CNRS Nantes University UFIP UFIP
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***  test1  ***

elNémo ID: 22012513052493687

Job options:

ID        	=	 22012513052493687
JOBID     	=	 test1
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 test1

HEADER    LIPID BINDING PROTEIN                   11-OCT-10   3P6C              
TITLE     HUMAN ADIPOCYTE LIPID-BINDING PROTEIN FABP4 IN COMPLEX WITH CITRIC    
TITLE    2 ACID                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FATTY ACID-BINDING PROTEIN, ADIPOCYTE;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ADIPOCYTE LIPID-BINDING PROTEIN, ALBP, ADIPOCYTE-TYPE FATTY 
COMPND   5 ACID-BINDING PROTEIN, A-FABP, AFABP, FATTY ACID-BINDING PROTEIN 4;   
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: FABP4;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    LIPOCALIN, BETA BARREL, FATTY ACID BINDING PROTEIN, LIPID BINDING     
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.GONZALEZ,E.POZHARSKI                                              
REVDAT   3   25-FEB-15 3P6C    1       JRNL                                     
REVDAT   2   11-FEB-15 3P6C    1       JRNL                                     
REVDAT   1   13-APR-11 3P6C    0                                                
JRNL        AUTH   J.M.GONZALEZ,S.Z.FISHER                                      
JRNL        TITL   STRUCTURAL ANALYSIS OF IBUPROFEN BINDING TO HUMAN ADIPOCYTE  
JRNL        TITL 2 FATTY-ACID BINDING PROTEIN (FABP4).                          
JRNL        REF    ACTA CRYSTALLOGR F STRUCT     V.  71   163 2015              
JRNL        REF  2 BIOL COMMUN                                                  
JRNL        REFN                                                                
JRNL        PMID   25664790                                                     
JRNL        DOI    10.1107/S2053230X14027897                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.46                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 36054                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1807                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2293                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.82                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1900                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 110                          
REMARK   3   BIN FREE R VALUE                    : 0.2440                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1072                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 13                                      
REMARK   3   SOLVENT ATOMS            : 162                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.34000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 0.40000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.033         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.642         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1150 ; 0.022 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):   784 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1551 ; 2.259 ; 1.974       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  1918 ; 0.977 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   146 ; 6.165 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    47 ;35.683 ;24.255       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   219 ;12.838 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;16.934 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   173 ; 0.124 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1287 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   227 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   708 ; 2.492 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   296 ; 0.838 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1151 ; 3.739 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   442 ; 5.113 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   400 ; 7.365 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  1934 ; 2.061 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL                                        
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   4                                                                      
REMARK   4 3P6C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062011.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36136                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.09200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M SODIUM CITRATE, PH 6.5, VAPOR      
REMARK 280  DIFFUSION, TEMPERATURE 293K                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       16.11950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.50100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.65800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.50100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.11950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.65800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A  -7    CG   CD   OE1  NE2                                  
REMARK 470     GLN A  -6    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASN A    15     O    HOH A   148              1.79            
REMARK 500   O5   CIT A   133     O    HOH A   275              1.80            
REMARK 500   C5   CIT A   133     O    HOH A   230              2.01            
REMARK 500   O2   CIT A   133     O    HOH A   230              2.02            
REMARK 500   O3   CIT A   133     O    HOH A   230              2.12            
REMARK 500   O    HOH A   232     O    HOH A   291              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 106   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 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    MET A   0      -63.53    -25.59                                   
REMARK 500    PHE A  57      -72.88    -81.28                                   
REMARK 500    ASP A 110     -134.54     56.35                                   
REMARK 500    LYS A 120     -124.36     56.88                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 153        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH A 166        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH A 178        DISTANCE =  5.70 ANGSTROMS                       
REMARK 525    HOH A 214        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH A 234        DISTANCE =  6.02 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 133                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3P6D   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P6E   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P6F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P6G   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P6H   RELATED DB: PDB                                   
DBREF  3P6C A    0   131  UNP    P15090   FABP4_HUMAN      1    132             
SEQADV 3P6C GLN A   -7  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6C GLN A   -6  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6C MET A   -5  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6C GLY A   -4  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6C ARG A   -3  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6C GLY A   -2  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6C SER A   -1  UNP  P15090              EXPRESSION TAG                 
SEQRES   1 A  139  GLN GLN MET GLY ARG GLY SER MET CYS ASP ALA PHE VAL          
SEQRES   2 A  139  GLY THR TRP LYS LEU VAL SER SER GLU ASN PHE ASP ASP          
SEQRES   3 A  139  TYR MET LYS GLU VAL GLY VAL GLY PHE ALA THR ARG LYS          
SEQRES   4 A  139  VAL ALA GLY MET ALA LYS PRO ASN MET ILE ILE SER VAL          
SEQRES   5 A  139  ASN GLY ASP VAL ILE THR ILE LYS SER GLU SER THR PHE          
SEQRES   6 A  139  LYS ASN THR GLU ILE SER PHE ILE LEU GLY GLN GLU PHE          
SEQRES   7 A  139  ASP GLU VAL THR ALA ASP ASP ARG LYS VAL LYS SER THR          
SEQRES   8 A  139  ILE THR LEU ASP GLY GLY VAL LEU VAL HIS VAL GLN LYS          
SEQRES   9 A  139  TRP ASP GLY LYS SER THR THR ILE LYS ARG LYS ARG GLU          
SEQRES  10 A  139  ASP ASP LYS LEU VAL VAL GLU CYS VAL MET LYS GLY VAL          
SEQRES  11 A  139  THR SER THR ARG VAL TYR GLU ARG ALA                          
HET    CIT  A 133      26                                                       
HETNAM     CIT CITRIC ACID                                                      
FORMUL   2  CIT    C6 H8 O7                                                     
FORMUL   3  HOH   *162(H2 O)                                                    
HELIX    1   1 SER A   -1  VAL A    5  5                                   7    
HELIX    2   2 ASN A   15  GLY A   24  1                                  10    
HELIX    3   3 GLY A   26  ALA A   36  1                                  11    
SHEET    1   A10 THR A  60  ILE A  65  0                                        
SHEET    2   A10 VAL A  48  GLU A  54 -1  N  ILE A  49   O  PHE A  64           
SHEET    3   A10 ASN A  39  ASN A  45 -1  N  ASN A  39   O  GLU A  54           
SHEET    4   A10 GLY A   6  GLU A  14 -1  N  TRP A   8   O  MET A  40           
SHEET    5   A10 VAL A 122  ARG A 130 -1  O  VAL A 127   N  VAL A  11           
SHEET    6   A10 LYS A 112  MET A 119 -1  N  VAL A 115   O  ARG A 126           
SHEET    7   A10 LYS A 100  GLU A 109 -1  N  LYS A 105   O  GLU A 116           
SHEET    8   A10 VAL A  90  TRP A  97 -1  N  TRP A  97   O  LYS A 100           
SHEET    9   A10 LYS A  79  ASP A  87 -1  N  THR A  85   O  VAL A  92           
SHEET   10   A10 PHE A  70  VAL A  73 -1  N  PHE A  70   O  SER A  82           
SITE     1 AC1 12 PHE A  16  ARG A  78  ILE A 104  CYS A 117                    
SITE     2 AC1 12 ARG A 126  TYR A 128  HOH A 206  HOH A 220                    
SITE     3 AC1 12 HOH A 230  HOH A 248  HOH A 273  HOH A 275                    
CRYST1   32.239   53.316   75.002  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.031018  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018756  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013333        0.00000                         
ATOM      1  N   GLN A  -7      -2.420  31.124  -8.680  1.00 40.50           N  
ANISOU    1  N   GLN A  -7     5037   5342   5006    -56   -305     88       N  
ATOM      2  CA  GLN A  -7      -1.575  29.974  -8.242  1.00 40.09           C  
ANISOU    2  CA  GLN A  -7     4985   5208   5039      0   -237    -27       C  
ATOM      3  C   GLN A  -7      -0.868  29.283  -9.412  1.00 38.99           C  
ANISOU    3  C   GLN A  -7     4856   5044   4913     37   -259    -21       C  
ATOM      4  O   GLN A  -7      -1.452  29.104 -10.470  1.00 39.77           O  
ANISOU    4  O   GLN A  -7     5004   5205   4898    -17   -276   -225       O  
ATOM      5  CB  GLN A  -7      -2.433  28.968  -7.481  1.00 40.48           C  
ANISOU    5  CB  GLN A  -7     4982   5282   5117    -13   -264     54       C  
ATOM      6  N   GLN A  -6       0.403  28.922  -9.244  1.00 37.04           N  
ANISOU    6  N   GLN A  -6     4735   4656   4682     24   -230      7       N  
ATOM      7  CA  GLN A  -6       1.042  28.004 -10.215  1.00 35.39           C  
ANISOU    7  CA  GLN A  -6     4504   4347   4594     33   -228     82       C  
ATOM      8  C   GLN A  -6       1.286  26.723  -9.454  1.00 34.22           C  
ANISOU    8  C   GLN A  -6     4445   4197   4358      6   -226    132       C  
ATOM      9  O   GLN A  -6       1.226  26.716  -8.222  1.00 33.30           O  
ANISOU    9  O   GLN A  -6     4506   3855   4292    -81   -260    -46       O  
ATOM     10  CB  GLN A  -6       2.345  28.548 -10.750  1.00 36.26           C  
ANISOU   10  CB  GLN A  -6     4717   4459   4600     -4   -211    198       C  
ATOM     11  N   MET A  -5       1.526  25.643 -10.192  1.00 33.01           N  
ANISOU   11  N   MET A  -5     4240   3957   4344    -43   -271    167       N  
ATOM     12  CA  MET A  -5       1.900  24.388  -9.573  1.00 31.44           C  
ANISOU   12  CA  MET A  -5     4025   3874   4044     15   -228    162       C  
ATOM     13  C   MET A  -5       3.343  24.434  -9.188  1.00 31.95           C  
ANISOU   13  C   MET A  -5     3990   3953   4195     51   -212    151       C  
ATOM     14  O   MET A  -5       4.233  24.667 -10.021  1.00 32.94           O  
ANISOU   14  O   MET A  -5     3951   4216   4348    112   -281    223       O  
ATOM     15  CB  MET A  -5       1.668  23.179 -10.477  1.00 32.07           C  
ANISOU   15  CB  MET A  -5     4183   3907   4093     11   -207    184       C  
ATOM     16  CG  MET A  -5       1.696  21.812  -9.654  1.00 29.22           C  
ANISOU   16  CG  MET A  -5     4319   3721   3060    162     56     44       C  
ATOM     17  SD  MET A  -5       1.246  20.376 -10.601  1.00 29.85           S  
ANISOU   17  SD  MET A  -5     4516   3611   3214   -112     88    -22       S  
ATOM     18  CE  MET A  -5      -0.424  20.799 -10.629  1.00 27.18           C  
ANISOU   18  CE  MET A  -5     4590   4798    937    830     55    621       C  
ATOM     19  N   GLY A  -4       3.559  24.147  -7.919  1.00 32.07           N  
ANISOU   19  N   GLY A  -4     3967   4016   4199     42   -185     45       N  
ATOM     20  CA  GLY A  -4       4.876  24.159  -7.338  1.00 32.76           C  
ANISOU   20  CA  GLY A  -4     4012   4131   4304     88   -210     59       C  
ATOM     21  C   GLY A  -4       5.644  22.963  -7.833  1.00 32.50           C  
ANISOU   21  C   GLY A  -4     4007   4036   4304     87   -215    163       C  
ATOM     22  O   GLY A  -4       5.081  22.001  -8.368  1.00 33.44           O  
ANISOU   22  O   GLY A  -4     4069   4134   4502    132   -233    -75       O  
ATOM     23  N   ARG A  -3       6.943  23.007  -7.650  1.00 32.90           N  
ANISOU   23  N   ARG A  -3     4156   4111   4231    -44   -154    240       N  
ATOM     24  CA  ARG A  -3       7.747  21.860  -7.969  1.00 32.28           C  
ANISOU   24  CA  ARG A  -3     4214   4003   4046     12   -176    432       C  
ATOM     25  C   ARG A  -3       7.858  20.957  -6.709  1.00 30.62           C  
ANISOU   25  C   ARG A  -3     4148   3794   3690    -57   -178    539       C  
ATOM     26  O   ARG A  -3       7.354  21.270  -5.609  1.00 31.74           O  
ANISOU   26  O   ARG A  -3     4317   3714   4026     30   -217    619       O  
ATOM     27  CB  ARG A  -3       9.110  22.279  -8.548  1.00 34.12           C  
ANISOU   27  CB  ARG A  -3     4403   4364   4195    -11   -138    325       C  
ATOM     28  CG  ARG A  -3       9.179  22.192 -10.139  1.00 37.02           C  
ANISOU   28  CG  ARG A  -3     4745   4960   4357   -127    120    192       C  
ATOM     29  CD  ARG A  -3       8.919  23.467 -10.873  1.00 42.74           C  
ANISOU   29  CD  ARG A  -3     5400   5463   5374   -210    179    160       C  
ATOM     30  NE  ARG A  -3      10.160  24.234 -11.047  1.00 45.23           N  
ANISOU   30  NE  ARG A  -3     5334   6236   5613   -313    632     83       N  
ATOM     31  CZ  ARG A  -3      10.861  24.376 -12.179  1.00 45.55           C  
ANISOU   31  CZ  ARG A  -3     5684   6165   5458   -267    557    139       C  
ATOM     32  NH1 ARG A  -3      11.973  25.105 -12.150  1.00 42.72           N  
ANISOU   32  NH1 ARG A  -3     5329   5837   5066   -281   1071    447       N  
ATOM     33  NH2 ARG A  -3      10.477  23.810 -13.327  1.00 47.09           N  
ANISOU   33  NH2 ARG A  -3     6107   6267   5518   -190    754    -87       N  
ATOM     34  N   GLY A  -2       8.487  19.814  -6.913  1.00 27.92           N  
ANISOU   34  N   GLY A  -2     3965   3378   3263   -157   -173    773       N  
ATOM     35  CA  GLY A  -2       8.579  18.813  -5.877  1.00 27.62           C  
ANISOU   35  CA  GLY A  -2     3923   3355   3215   -268   -360    775       C  
ATOM     36  C   GLY A  -2       9.690  19.158  -4.918  1.00 27.41           C  
ANISOU   36  C   GLY A  -2     3891   3328   3193   -305   -281    802       C  
ATOM     37  O   GLY A  -2      10.390  20.176  -5.022  1.00 28.95           O  
ANISOU   37  O   GLY A  -2     4256   3410   3332   -267   -421    742       O  
ATOM     38  N   SER A  -1       9.884  18.250  -3.994  1.00 26.79           N  
ANISOU   38  N   SER A  -1     3944   3293   2941   -308   -239    801       N  
ATOM     39  CA  SER A  -1      11.038  18.376  -3.151  1.00 27.32           C  
ANISOU   39  CA  SER A  -1     3933   3285   3162   -327   -140    734       C  
ATOM     40  C   SER A  -1      11.523  17.002  -2.682  1.00 26.33           C  
ANISOU   40  C   SER A  -1     3747   3312   2945   -337    -37    729       C  
ATOM     41  O   SER A  -1      10.875  16.001  -2.829  1.00 25.26           O  
ANISOU   41  O   SER A  -1     3746   3260   2590   -567    -82   1014       O  
ATOM     42  CB  SER A  -1      10.683  19.262  -1.980  1.00 29.12           C  
ANISOU   42  CB  SER A  -1     4247   3505   3310   -209     -4    729       C  
ATOM     43  OG  SER A  -1       9.870  18.615  -1.064  1.00 34.62           O  
ANISOU   43  OG  SER A  -1     4839   3990   4325   -553    355    451       O  
ATOM     44  N  AMET A   0      12.739  17.005  -2.150  0.50 27.54           N  
ANISOU   44  N  AMET A   0     3829   3486   3148   -224    -75    646       N  
ATOM     45  N  BMET A   0      12.714  16.937  -2.163  0.50 24.95           N  
ANISOU   45  N  BMET A   0     3541   3228   2708   -252    -24    571       N  
ATOM     46  CA AMET A   0      13.282  15.900  -1.335  0.50 27.96           C  
ANISOU   46  CA AMET A   0     3821   3538   3263   -205    -31    649       C  
ATOM     47  CA BMET A   0      13.179  15.645  -1.702  0.50 23.69           C  
ANISOU   47  CA BMET A   0     3295   3089   2616   -296     32    496       C  
ATOM     48  C  AMET A   0      12.230  15.104  -0.670  0.50 26.78           C  
ANISOU   48  C  AMET A   0     3744   3354   3075   -242    -86    649       C  
ATOM     49  C  BMET A   0      12.275  15.031  -0.616  0.50 24.67           C  
ANISOU   49  C  BMET A   0     3456   3174   2743   -336    -60    567       C  
ATOM     50  O  AMET A   0      12.074  13.900  -0.889  0.50 24.74           O  
ANISOU   50  O  AMET A   0     3626   3107   2665   -251     20    805       O  
ATOM     51  O  BMET A   0      12.234  13.802  -0.559  0.50 24.53           O  
ANISOU   51  O  BMET A   0     3440   3121   2757   -406    -44    513       O  
ATOM     52  CB AMET A   0      14.080  16.476  -0.161  0.50 29.36           C  
ANISOU   52  CB AMET A   0     3987   3742   3424   -123    -25    548       C  
ATOM     53  CB BMET A   0      14.646  15.762  -1.258  0.50 21.12           C  
ANISOU   53  CB BMET A   0     3056   2984   1982   -210     91    324       C  
ATOM     54  CG AMET A   0      15.452  16.767  -0.475  0.50 30.91           C  
ANISOU   54  CG AMET A   0     4051   3936   3755   -134    -38    387       C  
ATOM     55  CG BMET A   0      15.252  14.435  -0.907  0.50 21.64           C  
ANISOU   55  CG BMET A   0     2978   3108   2134   -233     93    399       C  
ATOM     56  SD AMET A   0      16.106  15.272  -1.209  0.50 31.88           S  
ANISOU   56  SD AMET A   0     4489   4245   3376    289   -282    208       S  
ATOM     57  SD BMET A   0      15.243  14.332   0.825  0.50 28.67           S  
ANISOU   57  SD BMET A   0     4745   3851   2294    -12   -195    604       S  
ATOM     58  CE AMET A   0      16.668  14.361   0.300  0.50 16.78           C  
ANISOU   58  CE AMET A   0     2403   2971    999    359    449   -393       C  
ATOM     59  CE BMET A   0      16.488  15.556   1.202  0.50 27.78           C  
ANISOU   59  CE BMET A   0     4232   3887   2434    194      5   1111       C  
ATOM     60  N   CYS A   1      11.544  15.824   0.199  1.00 25.28           N  
ANISOU   60  N   CYS A   1     3604   3152   2849   -318   -132    744       N  
ATOM     61  CA  CYS A   1      10.600  15.245   1.191  1.00 26.38           C  
ANISOU   61  CA  CYS A   1     3764   3246   3013   -259   -156    680       C  
ATOM     62  C   CYS A   1       9.468  14.488   0.534  1.00 22.51           C  
ANISOU   62  C   CYS A   1     3449   2826   2277   -213   -132    978       C  
ATOM     63  O   CYS A   1       8.783  13.731   1.218  1.00 23.01           O  
ANISOU   63  O   CYS A   1     3658   2658   2425   -268    172   1157       O  
ATOM     64  CB  CYS A   1      10.014  16.311   2.125  1.00 29.57           C  
ANISOU   64  CB  CYS A   1     4010   3813   3411     -1   -387    512       C  
ATOM     65  SG  CYS A   1      10.693  16.522   3.767  1.00 39.34           S  
ANISOU   65  SG  CYS A   1     5761   4978   4206    -50   -988    415       S  
ATOM     66  N   ASP A   2       9.346  14.586  -0.781  1.00 22.62           N  
ANISOU   66  N   ASP A   2     3445   2979   2171   -367   -141   1033       N  
ATOM     67  CA  ASP A   2       8.344  13.802  -1.456  1.00 23.26           C  
ANISOU   67  CA  ASP A   2     3562   2973   2302   -520   -220   1095       C  
ATOM     68  C   ASP A   2       8.532  12.301  -1.287  1.00 21.96           C  
ANISOU   68  C   ASP A   2     3537   3018   1787   -548    -37    981       C  
ATOM     69  O   ASP A   2       7.539  11.643  -1.399  1.00 22.20           O  
ANISOU   69  O   ASP A   2     3739   3097   1597   -639   -122    681       O  
ATOM     70  CB  ASP A   2       8.204  14.185  -2.913  1.00 25.08           C  
ANISOU   70  CB  ASP A   2     3661   3277   2589   -666   -234   1046       C  
ATOM     71  CG  ASP A   2       7.606  15.592  -3.117  1.00 27.66           C  
ANISOU   71  CG  ASP A   2     3822   3642   3045   -410   -511   1293       C  
ATOM     72  OD1 ASP A   2       6.904  16.139  -2.227  1.00 33.15           O  
ANISOU   72  OD1 ASP A   2     4246   4207   4142   -177   -144   1318       O  
ATOM     73  OD2 ASP A   2       7.868  16.189  -4.154  1.00 31.43           O  
ANISOU   73  OD2 ASP A   2     3885   4587   3470  -1043   -585   1103       O  
ATOM     74  N   ALA A   3       9.760  11.813  -1.050  1.00 20.75           N  
ANISOU   74  N   ALA A   3     3445   2870   1569   -547    320    962       N  
ATOM     75  CA  ALA A   3       9.988  10.396  -0.749  1.00 21.10           C  
ANISOU   75  CA  ALA A   3     3330   3016   1668   -252    176    666       C  
ATOM     76  C   ALA A   3       9.265   9.903   0.482  1.00 17.68           C  
ANISOU   76  C   ALA A   3     3291   2348   1077   -244    359    459       C  
ATOM     77  O   ALA A   3       9.014   8.725   0.589  1.00 18.38           O  
ANISOU   77  O   ALA A   3     3421   2230   1330    -45    441     50       O  
ATOM     78  CB  ALA A   3      11.445  10.121  -0.612  1.00 24.05           C  
ANISOU   78  CB  ALA A   3     3368   3307   2462    -79    245    992       C  
ATOM     79  N   PHE A   4       8.925  10.831   1.384  1.00 16.42           N  
ANISOU   79  N   PHE A   4     3110   2014   1114   -185    134    271       N  
ATOM     80  CA  PHE A   4       8.176  10.477   2.601  1.00 14.56           C  
ANISOU   80  CA  PHE A   4     2843   1555   1134    -91    151     98       C  
ATOM     81  C   PHE A   4       6.683  10.515   2.445  1.00 14.28           C  
ANISOU   81  C   PHE A   4     2876   1404   1143   -189     87    134       C  
ATOM     82  O   PHE A   4       5.991   9.926   3.242  1.00 15.26           O  
ANISOU   82  O   PHE A   4     3205   1563   1029   -207     47    233       O  
ATOM     83  CB  PHE A   4       8.586  11.379   3.775  1.00 15.88           C  
ANISOU   83  CB  PHE A   4     2906   1695   1432   -110     -8   -114       C  
ATOM     84  CG  PHE A   4      10.022  11.246   4.148  1.00 15.71           C  
ANISOU   84  CG  PHE A   4     2715   2033   1219    -48    -53    -68       C  
ATOM     85  CD1 PHE A   4      10.399  10.232   5.012  1.00 16.10           C  
ANISOU   85  CD1 PHE A   4     2963   1948   1206    -24   -174     65       C  
ATOM     86  CD2 PHE A   4      10.953  12.192   3.796  1.00 19.47           C  
ANISOU   86  CD2 PHE A   4     3450   2570   1378   -163   -262    398       C  
ATOM     87  CE1 PHE A   4      11.704  10.071   5.338  1.00 17.36           C  
ANISOU   87  CE1 PHE A   4     2853   2540   1201     76   -296    131       C  
ATOM     88  CE2 PHE A   4      12.298  12.039   4.131  1.00 19.83           C  
ANISOU   88  CE2 PHE A   4     3333   2839   1362   -487     79    365       C  
ATOM     89  CZ  PHE A   4      12.657  11.016   4.990  1.00 17.69           C  
ANISOU   89  CZ  PHE A   4     2938   2423   1357    110   -148   -289       C  
ATOM     90  N   VAL A   5       6.193  11.219   1.426  1.00 14.53           N  
ANISOU   90  N   VAL A   5     3025   1688    808   -107    121     84       N  
ATOM     91  CA  VAL A   5       4.793  11.469   1.336  1.00 14.86           C  
ANISOU   91  CA  VAL A   5     2929   1625   1090   -179    161     -2       C  
ATOM     92  C   VAL A   5       4.047  10.171   1.042  1.00 15.53           C  
ANISOU   92  C   VAL A   5     2784   1679   1434   -248    180   -267       C  
ATOM     93  O   VAL A   5       4.402   9.379   0.125  1.00 18.44           O  
ANISOU   93  O   VAL A   5     3461   1859   1684   -448    379   -447       O  
ATOM     94  CB  VAL A   5       4.537  12.555   0.305  1.00 16.09           C  
ANISOU   94  CB  VAL A   5     3139   1586   1388    -55      4    216       C  
ATOM     95  CG1 VAL A   5       3.105  12.537  -0.260  1.00 20.01           C  
ANISOU   95  CG1 VAL A   5     3715   1953   1934    -97     20    323       C  
ATOM     96  CG2 VAL A   5       5.074  13.912   0.840  1.00 17.18           C  
ANISOU   96  CG2 VAL A   5     3379   1523   1625   -124   -176    101       C  
ATOM     97  N   GLY A   6       2.889  10.007   1.642  1.00 14.84           N  
ANISOU   97  N   GLY A   6     2742   1589   1307   -216    128   -238       N  
ATOM     98  CA  GLY A   6       2.108   8.841   1.422  1.00 15.75           C  
ANISOU   98  CA  GLY A   6     2846   1774   1363   -183     70   -142       C  
ATOM     99  C   GLY A   6       1.414   8.382   2.648  1.00 13.74           C  
ANISOU   99  C   GLY A   6     2501   1637   1081   -316    -68     55       C  
ATOM    100  O   GLY A   6       1.350   9.063   3.665  1.00 16.22           O  
ANISOU  100  O   GLY A   6     3145   1775   1241   -277    208   -281       O  
ATOM    101  N   THR A   7       0.884   7.190   2.530  1.00 15.01           N  
ANISOU  101  N   THR A   7     2838   1608   1255   -237   -190     60       N  
ATOM    102  CA  THR A   7       0.168   6.516   3.586  1.00 15.98           C  
ANISOU  102  CA  THR A   7     2855   1545   1672    -44    -42    -33       C  
ATOM    103  C   THR A   7       0.943   5.256   3.959  1.00 14.76           C  
ANISOU  103  C   THR A   7     2866   1352   1387   -168   -152   -128       C  
ATOM    104  O   THR A   7       1.197   4.413   3.095  1.00 16.21           O  
ANISOU  104  O   THR A   7     3465   1470   1223     42   -223   -138       O  
ATOM    105  CB  THR A   7      -1.247   6.168   3.099  1.00 18.09           C  
ANISOU  105  CB  THR A   7     2915   1660   2295     55   -103    287       C  
ATOM    106  OG1 THR A   7      -1.844   7.285   2.425  1.00 24.87           O  
ANISOU  106  OG1 THR A   7     3546   1951   3950     22   -430    115       O  
ATOM    107  CG2 THR A   7      -2.110   5.715   4.256  1.00 22.02           C  
ANISOU  107  CG2 THR A   7     3196   2496   2673   -324     49      0       C  
ATOM    108  N   TRP A   8       1.258   5.140   5.245  1.00 14.49           N  
ANISOU  108  N   TRP A   8     2896   1537   1072    -54    106    -73       N  
ATOM    109  CA  TRP A   8       2.164   4.136   5.759  1.00 14.70           C  
ANISOU  109  CA  TRP A   8     3034   1374   1175    -61     70    147       C  
ATOM    110  C   TRP A   8       1.507   3.378   6.887  1.00 14.25           C  
ANISOU  110  C   TRP A   8     3090   1352    971    -71    176    -49       C  
ATOM    111  O   TRP A   8       0.688   3.952   7.607  1.00 18.63           O  
ANISOU  111  O   TRP A   8     4051   1438   1587    167    710    150       O  
ATOM    112  CB  TRP A   8       3.454   4.816   6.269  1.00 14.58           C  
ANISOU  112  CB  TRP A   8     2963   1502   1073    118     92    285       C  
ATOM    113  CG  TRP A   8       4.189   5.656   5.263  1.00 13.75           C  
ANISOU  113  CG  TRP A   8     3101   1382    740    -77    -12    128       C  
ATOM    114  CD1 TRP A   8       4.110   6.987   5.045  1.00 14.32           C  
ANISOU  114  CD1 TRP A   8     3069   1487    883     45      2     14       C  
ATOM    115  CD2 TRP A   8       5.166   5.151   4.349  1.00 13.34           C  
ANISOU  115  CD2 TRP A   8     2976   1354    736    -22      0      1       C  
ATOM    116  NE1 TRP A   8       4.947   7.361   4.017  1.00 14.41           N  
ANISOU  116  NE1 TRP A   8     2947   1655    873    -16     44     92       N  
ATOM    117  CE2 TRP A   8       5.625   6.250   3.596  1.00 13.11           C  
ANISOU  117  CE2 TRP A   8     2581   1504    896     16    299     56       C  
ATOM    118  CE3 TRP A   8       5.708   3.889   4.112  1.00 14.36           C  
ANISOU  118  CE3 TRP A   8     2837   1520   1098   -108    -87   -126       C  
ATOM    119  CZ2 TRP A   8       6.596   6.105   2.618  1.00 15.07           C  
ANISOU  119  CZ2 TRP A   8     2965   1704   1055   -314    152    -82       C  
ATOM    120  CZ3 TRP A   8       6.648   3.741   3.175  1.00 14.69           C  
ANISOU  120  CZ3 TRP A   8     2824   1442   1313    -52    138   -234       C  
ATOM    121  CH2 TRP A   8       7.085   4.816   2.420  1.00 15.36           C  
ANISOU  121  CH2 TRP A   8     2873   1753   1207   -210    102   -399       C  
ATOM    122  N   LYS A   9       1.810   2.129   7.020  1.00 13.84           N  
ANISOU  122  N   LYS A   9     2853   1351   1052   -169     32    155       N  
ATOM    123  CA  LYS A   9       1.264   1.294   8.138  1.00 14.74           C  
ANISOU  123  CA  LYS A   9     2646   1748   1206   -142     -5     29       C  
ATOM    124  C   LYS A   9       2.397   0.620   8.842  1.00 14.20           C  
ANISOU  124  C   LYS A   9     2541   1604   1248   -182    127    191       C  
ATOM    125  O   LYS A   9       3.356   0.128   8.258  1.00 13.95           O  
ANISOU  125  O   LYS A   9     2699   1634    966   -195    -88     99       O  
ATOM    126  CB  LYS A   9       0.312   0.279   7.509  1.00 16.61           C  
ANISOU  126  CB  LYS A   9     2839   1847   1623   -236    -48    615       C  
ATOM    127  CG  LYS A   9       0.916  -0.657   6.574  1.00 24.08           C  
ANISOU  127  CG  LYS A   9     3889   3014   2246   -159   -114    340       C  
ATOM    128  CD  LYS A   9      -0.016  -1.764   6.179  1.00 31.46           C  
ANISOU  128  CD  LYS A   9     4291   3824   3838   -391   -163    190       C  
ATOM    129  CE  LYS A   9       0.638  -2.719   5.184  1.00 33.30           C  
ANISOU  129  CE  LYS A   9     4513   4139   4001   -527   -235   -207       C  
ATOM    130  NZ  LYS A   9       0.457  -2.175   3.802  1.00 37.09           N  
ANISOU  130  NZ  LYS A   9     4935   4319   4838    -76   -352    676       N  
ATOM    131  N   LEU A  10       2.336   0.639  10.171  1.00 14.40           N  
ANISOU  131  N   LEU A  10     2434   2031   1005   -231     -4    130       N  
ATOM    132  CA  LEU A  10       3.371   0.021  11.014  1.00 14.59           C  
ANISOU  132  CA  LEU A  10     2479   1929   1134   -336    -89     44       C  
ATOM    133  C   LEU A  10       3.316  -1.499  10.807  1.00 15.09           C  
ANISOU  133  C   LEU A  10     2613   2066   1053   -339   -331    234       C  
ATOM    134  O   LEU A  10       2.251  -2.072  11.022  1.00 17.93           O  
ANISOU  134  O   LEU A  10     2892   2200   1719   -584   -224    370       O  
ATOM    135  CB  LEU A  10       3.168   0.372  12.496  1.00 16.08           C  
ANISOU  135  CB  LEU A  10     2702   2283   1123   -256    -59    137       C  
ATOM    136  CG  LEU A  10       4.252  -0.175  13.400  1.00 16.19           C  
ANISOU  136  CG  LEU A  10     2765   2172   1213   -284   -251     64       C  
ATOM    137  CD1 LEU A  10       5.593   0.452  13.197  1.00 16.79           C  
ANISOU  137  CD1 LEU A  10     2606   2424   1346   -218    -43    -12       C  
ATOM    138  CD2 LEU A  10       3.829  -0.005  14.869  1.00 21.36           C  
ANISOU  138  CD2 LEU A  10     3159   3791   1164    143   -311    -99       C  
ATOM    139  N   VAL A  11       4.473  -2.093  10.512  1.00 15.68           N  
ANISOU  139  N   VAL A  11     2863   1800   1292   -323   -355    389       N  
ATOM    140  CA  VAL A  11       4.582  -3.563  10.354  1.00 17.53           C  
ANISOU  140  CA  VAL A  11     3310   1847   1504   -229   -543    182       C  
ATOM    141  C   VAL A  11       5.527  -4.240  11.337  1.00 19.06           C  
ANISOU  141  C   VAL A  11     3486   1785   1970   -284   -619    540       C  
ATOM    142  O   VAL A  11       5.388  -5.447  11.548  1.00 23.10           O  
ANISOU  142  O   VAL A  11     4259   1804   2715   -593  -1052    696       O  
ATOM    143  CB  VAL A  11       4.918  -3.991   8.957  1.00 19.27           C  
ANISOU  143  CB  VAL A  11     3529   2012   1778    -13   -317     31       C  
ATOM    144  CG1 VAL A  11       3.869  -3.483   8.000  1.00 21.01           C  
ANISOU  144  CG1 VAL A  11     3826   2287   1868    117   -450     31       C  
ATOM    145  CG2 VAL A  11       6.305  -3.519   8.476  1.00 21.77           C  
ANISOU  145  CG2 VAL A  11     3958   2314   1997     -5    -37   -254       C  
ATOM    146  N   SER A  12       6.488  -3.535  11.923  1.00 16.97           N  
ANISOU  146  N   SER A  12     3502   1574   1371   -261   -626    299       N  
ATOM    147  CA  SER A  12       7.283  -4.166  12.953  1.00 18.45           C  
ANISOU  147  CA  SER A  12     3505   1756   1748   -117   -340    308       C  
ATOM    148  C   SER A  12       7.826  -3.134  13.874  1.00 15.67           C  
ANISOU  148  C   SER A  12     3014   1608   1331   -229   -310    184       C  
ATOM    149  O   SER A  12       8.005  -1.955  13.530  1.00 16.56           O  
ANISOU  149  O   SER A  12     3351   1640   1301   -309   -176    296       O  
ATOM    150  CB  SER A  12       8.433  -4.951  12.369  1.00 20.99           C  
ANISOU  150  CB  SER A  12     3690   2470   1813    -61   -361     52       C  
ATOM    151  OG  SER A  12       9.384  -4.143  11.741  1.00 22.78           O  
ANISOU  151  OG  SER A  12     4058   2602   1992    359   -219    318       O  
ATOM    152  N   SER A  13       8.142  -3.596  15.051  1.00 16.75           N  
ANISOU  152  N   SER A  13     3389   1649   1325   -377   -386    311       N  
ATOM    153  CA  SER A  13       8.715  -2.761  16.097  1.00 16.23           C  
ANISOU  153  CA  SER A  13     3097   1660   1408   -264   -414    580       C  
ATOM    154  C   SER A  13       9.682  -3.587  16.956  1.00 17.11           C  
ANISOU  154  C   SER A  13     3192   2024   1285   -285   -262    533       C  
ATOM    155  O   SER A  13       9.405  -4.772  17.264  1.00 19.36           O  
ANISOU  155  O   SER A  13     3644   1642   2067   -398   -485    687       O  
ATOM    156  CB  SER A  13       7.535  -2.233  16.929  1.00 18.74           C  
ANISOU  156  CB  SER A  13     3381   2060   1679   -442   -324    407       C  
ATOM    157  OG  SER A  13       7.930  -1.390  17.962  1.00 20.09           O  
ANISOU  157  OG  SER A  13     3913   2015   1705   -212   -607    141       O  
ATOM    158  N   GLU A  14      10.808  -2.979  17.318  1.00 14.88           N  
ANISOU  158  N   GLU A  14     3020   1394   1236   -165   -190    329       N  
ATOM    159  CA  GLU A  14      11.743  -3.597  18.224  1.00 16.04           C  
ANISOU  159  CA  GLU A  14     3087   1482   1525     75   -179     42       C  
ATOM    160  C   GLU A  14      12.118  -2.610  19.299  1.00 13.67           C  
ANISOU  160  C   GLU A  14     2642   1395   1155     75   -136    193       C  
ATOM    161  O   GLU A  14      12.407  -1.445  19.010  1.00 14.86           O  
ANISOU  161  O   GLU A  14     3128   1400   1118     67    -87     39       O  
ATOM    162  CB  GLU A  14      13.001  -3.968  17.417  1.00 18.45           C  
ANISOU  162  CB  GLU A  14     3217   2017   1774    243   -304     34       C  
ATOM    163  CG  GLU A  14      12.806  -5.200  16.536  1.00 25.14           C  
ANISOU  163  CG  GLU A  14     3848   2574   3128    172    -31   -511       C  
ATOM    164  CD  GLU A  14      12.775  -6.577  17.280  1.00 28.27           C  
ANISOU  164  CD  GLU A  14     4590   2607   3541    273   -102   -536       C  
ATOM    165  OE1 GLU A  14      12.954  -6.706  18.500  1.00 32.44           O  
ANISOU  165  OE1 GLU A  14     4830   3368   4126    538   -523  -1012       O  
ATOM    166  OE2 GLU A  14      12.455  -7.576  16.634  1.00 32.52           O  
ANISOU  166  OE2 GLU A  14     4752   3285   4316    543     74  -1126       O  
ATOM    167  N  AASN A  15      12.102  -3.087  20.521  0.50 13.21           N  
ANISOU  167  N  AASN A  15     2593   1299   1125    -15    -63    264       N  
ATOM    168  N  BASN A  15      12.116  -3.084  20.519  0.50 14.17           N  
ANISOU  168  N  BASN A  15     2680   1414   1288     -1    -13    192       N  
ATOM    169  CA AASN A  15      12.604  -2.355  21.690  0.50 12.94           C  
ANISOU  169  CA AASN A  15     2453   1465    995     20   -137    190       C  
ATOM    170  CA BASN A  15      12.569  -2.319  21.682  0.50 14.59           C  
ANISOU  170  CA BASN A  15     2607   1629   1307     62    -43     68       C  
ATOM    171  C  AASN A  15      11.775  -1.109  22.009  0.50 13.48           C  
ANISOU  171  C  AASN A  15     2509   1443   1168    -11    -45    297       C  
ATOM    172  C  BASN A  15      11.755  -1.105  22.020  0.50 14.38           C  
ANISOU  172  C  BASN A  15     2571   1551   1340     -4      0    217       C  
ATOM    173  O  AASN A  15      12.241  -0.245  22.751  0.50 14.04           O  
ANISOU  173  O  AASN A  15     2635   1559   1139      1   -203    126       O  
ATOM    174  O  BASN A  15      12.211  -0.255  22.782  0.50 14.57           O  
ANISOU  174  O  BASN A  15     2671   1621   1244      6   -141     64       O  
ATOM    175  CB AASN A  15      14.115  -2.061  21.560  0.50 13.22           C  
ANISOU  175  CB AASN A  15     2513   1428   1082     77   -149    227       C  
ATOM    176  CB BASN A  15      14.038  -1.940  21.581  0.50 15.73           C  
ANISOU  176  CB BASN A  15     2707   1760   1507    114     17     38       C  
ATOM    177  CG AASN A  15      14.869  -2.049  22.880  0.50 12.42           C  
ANISOU  177  CG AASN A  15     2307   1634    777     -2   -398    524       C  
ATOM    178  CG BASN A  15      14.899  -3.119  21.329  0.50 18.48           C  
ANISOU  178  CG BASN A  15     2734   2337   1949    405   -139    -89       C  
ATOM    179  OD1AASN A  15      14.719  -2.956  23.664  0.50 14.45           O  
ANISOU  179  OD1AASN A  15     2509   1522   1458    -25    -95    471       O  
ATOM    180  OD1BASN A  15      15.021  -3.936  22.188  0.50 20.62           O  
ANISOU  180  OD1BASN A  15     3461   1911   2462    501    -33    -37       O  
ATOM    181  ND2AASN A  15      15.696  -1.015  23.097  0.50 13.24           N  
ANISOU  181  ND2AASN A  15     2249   1791    991   -108    -45     76       N  
ATOM    182  ND2BASN A  15      15.331  -3.307  20.111  0.50 24.46           N  
ANISOU  182  ND2BASN A  15     3219   3083   2989    683    555    -73       N  
ATOM    183  N   PHE A  16      10.516  -1.047  21.568  1.00 13.64           N  
ANISOU  183  N   PHE A  16     2607   1291   1282    -61    -75     88       N  
ATOM    184  CA  PHE A  16       9.726   0.164  21.826  1.00 14.34           C  
ANISOU  184  CA  PHE A  16     2443   1770   1233     43    -21    105       C  
ATOM    185  C   PHE A  16       9.329   0.290  23.260  1.00 13.87           C  
ANISOU  185  C   PHE A  16     2592   1601   1076   -148   -160    207       C  
ATOM    186  O   PHE A  16       9.241   1.408  23.789  1.00 13.88           O  
ANISOU  186  O   PHE A  16     2776   1370   1125   -153   -112    -11       O  
ATOM    187  CB  PHE A  16       8.530   0.191  20.863  1.00 15.11           C  
ANISOU  187  CB  PHE A  16     2512   1833   1395     55   -147     74       C  
ATOM    188  CG  PHE A  16       7.766   1.497  20.856  1.00 14.49           C  
ANISOU  188  CG  PHE A  16     2499   2248    758    171   -103    -39       C  
ATOM    189  CD1 PHE A  16       8.383   2.677  20.511  1.00 16.71           C  
ANISOU  189  CD1 PHE A  16     3222   1924   1203    239    192    -83       C  
ATOM    190  CD2 PHE A  16       6.419   1.527  21.051  1.00 16.48           C  
ANISOU  190  CD2 PHE A  16     2798   2418   1045    276    -90   -197       C  
ATOM    191  CE1 PHE A  16       7.686   3.851  20.437  1.00 17.35           C  
ANISOU  191  CE1 PHE A  16     3553   1820   1217    229      4   -138       C  
ATOM    192  CE2 PHE A  16       5.695   2.692  20.971  1.00 18.98           C  
ANISOU  192  CE2 PHE A  16     3073   2863   1274    613     64   -158       C  
ATOM    193  CZ  PHE A  16       6.338   3.842  20.678  1.00 18.41           C  
ANISOU  193  CZ  PHE A  16     3611   2670    713    534   -193    -55       C  
ATOM    194  N   ASP A  17       9.087  -0.821  23.944  1.00 14.23           N  
ANISOU  194  N   ASP A  17     2634   1432   1339    -39    121     86       N  
ATOM    195  CA  ASP A  17       8.733  -0.754  25.361  1.00 15.29           C  
ANISOU  195  CA  ASP A  17     2834   1670   1304   -125    116    261       C  
ATOM    196  C   ASP A  17       9.914  -0.146  26.125  1.00 14.58           C  
ANISOU  196  C   ASP A  17     2611   1597   1331   -123    108    627       C  
ATOM    197  O   ASP A  17       9.744   0.747  26.973  1.00 15.53           O  
ANISOU  197  O   ASP A  17     3113   1713   1073   -208    219    210       O  
ATOM    198  CB  ASP A  17       8.308  -2.127  25.899  1.00 16.69           C  
ANISOU  198  CB  ASP A  17     3039   1601   1701   -185    165    411       C  
ATOM    199  CG  ASP A  17       7.825  -2.022  27.298  1.00 19.44           C  
ANISOU  199  CG  ASP A  17     3150   2347   1889   -184    242    724       C  
ATOM    200  OD1 ASP A  17       8.480  -2.552  28.199  1.00 27.42           O  
ANISOU  200  OD1 ASP A  17     4452   3819   2148    -35    -82    717       O  
ATOM    201  OD2 ASP A  17       6.794  -1.418  27.495  1.00 21.35           O  
ANISOU  201  OD2 ASP A  17     3906   2471   1735     50    503    380       O  
ATOM    202  N   ASP A  18      11.150  -0.597  25.878  1.00 14.92           N  
ANISOU  202  N   ASP A  18     2599   1665   1404     -8    138    457       N  
ATOM    203  CA  ASP A  18      12.313  -0.071  26.544  1.00 15.78           C  
ANISOU  203  CA  ASP A  18     2740   1755   1501     54     30    553       C  
ATOM    204  C   ASP A  18      12.541   1.377  26.200  1.00 14.17           C  
ANISOU  204  C   ASP A  18     2512   1670   1200     66    -27    407       C  
ATOM    205  O   ASP A  18      12.908   2.146  27.071  1.00 15.35           O  
ANISOU  205  O   ASP A  18     2855   1845   1130     -2   -134    108       O  
ATOM    206  CB  ASP A  18      13.488  -0.950  26.236  1.00 18.64           C  
ANISOU  206  CB  ASP A  18     2868   2328   1884     -6    -64    403       C  
ATOM    207  CG  ASP A  18      13.442  -2.311  27.020  1.00 25.87           C  
ANISOU  207  CG  ASP A  18     3797   2997   3033    268    191    919       C  
ATOM    208  OD1 ASP A  18      12.662  -2.454  27.944  1.00 35.35           O  
ANISOU  208  OD1 ASP A  18     5314   3966   4149    261    220   2025       O  
ATOM    209  OD2 ASP A  18      14.187  -3.188  26.703  1.00 33.23           O  
ANISOU  209  OD2 ASP A  18     5504   3689   3431    637   -246   1124       O  
ATOM    210  N   TYR A  19      12.343   1.795  24.958  1.00 13.71           N  
ANISOU  210  N   TYR A  19     2606   1543   1059     54    -27    233       N  
ATOM    211  CA  TYR A  19      12.399   3.211  24.599  1.00 12.92           C  
ANISOU  211  CA  TYR A  19     2231   1581   1093     92    -12    389       C  
ATOM    212  C   TYR A  19      11.406   4.005  25.413  1.00 12.77           C  
ANISOU  212  C   TYR A  19     2257   1718    876     39     11    375       C  
ATOM    213  O   TYR A  19      11.768   5.078  26.000  1.00 13.89           O  
ANISOU  213  O   TYR A  19     2836   1636    802   -118    -19     72       O  
ATOM    214  CB  TYR A  19      12.165   3.362  23.086  1.00 13.16           C  
ANISOU  214  CB  TYR A  19     2453   1684    863     56     61    238       C  
ATOM    215  CG  TYR A  19      11.972   4.837  22.697  1.00 12.10           C  
ANISOU  215  CG  TYR A  19     2385   1543    667   -158    129    -90       C  
ATOM    216  CD1 TYR A  19      13.047   5.671  22.609  1.00 12.63           C  
ANISOU  216  CD1 TYR A  19     2309   1720    768    -89     14    -35       C  
ATOM    217  CD2 TYR A  19      10.711   5.329  22.444  1.00 13.48           C  
ANISOU  217  CD2 TYR A  19     2490   1824    807    -30     70   -130       C  
ATOM    218  CE1 TYR A  19      12.854   7.052  22.277  1.00 12.12           C  
ANISOU  218  CE1 TYR A  19     2564   1254    788    -18   -147     54       C  
ATOM    219  CE2 TYR A  19      10.534   6.677  22.122  1.00 13.71           C  
ANISOU  219  CE2 TYR A  19     2564   1643   1000      8    100    125       C  
ATOM    220  CZ  TYR A  19      11.573   7.498  22.055  1.00 12.63           C  
ANISOU  220  CZ  TYR A  19     2630   1569    600     99    -44    -10       C  
ATOM    221  OH  TYR A  19      11.396   8.848  21.735  1.00 13.74           O  
ANISOU  221  OH  TYR A  19     2783   1352   1084     70   -129    243       O  
ATOM    222  N   MET A  20      10.148   3.583  25.447  1.00 12.34           N  
ANISOU  222  N   MET A  20     2076   1618    994     58     61    200       N  
ATOM    223  CA  MET A  20       9.143   4.299  26.216  1.00 13.62           C  
ANISOU  223  CA  MET A  20     2409   1807    955     26     93    238       C  
ATOM    224  C   MET A  20       9.517   4.371  27.715  1.00 13.78           C  
ANISOU  224  C   MET A  20     2541   1721    973   -133     94    123       C  
ATOM    225  O   MET A  20       9.305   5.403  28.348  1.00 15.13           O  
ANISOU  225  O   MET A  20     3059   1791    897   -309    -35     21       O  
ATOM    226  CB  MET A  20       7.756   3.709  26.026  1.00 13.72           C  
ANISOU  226  CB  MET A  20     2421   1785   1006    -55    226    140       C  
ATOM    227  CG  MET A  20       7.151   3.948  24.616  1.00 14.30           C  
ANISOU  227  CG  MET A  20     2654   2063    712    212     84     47       C  
ATOM    228  SD  MET A  20       5.437   3.496  24.571  1.00 15.99           S  
ANISOU  228  SD  MET A  20     2843   2278    952    -24     65    -18       S  
ATOM    229  CE  MET A  20       5.608   1.690  24.579  1.00 16.76           C  
ANISOU  229  CE  MET A  20     3132   1863   1372     22    220   -160       C  
ATOM    230  N   LYS A  21      10.072   3.287  28.295  1.00 14.42           N  
ANISOU  230  N   LYS A  21     2799   1800    878   -185     10    -53       N  
ATOM    231  CA  LYS A  21      10.490   3.322  29.690  1.00 16.21           C  
ANISOU  231  CA  LYS A  21     2988   2418    750   -173    153     89       C  
ATOM    232  C   LYS A  21      11.553   4.368  29.851  1.00 16.54           C  
ANISOU  232  C   LYS A  21     3051   2429    802   -190    162    150       C  
ATOM    233  O   LYS A  21      11.521   5.123  30.855  1.00 17.98           O  
ANISOU  233  O   LYS A  21     3508   2451    871   -251     84      7       O  
ATOM    234  CB  LYS A  21      11.125   1.962  30.095  1.00 17.81           C  
ANISOU  234  CB  LYS A  21     3101   2753    913   -144    154    142       C  
ATOM    235  CG  LYS A  21      10.154   0.861  30.335  1.00 20.35           C  
ANISOU  235  CG  LYS A  21     3526   2759   1447      2    171    337       C  
ATOM    236  CD  LYS A  21      10.806  -0.402  30.912  1.00 23.25           C  
ANISOU  236  CD  LYS A  21     3761   2789   2282    171    -79    420       C  
ATOM    237  CE  LYS A  21       9.782  -1.384  31.267  1.00 29.16           C  
ANISOU  237  CE  LYS A  21     4073   3671   3335     65   -256    456       C  
ATOM    238  NZ  LYS A  21      10.502  -2.584  31.662  1.00 34.54           N  
ANISOU  238  NZ  LYS A  21     4888   4026   4207    279   -344   1308       N  
ATOM    239  N   GLU A  22      12.489   4.495  28.912  1.00 16.60           N  
ANISOU  239  N   GLU A  22     3093   2265    949   -287     41    175       N  
ATOM    240  CA  GLU A  22      13.609   5.430  29.043  1.00 17.49           C  
ANISOU  240  CA  GLU A  22     3099   2588    955   -248    -86    148       C  
ATOM    241  C   GLU A  22      13.080   6.849  28.989  1.00 16.57           C  
ANISOU  241  C   GLU A  22     3136   2238    922   -282   -167    -35       C  
ATOM    242  O   GLU A  22      13.582   7.755  29.656  1.00 18.97           O  
ANISOU  242  O   GLU A  22     3727   2533    944   -286   -275     37       O  
ATOM    243  CB  GLU A  22      14.686   5.150  27.957  1.00 16.97           C  
ANISOU  243  CB  GLU A  22     3056   2272   1118   -335    -22     21       C  
ATOM    244  CG  GLU A  22      16.064   5.621  28.274  1.00 19.94           C  
ANISOU  244  CG  GLU A  22     2979   2909   1687    -70     43    330       C  
ATOM    245  CD  GLU A  22      16.765   4.845  29.381  1.00 22.79           C  
ANISOU  245  CD  GLU A  22     3545   3159   1953   -197   -223    449       C  
ATOM    246  OE1 GLU A  22      16.257   3.829  29.872  1.00 25.28           O  
ANISOU  246  OE1 GLU A  22     3638   3614   2352   -248   -376    556       O  
ATOM    247  OE2 GLU A  22      17.892   5.270  29.717  1.00 25.28           O  
ANISOU  247  OE2 GLU A  22     4391   2832   2380   -324   -741     68       O  
ATOM    248  N   VAL A  23      12.060   7.092  28.156  1.00 16.11           N  
ANISOU  248  N   VAL A  23     3258   1804   1058   -265   -194    124       N  
ATOM    249  CA  VAL A  23      11.415   8.373  28.018  1.00 15.52           C  
ANISOU  249  CA  VAL A  23     3236   1937    722   -237     27      0       C  
ATOM    250  C   VAL A  23      10.686   8.754  29.319  1.00 16.67           C  
ANISOU  250  C   VAL A  23     3410   1955    965   -281     31    -64       C  
ATOM    251  O   VAL A  23      10.538   9.913  29.593  1.00 19.83           O  
ANISOU  251  O   VAL A  23     4404   1875   1256   -197    470   -258       O  
ATOM    252  CB  VAL A  23      10.484   8.349  26.761  1.00 16.61           C  
ANISOU  252  CB  VAL A  23     3378   1903   1029   -217     86    105       C  
ATOM    253  CG1 VAL A  23       9.533   9.514  26.737  1.00 18.60           C  
ANISOU  253  CG1 VAL A  23     3754   2069   1242    124     19    180       C  
ATOM    254  CG2 VAL A  23      11.281   8.300  25.512  1.00 18.06           C  
ANISOU  254  CG2 VAL A  23     3918   2111    831    -71    182     60       C  
ATOM    255  N   GLY A  24      10.171   7.772  30.039  1.00 15.92           N  
ANISOU  255  N   GLY A  24     3342   1862    844   -328     30      0       N  
ATOM    256  CA  GLY A  24       9.383   7.972  31.249  1.00 16.43           C  
ANISOU  256  CA  GLY A  24     3156   2149    938   -358     16    -89       C  
ATOM    257  C   GLY A  24       7.902   7.650  31.144  1.00 15.75           C  
ANISOU  257  C   GLY A  24     3017   1954   1012   -221    155    -80       C  
ATOM    258  O   GLY A  24       7.098   8.057  31.994  1.00 18.54           O  
ANISOU  258  O   GLY A  24     3476   2258   1308   -400    242   -359       O  
ATOM    259  N   VAL A  25       7.498   6.905  30.111  1.00 14.38           N  
ANISOU  259  N   VAL A  25     2871   1695    896   -243    -47    -17       N  
ATOM    260  CA  VAL A  25       6.121   6.584  29.963  1.00 13.21           C  
ANISOU  260  CA  VAL A  25     2609   1563    844     53     23     46       C  
ATOM    261  C   VAL A  25       5.702   5.589  31.028  1.00 14.68           C  
ANISOU  261  C   VAL A  25     2705   1708   1163    -75    -90   -114       C  
ATOM    262  O   VAL A  25       6.430   4.609  31.235  1.00 15.85           O  
ANISOU  262  O   VAL A  25     3245   1822    954    -77    -49     53       O  
ATOM    263  CB  VAL A  25       5.871   6.022  28.529  1.00 13.40           C  
ANISOU  263  CB  VAL A  25     2533   1411   1147    126    -42     61       C  
ATOM    264  CG1 VAL A  25       4.440   5.764  28.352  1.00 14.54           C  
ANISOU  264  CG1 VAL A  25     2782   1765    976   -141     15      0       C  
ATOM    265  CG2 VAL A  25       6.422   6.973  27.451  1.00 16.61           C  
ANISOU  265  CG2 VAL A  25     3718   1684    907   -227    -27    583       C  
ATOM    266  N   GLY A  26       4.510   5.774  31.599  1.00 16.08           N  
ANISOU  266  N   GLY A  26     3078   1982   1049   -194    -73     72       N  
ATOM    267  CA  GLY A  26       4.086   4.884  32.647  1.00 15.81           C  
ANISOU  267  CA  GLY A  26     2977   2186    843   -200    -46      9       C  
ATOM    268  C   GLY A  26       3.529   3.558  32.097  1.00 15.75           C  
ANISOU  268  C   GLY A  26     3042   2028    911   -363     45    276       C  
ATOM    269  O   GLY A  26       3.268   3.408  30.932  1.00 16.25           O  
ANISOU  269  O   GLY A  26     3204   2215    753   -453    -40     57       O  
ATOM    270  N   PHE A  27       3.323   2.627  32.999  1.00 15.71           N  
ANISOU  270  N   PHE A  27     3213   2148    606   -336    -30     15       N  
ATOM    271  CA  PHE A  27       3.034   1.247  32.661  1.00 16.01           C  
ANISOU  271  CA  PHE A  27     3061   2032    987   -329    -79    340       C  
ATOM    272  C   PHE A  27       1.824   1.102  31.779  1.00 15.34           C  
ANISOU  272  C   PHE A  27     2854   1786   1188   -236     -5    424       C  
ATOM    273  O   PHE A  27       1.915   0.505  30.691  1.00 16.00           O  
ANISOU  273  O   PHE A  27     3227   1990    861   -359    -35     81       O  
ATOM    274  CB  PHE A  27       2.802   0.448  33.958  1.00 16.82           C  
ANISOU  274  CB  PHE A  27     3167   2351    872   -213   -119    311       C  
ATOM    275  CG  PHE A  27       2.388  -0.998  33.707  1.00 17.63           C  
ANISOU  275  CG  PHE A  27     3341   2377    978   -368    -96    483       C  
ATOM    276  CD1 PHE A  27       3.338  -1.975  33.563  1.00 19.86           C  
ANISOU  276  CD1 PHE A  27     3728   2709   1109   -472    -78    245       C  
ATOM    277  CD2 PHE A  27       1.064  -1.348  33.626  1.00 19.65           C  
ANISOU  277  CD2 PHE A  27     3674   2506   1285   -359   -194    674       C  
ATOM    278  CE1 PHE A  27       2.933  -3.324  33.290  1.00 20.95           C  
ANISOU  278  CE1 PHE A  27     3818   2738   1403   -623    211    559       C  
ATOM    279  CE2 PHE A  27       0.662  -2.670  33.365  1.00 21.49           C  
ANISOU  279  CE2 PHE A  27     3862   2833   1467   -669   -256    935       C  
ATOM    280  CZ  PHE A  27       1.615  -3.630  33.169  1.00 20.31           C  
ANISOU  280  CZ  PHE A  27     3892   2555   1267   -719    -73    214       C  
ATOM    281  N   ALA A  28       0.662   1.628  32.154  1.00 16.33           N  
ANISOU  281  N   ALA A  28     3027   1996   1178   -314    110    187       N  
ATOM    282  CA  ALA A  28      -0.568   1.366  31.424  1.00 16.83           C  
ANISOU  282  CA  ALA A  28     2929   2033   1431   -262    170    497       C  
ATOM    283  C   ALA A  28      -0.496   2.028  30.055  1.00 15.99           C  
ANISOU  283  C   ALA A  28     2818   1911   1344   -339    -17    352       C  
ATOM    284  O   ALA A  28      -0.938   1.451  29.057  1.00 17.21           O  
ANISOU  284  O   ALA A  28     2969   2093   1474   -215   -239    113       O  
ATOM    285  CB  ALA A  28      -1.742   1.920  32.116  1.00 18.82           C  
ANISOU  285  CB  ALA A  28     3176   2180   1794   -191    398    307       C  
ATOM    286  N   THR A  29       0.078   3.236  29.935  1.00 15.64           N  
ANISOU  286  N   THR A  29     2915   1912   1114   -284     94    220       N  
ATOM    287  CA  THR A  29       0.273   3.848  28.664  1.00 15.43           C  
ANISOU  287  CA  THR A  29     2780   1905   1176   -210    -60    333       C  
ATOM    288  C   THR A  29       1.207   3.007  27.820  1.00 14.90           C  
ANISOU  288  C   THR A  29     2658   1840   1164   -284     12     42       C  
ATOM    289  O   THR A  29       0.962   2.861  26.597  1.00 15.72           O  
ANISOU  289  O   THR A  29     3098   2090    782   -206   -137      0       O  
ATOM    290  CB  THR A  29       0.737   5.311  28.812  1.00 16.09           C  
ANISOU  290  CB  THR A  29     3028   1535   1548   -200   -115    317       C  
ATOM    291  OG1 THR A  29      -0.259   6.036  29.563  1.00 19.79           O  
ANISOU  291  OG1 THR A  29     3458   2267   1791    -81    -64     89       O  
ATOM    292  CG2 THR A  29       0.948   5.966  27.434  1.00 17.87           C  
ANISOU  292  CG2 THR A  29     3220   2032   1539   -244   -348    708       C  
ATOM    293  N   ARG A  30       2.339   2.538  28.327  1.00 15.03           N  
ANISOU  293  N   ARG A  30     2787   1851   1071   -321   -131    176       N  
ATOM    294  CA  ARG A  30       3.217   1.693  27.529  1.00 14.71           C  
ANISOU  294  CA  ARG A  30     2662   1944    980   -220    -42    261       C  
ATOM    295  C   ARG A  30       2.522   0.510  26.997  1.00 14.37           C  
ANISOU  295  C   ARG A  30     2528   1903   1026   -330    -52    355       C  
ATOM    296  O   ARG A  30       2.730   0.105  25.835  1.00 15.41           O  
ANISOU  296  O   ARG A  30     2775   2267    813   -263    -35     70       O  
ATOM    297  CB  ARG A  30       4.504   1.205  28.275  1.00 15.97           C  
ANISOU  297  CB  ARG A  30     3054   2036    974   -414   -210    325       C  
ATOM    298  CG  ARG A  30       5.438   2.290  28.668  1.00 15.65           C  
ANISOU  298  CG  ARG A  30     3094   1916    933   -191   -119    166       C  
ATOM    299  CD  ARG A  30       6.787   1.720  28.965  1.00 15.06           C  
ANISOU  299  CD  ARG A  30     2693   2172    854   -215    -38    275       C  
ATOM    300  NE  ARG A  30       6.739   0.536  29.825  1.00 15.43           N  
ANISOU  300  NE  ARG A  30     3032   1925    905   -141     39    104       N  
ATOM    301  CZ  ARG A  30       6.600   0.572  31.135  1.00 15.77           C  
ANISOU  301  CZ  ARG A  30     2956   1804   1229   -132    -99    179       C  
ATOM    302  NH1 ARG A  30       6.504   1.721  31.826  1.00 16.13           N  
ANISOU  302  NH1 ARG A  30     3439   1870    816   -168    -23    255       N  
ATOM    303  NH2 ARG A  30       6.564  -0.589  31.828  1.00 17.61           N  
ANISOU  303  NH2 ARG A  30     3483   2147   1060      5    216    -79       N  
ATOM    304  N   LYS A  31       1.714  -0.168  27.803  1.00 14.91           N  
ANISOU  304  N   LYS A  31     3029   1881    753   -240     13     72       N  
ATOM    305  CA  LYS A  31       1.115  -1.411  27.349  1.00 14.65           C  
ANISOU  305  CA  LYS A  31     3000   1557   1007   -208    -77    -19       C  
ATOM    306  C   LYS A  31       0.167  -1.133  26.225  1.00 14.75           C  
ANISOU  306  C   LYS A  31     2616   1837   1148   -135     -8   -115       C  
ATOM    307  O   LYS A  31       0.160  -1.869  25.211  1.00 16.95           O  
ANISOU  307  O   LYS A  31     3172   2091   1175   -190     36   -416       O  
ATOM    308  CB  LYS A  31       0.410  -2.138  28.496  1.00 16.39           C  
ANISOU  308  CB  LYS A  31     3283   1498   1444   -244      1     30       C  
ATOM    309  CG  LYS A  31       1.420  -2.611  29.601  1.00 19.70           C  
ANISOU  309  CG  LYS A  31     3645   2500   1339   -159     88    424       C  
ATOM    310  CD  LYS A  31       2.518  -3.490  29.008  1.00 26.04           C  
ANISOU  310  CD  LYS A  31     4137   3286   2468    668    -94    703       C  
ATOM    311  CE  LYS A  31       3.779  -3.639  29.797  1.00 29.91           C  
ANISOU  311  CE  LYS A  31     4324   4243   2796    537     16   -282       C  
ATOM    312  NZ  LYS A  31       4.826  -4.364  29.034  1.00 30.41           N  
ANISOU  312  NZ  LYS A  31     4559   4252   2740    545    215   -424       N  
ATOM    313  N   VAL A  32      -0.689  -0.157  26.375  1.00 14.69           N  
ANISOU  313  N   VAL A  32     2741   1765   1074   -142    -64   -143       N  
ATOM    314  CA  VAL A  32      -1.677   0.151  25.297  1.00 16.46           C  
ANISOU  314  CA  VAL A  32     2874   2007   1373   -185   -212   -163       C  
ATOM    315  C   VAL A  32      -1.011   0.811  24.104  1.00 15.29           C  
ANISOU  315  C   VAL A  32     2575   2101   1132   -158   -126     -4       C  
ATOM    316  O   VAL A  32      -1.340   0.480  22.934  1.00 16.39           O  
ANISOU  316  O   VAL A  32     2724   2462   1041   -280     -8   -312       O  
ATOM    317  CB  VAL A  32      -2.870   1.010  25.878  1.00 17.80           C  
ANISOU  317  CB  VAL A  32     2992   2354   1414    -24    -71    -35       C  
ATOM    318  CG1 VAL A  32      -3.732   1.540  24.802  1.00 21.57           C  
ANISOU  318  CG1 VAL A  32     3385   2899   1913    146   -223    -83       C  
ATOM    319  CG2 VAL A  32      -3.664   0.265  26.951  1.00 19.17           C  
ANISOU  319  CG2 VAL A  32     3139   2699   1446    143    108    181       C  
ATOM    320  N   ALA A  33      -0.025   1.667  24.309  1.00 14.90           N  
ANISOU  320  N   ALA A  33     2510   2159    991    -65   -177    179       N  
ATOM    321  CA  ALA A  33       0.640   2.302  23.188  1.00 15.68           C  
ANISOU  321  CA  ALA A  33     2775   2122   1059    -76   -147    397       C  
ATOM    322  C   ALA A  33       1.429   1.262  22.428  1.00 16.29           C  
ANISOU  322  C   ALA A  33     2814   2262   1113    -22      0    244       C  
ATOM    323  O   ALA A  33       1.526   1.333  21.198  1.00 16.83           O  
ANISOU  323  O   ALA A  33     3138   2352    903    -47     34    225       O  
ATOM    324  CB  ALA A  33       1.538   3.417  23.635  1.00 16.71           C  
ANISOU  324  CB  ALA A  33     2919   2263   1164   -205    -73    378       C  
ATOM    325  N   GLY A  34       2.006   0.271  23.096  1.00 16.07           N  
ANISOU  325  N   GLY A  34     2746   2086   1271    179    -43    273       N  
ATOM    326  CA  GLY A  34       2.856  -0.697  22.433  1.00 16.51           C  
ANISOU  326  CA  GLY A  34     2603   2175   1493    229     13    327       C  
ATOM    327  C   GLY A  34       2.065  -1.644  21.538  1.00 17.06           C  
ANISOU  327  C   GLY A  34     2716   2396   1368    142    124    260       C  
ATOM    328  O   GLY A  34       2.623  -2.196  20.575  1.00 19.15           O  
ANISOU  328  O   GLY A  34     2980   2944   1352     66    296   -148       O  
ATOM    329  N   MET A  35       0.758  -1.825  21.757  1.00 15.96           N  
ANISOU  329  N   MET A  35     2747   1980   1337    155    298    324       N  
ATOM    330  CA  MET A  35      -0.087  -2.670  20.894  1.00 16.20           C  
ANISOU  330  CA  MET A  35     2716   2000   1439     17    251    431       C  
ATOM    331  C   MET A  35      -0.458  -2.003  19.584  1.00 14.94           C  
ANISOU  331  C   MET A  35     2559   1734   1383     49    188    522       C  
ATOM    332  O   MET A  35      -0.754  -2.676  18.573  1.00 17.87           O  
ANISOU  332  O   MET A  35     3028   1984   1776   -258    -19    271       O  
ATOM    333  CB  MET A  35      -1.422  -3.008  21.538  1.00 17.19           C  
ANISOU  333  CB  MET A  35     2891   1521   2119      9    301    489       C  
ATOM    334  CG  MET A  35      -1.273  -3.899  22.762  1.00 16.62           C  
ANISOU  334  CG  MET A  35     3401   1635   1278   -139    415     83       C  
ATOM    335  SD  MET A  35      -0.633  -5.498  22.428  1.00 17.67           S  
ANISOU  335  SD  MET A  35     3636   1815   1262    121    206    255       S  
ATOM    336  CE  MET A  35      -1.658  -6.255  21.267  1.00 24.43           C  
ANISOU  336  CE  MET A  35     5610   2309   1363     60   -519    431       C  
ATOM    337  N   ALA A  36      -0.413  -0.683  19.535  1.00 15.26           N  
ANISOU  337  N   ALA A  36     2485   1731   1580    -76     97    532       N  
ATOM    338  CA  ALA A  36      -0.946   0.037  18.389  1.00 15.36           C  
ANISOU  338  CA  ALA A  36     2610   1977   1249    -40    190    432       C  
ATOM    339  C   ALA A  36      -0.134  -0.269  17.137  1.00 15.16           C  
ANISOU  339  C   ALA A  36     2573   1952   1233   -355     29    140       C  
ATOM    340  O   ALA A  36       1.090  -0.376  17.151  1.00 16.31           O  
ANISOU  340  O   ALA A  36     2493   2482   1221     -2     78    151       O  
ATOM    341  CB  ALA A  36      -1.001   1.518  18.635  1.00 17.16           C  
ANISOU  341  CB  ALA A  36     3069   1915   1533     66    181    454       C  
ATOM    342  N   LYS A  37      -0.804  -0.305  16.026  1.00 16.65           N  
ANISOU  342  N   LYS A  37     2730   2019   1577   -337    -97    371       N  
ATOM    343  CA  LYS A  37      -0.244  -0.443  14.673  1.00 16.55           C  
ANISOU  343  CA  LYS A  37     2999   1899   1390   -270      0    143       C  
ATOM    344  C   LYS A  37      -0.769   0.728  13.848  1.00 15.97           C  
ANISOU  344  C   LYS A  37     3039   1845   1184   -346     86    180       C  
ATOM    345  O   LYS A  37      -1.708   0.575  13.053  1.00 18.27           O  
ANISOU  345  O   LYS A  37     3249   2202   1490   -393   -173    340       O  
ATOM    346  CB  LYS A  37      -0.637  -1.794  14.082  1.00 18.95           C  
ANISOU  346  CB  LYS A  37     3305   2046   1848   -245   -109     98       C  
ATOM    347  CG  LYS A  37      -0.032  -2.972  14.812  1.00 22.24           C  
ANISOU  347  CG  LYS A  37     3454   2524   2471   -249   -284    -70       C  
ATOM    348  CD  LYS A  37       1.434  -3.043  14.511  1.00 24.53           C  
ANISOU  348  CD  LYS A  37     3848   3131   2338    205    -33    -10       C  
ATOM    349  CE  LYS A  37       2.010  -4.411  14.768  1.00 26.78           C  
ANISOU  349  CE  LYS A  37     4633   3236   2304    107     22    -23       C  
ATOM    350  NZ  LYS A  37       1.840  -4.774  16.156  1.00 30.52           N  
ANISOU  350  NZ  LYS A  37     5466   3706   2422    674     43    578       N  
ATOM    351  N   PRO A  38      -0.200   1.902  14.058  1.00 15.81           N  
ANISOU  351  N   PRO A  38     2865   1859   1280   -291    212    133       N  
ATOM    352  CA  PRO A  38      -0.777   3.060  13.415  1.00 15.91           C  
ANISOU  352  CA  PRO A  38     3050   1796   1199   -227    281    202       C  
ATOM    353  C   PRO A  38      -0.612   3.098  11.919  1.00 16.78           C  
ANISOU  353  C   PRO A  38     3239   1766   1368   -240    437     13       C  
ATOM    354  O   PRO A  38       0.322   2.532  11.351  1.00 17.90           O  
ANISOU  354  O   PRO A  38     3463   2135   1201   -268    431    236       O  
ATOM    355  CB  PRO A  38      -0.002   4.232  14.035  1.00 18.97           C  
ANISOU  355  CB  PRO A  38     3344   2254   1607   -218    214    111       C  
ATOM    356  CG  PRO A  38       1.117   3.662  14.716  1.00 23.45           C  
ANISOU  356  CG  PRO A  38     3652   2553   2705   -541   -150    171       C  
ATOM    357  CD  PRO A  38       0.848   2.265  15.011  1.00 16.37           C  
ANISOU  357  CD  PRO A  38     2848   1980   1392   -297     92    -21       C  
ATOM    358  N   ASN A  39      -1.475   3.914  11.360  1.00 16.70           N  
ANISOU  358  N   ASN A  39     3346   1835   1161   -128    370    175       N  
ATOM    359  CA  ASN A  39      -1.279   4.427   9.991  1.00 18.27           C  
ANISOU  359  CA  ASN A  39     3575   1778   1588    -47    442    198       C  
ATOM    360  C   ASN A  39      -0.757   5.829  10.060  1.00 18.83           C  
ANISOU  360  C   ASN A  39     3874   1712   1566   -219    551   -285       C  
ATOM    361  O   ASN A  39      -1.254   6.648  10.814  1.00 23.36           O  
ANISOU  361  O   ASN A  39     4533   1955   2387   -483   1456   -186       O  
ATOM    362  CB  ASN A  39      -2.588   4.418   9.288  1.00 21.15           C  
ANISOU  362  CB  ASN A  39     3948   2289   1800      4    241     93       C  
ATOM    363  CG  ASN A  39      -2.822   3.144   8.540  1.00 24.21           C  
ANISOU  363  CG  ASN A  39     4160   2431   2607    -53   -270    368       C  
ATOM    364  OD1 ASN A  39      -2.499   2.042   8.982  1.00 30.23           O  
ANISOU  364  OD1 ASN A  39     5642   2767   3077     13   -840     14       O  
ATOM    365  ND2 ASN A  39      -3.301   3.310   7.292  1.00 31.11           N  
ANISOU  365  ND2 ASN A  39     5078   4319   2423    342   -241   -224       N  
ATOM    366  N   MET A  40       0.296   6.098   9.303  1.00 17.24           N  
ANISOU  366  N   MET A  40     3593   1588   1366   -212    613    -34       N  
ATOM    367  CA  MET A  40       0.897   7.401   9.334  1.00 16.58           C  
ANISOU  367  CA  MET A  40     3399   1691   1209   -167    479    -66       C  
ATOM    368  C   MET A  40       0.745   7.994   7.927  1.00 16.36           C  
ANISOU  368  C   MET A  40     3477   1549   1188    -86    461     49       C  
ATOM    369  O   MET A  40       1.059   7.339   6.917  1.00 17.21           O  
ANISOU  369  O   MET A  40     3814   1594   1130     59    532    108       O  
ATOM    370  CB  MET A  40       2.348   7.259   9.677  1.00 17.17           C  
ANISOU  370  CB  MET A  40     3460   1675   1386    -61    480     65       C  
ATOM    371  CG  MET A  40       3.097   8.556   9.642  1.00 19.07           C  
ANISOU  371  CG  MET A  40     3528   1866   1850   -290    366    212       C  
ATOM    372  SD  MET A  40       4.767   8.420  10.258  1.00 21.54           S  
ANISOU  372  SD  MET A  40     4384   1943   1854   -138    -86   -115       S  
ATOM    373  CE  MET A  40       5.436   7.089   9.257  1.00 22.64           C  
ANISOU  373  CE  MET A  40     4048   2645   1909   -348    420   -201       C  
ATOM    374  N   ILE A  41       0.162   9.197   7.857  1.00 15.82           N  
ANISOU  374  N   ILE A  41     3225   1564   1219   -100    400    -42       N  
ATOM    375  CA  ILE A  41      -0.048   9.919   6.618  1.00 15.35           C  
ANISOU  375  CA  ILE A  41     3075   1684   1071   -150    256      5       C  
ATOM    376  C   ILE A  41       0.888  11.116   6.619  1.00 14.43           C  
ANISOU  376  C   ILE A  41     3025   1394   1063   -225     98     76       C  
ATOM    377  O   ILE A  41       0.772  11.979   7.498  1.00 15.32           O  
ANISOU  377  O   ILE A  41     3299   1511   1010   -266    233    -84       O  
ATOM    378  CB  ILE A  41      -1.504  10.354   6.433  1.00 17.29           C  
ANISOU  378  CB  ILE A  41     2957   1828   1783   -246    161   -313       C  
ATOM    379  CG1 ILE A  41      -2.467   9.158   6.525  1.00 22.57           C  
ANISOU  379  CG1 ILE A  41     3227   2597   2749   -440    287   -463       C  
ATOM    380  CG2 ILE A  41      -1.752  11.100   5.072  1.00 21.03           C  
ANISOU  380  CG2 ILE A  41     3419   2755   1815   -112   -393    -57       C  
ATOM    381  CD1 ILE A  41      -3.919   9.592   6.564  1.00 26.48           C  
ANISOU  381  CD1 ILE A  41     3275   3243   3541   -626   -146   -607       C  
ATOM    382  N   ILE A  42       1.769  11.198   5.617  1.00 13.73           N  
ANISOU  382  N   ILE A  42     2917   1425    874   -149    133   -137       N  
ATOM    383  CA  ILE A  42       2.688  12.283   5.487  1.00 12.58           C  
ANISOU  383  CA  ILE A  42     2823   1421    535    -32    -95    -86       C  
ATOM    384  C   ILE A  42       2.365  13.024   4.243  1.00 12.63           C  
ANISOU  384  C   ILE A  42     2544   1435    820    -76    -51    -42       C  
ATOM    385  O   ILE A  42       2.217  12.449   3.159  1.00 14.30           O  
ANISOU  385  O   ILE A  42     3258   1493    680    -41   -126    -24       O  
ATOM    386  CB  ILE A  42       4.171  11.801   5.506  1.00 13.35           C  
ANISOU  386  CB  ILE A  42     2924   1576    572    -32     86   -145       C  
ATOM    387  CG1 ILE A  42       4.464  11.030   6.776  1.00 14.03           C  
ANISOU  387  CG1 ILE A  42     2894   1728    707    -73    -57     88       C  
ATOM    388  CG2 ILE A  42       5.105  12.959   5.283  1.00 14.19           C  
ANISOU  388  CG2 ILE A  42     2759   1623   1008   -227    -31    -90       C  
ATOM    389  CD1 ILE A  42       5.859  10.468   6.871  1.00 16.98           C  
ANISOU  389  CD1 ILE A  42     3261   2217    972    352   -173    -33       C  
ATOM    390  N   SER A  43       2.207  14.348   4.340  1.00 13.44           N  
ANISOU  390  N   SER A  43     2997   1396    711    -50    -47    -88       N  
ATOM    391  CA  SER A  43       1.892  15.211   3.207  1.00 14.33           C  
ANISOU  391  CA  SER A  43     2960   1672    813    -47   -109     81       C  
ATOM    392  C   SER A  43       2.691  16.485   3.261  1.00 13.43           C  
ANISOU  392  C   SER A  43     3038   1411    654     53   -161    -74       C  
ATOM    393  O   SER A  43       3.152  16.885   4.338  1.00 14.19           O  
ANISOU  393  O   SER A  43     3143   1497    750     14    -83      8       O  
ATOM    394  CB  SER A  43       0.397  15.458   3.162  1.00 16.52           C  
ANISOU  394  CB  SER A  43     3178   1805   1294   -135   -102    269       C  
ATOM    395  OG  SER A  43      -0.035  16.107   4.318  1.00 20.16           O  
ANISOU  395  OG  SER A  43     3583   2326   1748    201    -91    171       O  
ATOM    396  N   VAL A  44       2.813  17.122   2.123  1.00 14.51           N  
ANISOU  396  N   VAL A  44     3298   1536    677     -4   -188     36       N  
ATOM    397  CA  VAL A  44       3.498  18.393   2.014  1.00 15.00           C  
ANISOU  397  CA  VAL A  44     3431   1309    959    -79    -85    169       C  
ATOM    398  C   VAL A  44       2.663  19.351   1.255  1.00 15.89           C  
ANISOU  398  C   VAL A  44     3596   1612    827    -49   -233     44       C  
ATOM    399  O   VAL A  44       2.071  18.988   0.223  1.00 19.41           O  
ANISOU  399  O   VAL A  44     4688   1615   1072     41   -822     39       O  
ATOM    400  CB  VAL A  44       4.889  18.192   1.353  1.00 16.67           C  
ANISOU  400  CB  VAL A  44     3361   1614   1359   -315   -186    -55       C  
ATOM    401  CG1 VAL A  44       5.668  19.504   1.220  1.00 23.86           C  
ANISOU  401  CG1 VAL A  44     3942   1964   3160   -476     99    520       C  
ATOM    402  CG2 VAL A  44       5.707  17.182   2.111  1.00 20.82           C  
ANISOU  402  CG2 VAL A  44     3485   2196   2227    -71   -376    -85       C  
ATOM    403  N   ASN A  45       2.660  20.580   1.697  1.00 15.14           N  
ANISOU  403  N   ASN A  45     3496   1522    732    -74   -161    111       N  
ATOM    404  CA  ASN A  45       1.958  21.670   1.033  1.00 14.45           C  
ANISOU  404  CA  ASN A  45     3121   1590    780   -225   -244    127       C  
ATOM    405  C   ASN A  45       2.810  22.892   1.152  1.00 14.62           C  
ANISOU  405  C   ASN A  45     3038   1630    885    -43     -2    149       C  
ATOM    406  O   ASN A  45       2.891  23.462   2.228  1.00 14.75           O  
ANISOU  406  O   ASN A  45     3226   1530    846     21   -127     40       O  
ATOM    407  CB  ASN A  45       0.564  21.807   1.590  1.00 15.17           C  
ANISOU  407  CB  ASN A  45     2994   1721   1049    -71   -378    -15       C  
ATOM    408  CG  ASN A  45      -0.325  22.852   0.910  1.00 16.07           C  
ANISOU  408  CG  ASN A  45     2866   2088   1151   -182   -428    -13       C  
ATOM    409  OD1 ASN A  45      -1.588  22.682   0.811  1.00 18.03           O  
ANISOU  409  OD1 ASN A  45     3482   2159   1208   -115   -257    -38       O  
ATOM    410  ND2 ASN A  45       0.283  23.914   0.446  1.00 15.72           N  
ANISOU  410  ND2 ASN A  45     3165   1592   1213   -168   -452    259       N  
ATOM    411  N   GLY A  46       3.453  23.269   0.069  1.00 16.68           N  
ANISOU  411  N   GLY A  46     3553   1944    838   -311     72    239       N  
ATOM    412  CA  GLY A  46       4.443  24.330   0.138  1.00 17.05           C  
ANISOU  412  CA  GLY A  46     3432   1930   1116   -320      5    205       C  
ATOM    413  C   GLY A  46       5.544  23.957   1.112  1.00 17.69           C  
ANISOU  413  C   GLY A  46     3310   2116   1294   -264     -3    143       C  
ATOM    414  O   GLY A  46       6.162  22.915   0.985  1.00 19.85           O  
ANISOU  414  O   GLY A  46     3628   2304   1610     -4     94     21       O  
ATOM    415  N   ASP A  47       5.800  24.826   2.057  1.00 16.93           N  
ANISOU  415  N   ASP A  47     3285   1992   1154   -219     34    180       N  
ATOM    416  CA  ASP A  47       6.812  24.589   3.055  1.00 17.47           C  
ANISOU  416  CA  ASP A  47     3138   2067   1432   -175    -68    338       C  
ATOM    417  C   ASP A  47       6.332  23.775   4.255  1.00 14.38           C  
ANISOU  417  C   ASP A  47     2743   1692   1027     33     45    118       C  
ATOM    418  O   ASP A  47       7.140  23.490   5.169  1.00 15.99           O  
ANISOU  418  O   ASP A  47     2829   1961   1284   -175    -23    229       O  
ATOM    419  CB  ASP A  47       7.356  25.921   3.583  1.00 18.92           C  
ANISOU  419  CB  ASP A  47     3352   2311   1524   -355   -257    331       C  
ATOM    420  CG  ASP A  47       8.059  26.734   2.560  1.00 25.29           C  
ANISOU  420  CG  ASP A  47     4077   2947   2583   -351   -223    551       C  
ATOM    421  OD1 ASP A  47       8.555  26.170   1.569  1.00 30.44           O  
ANISOU  421  OD1 ASP A  47     4113   4720   2730   -944    872    911       O  
ATOM    422  OD2 ASP A  47       8.054  27.974   2.711  1.00 31.81           O  
ANISOU  422  OD2 ASP A  47     5661   3121   3303   -589   -408    950       O  
ATOM    423  N   VAL A  48       5.027  23.503   4.303  1.00 13.21           N  
ANISOU  423  N   VAL A  48     2512   1611    895    127    -97    157       N  
ATOM    424  CA  VAL A  48       4.457  22.875   5.495  1.00 12.07           C  
ANISOU  424  CA  VAL A  48     2394   1442    748    -38   -134    157       C  
ATOM    425  C   VAL A  48       4.339  21.375   5.280  1.00 12.59           C  
ANISOU  425  C   VAL A  48     2524   1446    813    -36    -61   -101       C  
ATOM    426  O   VAL A  48       3.742  20.889   4.333  1.00 14.25           O  
ANISOU  426  O   VAL A  48     3056   1503    853    -37   -240     63       O  
ATOM    427  CB  VAL A  48       3.065  23.448   5.778  1.00 13.52           C  
ANISOU  427  CB  VAL A  48     2646   1697    793    120    -55    208       C  
ATOM    428  CG1 VAL A  48       2.488  22.818   7.051  1.00 15.91           C  
ANISOU  428  CG1 VAL A  48     2985   1993   1065     46     60    148       C  
ATOM    429  CG2 VAL A  48       3.130  24.968   5.955  1.00 16.68           C  
ANISOU  429  CG2 VAL A  48     3093   1418   1825    210     78   -144       C  
ATOM    430  N   ILE A  49       4.955  20.637   6.202  1.00 11.94           N  
ANISOU  430  N   ILE A  49     2397   1341    799   -147   -133     49       N  
ATOM    431  CA  ILE A  49       4.866  19.179   6.229  1.00 11.94           C  
ANISOU  431  CA  ILE A  49     2259   1385    889   -124     22    -39       C  
ATOM    432  C   ILE A  49       3.861  18.824   7.309  1.00 11.59           C  
ANISOU  432  C   ILE A  49     2129   1518    755   -159    -28    170       C  
ATOM    433  O   ILE A  49       3.899  19.398   8.428  1.00 13.18           O  
ANISOU  433  O   ILE A  49     2612   1535    860   -109    -26    -80       O  
ATOM    434  CB  ILE A  49       6.244  18.571   6.478  1.00 13.10           C  
ANISOU  434  CB  ILE A  49     2397   1611    969     15     86    -35       C  
ATOM    435  CG1 ILE A  49       7.271  19.010   5.447  1.00 14.33           C  
ANISOU  435  CG1 ILE A  49     2436   1990   1018    113    243   -140       C  
ATOM    436  CG2 ILE A  49       6.198  17.007   6.567  1.00 14.14           C  
ANISOU  436  CG2 ILE A  49     2994   1440    938    115   -158      7       C  
ATOM    437  CD1 ILE A  49       8.699  18.742   5.839  1.00 20.30           C  
ANISOU  437  CD1 ILE A  49     2548   2983   2182    177    370     60       C  
ATOM    438  N   THR A  50       2.987  17.870   7.036  1.00 12.49           N  
ANISOU  438  N   THR A  50     2462   1541    741   -262     -1     77       N  
ATOM    439  CA  THR A  50       2.082  17.316   8.029  1.00 12.42           C  
ANISOU  439  CA  THR A  50     2548   1329    840   -119      5    -47       C  
ATOM    440  C   THR A  50       2.330  15.819   8.179  1.00 12.12           C  
ANISOU  440  C   THR A  50     2488   1465    650   -189    -36   -108       C  
ATOM    441  O   THR A  50       2.442  15.075   7.194  1.00 13.36           O  
ANISOU  441  O   THR A  50     2991   1366    718   -146     56    -23       O  
ATOM    442  CB  THR A  50       0.583  17.591   7.666  1.00 13.51           C  
ANISOU  442  CB  THR A  50     2640   1491   1001   -244    -57   -171       C  
ATOM    443  OG1 THR A  50       0.428  19.009   7.526  1.00 15.05           O  
ANISOU  443  OG1 THR A  50     2823   1735   1157    -12    -88    105       O  
ATOM    444  CG2 THR A  50      -0.412  17.026   8.599  1.00 15.68           C  
ANISOU  444  CG2 THR A  50     2603   1982   1371   -231    271     30       C  
ATOM    445  N   ILE A  51       2.434  15.387   9.447  1.00 12.75           N  
ANISOU  445  N   ILE A  51     2784   1275    783   -174     14    -89       N  
ATOM    446  CA  ILE A  51       2.502  13.986   9.817  1.00 13.11           C  
ANISOU  446  CA  ILE A  51     2484   1284   1211   -136     95   -229       C  
ATOM    447  C   ILE A  51       1.309  13.678  10.699  1.00 13.58           C  
ANISOU  447  C   ILE A  51     2720   1388   1051   -209    136    -91       C  
ATOM    448  O   ILE A  51       1.213  14.189  11.839  1.00 14.43           O  
ANISOU  448  O   ILE A  51     3079   1554    849     -7      9   -138       O  
ATOM    449  CB  ILE A  51       3.857  13.617  10.497  1.00 13.41           C  
ANISOU  449  CB  ILE A  51     2498   1403   1193   -154     61   -139       C  
ATOM    450  CG1 ILE A  51       5.056  14.004   9.630  1.00 14.28           C  
ANISOU  450  CG1 ILE A  51     2584   1546   1292    -98    184   -432       C  
ATOM    451  CG2 ILE A  51       3.853  12.173  10.919  1.00 15.36           C  
ANISOU  451  CG2 ILE A  51     2942   1426   1467    157    248     51       C  
ATOM    452  CD1 ILE A  51       6.432  13.788  10.233  1.00 18.29           C  
ANISOU  452  CD1 ILE A  51     2446   2271   2231    137     52   -405       C  
ATOM    453  N   LYS A  52       0.412  12.852  10.228  1.00 14.57           N  
ANISOU  453  N   LYS A  52     2964   1687    884   -341    274    -78       N  
ATOM    454  CA  LYS A  52      -0.757  12.376  10.938  1.00 15.49           C  
ANISOU  454  CA  LYS A  52     3115   1453   1318   -149    369   -283       C  
ATOM    455  C   LYS A  52      -0.566  10.939  11.298  1.00 15.60           C  
ANISOU  455  C   LYS A  52     3250   1523   1151   -234    323   -314       C  
ATOM    456  O   LYS A  52      -0.196  10.150  10.455  1.00 19.42           O  
ANISOU  456  O   LYS A  52     4529   1461   1389   -337    735    -59       O  
ATOM    457  CB  LYS A  52      -2.006  12.570  10.059  1.00 18.74           C  
ANISOU  457  CB  LYS A  52     3058   2560   1500   -366    331   -478       C  
ATOM    458  CG  LYS A  52      -3.326  12.215  10.622  1.00 24.82           C  
ANISOU  458  CG  LYS A  52     3598   3073   2757   -219    216    228       C  
ATOM    459  CD  LYS A  52      -4.423  12.631   9.655  1.00 28.66           C  
ANISOU  459  CD  LYS A  52     3948   4082   2860     82   -137    334       C  
ATOM    460  CE  LYS A  52      -5.834  12.429  10.157  1.00 32.63           C  
ANISOU  460  CE  LYS A  52     4130   4478   3790     27   -354    445       C  
ATOM    461  NZ  LYS A  52      -6.758  12.483   8.938  1.00 37.94           N  
ANISOU  461  NZ  LYS A  52     4311   5818   4287    194   -650    676       N  
ATOM    462  N   SER A  53      -0.865  10.572  12.539  1.00 16.00           N  
ANISOU  462  N   SER A  53     3289   1601   1189   -243    331     -2       N  
ATOM    463  CA  SER A  53      -0.860   9.190  13.000  1.00 16.45           C  
ANISOU  463  CA  SER A  53     3058   1721   1470   -378    362   -119       C  
ATOM    464  C   SER A  53      -2.288   8.844  13.414  1.00 15.49           C  
ANISOU  464  C   SER A  53     3263   1540   1080   -451    362   -139       C  
ATOM    465  O   SER A  53      -2.841   9.516  14.278  1.00 17.91           O  
ANISOU  465  O   SER A  53     3584   1836   1384   -509    596   -243       O  
ATOM    466  CB  SER A  53       0.108   9.016  14.111  1.00 17.47           C  
ANISOU  466  CB  SER A  53     3197   1558   1883   -181    204    156       C  
ATOM    467  OG  SER A  53       0.157   7.688  14.580  1.00 21.01           O  
ANISOU  467  OG  SER A  53     4136   1917   1930   -273    104    266       O  
ATOM    468  N   GLU A  54      -2.834   7.837  12.778  1.00 17.28           N  
ANISOU  468  N   GLU A  54     3389   1962   1214   -558    413   -239       N  
ATOM    469  CA  GLU A  54      -4.186   7.330  13.075  1.00 17.37           C  
ANISOU  469  CA  GLU A  54     3380   1777   1439   -490    364   -227       C  
ATOM    470  C   GLU A  54      -3.984   6.018  13.805  1.00 18.23           C  
ANISOU  470  C   GLU A  54     3304   2134   1486   -512    297     23       C  
ATOM    471  O   GLU A  54      -3.384   5.068  13.235  1.00 17.27           O  
ANISOU  471  O   GLU A  54     3262   2002   1295   -316    169    238       O  
ATOM    472  CB  GLU A  54      -5.030   7.128  11.850  1.00 20.95           C  
ANISOU  472  CB  GLU A  54     3762   2208   1987   -332    323     74       C  
ATOM    473  CG  GLU A  54      -5.250   8.413  10.994  1.00 26.47           C  
ANISOU  473  CG  GLU A  54     4394   2838   2822   -226    372    419       C  
ATOM    474  CD  GLU A  54      -6.127   8.123   9.803  1.00 31.35           C  
ANISOU  474  CD  GLU A  54     4952   3400   3560    259   -149    650       C  
ATOM    475  OE1 GLU A  54      -5.796   7.196   9.066  1.00 36.61           O  
ANISOU  475  OE1 GLU A  54     5924   4403   3583    137   -296     65       O  
ATOM    476  OE2 GLU A  54      -7.146   8.819   9.590  1.00 42.36           O  
ANISOU  476  OE2 GLU A  54     5661   4852   5582    492   -181    404       O  
ATOM    477  N   SER A  55      -4.471   5.933  15.033  1.00 18.62           N  
ANISOU  477  N   SER A  55     3213   2474   1385   -326    149     61       N  
ATOM    478  CA  SER A  55      -4.109   4.902  15.879  1.00 20.17           C  
ANISOU  478  CA  SER A  55     3278   2581   1802     88    330    251       C  
ATOM    479  C   SER A  55      -5.276   4.489  16.776  1.00 19.92           C  
ANISOU  479  C   SER A  55     3557   2474   1535    263    419    368       C  
ATOM    480  O   SER A  55      -6.068   5.299  17.154  1.00 19.95           O  
ANISOU  480  O   SER A  55     3560   2350   1668    347    597    808       O  
ATOM    481  CB  SER A  55      -2.996   5.526  16.750  1.00 21.69           C  
ANISOU  481  CB  SER A  55     3557   2546   2137     11    281    315       C  
ATOM    482  OG  SER A  55      -2.715   4.612  17.756  1.00 21.18           O  
ANISOU  482  OG  SER A  55     3691   2563   1792    190    197    833       O  
ATOM    483  N   THR A  56      -5.358   3.221  17.120  1.00 19.26           N  
ANISOU  483  N   THR A  56     3579   2202   1537    134    345    188       N  
ATOM    484  CA  THR A  56      -6.331   2.809  18.153  1.00 19.97           C  
ANISOU  484  CA  THR A  56     3902   1884   1798   -175    244     97       C  
ATOM    485  C   THR A  56      -5.961   3.321  19.529  1.00 18.56           C  
ANISOU  485  C   THR A  56     3633   1966   1452   -337    416    306       C  
ATOM    486  O   THR A  56      -6.806   3.311  20.437  1.00 23.48           O  
ANISOU  486  O   THR A  56     4159   2846   1914   -825    826     92       O  
ATOM    487  CB  THR A  56      -6.342   1.243  18.197  1.00 23.47           C  
ANISOU  487  CB  THR A  56     4120   2215   2581   -208     -7   -164       C  
ATOM    488  OG1 THR A  56      -4.948   0.786  18.197  1.00 23.51           O  
ANISOU  488  OG1 THR A  56     4442   2173   2316    104    -97   -385       O  
ATOM    489  CG2 THR A  56      -7.082   0.708  16.957  1.00 23.75           C  
ANISOU  489  CG2 THR A  56     4679   1967   2375   -100   -417   -484       C  
ATOM    490  N   PHE A  57      -4.698   3.661  19.733  1.00 17.36           N  
ANISOU  490  N   PHE A  57     3584   1883   1129      7    320    139       N  
ATOM    491  CA  PHE A  57      -4.261   4.259  20.986  1.00 17.81           C  
ANISOU  491  CA  PHE A  57     3580   1903   1282    -96    320     90       C  
ATOM    492  C   PHE A  57      -4.564   5.754  21.002  1.00 19.64           C  
ANISOU  492  C   PHE A  57     3734   1995   1731    -26    384    378       C  
ATOM    493  O   PHE A  57      -5.431   6.203  21.731  1.00 22.31           O  
ANISOU  493  O   PHE A  57     3788   2186   2500     31    972    431       O  
ATOM    494  CB  PHE A  57      -2.780   4.021  21.218  1.00 18.90           C  
ANISOU  494  CB  PHE A  57     3840   1961   1380    179    187    359       C  
ATOM    495  CG  PHE A  57      -2.179   4.822  22.338  1.00 22.71           C  
ANISOU  495  CG  PHE A  57     4404   2342   1881     64   -185    459       C  
ATOM    496  CD1 PHE A  57      -2.699   4.785  23.597  1.00 23.99           C  
ANISOU  496  CD1 PHE A  57     4802   2696   1614    148   -359    137       C  
ATOM    497  CD2 PHE A  57      -1.039   5.618  22.119  1.00 22.97           C  
ANISOU  497  CD2 PHE A  57     4272   2384   2070    103   -144    288       C  
ATOM    498  CE1 PHE A  57      -2.110   5.545  24.599  1.00 27.75           C  
ANISOU  498  CE1 PHE A  57     4888   2970   2684   -261   -779    225       C  
ATOM    499  CE2 PHE A  57      -0.473   6.320  23.129  1.00 26.27           C  
ANISOU  499  CE2 PHE A  57     4702   2316   2961    112   -726    736       C  
ATOM    500  CZ  PHE A  57      -1.014   6.288  24.332  1.00 26.70           C  
ANISOU  500  CZ  PHE A  57     4848   2487   2809   -132   -731    430       C  
ATOM    501  N   LYS A  58      -3.830   6.576  20.247  1.00 19.60           N  
ANISOU  501  N   LYS A  58     3532   1941   1972    113    636    481       N  
ATOM    502  CA  LYS A  58      -4.061   8.044  20.260  1.00 19.44           C  
ANISOU  502  CA  LYS A  58     3535   1861   1989    160    446    342       C  
ATOM    503  C   LYS A  58      -3.718   8.646  18.924  1.00 19.30           C  
ANISOU  503  C   LYS A  58     3369   1949   2014     99    686    268       C  
ATOM    504  O   LYS A  58      -2.540   8.600  18.599  1.00 20.88           O  
ANISOU  504  O   LYS A  58     3653   2450   1827    216    421    372       O  
ATOM    505  CB  LYS A  58      -3.196   8.686  21.372  1.00 21.56           C  
ANISOU  505  CB  LYS A  58     3419   2104   2665      8    330    320       C  
ATOM    506  CG  LYS A  58      -3.291  10.136  21.509  1.00 23.34           C  
ANISOU  506  CG  LYS A  58     3960   2433   2472   -113    161    417       C  
ATOM    507  CD  LYS A  58      -4.625  10.539  22.029  1.00 29.55           C  
ANISOU  507  CD  LYS A  58     4023   3564   3641   -297    201     38       C  
ATOM    508  CE  LYS A  58      -4.692  12.018  22.351  1.00 32.43           C  
ANISOU  508  CE  LYS A  58     4508   3816   3997   -147    143     94       C  
ATOM    509  NZ  LYS A  58      -6.091  12.558  22.405  1.00 36.58           N  
ANISOU  509  NZ  LYS A  58     4728   4784   4386    113    172     29       N  
ATOM    510  N   ASN A  59      -4.698   9.293  18.280  1.00 17.65           N  
ANISOU  510  N   ASN A  59     3084   1803   1817    -90    678    174       N  
ATOM    511  CA  ASN A  59      -4.505   9.994  16.994  1.00 17.52           C  
ANISOU  511  CA  ASN A  59     2922   1879   1854   -107    663     58       C  
ATOM    512  C   ASN A  59      -3.739  11.253  17.283  1.00 17.77           C  
ANISOU  512  C   ASN A  59     2969   1944   1836   -169    590    -54       C  
ATOM    513  O   ASN A  59      -3.980  11.934  18.289  1.00 19.47           O  
ANISOU  513  O   ASN A  59     3340   1958   2099   -320    779   -302       O  
ATOM    514  CB  ASN A  59      -5.868  10.380  16.470  1.00 18.72           C  
ANISOU  514  CB  ASN A  59     3080   2030   2001   -199    579    184       C  
ATOM    515  CG  ASN A  59      -6.705   9.212  16.066  1.00 19.62           C  
ANISOU  515  CG  ASN A  59     2631   2510   2313    259    470    249       C  
ATOM    516  OD1 ASN A  59      -6.264   8.233  15.544  1.00 18.85           O  
ANISOU  516  OD1 ASN A  59     2971   2243   1947    141    347    289       O  
ATOM    517  ND2 ASN A  59      -7.990   9.301  16.415  1.00 24.68           N  
ANISOU  517  ND2 ASN A  59     2558   3242   3577    119    564     59       N  
ATOM    518  N   THR A  60      -2.777  11.546  16.425  1.00 15.08           N  
ANISOU  518  N   THR A  60     2611   1767   1351   -119    419    -34       N  
ATOM    519  CA  THR A  60      -1.998  12.755  16.541  1.00 15.23           C  
ANISOU  519  CA  THR A  60     2797   1794   1194   -201    394     13       C  
ATOM    520  C   THR A  60      -1.860  13.375  15.140  1.00 14.83           C  
ANISOU  520  C   THR A  60     2739   1698   1197    -99    323   -128       C  
ATOM    521  O   THR A  60      -1.948  12.699  14.129  1.00 15.22           O  
ANISOU  521  O   THR A  60     2968   1682   1131   -157    295    -26       O  
ATOM    522  CB  THR A  60      -0.575  12.502  17.101  1.00 15.30           C  
ANISOU  522  CB  THR A  60     2836   1798   1178   -170    316    -66       C  
ATOM    523  OG1 THR A  60       0.166  11.652  16.232  1.00 17.44           O  
ANISOU  523  OG1 THR A  60     3416   1783   1428   -150    225    113       O  
ATOM    524  CG2 THR A  60      -0.587  11.913  18.506  1.00 18.12           C  
ANISOU  524  CG2 THR A  60     3286   2342   1255   -100    341    221       C  
ATOM    525  N   GLU A  61      -1.592  14.667  15.113  1.00 14.41           N  
ANISOU  525  N   GLU A  61     2878   1504   1090   -243    324     64       N  
ATOM    526  CA  GLU A  61      -1.303  15.382  13.880  1.00 15.98           C  
ANISOU  526  CA  GLU A  61     2726   1875   1469   -181    296     18       C  
ATOM    527  C   GLU A  61      -0.366  16.532  14.180  1.00 15.42           C  
ANISOU  527  C   GLU A  61     2785   1418   1655   -185    382    -94       C  
ATOM    528  O   GLU A  61      -0.638  17.315  15.126  1.00 17.34           O  
ANISOU  528  O   GLU A  61     3462   1741   1383   -166    507   -176       O  
ATOM    529  CB  GLU A  61      -2.589  15.862  13.236  1.00 17.55           C  
ANISOU  529  CB  GLU A  61     2907   1902   1856    -92    257    161       C  
ATOM    530  CG  GLU A  61      -2.360  16.576  11.912  1.00 21.47           C  
ANISOU  530  CG  GLU A  61     3333   2713   2110   -164    -83    773       C  
ATOM    531  CD  GLU A  61      -3.622  17.155  11.356  1.00 28.99           C  
ANISOU  531  CD  GLU A  61     3399   3620   3995   -330    -70   1210       C  
ATOM    532  OE1 GLU A  61      -3.567  18.261  10.799  1.00 33.17           O  
ANISOU  532  OE1 GLU A  61     3741   4038   4821   -380    -58   1789       O  
ATOM    533  OE2 GLU A  61      -4.684  16.526  11.485  1.00 33.81           O  
ANISOU  533  OE2 GLU A  61     3629   4610   4608   -711   -346   1157       O  
ATOM    534  N   ILE A  62       0.761  16.602  13.494  1.00 13.54           N  
ANISOU  534  N   ILE A  62     2634   1467   1044   -333    169    -79       N  
ATOM    535  CA  ILE A  62       1.675  17.701  13.602  1.00 13.38           C  
ANISOU  535  CA  ILE A  62     2712   1475    895   -158    235   -104       C  
ATOM    536  C   ILE A  62       1.874  18.331  12.222  1.00 13.11           C  
ANISOU  536  C   ILE A  62     2651   1489    841   -252    164    -32       C  
ATOM    537  O   ILE A  62       1.991  17.612  11.222  1.00 14.80           O  
ANISOU  537  O   ILE A  62     3479   1354    788   -291    140    -60       O  
ATOM    538  CB  ILE A  62       3.035  17.346  14.274  1.00 13.93           C  
ANISOU  538  CB  ILE A  62     2649   1672    969   -169     59    -82       C  
ATOM    539  CG1 ILE A  62       3.791  16.262  13.553  1.00 15.36           C  
ANISOU  539  CG1 ILE A  62     2822   1984   1028   -212     66    112       C  
ATOM    540  CG2 ILE A  62       2.806  16.896  15.737  1.00 17.60           C  
ANISOU  540  CG2 ILE A  62     3673   2304    708    139    143    253       C  
ATOM    541  CD1 ILE A  62       5.207  16.067  13.975  1.00 17.02           C  
ANISOU  541  CD1 ILE A  62     2785   2089   1591    149   -172     41       C  
ATOM    542  N   SER A  63       1.956  19.662  12.152  1.00 11.94           N  
ANISOU  542  N   SER A  63     2548   1331    657    -52    157    -20       N  
ATOM    543  CA  SER A  63       2.307  20.396  10.967  1.00 12.07           C  
ANISOU  543  CA  SER A  63     2473   1442    672    -38     61    -18       C  
ATOM    544  C   SER A  63       3.465  21.317  11.296  1.00 12.82           C  
ANISOU  544  C   SER A  63     2383   1482   1006    -95     71     51       C  
ATOM    545  O   SER A  63       3.466  21.933  12.376  1.00 13.34           O  
ANISOU  545  O   SER A  63     2663   1456    947   -166    268   -213       O  
ATOM    546  CB  SER A  63       1.154  21.180  10.373  1.00 14.21           C  
ANISOU  546  CB  SER A  63     2546   1765   1088   -102    106     20       C  
ATOM    547  OG  SER A  63       0.090  20.335   9.907  1.00 15.77           O  
ANISOU  547  OG  SER A  63     2641   1990   1357     50   -126   -137       O  
ATOM    548  N   PHE A  64       4.426  21.465  10.404  1.00 11.61           N  
ANISOU  548  N   PHE A  64     2345   1368    697   -240    101     43       N  
ATOM    549  CA  PHE A  64       5.650  22.163  10.725  1.00 12.10           C  
ANISOU  549  CA  PHE A  64     2464   1299    834    -63     32     53       C  
ATOM    550  C   PHE A  64       6.348  22.588   9.446  1.00 11.60           C  
ANISOU  550  C   PHE A  64     2232   1401    774   -153      5    237       C  
ATOM    551  O   PHE A  64       6.135  22.029   8.376  1.00 12.55           O  
ANISOU  551  O   PHE A  64     2561   1457    748   -185    -38   -105       O  
ATOM    552  CB  PHE A  64       6.531  21.279  11.650  1.00 13.04           C  
ANISOU  552  CB  PHE A  64     2480   1533    942   -207   -129     79       C  
ATOM    553  CG  PHE A  64       6.862  19.982  11.039  1.00 13.36           C  
ANISOU  553  CG  PHE A  64     2759   1444    871    -68    -15   -118       C  
ATOM    554  CD1 PHE A  64       6.052  18.870  11.199  1.00 13.91           C  
ANISOU  554  CD1 PHE A  64     2618   1661   1005    -72    -55     55       C  
ATOM    555  CD2 PHE A  64       8.004  19.834  10.303  1.00 13.27           C  
ANISOU  555  CD2 PHE A  64     2683   1498    859    -21    -50     85       C  
ATOM    556  CE1 PHE A  64       6.361  17.668  10.547  1.00 14.92           C  
ANISOU  556  CE1 PHE A  64     2682   1704   1280      0   -339     92       C  
ATOM    557  CE2 PHE A  64       8.274  18.626   9.660  1.00 13.76           C  
ANISOU  557  CE2 PHE A  64     2619   2005    601    204    -24     50       C  
ATOM    558  CZ  PHE A  64       7.483  17.550   9.816  1.00 14.31           C  
ANISOU  558  CZ  PHE A  64     2729   1588   1117    -29   -110    -55       C  
ATOM    559  N   ILE A  65       7.294  23.480   9.665  1.00 12.22           N  
ANISOU  559  N   ILE A  65     2359   1603    681   -274    -18     23       N  
ATOM    560  CA  ILE A  65       8.243  23.962   8.689  1.00 12.18           C  
ANISOU  560  CA  ILE A  65     2424   1240    961    -94     29     14       C  
ATOM    561  C   ILE A  65       9.648  23.533   9.147  1.00 12.63           C  
ANISOU  561  C   ILE A  65     2300   1232   1267     14     16     87       C  
ATOM    562  O   ILE A  65       9.958  23.601  10.333  1.00 13.12           O  
ANISOU  562  O   ILE A  65     2564   1425    995    -10   -122     64       O  
ATOM    563  CB  ILE A  65       8.142  25.470   8.435  1.00 13.75           C  
ANISOU  563  CB  ILE A  65     2623   1252   1346    -73      3    -66       C  
ATOM    564  CG1 ILE A  65       6.735  25.802   7.902  1.00 15.54           C  
ANISOU  564  CG1 ILE A  65     2630   1590   1682     17   -189    204       C  
ATOM    565  CG2 ILE A  65       9.268  25.926   7.553  1.00 14.28           C  
ANISOU  565  CG2 ILE A  65     2612   1536   1276    -28    102    202       C  
ATOM    566  CD1 ILE A  65       6.491  27.332   7.784  1.00 18.98           C  
ANISOU  566  CD1 ILE A  65     3217   1582   2410    230    115    278       C  
ATOM    567  N   LEU A  66      10.424  22.926   8.281  1.00 12.37           N  
ANISOU  567  N   LEU A  66     2308   1175   1216    -63    112     -7       N  
ATOM    568  CA  LEU A  66      11.728  22.463   8.629  1.00 12.11           C  
ANISOU  568  CA  LEU A  66     2383   1290    927    -51    184     39       C  
ATOM    569  C   LEU A  66      12.568  23.539   9.266  1.00 12.98           C  
ANISOU  569  C   LEU A  66     2426   1428   1076    -39     41    122       C  
ATOM    570  O   LEU A  66      12.603  24.674   8.785  1.00 14.09           O  
ANISOU  570  O   LEU A  66     2635   1322   1395    -75   -139    152       O  
ATOM    571  CB  LEU A  66      12.486  21.890   7.410  1.00 13.91           C  
ANISOU  571  CB  LEU A  66     2521   1548   1214      9    -66    -76       C  
ATOM    572  CG  LEU A  66      11.857  20.628   6.774  1.00 15.30           C  
ANISOU  572  CG  LEU A  66     2741   1750   1321   -154    -55   -227       C  
ATOM    573  CD1 LEU A  66      12.537  20.350   5.402  1.00 18.35           C  
ANISOU  573  CD1 LEU A  66     3504   2222   1243    237    176   -322       C  
ATOM    574  CD2 LEU A  66      11.985  19.456   7.724  1.00 16.38           C  
ANISOU  574  CD2 LEU A  66     3215   1401   1606   -194   -255    110       C  
ATOM    575  N   GLY A  67      13.158  23.202  10.390  1.00 12.92           N  
ANISOU  575  N   GLY A  67     2526   1371   1011    -93    -16    138       N  
ATOM    576  CA  GLY A  67      14.002  24.131  11.108  1.00 14.12           C  
ANISOU  576  CA  GLY A  67     2445   1456   1463    111    -40    146       C  
ATOM    577  C   GLY A  67      13.357  25.047  12.096  1.00 12.69           C  
ANISOU  577  C   GLY A  67     2389   1349   1084     41    -90    167       C  
ATOM    578  O   GLY A  67      14.055  25.788  12.797  1.00 14.01           O  
ANISOU  578  O   GLY A  67     2478   1540   1305   -133    -86     63       O  
ATOM    579  N   GLN A  68      12.038  25.008  12.159  1.00 12.13           N  
ANISOU  579  N   GLN A  68     2396   1113   1098      0   -161     13       N  
ATOM    580  CA  GLN A  68      11.239  25.961  12.914  1.00 13.38           C  
ANISOU  580  CA  GLN A  68     2442   1216   1426     16   -101   -115       C  
ATOM    581  C   GLN A  68      10.514  25.283  14.059  1.00 13.59           C  
ANISOU  581  C   GLN A  68     2539   1464   1160     20    -93    -15       C  
ATOM    582  O   GLN A  68       9.577  24.468  13.856  1.00 13.65           O  
ANISOU  582  O   GLN A  68     2495   1388   1302    -41    -15    -96       O  
ATOM    583  CB  GLN A  68      10.254  26.686  11.987  1.00 13.60           C  
ANISOU  583  CB  GLN A  68     2705   1118   1343    -34   -151   -203       C  
ATOM    584  CG  GLN A  68      11.015  27.367  10.832  1.00 16.16           C  
ANISOU  584  CG  GLN A  68     3050   1539   1549    -32   -434    -22       C  
ATOM    585  CD  GLN A  68      10.336  28.371  10.052  1.00 18.22           C  
ANISOU  585  CD  GLN A  68     2969   1659   2293   -245   -589     62       C  
ATOM    586  OE1 GLN A  68       9.146  28.654  10.262  1.00 21.56           O  
ANISOU  586  OE1 GLN A  68     3331   1722   3137    126  -1064    249       O  
ATOM    587  NE2 GLN A  68      11.088  28.937   9.079  1.00 17.88           N  
ANISOU  587  NE2 GLN A  68     3217   1602   1973   -261   -562    196       N  
ATOM    588  N   GLU A  69      10.893  25.624  15.274  1.00 12.79           N  
ANISOU  588  N   GLU A  69     2434   1328   1096   -118     16    -63       N  
ATOM    589  CA  GLU A  69      10.403  24.979  16.511  1.00 13.65           C  
ANISOU  589  CA  GLU A  69     2478   1523   1184   -123   -102    164       C  
ATOM    590  C   GLU A  69       8.907  25.151  16.647  1.00 12.79           C  
ANISOU  590  C   GLU A  69     2547   1483    828    -61      7   -101       C  
ATOM    591  O   GLU A  69       8.360  26.224  16.306  1.00 13.43           O  
ANISOU  591  O   GLU A  69     2655   1178   1269    129     18    -74       O  
ATOM    592  CB  GLU A  69      11.127  25.540  17.724  1.00 16.84           C  
ANISOU  592  CB  GLU A  69     2750   2342   1303   -245   -213    373       C  
ATOM    593  CG  GLU A  69      10.819  25.006  19.065  1.00 21.11           C  
ANISOU  593  CG  GLU A  69     3828   2539   1651   -178   -174    251       C  
ATOM    594  CD  GLU A  69      11.592  25.719  20.096  1.00 31.71           C  
ANISOU  594  CD  GLU A  69     5253   4460   2333   -472   -648    -88       C  
ATOM    595  OE1 GLU A  69      11.400  26.991  20.220  1.00 36.86           O  
ANISOU  595  OE1 GLU A  69     5580   5435   2990   -754  -1074   -766       O  
ATOM    596  OE2 GLU A  69      12.387  24.962  20.705  1.00 34.59           O  
ANISOU  596  OE2 GLU A  69     5013   5897   2232  -1005   -319    366       O  
ATOM    597  N   PHE A  70       8.251  24.141  17.213  1.00 12.30           N  
ANISOU  597  N   PHE A  70     2541   1315    815     14     82    -92       N  
ATOM    598  CA  PHE A  70       6.833  24.158  17.438  1.00 12.05           C  
ANISOU  598  CA  PHE A  70     2466   1318    792    184    118   -116       C  
ATOM    599  C   PHE A  70       6.524  23.409  18.747  1.00 12.96           C  
ANISOU  599  C   PHE A  70     2518   1366   1040    204    -21   -250       C  
ATOM    600  O   PHE A  70       7.335  22.605  19.218  1.00 13.80           O  
ANISOU  600  O   PHE A  70     2564   1666   1012    344     91    -50       O  
ATOM    601  CB  PHE A  70       6.097  23.555  16.248  1.00 12.53           C  
ANISOU  601  CB  PHE A  70     2424   1450    887    134    110   -176       C  
ATOM    602  CG  PHE A  70       6.422  22.151  15.909  1.00 12.67           C  
ANISOU  602  CG  PHE A  70     2517   1417    877     -1     30    -83       C  
ATOM    603  CD1 PHE A  70       7.533  21.815  15.124  1.00 12.41           C  
ANISOU  603  CD1 PHE A  70     2410   1449    856    -40     63    -46       C  
ATOM    604  CD2 PHE A  70       5.627  21.102  16.335  1.00 14.61           C  
ANISOU  604  CD2 PHE A  70     2567   1753   1229   -184    323   -353       C  
ATOM    605  CE1 PHE A  70       7.815  20.521  14.773  1.00 11.97           C  
ANISOU  605  CE1 PHE A  70     2234   1449    861     95     64   -159       C  
ATOM    606  CE2 PHE A  70       5.923  19.795  16.006  1.00 15.15           C  
ANISOU  606  CE2 PHE A  70     2974   1473   1308   -388    356     -9       C  
ATOM    607  CZ  PHE A  70       7.010  19.498  15.225  1.00 14.28           C  
ANISOU  607  CZ  PHE A  70     2949   1546    930     -5    178   -193       C  
ATOM    608  N   ASP A  71       5.296  23.625  19.250  1.00 13.80           N  
ANISOU  608  N   ASP A  71     2631   1350   1264    323     91    167       N  
ATOM    609  CA  ASP A  71       4.795  22.889  20.426  1.00 14.70           C  
ANISOU  609  CA  ASP A  71     2941   1549   1091    270    251     74       C  
ATOM    610  C   ASP A  71       4.085  21.654  19.975  1.00 14.23           C  
ANISOU  610  C   ASP A  71     2986   1537    882     26    148     75       C  
ATOM    611  O   ASP A  71       3.391  21.627  18.941  1.00 16.79           O  
ANISOU  611  O   ASP A  71     2931   1834   1612    223      2    480       O  
ATOM    612  CB  ASP A  71       3.742  23.723  21.121  1.00 16.78           C  
ANISOU  612  CB  ASP A  71     3166   1734   1476    404    250     14       C  
ATOM    613  CG  ASP A  71       4.257  24.909  21.725  1.00 19.31           C  
ANISOU  613  CG  ASP A  71     3343   2533   1459    421    -15   -323       C  
ATOM    614  OD1 ASP A  71       5.241  24.756  22.486  1.00 20.23           O  
ANISOU  614  OD1 ASP A  71     3557   2286   1841    295   -203   -201       O  
ATOM    615  OD2 ASP A  71       3.669  26.004  21.501  1.00 19.09           O  
ANISOU  615  OD2 ASP A  71     3221   2342   1690    171   -312   -296       O  
ATOM    616  N   GLU A  72       4.336  20.557  20.680  1.00 14.59           N  
ANISOU  616  N   GLU A  72     2880   1625   1036    126    235    300       N  
ATOM    617  CA  GLU A  72       3.777  19.239  20.366  1.00 15.83           C  
ANISOU  617  CA  GLU A  72     2821   1912   1278    142    216    428       C  
ATOM    618  C   GLU A  72       3.290  18.556  21.630  1.00 15.04           C  
ANISOU  618  C   GLU A  72     2695   1778   1241    218    129    391       C  
ATOM    619  O   GLU A  72       3.989  18.591  22.634  1.00 18.10           O  
ANISOU  619  O   GLU A  72     2945   2557   1373     32    210    513       O  
ATOM    620  CB  GLU A  72       4.861  18.388  19.643  1.00 15.37           C  
ANISOU  620  CB  GLU A  72     2872   1722   1244     33    392    348       C  
ATOM    621  CG  GLU A  72       4.440  16.974  19.340  1.00 16.95           C  
ANISOU  621  CG  GLU A  72     3374   1924   1140    180    164    395       C  
ATOM    622  CD  GLU A  72       5.433  16.146  18.612  1.00 15.24           C  
ANISOU  622  CD  GLU A  72     3292   1674    821     50    397    227       C  
ATOM    623  OE1 GLU A  72       6.604  16.532  18.544  1.00 16.22           O  
ANISOU  623  OE1 GLU A  72     2991   1829   1340    -47    119   -104       O  
ATOM    624  OE2 GLU A  72       5.069  15.012  18.166  1.00 18.70           O  
ANISOU  624  OE2 GLU A  72     3506   1644   1951     25    398   -127       O  
ATOM    625  N   VAL A  73       2.057  18.041  21.601  1.00 15.47           N  
ANISOU  625  N   VAL A  73     2700   1911   1264    161     46    499       N  
ATOM    626  CA  VAL A  73       1.607  17.148  22.701  1.00 16.17           C  
ANISOU  626  CA  VAL A  73     2734   1940   1469    230    202    413       C  
ATOM    627  C   VAL A  73       1.692  15.731  22.119  1.00 15.54           C  
ANISOU  627  C   VAL A  73     2599   1981   1324    111     47    368       C  
ATOM    628  O   VAL A  73       0.977  15.390  21.193  1.00 16.62           O  
ANISOU  628  O   VAL A  73     2931   2024   1360     89    -40    354       O  
ATOM    629  CB  VAL A  73       0.220  17.506  23.149  1.00 18.07           C  
ANISOU  629  CB  VAL A  73     3031   2229   1602    248    403    319       C  
ATOM    630  CG1 VAL A  73      -0.197  16.569  24.259  1.00 21.42           C  
ANISOU  630  CG1 VAL A  73     3527   2501   2112    -24    640    472       C  
ATOM    631  CG2 VAL A  73       0.179  18.978  23.666  1.00 20.56           C  
ANISOU  631  CG2 VAL A  73     3041   2318   2452    379    666     38       C  
ATOM    632  N   THR A  74       2.607  14.914  22.625  1.00 15.10           N  
ANISOU  632  N   THR A  74     2634   2065   1038     99     -5    268       N  
ATOM    633  CA  THR A  74       2.886  13.624  22.112  1.00 15.34           C  
ANISOU  633  CA  THR A  74     2599   1984   1242    -50    186    222       C  
ATOM    634  C   THR A  74       1.753  12.640  22.438  1.00 17.00           C  
ANISOU  634  C   THR A  74     2865   2052   1542    -53    140    344       C  
ATOM    635  O   THR A  74       0.911  12.896  23.276  1.00 17.13           O  
ANISOU  635  O   THR A  74     3163   1905   1438    -31    334    395       O  
ATOM    636  CB  THR A  74       4.246  13.086  22.610  1.00 14.87           C  
ANISOU  636  CB  THR A  74     2593   1914   1142    -64    268      6       C  
ATOM    637  OG1 THR A  74       4.119  12.859  24.008  1.00 16.17           O  
ANISOU  637  OG1 THR A  74     2929   2321    894    191    249    292       O  
ATOM    638  CG2 THR A  74       5.375  14.042  22.357  1.00 15.30           C  
ANISOU  638  CG2 THR A  74     2558   1855   1400     80    316    181       C  
ATOM    639  N   ALA A  75       1.770  11.497  21.754  1.00 16.84           N  
ANISOU  639  N   ALA A  75     2845   2006   1547   -133    278    258       N  
ATOM    640  CA  ALA A  75       0.744  10.441  21.921  1.00 17.91           C  
ANISOU  640  CA  ALA A  75     2803   2282   1717   -202    120    309       C  
ATOM    641  C   ALA A  75       0.657  10.030  23.384  1.00 19.20           C  
ANISOU  641  C   ALA A  75     2925   2453   1914   -119    208    298       C  
ATOM    642  O   ALA A  75      -0.436   9.784  23.863  1.00 20.90           O  
ANISOU  642  O   ALA A  75     3198   2624   2118   -522    178    315       O  
ATOM    643  CB  ALA A  75       1.003   9.251  21.019  1.00 18.01           C  
ANISOU  643  CB  ALA A  75     3119   1925   1799   -298     94    178       C  
ATOM    644  N   ASP A  76       1.805   9.994  24.067  1.00 18.62           N  
ANISOU  644  N   ASP A  76     3124   2243   1707    -62    240    611       N  
ATOM    645  CA  ASP A  76       1.863   9.639  25.486  1.00 18.91           C  
ANISOU  645  CA  ASP A  76     3151   2489   1542   -152    145    591       C  
ATOM    646  C   ASP A  76       1.644  10.829  26.425  1.00 18.83           C  
ANISOU  646  C   ASP A  76     3234   2525   1394   -175    432    665       C  
ATOM    647  O   ASP A  76       1.755  10.695  27.624  1.00 22.29           O  
ANISOU  647  O   ASP A  76     3933   3274   1261    -51    382    535       O  
ATOM    648  CB  ASP A  76       3.168   8.939  25.758  1.00 19.59           C  
ANISOU  648  CB  ASP A  76     3304   2440   1697   -123    102    380       C  
ATOM    649  CG  ASP A  76       4.380   9.814  25.528  1.00 19.08           C  
ANISOU  649  CG  ASP A  76     3236   2297   1714    198    -52    407       C  
ATOM    650  OD1 ASP A  76       4.552  10.219  24.355  1.00 19.12           O  
ANISOU  650  OD1 ASP A  76     3857   2077   1328    -33     35    616       O  
ATOM    651  OD2 ASP A  76       5.173  10.031  26.466  1.00 19.27           O  
ANISOU  651  OD2 ASP A  76     3967   1833   1522    -96     97    607       O  
ATOM    652  N   ASP A  77       1.237  11.972  25.905  1.00 19.64           N  
ANISOU  652  N   ASP A  77     3342   2474   1643   -219    488    656       N  
ATOM    653  CA  ASP A  77       0.845  13.186  26.636  1.00 21.15           C  
ANISOU  653  CA  ASP A  77     3429   2877   1727   -208    594    513       C  
ATOM    654  C   ASP A  77       1.993  13.998  27.243  1.00 20.51           C  
ANISOU  654  C   ASP A  77     3338   2743   1711   -132    594    536       C  
ATOM    655  O   ASP A  77       1.792  14.686  28.254  1.00 24.00           O  
ANISOU  655  O   ASP A  77     3620   3597   1899    -92    718   -220       O  
ATOM    656  CB  ASP A  77      -0.288  12.888  27.639  1.00 23.18           C  
ANISOU  656  CB  ASP A  77     3606   3130   2069   -215    588    563       C  
ATOM    657  CG  ASP A  77      -1.118  14.115  27.971  1.00 29.04           C  
ANISOU  657  CG  ASP A  77     4141   4141   2749     19    974    464       C  
ATOM    658  OD1 ASP A  77      -1.646  14.142  29.108  1.00 34.77           O  
ANISOU  658  OD1 ASP A  77     4833   4917   3461     80   1588    115       O  
ATOM    659  OD2 ASP A  77      -1.291  15.016  27.108  1.00 34.55           O  
ANISOU  659  OD2 ASP A  77     4640   4432   4052    -57   1193    940       O  
ATOM    660  N   ARG A  78       3.206  13.935  26.696  1.00 17.76           N  
ANISOU  660  N   ARG A  78     3209   2288   1247    -24    567    375       N  
ATOM    661  CA  ARG A  78       4.216  14.907  26.983  1.00 17.10           C  
ANISOU  661  CA  ARG A  78     3221   2165   1108     44    276    432       C  
ATOM    662  C   ARG A  78       3.981  16.166  26.202  1.00 15.60           C  
ANISOU  662  C   ARG A  78     3101   1847    980    103    419    240       C  
ATOM    663  O   ARG A  78       3.642  16.140  25.052  1.00 17.98           O  
ANISOU  663  O   ARG A  78     3634   2022   1175    127    270    283       O  
ATOM    664  CB  ARG A  78       5.643  14.422  26.735  1.00 16.33           C  
ANISOU  664  CB  ARG A  78     3332   1781   1091    127    325    284       C  
ATOM    665  CG  ARG A  78       6.193  13.326  27.620  1.00 17.27           C  
ANISOU  665  CG  ARG A  78     3192   2041   1326    118    236    582       C  
ATOM    666  CD  ARG A  78       7.487  12.724  27.118  1.00 17.16           C  
ANISOU  666  CD  ARG A  78     3255   1915   1349    119     91    246       C  
ATOM    667  NE  ARG A  78       7.201  11.913  25.946  1.00 17.17           N  
ANISOU  667  NE  ARG A  78     3064   1998   1460    123    -55    350       N  
ATOM    668  CZ  ARG A  78       7.775  11.972  24.743  1.00 17.20           C  
ANISOU  668  CZ  ARG A  78     3084   1937   1511     66     79    -10       C  
ATOM    669  NH1 ARG A  78       8.835  12.738  24.524  1.00 16.47           N  
ANISOU  669  NH1 ARG A  78     3084   1863   1311   -105     -2     29       N  
ATOM    670  NH2 ARG A  78       7.304  11.188  23.775  1.00 17.67           N  
ANISOU  670  NH2 ARG A  78     3234   1877   1600     18     -7    -83       N  
ATOM    671  N   LYS A  79       4.234  17.302  26.858  1.00 16.61           N  
ANISOU  671  N   LYS A  79     3359   1998    953    153    252      9       N  
ATOM    672  CA  LYS A  79       4.205  18.625  26.225  1.00 16.79           C  
ANISOU  672  CA  LYS A  79     2991   2011   1375    281    160     25       C  
ATOM    673  C   LYS A  79       5.647  18.972  25.915  1.00 15.94           C  
ANISOU  673  C   LYS A  79     2987   1889   1180    265     85    -16       C  
ATOM    674  O   LYS A  79       6.452  19.227  26.815  1.00 18.67           O  
ANISOU  674  O   LYS A  79     3741   2379    971    304    286    -51       O  
ATOM    675  CB  LYS A  79       3.564  19.657  27.153  1.00 18.50           C  
ANISOU  675  CB  LYS A  79     3273   1950   1806    409    285    105       C  
ATOM    676  CG  LYS A  79       2.087  19.483  27.270  1.00 25.09           C  
ANISOU  676  CG  LYS A  79     3863   3059   2609    532    190   -482       C  
ATOM    677  CD  LYS A  79       1.650  18.233  27.910  1.00 32.24           C  
ANISOU  677  CD  LYS A  79     4692   3938   3618    357    306     11       C  
ATOM    678  CE  LYS A  79       0.326  18.376  28.657  1.00 34.76           C  
ANISOU  678  CE  LYS A  79     4772   4412   4024    155    324    336       C  
ATOM    679  NZ  LYS A  79      -0.588  17.207  28.382  1.00 33.57           N  
ANISOU  679  NZ  LYS A  79     5449   3818   3487     33    195    492       N  
ATOM    680  N   VAL A  80       6.001  18.941  24.628  1.00 14.90           N  
ANISOU  680  N   VAL A  80     3088   1781    792    194    190     32       N  
ATOM    681  CA  VAL A  80       7.400  19.062  24.262  1.00 14.55           C  
ANISOU  681  CA  VAL A  80     2961   1785    779    153     89     28       C  
ATOM    682  C   VAL A  80       7.562  20.234  23.255  1.00 14.07           C  
ANISOU  682  C   VAL A  80     2923   1612    809    166     45   -220       C  
ATOM    683  O   VAL A  80       6.575  20.693  22.669  1.00 15.76           O  
ANISOU  683  O   VAL A  80     2971   1762   1252    117    166     44       O  
ATOM    684  CB  VAL A  80       7.916  17.735  23.621  1.00 14.75           C  
ANISOU  684  CB  VAL A  80     2917   1561   1123    157    201     -2       C  
ATOM    685  CG1 VAL A  80       7.616  16.526  24.524  1.00 15.76           C  
ANISOU  685  CG1 VAL A  80     3593   1397    997    218    301    236       C  
ATOM    686  CG2 VAL A  80       7.333  17.474  22.196  1.00 15.70           C  
ANISOU  686  CG2 VAL A  80     3631   1592    740     61     75    -28       C  
ATOM    687  N   LYS A  81       8.803  20.649  23.140  1.00 13.96           N  
ANISOU  687  N   LYS A  81     3133   1409    761    120    105      4       N  
ATOM    688  CA  LYS A  81       9.180  21.607  22.121  1.00 14.18           C  
ANISOU  688  CA  LYS A  81     3092   1389    907    273     11    -11       C  
ATOM    689  C   LYS A  81       9.960  20.810  21.093  1.00 13.29           C  
ANISOU  689  C   LYS A  81     2743   1485    822    190    100    -83       C  
ATOM    690  O   LYS A  81      10.994  20.217  21.414  1.00 14.51           O  
ANISOU  690  O   LYS A  81     3034   1738    739    361   -148   -112       O  
ATOM    691  CB  LYS A  81      10.062  22.695  22.743  1.00 16.86           C  
ANISOU  691  CB  LYS A  81     3357   1543   1502     79    164     -4       C  
ATOM    692  CG  LYS A  81       9.469  23.581  23.752  1.00 24.26           C  
ANISOU  692  CG  LYS A  81     4019   2556   2641    -20    284   -420       C  
ATOM    693  CD  LYS A  81       8.502  24.541  23.216  1.00 28.57           C  
ANISOU  693  CD  LYS A  81     4574   3478   2800    319     21   -504       C  
ATOM    694  CE  LYS A  81       8.106  25.509  24.345  1.00 31.34           C  
ANISOU  694  CE  LYS A  81     5000   3715   3192    295   -688   -940       C  
ATOM    695  NZ  LYS A  81       6.948  26.388  24.015  1.00 33.72           N  
ANISOU  695  NZ  LYS A  81     5675   3768   3369    388  -1391   -837       N  
ATOM    696  N   SER A  82       9.498  20.889  19.846  1.00 13.20           N  
ANISOU  696  N   SER A  82     2918   1426    669    277    111    105       N  
ATOM    697  CA  SER A  82      10.020  20.044  18.776  1.00 12.80           C  
ANISOU  697  CA  SER A  82     2759   1286    818    174     75    262       C  
ATOM    698  C   SER A  82      10.576  20.852  17.645  1.00 12.59           C  
ANISOU  698  C   SER A  82     2582   1262    937    250    -89    388       C  
ATOM    699  O   SER A  82      10.106  21.905  17.301  1.00 12.54           O  
ANISOU  699  O   SER A  82     2645   1209    911    111      3    100       O  
ATOM    700  CB  SER A  82       8.876  19.189  18.236  1.00 14.04           C  
ANISOU  700  CB  SER A  82     2844   1606    884    183    111    209       C  
ATOM    701  OG  SER A  82       8.513  18.226  19.197  1.00 15.79           O  
ANISOU  701  OG  SER A  82     3253   1574   1169    184    279    401       O  
ATOM    702  N   THR A  83      11.679  20.321  17.070  1.00 12.49           N  
ANISOU  702  N   THR A  83     2462   1312    971    260     30    183       N  
ATOM    703  CA  THR A  83      12.244  20.904  15.853  1.00 12.50           C  
ANISOU  703  CA  THR A  83     2671   1364    714     30    -63    137       C  
ATOM    704  C   THR A  83      12.526  19.745  14.933  1.00 12.64           C  
ANISOU  704  C   THR A  83     2732   1340    728    119     -6    168       C  
ATOM    705  O   THR A  83      13.157  18.769  15.334  1.00 13.72           O  
ANISOU  705  O   THR A  83     3057   1516    637    199   -114     29       O  
ATOM    706  CB  THR A  83      13.531  21.674  16.138  1.00 13.50           C  
ANISOU  706  CB  THR A  83     2697   1281   1150     55    -65     67       C  
ATOM    707  OG1 THR A  83      13.319  22.596  17.212  1.00 15.80           O  
ANISOU  707  OG1 THR A  83     3090   1535   1378   -205    -96   -277       O  
ATOM    708  CG2 THR A  83      13.961  22.432  14.889  1.00 15.78           C  
ANISOU  708  CG2 THR A  83     2961   1700   1332   -119    173     80       C  
ATOM    709  N   ILE A  84      12.097  19.846  13.681  1.00 12.18           N  
ANISOU  709  N   ILE A  84     2647   1222    757    109    -26      0       N  
ATOM    710  CA  ILE A  84      12.303  18.832  12.694  1.00 11.96           C  
ANISOU  710  CA  ILE A  84     2409   1382    750    133    181    138       C  
ATOM    711  C   ILE A  84      13.080  19.417  11.540  1.00 12.63           C  
ANISOU  711  C   ILE A  84     2778   1180    841     98     95    140       C  
ATOM    712  O   ILE A  84      12.798  20.509  11.026  1.00 13.38           O  
ANISOU  712  O   ILE A  84     2912   1291    879     18     71     80       O  
ATOM    713  CB  ILE A  84      10.969  18.227  12.178  1.00 12.92           C  
ANISOU  713  CB  ILE A  84     2704   1349    853    183     12     94       C  
ATOM    714  CG1 ILE A  84      10.207  17.600  13.363  1.00 12.94           C  
ANISOU  714  CG1 ILE A  84     2578   1484    854    215     55    333       C  
ATOM    715  CG2 ILE A  84      11.262  17.134  11.112  1.00 14.23           C  
ANISOU  715  CG2 ILE A  84     2994   1497    914    125    186     56       C  
ATOM    716  CD1 ILE A  84       8.849  17.064  13.052  1.00 13.03           C  
ANISOU  716  CD1 ILE A  84     2262   1553   1137     19      3      0       C  
ATOM    717  N   THR A  85      14.190  18.758  11.185  1.00 12.87           N  
ANISOU  717  N   THR A  85     2774   1356    759    172    233    250       N  
ATOM    718  CA  THR A  85      15.061  19.170  10.112  1.00 13.67           C  
ANISOU  718  CA  THR A  85     2860   1233   1098    108    150     90       C  
ATOM    719  C   THR A  85      15.323  18.003   9.205  1.00 13.86           C  
ANISOU  719  C   THR A  85     2876   1356   1034    -67    271    242       C  
ATOM    720  O   THR A  85      15.017  16.857   9.514  1.00 14.48           O  
ANISOU  720  O   THR A  85     3238   1385    878    111    448    136       O  
ATOM    721  CB  THR A  85      16.406  19.688  10.686  1.00 15.41           C  
ANISOU  721  CB  THR A  85     2858   1325   1672     -4    229     81       C  
ATOM    722  OG1 THR A  85      16.997  18.658  11.488  1.00 17.90           O  
ANISOU  722  OG1 THR A  85     3418   1818   1566    341    -15   -127       O  
ATOM    723  CG2 THR A  85      16.166  20.971  11.427  1.00 16.52           C  
ANISOU  723  CG2 THR A  85     2918   1558   1799    -83   -126   -426       C  
ATOM    724  N   LEU A  86      15.893  18.273   8.047  1.00 15.66           N  
ANISOU  724  N   LEU A  86     3419   1294   1235   -168    548    105       N  
ATOM    725  CA  LEU A  86      16.471  17.214   7.191  1.00 17.66           C  
ANISOU  725  CA  LEU A  86     3518   1648   1542   -309    524   -111       C  
ATOM    726  C   LEU A  86      18.003  17.155   7.362  1.00 20.08           C  
ANISOU  726  C   LEU A  86     3414   2006   2207   -373    641   -157       C  
ATOM    727  O   LEU A  86      18.713  18.218   7.380  1.00 24.64           O  
ANISOU  727  O   LEU A  86     3796   2245   3320   -545    801   -278       O  
ATOM    728  CB  LEU A  86      16.201  17.435   5.728  1.00 20.25           C  
ANISOU  728  CB  LEU A  86     4084   2215   1395   -262    680     12       C  
ATOM    729  CG  LEU A  86      14.835  17.048   5.271  1.00 21.23           C  
ANISOU  729  CG  LEU A  86     3876   2337   1851    -42    515    780       C  
ATOM    730  CD1 LEU A  86      14.529  17.611   3.890  1.00 22.56           C  
ANISOU  730  CD1 LEU A  86     4628   2646   1297    301    597    235       C  
ATOM    731  CD2 LEU A  86      14.695  15.489   5.210  1.00 19.19           C  
ANISOU  731  CD2 LEU A  86     3710   2084   1494    -39    200    149       C  
ATOM    732  N   ASP A  87      18.515  15.957   7.567  1.00 19.11           N  
ANISOU  732  N   ASP A  87     3180   2088   1991   -451    708   -427       N  
ATOM    733  CA  ASP A  87      19.966  15.691   7.670  1.00 20.92           C  
ANISOU  733  CA  ASP A  87     3182   2640   2124   -535    447   -364       C  
ATOM    734  C   ASP A  87      20.213  14.736   6.546  1.00 18.77           C  
ANISOU  734  C   ASP A  87     3144   2439   1547   -346    426   -450       C  
ATOM    735  O   ASP A  87      19.947  13.567   6.700  1.00 20.20           O  
ANISOU  735  O   ASP A  87     3062   2596   2014   -510    243   -197       O  
ATOM    736  CB  ASP A  87      20.374  15.088   9.047  1.00 24.25           C  
ANISOU  736  CB  ASP A  87     3491   3188   2535   -490    375   -121       C  
ATOM    737  CG  ASP A  87      21.880  14.707   9.144  1.00 29.35           C  
ANISOU  737  CG  ASP A  87     4073   3989   3087   -268    166    269       C  
ATOM    738  OD1 ASP A  87      22.696  15.179   8.330  1.00 36.35           O  
ANISOU  738  OD1 ASP A  87     4250   5685   3875    -53    394    142       O  
ATOM    739  OD2 ASP A  87      22.250  13.905  10.053  1.00 38.36           O  
ANISOU  739  OD2 ASP A  87     5091   5535   3947    188    284    698       O  
ATOM    740  N   GLY A  88      20.655  15.230   5.393  1.00 19.90           N  
ANISOU  740  N   GLY A  88     3418   2283   1861   -341    369   -269       N  
ATOM    741  CA  GLY A  88      20.987  14.342   4.335  1.00 22.09           C  
ANISOU  741  CA  GLY A  88     3527   2817   2049   -299    480   -251       C  
ATOM    742  C   GLY A  88      19.903  13.379   4.001  1.00 24.30           C  
ANISOU  742  C   GLY A  88     3820   3621   1792   -263    418   -155       C  
ATOM    743  O   GLY A  88      20.070  12.150   3.955  1.00 26.28           O  
ANISOU  743  O   GLY A  88     4606   3229   2149   -522    558    -64       O  
ATOM    744  N   GLY A  89      18.753  13.847   3.758  1.00 22.81           N  
ANISOU  744  N   GLY A  89     3478   4245    945   -334    414     79       N  
ATOM    745  CA  GLY A  89      17.719  12.774   3.459  1.00 21.76           C  
ANISOU  745  CA  GLY A  89     3729   3675    863   -394    230   -284       C  
ATOM    746  C   GLY A  89      16.960  12.092   4.630  1.00 19.62           C  
ANISOU  746  C   GLY A  89     3217   3281    957   -451    408   -362       C  
ATOM    747  O   GLY A  89      15.959  11.419   4.408  1.00 22.39           O  
ANISOU  747  O   GLY A  89     3456   3785   1265   -697    193   -771       O  
ATOM    748  N   VAL A  90      17.377  12.305   5.865  1.00 17.30           N  
ANISOU  748  N   VAL A  90     3090   2556    925   -379    282   -372       N  
ATOM    749  CA  VAL A  90      16.746  11.755   7.085  1.00 15.96           C  
ANISOU  749  CA  VAL A  90     2809   1851   1403   -147    383   -203       C  
ATOM    750  C   VAL A  90      15.998  12.889   7.747  1.00 13.29           C  
ANISOU  750  C   VAL A  90     2588   1585    873   -137    -15   -106       C  
ATOM    751  O   VAL A  90      16.576  13.985   7.961  1.00 14.60           O  
ANISOU  751  O   VAL A  90     2999   1607    940   -272    158    -63       O  
ATOM    752  CB  VAL A  90      17.813  11.210   8.023  1.00 16.95           C  
ANISOU  752  CB  VAL A  90     3055   1737   1648   -109    345   -131       C  
ATOM    753  CG1 VAL A  90      17.225  10.710   9.317  1.00 16.76           C  
ANISOU  753  CG1 VAL A  90     2953   1849   1564      9    426     26       C  
ATOM    754  CG2 VAL A  90      18.651  10.105   7.394  1.00 19.34           C  
ANISOU  754  CG2 VAL A  90     2915   2120   2314    337    478   -125       C  
ATOM    755  N   LEU A  91      14.710  12.686   8.013  1.00 13.60           N  
ANISOU  755  N   LEU A  91     2688   1581    895   -149    -23    -48       N  
ATOM    756  CA  LEU A  91      13.965  13.663   8.818  1.00 13.02           C  
ANISOU  756  CA  LEU A  91     2662   1427    855    -45    155    289       C  
ATOM    757  C   LEU A  91      14.343  13.420  10.275  1.00 13.04           C  
ANISOU  757  C   LEU A  91     2681   1365    907    114    244    215       C  
ATOM    758  O   LEU A  91      14.197  12.322  10.804  1.00 13.11           O  
ANISOU  758  O   LEU A  91     2916   1316    748     12    188     83       O  
ATOM    759  CB  LEU A  91      12.467  13.501   8.632  1.00 15.82           C  
ANISOU  759  CB  LEU A  91     3017   1893   1101   -391    182    416       C  
ATOM    760  CG  LEU A  91      11.847  14.100   7.400  1.00 17.27           C  
ANISOU  760  CG  LEU A  91     3315   2259    988   -103     42    126       C  
ATOM    761  CD1 LEU A  91      10.463  13.561   7.285  1.00 20.16           C  
ANISOU  761  CD1 LEU A  91     3137   2684   1837   -333   -187      2       C  
ATOM    762  CD2 LEU A  91      11.840  15.646   7.616  1.00 16.95           C  
ANISOU  762  CD2 LEU A  91     3351   1157   1932    262     85    407       C  
ATOM    763  N   VAL A  92      14.874  14.443  10.944  1.00 12.67           N  
ANISOU  763  N   VAL A  92     2753   1252    807     95    245    158       N  
ATOM    764  CA  VAL A  92      15.309  14.364  12.344  1.00 12.43           C  
ANISOU  764  CA  VAL A  92     2742   1342    636    155    211    230       C  
ATOM    765  C   VAL A  92      14.436  15.216  13.193  1.00 12.80           C  
ANISOU  765  C   VAL A  92     2756   1260    848    256    118     54       C  
ATOM    766  O   VAL A  92      14.373  16.453  13.011  1.00 14.47           O  
ANISOU  766  O   VAL A  92     3164   1357    974    226    306    136       O  
ATOM    767  CB  VAL A  92      16.788  14.817  12.419  1.00 13.88           C  
ANISOU  767  CB  VAL A  92     2735   1684    854    239     85     -3       C  
ATOM    768  CG1 VAL A  92      17.301  14.786  13.857  1.00 15.97           C  
ANISOU  768  CG1 VAL A  92     2887   2272    906    -41    -32    -62       C  
ATOM    769  CG2 VAL A  92      17.724  14.033  11.505  1.00 15.89           C  
ANISOU  769  CG2 VAL A  92     2975   1831   1229    138    238   -126       C  
ATOM    770  N   HIS A  93      13.754  14.571  14.142  1.00 12.83           N  
ANISOU  770  N   HIS A  93     2751   1304    817    207     98    167       N  
ATOM    771  CA  HIS A  93      12.737  15.209  14.989  1.00 12.67           C  
ANISOU  771  CA  HIS A  93     2674   1325    813    236    271    260       C  
ATOM    772  C   HIS A  93      13.204  15.158  16.398  1.00 12.50           C  
ANISOU  772  C   HIS A  93     2849   1219    681    241    219    180       C  
ATOM    773  O   HIS A  93      13.276  14.094  16.997  1.00 13.84           O  
ANISOU  773  O   HIS A  93     3278   1223    755     56     45    136       O  
ATOM    774  CB  HIS A  93      11.434  14.402  14.792  1.00 13.59           C  
ANISOU  774  CB  HIS A  93     2790   1552    818    268    181    146       C  
ATOM    775  CG  HIS A  93      10.220  14.836  15.529  1.00 13.23           C  
ANISOU  775  CG  HIS A  93     2457   1825    741    124    144    490       C  
ATOM    776  ND1 HIS A  93       9.035  14.168  15.357  1.00 15.69           N  
ANISOU  776  ND1 HIS A  93     2513   1950   1499    167    152    641       N  
ATOM    777  CD2 HIS A  93       9.994  15.775  16.504  1.00 14.80           C  
ANISOU  777  CD2 HIS A  93     3122   1809    691    600    180    109       C  
ATOM    778  CE1 HIS A  93       8.108  14.715  16.114  1.00 17.31           C  
ANISOU  778  CE1 HIS A  93     2471   2426   1678    399    491    882       C  
ATOM    779  NE2 HIS A  93       8.657  15.696  16.810  1.00 17.31           N  
ANISOU  779  NE2 HIS A  93     3188   2113   1276    586    394    549       N  
ATOM    780  N   VAL A  94      13.602  16.313  16.942  1.00 12.35           N  
ANISOU  780  N   VAL A  94     2608   1223    861    184     33    136       N  
ATOM    781  CA  VAL A  94      14.097  16.418  18.316  1.00 12.57           C  
ANISOU  781  CA  VAL A  94     2513   1373    889    166     87    131       C  
ATOM    782  C   VAL A  94      12.996  16.995  19.187  1.00 12.64           C  
ANISOU  782  C   VAL A  94     2465   1342    992    135     30    214       C  
ATOM    783  O   VAL A  94      12.446  18.041  18.863  1.00 14.78           O  
ANISOU  783  O   VAL A  94     3185   1551    881    495    223    106       O  
ATOM    784  CB  VAL A  94      15.399  17.263  18.380  1.00 14.40           C  
ANISOU  784  CB  VAL A  94     2672   1555   1241    153     41    143       C  
ATOM    785  CG1 VAL A  94      15.926  17.301  19.784  1.00 18.22           C  
ANISOU  785  CG1 VAL A  94     3007   2523   1390    -31   -384    -58       C  
ATOM    786  CG2 VAL A  94      16.421  16.732  17.405  1.00 17.47           C  
ANISOU  786  CG2 VAL A  94     3084   2323   1231    112    201   -175       C  
ATOM    787  N   GLN A  95      12.724  16.322  20.295  1.00 12.98           N  
ANISOU  787  N   GLN A  95     2889   1257    785    146    -25     33       N  
ATOM    788  CA  GLN A  95      11.728  16.747  21.294  1.00 13.50           C  
ANISOU  788  CA  GLN A  95     2832   1469    826     72    125    -77       C  
ATOM    789  C   GLN A  95      12.449  17.068  22.607  1.00 13.78           C  
ANISOU  789  C   GLN A  95     2976   1591    668    287     19   -132       C  
ATOM    790  O   GLN A  95      13.201  16.230  23.126  1.00 14.94           O  
ANISOU  790  O   GLN A  95     3331   1517    827    217    -55    -92       O  
ATOM    791  CB  GLN A  95      10.724  15.608  21.542  1.00 13.19           C  
ANISOU  791  CB  GLN A  95     3079   1269    662    167    111    -28       C  
ATOM    792  CG  GLN A  95       9.936  15.202  20.349  1.00 14.26           C  
ANISOU  792  CG  GLN A  95     3029   1650    738    115     31     62       C  
ATOM    793  CD  GLN A  95       8.968  14.057  20.544  1.00 14.42           C  
ANISOU  793  CD  GLN A  95     2931   1471   1074      2    214    247       C  
ATOM    794  OE1 GLN A  95       7.921  13.927  19.823  1.00 17.48           O  
ANISOU  794  OE1 GLN A  95     2920   2190   1528     53    -15    292       O  
ATOM    795  NE2 GLN A  95       9.266  13.208  21.468  1.00 14.36           N  
ANISOU  795  NE2 GLN A  95     3159   1355    942   -148   -135    221       N  
ATOM    796  N   LYS A  96      12.161  18.229  23.144  1.00 14.38           N  
ANISOU  796  N   LYS A  96     3207   1508    747    118    -75      2       N  
ATOM    797  CA  LYS A  96      12.738  18.708  24.432  1.00 15.04           C  
ANISOU  797  CA  LYS A  96     3256   1595    863    341    -88   -130       C  
ATOM    798  C   LYS A  96      11.613  18.963  25.418  1.00 15.35           C  
ANISOU  798  C   LYS A  96     3441   1629    760    301      1   -182       C  
ATOM    799  O   LYS A  96      10.582  19.588  25.144  1.00 16.28           O  
ANISOU  799  O   LYS A  96     3678   1626    879    344     17   -125       O  
ATOM    800  CB  LYS A  96      13.439  20.052  24.214  1.00 17.32           C  
ANISOU  800  CB  LYS A  96     3328   2096   1155     46   -240   -225       C  
ATOM    801  CG  LYS A  96      14.499  20.063  23.169  1.00 20.37           C  
ANISOU  801  CG  LYS A  96     3779   2198   1760    213    -74    -14       C  
ATOM    802  CD  LYS A  96      15.698  19.203  23.442  1.00 20.58           C  
ANISOU  802  CD  LYS A  96     3757   2123   1939    -51   -135   -110       C  
ATOM    803  CE  LYS A  96      16.881  19.510  22.563  1.00 23.34           C  
ANISOU  803  CE  LYS A  96     3472   2618   2778   -357   -130   -338       C  
ATOM    804  NZ  LYS A  96      18.053  18.643  22.789  1.00 25.69           N  
ANISOU  804  NZ  LYS A  96     3992   2106   3662   -601   -281    -82       N  
ATOM    805  N   TRP A  97      11.815  18.431  26.625  1.00 16.30           N  
ANISOU  805  N   TRP A  97     3672   1606    916    297     -8   -141       N  
ATOM    806  CA  TRP A  97      10.846  18.632  27.727  1.00 17.71           C  
ANISOU  806  CA  TRP A  97     3810   2034    885    275    -37     26       C  
ATOM    807  C   TRP A  97      11.498  18.309  29.047  1.00 19.15           C  
ANISOU  807  C   TRP A  97     4239   2214    823    429    -61   -131       C  
ATOM    808  O   TRP A  97      12.314  17.398  29.115  1.00 19.96           O  
ANISOU  808  O   TRP A  97     4486   2337    758    502   -239    -18       O  
ATOM    809  CB  TRP A  97       9.551  17.775  27.542  1.00 17.91           C  
ANISOU  809  CB  TRP A  97     3967   2004    832    277     72     21       C  
ATOM    810  CG  TRP A  97       9.731  16.343  27.918  1.00 16.90           C  
ANISOU  810  CG  TRP A  97     3786   1722    911    187    183    -76       C  
ATOM    811  CD1 TRP A  97       9.245  15.748  29.050  1.00 18.84           C  
ANISOU  811  CD1 TRP A  97     4255   2034    868    375    273     53       C  
ATOM    812  CD2 TRP A  97      10.525  15.339  27.255  1.00 16.32           C  
ANISOU  812  CD2 TRP A  97     3587   1711    900    -34    -80    -53       C  
ATOM    813  NE1 TRP A  97       9.629  14.469  29.103  1.00 17.70           N  
ANISOU  813  NE1 TRP A  97     3976   1814    932    190    314     79       N  
ATOM    814  CE2 TRP A  97      10.420  14.180  28.025  1.00 16.85           C  
ANISOU  814  CE2 TRP A  97     3866   1714    819    -91    -99     56       C  
ATOM    815  CE3 TRP A  97      11.235  15.272  26.078  1.00 16.98           C  
ANISOU  815  CE3 TRP A  97     3795   1697    960   -133    249   -144       C  
ATOM    816  CZ2 TRP A  97      11.092  13.003  27.702  1.00 17.37           C  
ANISOU  816  CZ2 TRP A  97     3845   1869    883   -260    -44    186       C  
ATOM    817  CZ3 TRP A  97      11.887  14.141  25.760  1.00 16.72           C  
ANISOU  817  CZ3 TRP A  97     3631   1842    876   -140    168     89       C  
ATOM    818  CH2 TRP A  97      11.802  13.019  26.551  1.00 17.31           C  
ANISOU  818  CH2 TRP A  97     3580   1826   1171   -203     -4   -322       C  
ATOM    819  N   ASP A  98      11.230  19.123  30.060  1.00 20.18           N  
ANISOU  819  N   ASP A  98     4533   2462    670    391    -71   -443       N  
ATOM    820  CA  ASP A  98      11.641  18.764  31.446  1.00 23.27           C  
ANISOU  820  CA  ASP A  98     4721   2891   1227    268   -234   -439       C  
ATOM    821  C   ASP A  98      13.155  18.543  31.520  1.00 22.79           C  
ANISOU  821  C   ASP A  98     4604   2797   1256    227   -324   -536       C  
ATOM    822  O   ASP A  98      13.671  17.691  32.287  1.00 25.77           O  
ANISOU  822  O   ASP A  98     5246   3477   1068    343   -444   -334       O  
ATOM    823  CB  ASP A  98      10.937  17.471  31.908  1.00 25.34           C  
ANISOU  823  CB  ASP A  98     4962   3206   1459    258   -268   -173       C  
ATOM    824  CG  ASP A  98      10.948  17.272  33.401  1.00 31.81           C  
ANISOU  824  CG  ASP A  98     5673   4193   2220    205   -530   -157       C  
ATOM    825  OD1 ASP A  98      10.960  18.282  34.103  1.00 37.41           O  
ANISOU  825  OD1 ASP A  98     7066   5095   2051    274   -225   -640       O  
ATOM    826  OD2 ASP A  98      10.914  16.109  33.879  1.00 38.96           O  
ANISOU  826  OD2 ASP A  98     7093   4902   2808    112   -382    438       O  
ATOM    827  N   GLY A  99      13.901  19.301  30.733  1.00 22.70           N  
ANISOU  827  N   GLY A  99     4526   2681   1416    278   -331   -609       N  
ATOM    828  CA  GLY A  99      15.333  19.131  30.709  1.00 22.38           C  
ANISOU  828  CA  GLY A  99     4241   2710   1549    -13   -521   -640       C  
ATOM    829  C   GLY A  99      15.848  17.863  30.018  1.00 21.56           C  
ANISOU  829  C   GLY A  99     4046   2632   1511     70   -609   -526       C  
ATOM    830  O   GLY A  99      17.078  17.616  30.030  1.00 25.52           O  
ANISOU  830  O   GLY A  99     4243   3163   2287    107   -859   -950       O  
ATOM    831  N   LYS A 100      14.980  17.122  29.309  1.00 19.95           N  
ANISOU  831  N   LYS A 100     3932   2373   1273    -21   -483   -354       N  
ATOM    832  CA  LYS A 100      15.270  15.851  28.632  1.00 18.70           C  
ANISOU  832  CA  LYS A 100     3712   2192   1198     72   -488   -278       C  
ATOM    833  C   LYS A 100      15.168  16.090  27.127  1.00 17.35           C  
ANISOU  833  C   LYS A 100     3535   1965   1089    141   -483   -118       C  
ATOM    834  O   LYS A 100      14.593  17.071  26.670  1.00 17.35           O  
ANISOU  834  O   LYS A 100     4004   1613    973    179   -304    -89       O  
ATOM    835  CB  LYS A 100      14.256  14.799  29.031  1.00 18.07           C  
ANISOU  835  CB  LYS A 100     3881   1972   1011    167   -612   -250       C  
ATOM    836  CG  LYS A 100      14.269  14.470  30.548  1.00 23.93           C  
ANISOU  836  CG  LYS A 100     4344   3186   1562   -203   -460   -208       C  
ATOM    837  CD  LYS A 100      12.992  13.692  30.965  1.00 27.58           C  
ANISOU  837  CD  LYS A 100     4490   4190   1796   -349   -622    189       C  
ATOM    838  CE  LYS A 100      12.810  13.331  32.429  1.00 32.69           C  
ANISOU  838  CE  LYS A 100     5131   4760   2529   -483   -315    207       C  
ATOM    839  NZ  LYS A 100      11.397  12.816  32.694  1.00 36.81           N  
ANISOU  839  NZ  LYS A 100     5483   5878   2622   -533   -241   1024       N  
ATOM    840  N   SER A 101      15.662  15.132  26.346  1.00 16.31           N  
ANISOU  840  N   SER A 101     3436   1618   1143    115   -297   -131       N  
ATOM    841  CA  SER A 101      15.612  15.211  24.884  1.00 15.15           C  
ANISOU  841  CA  SER A 101     3027   1766    961    -38   -285   -101       C  
ATOM    842  C   SER A 101      15.528  13.820  24.360  1.00 14.79           C  
ANISOU  842  C   SER A 101     3030   1517   1070    120   -235      8       C  
ATOM    843  O   SER A 101      16.193  12.910  24.848  1.00 15.74           O  
ANISOU  843  O   SER A 101     3169   1642   1168     97   -409     26       O  
ATOM    844  CB  SER A 101      16.932  15.826  24.414  1.00 16.72           C  
ANISOU  844  CB  SER A 101     3220   1799   1333   -205   -230   -251       C  
ATOM    845  OG  SER A 101      16.938  16.036  23.049  1.00 18.83           O  
ANISOU  845  OG  SER A 101     3651   2010   1494   -238    -54    -71       O  
ATOM    846  N   THR A 102      14.752  13.653  23.287  1.00 13.08           N  
ANISOU  846  N   THR A 102     2717   1362    889     36   -334    -91       N  
ATOM    847  CA  THR A 102      14.724  12.432  22.516  1.00 12.48           C  
ANISOU  847  CA  THR A 102     2605   1251    883    166    -51    -27       C  
ATOM    848  C   THR A 102      14.678  12.811  21.057  1.00 12.16           C  
ANISOU  848  C   THR A 102     2599   1309    713    154   -110      7       C  
ATOM    849  O   THR A 102      14.186  13.879  20.687  1.00 13.68           O  
ANISOU  849  O   THR A 102     3087   1277    833    226    -76     36       O  
ATOM    850  CB  THR A 102      13.528  11.597  22.924  1.00 13.53           C  
ANISOU  850  CB  THR A 102     2696   1368   1077      2      3   -333       C  
ATOM    851  OG1 THR A 102      13.608  10.280  22.343  1.00 14.31           O  
ANISOU  851  OG1 THR A 102     3030   1316   1087    -30     29     55       O  
ATOM    852  CG2 THR A 102      12.168  12.170  22.636  1.00 14.56           C  
ANISOU  852  CG2 THR A 102     2929   1529   1072    219    -43    -31       C  
ATOM    853  N   THR A 103      15.177  11.895  20.215  1.00 12.43           N  
ANISOU  853  N   THR A 103     2743   1086    894    251   -108    -36       N  
ATOM    854  CA  THR A 103      15.212  12.106  18.756  1.00 13.13           C  
ANISOU  854  CA  THR A 103     2960   1365    662    265    -59     -4       C  
ATOM    855  C   THR A 103      14.557  10.946  18.057  1.00 13.61           C  
ANISOU  855  C   THR A 103     3244   1265    660    251   -115     -9       C  
ATOM    856  O   THR A 103      14.829   9.804  18.336  1.00 15.34           O  
ANISOU  856  O   THR A 103     3676   1265    888    277   -366    137       O  
ATOM    857  CB  THR A 103      16.678  12.272  18.329  1.00 14.89           C  
ANISOU  857  CB  THR A 103     3208   1422   1026    253     67     13       C  
ATOM    858  OG1 THR A 103      17.269  13.413  18.972  1.00 18.59           O  
ANISOU  858  OG1 THR A 103     3433   2080   1549   -178    178     67       O  
ATOM    859  CG2 THR A 103      16.794  12.502  16.854  1.00 17.69           C  
ANISOU  859  CG2 THR A 103     3786   1824   1109     31     63    226       C  
ATOM    860  N   ILE A 104      13.734  11.292  17.103  1.00 13.12           N  
ANISOU  860  N   ILE A 104     3102   1148    732     99   -120    101       N  
ATOM    861  CA  ILE A 104      13.053  10.353  16.226  1.00 12.03           C  
ANISOU  861  CA  ILE A 104     2910   1015    643    105     55     71       C  
ATOM    862  C   ILE A 104      13.531  10.656  14.829  1.00 12.10           C  
ANISOU  862  C   ILE A 104     2953   1102    540    129    -73    234       C  
ATOM    863  O   ILE A 104      13.375  11.736  14.327  1.00 13.42           O  
ANISOU  863  O   ILE A 104     3150   1288    661    235    144    109       O  
ATOM    864  CB  ILE A 104      11.521  10.525  16.267  1.00 13.40           C  
ANISOU  864  CB  ILE A 104     3052   1416    623    152     86    160       C  
ATOM    865  CG1 ILE A 104      11.038  10.331  17.709  1.00 14.74           C  
ANISOU  865  CG1 ILE A 104     3106   1565    927    102    165     -2       C  
ATOM    866  CG2 ILE A 104      10.811   9.564  15.293  1.00 16.42           C  
ANISOU  866  CG2 ILE A 104     3468   1736   1033    -71    -94     48       C  
ATOM    867  CD1 ILE A 104       9.591  10.697  17.816  1.00 18.94           C  
ANISOU  867  CD1 ILE A 104     3427   2522   1244    -23    438    -89       C  
ATOM    868  N   LYS A 105      14.187   9.669  14.217  1.00 12.24           N  
ANISOU  868  N   LYS A 105     2765   1232    651     79    -37    211       N  
ATOM    869  CA  LYS A 105      14.650   9.766  12.843  1.00 11.47           C  
ANISOU  869  CA  LYS A 105     2454   1277    625     25   -161     85       C  
ATOM    870  C   LYS A 105      13.803   8.963  11.916  1.00 13.00           C  
ANISOU  870  C   LYS A 105     2577   1530    830   -109     65     80       C  
ATOM    871  O   LYS A 105      13.423   7.837  12.267  1.00 14.27           O  
ANISOU  871  O   LYS A 105     3249   1477    696   -210   -126     77       O  
ATOM    872  CB  LYS A 105      16.116   9.322  12.748  1.00 13.53           C  
ANISOU  872  CB  LYS A 105     2419   1941    779    -16    -68    226       C  
ATOM    873  CG  LYS A 105      17.114  10.284  13.466  1.00 18.52           C  
ANISOU  873  CG  LYS A 105     2590   2798   1648    138   -589    -84       C  
ATOM    874  CD  LYS A 105      18.585   9.945  13.250  1.00 23.59           C  
ANISOU  874  CD  LYS A 105     2934   3679   2348   -241   -421    258       C  
ATOM    875  CE  LYS A 105      19.511  10.844  14.058  1.00 29.15           C  
ANISOU  875  CE  LYS A 105     3227   3917   3930   -207   -749     83       C  
ATOM    876  NZ  LYS A 105      20.979  10.611  13.803  1.00 33.91           N  
ANISOU  876  NZ  LYS A 105     3691   4318   4873    -34   -604     84       N  
ATOM    877  N   ARG A 106      13.500   9.522  10.756  1.00 12.37           N  
ANISOU  877  N   ARG A 106     2682   1337    677    -69    -23    143       N  
ATOM    878  CA  ARG A 106      12.697   8.829   9.747  1.00 12.48           C  
ANISOU  878  CA  ARG A 106     2620   1465    656   -191     98     43       C  
ATOM    879  C   ARG A 106      13.456   8.800   8.435  1.00 12.34           C  
ANISOU  879  C   ARG A 106     2699   1366    620   -130    -17      0       C  
ATOM    880  O   ARG A 106      13.925   9.858   7.992  1.00 13.47           O  
ANISOU  880  O   ARG A 106     3056   1320    739   -185    110    -15       O  
ATOM    881  CB  ARG A 106      11.327   9.492   9.610  1.00 14.39           C  
ANISOU  881  CB  ARG A 106     2755   1857    854   -298    -84     71       C  
ATOM    882  CG  ARG A 106      10.566   9.496  10.905  1.00 14.36           C  
ANISOU  882  CG  ARG A 106     2515   1999    940   -176    228     71       C  
ATOM    883  CD  ARG A 106       9.241  10.179  10.791  1.00 18.72           C  
ANISOU  883  CD  ARG A 106     2883   3294    933   -332    199   -104       C  
ATOM    884  NE  ARG A 106       8.407  10.127  12.006  1.00 20.20           N  
ANISOU  884  NE  ARG A 106     3091   3204   1380   -250    362    -81       N  
ATOM    885  CZ  ARG A 106       8.297  11.035  12.938  1.00 18.61           C  
ANISOU  885  CZ  ARG A 106     2834   3029   1206   -121     70    592       C  
ATOM    886  NH1 ARG A 106       9.081  12.081  13.015  1.00 17.34           N  
ANISOU  886  NH1 ARG A 106     2683   2344   1560    148    342    360       N  
ATOM    887  NH2 ARG A 106       7.429  10.804  13.906  1.00 22.54           N  
ANISOU  887  NH2 ARG A 106     3706   3514   1341    -45    703    350       N  
ATOM    888  N   LYS A 107      13.590   7.627   7.844  1.00 13.26           N  
ANISOU  888  N   LYS A 107     2961   1261    815    -97    161   -108       N  
ATOM    889  CA  LYS A 107      14.427   7.438   6.636  1.00 14.71           C  
ANISOU  889  CA  LYS A 107     3063   1599    926   -104    147   -116       C  
ATOM    890  C   LYS A 107      13.792   6.424   5.720  1.00 14.27           C  
ANISOU  890  C   LYS A 107     2938   1630    852   -329    132    -35       C  
ATOM    891  O   LYS A 107      13.260   5.406   6.156  1.00 16.49           O  
ANISOU  891  O   LYS A 107     3724   1846    693   -500    176     -7       O  
ATOM    892  CB  LYS A 107      15.874   7.004   6.983  1.00 16.95           C  
ANISOU  892  CB  LYS A 107     3284   2195    960   -163     45   -336       C  
ATOM    893  CG  LYS A 107      16.922   7.061   5.873  1.00 20.85           C  
ANISOU  893  CG  LYS A 107     3686   2865   1370   -159     24   -503       C  
ATOM    894  CD  LYS A 107      18.249   6.516   6.368  1.00 23.39           C  
ANISOU  894  CD  LYS A 107     3772   3221   1895     -6    -17   -570       C  
ATOM    895  CE  LYS A 107      19.257   6.317   5.370  1.00 33.10           C  
ANISOU  895  CE  LYS A 107     4631   4548   3395     61    297   -488       C  
ATOM    896  NZ  LYS A 107      19.909   7.568   5.193  1.00 34.25           N  
ANISOU  896  NZ  LYS A 107     5326   4343   3343   -241    414   -597       N  
ATOM    897  N   ARG A 108      13.829   6.682   4.435  1.00 13.89           N  
ANISOU  897  N   ARG A 108     2763   1843    671   -238    220    137       N  
ATOM    898  CA  ARG A 108      13.416   5.671   3.438  1.00 14.40           C  
ANISOU  898  CA  ARG A 108     2768   2023    677    -78    176     74       C  
ATOM    899  C   ARG A 108      14.501   4.647   3.281  1.00 15.32           C  
ANISOU  899  C   ARG A 108     2706   2156    956   -108     90   -353       C  
ATOM    900  O   ARG A 108      15.693   4.971   3.081  1.00 17.19           O  
ANISOU  900  O   ARG A 108     2901   2059   1570   -185    197   -504       O  
ATOM    901  CB  ARG A 108      13.115   6.310   2.113  1.00 16.52           C  
ANISOU  901  CB  ARG A 108     3026   2416    834   -208    132     54       C  
ATOM    902  CG  ARG A 108      11.825   6.999   2.133  1.00 18.30           C  
ANISOU  902  CG  ARG A 108     3075   2748   1127    -70    -75    569       C  
ATOM    903  CD  ARG A 108      10.583   6.037   2.119  1.00 21.48           C  
ANISOU  903  CD  ARG A 108     3114   3557   1488   -239    102    886       C  
ATOM    904  NE  ARG A 108      10.725   4.976   1.072  1.00 23.72           N  
ANISOU  904  NE  ARG A 108     3290   3109   2612   -304    -87    421       N  
ATOM    905  CZ  ARG A 108      10.446   5.155  -0.210  1.00 21.43           C  
ANISOU  905  CZ  ARG A 108     3198   1903   3038   -191   -358   -115       C  
ATOM    906  NH1 ARG A 108       9.875   6.259  -0.644  1.00 21.89           N  
ANISOU  906  NH1 ARG A 108     3671   2423   2222     -9   -384     90       N  
ATOM    907  NH2 ARG A 108      10.661   4.163  -1.060  1.00 25.49           N  
ANISOU  907  NH2 ARG A 108     3707   2726   3252    -24   -437   -406       N  
ATOM    908  N   GLU A 109      14.096   3.364   3.295  1.00 15.02           N  
ANISOU  908  N   GLU A 109     2846   1852   1007    -89    170   -320       N  
ATOM    909  CA  GLU A 109      15.007   2.249   3.072  1.00 16.56           C  
ANISOU  909  CA  GLU A 109     3002   2120   1169      0    315   -232       C  
ATOM    910  C   GLU A 109      14.269   1.256   2.213  1.00 15.20           C  
ANISOU  910  C   GLU A 109     2948   1753   1071    -31    213   -201       C  
ATOM    911  O   GLU A 109      13.253   0.717   2.621  1.00 16.06           O  
ANISOU  911  O   GLU A 109     3284   1896    920   -251    231   -103       O  
ATOM    912  CB  GLU A 109      15.379   1.526   4.343  1.00 17.59           C  
ANISOU  912  CB  GLU A 109     3280   2093   1309     92    162   -184       C  
ATOM    913  CG  GLU A 109      16.130   2.390   5.322  1.00 21.59           C  
ANISOU  913  CG  GLU A 109     3631   2743   1828     76    -61   -374       C  
ATOM    914  CD  GLU A 109      17.562   2.643   4.968  1.00 26.72           C  
ANISOU  914  CD  GLU A 109     4241   3319   2593   -292    195   -421       C  
ATOM    915  OE1 GLU A 109      18.223   3.431   5.669  1.00 31.72           O  
ANISOU  915  OE1 GLU A 109     4850   4042   3159   -208    -66   -685       O  
ATOM    916  OE2 GLU A 109      18.050   2.038   4.003  1.00 32.36           O  
ANISOU  916  OE2 GLU A 109     5174   3924   3196     44    305   -824       O  
ATOM    917  N   ASP A 110      14.674   1.092   0.961  1.00 14.78           N  
ANISOU  917  N   ASP A 110     3006   1804    803    100    125    -90       N  
ATOM    918  CA  ASP A 110      13.910   0.274   0.011  1.00 14.99           C  
ANISOU  918  CA  ASP A 110     3094   1787    814    -41    213     13       C  
ATOM    919  C   ASP A 110      12.515   0.815  -0.057  1.00 13.99           C  
ANISOU  919  C   ASP A 110     2804   1990    522   -161     85   -171       C  
ATOM    920  O   ASP A 110      12.380   2.074  -0.171  1.00 15.25           O  
ANISOU  920  O   ASP A 110     3165   1725    904    -34    167    -20       O  
ATOM    921  CB  ASP A 110      14.034  -1.217   0.297  1.00 15.46           C  
ANISOU  921  CB  ASP A 110     3324   1876    672    -21    390    -35       C  
ATOM    922  CG  ASP A 110      15.466  -1.675   0.269  1.00 18.56           C  
ANISOU  922  CG  ASP A 110     3442   2306   1301     41    341    267       C  
ATOM    923  OD1 ASP A 110      16.225  -1.258  -0.625  1.00 20.70           O  
ANISOU  923  OD1 ASP A 110     3733   2367   1763    208    490     33       O  
ATOM    924  OD2 ASP A 110      15.818  -2.521   1.135  1.00 27.84           O  
ANISOU  924  OD2 ASP A 110     4667   3307   2602    844    376   1073       O  
ATOM    925  N   ASP A 111      11.466   0.028  -0.018  1.00 15.14           N  
ANISOU  925  N   ASP A 111     2924   2118    711    -87     42   -287       N  
ATOM    926  CA  ASP A 111      10.099   0.509  -0.074  1.00 15.48           C  
ANISOU  926  CA  ASP A 111     2991   2155    736    -43     15   -280       C  
ATOM    927  C   ASP A 111       9.555   0.862   1.286  1.00 15.46           C  
ANISOU  927  C   ASP A 111     2963   1901   1009    -27     15   -390       C  
ATOM    928  O   ASP A 111       8.368   1.122   1.403  1.00 18.67           O  
ANISOU  928  O   ASP A 111     2934   2837   1323    115    -95   -763       O  
ATOM    929  CB  ASP A 111       9.243  -0.528  -0.821  1.00 16.52           C  
ANISOU  929  CB  ASP A 111     2972   2368    935     18    -72   -331       C  
ATOM    930  CG  ASP A 111       9.565  -0.575  -2.301  1.00 16.76           C  
ANISOU  930  CG  ASP A 111     3464   2106    797     23    160   -289       C  
ATOM    931  OD1 ASP A 111       9.827   0.483  -2.892  1.00 19.62           O  
ANISOU  931  OD1 ASP A 111     4203   2370    880   -262     21   -128       O  
ATOM    932  OD2 ASP A 111       9.551  -1.654  -2.847  1.00 20.17           O  
ANISOU  932  OD2 ASP A 111     4347   2283   1031      4    187   -590       O  
ATOM    933  N   LYS A 112      10.371   0.812   2.323  1.00 15.80           N  
ANISOU  933  N   LYS A 112     3155   1937    912     32    127    -60       N  
ATOM    934  CA  LYS A 112       9.911   1.040   3.695  1.00 14.42           C  
ANISOU  934  CA  LYS A 112     3122   1748    607    -95    210   -185       C  
ATOM    935  C   LYS A 112      10.277   2.430   4.143  1.00 14.18           C  
ANISOU  935  C   LYS A 112     2848   1753    785   -111    145   -153       C  
ATOM    936  O   LYS A 112      11.131   3.111   3.615  1.00 15.05           O  
ANISOU  936  O   LYS A 112     3068   1606   1043   -147    115    -45       O  
ATOM    937  CB  LYS A 112      10.543   0.027   4.606  1.00 16.86           C  
ANISOU  937  CB  LYS A 112     3630   1922    854     51    305    -11       C  
ATOM    938  CG  LYS A 112      10.221  -1.419   4.226  1.00 21.45           C  
ANISOU  938  CG  LYS A 112     4058   2360   1729    284    359   -441       C  
ATOM    939  CD  LYS A 112      10.996  -2.449   4.942  1.00 27.19           C  
ANISOU  939  CD  LYS A 112     4710   3159   2459    501    408   -648       C  
ATOM    940  CE  LYS A 112      10.588  -3.859   4.448  1.00 32.91           C  
ANISOU  940  CE  LYS A 112     5304   3727   3473    297    327   -554       C  
ATOM    941  NZ  LYS A 112      11.518  -4.906   4.935  1.00 39.71           N  
ANISOU  941  NZ  LYS A 112     6105   4480   4503    532    150   -171       N  
ATOM    942  N   LEU A 113       9.654   2.804   5.250  1.00 13.55           N  
ANISOU  942  N   LEU A 113     2858   1581    706    -82    101    -81       N  
ATOM    943  CA  LEU A 113       9.960   4.026   6.003  1.00 13.14           C  
ANISOU  943  CA  LEU A 113     2804   1577    610   -100    155    -79       C  
ATOM    944  C   LEU A 113      10.342   3.530   7.433  1.00 12.62           C  
ANISOU  944  C   LEU A 113     2458   1504    830   -279    282   -287       C  
ATOM    945  O   LEU A 113       9.523   2.915   8.088  1.00 14.09           O  
ANISOU  945  O   LEU A 113     2751   1661    940   -304    166    -56       O  
ATOM    946  CB  LEU A 113       8.752   4.950   5.990  1.00 14.61           C  
ANISOU  946  CB  LEU A 113     2816   1850    884   -141    214   -237       C  
ATOM    947  CG  LEU A 113       8.974   6.343   6.649  1.00 17.00           C  
ANISOU  947  CG  LEU A 113     2926   2171   1360    -36    134   -370       C  
ATOM    948  CD1 LEU A 113       7.777   7.218   6.305  1.00 19.63           C  
ANISOU  948  CD1 LEU A 113     3413   1896   2147    115    -99   -424       C  
ATOM    949  CD2 LEU A 113       9.189   6.423   8.015  1.00 21.33           C  
ANISOU  949  CD2 LEU A 113     3656   2701   1746   -116    525    277       C  
ATOM    950  N   VAL A 114      11.642   3.672   7.729  1.00 12.10           N  
ANISOU  950  N   VAL A 114     2524   1458    615   -193     72     98       N  
ATOM    951  CA  VAL A 114      12.186   3.183   8.978  1.00 13.22           C  
ANISOU  951  CA  VAL A 114     2692   1503    827   -216     79    208       C  
ATOM    952  C   VAL A 114      12.264   4.361   9.948  1.00 13.53           C  
ANISOU  952  C   VAL A 114     2779   1570    791   -335     77    192       C  
ATOM    953  O   VAL A 114      12.707   5.460   9.619  1.00 14.83           O  
ANISOU  953  O   VAL A 114     3267   1529    838   -352    194     26       O  
ATOM    954  CB  VAL A 114      13.557   2.576   8.774  1.00 15.11           C  
ANISOU  954  CB  VAL A 114     2913   1835    993   -102    -48    206       C  
ATOM    955  CG1 VAL A 114      14.110   2.065  10.104  1.00 16.77           C  
ANISOU  955  CG1 VAL A 114     3261   2152    956      4   -120    228       C  
ATOM    956  CG2 VAL A 114      13.415   1.426   7.749  1.00 17.28           C  
ANISOU  956  CG2 VAL A 114     3167   2014   1385     52    176   -208       C  
ATOM    957  N   VAL A 115      11.796   4.119  11.161  1.00 13.40           N  
ANISOU  957  N   VAL A 115     2877   1407    804   -301    104    188       N  
ATOM    958  CA  VAL A 115      11.734   5.104  12.247  1.00 13.50           C  
ANISOU  958  CA  VAL A 115     2863   1386    877   -311   -190     31       C  
ATOM    959  C   VAL A 115      12.580   4.658  13.389  1.00 12.98           C  
ANISOU  959  C   VAL A 115     2796   1384    750   -183   -134    183       C  
ATOM    960  O   VAL A 115      12.353   3.600  13.962  1.00 16.60           O  
ANISOU  960  O   VAL A 115     3518   1562   1226   -456   -371    452       O  
ATOM    961  CB  VAL A 115      10.256   5.369  12.645  1.00 14.50           C  
ANISOU  961  CB  VAL A 115     3103   1457    945   -412    -28    108       C  
ATOM    962  CG1 VAL A 115      10.193   6.474  13.703  1.00 17.00           C  
ANISOU  962  CG1 VAL A 115     3478   1974   1007   -199   -115   -203       C  
ATOM    963  CG2 VAL A 115       9.352   5.666  11.469  1.00 16.39           C  
ANISOU  963  CG2 VAL A 115     3059   1891   1275   -254   -186    106       C  
ATOM    964  N  AGLU A 116      13.630   5.417  13.695  0.50 13.51           N  
ANISOU  964  N  AGLU A 116     3016   1361    754   -132   -104    163       N  
ATOM    965  N  BGLU A 116      13.574   5.449  13.725  0.50 13.40           N  
ANISOU  965  N  BGLU A 116     3003   1390    697   -151    -52    113       N  
ATOM    966  CA AGLU A 116      14.564   5.116  14.811  0.50 13.77           C  
ANISOU  966  CA AGLU A 116     3051   1230    951    -29    -99    112       C  
ATOM    967  CA BGLU A 116      14.466   5.114  14.821  0.50 14.02           C  
ANISOU  967  CA BGLU A 116     2996   1314   1016    -11    -64     70       C  
ATOM    968  C  AGLU A 116      14.323   6.122  15.936  0.50 13.65           C  
ANISOU  968  C  AGLU A 116     3062   1300    823    -64   -202    113       C  
ATOM    969  C  BGLU A 116      14.278   6.125  15.933  0.50 13.81           C  
ANISOU  969  C  BGLU A 116     3054   1345    846    -58   -180     92       C  
ATOM    970  O  AGLU A 116      14.445   7.322  15.723  0.50 14.92           O  
ANISOU  970  O  AGLU A 116     3618   1258    790     -1    -57    164       O  
ATOM    971  O  BGLU A 116      14.387   7.324  15.712  0.50 14.88           O  
ANISOU  971  O  BGLU A 116     3628   1287    736      3    -65    158       O  
ATOM    972  CB AGLU A 116      16.046   5.230  14.383  0.50 15.87           C  
ANISOU  972  CB AGLU A 116     3089   1564   1374     79   -162    -40       C  
ATOM    973  CB BGLU A 116      15.907   5.186  14.379  0.50 16.15           C  
ANISOU  973  CB BGLU A 116     3014   1652   1467     46    -79   -121       C  
ATOM    974  CG AGLU A 116      17.124   4.952  15.448  0.50 17.81           C  
ANISOU  974  CG AGLU A 116     3409   1854   1502    100    -96     87       C  
ATOM    975  CG BGLU A 116      16.888   4.383  15.149  0.50 20.22           C  
ANISOU  975  CG BGLU A 116     3277   2307   2096    240     35    -16       C  
ATOM    976  CD AGLU A 116      18.518   5.482  15.153  0.50 21.20           C  
ANISOU  976  CD AGLU A 116     3425   2659   1970    244     81    217       C  
ATOM    977  CD BGLU A 116      18.253   4.329  14.465  0.50 22.51           C  
ANISOU  977  CD BGLU A 116     3018   2798   2734    227     19    -23       C  
ATOM    978  OE1AGLU A 116      18.698   6.711  15.034  0.50 21.16           O  
ANISOU  978  OE1AGLU A 116     3455   2438   2145   -114    135     91       O  
ATOM    979  OE1BGLU A 116      18.999   5.323  14.523  0.50 25.59           O  
ANISOU  979  OE1BGLU A 116     3393   3073   3256    140    -88   -406       O  
ATOM    980  OE2AGLU A 116      19.478   4.694  15.069  0.50 22.66           O  
ANISOU  980  OE2AGLU A 116     3203   3058   2349    210    278    868       O  
ATOM    981  OE2BGLU A 116      18.586   3.285  13.851  0.50 23.53           O  
ANISOU  981  OE2BGLU A 116     3432   3048   2458    201    251   -288       O  
ATOM    982  N   CYS A 117      13.917   5.630  17.107  1.00 13.19           N  
ANISOU  982  N   CYS A 117     3076   1159    775     66    -92    114       N  
ATOM    983  CA  CYS A 117      13.632   6.466  18.253  1.00 13.88           C  
ANISOU  983  CA  CYS A 117     3028   1232   1011     59   -202   -193       C  
ATOM    984  C   CYS A 117      14.746   6.251  19.243  1.00 13.49           C  
ANISOU  984  C   CYS A 117     2707   1357   1060     93   -192    -22       C  
ATOM    985  O   CYS A 117      14.949   5.145  19.692  1.00 13.95           O  
ANISOU  985  O   CYS A 117     3085   1186   1026     -2   -316     74       O  
ATOM    986  CB  CYS A 117      12.292   6.033  18.894  1.00 15.02           C  
ANISOU  986  CB  CYS A 117     2877   1902    925    334   -257   -303       C  
ATOM    987  SG  CYS A 117      10.915   5.947  17.687  1.00 19.57           S  
ANISOU  987  SG  CYS A 117     3341   3002   1091     89   -279    145       S  
ATOM    988  N   VAL A 118      15.345   7.328  19.681  1.00 12.90           N  
ANISOU  988  N   VAL A 118     2673   1283    942    143   -183     -9       N  
ATOM    989  CA  VAL A 118      16.539   7.267  20.508  1.00 13.92           C  
ANISOU  989  CA  VAL A 118     2607   1231   1450    113    -63   -158       C  
ATOM    990  C   VAL A 118      16.361   8.090  21.771  1.00 13.00           C  
ANISOU  990  C   VAL A 118     2481   1230   1228     42    -84    -26       C  
ATOM    991  O   VAL A 118      16.037   9.290  21.717  1.00 13.73           O  
ANISOU  991  O   VAL A 118     3049   1262    905    219   -115     12       O  
ATOM    992  CB  VAL A 118      17.830   7.720  19.759  1.00 16.45           C  
ANISOU  992  CB  VAL A 118     2850   1771   1626    -78     77   -235       C  
ATOM    993  CG1 VAL A 118      18.992   7.772  20.662  1.00 21.34           C  
ANISOU  993  CG1 VAL A 118     2894   2435   2776    -76     50     23       C  
ATOM    994  CG2 VAL A 118      18.130   6.839  18.557  1.00 20.33           C  
ANISOU  994  CG2 VAL A 118     3590   2378   1756   -134    253   -612       C  
ATOM    995  N   MET A 119      16.601   7.472  22.924  1.00 13.90           N  
ANISOU  995  N   MET A 119     2857   1368   1054    245   -239     91       N  
ATOM    996  CA  MET A 119      16.598   8.203  24.214  1.00 15.57           C  
ANISOU  996  CA  MET A 119     2858   1663   1394    256   -230    -16       C  
ATOM    997  C   MET A 119      17.813   7.639  24.942  1.00 15.46           C  
ANISOU  997  C   MET A 119     2761   1809   1305    214   -185    -49       C  
ATOM    998  O   MET A 119      17.849   6.483  25.325  1.00 15.08           O  
ANISOU  998  O   MET A 119     2974   1596   1157    236   -297     12       O  
ATOM    999  CB  MET A 119      15.275   7.948  24.947  1.00 16.01           C  
ANISOU  999  CB  MET A 119     2908   1872   1301    470   -246   -171       C  
ATOM   1000  CG  MET A 119      15.208   8.457  26.380  1.00 18.49           C  
ANISOU 1000  CG  MET A 119     3162   2165   1698    409   -318   -167       C  
ATOM   1001  SD  MET A 119      15.000  10.181  26.274  1.00 22.65           S  
ANISOU 1001  SD  MET A 119     4775   2020   1811    555   -746   -367       S  
ATOM   1002  CE  MET A 119      15.004  10.800  27.966  1.00 20.96           C  
ANISOU 1002  CE  MET A 119     4326   1710   1926     -5   -258   -242       C  
ATOM   1003  N   LYS A 120      18.830   8.469  25.072  1.00 17.91           N  
ANISOU 1003  N   LYS A 120     3071   1967   1764    135   -262     98       N  
ATOM   1004  CA  LYS A 120      20.080   8.175  25.678  1.00 20.18           C  
ANISOU 1004  CA  LYS A 120     3026   2252   2389     20   -186    126       C  
ATOM   1005  C   LYS A 120      20.623   6.953  24.892  1.00 19.03           C  
ANISOU 1005  C   LYS A 120     2822   2170   2239     18   -224    279       C  
ATOM   1006  O   LYS A 120      20.715   6.961  23.649  1.00 20.66           O  
ANISOU 1006  O   LYS A 120     3031   2255   2561    151    -38    427       O  
ATOM   1007  CB  LYS A 120      19.885   8.004  27.221  1.00 19.52           C  
ANISOU 1007  CB  LYS A 120     3188   1846   2379     66   -253    243       C  
ATOM   1008  CG  LYS A 120      19.420   9.335  27.916  1.00 24.06           C  
ANISOU 1008  CG  LYS A 120     3717   2700   2724     79   -295    -94       C  
ATOM   1009  CD  LYS A 120      18.718   9.118  29.244  1.00 31.44           C  
ANISOU 1009  CD  LYS A 120     4656   3802   3486    162    -10   -107       C  
ATOM   1010  CE  LYS A 120      19.581   8.506  30.286  1.00 35.66           C  
ANISOU 1010  CE  LYS A 120     5151   4570   3826     87     17    222       C  
ATOM   1011  NZ  LYS A 120      18.716   7.859  31.345  1.00 37.28           N  
ANISOU 1011  NZ  LYS A 120     5831   5386   2945   -206   -142    402       N  
ATOM   1012  N   GLY A 121      20.926   5.899  25.589  1.00 19.36           N  
ANISOU 1012  N   GLY A 121     2817   2142   2394     42   -306    331       N  
ATOM   1013  CA  GLY A 121      21.457   4.705  24.975  1.00 18.38           C  
ANISOU 1013  CA  GLY A 121     2755   2074   2154    132   -141    306       C  
ATOM   1014  C   GLY A 121      20.437   3.728  24.431  1.00 15.02           C  
ANISOU 1014  C   GLY A 121     2363   1924   1419    125   -136    388       C  
ATOM   1015  O   GLY A 121      20.833   2.645  24.018  1.00 17.26           O  
ANISOU 1015  O   GLY A 121     2615   1944   1996    388    123    524       O  
ATOM   1016  N   VAL A 122      19.155   4.037  24.552  1.00 14.80           N  
ANISOU 1016  N   VAL A 122     2518   1751   1353     76   -121    315       N  
ATOM   1017  CA  VAL A 122      18.103   3.110  24.136  1.00 13.99           C  
ANISOU 1017  CA  VAL A 122     2474   1605   1235    101     10    384       C  
ATOM   1018  C   VAL A 122      17.549   3.523  22.805  1.00 13.66           C  
ANISOU 1018  C   VAL A 122     2563   1410   1215     80    -25    156       C  
ATOM   1019  O   VAL A 122      17.116   4.670  22.636  1.00 15.37           O  
ANISOU 1019  O   VAL A 122     3133   1422   1281    379   -308     63       O  
ATOM   1020  CB  VAL A 122      16.990   3.026  25.189  1.00 15.24           C  
ANISOU 1020  CB  VAL A 122     2473   1738   1577     97     91    288       C  
ATOM   1021  CG1 VAL A 122      15.936   2.103  24.742  1.00 17.68           C  
ANISOU 1021  CG1 VAL A 122     2578   1821   2316     70    171    446       C  
ATOM   1022  CG2 VAL A 122      17.574   2.613  26.564  1.00 17.78           C  
ANISOU 1022  CG2 VAL A 122     3123   2213   1418    350    101    483       C  
ATOM   1023  N   THR A 123      17.562   2.602  21.870  1.00 14.19           N  
ANISOU 1023  N   THR A 123     2654   1320   1416     35   -316     95       N  
ATOM   1024  CA  THR A 123      17.004   2.797  20.537  1.00 14.71           C  
ANISOU 1024  CA  THR A 123     2742   1518   1329      3   -132     25       C  
ATOM   1025  C   THR A 123      15.856   1.853  20.263  1.00 14.95           C  
ANISOU 1025  C   THR A 123     2939   1318   1420      0   -353   -129       C  
ATOM   1026  O   THR A 123      15.945   0.658  20.612  1.00 18.49           O  
ANISOU 1026  O   THR A 123     3415   1402   2206     83   -491    366       O  
ATOM   1027  CB  THR A 123      18.061   2.634  19.501  1.00 17.90           C  
ANISOU 1027  CB  THR A 123     3085   2093   1620    -18      6    -14       C  
ATOM   1028  OG1 THR A 123      19.108   3.535  19.755  1.00 20.98           O  
ANISOU 1028  OG1 THR A 123     3555   2629   1787    -31    380     -7       O  
ATOM   1029  CG2 THR A 123      17.506   2.850  18.052  1.00 18.13           C  
ANISOU 1029  CG2 THR A 123     3499   2306   1084    159     62    -28       C  
ATOM   1030  N   SER A 124      14.791   2.334  19.654  1.00 14.19           N  
ANISOU 1030  N   SER A 124     2836   1422   1133   -130   -233    325       N  
ATOM   1031  CA  SER A 124      13.779   1.487  19.102  1.00 14.59           C  
ANISOU 1031  CA  SER A 124     2847   1505   1191    -35   -278    535       C  
ATOM   1032  C   SER A 124      13.691   1.704  17.621  1.00 13.79           C  
ANISOU 1032  C   SER A 124     2802   1323   1114    235    -67    434       C  
ATOM   1033  O   SER A 124      13.729   2.827  17.142  1.00 15.33           O  
ANISOU 1033  O   SER A 124     3622   1399    802    -33   -147    288       O  
ATOM   1034  CB  SER A 124      12.426   1.794  19.733  1.00 15.04           C  
ANISOU 1034  CB  SER A 124     2859   1648   1205    -64   -245    483       C  
ATOM   1035  OG  SER A 124      11.341   1.151  19.124  1.00 15.94           O  
ANISOU 1035  OG  SER A 124     3099   1819   1139    -82    -72    232       O  
ATOM   1036  N   THR A 125      13.503   0.623  16.863  1.00 13.59           N  
ANISOU 1036  N   THR A 125     3124   1219    819     98    -56    294       N  
ATOM   1037  CA  THR A 125      13.348   0.686  15.434  1.00 13.43           C  
ANISOU 1037  CA  THR A 125     2659   1434   1008     46     92    486       C  
ATOM   1038  C   THR A 125      11.935   0.241  15.085  1.00 13.67           C  
ANISOU 1038  C   THR A 125     2737   1622    832   -220    -18    300       C  
ATOM   1039  O   THR A 125      11.532  -0.881  15.437  1.00 15.04           O  
ANISOU 1039  O   THR A 125     3075   1470   1169   -236   -137    206       O  
ATOM   1040  CB  THR A 125      14.375  -0.156  14.714  1.00 16.37           C  
ANISOU 1040  CB  THR A 125     2907   1854   1456    205    152    283       C  
ATOM   1041  OG1 THR A 125      15.681   0.296  15.063  1.00 19.30           O  
ANISOU 1041  OG1 THR A 125     3123   2293   1916    223    327    -16       O  
ATOM   1042  CG2 THR A 125      14.204  -0.089  13.191  1.00 19.29           C  
ANISOU 1042  CG2 THR A 125     3465   2653   1210     96    271    254       C  
ATOM   1043  N  AARG A 126      11.222   1.070  14.328  0.50 13.91           N  
ANISOU 1043  N  AARG A 126     2851   1622    811   -198     31    291       N  
ATOM   1044  N  BARG A 126      11.246   1.058  14.297  0.50 13.85           N  
ANISOU 1044  N  BARG A 126     2841   1617    804   -172     26    341       N  
ATOM   1045  CA AARG A 126       9.877   0.770  13.917  0.50 13.78           C  
ANISOU 1045  CA AARG A 126     2731   1688    815   -271     64    401       C  
ATOM   1046  CA BARG A 126       9.899   0.774  13.896  0.50 13.75           C  
ANISOU 1046  CA BARG A 126     2707   1644    870   -228     50    511       C  
ATOM   1047  C  AARG A 126       9.887   0.823  12.382  0.50 14.77           C  
ANISOU 1047  C  AARG A 126     2902   1806    902   -268      1    297       C  
ATOM   1048  C  BARG A 126       9.814   0.874  12.371  0.50 14.76           C  
ANISOU 1048  C  BARG A 126     2900   1784    921   -249     29    342       C  
ATOM   1049  O  AARG A 126      10.490   1.714  11.798  0.50 17.26           O  
ANISOU 1049  O  AARG A 126     3616   2070    871   -688   -114    129       O  
ATOM   1050  O  BARG A 126      10.221   1.867  11.788  0.50 16.25           O  
ANISOU 1050  O  BARG A 126     3616   1939    616   -603   -137    287       O  
ATOM   1051  CB AARG A 126       8.873   1.751  14.474  0.50 15.19           C  
ANISOU 1051  CB AARG A 126     2896   1984    890   -273    -14    173       C  
ATOM   1052  CB BARG A 126       8.923   1.717  14.542  0.50 15.35           C  
ANISOU 1052  CB BARG A 126     2864   1941   1026   -198    -46    324       C  
ATOM   1053  CG AARG A 126       9.128   2.091  15.926  0.50 15.04           C  
ANISOU 1053  CG AARG A 126     2672   2050    992   -377    183    -64       C  
ATOM   1054  CG BARG A 126       8.669   1.300  15.943  0.50 15.53           C  
ANISOU 1054  CG BARG A 126     2539   1992   1369   -106     20    382       C  
ATOM   1055  CD AARG A 126       7.890   2.644  16.588  0.50 19.72           C  
ANISOU 1055  CD AARG A 126     2789   2774   1928   -300    177   -282       C  
ATOM   1056  CD BARG A 126       8.224   2.364  16.843  0.50 16.18           C  
ANISOU 1056  CD BARG A 126     2369   2587   1189    -15    -73    318       C  
ATOM   1057  NE AARG A 126       7.121   1.545  17.162  0.50 18.73           N  
ANISOU 1057  NE AARG A 126     2630   2577   1907   -339    301   -608       N  
ATOM   1058  NE BARG A 126       6.786   2.668  16.734  0.50 15.73           N  
ANISOU 1058  NE BARG A 126     2064   2661   1251   -117    143    -95       N  
ATOM   1059  CZ AARG A 126       5.847   1.611  17.523  0.50 18.49           C  
ANISOU 1059  CZ AARG A 126     2577   2750   1698   -469   -114   -425       C  
ATOM   1060  CZ BARG A 126       5.796   1.976  17.299  0.50 15.83           C  
ANISOU 1060  CZ BARG A 126     2154   2518   1342   -376   -258    -78       C  
ATOM   1061  NH1AARG A 126       5.260   0.560  18.035  0.50 18.10           N  
ANISOU 1061  NH1AARG A 126     2408   2791   1678   -746   -205   -618       N  
ATOM   1062  NH1BARG A 126       6.039   0.825  17.907  0.50 15.94           N  
ANISOU 1062  NH1BARG A 126     2419   2504   1133   -391   -216     44       N  
ATOM   1063  NH2AARG A 126       5.170   2.717  17.385  0.50 18.13           N  
ANISOU 1063  NH2AARG A 126     2578   2564   1744   -580   -151     55       N  
ATOM   1064  NH2BARG A 126       4.551   2.407  17.212  0.50 16.41           N  
ANISOU 1064  NH2BARG A 126     2250   2512   1472   -756   -279   -392       N  
ATOM   1065  N   VAL A 127       9.206  -0.095  11.718  1.00 13.61           N  
ANISOU 1065  N   VAL A 127     2712   1649    808   -229    -13    269       N  
ATOM   1066  CA  VAL A 127       9.253  -0.162  10.286  1.00 13.45           C  
ANISOU 1066  CA  VAL A 127     2524   1746    837   -152    187     46       C  
ATOM   1067  C   VAL A 127       7.851  -0.027   9.790  1.00 12.65           C  
ANISOU 1067  C   VAL A 127     2459   1433    914   -161    200   -238       C  
ATOM   1068  O   VAL A 127       6.940  -0.738  10.173  1.00 13.76           O  
ANISOU 1068  O   VAL A 127     2622   1687    918   -298     68     10       O  
ATOM   1069  CB  VAL A 127       9.854  -1.487   9.824  1.00 14.96           C  
ANISOU 1069  CB  VAL A 127     2727   1962    995     85    122    285       C  
ATOM   1070  CG1 VAL A 127       9.876  -1.548   8.270  1.00 17.89           C  
ANISOU 1070  CG1 VAL A 127     3295   2474   1028    239     84    -31       C  
ATOM   1071  CG2 VAL A 127      11.249  -1.636  10.289  1.00 17.91           C  
ANISOU 1071  CG2 VAL A 127     2831   2438   1536    313    189     96       C  
ATOM   1072  N   TYR A 128       7.677   0.903   8.825  1.00 12.59           N  
ANISOU 1072  N   TYR A 128     2543   1345    894    -82     41     26       N  
ATOM   1073  CA  TYR A 128       6.410   1.119   8.156  1.00 13.01           C  
ANISOU 1073  CA  TYR A 128     2429   1491   1021   -141    124    -11       C  
ATOM   1074  C   TYR A 128       6.490   0.712   6.668  1.00 13.75           C  
ANISOU 1074  C   TYR A 128     2401   1561   1262    -23    -56    -85       C  
ATOM   1075  O   TYR A 128       7.561   0.887   6.080  1.00 14.14           O  
ANISOU 1075  O   TYR A 128     2713   1685    975   -152      2   -232       O  
ATOM   1076  CB  TYR A 128       5.977   2.585   8.216  1.00 13.04           C  
ANISOU 1076  CB  TYR A 128     2524   1588    842   -138      3     37       C  
ATOM   1077  CG  TYR A 128       5.573   3.117   9.580  1.00 13.25           C  
ANISOU 1077  CG  TYR A 128     2526   1506   1000   -205   -105     -6       C  
ATOM   1078  CD1 TYR A 128       6.519   3.404  10.554  1.00 14.32           C  
ANISOU 1078  CD1 TYR A 128     2390   1669   1380   -206   -124   -107       C  
ATOM   1079  CD2 TYR A 128       4.246   3.320   9.843  1.00 13.59           C  
ANISOU 1079  CD2 TYR A 128     2543   1607   1014    -37   -181    -26       C  
ATOM   1080  CE1 TYR A 128       6.143   3.915  11.847  1.00 14.67           C  
ANISOU 1080  CE1 TYR A 128     2674   1975    922    -35   -246   -471       C  
ATOM   1081  CE2 TYR A 128       3.865   3.855  11.113  1.00 14.79           C  
ANISOU 1081  CE2 TYR A 128     2366   1867   1384   -338     96    -79       C  
ATOM   1082  CZ  TYR A 128       4.813   4.170  12.051  1.00 15.19           C  
ANISOU 1082  CZ  TYR A 128     2293   2000   1475   -239   -181   -181       C  
ATOM   1083  OH  TYR A 128       4.447   4.644  13.297  1.00 18.12           O  
ANISOU 1083  OH  TYR A 128     3186   2579   1119   -144    234   -536       O  
ATOM   1084  N   GLU A 129       5.388   0.169   6.186  1.00 13.68           N  
ANISOU 1084  N   GLU A 129     2680   1594    924   -103    -56   -150       N  
ATOM   1085  CA  GLU A 129       5.278  -0.150   4.746  1.00 15.36           C  
ANISOU 1085  CA  GLU A 129     2653   2034   1148    132     20   -538       C  
ATOM   1086  C   GLU A 129       4.163   0.685   4.189  1.00 13.90           C  
ANISOU 1086  C   GLU A 129     2472   1774   1032    -82    -29   -218       C  
ATOM   1087  O   GLU A 129       3.302   1.182   4.856  1.00 14.96           O  
ANISOU 1087  O   GLU A 129     2846   1732   1104     34     -6     18       O  
ATOM   1088  CB  GLU A 129       5.013  -1.641   4.531  1.00 17.76           C  
ANISOU 1088  CB  GLU A 129     3326   2037   1383    238   -360   -508       C  
ATOM   1089  CG  GLU A 129       6.200  -2.432   4.952  1.00 25.72           C  
ANISOU 1089  CG  GLU A 129     4124   2919   2727    298   -439   -476       C  
ATOM   1090  CD  GLU A 129       6.108  -3.872   4.590  1.00 32.72           C  
ANISOU 1090  CD  GLU A 129     5370   3273   3788    445   -599   -983       C  
ATOM   1091  OE1 GLU A 129       4.998  -4.337   4.236  1.00 34.89           O  
ANISOU 1091  OE1 GLU A 129     6235   2522   4497   -230   -994   -826       O  
ATOM   1092  OE2 GLU A 129       7.167  -4.523   4.696  1.00 40.24           O  
ANISOU 1092  OE2 GLU A 129     5975   4366   4948    899   -722  -1260       O  
ATOM   1093  N   ARG A 130       4.147   0.801   2.857  1.00 15.06           N  
ANISOU 1093  N   ARG A 130     2742   2027    950    -41    -99   -314       N  
ATOM   1094  CA  ARG A 130       3.038   1.506   2.203  1.00 16.08           C  
ANISOU 1094  CA  ARG A 130     2977   2052   1079   -160   -238   -394       C  
ATOM   1095  C   ARG A 130       1.752   0.855   2.477  1.00 17.47           C  
ANISOU 1095  C   ARG A 130     2985   2219   1433   -213   -291   -392       C  
ATOM   1096  O   ARG A 130       1.649  -0.412   2.386  1.00 19.06           O  
ANISOU 1096  O   ARG A 130     3388   1774   2078   -497   -439   -351       O  
ATOM   1097  CB  ARG A 130       3.258   1.603   0.710  1.00 18.09           C  
ANISOU 1097  CB  ARG A 130     3145   2523   1204    -34   -322   -337       C  
ATOM   1098  CG  ARG A 130       4.512   2.306   0.351  1.00 19.40           C  
ANISOU 1098  CG  ARG A 130     3567   2588   1213    -96    -97     31       C  
ATOM   1099  CD  ARG A 130       4.227   3.736   0.143  1.00 22.67           C  
ANISOU 1099  CD  ARG A 130     3459   2605   2548   -151   -324   -137       C  
ATOM   1100  NE  ARG A 130       5.370   4.454  -0.408  1.00 22.16           N  
ANISOU 1100  NE  ARG A 130     3535   2247   2637    -90   -194    341       N  
ATOM   1101  CZ  ARG A 130       5.419   5.761  -0.559  1.00 19.99           C  
ANISOU 1101  CZ  ARG A 130     3415   2366   1813   -170   -281    261       C  
ATOM   1102  NH1 ARG A 130       4.353   6.471  -0.341  1.00 20.55           N  
ANISOU 1102  NH1 ARG A 130     3619   2513   1674   -281   -376    283       N  
ATOM   1103  NH2 ARG A 130       6.549   6.305  -0.894  1.00 21.36           N  
ANISOU 1103  NH2 ARG A 130     3530   2384   2202   -119     56    493       N  
ATOM   1104  N   ALA A 131       0.722   1.629   2.726  1.00 18.91           N  
ANISOU 1104  N   ALA A 131     3054   2217   1912   -252   -345   -169       N  
ATOM   1105  CA  ALA A 131      -0.567   1.064   3.090  1.00 22.98           C  
ANISOU 1105  CA  ALA A 131     3166   2668   2897   -290   -334   -243       C  
ATOM   1106  C   ALA A 131      -1.263   0.532   1.862  1.00 26.92           C  
ANISOU 1106  C   ALA A 131     3589   3105   3532   -370   -294   -283       C  
ATOM   1107  O   ALA A 131      -0.885   0.886   0.751  1.00 29.50           O  
ANISOU 1107  O   ALA A 131     3842   3362   4001   -277   -308   -195       O  
ATOM   1108  CB  ALA A 131      -1.392   2.060   3.927  1.00 25.45           C  
ANISOU 1108  CB  ALA A 131     3318   2981   3371   -294    -90   -332       C  
TER    1109      ALA A 131                                                      
HETATM 1110  C1 ACIT A 133       6.554   5.861  15.906  0.50 24.90           C  
ANISOU 1110  C1 ACIT A 133     3716   2972   2772     60    504    115       C  
HETATM 1111  C1 BCIT A 133       6.006   8.825  20.041  0.50 32.66           C  
ANISOU 1111  C1 BCIT A 133     4807   4247   3354     95   -208     60       C  
HETATM 1112  O1 ACIT A 133       6.536   5.733  14.668  0.50 24.08           O  
ANISOU 1112  O1 ACIT A 133     3565   2971   2611    -36    395   -975       O  
HETATM 1113  O1 BCIT A 133       6.489   9.905  20.410  0.50 36.02           O  
ANISOU 1113  O1 BCIT A 133     5185   4278   4221   -129   -131    326       O  
HETATM 1114  O2 ACIT A 133       5.753   5.131  16.503  0.50 27.35           O  
ANISOU 1114  O2 ACIT A 133     4298   2423   3669   -231    742    964       O  
HETATM 1115  O2 BCIT A 133       4.764   8.723  20.150  0.50 36.77           O  
ANISOU 1115  O2 BCIT A 133     5139   4711   4118   -132     21    -55       O  
HETATM 1116  C2 ACIT A 133       7.452   6.736  16.780  0.50 28.61           C  
ANISOU 1116  C2 ACIT A 133     4011   3121   3737    -57   -116     88       C  
HETATM 1117  C2 BCIT A 133       6.877   7.696  19.530  0.50 29.83           C  
ANISOU 1117  C2 BCIT A 133     4762   3722   2850    139   -277   -235       C  
HETATM 1118  C3 ACIT A 133       6.590   7.190  18.012  0.50 29.42           C  
ANISOU 1118  C3 ACIT A 133     4885   3721   2571   -301   -276    202       C  
HETATM 1119  C3 BCIT A 133       6.338   7.381  18.136  0.50 30.63           C  
ANISOU 1119  C3 BCIT A 133     4803   4028   2804     65   -331   -141       C  
HETATM 1120  O7 ACIT A 133       5.467   6.275  18.050  0.50 32.37           O  
ANISOU 1120  O7 ACIT A 133     4870   3848   3580   -545   -488     94       O  
HETATM 1121  O7 BCIT A 133       5.768   8.618  17.700  0.50 27.36           O  
ANISOU 1121  O7 BCIT A 133     4310   3503   2580    137   -531   -715       O  
HETATM 1122  C4 ACIT A 133       6.928   7.418  19.507  0.50 28.46           C  
ANISOU 1122  C4 ACIT A 133     4900   3242   2668   -198   -438    -30       C  
HETATM 1123  C4 BCIT A 133       7.209   6.845  16.946  0.50 31.49           C  
ANISOU 1123  C4 BCIT A 133     4219   3948   3798     93   -176   -302       C  
HETATM 1124  C5 ACIT A 133       5.857   8.324  20.050  0.50 32.55           C  
ANISOU 1124  C5 ACIT A 133     4728   4366   3274   -148   -361    161       C  
HETATM 1125  C5 BCIT A 133       6.427   5.832  16.136  0.50 30.17           C  
ANISOU 1125  C5 BCIT A 133     4234   4099   3128    100    207   -533       C  
HETATM 1126  O3 ACIT A 133       4.654   8.165  19.717  0.50 39.80           O  
ANISOU 1126  O3 ACIT A 133     5240   5357   4525   -203   -171     50       O  
HETATM 1127  O3 BCIT A 133       6.483   5.665  14.895  0.50 30.42           O  
ANISOU 1127  O3 BCIT A 133     4012   4705   2837     29   -160   -999       O  
HETATM 1128  O4 ACIT A 133       6.128   9.242  20.872  0.50 36.02           O  
ANISOU 1128  O4 ACIT A 133     5396   4112   4176   -258   -226    -60       O  
HETATM 1129  O4 BCIT A 133       5.685   5.087  16.796  0.50 29.03           O  
ANISOU 1129  O4 BCIT A 133     4672   4267   2089     49    253   -400       O  
HETATM 1130  C6 ACIT A 133       6.045   8.501  17.519  0.50 32.54           C  
ANISOU 1130  C6 ACIT A 133     5041   3749   3574   -185   -367     83       C  
HETATM 1131  C6 BCIT A 133       5.185   6.495  18.580  0.50 33.55           C  
ANISOU 1131  C6 BCIT A 133     4752   4567   3426    131   -153   -114       C  
HETATM 1132  O5 ACIT A 133       5.478   8.556  16.398  0.50 35.36           O  
ANISOU 1132  O5 ACIT A 133     5548   4359   3527   -688   -427   -496       O  
HETATM 1133  O5 BCIT A 133       5.227   6.171  19.769  0.50 34.57           O  
ANISOU 1133  O5 BCIT A 133     4821   5361   2953    715    129   -660       O  
HETATM 1134  O6 ACIT A 133       6.189   9.516  18.222  0.50 35.96           O  
ANISOU 1134  O6 ACIT A 133     5402   4264   3994   -550   -276   -141       O  
HETATM 1135  O6 BCIT A 133       4.194   6.112  17.911  0.50 35.75           O  
ANISOU 1135  O6 BCIT A 133     4789   4799   3994    314   -409   -108       O  
HETATM 1136  O   HOH A 134      14.949  24.693   5.117  1.00 94.55           O  
ANISOU 1136  O   HOH A 134    16180   5945  13798    344   5713   -190       O  
HETATM 1137  O   HOH A 135      -3.637   3.197  28.919  1.00 27.81           O  
ANISOU 1137  O   HOH A 135     4491   2483   3592    -12   -420   -418       O  
HETATM 1138  O   HOH A 136      10.372  21.982  12.757  1.00 13.03           O  
ANISOU 1138  O   HOH A 136     2743   1371    835    -13     24     99       O  
HETATM 1139  O   HOH A 137      -2.491  18.465  16.358  1.00 52.79           O  
ANISOU 1139  O   HOH A 137     5413   9313   5331  -3144    650  -1499       O  
HETATM 1140  O   HOH A 138       7.176  24.844  12.329  1.00 14.09           O  
ANISOU 1140  O   HOH A 138     2398   1767   1188   -104     50   -350       O  
HETATM 1141  O   HOH A 139      -0.473  -5.051  17.547  1.00 33.43           O  
ANISOU 1141  O   HOH A 139     3963   2843   5894    -30    558   1111       O  
HETATM 1142  O   HOH A 140      -3.776  -0.615  22.290  1.00 15.50           O  
ANISOU 1142  O   HOH A 140     2978   1679   1231   -342   -148    147       O  
HETATM 1143  O   HOH A 141       8.819  -3.038  20.084  1.00 19.21           O  
ANISOU 1143  O   HOH A 141     3575   2199   1525    303   -131    -86       O  
HETATM 1144  O   HOH A 142      11.690  12.310  12.115  1.00 14.29           O  
ANISOU 1144  O   HOH A 142     3007   1528    893    143    139     32       O  
HETATM 1145  O   HOH A 143       3.838  16.618  -1.993  1.00 34.90           O  
ANISOU 1145  O   HOH A 143     6447   4101   2713  -1136    357     94       O  
HETATM 1146  O   HOH A 144      -6.828   5.276  23.735  1.00 39.76           O  
ANISOU 1146  O   HOH A 144     7462   3706   3937  -1312   1439    338       O  
HETATM 1147  O   HOH A 145       9.947  -5.477   8.888  1.00100.76           O  
ANISOU 1147  O   HOH A 145    23348   7231   7703   2879    229  -2054       O  
HETATM 1148  O   HOH A 146      14.481   4.435  32.529  1.00110.62           O  
ANISOU 1148  O   HOH A 146    20343  13876   7810 -13015  -8967   7850       O  
HETATM 1149  O   HOH A 147       3.060   8.299  30.927  1.00 31.46           O  
ANISOU 1149  O   HOH A 147     4971   3041   3941    824    754    -12       O  
HETATM 1150  O   HOH A 148      14.507  -5.574  22.682  1.00 34.20           O  
ANISOU 1150  O   HOH A 148     6886   2955   3153   -387  -1769    438       O  
HETATM 1151  O   HOH A 149      -2.711   5.932  28.663  1.00 42.57           O  
ANISOU 1151  O   HOH A 149     4711   3807   7653    952  -2262  -2230       O  
HETATM 1152  O   HOH A 150      -2.194  13.282  24.092  1.00 80.04           O  
ANISOU 1152  O   HOH A 150     6020  13546  10845  -2590  -1144    448       O  
HETATM 1153  O   HOH A 151      13.137  -4.061   2.346  1.00 78.87           O  
ANISOU 1153  O   HOH A 151    17177   4533   8256     95   -459  -1279       O  
HETATM 1154  O   HOH A 152      13.690  26.596  15.352  1.00 14.74           O  
ANISOU 1154  O   HOH A 152     2563   1476   1560   -133    -86    -52       O  
HETATM 1155  O   HOH A 153       7.574  -9.965  15.984  1.00103.96           O  
ANISOU 1155  O   HOH A 153    20306  10671   8523   3045   5161   5031       O  
HETATM 1156  O   HOH A 154       1.023  20.232   5.099  1.00 17.85           O  
ANISOU 1156  O   HOH A 154     3171   2080   1530     34   -153    293       O  
HETATM 1157  O   HOH A 155       7.518  25.966  -0.912  1.00 43.67           O  
ANISOU 1157  O   HOH A 155     5774   7750   3068  -2362    373    345       O  
HETATM 1158  O   HOH A 156      15.188   8.968   3.273  1.00 20.30           O  
ANISOU 1158  O   HOH A 156     4015   2100   1595   -264    510    280       O  
HETATM 1159  O   HOH A 157      16.114  18.746  14.211  1.00 21.91           O  
ANISOU 1159  O   HOH A 157     4268   2556   1499   -145    -85    171       O  
HETATM 1160  O   HOH A 158       9.715  22.933   5.352  1.00 17.81           O  
ANISOU 1160  O   HOH A 158     3130   2561   1075    214     83    172       O  
HETATM 1161  O   HOH A 159       1.586  15.732  -0.150  1.00 22.20           O  
ANISOU 1161  O   HOH A 159     5064   2256   1112    174   -545   -201       O  
HETATM 1162  O   HOH A 160      -3.927   1.788  15.020  1.00 30.31           O  
ANISOU 1162  O   HOH A 160     5438   2315   3764    368   1512    447       O  
HETATM 1163  O   HOH A 161       3.097  -4.644  22.505  1.00 35.86           O  
ANISOU 1163  O   HOH A 161     7053   4104   2466   1479    641    307       O  
HETATM 1164  O   HOH A 162      16.301  21.039   7.306  1.00 19.90           O  
ANISOU 1164  O   HOH A 162     3808   1796   1957   -210    275    306       O  
HETATM 1165  O   HOH A 163      -3.720  -1.110  19.538  1.00 17.80           O  
ANISOU 1165  O   HOH A 163     2933   2387   1440   -527     44    302       O  
HETATM 1166  O   HOH A 164       3.057  21.606  24.172  1.00 73.65           O  
ANISOU 1166  O   HOH A 164    15563   6420   5999    240   -975   1677       O  
HETATM 1167  O   HOH A 165       2.552  -6.455  11.623  1.00 38.12           O  
ANISOU 1167  O   HOH A 165     5808   4026   4646  -1737     28    348       O  
HETATM 1168  O   HOH A 166      23.167  19.884  11.811  1.00 96.57           O  
ANISOU 1168  O   HOH A 166    10462  18310   7919   6373    257   1901       O  
HETATM 1169  O   HOH A 167       4.624  24.300  13.251  1.00 14.39           O  
ANISOU 1169  O   HOH A 167     2648   1737   1081     15     80   -194       O  
HETATM 1170  O   HOH A 168       1.671  12.753  14.266  1.00 24.46           O  
ANISOU 1170  O   HOH A 168     3798   3437   2055    172    523   1344       O  
HETATM 1171  O   HOH A 169      11.476  -3.183  13.728  1.00 23.34           O  
ANISOU 1171  O   HOH A 169     5031   2195   1639    -83    373     18       O  
HETATM 1172  O   HOH A 170      18.640   2.441  33.552  1.00 71.49           O  
ANISOU 1172  O   HOH A 170    18152   5704   3305  -3295    696   3394       O  
HETATM 1173  O   HOH A 171      14.329   0.626  31.677  1.00 34.37           O  
ANISOU 1173  O   HOH A 171     5368   4388   3302    163    378    524       O  
HETATM 1174  O   HOH A 172      16.554  -0.595  28.840  1.00 30.29           O  
ANISOU 1174  O   HOH A 172     5083   4085   2338   1760   -131     -2       O  
HETATM 1175  O   HOH A 173      11.464  -5.787  21.059  1.00 27.09           O  
ANISOU 1175  O   HOH A 173     5409   1427   3453   -134    440    517       O  
HETATM 1176  O   HOH A 174      14.068  19.652   0.326  1.00117.25           O  
ANISOU 1176  O   HOH A 174    26196   8499   9852  -5767  -3942   2823       O  
HETATM 1177  O   HOH A 175       0.751   7.281  -1.959  1.00 33.57           O  
ANISOU 1177  O   HOH A 175     5835   4708   2211    146   -871    667       O  
HETATM 1178  O   HOH A 176       6.063  27.498  15.451  1.00 19.50           O  
ANISOU 1178  O   HOH A 176     2954   2091   2363     53   -501   -348       O  
HETATM 1179  O   HOH A 177       1.628  26.157   2.247  1.00 22.52           O  
ANISOU 1179  O   HOH A 177     3724   1807   3025    -51     17   -379       O  
HETATM 1180  O   HOH A 178     -11.848  11.021  20.248  1.00 40.90           O  
ANISOU 1180  O   HOH A 178     6055   3431   6054  -1402   1000   -463       O  
HETATM 1181  O   HOH A 179       1.037   2.600  -2.611  1.00 93.34           O  
ANISOU 1181  O   HOH A 179    21868   9424   4171   8137   2080  -3982       O  
HETATM 1182  O   HOH A 180       4.101  27.086   2.426  1.00 21.75           O  
ANISOU 1182  O   HOH A 180     3748   2216   2297    132   -118    -58       O  
HETATM 1183  O   HOH A 181       1.597   5.741   0.074  1.00 20.18           O  
ANISOU 1183  O   HOH A 181     3760   2468   1438   -327    -36   -285       O  
HETATM 1184  O   HOH A 182      12.012 -10.483  17.084  1.00 47.24           O  
ANISOU 1184  O   HOH A 182     7416   4497   6034   -982  -1903   -370       O  
HETATM 1185  O   HOH A 183      -1.986  15.901  17.748  1.00 22.63           O  
ANISOU 1185  O   HOH A 183     4938   2170   1490    108    130   -233       O  
HETATM 1186  O   HOH A 184       2.572  -7.878  16.822  1.00 41.85           O  
ANISOU 1186  O   HOH A 184     5135   6202   4564   -367   -744   -247       O  
HETATM 1187  O   HOH A 185      -0.680  14.306   6.404  1.00 18.68           O  
ANISOU 1187  O   HOH A 185     3579   1762   1757     -6   -203   -102       O  
HETATM 1188  O   HOH A 186       8.987  -3.998  -1.862  1.00 57.54           O  
ANISOU 1188  O   HOH A 186    11805   5425   4632   -532    630   -730       O  
HETATM 1189  O   HOH A 187      21.665  10.162   5.341  1.00 55.88           O  
ANISOU 1189  O   HOH A 187     6364   6755   8110  -1950   3590    480       O  
HETATM 1190  O   HOH A 188       8.495  -3.507  22.763  1.00 28.89           O  
ANISOU 1190  O   HOH A 188     5325   2842   2809   -486    875   -493       O  
HETATM 1191  O   HOH A 189       2.144  30.347  -7.228  1.00 43.18           O  
ANISOU 1191  O   HOH A 189     8712   5242   2452    264    482   -254       O  
HETATM 1192  O   HOH A 190      -2.517  19.410  14.332  1.00 47.77           O  
ANISOU 1192  O   HOH A 190     8845   3616   5686   1389    475   -566       O  
HETATM 1193  O   HOH A 191      11.244  -2.828   0.861  1.00 22.52           O  
ANISOU 1193  O   HOH A 191     4602   1907   2047   -354     20     93       O  
HETATM 1194  O   HOH A 192      17.287   8.908  16.436  1.00 34.36           O  
ANISOU 1194  O   HOH A 192     7091   2906   3055    922    -59    191       O  
HETATM 1195  O   HOH A 193      21.026   4.615  12.743  1.00 75.51           O  
ANISOU 1195  O   HOH A 193     4883  12727  11077    320   1782    597       O  
HETATM 1196  O   HOH A 194      20.343   4.895  28.436  1.00 24.82           O  
ANISOU 1196  O   HOH A 194     5065   2450   1914    115   -210    256       O  
HETATM 1197  O   HOH A 195       7.857  25.788  -6.291  1.00 67.36           O  
ANISOU 1197  O   HOH A 195     7105   7944  10544   1329  -3056  -4513       O  
HETATM 1198  O   HOH A 196      14.663  24.992  17.406  1.00 21.93           O  
ANISOU 1198  O   HOH A 196     3966   2222   2143   -126   -687    -19       O  
HETATM 1199  O   HOH A 197      13.036  21.569  19.865  1.00 21.85           O  
ANISOU 1199  O   HOH A 197     3482   3653   1166   -367   -106    101       O  
HETATM 1200  O   HOH A 198       2.807   1.044  18.742  1.00 22.97           O  
ANISOU 1200  O   HOH A 198     3408   3944   1375   -752    203    361       O  
HETATM 1201  O   HOH A 199       0.497   5.090  32.234  1.00 25.64           O  
ANISOU 1201  O   HOH A 199     5278   2787   1674   -491    199    -73       O  
HETATM 1202  O   HOH A 200       5.263  22.645  24.236  1.00 28.73           O  
ANISOU 1202  O   HOH A 200     4770   3064   3081    770    360   -169       O  
HETATM 1203  O   HOH A 201       2.609   6.821  13.737  1.00 27.12           O  
ANISOU 1203  O   HOH A 201     4752   2528   3022      2    788    221       O  
HETATM 1204  O   HOH A 202       2.475  -5.302  19.750  1.00 37.12           O  
ANISOU 1204  O   HOH A 202     6686   4533   2884   -399    584  -1387       O  
HETATM 1205  O   HOH A 203       0.340   3.044  34.675  1.00 28.88           O  
ANISOU 1205  O   HOH A 203     6637   3035   1301    689    -48   -380       O  
HETATM 1206  O   HOH A 204      -2.060  -2.018  10.811  1.00114.56           O  
ANISOU 1206  O   HOH A 204     4452  28123  10951  -1163    536  -3227       O  
HETATM 1207  O   HOH A 205       1.615   3.999  19.723  1.00 35.18           O  
ANISOU 1207  O   HOH A 205     5602   3621   4142   -143   -716    329       O  
HETATM 1208  O   HOH A 206       9.019  10.468  21.622  1.00 18.87           O  
ANISOU 1208  O   HOH A 206     3423   2018   1727   -124    320    175       O  
HETATM 1209  O   HOH A 207      -0.155   7.744  17.381  1.00 33.69           O  
ANISOU 1209  O   HOH A 207     5210   4662   2927   1315   1476   1656       O  
HETATM 1210  O   HOH A 208      17.588  13.314  27.901  1.00 29.47           O  
ANISOU 1210  O   HOH A 208     3900   3414   3881    547   -730    812       O  
HETATM 1211  O   HOH A 209       3.282  11.530  19.270  1.00 20.78           O  
ANISOU 1211  O   HOH A 209     3464   2578   1850   -207    297    -46       O  
HETATM 1212  O   HOH A 210       2.702  13.966  17.938  1.00 26.48           O  
ANISOU 1212  O   HOH A 210     3787   2393   3878   -321   -205    580       O  
HETATM 1213  O   HOH A 211       0.818  15.699  18.507  1.00 23.94           O  
ANISOU 1213  O   HOH A 211     4827   2806   1461   -335    644    -21       O  
HETATM 1214  O   HOH A 212       0.459  18.567  19.207  1.00 27.34           O  
ANISOU 1214  O   HOH A 212     4680   2833   2872   -603  -1086   1007       O  
HETATM 1215  O   HOH A 213       8.767  -6.007  20.225  1.00 35.18           O  
ANISOU 1215  O   HOH A 213     4770   4551   4043    162    750    720       O  
HETATM 1216  O   HOH A 214      -8.058  16.355  18.867  1.00 85.15           O  
ANISOU 1216  O   HOH A 214    11350  12764   8238   2336  -1225     90       O  
HETATM 1217  O   HOH A 215       6.203  -0.562   1.412  1.00 21.46           O  
ANISOU 1217  O   HOH A 215     3221   3139   1792    147    266   -452       O  
HETATM 1218  O   HOH A 216      -8.709  11.739  17.922  1.00 39.88           O  
ANISOU 1218  O   HOH A 216     4318   5251   5582    655    493  -1406       O  
HETATM 1219  O   HOH A 217       7.141  -6.278  15.596  1.00 30.89           O  
ANISOU 1219  O   HOH A 217     5645   2684   3405  -1013   -926   1318       O  
HETATM 1220  O   HOH A 218       5.313  -1.796  19.744  1.00 33.06           O  
ANISOU 1220  O   HOH A 218     4015   3734   4812  -1030   1091   -666       O  
HETATM 1221  O   HOH A 219       8.115   2.482  -2.901  1.00 33.86           O  
ANISOU 1221  O   HOH A 219     6335   3407   3121   1090     99   -103       O  
HETATM 1222  O   HOH A 220       6.055  11.930  19.103  1.00 37.04           O  
ANISOU 1222  O   HOH A 220     3964   6153   3955  -1650    803  -2280       O  
HETATM 1223  O   HOH A 221       9.347   5.757  -3.957  1.00 57.30           O  
ANISOU 1223  O   HOH A 221     7274   7219   7278  -1700   -723   -648       O  
HETATM 1224  O   HOH A 222      11.360  -3.240  24.688  1.00 29.57           O  
ANISOU 1224  O   HOH A 222     5501   2447   3284     27   1072    202       O  
HETATM 1225  O   HOH A 223       6.226  23.418  -3.970  1.00 44.27           O  
ANISOU 1225  O   HOH A 223     5388   5704   5728    871    258    169       O  
HETATM 1226  O   HOH A 224      18.447   4.616   2.426  1.00 28.18           O  
ANISOU 1226  O   HOH A 224     5232   4113   1361    141     53   -634       O  
HETATM 1227  O   HOH A 225      21.862  11.484   7.558  1.00 40.86           O  
ANISOU 1227  O   HOH A 225     4966   4630   5925  -1020   -494   1486       O  
HETATM 1228  O   HOH A 226      -0.210   5.027  18.304  1.00 38.93           O  
ANISOU 1228  O   HOH A 226     5148   4388   5255   -599   -524   2593       O  
HETATM 1229  O   HOH A 227       6.634  19.962  29.459  1.00 38.61           O  
ANISOU 1229  O   HOH A 227     5871   6058   2741    813     62  -1448       O  
HETATM 1230  O   HOH A 228      19.972   1.827  15.068  1.00 39.51           O  
ANISOU 1230  O   HOH A 228     6056   5610   3345    550   -481   1270       O  
HETATM 1231  O   HOH A 229      10.436  -4.224  27.916  1.00 42.53           O  
ANISOU 1231  O   HOH A 229     6093   4855   5209    889     67   2670       O  
HETATM 1232  O   HOH A 230       5.054   7.408  21.653  1.00 36.65           O  
ANISOU 1232  O   HOH A 230     6177   3650   4097   1812   2103    645       O  
HETATM 1233  O   HOH A 231       9.992  21.254   2.956  1.00 37.77           O  
ANISOU 1233  O   HOH A 231     6744   4964   2642   -190    396  -1719       O  
HETATM 1234  O   HOH A 232      21.972   3.070  18.602  1.00 42.31           O  
ANISOU 1234  O   HOH A 232     5931   6002   4141  -1004   -595   2498       O  
HETATM 1235  O   HOH A 233      19.515  -1.219  31.410  1.00 32.99           O  
ANISOU 1235  O   HOH A 233     6162   3301   3070    435    487   -797       O  
HETATM 1236  O   HOH A 234       9.826  -7.976  23.490  1.00 43.59           O  
ANISOU 1236  O   HOH A 234     5581   6170   4811   -217  -1179    517       O  
HETATM 1237  O   HOH A 235      20.911   4.940  21.597  1.00 26.53           O  
ANISOU 1237  O   HOH A 235     4800   2962   2317    493    232     85       O  
HETATM 1238  O   HOH A 236       0.129   3.428  -0.292  1.00 29.19           O  
ANISOU 1238  O   HOH A 236     4246   2610   4231    225  -1226   -746       O  
HETATM 1239  O   HOH A 237       6.308   9.120  -1.810  1.00 25.58           O  
ANISOU 1239  O   HOH A 237     4535   2392   2790   -716    674   -538       O  
HETATM 1240  O   HOH A 238      -0.714  18.631   3.772  1.00 24.02           O  
ANISOU 1240  O   HOH A 238     4616   2158   2351    122   -975     73       O  
HETATM 1241  O   HOH A 239       2.077   9.955  17.337  1.00 21.89           O  
ANISOU 1241  O   HOH A 239     3887   2885   1543    -37    -52   -270       O  
HETATM 1242  O   HOH A 240      13.262  21.159  28.406  1.00 27.90           O  
ANISOU 1242  O   HOH A 240     5266   2978   2356    274   -347   -445       O  
HETATM 1243  O   HOH A 241      11.346  24.835   4.327  1.00 33.29           O  
ANISOU 1243  O   HOH A 241     4448   4712   3488  -1078   1113    937       O  
HETATM 1244  O   HOH A 242      14.711   1.502  29.148  1.00 23.78           O  
ANISOU 1244  O   HOH A 242     3907   3563   1565    722   -302    285       O  
HETATM 1245  O   HOH A 243       9.261  21.207  29.725  1.00 30.23           O  
ANISOU 1245  O   HOH A 243     6029   3402   2052   1532     11   -635       O  
HETATM 1246  O   HOH A 244      -3.276  14.361  19.655  1.00 30.56           O  
ANISOU 1246  O   HOH A 244     5160   3432   3016   -821    966   -823       O  
HETATM 1247  O   HOH A 245      -7.044   9.591  19.959  1.00 78.24           O  
ANISOU 1247  O   HOH A 245     9272  18620   1835   1080   1087   2503       O  
HETATM 1248  O   HOH A 246      18.370  11.279  24.157  1.00 28.72           O  
ANISOU 1248  O   HOH A 246     3744   2290   4878    227   -456    805       O  
HETATM 1249  O   HOH A 247       3.633   3.663  35.635  1.00 32.99           O  
ANISOU 1249  O   HOH A 247     8602   3386    547  -1880   -481    957       O  
HETATM 1250  O   HOH A 248       6.518   8.105  12.917  1.00 25.71           O  
ANISOU 1250  O   HOH A 248     3913   3965   1887   -627    269    261       O  
HETATM 1251  O   HOH A 249      22.876   3.993  20.718  1.00 20.43           O  
ANISOU 1251  O   HOH A 249     4047   1806   1907    375    580    162       O  
HETATM 1252  O   HOH A 250      -7.223   2.580  23.613  1.00 27.53           O  
ANISOU 1252  O   HOH A 250     5913   2399   2148    117    320    179       O  
HETATM 1253  O   HOH A 251       4.964  -1.546  25.392  1.00 27.94           O  
ANISOU 1253  O   HOH A 251     4047   4702   1866    690    -27   -179       O  
HETATM 1254  O   HOH A 252      -2.723  20.022   1.549  1.00 28.62           O  
ANISOU 1254  O   HOH A 252     5361   3188   2323  -1827   -217    212       O  
HETATM 1255  O   HOH A 253       4.958  10.073  29.254  1.00 29.05           O  
ANISOU 1255  O   HOH A 253     6278   2968   1789    -93    427    762       O  
HETATM 1256  O   HOH A 254       2.151  -3.716  24.763  1.00 24.17           O  
ANISOU 1256  O   HOH A 254     3840   3338   2005    305   -112   -409       O  
HETATM 1257  O   HOH A 255       2.500   9.416  -2.440  1.00 39.19           O  
ANISOU 1257  O   HOH A 255     6605   4160   4122     -6  -1865   -764       O  
HETATM 1258  O   HOH A 256       2.875  -2.447  17.635  1.00 27.24           O  
ANISOU 1258  O   HOH A 256     4949   3487   1913    507   -468     71       O  
HETATM 1259  O   HOH A 257       5.789  -2.467  22.882  1.00 35.96           O  
ANISOU 1259  O   HOH A 257     4789   6881   1993   1548   -457   -916       O  
HETATM 1260  O   HOH A 258       4.869  16.984  29.759  1.00 33.11           O  
ANISOU 1260  O   HOH A 258     7375   3332   1873   -428    192   -279       O  
HETATM 1261  O   HOH A 259       5.022  29.013   4.206  1.00 41.68           O  
ANISOU 1261  O   HOH A 259     4572   2441   8824  -1140   1990  -1911       O  
HETATM 1262  O   HOH A 260      15.936  20.998  19.285  1.00 39.62           O  
ANISOU 1262  O   HOH A 260     4705   2814   7535  -1025  -2496   2003       O  
HETATM 1263  O   HOH A 261      17.791  13.808  21.634  1.00 25.89           O  
ANISOU 1263  O   HOH A 261     4126   4047   1662   -371    -46   -190       O  
HETATM 1264  O   HOH A 262      -7.750   6.491  19.060  1.00 35.11           O  
ANISOU 1264  O   HOH A 262     4853   4553   3934   1012    800   -643       O  
HETATM 1265  O   HOH A 263      -3.166  14.886   7.041  1.00 41.09           O  
ANISOU 1265  O   HOH A 263     3751   6583   5277    592    622   2522       O  
HETATM 1266  O   HOH A 264      22.812   2.075  22.201  1.00 23.03           O  
ANISOU 1266  O   HOH A 264     3815   2018   2914    304    264   -120       O  
HETATM 1267  O   HOH A 265       9.036  11.964  30.716  1.00 27.29           O  
ANISOU 1267  O   HOH A 265     5191   3128   2049    104   1008    556       O  
HETATM 1268  O   HOH A 266      -1.119  18.302   0.852  1.00 29.53           O  
ANISOU 1268  O   HOH A 266     4830   2854   3534   1056    -79     97       O  
HETATM 1269  O   HOH A 267      15.486  19.732  27.307  1.00 29.98           O  
ANISOU 1269  O   HOH A 267     7612   2234   1545   -375   -393   -218       O  
HETATM 1270  O   HOH A 268      16.995   7.181   2.124  1.00 31.58           O  
ANISOU 1270  O   HOH A 268     5239   3435   3323   -476   1303   -378       O  
HETATM 1271  O   HOH A 269      -7.089   1.062  25.684  1.00 22.32           O  
ANISOU 1271  O   HOH A 269     3370   2288   2823   -448   -361    409       O  
HETATM 1272  O   HOH A 270       1.890  -6.423  25.927  1.00 34.79           O  
ANISOU 1272  O   HOH A 270     4778   2968   5471    787   2465    384       O  
HETATM 1273  O   HOH A 271      -5.978   3.301  27.346  1.00 29.34           O  
ANISOU 1273  O   HOH A 271     3934   3363   3850    -60    -14   -238       O  
HETATM 1274  O   HOH A 272       6.978  -3.065  30.487  1.00 30.80           O  
ANISOU 1274  O   HOH A 272     7653   1966   2082   -430    388    -20       O  
HETATM 1275  O   HOH A 273       6.010  11.732  16.285  1.00 33.23           O  
ANISOU 1275  O   HOH A 273     3292   6471   2863    127    909    293       O  
HETATM 1276  O   HOH A 274       3.920  13.244  15.515  1.00 29.85           O  
ANISOU 1276  O   HOH A 274     5328   3323   2688    120   -226     61       O  
HETATM 1277  O   HOH A 275       4.010   9.175  15.566  1.00 47.55           O  
ANISOU 1277  O   HOH A 275     8884   4156   5025   1989   2604   1302       O  
HETATM 1278  O   HOH A 276       8.799   4.902  32.767  1.00 29.68           O  
ANISOU 1278  O   HOH A 276     4457   3579   3239   -299  -1374    500       O  
HETATM 1279  O   HOH A 277      10.338  22.098  26.598  1.00104.51           O  
ANISOU 1279  O   HOH A 277    21059   9169   9478  -1036  -2467   1372       O  
HETATM 1280  O   HOH A 278      10.493  29.528   6.322  1.00 53.03           O  
ANISOU 1280  O   HOH A 278    12253   3994   3901  -1477  -1795   -322       O  
HETATM 1281  O   HOH A 279      11.681  27.775   5.295  1.00 68.34           O  
ANISOU 1281  O   HOH A 279    15432   7334   3199   -921   1744   3028       O  
HETATM 1282  O   HOH A 280      -8.086   6.213  14.787  1.00 36.72           O  
ANISOU 1282  O   HOH A 280     5125   3390   5435   -832  -1414    327       O  
HETATM 1283  O   HOH A 281      20.212  20.156  14.130  1.00 31.66           O  
ANISOU 1283  O   HOH A 281     5731   3226   3071   -162    492   -472       O  
HETATM 1284  O   HOH A 282       7.889  30.683   8.467  1.00 42.17           O  
ANISOU 1284  O   HOH A 282     4213   2618   9189   -203  -1717   1414       O  
HETATM 1285  O   HOH A 283      -1.813   9.303  26.237  1.00 41.61           O  
ANISOU 1285  O   HOH A 283     5778   4628   5401   -838   2519     97       O  
HETATM 1286  O   HOH A 284      -4.859  11.765  13.316  1.00 35.82           O  
ANISOU 1286  O   HOH A 284     3683   7378   2545    654     64   1336       O  
HETATM 1287  O   HOH A 285      18.717   1.495  29.630  1.00 44.57           O  
ANISOU 1287  O   HOH A 285     6581   7737   2614  -1405  -1008    360       O  
HETATM 1288  O   HOH A 286      17.748   0.918  13.379  1.00 33.14           O  
ANISOU 1288  O   HOH A 286     3319   3947   5322   -179   1165   -729       O  
HETATM 1289  O   HOH A 287       9.110  14.035  -6.019  1.00118.30           O  
ANISOU 1289  O   HOH A 287    25190  11583   8174  -6537   1661   -414       O  
HETATM 1290  O   HOH A 288       3.010  12.172  30.051  1.00 37.35           O  
ANISOU 1290  O   HOH A 288     7577   4010   2601    941    -17    165       O  
HETATM 1291  O   HOH A 289       5.293  19.272  -8.099  1.00 38.00           O  
ANISOU 1291  O   HOH A 289     5110   5105   4224  -1255   1066  -1429       O  
HETATM 1292  O   HOH A 290      19.530  14.638  18.077  1.00 29.94           O  
ANISOU 1292  O   HOH A 290     3028   3674   4673   -295    226   1241       O  
HETATM 1293  O   HOH A 291      20.623   4.414  17.557  1.00 35.99           O  
ANISOU 1293  O   HOH A 291     5903   3491   4281    -90   2142    565       O  
HETATM 1294  O   HOH A 292      18.873  17.805  14.640  1.00 36.53           O  
ANISOU 1294  O   HOH A 292     5428   3469   4983    -44   -638    882       O  
HETATM 1295  O   HOH A 293      -1.534  14.163  21.809  1.00 30.50           O  
ANISOU 1295  O   HOH A 293     4111   4540   2935   -396     92  -1096       O  
HETATM 1296  O   HOH A 294       4.395  -4.470  26.213  1.00 43.27           O  
ANISOU 1296  O   HOH A 294     7559   5770   3109   -394    397    309       O  
HETATM 1297  O   HOH A 295      -2.406  19.533   6.712  1.00 37.83           O  
ANISOU 1297  O   HOH A 295     4932   5476   3964     -2  -1384   1463       O  
CONECT 1110 1112 1114 1116                                                      
CONECT 1111 1113 1115 1117                                                      
CONECT 1112 1110                                                                
CONECT 1113 1111                                                                
CONECT 1114 1110                                                                
CONECT 1115 1111                                                                
CONECT 1116 1110 1118                                                           
CONECT 1117 1111 1119                                                           
CONECT 1118 1116 1120 1122 1130                                                 
CONECT 1119 1117 1121 1123 1131                                                 
CONECT 1120 1118                                                                
CONECT 1121 1119                                                                
CONECT 1122 1118 1124                                                           
CONECT 1123 1119 1125                                                           
CONECT 1124 1122 1126 1128                                                      
CONECT 1125 1123 1127 1129                                                      
CONECT 1126 1124                                                                
CONECT 1127 1125                                                                
CONECT 1128 1124                                                                
CONECT 1129 1125                                                                
CONECT 1130 1118 1132 1134                                                      
CONECT 1131 1119 1133 1135                                                      
CONECT 1132 1130                                                                
CONECT 1133 1131                                                                
CONECT 1134 1130                                                                
CONECT 1135 1131                                                                
MASTER      326    0    1    3   10    0    3    6 1247    1   26   11          
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.