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***  OXYGEN STORAGE/TRANSPORT 03-SEP-01 1JW8  ***

elNémo ID: 210217152258104731

Job options:

ID        	=	 210217152258104731
JOBID     	=	 OXYGEN STORAGE/TRANSPORT 03-SEP-01 1JW8
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    OXYGEN STORAGE/TRANSPORT                03-SEP-01   1JW8              
TITLE     1.3 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF P6 FORM OF MYOGLOBIN     
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;                                                
SOURCE   5 GENE: MB (SYNTHESIZED);                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ANISOTROPIC REFINEMENT MYOGLOBIN, OXYGEN STORAGE-TRANSPORT COMPLEX    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.N.PHILLIPS JR.                                                      
REVDAT   6   04-OCT-17 1JW8    1       REMARK                                   
REVDAT   5   30-JAN-13 1JW8    1       JRNL   AUTHOR                            
REVDAT   4   13-JUL-11 1JW8    1       VERSN                                    
REVDAT   3   24-FEB-09 1JW8    1       VERSN                                    
REVDAT   2   18-NOV-08 1JW8    1       JRNL                                     
REVDAT   1   10-OCT-01 1JW8    0                                                
JRNL        AUTH   D.A.KONDRASHOV,W.ZHANG,R.ARANDA,B.STEC,G.N.PHILLIPS JR.      
JRNL        TITL   SAMPLING OF THE NATIVE CONFORMATIONAL ENSEMBLE OF MYOGLOBIN  
JRNL        TITL 2 VIA STRUCTURES IN DIFFERENT CRYSTALLINE ENVIRONMENTS.        
JRNL        REF    PROTEINS                      V.  70   353 2008              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   17680690                                                     
JRNL        DOI    10.1002/PROT.21499                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 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) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.135                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.133                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.157                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 4.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 1970                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 47301                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.125                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.147                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 4.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 1770                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 42202                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1225                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 60                                            
REMARK   3   SOLVENT ATOMS      : 260                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL                    
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 9                       
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 14307                   
REMARK   3   NUMBER OF RESTRAINTS                     : 17825                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.013                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.027                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : NULL                    
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.066                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.076                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.022                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL                    
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL                    
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL                    
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : NULL                                
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1JW8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-01.                  
REMARK 100 THE DEPOSITION ID IS D_1000014256.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL; NULL                         
REMARK 200  TEMPERATURE           (KELVIN) : 100; NULL                          
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; N                               
REMARK 200  RADIATION SOURCE               : NSLS; ROTATING ANODE               
REMARK 200  BEAMLINE                       : X12C; NULL                         
REMARK 200  X-RAY GENERATOR MODEL          : NULL; RIGAKU RU200                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91; 1.5418                       
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL; NULL                         
REMARK 200  DETECTOR MANUFACTURER          : NULL; NULL                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49946                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : 0.05100                            
REMARK 200   FOR THE DATA SET  : 28.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MERLOT                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, TRIS, PH 9.0, VAPOR    
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 295K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z                                                
REMARK 290       6555   X-Y,X,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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -186.0 KCAL/MOL                       
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 350   BIOMT1   2 -0.500000 -0.866025  0.000000       90.38000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000       45.19000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000       78.27138            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 S    SO4 A 158  LIES ON A SPECIAL POSITION.                          
REMARK 375 O2   SO4 A 158  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1243  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1248  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  32   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG A  46   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    GLU A 110   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.3 DEGREES          
REMARK 500    TYR A 147   CB  -  CG  -  CD2 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    GLU A 149   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.5 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  21       77.17   -157.45                                   
REMARK 500    HIS A  82       59.86    -90.21                                   
REMARK 500    LYS A  99       64.75     60.46                                   
REMARK 500    PHE A 124       47.73   -142.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 155  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CMO A 156   C                                                      
REMARK 620 2 HEM A 155   NA   97.8                                              
REMARK 620 3 HEM A 155   NB   92.9  90.6                                        
REMARK 620 4 HEM A 155   NC   81.7 178.6  90.7                                  
REMARK 620 5 HEM A 155   ND   87.8  89.5 179.3  89.2                            
REMARK 620 6 HIS A  94   NE2 171.6  90.1  89.9  90.4  89.4                      
REMARK 620 7 CMO A 156   O     1.7  98.9  94.2  80.5  86.5 170.1                
REMARK 620 N                    1     2     3     4     5     6                 
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 157                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 158                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 159                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 155                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO A 156                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2MBW   RELATED DB: PDB                                   
REMARK 900 RECOMBINANT SPERM WHALE MYOGLOBIN (MET)                              
DBREF  1JW8 A    2   154  UNP    P02185   MYG_PHYCA        1    153             
SEQADV 1JW8 MET A    1  UNP  P02185              SEE REMARK 999                 
SEQADV 1JW8 ASN A  123  UNP  P02185    ASP   122 SEE REMARK 999                 
SEQRES   1 A  154  MET VAL LEU SER GLU GLY GLU TRP GLN LEU VAL LEU HIS          
SEQRES   2 A  154  VAL TRP ALA LYS VAL GLU ALA ASP VAL ALA GLY HIS GLY          
SEQRES   3 A  154  GLN ASP ILE LEU ILE ARG LEU PHE LYS SER HIS PRO GLU          
SEQRES   4 A  154  THR LEU GLU LYS PHE ASP ARG PHE LYS HIS LEU LYS THR          
SEQRES   5 A  154  GLU ALA GLU MET LYS ALA SER GLU ASP LEU LYS LYS HIS          
SEQRES   6 A  154  GLY VAL THR VAL LEU THR ALA LEU GLY ALA ILE LEU LYS          
SEQRES   7 A  154  LYS LYS GLY HIS HIS GLU ALA GLU LEU LYS PRO LEU ALA          
SEQRES   8 A  154  GLN SER HIS ALA THR LYS HIS LYS ILE PRO ILE LYS TYR          
SEQRES   9 A  154  LEU GLU PHE ILE SER GLU ALA ILE ILE HIS VAL LEU HIS          
SEQRES  10 A  154  SER ARG HIS PRO GLY ASN PHE GLY ALA ASP ALA GLN GLY          
SEQRES  11 A  154  ALA MET ASN LYS ALA LEU GLU LEU PHE ARG LYS ASP ILE          
SEQRES  12 A  154  ALA ALA LYS TYR LYS GLU LEU GLY TYR GLN GLY                  
HET    SO4  A 157       5                                                       
HET    SO4  A 158       5                                                       
HET    SO4  A 159       5                                                       
HET    HEM  A 155      43                                                       
HET    CMO  A 156       2                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     CMO CARBON MONOXIDE                                                  
HETSYN     HEM HEME                                                             
FORMUL   2  SO4    3(O4 S 2-)                                                   
FORMUL   5  HEM    C34 H32 FE N4 O4                                             
FORMUL   6  CMO    C O                                                          
FORMUL   7  HOH   *260(H2 O)                                                    
HELIX    1   1 SER A    4  GLU A   19  1                                  16    
HELIX    2   2 ASP A   21  HIS A   37  1                                  17    
HELIX    3   3 PRO A   38  PHE A   44  5                                   7    
HELIX    4   4 THR A   52  SER A   59  1                                   8    
HELIX    5   5 SER A   59  LYS A   79  1                                  21    
HELIX    6   6 HIS A   83  LYS A   97  1                                  15    
HELIX    7   7 PRO A  101  HIS A  120  1                                  20    
HELIX    8   8 GLY A  125  GLY A  151  1                                  27    
LINK        FE   HEM A 155                 C   CMO A 156     1555   1555  1.77  
LINK        FE   HEM A 155                 NE2 HIS A  94     1555   1555  2.06  
LINK        FE   HEM A 155                 O   CMO A 156     1555   1555  2.91  
SITE     1 AC1  8 SER A   4  GLU A   5  THR A  52  GLU A  53                    
SITE     2 AC1  8 ALA A  54  HOH A1093  HOH A1227  HOH A1232                    
SITE     1 AC2  2 LYS A  17  HOH A1236                                          
SITE     1 AC3  8 GLY A 125  ALA A 126  ASP A 127  HOH A1025                    
SITE     2 AC3  8 HOH A1028  HOH A1166  HOH A1211  HOH A1256                    
SITE     1 AC4 22 THR A  40  LYS A  43  PHE A  44  ARG A  46                    
SITE     2 AC4 22 HIS A  65  THR A  68  VAL A  69  ALA A  72                    
SITE     3 AC4 22 LEU A  90  SER A  93  HIS A  94  HIS A  98                    
SITE     4 AC4 22 ILE A 100  TYR A 104  LEU A 105  CMO A 156                    
SITE     5 AC4 22 HOH A1036  HOH A1078  HOH A1081  HOH A1082                    
SITE     6 AC4 22 HOH A1110  HOH A1136                                          
SITE     1 AC5  4 PHE A  44  HIS A  65  VAL A  69  HEM A 155                    
CRYST1   90.380   90.380   45.340  90.00  90.00 120.00 P 6           6          
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      0.011064  0.006388  0.000000        0.00000                         
SCALE2      0.000000  0.012776  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022056        0.00000                         
ATOM      1  N   MET A   1      24.219   8.328  -8.715  1.00 40.93           N  
ANISOU    1  N   MET A   1     4526   5859   5167  -3437  -1423   1153       N  
ATOM      2  CA  MET A   1      24.039   9.660  -9.304  1.00 45.36           C  
ANISOU    2  CA  MET A   1     4773   6067   6395  -2587   -294   1566       C  
ATOM      3  C   MET A   1      25.324  10.160  -9.917  1.00 37.92           C  
ANISOU    3  C   MET A   1     3735   4780   5892  -1448   -866   1795       C  
ATOM      4  O   MET A   1      26.370   9.528  -9.640  1.00 52.87           O  
ANISOU    4  O   MET A   1     4738   7346   8004   -559   -940   4914       O  
ATOM      5  CB  MET A   1      23.548  10.568  -8.167  1.00 47.75           C  
ANISOU    5  CB  MET A   1     5526   6386   6229  -2051    430   2060       C  
ATOM      6  CG  MET A   1      22.873   9.760  -7.072  1.00 47.55           C  
ANISOU    6  CG  MET A   1     6145   6761   5160  -1165  -1050   3448       C  
ATOM      7  SD  MET A   1      23.921   9.180  -5.724  1.00 34.72           S  
ANISOU    7  SD  MET A   1     3845   4685   4661    529  -1139   -640       S  
ATOM      8  CE  MET A   1      22.659   9.210  -4.423  1.00 55.46           C  
ANISOU    8  CE  MET A   1    14120   2746   4206   2955   3549   -517       C  
ATOM      9  N   VAL A   2      25.405  11.229 -10.708  1.00 23.96           N  
ANISOU    9  N   VAL A   2     2256   2927   3923   -902   -874   -156       N  
ATOM     10  CA  VAL A   2      26.757  11.589 -11.178  1.00 20.19           C  
ANISOU   10  CA  VAL A   2     2171   1633   3866   -277   -568   -748       C  
ATOM     11  C   VAL A   2      27.077  13.091 -11.040  1.00 15.78           C  
ANISOU   11  C   VAL A   2     1687   1392   2916    182   -704   -383       C  
ATOM     12  O   VAL A   2      26.351  13.949 -11.538  1.00 18.12           O  
ANISOU   12  O   VAL A   2     2250   1986   2649    395   -935   -295       O  
ATOM     13  CB  VAL A   2      26.966  11.200 -12.651  1.00 24.24           C  
ANISOU   13  CB  VAL A   2     2847   2221   4144     50   -500  -1292       C  
ATOM     14  CG1 VAL A   2      25.915  11.919 -13.469  1.00 32.26           C  
ANISOU   14  CG1 VAL A   2     1943   5813   4501   -801  -1409   -553       C  
ATOM     15  CG2 VAL A   2      28.380  11.519 -13.111  1.00 22.75           C  
ANISOU   15  CG2 VAL A   2     2288   3156   3201    506   -986  -1390       C  
ATOM     16  N   LEU A   3      28.159  13.439 -10.380  1.00 10.38           N  
ANISOU   16  N   LEU A   3     1593   1332   1018    -27    -22   -159       N  
ATOM     17  CA  LEU A   3      28.500  14.835 -10.156  1.00  9.69           C  
ANISOU   17  CA  LEU A   3     1562   1322    798     36   -135    -33       C  
ATOM     18  C   LEU A   3      29.137  15.459 -11.415  1.00  9.39           C  
ANISOU   18  C   LEU A   3     1608   1318    643    246   -109    -65       C  
ATOM     19  O   LEU A   3      29.859  14.777 -12.157  1.00 11.36           O  
ANISOU   19  O   LEU A   3     1937   1286   1092    368    178    -94       O  
ATOM     20  CB  LEU A   3      29.479  15.068  -8.998  1.00  9.59           C  
ANISOU   20  CB  LEU A   3     1508   1501    634    225    -96   -129       C  
ATOM     21  CG  LEU A   3      28.831  15.017  -7.604  1.00  9.06           C  
ANISOU   21  CG  LEU A   3     1384   1249    811      6    165   -261       C  
ATOM     22  CD1 LEU A   3      28.359  13.605  -7.238  1.00 12.02           C  
ANISOU   22  CD1 LEU A   3     1272   1502   1793    -78     49    211       C  
ATOM     23  CD2 LEU A   3      29.836  15.554  -6.585  1.00 10.78           C  
ANISOU   23  CD2 LEU A   3     1793   1561    743    -20   -136   -119       C  
ATOM     24  N   SER A   4      28.861  16.743 -11.641  1.00  9.29           N  
ANISOU   24  N   SER A   4     1291   1226   1014     68   -254     18       N  
ATOM     25  CA  SER A   4      29.646  17.448 -12.696  1.00  9.43           C  
ANISOU   25  CA  SER A   4     1309   1333    939    232   -261     87       C  
ATOM     26  C   SER A   4      31.039  17.765 -12.217  1.00  8.88           C  
ANISOU   26  C   SER A   4     1393   1252    728    -20   -133   -179       C  
ATOM     27  O   SER A   4      31.328  17.736 -11.013  1.00  9.04           O  
ANISOU   27  O   SER A   4     1733    967    736     43   -291    -70       O  
ATOM     28  CB  SER A   4      28.935  18.745 -13.102  1.00 10.53           C  
ANISOU   28  CB  SER A   4     1921   1122    958    250   -438    -21       C  
ATOM     29  OG  SER A   4      29.027  19.605 -11.952  1.00 10.72           O  
ANISOU   29  OG  SER A   4     1769   1398    906    164   -293   -110       O  
ATOM     30  N   GLU A   5      31.934  18.085 -13.147  1.00  9.85           N  
ANISOU   30  N   GLU A   5     1579   1110   1055    -87     64     24       N  
ATOM     31  CA  GLU A   5      33.275  18.540 -12.742  1.00  8.93           C  
ANISOU   31  CA  GLU A   5     1486   1119    788     46    102   -111       C  
ATOM     32  C   GLU A   5      33.155  19.784 -11.878  1.00  9.25           C  
ANISOU   32  C   GLU A   5     1696   1210    610    122    -64    -40       C  
ATOM     33  O   GLU A   5      33.930  19.945 -10.924  1.00 10.08           O  
ANISOU   33  O   GLU A   5     1929   1271    629   -132    -46    -18       O  
ATOM     34  CB  GLU A   5      34.137  18.788 -13.971  1.00 10.68           C  
ANISOU   34  CB  GLU A   5     1824   1534    701   -350    162   -175       C  
ATOM     35  CG  GLU A   5      35.452  19.453 -13.688  1.00 11.40           C  
ANISOU   35  CG  GLU A   5     1707   1625   1000   -267    153   -109       C  
ATOM     36  CD  GLU A   5      36.468  18.614 -12.948  1.00 11.48           C  
ANISOU   36  CD  GLU A   5     1875   1624    864   -197     51   -154       C  
ATOM     37  OE1 GLU A   5      36.231  17.420 -12.717  1.00 12.82           O  
ANISOU   37  OE1 GLU A   5     1866   1690   1314   -110    325    -30       O  
ATOM     38  OE2 GLU A   5      37.534  19.170 -12.607  1.00 14.70           O  
ANISOU   38  OE2 GLU A   5     1755   2100   1731   -235     14   -549       O  
ATOM     39  N   GLY A   6      32.246  20.713 -12.195  1.00  9.96           N  
ANISOU   39  N   GLY A   6     2054    944    785    200    141     64       N  
ATOM     40  CA  GLY A   6      32.107  21.894 -11.354  1.00 10.04           C  
ANISOU   40  CA  GLY A   6     2139    879    797    -68     65     -8       C  
ATOM     41  C   GLY A   6      31.732  21.539  -9.927  1.00  8.78           C  
ANISOU   41  C   GLY A   6     1498   1095    741    135    -42     49       C  
ATOM     42  O   GLY A   6      32.232  22.131  -8.943  1.00  9.53           O  
ANISOU   42  O   GLY A   6     1884    964    774     47     21      8       O  
ATOM     43  N   GLU A   7      30.837  20.566  -9.763  1.00  8.69           N  
ANISOU   43  N   GLU A   7     1456   1012    834    237     44    106       N  
ATOM     44  CA  GLU A   7      30.490  20.116  -8.399  1.00  8.45           C  
ANISOU   44  CA  GLU A   7     1290   1002    917     91      1     98       C  
ATOM     45  C   GLU A   7      31.699  19.501  -7.719  1.00  7.67           C  
ANISOU   45  C   GLU A   7     1296    895    723     63    -89   -113       C  
ATOM     46  O   GLU A   7      31.976  19.772  -6.550  1.00  7.78           O  
ANISOU   46  O   GLU A   7     1350    896    709     53     22   -103       O  
ATOM     47  CB  GLU A   7      29.308  19.146  -8.495  1.00  9.38           C  
ANISOU   47  CB  GLU A   7     1170   1160   1236     67    -15    -81       C  
ATOM     48  CG  GLU A   7      28.003  19.884  -8.841  1.00 10.80           C  
ANISOU   48  CG  GLU A   7     1372   1238   1492    267   -251   -212       C  
ATOM     49  CD  GLU A   7      26.884  18.946  -9.228  1.00 10.93           C  
ANISOU   49  CD  GLU A   7     1368   1476   1311    226   -332   -349       C  
ATOM     50  OE1 GLU A   7      25.710  19.365  -9.103  1.00 16.11           O  
ANISOU   50  OE1 GLU A   7     1355   2003   2763    297   -162   -805       O  
ATOM     51  OE2 GLU A   7      27.070  17.819  -9.709  1.00 11.03           O  
ANISOU   51  OE2 GLU A   7     1547   1423   1219    237   -219   -271       O  
ATOM     52  N   TRP A   8      32.446  18.625  -8.424  1.00  7.78           N  
ANISOU   52  N   TRP A   8     1283    872    802    105     58      7       N  
ATOM     53  CA  TRP A   8      33.637  18.074  -7.777  1.00  7.71           C  
ANISOU   53  CA  TRP A   8     1269    978    682     76    -50   -193       C  
ATOM     54  C   TRP A   8      34.605  19.186  -7.389  1.00  7.97           C  
ANISOU   54  C   TRP A   8     1420   1067    541    -26    116   -317       C  
ATOM     55  O   TRP A   8      35.234  19.074  -6.340  1.00  8.06           O  
ANISOU   55  O   TRP A   8     1258   1127    678     46      9   -182       O  
ATOM     56  CB  TRP A   8      34.386  17.089  -8.719  1.00  8.59           C  
ANISOU   56  CB  TRP A   8     1344    792   1128    138     22   -219       C  
ATOM     57  CG  TRP A   8      33.652  15.766  -8.823  1.00  7.45           C  
ANISOU   57  CG  TRP A   8     1210    862    758    158     28    -22       C  
ATOM     58  CD1 TRP A   8      33.122  15.199  -9.961  1.00  8.46           C  
ANISOU   58  CD1 TRP A   8     1418   1055    742    -29     66   -114       C  
ATOM     59  CD2 TRP A   8      33.399  14.854  -7.754  1.00  7.64           C  
ANISOU   59  CD2 TRP A   8     1182    985    736    103      7    -58       C  
ATOM     60  NE1 TRP A   8      32.545  13.987  -9.665  1.00  8.10           N  
ANISOU   60  NE1 TRP A   8     1400    928    750    186    -75    -36       N  
ATOM     61  CE2 TRP A   8      32.707  13.761  -8.300  1.00  8.14           C  
ANISOU   61  CE2 TRP A   8     1250   1057    787     12     27      7       C  
ATOM     62  CE3 TRP A   8      33.723  14.859  -6.369  1.00  8.00           C  
ANISOU   62  CE3 TRP A   8     1355    970    714    258     52     68       C  
ATOM     63  CZ2 TRP A   8      32.287  12.678  -7.512  1.00  8.13           C  
ANISOU   63  CZ2 TRP A   8     1343   1004    742    127    145    -13       C  
ATOM     64  CZ3 TRP A   8      33.297  13.782  -5.620  1.00  7.85           C  
ANISOU   64  CZ3 TRP A   8     1236    921    825    288     -7     22       C  
ATOM     65  CH2 TRP A   8      32.604  12.711  -6.164  1.00  8.12           C  
ANISOU   65  CH2 TRP A   8     1427    916    743    248    135    -33       C  
ATOM     66  N   GLN A   9      34.716  20.229  -8.196  1.00  8.45           N  
ANISOU   66  N   GLN A   9     1180   1040    989     91     10   -120       N  
ATOM     67  CA  GLN A   9      35.687  21.258  -7.790  1.00  8.73           C  
ANISOU   67  CA  GLN A   9     1353   1173    791   -102     91   -118       C  
ATOM     68  C   GLN A   9      35.205  21.985  -6.539  1.00  8.50           C  
ANISOU   68  C   GLN A   9     1439   1193    597     99     39     23       C  
ATOM     69  O   GLN A   9      36.021  22.358  -5.705  1.00  8.74           O  
ANISOU   69  O   GLN A   9     1476   1073    771   -164     27    -30       O  
ATOM     70  CB  GLN A   9      35.955  22.268  -8.921  1.00 11.66           C  
ANISOU   70  CB  GLN A   9     2253   1418    760   -258    397    -10       C  
ATOM     71  CG  GLN A   9      36.808  21.598 -10.033  1.00 13.48           C  
ANISOU   71  CG  GLN A   9     2009   1912   1200   -497    605   -423       C  
ATOM     72  CD  GLN A   9      38.133  21.090  -9.501  1.00 16.32           C  
ANISOU   72  CD  GLN A   9     1735   2905   1562   -558    494   -905       C  
ATOM     73  OE1 GLN A   9      38.727  21.589  -8.559  1.00 21.10           O  
ANISOU   73  OE1 GLN A   9     2159   4165   1694   -878    333  -1129       O  
ATOM     74  NE2 GLN A   9      38.699  20.042 -10.086  1.00 19.54           N  
ANISOU   74  NE2 GLN A   9     2230   3081   2114    114    268   -790       N  
ATOM     75  N   LEU A  10      33.899  22.169  -6.350  1.00  8.12           N  
ANISOU   75  N   LEU A  10     1407    818    860     60    107     42       N  
ATOM     76  CA  LEU A  10      33.420  22.756  -5.083  1.00  7.39           C  
ANISOU   76  CA  LEU A  10     1309    768    730    -28     66     49       C  
ATOM     77  C   LEU A  10      33.746  21.858  -3.918  1.00  6.85           C  
ANISOU   77  C   LEU A  10     1076    738    788     80    -13    -40       C  
ATOM     78  O   LEU A  10      34.146  22.334  -2.835  1.00  9.29           O  
ANISOU   78  O   LEU A  10     1961    927    642   -196     94   -104       O  
ATOM     79  CB  LEU A  10      31.908  23.013  -5.159  1.00  8.39           C  
ANISOU   79  CB  LEU A  10     1400   1064    722    213    -40     74       C  
ATOM     80  CG  LEU A  10      31.475  24.111  -6.123  1.00  9.38           C  
ANISOU   80  CG  LEU A  10     1616   1041    906     98   -139    166       C  
ATOM     81  CD1 LEU A  10      29.953  24.124  -6.285  1.00 12.36           C  
ANISOU   81  CD1 LEU A  10     1577   1636   1485    276   -189    504       C  
ATOM     82  CD2 LEU A  10      31.999  25.473  -5.656  1.00 14.79           C  
ANISOU   82  CD2 LEU A  10     2668   1054   1899   -273   -361    227       C  
ATOM     83  N   VAL A  11      33.614  20.544  -4.102  1.00  6.74           N  
ANISOU   83  N   VAL A  11     1037    681    842      2     17    -22       N  
ATOM     84  CA  VAL A  11      33.952  19.574  -3.067  1.00  6.72           C  
ANISOU   84  CA  VAL A  11      982    812    760     45     29     -1       C  
ATOM     85  C   VAL A  11      35.442  19.674  -2.700  1.00  6.70           C  
ANISOU   85  C   VAL A  11     1016    894    637    -44     15   -139       C  
ATOM     86  O   VAL A  11      35.840  19.751  -1.561  1.00  7.76           O  
ANISOU   86  O   VAL A  11     1184   1111    652    -35    -79    -17       O  
ATOM     87  CB  VAL A  11      33.600  18.149  -3.532  1.00  6.67           C  
ANISOU   87  CB  VAL A  11     1063    796    675   -165    -71    129       C  
ATOM     88  CG1 VAL A  11      34.163  17.068  -2.615  1.00  8.57           C  
ANISOU   88  CG1 VAL A  11     1401    868    987   -150   -181    277       C  
ATOM     89  CG2 VAL A  11      32.092  18.011  -3.639  1.00  8.43           C  
ANISOU   89  CG2 VAL A  11     1027   1412    764   -125     58    -50       C  
ATOM     90  N   LEU A  12      36.277  19.652  -3.760  1.00  7.13           N  
ANISOU   90  N   LEU A  12      980    950    778    -39     54   -152       N  
ATOM     91  CA  LEU A  12      37.740  19.610  -3.519  1.00  7.78           C  
ANISOU   91  CA  LEU A  12      945   1079    932   -157     26   -105       C  
ATOM     92  C   LEU A  12      38.248  20.951  -2.994  1.00  8.09           C  
ANISOU   92  C   LEU A  12     1029   1178    865   -237    -46     -4       C  
ATOM     93  O   LEU A  12      39.245  20.976  -2.257  1.00  8.84           O  
ANISOU   93  O   LEU A  12      974   1470    914   -276   -116    -12       O  
ATOM     94  CB  LEU A  12      38.434  19.190  -4.805  1.00 10.41           C  
ANISOU   94  CB  LEU A  12     1166   1611   1180      4    231   -293       C  
ATOM     95  CG  LEU A  12      38.098  17.747  -5.237  1.00 11.96           C  
ANISOU   95  CG  LEU A  12     1536   1579   1428    406      8   -593       C  
ATOM     96  CD1 LEU A  12      38.693  17.420  -6.581  1.00 17.24           C  
ANISOU   96  CD1 LEU A  12     1780   2925   1846    463    287  -1166       C  
ATOM     97  CD2 LEU A  12      38.560  16.740  -4.190  1.00 16.73           C  
ANISOU   97  CD2 LEU A  12     2343   1642   2370    781   -375   -333       C  
ATOM     98  N   HIS A  13      37.596  22.063  -3.330  1.00  7.99           N  
ANISOU   98  N   HIS A  13     1155   1027    854   -182    138    115       N  
ATOM     99  CA  HIS A  13      38.095  23.363  -2.817  1.00  8.46           C  
ANISOU   99  CA  HIS A  13     1108   1192    912   -295     60      7       C  
ATOM    100  C   HIS A  13      37.828  23.514  -1.334  1.00  8.56           C  
ANISOU  100  C   HIS A  13     1233   1008   1010   -201    153     -8       C  
ATOM    101  O   HIS A  13      38.656  24.113  -0.643  1.00 10.81           O  
ANISOU  101  O   HIS A  13     1448   1620   1038   -578    -36     20       O  
ATOM    102  CB  HIS A  13      37.517  24.524  -3.602  1.00 13.03           C  
ANISOU  102  CB  HIS A  13     2647   1043   1262   -410   -168    239       C  
ATOM    103  CG  HIS A  13      38.270  24.791  -4.871  1.00 19.96           C  
ANISOU  103  CG  HIS A  13     3885   2361   1339  -1064     41    555       C  
ATOM    104  ND1 HIS A  13      38.240  23.928  -5.939  1.00 19.44           N  
ANISOU  104  ND1 HIS A  13     3137   2642   1608   -635    476    253       N  
ATOM    105  CD2 HIS A  13      39.063  25.820  -5.231  1.00 28.31           C  
ANISOU  105  CD2 HIS A  13     5605   3077   2073  -1974   1180    196       C  
ATOM    106  CE1 HIS A  13      38.985  24.415  -6.932  1.00 24.87           C  
ANISOU  106  CE1 HIS A  13     3889   3076   2485  -1253   1386   -123       C  
ATOM    107  NE2 HIS A  13      39.493  25.570  -6.515  1.00 31.23           N  
ANISOU  107  NE2 HIS A  13     5673   4093   2099  -2570   1193   -226       N  
ATOM    108  N   VAL A  14      36.727  22.966  -0.811  1.00  7.16           N  
ANISOU  108  N   VAL A  14     1032    901    787     -1     47     78       N  
ATOM    109  CA  VAL A  14      36.602  22.995   0.654  1.00  6.86           C  
ANISOU  109  CA  VAL A  14      814   1015    776     39   -112      0       C  
ATOM    110  C   VAL A  14      37.499  21.938   1.282  1.00  6.24           C  
ANISOU  110  C   VAL A  14      810    812    749    -64     -4    -29       C  
ATOM    111  O   VAL A  14      38.031  22.176   2.370  1.00  6.85           O  
ANISOU  111  O   VAL A  14      806   1024    773    -14    -86    -63       O  
ATOM    112  CB  VAL A  14      35.123  22.923   1.096  1.00  7.48           C  
ANISOU  112  CB  VAL A  14      816   1079    946    -25     10   -249       C  
ATOM    113  CG1 VAL A  14      34.508  21.538   0.944  1.00  9.33           C  
ANISOU  113  CG1 VAL A  14     1110   1271   1165   -285    208   -393       C  
ATOM    114  CG2 VAL A  14      34.980  23.371   2.576  1.00  8.67           C  
ANISOU  114  CG2 VAL A  14     1189   1190    915   -122     14   -242       C  
ATOM    115  N   TRP A  15      37.674  20.791   0.605  1.00  7.02           N  
ANISOU  115  N   TRP A  15      954    850    864    -46     62    -82       N  
ATOM    116  CA  TRP A  15      38.541  19.777   1.219  1.00  6.65           C  
ANISOU  116  CA  TRP A  15      922    732    872    -95     62    -64       C  
ATOM    117  C   TRP A  15      39.956  20.282   1.354  1.00  6.58           C  
ANISOU  117  C   TRP A  15      911    960    629    -73     86    -84       C  
ATOM    118  O   TRP A  15      40.679  19.911   2.300  1.00  7.71           O  
ANISOU  118  O   TRP A  15     1017   1129    783    -11    -31    -67       O  
ATOM    119  CB  TRP A  15      38.481  18.457   0.406  1.00  8.27           C  
ANISOU  119  CB  TRP A  15     1526    806    811    -26   -133   -156       C  
ATOM    120  CG  TRP A  15      38.831  17.331   1.318  1.00  7.30           C  
ANISOU  120  CG  TRP A  15      996    849    930     25   -245   -184       C  
ATOM    121  CD1 TRP A  15      40.002  16.623   1.425  1.00  9.29           C  
ANISOU  121  CD1 TRP A  15     1239    743   1548    106   -248   -503       C  
ATOM    122  CD2 TRP A  15      37.950  16.789   2.334  1.00  7.92           C  
ANISOU  122  CD2 TRP A  15     1229    874    907   -123   -322    -52       C  
ATOM    123  NE1 TRP A  15      39.872  15.682   2.422  1.00 11.15           N  
ANISOU  123  NE1 TRP A  15     1875    761   1602    343   -728   -344       N  
ATOM    124  CE2 TRP A  15      38.622  15.760   2.998  1.00 10.16           C  
ANISOU  124  CE2 TRP A  15     2166    760    934     12   -534   -137       C  
ATOM    125  CE3 TRP A  15      36.615  17.090   2.715  1.00  9.59           C  
ANISOU  125  CE3 TRP A  15     1294   1052   1298   -461     92   -127       C  
ATOM    126  CZ2 TRP A  15      38.018  15.041   4.033  1.00 13.47           C  
ANISOU  126  CZ2 TRP A  15     3083    752   1284   -318   -476     75       C  
ATOM    127  CZ3 TRP A  15      36.001  16.395   3.743  1.00 12.73           C  
ANISOU  127  CZ3 TRP A  15     2361    972   1505   -552    612   -226       C  
ATOM    128  CH2 TRP A  15      36.749  15.369   4.370  1.00 16.32           C  
ANISOU  128  CH2 TRP A  15     3130   1832   1239   -531    -12    242       C  
ATOM    129  N   ALA A  16      40.392  21.186   0.450  1.00  7.35           N  
ANISOU  129  N   ALA A  16      845    897   1053    -91    123     42       N  
ATOM    130  CA  ALA A  16      41.703  21.766   0.546  1.00  7.82           C  
ANISOU  130  CA  ALA A  16      943   1273    757   -263    201   -142       C  
ATOM    131  C   ALA A  16      41.881  22.511   1.866  1.00  7.47           C  
ANISOU  131  C   ALA A  16      964    853   1022    217     -9   -185       C  
ATOM    132  O   ALA A  16      43.013  22.579   2.392  1.00  8.64           O  
ANISOU  132  O   ALA A  16      989   1104   1190    119   -213   -219       O  
ATOM    133  CB  ALA A  16      41.919  22.722  -0.637  1.00  9.70           C  
ANISOU  133  CB  ALA A  16     1178   1465   1043   -335    276    134       C  
ATOM    134  N   LYS A  17      40.791  23.093   2.372  1.00  7.60           N  
ANISOU  134  N   LYS A  17     1002    953    933    160    215    -41       N  
ATOM    135  CA  LYS A  17      40.852  23.801   3.648  1.00  7.27           C  
ANISOU  135  CA  LYS A  17      861    869   1033     68    112   -140       C  
ATOM    136  C   LYS A  17      40.902  22.828   4.833  1.00  6.87           C  
ANISOU  136  C   LYS A  17      750    927    934    -30    124   -172       C  
ATOM    137  O   LYS A  17      41.616  23.027   5.804  1.00  8.25           O  
ANISOU  137  O   LYS A  17      911   1164   1059    -76    -63   -134       O  
ATOM    138  CB  LYS A  17      39.697  24.780   3.809  1.00  8.09           C  
ANISOU  138  CB  LYS A  17      966   1061   1045    244    164   -156       C  
ATOM    139  CG  LYS A  17      39.545  25.750   2.636  1.00  9.17           C  
ANISOU  139  CG  LYS A  17     1260    906   1320    145     14    -44       C  
ATOM    140  CD  LYS A  17      40.816  26.532   2.280  1.00 12.80           C  
ANISOU  140  CD  LYS A  17     1661   1121   2083   -582   -848    590       C  
ATOM    141  CE  LYS A  17      40.695  27.385   1.022  1.00 14.14           C  
ANISOU  141  CE  LYS A  17     1862   1660   1849   -309   -365    600       C  
ATOM    142  NZ  LYS A  17      42.078  27.764   0.526  1.00 19.90           N  
ANISOU  142  NZ  LYS A  17     2855   2398   2306  -1402    520   -298       N  
ATOM    143  N   VAL A  18      40.109  21.755   4.760  1.00  7.09           N  
ANISOU  143  N   VAL A  18      815    895    983    -73    248   -137       N  
ATOM    144  CA  VAL A  18      40.175  20.692   5.754  1.00  7.29           C  
ANISOU  144  CA  VAL A  18      932    979    860   -141     87    -93       C  
ATOM    145  C   VAL A  18      41.623  20.234   5.913  1.00  7.48           C  
ANISOU  145  C   VAL A  18      886   1109    848   -152     83   -123       C  
ATOM    146  O   VAL A  18      42.120  20.013   7.022  1.00  7.86           O  
ANISOU  146  O   VAL A  18      917   1038   1032   -311    -21    -18       O  
ATOM    147  CB  VAL A  18      39.292  19.485   5.358  1.00  8.18           C  
ANISOU  147  CB  VAL A  18      971   1002   1134   -224      6    -58       C  
ATOM    148  CG1 VAL A  18      39.528  18.275   6.249  1.00  9.47           C  
ANISOU  148  CG1 VAL A  18     1387   1168   1044   -503    195    117       C  
ATOM    149  CG2 VAL A  18      37.813  19.889   5.327  1.00 10.08           C  
ANISOU  149  CG2 VAL A  18      937   1780   1113   -255     90   -273       C  
ATOM    150  N   GLU A  19      42.331  20.107   4.780  1.00  7.19           N  
ANISOU  150  N   GLU A  19     1033    680   1020    -45    211    -77       N  
ATOM    151  CA  GLU A  19      43.722  19.588   4.797  1.00  7.23           C  
ANISOU  151  CA  GLU A  19     1060    854    833     46     98   -272       C  
ATOM    152  C   GLU A  19      44.722  20.566   5.376  1.00  6.68           C  
ANISOU  152  C   GLU A  19     1203    824    513     76   -197     35       C  
ATOM    153  O   GLU A  19      45.873  20.158   5.597  1.00  8.23           O  
ANISOU  153  O   GLU A  19     1122    939   1067    169    -80     92       O  
ATOM    154  CB  GLU A  19      44.103  19.165   3.388  1.00  8.09           C  
ANISOU  154  CB  GLU A  19     1231    902    940     -9     68   -436       C  
ATOM    155  CG  GLU A  19      43.341  17.900   2.944  1.00  8.33           C  
ANISOU  155  CG  GLU A  19     1304    895    967    -28     -1   -412       C  
ATOM    156  CD  GLU A  19      43.702  17.482   1.541  1.00  7.33           C  
ANISOU  156  CD  GLU A  19     1005    930    850    -42   -104   -267       C  
ATOM    157  OE1 GLU A  19      43.623  16.253   1.294  1.00 10.20           O  
ANISOU  157  OE1 GLU A  19     1858   1041    976   -166     80   -509       O  
ATOM    158  OE2 GLU A  19      44.070  18.322   0.713  1.00  9.65           O  
ANISOU  158  OE2 GLU A  19     1243   1326   1098    -40   -110    108       O  
ATOM    159  N   ALA A  20      44.343  21.805   5.681  1.00  6.88           N  
ANISOU  159  N   ALA A  20      998    775    841    -52     14    -99       N  
ATOM    160  CA  ALA A  20      45.261  22.630   6.488  1.00  7.47           C  
ANISOU  160  CA  ALA A  20     1213    787    837   -185   -121     96       C  
ATOM    161  C   ALA A  20      45.486  22.008   7.856  1.00  8.25           C  
ANISOU  161  C   ALA A  20      943   1276    915   -287    -96    287       C  
ATOM    162  O   ALA A  20      46.524  22.207   8.462  1.00  8.10           O  
ANISOU  162  O   ALA A  20     1089   1109    878   -201   -189     73       O  
ATOM    163  CB  ALA A  20      44.705  24.043   6.639  1.00  8.24           C  
ANISOU  163  CB  ALA A  20     1056    761   1313   -180    -23     22       C  
ATOM    164  N   ASP A  21      44.469  21.303   8.362  1.00  7.74           N  
ANISOU  164  N   ASP A  21     1135    875    933   -163    165    145       N  
ATOM    165  CA  ASP A  21      44.521  20.733   9.727  1.00  8.08           C  
ANISOU  165  CA  ASP A  21     1322    878    870   -409     62     48       C  
ATOM    166  C   ASP A  21      43.535  19.577   9.785  1.00  6.00           C  
ANISOU  166  C   ASP A  21      773    676    831    -70     15    124       C  
ATOM    167  O   ASP A  21      42.462  19.716  10.395  1.00  7.07           O  
ANISOU  167  O   ASP A  21      899    937    849      9    105    -37       O  
ATOM    168  CB  ASP A  21      44.244  21.821  10.745  1.00 10.23           C  
ANISOU  168  CB  ASP A  21     2002    892    995   -331     99    -37       C  
ATOM    169  CG  ASP A  21      44.138  21.324  12.169  1.00 10.32           C  
ANISOU  169  CG  ASP A  21     2015    974    931   -300    107    -55       C  
ATOM    170  OD1 ASP A  21      43.501  22.017  12.975  1.00 15.80           O  
ANISOU  170  OD1 ASP A  21     2987   1675   1340    167    456   -251       O  
ATOM    171  OD2 ASP A  21      44.637  20.229  12.480  1.00  9.22           O  
ANISOU  171  OD2 ASP A  21     1545   1071    885   -490    -45     19       O  
ATOM    172  N   VAL A  22      43.899  18.445   9.231  1.00  5.82           N  
ANISOU  172  N   VAL A  22      726    736    750    -26    -29     49       N  
ATOM    173  CA  VAL A  22      42.916  17.376   9.166  1.00  6.58           C  
ANISOU  173  CA  VAL A  22      996    716    789   -159    113     22       C  
ATOM    174  C   VAL A  22      42.619  16.901  10.572  1.00  6.66           C  
ANISOU  174  C   VAL A  22      650    992    889    -50    119     83       C  
ATOM    175  O   VAL A  22      41.487  16.545  10.876  1.00  6.64           O  
ANISOU  175  O   VAL A  22      797    916    811   -112    171    -58       O  
ATOM    176  CB  VAL A  22      43.371  16.258   8.198  1.00  7.50           C  
ANISOU  176  CB  VAL A  22      849    977   1023   -111    115   -261       C  
ATOM    177  CG1 VAL A  22      44.569  15.470   8.654  1.00  9.50           C  
ANISOU  177  CG1 VAL A  22     1381   1248    982    290    244     81       C  
ATOM    178  CG2 VAL A  22      42.187  15.303   8.010  1.00 10.31           C  
ANISOU  178  CG2 VAL A  22     1458   1059   1402   -502    330   -311       C  
ATOM    179  N   ALA A  23      43.627  16.872  11.470  1.00  6.62           N  
ANISOU  179  N   ALA A  23      924    845    748    -51     29     81       N  
ATOM    180  CA  ALA A  23      43.377  16.397  12.833  1.00  6.91           C  
ANISOU  180  CA  ALA A  23      951    894    780     29     89      9       C  
ATOM    181  C   ALA A  23      42.325  17.218  13.540  1.00  6.84           C  
ANISOU  181  C   ALA A  23      863    932    803    -15     83    -35       C  
ATOM    182  O   ALA A  23      41.438  16.650  14.207  1.00  6.97           O  
ANISOU  182  O   ALA A  23      861    845    943     19     56     96       O  
ATOM    183  CB  ALA A  23      44.709  16.383  13.619  1.00  7.87           C  
ANISOU  183  CB  ALA A  23      849   1217    925    -38      2     81       C  
ATOM    184  N   GLY A  24      42.398  18.527  13.482  1.00  6.84           N  
ANISOU  184  N   GLY A  24     1007    862    729    -33   -109   -109       N  
ATOM    185  CA  GLY A  24      41.390  19.336  14.199  1.00  7.20           C  
ANISOU  185  CA  GLY A  24     1080    951    705    -23   -128   -250       C  
ATOM    186  C   GLY A  24      40.002  19.183  13.598  1.00  6.77           C  
ANISOU  186  C   GLY A  24     1052    878    644    -15    -31   -128       C  
ATOM    187  O   GLY A  24      38.991  19.158  14.312  1.00  7.41           O  
ANISOU  187  O   GLY A  24      995   1041    778     43     74    -95       O  
ATOM    188  N   HIS A  25      39.929  19.087  12.261  1.00  6.15           N  
ANISOU  188  N   HIS A  25      937    781    621   -129   -117    -14       N  
ATOM    189  CA  HIS A  25      38.625  18.837  11.623  1.00  6.27           C  
ANISOU  189  CA  HIS A  25      980    703    699    -54   -124    -33       C  
ATOM    190  C   HIS A  25      38.053  17.493  12.024  1.00  5.49           C  
ANISOU  190  C   HIS A  25      736    721    629     23    117    -62       C  
ATOM    191  O   HIS A  25      36.855  17.370  12.247  1.00  7.20           O  
ANISOU  191  O   HIS A  25      714   1184    836     14     72     65       O  
ATOM    192  CB  HIS A  25      38.758  18.907  10.074  1.00  6.30           C  
ANISOU  192  CB  HIS A  25      898    844    653     -3   -146    207       C  
ATOM    193  CG  HIS A  25      38.922  20.307   9.565  1.00  6.40           C  
ANISOU  193  CG  HIS A  25     1115    673    644     20    -42    -58       C  
ATOM    194  ND1 HIS A  25      40.138  20.993   9.584  1.00  6.90           N  
ANISOU  194  ND1 HIS A  25     1188    617    816     40     -7    -32       N  
ATOM    195  CD2 HIS A  25      38.023  21.175   9.005  1.00  7.37           C  
ANISOU  195  CD2 HIS A  25     1222    842    737    186    136    111       C  
ATOM    196  CE1 HIS A  25      39.946  22.198   9.059  1.00  7.17           C  
ANISOU  196  CE1 HIS A  25     1202    669    854    122    -62    173       C  
ATOM    197  NE2 HIS A  25      38.687  22.371   8.704  1.00  7.67           N  
ANISOU  197  NE2 HIS A  25     1238    784    895    102   -117     73       N  
ATOM    198  N   GLY A  26      38.891  16.450  12.104  1.00  6.47           N  
ANISOU  198  N   GLY A  26      854    700    904     72    101    -19       N  
ATOM    199  CA  GLY A  26      38.415  15.126  12.476  1.00  6.71           C  
ANISOU  199  CA  GLY A  26      895    807    846      9     -5    116       C  
ATOM    200  C   GLY A  26      37.908  15.092  13.878  1.00  6.88           C  
ANISOU  200  C   GLY A  26      676   1125    813     76   -131    197       C  
ATOM    201  O   GLY A  26      36.914  14.439  14.178  1.00  8.10           O  
ANISOU  201  O   GLY A  26      955   1022   1100   -109     25    197       O  
ATOM    202  N   GLN A  27      38.546  15.812  14.811  1.00  7.46           N  
ANISOU  202  N   GLN A  27      878   1170    785    -15   -108    145       N  
ATOM    203  CA  GLN A  27      38.068  15.898  16.185  1.00  7.63           C  
ANISOU  203  CA  GLN A  27     1017   1116    765    -66    -13    162       C  
ATOM    204  C   GLN A  27      36.709  16.545  16.194  1.00  7.96           C  
ANISOU  204  C   GLN A  27     1091   1074    857    -63     67    181       C  
ATOM    205  O   GLN A  27      35.761  16.045  16.823  1.00  7.50           O  
ANISOU  205  O   GLN A  27     1008   1124    716    -88     90    104       O  
ATOM    206  CB  GLN A  27      38.971  16.756  17.087  1.00  9.30           C  
ANISOU  206  CB  GLN A  27     1324   1085   1125     -3   -242    -62       C  
ATOM    207  CG  GLN A  27      40.328  16.089  17.353  1.00 10.31           C  
ANISOU  207  CG  GLN A  27     1266   1627   1025    100   -220   -134       C  
ATOM    208  CD  GLN A  27      41.236  17.012  18.153  1.00 11.48           C  
ANISOU  208  CD  GLN A  27     1696   1493   1175    -95   -454     10       C  
ATOM    209  OE1 GLN A  27      41.513  18.108  17.653  1.00 16.54           O  
ANISOU  209  OE1 GLN A  27     2333   2012   1941   -665   -877    771       O  
ATOM    210  NE2 GLN A  27      41.669  16.539  19.320  1.00 14.53           N  
ANISOU  210  NE2 GLN A  27     2424   1816   1279   -530   -748    298       N  
ATOM    211  N   ASP A  28      36.550  17.665  15.486  1.00  7.26           N  
ANISOU  211  N   ASP A  28     1022    973    764     41    150     53       N  
ATOM    212  CA  ASP A  28      35.261  18.340  15.509  1.00  7.15           C  
ANISOU  212  CA  ASP A  28      986   1069    661     -4    -72     24       C  
ATOM    213  C   ASP A  28      34.165  17.459  14.932  1.00  7.25           C  
ANISOU  213  C   ASP A  28      988   1082    684    -78     29     53       C  
ATOM    214  O   ASP A  28      33.044  17.424  15.427  1.00  7.53           O  
ANISOU  214  O   ASP A  28     1072    964    826    -80    136    113       O  
ATOM    215  CB  ASP A  28      35.305  19.621  14.683  1.00  8.12           C  
ANISOU  215  CB  ASP A  28     1311    901    874      2    -46     36       C  
ATOM    216  CG  ASP A  28      36.072  20.781  15.311  1.00  9.90           C  
ANISOU  216  CG  ASP A  28     1625    912   1226     23   -179    -67       C  
ATOM    217  OD1 ASP A  28      36.588  20.613  16.426  1.00 12.17           O  
ANISOU  217  OD1 ASP A  28     2030   1486   1108   -323   -290    -53       O  
ATOM    218  OD2 ASP A  28      36.085  21.852  14.657  1.00 10.82           O  
ANISOU  218  OD2 ASP A  28     1709   1014   1389   -129     16     74       O  
ATOM    219  N   ILE A  29      34.452  16.745  13.835  1.00  6.92           N  
ANISOU  219  N   ILE A  29      944    956    728   -103    -57     62       N  
ATOM    220  CA  ILE A  29      33.432  15.903  13.185  1.00  6.55           C  
ANISOU  220  CA  ILE A  29      993    892    606   -142     22    156       C  
ATOM    221  C   ILE A  29      33.074  14.705  14.033  1.00  6.81           C  
ANISOU  221  C   ILE A  29      926    817    843    -42    -14    181       C  
ATOM    222  O   ILE A  29      31.870  14.439  14.181  1.00  7.29           O  
ANISOU  222  O   ILE A  29      919    973    878   -236    116    135       O  
ATOM    223  CB  ILE A  29      33.958  15.494  11.778  1.00  6.41           C  
ANISOU  223  CB  ILE A  29      928    737    770    -15     91     35       C  
ATOM    224  CG1 ILE A  29      33.912  16.754  10.906  1.00  7.44           C  
ANISOU  224  CG1 ILE A  29      995   1072    760     94    189    346       C  
ATOM    225  CG2 ILE A  29      33.166  14.334  11.209  1.00  8.80           C  
ANISOU  225  CG2 ILE A  29     1292   1164    886   -281     92   -187       C  
ATOM    226  CD1 ILE A  29      34.687  16.625   9.579  1.00  8.75           C  
ANISOU  226  CD1 ILE A  29     1256   1196    871   -127    353     69       C  
ATOM    227  N   LEU A  30      34.039  13.977  14.601  1.00  7.22           N  
ANISOU  227  N   LEU A  30     1185    694    864    -15   -171     77       N  
ATOM    228  CA  LEU A  30      33.655  12.846  15.437  1.00  7.98           C  
ANISOU  228  CA  LEU A  30     1298    812    922     82     44    242       C  
ATOM    229  C   LEU A  30      32.952  13.277  16.688  1.00  8.36           C  
ANISOU  229  C   LEU A  30     1104   1066   1008    -57    -22    130       C  
ATOM    230  O   LEU A  30      31.977  12.652  17.118  1.00  9.47           O  
ANISOU  230  O   LEU A  30     1129   1358   1110   -205     36    250       O  
ATOM    231  CB  LEU A  30      34.917  12.034  15.769  1.00  9.70           C  
ANISOU  231  CB  LEU A  30     1218   1183   1286    209     61    414       C  
ATOM    232  CG  LEU A  30      35.531  11.255  14.598  1.00 10.23           C  
ANISOU  232  CG  LEU A  30     1044   1333   1509     90    232    266       C  
ATOM    233  CD1 LEU A  30      36.854  10.631  15.031  1.00 12.97           C  
ANISOU  233  CD1 LEU A  30     1317   2058   1552    515    257    695       C  
ATOM    234  CD2 LEU A  30      34.567  10.197  14.051  1.00 14.39           C  
ANISOU  234  CD2 LEU A  30     1113   1530   2824     33    620   -541       C  
ATOM    235  N   ILE A  31      33.370  14.362  17.329  1.00  8.06           N  
ANISOU  235  N   ILE A  31     1098   1070    894    -30     16    133       N  
ATOM    236  CA  ILE A  31      32.660  14.849  18.524  1.00  8.86           C  
ANISOU  236  CA  ILE A  31     1007   1589    771   -201     20     13       C  
ATOM    237  C   ILE A  31      31.245  15.270  18.165  1.00  8.19           C  
ANISOU  237  C   ILE A  31     1073   1244    796   -184      1   -156       C  
ATOM    238  O   ILE A  31      30.288  14.979  18.900  1.00  9.03           O  
ANISOU  238  O   ILE A  31     1048   1177   1207   -173     80    -16       O  
ATOM    239  CB  ILE A  31      33.476  15.991  19.187  1.00  9.97           C  
ANISOU  239  CB  ILE A  31     1088   1832    869   -326    -13   -141       C  
ATOM    240  CG1 ILE A  31      34.778  15.371  19.740  1.00 11.36           C  
ANISOU  240  CG1 ILE A  31     1232   1902   1185   -523   -207    479       C  
ATOM    241  CG2 ILE A  31      32.602  16.727  20.204  1.00 11.79           C  
ANISOU  241  CG2 ILE A  31     1794   1920    766   -426    168   -264       C  
ATOM    242  CD1 ILE A  31      35.765  16.421  20.224  1.00 15.23           C  
ANISOU  242  CD1 ILE A  31     1252   2827   1706   -921   -157    139       C  
ATOM    243  N   ARG A  32      31.066  15.945  17.018  1.00  8.09           N  
ANISOU  243  N   ARG A  32     1217   1014    844     61    -60   -177       N  
ATOM    244  CA  ARG A  32      29.716  16.320  16.600  1.00  9.00           C  
ANISOU  244  CA  ARG A  32     1114   1077   1229    -16     62      5       C  
ATOM    245  C   ARG A  32      28.868  15.065  16.400  1.00  9.04           C  
ANISOU  245  C   ARG A  32      966   1185   1285     17    197   -205       C  
ATOM    246  O   ARG A  32      27.693  15.060  16.825  1.00 10.87           O  
ANISOU  246  O   ARG A  32      922   1838   1372     -5    280   -232       O  
ATOM    247  CB  ARG A  32      29.754  17.161  15.320  1.00  9.74           C  
ANISOU  247  CB  ARG A  32     1303   1277   1122    144    -52     69       C  
ATOM    248  CG  ARG A  32      28.381  17.499  14.751  1.00 13.68           C  
ANISOU  248  CG  ARG A  32     1546   2106   1546    524   -300   -221       C  
ATOM    249  CD  ARG A  32      27.708  18.544  15.672  1.00 15.54           C  
ANISOU  249  CD  ARG A  32     1892   2175   1839    925      3     15       C  
ATOM    250  NE  ARG A  32      26.385  18.725  15.027  1.00 19.26           N  
ANISOU  250  NE  ARG A  32     1249   2924   3146    417    260    561       N  
ATOM    251  CZ  ARG A  32      25.530  19.624  15.444  1.00 20.32           C  
ANISOU  251  CZ  ARG A  32     1771   2787   3164    882    -69    880       C  
ATOM    252  NH1 ARG A  32      25.848  20.413  16.453  1.00 26.27           N  
ANISOU  252  NH1 ARG A  32     2581   3087   4315   1049   -154     -3       N  
ATOM    253  NH2 ARG A  32      24.377  19.676  14.785  1.00 25.85           N  
ANISOU  253  NH2 ARG A  32     1778   3238   4805    695   -539   1213       N  
ATOM    254  N   LEU A  33      29.412  14.066  15.738  1.00  8.30           N  
ANISOU  254  N   LEU A  33     1088   1003   1061     -1    111   -112       N  
ATOM    255  CA  LEU A  33      28.660  12.797  15.544  1.00  8.24           C  
ANISOU  255  CA  LEU A  33     1143   1159    829    -86    181   -127       C  
ATOM    256  C   LEU A  33      28.226  12.240  16.875  1.00  9.49           C  
ANISOU  256  C   LEU A  33     1023   1640    942   -226    196     30       C  
ATOM    257  O   LEU A  33      27.063  11.825  17.064  1.00 10.14           O  
ANISOU  257  O   LEU A  33     1104   1540   1210   -214    400   -233       O  
ATOM    258  CB  LEU A  33      29.577  11.842  14.783  1.00 10.13           C  
ANISOU  258  CB  LEU A  33     1442   1141   1264   -280    408   -470       C  
ATOM    259  CG  LEU A  33      29.011  10.407  14.643  1.00  9.40           C  
ANISOU  259  CG  LEU A  33     1329    993   1249   -163    -95   -116       C  
ATOM    260  CD1 LEU A  33      27.766  10.443  13.785  1.00 10.84           C  
ANISOU  260  CD1 LEU A  33     1588   1684    846   -427   -106     97       C  
ATOM    261  CD2 LEU A  33      30.107   9.501  14.092  1.00 10.56           C  
ANISOU  261  CD2 LEU A  33     1811   1194   1009    -64    146   -318       C  
ATOM    262  N   PHE A  34      29.179  12.125  17.816  1.00  8.67           N  
ANISOU  262  N   PHE A  34     1352   1147    796   -184     95      2       N  
ATOM    263  CA  PHE A  34      28.872  11.486  19.107  1.00 10.16           C  
ANISOU  263  CA  PHE A  34     1693   1517    649   -222    257   -173       C  
ATOM    264  C   PHE A  34      27.903  12.325  19.933  1.00 12.78           C  
ANISOU  264  C   PHE A  34     1595   1683   1577   -415    795   -276       C  
ATOM    265  O   PHE A  34      27.087  11.738  20.670  1.00 15.13           O  
ANISOU  265  O   PHE A  34     2142   1992   1614   -671   1019   -307       O  
ATOM    266  CB  PHE A  34      30.139  11.218  19.901  1.00  9.94           C  
ANISOU  266  CB  PHE A  34     1690   1387    698   -262    187     25       C  
ATOM    267  CG  PHE A  34      31.154  10.315  19.224  1.00 10.11           C  
ANISOU  267  CG  PHE A  34     1711   1356    776   -297    306     73       C  
ATOM    268  CD1 PHE A  34      30.757   9.335  18.317  1.00 11.78           C  
ANISOU  268  CD1 PHE A  34     2360   1320    796   -113    138     29       C  
ATOM    269  CD2 PHE A  34      32.520  10.501  19.492  1.00 11.16           C  
ANISOU  269  CD2 PHE A  34     1630   1290   1322   -355    495    463       C  
ATOM    270  CE1 PHE A  34      31.713   8.518  17.707  1.00 12.02           C  
ANISOU  270  CE1 PHE A  34     2347   1422    797     56    -34     53       C  
ATOM    271  CE2 PHE A  34      33.425   9.646  18.912  1.00 11.66           C  
ANISOU  271  CE2 PHE A  34     1745   1517   1169   -270    356    277       C  
ATOM    272  CZ  PHE A  34      33.048   8.677  18.022  1.00 12.23           C  
ANISOU  272  CZ  PHE A  34     2260   1517    869   -215    226    370       C  
ATOM    273  N   LYS A  35      27.967  13.641  19.858  1.00 11.48           N  
ANISOU  273  N   LYS A  35     1516   1654   1192   -149    575   -297       N  
ATOM    274  CA  LYS A  35      27.044  14.452  20.647  1.00 14.05           C  
ANISOU  274  CA  LYS A  35     1727   1944   1667   -406    626   -887       C  
ATOM    275  C   LYS A  35      25.647  14.466  20.026  1.00 13.09           C  
ANISOU  275  C   LYS A  35     1467   1677   1829   -343    848   -651       C  
ATOM    276  O   LYS A  35      24.623  14.385  20.709  1.00 16.56           O  
ANISOU  276  O   LYS A  35     1768   2160   2363   -238   1216   -746       O  
ATOM    277  CB  LYS A  35      27.642  15.859  20.728  1.00 17.27           C  
ANISOU  277  CB  LYS A  35     2153   1988   2423   -609    435  -1073       C  
ATOM    278  CG  LYS A  35      28.789  16.051  21.721  1.00 20.50           C  
ANISOU  278  CG  LYS A  35     2613   3002   2176  -1209    356   -939       C  
ATOM    279  CD  LYS A  35      29.554  17.307  21.305  1.00 35.88           C  
ANISOU  279  CD  LYS A  35     4802   3520   5309  -2584  -1699    239       C  
ATOM    280  CE  LYS A  35      29.299  18.630  21.968  1.00 45.61           C  
ANISOU  280  CE  LYS A  35     6695   2971   7663  -2206   -651    476       C  
ATOM    281  NZ  LYS A  35      29.708  19.813  21.128  1.00 39.73           N  
ANISOU  281  NZ  LYS A  35     2873   3481   8743    -22   -942   2048       N  
ATOM    282  N   SER A  36      25.546  14.555  18.713  1.00 12.27           N  
ANISOU  282  N   SER A  36     1467   1264   1930   -181    551   -364       N  
ATOM    283  CA  SER A  36      24.247  14.607  18.054  1.00 13.99           C  
ANISOU  283  CA  SER A  36     1433   1261   2623     42    349   -387       C  
ATOM    284  C   SER A  36      23.590  13.235  18.042  1.00 13.40           C  
ANISOU  284  C   SER A  36     1118   1481   2491    -57    915   -812       C  
ATOM    285  O   SER A  36      22.354  13.166  18.033  1.00 15.11           O  
ANISOU  285  O   SER A  36     1148   1973   2619   -100    731   -599       O  
ATOM    286  CB  SER A  36      24.369  15.102  16.606  1.00 15.81           C  
ANISOU  286  CB  SER A  36     1732   1577   2699     98    -27   -131       C  
ATOM    287  OG  SER A  36      24.746  16.465  16.531  1.00 19.74           O  
ANISOU  287  OG  SER A  36     2712   1599   3189    -11    406     21       O  
ATOM    288  N   HIS A  37      24.349  12.148  17.977  1.00 12.35           N  
ANISOU  288  N   HIS A  37     1418   1267   2008    -98    751   -452       N  
ATOM    289  CA  HIS A  37      23.779  10.811  17.860  1.00 11.90           C  
ANISOU  289  CA  HIS A  37     1573   1355   1593   -337    826   -261       C  
ATOM    290  C   HIS A  37      24.589   9.883  18.757  1.00 11.98           C  
ANISOU  290  C   HIS A  37     1600   1471   1480   -405    717   -263       C  
ATOM    291  O   HIS A  37      25.416   9.112  18.280  1.00 11.51           O  
ANISOU  291  O   HIS A  37     1458   1566   1350   -359    532   -330       O  
ATOM    292  CB  HIS A  37      23.763  10.343  16.381  1.00 12.74           C  
ANISOU  292  CB  HIS A  37     1240   1943   1657   -265    411   -445       C  
ATOM    293  CG  HIS A  37      23.033  11.279  15.456  1.00 14.22           C  
ANISOU  293  CG  HIS A  37     1688   1918   1797   -109    364   -404       C  
ATOM    294  ND1 HIS A  37      21.665  11.312  15.299  1.00 15.50           N  
ANISOU  294  ND1 HIS A  37     1739   2111   2040    -60     50   -274       N  
ATOM    295  CD2 HIS A  37      23.523  12.240  14.621  1.00 15.43           C  
ANISOU  295  CD2 HIS A  37     2002   1582   2278      5    421   -356       C  
ATOM    296  CE1 HIS A  37      21.338  12.241  14.426  1.00 16.33           C  
ANISOU  296  CE1 HIS A  37     2028   2021   2154    112    271   -225       C  
ATOM    297  NE2 HIS A  37      22.437  12.850  13.985  1.00 16.35           N  
ANISOU  297  NE2 HIS A  37     2162   1884   2165    -25    165   -353       N  
ATOM    298  N   PRO A  38      24.357   9.973  20.049  1.00 12.87           N  
ANISOU  298  N   PRO A  38     1606   1778   1507   -218    457   -613       N  
ATOM    299  CA  PRO A  38      25.181   9.230  21.006  1.00 13.10           C  
ANISOU  299  CA  PRO A  38     1582   1984   1411   -276    533   -514       C  
ATOM    300  C   PRO A  38      25.230   7.736  20.777  1.00 12.83           C  
ANISOU  300  C   PRO A  38     1731   1914   1229   -316    503   -329       C  
ATOM    301  O   PRO A  38      26.240   7.129  21.117  1.00 13.41           O  
ANISOU  301  O   PRO A  38     1999   2019   1078   -162    465   -237       O  
ATOM    302  CB  PRO A  38      24.519   9.497  22.367  1.00 15.55           C  
ANISOU  302  CB  PRO A  38     1957   2490   1463     42    654   -527       C  
ATOM    303  CG  PRO A  38      23.932  10.867  22.146  1.00 17.30           C  
ANISOU  303  CG  PRO A  38     2124   2614   1838    274    294   -973       C  
ATOM    304  CD  PRO A  38      23.396  10.844  20.738  1.00 14.14           C  
ANISOU  304  CD  PRO A  38     1969   1834   1571    -94    721   -514       C  
ATOM    305  N   GLU A  39      24.190   7.150  20.205  1.00 12.96           N  
ANISOU  305  N   GLU A  39     1671   1837   1415   -633    750   -145       N  
ATOM    306  CA  GLU A  39      24.210   5.705  19.915  1.00 14.20           C  
ANISOU  306  CA  GLU A  39     1737   1631   2027   -619    643    140       C  
ATOM    307  C   GLU A  39      25.374   5.342  19.023  1.00 13.67           C  
ANISOU  307  C   GLU A  39     2043   1275   1878   -568    650    -43       C  
ATOM    308  O   GLU A  39      25.863   4.200  19.057  1.00 14.43           O  
ANISOU  308  O   GLU A  39     2222   1393   1867   -343    386    132       O  
ATOM    309  CB  GLU A  39      22.880   5.294  19.273  1.00 15.69           C  
ANISOU  309  CB  GLU A  39     2029   1642   2289   -776    331    209       C  
ATOM    310  CG  GLU A  39      22.593   5.863  17.911  1.00 15.83           C  
ANISOU  310  CG  GLU A  39     2115   1912   1988   -450    537    -24       C  
ATOM    311  CD  GLU A  39      21.789   7.164  17.909  1.00 16.71           C  
ANISOU  311  CD  GLU A  39     1901   2313   2135   -171    294     52       C  
ATOM    312  OE1 GLU A  39      20.967   7.302  16.952  1.00 21.84           O  
ANISOU  312  OE1 GLU A  39     2379   4069   1851    193    318    414       O  
ATOM    313  OE2 GLU A  39      21.980   8.041  18.785  1.00 19.25           O  
ANISOU  313  OE2 GLU A  39     2087   2173   3055   -207    239   -350       O  
ATOM    314  N   THR A  40      25.863   6.270  18.192  1.00 10.94           N  
ANISOU  314  N   THR A  40     1490   1501   1167   -234    208    120       N  
ATOM    315  CA  THR A  40      26.993   5.931  17.305  1.00 10.74           C  
ANISOU  315  CA  THR A  40     1391   1455   1233   -320    126     48       C  
ATOM    316  C   THR A  40      28.272   5.669  18.077  1.00 10.13           C  
ANISOU  316  C   THR A  40     1668   1332    850     52    126   -110       C  
ATOM    317  O   THR A  40      29.119   4.870  17.643  1.00 10.55           O  
ANISOU  317  O   THR A  40     1650   1261   1097    -36    254   -102       O  
ATOM    318  CB  THR A  40      27.269   7.041  16.262  1.00  8.82           C  
ANISOU  318  CB  THR A  40     1208    984   1160   -154    119    -64       C  
ATOM    319  OG1 THR A  40      27.649   8.250  16.917  1.00 10.13           O  
ANISOU  319  OG1 THR A  40     1439   1212   1199   -193    365   -223       O  
ATOM    320  CG2 THR A  40      26.042   7.267  15.401  1.00 11.22           C  
ANISOU  320  CG2 THR A  40     1363   1537   1364    160     29   -210       C  
ATOM    321  N   LEU A  41      28.471   6.318  19.215  1.00  9.55           N  
ANISOU  321  N   LEU A  41     1545   1142    940   -307    236   -143       N  
ATOM    322  CA  LEU A  41      29.699   6.105  20.011  1.00 10.80           C  
ANISOU  322  CA  LEU A  41     1829   1135   1137    -84      9   -225       C  
ATOM    323  C   LEU A  41      29.789   4.662  20.489  1.00 10.42           C  
ANISOU  323  C   LEU A  41     1926   1276    756     16    457   -113       C  
ATOM    324  O   LEU A  41      30.869   4.092  20.630  1.00 11.50           O  
ANISOU  324  O   LEU A  41     2102   1176   1092    128    367   -129       O  
ATOM    325  CB  LEU A  41      29.652   7.050  21.210  1.00 11.31           C  
ANISOU  325  CB  LEU A  41     1813   1357   1126   -214     17   -302       C  
ATOM    326  CG  LEU A  41      30.877   6.981  22.128  1.00 10.95           C  
ANISOU  326  CG  LEU A  41     1724   1585    851    -36    208   -230       C  
ATOM    327  CD1 LEU A  41      32.219   7.184  21.430  1.00 12.18           C  
ANISOU  327  CD1 LEU A  41     1786   1729   1112   -402    142    479       C  
ATOM    328  CD2 LEU A  41      30.692   7.974  23.275  1.00 14.45           C  
ANISOU  328  CD2 LEU A  41     2628   1608   1255   -226    -53   -592       C  
ATOM    329  N   GLU A  42      28.637   4.024  20.723  1.00 11.81           N  
ANISOU  329  N   GLU A  42     2167   1620    701   -276    440     12       N  
ATOM    330  CA  GLU A  42      28.590   2.654  21.208  1.00 12.47           C  
ANISOU  330  CA  GLU A  42     2289   1691    757   -268    625     81       C  
ATOM    331  C   GLU A  42      29.167   1.674  20.198  1.00 11.86           C  
ANISOU  331  C   GLU A  42     1974   1508   1026   -269    551    104       C  
ATOM    332  O   GLU A  42      29.510   0.556  20.602  1.00 16.02           O  
ANISOU  332  O   GLU A  42     3260   1284   1542   -311    669    290       O  
ATOM    333  CB AGLU A  42      27.136   2.299  21.581  0.82 14.58           C  
ANISOU  333  CB AGLU A  42     2277   1469   1794    102    975    328       C  
ATOM    334  CB BGLU A  42      27.151   2.207  21.505  0.18 13.46           C  
ANISOU  334  CB BGLU A  42     2146   1547   1420    147    770    575       C  
ATOM    335  CG AGLU A  42      26.618   3.173  22.733  0.82 19.26           C  
ANISOU  335  CG AGLU A  42     3271   2242   1807    -74   1682    165       C  
ATOM    336  CG BGLU A  42      27.108   0.810  22.125  0.18 15.85           C  
ANISOU  336  CG BGLU A  42     2571   2098   1353    -82    513   1190       C  
ATOM    337  CD AGLU A  42      27.581   3.323  23.893  0.82 23.40           C  
ANISOU  337  CD AGLU A  42     4583   2339   1969    843    999   -249       C  
ATOM    338  CD BGLU A  42      26.816   0.900  23.615  0.18 22.20           C  
ANISOU  338  CD BGLU A  42     4428   2216   1793   -537   1735    771       C  
ATOM    339  OE1AGLU A  42      28.019   2.244  24.386  0.82 24.34           O  
ANISOU  339  OE1AGLU A  42     4253   2471   2523    523   1332    377       O  
ATOM    340  OE1BGLU A  42      26.185   1.901  24.021  0.18 23.33           O  
ANISOU  340  OE1BGLU A  42     1721   3885   3259   -293   1771    144       O  
ATOM    341  OE2AGLU A  42      27.916   4.457  24.356  0.82 27.31           O  
ANISOU  341  OE2AGLU A  42     5413   2451   2514   1013     46   -416       O  
ATOM    342  OE2BGLU A  42      27.213  -0.013  24.369  0.18 28.16           O  
ANISOU  342  OE2BGLU A  42     7949   1864    885   -717   1965    802       O  
ATOM    343  N   LYS A  43      29.325   2.003  18.923  1.00 11.09           N  
ANISOU  343  N   LYS A  43     2010   1455    747   -425    275   -218       N  
ATOM    344  CA  LYS A  43      29.943   1.138  17.955  1.00 10.59           C  
ANISOU  344  CA  LYS A  43     2130   1003    889   -224    182    -35       C  
ATOM    345  C   LYS A  43      31.465   1.108  18.101  1.00 10.35           C  
ANISOU  345  C   LYS A  43     2153   1002    778    -58     56   -159       C  
ATOM    346  O   LYS A  43      32.105   0.270  17.493  1.00 11.78           O  
ANISOU  346  O   LYS A  43     2446    920   1110   -122    406   -192       O  
ATOM    347  CB  LYS A  43      29.589   1.587  16.521  1.00 11.29           C  
ANISOU  347  CB  LYS A  43     1800   1766    723   -420     75   -230       C  
ATOM    348  CG  LYS A  43      28.125   1.315  16.147  1.00 12.27           C  
ANISOU  348  CG  LYS A  43     1855   1345   1461   -510     10   -229       C  
ATOM    349  CD  LYS A  43      27.906  -0.185  15.928  1.00 12.69           C  
ANISOU  349  CD  LYS A  43     1738   1250   1833   -351    210    -63       C  
ATOM    350  CE  LYS A  43      26.465  -0.500  15.585  1.00 15.08           C  
ANISOU  350  CE  LYS A  43     1701   1691   2340   -449    308   -919       C  
ATOM    351  NZ  LYS A  43      26.328  -1.952  15.233  1.00 16.21           N  
ANISOU  351  NZ  LYS A  43     2710   1668   1782   -903    561   -546       N  
ATOM    352  N   PHE A  44      32.072   2.004  18.872  1.00 10.08           N  
ANISOU  352  N   PHE A  44     1902    963    963    -60    164   -178       N  
ATOM    353  CA  PHE A  44      33.513   2.127  18.980  1.00 10.16           C  
ANISOU  353  CA  PHE A  44     1810   1025   1025     45    236     42       C  
ATOM    354  C   PHE A  44      33.934   1.539  20.315  1.00 10.62           C  
ANISOU  354  C   PHE A  44     2049   1081    904     22    263     10       C  
ATOM    355  O   PHE A  44      33.975   2.224  21.342  1.00 12.39           O  
ANISOU  355  O   PHE A  44     2436   1310    961   -193    325   -121       O  
ATOM    356  CB  PHE A  44      33.971   3.585  18.925  1.00 10.24           C  
ANISOU  356  CB  PHE A  44     2024   1097    770   -140    427     10       C  
ATOM    357  CG  PHE A  44      33.761   4.254  17.587  1.00  9.49           C  
ANISOU  357  CG  PHE A  44     1845    978    784   -113    247   -150       C  
ATOM    358  CD1 PHE A  44      34.780   4.300  16.652  1.00 10.98           C  
ANISOU  358  CD1 PHE A  44     2264   1287    621   -403    429   -119       C  
ATOM    359  CD2 PHE A  44      32.540   4.812  17.262  1.00 11.84           C  
ANISOU  359  CD2 PHE A  44     2040   1028   1430    -70   -135   -136       C  
ATOM    360  CE1 PHE A  44      34.589   4.895  15.398  1.00  9.73           C  
ANISOU  360  CE1 PHE A  44     1665   1126    905   -135    199     29       C  
ATOM    361  CE2 PHE A  44      32.356   5.419  16.032  1.00 10.50           C  
ANISOU  361  CE2 PHE A  44     1673   1246   1070    -87     80   -319       C  
ATOM    362  CZ  PHE A  44      33.380   5.456  15.099  1.00 11.16           C  
ANISOU  362  CZ  PHE A  44     1614   1169   1457      8    224   -569       C  
ATOM    363  N   ASP A  45      34.310   0.263  20.292  1.00 13.77           N  
ANISOU  363  N   ASP A  45     3117    870   1245   -185   -221    177       N  
ATOM    364  CA  ASP A  45      34.750  -0.344  21.550  1.00 15.73           C  
ANISOU  364  CA  ASP A  45     3309   1255   1413   -262   -395    396       C  
ATOM    365  C   ASP A  45      35.942   0.399  22.137  1.00 15.47           C  
ANISOU  365  C   ASP A  45     2918   1782   1179   -123   -200    304       C  
ATOM    366  O   ASP A  45      36.086   0.451  23.373  1.00 16.15           O  
ANISOU  366  O   ASP A  45     3593   1376   1168    261   -429    175       O  
ATOM    367  CB  ASP A  45      35.068  -1.827  21.344  1.00 23.23           C  
ANISOU  367  CB  ASP A  45     5362   1131   2335    -24   -806    700       C  
ATOM    368  CG  ASP A  45      33.827  -2.666  21.088  1.00 31.95           C  
ANISOU  368  CG  ASP A  45     6197   1508   4434  -1049    494   -301       C  
ATOM    369  OD1 ASP A  45      32.721  -2.214  21.479  1.00 36.16           O  
ANISOU  369  OD1 ASP A  45     6143   2903   4692  -1753   1530   -660       O  
ATOM    370  OD2 ASP A  45      33.974  -3.777  20.524  1.00 35.96           O  
ANISOU  370  OD2 ASP A  45     7630   1919   4114   -530   -737   -658       O  
ATOM    371  N   ARG A  46      36.792   1.034  21.345  1.00 13.79           N  
ANISOU  371  N   ARG A  46     2319   1331   1591    480     98    118       N  
ATOM    372  CA  ARG A  46      37.963   1.718  21.857  1.00 15.11           C  
ANISOU  372  CA  ARG A  46     2273   1596   1873    435    161    142       C  
ATOM    373  C   ARG A  46      37.656   3.072  22.488  1.00 13.31           C  
ANISOU  373  C   ARG A  46     2099   1455   1502    277   -167    279       C  
ATOM    374  O   ARG A  46      38.478   3.564  23.271  1.00 15.37           O  
ANISOU  374  O   ARG A  46     2055   2443   1343    272   -116    -45       O  
ATOM    375  CB  ARG A  46      38.911   1.931  20.663  1.00 20.91           C  
ANISOU  375  CB  ARG A  46     2813   2869   2263   -118    693   -296       C  
ATOM    376  CG  ARG A  46      40.361   2.001  21.045  1.00 25.76           C  
ANISOU  376  CG  ARG A  46     2732   4972   2083    111    759    437       C  
ATOM    377  CD  ARG A  46      41.252   1.290  20.013  1.00 22.34           C  
ANISOU  377  CD  ARG A  46     2731   4178   1580    605     38    577       C  
ATOM    378  NE  ARG A  46      41.186   1.966  18.724  1.00 17.10           N  
ANISOU  378  NE  ARG A  46     2292   2545   1660    563     73    194       N  
ATOM    379  CZ  ARG A  46      41.928   2.948  18.275  1.00 24.64           C  
ANISOU  379  CZ  ARG A  46     3988   3507   1868   -901    138    -90       C  
ATOM    380  NH1 ARG A  46      42.872   3.394  19.100  1.00 24.77           N  
ANISOU  380  NH1 ARG A  46     4222   2897   2291   -587   -239   -120       N  
ATOM    381  NH2 ARG A  46      41.678   3.420  17.045  1.00 21.02           N  
ANISOU  381  NH2 ARG A  46     3335   2484   2166   -602    173     33       N  
ATOM    382  N   PHE A  47      36.513   3.657  22.119  1.00 10.35           N  
ANISOU  382  N   PHE A  47     1645   1261   1026      3    273    165       N  
ATOM    383  CA  PHE A  47      36.212   5.046  22.465  1.00 10.19           C  
ANISOU  383  CA  PHE A  47     1616   1242   1014     16    -13    165       C  
ATOM    384  C   PHE A  47      34.963   5.210  23.316  1.00 10.63           C  
ANISOU  384  C   PHE A  47     1757   1187   1097     31    139     19       C  
ATOM    385  O   PHE A  47      34.723   6.306  23.830  1.00 11.83           O  
ANISOU  385  O   PHE A  47     2493   1218    785    114     90     48       O  
ATOM    386  CB  PHE A  47      36.056   5.912  21.211  1.00 11.24           C  
ANISOU  386  CB  PHE A  47     1725   1551    993   -172   -181    322       C  
ATOM    387  CG  PHE A  47      37.361   5.936  20.406  1.00 13.14           C  
ANISOU  387  CG  PHE A  47     2114   1652   1226   -603    146    170       C  
ATOM    388  CD1 PHE A  47      38.561   6.260  21.018  1.00 13.14           C  
ANISOU  388  CD1 PHE A  47     1833   1528   1631   -403    111    666       C  
ATOM    389  CD2 PHE A  47      37.358   5.625  19.054  1.00 15.54           C  
ANISOU  389  CD2 PHE A  47     2776   1781   1346   -863    560    -32       C  
ATOM    390  CE1 PHE A  47      39.761   6.304  20.315  1.00 15.60           C  
ANISOU  390  CE1 PHE A  47     2079   2021   1825   -485    404    362       C  
ATOM    391  CE2 PHE A  47      38.542   5.629  18.340  1.00 16.82           C  
ANISOU  391  CE2 PHE A  47     2818   1894   1680   -975    726    -72       C  
ATOM    392  CZ  PHE A  47      39.742   5.946  18.971  1.00 17.45           C  
ANISOU  392  CZ  PHE A  47     2649   2199   1782   -448    410    423       C  
ATOM    393  N   LYS A  48      34.175   4.158  23.481  1.00 10.22           N  
ANISOU  393  N   LYS A  48     1771   1324    787    -53    109    147       N  
ATOM    394  CA  LYS A  48      32.863   4.330  24.132  1.00 10.70           C  
ANISOU  394  CA  LYS A  48     1764   1380    922   -133     78    -72       C  
ATOM    395  C   LYS A  48      32.959   4.630  25.622  1.00 11.13           C  
ANISOU  395  C   LYS A  48     2256   1087    884    144    231    -22       C  
ATOM    396  O   LYS A  48      31.948   4.984  26.241  1.00 15.83           O  
ANISOU  396  O   LYS A  48     2712   2010   1294    494    615      0       O  
ATOM    397  CB  LYS A  48      31.980   3.131  23.890  1.00 12.98           C  
ANISOU  397  CB  LYS A  48     2091   1670   1169   -501    -35    153       C  
ATOM    398  CG  LYS A  48      32.486   1.849  24.517  1.00 14.30           C  
ANISOU  398  CG  LYS A  48     2440   1287   1707   -284    300   -149       C  
ATOM    399  CD  LYS A  48      31.458   0.764  24.138  1.00 20.66           C  
ANISOU  399  CD  LYS A  48     3758   1902   2190  -1435    799   -244       C  
ATOM    400  CE  LYS A  48      31.923  -0.612  24.568  1.00 26.18           C  
ANISOU  400  CE  LYS A  48     5693   1804   2450  -1638    531     77       C  
ATOM    401  NZ  LYS A  48      30.949  -1.618  24.055  1.00 26.72           N  
ANISOU  401  NZ  LYS A  48     4130   1691   4329  -1027    889   -348       N  
ATOM    402  N   HIS A  49      34.123   4.520  26.217  1.00 12.19           N  
ANISOU  402  N   HIS A  49     2540   1332    761     68    -13     45       N  
ATOM    403  CA  HIS A  49      34.325   4.945  27.601  1.00 13.77           C  
ANISOU  403  CA  HIS A  49     3057   1368    807     45    -15     -3       C  
ATOM    404  C   HIS A  49      34.364   6.455  27.716  1.00 14.14           C  
ANISOU  404  C   HIS A  49     3150   1377    845    285    157    -67       C  
ATOM    405  O   HIS A  49      34.268   6.955  28.854  1.00 16.46           O  
ANISOU  405  O   HIS A  49     4071   1369    816    288    -92      1       O  
ATOM    406  CB  HIS A  49      35.621   4.368  28.155  1.00 17.26           C  
ANISOU  406  CB  HIS A  49     3698   1564   1298    292   -658    223       C  
ATOM    407  CG  HIS A  49      36.840   4.936  27.472  1.00 17.39           C  
ANISOU  407  CG  HIS A  49     3010   2044   1554    429   -801   -176       C  
ATOM    408  ND1 HIS A  49      37.248   4.527  26.207  1.00 18.48           N  
ANISOU  408  ND1 HIS A  49     3757   2096   1168   -179   -747     93       N  
ATOM    409  CD2 HIS A  49      37.711   5.900  27.894  1.00 18.50           C  
ANISOU  409  CD2 HIS A  49     2604   2373   2053    599   -805   -695       C  
ATOM    410  CE1 HIS A  49      38.353   5.228  25.896  1.00 17.78           C  
ANISOU  410  CE1 HIS A  49     2866   2252   1637    225   -854   -308       C  
ATOM    411  NE2 HIS A  49      38.639   6.051  26.899  1.00 18.52           N  
ANISOU  411  NE2 HIS A  49     2921   2014   2104    425   -716   -535       N  
ATOM    412  N   LEU A  50      34.533   7.208  26.633  1.00 12.92           N  
ANISOU  412  N   LEU A  50     2579   1344    986    178     52     79       N  
ATOM    413  CA  LEU A  50      34.644   8.673  26.753  1.00 11.85           C  
ANISOU  413  CA  LEU A  50     2105   1335   1063    152     99   -166       C  
ATOM    414  C   LEU A  50      33.305   9.288  27.117  1.00 12.46           C  
ANISOU  414  C   LEU A  50     1993   1700   1041    100    -35   -401       C  
ATOM    415  O   LEU A  50      32.308   9.057  26.423  1.00 14.24           O  
ANISOU  415  O   LEU A  50     2004   2007   1400     -2   -105   -427       O  
ATOM    416  CB  LEU A  50      35.166   9.274  25.433  1.00 12.44           C  
ANISOU  416  CB  LEU A  50     2294   1270   1164     -6    155    -95       C  
ATOM    417  CG  LEU A  50      36.558   8.781  25.016  1.00 11.98           C  
ANISOU  417  CG  LEU A  50     2266   1047   1239   -130    213   -250       C  
ATOM    418  CD1 LEU A  50      36.800   9.073  23.548  1.00 14.15           C  
ANISOU  418  CD1 LEU A  50     2718   1282   1377   -217    395     67       C  
ATOM    419  CD2 LEU A  50      37.663   9.394  25.874  1.00 15.89           C  
ANISOU  419  CD2 LEU A  50     2246   2110   1682   -336    349   -784       C  
ATOM    420  N   LYS A  51      33.213  10.061  28.209  1.00 11.28           N  
ANISOU  420  N   LYS A  51     2300   1132    853      5    245    -70       N  
ATOM    421  CA  LYS A  51      31.949  10.464  28.790  1.00 11.79           C  
ANISOU  421  CA  LYS A  51     2259   1450    771     47    229     55       C  
ATOM    422  C   LYS A  51      31.488  11.854  28.369  1.00 12.13           C  
ANISOU  422  C   LYS A  51     1731   1531   1346    -20   -448      8       C  
ATOM    423  O   LYS A  51      30.305  12.200  28.420  1.00 16.11           O  
ANISOU  423  O   LYS A  51     1837   2114   2169    161    -60   -105       O  
ATOM    424  CB  LYS A  51      32.075  10.498  30.339  1.00 12.47           C  
ANISOU  424  CB  LYS A  51     2486   1506    746    -79    207   -137       C  
ATOM    425  CG  LYS A  51      32.181   9.087  30.937  1.00 14.95           C  
ANISOU  425  CG  LYS A  51     3030   1757    893   -138     84    156       C  
ATOM    426  CD  LYS A  51      32.199   9.179  32.472  1.00 13.73           C  
ANISOU  426  CD  LYS A  51     2597   1742    880     75    334     43       C  
ATOM    427  CE  LYS A  51      32.416   7.829  33.165  1.00 15.51           C  
ANISOU  427  CE  LYS A  51     2678   2015   1199   -378   -521    355       C  
ATOM    428  NZ  LYS A  51      31.316   6.858  32.948  1.00 18.95           N  
ANISOU  428  NZ  LYS A  51     3193   2259   1748   -927    293    -64       N  
ATOM    429  N   THR A  52      32.468  12.708  28.036  1.00 11.44           N  
ANISOU  429  N   THR A  52     1999   1448    901    115    -46    182       N  
ATOM    430  CA  THR A  52      32.242  14.123  27.807  1.00 10.73           C  
ANISOU  430  CA  THR A  52     1811   1457    808    229    -34     98       C  
ATOM    431  C   THR A  52      33.025  14.647  26.612  1.00 11.43           C  
ANISOU  431  C   THR A  52     2278   1131    934     86    257   -117       C  
ATOM    432  O   THR A  52      33.977  14.019  26.173  1.00 11.30           O  
ANISOU  432  O   THR A  52     1892   1604    797    166    -37    -57       O  
ATOM    433  CB  THR A  52      32.652  14.978  29.059  1.00 12.00           C  
ANISOU  433  CB  THR A  52     2073   1667    817     73    107     13       C  
ATOM    434  OG1 THR A  52      34.075  14.781  29.186  1.00 11.51           O  
ANISOU  434  OG1 THR A  52     2046   1372    955   -244     -8    -15       O  
ATOM    435  CG2 THR A  52      31.954  14.528  30.325  1.00 14.20           C  
ANISOU  435  CG2 THR A  52     2336   2236    823     63    289    -11       C  
ATOM    436  N   GLU A  53      32.621  15.803  26.118  1.00 11.08           N  
ANISOU  436  N   GLU A  53     2035   1302    874     25   -185     45       N  
ATOM    437  CA  GLU A  53      33.383  16.440  25.050  1.00 10.70           C  
ANISOU  437  CA  GLU A  53     2061   1190    814    148   -199     16       C  
ATOM    438  C   GLU A  53      34.828  16.707  25.482  1.00 10.98           C  
ANISOU  438  C   GLU A  53     2109   1386    678    -16    -21   -167       C  
ATOM    439  O   GLU A  53      35.762  16.541  24.695  1.00 11.00           O  
ANISOU  439  O   GLU A  53     2169   1176    835    -33    179     55       O  
ATOM    440  CB  GLU A  53      32.662  17.722  24.614  1.00 13.25           C  
ANISOU  440  CB  GLU A  53     2737   1332    965    441   -124    206       C  
ATOM    441  CG  GLU A  53      33.461  18.532  23.585  1.00 16.96           C  
ANISOU  441  CG  GLU A  53     3528   1677   1238    545    278    461       C  
ATOM    442  CD  GLU A  53      32.614  19.578  22.882  1.00 18.73           C  
ANISOU  442  CD  GLU A  53     4392   1223   1500    838    461    418       C  
ATOM    443  OE1 GLU A  53      33.188  20.164  21.949  1.00 25.83           O  
ANISOU  443  OE1 GLU A  53     5812   2212   1790    949    967    940       O  
ATOM    444  OE2 GLU A  53      31.456  19.807  23.303  1.00 23.48           O  
ANISOU  444  OE2 GLU A  53     4474   2510   1936   1586    422    619       O  
ATOM    445  N   ALA A  54      35.032  17.107  26.743  1.00 11.73           N  
ANISOU  445  N   ALA A  54     2602   1202    654     44   -349    -85       N  
ATOM    446  CA  ALA A  54      36.389  17.332  27.190  1.00 11.73           C  
ANISOU  446  CA  ALA A  54     2461   1381    616    101   -173   -268       C  
ATOM    447  C   ALA A  54      37.243  16.093  27.097  1.00 11.38           C  
ANISOU  447  C   ALA A  54     2307   1284    734   -125   -118   -348       C  
ATOM    448  O   ALA A  54      38.390  16.174  26.623  1.00 12.51           O  
ANISOU  448  O   ALA A  54     2297   1568    889     -2      1   -138       O  
ATOM    449  CB  ALA A  54      36.349  17.862  28.640  1.00 16.04           C  
ANISOU  449  CB  ALA A  54     3383   1938    775    392   -493   -736       C  
ATOM    450  N   GLU A  55      36.677  14.958  27.511  1.00 11.39           N  
ANISOU  450  N   GLU A  55     2187   1335    805    -18   -231    -99       N  
ATOM    451  CA  GLU A  55      37.445  13.721  27.394  1.00 11.31           C  
ANISOU  451  CA  GLU A  55     2376   1285    635    -80    -92    -78       C  
ATOM    452  C   GLU A  55      37.734  13.388  25.941  1.00 10.34           C  
ANISOU  452  C   GLU A  55     1706   1563    661    -90   -138    -24       C  
ATOM    453  O   GLU A  55      38.806  12.922  25.556  1.00 10.99           O  
ANISOU  453  O   GLU A  55     1692   1748    733   -115   -223    -73       O  
ATOM    454  CB  GLU A  55      36.696  12.556  28.061  1.00 10.67           C  
ANISOU  454  CB  GLU A  55     1965   1420    670      9    -95     30       C  
ATOM    455  CG  GLU A  55      36.699  12.703  29.585  1.00 12.28           C  
ANISOU  455  CG  GLU A  55     2415   1693    558    276   -218    202       C  
ATOM    456  CD  GLU A  55      36.118  11.526  30.325  1.00 12.86           C  
ANISOU  456  CD  GLU A  55     2429   1561    895    383    -38    221       C  
ATOM    457  OE1 GLU A  55      36.224  11.559  31.573  1.00 15.34           O  
ANISOU  457  OE1 GLU A  55     2916   2066    846    157    256    355       O  
ATOM    458  OE2 GLU A  55      35.605  10.584  29.658  1.00 17.22           O  
ANISOU  458  OE2 GLU A  55     2437   2671   1437   -639   -463    325       O  
ATOM    459  N   MET A  56      36.724  13.601  25.072  1.00  9.37           N  
ANISOU  459  N   MET A  56     1841   1113    605   -133   -196     68       N  
ATOM    460  CA  MET A  56      36.922  13.311  23.639  1.00  9.96           C  
ANISOU  460  CA  MET A  56     1601   1575    610   -225    -36     57       C  
ATOM    461  C   MET A  56      38.016  14.191  23.059  1.00 10.01           C  
ANISOU  461  C   MET A  56     1596   1420    787   -206     43   -124       C  
ATOM    462  O   MET A  56      38.861  13.722  22.303  1.00 10.51           O  
ANISOU  462  O   MET A  56     1519   1621    854   -198     87     -6       O  
ATOM    463  CB  MET A  56      35.610  13.571  22.909  1.00 10.47           C  
ANISOU  463  CB  MET A  56     1671   1689    619   -300   -106    -52       C  
ATOM    464  CG  MET A  56      34.567  12.537  23.260  1.00  9.88           C  
ANISOU  464  CG  MET A  56     1555   1430    769   -123     48     27       C  
ATOM    465  SD  MET A  56      32.956  13.049  22.584  1.00 11.58           S  
ANISOU  465  SD  MET A  56     1672   1764    965    -85    -67     43       S  
ATOM    466  CE  MET A  56      31.887  11.878  23.424  1.00 17.44           C  
ANISOU  466  CE  MET A  56     1613   2906   2108   -521    -35    674       C  
ATOM    467  N   LYS A  57      38.040  15.473  23.397  1.00 11.31           N  
ANISOU  467  N   LYS A  57     1959   1473    866   -383     91   -133       N  
ATOM    468  CA  LYS A  57      39.032  16.398  22.840  1.00 12.01           C  
ANISOU  468  CA  LYS A  57     2092   1446   1026   -333    -36    103       C  
ATOM    469  C   LYS A  57      40.437  16.059  23.319  1.00 12.65           C  
ANISOU  469  C   LYS A  57     1973   1930    902   -545   -143   -178       C  
ATOM    470  O   LYS A  57      41.428  16.270  22.617  1.00 15.42           O  
ANISOU  470  O   LYS A  57     2161   2345   1353   -787    127   -233       O  
ATOM    471  CB  LYS A  57      38.682  17.844  23.254  1.00 14.86           C  
ANISOU  471  CB  LYS A  57     2661   1486   1499   -428     77   -305       C  
ATOM    472  CG  LYS A  57      37.536  18.489  22.494  1.00 18.48           C  
ANISOU  472  CG  LYS A  57     3280   1921   1819    508    176   -351       C  
ATOM    473  CD  LYS A  57      37.348  19.962  22.792  1.00 28.26           C  
ANISOU  473  CD  LYS A  57     5908   1640   3192    481   -457     88       C  
ATOM    474  CE  LYS A  57      36.193  20.570  22.018  1.00 31.66           C  
ANISOU  474  CE  LYS A  57     5415   1685   4928    788   -378    202       C  
ATOM    475  NZ  LYS A  57      35.380  21.470  22.889  1.00 36.52           N  
ANISOU  475  NZ  LYS A  57     5509   4356   4010   1185    143     76       N  
ATOM    476  N   ALA A  58      40.558  15.495  24.529  1.00 12.16           N  
ANISOU  476  N   ALA A  58     2011   1708    902   -350   -314   -348       N  
ATOM    477  CA  ALA A  58      41.829  15.182  25.158  1.00 12.99           C  
ANISOU  477  CA  ALA A  58     2091   1855    989   -301   -389   -450       C  
ATOM    478  C   ALA A  58      42.338  13.831  24.706  1.00 14.25           C  
ANISOU  478  C   ALA A  58     2256   2112   1048     -1   -524   -589       C  
ATOM    479  O   ALA A  58      43.466  13.431  25.030  1.00 16.59           O  
ANISOU  479  O   ALA A  58     2077   2377   1851    -31   -550   -798       O  
ATOM    480  CB  ALA A  58      41.624  15.212  26.680  1.00 15.60           C  
ANISOU  480  CB  ALA A  58     2684   2340    903    381   -381   -380       C  
ATOM    481  N   SER A  59      41.551  13.061  23.984  1.00 11.40           N  
ANISOU  481  N   SER A  59     1845   1797    691   -355     -9   -285       N  
ATOM    482  CA  SER A  59      41.959  11.728  23.541  1.00 12.19           C  
ANISOU  482  CA  SER A  59     1688   1870   1075   -362    136   -305       C  
ATOM    483  C   SER A  59      42.868  11.741  22.338  1.00 11.37           C  
ANISOU  483  C   SER A  59     1533   1817    972    105    -21    -11       C  
ATOM    484  O   SER A  59      42.455  12.041  21.219  1.00 11.66           O  
ANISOU  484  O   SER A  59     1836   1657    938    -73   -137    -32       O  
ATOM    485  CB  SER A  59      40.731  10.874  23.190  1.00 11.72           C  
ANISOU  485  CB  SER A  59     1715   1510   1229   -220    -78   -109       C  
ATOM    486  OG  SER A  59      41.154   9.616  22.642  1.00 11.91           O  
ANISOU  486  OG  SER A  59     2020   1602    902   -130     40   -148       O  
ATOM    487  N   GLU A  60      44.147  11.417  22.510  1.00 12.89           N  
ANISOU  487  N   GLU A  60     1427   2240   1229    -87    -72   -161       N  
ATOM    488  CA  GLU A  60      45.070  11.346  21.393  1.00 12.92           C  
ANISOU  488  CA  GLU A  60     1266   2298   1347   -423    -31   -379       C  
ATOM    489  C   GLU A  60      44.663  10.273  20.413  1.00 10.90           C  
ANISOU  489  C   GLU A  60     1363   1871    906      8   -375     92       C  
ATOM    490  O   GLU A  60      44.765  10.445  19.204  1.00 11.58           O  
ANISOU  490  O   GLU A  60     1361   2047    990    119   -117    -25       O  
ATOM    491  CB AGLU A  60      46.517  11.101  21.844  0.57 17.41           C  
ANISOU  491  CB AGLU A  60     1308   3752   1554   -208   -202   -915       C  
ATOM    492  CB BGLU A  60      46.467  11.080  21.978  0.43 18.00           C  
ANISOU  492  CB BGLU A  60     1296   3717   1827   -222   -295  -1010       C  
ATOM    493  CG AGLU A  60      47.512  11.198  20.689  0.57 17.84           C  
ANISOU  493  CG AGLU A  60     1296   3840   1643   -137    -81  -1111       C  
ATOM    494  CG BGLU A  60      46.946  12.248  22.840  0.43 20.66           C  
ANISOU  494  CG BGLU A  60     1642   4484   1722   -919     41  -1297       C  
ATOM    495  CD AGLU A  60      47.798  12.617  20.245  0.57 20.78           C  
ANISOU  495  CD AGLU A  60     1620   4165   2108     10    207   -492       C  
ATOM    496  CD BGLU A  60      46.953  13.538  22.042  0.43 28.04           C  
ANISOU  496  CD BGLU A  60     3632   4303   2718  -1898   -462  -1140       C  
ATOM    497  OE1AGLU A  60      48.010  12.830  19.025  0.57 42.09           O  
ANISOU  497  OE1AGLU A  60     6915   6554   2521    112    700    797       O  
ATOM    498  OE1BGLU A  60      47.160  13.482  20.805  0.43 21.74           O  
ANISOU  498  OE1BGLU A  60     1206   4211   2841   -244   -169   -371       O  
ATOM    499  OE2AGLU A  60      47.838  13.524  21.102  0.57 37.85           O  
ANISOU  499  OE2AGLU A  60     5589   4282   4509  -1922   1826  -1697       O  
ATOM    500  OE2BGLU A  60      46.744  14.608  22.642  0.43 40.27           O  
ANISOU  500  OE2BGLU A  60     8049   3826   3424  -4065    553  -1612       O  
ATOM    501  N   ASP A  61      44.182   9.157  20.943  1.00 12.12           N  
ANISOU  501  N   ASP A  61     1589   1653   1361     48   -419    116       N  
ATOM    502  CA  ASP A  61      43.777   8.098  20.029  1.00 12.07           C  
ANISOU  502  CA  ASP A  61     1688   1696   1204    214   -183    -54       C  
ATOM    503  C   ASP A  61      42.577   8.510  19.212  1.00  9.97           C  
ANISOU  503  C   ASP A  61     1466   1371    952   -128    -25    -14       C  
ATOM    504  O   ASP A  61      42.512   8.136  18.012  1.00  9.97           O  
ANISOU  504  O   ASP A  61     1527   1347    916   -121     -7     34       O  
ATOM    505  CB  ASP A  61      43.507   6.831  20.831  1.00 15.51           C  
ANISOU  505  CB  ASP A  61     2967   1579   1348    105   -537     35       C  
ATOM    506  CG  ASP A  61      44.768   6.180  21.353  1.00 21.07           C  
ANISOU  506  CG  ASP A  61     3390   2200   2415    -13  -1375    502       C  
ATOM    507  OD1 ASP A  61      44.549   5.322  22.227  1.00 25.19           O  
ANISOU  507  OD1 ASP A  61     4618   2482   2472    157  -1518    753       O  
ATOM    508  OD2 ASP A  61      45.899   6.524  20.945  1.00 24.08           O  
ANISOU  508  OD2 ASP A  61     3179   3464   2508    863   -684    218       O  
ATOM    509  N   LEU A  62      41.611   9.238  19.771  1.00 10.12           N  
ANISOU  509  N   LEU A  62     1388   1484    974   -104     66    202       N  
ATOM    510  CA  LEU A  62      40.452   9.666  18.951  1.00  8.63           C  
ANISOU  510  CA  LEU A  62     1293   1345    643   -261     36     22       C  
ATOM    511  C   LEU A  62      40.912  10.638  17.873  1.00  8.23           C  
ANISOU  511  C   LEU A  62     1345   1018    766   -228    -31    -79       C  
ATOM    512  O   LEU A  62      40.419  10.583  16.730  1.00  8.06           O  
ANISOU  512  O   LEU A  62     1202   1274    587   -102      7   -140       O  
ATOM    513  CB  LEU A  62      39.424  10.361  19.848  1.00  9.49           C  
ANISOU  513  CB  LEU A  62     1513   1413    678    -53     21     45       C  
ATOM    514  CG  LEU A  62      38.113  10.679  19.108  1.00  9.11           C  
ANISOU  514  CG  LEU A  62     1364   1301    796   -166     66    -54       C  
ATOM    515  CD1 LEU A  62      37.410   9.446  18.569  1.00 13.19           C  
ANISOU  515  CD1 LEU A  62     1748   2051   1214   -692    253   -541       C  
ATOM    516  CD2 LEU A  62      37.180  11.497  19.996  1.00 11.60           C  
ANISOU  516  CD2 LEU A  62     1590   1675   1143     41    176   -126       C  
ATOM    517  N   LYS A  63      41.843  11.512  18.207  1.00  8.49           N  
ANISOU  517  N   LYS A  63     1460    961    806   -284      3   -137       N  
ATOM    518  CA  LYS A  63      42.419  12.459  17.225  1.00  8.52           C  
ANISOU  518  CA  LYS A  63     1461    925    853   -253    132   -176       C  
ATOM    519  C   LYS A  63      43.053  11.711  16.076  1.00  8.21           C  
ANISOU  519  C   LYS A  63     1246    972    903      6     51     -6       C  
ATOM    520  O   LYS A  63      42.816  11.996  14.887  1.00  8.21           O  
ANISOU  520  O   LYS A  63     1173   1116    831      0    115    -21       O  
ATOM    521  CB  LYS A  63      43.410  13.381  17.913  1.00 10.42           C  
ANISOU  521  CB  LYS A  63     1406   1537   1017   -512    167   -212       C  
ATOM    522  CG  LYS A  63      44.042  14.382  16.947  1.00 13.52           C  
ANISOU  522  CG  LYS A  63     1994   1618   1523   -801    146    106       C  
ATOM    523  CD  LYS A  63      44.902  15.370  17.702  1.00 26.81           C  
ANISOU  523  CD  LYS A  63     4028   3878   2280  -2952   -507    364       C  
ATOM    524  CE  LYS A  63      46.129  14.779  18.330  1.00 37.37           C  
ANISOU  524  CE  LYS A  63     3632   6351   4215  -3271  -1401    558       C  
ATOM    525  NZ  LYS A  63      47.061  15.915  18.650  1.00 57.83           N  
ANISOU  525  NZ  LYS A  63     7526   6921   7524  -4383  -5070    744       N  
ATOM    526  N   LYS A  64      43.874  10.700  16.375  1.00  9.18           N  
ANISOU  526  N   LYS A  64     1279   1229    981    153     83      5       N  
ATOM    527  CA  LYS A  64      44.544   9.905  15.323  1.00  8.89           C  
ANISOU  527  CA  LYS A  64     1045   1308   1023    117   -101   -238       C  
ATOM    528  C   LYS A  64      43.492   9.191  14.495  1.00  8.63           C  
ANISOU  528  C   LYS A  64     1130   1356    791    -76     31     95       C  
ATOM    529  O   LYS A  64      43.629   9.099  13.253  1.00  8.79           O  
ANISOU  529  O   LYS A  64     1104   1527    707    -20     -5     17       O  
ATOM    530  CB  LYS A  64      45.494   8.903  15.976  1.00 10.56           C  
ANISOU  530  CB  LYS A  64     1166   1457   1390    199   -155    -93       C  
ATOM    531  CG  LYS A  64      46.759   9.589  16.527  1.00 14.94           C  
ANISOU  531  CG  LYS A  64     1180   2764   1733     46   -418   -279       C  
ATOM    532  CD  LYS A  64      47.666   8.548  17.181  1.00 22.91           C  
ANISOU  532  CD  LYS A  64     2266   3099   3339    839  -1579   -932       C  
ATOM    533  CE  LYS A  64      48.975   9.212  17.634  1.00 34.10           C  
ANISOU  533  CE  LYS A  64     2824   4969   5163    352  -2829   -603       C  
ATOM    534  NZ  LYS A  64      49.854   8.154  18.211  1.00 57.47           N  
ANISOU  534  NZ  LYS A  64     4293   8063   9480    636  -4676   2352       N  
ATOM    535  N   HIS A  65      42.442   8.701  15.117  1.00  8.62           N  
ANISOU  535  N   HIS A  65     1145   1260    870   -114    113   -164       N  
ATOM    536  CA  HIS A  65      41.401   7.998  14.346  1.00  7.92           C  
ANISOU  536  CA  HIS A  65     1241    991    777    -44     63     -6       C  
ATOM    537  C   HIS A  65      40.703   8.985  13.432  1.00  7.53           C  
ANISOU  537  C   HIS A  65     1244    958    659    -68    125   -105       C  
ATOM    538  O   HIS A  65      40.406   8.625  12.252  1.00  8.46           O  
ANISOU  538  O   HIS A  65     1349   1166    700   -300     23    -83       O  
ATOM    539  CB AHIS A  65      40.366   7.312  15.246  0.60  9.03           C  
ANISOU  539  CB AHIS A  65     1493    814   1125   -301    136    -30       C  
ATOM    540  CB BHIS A  65      40.486   7.318  15.369  0.40  8.33           C  
ANISOU  540  CB BHIS A  65     1301   1006    860   -176     67    -12       C  
ATOM    541  CG AHIS A  65      39.565   6.384  14.365  0.60  7.54           C  
ANISOU  541  CG AHIS A  65     1529    756    582    -46   -105    161       C  
ATOM    542  CG BHIS A  65      39.207   6.828  14.768  0.40  8.56           C  
ANISOU  542  CG BHIS A  65     1357    908    985   -158    109   -251       C  
ATOM    543  ND1AHIS A  65      40.271   5.394  13.712  0.60 10.37           N  
ANISOU  543  ND1AHIS A  65     1509   1355   1075   -171    169   -383       N  
ATOM    544  ND1BHIS A  65      39.138   5.687  14.014  0.40 10.94           N  
ANISOU  544  ND1BHIS A  65     1609   1415   1134   -316    348   -643       N  
ATOM    545  CD2AHIS A  65      38.276   6.249  13.991  0.60  8.83           C  
ANISOU  545  CD2AHIS A  65     1446   1050    860   -207    121    -42       C  
ATOM    546  CD2BHIS A  65      37.947   7.315  14.831  0.40  7.33           C  
ANISOU  546  CD2BHIS A  65     1260    720    806   -321    117    185       C  
ATOM    547  CE1AHIS A  65      39.424   4.689  12.980  0.60 10.29           C  
ANISOU  547  CE1AHIS A  65     1601   1266   1044   -323    231   -362       C  
ATOM    548  CE1BHIS A  65      37.887   5.499  13.624  0.40  9.58           C  
ANISOU  548  CE1BHIS A  65     1664   1251    727   -622    352   -175       C  
ATOM    549  NE2AHIS A  65      38.200   5.169  13.129  0.60 10.51           N  
ANISOU  549  NE2AHIS A  65     1620   1700    672   -209     77   -378       N  
ATOM    550  NE2BHIS A  65      37.152   6.480  14.102  0.40  8.62           N  
ANISOU  550  NE2BHIS A  65     1323   1112    840   -702    401     73       N  
ATOM    551  N   GLY A  66      40.413  10.203  13.869  1.00  6.97           N  
ANISOU  551  N   GLY A  66      939    956    754     -3    209     13       N  
ATOM    552  CA  GLY A  66      39.798  11.161  12.973  1.00  7.50           C  
ANISOU  552  CA  GLY A  66      870   1147    833    -98    162    250       C  
ATOM    553  C   GLY A  66      40.652  11.460  11.769  1.00  6.08           C  
ANISOU  553  C   GLY A  66      794    955    562     28    114   -203       C  
ATOM    554  O   GLY A  66      40.148  11.639  10.658  1.00  6.91           O  
ANISOU  554  O   GLY A  66     1028    944    652    -54     29    -89       O  
ATOM    555  N   VAL A  67      41.986  11.490  11.963  1.00  6.44           N  
ANISOU  555  N   VAL A  67      753    868    826   -113    175    -12       N  
ATOM    556  CA  VAL A  67      42.835  11.680  10.781  1.00  6.48           C  
ANISOU  556  CA  VAL A  67      743    995    723    -50    128   -217       C  
ATOM    557  C   VAL A  67      42.704  10.521   9.825  1.00  6.48           C  
ANISOU  557  C   VAL A  67      949    843    669    -15   -146    -54       C  
ATOM    558  O   VAL A  67      42.633  10.716   8.589  1.00  6.72           O  
ANISOU  558  O   VAL A  67      996    970    589    -29    -28    -18       O  
ATOM    559  CB  VAL A  67      44.311  11.823  11.260  1.00  7.10           C  
ANISOU  559  CB  VAL A  67      682   1125    892   -230    150   -233       C  
ATOM    560  CG1 VAL A  67      45.262  11.789  10.065  1.00  8.37           C  
ANISOU  560  CG1 VAL A  67      810   1439    932    -93    245    -96       C  
ATOM    561  CG2 VAL A  67      44.425  13.082  12.081  1.00  7.52           C  
ANISOU  561  CG2 VAL A  67     1027   1015    816   -113    -55   -101       C  
ATOM    562  N   THR A  68      42.703   9.291  10.342  1.00  6.68           N  
ANISOU  562  N   THR A  68      951    837    751   -128     54    -17       N  
ATOM    563  CA  THR A  68      42.536   8.107   9.493  1.00  7.45           C  
ANISOU  563  CA  THR A  68     1077    819    936    -35   -207    -10       C  
ATOM    564  C   THR A  68      41.237   8.184   8.709  1.00  6.24           C  
ANISOU  564  C   THR A  68      988    814    567    -20     17    -17       C  
ATOM    565  O   THR A  68      41.181   7.932   7.501  1.00  6.96           O  
ANISOU  565  O   THR A  68     1076    885    682    -23    -50    -52       O  
ATOM    566  CB  THR A  68      42.539   6.836  10.398  1.00  8.70           C  
ANISOU  566  CB  THR A  68     1429    755   1123     52   -331     44       C  
ATOM    567  OG1 THR A  68      43.866   6.797  10.936  1.00 12.14           O  
ANISOU  567  OG1 THR A  68     1706   1090   1817     41   -769    129       O  
ATOM    568  CG2 THR A  68      42.234   5.569   9.609  1.00 11.25           C  
ANISOU  568  CG2 THR A  68     1933    803   1540     51   -498   -157       C  
ATOM    569  N   VAL A  69      40.151   8.527   9.393  1.00  6.73           N  
ANISOU  569  N   VAL A  69      899    801    858   -189     55    -27       N  
ATOM    570  CA  VAL A  69      38.829   8.576   8.747  1.00  6.87           C  
ANISOU  570  CA  VAL A  69      940    866    805   -175    114     83       C  
ATOM    571  C   VAL A  69      38.764   9.639   7.676  1.00  6.25           C  
ANISOU  571  C   VAL A  69      888    827    660    -49    212    -48       C  
ATOM    572  O   VAL A  69      38.349   9.348   6.532  1.00  7.13           O  
ANISOU  572  O   VAL A  69     1142    892    675     16     -2    -40       O  
ATOM    573  CB  VAL A  69      37.751   8.825   9.837  1.00  7.77           C  
ANISOU  573  CB  VAL A  69      941   1313    699   -251    161     83       C  
ATOM    574  CG1 VAL A  69      36.413   9.129   9.193  1.00  8.98           C  
ANISOU  574  CG1 VAL A  69      916   1239   1255    -44     88   -355       C  
ATOM    575  CG2 VAL A  69      37.699   7.614  10.775  1.00  9.34           C  
ANISOU  575  CG2 VAL A  69     1354   1390    805   -319    298    120       C  
ATOM    576  N   LEU A  70      39.182  10.872   7.994  1.00  6.37           N  
ANISOU  576  N   LEU A  70      829    735    855     31     10      0       N  
ATOM    577  CA  LEU A  70      39.059  11.922   6.998  1.00  6.64           C  
ANISOU  577  CA  LEU A  70     1150    699    673    147    149   -120       C  
ATOM    578  C   LEU A  70      40.059  11.739   5.871  1.00  6.61           C  
ANISOU  578  C   LEU A  70     1018    891    604     98     52   -177       C  
ATOM    579  O   LEU A  70      39.763  12.124   4.727  1.00  7.13           O  
ANISOU  579  O   LEU A  70     1084   1060    566     38    -42   -141       O  
ATOM    580  CB  LEU A  70      39.248  13.320   7.609  1.00  7.02           C  
ANISOU  580  CB  LEU A  70     1206    747    715    -92    149   -263       C  
ATOM    581  CG  LEU A  70      38.131  13.754   8.604  1.00  7.75           C  
ANISOU  581  CG  LEU A  70     1080   1000    866     52     69   -436       C  
ATOM    582  CD1 LEU A  70      38.417  15.206   8.957  1.00  8.36           C  
ANISOU  582  CD1 LEU A  70     1139    887   1152    174    100   -336       C  
ATOM    583  CD2 LEU A  70      36.731  13.508   8.072  1.00 10.56           C  
ANISOU  583  CD2 LEU A  70     1093   1343   1577    -11   -111    -49       C  
ATOM    584  N   THR A  71      41.232  11.139   6.127  1.00  6.32           N  
ANISOU  584  N   THR A  71      835    863    703    -68    116    -95       N  
ATOM    585  CA  THR A  71      42.146  10.880   5.002  1.00  6.37           C  
ANISOU  585  CA  THR A  71      759    873    788    -85     94   -156       C  
ATOM    586  C   THR A  71      41.562   9.855   4.086  1.00  6.14           C  
ANISOU  586  C   THR A  71      563   1099    672   -185     35    -74       C  
ATOM    587  O   THR A  71      41.678   9.961   2.843  1.00  6.80           O  
ANISOU  587  O   THR A  71      894    952    736   -107    -98    -33       O  
ATOM    588  CB  THR A  71      43.515  10.466   5.569  1.00  7.63           C  
ANISOU  588  CB  THR A  71      704   1424    770   -219     23   -220       C  
ATOM    589  OG1 THR A  71      43.993  11.556   6.367  1.00  8.39           O  
ANISOU  589  OG1 THR A  71     1069   1269    848   -497   -117     65       O  
ATOM    590  CG2 THR A  71      44.522  10.208   4.441  1.00 10.71           C  
ANISOU  590  CG2 THR A  71      895   2219    954    123    247    -14       C  
ATOM    591  N   ALA A  72      40.904   8.799   4.591  1.00  6.03           N  
ANISOU  591  N   ALA A  72      687    696    908      6     84   -127       N  
ATOM    592  CA  ALA A  72      40.267   7.818   3.729  1.00  6.44           C  
ANISOU  592  CA  ALA A  72      903    736    810    -88   -138     89       C  
ATOM    593  C   ALA A  72      39.156   8.464   2.909  1.00  6.07           C  
ANISOU  593  C   ALA A  72      875    804    627     86     78     22       C  
ATOM    594  O   ALA A  72      39.009   8.222   1.723  1.00  6.97           O  
ANISOU  594  O   ALA A  72     1151    862    635     62    -64    -19       O  
ATOM    595  CB  ALA A  72      39.704   6.671   4.556  1.00  6.97           C  
ANISOU  595  CB  ALA A  72     1107    823    720   -181    -36    137       C  
ATOM    596  N   LEU A  73      38.324   9.311   3.541  1.00  6.42           N  
ANISOU  596  N   LEU A  73      782    851    807      2     62    -68       N  
ATOM    597  CA  LEU A  73      37.258   9.977   2.811  1.00  6.01           C  
ANISOU  597  CA  LEU A  73      681    699    905     -4     70    -34       C  
ATOM    598  C   LEU A  73      37.847  10.903   1.766  1.00  5.82           C  
ANISOU  598  C   LEU A  73      622    912    679    -15     47   -141       C  
ATOM    599  O   LEU A  73      37.351  10.985   0.624  1.00  7.64           O  
ANISOU  599  O   LEU A  73     1000   1196    708    -35   -156   -114       O  
ATOM    600  CB  LEU A  73      36.362  10.749   3.773  1.00  6.75           C  
ANISOU  600  CB  LEU A  73      843    857    864     86    139     64       C  
ATOM    601  CG  LEU A  73      35.217  11.507   3.081  1.00  7.89           C  
ANISOU  601  CG  LEU A  73      773   1111   1113    258    -21   -165       C  
ATOM    602  CD1 LEU A  73      34.260  10.584   2.330  1.00 11.22           C  
ANISOU  602  CD1 LEU A  73      824   1677   1763    147   -177   -406       C  
ATOM    603  CD2 LEU A  73      34.458  12.276   4.159  1.00  9.45           C  
ANISOU  603  CD2 LEU A  73     1232   1228   1129    403    419     74       C  
ATOM    604  N   GLY A  74      38.922  11.641   2.107  1.00  6.19           N  
ANISOU  604  N   GLY A  74      849    734    767   -159     27    -84       N  
ATOM    605  CA  GLY A  74      39.514  12.543   1.138  1.00  6.18           C  
ANISOU  605  CA  GLY A  74     1018    762    569    -46    118    -64       C  
ATOM    606  C   GLY A  74      40.036  11.774  -0.058  1.00  6.63           C  
ANISOU  606  C   GLY A  74      914   1023    582    269   -146   -220       C  
ATOM    607  O   GLY A  74      39.933  12.263  -1.190  1.00  7.31           O  
ANISOU  607  O   GLY A  74     1070   1172    537   -136   -124   -126       O  
ATOM    608  N   ALA A  75      40.607  10.589   0.132  1.00  6.65           N  
ANISOU  608  N   ALA A  75      820    885    822     65     81   -235       N  
ATOM    609  CA  ALA A  75      41.088   9.827  -1.010  1.00  7.21           C  
ANISOU  609  CA  ALA A  75      949   1044    745    278    -33   -266       C  
ATOM    610  C   ALA A  75      39.922   9.400  -1.884  1.00  8.11           C  
ANISOU  610  C   ALA A  75     1137   1117    829   -162    -61   -202       C  
ATOM    611  O   ALA A  75      40.031   9.410  -3.135  1.00  8.60           O  
ANISOU  611  O   ALA A  75     1129   1293    846    -38    -57   -307       O  
ATOM    612  CB  ALA A  75      41.898   8.607  -0.531  1.00  8.71           C  
ANISOU  612  CB  ALA A  75     1585    902    823    382    -44    -69       C  
ATOM    613  N   ILE A  76      38.788   9.059  -1.273  1.00  7.27           N  
ANISOU  613  N   ILE A  76     1113    738    911    -33   -107    -83       N  
ATOM    614  CA  ILE A  76      37.569   8.750  -2.066  1.00  6.89           C  
ANISOU  614  CA  ILE A  76      955    940    721    194    -23    -32       C  
ATOM    615  C   ILE A  76      37.111   9.981  -2.818  1.00  7.32           C  
ANISOU  615  C   ILE A  76     1200    738    844     87   -116   -110       C  
ATOM    616  O   ILE A  76      36.841   9.904  -4.055  1.00  7.64           O  
ANISOU  616  O   ILE A  76     1263    910    729     -7    -83     -8       O  
ATOM    617  CB  ILE A  76      36.475   8.208  -1.118  1.00  7.24           C  
ANISOU  617  CB  ILE A  76      969    994    789     58    -22   -101       C  
ATOM    618  CG1 ILE A  76      36.880   6.805  -0.669  1.00  8.91           C  
ANISOU  618  CG1 ILE A  76     1624   1000    762     62   -119     17       C  
ATOM    619  CG2 ILE A  76      35.070   8.280  -1.741  1.00  9.64           C  
ANISOU  619  CG2 ILE A  76     1037   1461   1166    -75   -152    206       C  
ATOM    620  CD1 ILE A  76      36.168   6.336   0.570  1.00 10.48           C  
ANISOU  620  CD1 ILE A  76     1792   1268    922    -37    102     23       C  
ATOM    621  N   LEU A  77      37.029  11.132  -2.191  1.00  6.80           N  
ANISOU  621  N   LEU A  77      968    774    840     56    -96    -25       N  
ATOM    622  CA  LEU A  77      36.519  12.315  -2.876  1.00  6.92           C  
ANISOU  622  CA  LEU A  77     1110    688    831    192    256     24       C  
ATOM    623  C   LEU A  77      37.430  12.679  -4.033  1.00  6.86           C  
ANISOU  623  C   LEU A  77      953   1006    645    -90     30    -53       C  
ATOM    624  O   LEU A  77      36.953  13.111  -5.075  1.00  7.82           O  
ANISOU  624  O   LEU A  77     1322    951    699     28    -40      0       O  
ATOM    625  CB  LEU A  77      36.386  13.520  -1.913  1.00  7.84           C  
ANISOU  625  CB  LEU A  77     1322    835    823     50    147   -161       C  
ATOM    626  CG  LEU A  77      35.367  13.304  -0.777  1.00  7.80           C  
ANISOU  626  CG  LEU A  77     1040   1039    883    111    145   -189       C  
ATOM    627  CD1 LEU A  77      35.479  14.487   0.196  1.00  9.32           C  
ANISOU  627  CD1 LEU A  77     1614   1110    818    401    -42   -267       C  
ATOM    628  CD2 LEU A  77      33.941  13.168  -1.314  1.00  9.69           C  
ANISOU  628  CD2 LEU A  77     1194   1295   1194     94   -233    130       C  
ATOM    629  N   LYS A  78      38.757  12.545  -3.854  1.00  7.25           N  
ANISOU  629  N   LYS A  78      929    854    971   -139     85   -132       N  
ATOM    630  CA  LYS A  78      39.672  12.916  -4.929  1.00  7.13           C  
ANISOU  630  CA  LYS A  78      940    940    830   -118     76   -164       C  
ATOM    631  C   LYS A  78      39.543  12.003  -6.154  1.00  7.88           C  
ANISOU  631  C   LYS A  78     1184   1029    782    -81    -65   -121       C  
ATOM    632  O   LYS A  78      39.967  12.380  -7.250  1.00  8.82           O  
ANISOU  632  O   LYS A  78     1419   1158    773    -31     20    -13       O  
ATOM    633  CB  LYS A  78      41.129  12.896  -4.385  1.00  8.35           C  
ANISOU  633  CB  LYS A  78      941   1423    809    -48     64   -383       C  
ATOM    634  CG  LYS A  78      41.370  14.062  -3.401  1.00  8.56           C  
ANISOU  634  CG  LYS A  78     1111   1296    846    -47    -64   -239       C  
ATOM    635  CD  LYS A  78      42.702  13.886  -2.719  1.00  9.38           C  
ANISOU  635  CD  LYS A  78      981   1782    802   -159      2   -337       C  
ATOM    636  CE  LYS A  78      42.816  14.900  -1.587  1.00  9.41           C  
ANISOU  636  CE  LYS A  78      941   1613   1021    -57    -38   -392       C  
ATOM    637  NZ  LYS A  78      44.173  14.916  -0.993  1.00 10.31           N  
ANISOU  637  NZ  LYS A  78      925   1839   1155   -133    -65   -440       N  
ATOM    638  N   LYS A  79      38.949  10.822  -5.977  1.00  6.98           N  
ANISOU  638  N   LYS A  79      973    891    789     49   -161   -182       N  
ATOM    639  CA  LYS A  79      38.657   9.966  -7.135  1.00  7.34           C  
ANISOU  639  CA  LYS A  79     1189    866    733    165   -164   -204       C  
ATOM    640  C   LYS A  79      37.477  10.470  -7.944  1.00  7.99           C  
ANISOU  640  C   LYS A  79     1144   1097    796    173   -155   -160       C  
ATOM    641  O   LYS A  79      37.252   9.917  -9.049  1.00  8.21           O  
ANISOU  641  O   LYS A  79     1280   1106    733    144   -229   -112       O  
ATOM    642  CB  LYS A  79      38.417   8.514  -6.729  1.00  9.56           C  
ANISOU  642  CB  LYS A  79     1441    860   1332     68   -211    -52       C  
ATOM    643  CG  LYS A  79      39.737   7.810  -6.276  1.00 10.51           C  
ANISOU  643  CG  LYS A  79     1826    955   1210    190   -397    112       C  
ATOM    644  CD  LYS A  79      40.663   7.656  -7.499  1.00 17.22           C  
ANISOU  644  CD  LYS A  79     1353   2845   2345    488    239    645       C  
ATOM    645  CE  LYS A  79      41.658   6.526  -7.470  1.00 26.42           C  
ANISOU  645  CE  LYS A  79     3701   2802   3536   1460   1093    112       C  
ATOM    646  NZ  LYS A  79      40.988   5.194  -7.514  1.00 37.66           N  
ANISOU  646  NZ  LYS A  79     9405   2654   2248    156   1595   -273       N  
ATOM    647  N   LYS A  80      36.724  11.468  -7.475  1.00  7.58           N  
ANISOU  647  N   LYS A  80      967   1000    912     52    -20    -75       N  
ATOM    648  CA  LYS A  80      35.624  12.085  -8.235  1.00  7.55           C  
ANISOU  648  CA  LYS A  80     1289    741    838    153   -130      2       C  
ATOM    649  C   LYS A  80      34.715  10.975  -8.804  1.00  7.08           C  
ANISOU  649  C   LYS A  80     1146    853    692    215   -128     25       C  
ATOM    650  O   LYS A  80      34.320  11.023  -9.972  1.00  8.89           O  
ANISOU  650  O   LYS A  80     1612   1196    571    154    -67    -80       O  
ATOM    651  CB  LYS A  80      36.167  13.008  -9.310  1.00  9.17           C  
ANISOU  651  CB  LYS A  80     1425    989   1070      3    -14     69       C  
ATOM    652  CG  LYS A  80      37.054  14.133  -8.756  1.00 10.15           C  
ANISOU  652  CG  LYS A  80     1122   1464   1268   -238    -12    141       C  
ATOM    653  CD  LYS A  80      37.276  15.188  -9.853  1.00 13.98           C  
ANISOU  653  CD  LYS A  80     2333   1427   1551   -516    369    153       C  
ATOM    654  CE  LYS A  80      38.001  14.689 -11.066  1.00 16.60           C  
ANISOU  654  CE  LYS A  80     2845   2176   1286   -480    261    136       C  
ATOM    655  NZ  LYS A  80      38.436  15.910 -11.831  1.00 17.27           N  
ANISOU  655  NZ  LYS A  80     2265   2336   1960     30    814    577       N  
ATOM    656  N   GLY A  81      34.340  10.032  -7.929  1.00  7.31           N  
ANISOU  656  N   GLY A  81     1183    888    706     67    -65     -3       N  
ATOM    657  CA  GLY A  81      33.321   9.047  -8.288  1.00  8.63           C  
ANISOU  657  CA  GLY A  81     1374    878   1025     63    -58   -192       C  
ATOM    658  C   GLY A  81      33.941   7.715  -8.722  1.00  7.82           C  
ANISOU  658  C   GLY A  81     1426    861    685    181    -43    -59       C  
ATOM    659  O   GLY A  81      33.267   6.668  -8.679  1.00  9.80           O  
ANISOU  659  O   GLY A  81     1744   1002    975     25   -101    -20       O  
ATOM    660  N   HIS A  82      35.226   7.721  -9.105  1.00  8.56           N  
ANISOU  660  N   HIS A  82     1439   1222    591    237    -45   -169       N  
ATOM    661  CA  HIS A  82      35.900   6.485  -9.547  1.00  8.57           C  
ANISOU  661  CA  HIS A  82     1439   1117    701    173     61    -98       C  
ATOM    662  C   HIS A  82      36.547   5.789  -8.348  1.00  8.46           C  
ANISOU  662  C   HIS A  82     1332   1104    776     75    -42    -42       C  
ATOM    663  O   HIS A  82      37.779   5.612  -8.308  1.00  9.45           O  
ANISOU  663  O   HIS A  82     1377   1374    841     11    -25    -18       O  
ATOM    664  CB  HIS A  82      36.965   6.784 -10.588  1.00  9.73           C  
ANISOU  664  CB  HIS A  82     1570   1316    812    246    138     60       C  
ATOM    665  CG  HIS A  82      36.457   7.477 -11.823  1.00  9.60           C  
ANISOU  665  CG  HIS A  82     1604   1270    774     77     32    -53       C  
ATOM    666  ND1 HIS A  82      36.083   6.796 -12.948  1.00 13.84           N  
ANISOU  666  ND1 HIS A  82     2386   1870   1003     92   -373   -176       N  
ATOM    667  CD2 HIS A  82      36.254   8.784 -12.093  1.00 11.33           C  
ANISOU  667  CD2 HIS A  82     1608   1403   1295     40   -221    282       C  
ATOM    668  CE1 HIS A  82      35.700   7.689 -13.867  1.00 12.98           C  
ANISOU  668  CE1 HIS A  82     1755   2330    847   -117    -35    233       C  
ATOM    669  NE2 HIS A  82      35.788   8.891 -13.371  1.00 13.51           N  
ANISOU  669  NE2 HIS A  82     1805   2083   1245    -45   -123    485       N  
ATOM    670  N   HIS A  83      35.755   5.430  -7.385  1.00  8.71           N  
ANISOU  670  N   HIS A  83     1425   1073    813     -2    -78     60       N  
ATOM    671  CA  HIS A  83      36.247   5.033  -6.070  1.00  8.47           C  
ANISOU  671  CA  HIS A  83     1478    989    752    200     -6    -10       C  
ATOM    672  C   HIS A  83      36.002   3.577  -5.760  1.00  8.32           C  
ANISOU  672  C   HIS A  83     1326   1039    794    123    -17      8       C  
ATOM    673  O   HIS A  83      36.029   3.192  -4.579  1.00  9.90           O  
ANISOU  673  O   HIS A  83     1753   1145    863    312    143    156       O  
ATOM    674  CB  HIS A  83      35.606   5.950  -4.993  1.00  9.18           C  
ANISOU  674  CB  HIS A  83     1384   1207    896    328   -104   -132       C  
ATOM    675  CG  HIS A  83      34.117   6.042  -5.075  1.00  8.30           C  
ANISOU  675  CG  HIS A  83     1407    970    775    268   -163      4       C  
ATOM    676  ND1 HIS A  83      33.478   7.257  -4.874  1.00  9.13           N  
ANISOU  676  ND1 HIS A  83     1335   1006   1130    242   -193    -98       N  
ATOM    677  CD2 HIS A  83      33.152   5.122  -5.358  1.00  9.47           C  
ANISOU  677  CD2 HIS A  83     1475   1041   1080    162    -75    -71       C  
ATOM    678  CE1 HIS A  83      32.173   7.040  -5.015  1.00  8.81           C  
ANISOU  678  CE1 HIS A  83     1287   1051   1010    200     -4    -94       C  
ATOM    679  NE2 HIS A  83      31.930   5.763  -5.312  1.00  9.39           N  
ANISOU  679  NE2 HIS A  83     1478   1084   1007    219   -212   -210       N  
ATOM    680  N   GLU A  84      35.768   2.718  -6.733  1.00 10.05           N  
ANISOU  680  N   GLU A  84     1708   1091   1018      7    -53   -131       N  
ATOM    681  CA  GLU A  84      35.503   1.308  -6.451  1.00 10.75           C  
ANISOU  681  CA  GLU A  84     1795   1148   1139     22   -199   -146       C  
ATOM    682  C   GLU A  84      36.614   0.678  -5.625  1.00 11.14           C  
ANISOU  682  C   GLU A  84     1752   1415   1066    388    180     24       C  
ATOM    683  O   GLU A  84      36.370  -0.070  -4.643  1.00 12.63           O  
ANISOU  683  O   GLU A  84     2362   1080   1357    371    270     97       O  
ATOM    684  CB AGLU A  84      35.267   0.590  -7.793  0.56 14.50           C  
ANISOU  684  CB AGLU A  84     2582   1316   1612    553   -458   -698       C  
ATOM    685  CB BGLU A  84      35.398   0.531  -7.778  0.44 15.08           C  
ANISOU  685  CB BGLU A  84     3147   1161   1420    109   -422   -371       C  
ATOM    686  CG AGLU A  84      34.203   1.121  -8.711  0.56 18.47           C  
ANISOU  686  CG AGLU A  84     3316   1948   1753    250  -1128   -467       C  
ATOM    687  CG BGLU A  84      35.628  -0.980  -7.571  0.44 20.63           C  
ANISOU  687  CG BGLU A  84     5566    969   1303   -535   -898    -94       C  
ATOM    688  CD AGLU A  84      34.346   2.490  -9.345  0.56 32.03           C  
ANISOU  688  CD AGLU A  84     6739   1870   3560    154  -2999     50       C  
ATOM    689  CD BGLU A  84      34.276  -1.528  -7.180  0.44 20.45           C  
ANISOU  689  CD BGLU A  84     5156    748   1865    131   -905    414       C  
ATOM    690  OE1AGLU A  84      35.437   3.114  -9.494  0.56 25.86           O  
ANISOU  690  OE1AGLU A  84     7525    603   1696    295  -1346    102       O  
ATOM    691  OE1BGLU A  84      33.374  -0.659  -7.143  0.44 29.41           O  
ANISOU  691  OE1BGLU A  84     6234   1917   3023   1153   -314  -1013       O  
ATOM    692  OE2AGLU A  84      33.281   3.047  -9.720  0.56 48.94           O  
ANISOU  692  OE2AGLU A  84     8027   3956   6613    827  -4279   1759       O  
ATOM    693  OE2BGLU A  84      33.997  -2.701  -6.858  0.44 28.37           O  
ANISOU  693  OE2BGLU A  84     7515   1039   2226   -444   1272    369       O  
ATOM    694  N   ALA A  85      37.882   0.921  -5.993  1.00 10.89           N  
ANISOU  694  N   ALA A  85     1713   1164   1261    255    -11   -202       N  
ATOM    695  CA  ALA A  85      38.961   0.251  -5.258  1.00 10.39           C  
ANISOU  695  CA  ALA A  85     1687   1356    904    361    222   -103       C  
ATOM    696  C   ALA A  85      38.985   0.671  -3.800  1.00 10.59           C  
ANISOU  696  C   ALA A  85     1957   1195    871    539    369    -12       C  
ATOM    697  O   ALA A  85      39.272  -0.126  -2.885  1.00 13.63           O  
ANISOU  697  O   ALA A  85     2697   1521    962    648    378    253       O  
ATOM    698  CB  ALA A  85      40.325   0.541  -5.866  1.00 13.26           C  
ANISOU  698  CB  ALA A  85     1750   2132   1157    420    484    139       C  
ATOM    699  N   GLU A  86      38.716   1.928  -3.511  1.00  9.59           N  
ANISOU  699  N   GLU A  86     1334   1214   1094    270     90   -224       N  
ATOM    700  CA  GLU A  86      38.732   2.469  -2.155  1.00  8.87           C  
ANISOU  700  CA  GLU A  86     1489    873   1007    102    123    -81       C  
ATOM    701  C   GLU A  86      37.536   1.991  -1.348  1.00  8.57           C  
ANISOU  701  C   GLU A  86     1439   1014    804     65   -102    -13       C  
ATOM    702  O   GLU A  86      37.630   1.783  -0.134  1.00  9.19           O  
ANISOU  702  O   GLU A  86     1749    992    750    105    -58     23       O  
ATOM    703  CB  GLU A  86      38.700   4.012  -2.226  1.00 10.74           C  
ANISOU  703  CB  GLU A  86     1708    854   1517   -195   -338   -117       C  
ATOM    704  CG  GLU A  86      39.990   4.628  -2.758  1.00 12.85           C  
ANISOU  704  CG  GLU A  86     1776   1313   1792   -427   -497    249       C  
ATOM    705  CD  GLU A  86      40.203   4.569  -4.248  1.00 13.18           C  
ANISOU  705  CD  GLU A  86     1834   1225   1949    -94    -47    151       C  
ATOM    706  OE1 GLU A  86      39.256   4.284  -5.020  1.00 11.59           O  
ANISOU  706  OE1 GLU A  86     1646   1361   1398    116    135    382       O  
ATOM    707  OE2 GLU A  86      41.346   4.788  -4.713  1.00 16.79           O  
ANISOU  707  OE2 GLU A  86     1863   1927   2590   -229    186   -537       O  
ATOM    708  N   LEU A  87      36.384   1.838  -1.993  1.00  8.67           N  
ANISOU  708  N   LEU A  87     1356    866   1074    172   -130    -85       N  
ATOM    709  CA  LEU A  87      35.219   1.414  -1.231  1.00  9.59           C  
ANISOU  709  CA  LEU A  87     1387   1205   1050     95   -156    -63       C  
ATOM    710  C   LEU A  87      35.264  -0.058  -0.825  1.00  9.93           C  
ANISOU  710  C   LEU A  87     1454   1241   1078    175     51     77       C  
ATOM    711  O   LEU A  87      34.631  -0.414   0.148  1.00 10.94           O  
ANISOU  711  O   LEU A  87     1501   1739    916    221    -49    188       O  
ATOM    712  CB  LEU A  87      33.916   1.671  -1.997  1.00 11.36           C  
ANISOU  712  CB  LEU A  87     1409   1658   1249    408   -296   -165       C  
ATOM    713  CG  LEU A  87      33.544   3.117  -2.235  1.00 14.87           C  
ANISOU  713  CG  LEU A  87     1974   1621   2054    536   -849   -444       C  
ATOM    714  CD1 LEU A  87      32.095   3.181  -2.724  1.00 14.35           C  
ANISOU  714  CD1 LEU A  87     1596   1948   1907    584   -280    150       C  
ATOM    715  CD2 LEU A  87      33.698   3.981  -1.002  1.00 18.88           C  
ANISOU  715  CD2 LEU A  87     3158   2025   1992   1009   -862   -639       C  
ATOM    716  N   LYS A  88      35.980  -0.904  -1.559  1.00 10.06           N  
ANISOU  716  N   LYS A  88     1381   1282   1158    289   -148    -69       N  
ATOM    717  CA  LYS A  88      35.967  -2.338  -1.219  1.00 10.91           C  
ANISOU  717  CA  LYS A  88     1592   1192   1363    -39    -47   -159       C  
ATOM    718  C   LYS A  88      36.427  -2.594   0.204  1.00  8.94           C  
ANISOU  718  C   LYS A  88     1207    901   1289    -53    131    -40       C  
ATOM    719  O   LYS A  88      35.687  -3.257   0.973  1.00  9.47           O  
ANISOU  719  O   LYS A  88     1267    919   1412   -210    113   -150       O  
ATOM    720  CB  LYS A  88      36.836  -3.137  -2.228  1.00 11.64           C  
ANISOU  720  CB  LYS A  88     1888   1219   1315    188    -41   -152       C  
ATOM    721  CG  LYS A  88      36.113  -3.366  -3.550  1.00 12.76           C  
ANISOU  721  CG  LYS A  88     2254   1302   1293     63   -141    -39       C  
ATOM    722  CD  LYS A  88      36.931  -4.194  -4.537  1.00 17.77           C  
ANISOU  722  CD  LYS A  88     2883   2424   1447   -192    560   -414       C  
ATOM    723  CE  LYS A  88      36.160  -4.258  -5.870  1.00 22.93           C  
ANISOU  723  CE  LYS A  88     4130   3391   1189    271    406   -158       C  
ATOM    724  NZ  LYS A  88      36.843  -5.171  -6.781  1.00 34.67           N  
ANISOU  724  NZ  LYS A  88     9462   1893   1819   -247   1821   -528       N  
ATOM    725  N   PRO A  89      37.633  -2.169   0.617  1.00  8.88           N  
ANISOU  725  N   PRO A  89     1184    973   1217    -56    168    -57       N  
ATOM    726  CA  PRO A  89      38.059  -2.515   1.986  1.00  8.98           C  
ANISOU  726  CA  PRO A  89     1011   1088   1314    199    180    -62       C  
ATOM    727  C   PRO A  89      37.203  -1.832   3.045  1.00  6.51           C  
ANISOU  727  C   PRO A  89      744    593   1136    -48    -16    -42       C  
ATOM    728  O   PRO A  89      36.933  -2.426   4.114  1.00  8.64           O  
ANISOU  728  O   PRO A  89     1147    899   1236    -45    122    182       O  
ATOM    729  CB  PRO A  89      39.538  -2.086   2.057  1.00 10.14           C  
ANISOU  729  CB  PRO A  89     1029   1363   1463     -3    295    137       C  
ATOM    730  CG  PRO A  89      39.648  -1.025   0.960  1.00 10.58           C  
ANISOU  730  CG  PRO A  89     1139   1585   1296   -121    -67    185       C  
ATOM    731  CD  PRO A  89      38.729  -1.495  -0.126  1.00  9.80           C  
ANISOU  731  CD  PRO A  89     1183   1244   1294    -70    212   -198       C  
ATOM    732  N   LEU A  90      36.781  -0.609   2.751  1.00  7.75           N  
ANISOU  732  N   LEU A  90     1247    697   1000    113   -176   -199       N  
ATOM    733  CA  LEU A  90      35.995   0.172   3.712  1.00  7.42           C  
ANISOU  733  CA  LEU A  90     1035    636   1148     45   -101   -247       C  
ATOM    734  C   LEU A  90      34.627  -0.447   3.930  1.00  7.74           C  
ANISOU  734  C   LEU A  90     1239    789    912    -75    -79     19       C  
ATOM    735  O   LEU A  90      34.140  -0.618   5.055  1.00  7.90           O  
ANISOU  735  O   LEU A  90     1191    863    946     41    -73     72       O  
ATOM    736  CB  LEU A  90      35.885   1.629   3.180  1.00  8.32           C  
ANISOU  736  CB  LEU A  90     1380    680   1102     82    180      6       C  
ATOM    737  CG  LEU A  90      35.234   2.593   4.128  1.00  9.12           C  
ANISOU  737  CG  LEU A  90     1678    735   1053    165     -3   -132       C  
ATOM    738  CD1 LEU A  90      36.207   2.850   5.286  1.00 15.12           C  
ANISOU  738  CD1 LEU A  90     3024   1305   1417    250   -806   -248       C  
ATOM    739  CD2 LEU A  90      34.927   3.920   3.448  1.00 11.28           C  
ANISOU  739  CD2 LEU A  90     1825    834   1627    303      6    107       C  
ATOM    740  N   ALA A  91      33.979  -0.838   2.833  1.00  7.82           N  
ANISOU  740  N   ALA A  91      987    982   1001    -49    -12   -100       N  
ATOM    741  CA  ALA A  91      32.691  -1.525   2.939  1.00  7.67           C  
ANISOU  741  CA  ALA A  91      992    809   1114     81   -185     33       C  
ATOM    742  C   ALA A  91      32.829  -2.848   3.667  1.00  7.60           C  
ANISOU  742  C   ALA A  91     1096    779   1013     82     72    -64       C  
ATOM    743  O   ALA A  91      32.015  -3.207   4.497  1.00  8.49           O  
ANISOU  743  O   ALA A  91     1149   1107    969   -155     38   -100       O  
ATOM    744  CB  ALA A  91      32.099  -1.749   1.570  1.00  9.73           C  
ANISOU  744  CB  ALA A  91     1556   1090   1050    -58   -262   -174       C  
ATOM    745  N   GLN A  92      33.888  -3.616   3.368  1.00  7.34           N  
ANISOU  745  N   GLN A  92     1059    584   1144     28    -47    -19       N  
ATOM    746  CA  GLN A  92      34.020  -4.908   4.006  1.00  7.56           C  
ANISOU  746  CA  GLN A  92     1483    489    900     20     77   -155       C  
ATOM    747  C   GLN A  92      34.201  -4.743   5.514  1.00  7.31           C  
ANISOU  747  C   GLN A  92     1141    700    935    -94     29   -203       C  
ATOM    748  O   GLN A  92      33.577  -5.461   6.315  1.00  8.54           O  
ANISOU  748  O   GLN A  92     1310    934   1002   -286    -30    -17       O  
ATOM    749  CB  GLN A  92      35.156  -5.736   3.410  1.00  8.40           C  
ANISOU  749  CB  GLN A  92     1344    791   1058    178    148      8       C  
ATOM    750  CG  GLN A  92      35.209  -7.124   4.035  1.00  8.19           C  
ANISOU  750  CG  GLN A  92     1056    778   1276    144     34     -3       C  
ATOM    751  CD  GLN A  92      36.255  -8.018   3.424  1.00  8.54           C  
ANISOU  751  CD  GLN A  92     1028    841   1377    111    -17   -229       C  
ATOM    752  OE1 GLN A  92      37.393  -7.614   3.180  1.00 11.15           O  
ANISOU  752  OE1 GLN A  92     1176    905   2157     71    301    -50       O  
ATOM    753  NE2 GLN A  92      35.881  -9.277   3.197  1.00  8.87           N  
ANISOU  753  NE2 GLN A  92     1591    828    953    -30   -153   -159       N  
ATOM    754  N   SER A  93      35.056  -3.813   5.950  1.00  6.91           N  
ANISOU  754  N   SER A  93     1054    608    963    -77     26    -86       N  
ATOM    755  CA  SER A  93      35.273  -3.669   7.395  1.00  7.96           C  
ANISOU  755  CA  SER A  93     1023    957   1045     -2   -143   -247       C  
ATOM    756  C   SER A  93      34.025  -3.090   8.059  1.00  7.59           C  
ANISOU  756  C   SER A  93     1249    617   1019    -69    145     38       C  
ATOM    757  O   SER A  93      33.631  -3.547   9.134  1.00  8.44           O  
ANISOU  757  O   SER A  93     1350    978    879    -62    -41     -4       O  
ATOM    758  CB  SER A  93      36.491  -2.837   7.726  1.00  9.08           C  
ANISOU  758  CB  SER A  93     1149    864   1435   -117   -422     82       C  
ATOM    759  OG  SER A  93      36.292  -1.514   7.278  1.00  9.29           O  
ANISOU  759  OG  SER A  93     1433    947   1150     67    -34    -67       O  
ATOM    760  N   HIS A  94      33.416  -2.096   7.414  1.00  7.23           N  
ANISOU  760  N   HIS A  94     1138    593   1017    -25   -105   -156       N  
ATOM    761  CA  HIS A  94      32.279  -1.413   8.073  1.00  8.39           C  
ANISOU  761  CA  HIS A  94     1201    588   1398    -67    107   -100       C  
ATOM    762  C   HIS A  94      31.056  -2.298   8.072  1.00  7.57           C  
ANISOU  762  C   HIS A  94     1104    705   1068    -29     18   -150       C  
ATOM    763  O   HIS A  94      30.262  -2.224   9.027  1.00  9.62           O  
ANISOU  763  O   HIS A  94     1374    966   1314    -24    341   -121       O  
ATOM    764  CB  HIS A  94      32.066  -0.030   7.463  1.00  7.98           C  
ANISOU  764  CB  HIS A  94     1077    606   1348    -32    -64   -129       C  
ATOM    765  CG  HIS A  94      33.093   0.921   8.034  1.00  7.36           C  
ANISOU  765  CG  HIS A  94     1019    627   1150     -2    -79      4       C  
ATOM    766  ND1 HIS A  94      34.430   0.765   7.820  1.00  8.97           N  
ANISOU  766  ND1 HIS A  94     1076    996   1338   -175     45   -392       N  
ATOM    767  CD2 HIS A  94      32.993   2.033   8.803  1.00  6.62           C  
ANISOU  767  CD2 HIS A  94     1068    561    887   -266     67    127       C  
ATOM    768  CE1 HIS A  94      35.086   1.745   8.449  1.00  7.81           C  
ANISOU  768  CE1 HIS A  94     1047    654   1266      2    -30   -302       C  
ATOM    769  NE2 HIS A  94      34.243   2.532   9.076  1.00  6.25           N  
ANISOU  769  NE2 HIS A  94      931    442   1000     21      5     45       N  
ATOM    770  N   ALA A  95      30.836  -3.187   7.088  1.00  7.76           N  
ANISOU  770  N   ALA A  95     1235    730    984   -157    -88    -23       N  
ATOM    771  CA  ALA A  95      29.694  -4.111   7.090  1.00  7.76           C  
ANISOU  771  CA  ALA A  95     1236    632   1083   -176    -98     11       C  
ATOM    772  C   ALA A  95      29.946  -5.247   8.060  1.00  8.18           C  
ANISOU  772  C   ALA A  95     1209    727   1170      2    286     59       C  
ATOM    773  O   ALA A  95      29.071  -5.609   8.828  1.00 10.54           O  
ANISOU  773  O   ALA A  95     1420   1050   1534     58    457    301       O  
ATOM    774  CB  ALA A  95      29.481  -4.702   5.696  1.00  9.17           C  
ANISOU  774  CB  ALA A  95     1274   1024   1186   -318    -14   -198       C  
ATOM    775  N   THR A  96      31.134  -5.840   8.003  1.00  8.19           N  
ANISOU  775  N   THR A  96     1249    770   1093     66     56    -31       N  
ATOM    776  CA  THR A  96      31.325  -7.163   8.596  1.00  8.93           C  
ANISOU  776  CA  THR A  96     1429    664   1298    -16   -142    -72       C  
ATOM    777  C   THR A  96      31.937  -7.126   9.984  1.00 10.62           C  
ANISOU  777  C   THR A  96     2068    683   1286    -45   -238    102       C  
ATOM    778  O   THR A  96      31.569  -7.936  10.820  1.00 12.43           O  
ANISOU  778  O   THR A  96     2434    984   1306      9     97    217       O  
ATOM    779  CB  THR A  96      32.234  -8.027   7.703  1.00  9.36           C  
ANISOU  779  CB  THR A  96     1441    800   1315    162   -300    -54       C  
ATOM    780  OG1 THR A  96      31.689  -7.934   6.368  1.00 17.14           O  
ANISOU  780  OG1 THR A  96     3605   1529   1379   1115   -989   -566       O  
ATOM    781  CG2 THR A  96      32.276  -9.483   8.101  1.00 10.60           C  
ANISOU  781  CG2 THR A  96     1427    706   1893     82   -172    -85       C  
ATOM    782  N   LYS A  97      32.907  -6.221  10.148  1.00 10.07           N  
ANISOU  782  N   LYS A  97     2038    700   1089     19   -330   -192       N  
ATOM    783  CA  LYS A  97      33.536  -6.127  11.458  1.00 11.70           C  
ANISOU  783  CA  LYS A  97     2364   1061   1020    240   -373   -210       C  
ATOM    784  C   LYS A  97      32.863  -5.079  12.337  1.00 10.15           C  
ANISOU  784  C   LYS A  97     2345    705    808    -55   -104     38       C  
ATOM    785  O   LYS A  97      32.435  -5.388  13.473  1.00 14.00           O  
ANISOU  785  O   LYS A  97     3341   1047    931    151     77    106       O  
ATOM    786  CB  LYS A  97      35.032  -5.839  11.335  1.00 14.77           C  
ANISOU  786  CB  LYS A  97     2187   1716   1707    404   -560   -649       C  
ATOM    787  CG  LYS A  97      35.695  -5.741  12.720  1.00 18.60           C  
ANISOU  787  CG  LYS A  97     3099   1845   2122    324  -1245   -724       C  
ATOM    788  CD  LYS A  97      37.193  -5.493  12.603  1.00 24.21           C  
ANISOU  788  CD  LYS A  97     2839   2979   3379    850  -1534  -1333       C  
ATOM    789  CE  LYS A  97      37.859  -5.297  13.959  1.00 32.19           C  
ANISOU  789  CE  LYS A  97     4119   4194   3918   -140  -2522   -494       C  
ATOM    790  NZ  LYS A  97      37.403  -6.374  14.897  1.00 44.75           N  
ANISOU  790  NZ  LYS A  97     7843   4578   4582   1613   -986    596       N  
ATOM    791  N   HIS A  98      32.714  -3.853  11.854  1.00  9.63           N  
ANISOU  791  N   HIS A  98     1896    733   1029    -11   -168    -50       N  
ATOM    792  CA  HIS A  98      32.187  -2.790  12.712  1.00  9.94           C  
ANISOU  792  CA  HIS A  98     1788    716   1274   -159     29   -171       C  
ATOM    793  C   HIS A  98      30.651  -2.789  12.766  1.00 11.28           C  
ANISOU  793  C   HIS A  98     1831   1067   1390   -417    317   -215       C  
ATOM    794  O   HIS A  98      30.098  -2.291  13.774  1.00 12.63           O  
ANISOU  794  O   HIS A  98     2163   1240   1395   -114    448   -113       O  
ATOM    795  CB  HIS A  98      32.699  -1.430  12.206  1.00  9.55           C  
ANISOU  795  CB  HIS A  98     1556    813   1259   -190     81    -92       C  
ATOM    796  CG  HIS A  98      34.180  -1.408  12.000  1.00  9.37           C  
ANISOU  796  CG  HIS A  98     1517    885   1160    -28    -28    -82       C  
ATOM    797  ND1 HIS A  98      35.048  -1.927  12.935  1.00 10.63           N  
ANISOU  797  ND1 HIS A  98     1761   1003   1274     62   -163    -71       N  
ATOM    798  CD2 HIS A  98      34.915  -0.907  10.994  1.00  9.54           C  
ANISOU  798  CD2 HIS A  98     1392    964   1269   -203    -81   -102       C  
ATOM    799  CE1 HIS A  98      36.297  -1.772  12.489  1.00 11.11           C  
ANISOU  799  CE1 HIS A  98     1659    892   1672    112   -181    -22       C  
ATOM    800  NE2 HIS A  98      36.245  -1.133  11.302  1.00 10.28           N  
ANISOU  800  NE2 HIS A  98     1408    927   1571    -84   -121   -104       N  
ATOM    801  N   LYS A  99      29.980  -3.261  11.733  1.00 10.63           N  
ANISOU  801  N   LYS A  99     1724    856   1459   -143     89   -170       N  
ATOM    802  CA  LYS A  99      28.516  -3.348  11.608  1.00 11.03           C  
ANISOU  802  CA  LYS A  99     1660    943   1589    -87    133    254       C  
ATOM    803  C   LYS A  99      27.901  -1.958  11.702  1.00 10.01           C  
ANISOU  803  C   LYS A  99     1650    813   1339   -296    351   -179       C  
ATOM    804  O   LYS A  99      27.126  -1.639  12.595  1.00 11.79           O  
ANISOU  804  O   LYS A  99     1787   1375   1319   -321    368   -203       O  
ATOM    805  CB  LYS A  99      27.907  -4.329  12.643  1.00 14.53           C  
ANISOU  805  CB  LYS A  99     2448   1062   2011   -297    602    230       C  
ATOM    806  CG  LYS A  99      28.329  -5.752  12.288  1.00 26.29           C  
ANISOU  806  CG  LYS A  99     4660    967   4362    196   1371    495       C  
ATOM    807  CD  LYS A  99      27.858  -6.733  13.329  1.00 34.23           C  
ANISOU  807  CD  LYS A  99     5905   1212   5888     81   2362    978       C  
ATOM    808  CE  LYS A  99      28.756  -7.950  13.379  1.00 42.87           C  
ANISOU  808  CE  LYS A  99     6772   1855   7663    761   1199   1961       C  
ATOM    809  NZ  LYS A  99      28.816  -8.614  14.712  1.00 41.51           N  
ANISOU  809  NZ  LYS A  99     4239   4558   6973   1225    982   1843       N  
ATOM    810  N   ILE A 100      28.234  -1.127  10.703  1.00 10.85           N  
ANISOU  810  N   ILE A 100     1805    829   1490   -104    340     90       N  
ATOM    811  CA  ILE A 100      27.767   0.274  10.705  1.00  9.67           C  
ANISOU  811  CA  ILE A 100     1431    884   1359   -206    297   -152       C  
ATOM    812  C   ILE A 100      26.619   0.432   9.723  1.00  9.51           C  
ANISOU  812  C   ILE A 100     1395    742   1476   -242    186   -344       C  
ATOM    813  O   ILE A 100      26.780   0.365   8.500  1.00 11.17           O  
ANISOU  813  O   ILE A 100     1509   1261   1474   -153    132   -452       O  
ATOM    814  CB  ILE A 100      28.916   1.224  10.334  1.00  9.68           C  
ANISOU  814  CB  ILE A 100     1243    810   1627   -135    -14      1       C  
ATOM    815  CG1 ILE A 100      30.137   0.993  11.210  1.00 10.02           C  
ANISOU  815  CG1 ILE A 100     1391   1224   1192    -92     37    164       C  
ATOM    816  CG2 ILE A 100      28.454   2.672  10.335  1.00 10.33           C  
ANISOU  816  CG2 ILE A 100     1532    785   1609    -46     -5   -262       C  
ATOM    817  CD1 ILE A 100      29.854   1.041  12.707  1.00 10.65           C  
ANISOU  817  CD1 ILE A 100     1712   1048   1287   -446    262     25       C  
ATOM    818  N   PRO A 101      25.413   0.654  10.233  1.00 11.16           N  
ANISOU  818  N   PRO A 101     1417   1250   1573   -245    272     49       N  
ATOM    819  CA  PRO A 101      24.278   0.811   9.301  1.00 11.37           C  
ANISOU  819  CA  PRO A 101     1503   1153   1667   -110    179     33       C  
ATOM    820  C   PRO A 101      24.385   2.073   8.452  1.00 10.11           C  
ANISOU  820  C   PRO A 101     1464    910   1468   -182    130   -278       C  
ATOM    821  O   PRO A 101      25.004   3.062   8.818  1.00 10.75           O  
ANISOU  821  O   PRO A 101     1327   1027   1732   -311    383   -439       O  
ATOM    822  CB  PRO A 101      23.037   0.913  10.186  1.00 14.89           C  
ANISOU  822  CB  PRO A 101     1449   2253   1954   -204    261    325       C  
ATOM    823  CG  PRO A 101      23.577   1.097  11.564  1.00 16.77           C  
ANISOU  823  CG  PRO A 101     1588   2991   1793    108    372     37       C  
ATOM    824  CD  PRO A 101      25.016   0.744  11.627  1.00 12.28           C  
ANISOU  824  CD  PRO A 101     1464   1624   1578   -281    372    -94       C  
ATOM    825  N   ILE A 102      23.759   2.043   7.268  1.00 11.53           N  
ANISOU  825  N   ILE A 102     1618   1278   1484    -83    -25   -148       N  
ATOM    826  CA  ILE A 102      23.717   3.235   6.397  1.00 11.97           C  
ANISOU  826  CA  ILE A 102     1756   1338   1454   -494    106    -79       C  
ATOM    827  C   ILE A 102      23.183   4.448   7.154  1.00 11.50           C  
ANISOU  827  C   ILE A 102     2000   1093   1276   -449    -90     32       C  
ATOM    828  O   ILE A 102      23.721   5.536   6.924  1.00 12.14           O  
ANISOU  828  O   ILE A 102     1981   1287   1346   -634   -340     40       O  
ATOM    829  CB  ILE A 102      22.880   2.921   5.163  1.00 15.55           C  
ANISOU  829  CB  ILE A 102     3081   1408   1420    -72   -385   -232       C  
ATOM    830  CG1 ILE A 102      23.527   1.861   4.262  1.00 16.69           C  
ANISOU  830  CG1 ILE A 102     2480   1552   2309   -457   -114   -716       C  
ATOM    831  CG2 ILE A 102      22.584   4.206   4.366  1.00 17.66           C  
ANISOU  831  CG2 ILE A 102     3667   1310   1733   -468   -560    -38       C  
ATOM    832  CD1 ILE A 102      24.816   2.378   3.643  1.00 23.22           C  
ANISOU  832  CD1 ILE A 102     3193   3207   2421  -1130    393   -918       C  
ATOM    833  N   LYS A 103      22.212   4.290   8.059  1.00 11.52           N  
ANISOU  833  N   LYS A 103     1754   1161   1460   -329    -86   -147       N  
ATOM    834  CA  LYS A 103      21.732   5.420   8.842  1.00 12.06           C  
ANISOU  834  CA  LYS A 103     1302   1222   2057   -321   -181   -302       C  
ATOM    835  C   LYS A 103      22.861   6.109   9.585  1.00 10.51           C  
ANISOU  835  C   LYS A 103     1136    999   1859   -334    -88   -172       C  
ATOM    836  O   LYS A 103      22.802   7.350   9.761  1.00 11.27           O  
ANISOU  836  O   LYS A 103     1426    988   1867   -267   -227   -118       O  
ATOM    837  CB  LYS A 103      20.673   4.952   9.859  1.00 20.36           C  
ANISOU  837  CB  LYS A 103     1253   2821   3662  -1008    854  -1286       C  
ATOM    838  CG  LYS A 103      20.012   6.124  10.533  1.00 31.99           C  
ANISOU  838  CG  LYS A 103     2182   3660   6311   -430   1996  -1783       C  
ATOM    839  CD  LYS A 103      18.589   6.415  10.073  1.00 43.35           C  
ANISOU  839  CD  LYS A 103     2771   4816   8883    654   1282  -1784       C  
ATOM    840  CE  LYS A 103      17.891   7.446  10.942  1.00 48.35           C  
ANISOU  840  CE  LYS A 103     2615   5733  10022    593   1653  -2570       C  
ATOM    841  NZ  LYS A 103      17.570   8.760  10.327  1.00 46.58           N  
ANISOU  841  NZ  LYS A 103     2803   5029   9868    616  -1035  -4036       N  
ATOM    842  N   TYR A 104      23.837   5.371  10.070  1.00  9.19           N  
ANISOU  842  N   TYR A 104     1132    877   1482   -352    137   -127       N  
ATOM    843  CA  TYR A 104      24.948   5.988  10.824  1.00  8.64           C  
ANISOU  843  CA  TYR A 104     1225    878   1180   -349      3    169       C  
ATOM    844  C   TYR A 104      25.901   6.666   9.860  1.00  7.42           C  
ANISOU  844  C   TYR A 104      988    825   1008   -146     15     37       C  
ATOM    845  O   TYR A 104      26.524   7.680  10.209  1.00  8.12           O  
ANISOU  845  O   TYR A 104     1126    776   1182   -243    125     12       O  
ATOM    846  CB  TYR A 104      25.699   4.962  11.677  1.00  8.68           C  
ANISOU  846  CB  TYR A 104     1454    824   1019     12    280     17       C  
ATOM    847  CG  TYR A 104      24.976   4.460  12.900  1.00  8.59           C  
ANISOU  847  CG  TYR A 104     1370    772   1123   -203    229      3       C  
ATOM    848  CD1 TYR A 104      25.672   3.641  13.786  1.00  9.84           C  
ANISOU  848  CD1 TYR A 104     1763    858   1118   -156    226    118       C  
ATOM    849  CD2 TYR A 104      23.651   4.814  13.191  1.00 10.85           C  
ANISOU  849  CD2 TYR A 104     1270   1521   1330   -345    331     31       C  
ATOM    850  CE1 TYR A 104      25.044   3.181  14.926  1.00 11.71           C  
ANISOU  850  CE1 TYR A 104     2085   1066   1298   -340    382    186       C  
ATOM    851  CE2 TYR A 104      23.019   4.344  14.342  1.00 12.82           C  
ANISOU  851  CE2 TYR A 104     1779   1691   1401   -309    591    115       C  
ATOM    852  CZ  TYR A 104      23.728   3.519  15.191  1.00 13.44           C  
ANISOU  852  CZ  TYR A 104     2092   1565   1447   -355    579    177       C  
ATOM    853  OH  TYR A 104      23.140   3.011  16.357  1.00 15.56           O  
ANISOU  853  OH  TYR A 104     2286   2049   1577   -286    642    429       O  
ATOM    854  N   LEU A 105      26.067   6.133   8.620  1.00  8.39           N  
ANISOU  854  N   LEU A 105     1192    908   1086      0     54    -14       N  
ATOM    855  CA  LEU A 105      26.851   6.866   7.611  1.00  7.88           C  
ANISOU  855  CA  LEU A 105     1400    724    870    110    119    -85       C  
ATOM    856  C   LEU A 105      26.121   8.139   7.239  1.00  7.41           C  
ANISOU  856  C   LEU A 105      942    756   1116    -29    100    -54       C  
ATOM    857  O   LEU A 105      26.773   9.188   6.956  1.00  8.23           O  
ANISOU  857  O   LEU A 105     1213    800   1113   -146    -81     82       O  
ATOM    858  CB  LEU A 105      27.077   6.008   6.357  1.00  8.62           C  
ANISOU  858  CB  LEU A 105     1434    782   1058     38     23   -229       C  
ATOM    859  CG  LEU A 105      27.825   4.711   6.598  1.00  9.44           C  
ANISOU  859  CG  LEU A 105     1445    724   1419     58    102   -358       C  
ATOM    860  CD1 LEU A 105      27.995   4.012   5.238  1.00 13.82           C  
ANISOU  860  CD1 LEU A 105     2824   1113   1313    357     36   -500       C  
ATOM    861  CD2 LEU A 105      29.180   4.934   7.237  1.00 11.40           C  
ANISOU  861  CD2 LEU A 105     1199   1182   1950     54     59   -380       C  
ATOM    862  N   GLU A 106      24.791   8.203   7.240  1.00  8.04           N  
ANISOU  862  N   GLU A 106      948   1145    961     18     96   -196       N  
ATOM    863  CA  GLU A 106      24.024   9.446   7.073  1.00  8.87           C  
ANISOU  863  CA  GLU A 106      826   1144   1401     47    -87   -432       C  
ATOM    864  C   GLU A 106      24.389  10.397   8.217  1.00  7.04           C  
ANISOU  864  C   GLU A 106      771    812   1092    -39    -69    -11       C  
ATOM    865  O   GLU A 106      24.644  11.593   8.031  1.00  8.24           O  
ANISOU  865  O   GLU A 106      990    841   1299    -97    -10    -56       O  
ATOM    866  CB  GLU A 106      22.500   9.202   7.029  1.00 11.74           C  
ANISOU  866  CB  GLU A 106      920   1628   1914   -103   -538   -158       C  
ATOM    867  CG  GLU A 106      22.066   8.376   5.835  1.00 16.56           C  
ANISOU  867  CG  GLU A 106     1777   2246   2268   -629   -668   -443       C  
ATOM    868  CD  GLU A 106      20.666   7.822   5.833  1.00 16.01           C  
ANISOU  868  CD  GLU A 106     1890   2376   1816   -913   -382   -198       C  
ATOM    869  OE1 GLU A 106      19.904   7.984   6.828  1.00 20.08           O  
ANISOU  869  OE1 GLU A 106     2312   3232   2084   -723    -88   -502       O  
ATOM    870  OE2 GLU A 106      20.340   7.175   4.817  1.00 19.68           O  
ANISOU  870  OE2 GLU A 106     1991   3281   2205  -1161   -232   -782       O  
ATOM    871  N   PHE A 107      24.437   9.891   9.463  1.00  8.12           N  
ANISOU  871  N   PHE A 107     1061    954   1069     47     80    -69       N  
ATOM    872  CA  PHE A 107      24.740  10.756  10.591  1.00  7.40           C  
ANISOU  872  CA  PHE A 107      947    857   1009   -206    246     10       C  
ATOM    873  C   PHE A 107      26.125  11.356  10.482  1.00  7.24           C  
ANISOU  873  C   PHE A 107      986    746   1019   -111    431   -148       C  
ATOM    874  O   PHE A 107      26.298  12.562  10.731  1.00  7.99           O  
ANISOU  874  O   PHE A 107     1092    754   1188   -130    120   -181       O  
ATOM    875  CB  PHE A 107      24.610   9.993  11.924  1.00  8.43           C  
ANISOU  875  CB  PHE A 107      992   1101   1108   -180    358    155       C  
ATOM    876  CG  PHE A 107      23.209   9.549  12.325  1.00  9.17           C  
ANISOU  876  CG  PHE A 107      985   1198   1300   -264    302    192       C  
ATOM    877  CD1 PHE A 107      23.098   8.466  13.191  1.00 10.38           C  
ANISOU  877  CD1 PHE A 107     1459   1272   1214   -500    343    183       C  
ATOM    878  CD2 PHE A 107      22.049  10.179  11.865  1.00 10.84           C  
ANISOU  878  CD2 PHE A 107      974   1154   1992    -61    331   -138       C  
ATOM    879  CE1 PHE A 107      21.839   8.032  13.613  1.00 11.59           C  
ANISOU  879  CE1 PHE A 107     1465   1369   1568   -450    491    216       C  
ATOM    880  CE2 PHE A 107      20.800   9.757  12.276  1.00 13.08           C  
ANISOU  880  CE2 PHE A 107     1024   1672   2273   -278    276    344       C  
ATOM    881  CZ  PHE A 107      20.720   8.673  13.146  1.00 13.41           C  
ANISOU  881  CZ  PHE A 107     1509   1862   1726   -390    250    201       C  
ATOM    882  N   ILE A 108      27.153  10.581  10.081  1.00  6.94           N  
ANISOU  882  N   ILE A 108      873    919    846     18    152    -71       N  
ATOM    883  CA  ILE A 108      28.485  11.176   9.990  1.00  6.39           C  
ANISOU  883  CA  ILE A 108      867    657    905    -32      4     43       C  
ATOM    884  C   ILE A 108      28.512  12.163   8.829  1.00  6.79           C  
ANISOU  884  C   ILE A 108     1196    746    639   -102     19    -94       C  
ATOM    885  O   ILE A 108      29.207  13.180   8.911  1.00  6.75           O  
ANISOU  885  O   ILE A 108      994    654    918     16     70    -18       O  
ATOM    886  CB  ILE A 108      29.621  10.149   9.936  1.00  6.79           C  
ANISOU  886  CB  ILE A 108      914    844    823      0      8    -60       C  
ATOM    887  CG1 ILE A 108      30.942  10.839  10.332  1.00  8.30           C  
ANISOU  887  CG1 ILE A 108      843   1046   1262     70    -85      5       C  
ATOM    888  CG2 ILE A 108      29.718   9.446   8.580  1.00  7.98           C  
ANISOU  888  CG2 ILE A 108     1209    999    823     13    230   -123       C  
ATOM    889  CD1 ILE A 108      32.116   9.845  10.442  1.00  8.57           C  
ANISOU  889  CD1 ILE A 108      952   1105   1198    173    -95     45       C  
ATOM    890  N   SER A 109      27.761  11.921   7.751  1.00  6.90           N  
ANISOU  890  N   SER A 109      996    912    712    118     71    -13       N  
ATOM    891  CA  SER A 109      27.704  12.884   6.629  1.00  6.44           C  
ANISOU  891  CA  SER A 109      979    871    599     47     74    -25       C  
ATOM    892  C   SER A 109      27.147  14.209   7.111  1.00  6.07           C  
ANISOU  892  C   SER A 109      719    828    760     53    -33    -22       C  
ATOM    893  O   SER A 109      27.629  15.283   6.759  1.00  7.84           O  
ANISOU  893  O   SER A 109      964    839   1174    -71    -64     63       O  
ATOM    894  CB  SER A 109      26.837  12.312   5.521  1.00  7.63           C  
ANISOU  894  CB  SER A 109     1070    859    970     69   -161   -142       C  
ATOM    895  OG  SER A 109      27.434  11.135   4.944  1.00  8.43           O  
ANISOU  895  OG  SER A 109     1273    976    953     31     36   -235       O  
ATOM    896  N   GLU A 110      26.095  14.141   7.947  1.00  7.05           N  
ANISOU  896  N   GLU A 110      862    909    909     78     79   -145       N  
ATOM    897  CA  GLU A 110      25.488  15.344   8.523  1.00  7.35           C  
ANISOU  897  CA  GLU A 110      709    991   1095    -27    117   -301       C  
ATOM    898  C   GLU A 110      26.516  16.101   9.378  1.00  6.91           C  
ANISOU  898  C   GLU A 110      856    826    945   -169     66    -14       C  
ATOM    899  O   GLU A 110      26.618  17.319   9.362  1.00  7.73           O  
ANISOU  899  O   GLU A 110      877    829   1232     18    -21   -155       O  
ATOM    900  CB AGLU A 110      24.290  14.913   9.359  0.42  8.88           C  
ANISOU  900  CB AGLU A 110      735   1100   1540   -157    262   -417       C  
ATOM    901  CB BGLU A 110      24.260  14.922   9.330  0.58  9.24           C  
ANISOU  901  CB BGLU A 110      741   1196   1571   -103    311   -321       C  
ATOM    902  CG AGLU A 110      23.555  16.006  10.089  0.42  9.07           C  
ANISOU  902  CG AGLU A 110      804   1351   1292    -17    196   -468       C  
ATOM    903  CG BGLU A 110      23.171  14.328   8.467  0.58 11.88           C  
ANISOU  903  CG BGLU A 110      713   1668   2135   -145    -91    -37       C  
ATOM    904  CD AGLU A 110      22.566  15.538  11.152  0.42 14.82           C  
ANISOU  904  CD AGLU A 110     1804   1401   2426    453   1212    172       C  
ATOM    905  CD BGLU A 110      22.131  13.422   9.082  0.58 15.55           C  
ANISOU  905  CD BGLU A 110      746   2189   2971   -406   -613    957       C  
ATOM    906  OE1AGLU A 110      21.420  16.055  11.174  0.42 26.23           O  
ANISOU  906  OE1AGLU A 110     1699   3771   4496    888   1844   2428       O  
ATOM    907  OE1BGLU A 110      21.934  13.341  10.317  0.58 21.24           O  
ANISOU  907  OE1BGLU A 110     2742   1845   3484    541   1343    788       O  
ATOM    908  OE2AGLU A 110      22.783  14.684  12.054  0.42 14.12           O  
ANISOU  908  OE2AGLU A 110      897   2533   1936   -341    155    363       O  
ATOM    909  OE2BGLU A 110      21.425  12.720   8.306  0.58 27.83           O  
ANISOU  909  OE2BGLU A 110     1393   3738   5443  -1281   -922   -243       O  
ATOM    910  N   ALA A 111      27.325  15.350  10.133  1.00  6.81           N  
ANISOU  910  N   ALA A 111      727    933    927    -74     96   -104       N  
ATOM    911  CA  ALA A 111      28.325  15.982  11.000  1.00  7.06           C  
ANISOU  911  CA  ALA A 111      860    921    902   -253     26    111       C  
ATOM    912  C   ALA A 111      29.405  16.654  10.177  1.00  6.14           C  
ANISOU  912  C   ALA A 111      826    750    759    -87     66    -65       C  
ATOM    913  O   ALA A 111      29.871  17.766  10.500  1.00  6.93           O  
ANISOU  913  O   ALA A 111      946    698    991   -142    159    -88       O  
ATOM    914  CB  ALA A 111      28.932  14.934  11.944  1.00  7.98           C  
ANISOU  914  CB  ALA A 111     1215   1011    806    182    113     77       C  
ATOM    915  N   ILE A 112      29.826  16.004   9.083  1.00  6.22           N  
ANISOU  915  N   ILE A 112      860    835    669      5    -19    -22       N  
ATOM    916  CA  ILE A 112      30.812  16.588   8.162  1.00  6.22           C  
ANISOU  916  CA  ILE A 112      920    698    744     89     90     19       C  
ATOM    917  C   ILE A 112      30.271  17.898   7.626  1.00  5.66           C  
ANISOU  917  C   ILE A 112      721    619    812     26     53    -37       C  
ATOM    918  O   ILE A 112      30.941  18.955   7.641  1.00  6.40           O  
ANISOU  918  O   ILE A 112      876    661    896   -112     42    -54       O  
ATOM    919  CB  ILE A 112      31.154  15.601   7.032  1.00  6.42           C  
ANISOU  919  CB  ILE A 112     1002    661    774     50     83    -54       C  
ATOM    920  CG1 ILE A 112      31.963  14.432   7.561  1.00  7.96           C  
ANISOU  920  CG1 ILE A 112     1161    664   1200    117    -31    -37       C  
ATOM    921  CG2 ILE A 112      31.926  16.310   5.897  1.00  7.39           C  
ANISOU  921  CG2 ILE A 112      878   1000    932    -21    148     75       C  
ATOM    922  CD1 ILE A 112      31.940  13.223   6.640  1.00  8.41           C  
ANISOU  922  CD1 ILE A 112     1127    903   1168    259    167   -268       C  
ATOM    923  N   ILE A 113      29.015  17.872   7.120  1.00  6.37           N  
ANISOU  923  N   ILE A 113      788    829    804     23     58     97       N  
ATOM    924  CA  ILE A 113      28.427  19.103   6.526  1.00  6.41           C  
ANISOU  924  CA  ILE A 113      771    818    845     79   -126    -83       C  
ATOM    925  C   ILE A 113      28.332  20.174   7.599  1.00  6.30           C  
ANISOU  925  C   ILE A 113      674    832    887    -11    -45   -107       C  
ATOM    926  O   ILE A 113      28.624  21.331   7.355  1.00  7.60           O  
ANISOU  926  O   ILE A 113      870    875   1143    -55    -94    -67       O  
ATOM    927  CB  ILE A 113      27.088  18.743   5.911  1.00  7.31           C  
ANISOU  927  CB  ILE A 113      897    651   1229     83   -271   -135       C  
ATOM    928  CG1 ILE A 113      27.284  17.980   4.602  1.00  9.05           C  
ANISOU  928  CG1 ILE A 113     1370   1214    853   -310   -241    -90       C  
ATOM    929  CG2 ILE A 113      26.227  19.983   5.673  1.00  9.69           C  
ANISOU  929  CG2 ILE A 113      985    812   1884     75   -511    405       C  
ATOM    930  CD1 ILE A 113      26.001  17.367   4.064  1.00 11.70           C  
ANISOU  930  CD1 ILE A 113     1542   1217   1685   -262   -700   -150       C  
ATOM    931  N   HIS A 114      27.917  19.820   8.810  1.00  6.65           N  
ANISOU  931  N   HIS A 114      737    904    887    132     19   -205       N  
ATOM    932  CA  HIS A 114      27.784  20.799   9.886  1.00  7.67           C  
ANISOU  932  CA  HIS A 114      925    980   1010   -135    186   -290       C  
ATOM    933  C   HIS A 114      29.097  21.497  10.180  1.00  6.47           C  
ANISOU  933  C   HIS A 114      885    570   1004      2    159    -84       C  
ATOM    934  O   HIS A 114      29.159  22.710  10.362  1.00  6.70           O  
ANISOU  934  O   HIS A 114      921    656    971     44     18   -144       O  
ATOM    935  CB AHIS A 114      27.153  20.128  11.110  0.51  9.23           C  
ANISOU  935  CB AHIS A 114     1160   1030   1315   -195    708   -399       C  
ATOM    936  CB BHIS A 114      27.362  20.104  11.201  0.49 10.56           C  
ANISOU  936  CB BHIS A 114     1611   1110   1290   -404    949   -452       C  
ATOM    937  CG AHIS A 114      26.559  21.205  11.974  0.51 10.60           C  
ANISOU  937  CG AHIS A 114     1263   1147   1616   -114    741   -501       C  
ATOM    938  CG BHIS A 114      27.431  20.957  12.442  0.49  9.45           C  
ANISOU  938  CG BHIS A 114     1224   1219   1146    131    619   -334       C  
ATOM    939  ND1AHIS A 114      25.279  21.672  11.960  0.51 10.95           N  
ANISOU  939  ND1AHIS A 114     1503    837   1819     84    575   -481       N  
ATOM    940  ND1BHIS A 114      26.321  21.673  12.833  0.49 11.25           N  
ANISOU  940  ND1BHIS A 114     1556   1164   1555    490    365   -448       N  
ATOM    941  CD2AHIS A 114      27.207  21.930  12.924  0.51 10.62           C  
ANISOU  941  CD2AHIS A 114     1636   1282   1115    317    485   -430       C  
ATOM    942  CD2BHIS A 114      28.346  21.242  13.392  0.49 10.43           C  
ANISOU  942  CD2BHIS A 114     1704   1373    887    515    319    -33       C  
ATOM    943  CE1AHIS A 114      25.128  22.621  12.866  0.51  9.91           C  
ANISOU  943  CE1AHIS A 114     1381    635   1750   -160    627   -400       C  
ATOM    944  CE1BHIS A 114      26.551  22.362  13.936  0.49 12.14           C  
ANISOU  944  CE1BHIS A 114     1883   1556   1174    496    674   -379       C  
ATOM    945  NE2AHIS A 114      26.298  22.799  13.470  0.51 11.95           N  
ANISOU  945  NE2AHIS A 114     1519   1453   1570    318    455   -587       N  
ATOM    946  NE2BHIS A 114      27.784  22.120  14.304  0.49 13.05           N  
ANISOU  946  NE2BHIS A 114     1958   1850   1151    336    392   -489       N  
ATOM    947  N   VAL A 115      30.162  20.712  10.320  1.00  6.52           N  
ANISOU  947  N   VAL A 115      849    844    784    109     82   -183       N  
ATOM    948  CA  VAL A 115      31.460  21.287  10.673  1.00  6.86           C  
ANISOU  948  CA  VAL A 115      799    893    915     59    136    -18       C  
ATOM    949  C   VAL A 115      32.027  22.109   9.531  1.00  6.73           C  
ANISOU  949  C   VAL A 115     1049    694    816     -6    -81    -47       C  
ATOM    950  O   VAL A 115      32.601  23.199   9.758  1.00  7.43           O  
ANISOU  950  O   VAL A 115     1106    780    936    -90   -139    -52       O  
ATOM    951  CB  VAL A 115      32.432  20.143  11.057  1.00  6.87           C  
ANISOU  951  CB  VAL A 115      753    898    959    -66     87    197       C  
ATOM    952  CG1 VAL A 115      33.869  20.641  11.190  1.00  8.44           C  
ANISOU  952  CG1 VAL A 115      810   1370   1026   -168   -187    156       C  
ATOM    953  CG2 VAL A 115      31.975  19.548  12.398  1.00  8.62           C  
ANISOU  953  CG2 VAL A 115     1401   1087    786   -135    215     84       C  
ATOM    954  N   LEU A 116      31.880  21.644   8.282  1.00  6.43           N  
ANISOU  954  N   LEU A 116      687   1029    730    145    -97    -10       N  
ATOM    955  CA  LEU A 116      32.348  22.508   7.170  1.00  6.96           C  
ANISOU  955  CA  LEU A 116     1093    740    812    110    -14    -33       C  
ATOM    956  C   LEU A 116      31.547  23.792   7.083  1.00  6.10           C  
ANISOU  956  C   LEU A 116      805    748    765    -49   -174   -207       C  
ATOM    957  O   LEU A 116      32.128  24.842   6.783  1.00  7.09           O  
ANISOU  957  O   LEU A 116     1049    774    870   -150    -28   -132       O  
ATOM    958  CB  LEU A 116      32.259  21.713   5.848  1.00  6.78           C  
ANISOU  958  CB  LEU A 116      901    827    848    122    158   -101       C  
ATOM    959  CG  LEU A 116      33.129  20.469   5.811  1.00  9.91           C  
ANISOU  959  CG  LEU A 116     1312   1233   1220    557   -533   -513       C  
ATOM    960  CD1 LEU A 116      33.068  19.839   4.416  1.00 11.37           C  
ANISOU  960  CD1 LEU A 116     2141   1166   1012    681   -191   -302       C  
ATOM    961  CD2 LEU A 116      34.545  20.703   6.170  1.00 17.30           C  
ANISOU  961  CD2 LEU A 116     1116   1929   3528    561   -474  -1547       C  
ATOM    962  N   HIS A 117      30.231  23.699   7.337  1.00  6.95           N  
ANISOU  962  N   HIS A 117      784    863    993    119    -94     23       N  
ATOM    963  CA  HIS A 117      29.425  24.928   7.308  1.00  6.89           C  
ANISOU  963  CA  HIS A 117      939    609   1068     47   -154   -143       C  
ATOM    964  C   HIS A 117      29.893  25.923   8.350  1.00  7.27           C  
ANISOU  964  C   HIS A 117      958    832    973    -41    -50   -115       C  
ATOM    965  O   HIS A 117      29.940  27.144   8.094  1.00  8.60           O  
ANISOU  965  O   HIS A 117     1226    731   1312    -60    119   -217       O  
ATOM    966  CB  HIS A 117      27.953  24.512   7.493  1.00  7.63           C  
ANISOU  966  CB  HIS A 117      841    673   1386    110     -9   -110       C  
ATOM    967  CG  HIS A 117      27.022  25.683   7.672  1.00  8.63           C  
ANISOU  967  CG  HIS A 117     1103    707   1469    159     -9   -163       C  
ATOM    968  ND1 HIS A 117      26.666  26.179   8.891  1.00 10.22           N  
ANISOU  968  ND1 HIS A 117     1184   1090   1610    288    180   -235       N  
ATOM    969  CD2 HIS A 117      26.421  26.423   6.737  1.00 10.22           C  
ANISOU  969  CD2 HIS A 117     1132    993   1760    366   -241   -163       C  
ATOM    970  CE1 HIS A 117      25.856  27.206   8.703  1.00 11.14           C  
ANISOU  970  CE1 HIS A 117     1297   1004   1932    303    187   -115       C  
ATOM    971  NE2 HIS A 117      25.691  27.382   7.397  1.00 11.55           N  
ANISOU  971  NE2 HIS A 117     1099   1315   1976    460   -415   -543       N  
ATOM    972  N   SER A 118      30.233  25.455   9.554  1.00  6.93           N  
ANISOU  972  N   SER A 118      760   1069    802    -17    106   -275       N  
ATOM    973  CA  SER A 118      30.678  26.296  10.636  1.00  8.22           C  
ANISOU  973  CA  SER A 118      962   1292    872   -192    107   -373       C  
ATOM    974  C   SER A 118      32.072  26.852  10.376  1.00  6.92           C  
ANISOU  974  C   SER A 118      969    874    786    -44     32   -187       C  
ATOM    975  O   SER A 118      32.305  28.045  10.620  1.00  8.22           O  
ANISOU  975  O   SER A 118      948    835   1341    -23    -21   -233       O  
ATOM    976  CB ASER A 118      30.711  25.485  11.951  0.51  9.83           C  
ANISOU  976  CB ASER A 118     1243   1760    732   -566    236   -331       C  
ATOM    977  CB BSER A 118      30.601  25.598  11.997  0.21  9.94           C  
ANISOU  977  CB BSER A 118     1343   1685    750   -453    339   -418       C  
ATOM    978  CB CSER A 118      30.779  25.502  11.950  0.28 10.43           C  
ANISOU  978  CB CSER A 118     1538   1745    679   -519    324   -326       C  
ATOM    979  OG ASER A 118      31.156  26.392  12.950  0.51  9.97           O  
ANISOU  979  OG ASER A 118     1680   1326    783   -249    222   -353       O  
ATOM    980  OG BSER A 118      31.443  24.479  12.057  0.21 13.49           O  
ANISOU  980  OG BSER A 118     3231    989    903   -242    363   -152       O  
ATOM    981  OG CSER A 118      29.577  24.935  12.403  0.28 14.21           O  
ANISOU  981  OG CSER A 118     1945   2468    985  -1107    432   -459       O  
ATOM    982  N   ARG A 119      33.000  26.015   9.982  1.00  6.08           N  
ANISOU  982  N   ARG A 119      795    844    672     17     13    -25       N  
ATOM    983  CA  ARG A 119      34.401  26.450   9.877  1.00  6.24           C  
ANISOU  983  CA  ARG A 119      855    629    888    -17   -105     74       C  
ATOM    984  C   ARG A 119      34.695  27.183   8.580  1.00  5.70           C  
ANISOU  984  C   ARG A 119      812    555    799    -84      5   -104       C  
ATOM    985  O   ARG A 119      35.616  28.008   8.574  1.00  6.88           O  
ANISOU  985  O   ARG A 119      961    937    718   -302    -51      3       O  
ATOM    986  CB AARG A 119      35.333  25.219   9.992  0.60  7.04           C  
ANISOU  986  CB AARG A 119      992    899    783    254    -25    -41       C  
ATOM    987  CB BARG A 119      35.349  25.244   9.883  0.40  7.51           C  
ANISOU  987  CB BARG A 119      940    960    952    257   -230     18       C  
ATOM    988  CG AARG A 119      35.261  24.547  11.369  0.60  6.14           C  
ANISOU  988  CG AARG A 119      869    714    752    234   -148    -86       C  
ATOM    989  CG BARG A 119      35.780  24.714  11.244  0.40  6.50           C  
ANISOU  989  CG BARG A 119      581    920    971    181   -212    -30       C  
ATOM    990  CD AARG A 119      36.286  23.448  11.530  0.60  8.29           C  
ANISOU  990  CD AARG A 119      806    934   1411    266    -18    155       C  
ATOM    991  CD BARG A 119      36.549  23.424  11.016  0.40  7.38           C  
ANISOU  991  CD BARG A 119      813    931   1061    251   -331    -55       C  
ATOM    992  NE AARG A 119      37.682  23.869  11.498  0.60  9.34           N  
ANISOU  992  NE AARG A 119      785    967   1796    293    -34   -266       N  
ATOM    993  NE BARG A 119      37.137  22.902  12.238  0.40  6.81           N  
ANISOU  993  NE BARG A 119      911    534   1143     33   -434    -29       N  
ATOM    994  CZ AARG A 119      38.668  23.414  12.248  0.60  8.27           C  
ANISOU  994  CZ AARG A 119      858    778   1508    -39   -105   -106       C  
ATOM    995  CZ BARG A 119      38.405  23.070  12.612  0.40  7.64           C  
ANISOU  995  CZ BARG A 119      861    721   1319     35   -440    490       C  
ATOM    996  NH1AARG A 119      39.887  23.910  12.082  0.60 10.19           N  
ANISOU  996  NH1AARG A 119      939   2005    928   -416   -148     -5       N  
ATOM    997  NH1BARG A 119      38.842  22.535  13.761  0.40  9.20           N  
ANISOU  997  NH1BARG A 119     1329    983   1184    595   -446    318       N  
ATOM    998  NH2AARG A 119      38.491  22.472  13.173  0.60 12.17           N  
ANISOU  998  NH2AARG A 119     1457   1474   1692   -296    -23    263       N  
ATOM    999  NH2BARG A 119      39.255  23.759  11.864  0.40  6.52           N  
ANISOU  999  NH2BARG A 119     1069    614    793    -71     26   -412       N  
ATOM   1000  N   HIS A 120      33.976  26.867   7.499  1.00  6.00           N  
ANISOU 1000  N   HIS A 120      715    750    815    -76    -42     18       N  
ATOM   1001  CA  HIS A 120      34.406  27.293   6.173  1.00  6.39           C  
ANISOU 1001  CA  HIS A 120      916    768    745      9    -65     23       C  
ATOM   1002  C   HIS A 120      33.327  28.023   5.405  1.00  5.97           C  
ANISOU 1002  C   HIS A 120      866    658    744    -49    -28      4       C  
ATOM   1003  O   HIS A 120      33.051  27.696   4.242  1.00  7.71           O  
ANISOU 1003  O   HIS A 120     1203    957    770    -46   -193    -29       O  
ATOM   1004  CB  HIS A 120      34.885  26.082   5.344  1.00  7.84           C  
ANISOU 1004  CB  HIS A 120     1124    901    953    207   -104   -177       C  
ATOM   1005  CG  HIS A 120      36.146  25.561   5.974  1.00  6.76           C  
ANISOU 1005  CG  HIS A 120     1110    657    802     42     61     65       C  
ATOM   1006  ND1 HIS A 120      37.282  26.345   6.081  1.00  7.72           N  
ANISOU 1006  ND1 HIS A 120     1063    699   1170     85    153   -120       N  
ATOM   1007  CD2 HIS A 120      36.419  24.401   6.616  1.00  6.71           C  
ANISOU 1007  CD2 HIS A 120      920    778    853    135    226     69       C  
ATOM   1008  CE1 HIS A 120      38.202  25.650   6.732  1.00  7.95           C  
ANISOU 1008  CE1 HIS A 120     1147    630   1244    104     41    -22       C  
ATOM   1009  NE2 HIS A 120      37.715  24.454   7.082  1.00  6.96           N  
ANISOU 1009  NE2 HIS A 120      918    757    968     23     41   -107       N  
ATOM   1010  N   PRO A 121      32.731  29.093   5.938  1.00  7.01           N  
ANISOU 1010  N   PRO A 121     1068    686    911      0   -169    -70       N  
ATOM   1011  CA  PRO A 121      31.707  29.796   5.137  1.00  7.61           C  
ANISOU 1011  CA  PRO A 121      995    799   1097    124    -64    -66       C  
ATOM   1012  C   PRO A 121      32.306  30.394   3.864  1.00  8.31           C  
ANISOU 1012  C   PRO A 121     1190   1033    932     80   -283     32       C  
ATOM   1013  O   PRO A 121      31.517  30.551   2.896  1.00 11.40           O  
ANISOU 1013  O   PRO A 121     1494   1588   1249    208   -435     41       O  
ATOM   1014  CB  PRO A 121      31.181  30.843   6.110  1.00  9.80           C  
ANISOU 1014  CB  PRO A 121     1532   1171   1021    377   -278   -308       C  
ATOM   1015  CG  PRO A 121      32.314  31.041   7.089  1.00  8.99           C  
ANISOU 1015  CG  PRO A 121     1397    827   1193    153   -318   -114       C  
ATOM   1016  CD  PRO A 121      32.946  29.675   7.257  1.00  8.13           C  
ANISOU 1016  CD  PRO A 121     1461    809    818    150    -71   -122       C  
ATOM   1017  N   GLY A 122      33.610  30.643   3.791  1.00  8.43           N  
ANISOU 1017  N   GLY A 122     1316    819   1068   -255    -77     -9       N  
ATOM   1018  CA  GLY A 122      34.209  31.143   2.554  1.00 10.07           C  
ANISOU 1018  CA  GLY A 122     1976    896    954   -196     28      2       C  
ATOM   1019  C   GLY A 122      34.188  30.132   1.413  1.00  9.57           C  
ANISOU 1019  C   GLY A 122     1655   1030    952    -81   -321    -11       C  
ATOM   1020  O   GLY A 122      34.323  30.509   0.232  1.00 11.17           O  
ANISOU 1020  O   GLY A 122     1964   1315    964    -92   -123     39       O  
ATOM   1021  N   ASN A 123      34.092  28.846   1.727  1.00  8.02           N  
ANISOU 1021  N   ASN A 123      997    959   1089   -133     81   -123       N  
ATOM   1022  CA  ASN A 123      34.185  27.820   0.710  1.00  8.62           C  
ANISOU 1022  CA  ASN A 123     1048   1208   1017   -120    144   -258       C  
ATOM   1023  C   ASN A 123      33.029  26.839   0.864  1.00  7.53           C  
ANISOU 1023  C   ASN A 123     1040   1034    789    -72    -54   -103       C  
ATOM   1024  O   ASN A 123      33.033  25.757   0.301  1.00  9.41           O  
ANISOU 1024  O   ASN A 123     1140   1221   1215     44   -215   -391       O  
ATOM   1025  CB  ASN A 123      35.512  27.054   0.779  1.00  9.75           C  
ANISOU 1025  CB  ASN A 123     1098   1197   1410     -5    219     15       C  
ATOM   1026  CG  ASN A 123      36.649  27.944   0.277  1.00 12.62           C  
ANISOU 1026  CG  ASN A 123     1072   2102   1620   -367     92    102       C  
ATOM   1027  OD1 ASN A 123      37.401  28.480   1.098  1.00 14.99           O  
ANISOU 1027  OD1 ASN A 123     1489   1749   2457   -285   -214   -441       O  
ATOM   1028  ND2 ASN A 123      36.742  28.106  -1.035  1.00 12.74           N  
ANISOU 1028  ND2 ASN A 123     1705   1473   1660   -376    620   -179       N  
ATOM   1029  N   PHE A 124      32.013  27.219   1.630  1.00  7.63           N  
ANISOU 1029  N   PHE A 124     1109   1016    772   -225     61   -150       N  
ATOM   1030  CA  PHE A 124      30.902  26.299   1.902  1.00  6.66           C  
ANISOU 1030  CA  PHE A 124     1050    667    813    -68     -3   -172       C  
ATOM   1031  C   PHE A 124      29.590  27.059   1.932  1.00  7.76           C  
ANISOU 1031  C   PHE A 124     1140    709   1101    -56    -81    -84       C  
ATOM   1032  O   PHE A 124      28.787  26.884   2.870  1.00  8.61           O  
ANISOU 1032  O   PHE A 124      980   1076   1215     -3      9    -86       O  
ATOM   1033  CB  PHE A 124      31.148  25.510   3.181  1.00  7.29           C  
ANISOU 1033  CB  PHE A 124     1030    752    987   -175   -157    -85       C  
ATOM   1034  CG  PHE A 124      30.525  24.097   3.157  1.00  6.50           C  
ANISOU 1034  CG  PHE A 124      919    719    832   -106    -93    -73       C  
ATOM   1035  CD1 PHE A 124      31.060  23.154   2.280  1.00  7.23           C  
ANISOU 1035  CD1 PHE A 124      788    829   1130     90   -224   -192       C  
ATOM   1036  CD2 PHE A 124      29.494  23.749   3.971  1.00  6.97           C  
ANISOU 1036  CD2 PHE A 124      748    912    989   -129   -205    -38       C  
ATOM   1037  CE1 PHE A 124      30.572  21.858   2.236  1.00  7.38           C  
ANISOU 1037  CE1 PHE A 124     1019    928    856    -13    -36   -294       C  
ATOM   1038  CE2 PHE A 124      29.002  22.461   3.978  1.00  7.04           C  
ANISOU 1038  CE2 PHE A 124      926    847    902   -145     14   -112       C  
ATOM   1039  CZ  PHE A 124      29.570  21.486   3.128  1.00  7.59           C  
ANISOU 1039  CZ  PHE A 124     1002   1063    821     -8    -42   -170       C  
ATOM   1040  N   GLY A 125      29.374  27.898   0.928  1.00  8.84           N  
ANISOU 1040  N   GLY A 125     1391    801   1166     95    -11      4       N  
ATOM   1041  CA  GLY A 125      28.043  28.465   0.697  1.00 10.35           C  
ANISOU 1041  CA  GLY A 125     1478    766   1687    108   -369   -134       C  
ATOM   1042  C   GLY A 125      27.089  27.412   0.166  1.00  7.91           C  
ANISOU 1042  C   GLY A 125     1320    732    954    278   -201    -93       C  
ATOM   1043  O   GLY A 125      27.353  26.215   0.151  1.00  7.99           O  
ANISOU 1043  O   GLY A 125     1248    664   1122    155   -200   -120       O  
ATOM   1044  N   ALA A 126      25.873  27.832  -0.213  1.00  9.68           N  
ANISOU 1044  N   ALA A 126     1365   1150   1162    404   -342    -77       N  
ATOM   1045  CA  ALA A 126      24.834  26.882  -0.528  1.00  9.12           C  
ANISOU 1045  CA  ALA A 126     1146    969   1349    487   -184   -212       C  
ATOM   1046  C   ALA A 126      25.220  25.981  -1.685  1.00  8.28           C  
ANISOU 1046  C   ALA A 126     1350    663   1133    552   -137    176       C  
ATOM   1047  O   ALA A 126      24.987  24.751  -1.617  1.00  8.35           O  
ANISOU 1047  O   ALA A 126     1235    714   1224    314   -132     18       O  
ATOM   1048  CB  ALA A 126      23.508  27.604  -0.855  1.00 10.78           C  
ANISOU 1048  CB  ALA A 126     1262   1559   1275    742   -180   -288       C  
ATOM   1049  N   ASP A 127      25.792  26.482  -2.755  1.00  8.75           N  
ANISOU 1049  N   ASP A 127     1333    838   1152    264    -95     51       N  
ATOM   1050  CA  ASP A 127      26.114  25.624  -3.897  1.00  8.66           C  
ANISOU 1050  CA  ASP A 127     1475    772   1043    428   -177    136       C  
ATOM   1051  C   ASP A 127      27.182  24.627  -3.484  1.00  7.30           C  
ANISOU 1051  C   ASP A 127     1220    710    845    184   -238     16       C  
ATOM   1052  O   ASP A 127      27.136  23.467  -3.873  1.00  7.66           O  
ANISOU 1052  O   ASP A 127     1129    715   1068    275   -154    -22       O  
ATOM   1053  CB  ASP A 127      26.587  26.435  -5.090  1.00 10.56           C  
ANISOU 1053  CB  ASP A 127     1962   1079    971    154   -232    215       C  
ATOM   1054  CG  ASP A 127      25.475  27.233  -5.740  1.00 14.93           C  
ANISOU 1054  CG  ASP A 127     2525   1703   1444    346   -625    618       C  
ATOM   1055  OD1 ASP A 127      25.841  28.163  -6.476  1.00 26.74           O  
ANISOU 1055  OD1 ASP A 127     3902   2354   3906    -75  -1105   2067       O  
ATOM   1056  OD2 ASP A 127      24.280  26.915  -5.556  1.00 15.74           O  
ANISOU 1056  OD2 ASP A 127     2260   2063   1655    730   -644    130       O  
ATOM   1057  N   ALA A 128      28.208  25.083  -2.730  1.00  7.41           N  
ANISOU 1057  N   ALA A 128     1118   1083    615    192    -90   -111       N  
ATOM   1058  CA  ALA A 128      29.284  24.167  -2.313  1.00  7.64           C  
ANISOU 1058  CA  ALA A 128      868    979   1055    -21    -41     92       C  
ATOM   1059  C   ALA A 128      28.741  23.096  -1.362  1.00  6.97           C  
ANISOU 1059  C   ALA A 128     1050    718    879     54     14   -156       C  
ATOM   1060  O   ALA A 128      29.121  21.942  -1.436  1.00  7.52           O  
ANISOU 1060  O   ALA A 128      977    825   1058    236    -83    -70       O  
ATOM   1061  CB  ALA A 128      30.441  24.957  -1.691  1.00  9.02           C  
ANISOU 1061  CB  ALA A 128     1141    947   1339    -61   -255     -3       C  
ATOM   1062  N   GLN A 129      27.806  23.500  -0.478  1.00  6.87           N  
ANISOU 1062  N   GLN A 129      948    895    766    145    -56      3       N  
ATOM   1063  CA  GLN A 129      27.253  22.481   0.420  1.00  6.85           C  
ANISOU 1063  CA  GLN A 129      867    894    841    178     40   -122       C  
ATOM   1064  C   GLN A 129      26.407  21.499  -0.364  1.00  7.13           C  
ANISOU 1064  C   GLN A 129      962    762    984    217    -83    -78       C  
ATOM   1065  O   GLN A 129      26.436  20.286  -0.094  1.00  7.80           O  
ANISOU 1065  O   GLN A 129     1250    787    926    263     94    -14       O  
ATOM   1066  CB  GLN A 129      26.453  23.176   1.536  1.00  7.96           C  
ANISOU 1066  CB  GLN A 129     1244    859    923    280    209   -126       C  
ATOM   1067  CG  GLN A 129      25.727  22.168   2.409  1.00  8.39           C  
ANISOU 1067  CG  GLN A 129     1252   1064    873    181    175     -5       C  
ATOM   1068  CD  GLN A 129      25.057  22.808   3.628  1.00  8.16           C  
ANISOU 1068  CD  GLN A 129     1162   1014    924    297     71    -26       C  
ATOM   1069  OE1 GLN A 129      25.493  23.843   4.095  1.00 10.23           O  
ANISOU 1069  OE1 GLN A 129     1685   1123   1080    341   -116   -193       O  
ATOM   1070  NE2 GLN A 129      24.024  22.145   4.132  1.00  8.67           N  
ANISOU 1070  NE2 GLN A 129      838   1492    965    526     -9    255       N  
ATOM   1071  N   GLY A 130      25.671  21.972  -1.389  1.00  7.10           N  
ANISOU 1071  N   GLY A 130      843    940    914    171    -83    -99       N  
ATOM   1072  CA  GLY A 130      24.907  21.006  -2.188  1.00  7.64           C  
ANISOU 1072  CA  GLY A 130      999    846   1058    205   -122   -261       C  
ATOM   1073  C   GLY A 130      25.834  20.026  -2.899  1.00  6.89           C  
ANISOU 1073  C   GLY A 130      900    733    985    287   -151     20       C  
ATOM   1074  O   GLY A 130      25.491  18.838  -3.023  1.00  7.90           O  
ANISOU 1074  O   GLY A 130     1115    744   1141    237   -152    -58       O  
ATOM   1075  N   ALA A 131      26.978  20.509  -3.401  1.00  7.00           N  
ANISOU 1075  N   ALA A 131      913    824    925    320   -162     49       N  
ATOM   1076  CA  ALA A 131      27.930  19.619  -4.089  1.00  6.17           C  
ANISOU 1076  CA  ALA A 131      919    639    786    107    -83     80       C  
ATOM   1077  C   ALA A 131      28.491  18.599  -3.104  1.00  6.14           C  
ANISOU 1077  C   ALA A 131      927    643    764    236   -246    -95       C  
ATOM   1078  O   ALA A 131      28.602  17.399  -3.440  1.00  6.35           O  
ANISOU 1078  O   ALA A 131      904    663    844    148   -117    -60       O  
ATOM   1079  CB  ALA A 131      29.050  20.406  -4.708  1.00  7.82           C  
ANISOU 1079  CB  ALA A 131     1027    741   1203    -34    -38     83       C  
ATOM   1080  N   MET A 132      28.858  19.030  -1.897  1.00  6.12           N  
ANISOU 1080  N   MET A 132      873    844    609    109    -96     15       N  
ATOM   1081  CA  MET A 132      29.345  18.048  -0.895  1.00  5.91           C  
ANISOU 1081  CA  MET A 132      965    646    636    -71    -97    -14       C  
ATOM   1082  C   MET A 132      28.259  17.048  -0.556  1.00  5.77           C  
ANISOU 1082  C   MET A 132      714    582    898     33    -73   -174       C  
ATOM   1083  O   MET A 132      28.525  15.836  -0.411  1.00  6.46           O  
ANISOU 1083  O   MET A 132     1002    546    908    111     32   -107       O  
ATOM   1084  CB  MET A 132      29.845  18.808   0.325  1.00  6.41           C  
ANISOU 1084  CB  MET A 132     1052    621    764     -3   -302    -93       C  
ATOM   1085  CG  MET A 132      30.378  17.899   1.437  1.00  6.89           C  
ANISOU 1085  CG  MET A 132     1197    761    661    272    -63    -59       C  
ATOM   1086  SD  MET A 132      31.807  16.869   0.967  1.00  8.09           S  
ANISOU 1086  SD  MET A 132     1022    983   1071    177   -147    -82       S  
ATOM   1087  CE  MET A 132      33.075  18.145   0.998  1.00  9.82           C  
ANISOU 1087  CE  MET A 132     1280   1311   1138   -136     85   -455       C  
ATOM   1088  N   ASN A 133      27.033  17.520  -0.359  1.00  6.74           N  
ANISOU 1088  N   ASN A 133      735    851    973     83   -125    -30       N  
ATOM   1089  CA  ASN A 133      25.949  16.583  -0.092  1.00  6.80           C  
ANISOU 1089  CA  ASN A 133      622    889   1075     77     41   -271       C  
ATOM   1090  C   ASN A 133      25.822  15.572  -1.236  1.00  7.15           C  
ANISOU 1090  C   ASN A 133      977    747    991    201   -133   -144       C  
ATOM   1091  O   ASN A 133      25.662  14.384  -0.962  1.00  7.33           O  
ANISOU 1091  O   ASN A 133      871    750   1163    125    -45    -51       O  
ATOM   1092  CB  ASN A 133      24.629  17.338   0.122  1.00  8.20           C  
ANISOU 1092  CB  ASN A 133      711    836   1570    226    -31   -121       C  
ATOM   1093  CG  ASN A 133      23.517  16.315   0.362  1.00  8.62           C  
ANISOU 1093  CG  ASN A 133      642   1029   1603    269    230    -93       C  
ATOM   1094  OD1 ASN A 133      23.579  15.509   1.283  1.00 11.10           O  
ANISOU 1094  OD1 ASN A 133     1088    978   2151    248    428    154       O  
ATOM   1095  ND2 ASN A 133      22.534  16.364  -0.513  1.00 11.31           N  
ANISOU 1095  ND2 ASN A 133      794   1414   2090    189   -140   -604       N  
ATOM   1096  N   LYS A 134      25.912  16.040  -2.491  1.00  7.35           N  
ANISOU 1096  N   LYS A 134      907    870   1016    154    -66   -140       N  
ATOM   1097  CA  LYS A 134      25.795  15.088  -3.594  1.00  7.78           C  
ANISOU 1097  CA  LYS A 134     1101    923    933    318    -13   -107       C  
ATOM   1098  C   LYS A 134      26.930  14.068  -3.534  1.00  6.51           C  
ANISOU 1098  C   LYS A 134      943    668    863     57    -70    -64       C  
ATOM   1099  O   LYS A 134      26.717  12.879  -3.786  1.00  7.58           O  
ANISOU 1099  O   LYS A 134     1238    716    926     87    -21   -186       O  
ATOM   1100  CB  LYS A 134      25.828  15.873  -4.912  1.00 10.57           C  
ANISOU 1100  CB  LYS A 134     1478   1457   1082    130   -363    277       C  
ATOM   1101  CG  LYS A 134      25.182  15.179  -6.086  1.00 16.41           C  
ANISOU 1101  CG  LYS A 134     2453   2510   1273   -556   -642    364       C  
ATOM   1102  CD  LYS A 134      24.916  16.208  -7.193  1.00 17.69           C  
ANISOU 1102  CD  LYS A 134     2455   3191   1074   -605   -470    685       C  
ATOM   1103  CE  LYS A 134      24.879  15.512  -8.540  1.00 23.85           C  
ANISOU 1103  CE  LYS A 134     3264   4525   1274   -569   -508    143       C  
ATOM   1104  NZ  LYS A 134      24.499  16.528  -9.546  1.00 34.65           N  
ANISOU 1104  NZ  LYS A 134     5580   6017   1569  -3000  -1719   1648       N  
ATOM   1105  N   ALA A 135      28.168  14.499  -3.242  1.00  7.02           N  
ANISOU 1105  N   ALA A 135      901    794    972    125     -1    -71       N  
ATOM   1106  CA  ALA A 135      29.297  13.580  -3.166  1.00  6.30           C  
ANISOU 1106  CA  ALA A 135      810    711    873     87    116    -56       C  
ATOM   1107  C   ALA A 135      29.106  12.573  -2.060  1.00  7.97           C  
ANISOU 1107  C   ALA A 135     1584    655    789      3     14    -86       C  
ATOM   1108  O   ALA A 135      29.411  11.371  -2.212  1.00  7.41           O  
ANISOU 1108  O   ALA A 135     1196    723    898     75     68    -11       O  
ATOM   1109  CB  ALA A 135      30.590  14.367  -2.932  1.00  7.53           C  
ANISOU 1109  CB  ALA A 135      941    829   1093     47    -74    -98       C  
ATOM   1110  N   LEU A 136      28.598  13.032  -0.895  1.00  6.86           N  
ANISOU 1110  N   LEU A 136     1035    821    749     15      5     49       N  
ATOM   1111  CA  LEU A 136      28.387  12.090   0.219  1.00  7.24           C  
ANISOU 1111  CA  LEU A 136     1332    799    622   -115    -89    -11       C  
ATOM   1112  C   LEU A 136      27.206  11.162  -0.060  1.00  6.84           C  
ANISOU 1112  C   LEU A 136     1252    588    759     10     45   -177       C  
ATOM   1113  O   LEU A 136      27.251   9.993   0.339  1.00  8.01           O  
ANISOU 1113  O   LEU A 136     1399    656    987     45    109    -87       O  
ATOM   1114  CB  LEU A 136      28.167  12.873   1.507  1.00  6.73           C  
ANISOU 1114  CB  LEU A 136      958    912    688    -56   -133   -100       C  
ATOM   1115  CG  LEU A 136      29.416  13.641   1.953  1.00  7.67           C  
ANISOU 1115  CG  LEU A 136      801   1088   1027    200   -293   -310       C  
ATOM   1116  CD1 LEU A 136      29.133  14.495   3.197  1.00 10.34           C  
ANISOU 1116  CD1 LEU A 136     1679   1268    981   -370    134   -451       C  
ATOM   1117  CD2 LEU A 136      30.586  12.691   2.223  1.00 13.45           C  
ANISOU 1117  CD2 LEU A 136     1177   1430   2502    400   -923   -427       C  
ATOM   1118  N   GLU A 137      26.163  11.652  -0.746  1.00  7.66           N  
ANISOU 1118  N   GLU A 137      910    897   1102     24    156     -7       N  
ATOM   1119  CA  GLU A 137      25.058  10.770  -1.153  1.00  7.44           C  
ANISOU 1119  CA  GLU A 137     1054    760   1013     -6    122     79       C  
ATOM   1120  C   GLU A 137      25.572   9.708  -2.104  1.00  8.08           C  
ANISOU 1120  C   GLU A 137     1147    816   1108     82    141     96       C  
ATOM   1121  O   GLU A 137      25.138   8.539  -2.026  1.00  7.83           O  
ANISOU 1121  O   GLU A 137     1083    754   1140     16    -47     30       O  
ATOM   1122  CB  GLU A 137      23.925  11.595  -1.786  1.00  9.31           C  
ANISOU 1122  CB  GLU A 137     1144   1260   1134    292    -18   -106       C  
ATOM   1123  CG  GLU A 137      23.054  12.330  -0.818  1.00 11.95           C  
ANISOU 1123  CG  GLU A 137     1393   1544   1605    383     35   -532       C  
ATOM   1124  CD  GLU A 137      21.902  13.142  -1.389  1.00 16.78           C  
ANISOU 1124  CD  GLU A 137     1480   2378   2516    826    117    -39       C  
ATOM   1125  OE1 GLU A 137      21.080  13.610  -0.591  1.00 19.67           O  
ANISOU 1125  OE1 GLU A 137     1236   2610   3627    371    445   -481       O  
ATOM   1126  OE2 GLU A 137      21.850  13.335  -2.599  1.00 22.25           O  
ANISOU 1126  OE2 GLU A 137     2777   3109   2569   1159   -597     21       O  
ATOM   1127  N   LEU A 138      26.477  10.041  -3.021  1.00  7.17           N  
ANISOU 1127  N   LEU A 138      934    780   1009     83     57    -83       N  
ATOM   1128  CA  LEU A 138      27.029   9.046  -3.956  1.00  7.23           C  
ANISOU 1128  CA  LEU A 138     1134    819    795    151    -20    -39       C  
ATOM   1129  C   LEU A 138      27.834   8.025  -3.200  1.00  7.27           C  
ANISOU 1129  C   LEU A 138     1083    788    892    141   -152   -180       C  
ATOM   1130  O   LEU A 138      27.726   6.818  -3.423  1.00  7.84           O  
ANISOU 1130  O   LEU A 138     1154    705   1118     47    102    -76       O  
ATOM   1131  CB  LEU A 138      27.913   9.786  -4.989  1.00  8.34           C  
ANISOU 1131  CB  LEU A 138     1260    924    985    108    192    -36       C  
ATOM   1132  CG  LEU A 138      28.632   8.843  -5.967  1.00  7.95           C  
ANISOU 1132  CG  LEU A 138     1360    805    854     15    102   -115       C  
ATOM   1133  CD1 LEU A 138      27.632   8.074  -6.837  1.00 11.09           C  
ANISOU 1133  CD1 LEU A 138     1449   1569   1196   -289      0   -316       C  
ATOM   1134  CD2 LEU A 138      29.612   9.641  -6.829  1.00 10.21           C  
ANISOU 1134  CD2 LEU A 138     1374   1197   1309   -145    379   -115       C  
ATOM   1135  N   PHE A 139      28.682   8.488  -2.272  1.00  6.88           N  
ANISOU 1135  N   PHE A 139      989   1011    612     60     19    -46       N  
ATOM   1136  CA  PHE A 139      29.472   7.577  -1.399  1.00  7.17           C  
ANISOU 1136  CA  PHE A 139      954    920    850   -183    -95     36       C  
ATOM   1137  C   PHE A 139      28.552   6.629  -0.701  1.00  6.97           C  
ANISOU 1137  C   PHE A 139      889    629   1132      0    -42    -24       C  
ATOM   1138  O   PHE A 139      28.759   5.413  -0.685  1.00  7.64           O  
ANISOU 1138  O   PHE A 139     1185    654   1064      1   -111    -76       O  
ATOM   1139  CB  PHE A 139      30.238   8.475  -0.413  1.00  7.77           C  
ANISOU 1139  CB  PHE A 139     1060    961    933   -116   -241    -94       C  
ATOM   1140  CG  PHE A 139      30.772   7.704   0.774  1.00  8.33           C  
ANISOU 1140  CG  PHE A 139     1099   1084    980     40   -283   -198       C  
ATOM   1141  CD1 PHE A 139      30.176   7.892   2.022  1.00 10.20           C  
ANISOU 1141  CD1 PHE A 139     1424   1554    900    -27   -142    -45       C  
ATOM   1142  CD2 PHE A 139      31.842   6.833   0.644  1.00  9.24           C  
ANISOU 1142  CD2 PHE A 139     1034    982   1496    -39   -157     49       C  
ATOM   1143  CE1 PHE A 139      30.646   7.215   3.114  1.00 10.89           C  
ANISOU 1143  CE1 PHE A 139     1474   1572   1092    335   -177    -41       C  
ATOM   1144  CE2 PHE A 139      32.287   6.135   1.769  1.00 10.26           C  
ANISOU 1144  CE2 PHE A 139     1389   1220   1290    200    -24     99       C  
ATOM   1145  CZ  PHE A 139      31.727   6.337   3.019  1.00 11.17           C  
ANISOU 1145  CZ  PHE A 139     1236   1568   1438    194     93   -131       C  
ATOM   1146  N   ARG A 140      27.469   7.145  -0.083  1.00  6.73           N  
ANISOU 1146  N   ARG A 140      893    819    844   -106     -7    -33       N  
ATOM   1147  CA  ARG A 140      26.559   6.252   0.660  1.00  6.95           C  
ANISOU 1147  CA  ARG A 140      924    769    948   -100    -35    -90       C  
ATOM   1148  C   ARG A 140      25.793   5.321  -0.263  1.00  6.95           C  
ANISOU 1148  C   ARG A 140      975    643   1022      8   -108    -64       C  
ATOM   1149  O   ARG A 140      25.570   4.154   0.099  1.00  8.39           O  
ANISOU 1149  O   ARG A 140     1291    593   1304    -76    100   -131       O  
ATOM   1150  CB  ARG A 140      25.551   7.054   1.502  1.00  7.73           C  
ANISOU 1150  CB  ARG A 140     1040    777   1122   -184    175   -126       C  
ATOM   1151  CG  ARG A 140      26.208   7.833   2.628  1.00  7.92           C  
ANISOU 1151  CG  ARG A 140     1374    877    757    -52    118    -42       C  
ATOM   1152  CD  ARG A 140      25.199   8.311   3.649  1.00  8.09           C  
ANISOU 1152  CD  ARG A 140     1116   1029    929     90    112     78       C  
ATOM   1153  NE  ARG A 140      24.072   9.026   3.077  1.00  8.90           N  
ANISOU 1153  NE  ARG A 140     1284    901   1196     11   -122     -8       N  
ATOM   1154  CZ  ARG A 140      24.011  10.334   2.846  1.00  8.52           C  
ANISOU 1154  CZ  ARG A 140     1107    929   1200    -62     -8    158       C  
ATOM   1155  NH1 ARG A 140      22.909  10.875   2.340  1.00 11.76           N  
ANISOU 1155  NH1 ARG A 140     1441   1372   1656    314   -262     81       N  
ATOM   1156  NH2 ARG A 140      25.072  11.115   3.123  1.00  9.65           N  
ANISOU 1156  NH2 ARG A 140     1358   1060   1248   -230    149    -67       N  
ATOM   1157  N   LYS A 141      25.388   5.787  -1.439  1.00  8.27           N  
ANISOU 1157  N   LYS A 141     1205   1077    861     11   -175   -196       N  
ATOM   1158  CA  LYS A 141      24.705   4.889  -2.410  1.00  8.15           C  
ANISOU 1158  CA  LYS A 141     1139    918   1038     90   -197   -300       C  
ATOM   1159  C   LYS A 141      25.615   3.732  -2.774  1.00  7.97           C  
ANISOU 1159  C   LYS A 141     1062    918   1046     16   -214   -161       C  
ATOM   1160  O   LYS A 141      25.231   2.531  -2.795  1.00  8.58           O  
ANISOU 1160  O   LYS A 141     1156    804   1298    126   -257   -191       O  
ATOM   1161  CB  LYS A 141      24.350   5.675  -3.677  1.00 10.30           C  
ANISOU 1161  CB  LYS A 141     1517   1153   1244     18   -595   -112       C  
ATOM   1162  CG  LYS A 141      23.742   4.852  -4.821  1.00 13.50           C  
ANISOU 1162  CG  LYS A 141     1897   1691   1540   -419   -915   -109       C  
ATOM   1163  CD  LYS A 141      23.571   5.736  -6.065  1.00 20.19           C  
ANISOU 1163  CD  LYS A 141     4049   1545   2079   -269  -2187     43       C  
ATOM   1164  CE  LYS A 141      23.087   4.896  -7.240  1.00 24.98           C  
ANISOU 1164  CE  LYS A 141     5069   2598   1826    -91  -1768   -516       C  
ATOM   1165  NZ  LYS A 141      21.835   4.149  -6.909  1.00 52.98           N  
ANISOU 1165  NZ  LYS A 141     7355   7198   5576  -4155  -2150  -1980       N  
ATOM   1166  N   ASP A 142      26.856   4.059  -3.108  1.00  8.09           N  
ANISOU 1166  N   ASP A 142     1090    908   1075    130   -157   -202       N  
ATOM   1167  CA  ASP A 142      27.778   3.010  -3.591  1.00  7.89           C  
ANISOU 1167  CA  ASP A 142     1226    782    990    125    -42   -175       C  
ATOM   1168  C   ASP A 142      28.188   2.103  -2.443  1.00  8.27           C  
ANISOU 1168  C   ASP A 142     1199    761   1183     57   -211   -153       C  
ATOM   1169  O   ASP A 142      28.328   0.875  -2.645  1.00  9.39           O  
ANISOU 1169  O   ASP A 142     1535    730   1304     80   -102    -90       O  
ATOM   1170  CB  ASP A 142      28.962   3.687  -4.279  1.00  9.38           C  
ANISOU 1170  CB  ASP A 142     1282   1252   1030     96     20    -53       C  
ATOM   1171  CG  ASP A 142      28.664   4.247  -5.664  1.00  9.70           C  
ANISOU 1171  CG  ASP A 142     1321   1350   1013    -82   -104    -76       C  
ATOM   1172  OD1 ASP A 142      27.521   4.060  -6.132  1.00 11.22           O  
ANISOU 1172  OD1 ASP A 142     1374   1643   1247   -221   -221    -45       O  
ATOM   1173  OD2 ASP A 142      29.571   4.863  -6.247  1.00 10.74           O  
ANISOU 1173  OD2 ASP A 142     1287   1605   1189    -85     55     47       O  
ATOM   1174  N   ILE A 143      28.375   2.633  -1.241  1.00  8.06           N  
ANISOU 1174  N   ILE A 143     1124    934   1006     45   -187    -21       N  
ATOM   1175  CA  ILE A 143      28.687   1.730  -0.114  1.00  8.98           C  
ANISOU 1175  CA  ILE A 143     1318    819   1274   -184   -364     33       C  
ATOM   1176  C   ILE A 143      27.502   0.862   0.230  1.00  8.47           C  
ANISOU 1176  C   ILE A 143     1301    750   1167     -3   -103    -15       C  
ATOM   1177  O   ILE A 143      27.704  -0.331   0.524  1.00  9.79           O  
ANISOU 1177  O   ILE A 143     1885    649   1185     51    -27     20       O  
ATOM   1178  CB AILE A 143      28.972   2.505   1.203  0.51 10.10           C  
ANISOU 1178  CB AILE A 143     1679   1061   1099   -344   -395    204       C  
ATOM   1179  CB BILE A 143      29.396   2.502   1.013  0.49  8.83           C  
ANISOU 1179  CB BILE A 143     1389    713   1251    274   -477   -166       C  
ATOM   1180  CG1AILE A 143      30.339   3.188   1.191  0.51  9.73           C  
ANISOU 1180  CG1AILE A 143     1422    557   1716    -52   -428    -72       C  
ATOM   1181  CG1BILE A 143      30.429   1.540   1.638  0.49  9.12           C  
ANISOU 1181  CG1BILE A 143     1580    930    955    437   -220    130       C  
ATOM   1182  CG2AILE A 143      28.785   1.608   2.431  0.51 12.49           C  
ANISOU 1182  CG2AILE A 143     2517    945   1284   -128     -5    240       C  
ATOM   1183  CG2BILE A 143      28.416   3.101   1.963  0.49  9.56           C  
ANISOU 1183  CG2BILE A 143     1460   1068   1103    376   -219    198       C  
ATOM   1184  CD1AILE A 143      31.507   2.240   1.357  0.51 10.80           C  
ANISOU 1184  CD1AILE A 143     1783    837   1482    231   -251    412       C  
ATOM   1185  CD1BILE A 143      31.211   2.205   2.752  0.49  9.43           C  
ANISOU 1185  CD1BILE A 143     1719    573   1292     94   -582    531       C  
ATOM   1186  N   ALA A 144      26.264   1.362   0.126  1.00  8.20           N  
ANISOU 1186  N   ALA A 144     1297    782   1035    -21    175    -30       N  
ATOM   1187  CA  ALA A 144      25.118   0.512   0.400  1.00  9.46           C  
ANISOU 1187  CA  ALA A 144     1331    742   1522   -109    264   -154       C  
ATOM   1188  C   ALA A 144      25.032  -0.625  -0.627  1.00  9.46           C  
ANISOU 1188  C   ALA A 144     1256    781   1558     63    -22   -165       C  
ATOM   1189  O   ALA A 144      24.692  -1.771  -0.285  1.00 10.53           O  
ANISOU 1189  O   ALA A 144     1325    689   1989    -81   -161    -24       O  
ATOM   1190  CB  ALA A 144      23.826   1.348   0.387  1.00 11.03           C  
ANISOU 1190  CB  ALA A 144     1370    967   1854     75    387    -95       C  
ATOM   1191  N   ALA A 145      25.359  -0.327  -1.887  1.00  9.42           N  
ANISOU 1191  N   ALA A 145     1170    922   1488    -28   -143   -235       N  
ATOM   1192  CA  ALA A 145      25.304  -1.431  -2.860  1.00  9.59           C  
ANISOU 1192  CA  ALA A 145     1169   1037   1438    128   -223   -268       C  
ATOM   1193  C   ALA A 145      26.379  -2.456  -2.510  1.00  9.30           C  
ANISOU 1193  C   ALA A 145     1288    869   1375    -19   -363   -283       C  
ATOM   1194  O   ALA A 145      26.163  -3.682  -2.666  1.00 11.90           O  
ANISOU 1194  O   ALA A 145     1737    835   1951      1   -718   -418       O  
ATOM   1195  CB  ALA A 145      25.489  -0.829  -4.243  1.00 12.01           C  
ANISOU 1195  CB  ALA A 145     1731   1478   1353     53   -571   -117       C  
ATOM   1196  N   LYS A 146      27.546  -2.026  -2.075  1.00  8.50           N  
ANISOU 1196  N   LYS A 146     1162    841   1225     14   -189   -170       N  
ATOM   1197  CA  LYS A 146      28.627  -2.976  -1.729  1.00  8.26           C  
ANISOU 1197  CA  LYS A 146     1180    919   1041     18   -225   -105       C  
ATOM   1198  C   LYS A 146      28.223  -3.760  -0.476  1.00  8.81           C  
ANISOU 1198  C   LYS A 146     1662    728    958    -83   -225   -271       C  
ATOM   1199  O   LYS A 146      28.460  -4.980  -0.386  1.00  9.45           O  
ANISOU 1199  O   LYS A 146     1663    729   1196    -32     -5   -200       O  
ATOM   1200  CB  LYS A 146      29.952  -2.257  -1.556  1.00 10.95           C  
ANISOU 1200  CB  LYS A 146     1277   1095   1788   -160   -509    100       C  
ATOM   1201  CG  LYS A 146      31.104  -3.218  -1.390  1.00 14.26           C  
ANISOU 1201  CG  LYS A 146     1293   1778   2347    232   -256   -131       C  
ATOM   1202  CD  LYS A 146      31.300  -4.091  -2.622  1.00 18.02           C  
ANISOU 1202  CD  LYS A 146     2252   1973   2622    184   -192   -470       C  
ATOM   1203  CE  LYS A 146      31.764  -3.339  -3.857  1.00 20.85           C  
ANISOU 1203  CE  LYS A 146     3917   2154   1850   -480   -881   -651       C  
ATOM   1204  NZ  LYS A 146      32.051  -4.335  -4.937  1.00 21.05           N  
ANISOU 1204  NZ  LYS A 146     2962   2394   2642    689    -88   -598       N  
ATOM   1205  N   TYR A 147      27.604  -3.092   0.512  1.00  9.11           N  
ANISOU 1205  N   TYR A 147     1458    799   1206    -45     93    -59       N  
ATOM   1206  CA  TYR A 147      27.075  -3.776   1.704  1.00  9.17           C  
ANISOU 1206  CA  TYR A 147     1290    817   1379    -91    144    -24       C  
ATOM   1207  C   TYR A 147      26.207  -4.951   1.275  1.00 10.50           C  
ANISOU 1207  C   TYR A 147     1565    841   1584   -172    214   -133       C  
ATOM   1208  O   TYR A 147      26.351  -6.074   1.786  1.00 11.47           O  
ANISOU 1208  O   TYR A 147     1743    732   1883   -129    359    -92       O  
ATOM   1209  CB  TYR A 147      26.256  -2.801   2.536  1.00 10.54           C  
ANISOU 1209  CB  TYR A 147     1405   1137   1463    -79    131   -372       C  
ATOM   1210  CG  TYR A 147      26.974  -1.983   3.593  1.00  9.39           C  
ANISOU 1210  CG  TYR A 147     1351   1046   1172   -108     41    -18       C  
ATOM   1211  CD1 TYR A 147      26.196  -1.313   4.522  1.00 15.26           C  
ANISOU 1211  CD1 TYR A 147     1635   2127   2036   -509    399  -1103       C  
ATOM   1212  CD2 TYR A 147      28.346  -1.833   3.681  1.00 10.19           C  
ANISOU 1212  CD2 TYR A 147     1394   1513    964    -35   -115    117       C  
ATOM   1213  CE1 TYR A 147      26.737  -0.529   5.503  1.00 13.96           C  
ANISOU 1213  CE1 TYR A 147     1427   1935   1943   -230    152   -848       C  
ATOM   1214  CE2 TYR A 147      28.918  -1.092   4.697  1.00  9.86           C  
ANISOU 1214  CE2 TYR A 147     1258   1567    921   -216     71    144       C  
ATOM   1215  CZ  TYR A 147      28.123  -0.454   5.603  1.00 11.94           C  
ANISOU 1215  CZ  TYR A 147     1414   1691   1431   -414    346   -238       C  
ATOM   1216  OH  TYR A 147      28.740   0.275   6.598  1.00 11.88           O  
ANISOU 1216  OH  TYR A 147     1402   1384   1726   -130     99   -300       O  
ATOM   1217  N   LYS A 148      25.275  -4.670   0.350  1.00 10.86           N  
ANISOU 1217  N   LYS A 148     1187    871   2070   -170    106   -226       N  
ATOM   1218  CA  LYS A 148      24.357  -5.733  -0.105  1.00 12.90           C  
ANISOU 1218  CA  LYS A 148     1194   1166   2541   -228    226   -567       C  
ATOM   1219  C   LYS A 148      25.127  -6.874  -0.723  1.00 12.60           C  
ANISOU 1219  C   LYS A 148     1525   1034   2228   -213    112   -547       C  
ATOM   1220  O   LYS A 148      24.857  -8.073  -0.441  1.00 13.55           O  
ANISOU 1220  O   LYS A 148     1651   1030   2466   -224   -113   -354       O  
ATOM   1221  CB  LYS A 148      23.354  -5.120  -1.079  1.00 17.98           C  
ANISOU 1221  CB  LYS A 148     1540   1841   3450    242   -579  -1256       C  
ATOM   1222  CG  LYS A 148      22.352  -5.960  -1.836  1.00 37.58           C  
ANISOU 1222  CG  LYS A 148     5585   3115   5580  -2108  -3558    609       C  
ATOM   1223  CD  LYS A 148      21.517  -5.085  -2.775  1.00 45.27           C  
ANISOU 1223  CD  LYS A 148     5725   5038   6437  -1332  -4155    826       C  
ATOM   1224  CE  LYS A 148      20.152  -5.673  -3.057  1.00 51.76           C  
ANISOU 1224  CE  LYS A 148     5258   7216   7193  -1355  -3644    246       C  
ATOM   1225  NZ  LYS A 148      19.450  -4.919  -4.145  1.00 59.21           N  
ANISOU 1225  NZ  LYS A 148     5081   9923   7492   -618  -3986    531       N  
ATOM   1226  N   GLU A 149      26.075  -6.598  -1.578  1.00 10.24           N  
ANISOU 1226  N   GLU A 149     1287   1044   1558     51   -273   -431       N  
ATOM   1227  CA  GLU A 149      26.897  -7.641  -2.195  1.00  9.62           C  
ANISOU 1227  CA  GLU A 149     1505    814   1338    -15   -223   -315       C  
ATOM   1228  C   GLU A 149      27.624  -8.470  -1.133  1.00  9.56           C  
ANISOU 1228  C   GLU A 149     1658    786   1191    -26    -38   -189       C  
ATOM   1229  O   GLU A 149      27.784  -9.678  -1.315  1.00 10.24           O  
ANISOU 1229  O   GLU A 149     1554    735   1600   -149   -115   -209       O  
ATOM   1230  CB  GLU A 149      27.955  -7.000  -3.124  1.00 10.49           C  
ANISOU 1230  CB  GLU A 149     1709   1082   1194     92   -124    -27       C  
ATOM   1231  CG  GLU A 149      27.351  -6.379  -4.375  1.00 13.46           C  
ANISOU 1231  CG  GLU A 149     2548   1328   1239    266   -400    -56       C  
ATOM   1232  CD  GLU A 149      28.333  -5.604  -5.202  1.00 18.30           C  
ANISOU 1232  CD  GLU A 149     3233   2709   1010   -360   -416    319       C  
ATOM   1233  OE1 GLU A 149      27.868  -4.847  -6.087  1.00 25.08           O  
ANISOU 1233  OE1 GLU A 149     4173   3146   2210   -278   -523   1199       O  
ATOM   1234  OE2 GLU A 149      29.572  -5.594  -5.078  1.00 22.76           O  
ANISOU 1234  OE2 GLU A 149     3083   3478   2087    -58    254    719       O  
ATOM   1235  N   LEU A 150      28.072  -7.840  -0.036  1.00  9.20           N  
ANISOU 1235  N   LEU A 150     1236    875   1386    -44   -178   -245       N  
ATOM   1236  CA  LEU A 150      28.800  -8.490   1.042  1.00  9.80           C  
ANISOU 1236  CA  LEU A 150     1332    867   1526   -138   -274    -79       C  
ATOM   1237  C   LEU A 150      27.910  -9.220   2.025  1.00 10.22           C  
ANISOU 1237  C   LEU A 150     1725    751   1407   -108      1   -315       C  
ATOM   1238  O   LEU A 150      28.428  -9.908   2.917  1.00 12.83           O  
ANISOU 1238  O   LEU A 150     1993   1055   1825   -381   -244     99       O  
ATOM   1239  CB  LEU A 150      29.569  -7.386   1.800  1.00 10.45           C  
ANISOU 1239  CB  LEU A 150     1571    949   1450   -223   -290   -137       C  
ATOM   1240  CG  LEU A 150      30.742  -6.796   1.022  1.00 10.35           C  
ANISOU 1240  CG  LEU A 150     1439    920   1572    -94   -324     42       C  
ATOM   1241  CD1 LEU A 150      31.189  -5.486   1.703  1.00 12.89           C  
ANISOU 1241  CD1 LEU A 150     1714   1508   1674   -563   -256   -281       C  
ATOM   1242  CD2 LEU A 150      31.922  -7.722   0.944  1.00 14.82           C  
ANISOU 1242  CD2 LEU A 150     1886   1622   2121    408    256    622       C  
ATOM   1243  N   GLY A 151      26.594  -9.070   1.899  1.00 10.94           N  
ANISOU 1243  N   GLY A 151     1611    962   1583   -427     63   -369       N  
ATOM   1244  CA  GLY A 151      25.679  -9.803   2.747  1.00 14.18           C  
ANISOU 1244  CA  GLY A 151     2236   1196   1957   -746    469   -458       C  
ATOM   1245  C   GLY A 151      25.096  -9.034   3.910  1.00 13.22           C  
ANISOU 1245  C   GLY A 151     2641   1055   1327   -547    249   -148       C  
ATOM   1246  O   GLY A 151      24.419  -9.617   4.742  1.00 17.18           O  
ANISOU 1246  O   GLY A 151     3759   1121   1646  -1026    704   -291       O  
ATOM   1247  N   TYR A 152      25.321  -7.727   3.953  1.00 10.95           N  
ANISOU 1247  N   TYR A 152     1471   1010   1679   -330    266   -177       N  
ATOM   1248  CA  TYR A 152      24.865  -6.931   5.085  1.00 11.50           C  
ANISOU 1248  CA  TYR A 152     1435   1064   1872   -116    159   -302       C  
ATOM   1249  C   TYR A 152      23.756  -5.975   4.653  1.00 13.21           C  
ANISOU 1249  C   TYR A 152     1471   1177   2373    -85     59   -186       C  
ATOM   1250  O   TYR A 152      23.931  -5.238   3.671  1.00 16.43           O  
ANISOU 1250  O   TYR A 152     2138   1754   2351    -87   -524     80       O  
ATOM   1251  CB  TYR A 152      26.051  -6.154   5.637  1.00 11.56           C  
ANISOU 1251  CB  TYR A 152     1474   1297   1620   -214    145   -328       C  
ATOM   1252  CG  TYR A 152      25.794  -5.154   6.752  1.00 13.93           C  
ANISOU 1252  CG  TYR A 152     2434   1298   1559   -175    171   -307       C  
ATOM   1253  CD1 TYR A 152      26.157  -3.805   6.693  1.00 12.80           C  
ANISOU 1253  CD1 TYR A 152     1963   1222   1678     46   -437   -261       C  
ATOM   1254  CD2 TYR A 152      25.165  -5.588   7.910  1.00 17.79           C  
ANISOU 1254  CD2 TYR A 152     3475   1638   1645   -291    556   -413       C  
ATOM   1255  CE1 TYR A 152      25.901  -2.924   7.734  1.00 14.68           C  
ANISOU 1255  CE1 TYR A 152     2291   1316   1972    -29     21   -349       C  
ATOM   1256  CE2 TYR A 152      24.905  -4.735   8.969  1.00 23.83           C  
ANISOU 1256  CE2 TYR A 152     4854   1948   2251  -1142   1437   -878       C  
ATOM   1257  CZ  TYR A 152      25.271  -3.416   8.874  1.00 17.21           C  
ANISOU 1257  CZ  TYR A 152     2914   1480   2146    -62    382   -420       C  
ATOM   1258  OH  TYR A 152      25.018  -2.560   9.929  1.00 23.60           O  
ANISOU 1258  OH  TYR A 152     3996   2003   2968   -898   1502  -1055       O  
ATOM   1259  N   GLN A 153      22.645  -5.998   5.381  1.00 17.91           N  
ANISOU 1259  N   GLN A 153     1422   1693   3691   -246    459   -680       N  
ATOM   1260  CA  GLN A 153      21.517  -5.168   4.993  1.00 24.23           C  
ANISOU 1260  CA  GLN A 153     1417   2549   5242     66    -96   -976       C  
ATOM   1261  C   GLN A 153      21.774  -3.689   5.198  1.00 25.47           C  
ANISOU 1261  C   GLN A 153     2138   2351   5190    618   -809   -798       C  
ATOM   1262  O   GLN A 153      21.192  -2.830   4.522  1.00 27.98           O  
ANISOU 1262  O   GLN A 153     2693   3126   4815    585   -373     62       O  
ATOM   1263  CB  GLN A 153      20.268  -5.553   5.782  1.00 36.84           C  
ANISOU 1263  CB  GLN A 153     1611   4461   7924    357    836    327       C  
ATOM   1264  CG  GLN A 153      20.093  -7.004   6.123  1.00 55.40           C  
ANISOU 1264  CG  GLN A 153     6010   5580   9458  -2021    764   1733       C  
ATOM   1265  CD  GLN A 153      18.976  -7.376   7.075  1.00 72.55           C  
ANISOU 1265  CD  GLN A 153     9355   8978   9235  -4337   2093   1164       C  
ATOM   1266  OE1 GLN A 153      18.872  -8.550   7.473  1.00 85.31           O  
ANISOU 1266  OE1 GLN A 153    12633   8976  10805  -5630   3647   1104       O  
ATOM   1267  NE2 GLN A 153      18.121  -6.428   7.450  1.00 66.92           N  
ANISOU 1267  NE2 GLN A 153     8075  10785   6566  -4198   2569   1598       N  
ATOM   1268  N   GLY A 154      22.615  -3.338   6.145  1.00 22.61           N  
ANISOU 1268  N   GLY A 154     2263   2163   4165     47   -162   -586       N  
ATOM   1269  CA  GLY A 154      22.969  -1.915   6.380  1.00 23.27           C  
ANISOU 1269  CA  GLY A 154     2699   2381   3761   -795   1474   -631       C  
ATOM   1270  C   GLY A 154      21.862  -1.207   7.087  1.00 18.24           C  
ANISOU 1270  C   GLY A 154     1440   1935   3554   -813    384   -551       C  
ATOM   1271  O   GLY A 154      20.948  -1.835   7.705  1.00 28.14           O  
ANISOU 1271  O   GLY A 154     3291   2298   5105   -244   2376    232       O  
ATOM   1272  OXT GLY A 154      21.858   0.019   7.030  1.00 18.50           O  
ANISOU 1272  OXT GLY A 154     2383   1974   2671   -829    -86   -590       O  
TER    1273      GLY A 154                                                      
HETATM 1274  S   SO4 A 157      31.178  18.341  28.294  1.00 17.97           S  
ANISOU 1274  S   SO4 A 157     3148   2227   1453    778   -249   -168       S  
HETATM 1275  O1  SO4 A 157      30.642  19.706  28.114  1.00 22.37           O  
ANISOU 1275  O1  SO4 A 157     3977   2323   2202   1192    185    -83       O  
HETATM 1276  O2  SO4 A 157      30.628  17.439  27.255  1.00 17.56           O  
ANISOU 1276  O2  SO4 A 157     2750   2776   1147    827    -23   -470       O  
HETATM 1277  O3  SO4 A 157      30.884  17.844  29.635  1.00 16.85           O  
ANISOU 1277  O3  SO4 A 157     2507   2808   1087    558   -239   -312       O  
HETATM 1278  O4  SO4 A 157      32.675  18.394  28.123  1.00 16.31           O  
ANISOU 1278  O4  SO4 A 157     3148   1857   1191    501     34   -129       O  
HETATM 1279  S   SO4 A 158      45.190  26.090  -0.627  0.33 21.08           S  
ANISOU 1279  S   SO4 A 158     3019   3019   1971      0      0      0       S  
HETATM 1280  O1  SO4 A 158      46.073  25.009  -0.128  0.33 26.09           O  
ANISOU 1280  O1  SO4 A 158     1758   3631   4525    395    225   -105       O  
HETATM 1281  O2  SO4 A 158      45.190  26.090  -2.103  0.33 48.38           O  
ANISOU 1281  O2  SO4 A 158     8198   8198   1986      0      0      0       O  
HETATM 1282  O3  SO4 A 158      45.687  27.393  -0.126  0.33 33.56           O  
ANISOU 1282  O3  SO4 A 158     4927   3092   4733   -992     61    -32       O  
HETATM 1283  O4  SO4 A 158      43.815  25.866  -0.123  0.33 24.89           O  
ANISOU 1283  O4  SO4 A 158     2138   2956   4363    774   -399    213       O  
HETATM 1284  S   SO4 A 159      26.626  30.565  -2.691  1.00 22.03           S  
ANISOU 1284  S   SO4 A 159     3671   1888   2810    164   -126    224       S  
HETATM 1285  O1  SO4 A 159      26.046  30.627  -1.317  1.00 30.95           O  
ANISOU 1285  O1  SO4 A 159     7066   2039   2655    928    571    517       O  
HETATM 1286  O2  SO4 A 159      26.244  29.311  -3.329  1.00 18.08           O  
ANISOU 1286  O2  SO4 A 159     3040   1654   2176   -388      6    755       O  
HETATM 1287  O3  SO4 A 159      28.118  30.623  -2.546  1.00 38.82           O  
ANISOU 1287  O3  SO4 A 159     4117   7095   3537  -2908  -1637   2248       O  
HETATM 1288  O4  SO4 A 159      26.188  31.745  -3.462  1.00 31.38           O  
ANISOU 1288  O4  SO4 A 159     6764   1835   3324    452    909   1034       O  
HETATM 1289  CHA HEM A 155      37.440   2.337  11.440  1.00  7.26           C  
ANISOU 1289  CHA HEM A 155     1223    761    772    -94     90   -105       C  
HETATM 1290  CHB HEM A 155      36.701   5.295   7.707  1.00  6.93           C  
ANISOU 1290  CHB HEM A 155     1040    640    953    -62    -31   -163       C  
HETATM 1291  CHC HEM A 155      32.164   5.985   9.138  1.00  7.56           C  
ANISOU 1291  CHC HEM A 155     1036    864    973   -112     82    -46       C  
HETATM 1292  CHD HEM A 155      32.880   3.033  12.877  1.00  7.46           C  
ANISOU 1292  CHD HEM A 155     1144    746    946   -122      6   -164       C  
HETATM 1293  C1A HEM A 155      37.648   3.070  10.270  1.00  6.84           C  
ANISOU 1293  C1A HEM A 155     1036    643    918    -73    149   -105       C  
HETATM 1294  C2A HEM A 155      38.867   3.077   9.498  1.00  6.83           C  
ANISOU 1294  C2A HEM A 155      822    838    935   -152    -38    -66       C  
HETATM 1295  C3A HEM A 155      38.678   3.921   8.467  1.00  6.81           C  
ANISOU 1295  C3A HEM A 155     1024    812    751      5     70   -159       C  
HETATM 1296  C4A HEM A 155      37.322   4.424   8.594  1.00  6.54           C  
ANISOU 1296  C4A HEM A 155      953    630    901   -212    -19    -97       C  
HETATM 1297  CMA HEM A 155      39.631   4.278   7.327  1.00  8.57           C  
ANISOU 1297  CMA HEM A 155     1431    787   1037     63    385   -113       C  
HETATM 1298  CAA HEM A 155      40.081   2.190   9.798  1.00  7.88           C  
ANISOU 1298  CAA HEM A 155      906    838   1248    -46   -166    -74       C  
HETATM 1299  CBA HEM A 155      40.185   0.960   8.851  1.00  9.99           C  
ANISOU 1299  CBA HEM A 155     1416    823   1556    -88     24   -273       C  
HETATM 1300  CGA HEM A 155      38.910   0.142   8.852  1.00 10.29           C  
ANISOU 1300  CGA HEM A 155     1487    759   1662   -108   -122   -151       C  
HETATM 1301  O1A HEM A 155      38.650  -0.503   9.911  1.00 11.84           O  
ANISOU 1301  O1A HEM A 155     1577    976   1946    -23      4    116       O  
HETATM 1302  O2A HEM A 155      38.202   0.146   7.825  1.00 11.67           O  
ANISOU 1302  O2A HEM A 155     1558   1031   1844   -123   -256    -80       O  
HETATM 1303  C1B HEM A 155      35.383   5.723   7.729  1.00  6.57           C  
ANISOU 1303  C1B HEM A 155     1094    530    872   -113     41    -11       C  
HETATM 1304  C2B HEM A 155      34.797   6.642   6.783  1.00  6.46           C  
ANISOU 1304  C2B HEM A 155     1113    635    707   -135    -10    -91       C  
HETATM 1305  C3B HEM A 155      33.527   6.856   7.191  1.00  7.36           C  
ANISOU 1305  C3B HEM A 155     1233    698    867     49     52     10       C  
HETATM 1306  C4B HEM A 155      33.329   6.061   8.385  1.00  7.27           C  
ANISOU 1306  C4B HEM A 155     1136    612   1015    -19    106     75       C  
HETATM 1307  CMB HEM A 155      35.525   7.194   5.557  1.00  8.71           C  
ANISOU 1307  CMB HEM A 155     1531   1051    727   -389     75     68       C  
HETATM 1308  CAB HEM A 155      32.474   7.689   6.649  1.00  8.52           C  
ANISOU 1308  CAB HEM A 155     1393    983    861    272      4    -23       C  
HETATM 1309  CBB HEM A 155      32.734   8.927   6.052  1.00  9.65           C  
ANISOU 1309  CBB HEM A 155     1143   1263   1259    347    -86    355       C  
HETATM 1310  C1C HEM A 155      31.966   5.295  10.334  1.00  7.17           C  
ANISOU 1310  C1C HEM A 155     1047    642   1036   -113    108    -89       C  
HETATM 1311  C2C HEM A 155      30.811   5.439  11.184  1.00  6.89           C  
ANISOU 1311  C2C HEM A 155      982    612   1026   -132     94    -66       C  
HETATM 1312  C3C HEM A 155      30.991   4.594  12.243  1.00  7.49           C  
ANISOU 1312  C3C HEM A 155     1213    640    993    -10    234    -63       C  
HETATM 1313  C4C HEM A 155      32.275   3.958  12.031  1.00  7.64           C  
ANISOU 1313  C4C HEM A 155     1094    721   1086    -49    217     -4       C  
HETATM 1314  CMC HEM A 155      29.642   6.388  10.910  1.00  9.19           C  
ANISOU 1314  CMC HEM A 155     1133    983   1376    112    -31      3       C  
HETATM 1315  CAC HEM A 155      30.266   4.340  13.470  1.00  8.89           C  
ANISOU 1315  CAC HEM A 155     1337    881   1160   -335    436   -167       C  
HETATM 1316  CBC HEM A 155      29.008   4.939  13.771  1.00 11.85           C  
ANISOU 1316  CBC HEM A 155     1659   1159   1683     58    670   -111       C  
HETATM 1317  C1D HEM A 155      34.183   2.541  12.800  1.00  7.59           C  
ANISOU 1317  C1D HEM A 155     1328    541   1015     24    191     79       C  
HETATM 1318  C2D HEM A 155      34.806   1.714  13.800  1.00  7.90           C  
ANISOU 1318  C2D HEM A 155     1384    596   1021     23    204     72       C  
HETATM 1319  C3D HEM A 155      36.101   1.584  13.439  1.00  7.36           C  
ANISOU 1319  C3D HEM A 155     1276    779    739   -112     21     31       C  
HETATM 1320  C4D HEM A 155      36.262   2.271  12.183  1.00  6.55           C  
ANISOU 1320  C4D HEM A 155     1161    550    778   -104     25     25       C  
HETATM 1321  CMD HEM A 155      34.087   1.164  15.028  1.00 10.20           C  
ANISOU 1321  CMD HEM A 155     1329   1455   1090   -176    153    322       C  
HETATM 1322  CAD HEM A 155      37.239   0.927  14.243  1.00  9.29           C  
ANISOU 1322  CAD HEM A 155     1613   1050    865    193   -123     78       C  
HETATM 1323  CBD HEM A 155      37.941   1.946  15.159  1.00 11.77           C  
ANISOU 1323  CBD HEM A 155     1513   1757   1203    -78   -265   -198       C  
HETATM 1324  CGD HEM A 155      39.059   1.371  16.003  1.00 13.01           C  
ANISOU 1324  CGD HEM A 155     1620   2074   1248     79   -291    -45       C  
HETATM 1325  O1D HEM A 155      38.806   1.065  17.162  1.00 19.63           O  
ANISOU 1325  O1D HEM A 155     2193   3796   1468    733      7    523       O  
HETATM 1326  O2D HEM A 155      40.171   1.280  15.456  1.00 18.73           O  
ANISOU 1326  O2D HEM A 155     1917   3523   1677    827     65     82       O  
HETATM 1327  NA  HEM A 155      36.685   3.898   9.712  1.00  6.70           N  
ANISOU 1327  NA  HEM A 155     1096    487    963     18    252    -89       N  
HETATM 1328  NB  HEM A 155      34.483   5.355   8.716  1.00  6.60           N  
ANISOU 1328  NB  HEM A 155     1022    841    646    -53    -15    -28       N  
HETATM 1329  NC  HEM A 155      32.867   4.372  10.838  1.00  7.29           N  
ANISOU 1329  NC  HEM A 155     1042    851    877     22    177   -102       N  
HETATM 1330  ND  HEM A 155      35.076   2.888  11.792  1.00  7.19           N  
ANISOU 1330  ND  HEM A 155     1294    684    755     93     54    -82       N  
HETATM 1331 FE   HEM A 155      34.783   4.140  10.249  1.00  7.45          FE  
ANISOU 1331 FE   HEM A 155     1162    766    901    -95     37    -41      FE  
HETATM 1332  C   CMO A 156      35.022   5.476  11.377  1.00  7.47           C  
ANISOU 1332  C   CMO A 156     1288    632    918      2    251   -294       C  
HETATM 1333  O   CMO A 156      35.129   6.298  12.164  1.00  9.26           O  
ANISOU 1333  O   CMO A 156     1451    927   1141   -135    246   -398       O  
HETATM 1334  O   HOH A1001      34.724  -2.623  15.610  1.00 19.01           O  
ANISOU 1334  O   HOH A1001     3847   1699   1678   -227     33    190       O  
HETATM 1335  O   HOH A1002      32.308  19.352  17.257  1.00 14.51           O  
ANISOU 1335  O   HOH A1002     1742   1943   1828     28    234   -553       O  
HETATM 1336  O   HOH A1003      25.602  14.144  13.027  1.00 13.86           O  
ANISOU 1336  O   HOH A1003     1673   2064   1529   -217    507   -602       O  
HETATM 1337  O   HOH A1004      21.944   7.248   2.721  1.00 19.58           O  
ANISOU 1337  O   HOH A1004     2648   2496   2296  -1480   -656    157       O  
HETATM 1338  O   HOH A1005      30.448   6.351  -8.478  1.00 13.88           O  
ANISOU 1338  O   HOH A1005     1787   1762   1724    260     69   -191       O  
HETATM 1339  O   HOH A1006      24.375  29.775   6.718  1.00 18.52           O  
ANISOU 1339  O   HOH A1006     3679    959   2398   -560   -155    266       O  
HETATM 1340  O   HOH A1007      24.988  13.914   3.088  1.00 11.59           O  
ANISOU 1340  O   HOH A1007     1376    841   2187   -166   -272    -30       O  
HETATM 1341  O   HOH A1008      21.782  13.541   1.961  1.00 15.38           O  
ANISOU 1341  O   HOH A1008     1362   1521   2962    280     16     17       O  
HETATM 1342  O   HOH A1009      29.524   8.394 -10.273  1.00 14.92           O  
ANISOU 1342  O   HOH A1009     2534   1883   1252   -455    264   -307       O  
HETATM 1343  O   HOH A1010      30.069  11.234  -9.964  1.00 11.42           O  
ANISOU 1343  O   HOH A1010     1708   1534   1095    -28    -20   -194       O  
HETATM 1344  O   HOH A1011      31.495  12.564 -12.003  1.00 10.14           O  
ANISOU 1344  O   HOH A1011     1727   1202    925     63   -135    -78       O  
HETATM 1345  O   HOH A1012      34.279  12.685 -12.282  1.00 10.82           O  
ANISOU 1345  O   HOH A1012     1853   1338    919     37    -65    -41       O  
HETATM 1346  O   HOH A1013      35.987  30.506   5.429  1.00  9.84           O  
ANISOU 1346  O   HOH A1013     1528   1040   1169    -48    -92    -33       O  
HETATM 1347  O   HOH A1014      36.878  28.291   3.933  1.00 10.96           O  
ANISOU 1347  O   HOH A1014     1278   1410   1477    -13    284    124       O  
HETATM 1348  O   HOH A1015      37.764  29.282   7.339  1.00  9.53           O  
ANISOU 1348  O   HOH A1015     1289   1011   1320   -221    120   -195       O  
HETATM 1349  O   HOH A1016      35.518  33.157   5.214  1.00  9.36           O  
ANISOU 1349  O   HOH A1016     1452   1052   1052    211   -107     89       O  
HETATM 1350  O   HOH A1017      33.200  33.501  -0.484  1.00 12.03           O  
ANISOU 1350  O   HOH A1017     2017   1637    918   -244   -290    131       O  
HETATM 1351  O   HOH A1018      22.257  26.082  -3.950  1.00 16.83           O  
ANISOU 1351  O   HOH A1018     2025   2498   1870   -188   -131   -315       O  
HETATM 1352  O   HOH A1019      34.030  25.028  -2.203  1.00 10.73           O  
ANISOU 1352  O   HOH A1019     1584   1392   1100   -119    185   -207       O  
HETATM 1353  O   HOH A1020      43.037   4.863  13.136  1.00 26.30           O  
ANISOU 1353  O   HOH A1020     3355   3558   3081    614   1407    395       O  
HETATM 1354  O   HOH A1021      34.818  15.189 -13.555  1.00 15.64           O  
ANISOU 1354  O   HOH A1021     3332   1634    977   -317   -333   -143       O  
HETATM 1355  O   HOH A1022      34.274   9.928  -5.099  1.00  8.37           O  
ANISOU 1355  O   HOH A1022     1358   1118    704     47    -58    123       O  
HETATM 1356  O   HOH A1023      43.297  10.433  -6.647  1.00 25.14           O  
ANISOU 1356  O   HOH A1023     3905   3385   2264    762  -1092  -1050       O  
HETATM 1357  O   HOH A1024      41.521  19.422  -2.798  1.00 27.48           O  
ANISOU 1357  O   HOH A1024     2753   4666   3024   1402   -336  -1365       O  
HETATM 1358  O   HOH A1025      28.912  28.014  -2.658  1.00 15.48           O  
ANISOU 1358  O   HOH A1025     2557   1336   1988    653   -575   -196       O  
HETATM 1359  O   HOH A1026      36.350   1.950  25.574  1.00 20.13           O  
ANISOU 1359  O   HOH A1026     3360   2924   1366   -584    158   -186       O  
HETATM 1360  O   HOH A1027      46.633  16.989  10.875  1.00  8.88           O  
ANISOU 1360  O   HOH A1027      831   1527   1015     -8    110     29       O  
HETATM 1361  O   HOH A1028      24.125  31.426  -0.237  1.00 29.97           O  
ANISOU 1361  O   HOH A1028     4135   4376   2877  -1007   -209   -698       O  
HETATM 1362  O   HOH A1029      47.170  19.378  12.079  1.00 11.52           O  
ANISOU 1362  O   HOH A1029     1690   1495   1193    -70    155    303       O  
HETATM 1363  O   HOH A1030      32.263  21.724  15.823  1.00 49.21           O  
ANISOU 1363  O   HOH A1030     6618   4979   7099    776   1367    229       O  
HETATM 1364  O   HOH A1031      40.943  13.843  14.199  1.00  9.45           O  
ANISOU 1364  O   HOH A1031      999   1315   1278   -148     25   -305       O  
HETATM 1365  O   HOH A1032      25.516  16.936  12.837  1.00 21.82           O  
ANISOU 1365  O   HOH A1032     2471   2790   3029    483   1014    130       O  
HETATM 1366  O   HOH A1033      26.811   6.838  23.776  1.00 19.82           O  
ANISOU 1366  O   HOH A1033     2804   2926   1801    199    159    -70       O  
HETATM 1367  O   HOH A1034      34.634  -0.980  17.808  1.00 27.15           O  
ANISOU 1367  O   HOH A1034     6709   2106   1501    102   -753   -459       O  
HETATM 1368  O   HOH A1035      31.509  -2.005  16.071  1.00 16.00           O  
ANISOU 1368  O   HOH A1035     3070   1204   1803     31    -77   -309       O  
HETATM 1369  O   HOH A1036      36.559   1.200  18.465  1.00 15.68           O  
ANISOU 1369  O   HOH A1036     2350   2634    976    369     55     29       O  
HETATM 1370  O   HOH A1037      34.005  19.915  19.288  1.00 23.42           O  
ANISOU 1370  O   HOH A1037     3238   3419   2242   -585    122   -272       O  
HETATM 1371  O   HOH A1038      44.460   8.299  23.656  1.00 19.45           O  
ANISOU 1371  O   HOH A1038     3060   2358   1973    439   -710    282       O  
HETATM 1372  O   HOH A1039      43.150   6.523   6.042  1.00 13.81           O  
ANISOU 1372  O   HOH A1039     1418   2178   1651    492    251   -146       O  
HETATM 1373  O   HOH A1040      43.099  12.097   1.678  1.00  9.55           O  
ANISOU 1373  O   HOH A1040     1667    986    976   -191    -78    -78       O  
HETATM 1374  O   HOH A1041      23.059  31.351   4.945  1.00 12.91           O  
ANISOU 1374  O   HOH A1041     1308   1636   1961   -101   -363    262       O  
HETATM 1375  O   HOH A1042      34.145  29.350  12.299  1.00 12.40           O  
ANISOU 1375  O   HOH A1042     1227   1391   2094   -235    128   -540       O  
HETATM 1376  O   HOH A1043      42.485  14.380   2.896  1.00  8.89           O  
ANISOU 1376  O   HOH A1043     1089   1231   1055     35    -97   -188       O  
HETATM 1377  O   HOH A1044      42.576   9.300  -4.192  1.00 11.74           O  
ANISOU 1377  O   HOH A1044     1493   1722   1247   -256    332   -473       O  
HETATM 1378  O   HOH A1045      39.989   5.654   0.812  1.00 10.47           O  
ANISOU 1378  O   HOH A1045     1472   1322   1186     79   -183    -89       O  
HETATM 1379  O   HOH A1046      39.416   9.876 -10.787  1.00 14.66           O  
ANISOU 1379  O   HOH A1046     1963   2363   1246   -168    212    -50       O  
HETATM 1380  O   HOH A1047      39.074   3.067  -7.791  1.00 21.85           O  
ANISOU 1380  O   HOH A1047     2276   3082   2945    974    915    965       O  
HETATM 1381  O   HOH A1048      39.538   2.987   1.409  1.00 14.46           O  
ANISOU 1381  O   HOH A1048     2178   1535   1781    -81   -482    177       O  
HETATM 1382  O   HOH A1049      40.710  -2.400  -3.236  1.00 23.98           O  
ANISOU 1382  O   HOH A1049     3613   2349   3150   1204    706    336       O  
HETATM 1383  O   HOH A1050      22.766  19.932  -5.700  1.00 23.23           O  
ANISOU 1383  O   HOH A1050     2311   2607   3907    425    131   -240       O  
HETATM 1384  O   HOH A1051      27.066  24.521  11.096  1.00 14.11           O  
ANISOU 1384  O   HOH A1051     1690   1640   2030   -190    252   -367       O  
HETATM 1385  O   HOH A1052      30.521  30.096 -34.636  1.00 19.35           O  
ANISOU 1385  O   HOH A1052     2447   1659   3247   -354  -1017    -88       O  
HETATM 1386  O   HOH A1053      22.554  22.664  -4.627  1.00 20.45           O  
ANISOU 1386  O   HOH A1053     2401   2497   2871    489     69    571       O  
HETATM 1387  O   HOH A1054      19.065  15.388   0.936  1.00 42.39           O  
ANISOU 1387  O   HOH A1054     2910   5152   8044    823   1590    323       O  
HETATM 1388  O   HOH A1055      26.993   4.847  -8.702  1.00 23.78           O  
ANISOU 1388  O   HOH A1055     4253   2921   1863  -1469  -1210    355       O  
HETATM 1389  O   HOH A1056      31.470   2.815  -7.349  1.00 23.21           O  
ANISOU 1389  O   HOH A1056     3366   2118   3336   -483    793   -637       O  
HETATM 1390  O   HOH A1057      22.516   7.955  -1.256  1.00 21.15           O  
ANISOU 1390  O   HOH A1057     1828   2736   3473   -186    867   -745       O  
HETATM 1391  O   HOH A1058      33.059  28.440  -3.265  1.00 36.60           O  
ANISOU 1391  O   HOH A1058     3352   6917   3635   -940    621    326       O  
HETATM 1392  O   HOH A1059      27.013 -10.750  -3.833  1.00 22.63           O  
ANISOU 1392  O   HOH A1059     3883   1557   3160    791  -1757   -983       O  
HETATM 1393  O   HOH A1060      24.127  -4.381  -4.468  1.00 24.10           O  
ANISOU 1393  O   HOH A1060     2838   2187   4132    127  -1512  -1206       O  
HETATM 1394  O   HOH A1061      26.054  15.918 -13.712  1.00 35.30           O  
ANISOU 1394  O   HOH A1061     4694   3926   4793    410   -583   1698       O  
HETATM 1395  O   HOH A1062      28.122  22.467 -12.938  1.00 36.24           O  
ANISOU 1395  O   HOH A1062     4120   3351   6297   1881    312  -1989       O  
HETATM 1396  O   HOH A1063      25.939  22.753  -6.202  1.00 19.88           O  
ANISOU 1396  O   HOH A1063     3620   1354   2581     -6  -1783   -202       O  
HETATM 1397  O   HOH A1064      31.843  21.385  -0.973  1.00 12.72           O  
ANISOU 1397  O   HOH A1064     1646   1597   1589    195     85     68       O  
HETATM 1398  O   HOH A1065      45.494  16.495  -2.643  1.00 32.70           O  
ANISOU 1398  O   HOH A1065     3172   5440   3813  -2001   -861    684       O  
HETATM 1399  O   HOH A1066      40.577  11.651  27.241  1.00 19.18           O  
ANISOU 1399  O   HOH A1066     2625   2635   2028    572  -1041     38       O  
HETATM 1400  O   HOH A1067      42.718  24.831   9.698  1.00 15.48           O  
ANISOU 1400  O   HOH A1067     1960   1668   2255    273     71    163       O  
HETATM 1401  O   HOH A1068      48.439  20.846  10.096  1.00 11.43           O  
ANISOU 1401  O   HOH A1068     1238   1889   1215   -114   -163    283       O  
HETATM 1402  O   HOH A1069      39.915   2.846   4.060  1.00 20.23           O  
ANISOU 1402  O   HOH A1069     3323   2418   1946   -811   -854    124       O  
HETATM 1403  O   HOH A1070      27.544  29.742   4.550  1.00 25.56           O  
ANISOU 1403  O   HOH A1070     2873   2408   4432     27  -1691   -215       O  
HETATM 1404  O   HOH A1071      40.631  14.030  20.184  1.00 11.79           O  
ANISOU 1404  O   HOH A1071     1934   1589    955    -66     -5    148       O  
HETATM 1405  O   HOH A1072      27.855  11.605  23.434  1.00 28.84           O  
ANISOU 1405  O   HOH A1072     3547   5120   2290   -919    474    775       O  
HETATM 1406  O   HOH A1073      39.851  18.421  26.933  1.00 19.32           O  
ANISOU 1406  O   HOH A1073     2689   2096   2556   -265     96   -982       O  
HETATM 1407  O   HOH A1074      45.152  10.287  25.050  1.00 27.97           O  
ANISOU 1407  O   HOH A1074     3016   6554   1060    712   -616    396       O  
HETATM 1408  O   HOH A1075      40.970   5.183  23.585  1.00 33.48           O  
ANISOU 1408  O   HOH A1075     4549   4618   3555    -71    769    401       O  
HETATM 1409  O   HOH A1076      45.975   8.701   7.572  1.00 31.93           O  
ANISOU 1409  O   HOH A1076     3608   2390   6133    888    792   -216       O  
HETATM 1410  O   HOH A1077      38.767  11.441 -12.905  1.00 31.34           O  
ANISOU 1410  O   HOH A1077     4226   5737   1943  -1570   -501   1454       O  
HETATM 1411  O   HOH A1078      39.220   0.423   5.268  1.00 15.89           O  
ANISOU 1411  O   HOH A1078     2243   1988   1806   -625   -522    -97       O  
HETATM 1412  O   HOH A1079      23.131  14.909   5.100  1.00 27.09           O  
ANISOU 1412  O   HOH A1079     4914   2322   3058    665   1423    812       O  
HETATM 1413  O   HOH A1080      31.070  28.754  -1.246  1.00 15.16           O  
ANISOU 1413  O   HOH A1080     2015   1919   1827   -195    -53    363       O  
HETATM 1414  O   HOH A1081      40.958   1.620  13.020  1.00 17.13           O  
ANISOU 1414  O   HOH A1081     2778   2399   1332    422   -224   -296       O  
HETATM 1415  O   HOH A1082      40.378  -0.720  11.973  1.00 17.50           O  
ANISOU 1415  O   HOH A1082     2267   2057   2324    199   -493    455       O  
HETATM 1416  O   HOH A1083      41.317   7.506  24.346  1.00 34.31           O  
ANISOU 1416  O   HOH A1083     7067   3024   2943    434   -500   1337       O  
HETATM 1417  O   HOH A1084      24.981   1.596  18.370  1.00 23.91           O  
ANISOU 1417  O   HOH A1084     3360   2618   3109   -461    669   -564       O  
HETATM 1418  O   HOH A1085      20.532   3.281   1.148  1.00 34.48           O  
ANISOU 1418  O   HOH A1085     2693   4142   6264    -95   -662   -629       O  
HETATM 1419  O   HOH A1086      22.671   1.734  -3.291  1.00 16.10           O  
ANISOU 1419  O   HOH A1086     1446   1626   3045    -86   -831    379       O  
HETATM 1420  O   HOH A1087      38.564  20.741  26.632  1.00 29.98           O  
ANISOU 1420  O   HOH A1087     4150   2452   4791   -923    735    236       O  
HETATM 1421  O   HOH A1088      27.440  -7.808   9.475  1.00 30.86           O  
ANISOU 1421  O   HOH A1088     3750   2686   5289    127   1331   1419       O  
HETATM 1422  O   HOH A1089      20.158   9.660  16.784  1.00 26.17           O  
ANISOU 1422  O   HOH A1089     3267   2985   3690   -806   1118    340       O  
HETATM 1423  O   HOH A1090      23.698  18.196  11.816  1.00 42.76           O  
ANISOU 1423  O   HOH A1090     2915   5825   7506  -1728  -1950   1032       O  
HETATM 1424  O   HOH A1091      24.406  18.996   8.651  1.00 27.93           O  
ANISOU 1424  O   HOH A1091     2182   3850   4578    110    336    559       O  
HETATM 1425  O   HOH A1092      39.399  20.784  17.011  1.00 29.20           O  
ANISOU 1425  O   HOH A1092     4376   4432   2287   -958   -502   -493       O  
HETATM 1426  O   HOH A1093      30.926  21.153 -14.754  1.00 15.57           O  
ANISOU 1426  O   HOH A1093     2827   1741   1347    120   -614    472       O  
HETATM 1427  O   HOH A1094      11.667  18.564  -2.781  1.00 25.61           O  
ANISOU 1427  O   HOH A1094     2550   1968   5214    546  -1098   -444       O  
HETATM 1428  O   HOH A1095      25.300  20.123  -6.393  1.00 17.19           O  
ANISOU 1428  O   HOH A1095     2744   1856   1932    330   -239   -170       O  
HETATM 1429  O   HOH A1096      41.292  14.794  -7.816  1.00 21.36           O  
ANISOU 1429  O   HOH A1096     2830   2049   3238   -371    576    -80       O  
HETATM 1430  O   HOH A1097      39.523   6.824 -14.234  1.00 26.70           O  
ANISOU 1430  O   HOH A1097     4668   2740   2736    -26    371   -376       O  
HETATM 1431  O   HOH A1098      31.585   9.887  -3.586  1.00 15.78           O  
ANISOU 1431  O   HOH A1098     2062   1682   2253    273    282   -362       O  
HETATM 1432  O   HOH A1099      37.609  26.339  14.310  1.00 21.63           O  
ANISOU 1432  O   HOH A1099     3874   2495   1850   -765    -67    300       O  
HETATM 1433  O   HOH A1100      33.531  22.870  14.125  1.00 20.36           O  
ANISOU 1433  O   HOH A1100     3237   1930   2568    359    479   -221       O  
HETATM 1434  O   HOH A1101      44.564  10.193  -2.555  1.00 16.93           O  
ANISOU 1434  O   HOH A1101     2090   2642   1700   -556    184  -1086       O  
HETATM 1435  O   HOH A1102      32.533   5.549 -14.740  1.00 23.50           O  
ANISOU 1435  O   HOH A1102     4634   2471   1824  -1028    465   -360       O  
HETATM 1436  O   HOH A1103      43.123   6.550  -3.815  1.00 16.35           O  
ANISOU 1436  O   HOH A1103     2017   2116   2080    141   -118   -398       O  
HETATM 1437  O   HOH A1104      36.557  24.260  15.777  1.00 24.43           O  
ANISOU 1437  O   HOH A1104     4688   1638   2956   -588    395   -801       O  
HETATM 1438  O   HOH A1105      36.945  19.307  18.716  1.00 18.43           O  
ANISOU 1438  O   HOH A1105     2809   2271   1923    315   -448     35       O  
HETATM 1439  O   HOH A1106      23.498  -3.336  11.860  1.00 25.02           O  
ANISOU 1439  O   HOH A1106     3434   2691   3381    847   1103    445       O  
HETATM 1440  O   HOH A1107      34.522   0.703 -17.864  1.00 34.35           O  
ANISOU 1440  O   HOH A1107     7559   2980   2514   -817   -109    660       O  
HETATM 1441  O   HOH A1108      30.029  34.599   1.475  1.00 32.31           O  
ANISOU 1441  O   HOH A1108     5143   3393   3740   -300  -1145   -386       O  
HETATM 1442  O   HOH A1109      13.252  17.884  -4.539  1.00 29.11           O  
ANISOU 1442  O   HOH A1109     3701   2585   4774   -625   -570   -991       O  
HETATM 1443  O   HOH A1110      22.459  32.378   9.915  1.00 23.37           O  
ANISOU 1443  O   HOH A1110     1898   2797   4187    680    229  -1015       O  
HETATM 1444  O   HOH A1111      19.752   5.813  15.520  1.00 35.70           O  
ANISOU 1444  O   HOH A1111     4049   5218   4297     44    992   1006       O  
HETATM 1445  O   HOH A1112      43.047   2.504  12.742  1.00 43.38           O  
ANISOU 1445  O   HOH A1112     5665   3183   7635   1559   1324  -1039       O  
HETATM 1446  O   HOH A1113      43.570   5.630  17.286  1.00 19.10           O  
ANISOU 1446  O   HOH A1113     2423   2636   2199    331   -242   -402       O  
HETATM 1447  O   HOH A1114      22.486  23.891  -2.467  1.00 21.31           O  
ANISOU 1447  O   HOH A1114     2568   2411   3118     63     -5    975       O  
HETATM 1448  O   HOH A1115      29.905  19.382 -26.721  1.00 22.49           O  
ANISOU 1448  O   HOH A1115     2795   3381   2369    104    478   -532       O  
HETATM 1449  O   HOH A1116      44.645  24.766   3.105  1.00 25.89           O  
ANISOU 1449  O   HOH A1116     2768   2773   4298  -1196    502    -25       O  
HETATM 1450  O   HOH A1117      40.577   5.271 -10.203  1.00 35.50           O  
ANISOU 1450  O   HOH A1117     5748   3515   4226    386  -2031    391       O  
HETATM 1451  O   HOH A1118      31.649   1.045  -5.617  1.00 26.32           O  
ANISOU 1451  O   HOH A1118     3594   2508   3901    192   -151   -335       O  
HETATM 1452  O   HOH A1119      33.305  24.706  -9.284  1.00 17.98           O  
ANISOU 1452  O   HOH A1119     3729   1300   1804   -467    750   -127       O  
HETATM 1453  O   HOH A1120      23.050   1.627  -6.072  1.00 23.90           O  
ANISOU 1453  O   HOH A1120     3449   2037   3594    412   -718   -256       O  
HETATM 1454  O   HOH A1121      29.525   1.642 -18.369  1.00 40.76           O  
ANISOU 1454  O   HOH A1121     4599   6798   4090   -303   1498   1123       O  
HETATM 1455  O   HOH A1122      26.939  31.580   6.506  1.00 50.36           O  
ANISOU 1455  O   HOH A1122     5739   6769   6625   -375   -291   -753       O  
HETATM 1456  O   HOH A1123      24.656  31.092   2.569  1.00 16.96           O  
ANISOU 1456  O   HOH A1123     1878   1959   2607    240    -22    414       O  
HETATM 1457  O   HOH A1124      29.531  33.966  12.022  1.00 18.36           O  
ANISOU 1457  O   HOH A1124     1719   2087   3172   -119    134   -542       O  
HETATM 1458  O   HOH A1125      22.561   5.140   0.848  1.00 25.87           O  
ANISOU 1458  O   HOH A1125     2952   4221   2657   -540    477  -1030       O  
HETATM 1459  O   HOH A1126      19.352  13.603  11.802  1.00 34.58           O  
ANISOU 1459  O   HOH A1126     2694   4682   5762   -248   -745    355       O  
HETATM 1460  O   HOH A1127      32.716  30.942 -30.968  1.00 20.91           O  
ANISOU 1460  O   HOH A1127     2611   2682   2652   -126    602    228       O  
HETATM 1461  O   HOH A1128      33.189  25.528 -30.964  1.00 22.20           O  
ANISOU 1461  O   HOH A1128     2925   2087   3422    247    -21    143       O  
HETATM 1462  O   HOH A1129      47.980   6.599 -31.690  1.00 41.90           O  
ANISOU 1462  O   HOH A1129     6446   5239   4234   -658    -58    527       O  
HETATM 1463  O   HOH A1130      35.115  27.418 -31.114  1.00 25.57           O  
ANISOU 1463  O   HOH A1130     3483   2623   3608   -289   -564    934       O  
HETATM 1464  O   HOH A1131      40.881  22.620 -30.156  1.00 25.94           O  
ANISOU 1464  O   HOH A1131     3111   2409   4335    505  -1361   -349       O  
HETATM 1465  O   HOH A1132      29.728  -8.587  17.035  1.00 33.75           O  
ANISOU 1465  O   HOH A1132     2639   4256   5929   1551   -524   1302       O  
HETATM 1466  O   HOH A1133      45.058   5.497 -31.257  1.00 39.33           O  
ANISOU 1466  O   HOH A1133     4605   2496   7843    263   -241    -80       O  
HETATM 1467  O   HOH A1134      17.367  22.406 -28.724  1.00 27.80           O  
ANISOU 1467  O   HOH A1134     3732   4081   2751    860    434    379       O  
HETATM 1468  O   HOH A1135      19.466  23.790 -29.666  1.00 25.70           O  
ANISOU 1468  O   HOH A1135     3287   3061   3418   1083    309    -64       O  
HETATM 1469  O   HOH A1136      41.987  -0.234  16.327  1.00 37.63           O  
ANISOU 1469  O   HOH A1136     3374   4673   6250   -828   -164  -1063       O  
HETATM 1470  O   HOH A1137      28.101  20.908 -27.347  1.00 41.23           O  
ANISOU 1470  O   HOH A1137     4623   6534   4508    701   -449  -1660       O  
HETATM 1471  O   HOH A1138      43.731  15.107 -23.775  1.00 27.30           O  
ANISOU 1471  O   HOH A1138     3186   4733   2455    142    109   -276       O  
HETATM 1472  O   HOH A1139      24.474  14.613 -21.945  1.00 31.10           O  
ANISOU 1472  O   HOH A1139     3333   5050   3433    306   1546   -465       O  
HETATM 1473  O   HOH A1140      27.485   9.235 -20.427  1.00 23.46           O  
ANISOU 1473  O   HOH A1140     3185   3597   2133    107    -64    -23       O  
HETATM 1474  O   HOH A1141      42.178  18.766 -19.727  1.00 33.98           O  
ANISOU 1474  O   HOH A1141     5914   3433   3565  -1956   -501    563       O  
HETATM 1475  O   HOH A1142      43.515  11.269 -18.194  1.00 28.17           O  
ANISOU 1475  O   HOH A1142     3794   4735   2176    270   -246   1075       O  
HETATM 1476  O   HOH A1143      20.079   9.374 -25.379  1.00 35.78           O  
ANISOU 1476  O   HOH A1143     3136   5811   4648   -262    852  -1698       O  
HETATM 1477  O   HOH A1144      32.833   2.024 -17.042  1.00 42.67           O  
ANISOU 1477  O   HOH A1144     6415   5361   4439   -802    848   -183       O  
HETATM 1478  O   HOH A1145      28.606   9.818 -16.641  1.00 31.14           O  
ANISOU 1478  O   HOH A1145     3948   4360   3525   -862    995  -1836       O  
HETATM 1479  O   HOH A1146      40.528  17.502 -15.819  1.00 42.27           O  
ANISOU 1479  O   HOH A1146     7180   6065   2814   -685    634  -1846       O  
HETATM 1480  O   HOH A1147      40.277   7.415 -11.790  1.00 22.84           O  
ANISOU 1480  O   HOH A1147     2320   3628   2729   -307    649   -912       O  
HETATM 1481  O   HOH A1148      31.915   4.716 -11.212  1.00 43.67           O  
ANISOU 1481  O   HOH A1148     7887   2894   5811   1255   1443    317       O  
HETATM 1482  O   HOH A1149      29.294  23.610 -10.086  1.00 26.18           O  
ANISOU 1482  O   HOH A1149     3410   2582   3955    577   -616   -347       O  
HETATM 1483  O   HOH A1150      25.373  21.928 -10.213  1.00 34.84           O  
ANISOU 1483  O   HOH A1150     4510   4013   4713   1324  -2167    732       O  
HETATM 1484  O   HOH A1151      40.513  16.758  -9.887  1.00 31.35           O  
ANISOU 1484  O   HOH A1151     4380   4408   3124   -713    346    313       O  
HETATM 1485  O   HOH A1152      16.919  25.571  -8.356  1.00 31.63           O  
ANISOU 1485  O   HOH A1152     3739   3951   4327   -350    131    730       O  
HETATM 1486  O   HOH A1153      33.303  22.540 -15.095  1.00 26.89           O  
ANISOU 1486  O   HOH A1153     4092   2720   3405    219     76    955       O  
HETATM 1487  O   HOH A1154      38.384   9.072 -15.663  1.00 32.70           O  
ANISOU 1487  O   HOH A1154     5050   4200   3174   1412    996   1019       O  
HETATM 1488  O   HOH A1155      35.541  25.333  -7.544  1.00 26.24           O  
ANISOU 1488  O   HOH A1155     4663   2690   2616   -719   -538      0       O  
HETATM 1489  O   HOH A1156      26.154   1.940  -6.886  1.00 33.61           O  
ANISOU 1489  O   HOH A1156     5467   4550   2752  -2748   -869   -559       O  
HETATM 1490  O   HOH A1157      16.356  23.518  -6.125  1.00 29.94           O  
ANISOU 1490  O   HOH A1157     2025   4292   5058    605    823     20       O  
HETATM 1491  O   HOH A1158      42.629  15.952  -6.311  1.00 32.52           O  
ANISOU 1491  O   HOH A1158     4542   5075   2740   -873    379    823       O  
HETATM 1492  O   HOH A1159      16.601  20.163  -6.817  1.00 33.49           O  
ANISOU 1492  O   HOH A1159     4195   4257   4271   -428  -1632   -447       O  
HETATM 1493  O   HOH A1160      22.378  12.781  -5.125  1.00 27.70           O  
ANISOU 1493  O   HOH A1160     2419   3991   4113    558   -502     31       O  
HETATM 1494  O   HOH A1161      33.559  -0.828  -4.595  1.00 23.13           O  
ANISOU 1494  O   HOH A1161     2794   2390   3602   -174    -74    191       O  
HETATM 1495  O   HOH A1162      29.968  28.619  -5.587  1.00 29.26           O  
ANISOU 1495  O   HOH A1162     4229   2443   4444    -96   1357   -778       O  
HETATM 1496  O   HOH A1163      34.953  27.149  -3.117  1.00 22.83           O  
ANISOU 1496  O   HOH A1163     3838   2437   2401   -359     38   -207       O  
HETATM 1497  O   HOH A1164      29.190  34.649  -1.294  1.00 27.33           O  
ANISOU 1497  O   HOH A1164     4226   2523   3633   -411   -693    805       O  
HETATM 1498  O   HOH A1165      45.466   6.603  -5.434  1.00 44.85           O  
ANISOU 1498  O   HOH A1165     3881   5706   7453   1626   2161   -649       O  
HETATM 1499  O   HOH A1166      26.384  34.307  -3.056  1.00 37.83           O  
ANISOU 1499  O   HOH A1166     3896   3967   6511  -1479    312    119       O  
HETATM 1500  O   HOH A1167      23.612  23.889  -6.642  1.00 31.36           O  
ANISOU 1500  O   HOH A1167     4046   3688   4183   -124    310    983       O  
HETATM 1501  O   HOH A1168      42.051   2.084   0.589  1.00 36.66           O  
ANISOU 1501  O   HOH A1168     3227   4294   6408   -545    610  -2446       O  
HETATM 1502  O   HOH A1169      27.233  32.175   1.198  1.00 32.14           O  
ANISOU 1502  O   HOH A1169     3992   2002   6217   -243   -802    457       O  
HETATM 1503  O   HOH A1170      42.638   5.366   1.404  1.00 25.22           O  
ANISOU 1503  O   HOH A1170     1793   2649   5140    753    349   -100       O  
HETATM 1504  O   HOH A1171      31.252  31.427   0.195  1.00 20.97           O  
ANISOU 1504  O   HOH A1171     2464   3222   2281     89   -560   1080       O  
HETATM 1505  O   HOH A1172      43.744   7.004   3.252  1.00 27.15           O  
ANISOU 1505  O   HOH A1172     3913   2765   3638   -232    160    588       O  
HETATM 1506  O   HOH A1173      42.259   3.722   5.023  1.00 22.48           O  
ANISOU 1506  O   HOH A1173     2002   3101   3440    247     99   -419       O  
HETATM 1507  O   HOH A1174      29.066  28.043   5.438  1.00 15.52           O  
ANISOU 1507  O   HOH A1174     2086   1823   1989   -253   -172    146       O  
HETATM 1508  O   HOH A1175      18.053  15.325   7.548  1.00 30.05           O  
ANISOU 1508  O   HOH A1175     4767   2417   4234    572    550   1028       O  
HETATM 1509  O   HOH A1176      28.373  29.339   9.011  1.00 22.36           O  
ANISOU 1509  O   HOH A1176     1559   2250   4688    344    227   -749       O  
HETATM 1510  O   HOH A1177      20.380  15.212   7.626  1.00 32.34           O  
ANISOU 1510  O   HOH A1177     3655   3834   4799    163   1856    280       O  
HETATM 1511  O   HOH A1178      20.072   8.683   9.409  1.00 19.56           O  
ANISOU 1511  O   HOH A1178     2050   2583   2800     60    530   -232       O  
HETATM 1512  O   HOH A1179      23.844  30.089   9.243  1.00 18.76           O  
ANISOU 1512  O   HOH A1179     2076   2840   2211    448    -55   -482       O  
HETATM 1513  O   HOH A1180      42.411  24.211  12.459  1.00 19.79           O  
ANISOU 1513  O   HOH A1180     2869   2266   2383    635    631   -254       O  
HETATM 1514  O   HOH A1181      43.272  -1.536   9.795  1.00 35.10           O  
ANISOU 1514  O   HOH A1181     3221   5067   5047   -806    -49    255       O  
HETATM 1515  O   HOH A1182      43.864   1.690   9.712  1.00 36.48           O  
ANISOU 1515  O   HOH A1182     4390   5743   3729    -18    -41   -749       O  
HETATM 1516  O   HOH A1183      20.839   9.394   0.898  1.00 35.79           O  
ANISOU 1516  O   HOH A1183     2975   4819   5805  -1389   -361   -768       O  
HETATM 1517  O   HOH A1184      26.265  29.684 -34.663  1.00 39.06           O  
ANISOU 1517  O   HOH A1184     4586   5791   4463   -522   1304  -2965       O  
HETATM 1518  O   HOH A1185      30.551  31.659 -32.340  1.00 17.07           O  
ANISOU 1518  O   HOH A1185     2105   2241   2138    137     47   -195       O  
HETATM 1519  O   HOH A1186      43.542  19.486 -28.087  1.00 38.21           O  
ANISOU 1519  O   HOH A1186     5646   6012   2861  -2730   -939    932       O  
HETATM 1520  O   HOH A1187      39.427  -3.016  13.538  1.00 50.14           O  
ANISOU 1520  O   HOH A1187     5793   6665   6593   -125  -4250    661       O  
HETATM 1521  O   HOH A1188      43.054  18.562 -24.523  1.00 36.66           O  
ANISOU 1521  O   HOH A1188     6060   4756   3114  -3016  -1846    197       O  
HETATM 1522  O   HOH A1189      22.271  17.651 -28.685  1.00 38.30           O  
ANISOU 1522  O   HOH A1189     4346   3913   6295    210    199   1215       O  
HETATM 1523  O   HOH A1190      20.779  15.349 -28.057  1.00 42.73           O  
ANISOU 1523  O   HOH A1190     3288   4646   8302   1411   1306    -92       O  
HETATM 1524  O   HOH A1191      46.594   5.764   9.532  1.00 54.78           O  
ANISOU 1524  O   HOH A1191     6495   7801   6519    599   2613    -41       O  
HETATM 1525  O   HOH A1192      22.966  -1.283  14.462  1.00 39.31           O  
ANISOU 1525  O   HOH A1192     7611   3254   4070     69  -1347    775       O  
HETATM 1526  O   HOH A1193      25.413  12.624 -20.187  1.00 37.36           O  
ANISOU 1526  O   HOH A1193     6276   4839   3078    408   -206   -528       O  
HETATM 1527  O   HOH A1194      29.348   5.980 -19.273  1.00 34.59           O  
ANISOU 1527  O   HOH A1194     3798   5559   3787     57    496  -1219       O  
HETATM 1528  O   HOH A1195      29.556   8.369 -18.823  1.00 30.87           O  
ANISOU 1528  O   HOH A1195     4005   5344   2378   -185    439  -1041       O  
HETATM 1529  O   HOH A1196      39.060  15.400 -15.151  1.00 41.07           O  
ANISOU 1529  O   HOH A1196     5472   5860   4275  -1307  -1235   -721       O  
HETATM 1530  O   HOH A1197      39.914  18.402 -13.297  1.00 29.95           O  
ANISOU 1530  O   HOH A1197     3446   4180   3753     -8    994   -231       O  
HETATM 1531  O   HOH A1198      37.965  21.731 -13.442  1.00 23.71           O  
ANISOU 1531  O   HOH A1198     3601   2923   2483   -729     66    -43       O  
HETATM 1532  O   HOH A1199      36.601   3.994 -13.423  1.00 38.04           O  
ANISOU 1532  O   HOH A1199     8606   3449   2397   -559   -945  -1482       O  
HETATM 1533  O   HOH A1200      25.455  17.110 -11.775  1.00 39.16           O  
ANISOU 1533  O   HOH A1200     2701   6607   5571   -101  -1187  -1858       O  
HETATM 1534  O   HOH A1201      25.958   6.742  -9.725  1.00 42.49           O  
ANISOU 1534  O   HOH A1201     7792   4782   3571    994  -2464   -843       O  
HETATM 1535  O   HOH A1202      41.288  11.405  -9.609  1.00 26.44           O  
ANISOU 1535  O   HOH A1202     4183   3726   2136  -1102    739   -629       O  
HETATM 1536  O   HOH A1203      26.891  23.877  -8.662  1.00 26.46           O  
ANISOU 1536  O   HOH A1203     3394   4240   2420    556   -582    338       O  
HETATM 1537  O   HOH A1204      29.345  27.738  -7.772  1.00 37.95           O  
ANISOU 1537  O   HOH A1204     6093   3932   4393     85   -783   1786       O  
HETATM 1538  O   HOH A1205      41.078  21.138  -7.258  1.00 31.17           O  
ANISOU 1538  O   HOH A1205     3054   4897   3893   -944   -239   -595       O  
HETATM 1539  O   HOH A1206      24.842  11.959  -5.655  1.00 16.59           O  
ANISOU 1539  O   HOH A1206     2096   2147   2060    -29   -402   -284       O  
HETATM 1540  O   HOH A1207      44.972  15.607  -5.493  1.00 36.78           O  
ANISOU 1540  O   HOH A1207     3841   5532   4603   1044    641   1503       O  
HETATM 1541  O   HOH A1208      44.671  12.672  -6.324  1.00 37.36           O  
ANISOU 1541  O   HOH A1208     4342   4945   4909  -1334   1331   -346       O  
HETATM 1542  O   HOH A1209      44.110   5.829  -1.451  1.00 32.73           O  
ANISOU 1542  O   HOH A1209     3652   3965   4819   1618   -130    -15       O  
HETATM 1543  O   HOH A1210      40.261  25.850  -1.927  1.00 22.76           O  
ANISOU 1543  O   HOH A1210     3289   3420   1937  -1625   -300   -106       O  
HETATM 1544  O   HOH A1211      28.753  32.110  -0.521  1.00 28.19           O  
ANISOU 1544  O   HOH A1211     2998   3551   4163     36  -1081    503       O  
HETATM 1545  O   HOH A1212      23.976  34.034  -1.242  1.00 30.16           O  
ANISOU 1545  O   HOH A1212     2954   5654   2850   -941   -654   1692       O  
HETATM 1546  O   HOH A1213      28.897  31.492   3.154  1.00 24.36           O  
ANISOU 1546  O   HOH A1213     2168   3592   3494    865   -485   -283       O  
HETATM 1547  O   HOH A1214      43.065   2.359   7.357  1.00 39.40           O  
ANISOU 1547  O   HOH A1214     3141   5438   6390    174   1515    566       O  
HETATM 1548  O   HOH A1215      23.126  33.939   5.948  1.00 37.24           O  
ANISOU 1548  O   HOH A1215     6029   2958   5164   -358   1688   -756       O  
HETATM 1549  O   HOH A1216      28.427  14.236 -17.134  1.00 33.68           O  
ANISOU 1549  O   HOH A1216     2574   4007   6217    531   -636      4       O  
HETATM 1550  O   HOH A1217      45.081  20.122 -30.065  1.00 31.68           O  
ANISOU 1550  O   HOH A1217     5360   4934   1742  -2563  -1377    849       O  
HETATM 1551  O   HOH A1218      34.905  24.804 -11.588  1.00 30.90           O  
ANISOU 1551  O   HOH A1218     6171   2620   2948   -403   2144    526       O  
HETATM 1552  O   HOH A1219      38.219   3.390 -11.026  1.00 46.21           O  
ANISOU 1552  O   HOH A1219     7631   3225   6701    706   -819   -268       O  
HETATM 1553  O   HOH A1220      43.225  22.045 -29.402  1.00 30.29           O  
ANISOU 1553  O   HOH A1220     3627   3347   4536   -115  -1408    466       O  
HETATM 1554  O   HOH A1221      41.379  -0.836   5.186  1.00 42.84           O  
ANISOU 1554  O   HOH A1221     5901   4801   5574   -685  -2419    833       O  
HETATM 1555  O   HOH A1222      41.394  21.894 -49.901  1.00 31.05           O  
ANISOU 1555  O   HOH A1222     4291   4548   2959  -1461   1114   -206       O  
HETATM 1556  O   HOH A1223      35.336  27.573 -51.126  1.00 30.71           O  
ANISOU 1556  O   HOH A1223     4756   3839   3072  -1429    335   -636       O  
HETATM 1557  O   HOH A1224      39.084  27.985 -48.129  1.00 33.74           O  
ANISOU 1557  O   HOH A1224     4091   5072   3657  -1444    927   -289       O  
HETATM 1558  O   HOH A1225      17.640  14.384 -42.908  1.00 42.74           O  
ANISOU 1558  O   HOH A1225     6461   3783   5995   1798   1283    -15       O  
HETATM 1559  O   HOH A1226      23.439  20.517 -34.612  1.00 39.76           O  
ANISOU 1559  O   HOH A1226     4364   4908   5833   2182    852   2336       O  
HETATM 1560  O   HOH A1227      28.679  16.673 -15.948  1.00 25.81           O  
ANISOU 1560  O   HOH A1227     3463   3934   2409    909  -1040  -1108       O  
HETATM 1561  O   HOH A1228      36.976  28.447 -29.505  1.00 38.40           O  
ANISOU 1561  O   HOH A1228     7284   3164   4143   -616   1649   -492       O  
HETATM 1562  O   HOH A1229      41.023  13.137 -15.887  1.00 39.68           O  
ANISOU 1562  O   HOH A1229     6046   5989   3043   -141   1027   -918       O  
HETATM 1563  O   HOH A1230      21.643  14.689 -24.577  1.00 41.62           O  
ANISOU 1563  O   HOH A1230     5375   4858   5582   1069   2351  -1635       O  
HETATM 1564  O   HOH A1231      41.297   8.052 -18.732  1.00 44.05           O  
ANISOU 1564  O   HOH A1231     5970   5983   4785    614  -3000    603       O  
HETATM 1565  O   HOH A1232      33.953  20.785 -17.677  1.00 29.43           O  
ANISOU 1565  O   HOH A1232     2759   2646   5777    -72    997    -59       O  
HETATM 1566  O   HOH A1233      35.447  23.201 -13.295  1.00 29.62           O  
ANISOU 1566  O   HOH A1233     4808   3124   3321   -708    430   -506       O  
HETATM 1567  O   HOH A1234      29.179  -0.059  -5.097  1.00 15.64           O  
ANISOU 1567  O   HOH A1234     2299   1664   1980    189    237   -430       O  
HETATM 1568  O   HOH A1235      43.690  18.613  -1.854  1.00 29.94           O  
ANISOU 1568  O   HOH A1235     3349   5729   2298   -203     80   1520       O  
HETATM 1569  O   HOH A1236      42.454  25.328  -2.947  1.00 36.53           O  
ANISOU 1569  O   HOH A1236     4874   5601   3406   -875   1500   1176       O  
HETATM 1570  O   HOH A1237      41.063  29.013  -1.943  1.00 45.38           O  
ANISOU 1570  O   HOH A1237     6937   6033   4271   -892  -2156   1825       O  
HETATM 1571  O   HOH A1238      19.654  11.198   9.371  1.00 29.02           O  
ANISOU 1571  O   HOH A1238     3489   3306   4231   -279   1201    663       O  
HETATM 1572  O   HOH A1239      44.796   2.506  15.394  1.00 43.18           O  
ANISOU 1572  O   HOH A1239     5652   4060   6697   1117     31    242       O  
HETATM 1573  O   HOH A1240      30.778  26.133  -9.559  1.00 36.47           O  
ANISOU 1573  O   HOH A1240     6794   4215   2848    937   -592   1072       O  
HETATM 1574  O   HOH A1241      39.101  -2.284  20.585  1.00 45.64           O  
ANISOU 1574  O   HOH A1241     6707   4591   6043   -208  -2608   1694       O  
HETATM 1575  O   HOH A1242      42.893   3.741  22.013  1.00 36.41           O  
ANISOU 1575  O   HOH A1242     6421   4324   3090  -1424    -85    799       O  
HETATM 1576  O   HOH A1243      45.190  26.090  10.018  0.33 19.19           O  
ANISOU 1576  O   HOH A1243     2430   2430   2430      0      0      0       O  
HETATM 1577  O   HOH A1244      43.628   3.249   2.060  1.00 46.19           O  
ANISOU 1577  O   HOH A1244     6651   3829   7069   -900  -1741   1007       O  
HETATM 1578  O   HOH A1245      20.460   1.931   8.055  1.00 16.46           O  
ANISOU 1578  O   HOH A1245     1752   1556   2945   -655    215   -239       O  
HETATM 1579  O   HOH A1246      50.249   5.353  16.633  1.00 46.48           O  
ANISOU 1579  O   HOH A1246     6719   5500   5441   1248    283    583       O  
HETATM 1580  O   HOH A1247      22.457  12.774   6.252  1.00 38.65           O  
ANISOU 1580  O   HOH A1247     5788   3806   5092   1114   -244   1573       O  
HETATM 1581  O   HOH A1248      45.190  26.090  12.496  0.33 48.15           O  
ANISOU 1581  O   HOH A1248     6576   6576   5142      0      0      0       O  
HETATM 1582  O   HOH A1249      43.185  -0.135   7.037  1.00 43.83           O  
ANISOU 1582  O   HOH A1249     5080   4849   6724    299   1766  -2254       O  
HETATM 1583  O   HOH A1250      31.789  -3.731  18.360  1.00 37.37           O  
ANISOU 1583  O   HOH A1250     7023   4283   2894   -782    480    747       O  
HETATM 1584  O   HOH A1251      32.407  29.305 -28.789  1.00 35.28           O  
ANISOU 1584  O   HOH A1251     5302   3325   4779    252     52    419       O  
HETATM 1585  O   HOH A1252      18.863   1.542  10.251  1.00 41.79           O  
ANISOU 1585  O   HOH A1252     6278   5441   4159  -1265   1677   -999       O  
HETATM 1586  O   HOH A1253      24.013  -9.466  -3.189  1.00 53.05           O  
ANISOU 1586  O   HOH A1253     6138   7449   6568  -1098   -246    -89       O  
HETATM 1587  O   HOH A1254      46.452  11.893  -3.796  1.00 42.17           O  
ANISOU 1587  O   HOH A1254     4192   5634   6198    405   2176   -543       O  
HETATM 1588  O   HOH A1255      42.890  26.290  13.874  1.00 43.56           O  
ANISOU 1588  O   HOH A1255     5825   5407   5319    748   -449   1463       O  
HETATM 1589  O   HOH A1256      29.614  31.249  -4.890  1.00 42.26           O  
ANISOU 1589  O   HOH A1256     5885   5179   4992    -68  -1116   1494       O  
HETATM 1590  O   HOH A1257      45.525  14.852  26.306  1.00 46.70           O  
ANISOU 1590  O   HOH A1257     4441   5602   7701   -707  -2104    432       O  
HETATM 1591  O   HOH A1258      33.471   2.720 -13.550  1.00 61.05           O  
ANISOU 1591  O   HOH A1258     7514   7770   7911    348    869   -333       O  
HETATM 1592  O   HOH A1259      34.239  -4.986  16.473  1.00 41.03           O  
ANISOU 1592  O   HOH A1259     8165   4103   3320  -1466   1094    302       O  
HETATM 1593  O   HOH A1260      29.209   4.860 -10.644  1.00 46.09           O  
ANISOU 1593  O   HOH A1260     6201   5401   5911  -1176    618  -1180       O  
CONECT  769 1331                                                                
CONECT 1274 1275 1276 1277 1278                                                 
CONECT 1275 1274                                                                
CONECT 1276 1274                                                                
CONECT 1277 1274                                                                
CONECT 1278 1274                                                                
CONECT 1279 1280 1281 1282 1283                                                 
CONECT 1280 1279                                                                
CONECT 1281 1279                                                                
CONECT 1282 1279                                                                
CONECT 1283 1279                                                                
CONECT 1284 1285 1286 1287 1288                                                 
CONECT 1285 1284                                                                
CONECT 1286 1284                                                                
CONECT 1287 1284                                                                
CONECT 1288 1284                                                                
CONECT 1289 1293 1320                                                           
CONECT 1290 1296 1303                                                           
CONECT 1291 1306 1310                                                           
CONECT 1292 1313 1317                                                           
CONECT 1293 1289 1294 1327                                                      
CONECT 1294 1293 1295 1298                                                      
CONECT 1295 1294 1296 1297                                                      
CONECT 1296 1290 1295 1327                                                      
CONECT 1297 1295                                                                
CONECT 1298 1294 1299                                                           
CONECT 1299 1298 1300                                                           
CONECT 1300 1299 1301 1302                                                      
CONECT 1301 1300                                                                
CONECT 1302 1300                                                                
CONECT 1303 1290 1304 1328                                                      
CONECT 1304 1303 1305 1307                                                      
CONECT 1305 1304 1306 1308                                                      
CONECT 1306 1291 1305 1328                                                      
CONECT 1307 1304                                                                
CONECT 1308 1305 1309                                                           
CONECT 1309 1308                                                                
CONECT 1310 1291 1311 1329                                                      
CONECT 1311 1310 1312 1314                                                      
CONECT 1312 1311 1313 1315                                                      
CONECT 1313 1292 1312 1329                                                      
CONECT 1314 1311                                                                
CONECT 1315 1312 1316                                                           
CONECT 1316 1315                                                                
CONECT 1317 1292 1318 1330                                                      
CONECT 1318 1317 1319 1321                                                      
CONECT 1319 1318 1320 1322                                                      
CONECT 1320 1289 1319 1330                                                      
CONECT 1321 1318                                                                
CONECT 1322 1319 1323                                                           
CONECT 1323 1322 1324                                                           
CONECT 1324 1323 1325 1326                                                      
CONECT 1325 1324                                                                
CONECT 1326 1324                                                                
CONECT 1327 1293 1296 1331                                                      
CONECT 1328 1303 1306 1331                                                      
CONECT 1329 1310 1313 1331                                                      
CONECT 1330 1317 1320 1331                                                      
CONECT 1331  769 1327 1328 1329                                                 
CONECT 1331 1330 1332 1333                                                      
CONECT 1332 1331 1333                                                           
CONECT 1333 1331 1332                                                           
MASTER      319    0    5    8    0    0   12    6 1545    1   62   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.