   2003   1423    282    -61    227       C  
HETATM 1402  C3C HEM A 154      14.700  25.377   1.220  1.00 11.49           C  
ANISOU 1402  C3C HEM A 154      942   1920   1503    425    -25    281       C  
HETATM 1403  C4C HEM A 154      14.902  26.634   1.946  1.00 11.57           C  
ANISOU 1403  C4C HEM A 154     1057   2000   1341    364   -188    402       C  
HETATM 1404  CMC HEM A 154      13.664  23.054   1.795  1.00 12.21           C  
ANISOU 1404  CMC HEM A 154     1302   1998   1339    194     -4    202       C  
HETATM 1405  CAC HEM A 154      15.247  25.156  -0.167  1.00 12.96           C  
ANISOU 1405  CAC HEM A 154     1291   2182   1453    293    -27    335       C  
HETATM 1406  CBC HEM A 154      15.155  24.077  -0.888  1.00 14.65           C  
ANISOU 1406  CBC HEM A 154     1781   2251   1536    362    229    180       C  
HETATM 1407  ND  HEM A 154      15.464  29.084   3.481  1.00 12.22           N  
ANISOU 1407  ND  HEM A 154      847   2167   1629   -141   -190    311       N  
HETATM 1408  C1D HEM A 154      15.738  28.925   2.139  1.00 11.61           C  
ANISOU 1408  C1D HEM A 154      815   2058   1538    180   -114    540       C  
HETATM 1409  C2D HEM A 154      16.452  30.069   1.609  1.00 13.21           C  
ANISOU 1409  C2D HEM A 154     1138   2172   1710    -30   -195    569       C  
HETATM 1410  C3D HEM A 154      16.638  30.898   2.629  1.00 13.38           C  
ANISOU 1410  C3D HEM A 154     1067   2160   1858   -123   -107    555       C  
HETATM 1411  C4D HEM A 154      16.015  30.311   3.762  1.00 12.11           C  
ANISOU 1411  C4D HEM A 154      810   2076   1715     -6   -259    511       C  
HETATM 1412  CMD HEM A 154      16.924  30.178   0.162  1.00 13.98           C  
ANISOU 1412  CMD HEM A 154     1225   2302   1786    -13     15    674       C  
HETATM 1413  CAD HEM A 154      17.470  32.186   2.652  1.00 15.02           C  
ANISOU 1413  CAD HEM A 154     1340   2227   2139   -264   -231    644       C  
HETATM 1414  CBD HEM A 154      18.965  31.896   2.978  1.00 18.99           C  
ANISOU 1414  CBD HEM A 154     1347   2523   3347   -402   -632   1226       C  
HETATM 1415  CGD HEM A 154      19.890  33.045   2.829  1.00 19.72           C  
ANISOU 1415  CGD HEM A 154     1552   2479   3462   -501   -164    815       C  
HETATM 1416  O1D HEM A 154      20.224  33.371   1.661  1.00 23.54           O  
ANISOU 1416  O1D HEM A 154     2330   3083   3531   -848   -277   1117       O  
HETATM 1417  O2D HEM A 154      20.269  33.573   3.948  1.00 21.08           O  
ANISOU 1417  O2D HEM A 154     2114   2193   3704   -435    218    242       O  
HETATM 1418  C   CMO A 157      16.250  26.974   4.896  0.73 11.14           C  
ANISOU 1418  C   CMO A 157      484   2307   1441     84   -237    943       C  
HETATM 1419  O   CMO A 157      17.216  26.470   4.820  0.73 15.03           O  
ANISOU 1419  O   CMO A 157      893   3222   1595    704    -12    878       O  
HETATM 1420  O   HOH A1002      19.480   7.871  20.765  0.95 15.76           O  
ANISOU 1420  O   HOH A1002     1523   2231   2236     19   -302    328       O  
HETATM 1421  O   HOH A1003      11.900   9.170  20.741  0.84 13.29           O  
ANISOU 1421  O   HOH A1003     1642   1924   1484    428   -140    -87       O  
HETATM 1422  O   HOH A1004      32.813  24.752  12.638  0.96 13.28           O  
ANISOU 1422  O   HOH A1004     1349   2187   1510   -392    -79   -277       O  
HETATM 1423  O   HOH A1005      33.696  25.183   1.464  1.00 15.93           O  
ANISOU 1423  O   HOH A1005     1334   1545   3173   -395      4    206       O  
HETATM 1424  O   HOH A1006       4.288  21.587  15.930  0.86 11.34           O  
ANISOU 1424  O   HOH A1006     1224   1658   1429   -189   -170    147       O  
HETATM 1425  O   HOH A1007      32.574  27.710   0.998  0.92 16.79           O  
ANISOU 1425  O   HOH A1007     2658   1382   2341   -496    390    208       O  
HETATM 1426  O   HOH A1008      12.567  18.586  22.405  0.81 15.44           O  
ANISOU 1426  O   HOH A1008     1975   2408   1482    181    382    -45       O  
HETATM 1427  O   HOH A1009      22.421  22.170  -7.901  0.90 18.24           O  
ANISOU 1427  O   HOH A1009     1613   3061   2258    204    681    363       O  
HETATM 1428  O   HOH A1010      -3.529  23.454   1.393  1.00 21.47           O  
ANISOU 1428  O   HOH A1010     2758   2452   2948   -548  -1487    283       O  
HETATM 1429  O   HOH A1011      24.270  23.131  10.900  0.86 16.32           O  
ANISOU 1429  O   HOH A1011     1512   2026   2662   -428    180    106       O  
HETATM 1430  O   HOH A1012      -2.912  21.999   3.534  0.97 20.46           O  
ANISOU 1430  O   HOH A1012     2359   2769   2647   -394  -1283    604       O  
HETATM 1431  O   HOH A1013       9.196  29.259  11.988  0.75 15.29           O  
ANISOU 1431  O   HOH A1013     1586   1800   2422    310   -499   -569       O  
HETATM 1432  O   HOH A1014      10.040  28.754  14.542  1.00 12.20           O  
ANISOU 1432  O   HOH A1014     1148   1327   2161     94     45   -168       O  
HETATM 1433  O   HOH A1015       5.543  12.102  -2.411  1.00 19.40           O  
ANISOU 1433  O   HOH A1015     1293   2612   3466   -110   -654   -617       O  
HETATM 1434  O   HOH A1016      25.399  23.349  17.882  0.98 30.48           O  
ANISOU 1434  O   HOH A1016     3188   5148   3243  -2714   -937    424       O  
HETATM 1435  O   HOH A1017      11.949   4.538  19.407  1.00 27.88           O  
ANISOU 1435  O   HOH A1017     4664   2788   3142    866    458    505       O  
HETATM 1436  O   HOH A1018       8.523  27.018  21.017  0.79 19.66           O  
ANISOU 1436  O   HOH A1018     2526   3535   1408    803    -62   -899       O  
HETATM 1437  O   HOH A1019       0.251  19.718  25.700  0.80 23.56           O  
ANISOU 1437  O   HOH A1019     2256   3692   3004    870     87     58       O  
HETATM 1438  O   HOH A1020      11.554  13.023  26.719  1.00 17.11           O  
ANISOU 1438  O   HOH A1020     2062   2636   1804    800   -383   -749       O  
HETATM 1439  O   HOH A1021       4.104   6.123  16.079  0.91 16.43           O  
ANISOU 1439  O   HOH A1021     1306   1778   3157   -177    181   -294       O  
HETATM 1440  O   HOH A1022       5.440  12.118   4.804  0.79 16.60           O  
ANISOU 1440  O   HOH A1022     2503   1979   1825    -64   -191   -151       O  
HETATM 1441  O   HOH A1023       3.563  35.323  13.772  1.00 22.08           O  
ANISOU 1441  O   HOH A1023     3902   1906   2582    154    193   -410       O  
HETATM 1442  O   HOH A1024      20.558  31.729  -0.539  0.70 20.01           O  
ANISOU 1442  O   HOH A1024     2096   2766   2740    242    606    367       O  
HETATM 1443  O   HOH A1025      24.605  14.132   5.325  0.99 18.62           O  
ANISOU 1443  O   HOH A1025     1851   2866   2357    676     49     35       O  
HETATM 1444  O   HOH A1026      35.303  26.797   3.527  1.00 26.59           O  
ANISOU 1444  O   HOH A1026     2818   2799   4487   -378   1595    558       O  
HETATM 1445  O   HOH A1027       0.118  14.863  10.674  0.96 15.91           O  
ANISOU 1445  O   HOH A1027     1197   2402   2446   -298   -390    158       O  
HETATM 1446  O   HOH A1028       9.517  13.728  25.228  0.86 18.78           O  
ANISOU 1446  O   HOH A1028     2268   3287   1582   1129   -560   -636       O  
HETATM 1447  O   HOH A1029      13.231  31.519  12.920  0.79 15.97           O  
ANISOU 1447  O   HOH A1029     1570   1842   2656    306    -52   -582       O  
HETATM 1448  O   HOH A1030      23.268  14.933  19.558  0.76 17.45           O  
ANISOU 1448  O   HOH A1030     1408   3686   1538     50   -100    793       O  
HETATM 1449  O   HOH A1031      11.261  30.817  11.056  0.77 20.85           O  
ANISOU 1449  O   HOH A1031     1273   4229   2420   -160   -417     74       O  
HETATM 1450  O   HOH A1032       4.986   8.047  23.750  1.00 29.62           O  
ANISOU 1450  O   HOH A1032     3345   4058   3853    584    808   1873       O  
HETATM 1451  O   HOH A1033      16.501  35.059   5.583  0.93 22.14           O  
ANISOU 1451  O   HOH A1033     2034   2574   3807   -675    215   -204       O  
HETATM 1452  O   HOH A1034      11.911  -0.070  15.342  0.79 17.14           O  
ANISOU 1452  O   HOH A1034     1842   1112   3559    329  -1167   -163       O  
HETATM 1453  O   HOH A1035      15.636  31.301  -3.596  1.00 24.90           O  
ANISOU 1453  O   HOH A1035     1703   3076   4682    100   -179   1770       O  
HETATM 1454  O   HOH A1036      23.672  22.339  20.223  0.82 30.76           O  
ANISOU 1454  O   HOH A1036     4880   3743   3064    747  -2429   -966       O  
HETATM 1455  O   HOH A1037      -1.302   9.571  23.777  1.00 26.10           O  
ANISOU 1455  O   HOH A1037     2587   4173   3156   -493   1016   1005       O  
HETATM 1456  O   HOH A1038      32.337  31.872   7.150  1.00 22.04           O  
ANISOU 1456  O   HOH A1038     4382   1911   2080   -394   -783   -312       O  
HETATM 1457  O   HOH A1039      15.719  13.165  25.237  0.92 19.20           O  
ANISOU 1457  O   HOH A1039     2318   3053   1926    461   -315    169       O  
HETATM 1458  O   HOH A1040      35.488  19.004   4.281  1.00 19.97           O  
ANISOU 1458  O   HOH A1040     2025   2137   3425     84   -927    225       O  
HETATM 1459  O   HOH A1041      -3.695  24.538   8.098  0.83 22.06           O  
ANISOU 1459  O   HOH A1041     1893   4197   2292    587    204    132       O  
HETATM 1460  O   HOH A1042      -3.490  12.602  23.044  0.70 19.95           O  
ANISOU 1460  O   HOH A1042     1830   3790   1961   -751    928   -258       O  
HETATM 1461  O   HOH A1043      33.187  22.327   9.074  0.76 25.09           O  
ANISOU 1461  O   HOH A1043     5504   2195   1836  -1149   -787    302       O  
HETATM 1462  O   HOH A1044      -1.216  17.782  16.176  1.00 22.39           O  
ANISOU 1462  O   HOH A1044     1595   3043   3868   -200     57   -196       O  
HETATM 1463  O   HOH A1045      29.793  18.888  12.924  1.00 31.57           O  
ANISOU 1463  O   HOH A1045     2365   4906   4726    259    -56   2439       O  
HETATM 1464  O   HOH A1046      -1.808  22.618  13.578  0.86 21.27           O  
ANISOU 1464  O   HOH A1046     2128   3042   2912   -649    533   -435       O  
HETATM 1465  O   HOH A1047      -0.788  17.509  22.599  0.72 29.17           O  
ANISOU 1465  O   HOH A1047     3210   4672   3202    221   1047    750       O  
HETATM 1466  O   HOH A1048      -3.859  21.627  10.768  0.76 21.51           O  
ANISOU 1466  O   HOH A1048     1853   3177   3143     74    409    227       O  
HETATM 1467  O   HOH A1049       2.921  36.124  18.425  0.89 25.23           O  
ANISOU 1467  O   HOH A1049     3221   3241   3126   -825    902    150       O  
HETATM 1468  O   HOH A1050      16.830  15.565  -7.782  0.84 13.07           O  
ANISOU 1468  O   HOH A1050     1378   2248   1341     59     84   -172       O  
HETATM 1469  O   HOH A1051      33.055  24.894   8.773  1.00 18.88           O  
ANISOU 1469  O   HOH A1051     2149   3013   2010    102    -23   -334       O  
HETATM 1470  O   HOH A1052      29.176  19.443  15.717  0.84 25.81           O  
ANISOU 1470  O   HOH A1052     1675   3539   4594   -661   -477   1006       O  
HETATM 1471  O   HOH A1053      29.237  22.723   7.006  1.00 14.96           O  
ANISOU 1471  O   HOH A1053     1448   2600   1637   -147    278   -250       O  
HETATM 1472  O   HOH A1054      30.103  21.775  15.960  0.91 27.24           O  
ANISOU 1472  O   HOH A1054     2070   4427   3851     92    392   2179       O  
HETATM 1473  O   HOH A1055      28.390  23.805  17.776  0.70 37.22           O  
ANISOU 1473  O   HOH A1055     3773   5532   4838  -3058  -1006    374       O  
HETATM 1474  O   HOH A1056       4.326  20.315  13.197  0.88 17.29           O  
ANISOU 1474  O   HOH A1056     1777   2745   2049    858   -371   -368       O  
HETATM 1475  O   HOH A1057       8.328  36.504   6.691  0.74 25.17           O  
ANISOU 1475  O   HOH A1057     4195   1353   4014    -36  -1035    116       O  
HETATM 1476  O   HOH A1058      19.017  32.426  -2.615  0.86 25.93           O  
ANISOU 1476  O   HOH A1058     1911   2605   5334    741   -566     73       O  
HETATM 1477  O   HOH A1059      10.995  32.713   9.363  0.85 20.35           O  
ANISOU 1477  O   HOH A1059     1508   2643   3582   -238   -331   -443       O  
HETATM 1478  O   HOH A1060      22.913  30.541  12.929  0.96 30.38           O  
ANISOU 1478  O   HOH A1060     5589   3256   2698  -1656    390   -805       O  
HETATM 1479  O   HOH A1061      36.185  18.890  -2.638  1.00 16.12           O  
ANISOU 1479  O   HOH A1061     1001   2102   3023    -49    146   -322       O  
HETATM 1480  O   HOH A1062       7.331  13.834   6.662  0.94 26.07           O  
ANISOU 1480  O   HOH A1062     4366   2275   3263   -321  -1756   -105       O  
HETATM 1481  O   HOH A1063      33.333  16.841  13.978  0.70 34.34           O  
ANISOU 1481  O   HOH A1063     6711   2199   4139   -243  -2150    617       O  
HETATM 1482  O   HOH A1064      -0.784  20.033  21.535  1.00 28.95           O  
ANISOU 1482  O   HOH A1064     2446   5270   3284    336    583    737       O  
HETATM 1483  O   HOH A1065      24.300  11.988  10.023  1.00 32.25           O  
ANISOU 1483  O   HOH A1065     3377   4031   4847   1101    399   -256       O  
HETATM 1484  O   HOH A1066      20.104  15.584  24.668  0.73 18.51           O  
ANISOU 1484  O   HOH A1066     2246   2943   1844    273   -479    112       O  
HETATM 1485  O   HOH A1067      18.695   0.680  18.321  1.00 39.91           O  
ANISOU 1485  O   HOH A1067     5892   4220   5051    725    578   -730       O  
HETATM 1486  O   HOH A1068      15.800  34.484  -0.935  1.00 28.09           O  
ANISOU 1486  O   HOH A1068     2571   4605   3496   -189   -600    242       O  
HETATM 1487  O   HOH A1069      22.297  25.761 -12.321  0.72 23.01           O  
ANISOU 1487  O   HOH A1069     2148   3873   2722   -292    309   -370       O  
HETATM 1488  O   HOH A1070      14.411  15.563  -6.585  0.95 16.44           O  
ANISOU 1488  O   HOH A1070     2087   2598   1561   -193    388   -253       O  
HETATM 1489  O   HOH A1071      29.322  10.388   1.349  0.74 24.87           O  
ANISOU 1489  O   HOH A1071     3116   2011   4322    912    994   1232       O  
HETATM 1490  O   HOH A1072      28.383  16.167  14.596  0.83 30.38           O  
ANISOU 1490  O   HOH A1072     2199   5585   3759   -252    -76   -662       O  
HETATM 1491  O   HOH A1073       9.416   1.141  18.044  0.85 28.79           O  
ANISOU 1491  O   HOH A1073     5164   3303   2472  -1118    -92    -25       O  
HETATM 1492  O   HOH A1074      17.021   8.427  26.293  0.74 23.29           O  
ANISOU 1492  O   HOH A1074     3152   3420   2276   -522   -811    933       O  
HETATM 1493  O   HOH A1075      24.388  18.357  -4.976  1.00 25.90           O  
ANISOU 1493  O   HOH A1075     1493   4396   3952   -174    961    427       O  
HETATM 1494  O   HOH A1076      -5.889  24.737   2.272  0.90 21.31           O  
ANISOU 1494  O   HOH A1076     2452   2477   3168   -478  -1042    474       O  
HETATM 1495  O   HOH A1077      18.650  18.801  25.242  0.74 26.22           O  
ANISOU 1495  O   HOH A1077     1965   3237   4762    509  -1207  -1770       O  
HETATM 1496  O   HOH A1078       0.987  31.815  -8.892  0.80 19.65           O  
ANISOU 1496  O   HOH A1078     2062   2827   2577   -394   -570    529       O  
HETATM 1497  O   HOH A1079       3.605   8.537   9.848  1.00 29.94           O  
ANISOU 1497  O   HOH A1079     4396   3588   3391   -315    332   -412       O  
HETATM 1498  O   HOH A1080       2.491   6.999  20.627  0.79 27.89           O  
ANISOU 1498  O   HOH A1080     3597   2905   4094    180     34    -98       O  
HETATM 1499  O   HOH A1081      24.223  13.155  17.187  0.66 22.81           O  
ANISOU 1499  O   HOH A1081     2640   3282   2747     79  -1006    694       O  
HETATM 1500  O   HOH A1082      22.928  10.678   8.155  0.96 33.18           O  
ANISOU 1500  O   HOH A1082     3977   2804   5828   1530   1139    852       O  
HETATM 1501  O   HOH A1083      27.679  31.171   2.105  1.00 27.45           O  
ANISOU 1501  O   HOH A1083     1582   5819   3031  -1210   -504   1025       O  
HETATM 1502  O   HOH A1084      24.264  14.517  -5.788  0.99 26.65           O  
ANISOU 1502  O   HOH A1084     2166   5673   2288   -437    190  -1174       O  
HETATM 1503  O   HOH A1085      34.470  17.365  -8.114  0.79 24.61           O  
ANISOU 1503  O   HOH A1085     2225   4940   2187    -99   -507    243       O  
HETATM 1504  O   HOH A1086      30.251  30.643   1.529  1.00 15.47           O  
ANISOU 1504  O   HOH A1086     1967   1993   1918   -779   -359    579       O  
HETATM 1505  O   HOH A1087      -5.373  36.794   4.561  0.98 22.85           O  
ANISOU 1505  O   HOH A1087     2396   3590   2696    318  -1432   -286       O  
HETATM 1506  O   HOH A1088      18.775  33.500   6.197  0.86 21.62           O  
ANISOU 1506  O   HOH A1088     1675   3402   3138    -69    231    352       O  
HETATM 1507  O   HOH A1089      11.658   6.650  21.679  0.71 29.11           O  
ANISOU 1507  O   HOH A1089     2160   3727   5172    317    136   1032       O  
HETATM 1508  O   HOH A1090      14.619  26.113  18.959  1.00 28.65           O  
ANISOU 1508  O   HOH A1090     2090   6554   2241  -1214   -203   -341       O  
HETATM 1509  O   HOH A1091      -4.337  19.406  12.134  1.00 32.41           O  
ANISOU 1509  O   HOH A1091     2348   5037   4930    711    939   1147       O  
HETATM 1510  O   HOH A1092      20.757  35.936   3.903  0.86 43.94           O  
ANISOU 1510  O   HOH A1092     7105   4188   5401   1001    612  -1253       O  
HETATM 1511  O   HOH A1093       0.550  35.234  14.636  0.70 27.56           O  
ANISOU 1511  O   HOH A1093     2680   3461   4329    765    338   -183       O  
HETATM 1512  O   HOH A1094      16.230  26.964  -9.571  0.90 34.75           O  
ANISOU 1512  O   HOH A1094     5150   4373   3678    792   -503   -545       O  
HETATM 1513  O   HOH A1095      -1.970  27.004   7.982  0.78 19.50           O  
ANISOU 1513  O   HOH A1095     2307   2572   2531    987    121   -228       O  
HETATM 1514  O   HOH A1096       2.739   8.136  14.787  1.00 18.59           O  
ANISOU 1514  O   HOH A1096     1849   2701   2511    -93   -243   -184       O  
HETATM 1515  O   HOH A1097      -1.655  17.508  18.552  1.00 27.89           O  
ANISOU 1515  O   HOH A1097     1612   4581   4405    227   -509     30       O  
HETATM 1516  O   HOH A1098      28.425  16.505  11.066  0.81 35.90           O  
ANISOU 1516  O   HOH A1098     2213   5938   5490  -2055   -270    514       O  
HETATM 1517  O   HOH A1099      13.345   5.915  23.621  0.70 28.57           O  
ANISOU 1517  O   HOH A1099     3755   4402   2698   -570   -559     54       O  
HETATM 1518  O   HOH A1100      19.286   6.686   8.478  0.86 25.39           O  
ANISOU 1518  O   HOH A1100     2860   2670   4116    304    -40    -60       O  
HETATM 1519  O   HOH A1101      -3.615  16.669  25.333  0.70 30.48           O  
ANISOU 1519  O   HOH A1101     3138   4986   3457   -603    217    388       O  
HETATM 1520  O   HOH A1102      18.206  34.592  -0.296  0.71 36.70           O  
ANISOU 1520  O   HOH A1102     3238   4405   6301    165   -318   1772       O  
HETATM 1521  O   HOH A1103      27.515  30.907  -3.944  1.00 31.28           O  
ANISOU 1521  O   HOH A1103     2734   5782   3369   1459   -523   1109       O  
HETATM 1522  O   HOH A1104      13.801   9.539   5.343  0.86 24.63           O  
ANISOU 1522  O   HOH A1104     3462   2214   3684   -654  -1052   -246       O  
HETATM 1523  O   HOH A1105      -1.578  25.768  12.234  1.00 35.27           O  
ANISOU 1523  O   HOH A1105     4152   6196   3054   1886  -1222   -985       O  
HETATM 1524  O   HOH A1106       4.381  24.311  -3.890  1.00 31.90           O  
ANISOU 1524  O   HOH A1106     2231   5638   4252    950  -1688  -1536       O  
HETATM 1525  O   HOH A1107      16.481  14.788   1.118  1.00 16.30           O  
ANISOU 1525  O   HOH A1107     1611   2756   1824    295    306   -469       O  
HETATM 1526  O   HOH A1108      15.397   1.410  18.080  0.70 34.25           O  
ANISOU 1526  O   HOH A1108     4146   3076   5791    222  -2224  -1401       O  
HETATM 1527  O   HOH A1109      -2.768  19.915  14.680  0.73 24.68           O  
ANISOU 1527  O   HOH A1109     1529   4514   3336    736    563    119       O  
HETATM 1528  O   HOH A1110      -2.181  23.341  -0.986  0.70 35.04           O  
ANISOU 1528  O   HOH A1110     3728   3909   5676   1190  -1105    370       O  
HETATM 1529  O   HOH A1111      16.677   6.168   7.734  0.75 32.36           O  
ANISOU 1529  O   HOH A1111     5007   3612   3676  -1151   -722  -1225       O  
HETATM 1530  O   HOH A1112       0.173  30.169   9.590  0.71 35.94           O  
ANISOU 1530  O   HOH A1112     4785   3146   5724   1217   1328    306       O  
HETATM 1531  O   HOH A1113      10.938   9.280   5.666  0.92 44.08           O  
ANISOU 1531  O   HOH A1113     5659   5986   5102  -1093    -79   -161       O  
HETATM 1532  O   HOH A1114      22.031  11.420  -0.840  1.00 39.43           O  
ANISOU 1532  O   HOH A1114     3769   5336   5875    316   1651   1714       O  
HETATM 1533  O   HOH A1115      -0.302  24.785  -1.445  1.00 44.93           O  
ANISOU 1533  O   HOH A1115     5478   5581   6011     47   -956   1250       O  
HETATM 1534  O   HOH A1116      11.388  30.758  19.164  0.81 42.38           O  
ANISOU 1534  O   HOH A1116     6643   3977   5482  -1683   -196    252       O  
HETATM 1535  O   HOH A1117      -6.856  24.009   4.964  0.74 29.84           O  
ANISOU 1535  O   HOH A1117     2405   3191   5743     34   -467    725       O  
HETATM 1536  O   HOH A1118      13.091  36.396   4.917  0.74 25.45           O  
ANISOU 1536  O   HOH A1118     2101   2135   5435   -560    225   -542       O  
HETATM 1537  O   HOH A1119      20.095  32.249  13.339  0.74 23.25           O  
ANISOU 1537  O   HOH A1119     4363   2214   2257   -206    947   -743       O  
HETATM 1538  O   HOH A1120      -0.401   7.335  20.907  1.00 42.21           O  
ANISOU 1538  O   HOH A1120     6699   3331   6007   1707   1416   -709       O  
HETATM 1539  O   HOH A1121       5.445   4.023  21.833  0.96 45.93           O  
ANISOU 1539  O   HOH A1121     4612   6365   6474   -946    259    929       O  
HETATM 1540  O   HOH A1122      -4.383  30.327   5.183  0.82 31.30           O  
ANISOU 1540  O   HOH A1122     4179   4538   3173    101  -1689    756       O  
HETATM 1541  O   HOH A1123      20.973   3.977  12.616  0.86 23.78           O  
ANISOU 1541  O   HOH A1123     3701   2187   3148    623   1316    115       O  
HETATM 1542  O   HOH A1124      20.546  23.353  22.010  0.70 37.35           O  
ANISOU 1542  O   HOH A1124     4041   3841   6307  -1264    345    185       O  
HETATM 1543  O   HOH A1125      -8.708  24.853  -5.418  1.00 37.71           O  
ANISOU 1543  O   HOH A1125     4496   3875   5959    904  -1211  -1044       O  
HETATM 1544  O   HOH A1126       1.987  29.626  17.987  0.87 33.03           O  
ANISOU 1544  O   HOH A1126     3864   4014   4672   -562    614   -331       O  
HETATM 1545  O   HOH A1127      18.684  31.196  -6.514  0.73 34.75           O  
ANISOU 1545  O   HOH A1127     3747   4206   5249   -167     57   1897       O  
HETATM 1546  O   HOH A1128      33.967  19.962  -8.415  1.00 44.91           O  
ANISOU 1546  O   HOH A1128     6659   6183   4222    996   -148    602       O  
HETATM 1547  O  BHOH A1129       4.933  37.256   8.740  0.29 24.61           O  
ANISOU 1547  O  BHOH A1129     3116   3117   3117      0      0      0       O  
HETATM 1548  O  AHOH A1130      23.251  24.478  -7.907  0.54 22.18           O  
ANISOU 1548  O  AHOH A1130     2325   2099   4005   -381   1067    111       O  
HETATM 1549  O   HOH A1131      -4.935  22.944   6.296  0.80 37.72           O  
ANISOU 1549  O   HOH A1131     5004   3904   5425   -696   -317   1089       O  
HETATM 1550  O  BHOH A1132      -0.146  12.867   9.028  0.48 39.89           O  
ANISOU 1550  O  BHOH A1132     5677   3646   5835  -2237   -508  -1548       O  
HETATM 1551  O   HOH A1133       4.019   6.017  22.718  0.70 36.70           O  
ANISOU 1551  O   HOH A1133     5325   5574   3046    276    666    164       O  
HETATM 1552  O   HOH A1134       3.462  34.188  19.678  1.00 45.32           O  
ANISOU 1552  O   HOH A1134     5136   6860   5224    963    406    237       O  
HETATM 1553  O   HOH A1135      36.622  20.887  -4.879  0.77 26.91           O  
ANISOU 1553  O   HOH A1135     2250   3876   4099     10    919    674       O  
HETATM 1554  O   HOH A1136      35.657  20.005   6.834  0.74 25.98           O  
ANISOU 1554  O   HOH A1136     2411   4591   2868     43   -559    -32       O  
HETATM 1555  O   HOH A1137      14.813   6.565   9.304  0.87 34.14           O  
ANISOU 1555  O   HOH A1137     4620   3902   4450    549   -506   -455       O  
HETATM 1556  O   HOH A1138      -2.780   9.980  16.628  0.70 38.45           O  
ANISOU 1556  O   HOH A1138     4478   5565   4565   -356    375   -645       O  
HETATM 1557  O  BHOH A1139      20.527  28.453 -11.978  0.46 23.03           O  
ANISOU 1557  O  BHOH A1139     3191   3063   2495  -1182    -97    567       O  
HETATM 1558  O   HOH A1140      13.489   2.113  20.179  0.91 42.48           O  
ANISOU 1558  O   HOH A1140     5168   5425   5546    526   -556    575       O  
HETATM 1559  O   HOH A1141       2.676  37.460  12.176  1.00 34.08           O  
ANISOU 1559  O   HOH A1141     4751   4476   3721   -573  -1405   -383       O  
HETATM 1560  O   HOH A1142      34.898  16.510   5.345  0.83 30.84           O  
ANISOU 1560  O   HOH A1142     4074   2269   5376    357    112    -83       O  
HETATM 1561  O   HOH A1143      37.682  20.495  -1.078  1.00 25.88           O  
ANISOU 1561  O   HOH A1143     1881   3028   4924   -260   -640   -488       O  
HETATM 1562  O   HOH A1144      15.490   7.965  28.356  0.77 38.03           O  
ANISOU 1562  O   HOH A1144     3651   5876   4922   -104    625   1225       O  
HETATM 1563  O   HOH A1145       0.382   6.138  17.077  0.84 35.56           O  
ANISOU 1563  O   HOH A1145     4661   3586   5262  -1140   -867    533       O  
HETATM 1564  O   HOH A1146       3.262  11.987  27.307  0.81 34.44           O  
ANISOU 1564  O   HOH A1146     5762   3849   3473   -925  -1056   1853       O  
HETATM 1565  O   HOH A1147      19.060  30.626  -9.477  0.77 33.73           O  
ANISOU 1565  O   HOH A1147     4807   4809   3200   1305    527   -325       O  
HETATM 1566  O   HOH A1148      30.388  18.183  17.858  1.00 41.30           O  
ANISOU 1566  O   HOH A1148     4817   4156   6718    209  -1627   2029       O  
HETATM 1567  O   HOH A1150      18.496   7.063  24.900  0.90 35.31           O  
ANISOU 1567  O   HOH A1150     3913   5727   3776   1785  -1315     23       O  
HETATM 1568  O   HOH A1151       7.088  36.137  -5.075  0.79 37.67           O  
ANISOU 1568  O   HOH A1151     4250   6295   3769   2449    131   1610       O  
HETATM 1569  O   HOH A1152      14.682  12.305  -0.007  0.82 27.22           O  
ANISOU 1569  O   HOH A1152     4543   2800   3000  -1521    783  -1300       O  
HETATM 1570  O   HOH A1153       7.851  30.327  19.700  0.86 35.25           O  
ANISOU 1570  O   HOH A1153     4167   4831   4395   -114    373   1513       O  
HETATM 1571  O   HOH A1154      10.409  10.932  16.710  0.71 30.44           O  
ANISOU 1571  O   HOH A1154     4581   2933   4053   -505    840    381       O  
HETATM 1572  O   HOH A1155       9.666   4.481  22.384  0.87 44.06           O  
ANISOU 1572  O   HOH A1155     5342   4653   6746   -893     73   1872       O  
HETATM 1573  O   HOH A1156      18.470  31.019  15.063  0.75 37.95           O  
ANISOU 1573  O   HOH A1156     5912   3683   4823  -2862    991  -1612       O  
HETATM 1574  O   HOH A1157      24.007   4.734  13.453  1.00 44.63           O  
ANISOU 1574  O   HOH A1157     5512   4372   7073   1891  -1488  -1062       O  
HETATM 1575  O   HOH A1158      14.916   7.490   6.564  0.70 29.18           O  
ANISOU 1575  O   HOH A1158     3251   2579   5258   -479   -288   -494       O  
HETATM 1576  O   HOH A1159      16.819  29.119  -8.355  0.84 34.31           O  
ANISOU 1576  O   HOH A1159     4071   5073   3893   1219    178  -1228       O  
HETATM 1577  O   HOH A1160      25.791  35.059  -3.497  0.81 32.73           O  
ANISOU 1577  O   HOH A1160     2000   4760   5676    -22    396    841       O  
HETATM 1578  O   HOH A1161      36.677  21.733   0.983  0.78 26.86           O  
ANISOU 1578  O   HOH A1161     1953   4280   3974     95   -421  -1407       O  
HETATM 1579  O   HOH A1162      26.922  11.405   3.129  0.77 38.26           O  
ANISOU 1579  O   HOH A1162     4241   4815   5482   1417    824   -190       O  
HETATM 1580  O   HOH A1163       0.251  21.515  24.143  1.00 42.03           O  
ANISOU 1580  O   HOH A1163     6053   6002   3913    865    912   -907       O  
HETATM 1581  O   HOH A1164      27.615  20.551  18.873  0.87 42.30           O  
ANISOU 1581  O   HOH A1164     4354   6043   5673  -1747   -351   -591       O  
HETATM 1582  O   HOH A1165      22.641  29.076  18.722  0.79 19.06           O  
ANISOU 1582  O   HOH A1165     2937   2052   2252   -402     11   -117       O  
HETATM 1583  O   HOH A1166      27.882  16.492   7.598  1.00 35.30           O  
ANISOU 1583  O   HOH A1166     4084   3991   5339    -16  -1092   1114       O  
HETATM 1584  O   HOH A1167      -5.078  10.979  20.931  0.75 36.40           O  
ANISOU 1584  O   HOH A1167     1793   5197   6841   -757    288  -1560       O  
HETATM 1585  O   HOH A1168      -0.502  32.637   4.450  1.00 37.36           O  
ANISOU 1585  O   HOH A1168     4589   4391   5216     94   -897   -956       O  
HETATM 1586  O   HOH A1169      25.873  24.416  -7.876  0.95 31.36           O  
ANISOU 1586  O   HOH A1169     2858   5261   3797  -1007    397  -1159       O  
HETATM 1587  O   HOH A1170      26.815  21.765  -6.887  0.99 37.82           O  
ANISOU 1587  O   HOH A1170     2759   6755   4856  -1789   -398    374       O  
HETATM 1588  O   HOH A1171      -1.000  27.702  10.455  0.80 32.52           O  
ANISOU 1588  O   HOH A1171     4328   3953   4076  -1261   -543  -1114       O  
HETATM 1589  O   HOH A1172      16.890  24.635  19.305  0.70 33.15           O  
ANISOU 1589  O   HOH A1172     2926   5251   4419    987    104    287       O  
HETATM 1590  O   HOH A1173      15.767  24.853  -8.080  1.00 28.32           O  
ANISOU 1590  O   HOH A1173     2940   3056   4764    645  -1848    659       O  
HETATM 1591  O   HOH A1174      16.906  30.367  20.050  1.00 36.96           O  
ANISOU 1591  O   HOH A1174     4010   4808   5226   -942    359  -1118       O  
HETATM 1592  O   HOH A1175      26.007  28.490  14.169  1.00 45.94           O  
ANISOU 1592  O   HOH A1175     5490   5556   6407  -1130  -1080   1108       O  
HETATM 1593  O   HOH A1176      -2.510  15.943  21.312  0.70 28.93           O  
ANISOU 1593  O   HOH A1176     4613   3963   2416   -101   1515   -337       O  
HETATM 1594  O   HOH A1177      16.114  23.044  17.873  0.82 32.29           O  
ANISOU 1594  O   HOH A1177     2795   4446   5026   -634   -148    700       O  
HETATM 1595  O   HOH A1178      -5.528  23.369  11.609  0.70 34.41           O  
ANISOU 1595  O   HOH A1178     4322   3412   5340    944   1031   -152       O  
HETATM 1596  O  AHOH A1181      14.294  -0.487  15.847  0.43 16.34           O  
ANISOU 1596  O  AHOH A1181     1062   2924   2223    230    443   -362       O  
HETATM 1597  O  BHOH A1181      13.264  -0.139  17.574  0.57 29.76           O  
ANISOU 1597  O  BHOH A1181     4278   3232   3799    550  -1036   -353       O  
HETATM 1598  O  AHOH A1182      11.008   6.511   6.386  0.51 28.50           O  
ANISOU 1598  O  AHOH A1182     2056   4593   4180    608    605    607       O  
HETATM 1599  O  BHOH A1182       9.958   7.827   7.284  0.49 23.86           O  
ANISOU 1599  O  BHOH A1182     2955   3486   2625      0   -523    471       O  
HETATM 1600  O  AHOH A1183      29.379  25.662  15.926  0.59 20.22           O  
ANISOU 1600  O  AHOH A1183     1456   2687   3541    158   -668     66       O  
HETATM 1601  O  BHOH A1183      30.358  26.365  14.598  0.41 11.41           O  
ANISOU 1601  O  BHOH A1183     1061   1843   1431    -59     -5    256       O  
HETATM 1602  O  AHOH A1184      15.555  32.198  12.752  0.86 14.65           O  
ANISOU 1602  O  AHOH A1184     1485   1881   2202    153    188    -44       O  
HETATM 1603  O  BHOH A1184      15.932  30.228  13.458  0.14  9.90           O  
ANISOU 1603  O  BHOH A1184      636   1508   1620   -284    137    424       O  
HETATM 1604  O  AHOH A1185      24.386  12.801   2.936  0.50 22.80           O  
ANISOU 1604  O  AHOH A1185     2561   3256   2848   1249    172   -530       O  
HETATM 1605  O  BHOH A1185      24.209  11.793   1.254  0.50 25.44           O  
ANISOU 1605  O  BHOH A1185     3239   2891   3537   -427   -198   -758       O  
HETATM 1606  O  AHOH A1186      27.097  18.027  -5.626  0.50 23.74           O  
ANISOU 1606  O  AHOH A1186     2925   3291   2803    118   -335  -1001       O  
HETATM 1607  O  BHOH A1186      16.679  16.155  28.069  0.50 27.23           O  
ANISOU 1607  O  BHOH A1186     2310   4231   3804   1176  -1135   -405       O  
HETATM 1608  O  AHOH A1187      24.874  19.935  -6.984  0.57 23.83           O  
ANISOU 1608  O  AHOH A1187     3239   3595   2219  -1207   1201   -309       O  
HETATM 1609  O  BHOH A1187      14.528  19.982  23.747  0.43 16.67           O  
ANISOU 1609  O  BHOH A1187     1435   2290   2608     68   -709   -207       O  
HETATM 1610  O   HOH A1188      21.402  31.456   8.884  1.00 21.72           O  
ANISOU 1610  O   HOH A1188     3225   2311   2716   -350    528    -82       O  
CONECT  824 1375                                                                
CONECT 1365 1366 1367 1368 1369                                                 
CONECT 1366 1365                                                                
CONECT 1367 1365                                                                
CONECT 1368 1365                                                                
CONECT 1369 1365                                                                
CONECT 1370 1371 1372 1373 1374                                                 
CONECT 1371 1370                                                                
CONECT 1372 1370                                                                
CONECT 1373 1370                                                                
CONECT 1374 1370                                                                
CONECT 1375  824 1380 1391 1399                                                 
CONECT 1375 1407 1418 1419                                                      
CONECT 1376 1381 1411                                                           
CONECT 1377 1384 1392                                                           
CONECT 1378 1395 1400                                                           
CONECT 1379 1403 1408                                                           
CONECT 1380 1375 1381 1384                                                      
CONECT 1381 1376 1380 1382                                                      
CONECT 1382 1381 1383 1386                                                      
CONECT 1383 1382 1384 1385                                                      
CONECT 1384 1377 1380 1383                                                      
CONECT 1385 1383                                                                
CONECT 1386 1382 1387                                                           
CONECT 1387 1386 1388                                                           
CONECT 1388 1387 1389 1390                                                      
CONECT 1389 1388                                                                
CONECT 1390 1388                                                                
CONECT 1391 1375 1392 1395                                                      
CONECT 1392 1377 1391 1393                                                      
CONECT 1393 1392 1394 1396                                                      
CONECT 1394 1393 1395 1397                                                      
CONECT 1395 1378 1391 1394                                                      
CONECT 1396 1393                                                                
CONECT 1397 1394 1398                                                           
CONECT 1398 1397                                                                
CONECT 1399 1375 1400 1403                                                      
CONECT 1400 1378 1399 1401                                                      
CONECT 1401 1400 1402 1404                                                      
CONECT 1402 1401 1403 1405                                                      
CONECT 1403 1379 1399 1402                                                      
CONECT 1404 1401                                                                
CONECT 1405 1402 1406                                                           
CONECT 1406 1405                                                                
CONECT 1407 1375 1408 1411                                                      
CONECT 1408 1379 1407 1409                                                      
CONECT 1409 1408 1410 1412                                                      
CONECT 1410 1409 1411 1413                                                      
CONECT 1411 1376 1407 1410                                                      
CONECT 1412 1409                                                                
CONECT 1413 1410 1414                                                           
CONECT 1414 1413 1415                                                           
CONECT 1415 1414 1416 1417                                                      
CONECT 1416 1415                                                                
CONECT 1417 1415                                                                
CONECT 1418 1375 1419                                                           
CONECT 1419 1375 1418                                                           
MASTER      265    0    4    8    0    0   11    6 1609    1   57   12          
END                                                                             



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