CNRS Nantes University UFIP UFIP
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***  LIPID BINDING PROTEIN 11-OCT-10 3P6D  ***

elNémo ID: 22012616524746112

Job options:

ID        	=	 22012616524746112
JOBID     	=	 LIPID BINDING PROTEIN 11-OCT-10 3P6D
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    LIPID BINDING PROTEIN                   11-OCT-10   3P6D              
TITLE     HUMAN ADIPOCYTE LIPID-BINDING PROTEIN FABP4 IN COMPLEX WITH 3-(4-     
TITLE    2 METHOXY-3-METHYLPHENYL) PROPIONIC 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 3P6D    1       JRNL                                     
REVDAT   2   11-FEB-15 3P6D    1       JRNL                                     
REVDAT   1   13-APR-11 3P6D    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.    1.06 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) : 1.06                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 59310                          
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) : 0.141                           
REMARK   3   R VALUE            (WORKING SET) : 0.140                           
REMARK   3   FREE R VALUE                     : 0.161                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2995                            
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) : 1.06                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.09                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3996                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.10                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2010                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 231                          
REMARK   3   BIN FREE R VALUE                    : 0.2180                       
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          : 14                                      
REMARK   3   SOLVENT ATOMS            : 230                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.86000                                             
REMARK   3    B22 (A**2) : 0.53000                                              
REMARK   3    B33 (A**2) : 0.33000                                              
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): 0.017         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.719         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.964                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1263 ; 0.021 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):   862 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1714 ; 2.016 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2105 ; 1.006 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   169 ; 6.436 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    51 ;35.084 ;24.902       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   243 ;13.623 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;16.120 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   192 ; 0.111 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1438 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   245 ; 0.004 ; 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):   777 ; 2.138 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   327 ; 0.618 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1273 ; 3.316 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   486 ; 4.474 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   435 ; 6.291 ; 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):  2125 ; 1.793 ; 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 3P6D 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 RCSB062012.                                      
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   : 59374                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.060                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.10300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.06                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26800                            
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   (%): 41.00                                     
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       16.12200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.50750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.69600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.50750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.12200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.69600            
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   OE2  GLU A    69     O    HOH A   183              1.82            
REMARK 500   O    HOH A   314     O    HOH A   318              1.97            
REMARK 500   O    HOH A   137     O    HOH A   269              2.01            
REMARK 500   O    HOH A   182     O    HOH A   357              2.10            
REMARK 500   O    VAL A    73     O    HOH A   295              2.13            
REMARK 500   O    HOH A   206     O    HOH A   233              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   302     O    HOH A   314     3555     1.73            
REMARK 500   O    HOH A   302     O    HOH A   348     3655     2.14            
REMARK 500   O    HOH A   228     O    HOH A   317     3645     2.17            
REMARK 500   O    HOH A   209     O    HOH A   222     4555     2.18            
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 126   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  57      -70.89    -87.35                                   
REMARK 500    ASP A 110     -133.93     54.49                                   
REMARK 500    LYS A 120     -123.45     48.32                                   
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 193        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH A 258        DISTANCE =  8.59 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZGB A 133                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3P6C   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  3P6D A    0   131  UNP    P15090   FABP4_HUMAN      1    132             
SEQADV 3P6D GLN A   -7  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6D GLN A   -6  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6D MET A   -5  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6D GLY A   -4  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6D ARG A   -3  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6D GLY A   -2  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6D 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    ZGB  A 133      28                                                       
HETNAM     ZGB 3-(4-METHOXY-3-METHYLPHENYL)PROPANOIC ACID                       
FORMUL   2  ZGB    C11 H14 O3                                                   
FORMUL   3  HOH   *230(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  PHE A  64  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  THR A 103   O  VAL A 118           
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  MET A  20  VAL A  25  ALA A  33                    
SITE     2 AC1 12 PHE A  57  ALA A  75  ASP A  76  ARG A  78                    
SITE     3 AC1 12 ARG A 126  TYR A 128  HOH A 281  HOH A 319                    
CRYST1   32.244   53.392   75.015  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      0.031014  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018729  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013331        0.00000                         

ATOM     44  N  AMET A   0      12.832  16.856  -2.362  0.50 15.58           N  
ANISOU   44  N  AMET A   0     2791   1597   1530   -297     -5    561       N  
ATOM     45  N  BMET A   0      12.804  16.914  -2.316  0.50 17.67           N  
ANISOU   45  N  BMET A   0     2881   1905   1925   -262      3    473       N  
ATOM     46  CA AMET A   0      13.333  15.576  -1.860  0.50 15.33           C  
ANISOU   46  CA AMET A   0     2746   1676   1400   -198    -50    534       C  
ATOM     47  CA BMET A   0      13.372  15.679  -1.855  0.50 18.34           C  
ANISOU   47  CA BMET A   0     2920   2033   2014   -197    -11    467       C  
ATOM     48  C  AMET A   0      12.351  14.937  -0.858  0.50 15.42           C  
ANISOU   48  C  AMET A   0     2785   1578   1494   -121    -83    568       C  
ATOM     49  C  BMET A   0      12.487  14.996  -0.802  0.50 17.36           C  
ANISOU   49  C  BMET A   0     2911   1836   1850   -126    -89    531       C  
ATOM     50  O  AMET A   0      12.137  13.722  -0.900  0.50 15.62           O  
ANISOU   50  O  AMET A   0     2642   1685   1608     80   -103    433       O  
ATOM     51  O  BMET A   0      12.496  13.776  -0.730  0.50 17.86           O  
ANISOU   51  O  BMET A   0     3014   1813   1958   -138    -87    693       O  
ATOM     52  CB AMET A   0      14.721  15.767  -1.254  0.50 15.13           C  
ANISOU   52  CB AMET A   0     2761   1671   1316   -126    -19    440       C  
ATOM     53  CB BMET A   0      14.776  15.969  -1.349  0.50 19.47           C  
ANISOU   53  CB BMET A   0     2987   2300   2108   -121    -24    393       C  
ATOM     54  CG AMET A   0      15.467  14.488  -0.953  0.50 14.81           C  
ANISOU   54  CG AMET A   0     2671   1903   1052    -70   -194    597       C  
ATOM     55  CG BMET A   0      15.794  14.958  -1.763  0.50 22.23           C  
ANISOU   55  CG BMET A   0     2939   2663   2845    -38    208    319       C  
ATOM     56  SD AMET A   0      16.770  14.508   0.340  0.50 21.58           S  
ANISOU   56  SD AMET A   0     3713   2651   1835    171   -578   -291       S  
ATOM     57  SD BMET A   0      16.345  14.079  -0.312  0.50 29.90           S  
ANISOU   57  SD BMET A   0     4091   3751   3517    139    -47     30       S  
ATOM     58  CE AMET A   0      15.774  14.665   1.789  0.50 23.91           C  
ANISOU   58  CE AMET A   0     3564   2874   2646    153    111   -542       C  
ATOM     59  CE BMET A   0      14.958  14.286   0.824  0.50 10.59           C  
ANISOU   59  CE BMET A   0     2199   1075    747    -17   -290    273       C  
ATOM     60  N   CYS A   1      11.715  15.755  -0.001  1.00 17.31           N  
ANISOU   60  N   CYS A   1     2821   1899   1855   -156     -1    531       N  
ATOM     61  CA ACYS A   1      10.748  15.293   1.043  0.50 17.00           C  
ANISOU   61  CA ACYS A   1     2986   1701   1771    -49      7    604       C  
ATOM     62  CA BCYS A   1      10.809  15.133   1.010  0.50 16.52           C  
ANISOU   62  CA BCYS A   1     2945   1760   1571   -142    -40    520       C  
ATOM     63  C   CYS A   1       9.566  14.495   0.410  1.00 15.82           C  
ANISOU   63  C   CYS A   1     2709   1620   1680      4     74    711       C  
ATOM     64  O   CYS A   1       8.836  13.785   1.133  1.00 16.64           O  
ANISOU   64  O   CYS A   1     2963   1499   1859     96    334    959       O  
ATOM     65  CB ACYS A   1      10.256  16.513   1.865  0.50 19.14           C  
ANISOU   65  CB ACYS A   1     2965   2089   2216      5    154    366       C  
ATOM     66  CB BCYS A   1      10.368  16.069   2.113  0.50 17.06           C  
ANISOU   66  CB BCYS A   1     2895   1990   1595      6    101    409       C  
ATOM     67  SG ACYS A   1      10.336  16.441   3.749  0.50 26.21           S  
ANISOU   67  SG ACYS A   1     4155   3019   2782    138    520    476       S  
ATOM     68  SG BCYS A   1      11.656  16.811   3.034  0.50 23.25           S  
ANISOU   68  SG BCYS A   1     3671   3095   2066   -332    -63   -663       S  
ATOM     69  N   ASP A   2       9.427  14.585  -0.895  1.00 15.81           N  
ANISOU   69  N   ASP A   2     2613   1747   1645   -366    -81    853       N  
ATOM     70  CA  ASP A   2       8.382  13.852  -1.526  1.00 17.65           C  
ANISOU   70  CA  ASP A   2     2818   1931   1956   -469   -206    872       C  
ATOM     71  C   ASP A   2       8.554  12.339  -1.314  1.00 16.28           C  
ANISOU   71  C   ASP A   2     2803   1960   1422   -443    -60    763       C  
ATOM     72  O   ASP A   2       7.547  11.665  -1.348  1.00 16.49           O  
ANISOU   72  O   ASP A   2     2912   1860   1491   -506    -79    499       O  
ATOM     73  CB  ASP A   2       8.235  14.246  -2.958  1.00 19.35           C  
ANISOU   73  CB  ASP A   2     3099   2253   1999   -616   -318   1059       C  
ATOM     74  CG  ASP A   2       7.635  15.673  -3.145  1.00 20.64           C  
ANISOU   74  CG  ASP A   2     3260   2310   2272    -48   -468   1210       C  
ATOM     75  OD1 ASP A   2       6.970  16.213  -2.192  1.00 25.28           O  
ANISOU   75  OD1 ASP A   2     3719   2821   3064    151   -315    899       O  
ATOM     76  OD2 ASP A   2       7.849  16.259  -4.178  1.00 24.21           O  
ANISOU   76  OD2 ASP A   2     3408   2870   2918   -312   -606   1081       O  
ATOM     77  N   ALA A   3       9.776  11.825  -1.048  1.00 16.21           N  
ANISOU   77  N   ALA A   3     2739   2073   1347   -436    285    624       N  
ATOM     78  CA  ALA A   3      10.004  10.412  -0.787  1.00 16.02           C  
ANISOU   78  CA  ALA A   3     2778   1923   1385   -142    253    417       C  
ATOM     79  C   ALA A   3       9.266   9.958   0.462  1.00 13.48           C  
ANISOU   79  C   ALA A   3     2687   1428   1004    -70    156    412       C  
ATOM     80  O   ALA A   3       9.001   8.752   0.593  1.00 14.02           O  
ANISOU   80  O   ALA A   3     2935   1364   1028     16    435     14       O  
ATOM     81  CB  ALA A   3      11.451  10.157  -0.588  1.00 19.48           C  
ANISOU   81  CB  ALA A   3     2949   2483   1967   -179    347    802       C  
ATOM     82  N   PHE A   4       8.957  10.861   1.383  1.00 11.60           N  
ANISOU   82  N   PHE A   4     2561    947    897    -76    159    270       N  
ATOM     83  CA  PHE A   4       8.226  10.506   2.574  1.00 10.49           C  
ANISOU   83  CA  PHE A   4     2496    714    774     51     79    224       C  
ATOM     84  C   PHE A   4       6.722  10.551   2.415  1.00  9.75           C  
ANISOU   84  C   PHE A   4     2393    609    701    -80    167    139       C  
ATOM     85  O   PHE A   4       6.019   9.994   3.256  1.00 10.85           O  
ANISOU   85  O   PHE A   4     2524    790    806    -90     91    174       O  
ATOM     86  CB  PHE A   4       8.609  11.442   3.712  1.00 11.06           C  
ANISOU   86  CB  PHE A   4     2418    815    968     30    -24     24       C  
ATOM     87  CG  PHE A   4      10.025  11.346   4.130  1.00 10.85           C  
ANISOU   87  CG  PHE A   4     2328    924    868     96    -45      1       C  
ATOM     88  CD1 PHE A   4      10.405  10.322   4.992  1.00 12.76           C  
ANISOU   88  CD1 PHE A   4     2413   1322   1111    -80   -104    -36       C  
ATOM     89  CD2 PHE A   4      10.970  12.246   3.761  1.00 14.35           C  
ANISOU   89  CD2 PHE A   4     2648   1483   1321   -213   -250    339       C  
ATOM     90  CE1 PHE A   4      11.707  10.166   5.417  1.00 13.55           C  
ANISOU   90  CE1 PHE A   4     2637   1477   1034     -8      0    126       C  
ATOM     91  CE2 PHE A   4      12.317  12.090   4.161  1.00 15.38           C  
ANISOU   91  CE2 PHE A   4     2778   1543   1523   -408    136    310       C  
ATOM     92  CZ  PHE A   4      12.666  11.050   4.993  1.00 13.13           C  
ANISOU   92  CZ  PHE A   4     2340   1521   1128     84    -13   -168       C  
ATOM     93  N   VAL A   5       6.221  11.267   1.427  1.00 10.05           N  
ANISOU   93  N   VAL A   5     2495    686    636    -73     63    148       N  
ATOM     94  CA  VAL A   5       4.798  11.479   1.342  1.00 10.42           C  
ANISOU   94  CA  VAL A   5     2423    795    739    -69     63    -17       C  
ATOM     95  C   VAL A   5       4.051  10.211   1.022  1.00 10.98           C  
ANISOU   95  C   VAL A   5     2485    870    816   -139     65   -309       C  
ATOM     96  O   VAL A   5       4.439   9.439   0.164  1.00 13.99           O  
ANISOU   96  O   VAL A   5     2936   1082   1295   -417    452   -491       O  
ATOM     97  CB  VAL A   5       4.539  12.601   0.317  1.00 12.01           C  
ANISOU   97  CB  VAL A   5     2635    966    963    -45     -8    148       C  
ATOM     98  CG1 VAL A   5       3.106  12.649  -0.216  1.00 14.86           C  
ANISOU   98  CG1 VAL A   5     3196   1351   1100    -84   -233     92       C  
ATOM     99  CG2 VAL A   5       5.116  13.933   0.809  1.00 13.29           C  
ANISOU   99  CG2 VAL A   5     2939    695   1414   -131     -2    292       C  
ATOM    100  N   GLY A   6       2.929  10.037   1.672  1.00 10.94           N  
ANISOU  100  N   GLY A   6     2450    900    804   -160    128   -249       N  
ATOM    101  CA  GLY A   6       2.086   8.920   1.431  1.00 11.98           C  
ANISOU  101  CA  GLY A   6     2541   1120    891   -312     35   -267       C  
ATOM    102  C   GLY A   6       1.435   8.420   2.684  1.00 10.18           C  
ANISOU  102  C   GLY A   6     2265    828    774   -116    -84    -48       C  
ATOM    103  O   GLY A   6       1.346   9.120   3.672  1.00 11.89           O  
ANISOU  103  O   GLY A   6     2799    796    920   -304    145   -232       O  
ATOM    104  N   THR A   7       0.931   7.215   2.594  1.00 10.26           N  
ANISOU  104  N   THR A   7     2414    707    774   -116   -226      2       N  
ATOM    105  CA  THR A   7       0.189   6.561   3.634  1.00 10.70           C  
ANISOU  105  CA  THR A   7     2461    654    950    -69   -173      0       C  
ATOM    106  C   THR A   7       0.949   5.290   4.007  1.00 10.28           C  
ANISOU  106  C   THR A   7     2421    687    798   -220    -69     55       C  
ATOM    107  O   THR A   7       1.211   4.461   3.150  1.00 12.26           O  
ANISOU  107  O   THR A   7     2896    854    907     47   -277   -161       O  
ATOM    108  CB  THR A   7      -1.206   6.229   3.146  1.00 12.81           C  
ANISOU  108  CB  THR A   7     2508    973   1385    -36   -128    141       C  
ATOM    109  OG1 THR A   7      -1.776   7.333   2.447  1.00 16.62           O  
ANISOU  109  OG1 THR A   7     2962   1326   2025    -21   -327    241       O  
ATOM    110  CG2 THR A   7      -2.103   5.812   4.269  1.00 16.07           C  
ANISOU  110  CG2 THR A   7     2780   1468   1858    129     68    218       C  
ATOM    111  N   TRP A   8       1.298   5.176   5.276  1.00 10.06           N  
ANISOU  111  N   TRP A   8     2359    764    699   -127     75     70       N  
ATOM    112  CA  TRP A   8       2.214   4.164   5.807  1.00  9.70           C  
ANISOU  112  CA  TRP A   8     2463    585    637     -9      8    112       C  
ATOM    113  C   TRP A   8       1.546   3.416   6.937  1.00 10.00           C  
ANISOU  113  C   TRP A   8     2581    635    580   -128    103     73       C  
ATOM    114  O   TRP A   8       0.736   3.988   7.666  1.00 14.15           O  
ANISOU  114  O   TRP A   8     3308    876   1191    -22    671    182       O  
ATOM    115  CB  TRP A   8       3.435   4.890   6.344  1.00  9.68           C  
ANISOU  115  CB  TRP A   8     2303    792    580     89     31    192       C  
ATOM    116  CG  TRP A   8       4.220   5.699   5.310  1.00  9.50           C  
ANISOU  116  CG  TRP A   8     2432    604    574    -24    -23    111       C  
ATOM    117  CD1 TRP A   8       4.103   7.027   5.072  1.00  9.55           C  
ANISOU  117  CD1 TRP A   8     2359    735    532    -64     82     49       C  
ATOM    118  CD2 TRP A   8       5.185   5.204   4.401  1.00  9.37           C  
ANISOU  118  CD2 TRP A   8     2200    690    667    -91   -144     65       C  
ATOM    119  NE1 TRP A   8       4.934   7.412   4.056  1.00 10.13           N  
ANISOU  119  NE1 TRP A   8     2452    657    738   -130     48     82       N  
ATOM    120  CE2 TRP A   8       5.620   6.302   3.628  1.00  9.70           C  
ANISOU  120  CE2 TRP A   8     2186    923    576   -174     63      9       C  
ATOM    121  CE3 TRP A   8       5.745   3.943   4.151  1.00 10.31           C  
ANISOU  121  CE3 TRP A   8     2323    936    657   -188   -146    -10       C  
ATOM    122  CZ2 TRP A   8       6.616   6.158   2.662  1.00 11.12           C  
ANISOU  122  CZ2 TRP A   8     2365    995    861   -270     26    -64       C  
ATOM    123  CZ3 TRP A   8       6.698   3.812   3.210  1.00 10.79           C  
ANISOU  123  CZ3 TRP A   8     2313    990    796   -108    -72   -148       C  
ATOM    124  CH2 TRP A   8       7.114   4.884   2.455  1.00 11.77           C  
ANISOU  124  CH2 TRP A   8     2308   1386    779   -237    150   -304       C  
ATOM    125  N   LYS A   9       1.872   2.164   7.086  1.00  9.54           N  
ANISOU  125  N   LYS A   9     2392    617    616   -152    -63    194       N  
ATOM    126  CA  LYS A   9       1.321   1.341   8.149  1.00 10.46           C  
ANISOU  126  CA  LYS A   9     2276    824    873   -103    -48    205       C  
ATOM    127  C   LYS A   9       2.459   0.676   8.917  1.00  9.98           C  
ANISOU  127  C   LYS A   9     2212    795    784   -210     26    189       C  
ATOM    128  O   LYS A   9       3.416   0.178   8.315  1.00 10.18           O  
ANISOU  128  O   LYS A   9     2333    806    726    -69    -17    137       O  
ATOM    129  CB  LYS A   9       0.395   0.282   7.577  1.00 12.32           C  
ANISOU  129  CB  LYS A   9     2424   1003   1252   -378   -256    450       C  
ATOM    130  CG  LYS A   9       0.951  -0.672   6.629  1.00 18.74           C  
ANISOU  130  CG  LYS A   9     3434   1578   2108   -508   -368    140       C  
ATOM    131  CD  LYS A   9      -0.097  -1.660   6.213  1.00 24.47           C  
ANISOU  131  CD  LYS A   9     3808   2436   3050   -581   -524   -282       C  
ATOM    132  CE  LYS A   9       0.439  -2.706   5.295  1.00 26.43           C  
ANISOU  132  CE  LYS A   9     3993   2215   3831   -831   -543   -646       C  
ATOM    133  NZ  LYS A   9       0.555  -2.172   3.905  1.00 33.37           N  
ANISOU  133  NZ  LYS A   9     4648   3516   4514   -271   -318     87       N  
ATOM    134  N   LEU A  10       2.397   0.686  10.238  1.00 10.56           N  
ANISOU  134  N   LEU A  10     2154   1125    733   -184     13    289       N  
ATOM    135  CA  LEU A  10       3.447   0.048  11.055  1.00 10.43           C  
ANISOU  135  CA  LEU A  10     2126   1107    728   -310    -43    222       C  
ATOM    136  C   LEU A  10       3.403  -1.464  10.864  1.00 11.22           C  
ANISOU  136  C   LEU A  10     2387   1032    844   -381   -143    298       C  
ATOM    137  O   LEU A  10       2.345  -2.053  11.078  1.00 13.82           O  
ANISOU  137  O   LEU A  10     2403   1390   1455   -559   -192    463       O  
ATOM    138  CB  LEU A  10       3.245   0.393  12.529  1.00 11.23           C  
ANISOU  138  CB  LEU A  10     2147   1413    706   -142      1    304       C  
ATOM    139  CG  LEU A  10       4.329  -0.173  13.464  1.00 11.67           C  
ANISOU  139  CG  LEU A  10     2263   1459    711   -241    -19    247       C  
ATOM    140  CD1 LEU A  10       5.633   0.506  13.259  1.00 12.26           C  
ANISOU  140  CD1 LEU A  10     2038   1658    963    -71     23     86       C  
ATOM    141  CD2 LEU A  10       3.898  -0.053  14.925  1.00 16.13           C  
ANISOU  141  CD2 LEU A  10     2366   2841    920     72    -23    310       C  
ATOM    142  N   VAL A  11       4.558  -2.045  10.538  1.00 11.45           N  
ANISOU  142  N   VAL A  11     2479    865   1003   -381   -314    254       N  
ATOM    143  CA  VAL A  11       4.673  -3.488  10.389  1.00 13.24           C  
ANISOU  143  CA  VAL A  11     2963    790   1275   -270   -427    210       C  
ATOM    144  C   VAL A  11       5.612  -4.185  11.377  1.00 14.07           C  
ANISOU  144  C   VAL A  11     3077    820   1448   -274   -484    426       C  
ATOM    145  O   VAL A  11       5.492  -5.378  11.551  1.00 18.26           O  
ANISOU  145  O   VAL A  11     3699    934   2302   -382  -1097    541       O  
ATOM    146  CB  VAL A  11       5.012  -3.906   8.986  1.00 14.05           C  
ANISOU  146  CB  VAL A  11     3091    710   1537    -92   -407     10       C  
ATOM    147  CG1 VAL A  11       3.932  -3.451   8.037  1.00 16.46           C  
ANISOU  147  CG1 VAL A  11     3556   1130   1567     68   -495    -94       C  
ATOM    148  CG2 VAL A  11       6.411  -3.500   8.514  1.00 16.84           C  
ANISOU  148  CG2 VAL A  11     3471   1368   1559      0     26   -388       C  
ATOM    149  N   SER A  12       6.566  -3.472  11.977  1.00 12.54           N  
ANISOU  149  N   SER A  12     2872    709   1181   -185   -473    182       N  
ATOM    150  CA  SER A  12       7.388  -4.107  12.960  1.00 13.14           C  
ANISOU  150  CA  SER A  12     2818    940   1232    -63   -450    249       C  
ATOM    151  C   SER A  12       7.901  -3.055  13.919  1.00 11.80           C  
ANISOU  151  C   SER A  12     2430    951   1100   -154   -367    329       C  
ATOM    152  O   SER A  12       8.052  -1.881  13.572  1.00 11.52           O  
ANISOU  152  O   SER A  12     2597    822    959   -293   -245    393       O  
ATOM    153  CB  SER A  12       8.526  -4.860  12.337  1.00 16.52           C  
ANISOU  153  CB  SER A  12     3016   1588   1673    155   -561    132       C  
ATOM    154  OG  SER A  12       9.492  -4.040  11.817  1.00 18.53           O  
ANISOU  154  OG  SER A  12     3408   1960   1670    376   -281    339       O  
ATOM    155  N   SER A  13       8.186  -3.529  15.122  1.00 12.35           N  
ANISOU  155  N   SER A  13     2682    854   1155   -318   -464    468       N  
ATOM    156  CA  SER A  13       8.747  -2.675  16.131  1.00 13.05           C  
ANISOU  156  CA  SER A  13     2833   1028   1098   -325   -395    495       C  
ATOM    157  C   SER A  13       9.703  -3.472  17.005  1.00 12.78           C  
ANISOU  157  C   SER A  13     2790    931   1133   -202   -446    568       C  
ATOM    158  O   SER A  13       9.407  -4.605  17.363  1.00 16.35           O  
ANISOU  158  O   SER A  13     3194   1199   1819   -395   -765    868       O  
ATOM    159  CB  SER A  13       7.561  -2.157  16.965  1.00 14.64           C  
ANISOU  159  CB  SER A  13     3059   1208   1294   -271   -487    403       C  
ATOM    160  OG  SER A  13       7.931  -1.276  18.008  1.00 16.58           O  
ANISOU  160  OG  SER A  13     3789   1268   1243   -265   -696    283       O  
ATOM    161  N  AGLU A  14      10.792  -2.842  17.367  0.33  8.30           N  
ANISOU  161  N  AGLU A  14     2356    366    430   -271   -329     93       N  
ATOM    162  N  CGLU A  14      10.881  -2.916  17.288  0.33  9.83           N  
ANISOU  162  N  CGLU A  14     2425    606    703    -99   -264    385       N  
ATOM    163  CA AGLU A  14      11.747  -3.447  18.220  0.50 10.27           C  
ANISOU  163  CA AGLU A  14     2606    416    880    107   -203   -160       C  
ATOM    164  CA CGLU A  14      11.922  -3.499  18.167  0.50 12.39           C  
ANISOU  164  CA CGLU A  14     2654    924   1126    104   -274    158       C  
ATOM    165  C   GLU A  14      12.151  -2.522  19.298  1.00  9.93           C  
ANISOU  165  C   GLU A  14     2348    562    861    139   -199    129       C  
ATOM    166  O   GLU A  14      12.436  -1.349  19.042  1.00 10.53           O  
ANISOU  166  O   GLU A  14     2599    530    872     38   -188     95       O  
ATOM    167  CB AGLU A  14      12.990  -3.853  17.426  0.50 12.87           C  
ANISOU  167  CB AGLU A  14     2654    975   1257    187   -143   -207       C  
ATOM    168  CB CGLU A  14      13.254  -3.804  17.384  0.50 14.57           C  
ANISOU  168  CB CGLU A  14     2830   1269   1435    196   -180     -3       C  
ATOM    169  CG AGLU A  14      12.826  -5.013  16.505  0.50 13.75           C  
ANISOU  169  CG AGLU A  14     2890    846   1488    319    -89   -724       C  
ATOM    170  CG CGLU A  14      14.633  -3.703  18.184  0.50 20.78           C  
ANISOU  170  CG CGLU A  14     2975   2606   2312    140   -144     47       C  
ATOM    171  CD AGLU A  14      12.756  -6.416  17.187  0.50 14.32           C  
ANISOU  171  CD AGLU A  14     2774    758   1906    182   -230   -428       C  
ATOM    172  CD CGLU A  14      15.385  -5.030  18.566  0.50 22.69           C  
ANISOU  172  CD CGLU A  14     3124   2687   2810    -18   -140    148       C  
ATOM    173  OE1AGLU A  14      13.002  -6.528  18.394  0.50 16.14           O  
ANISOU  173  OE1AGLU A  14     2883   1205   2045    193   -664   -140       O  
ATOM    174  OE1CGLU A  14      16.336  -5.511  17.858  0.50 19.57           O  
ANISOU  174  OE1CGLU A  14     2723   1278   3433    295   -444   -229       O  
ATOM    175  OE2AGLU A  14      12.462  -7.381  16.469  0.50 17.38           O  
ANISOU  175  OE2AGLU A  14     2928   1148   2526     67   -237   -700       O  
ATOM    176  OE2CGLU A  14      15.131  -5.551  19.686  0.50 21.20           O  
ANISOU  176  OE2CGLU A  14     2849   3302   1902   -189   -772    510       O  
ATOM    177  N   ASN A  15      12.145  -3.018  20.525  1.00  9.79           N  
ANISOU  177  N   ASN A  15     2336    514    870     14   -196    141       N  
ATOM    178  CA AASN A  15      12.665  -2.288  21.687  0.50  8.84           C  
ANISOU  178  CA AASN A  15     2169    494    695     57   -111    159       C  
ATOM    179  CA BASN A  15      12.617  -2.315  21.699  0.50 10.52           C  
ANISOU  179  CA BASN A  15     2326    710    960     11    -95     87       C  
ATOM    180  C   ASN A  15      11.836  -1.060  22.049  1.00  9.62           C  
ANISOU  180  C   ASN A  15     2188    620    845    -43    -83     41       C  
ATOM    181  O   ASN A  15      12.312  -0.207  22.776  1.00 10.04           O  
ANISOU  181  O   ASN A  15     2223    701    888     19    -38     83       O  
ATOM    182  CB AASN A  15      14.137  -1.881  21.558  0.50  8.44           C  
ANISOU  182  CB AASN A  15     2103    597    507    150    -64     50       C  
ATOM    183  CB BASN A  15      14.109  -2.083  21.624  0.50 11.67           C  
ANISOU  183  CB BASN A  15     2433    888   1112    -54    -74    159       C  
ATOM    184  CG AASN A  15      14.906  -1.956  22.895  0.50  8.39           C  
ANISOU  184  CG AASN A  15     1875    708    605    191    -63    208       C  
ATOM    185  CG BASN A  15      14.858  -3.389  21.548  0.50 15.76           C  
ANISOU  185  CG BASN A  15     2617   1660   1711     51    169   -369       C  
ATOM    186  OD1AASN A  15      14.741  -2.878  23.700  0.50  9.53           O  
ANISOU  186  OD1AASN A  15     2177    611    831    -53   -133    384       O  
ATOM    187  OD1BASN A  15      14.866  -4.159  22.502  0.50 19.64           O  
ANISOU  187  OD1BASN A  15     2992   2070   2399     51     45   -239       O  
ATOM    188  ND2AASN A  15      15.741  -0.947  23.114  0.50  8.32           N  
ANISOU  188  ND2AASN A  15     1826    548    784     29    -81    139       N  
ATOM    189  ND2BASN A  15      15.427  -3.670  20.410  0.50 17.03           N  
ANISOU  189  ND2BASN A  15     3267   1237   1965   -193    389   -361       N  
ATOM    190  N   PHE A  16      10.582  -1.010  21.607  1.00  9.90           N  
ANISOU  190  N   PHE A  16     2217    578    966     16    -76      1       N  
ATOM    191  CA  PHE A  16       9.758   0.175  21.869  1.00 10.07           C  
ANISOU  191  CA  PHE A  16     2158    708    959    -45    -77     23       C  
ATOM    192  C   PHE A  16       9.395   0.307  23.323  1.00 10.01           C  
ANISOU  192  C   PHE A  16     2073    894    836    -36    -23    108       C  
ATOM    193  O   PHE A  16       9.327   1.425  23.841  1.00  9.93           O  
ANISOU  193  O   PHE A  16     2224    677    870    -35    -61     26       O  
ATOM    194  CB  PHE A  16       8.543   0.180  20.950  1.00 10.41           C  
ANISOU  194  CB  PHE A  16     2174    753   1027     -3    -95     11       C  
ATOM    195  CG  PHE A  16       7.778   1.505  20.919  1.00 11.08           C  
ANISOU  195  CG  PHE A  16     2314   1094    801    126   -143    -51       C  
ATOM    196  CD1 PHE A  16       8.402   2.667  20.550  1.00 12.38           C  
ANISOU  196  CD1 PHE A  16     2619   1015   1068    350   -282    -22       C  
ATOM    197  CD2 PHE A  16       6.433   1.529  21.181  1.00 12.86           C  
ANISOU  197  CD2 PHE A  16     2429   1523    934    323    -93    -55       C  
ATOM    198  CE1 PHE A  16       7.699   3.895  20.466  1.00 13.70           C  
ANISOU  198  CE1 PHE A  16     2934   1113   1157    188   -449    -43       C  
ATOM    199  CE2 PHE A  16       5.725   2.745  21.093  1.00 14.86           C  
ANISOU  199  CE2 PHE A  16     2492   2152   1000    729     53   -319       C  
ATOM    200  CZ  PHE A  16       6.398   3.880  20.737  1.00 14.55           C  
ANISOU  200  CZ  PHE A  16     2890   1578   1060    588   -425   -247       C  
ATOM    201  N   ASP A  17       9.173  -0.816  24.017  1.00 11.01           N  
ANISOU  201  N   ASP A  17     2478    673   1029    -98    119    152       N  
ATOM    202  CA  ASP A  17       8.863  -0.720  25.440  1.00 11.79           C  
ANISOU  202  CA  ASP A  17     2562    906   1009    -92     34    300       C  
ATOM    203  C   ASP A  17      10.029  -0.105  26.211  1.00 11.26           C  
ANISOU  203  C   ASP A  17     2474    753   1049    -40     53    496       C  
ATOM    204  O   ASP A  17       9.831   0.775  27.048  1.00 11.53           O  
ANISOU  204  O   ASP A  17     2652    863    863    -63    127    197       O  
ATOM    205  CB  ASP A  17       8.500  -2.091  25.990  1.00 13.18           C  
ANISOU  205  CB  ASP A  17     2841    971   1195   -144     71    262       C  
ATOM    206  CG  ASP A  17       7.965  -2.004  27.383  1.00 15.52           C  
ANISOU  206  CG  ASP A  17     3130   1282   1482   -277    228    479       C  
ATOM    207  OD1 ASP A  17       8.594  -2.575  28.277  1.00 21.98           O  
ANISOU  207  OD1 ASP A  17     3590   2933   1828    132    247    722       O  
ATOM    208  OD2 ASP A  17       6.941  -1.367  27.626  1.00 17.23           O  
ANISOU  208  OD2 ASP A  17     3416   1672   1457     25    485    380       O  
ATOM    209  N   ASP A  18      11.248  -0.523  25.903  1.00 11.82           N  
ANISOU  209  N   ASP A  18     2445    751   1292     64     30    379       N  
ATOM    210  CA  ASP A  18      12.382   0.025  26.574  1.00 12.86           C  
ANISOU  210  CA  ASP A  18     2401   1107   1375    162   -168    493       C  
ATOM    211  C   ASP A  18      12.611   1.478  26.244  1.00 11.12           C  
ANISOU  211  C   ASP A  18     2212    887   1123    124    -33    284       C  
ATOM    212  O   ASP A  18      12.987   2.274  27.110  1.00 11.78           O  
ANISOU  212  O   ASP A  18     2422   1142    910     92   -110    248       O  
ATOM    213  CB  ASP A  18      13.623  -0.793  26.289  1.00 16.11           C  
ANISOU  213  CB  ASP A  18     2596   1319   2205    160     13    582       C  
ATOM    214  CG  ASP A  18      13.661  -2.098  27.163  1.00 25.09           C  
ANISOU  214  CG  ASP A  18     3523   3010   2998    420   -253    869       C  
ATOM    215  OD1 ASP A  18      12.982  -2.238  28.168  1.00 32.08           O  
ANISOU  215  OD1 ASP A  18     4814   3044   4329    421    -34   1995       O  
ATOM    216  OD2 ASP A  18      14.296  -3.033  26.791  1.00 30.88           O  
ANISOU  216  OD2 ASP A  18     5332   2751   3647    331   -560   1705       O  
ATOM    217  N   TYR A  19      12.371   1.880  24.996  1.00  9.83           N  
ANISOU  217  N   TYR A  19     2184    758    792    -16      9    159       N  
ATOM    218  CA  TYR A  19      12.411   3.288  24.642  1.00  9.41           C  
ANISOU  218  CA  TYR A  19     2172    701    703    -64      0    172       C  
ATOM    219  C   TYR A  19      11.418   4.096  25.462  1.00  9.30           C  
ANISOU  219  C   TYR A  19     2105    875    552    -12     61    175       C  
ATOM    220  O   TYR A  19      11.756   5.134  26.053  1.00  9.68           O  
ANISOU  220  O   TYR A  19     2293    788    595   -126    -43      6       O  
ATOM    221  CB  TYR A  19      12.182   3.465  23.137  1.00  9.51           C  
ANISOU  221  CB  TYR A  19     2111    810    691    -84     44    -36       C  
ATOM    222  CG  TYR A  19      11.983   4.904  22.721  1.00  9.38           C  
ANISOU  222  CG  TYR A  19     2140    854    569    -51     91    -39       C  
ATOM    223  CD1 TYR A  19      13.065   5.792  22.649  1.00  9.35           C  
ANISOU  223  CD1 TYR A  19     2152    725    674   -163     41     29       C  
ATOM    224  CD2 TYR A  19      10.696   5.362  22.467  1.00  9.49           C  
ANISOU  224  CD2 TYR A  19     2185    852    567   -201      3     70       C  
ATOM    225  CE1 TYR A  19      12.837   7.138  22.354  1.00  9.45           C  
ANISOU  225  CE1 TYR A  19     2190    748    650   -184     84     39       C  
ATOM    226  CE2 TYR A  19      10.491   6.700  22.144  1.00 10.21           C  
ANISOU  226  CE2 TYR A  19     2047   1130    699    -63      4     63       C  
ATOM    227  CZ  TYR A  19      11.552   7.571  22.085  1.00  9.62           C  
ANISOU  227  CZ  TYR A  19     2260    882    512    -75    -27     -9       C  
ATOM    228  OH  TYR A  19      11.323   8.911  21.794  1.00 10.61           O  
ANISOU  228  OH  TYR A  19     2441    783    804     49    -28    151       O  
ATOM    229  N   MET A  20      10.179   3.634  25.500  1.00  9.03           N  
ANISOU  229  N   MET A  20     2168    658    604    -66     26     50       N  
ATOM    230  CA  MET A  20       9.161   4.323  26.255  1.00  9.55           C  
ANISOU  230  CA  MET A  20     2140    808    678    -63     27    167       C  
ATOM    231  C   MET A  20       9.544   4.411  27.746  1.00 10.04           C  
ANISOU  231  C   MET A  20     2265    937    611   -221     52    114       C  
ATOM    232  O   MET A  20       9.317   5.441  28.385  1.00 10.52           O  
ANISOU  232  O   MET A  20     2392    993    611   -207     -4    -40       O  
ATOM    233  CB  MET A  20       7.779   3.697  26.102  1.00  9.70           C  
ANISOU  233  CB  MET A  20     2179    902    602    -71     58     74       C  
ATOM    234  CG  MET A  20       7.158   3.908  24.717  1.00 10.04           C  
ANISOU  234  CG  MET A  20     2177    956    680    108    110    133       C  
ATOM    235  SD  MET A  20       5.433   3.368  24.667  1.00 12.06           S  
ANISOU  235  SD  MET A  20     2269   1571    742    -18     14    -31       S  
ATOM    236  CE  MET A  20       5.672   1.577  24.691  1.00 13.30           C  
ANISOU  236  CE  MET A  20     2340   1717    996   -209     -5    -87       C  
ATOM    237  N   LYS A  21      10.103   3.344  28.312  1.00 10.62           N  
ANISOU  237  N   LYS A  21     2404   1062    569   -103     59    199       N  
ATOM    238  CA  LYS A  21      10.530   3.379  29.697  1.00 12.33           C  
ANISOU  238  CA  LYS A  21     2672   1409    603   -270     65    362       C  
ATOM    239  C   LYS A  21      11.571   4.457  29.892  1.00 12.82           C  
ANISOU  239  C   LYS A  21     2653   1574    642   -213    -96    263       C  
ATOM    240  O   LYS A  21      11.516   5.206  30.902  1.00 14.05           O  
ANISOU  240  O   LYS A  21     3066   1569    701   -318    -79    131       O  
ATOM    241  CB  LYS A  21      11.110   2.041  30.149  1.00 13.35           C  
ANISOU  241  CB  LYS A  21     2803   1595    673   -110     20    542       C  
ATOM    242  CG  LYS A  21      10.199   0.902  30.349  1.00 15.03           C  
ANISOU  242  CG  LYS A  21     2778   1667   1265   -101     87    747       C  
ATOM    243  CD  LYS A  21      10.880  -0.274  30.930  1.00 18.06           C  
ANISOU  243  CD  LYS A  21     3284   1790   1786     96     75    904       C  
ATOM    244  CE  LYS A  21       9.950  -1.349  31.235  1.00 22.74           C  
ANISOU  244  CE  LYS A  21     3447   2534   2656    153    -50   1060       C  
ATOM    245  NZ  LYS A  21      10.575  -2.433  31.880  1.00 27.32           N  
ANISOU  245  NZ  LYS A  21     4121   2843   3416    317   -107   1185       N  
ATOM    246  N   GLU A  22      12.515   4.555  28.971  1.00 12.32           N  
ANISOU  246  N   GLU A  22     2532   1439    710   -253   -159    175       N  
ATOM    247  CA  GLU A  22      13.595   5.507  29.102  1.00 13.16           C  
ANISOU  247  CA  GLU A  22     2548   1651    800   -286   -209    178       C  
ATOM    248  C   GLU A  22      13.034   6.950  29.038  1.00 12.69           C  
ANISOU  248  C   GLU A  22     2605   1710    506   -473   -148      4       C  
ATOM    249  O   GLU A  22      13.495   7.838  29.735  1.00 14.73           O  
ANISOU  249  O   GLU A  22     2945   1785    866   -585   -321    -22       O  
ATOM    250  CB  GLU A  22      14.667   5.257  28.045  1.00 13.57           C  
ANISOU  250  CB  GLU A  22     2503   1607   1045   -261   -214    103       C  
ATOM    251  CG  GLU A  22      16.019   5.747  28.354  1.00 16.53           C  
ANISOU  251  CG  GLU A  22     2626   2180   1474   -132   -205     93       C  
ATOM    252  CD  GLU A  22      16.758   4.901  29.432  1.00 16.69           C  
ANISOU  252  CD  GLU A  22     2821   1787   1734     53   -375    532       C  
ATOM    253  OE1 GLU A  22      16.288   3.851  29.886  1.00 20.87           O  
ANISOU  253  OE1 GLU A  22     3491   2431   2006     77   -494    703       O  
ATOM    254  OE2 GLU A  22      17.902   5.317  29.772  1.00 21.94           O  
ANISOU  254  OE2 GLU A  22     3069   2977   2289     87   -547   -121       O  
ATOM    255  N   VAL A  23      12.017   7.173  28.184  1.00 11.50           N  
ANISOU  255  N   VAL A  23     2644   1063    663   -316    -88     49       N  
ATOM    256  CA  VAL A  23      11.351   8.420  28.052  1.00 11.97           C  
ANISOU  256  CA  VAL A  23     2721   1073    751   -336    -66     57       C  
ATOM    257  C   VAL A  23      10.587   8.828  29.345  1.00 12.55           C  
ANISOU  257  C   VAL A  23     2881   1235    650   -303    -23    -51       C  
ATOM    258  O   VAL A  23      10.483   9.998  29.638  1.00 15.04           O  
ANISOU  258  O   VAL A  23     3552   1125   1036   -317    212   -176       O  
ATOM    259  CB  VAL A  23      10.409   8.402  26.822  1.00 11.61           C  
ANISOU  259  CB  VAL A  23     2651   1008    750   -244    -90     48       C  
ATOM    260  CG1 VAL A  23       9.456   9.588  26.796  1.00 13.06           C  
ANISOU  260  CG1 VAL A  23     3000    896   1065   -174   -142    -43       C  
ATOM    261  CG2 VAL A  23      11.216   8.363  25.551  1.00 12.15           C  
ANISOU  261  CG2 VAL A  23     2783   1063    766    -77     36     71       C  
ATOM    262  N   GLY A  24      10.101   7.830  30.057  1.00 12.38           N  
ANISOU  262  N   GLY A  24     2830   1198    675   -451     17    -18       N  
ATOM    263  CA  GLY A  24       9.353   8.021  31.287  1.00 12.95           C  
ANISOU  263  CA  GLY A  24     2778   1436    704   -288    -38    -61       C  
ATOM    264  C   GLY A  24       7.880   7.661  31.207  1.00 12.26           C  
ANISOU  264  C   GLY A  24     2886   1167    604   -254    179    -95       C  
ATOM    265  O   GLY A  24       7.122   8.023  32.106  1.00 14.56           O  
ANISOU  265  O   GLY A  24     3131   1532    867   -407    239   -318       O  
ATOM    266  N   VAL A  25       7.478   6.899  30.208  1.00 10.90           N  
ANISOU  266  N   VAL A  25     2605    829    708   -107     48    -13       N  
ATOM    267  CA  VAL A  25       6.092   6.532  30.060  1.00 11.00           C  
ANISOU  267  CA  VAL A  25     2445    895    837    -32     64    -43       C  
ATOM    268  C   VAL A  25       5.733   5.504  31.104  1.00 11.44           C  
ANISOU  268  C   VAL A  25     2521   1118    706   -112     -5    -79       C  
ATOM    269  O   VAL A  25       6.472   4.547  31.339  1.00 12.12           O  
ANISOU  269  O   VAL A  25     2773   1064    767   -213    -25    128       O  
ATOM    270  CB  VAL A  25       5.851   5.935  28.656  1.00 10.88           C  
ANISOU  270  CB  VAL A  25     2426    971    735     -9    -38     11       C  
ATOM    271  CG1 VAL A  25       4.397   5.637  28.454  1.00 12.31           C  
ANISOU  271  CG1 VAL A  25     2468   1200   1007    -66    -45    -79       C  
ATOM    272  CG2 VAL A  25       6.360   6.887  27.558  1.00 12.31           C  
ANISOU  272  CG2 VAL A  25     2924    890    860     -9   -104    204       C  
ATOM    273  N   GLY A  26       4.569   5.670  31.724  1.00 12.98           N  
ANISOU  273  N   GLY A  26     2541   1478    911   -267     75   -193       N  
ATOM    274  CA  GLY A  26       4.087   4.751  32.739  1.00 13.62           C  
ANISOU  274  CA  GLY A  26     2636   1785    752   -395    154   -142       C  
ATOM    275  C   GLY A  26       3.581   3.438  32.210  1.00 12.39           C  
ANISOU  275  C   GLY A  26     2495   1564    647   -433     78   -130       C  
ATOM    276  O   GLY A  26       3.327   3.269  31.040  1.00 12.67           O  
ANISOU  276  O   GLY A  26     2776   1458    576   -413     37   -119       O  
ATOM    277  N   PHE A  27       3.363   2.506  33.123  1.00 12.81           N  
ANISOU  277  N   PHE A  27     2728   1636    503   -397    -27    -29       N  
ATOM    278  CA  PHE A  27       3.090   1.127  32.763  1.00 12.61           C  
ANISOU  278  CA  PHE A  27     2588   1502    698   -258     22     60       C  
ATOM    279  C   PHE A  27       1.858   1.008  31.844  1.00 11.87           C  
ANISOU  279  C   PHE A  27     2588   1223    698   -376     72    146       C  
ATOM    280  O   PHE A  27       1.927   0.390  30.776  1.00 12.26           O  
ANISOU  280  O   PHE A  27     2676   1353    627   -334    -68     40       O  
ATOM    281  CB  PHE A  27       2.851   0.303  34.049  1.00 13.47           C  
ANISOU  281  CB  PHE A  27     2658   1655    804   -155     16    193       C  
ATOM    282  CG  PHE A  27       2.447  -1.138  33.772  1.00 13.89           C  
ANISOU  282  CG  PHE A  27     2756   1765    754   -359   -125    352       C  
ATOM    283  CD1 PHE A  27       3.401  -2.133  33.652  1.00 16.14           C  
ANISOU  283  CD1 PHE A  27     3055   1886   1189   -323    -89    265       C  
ATOM    284  CD2 PHE A  27       1.124  -1.472  33.646  1.00 16.01           C  
ANISOU  284  CD2 PHE A  27     2827   1873   1382   -264   -441    814       C  
ATOM    285  CE1 PHE A  27       3.012  -3.463  33.390  1.00 17.39           C  
ANISOU  285  CE1 PHE A  27     3344   1684   1576   -281     48    318       C  
ATOM    286  CE2 PHE A  27       0.747  -2.807  33.364  1.00 17.02           C  
ANISOU  286  CE2 PHE A  27     3061   2117   1287   -614   -461    724       C  
ATOM    287  CZ  PHE A  27       1.688  -3.739  33.210  1.00 17.73           C  
ANISOU  287  CZ  PHE A  27     3460   1995   1278   -643   -349    352       C  
ATOM    288  N   ALA A  28       0.718   1.556  32.257  1.00 12.55           N  
ANISOU  288  N   ALA A  28     2706   1349    710   -285     69     76       N  
ATOM    289  CA  ALA A  28      -0.507   1.305  31.490  1.00 12.99           C  
ANISOU  289  CA  ALA A  28     2601   1355    979   -321    115     71       C  
ATOM    290  C   ALA A  28      -0.399   1.921  30.114  1.00 12.36           C  
ANISOU  290  C   ALA A  28     2563   1174    957   -138     88     54       C  
ATOM    291  O   ALA A  28      -0.860   1.339  29.115  1.00 13.77           O  
ANISOU  291  O   ALA A  28     2663   1604    964   -397   -138     10       O  
ATOM    292  CB  ALA A  28      -1.710   1.818  32.214  1.00 15.15           C  
ANISOU  292  CB  ALA A  28     2839   1495   1420   -181    338    198       C  
ATOM    293  N   THR A  29       0.150   3.141  30.017  1.00 11.96           N  
ANISOU  293  N   THR A  29     2603   1071    869   -202     -9    -12       N  
ATOM    294  CA  THR A  29       0.326   3.770  28.739  1.00 11.78           C  
ANISOU  294  CA  THR A  29     2500   1045    930   -166   -148     58       C  
ATOM    295  C   THR A  29       1.273   2.943  27.868  1.00 11.57           C  
ANISOU  295  C   THR A  29     2401   1100    893   -328     10    -51       C  
ATOM    296  O   THR A  29       1.005   2.778  26.683  1.00 12.24           O  
ANISOU  296  O   THR A  29     2649   1334    666   -256   -148    -80       O  
ATOM    297  CB  THR A  29       0.794   5.228  28.879  1.00 12.80           C  
ANISOU  297  CB  THR A  29     2571   1141   1151    -78   -152     70       C  
ATOM    298  OG1 THR A  29      -0.196   5.969  29.619  1.00 15.68           O  
ANISOU  298  OG1 THR A  29     2907   1401   1649      4    132    -11       O  
ATOM    299  CG2 THR A  29       0.998   5.868  27.542  1.00 14.91           C  
ANISOU  299  CG2 THR A  29     2978   1129   1557   -170   -257    414       C  
ATOM    300  N   ARG A  30       2.371   2.427  28.423  1.00 11.10           N  
ANISOU  300  N   ARG A  30     2400   1160    656   -286   -122     50       N  
ATOM    301  CA  ARG A  30       3.274   1.609  27.607  1.00 10.80           C  
ANISOU  301  CA  ARG A  30     2270   1309    522   -219     15     54       C  
ATOM    302  C   ARG A  30       2.560   0.403  27.070  1.00 10.58           C  
ANISOU  302  C   ARG A  30     2235   1191    594   -169   -125     10       C  
ATOM    303  O   ARG A  30       2.787   0.029  25.914  1.00 11.08           O  
ANISOU  303  O   ARG A  30     2280   1278    653   -205    -16     64       O  
ATOM    304  CB  ARG A  30       4.542   1.090  28.359  1.00 11.58           C  
ANISOU  304  CB  ARG A  30     2493   1302    602   -313    -59     98       C  
ATOM    305  CG  ARG A  30       5.499   2.191  28.743  1.00 11.48           C  
ANISOU  305  CG  ARG A  30     2388   1296    677   -326     68     97       C  
ATOM    306  CD  ARG A  30       6.880   1.648  29.055  1.00 11.25           C  
ANISOU  306  CD  ARG A  30     2378   1239    658   -208     40    109       C  
ATOM    307  NE  ARG A  30       6.837   0.474  29.932  1.00 11.68           N  
ANISOU  307  NE  ARG A  30     2556   1221    658   -185     -3     62       N  
ATOM    308  CZ  ARG A  30       6.692   0.518  31.246  1.00 11.21           C  
ANISOU  308  CZ  ARG A  30     2448   1070    740   -114     67    201       C  
ATOM    309  NH1 ARG A  30       6.573   1.674  31.899  1.00 12.02           N  
ANISOU  309  NH1 ARG A  30     2745   1209    612   -144     26    252       N  
ATOM    310  NH2 ARG A  30       6.645  -0.613  31.916  1.00 13.22           N  
ANISOU  310  NH2 ARG A  30     3027   1276    718     18     77     74       N  
ATOM    311  N   LYS A  31       1.762  -0.261  27.889  1.00 10.98           N  
ANISOU  311  N   LYS A  31     2344   1174    653   -273     18     39       N  
ATOM    312  CA  LYS A  31       1.108  -1.477  27.424  1.00 11.63           C  
ANISOU  312  CA  LYS A  31     2411   1124    882   -155    -26   -129       C  
ATOM    313  C   LYS A  31       0.142  -1.209  26.272  1.00 11.58           C  
ANISOU  313  C   LYS A  31     2199   1328    871   -236    -46   -131       C  
ATOM    314  O   LYS A  31       0.167  -1.918  25.250  1.00 13.40           O  
ANISOU  314  O   LYS A  31     2402   1692    997   -145    -62   -456       O  
ATOM    315  CB  LYS A  31       0.387  -2.212  28.549  1.00 12.61           C  
ANISOU  315  CB  LYS A  31     2675   1189    925   -273     75    -77       C  
ATOM    316  CG  LYS A  31       1.296  -2.704  29.628  1.00 16.33           C  
ANISOU  316  CG  LYS A  31     3217   1710   1276   -178   -114    300       C  
ATOM    317  CD  LYS A  31       2.238  -3.759  29.120  1.00 21.34           C  
ANISOU  317  CD  LYS A  31     3505   2529   2074    465   -240    863       C  
ATOM    318  CE  LYS A  31       3.562  -3.896  29.920  1.00 26.22           C  
ANISOU  318  CE  LYS A  31     3737   3589   2636    349   -112    -38       C  
ATOM    319  NZ  LYS A  31       4.748  -4.334  29.083  1.00 30.32           N  
ANISOU  319  NZ  LYS A  31     3991   4060   3469    364    235   -162       N  
ATOM    320  N   VAL A  32      -0.671  -0.171  26.408  1.00 11.43           N  
ANISOU  320  N   VAL A  32     2149   1380    810   -108    -22   -282       N  
ATOM    321  CA AVAL A  32      -1.660   0.192  25.377  0.50 12.53           C  
ANISOU  321  CA AVAL A  32     2210   1532   1018   -103    -64   -337       C  
ATOM    322  CA BVAL A  32      -1.631   0.077  25.347  0.50 12.94           C  
ANISOU  322  CA BVAL A  32     2199   1681   1036   -144    -72   -258       C  
ATOM    323  C   VAL A  32      -0.962   0.740  24.150  1.00 11.86           C  
ANISOU  323  C   VAL A  32     2112   1525    867    -36   -110   -245       C  
ATOM    324  O   VAL A  32      -1.307   0.426  23.004  1.00 12.88           O  
ANISOU  324  O   VAL A  32     2218   1870    803    -91    -93   -398       O  
ATOM    325  CB AVAL A  32      -2.722   1.220  25.925  0.50 12.84           C  
ANISOU  325  CB AVAL A  32     2195   1406   1276     60     18   -402       C  
ATOM    326  CB BVAL A  32      -2.886   0.816  25.868  0.50 13.69           C  
ANISOU  326  CB BVAL A  32     2119   1992   1091    -70     24   -302       C  
ATOM    327  CG1AVAL A  32      -3.664   1.659  24.826  0.50 13.83           C  
ANISOU  327  CG1AVAL A  32     2155   1737   1363    147     25   -512       C  
ATOM    328  CG1BVAL A  32      -3.595  -0.019  26.954  0.50 14.17           C  
ANISOU  328  CG1BVAL A  32     2139   1719   1524     -6    291   -308       C  
ATOM    329  CG2AVAL A  32      -3.556   0.581  27.048  0.50 15.72           C  
ANISOU  329  CG2AVAL A  32     2575   1905   1493    -57     32   -260       C  
ATOM    330  CG2BVAL A  32      -2.505   2.218  26.389  0.50 15.14           C  
ANISOU  330  CG2BVAL A  32     2546   1878   1326     79    -92   -352       C  
ATOM    331  N   ALA A  33       0.005   1.622  24.351  1.00 11.84           N  
ANISOU  331  N   ALA A  33     2280   1456    762     -1   -240    -91       N  
ATOM    332  CA  ALA A  33       0.706   2.222  23.224  1.00 11.94           C  
ANISOU  332  CA  ALA A  33     2462   1374    701     31   -204     81       C  
ATOM    333  C   ALA A  33       1.480   1.179  22.445  1.00 12.31           C  
ANISOU  333  C   ALA A  33     2429   1487    760    -82   -177    167       C  
ATOM    334  O   ALA A  33       1.598   1.265  21.225  1.00 13.05           O  
ANISOU  334  O   ALA A  33     2825   1518    614    -84    -94    180       O  
ATOM    335  CB  ALA A  33       1.620   3.314  23.691  1.00 13.26           C  
ANISOU  335  CB  ALA A  33     2637   1431    969   -164   -149    187       C  
ATOM    336  N   GLY A  34       2.052   0.184  23.129  1.00 12.46           N  
ANISOU  336  N   GLY A  34     2423   1673    638    188     -1    162       N  
ATOM    337  CA  GLY A  34       2.834  -0.826  22.459  1.00 13.03           C  
ANISOU  337  CA  GLY A  34     2312   1815    824    211      2    244       C  
ATOM    338  C   GLY A  34       2.026  -1.755  21.563  1.00 11.90           C  
ANISOU  338  C   GLY A  34     2351   1452    716    263     99    180       C  
ATOM    339  O   GLY A  34       2.592  -2.277  20.608  1.00 14.67           O  
ANISOU  339  O   GLY A  34     2376   2156   1042    217    163   -116       O  
ATOM    340  N   MET A  35       0.722  -1.883  21.779  1.00 11.72           N  
ANISOU  340  N   MET A  35     2475   1164    814    113    351    385       N  
ATOM    341  CA  MET A  35      -0.125  -2.685  20.890  1.00 11.34           C  
ANISOU  341  CA  MET A  35     2376   1021    909     21    186    190       C  
ATOM    342  C   MET A  35      -0.419  -2.008  19.567  1.00 10.83           C  
ANISOU  342  C   MET A  35     2165    934   1015    -27    225    412       C  
ATOM    343  O   MET A  35      -0.727  -2.670  18.558  1.00 12.85           O  
ANISOU  343  O   MET A  35     2592   1057   1232   -196    -40    248       O  
ATOM    344  CB  MET A  35      -1.456  -3.028  21.555  1.00 12.52           C  
ANISOU  344  CB  MET A  35     2438    808   1509     48    337    350       C  
ATOM    345  CG  MET A  35      -1.351  -3.895  22.782  1.00 12.67           C  
ANISOU  345  CG  MET A  35     2873    858   1081   -300    396    234       C  
ATOM    346  SD  MET A  35      -0.667  -5.500  22.482  1.00 12.89           S  
ANISOU  346  SD  MET A  35     2849    969   1080    106    225    302       S  
ATOM    347  CE  MET A  35      -1.632  -6.211  21.303  1.00 18.60           C  
ANISOU  347  CE  MET A  35     4103   1651   1310    112   -116    640       C  
ATOM    348  N   ALA A  36      -0.401  -0.685  19.543  1.00 10.90           N  
ANISOU  348  N   ALA A  36     2295    861    985   -111     53    418       N  
ATOM    349  CA  ALA A  36      -0.950   0.020  18.401  1.00 11.20           C  
ANISOU  349  CA  ALA A  36     2118   1116   1018   -131    117    433       C  
ATOM    350  C   ALA A  36      -0.122  -0.198  17.154  1.00 10.87           C  
ANISOU  350  C   ALA A  36     2164   1102    861   -200     99    311       C  
ATOM    351  O   ALA A  36       1.114  -0.292  17.188  1.00 12.63           O  
ANISOU  351  O   ALA A  36     2117   1743    938   -102     57    325       O  
ATOM    352  CB  ALA A  36      -0.999   1.488  18.719  1.00 13.76           C  
ANISOU  352  CB  ALA A  36     2882   1151   1196    103    101    388       C  
ATOM    353  N   LYS A  37      -0.808  -0.265  16.039  1.00 10.99           N  
ANISOU  353  N   LYS A  37     2142   1063    969   -222    -16    291       N  
ATOM    354  CA  LYS A  37      -0.209  -0.419  14.708  1.00 11.96           C  
ANISOU  354  CA  LYS A  37     2470   1126    944   -215    106    101       C  
ATOM    355  C   LYS A  37      -0.706   0.763  13.881  1.00 11.43           C  
ANISOU  355  C   LYS A  37     2318   1235    787   -261     55    177       C  
ATOM    356  O   LYS A  37      -1.624   0.624  13.099  1.00 13.17           O  
ANISOU  356  O   LYS A  37     2389   1589   1022   -452   -176    334       O  
ATOM    357  CB  LYS A  37      -0.594  -1.768  14.039  1.00 14.51           C  
ANISOU  357  CB  LYS A  37     2757   1426   1330   -195     63      0       C  
ATOM    358  CG  LYS A  37      -0.012  -2.965  14.746  1.00 17.56           C  
ANISOU  358  CG  LYS A  37     3141   1271   2259   -147    303    132       C  
ATOM    359  CD  LYS A  37       1.472  -3.042  14.523  1.00 20.40           C  
ANISOU  359  CD  LYS A  37     3371   2445   1932    130    100    415       C  
ATOM    360  CE  LYS A  37       2.023  -4.401  14.791  1.00 24.82           C  
ANISOU  360  CE  LYS A  37     3864   2877   2686    246    193    290       C  
ATOM    361  NZ  LYS A  37       1.837  -4.755  16.175  1.00 25.82           N  
ANISOU  361  NZ  LYS A  37     4039   2842   2927    483    292    669       N  
ATOM    362  N   PRO A  38      -0.147   1.927  14.093  1.00 10.97           N  
ANISOU  362  N   PRO A  38     2350   1055    763   -171     49     73       N  
ATOM    363  CA  PRO A  38      -0.721   3.124  13.474  1.00 12.07           C  
ANISOU  363  CA  PRO A  38     2517   1264    805   -119    204    164       C  
ATOM    364  C   PRO A  38      -0.570   3.175  11.976  1.00 11.49           C  
ANISOU  364  C   PRO A  38     2438   1076    851   -248    233     46       C  
ATOM    365  O   PRO A  38       0.329   2.585  11.389  1.00 12.07           O  
ANISOU  365  O   PRO A  38     2565   1137    884   -215    282     51       O  
ATOM    366  CB  PRO A  38       0.092   4.285  14.101  1.00 13.86           C  
ANISOU  366  CB  PRO A  38     3020   1309    938   -142    127   -241       C  
ATOM    367  CG  PRO A  38       0.750   3.759  15.183  1.00 17.49           C  
ANISOU  367  CG  PRO A  38     3123   1567   1952   -408   -223     35       C  
ATOM    368  CD  PRO A  38       0.926   2.304  15.013  1.00 11.98           C  
ANISOU  368  CD  PRO A  38     2411   1297    844   -263     95     32       C  
ATOM    369  N   ASN A  39      -1.440   3.971  11.381  1.00 11.34           N  
ANISOU  369  N   ASN A  39     2603    945    760    -91    278    179       N  
ATOM    370  CA  ASN A  39      -1.268   4.481  10.049  1.00 12.96           C  
ANISOU  370  CA  ASN A  39     3202    869    853    -12    262     67       C  
ATOM    371  C   ASN A  39      -0.770   5.879  10.107  1.00 13.97           C  
ANISOU  371  C   ASN A  39     3517    878    913   -229    515   -104       C  
ATOM    372  O   ASN A  39      -1.292   6.707  10.836  1.00 19.67           O  
ANISOU  372  O   ASN A  39     4280   1146   2044   -571   1476   -393       O  
ATOM    373  CB  ASN A  39      -2.586   4.492   9.335  1.00 16.48           C  
ANISOU  373  CB  ASN A  39     3637   1508   1116    106   -303     74       C  
ATOM    374  CG  ASN A  39      -2.760   3.288   8.555  1.00 20.91           C  
ANISOU  374  CG  ASN A  39     3712   2108   2123    106   -189    115       C  
ATOM    375  OD1 ASN A  39      -2.484   2.168   9.008  1.00 25.82           O  
ANISOU  375  OD1 ASN A  39     4831   2195   2782   -124   -714   -432       O  
ATOM    376  ND2 ASN A  39      -3.130   3.493   7.322  1.00 25.78           N  
ANISOU  376  ND2 ASN A  39     4068   3738   1986    758   -589   -866       N  
ATOM    377  N   MET A  40       0.281   6.144   9.372  1.00 13.14           N  
ANISOU  377  N   MET A  40     3458    728    804   -158    459    -29       N  
ATOM    378  CA  MET A  40       0.877   7.447   9.346  1.00 12.09           C  
ANISOU  378  CA  MET A  40     3020    778    794    -47    353      0       C  
ATOM    379  C   MET A  40       0.752   8.027   7.982  1.00 11.69           C  
ANISOU  379  C   MET A  40     3071    636    735   -217    339     32       C  
ATOM    380  O   MET A  40       1.133   7.396   6.996  1.00 13.11           O  
ANISOU  380  O   MET A  40     3430    727    823    107    437     86       O  
ATOM    381  CB  MET A  40       2.315   7.278   9.733  1.00 12.74           C  
ANISOU  381  CB  MET A  40     3241    803    796   -206    151     86       C  
ATOM    382  CG  MET A  40       3.132   8.555   9.621  1.00 14.05           C  
ANISOU  382  CG  MET A  40     3110    985   1242   -106    -76    312       C  
ATOM    383  SD  MET A  40       4.820   8.449  10.205  1.00 15.72           S  
ANISOU  383  SD  MET A  40     3585   1009   1377   -138   -125    -15       S  
ATOM    384  CE  MET A  40       5.478   7.098   9.278  1.00 16.69           C  
ANISOU  384  CE  MET A  40     3125   1524   1693    -64    -30    118       C  
ATOM    385  N   ILE A  41       0.223   9.234   7.921  1.00 11.50           N  
ANISOU  385  N   ILE A  41     2900    657    810   -184    273    -40       N  
ATOM    386  CA  ILE A  41      -0.003   9.951   6.687  1.00 11.47           C  
ANISOU  386  CA  ILE A  41     2694    748    913    -73    149    -57       C  
ATOM    387  C   ILE A  41       0.917  11.142   6.679  1.00  9.94           C  
ANISOU  387  C   ILE A  41     2631    523    622   -141    -62     66       C  
ATOM    388  O   ILE A  41       0.855  11.985   7.568  1.00 11.18           O  
ANISOU  388  O   ILE A  41     2791    712    745   -279    168   -102       O  
ATOM    389  CB  ILE A  41      -1.510  10.385   6.520  1.00 13.81           C  
ANISOU  389  CB  ILE A  41     2656   1141   1450   -208     -4   -287       C  
ATOM    390  CG1 ILE A  41      -2.488   9.207   6.598  1.00 18.00           C  
ANISOU  390  CG1 ILE A  41     2884   1718   2235   -262    -85   -426       C  
ATOM    391  CG2 ILE A  41      -1.725  11.127   5.214  1.00 16.82           C  
ANISOU  391  CG2 ILE A  41     3002   1667   1720   -104   -292    -72       C  
ATOM    392  CD1 ILE A  41      -3.963   9.672   6.711  1.00 22.89           C  
ANISOU  392  CD1 ILE A  41     3224   2507   2964    124   -257   -278       C  
ATOM    393  N   ILE A  42       1.767  11.225   5.669  1.00  9.92           N  
ANISOU  393  N   ILE A  42     2525    652    589   -103     55    -15       N  
ATOM    394  CA  ILE A  42       2.715  12.315   5.533  1.00  9.31           C  
ANISOU  394  CA  ILE A  42     2403    588    545    -97     53    -28       C  
ATOM    395  C   ILE A  42       2.364  13.062   4.258  1.00  9.28           C  
ANISOU  395  C   ILE A  42     2404    463    659    -98     -1      2       C  
ATOM    396  O   ILE A  42       2.232  12.467   3.196  1.00  9.99           O  
ANISOU  396  O   ILE A  42     2669    617    508   -102    -78    -55       O  
ATOM    397  CB  ILE A  42       4.181  11.810   5.493  1.00  9.55           C  
ANISOU  397  CB  ILE A  42     2503    664    460    -32    -13     -7       C  
ATOM    398  CG1 ILE A  42       4.489  11.042   6.789  1.00 10.32           C  
ANISOU  398  CG1 ILE A  42     2579    737    605     33    -30     38       C  
ATOM    399  CG2 ILE A  42       5.152  12.982   5.276  1.00 10.54           C  
ANISOU  399  CG2 ILE A  42     2483    733    787    -27      4     11       C  
ATOM    400  CD1 ILE A  42       5.904  10.487   6.821  1.00 12.47           C  
ANISOU  400  CD1 ILE A  42     2783   1118    835    170   -183    127       C  
ATOM    401  N   SER A  43       2.240  14.376   4.371  1.00  9.47           N  
ANISOU  401  N   SER A  43     2475    614    508    -28    -92     36       N  
ATOM    402  CA  SER A  43       1.925  15.223   3.244  1.00 10.36           C  
ANISOU  402  CA  SER A  43     2589    670    675     19   -110      8       C  
ATOM    403  C   SER A  43       2.711  16.491   3.294  1.00  9.83           C  
ANISOU  403  C   SER A  43     2645    550    539    174   -165     23       C  
ATOM    404  O   SER A  43       3.208  16.905   4.358  1.00 10.47           O  
ANISOU  404  O   SER A  43     2776    717    484    -57    -82     51       O  
ATOM    405  CB  SER A  43       0.445  15.508   3.224  1.00 13.03           C  
ANISOU  405  CB  SER A  43     2742   1042   1165   -143   -227    286       C  
ATOM    406  OG  SER A  43      -0.035  16.148   4.344  1.00 15.47           O  
ANISOU  406  OG  SER A  43     2894   1387   1596    140   -264    115       O  
ATOM    407  N   VAL A  44       2.828  17.134   2.157  1.00 10.51           N  
ANISOU  407  N   VAL A  44     2895    593    503      5   -186     35       N  
ATOM    408  CA  VAL A  44       3.544  18.406   2.038  1.00 11.42           C  
ANISOU  408  CA  VAL A  44     2977    741    619      3   -158    148       C  
ATOM    409  C   VAL A  44       2.711  19.358   1.242  1.00 11.40           C  
ANISOU  409  C   VAL A  44     3078    765    485    -48   -277     68       C  
ATOM    410  O   VAL A  44       2.133  18.989   0.216  1.00 15.21           O  
ANISOU  410  O   VAL A  44     4113    851    816    -86   -746     79       O  
ATOM    411  CB  VAL A  44       4.893  18.211   1.341  1.00 13.55           C  
ANISOU  411  CB  VAL A  44     3026   1007   1113    -54   -185    230       C  
ATOM    412  CG1 VAL A  44       5.658  19.549   1.181  1.00 20.51           C  
ANISOU  412  CG1 VAL A  44     3513   1506   2772   -248    -38    384       C  
ATOM    413  CG2 VAL A  44       5.785  17.272   2.076  1.00 15.81           C  
ANISOU  413  CG2 VAL A  44     2943   1482   1580   -226   -128    -46       C  
ATOM    414  N   ASN A  45       2.656  20.600   1.693  1.00 10.53           N  
ANISOU  414  N   ASN A  45     2747    672    583    -47   -213     67       N  
ATOM    415  CA  ASN A  45       1.947  21.654   0.998  1.00 10.63           C  
ANISOU  415  CA  ASN A  45     2691    797    550    -34   -166     59       C  
ATOM    416  C   ASN A  45       2.796  22.904   1.131  1.00 10.68           C  
ANISOU  416  C   ASN A  45     2771    711    576     21   -159    118       C  
ATOM    417  O   ASN A  45       2.922  23.467   2.212  1.00 10.38           O  
ANISOU  417  O   ASN A  45     2526    709    708    -25   -171    116       O  
ATOM    418  CB  ASN A  45       0.576  21.824   1.585  1.00 11.88           C  
ANISOU  418  CB  ASN A  45     2761    866    883   -173   -253    145       C  
ATOM    419  CG  ASN A  45      -0.291  22.832   0.893  1.00 11.42           C  
ANISOU  419  CG  ASN A  45     2497    976    865    -52   -398     69       C  
ATOM    420  OD1 ASN A  45      -1.545  22.647   0.799  1.00 13.14           O  
ANISOU  420  OD1 ASN A  45     2641   1175   1176   -173   -203    -34       O  
ATOM    421  ND2 ASN A  45       0.304  23.874   0.401  1.00 12.10           N  
ANISOU  421  ND2 ASN A  45     2598    818   1180   -143   -595    339       N  
ATOM    422  N   GLY A  46       3.486  23.263   0.058  1.00 12.47           N  
ANISOU  422  N   GLY A  46     3102   1004    629   -272    -65    203       N  
ATOM    423  CA  GLY A  46       4.442  24.372   0.154  1.00 13.14           C  
ANISOU  423  CA  GLY A  46     2963   1182    846   -249     43    274       C  
ATOM    424  C   GLY A  46       5.577  24.019   1.099  1.00 12.53           C  
ANISOU  424  C   GLY A  46     2713   1120    927   -203     74    313       C  
ATOM    425  O   GLY A  46       6.167  22.941   0.971  1.00 14.73           O  
ANISOU  425  O   GLY A  46     2925   1421   1248   -112    181     86       O  
ATOM    426  N   ASP A  47       5.828  24.869   2.066  1.00 11.55           N  
ANISOU  426  N   ASP A  47     2629    970    789   -146    103    222       N  
ATOM    427  CA  ASP A  47       6.863  24.629   3.054  1.00 12.37           C  
ANISOU  427  CA  ASP A  47     2455   1287    958   -168     65    270       C  
ATOM    428  C   ASP A  47       6.361  23.815   4.239  1.00 10.38           C  
ANISOU  428  C   ASP A  47     2350    842    750     11     31     92       C  
ATOM    429  O   ASP A  47       7.162  23.510   5.133  1.00 11.88           O  
ANISOU  429  O   ASP A  47     2271   1309    934      4    -54    212       O  
ATOM    430  CB  ASP A  47       7.408  25.965   3.600  1.00 14.44           C  
ANISOU  430  CB  ASP A  47     2781   1430   1275   -332   -200    379       C  
ATOM    431  CG  ASP A  47       8.081  26.803   2.582  1.00 19.85           C  
ANISOU  431  CG  ASP A  47     3323   1981   2237   -629   -234    404       C  
ATOM    432  OD1 ASP A  47       8.629  26.224   1.631  1.00 25.00           O  
ANISOU  432  OD1 ASP A  47     3530   3400   2567  -1119    617    655       O  
ATOM    433  OD2 ASP A  47       8.086  28.040   2.787  1.00 27.34           O  
ANISOU  433  OD2 ASP A  47     4871   2320   3196   -969   -299    970       O  
ATOM    434  N   VAL A  48       5.058  23.531   4.309  1.00  9.43           N  
ANISOU  434  N   VAL A  48     2221    661    700    -30    -51    141       N  
ATOM    435  CA  VAL A  48       4.506  22.894   5.472  1.00  9.04           C  
ANISOU  435  CA  VAL A  48     2207    669    556    -84     24    146       C  
ATOM    436  C   VAL A  48       4.405  21.400   5.273  1.00  8.76           C  
ANISOU  436  C   VAL A  48     2261    630    437    -54    -28    111       C  
ATOM    437  O   VAL A  48       3.760  20.910   4.358  1.00 10.19           O  
ANISOU  437  O   VAL A  48     2504    761    604    -65   -301    101       O  
ATOM    438  CB  VAL A  48       3.137  23.467   5.807  1.00 10.45           C  
ANISOU  438  CB  VAL A  48     2201    908    860     73     66    176       C  
ATOM    439  CG1 VAL A  48       2.575  22.834   7.083  1.00 11.66           C  
ANISOU  439  CG1 VAL A  48     2601    910    918     64    206    142       C  
ATOM    440  CG2 VAL A  48       3.166  24.979   5.977  1.00 12.74           C  
ANISOU  440  CG2 VAL A  48     2686    878   1275    224    125    144       C  
ATOM    441  N   ILE A  49       5.007  20.655   6.183  1.00  8.50           N  
ANISOU  441  N   ILE A  49     2153    635    441    -85    -70     11       N  
ATOM    442  CA  ILE A  49       4.912  19.200   6.249  1.00  8.61           C  
ANISOU  442  CA  ILE A  49     2142    652    477    -77    -98     -8       C  
ATOM    443  C   ILE A  49       3.939  18.823   7.343  1.00  8.10           C  
ANISOU  443  C   ILE A  49     2090    497    490    -49   -112     11       C  
ATOM    444  O   ILE A  49       3.981  19.402   8.437  1.00  8.93           O  
ANISOU  444  O   ILE A  49     2218    675    499   -153     33    -52       O  
ATOM    445  CB  ILE A  49       6.307  18.600   6.523  1.00  9.22           C  
ANISOU  445  CB  ILE A  49     2178    836    488    -75    -43    -61       C  
ATOM    446  CG1 ILE A  49       7.325  19.031   5.475  1.00 10.76           C  
ANISOU  446  CG1 ILE A  49     2261   1133    691    -59    129    -87       C  
ATOM    447  CG2 ILE A  49       6.272  17.072   6.620  1.00 10.44           C  
ANISOU  447  CG2 ILE A  49     2377    761    826     81   -130     11       C  
ATOM    448  CD1 ILE A  49       8.792  18.744   5.886  1.00 15.70           C  
ANISOU  448  CD1 ILE A  49     2310   2222   1430     65    178    198       C  
ATOM    449  N   THR A  50       3.072  17.873   7.055  1.00  8.47           N  
ANISOU  449  N   THR A  50     2239    552    427    -45    -52     23       N  
ATOM    450  CA  THR A  50       2.163  17.328   8.049  1.00  8.67           C  
ANISOU  450  CA  THR A  50     2121    710    463   -150     -6    -42       C  
ATOM    451  C   THR A  50       2.413  15.850   8.211  1.00  8.40           C  
ANISOU  451  C   THR A  50     2101    565    525   -108     13     75       C  
ATOM    452  O   THR A  50       2.496  15.105   7.233  1.00  9.64           O  
ANISOU  452  O   THR A  50     2643    524    495   -123     31     -6       O  
ATOM    453  CB  THR A  50       0.692  17.633   7.670  1.00  9.97           C  
ANISOU  453  CB  THR A  50     2304    820    662   -218    -15    -55       C  
ATOM    454  OG1 THR A  50       0.478  19.022   7.556  1.00 11.03           O  
ANISOU  454  OG1 THR A  50     2284    899   1007     -2    -48    134       O  
ATOM    455  CG2 THR A  50      -0.267  17.047   8.668  1.00 12.07           C  
ANISOU  455  CG2 THR A  50     2415   1125   1044   -244     65    -98       C  
ATOM    456  N   ILE A  51       2.513  15.420   9.473  1.00  8.65           N  
ANISOU  456  N   ILE A  51     2237    512    536   -101      9     25       N  
ATOM    457  CA  ILE A  51       2.637  13.999   9.841  1.00  9.28           C  
ANISOU  457  CA  ILE A  51     2372    590    561   -169     34    -62       C  
ATOM    458  C   ILE A  51       1.473  13.680  10.770  1.00  9.26           C  
ANISOU  458  C   ILE A  51     2391    594    531    -82    113     86       C  
ATOM    459  O   ILE A  51       1.391  14.225  11.877  1.00  9.97           O  
ANISOU  459  O   ILE A  51     2422    759    607    -80    123    -29       O  
ATOM    460  CB  ILE A  51       3.946  13.669  10.498  1.00  9.77           C  
ANISOU  460  CB  ILE A  51     2366    695    650    -25     90    -89       C  
ATOM    461  CG1 ILE A  51       5.143  14.022   9.603  1.00 10.57           C  
ANISOU  461  CG1 ILE A  51     2425    755    836    -97    117   -129       C  
ATOM    462  CG2 ILE A  51       3.993  12.190  10.904  1.00 11.70           C  
ANISOU  462  CG2 ILE A  51     2815    664    967     40    149      3       C  
ATOM    463  CD1 ILE A  51       6.484  13.810  10.226  1.00 13.06           C  
ANISOU  463  CD1 ILE A  51     2374   1067   1521    191    -81   -180       C  
ATOM    464  N   LYS A  52       0.550  12.854  10.304  1.00 10.05           N  
ANISOU  464  N   LYS A  52     2496    674    648   -214    203    -34       N  
ATOM    465  CA  LYS A  52      -0.600  12.426  11.050  1.00 11.64           C  
ANISOU  465  CA  LYS A  52     2575    919    927   -331    314   -171       C  
ATOM    466  C   LYS A  52      -0.435  10.964  11.406  1.00 11.71           C  
ANISOU  466  C   LYS A  52     2804    693    951   -312    425   -157       C  
ATOM    467  O   LYS A  52      -0.109  10.175  10.532  1.00 15.25           O  
ANISOU  467  O   LYS A  52     3970    692   1132   -348    808    -86       O  
ATOM    468  CB  LYS A  52      -1.855  12.637  10.209  1.00 14.88           C  
ANISOU  468  CB  LYS A  52     2516   1844   1291   -258    238   -313       C  
ATOM    469  CG  LYS A  52      -3.213  12.466  10.792  1.00 19.18           C  
ANISOU  469  CG  LYS A  52     3049   2230   2006   -448    194    115       C  
ATOM    470  CD  LYS A  52      -4.243  12.820   9.694  1.00 25.59           C  
ANISOU  470  CD  LYS A  52     3348   3542   2833    -76   -244   -147       C  
ATOM    471  CE  LYS A  52      -4.021  14.264   9.112  1.00 30.78           C  
ANISOU  471  CE  LYS A  52     3821   4056   3816   -343   -253   -230       C  
ATOM    472  NZ  LYS A  52      -3.131  14.480   7.902  1.00 34.71           N  
ANISOU  472  NZ  LYS A  52     3945   4650   4593   -100     35   -335       N  
ATOM    473  N   SER A  53      -0.741  10.607  12.641  1.00 11.33           N  
ANISOU  473  N   SER A  53     2647    816    841   -246    346   -114       N  
ATOM    474  CA  SER A  53      -0.761   9.236  13.071  1.00 11.41           C  
ANISOU  474  CA  SER A  53     2530    770   1033   -248    398     25       C  
ATOM    475  C   SER A  53      -2.196   8.902  13.486  1.00 11.01           C  
ANISOU  475  C   SER A  53     2645    775    762   -249    303   -139       C  
ATOM    476  O   SER A  53      -2.739   9.529  14.387  1.00 12.91           O  
ANISOU  476  O   SER A  53     2660   1032   1211   -381    448   -147       O  
ATOM    477  CB  SER A  53       0.176   9.059  14.269  1.00 13.05           C  
ANISOU  477  CB  SER A  53     2481    943   1531   -138    294    -43       C  
ATOM    478  OG  SER A  53       0.171   7.708  14.741  1.00 15.17           O  
ANISOU  478  OG  SER A  53     3001   1255   1508   -205    193     58       O  
ATOM    479  N   GLU A  54      -2.778   7.925  12.831  1.00 11.98           N  
ANISOU  479  N   GLU A  54     2604   1128    818   -346    333    -89       N  
ATOM    480  CA  GLU A  54      -4.123   7.446  13.139  1.00 12.66           C  
ANISOU  480  CA  GLU A  54     2556   1218   1034   -285    165    -97       C  
ATOM    481  C   GLU A  54      -3.904   6.103  13.870  1.00 11.78           C  
ANISOU  481  C   GLU A  54     2419   1127    927   -308    139     -7       C  
ATOM    482  O   GLU A  54      -3.383   5.160  13.293  1.00 12.49           O  
ANISOU  482  O   GLU A  54     2783   1059    901   -254    182    128       O  
ATOM    483  CB  GLU A  54      -4.928   7.196  11.870  1.00 14.99           C  
ANISOU  483  CB  GLU A  54     2917   1484   1294   -292    -88    209       C  
ATOM    484  CG  GLU A  54      -5.130   8.414  11.023  1.00 20.59           C  
ANISOU  484  CG  GLU A  54     3367   2307   2149   -418    -78    472       C  
ATOM    485  CD  GLU A  54      -6.112   8.223   9.911  1.00 23.40           C  
ANISOU  485  CD  GLU A  54     3680   2730   2480   -115   -372    720       C  
ATOM    486  OE1 GLU A  54      -5.997   7.233   9.176  1.00 27.48           O  
ANISOU  486  OE1 GLU A  54     4367   3630   2441   -656   -871   -188       O  
ATOM    487  OE2 GLU A  54      -6.983   9.109   9.741  1.00 31.27           O  
ANISOU  487  OE2 GLU A  54     4328   3233   4317    214   -283    294       O  
ATOM    488  N  ASER A  55      -4.300   6.115  15.106  0.50 10.94           N  
ANISOU  488  N  ASER A  55     2420    981    753   -165    117     -3       N  
ATOM    489  N  BSER A  55      -4.308   5.924  15.131  0.50 13.84           N  
ANISOU  489  N  BSER A  55     2460   1656   1142   -133    225     40       N  
ATOM    490  CA ASER A  55      -3.837   5.105  16.021  0.50  9.05           C  
ANISOU  490  CA ASER A  55     2119    635    684   -163    110     91       C  
ATOM    491  CA BSER A  55      -4.351   4.530  15.765  0.50 14.46           C  
ANISOU  491  CA BSER A  55     2310   1864   1318   -100    146    282       C  
ATOM    492  C  ASER A  55      -4.946   4.682  16.923  0.50  9.54           C  
ANISOU  492  C  ASER A  55     2057    837    729   -138     98    -23       C  
ATOM    493  C  BSER A  55      -5.523   4.346  16.725  0.50 12.82           C  
ANISOU  493  C  BSER A  55     2198   1618   1052   -146    265    318       C  
ATOM    494  O  ASER A  55      -5.667   5.514  17.446  0.50 10.87           O  
ANISOU  494  O  ASER A  55     2193   1069    865    105    190    154       O  
ATOM    495  O  BSER A  55      -6.244   5.265  17.061  0.50 12.50           O  
ANISOU  495  O  BSER A  55     2195   1347   1204   -123     89    470       O  
ATOM    496  CB ASER A  55      -2.735   5.618  16.893  0.50  9.48           C  
ANISOU  496  CB ASER A  55     2162    746    692    -46    171    182       C  
ATOM    497  CB BSER A  55      -3.068   4.039  16.501  0.50 15.87           C  
ANISOU  497  CB BSER A  55     2459   1818   1751   -102    229    198       C  
ATOM    498  OG ASER A  55      -2.269   4.698  17.876  0.50 11.19           O  
ANISOU  498  OG ASER A  55     2003   1264    982    -23     37    348       O  
ATOM    499  OG BSER A  55      -2.864   4.670  17.737  0.50 14.51           O  
ANISOU  499  OG BSER A  55     2042   2143   1329    137    -18    659       O  
ATOM    500  N  ATHR A  56      -5.002   3.400  17.220  0.50  8.76           N  
ANISOU  500  N  ATHR A  56     1754    822    753   -111    173     54       N  
ATOM    501  N  BTHR A  56      -5.674   3.128  17.204  0.50 13.17           N  
ANISOU  501  N  BTHR A  56     2247   1364   1393    -33    186    265       N  
ATOM    502  CA ATHR A  56      -5.928   2.856  18.231  0.50  8.87           C  
ANISOU  502  CA ATHR A  56     1841    665    861    -46    197     31       C  
ATOM    503  CA BTHR A  56      -6.653   2.835  18.227  0.50 13.20           C  
ANISOU  503  CA BTHR A  56     2280   1242   1494    -37    273    366       C  
ATOM    504  C  ATHR A  56      -5.485   3.250  19.636  0.50  9.05           C  
ANISOU  504  C  ATHR A  56     1734    838    864    -45    173    189       C  
ATOM    505  C  BTHR A  56      -6.205   3.405  19.565  0.50 12.62           C  
ANISOU  505  C  BTHR A  56     2093   1150   1552    -39    154    350       C  
ATOM    506  O  ATHR A  56      -6.261   3.034  20.594  0.50 10.67           O  
ANISOU  506  O  ATHR A  56     2200    909    945     74    202    150       O  
ATOM    507  O  BTHR A  56      -7.040   3.578  20.407  0.50 14.66           O  
ANISOU  507  O  BTHR A  56     2262   1673   1634   -118    361    141       O  
ATOM    508  CB ATHR A  56      -6.013   1.336  18.114  0.50  9.95           C  
ANISOU  508  CB ATHR A  56     1797   1030    953   -113    294    157       C  
ATOM    509  CB BTHR A  56      -6.909   1.345  18.390  0.50 15.07           C  
ANISOU  509  CB BTHR A  56     2637   1188   1899    -92    237    520       C  
ATOM    510  OG1ATHR A  56      -4.683   0.869  18.207  0.50  8.87           O  
ANISOU  510  OG1ATHR A  56     2071    642    657    -55    283     86       O  
ATOM    511  OG1BTHR A  56      -5.732   0.699  18.875  0.50 18.14           O  
ANISOU  511  OG1BTHR A  56     3012   1486   2394      7     97    161       O  
ATOM    512  CG2ATHR A  56      -6.654   0.875  16.824  0.50 12.56           C  
ANISOU  512  CG2ATHR A  56     1834   1372   1566   -238     51   -160       C  
ATOM    513  CG2BTHR A  56      -7.331   0.704  17.091  0.50 16.18           C  
ANISOU  513  CG2BTHR A  56     2856   1385   1904   -164    207    227       C  
ATOM    514  N  APHE A  57      -4.233   3.722  19.821  0.50  9.35           N  
ANISOU  514  N  APHE A  57     1933    773    844      4    183     93       N  
ATOM    515  N  BPHE A  57      -4.924   3.693  19.772  0.50 11.40           N  
ANISOU  515  N  BPHE A  57     1878   1299   1155   -150    311    361       N  
ATOM    516  CA APHE A  57      -3.764   4.269  21.098  0.50  9.92           C  
ANISOU  516  CA APHE A  57     1781   1135    852    -22    136    236       C  
ATOM    517  CA BPHE A  57      -4.478   4.301  21.039  0.50 11.70           C  
ANISOU  517  CA BPHE A  57     1898   1231   1316   -106    144    408       C  
ATOM    518  C  APHE A  57      -4.077   5.781  21.218  0.50 10.20           C  
ANISOU  518  C  APHE A  57     1974   1011    892     -8     95    193       C  
ATOM    519  C  BPHE A  57      -4.748   5.762  21.007  0.50 11.18           C  
ANISOU  519  C  BPHE A  57     2037   1039   1171    -69     93    439       C  
ATOM    520  O  APHE A  57      -4.892   6.167  22.066  0.50 12.50           O  
ANISOU  520  O  APHE A  57     2217   1237   1292     -8    338    241       O  
ATOM    521  O  BPHE A  57      -5.678   6.206  21.575  0.50 14.06           O  
ANISOU  521  O  BPHE A  57     2041   1586   1712    -77    346    395       O  
ATOM    522  CB APHE A  57      -2.249   3.985  21.314  0.50  9.93           C  
ANISOU  522  CB APHE A  57     1861   1022    888    -58     -7    310       C  
ATOM    523  CB BPHE A  57      -3.002   4.034  21.355  0.50 12.20           C  
ANISOU  523  CB BPHE A  57     1971   1167   1496     57    129    342       C  
ATOM    524  CG APHE A  57      -1.653   4.758  22.417  0.50 11.74           C  
ANISOU  524  CG APHE A  57     1967   1232   1262    116    -27    142       C  
ATOM    525  CG BPHE A  57      -2.484   4.794  22.536  0.50 14.95           C  
ANISOU  525  CG BPHE A  57     2334   1542   1804     47   -167    205       C  
ATOM    526  CD1APHE A  57      -2.220   4.759  23.656  0.50 12.95           C  
ANISOU  526  CD1APHE A  57     2103   1481   1335    -17    143     62       C  
ATOM    527  CD1BPHE A  57      -1.324   5.561  22.418  0.50 17.30           C  
ANISOU  527  CD1BPHE A  57     2536   1803   2232      9    -57    -68       C  
ATOM    528  CD2APHE A  57      -0.562   5.580  22.182  0.50 13.42           C  
ANISOU  528  CD2APHE A  57     2013   1561   1525     91    110    268       C  
ATOM    529  CD2BPHE A  57      -3.158   4.805  23.735  0.50 17.96           C  
ANISOU  529  CD2BPHE A  57     2729   1991   2103    -41   -267     45       C  
ATOM    530  CE1APHE A  57      -1.667   5.538  24.650  0.50 15.74           C  
ANISOU  530  CE1APHE A  57     2421   1881   1675   -181   -297     73       C  
ATOM    531  CE1BPHE A  57      -0.842   6.281  23.486  0.50 18.03           C  
ANISOU  531  CE1BPHE A  57     2437   2124   2288    304   -109      6       C  
ATOM    532  CE2APHE A  57      -0.010   6.352  23.161  0.50 15.84           C  
ANISOU  532  CE2APHE A  57     2491   1302   2225    -31   -285    632       C  
ATOM    533  CE2BPHE A  57      -2.667   5.537  24.816  0.50 20.41           C  
ANISOU  533  CE2BPHE A  57     2720   2634   2399    153   -364      0       C  
ATOM    534  CZ APHE A  57      -0.569   6.338  24.389  0.50 14.95           C  
ANISOU  534  CZ APHE A  57     2527   1315   1837    123   -354    101       C  
ATOM    535  CZ BPHE A  57      -1.517   6.275  24.668  0.50 18.10           C  
ANISOU  535  CZ BPHE A  57     2751   2015   2110    109   -258    -99       C  
ATOM    536  N  ALYS A  58      -3.405   6.647  20.471  0.50 10.75           N  
ANISOU  536  N  ALYS A  58     2022   1055   1008   -167     -5     93       N  
ATOM    537  N  BLYS A  58      -3.949   6.496  20.262  0.50 12.00           N  
ANISOU  537  N  BLYS A  58     2240    860   1458    -50    413    397       N  
ATOM    538  CA ALYS A  58      -3.726   8.090  20.519  0.50 11.35           C  
ANISOU  538  CA ALYS A  58     2178   1202    932   -128    -68    -74       C  
ATOM    539  CA BLYS A  58      -4.025   7.919  20.245  0.50 14.33           C  
ANISOU  539  CA BLYS A  58     2523   1273   1646    -96    322    235       C  
ATOM    540  C  ALYS A  58      -3.446   8.669  19.147  0.50  9.10           C  
ANISOU  540  C  ALYS A  58     1969    625    861   -223     69    -77       C  
ATOM    541  C  BLYS A  58      -3.795   8.302  18.756  0.50 14.47           C  
ANISOU  541  C  BLYS A  58     2575   1142   1780    -58    509    190       C  
ATOM    542  O  ALYS A  58      -2.333   8.520  18.675  0.50  9.12           O  
ANISOU  542  O  ALYS A  58     1868    697    899     -4    188    148       O  
ATOM    543  O  BLYS A  58      -3.309   7.617  17.822  0.50 17.69           O  
ANISOU  543  O  BLYS A  58     2996   1809   1914     94    603    256       O  
ATOM    544  CB ALYS A  58      -2.921   8.814  21.607  0.50 12.76           C  
ANISOU  544  CB ALYS A  58     2376   1233   1238   -120   -123   -206       C  
ATOM    545  CB BLYS A  58      -3.062   8.539  21.335  0.50 14.99           C  
ANISOU  545  CB BLYS A  58     2613   1191   1892   -200    217    219       C  
ATOM    546  CG ALYS A  58      -3.058   8.284  22.929  0.50 18.25           C  
ANISOU  546  CG ALYS A  58     2840   2328   1764   -201     -9   -268       C  
ATOM    547  CG BLYS A  58      -3.132  10.137  21.721  0.50 12.73           C  
ANISOU  547  CG BLYS A  58     2492   1155   1188   -181    122     11       C  
ATOM    548  CD ALYS A  58      -4.352   8.604  23.574  0.50 21.67           C  
ANISOU  548  CD ALYS A  58     3110   2465   2656    -55     65   -326       C  
ATOM    549  CD BLYS A  58      -4.532  10.519  22.118  0.50 15.90           C  
ANISOU  549  CD BLYS A  58     2725   1762   1552   -198    105   -270       C  
ATOM    550  CE ALYS A  58      -4.472   7.672  24.748  0.50 21.17           C  
ANISOU  550  CE ALYS A  58     3382   2419   2241     14    201   -558       C  
ATOM    551  CE BLYS A  58      -4.677  12.040  22.163  0.50 19.78           C  
ANISOU  551  CE BLYS A  58     3093   2288   2135    -79      3   -239       C  
ATOM    552  NZ ALYS A  58      -3.119   7.504  25.370  0.50 24.16           N  
ANISOU  552  NZ ALYS A  58     3839   2203   3137    266     73   -156       N  
ATOM    553  NZ BLYS A  58      -6.069  12.531  22.334  0.50 24.46           N  
ANISOU  553  NZ BLYS A  58     3348   3193   2752    106     79   -187       N  
ATOM    554  N   ASN A  59      -4.459   9.324  18.481  1.00 11.79           N  
ANISOU  554  N   ASN A  59     2317    974   1185    -36    438     97       N  
ATOM    555  CA  ASN A  59      -4.219  10.006  17.237  1.00 12.16           C  
ANISOU  555  CA  ASN A  59     2469    877   1275    -67    366     15       C  
ATOM    556  C   ASN A  59      -3.388  11.248  17.512  1.00 12.35           C  
ANISOU  556  C   ASN A  59     2736    816   1141    -27    498    -66       C  
ATOM    557  O   ASN A  59      -3.575  11.904  18.520  1.00 14.77           O  
ANISOU  557  O   ASN A  59     3111   1050   1449   -303    743   -208       O  
ATOM    558  CB  ASN A  59      -5.545  10.451  16.642  1.00 13.56           C  
ANISOU  558  CB  ASN A  59     2616   1046   1489    -80    295    250       C  
ATOM    559  CG  ASN A  59      -6.484   9.321  16.276  1.00 14.91           C  
ANISOU  559  CG  ASN A  59     2428   1510   1727    117     11    205       C  
ATOM    560  OD1 ASN A  59      -6.059   8.320  15.744  1.00 14.31           O  
ANISOU  560  OD1 ASN A  59     2343   1287   1806      4    107    271       O  
ATOM    561  ND2 ASN A  59      -7.769   9.427  16.653  1.00 21.54           N  
ANISOU  561  ND2 ASN A  59     2606   2660   2916    -53    205     11       N  
ATOM    562  N   THR A  60      -2.475  11.527  16.595  1.00 11.71           N  
ANISOU  562  N   THR A  60     2638    843    966    -75    448    -51       N  
ATOM    563  CA  THR A  60      -1.664  12.720  16.687  1.00 11.81           C  
ANISOU  563  CA  THR A  60     2704    725   1057   -148    455    -39       C  
ATOM    564  C   THR A  60      -1.552  13.360  15.309  1.00 10.77           C  
ANISOU  564  C   THR A  60     2547    533   1012   -112    405    -26       C  
ATOM    565  O   THR A  60      -1.677  12.711  14.281  1.00 10.96           O  
ANISOU  565  O   THR A  60     2552    676    935   -138    289    -35       O  
ATOM    566  CB  THR A  60      -0.241  12.451  17.246  1.00 12.78           C  
ANISOU  566  CB  THR A  60     2774   1047   1034   -236    259    -69       C  
ATOM    567  OG1 THR A  60       0.469  11.606  16.361  1.00 12.73           O  
ANISOU  567  OG1 THR A  60     2528   1285   1023    -64    168     94       O  
ATOM    568  CG2 THR A  60      -0.210  11.860  18.647  1.00 14.07           C  
ANISOU  568  CG2 THR A  60     3025   1373    947   -214    216    -12       C  
ATOM    569  N   GLU A  61      -1.268  14.640  15.288  1.00 11.28           N  
ANISOU  569  N   GLU A  61     2633    772    878    -75    424    -21       N  
ATOM    570  CA  GLU A  61      -0.991  15.353  14.045  1.00 11.27           C  
ANISOU  570  CA  GLU A  61     2499    747   1036    -66    336    -90       C  
ATOM    571  C   GLU A  61      -0.109  16.528  14.326  1.00 11.09           C  
ANISOU  571  C   GLU A  61     2561    638   1012    -60    306   -139       C  
ATOM    572  O   GLU A  61      -0.358  17.316  15.262  1.00 13.37           O  
ANISOU  572  O   GLU A  61     2978    871   1228   -220    630   -250       O  
ATOM    573  CB  GLU A  61      -2.300  15.815  13.431  1.00 13.63           C  
ANISOU  573  CB  GLU A  61     2555   1015   1608    -89    255    106       C  
ATOM    574  CG  GLU A  61      -2.148  16.551  12.146  1.00 17.60           C  
ANISOU  574  CG  GLU A  61     2649   1806   2230    -34     -5    624       C  
ATOM    575  CD  GLU A  61      -3.457  16.968  11.539  1.00 24.60           C  
ANISOU  575  CD  GLU A  61     2870   3344   3133   -122    -24    786       C  
ATOM    576  OE1 GLU A  61      -3.461  18.008  10.875  1.00 28.12           O  
ANISOU  576  OE1 GLU A  61     2900   4058   3724   -131   -447   1238       O  
ATOM    577  OE2 GLU A  61      -4.486  16.275  11.749  1.00 29.22           O  
ANISOU  577  OE2 GLU A  61     3104   3923   4073   -359    -95    581       O  
ATOM    578  N   ILE A  62       0.969  16.619  13.567  1.00  9.33           N  
ANISOU  578  N   ILE A  62     2294    693    555    -48    158    -45       N  
ATOM    579  CA  ILE A  62       1.843  17.766  13.647  1.00  9.41           C  
ANISOU  579  CA  ILE A  62     2369    555    650   -137     38    -74       C  
ATOM    580  C   ILE A  62       1.995  18.348  12.232  1.00  8.59           C  
ANISOU  580  C   ILE A  62     2210    501    550   -138     68    -11       C  
ATOM    581  O   ILE A  62       2.100  17.620  11.256  1.00 10.11           O  
ANISOU  581  O   ILE A  62     2758    544    538   -206     54    -41       O  
ATOM    582  CB  ILE A  62       3.224  17.406  14.237  1.00 10.14           C  
ANISOU  582  CB  ILE A  62     2453    807    592   -137    -91    -41       C  
ATOM    583  CG1 ILE A  62       3.988  16.317  13.475  1.00 10.60           C  
ANISOU  583  CG1 ILE A  62     2169   1032    824   -147   -147    -82       C  
ATOM    584  CG2 ILE A  62       3.068  16.987  15.726  1.00 12.55           C  
ANISOU  584  CG2 ILE A  62     2644   1443    679     68     -7    174       C  
ATOM    585  CD1 ILE A  62       5.391  16.124  13.913  1.00 13.36           C  
ANISOU  585  CD1 ILE A  62     2370   1452   1250   -109   -183   -208       C  
ATOM    586  N   SER A  63       2.044  19.654  12.174  1.00  8.51           N  
ANISOU  586  N   SER A  63     2122    612    500    -35     65   -107       N  
ATOM    587  CA  SER A  63       2.410  20.393  10.971  1.00  8.62           C  
ANISOU  587  CA  SER A  63     2206    521    547    -23     36    -14       C  
ATOM    588  C   SER A  63       3.530  21.356  11.305  1.00  8.40           C  
ANISOU  588  C   SER A  63     2049    541    602    -38     17   -176       C  
ATOM    589  O   SER A  63       3.508  21.985  12.355  1.00 10.04           O  
ANISOU  589  O   SER A  63     2256    741    817   -173    160   -190       O  
ATOM    590  CB  SER A  63       1.227  21.182  10.409  1.00  9.44           C  
ANISOU  590  CB  SER A  63     2151    822    613    -37     45    -59       C  
ATOM    591  OG  SER A  63       0.182  20.322   9.961  1.00 11.54           O  
ANISOU  591  OG  SER A  63     2244   1148    990     71   -134   -109       O  
ATOM    592  N   PHE A  64       4.498  21.485  10.399  1.00  8.52           N  
ANISOU  592  N   PHE A  64     2101    681    454    -39    -50     21       N  
ATOM    593  CA  PHE A  64       5.717  22.199  10.730  1.00  8.43           C  
ANISOU  593  CA  PHE A  64     2034    639    529    -97    -58    -51       C  
ATOM    594  C   PHE A  64       6.432  22.621   9.457  1.00  8.17           C  
ANISOU  594  C   PHE A  64     2084    515    504    -11    -30     47       C  
ATOM    595  O   PHE A  64       6.208  22.059   8.376  1.00  8.69           O  
ANISOU  595  O   PHE A  64     2131    693    476   -139    -47    -18       O  
ATOM    596  CB  PHE A  64       6.624  21.359  11.637  1.00  8.89           C  
ANISOU  596  CB  PHE A  64     2001    802    572   -187    -79     55       C  
ATOM    597  CG  PHE A  64       6.992  20.042  11.018  1.00  8.98           C  
ANISOU  597  CG  PHE A  64     2032    807    570    -17   -135     83       C  
ATOM    598  CD1 PHE A  64       6.160  18.913  11.164  1.00  9.29           C  
ANISOU  598  CD1 PHE A  64     1995    821    711    -91   -175     11       C  
ATOM    599  CD2 PHE A  64       8.111  19.909  10.270  1.00  9.27           C  
ANISOU  599  CD2 PHE A  64     2049    809    662    -19   -112    102       C  
ATOM    600  CE1 PHE A  64       6.447  17.728  10.547  1.00 10.28           C  
ANISOU  600  CE1 PHE A  64     2310    858    738   -134   -265     15       C  
ATOM    601  CE2 PHE A  64       8.408  18.727   9.650  1.00 10.64           C  
ANISOU  601  CE2 PHE A  64     2269   1116    657    112    -52    166       C  
ATOM    602  CZ  PHE A  64       7.593  17.625   9.810  1.00 10.55           C  
ANISOU  602  CZ  PHE A  64     2477    860    669     76   -210     14       C  
ATOM    603  N   ILE A  65       7.325  23.560   9.660  1.00  8.50           N  
ANISOU  603  N   ILE A  65     2053    587    587    -97    -34    -51       N  
ATOM    604  CA  ILE A  65       8.281  24.013   8.669  1.00  8.45           C  
ANISOU  604  CA  ILE A  65     2082    556    571    -28    -16      3       C  
ATOM    605  C   ILE A  65       9.673  23.577   9.137  1.00  8.58           C  
ANISOU  605  C   ILE A  65     2170    480    608   -112    -56      7       C  
ATOM    606  O   ILE A  65       9.990  23.704  10.335  1.00  8.55           O  
ANISOU  606  O   ILE A  65     2066    530    653    -51    -69    -57       O  
ATOM    607  CB  ILE A  65       8.195  25.545   8.476  1.00  9.59           C  
ANISOU  607  CB  ILE A  65     2281    555    805    -31   -114      7       C  
ATOM    608  CG1 ILE A  65       6.807  25.864   7.916  1.00 11.39           C  
ANISOU  608  CG1 ILE A  65     2268    929   1129    -26   -103    163       C  
ATOM    609  CG2 ILE A  65       9.306  26.030   7.563  1.00 10.50           C  
ANISOU  609  CG2 ILE A  65     2368    674    947    -94     79    167       C  
ATOM    610  CD1 ILE A  65       6.473  27.364   7.823  1.00 14.77           C  
ANISOU  610  CD1 ILE A  65     2630    845   2136    213    -26    421       C  
ATOM    611  N   LEU A  66      10.465  23.013   8.247  1.00  8.38           N  
ANISOU  611  N   LEU A  66     2054    562    568     -1     36    -34       N  
ATOM    612  CA  LEU A  66      11.793  22.569   8.634  1.00  8.81           C  
ANISOU  612  CA  LEU A  66     2188    525    632      1     96     22       C  
ATOM    613  C   LEU A  66      12.591  23.682   9.300  1.00  8.72           C  
ANISOU  613  C   LEU A  66     2038    501    772      1    133     71       C  
ATOM    614  O   LEU A  66      12.632  24.809   8.808  1.00  9.48           O  
ANISOU  614  O   LEU A  66     2078    571    952    -87     11    180       O  
ATOM    615  CB  LEU A  66      12.552  21.996   7.433  1.00  9.78           C  
ANISOU  615  CB  LEU A  66     2287    675    754     72    -12     81       C  
ATOM    616  CG  LEU A  66      11.929  20.749   6.788  1.00 10.61           C  
ANISOU  616  CG  LEU A  66     2387    855    788     43     98   -222       C  
ATOM    617  CD1 LEU A  66      12.662  20.433   5.482  1.00 14.20           C  
ANISOU  617  CD1 LEU A  66     3251   1085   1058     69    211   -377       C  
ATOM    618  CD2 LEU A  66      12.071  19.546   7.732  1.00 11.86           C  
ANISOU  618  CD2 LEU A  66     2729    636   1140    -44    -68    -34       C  
ATOM    619  N   GLY A  67      13.204  23.341  10.420  1.00  8.71           N  
ANISOU  619  N   GLY A  67     2044    544    718     36     13     84       N  
ATOM    620  CA  GLY A  67      14.063  24.280  11.151  1.00  9.48           C  
ANISOU  620  CA  GLY A  67     2053    733    817    -63    -64    -18       C  
ATOM    621  C   GLY A  67      13.355  25.195  12.099  1.00  8.31           C  
ANISOU  621  C   GLY A  67     1978    483    696    -69      2     15       C  
ATOM    622  O   GLY A  67      14.038  25.947  12.794  1.00  9.58           O  
ANISOU  622  O   GLY A  67     2016    695    929    -92   -121   -130       O  
ATOM    623  N   GLN A  68      12.033  25.153  12.167  1.00  8.39           N  
ANISOU  623  N   GLN A  68     1992    463    732   -137    -84    -55       N  
ATOM    624  CA  GLN A  68      11.224  26.113  12.930  1.00  8.53           C  
ANISOU  624  CA  GLN A  68     2109    413    718    -99   -111    -80       C  
ATOM    625  C   GLN A  68      10.517  25.419  14.072  1.00  8.68           C  
ANISOU  625  C   GLN A  68     2065    371    862      0    -24   -113       C  
ATOM    626  O   GLN A  68       9.637  24.563  13.876  1.00  8.95           O  
ANISOU  626  O   GLN A  68     2008    554    836    -58     16   -147       O  
ATOM    627  CB  GLN A  68      10.245  26.801  11.988  1.00  9.53           C  
ANISOU  627  CB  GLN A  68     2174    487    958    -31   -186   -219       C  
ATOM    628  CG  GLN A  68      11.008  27.517  10.885  1.00 11.77           C  
ANISOU  628  CG  GLN A  68     2780    762    928   -322   -274     97       C  
ATOM    629  CD  GLN A  68      10.277  28.513  10.090  1.00 13.47           C  
ANISOU  629  CD  GLN A  68     3119    583   1416   -102   -543    292       C  
ATOM    630  OE1 GLN A  68       9.065  28.791  10.368  1.00 17.05           O  
ANISOU  630  OE1 GLN A  68     3251    940   2285    202   -952    265       O  
ATOM    631  NE2 GLN A  68      10.975  29.061   9.117  1.00 15.04           N  
ANISOU  631  NE2 GLN A  68     3702    759   1251   -223   -380    390       N  
ATOM    632  N   GLU A  69      10.907  25.774  15.298  1.00  8.65           N  
ANISOU  632  N   GLU A  69     2072    444    772    -86    -10    -78       N  
ATOM    633  CA  GLU A  69      10.390  25.122  16.518  1.00  9.05           C  
ANISOU  633  CA  GLU A  69     2178    400    860    -81   -104    -14       C  
ATOM    634  C   GLU A  69       8.889  25.272  16.630  1.00  8.84           C  
ANISOU  634  C   GLU A  69     2216    480    659    -69      2      9       C  
ATOM    635  O   GLU A  69       8.336  26.327  16.292  1.00  9.85           O  
ANISOU  635  O   GLU A  69     2156    468   1117     27    -11     35       O  
ATOM    636  CB  GLU A  69      11.101  25.719  17.734  1.00 11.37           C  
ANISOU  636  CB  GLU A  69     2233   1243    843   -111   -131    215       C  
ATOM    637  CG  GLU A  69      10.727  25.153  19.075  1.00 13.52           C  
ANISOU  637  CG  GLU A  69     2821   1172   1143   -179   -122     20       C  
ATOM    638  CD  GLU A  69      11.631  25.664  20.167  1.00 19.64           C  
ANISOU  638  CD  GLU A  69     3640   2779   1041   -565   -398    162       C  
ATOM    639  OE1 GLU A  69      11.517  26.894  20.487  1.00 29.58           O  
ANISOU  639  OE1 GLU A  69     4885   4188   2165   -916   -509  -1365       O  
ATOM    640  OE2 GLU A  69      12.392  24.806  20.699  1.00 25.04           O  
ANISOU  640  OE2 GLU A  69     3917   3743   1851   -628   -819    116       O  
ATOM    641  N   PHE A  70       8.249  24.266  17.190  1.00  8.14           N  
ANISOU  641  N   PHE A  70     1983    460    648     97     15      9       N  
ATOM    642  CA  PHE A  70       6.826  24.242  17.409  1.00  8.50           C  
ANISOU  642  CA  PHE A  70     2103    429    695    128    100    -55       C  
ATOM    643  C   PHE A  70       6.509  23.485  18.682  1.00  9.03           C  
ANISOU  643  C   PHE A  70     2205    508    717    105    143    -51       C  
ATOM    644  O   PHE A  70       7.309  22.702  19.209  1.00  9.82           O  
ANISOU  644  O   PHE A  70     2197    794    738    209    149     35       O  
ATOM    645  CB  PHE A  70       6.090  23.655  16.208  1.00  8.70           C  
ANISOU  645  CB  PHE A  70     1984    685    634     48     21    -18       C  
ATOM    646  CG  PHE A  70       6.442  22.236  15.874  1.00  8.85           C  
ANISOU  646  CG  PHE A  70     2038    622    699    -72    -76     38       C  
ATOM    647  CD1 PHE A  70       7.554  21.938  15.094  1.00  8.49           C  
ANISOU  647  CD1 PHE A  70     2019    654    550    -11      8     25       C  
ATOM    648  CD2 PHE A  70       5.650  21.185  16.302  1.00 10.67           C  
ANISOU  648  CD2 PHE A  70     2183    939    932   -164    181   -208       C  
ATOM    649  CE1 PHE A  70       7.878  20.627  14.755  1.00  9.23           C  
ANISOU  649  CE1 PHE A  70     2240    668    599     15    -72    -81       C  
ATOM    650  CE2 PHE A  70       5.973  19.875  15.971  1.00 11.40           C  
ANISOU  650  CE2 PHE A  70     2519    922    888   -401    191   -136       C  
ATOM    651  CZ  PHE A  70       7.077  19.603  15.201  1.00 10.04           C  
ANISOU  651  CZ  PHE A  70     2481    644    690    -92    -32   -101       C  
ATOM    652  N   ASP A  71       5.283  23.683  19.164  1.00  9.63           N  
ANISOU  652  N   ASP A  71     2166    604    886    253    213    116       N  
ATOM    653  CA  ASP A  71       4.735  22.939  20.304  1.00 10.42           C  
ANISOU  653  CA  ASP A  71     2372    723    862    222    333    105       C  
ATOM    654  C   ASP A  71       4.074  21.664  19.812  1.00 10.84           C  
ANISOU  654  C   ASP A  71     2202   1002    913     70    220     90       C  
ATOM    655  O   ASP A  71       3.346  21.650  18.814  1.00 11.96           O  
ANISOU  655  O   ASP A  71     2423    985   1137     49     38    157       O  
ATOM    656  CB  ASP A  71       3.658  23.735  20.996  1.00 11.02           C  
ANISOU  656  CB  ASP A  71     2280    962    943    249    213    139       C  
ATOM    657  CG  ASP A  71       4.194  24.988  21.614  1.00 11.44           C  
ANISOU  657  CG  ASP A  71     2387   1138    819    170    -24    -99       C  
ATOM    658  OD1 ASP A  71       5.164  24.844  22.451  1.00 14.18           O  
ANISOU  658  OD1 ASP A  71     3012   1093   1283    315   -268   -247       O  
ATOM    659  OD2 ASP A  71       3.652  26.082  21.397  1.00 12.06           O  
ANISOU  659  OD2 ASP A  71     2555    900   1127    184     14     39       O  
ATOM    660  N   GLU A  72       4.314  20.578  20.556  1.00 11.06           N  
ANISOU  660  N   GLU A  72     2354    834   1011    136    225    291       N  
ATOM    661  CA  GLU A  72       3.767  19.267  20.219  1.00 11.91           C  
ANISOU  661  CA  GLU A  72     2242    974   1309     61    165    473       C  
ATOM    662  C   GLU A  72       3.248  18.600  21.500  1.00 13.11           C  
ANISOU  662  C   GLU A  72     2409   1015   1555    168    180    476       C  
ATOM    663  O   GLU A  72       3.897  18.662  22.519  1.00 13.75           O  
ANISOU  663  O   GLU A  72     2545   1344   1333     52    349    419       O  
ATOM    664  CB  GLU A  72       4.857  18.420  19.531  1.00 11.10           C  
ANISOU  664  CB  GLU A  72     2207   1008   1001     54    217    226       C  
ATOM    665  CG  GLU A  72       4.493  16.960  19.246  1.00 11.31           C  
ANISOU  665  CG  GLU A  72     2372   1012    912      2    101    271       C  
ATOM    666  CD  GLU A  72       5.573  16.163  18.574  1.00 11.94           C  
ANISOU  666  CD  GLU A  72     2475   1178    881    171    202    181       C  
ATOM    667  OE1 GLU A  72       6.729  16.608  18.487  1.00 12.35           O  
ANISOU  667  OE1 GLU A  72     2336   1241   1113     57    188    -97       O  
ATOM    668  OE2 GLU A  72       5.295  14.992  18.135  1.00 13.51           O  
ANISOU  668  OE2 GLU A  72     2759    859   1516     48    278    -32       O  
ATOM    669  N  AVAL A  73       2.036  18.088  21.591  0.50 13.80           N  
ANISOU  669  N  AVAL A  73     2391   1303   1549    177    170    478       N  
ATOM    670  N  BVAL A  73       2.137  17.868  21.228  0.50 13.55           N  
ANISOU  670  N  BVAL A  73     2173   1119   1853    214    290    766       N  
ATOM    671  CA AVAL A  73       1.696  17.240  22.749  0.50 11.92           C  
ANISOU  671  CA AVAL A  73     2347   1008   1174    186    200    356       C  
ATOM    672  CA BVAL A  73       1.531  16.928  22.153  0.50 13.69           C  
ANISOU  672  CA BVAL A  73     2168   1142   1890    130    244    742       C  
ATOM    673  C  AVAL A  73       1.734  15.782  22.145  0.50 12.59           C  
ANISOU  673  C  AVAL A  73     2323   1282   1179    143    314    431       C  
ATOM    674  C  BVAL A  73       1.833  15.561  21.694  0.50 13.90           C  
ANISOU  674  C  BVAL A  73     2259   1237   1782     52    162    734       C  
ATOM    675  O  AVAL A  73       1.012  15.474  21.262  0.50 11.33           O  
ANISOU  675  O  AVAL A  73     2472   1025    808    135    169    -24       O  
ATOM    676  O  BVAL A  73       1.367  15.104  20.572  0.50 14.21           O  
ANISOU  676  O  BVAL A  73     2373    799   2226     64     28    693       O  
ATOM    677  CB AVAL A  73       0.319  17.577  23.249  0.50 12.21           C  
ANISOU  677  CB AVAL A  73     2348   1147   1142    167    262    309       C  
ATOM    678  CB BVAL A  73       0.030  17.090  22.325  0.50 14.30           C  
ANISOU  678  CB BVAL A  73     2204   1264   1965    189    202    652       C  
ATOM    679  CG1AVAL A  73      -0.070  16.608  24.369  0.50 13.11           C  
ANISOU  679  CG1AVAL A  73     2467   1297   1216     23    468    124       C  
ATOM    680  CG1BVAL A  73      -0.498  16.056  23.345  0.50 16.87           C  
ANISOU  680  CG1BVAL A  73     2434   1640   2336    -90    359    562       C  
ATOM    681  CG2AVAL A  73       0.229  19.030  23.763  0.50 13.78           C  
ANISOU  681  CG2AVAL A  73     2581   1129   1522    232    324     49       C  
ATOM    682  CG2BVAL A  73      -0.237  18.467  22.782  0.50 16.30           C  
ANISOU  682  CG2BVAL A  73     2307   1653   2230    191    417    586       C  
ATOM    683  N   THR A  74       2.647  14.913  22.532  1.00 13.22           N  
ANISOU  683  N   THR A  74     2313   1446   1264    269    202    603       N  
ATOM    684  CA  THR A  74       2.978  13.594  22.029  1.00 12.87           C  
ANISOU  684  CA  THR A  74     2384   1487   1017     34    146    458       C  
ATOM    685  C   THR A  74       1.884  12.575  22.385  1.00 13.43           C  
ANISOU  685  C   THR A  74     2261   1623   1216    138     48    471       C  
ATOM    686  O   THR A  74       0.989  12.844  23.171  1.00 14.47           O  
ANISOU  686  O   THR A  74     2404   1582   1510    152    353    659       O  
ATOM    687  CB  THR A  74       4.333  13.105  22.589  1.00 11.54           C  
ANISOU  687  CB  THR A  74     2370   1214    801     81    132    232       C  
ATOM    688  OG1 THR A  74       4.170  12.920  23.992  1.00 12.02           O  
ANISOU  688  OG1 THR A  74     2464   1181    920    227    166    297       O  
ATOM    689  CG2 THR A  74       5.421  14.108  22.305  1.00 12.35           C  
ANISOU  689  CG2 THR A  74     2443   1060   1189     77    175    181       C  
ATOM    690  N   ALA A  75       1.943  11.403  21.750  1.00 14.05           N  
ANISOU  690  N   ALA A  75     2408   1860   1069    -53    129    515       N  
ATOM    691  CA  ALA A  75       0.929  10.339  21.933  1.00 14.58           C  
ANISOU  691  CA  ALA A  75     2425   1908   1205   -139     33    446       C  
ATOM    692  C   ALA A  75       0.834   9.945  23.413  1.00 14.85           C  
ANISOU  692  C   ALA A  75     2472   1787   1382   -154     -2    464       C  
ATOM    693  O   ALA A  75      -0.261   9.666  23.886  1.00 17.26           O  
ANISOU  693  O   ALA A  75     2724   2312   1521   -346    206    546       O  
ATOM    694  CB  ALA A  75       1.245   9.161  21.096  1.00 14.88           C  
ANISOU  694  CB  ALA A  75     2536   1823   1293   -186    -33    328       C  
ATOM    695  N   ASP A  76       1.970   9.931  24.119  1.00 14.09           N  
ANISOU  695  N   ASP A  76     2619   1587   1146   -179     33    513       N  
ATOM    696  CA  ASP A  76       2.032   9.626  25.552  1.00 14.60           C  
ANISOU  696  CA  ASP A  76     2753   1646   1147   -247     66    424       C  
ATOM    697  C   ASP A  76       1.787  10.885  26.435  1.00 14.77           C  
ANISOU  697  C   ASP A  76     2880   1754    978   -285    287    458       C  
ATOM    698  O   ASP A  76       1.956  10.845  27.616  1.00 17.28           O  
ANISOU  698  O   ASP A  76     3301   2083   1178   -125    205    392       O  
ATOM    699  CB  ASP A  76       3.377   8.980  25.911  1.00 14.80           C  
ANISOU  699  CB  ASP A  76     2878   1342   1401   -297    -43    478       C  
ATOM    700  CG  ASP A  76       4.559   9.838  25.610  1.00 13.39           C  
ANISOU  700  CG  ASP A  76     2943   1054   1089     43   -205    357       C  
ATOM    701  OD1 ASP A  76       4.666  10.323  24.446  1.00 12.80           O  
ANISOU  701  OD1 ASP A  76     2688   1142   1033      5    -96    334       O  
ATOM    702  OD2 ASP A  76       5.378  10.082  26.519  1.00 14.49           O  
ANISOU  702  OD2 ASP A  76     3279   1051   1175   -185   -261    469       O  
ATOM    703  N   ASP A  77       1.367  12.001  25.837  1.00 15.56           N  
ANISOU  703  N   ASP A  77     2831   1865   1216   -145    508    400       N  
ATOM    704  CA  ASP A  77       0.888  13.169  26.562  1.00 17.31           C  
ANISOU  704  CA  ASP A  77     2835   2158   1582    -69    679    306       C  
ATOM    705  C   ASP A  77       1.978  14.023  27.151  1.00 16.12           C  
ANISOU  705  C   ASP A  77     2958   1712   1454     65    681    198       C  
ATOM    706  O   ASP A  77       1.726  14.785  28.080  1.00 19.79           O  
ANISOU  706  O   ASP A  77     3256   2173   2088      2    875   -301       O  
ATOM    707  CB  ASP A  77      -0.185  12.859  27.591  1.00 19.29           C  
ANISOU  707  CB  ASP A  77     2999   2429   1901   -219    764    338       C  
ATOM    708  CG  ASP A  77      -1.142  14.027  27.789  1.00 23.21           C  
ANISOU  708  CG  ASP A  77     3283   2966   2568   -304   1028    315       C  
ATOM    709  OD1 ASP A  77      -1.700  14.119  28.905  1.00 28.68           O  
ANISOU  709  OD1 ASP A  77     3694   4145   3056     94   1509    -49       O  
ATOM    710  OD2 ASP A  77      -1.350  14.864  26.859  1.00 28.22           O  
ANISOU  710  OD2 ASP A  77     3644   3702   3375   -163    986    493       O  
ATOM    711  N   ARG A  78       3.184  13.978  26.597  1.00 14.30           N  
ANISOU  711  N   ARG A  78     2881   1404   1147    190    602    323       N  
ATOM    712  CA  ARG A  78       4.194  14.964  26.931  1.00 13.87           C  
ANISOU  712  CA  ARG A  78     2926   1336   1005    179    574    306       C  
ATOM    713  C   ARG A  78       3.941  16.236  26.149  1.00 13.68           C  
ANISOU  713  C   ARG A  78     2897   1183   1116    386    612    285       C  
ATOM    714  O   ARG A  78       3.555  16.199  24.982  1.00 15.06           O  
ANISOU  714  O   ARG A  78     3339   1204   1178    439    482    275       O  
ATOM    715  CB  ARG A  78       5.591  14.508  26.626  1.00 12.84           C  
ANISOU  715  CB  ARG A  78     2749   1163    966    100    345    337       C  
ATOM    716  CG  ARG A  78       6.144  13.437  27.538  1.00 12.64           C  
ANISOU  716  CG  ARG A  78     2845    960    995    -66    226    306       C  
ATOM    717  CD  ARG A  78       7.503  12.914  27.021  1.00 12.98           C  
ANISOU  717  CD  ARG A  78     2797   1146    987     81     12    266       C  
ATOM    718  NE  ARG A  78       7.238  12.024  25.883  1.00 11.97           N  
ANISOU  718  NE  ARG A  78     2700   1001    846    152    -13     65       N  
ATOM    719  CZ  ARG A  78       7.797  12.095  24.674  1.00 11.67           C  
ANISOU  719  CZ  ARG A  78     2391    982   1060    265    -79    120       C  
ATOM    720  NH1 ARG A  78       8.820  12.908  24.441  1.00 12.38           N  
ANISOU  720  NH1 ARG A  78     2515   1167   1021     52    -53     75       N  
ATOM    721  NH2 ARG A  78       7.327  11.299  23.731  1.00 12.17           N  
ANISOU  721  NH2 ARG A  78     2671    957    995    110   -167    -55       N  
ATOM    722  N   LYS A  79       4.175  17.387  26.786  1.00 14.20           N  
ANISOU  722  N   LYS A  79     2998   1255   1141    309    678    245       N  
ATOM    723  CA  LYS A  79       4.125  18.699  26.121  1.00 14.29           C  
ANISOU  723  CA  LYS A  79     2889   1187   1351    430    642    117       C  
ATOM    724  C   LYS A  79       5.554  19.077  25.830  1.00 13.43           C  
ANISOU  724  C   LYS A  79     2811   1048   1241    326    504     63       C  
ATOM    725  O   LYS A  79       6.345  19.371  26.755  1.00 15.84           O  
ANISOU  725  O   LYS A  79     3225   1711   1079    147    522   -119       O  
ATOM    726  CB  LYS A  79       3.462  19.696  27.027  1.00 16.27           C  
ANISOU  726  CB  LYS A  79     3120   1386   1676    434    818    161       C  
ATOM    727  CG  LYS A  79       1.977  19.397  27.242  1.00 23.20           C  
ANISOU  727  CG  LYS A  79     3436   2467   2910    612    699   -320       C  
ATOM    728  CD  LYS A  79       1.605  18.157  27.976  1.00 29.45           C  
ANISOU  728  CD  LYS A  79     4070   3314   3806    317    389    -60       C  
ATOM    729  CE  LYS A  79       0.128  18.224  28.367  1.00 32.54           C  
ANISOU  729  CE  LYS A  79     4186   4017   4161    107    385    121       C  
ATOM    730  NZ  LYS A  79      -0.566  16.941  28.177  1.00 34.02           N  
ANISOU  730  NZ  LYS A  79     4607   3982   4336     34    365    135       N  
ATOM    731  N   VAL A  80       5.941  19.014  24.556  1.00 12.00           N  
ANISOU  731  N   VAL A  80     2662   1038    858    259    414    141       N  
ATOM    732  CA  VAL A  80       7.326  19.167  24.183  1.00 10.90           C  
ANISOU  732  CA  VAL A  80     2572    809    760    305    240    121       C  
ATOM    733  C   VAL A  80       7.493  20.352  23.212  1.00 10.62           C  
ANISOU  733  C   VAL A  80     2447    921    666    302    162   -106       C  
ATOM    734  O   VAL A  80       6.529  20.778  22.582  1.00 11.63           O  
ANISOU  734  O   VAL A  80     2579    855    985    209    213     94       O  
ATOM    735  CB  VAL A  80       7.883  17.836  23.536  1.00 11.24           C  
ANISOU  735  CB  VAL A  80     2543    829    898    134    302    145       C  
ATOM    736  CG1 VAL A  80       7.596  16.650  24.455  1.00 12.56           C  
ANISOU  736  CG1 VAL A  80     3110    808    851    206    151    239       C  
ATOM    737  CG2 VAL A  80       7.284  17.601  22.196  1.00 11.54           C  
ANISOU  737  CG2 VAL A  80     2712    877    794    178    247    104       C  
ATOM    738  N   LYS A  81       8.725  20.787  23.104  1.00 10.22           N  
ANISOU  738  N   LYS A  81     2465    767    648    229    110     18       N  
ATOM    739  CA  LYS A  81       9.141  21.742  22.088  1.00 10.22           C  
ANISOU  739  CA  LYS A  81     2705    558    617    231    121    -18       C  
ATOM    740  C   LYS A  81       9.945  20.970  21.063  1.00  9.65           C  
ANISOU  740  C   LYS A  81     2433    557    675     86     18     53       C  
ATOM    741  O   LYS A  81      10.960  20.356  21.405  1.00 10.71           O  
ANISOU  741  O   LYS A  81     2497    901    671    207   -108      3       O  
ATOM    742  CB  LYS A  81       9.981  22.876  22.696  1.00 12.46           C  
ANISOU  742  CB  LYS A  81     3056    697    981     94    163   -201       C  
ATOM    743  CG  LYS A  81       9.356  23.686  23.686  1.00 17.51           C  
ANISOU  743  CG  LYS A  81     3600   1310   1740    122     88   -477       C  
ATOM    744  CD  LYS A  81       8.419  24.686  23.155  1.00 20.41           C  
ANISOU  744  CD  LYS A  81     3550   2313   1890    150    -99   -240       C  
ATOM    745  CE  LYS A  81       7.749  25.457  24.304  1.00 23.09           C  
ANISOU  745  CE  LYS A  81     3700   2733   2339    329   -197   -467       C  
ATOM    746  NZ  LYS A  81       6.779  26.486  23.888  1.00 23.75           N  
ANISOU  746  NZ  LYS A  81     4087   2386   2551    339   -755   -430       N  
ATOM    747  N   SER A  82       9.494  21.020  19.817  1.00  9.04           N  
ANISOU  747  N   SER A  82     2246    609    580    198     75     52       N  
ATOM    748  CA  SER A  82      10.041  20.190  18.771  1.00  8.78           C  
ANISOU  748  CA  SER A  82     2199    440    695    185     24     19       C  
ATOM    749  C   SER A  82      10.625  21.012  17.666  1.00  8.06           C  
ANISOU  749  C   SER A  82     2045    497    520      8     29     72       C  
ATOM    750  O   SER A  82      10.109  22.057  17.276  1.00  8.74           O  
ANISOU  750  O   SER A  82     2097    513    709     69     40     84       O  
ATOM    751  CB  SER A  82       8.938  19.307  18.182  1.00  9.55           C  
ANISOU  751  CB  SER A  82     2294    619    714     76    211     84       C  
ATOM    752  OG  SER A  82       8.575  18.350  19.149  1.00 11.84           O  
ANISOU  752  OG  SER A  82     2526    756   1215     96    266    285       O  
ATOM    753  N   THR A  83      11.693  20.478  17.067  1.00  8.32           N  
ANISOU  753  N   THR A  83     2033    586    543     74    -41     32       N  
ATOM    754  CA  THR A  83      12.281  21.048  15.848  1.00  8.72           C  
ANISOU  754  CA  THR A  83     2158    584    567     30     -7     27       C  
ATOM    755  C   THR A  83      12.630  19.905  14.928  1.00  8.81           C  
ANISOU  755  C   THR A  83     2211    518    615     64    107     95       C  
ATOM    756  O   THR A  83      13.259  18.926  15.367  1.00  9.53           O  
ANISOU  756  O   THR A  83     2372    663    583    205    -17     12       O  
ATOM    757  CB  THR A  83      13.564  21.881  16.172  1.00 10.38           C  
ANISOU  757  CB  THR A  83     2163    680   1101    -86    120    -49       C  
ATOM    758  OG1 THR A  83      13.301  22.783  17.219  1.00 11.93           O  
ANISOU  758  OG1 THR A  83     2474    825   1234   -238      8   -274       O  
ATOM    759  CG2 THR A  83      13.999  22.598  14.940  1.00 13.53           C  
ANISOU  759  CG2 THR A  83     2788    855   1494   -199    294    -93       C  
ATOM    760  N   ILE A  84      12.190  19.989  13.674  1.00  8.31           N  
ANISOU  760  N   ILE A  84     2185    517    455     99    -26     -9       N  
ATOM    761  CA  ILE A  84      12.431  18.961  12.698  1.00  8.42           C  
ANISOU  761  CA  ILE A  84     2241    449    508    106     21     43       C  
ATOM    762  C   ILE A  84      13.227  19.573  11.570  1.00  8.95           C  
ANISOU  762  C   ILE A  84     2329    575    494     -8     69     -3       C  
ATOM    763  O   ILE A  84      12.881  20.626  11.033  1.00  9.08           O  
ANISOU  763  O   ILE A  84     2325    476    646     70     15    108       O  
ATOM    764  CB  ILE A  84      11.117  18.343  12.182  1.00  9.05           C  
ANISOU  764  CB  ILE A  84     2310    567    559    101     49     99       C  
ATOM    765  CG1 ILE A  84      10.338  17.770  13.381  1.00  8.71           C  
ANISOU  765  CG1 ILE A  84     2127    628    553     75    -36    151       C  
ATOM    766  CG2 ILE A  84      11.411  17.267  11.130  1.00  9.85           C  
ANISOU  766  CG2 ILE A  84     2356    702    683     79    128    -59       C  
ATOM    767  CD1 ILE A  84       9.042  17.192  13.046  1.00 10.10           C  
ANISOU  767  CD1 ILE A  84     2214    895    727     23     91    213       C  
ATOM    768  N   THR A  85      14.323  18.892  11.203  1.00  9.27           N  
ANISOU  768  N   THR A  85     2365    549    608     52    174     86       N  
ATOM    769  CA  THR A  85      15.215  19.304  10.116  1.00  9.90           C  
ANISOU  769  CA  THR A  85     2360    696    705     26    134     -8       C  
ATOM    770  C   THR A  85      15.457  18.104   9.216  1.00  9.92           C  
ANISOU  770  C   THR A  85     2455    557    756    -75    195     66       C  
ATOM    771  O   THR A  85      15.125  16.974   9.541  1.00 10.86           O  
ANISOU  771  O   THR A  85     2773    653    699     39    382     24       O  
ATOM    772  CB  THR A  85      16.518  19.823  10.660  1.00 11.33           C  
ANISOU  772  CB  THR A  85     2376    849   1079     41    249      4       C  
ATOM    773  OG1 THR A  85      17.101  18.840  11.501  1.00 14.41           O  
ANISOU  773  OG1 THR A  85     2719   1319   1435    235   -114    -68       O  
ATOM    774  CG2 THR A  85      16.314  21.176  11.394  1.00 13.35           C  
ANISOU  774  CG2 THR A  85     2624    983   1464   -131    125   -440       C  
ATOM    775  N  ALEU A  86      15.744  18.408   7.944  0.50 10.20           N  
ANISOU  775  N  ALEU A  86     2417    693    764   -111    307     36       N  
ATOM    776  N  BLEU A  86      16.243  18.315   8.147  0.50 10.26           N  
ANISOU  776  N  BLEU A  86     2327    745    825    -89    359    -25       N  
ATOM    777  CA ALEU A  86      16.158  17.413   6.960  0.50 10.81           C  
ANISOU  777  CA ALEU A  86     2351    863    893   -118    255   -106       C  
ATOM    778  CA BLEU A  86      16.827  17.225   7.358  0.50 10.50           C  
ANISOU  778  CA BLEU A  86     2157    789   1043   -146    300   -240       C  
ATOM    779  C  ALEU A  86      17.673  17.400   6.865  0.50 12.63           C  
ANISOU  779  C  ALEU A  86     2372   1022   1402   -124    358   -133       C  
ATOM    780  C  BLEU A  86      18.317  17.154   7.616  0.50 10.88           C  
ANISOU  780  C  BLEU A  86     2123    883   1127   -177    386    -96       C  
ATOM    781  O  ALEU A  86      18.262  18.395   6.403  0.50 16.36           O  
ANISOU  781  O  ALEU A  86     2857   1044   2315   -212    625   -160       O  
ATOM    782  O  BLEU A  86      18.986  18.201   7.619  0.50 13.44           O  
ANISOU  782  O  BLEU A  86     2459   1065   1581   -340    363   -317       O  
ATOM    783  CB ALEU A  86      15.604  17.730   5.619  0.50 12.23           C  
ANISOU  783  CB ALEU A  86     2570   1176    899   -226     77     87       C  
ATOM    784  CB BLEU A  86      16.579  17.452   5.868  0.50 10.61           C  
ANISOU  784  CB BLEU A  86     2159   1000    870   -103    570     32       C  
ATOM    785  CG ALEU A  86      14.490  16.905   5.040  0.50 16.65           C  
ANISOU  785  CG ALEU A  86     2809   1676   1840   -316   -325    110       C  
ATOM    786  CG BLEU A  86      15.135  17.247   5.442  0.50 10.83           C  
ANISOU  786  CG BLEU A  86     2318   1017    779   -497    130    -11       C  
ATOM    787  CD1ALEU A  86      14.200  17.462   3.635  0.50 15.83           C  
ANISOU  787  CD1ALEU A  86     2846   1596   1572   -239   -353    312       C  
ATOM    788  CD1BLEU A  86      14.921  17.864   4.058  0.50 12.81           C  
ANISOU  788  CD1BLEU A  86     2676   1225    965     23    421      5       C  
ATOM    789  CD2ALEU A  86      14.775  15.387   5.034  0.50 14.65           C  
ANISOU  789  CD2ALEU A  86     3171   1108   1286   -329   -134   -116       C  
ATOM    790  CD2BLEU A  86      14.842  15.701   5.362  0.50 13.81           C  
ANISOU  790  CD2BLEU A  86     3081   1215    950   -167    472    -10       C  
ATOM    791  N  AASP A  87      18.297  16.288   7.251  0.50 12.56           N  
ANISOU  791  N  AASP A  87     2314   1141   1315    -78    336   -343       N  
ATOM    792  N  BASP A  87      18.831  15.919   7.764  0.50 11.50           N  
ANISOU  792  N  BASP A  87     1952   1161   1255   -224    257   -235       N  
ATOM    793  CA AASP A  87      19.753  16.158   7.343  0.50 14.88           C  
ANISOU  793  CA AASP A  87     2472   1640   1538   -134    196   -440       C  
ATOM    794  CA BASP A  87      20.251  15.611   7.828  0.50 12.96           C  
ANISOU  794  CA BASP A  87     2144   1345   1434   -133    108   -182       C  
ATOM    795  C  AASP A  87      20.124  15.040   6.400  0.50 13.97           C  
ANISOU  795  C  AASP A  87     2382   1590   1334   -102    215   -365       C  
ATOM    796  C  BASP A  87      20.455  14.689   6.656  0.50 12.82           C  
ANISOU  796  C  BASP A  87     2213   1333   1322    -96    127    -74       C  
ATOM    797  O  AASP A  87      19.938  13.852   6.681  0.50 14.65           O  
ANISOU  797  O  AASP A  87     2523   1577   1466   -340    213   -248       O  
ATOM    798  O  BASP A  87      20.096  13.514   6.713  0.50 14.54           O  
ANISOU  798  O  BASP A  87     2444   1372   1706   -219    272    -10       O  
ATOM    799  CB AASP A  87      20.174  15.873   8.800  0.50 17.02           C  
ANISOU  799  CB AASP A  87     2738   1941   1785   -131    175   -481       C  
ATOM    800  CB BASP A  87      20.607  14.893   9.138  0.50 14.85           C  
ANISOU  800  CB BASP A  87     2280   1738   1623   -112     40     12       C  
ATOM    801  CG AASP A  87      21.662  15.551   8.965  0.50 21.82           C  
ANISOU  801  CG AASP A  87     3146   2637   2506    -42    -26   -285       C  
ATOM    802  CG BASP A  87      22.048  14.418   9.185  0.50 18.69           C  
ANISOU  802  CG BASP A  87     2869   2000   2230     82    -43   -270       C  
ATOM    803  OD1AASP A  87      22.496  15.982   8.138  0.50 26.95           O  
ANISOU  803  OD1AASP A  87     3809   3125   3303   -122    118   -123       O  
ATOM    804  OD1BASP A  87      22.852  14.868   8.352  0.50 23.37           O  
ANISOU  804  OD1BASP A  87     2859   2958   3061     40   -147     64       O  
ATOM    805  OD2AASP A  87      22.008  14.858   9.948  0.50 27.97           O  
ANISOU  805  OD2AASP A  87     4028   3532   3064     65     85     44       O  
ATOM    806  OD2BASP A  87      22.384  13.614  10.082  0.50 24.26           O  
ANISOU  806  OD2BASP A  87     3245   2998   2973     82   -296    208       O  
ATOM    807  N  AGLY A  88      20.598  15.430   5.221  0.50 12.75           N  
ANISOU  807  N  AGLY A  88     2244   1380   1219   -121    244   -199       N  
ATOM    808  N  BGLY A  88      20.986  15.204   5.556  0.50 13.05           N  
ANISOU  808  N  BGLY A  88     2104   1231   1622    -78    316      7       N  
ATOM    809  CA AGLY A  88      20.738  14.525   4.153  0.50 13.85           C  
ANISOU  809  CA AGLY A  88     2299   1642   1319    -59    342   -138       C  
ATOM    810  CA BGLY A  88      21.188  14.345   4.411  0.50 14.05           C  
ANISOU  810  CA BGLY A  88     2295   1614   1428    -81    192    -26       C  
ATOM    811  C  AGLY A  88      19.341  14.147   3.835  0.50 13.01           C  
ANISOU  811  C  AGLY A  88     2289   1622   1031   -119    377   -224       C  
ATOM    812  C  BGLY A  88      20.030  13.392   4.096  0.50 13.32           C  
ANISOU  812  C  BGLY A  88     2281   1671   1107     19    266    -75       C  
ATOM    813  O  AGLY A  88      18.488  14.991   3.712  0.50 14.27           O  
ANISOU  813  O  AGLY A  88     2576   1815   1030     -2    293    153       O  
ATOM    814  O  BGLY A  88      20.231  12.167   4.033  0.50 14.89           O  
ANISOU  814  O  BGLY A  88     2653   1599   1405    118    114   -320       O  
ATOM    815  N  AGLY A  89      19.124  12.846   3.671  0.50 12.97           N  
ANISOU  815  N  AGLY A  89     2288   1680    957   -275    494   -320       N  
ATOM    816  N  BGLY A  89      18.835  13.925   3.838  0.50 13.73           N  
ANISOU  816  N  BGLY A  89     2384   1882    947     48    404      0       N  
ATOM    817  CA AGLY A  89      17.814  12.229   3.459  0.50 13.88           C  
ANISOU  817  CA AGLY A  89     2452   1850    968   -317    312   -547       C  
ATOM    818  CA BGLY A  89      17.725  13.085   3.430  0.50 12.98           C  
ANISOU  818  CA BGLY A  89     2574   1745    610    -34    373   -185       C  
ATOM    819  C  AGLY A  89      17.051  11.864   4.705  0.50 14.07           C  
ANISOU  819  C  AGLY A  89     2456   1811   1076   -430    361   -573       C  
ATOM    820  C  BGLY A  89      16.972  12.335   4.580  0.50 13.88           C  
ANISOU  820  C  BGLY A  89     2472   1888    914   -260    262   -240       C  
ATOM    821  O  AGLY A  89      16.083  11.097   4.651  0.50 15.59           O  
ANISOU  821  O  AGLY A  89     2599   2167   1157   -398    218   -850       O  
ATOM    822  O  BGLY A  89      15.959  11.735   4.299  0.50 15.35           O  
ANISOU  822  O  BGLY A  89     2597   2461    773   -499     14   -308       O  
ATOM    823  N   VAL A  90      17.454  12.383   5.854  1.00 12.72           N  
ANISOU  823  N   VAL A  90     2431   1577    823   -365    338   -383       N  
ATOM    824  CA  VAL A  90      16.825  11.897   7.060  1.00 11.60           C  
ANISOU  824  CA  VAL A  90     2361   1140    906   -282    367   -284       C  
ATOM    825  C   VAL A  90      16.098  13.017   7.741  1.00  9.88           C  
ANISOU  825  C   VAL A  90     2295    830    630   -128    150   -146       C  
ATOM    826  O   VAL A  90      16.660  14.094   7.971  1.00 10.87           O  
ANISOU  826  O   VAL A  90     2557    800    772   -200    283   -125       O  
ATOM    827  CB  VAL A  90      17.884  11.316   8.043  1.00 12.48           C  
ANISOU  827  CB  VAL A  90     2517    964   1261   -112    399   -153       C  
ATOM    828  CG1 VAL A  90      17.236  10.817   9.314  1.00 12.35           C  
ANISOU  828  CG1 VAL A  90     2430   1039   1222     11    261     93       C  
ATOM    829  CG2 VAL A  90      18.700  10.222   7.402  1.00 15.83           C  
ANISOU  829  CG2 VAL A  90     2615   1348   2050     53    649   -388       C  
ATOM    830  N   LEU A  91      14.808  12.825   8.043  1.00  9.38           N  
ANISOU  830  N   LEU A  91     2290    723    551   -201    106   -110       N  
ATOM    831  CA  LEU A  91      14.089  13.795   8.855  1.00  9.26           C  
ANISOU  831  CA  LEU A  91     2223    632    663    -45     47    148       C  
ATOM    832  C   LEU A  91      14.483  13.548  10.323  1.00  8.76           C  
ANISOU  832  C   LEU A  91     2150    703    475    128    176     91       C  
ATOM    833  O   LEU A  91      14.310  12.430  10.820  1.00  9.40           O  
ANISOU  833  O   LEU A  91     2441    596    532     31    156     56       O  
ATOM    834  CB  LEU A  91      12.601  13.630   8.702  1.00 11.00           C  
ANISOU  834  CB  LEU A  91     2465    858    853     -4     51    360       C  
ATOM    835  CG  LEU A  91      11.936  14.199   7.471  1.00 12.14           C  
ANISOU  835  CG  LEU A  91     2659   1135    817     32     27    -92       C  
ATOM    836  CD1 LEU A  91      10.551  13.658   7.343  1.00 14.83           C  
ANISOU  836  CD1 LEU A  91     2759   1586   1288      8     -3     56       C  
ATOM    837  CD2 LEU A  91      11.923  15.686   7.596  1.00 12.74           C  
ANISOU  837  CD2 LEU A  91     2568    661   1608    223     18    160       C  
ATOM    838  N   VAL A  92      14.982  14.587  10.969  1.00  9.01           N  
ANISOU  838  N   VAL A  92     2292    631    499    143    108     32       N  
ATOM    839  CA  VAL A  92      15.483  14.493  12.332  1.00  9.29           C  
ANISOU  839  CA  VAL A  92     2279    686    564    179     95     30       C  
ATOM    840  C   VAL A  92      14.558  15.332  13.218  1.00  8.90           C  
ANISOU  840  C   VAL A  92     2386    435    558    214    -31     39       C  
ATOM    841  O   VAL A  92      14.513  16.582  13.030  1.00 10.19           O  
ANISOU  841  O   VAL A  92     2515    640    717    182    202     93       O  
ATOM    842  CB  VAL A  92      16.936  14.945  12.427  1.00 10.47           C  
ANISOU  842  CB  VAL A  92     2320   1012    643    193     15    -72       C  
ATOM    843  CG1 VAL A  92      17.456  14.868  13.877  1.00 12.44           C  
ANISOU  843  CG1 VAL A  92     2336   1387   1002     94     10     -4       C  
ATOM    844  CG2 VAL A  92      17.853  14.155  11.490  1.00 12.21           C  
ANISOU  844  CG2 VAL A  92     2364   1273   1003    194    164   -211       C  
ATOM    845  N   HIS A  93      13.891  14.720  14.142  1.00  8.83           N  
ANISOU  845  N   HIS A  93     2516    358    478    225     57     73       N  
ATOM    846  CA  HIS A  93      12.856  15.344  14.988  1.00  8.85           C  
ANISOU  846  CA  HIS A  93     2260    598    505    217     78    138       C  
ATOM    847  C   HIS A  93      13.324  15.301  16.418  1.00  8.94           C  
ANISOU  847  C   HIS A  93     2334    587    473    247     74     78       C  
ATOM    848  O   HIS A  93      13.397  14.227  17.015  1.00  9.43           O  
ANISOU  848  O   HIS A  93     2546    519    518    141    -68     80       O  
ATOM    849  CB  HIS A  93      11.572  14.572  14.766  1.00  9.22           C  
ANISOU  849  CB  HIS A  93     2315    673    514    266     41    143       C  
ATOM    850  CG  HIS A  93      10.374  14.969  15.538  1.00  9.96           C  
ANISOU  850  CG  HIS A  93     2261    786    736    222    -31    297       C  
ATOM    851  ND1 HIS A  93       9.213  14.256  15.309  1.00 12.08           N  
ANISOU  851  ND1 HIS A  93     2350   1195   1045    394    221    407       N  
ATOM    852  CD2 HIS A  93      10.098  15.928  16.476  1.00 10.55           C  
ANISOU  852  CD2 HIS A  93     2502    737    770    354    201    227       C  
ATOM    853  CE1 HIS A  93       8.275  14.755  16.065  1.00 12.71           C  
ANISOU  853  CE1 HIS A  93     2531   1225   1072    359    185    398       C  
ATOM    854  NE2 HIS A  93       8.756  15.774  16.777  1.00 12.85           N  
ANISOU  854  NE2 HIS A  93     2694   1191    995    657    501    529       N  
ATOM    855  N   VAL A  94      13.643  16.468  16.980  1.00  8.88           N  
ANISOU  855  N   VAL A  94     2313    564    495    171     22      8       N  
ATOM    856  CA  VAL A  94      14.127  16.557  18.353  1.00  9.09           C  
ANISOU  856  CA  VAL A  94     2280    630    541    108     24     26       C  
ATOM    857  C   VAL A  94      13.012  17.122  19.203  1.00  8.60           C  
ANISOU  857  C   VAL A  94     2315    396    554    103    -35     47       C  
ATOM    858  O   VAL A  94      12.462  18.165  18.875  1.00 10.42           O  
ANISOU  858  O   VAL A  94     2604    670    685    260    264    212       O  
ATOM    859  CB  VAL A  94      15.409  17.392  18.438  1.00 10.30           C  
ANISOU  859  CB  VAL A  94     2256    716    940     63     30      0       C  
ATOM    860  CG1 VAL A  94      15.939  17.444  19.858  1.00 13.97           C  
ANISOU  860  CG1 VAL A  94     2380   1765   1161    -62   -235   -241       C  
ATOM    861  CG2 VAL A  94      16.480  16.936  17.453  1.00 14.34           C  
ANISOU  861  CG2 VAL A  94     2742   1373   1333    246    174    115       C  
ATOM    862  N   GLN A  95      12.689  16.430  20.301  1.00  8.68           N  
ANISOU  862  N   GLN A  95     2324    429    543    199    -57     41       N  
ATOM    863  CA  GLN A  95      11.674  16.855  21.272  1.00  8.84           C  
ANISOU  863  CA  GLN A  95     2321    540    498     83     23     14       C  
ATOM    864  C   GLN A  95      12.366  17.183  22.583  1.00  9.33           C  
ANISOU  864  C   GLN A  95     2378    605    559     45    -10     37       C  
ATOM    865  O   GLN A  95      13.107  16.349  23.124  1.00 10.49           O  
ANISOU  865  O   GLN A  95     2600    725    659    176    -98    -21       O  
ATOM    866  CB  GLN A  95      10.700  15.715  21.521  1.00  9.30           C  
ANISOU  866  CB  GLN A  95     2361    619    553     82     67     69       C  
ATOM    867  CG  GLN A  95       9.888  15.289  20.312  1.00  9.53           C  
ANISOU  867  CG  GLN A  95     2323    638    659    152    -10     -9       C  
ATOM    868  CD  GLN A  95       8.973  14.117  20.540  1.00  9.89           C  
ANISOU  868  CD  GLN A  95     2307    616    833    -10     64    140       C  
ATOM    869  OE1 GLN A  95       7.969  13.955  19.770  1.00 12.45           O  
ANISOU  869  OE1 GLN A  95     2432   1143   1152    -28    -50    135       O  
ATOM    870  NE2 GLN A  95       9.284  13.267  21.442  1.00  9.68           N  
ANISOU  870  NE2 GLN A  95     2348    546    783    -46    -70    213       N  
ATOM    871  N   LYS A  96      12.067  18.337  23.136  1.00  9.90           N  
ANISOU  871  N   LYS A  96     2578    641    542     92   -122    -88       N  
ATOM    872  CA  LYS A  96      12.625  18.823  24.397  1.00 11.01           C  
ANISOU  872  CA  LYS A  96     2740    755    687    159    -96    -95       C  
ATOM    873  C   LYS A  96      11.510  19.041  25.407  1.00 11.29           C  
ANISOU  873  C   LYS A  96     2897    745    647    153   -133   -207       C  
ATOM    874  O   LYS A  96      10.517  19.716  25.110  1.00 12.35           O  
ANISOU  874  O   LYS A  96     3123    961    609    303     -3   -172       O  
ATOM    875  CB  LYS A  96      13.329  20.171  24.189  1.00 12.92           C  
ANISOU  875  CB  LYS A  96     2695   1159   1054     -9   -234   -112       C  
ATOM    876  CG  LYS A  96      14.406  20.248  23.216  1.00 15.21           C  
ANISOU  876  CG  LYS A  96     2926   1321   1530     46     21   -153       C  
ATOM    877  CD  LYS A  96      15.584  19.362  23.503  1.00 16.03           C  
ANISOU  877  CD  LYS A  96     3300   1310   1479    -81    -48   -307       C  
ATOM    878  CE  LYS A  96      16.764  19.666  22.639  1.00 17.27           C  
ANISOU  878  CE  LYS A  96     3004   1349   2208    -70   -111   -424       C  
ATOM    879  NZ  LYS A  96      17.915  18.739  22.846  1.00 18.97           N  
ANISOU  879  NZ  LYS A  96     3227   1283   2696   -144    115     25       N  
ATOM    880  N   TRP A  97      11.689  18.546  26.623  1.00 11.87           N  
ANISOU  880  N   TRP A  97     3116    794    599    189    -99   -104       N  
ATOM    881  CA  TRP A  97      10.737  18.791  27.705  1.00 13.35           C  
ANISOU  881  CA  TRP A  97     3358   1124    587    329     40    -67       C  
ATOM    882  C   TRP A  97      11.427  18.476  29.016  1.00 14.99           C  
ANISOU  882  C   TRP A  97     3751   1292    653    279    -11   -214       C  
ATOM    883  O   TRP A  97      12.211  17.546  29.104  1.00 15.66           O  
ANISOU  883  O   TRP A  97     4044   1265    638    365   -123    -96       O  
ATOM    884  CB  TRP A  97       9.467  17.904  27.540  1.00 13.93           C  
ANISOU  884  CB  TRP A  97     3216   1314    762    269    185     50       C  
ATOM    885  CG  TRP A  97       9.643  16.458  27.930  1.00 13.39           C  
ANISOU  885  CG  TRP A  97     3081   1165    841    118    346     19       C  
ATOM    886  CD1 TRP A  97       9.174  15.876  29.042  1.00 14.38           C  
ANISOU  886  CD1 TRP A  97     3079   1417    966    142    351      9       C  
ATOM    887  CD2 TRP A  97      10.438  15.456  27.265  1.00 11.89           C  
ANISOU  887  CD2 TRP A  97     2919    943    654    103     88    -94       C  
ATOM    888  NE1 TRP A  97       9.566  14.585  29.135  1.00 13.55           N  
ANISOU  888  NE1 TRP A  97     2969   1352    826     26    267     99       N  
ATOM    889  CE2 TRP A  97      10.380  14.308  28.069  1.00 12.82           C  
ANISOU  889  CE2 TRP A  97     2921   1193    755   -119     64     16       C  
ATOM    890  CE3 TRP A  97      11.190  15.405  26.092  1.00 11.60           C  
ANISOU  890  CE3 TRP A  97     2707    924    776   -121     40   -106       C  
ATOM    891  CZ2 TRP A  97      11.042  13.116  27.720  1.00 13.12           C  
ANISOU  891  CZ2 TRP A  97     2931    966   1088   -172    -28    120       C  
ATOM    892  CZ3 TRP A  97      11.841  14.234  25.784  1.00 12.06           C  
ANISOU  892  CZ3 TRP A  97     2828    956    798   -113    181   -241       C  
ATOM    893  CH2 TRP A  97      11.762  13.116  26.581  1.00 12.50           C  
ANISOU  893  CH2 TRP A  97     2677   1088    984     46     90   -175       C  
ATOM    894  N   ASP A  98      11.074  19.257  30.039  1.00 16.40           N  
ANISOU  894  N   ASP A  98     3931   1669    631    432    -52   -233       N  
ATOM    895  CA AASP A  98      11.533  19.042  31.409  0.50 18.51           C  
ANISOU  895  CA AASP A  98     3890   2207    934    289    -86   -383       C  
ATOM    896  CA BASP A  98      11.501  18.926  31.394  0.50 18.29           C  
ANISOU  896  CA BASP A  98     3882   2167    897    293    -57   -333       C  
ATOM    897  C   ASP A  98      13.015  18.726  31.483  1.00 17.72           C  
ANISOU  897  C   ASP A  98     3903   2156    671    142   -144   -524       C  
ATOM    898  O   ASP A  98      13.452  17.886  32.284  1.00 21.21           O  
ANISOU  898  O   ASP A  98     4416   2716    925    248   -343   -258       O  
ATOM    899  CB AASP A  98      10.729  17.944  32.111  0.50 19.89           C  
ANISOU  899  CB AASP A  98     4031   2499   1027    245    -26   -258       C  
ATOM    900  CB BASP A  98      10.772  17.647  31.892  0.50 19.34           C  
ANISOU  900  CB BASP A  98     3986   2531    830    258     52   -108       C  
ATOM    901  CG AASP A  98       9.242  18.261  32.229  0.50 22.11           C  
ANISOU  901  CG AASP A  98     4080   2945   1373    140    -25   -184       C  
ATOM    902  CG BASP A  98      10.739  17.537  33.425  0.50 22.67           C  
ANISOU  902  CG BASP A  98     4191   3109   1310    165     52    109       C  
ATOM    903  OD1AASP A  98       8.885  19.456  32.347  0.50 27.89           O  
ANISOU  903  OD1AASP A  98     4486   3371   2737    285    101    257       O  
ATOM    904  OD1BASP A  98      10.956  18.558  34.107  0.50 24.93           O  
ANISOU  904  OD1BASP A  98     4679   3777   1015    216     -9   -101       O  
ATOM    905  OD2AASP A  98       8.437  17.296  32.233  0.50 26.71           O  
ANISOU  905  OD2AASP A  98     4251   3743   2153    -64     72   -352       O  
ATOM    906  OD2BASP A  98      10.494  16.427  33.974  0.50 26.89           O  
ANISOU  906  OD2BASP A  98     4973   3931   1311     85    191    630       O  
ATOM    907  N   GLY A  99      13.800  19.465  30.720  1.00 18.22           N  
ANISOU  907  N   GLY A  99     3730   1971   1218     53   -363   -621       N  
ATOM    908  CA  GLY A  99      15.208  19.310  30.653  1.00 18.19           C  
ANISOU  908  CA  GLY A  99     3635   1835   1439     -3   -556   -651       C  
ATOM    909  C   GLY A  99      15.736  18.046  29.986  1.00 18.35           C  
ANISOU  909  C   GLY A  99     3567   1704   1700     57   -505   -657       C  
ATOM    910  O   GLY A  99      16.947  17.817  30.003  1.00 20.61           O  
ANISOU  910  O   GLY A  99     3527   2135   2170   -101   -788   -799       O  
ATOM    911  N   LYS A 100      14.863  17.254  29.361  1.00 15.30           N  
ANISOU  911  N   LYS A 100     3542   1381    890     63   -569   -528       N  
ATOM    912  CA  LYS A 100      15.188  16.023  28.662  1.00 14.35           C  
ANISOU  912  CA  LYS A 100     3239   1409    802    133   -472   -136       C  
ATOM    913  C   LYS A 100      15.071  16.255  27.163  1.00 12.75           C  
ANISOU  913  C   LYS A 100     3023   1010    811    -44   -456   -236       C  
ATOM    914  O   LYS A 100      14.512  17.236  26.689  1.00 12.81           O  
ANISOU  914  O   LYS A 100     3187    882    797    114   -364   -135       O  
ATOM    915  CB  LYS A 100      14.204  14.934  29.091  1.00 14.28           C  
ANISOU  915  CB  LYS A 100     3367   1380    678    190   -251    -21       C  
ATOM    916  CG  LYS A 100      14.199  14.665  30.581  1.00 19.66           C  
ANISOU  916  CG  LYS A 100     4019   2197   1254     94   -258     -5       C  
ATOM    917  CD  LYS A 100      13.031  13.719  31.007  1.00 21.27           C  
ANISOU  917  CD  LYS A 100     4073   2681   1324    168     62    307       C  
ATOM    918  CE  LYS A 100      12.902  13.570  32.477  1.00 26.39           C  
ANISOU  918  CE  LYS A 100     4491   3411   2121     44    198    141       C  
ATOM    919  NZ  LYS A 100      11.476  13.319  32.878  1.00 32.53           N  
ANISOU  919  NZ  LYS A 100     4750   4184   3423    -66     92    253       N  
ATOM    920  N   SER A 101      15.590  15.285  26.414  1.00 12.02           N  
ANISOU  920  N   SER A 101     2890    926    751      8   -482    -95       N  
ATOM    921  CA  SER A 101      15.532  15.334  24.959  1.00 11.64           C  
ANISOU  921  CA  SER A 101     2721    873    828    -66   -276     59       C  
ATOM    922  C   SER A 101      15.449  13.930  24.408  1.00 10.40           C  
ANISOU  922  C   SER A 101     2586    706    659    -52   -167     81       C  
ATOM    923  O   SER A 101      16.076  13.003  24.921  1.00 11.82           O  
ANISOU  923  O   SER A 101     2752    807    932     83   -462     42       O  
ATOM    924  CB  SER A 101      16.834  15.946  24.466  1.00 12.98           C  
ANISOU  924  CB  SER A 101     2755    999   1177   -136   -178   -163       C  
ATOM    925  OG  SER A 101      16.840  16.162  23.113  1.00 15.00           O  
ANISOU  925  OG  SER A 101     3074   1248   1375   -399   -144     -5       O  
ATOM    926  N   THR A 102      14.679  13.752  23.325  1.00  9.48           N  
ANISOU  926  N   THR A 102     2325    654    621     52   -208     30       N  
ATOM    927  CA  THR A 102      14.665  12.526  22.550  1.00  8.91           C  
ANISOU  927  CA  THR A 102     2254    544    586     79    -94     17       C  
ATOM    928  C   THR A 102      14.656  12.904  21.078  1.00  8.85           C  
ANISOU  928  C   THR A 102     2252    451    659     20   -176    117       C  
ATOM    929  O   THR A 102      14.154  13.957  20.712  1.00  9.82           O  
ANISOU  929  O   THR A 102     2482    620    629    180     14     89       O  
ATOM    930  CB  THR A 102      13.471  11.668  22.960  1.00  9.77           C  
ANISOU  930  CB  THR A 102     2409    703    598     75   -115    -10       C  
ATOM    931  OG1 THR A 102      13.547  10.378  22.330  1.00 10.27           O  
ANISOU  931  OG1 THR A 102     2336    616    949      0    -44     20       O  
ATOM    932  CG2 THR A 102      12.147  12.219  22.632  1.00 10.85           C  
ANISOU  932  CG2 THR A 102     2512    826    784    115    -35    -57       C  
ATOM    933  N   THR A 103      15.198  12.015  20.245  1.00  9.02           N  
ANISOU  933  N   THR A 103     2298    533    595    136    -94     53       N  
ATOM    934  CA  THR A 103      15.290  12.253  18.805  1.00  9.47           C  
ANISOU  934  CA  THR A 103     2384    575    638    169     -3      0       C  
ATOM    935  C   THR A 103      14.619  11.096  18.084  1.00  9.74           C  
ANISOU  935  C   THR A 103     2644    601    454    222    -44     12       C  
ATOM    936  O   THR A 103      14.878   9.916  18.364  1.00 11.28           O  
ANISOU  936  O   THR A 103     3015    520    747    269   -340     38       O  
ATOM    937  CB  THR A 103      16.747  12.427  18.403  1.00 11.13           C  
ANISOU  937  CB  THR A 103     2410    938    879    173     16    -10       C  
ATOM    938  OG1 THR A 103      17.281  13.597  19.047  1.00 13.87           O  
ANISOU  938  OG1 THR A 103     2565   1428   1276   -241     41     19       O  
ATOM    939  CG2 THR A 103      16.889  12.660  16.888  1.00 12.85           C  
ANISOU  939  CG2 THR A 103     2686   1357    836    155     76    133       C  
ATOM    940  N   ILE A 104      13.777  11.444  17.122  1.00  8.90           N  
ANISOU  940  N   ILE A 104     2510    403    467    176    -41     24       N  
ATOM    941  CA  ILE A 104      13.103  10.505  16.238  1.00  8.86           C  
ANISOU  941  CA  ILE A 104     2417    512    435    168     38     28       C  
ATOM    942  C   ILE A 104      13.653  10.787  14.836  1.00  8.72           C  
ANISOU  942  C   ILE A 104     2335    523    452     59    -16     24       C  
ATOM    943  O   ILE A 104      13.482  11.898  14.333  1.00  9.91           O  
ANISOU  943  O   ILE A 104     2764    510    489    265     79     92       O  
ATOM    944  CB  ILE A 104      11.606  10.650  16.265  1.00  9.87           C  
ANISOU  944  CB  ILE A 104     2472    730    545     79     68     86       C  
ATOM    945  CG1 ILE A 104      11.045  10.439  17.683  1.00 11.61           C  
ANISOU  945  CG1 ILE A 104     2399   1211    801    -46    139    -40       C  
ATOM    946  CG2 ILE A 104      10.938   9.690  15.280  1.00 11.92           C  
ANISOU  946  CG2 ILE A 104     2696   1131    700     18    -55    -68       C  
ATOM    947  CD1 ILE A 104       9.635  10.839  17.792  1.00 15.91           C  
ANISOU  947  CD1 ILE A 104     2715   1975   1355    -27    338    115       C  
ATOM    948  N   LYS A 105      14.255   9.780  14.212  1.00  8.71           N  
ANISOU  948  N   LYS A 105     2365    505    439    122     -4    -44       N  
ATOM    949  CA  LYS A 105      14.748   9.888  12.838  1.00  8.85           C  
ANISOU  949  CA  LYS A 105     2333    559    469    118    -46     -2       C  
ATOM    950  C   LYS A 105      13.866   9.084  11.941  1.00  8.76           C  
ANISOU  950  C   LYS A 105     2374    497    457    132     46    -31       C  
ATOM    951  O   LYS A 105      13.466   7.965  12.280  1.00 10.89           O  
ANISOU  951  O   LYS A 105     2988    547    600   -119   -180    129       O  
ATOM    952  CB  LYS A 105      16.201   9.420  12.737  1.00 10.47           C  
ANISOU  952  CB  LYS A 105     2392    945    639    130    -23    -32       C  
ATOM    953  CG  LYS A 105      17.210  10.402  13.421  1.00 13.94           C  
ANISOU  953  CG  LYS A 105     2414   1552   1330    183   -105   -294       C  
ATOM    954  CD  LYS A 105      18.656  10.068  13.221  1.00 18.94           C  
ANISOU  954  CD  LYS A 105     2651   2658   1886     54    -37    -86       C  
ATOM    955  CE  LYS A 105      19.565  11.064  13.901  1.00 23.92           C  
ANISOU  955  CE  LYS A 105     2890   3118   3080    -93   -228     49       C  
ATOM    956  NZ  LYS A 105      21.005  10.663  13.844  1.00 28.74           N  
ANISOU  956  NZ  LYS A 105     3215   3689   4016     53   -263     93       N  
ATOM    957  N   ARG A 106      13.562   9.622  10.770  1.00  8.59           N  
ANISOU  957  N   ARG A 106     2348    457    456     -8     68     21       N  
ATOM    958  CA  ARG A 106      12.710   8.936   9.773  1.00  9.26           C  
ANISOU  958  CA  ARG A 106     2289    726    503    -99     39    111       C  
ATOM    959  C   ARG A 106      13.497   8.927   8.460  1.00  8.99           C  
ANISOU  959  C   ARG A 106     2238    744    431    -90     27     19       C  
ATOM    960  O   ARG A 106      13.969   9.966   8.002  1.00  9.61           O  
ANISOU  960  O   ARG A 106     2420    706    525   -156     51     38       O  
ATOM    961  CB  ARG A 106      11.384   9.634   9.627  1.00 10.31           C  
ANISOU  961  CB  ARG A 106     2332   1039    544   -228      0      3       C  
ATOM    962  CG  ARG A 106      10.571   9.651  10.926  1.00 11.14           C  
ANISOU  962  CG  ARG A 106     2290   1130    812    -88    106     62       C  
ATOM    963  CD  ARG A 106       9.297  10.445  10.864  1.00 13.41           C  
ANISOU  963  CD  ARG A 106     2325   1991    776   -267    141    -11       C  
ATOM    964  NE  ARG A 106       8.449  10.354  12.059  1.00 13.97           N  
ANISOU  964  NE  ARG A 106     2473   1771   1061   -257    150    -66       N  
ATOM    965  CZ  ARG A 106       8.376  11.250  13.010  1.00 14.12           C  
ANISOU  965  CZ  ARG A 106     2285   1892   1188    -29     97     74       C  
ATOM    966  NH1 ARG A 106       9.197  12.258  13.089  1.00 13.05           N  
ANISOU  966  NH1 ARG A 106     2320   1693    944    286     88     55       N  
ATOM    967  NH2 ARG A 106       7.490  11.105  13.992  1.00 16.37           N  
ANISOU  967  NH2 ARG A 106     2605   2526   1087   -220    538     14       N  
ATOM    968  N   LYS A 107      13.618   7.747   7.860  1.00  9.19           N  
ANISOU  968  N   LYS A 107     2284    723    483   -190    103    -51       N  
ATOM    969  CA  LYS A 107      14.434   7.572   6.649  1.00 10.13           C  
ANISOU  969  CA  LYS A 107     2295    902    651   -231    119   -201       C  
ATOM    970  C   LYS A 107      13.779   6.548   5.763  1.00  9.54           C  
ANISOU  970  C   LYS A 107     2354    759    509   -146     88     50       C  
ATOM    971  O   LYS A 107      13.323   5.521   6.207  1.00 11.79           O  
ANISOU  971  O   LYS A 107     2993    979    506   -493    126    -21       O  
ATOM    972  CB  LYS A 107      15.844   7.157   7.021  1.00 12.71           C  
ANISOU  972  CB  LYS A 107     2484   1380    964   -169    110   -503       C  
ATOM    973  CG  LYS A 107      16.874   7.149   5.894  1.00 15.57           C  
ANISOU  973  CG  LYS A 107     2594   1973   1348   -175     72   -492       C  
ATOM    974  CD  LYS A 107      18.278   6.727   6.319  1.00 17.80           C  
ANISOU  974  CD  LYS A 107     2610   2220   1930    128    294   -764       C  
ATOM    975  CE  LYS A 107      19.353   7.231   5.286  1.00 22.62           C  
ANISOU  975  CE  LYS A 107     3279   2923   2392    -24    337   -770       C  
ATOM    976  NZ  LYS A 107      18.926   8.443   4.510  1.00 30.57           N  
ANISOU  976  NZ  LYS A 107     4119   3391   4105     24    188   -511       N  
ATOM    977  N   ARG A 108      13.873   6.775   4.454  1.00  9.58           N  
ANISOU  977  N   ARG A 108     2336    762    540   -137    159    -27       N  
ATOM    978  CA  ARG A 108      13.453   5.791   3.503  1.00 10.59           C  
ANISOU  978  CA  ARG A 108     2339   1144    541   -188    185    -76       C  
ATOM    979  C   ARG A 108      14.544   4.714   3.318  1.00 11.07           C  
ANISOU  979  C   ARG A 108     2291   1222    690    -97    189   -352       C  
ATOM    980  O   ARG A 108      15.721   5.038   3.092  1.00 13.43           O  
ANISOU  980  O   ARG A 108     2371   1326   1403   -121    240   -540       O  
ATOM    981  CB  ARG A 108      13.199   6.396   2.145  1.00 12.12           C  
ANISOU  981  CB  ARG A 108     2640   1362    601   -274    104     40       C  
ATOM    982  CG  ARG A 108      11.893   7.109   2.073  1.00 13.45           C  
ANISOU  982  CG  ARG A 108     2730   1553    826   -131    105    271       C  
ATOM    983  CD  ARG A 108      10.646   6.306   2.281  1.00 16.59           C  
ANISOU  983  CD  ARG A 108     2918   2304   1082   -188   -209    712       C  
ATOM    984  NE  ARG A 108      10.712   5.154   1.346  1.00 18.38           N  
ANISOU  984  NE  ARG A 108     2926   1947   2108     51   -281   1051       N  
ATOM    985  CZ  ARG A 108      10.424   5.213   0.044  1.00 15.63           C  
ANISOU  985  CZ  ARG A 108     2633    878   2427   -106      0    -34       C  
ATOM    986  NH1 ARG A 108       9.900   6.325  -0.549  1.00 15.75           N  
ANISOU  986  NH1 ARG A 108     3001   1495   1486    130   -251    149       N  
ATOM    987  NH2 ARG A 108      10.603   4.166  -0.730  1.00 20.82           N  
ANISOU  987  NH2 ARG A 108     3126   2037   2746    127   -631   -254       N  
ATOM    988  N   GLU A 109      14.157   3.442   3.347  1.00 10.94           N  
ANISOU  988  N   GLU A 109     2293   1089    773    -86    107   -368       N  
ATOM    989  CA  GLU A 109      15.047   2.293   3.144  1.00 11.67           C  
ANISOU  989  CA  GLU A 109     2396   1192    845     51    132   -250       C  
ATOM    990  C   GLU A 109      14.286   1.339   2.259  1.00 11.25           C  
ANISOU  990  C   GLU A 109     2473   1073    726     10    141   -204       C  
ATOM    991  O   GLU A 109      13.284   0.782   2.702  1.00 11.72           O  
ANISOU  991  O   GLU A 109     2558   1273    621   -106    200   -141       O  
ATOM    992  CB  GLU A 109      15.442   1.617   4.453  1.00 13.52           C  
ANISOU  992  CB  GLU A 109     2572   1466   1097    159    -74   -222       C  
ATOM    993  CG  GLU A 109      16.193   2.481   5.408  1.00 17.17           C  
ANISOU  993  CG  GLU A 109     2961   2145   1418    162   -268   -162       C  
ATOM    994  CD  GLU A 109      17.595   2.746   4.988  1.00 20.82           C  
ANISOU  994  CD  GLU A 109     3414   2881   1615    -38   -235   -291       C  
ATOM    995  OE1 GLU A 109      18.271   3.478   5.735  1.00 24.80           O  
ANISOU  995  OE1 GLU A 109     3607   3383   2431   -294     38   -560       O  
ATOM    996  OE2 GLU A 109      18.025   2.214   3.936  1.00 25.41           O  
ANISOU  996  OE2 GLU A 109     3936   3327   2389    285    323   -538       O  
ATOM    997  N   ASP A 110      14.724   1.169   1.020  1.00 10.63           N  
ANISOU  997  N   ASP A 110     2386   1025    627    -28    207    -61       N  
ATOM    998  CA  ASP A 110      13.965   0.359   0.066  1.00 10.74           C  
ANISOU  998  CA  ASP A 110     2554    952    571     15    225    -31       C  
ATOM    999  C   ASP A 110      12.551   0.897   0.000  1.00 10.44           C  
ANISOU  999  C   ASP A 110     2340   1179    448   -108    199   -143       C  
ATOM   1000  O   ASP A 110      12.390   2.141  -0.095  1.00 10.91           O  
ANISOU 1000  O   ASP A 110     2538    904    701     10    166     -6       O  
ATOM   1001  CB  ASP A 110      14.112  -1.134   0.370  1.00 11.91           C  
ANISOU 1001  CB  ASP A 110     2639   1077    806     75    184    -96       C  
ATOM   1002  CG  ASP A 110      15.544  -1.575   0.343  1.00 14.49           C  
ANISOU 1002  CG  ASP A 110     2982   1210   1311      5    121    244       C  
ATOM   1003  OD1 ASP A 110      16.274  -1.167  -0.571  1.00 18.40           O  
ANISOU 1003  OD1 ASP A 110     3202   1875   1912    340    558    194       O  
ATOM   1004  OD2 ASP A 110      15.904  -2.454   1.143  1.00 22.37           O  
ANISOU 1004  OD2 ASP A 110     3428   2679   2390    760    291    943       O  
ATOM   1005  N   ASP A 111      11.518   0.081   0.045  1.00 11.29           N  
ANISOU 1005  N   ASP A 111     2586   1156    548    -45     95   -225       N  
ATOM   1006  CA  ASP A 111      10.142   0.520  -0.009  1.00 11.52           C  
ANISOU 1006  CA  ASP A 111     2634   1140    601    -75    123   -310       C  
ATOM   1007  C   ASP A 111       9.586   0.890   1.364  1.00 12.09           C  
ANISOU 1007  C   ASP A 111     2433   1253    905    -23     57   -326       C  
ATOM   1008  O   ASP A 111       8.405   1.170   1.462  1.00 15.30           O  
ANISOU 1008  O   ASP A 111     2715   1998   1098    223    -30   -721       O  
ATOM   1009  CB  ASP A 111       9.267  -0.463  -0.729  1.00 12.70           C  
ANISOU 1009  CB  ASP A 111     2658   1437    730   -127     71   -347       C  
ATOM   1010  CG  ASP A 111       9.559  -0.516  -2.209  1.00 12.75           C  
ANISOU 1010  CG  ASP A 111     2585   1450    807    -99    -12   -237       C  
ATOM   1011  OD1 ASP A 111       9.782   0.559  -2.811  1.00 15.41           O  
ANISOU 1011  OD1 ASP A 111     3526   1556    770   -365      1    -87       O  
ATOM   1012  OD2 ASP A 111       9.545  -1.620  -2.754  1.00 16.09           O  
ANISOU 1012  OD2 ASP A 111     3847   1489    778   -157    235   -368       O  
ATOM   1013  N   LYS A 112      10.428   0.870   2.391  1.00 10.95           N  
ANISOU 1013  N   LYS A 112     2482   1083    596   -136    191   -104       N  
ATOM   1014  CA  LYS A 112       9.977   1.119   3.780  1.00 10.45           C  
ANISOU 1014  CA  LYS A 112     2473    913    584    -70    251    -83       C  
ATOM   1015  C   LYS A 112      10.319   2.511   4.214  1.00  9.66           C  
ANISOU 1015  C   LYS A 112     2268    952    451   -102     34     98       C  
ATOM   1016  O   LYS A 112      11.165   3.195   3.636  1.00 10.53           O  
ANISOU 1016  O   LYS A 112     2407    921    671   -129    213      7       O  
ATOM   1017  CB  LYS A 112      10.648   0.096   4.697  1.00 11.95           C  
ANISOU 1017  CB  LYS A 112     2799    974    766     92    383    110       C  
ATOM   1018  CG  LYS A 112      10.334  -1.330   4.290  1.00 15.59           C  
ANISOU 1018  CG  LYS A 112     3271   1030   1622    130    511     72       C  
ATOM   1019  CD  LYS A 112      10.869  -2.392   5.048  1.00 21.04           C  
ANISOU 1019  CD  LYS A 112     4053   1919   2021    412    635    115       C  
ATOM   1020  CE  LYS A 112      10.533  -3.781   4.372  1.00 25.30           C  
ANISOU 1020  CE  LYS A 112     4431   2109   3070    199    462    156       C  
ATOM   1021  NZ  LYS A 112      11.037  -4.924   5.134  1.00 30.21           N  
ANISOU 1021  NZ  LYS A 112     4955   2744   3777    297    -74   -103       N  
ATOM   1022  N   LEU A 113       9.655   2.917   5.291  1.00  9.40           N  
ANISOU 1022  N   LEU A 113     2229    791    551   -146    104    -30       N  
ATOM   1023  CA ALEU A 113       9.995   4.120   6.031  0.50  9.56           C  
ANISOU 1023  CA ALEU A 113     2298    836    497    -37     90    -23       C  
ATOM   1024  CA BLEU A 113       9.974   4.113   6.040  0.50  9.52           C  
ANISOU 1024  CA BLEU A 113     2325    804    485    -22     62    -22       C  
ATOM   1025  C   LEU A 113      10.355   3.640   7.431  1.00  9.41           C  
ANISOU 1025  C   LEU A 113     2274    666    633   -121    149    -78       C  
ATOM   1026  O   LEU A 113       9.525   3.049   8.129  1.00 10.55           O  
ANISOU 1026  O   LEU A 113     2331   1030    647   -245    128     20       O  
ATOM   1027  CB ALEU A 113       8.824   5.092   5.981  0.50 10.30           C  
ANISOU 1027  CB ALEU A 113     2251   1050    610   -103     76   -142       C  
ATOM   1028  CB BLEU A 113       8.764   5.026   6.051  0.50 10.33           C  
ANISOU 1028  CB BLEU A 113     2347    848    728   -109      0    -12       C  
ATOM   1029  CG ALEU A 113       9.034   6.527   6.489  0.50 11.62           C  
ANISOU 1029  CG ALEU A 113     2331   1250    832   -124    199    -81       C  
ATOM   1030  CG BLEU A 113       8.967   6.298   6.866  0.50 11.56           C  
ANISOU 1030  CG BLEU A 113     2520   1242    628     31   -208   -246       C  
ATOM   1031  CD1ALEU A 113       7.832   7.383   6.075  0.50 10.88           C  
ANISOU 1031  CD1ALEU A 113     2499    775    858     48     13   -182       C  
ATOM   1032  CD1BLEU A 113      10.233   7.034   6.395  0.50 13.91           C  
ANISOU 1032  CD1BLEU A 113     2717    927   1640    -93   -342     12       C  
ATOM   1033  CD2ALEU A 113       9.246   6.605   7.965  0.50 12.16           C  
ANISOU 1033  CD2ALEU A 113     2089   1491   1038    -34    -45    -12       C  
ATOM   1034  CD2BLEU A 113       7.768   7.224   6.700  0.50 17.31           C  
ANISOU 1034  CD2BLEU A 113     2786   2035   1756    233    -93   -176       C  
ATOM   1035  N   VAL A 114      11.631   3.822   7.772  1.00  9.10           N  
ANISOU 1035  N   VAL A 114     2224    706    525    -87     68     73       N  
ATOM   1036  CA  VAL A 114      12.165   3.364   9.062  1.00  9.75           C  
ANISOU 1036  CA  VAL A 114     2254    801    647    -51    -27    124       C  
ATOM   1037  C   VAL A 114      12.220   4.533  10.002  1.00  9.67           C  
ANISOU 1037  C   VAL A 114     2316    766    590   -102    -76    115       C  
ATOM   1038  O   VAL A 114      12.662   5.635   9.664  1.00 10.55           O  
ANISOU 1038  O   VAL A 114     2635    783    587   -257     79     48       O  
ATOM   1039  CB  VAL A 114      13.532   2.753   8.858  1.00 11.48           C  
ANISOU 1039  CB  VAL A 114     2465   1048    848     24    -29    200       C  
ATOM   1040  CG1 VAL A 114      14.130   2.260  10.207  1.00 13.61           C  
ANISOU 1040  CG1 VAL A 114     2703   1343   1123    296    -18    276       C  
ATOM   1041  CG2 VAL A 114      13.512   1.583   7.848  1.00 14.00           C  
ANISOU 1041  CG2 VAL A 114     2841   1368   1109    299     73   -218       C  
ATOM   1042  N   VAL A 115      11.726   4.301  11.218  1.00  9.94           N  
ANISOU 1042  N   VAL A 115     2526    707    541   -290     39     92       N  
ATOM   1043  CA  VAL A 115      11.627   5.280  12.270  1.00 10.13           C  
ANISOU 1043  CA  VAL A 115     2641    629    576   -286    -53     34       C  
ATOM   1044  C   VAL A 115      12.498   4.808  13.437  1.00 10.40           C  
ANISOU 1044  C   VAL A 115     2731    730    491   -181    -44    161       C  
ATOM   1045  O   VAL A 115      12.211   3.789  14.025  1.00 13.41           O  
ANISOU 1045  O   VAL A 115     3149   1028    917   -537   -436    393       O  
ATOM   1046  CB  VAL A 115      10.160   5.500  12.680  1.00 11.10           C  
ANISOU 1046  CB  VAL A 115     2588    848    780   -274     35     82       C  
ATOM   1047  CG1 VAL A 115      10.043   6.566  13.769  1.00 13.35           C  
ANISOU 1047  CG1 VAL A 115     3128   1236    706   -147     72   -172       C  
ATOM   1048  CG2 VAL A 115       9.277   5.892  11.479  1.00 12.87           C  
ANISOU 1048  CG2 VAL A 115     2824   1128    934   -269   -177     42       C  
ATOM   1049  N  AGLU A 116      13.502   5.615  13.799  0.50  9.22           N  
ANISOU 1049  N  AGLU A 116     2573    391    539    -97     22   -160       N  
ATOM   1050  N  BGLU A 116      13.579   5.519  13.723  0.50  9.98           N  
ANISOU 1050  N  BGLU A 116     2536    825    430    -52    -22    166       N  
ATOM   1051  CA AGLU A 116      14.458   5.250  14.835  0.50  9.44           C  
ANISOU 1051  CA AGLU A 116     2446    524    615     43     18     31       C  
ATOM   1052  CA BGLU A 116      14.382   5.257  14.889  0.50 10.14           C  
ANISOU 1052  CA BGLU A 116     2470    661    720     88    -20    136       C  
ATOM   1053  C  AGLU A 116      14.346   6.234  15.976  0.50  8.94           C  
ANISOU 1053  C  AGLU A 116     2307    414    675    -17   -112    -16       C  
ATOM   1054  C  BGLU A 116      14.079   6.260  15.947  0.50  8.60           C  
ANISOU 1054  C  BGLU A 116     2245    507    516    194   -259     62       C  
ATOM   1055  O  AGLU A 116      14.696   7.417  15.795  0.50  8.62           O  
ANISOU 1055  O  AGLU A 116     2093    459    721     65   -224    -13       O  
ATOM   1056  O  BGLU A 116      14.087   7.462  15.721  0.50  8.48           O  
ANISOU 1056  O  BGLU A 116     2217    514    489    197   -263    182       O  
ATOM   1057  CB AGLU A 116      15.881   5.223  14.269  0.50 11.22           C  
ANISOU 1057  CB AGLU A 116     2555    859    849    208     13     42       C  
ATOM   1058  CB BGLU A 116      15.851   5.343  14.571  0.50 12.69           C  
ANISOU 1058  CB BGLU A 116     2651   1017   1153    156     -9     -8       C  
ATOM   1059  CG AGLU A 116      16.938   4.886  15.339  0.50 13.05           C  
ANISOU 1059  CG AGLU A 116     2590   1555    813    442    171    244       C  
ATOM   1060  CG BGLU A 116      16.446   4.116  13.991  0.50 16.46           C  
ANISOU 1060  CG BGLU A 116     2747   1524   1982    179    136     -2       C  
ATOM   1061  CD AGLU A 116      18.342   5.572  15.174  0.50 18.77           C  
ANISOU 1061  CD AGLU A 116     2956   2166   2009    301     -1     64       C  
ATOM   1062  CD BGLU A 116      17.968   4.101  14.170  0.50 20.49           C  
ANISOU 1062  CD BGLU A 116     2921   2168   2694    141    -30    -92       C  
ATOM   1063  OE1AGLU A 116      18.475   6.826  15.067  0.50 18.27           O  
ANISOU 1063  OE1AGLU A 116     2865   2255   1819    289    148    493       O  
ATOM   1064  OE1BGLU A 116      18.523   5.037  14.765  0.50 21.82           O  
ANISOU 1064  OE1BGLU A 116     2768   2960   2562    320   -462   -397       O  
ATOM   1065  OE2AGLU A 116      19.353   4.841  15.189  0.50 20.08           O  
ANISOU 1065  OE2AGLU A 116     2998   2695   1937    381    263    512       O  
ATOM   1066  OE2BGLU A 116      18.608   3.140  13.727  0.50 22.83           O  
ANISOU 1066  OE2BGLU A 116     3242   2658   2774    565    131    192       O  
ATOM   1067  N   CYS A 117      13.844   5.765  17.135  1.00  9.02           N  
ANISOU 1067  N   CYS A 117     2461    412    553    110   -117    103       N  
ATOM   1068  CA  CYS A 117      13.546   6.598  18.297  1.00  9.70           C  
ANISOU 1068  CA  CYS A 117     2421    665    598    191    -36     39       C  
ATOM   1069  C   CYS A 117      14.666   6.395  19.299  1.00  9.58           C  
ANISOU 1069  C   CYS A 117     2339    707    591    197     48    114       C  
ATOM   1070  O   CYS A 117      14.904   5.249  19.704  1.00 10.42           O  
ANISOU 1070  O   CYS A 117     2614    525    819    134   -309    141       O  
ATOM   1071  CB  CYS A 117      12.215   6.137  18.934  1.00 11.42           C  
ANISOU 1071  CB  CYS A 117     2398   1286    652    237   -212   -103       C  
ATOM   1072  SG  CYS A 117      10.805   6.200  17.781  1.00 13.99           S  
ANISOU 1072  SG  CYS A 117     2516   1774   1024     63   -259    224       S  
ATOM   1073  N   VAL A 118      15.305   7.487  19.732  1.00  9.34           N  
ANISOU 1073  N   VAL A 118     2350    529    669    106    -41    -32       N  
ATOM   1074  CA  VAL A 118      16.504   7.379  20.565  1.00  9.63           C  
ANISOU 1074  CA  VAL A 118     2209    584    864     54    -28     42       C  
ATOM   1075  C   VAL A 118      16.327   8.207  21.809  1.00  9.64           C  
ANISOU 1075  C   VAL A 118     2259    516    885     20   -108     49       C  
ATOM   1076  O   VAL A 118      15.980   9.405  21.731  1.00 10.15           O  
ANISOU 1076  O   VAL A 118     2507    516    831    148   -175     -1       O  
ATOM   1077  CB  VAL A 118      17.770   7.805  19.814  1.00 12.63           C  
ANISOU 1077  CB  VAL A 118     2478    901   1419     53    175    -58       C  
ATOM   1078  CG1 VAL A 118      18.961   7.828  20.711  1.00 16.72           C  
ANISOU 1078  CG1 VAL A 118     2237   1877   2236     58     55    -26       C  
ATOM   1079  CG2 VAL A 118      18.043   6.897  18.667  1.00 15.78           C  
ANISOU 1079  CG2 VAL A 118     2734   1404   1855     58    409   -167       C  
ATOM   1080  N  AMET A 119      16.333   7.565  22.968  0.50  8.64           N  
ANISOU 1080  N  AMET A 119     1946    437    897     60    -81    138       N  
ATOM   1081  N  BMET A 119      16.833   7.702  22.933  0.50  9.41           N  
ANISOU 1081  N  BMET A 119     2110    667    796    145    -83     34       N  
ATOM   1082  CA AMET A 119      16.392   8.239  24.249  0.50  8.69           C  
ANISOU 1082  CA AMET A 119     1777    631    893     23    -86     39       C  
ATOM   1083  CA BMET A 119      17.037   8.504  24.118  0.50 10.85           C  
ANISOU 1083  CA BMET A 119     2316    865    940     10   -168   -152       C  
ATOM   1084  C  AMET A 119      17.698   7.758  24.923  0.50  9.77           C  
ANISOU 1084  C  AMET A 119     2074    871    763     80   -220    -21       C  
ATOM   1085  C  BMET A 119      18.051   7.847  25.006  0.50 11.99           C  
ANISOU 1085  C  BMET A 119     2387   1087   1079    113   -401   -206       C  
ATOM   1086  O  AMET A 119      17.859   6.577  25.244  0.50 10.13           O  
ANISOU 1086  O  AMET A 119     2154    908    784    155   -135   -121       O  
ATOM   1087  O  BMET A 119      17.804   6.725  25.506  0.50 11.85           O  
ANISOU 1087  O  BMET A 119     2740    661   1099    368   -542    -31       O  
ATOM   1088  CB AMET A 119      15.158   7.903  25.055  0.50  8.61           C  
ANISOU 1088  CB AMET A 119     1947    633    691     33    -59    111       C  
ATOM   1089  CB BMET A 119      15.734   8.625  24.887  0.50 11.07           C  
ANISOU 1089  CB BMET A 119     2133   1235    837     -8   -239    137       C  
ATOM   1090  CG AMET A 119      15.131   8.563  26.436  0.50  9.35           C  
ANISOU 1090  CG AMET A 119     2221    678    651   -107   -228    195       C  
ATOM   1091  CG BMET A 119      15.856   9.718  25.988  0.50 13.61           C  
ANISOU 1091  CG BMET A 119     2373   1833    965    123   -324     81       C  
ATOM   1092  SD AMET A 119      15.021  10.366  26.221  0.50 10.93           S  
ANISOU 1092  SD AMET A 119     2411    845    895    219     26    119       S  
ATOM   1093  SD BMET A 119      14.289  10.017  26.771  0.50 14.85           S  
ANISOU 1093  SD BMET A 119     2838   1477   1325     53     76   -249       S  
ATOM   1094  CE AMET A 119      15.005  10.821  27.956  0.50 14.39           C  
ANISOU 1094  CE AMET A 119     3038    848   1581     78    201   -475       C  
ATOM   1095  CE BMET A 119      14.755  11.126  28.122  0.50 15.34           C  
ANISOU 1095  CE BMET A 119     3036   1737   1053    450   -150   -308       C  
ATOM   1096  N  ALYS A 120      18.651   8.673  25.105  0.50 11.42           N  
ANISOU 1096  N  ALYS A 120     2021    915   1401    115   -375    187       N  
ATOM   1097  N  BLYS A 120      19.127   8.571  25.304  0.50 15.29           N  
ANISOU 1097  N  BLYS A 120     2411   1446   1950    109   -303      3       N  
ATOM   1098  CA ALYS A 120      19.979   8.320  25.674  0.50 11.81           C  
ANISOU 1098  CA ALYS A 120     2111   1047   1328    -45   -372    245       C  
ATOM   1099  CA BLYS A 120      20.041   8.130  26.368  0.50 17.72           C  
ANISOU 1099  CA BLYS A 120     2598   2036   2096     58   -226     72       C  
ATOM   1100  C  ALYS A 120      20.553   7.083  24.957  0.50 10.26           C  
ANISOU 1100  C  ALYS A 120     2065    547   1286    -13   -341    247       C  
ATOM   1101  C  BLYS A 120      20.508   6.682  26.219  0.50 18.47           C  
ANISOU 1101  C  BLYS A 120     2639   2149   2227     37   -189    129       C  
ATOM   1102  O  ALYS A 120      20.731   7.124  23.734  0.50 12.11           O  
ANISOU 1102  O  ALYS A 120     2171    950   1478    -10   -102    570       O  
ATOM   1103  O  BLYS A 120      20.401   5.906  27.156  0.50 21.27           O  
ANISOU 1103  O  BLYS A 120     3039   2457   2583    -22   -155    175       O  
ATOM   1104  CB ALYS A 120      19.902   8.162  27.210  0.50 11.64           C  
ANISOU 1104  CB ALYS A 120     2171    944   1304     15   -195    -11       C  
ATOM   1105  CB BLYS A 120      19.333   8.151  27.711  0.50 17.43           C  
ANISOU 1105  CB BLYS A 120     2524   1884   2212     97   -253    141       C  
ATOM   1106  CG ALYS A 120      19.557   9.473  27.855  0.50 13.27           C  
ANISOU 1106  CG ALYS A 120     2175   1462   1402     21   -431   -209       C  
ATOM   1107  CG BLYS A 120      18.797   9.434  28.182  0.50 19.66           C  
ANISOU 1107  CG BLYS A 120     2564   2419   2486    133   -256     -6       C  
ATOM   1108  CD ALYS A 120      19.179   9.317  29.283  0.50 17.96           C  
ANISOU 1108  CD ALYS A 120     2700   2317   1805     72     15      0       C  
ATOM   1109  CD BLYS A 120      18.218   9.189  29.540  0.50 23.56           C  
ANISOU 1109  CD BLYS A 120     3020   3119   2809    -46    -49   -140       C  
ATOM   1110  CE ALYS A 120      20.399   9.149  30.162  0.50 22.47           C  
ANISOU 1110  CE ALYS A 120     2820   3047   2670     71    -68   -117       C  
ATOM   1111  CE BLYS A 120      19.317   8.711  30.486  0.50 24.72           C  
ANISOU 1111  CE BLYS A 120     3324   3338   2728   -165    -50      8       C  
ATOM   1112  NZ ALYS A 120      21.408  10.168  29.747  0.50 25.18           N  
ANISOU 1112  NZ ALYS A 120     3111   3213   3242      4     47    -26       N  
ATOM   1113  NZ BLYS A 120      18.796   7.793  31.529  0.50 26.78           N  
ANISOU 1113  NZ BLYS A 120     3764   3610   2800   -266    127     53       N  
ATOM   1114  N  AGLY A 121      20.882   6.015  25.691  0.50 10.59           N  
ANISOU 1114  N  AGLY A 121     2025    909   1087     50   -195    412       N  
ATOM   1115  N  BGLY A 121      21.003   6.293  25.059  0.50 17.64           N  
ANISOU 1115  N  BGLY A 121     2486   2103   2112     -6   -109    140       N  
ATOM   1116  CA AGLY A 121      21.469   4.828  25.112  0.50 12.72           C  
ANISOU 1116  CA AGLY A 121     2128   1244   1461     -9   -198    387       C  
ATOM   1117  CA BGLY A 121      21.496   4.939  24.863  0.50 16.09           C  
ANISOU 1117  CA BGLY A 121     2341   1841   1929    -12   -106    259       C  
ATOM   1118  C   GLY A 121      20.480   3.893  24.458  1.00 11.97           C  
ANISOU 1118  C   GLY A 121     2083   1173   1289    129   -107    372       C  
ATOM   1119  O   GLY A 121      20.875   2.803  24.041  1.00 13.47           O  
ANISOU 1119  O   GLY A 121     2303   1277   1539    391     47    337       O  
ATOM   1120  N   VAL A 122      19.193   4.215  24.557  1.00 11.16           N  
ANISOU 1120  N   VAL A 122     2190    925   1123    145   -135    163       N  
ATOM   1121  CA  VAL A 122      18.122   3.263  24.160  1.00 10.29           C  
ANISOU 1121  CA  VAL A 122     2240    786    880    247    -95    131       C  
ATOM   1122  C   VAL A 122      17.528   3.667  22.835  1.00 10.15           C  
ANISOU 1122  C   VAL A 122     2288    532   1035    125   -188    128       C  
ATOM   1123  O   VAL A 122      17.070   4.803  22.673  1.00 11.67           O  
ANISOU 1123  O   VAL A 122     2712    744    975    285   -382     -3       O  
ATOM   1124  CB  VAL A 122      17.036   3.217  25.233  1.00 11.54           C  
ANISOU 1124  CB  VAL A 122     2233    978   1173    269    -81    204       C  
ATOM   1125  CG1 VAL A 122      15.927   2.251  24.825  1.00 14.30           C  
ANISOU 1125  CG1 VAL A 122     2482   1307   1643    222    124    139       C  
ATOM   1126  CG2 VAL A 122      17.625   2.768  26.564  1.00 13.67           C  
ANISOU 1126  CG2 VAL A 122     2530   1527   1135    257     36    384       C  
ATOM   1127  N   THR A 123      17.545   2.754  21.892  1.00 10.42           N  
ANISOU 1127  N   THR A 123     2284    606   1069    188   -221     67       N  
ATOM   1128  CA  THR A 123      16.977   2.963  20.577  1.00 10.37           C  
ANISOU 1128  CA  THR A 123     2441    625    874    141   -132    109       C  
ATOM   1129  C   THR A 123      15.818   1.980  20.360  1.00 11.00           C  
ANISOU 1129  C   THR A 123     2637    627    915     54   -286    108       C  
ATOM   1130  O   THR A 123      15.886   0.796  20.721  1.00 14.06           O  
ANISOU 1130  O   THR A 123     2947    724   1670    -74   -507    471       O  
ATOM   1131  CB  THR A 123      18.044   2.698  19.519  1.00 12.93           C  
ANISOU 1131  CB  THR A 123     2624   1144   1142    100     19     56       C  
ATOM   1132  OG1 THR A 123      19.100   3.609  19.736  1.00 16.02           O  
ANISOU 1132  OG1 THR A 123     2983   1517   1584   -111    366    -65       O  
ATOM   1133  CG2 THR A 123      17.512   2.871  18.115  1.00 14.90           C  
ANISOU 1133  CG2 THR A 123     2802   1853   1006    154    137     94       C  
ATOM   1134  N   SER A 124      14.775   2.453  19.711  1.00 10.62           N  
ANISOU 1134  N   SER A 124     2728    454    853     -6   -293    115       N  
ATOM   1135  CA  SER A 124      13.737   1.593  19.147  1.00 10.78           C  
ANISOU 1135  CA  SER A 124     2661    584    850     33   -180    285       C  
ATOM   1136  C   SER A 124      13.656   1.817  17.654  1.00  9.96           C  
ANISOU 1136  C   SER A 124     2443    617    723     70    -66    173       C  
ATOM   1137  O   SER A 124      13.697   2.939  17.188  1.00 11.74           O  
ANISOU 1137  O   SER A 124     3148    581    732     -3   -195    189       O  
ATOM   1138  CB  SER A 124      12.393   1.886  19.803  1.00 10.87           C  
ANISOU 1138  CB  SER A 124     2665    669    796    -33    -99    179       C  
ATOM   1139  OG  SER A 124      11.313   1.225  19.166  1.00 11.82           O  
ANISOU 1139  OG  SER A 124     2768    798    922     55    -56    155       O  
ATOM   1140  N   THR A 125      13.522   0.733  16.892  1.00  9.42           N  
ANISOU 1140  N   THR A 125     2268    612    697     -9   -142    127       N  
ATOM   1141  CA  THR A 125      13.375   0.797  15.479  1.00  9.99           C  
ANISOU 1141  CA  THR A 125     2323    769    703     74     20    143       C  
ATOM   1142  C   THR A 125      11.986   0.333  15.105  1.00  9.75           C  
ANISOU 1142  C   THR A 125     2478    675    552   -117    -63    297       C  
ATOM   1143  O   THR A 125      11.607  -0.807  15.448  1.00 11.82           O  
ANISOU 1143  O   THR A 125     2839    786    863   -181   -206    306       O  
ATOM   1144  CB  THR A 125      14.447  -0.052  14.776  1.00 12.57           C  
ANISOU 1144  CB  THR A 125     2585   1144   1044    184     70     33       C  
ATOM   1145  OG1 THR A 125      15.750   0.411  15.166  1.00 15.72           O  
ANISOU 1145  OG1 THR A 125     2494   1498   1980    283    232   -126       O  
ATOM   1146  CG2 THR A 125      14.300  -0.030  13.264  1.00 15.05           C  
ANISOU 1146  CG2 THR A 125     3077   1660    980    311    230      8       C  
ATOM   1147  N   ARG A 126      11.282   1.143  14.352  1.00  9.98           N  
ANISOU 1147  N   ARG A 126     2368    760    661   -327    -30    208       N  
ATOM   1148  CA  ARG A 126       9.885   0.906  13.940  1.00 11.16           C  
ANISOU 1148  CA  ARG A 126     2441   1083    715   -399    -80    403       C  
ATOM   1149  C   ARG A 126       9.833   0.990  12.422  1.00 10.62           C  
ANISOU 1149  C   ARG A 126     2488    869    677   -256    -80    306       C  
ATOM   1150  O   ARG A 126      10.323   1.947  11.847  1.00 14.21           O  
ANISOU 1150  O   ARG A 126     3355   1326    717   -798   -228    309       O  
ATOM   1151  CB  ARG A 126       8.982   1.918  14.608  1.00 12.06           C  
ANISOU 1151  CB  ARG A 126     2283   1577    720   -254   -118    124       C  
ATOM   1152  CG  ARG A 126       8.929   1.567  16.093  1.00 16.03           C  
ANISOU 1152  CG  ARG A 126     2781   2267   1041     24   -161     36       C  
ATOM   1153  CD  ARG A 126       8.242   2.479  16.935  1.00 16.20           C  
ANISOU 1153  CD  ARG A 126     2622   2275   1259   -149     77    167       C  
ATOM   1154  NE  ARG A 126       6.840   2.735  16.697  1.00 16.24           N  
ANISOU 1154  NE  ARG A 126     2601   2564   1006     73    -31    -53       N  
ATOM   1155  CZ  ARG A 126       5.791   2.136  17.273  1.00 15.90           C  
ANISOU 1155  CZ  ARG A 126     2691   2466    884   -370   -282   -216       C  
ATOM   1156  NH1 ARG A 126       5.862   0.976  17.905  1.00 17.81           N  
ANISOU 1156  NH1 ARG A 126     3245   2698    824   -113   -266     23       N  
ATOM   1157  NH2 ARG A 126       4.619   2.665  17.113  1.00 16.91           N  
ANISOU 1157  NH2 ARG A 126     2843   2376   1206   -351     55    107       N  
ATOM   1158  N   VAL A 127       9.311  -0.001  11.779  1.00  9.52           N  
ANISOU 1158  N   VAL A 127     2221    756    640   -150    -12    160       N  
ATOM   1159  CA  VAL A 127       9.321  -0.078  10.314  1.00  9.97           C  
ANISOU 1159  CA  VAL A 127     2248    892    647   -120     20    130       C  
ATOM   1160  C   VAL A 127       7.908   0.067   9.823  1.00  9.33           C  
ANISOU 1160  C   VAL A 127     2186    731    626   -139     76    -20       C  
ATOM   1161  O   VAL A 127       6.999  -0.684  10.239  1.00 10.07           O  
ANISOU 1161  O   VAL A 127     2302    864    659   -153    -46     54       O  
ATOM   1162  CB  VAL A 127       9.921  -1.400   9.861  1.00 11.56           C  
ANISOU 1162  CB  VAL A 127     2504    998    890    155    -43     27       C  
ATOM   1163  CG1 VAL A 127       9.873  -1.451   8.302  1.00 13.39           C  
ANISOU 1163  CG1 VAL A 127     2716   1422    949    278    102   -207       C  
ATOM   1164  CG2 VAL A 127      11.344  -1.561  10.349  1.00 14.86           C  
ANISOU 1164  CG2 VAL A 127     2685   1619   1341    418     34    141       C  
ATOM   1165  N   TYR A 128       7.717   1.005   8.896  1.00  8.95           N  
ANISOU 1165  N   TYR A 128     2091    704    604   -136     10     87       N  
ATOM   1166  CA  TYR A 128       6.458   1.215   8.225  1.00  9.16           C  
ANISOU 1166  CA  TYR A 128     2114    734    631   -148     35      9       C  
ATOM   1167  C   TYR A 128       6.562   0.804   6.747  1.00  9.83           C  
ANISOU 1167  C   TYR A 128     2318    713    705   -112    -28     35       C  
ATOM   1168  O   TYR A 128       7.612   1.015   6.115  1.00 10.46           O  
ANISOU 1168  O   TYR A 128     2370    938    665   -170     83    -71       O  
ATOM   1169  CB  TYR A 128       6.054   2.688   8.289  1.00  9.46           C  
ANISOU 1169  CB  TYR A 128     2130    809    654   -142     34     69       C  
ATOM   1170  CG  TYR A 128       5.630   3.206   9.664  1.00  8.91           C  
ANISOU 1170  CG  TYR A 128     2023    770    592   -166      6     87       C  
ATOM   1171  CD1 TYR A 128       6.551   3.458  10.651  1.00 10.03           C  
ANISOU 1171  CD1 TYR A 128     2024   1009    776    -59     10   -101       C  
ATOM   1172  CD2 TYR A 128       4.297   3.418   9.934  1.00  9.43           C  
ANISOU 1172  CD2 TYR A 128     2132    804    646   -187    -16    170       C  
ATOM   1173  CE1 TYR A 128       6.127   3.958  11.901  1.00 11.03           C  
ANISOU 1173  CE1 TYR A 128     2213   1297    679   -104   -211    -46       C  
ATOM   1174  CE2 TYR A 128       3.879   3.913  11.170  1.00 10.42           C  
ANISOU 1174  CE2 TYR A 128     2143   1046    768    -64     22    168       C  
ATOM   1175  CZ  TYR A 128       4.799   4.177  12.132  1.00 10.84           C  
ANISOU 1175  CZ  TYR A 128     2173   1224    721    -40    106     46       C  
ATOM   1176  OH  TYR A 128       4.363   4.665  13.350  1.00 13.62           O  
ANISOU 1176  OH  TYR A 128     2434   2023    717    230    109   -163       O  
ATOM   1177  N   GLU A 129       5.476   0.252   6.227  1.00 10.52           N  
ANISOU 1177  N   GLU A 129     2384    969    643   -124     15   -117       N  
ATOM   1178  CA AGLU A 129       5.310  -0.130   4.827  0.50 10.93           C  
ANISOU 1178  CA AGLU A 129     2421    923    807     -2    -11   -193       C  
ATOM   1179  CA BGLU A 129       5.430   0.013   4.781  0.50 11.37           C  
ANISOU 1179  CA BGLU A 129     2520    937    863    -18    -54   -257       C  
ATOM   1180  C   GLU A 129       4.223   0.741   4.215  1.00  9.94           C  
ANISOU 1180  C   GLU A 129     2345    743    688    -82    -64    -98       C  
ATOM   1181  O   GLU A 129       3.382   1.249   4.905  1.00 10.53           O  
ANISOU 1181  O   GLU A 129     2464    819    717     40   -105    -34       O  
ATOM   1182  CB AGLU A 129       4.954  -1.629   4.746  0.50 10.87           C  
ANISOU 1182  CB AGLU A 129     2322    878    926    -28    -43   -117       C  
ATOM   1183  CB BGLU A 129       5.369  -1.468   4.450  0.50 12.36           C  
ANISOU 1183  CB BGLU A 129     2653    985   1056    142   -151   -135       C  
ATOM   1184  CG AGLU A 129       6.217  -2.449   5.048  0.50 15.99           C  
ANISOU 1184  CG AGLU A 129     2984   1638   1453    370   -201   -101       C  
ATOM   1185  CG BGLU A 129       4.033  -2.058   4.849  0.50 16.96           C  
ANISOU 1185  CG BGLU A 129     3139   1568   1736   -192   -254   -187       C  
ATOM   1186  CD AGLU A 129       6.110  -3.887   4.591  0.50 20.36           C  
ANISOU 1186  CD AGLU A 129     3508   2163   2061    232    -94    -94       C  
ATOM   1187  CD BGLU A 129       3.975  -3.596   4.588  0.50 23.02           C  
ANISOU 1187  CD BGLU A 129     3866   2218   2661   -103   -286   -215       C  
ATOM   1188  OE1AGLU A 129       5.375  -4.130   3.615  0.50 25.65           O  
ANISOU 1188  OE1AGLU A 129     4358   2816   2572     82   -146   -347       O  
ATOM   1189  OE1BGLU A 129       5.016  -4.284   4.563  0.50 22.58           O  
ANISOU 1189  OE1BGLU A 129     4963    921   2694    154   -129   -297       O  
ATOM   1190  OE2AGLU A 129       6.731  -4.755   5.231  0.50 23.97           O  
ANISOU 1190  OE2AGLU A 129     4276   2180   2651    393   -261   -319       O  
ATOM   1191  OE2BGLU A 129       2.884  -4.154   4.396  0.50 25.91           O  
ANISOU 1191  OE2BGLU A 129     4473   1876   3494   -549   -441    166       O  
ATOM   1192  N   ARG A 130       4.194   0.857   2.896  1.00 11.41           N  
ANISOU 1192  N   ARG A 130     2500   1188    646     -1    -46   -297       N  
ATOM   1193  CA  ARG A 130       3.097   1.551   2.259  1.00 11.65           C  
ANISOU 1193  CA  ARG A 130     2423   1227    777    -13   -148   -193       C  
ATOM   1194  C   ARG A 130       1.771   0.863   2.541  1.00 12.60           C  
ANISOU 1194  C   ARG A 130     2442   1257   1086    -86   -235   -359       C  
ATOM   1195  O   ARG A 130       1.663  -0.366   2.473  1.00 14.67           O  
ANISOU 1195  O   ARG A 130     2768    875   1929   -104   -514   -366       O  
ATOM   1196  CB  ARG A 130       3.268   1.622   0.761  1.00 14.52           C  
ANISOU 1196  CB  ARG A 130     2607   2051    858     37   -253    -54       C  
ATOM   1197  CG  ARG A 130       4.497   2.314   0.305  1.00 16.06           C  
ANISOU 1197  CG  ARG A 130     2994   1968   1140   -138   -221    198       C  
ATOM   1198  CD  ARG A 130       4.219   3.746   0.290  1.00 16.61           C  
ANISOU 1198  CD  ARG A 130     2990   2093   1227   -109   -104   -125       C  
ATOM   1199  NE  ARG A 130       5.357   4.490  -0.275  1.00 17.03           N  
ANISOU 1199  NE  ARG A 130     2990   1454   2026     16   -219    182       N  
ATOM   1200  CZ  ARG A 130       5.410   5.800  -0.497  1.00 15.05           C  
ANISOU 1200  CZ  ARG A 130     2959   1405   1352    -80   -112     71       C  
ATOM   1201  NH1 ARG A 130       4.370   6.539  -0.292  1.00 15.18           N  
ANISOU 1201  NH1 ARG A 130     3045   1397   1324   -121    -67     58       N  
ATOM   1202  NH2 ARG A 130       6.575   6.342  -0.855  1.00 17.89           N  
ANISOU 1202  NH2 ARG A 130     3246   1819   1731    -48    128    376       N  
ATOM   1203  N   ALA A 131       0.771   1.662   2.863  1.00 13.49           N  
ANISOU 1203  N   ALA A 131     2455   1114   1553   -112   -283   -267       N  
ATOM   1204  CA  ALA A 131      -0.546   1.116   3.203  1.00 17.42           C  
ANISOU 1204  CA  ALA A 131     2694   1646   2276   -234   -277   -199       C  
ATOM   1205  C   ALA A 131      -1.223   0.557   1.952  1.00 20.10           C  
ANISOU 1205  C   ALA A 131     3095   1762   2779   -298   -275   -216       C  
ATOM   1206  O   ALA A 131      -0.881   0.978   0.833  1.00 21.91           O  
ANISOU 1206  O   ALA A 131     3255   2336   2732   -414   -779    -63       O  
ATOM   1207  CB  ALA A 131      -1.382   2.160   3.957  1.00 19.65           C  
ANISOU 1207  CB  ALA A 131     2882   1895   2686   -183     23   -286       C  
TER    1208      ALA A 131                                                      
HETATM 1209  C1 AZGB A 133       3.605   6.441  22.354  0.70 18.58           C  
ANISOU 1209  C1 AZGB A 133     2763   2229   2068    295     38   -379       C  
HETATM 1210  C1 BZGB A 133       6.593   7.911  22.798  0.30 14.61           C  
ANISOU 1210  C1 BZGB A 133     2569   1368   1611   -271    263    998       C  
HETATM 1211  O1 AZGB A 133       6.046   7.366  23.632  0.70 16.19           O  
ANISOU 1211  O1 AZGB A 133     3059   1657   1435    284   -169    -14       O  
HETATM 1212  O1 BZGB A 133       4.228   6.624  23.643  0.30 21.97           O  
ANISOU 1212  O1 BZGB A 133     3377   2075   2896     72    215   -504       O  
HETATM 1213  C2 AZGB A 133       4.787   7.021  21.596  0.70 15.94           C  
ANISOU 1213  C2 AZGB A 133     2802   1537   1718    331   -125   -513       C  
HETATM 1214  C2 BZGB A 133       5.522   7.418  21.805  0.30 19.55           C  
ANISOU 1214  C2 BZGB A 133     2637   1885   2906    159     13    -56       C  
HETATM 1215  O2 AZGB A 133       5.654   7.142  15.226  0.70 14.72           O  
ANISOU 1215  O2 AZGB A 133     3203   1445    945    431   -216   -194       O  
HETATM 1216  O2 BZGB A 133       6.199   5.263  15.309  0.30 22.16           O  
ANISOU 1216  O2 BZGB A 133     3199   2801   2418     81   -127   -518       O  
HETATM 1217  C3 AZGB A 133       4.674   7.028  20.242  0.70 15.64           C  
ANISOU 1217  C3 AZGB A 133     2653   1416   1871    190      8    516       C  
HETATM 1218  C3 BZGB A 133       5.690   7.571  20.440  0.30 20.47           C  
ANISOU 1218  C3 BZGB A 133     2805   1962   3010    116     47     89       C  
HETATM 1219  O3 AZGB A 133       6.003   4.981  15.349  0.70 13.66           O  
ANISOU 1219  O3 AZGB A 133     2887   1545    755    537   -249   -169       O  
HETATM 1220  O3 BZGB A 133       6.245   7.481  15.530  0.30 23.23           O  
ANISOU 1220  O3 BZGB A 133     3288   3229   2306   -176    112    -36       O  
HETATM 1221  C4 AZGB A 133       5.956   7.446  22.304  0.70 14.06           C  
ANISOU 1221  C4 AZGB A 133     2948   1550    843    140   -289   -147       C  
HETATM 1222  C4 BZGB A 133       4.379   6.788  22.296  0.30 21.10           C  
ANISOU 1222  C4 BZGB A 133     2925   2230   2860     31    274   -118       C  
HETATM 1223  C5 AZGB A 133       7.310   7.762  24.189  0.70 15.41           C  
ANISOU 1223  C5 AZGB A 133     2899   1411   1544     35     -9    193       C  
HETATM 1224  C5 BZGB A 133       2.843   6.394  23.940  0.30 22.67           C  
ANISOU 1224  C5 BZGB A 133     3438   2078   3097   -211    135   -903       C  
HETATM 1225  C6 AZGB A 133       6.977   7.953  21.483  0.70 15.39           C  
ANISOU 1225  C6 AZGB A 133     3402   1194   1251    279    231    216       C  
HETATM 1226  C6 BZGB A 133       3.408   6.314  21.415  0.30 22.01           C  
ANISOU 1226  C6 BZGB A 133     3026   2531   2804    152     76     44       C  
HETATM 1227  C7 AZGB A 133       6.907   7.964  20.095  0.70 12.96           C  
ANISOU 1227  C7 AZGB A 133     2831   1183    908    304    -14    -70       C  
HETATM 1228  C7 BZGB A 133       3.567   6.471  20.034  0.30 21.32           C  
ANISOU 1228  C7 BZGB A 133     2950   2301   2848    333    133    -78       C  
HETATM 1229  C8 AZGB A 133       5.751   7.542  19.501  0.70 16.08           C  
ANISOU 1229  C8 AZGB A 133     2916   1306   1885    139   -457    248       C  
HETATM 1230  C8 BZGB A 133       4.708   7.097  19.560  0.30 22.50           C  
ANISOU 1230  C8 BZGB A 133     2832   2628   3088    133    -59     -1       C  
HETATM 1231  C9 AZGB A 133       5.656   7.557  18.018  0.70 17.40           C  
ANISOU 1231  C9 AZGB A 133     3211   1620   1779    115   -190   -523       C  
HETATM 1232  C9 BZGB A 133       4.884   7.263  18.060  0.30 20.89           C  
ANISOU 1232  C9 BZGB A 133     2551   2432   2952     -3     26   -439       C  
HETATM 1233  C10AZGB A 133       6.405   6.350  17.334  0.70 16.94           C  
ANISOU 1233  C10AZGB A 133     3122   1421   1893   -254   -524   -275       C  
HETATM 1234  C10BZGB A 133       5.776   6.154  17.480  0.30 20.64           C  
ANISOU 1234  C10BZGB A 133     2808   2605   2428     27    149   -425       C  
HETATM 1235  C11AZGB A 133       6.053   6.134  15.829  0.70 13.45           C  
ANISOU 1235  C11AZGB A 133     2665   1410   1035     72   -293    -87       C  
HETATM 1236  C11BZGB A 133       6.106   6.317  15.979  0.30 22.40           C  
ANISOU 1236  C11BZGB A 133     3295   2785   2431     26     55   -323       C  
HETATM 1237  O   HOH A 134       5.293  -0.966  -1.150  1.00 34.22           O  
ANISOU 1237  O   HOH A 134     5158   4262   3579    278   -633  -2464       O  
HETATM 1238  O   HOH A 135       3.126  21.325  23.859  1.00 30.50           O  
ANISOU 1238  O   HOH A 135     5476   2784   3327   1387   1499    370       O  
HETATM 1239  O   HOH A 136      12.985   5.958  33.550  1.00114.74           O  
ANISOU 1239  O   HOH A 136    17562  19829   6203   3732  -3152  -2200       O  
HETATM 1240  O   HOH A 137      18.438  11.998  21.593  1.00 36.67           O  
ANISOU 1240  O   HOH A 137     3774   5822   4335    480   -861  -1856       O  
HETATM 1241  O   HOH A 138      10.433  22.097  12.768  1.00  8.64           O  
ANISOU 1241  O   HOH A 138     2112    531    636     37     19     12       O  
HETATM 1242  O   HOH A 139      12.763  25.487   6.073  1.00 28.28           O  
ANISOU 1242  O   HOH A 139     5899   2588   2259   -125    767   1003       O  
HETATM 1243  O   HOH A 140      17.650   0.946  13.179  1.00 28.90           O  
ANISOU 1243  O   HOH A 140     3694   3654   3633     61    733    -31       O  
HETATM 1244  O   HOH A 141       7.212  24.890  12.324  1.00 10.26           O  
ANISOU 1244  O   HOH A 141     1992   1048    859    -58     -2   -322       O  
HETATM 1245  O   HOH A 142      17.800  10.950   0.148  1.00 18.05           O  
ANISOU 1245  O   HOH A 142     4233   1737    886     61    653   -283       O  
HETATM 1246  O   HOH A 143       4.401  14.552  30.862  1.00 35.81           O  
ANISOU 1246  O   HOH A 143     8110   2898   2595    -85    832   -214       O  
HETATM 1247  O   HOH A 144      14.783  10.359   0.761  1.00 32.02           O  
ANISOU 1247  O   HOH A 144     6263   3397   2506   -109   1035   1005       O  
HETATM 1248  O   HOH A 145       3.990   1.066  -3.114  1.00 94.02           O  
ANISOU 1248  O   HOH A 145    17060  13666   4995   1459   -115  -5484       O  
HETATM 1249  O  AHOH A 146      13.287   2.535  33.523  0.50 30.28           O  
ANISOU 1249  O  AHOH A 146     5135   4725   1642    914    331    246       O  
HETATM 1250  O  BHOH A 146      14.998   4.271  32.621  0.50 29.71           O  
ANISOU 1250  O  BHOH A 146     6052   3172   2062    -73   -756     55       O  
HETATM 1251  O   HOH A 147       1.912  22.801  25.856  1.00 37.13           O  
ANISOU 1251  O   HOH A 147     6177   4635   3294   2497   1617    753       O  
HETATM 1252  O   HOH A 148      18.622   0.097  22.150  1.00 10.67           O  
ANISOU 1252  O   HOH A 148     2240    770   1042    164   -101     63       O  
HETATM 1253  O   HOH A 149      15.052   8.330  -0.935  1.00 22.25           O  
ANISOU 1253  O   HOH A 149     3931   1979   2541   -513    436   -361       O  
HETATM 1254  O   HOH A 150      -1.690   7.754  -0.368  1.00 27.41           O  
ANISOU 1254  O   HOH A 150     5670   3377   1367  -1560    208     44       O  
HETATM 1255  O   HOH A 151       0.895   7.247  -1.939  1.00 23.44           O  
ANISOU 1255  O   HOH A 151     4089   3099   1716     76   -518    390       O  
HETATM 1256  O   HOH A 152       6.415  21.667  -1.424  1.00 34.58           O  
ANISOU 1256  O   HOH A 152     7189   3360   2590   -124   1558   -578       O  
HETATM 1257  O   HOH A 153      -2.277   4.626  -0.320  1.00 33.31           O  
ANISOU 1257  O   HOH A 153     4355   3152   5149   -147   -369    182       O  
HETATM 1258  O   HOH A 154      22.664   6.287  29.253  1.00 37.06           O  
ANISOU 1258  O   HOH A 154     4977   3121   5982    -30  -1765    994       O  
HETATM 1259  O   HOH A 155      13.834  -3.999   2.405  1.00 80.45           O  
ANISOU 1259  O   HOH A 155    15889   2596  12081    747   1787   1914       O  
HETATM 1260  O   HOH A 156       6.482  20.120  29.402  1.00 35.51           O  
ANISOU 1260  O   HOH A 156     5520   5573   2398    555    229  -1079       O  
HETATM 1261  O   HOH A 157       5.151  19.187  -8.226  1.00 29.88           O  
ANISOU 1261  O   HOH A 157     4146   3033   4173   -815     94    -59       O  
HETATM 1262  O   HOH A 158      -4.027   6.024   7.516  1.00 31.46           O  
ANISOU 1262  O   HOH A 158     3710   3754   4489   -319     -3   -194       O  
HETATM 1263  O   HOH A 159       3.309  27.628  -6.424  1.00 41.76           O  
ANISOU 1263  O   HOH A 159     5347   5315   5202   -662  -1177  -1366       O  
HETATM 1264  O   HOH A 160      -3.805  -0.553  22.383  1.00 11.23           O  
ANISOU 1264  O   HOH A 160     2363    944    956   -185   -135    144       O  
HETATM 1265  O   HOH A 161      -6.757   5.313  23.929  1.00 33.36           O  
ANISOU 1265  O   HOH A 161     6166   2855   3652  -1509    675     30       O  
HETATM 1266  O   HOH A 162      -2.576   0.851  -1.339  1.00 39.85           O  
ANISOU 1266  O   HOH A 162     6069   5490   3581    -40  -2327    133       O  
HETATM 1267  O   HOH A 163      -2.704  20.044   1.453  1.00 23.82           O  
ANISOU 1267  O   HOH A 163     4114   3001   1935  -1715    116   -160       O  
HETATM 1268  O   HOH A 164      14.686  -5.411  22.512  0.50 16.54           O  
ANISOU 1268  O   HOH A 164     3750    612   1920   -117  -1019     85       O  
HETATM 1269  O   HOH A 165      11.330  24.945   4.319  1.00 32.30           O  
ANISOU 1269  O   HOH A 165     4189   4678   3405   -592   1095   1561       O  
HETATM 1270  O   HOH A 166      12.042  -6.500  23.269  1.00 21.48           O  
ANISOU 1270  O   HOH A 166     4011   1817   2330    255    -40    257       O  
HETATM 1271  O   HOH A 167       4.677  24.371  13.210  1.00 10.58           O  
ANISOU 1271  O   HOH A 167     2215    888    917      0    -40   -254       O  
HETATM 1272  O   HOH A 168      19.659  10.134  17.661  1.00 30.38           O  
ANISOU 1272  O   HOH A 168     4491   3044   4009    457    682    446       O  
HETATM 1273  O  AHOH A 169      16.695  21.046   4.175  0.50 23.64           O  
ANISOU 1273  O  AHOH A 169     4828   2653   1500   -246    543     65       O  
HETATM 1274  O  BHOH A 169      15.597  22.225   4.952  0.50 29.83           O  
ANISOU 1274  O  BHOH A 169     4701   3904   2727    -20    760   1367       O  
HETATM 1275  O   HOH A 170      14.127  -2.085  31.552  1.00 32.47           O  
ANISOU 1275  O   HOH A 170     4540   3987   3808    827    757    892       O  
HETATM 1276  O   HOH A 171       9.960  21.365   2.794  1.00 39.86           O  
ANISOU 1276  O   HOH A 171     7299   4614   3231    366   1108   -956       O  
HETATM 1277  O   HOH A 172       3.440  10.029  13.405  1.00 30.87           O  
ANISOU 1277  O   HOH A 172     4254   5092   2382    777    462   1199       O  
HETATM 1278  O   HOH A 173       7.317   4.001  35.583  1.00 32.27           O  
ANISOU 1278  O   HOH A 173     6194   3591   2476  -1334   -274   -230       O  
HETATM 1279  O   HOH A 174       5.035  29.007   4.254  1.00 27.82           O  
ANISOU 1279  O   HOH A 174     3949   2374   4244   -402   -199  -1323       O  
HETATM 1280  O   HOH A 175       6.645  23.126  26.398  1.00 56.47           O  
ANISOU 1280  O   HOH A 175     9243   9286   2923   -927    391   -400       O  
HETATM 1281  O   HOH A 176      15.001  22.115  32.640  1.00 37.52           O  
ANISOU 1281  O   HOH A 176     8059   2877   3317  -1551   -201  -1027       O  
HETATM 1282  O   HOH A 177       6.104  -2.283  22.926  1.00 28.97           O  
ANISOU 1282  O   HOH A 177     4144   4218   2645    435   -348    -95       O  
HETATM 1283  O   HOH A 178       3.085  -4.682  22.524  1.00 31.08           O  
ANISOU 1283  O   HOH A 178     5041   3539   3228    752    993    769       O  
HETATM 1284  O   HOH A 179      -3.606   3.147  28.994  1.00 27.43           O  
ANISOU 1284  O   HOH A 179     4332   2515   3573   -148   -703   -441       O  
HETATM 1285  O   HOH A 180      -3.701  11.681  26.015  1.00 42.10           O  
ANISOU 1285  O   HOH A 180     5906   5064   5024   -545    106  -1079       O  
HETATM 1286  O   HOH A 181       1.239  -6.860  18.535  1.00 27.65           O  
ANISOU 1286  O   HOH A 181     4517   2610   3375   -715    -25     95       O  
HETATM 1287  O   HOH A 182       7.637   2.383  -2.753  1.00 33.42           O  
ANISOU 1287  O   HOH A 182     4925   4001   3769    684    264    857       O  
HETATM 1288  O   HOH A 183      13.505  23.658  21.561  1.00 34.47           O  
ANISOU 1288  O   HOH A 183     5669   3068   4358    -60  -1297  -1444       O  
HETATM 1289  O   HOH A 184      16.779   0.409  32.522  1.00 46.75           O  
ANISOU 1289  O   HOH A 184     6319   5662   5780     20  -2187   3150       O  
HETATM 1290  O   HOH A 185      11.824  12.422  12.138  1.00 10.74           O  
ANISOU 1290  O   HOH A 185     2544    811    722    141    111     36       O  
HETATM 1291  O   HOH A 186      16.596  -0.464  28.816  1.00 29.40           O  
ANISOU 1291  O   HOH A 186     4531   4002   2634   1763    280    -81       O  
HETATM 1292  O   HOH A 187      13.276  -8.672  22.743  1.00 30.51           O  
ANISOU 1292  O   HOH A 187     4010   3384   4198    551    -53   -579       O  
HETATM 1293  O   HOH A 188       9.019   6.846  -3.295  1.00 49.59           O  
ANISOU 1293  O   HOH A 188     7690   8121   3028    276   -120   -205       O  
HETATM 1294  O   HOH A 189       9.009  -4.009   0.951  1.00 34.55           O  
ANISOU 1294  O   HOH A 189     5222   3094   4808   -741    414   1330       O  
HETATM 1295  O   HOH A 190      -3.725  -1.095  19.713  1.00 12.06           O  
ANISOU 1295  O   HOH A 190     2233   1200   1147   -329      4     28       O  
HETATM 1296  O   HOH A 191      20.650   1.189  32.201  1.00 37.21           O  
ANISOU 1296  O   HOH A 191     6648   3880   3609    140   1470   -892       O  
HETATM 1297  O   HOH A 192       6.521  -1.569  -3.679  1.00 50.02           O  
ANISOU 1297  O   HOH A 192     6378   5928   6698   -283   -937   3035       O  
HETATM 1298  O   HOH A 193      -3.663  18.188  23.787  1.00 41.25           O  
ANISOU 1298  O   HOH A 193     4056   5180   6436   1562   -590  -1969       O  
HETATM 1299  O   HOH A 194       6.062  -7.512  13.140  1.00 36.52           O  
ANISOU 1299  O   HOH A 194     5471   2268   6134   -471  -1638   1072       O  
HETATM 1300  O   HOH A 195       8.010  -6.403  17.922  1.00 32.60           O  
ANISOU 1300  O   HOH A 195     5803   2542   4039   -801  -1586   1577       O  
HETATM 1301  O   HOH A 196       1.056  20.249   5.128  1.00 13.37           O  
ANISOU 1301  O   HOH A 196     2513   1332   1235   -104   -188    216       O  
HETATM 1302  O   HOH A 197      -0.564  28.137  -5.977  1.00 42.03           O  
ANISOU 1302  O   HOH A 197     8159   4606   3202    403   1157   1015       O  
HETATM 1303  O   HOH A 198      17.452  12.714  30.423  1.00 38.69           O  
ANISOU 1303  O   HOH A 198     6200   5186   3313   1184  -1330    841       O  
HETATM 1304  O   HOH A 199      21.541   8.347  17.243  1.00 45.62           O  
ANISOU 1304  O   HOH A 199     3561   6563   7209   -973   1521     81       O  
HETATM 1305  O   HOH A 200      15.207   9.062   3.228  1.00 15.80           O  
ANISOU 1305  O   HOH A 200     3440   1243   1320   -443    426     34       O  
HETATM 1306  O   HOH A 201      12.859  12.182  -3.229  1.00 34.99           O  
ANISOU 1306  O   HOH A 201     6561   3748   2986   -167   1011   -530       O  
HETATM 1307  O   HOH A 202      -2.800  19.019  20.697  1.00 38.22           O  
ANISOU 1307  O   HOH A 202     5466   4720   4333   -867      1    845       O  
HETATM 1308  O   HOH A 203      20.878   7.875  14.737  1.00 45.32           O  
ANISOU 1308  O   HOH A 203     5751   4357   7110   1157    810   1173       O  
HETATM 1309  O   HOH A 204       6.259  19.217  -2.773  1.00 36.02           O  
ANISOU 1309  O   HOH A 204     5730   4137   3817   1264    990    106       O  
HETATM 1310  O   HOH A 205       9.791  23.028   5.417  1.00 13.43           O  
ANISOU 1310  O   HOH A 205     2518   1839    743    220      1    -27       O  
HETATM 1311  O   HOH A 206      19.113  21.595   9.078  1.00 55.58           O  
ANISOU 1311  O   HOH A 206     6246   5101   9768  -2253   3406  -2256       O  
HETATM 1312  O   HOH A 207      -2.135   0.274  10.606  1.00 39.23           O  
ANISOU 1312  O   HOH A 207     7625   4433   2846  -1816  -1401   1013       O  
HETATM 1313  O   HOH A 208       7.666  25.652  -6.219  1.00 49.77           O  
ANISOU 1313  O   HOH A 208     6375   4517   8017    890  -1164  -2349       O  
HETATM 1314  O   HOH A 209       9.227  14.840  -5.759  1.00 36.74           O  
ANISOU 1314  O   HOH A 209     5939   4126   3891     59   -889   1291       O  
HETATM 1315  O   HOH A 210      20.229   1.477  14.813  1.00 99.22           O  
ANISOU 1315  O   HOH A 210    18387  14576   4735   -341  -3362   1954       O  
HETATM 1316  O   HOH A 211      16.098  23.277   8.709  1.00 30.90           O  
ANISOU 1316  O   HOH A 211     3993   3223   4522    198   1108    -75       O  
HETATM 1317  O   HOH A 212      -0.606  14.356   6.449  1.00 15.10           O  
ANISOU 1317  O   HOH A 212     3023   1175   1537     12   -237   -144       O  
HETATM 1318  O   HOH A 213       1.882   3.825  19.944  1.00 28.87           O  
ANISOU 1318  O   HOH A 213     4303   4010   2654   -384    163    429       O  
HETATM 1319  O   HOH A 214      -8.139   5.726  21.936  1.00 39.12           O  
ANISOU 1319  O   HOH A 214     4745   4824   5294   -537   -995    -81       O  
HETATM 1320  O   HOH A 215      12.510  10.372  31.766  1.00 38.24           O  
ANISOU 1320  O   HOH A 215     6697   5437   2396  -1754  -1570   -609       O  
HETATM 1321  O   HOH A 216      15.865  -3.209  15.003  1.00 98.74           O  
ANISOU 1321  O   HOH A 216     8383   7432  21700      3   -865    774       O  
HETATM 1322  O   HOH A 217      10.661  -4.247  27.929  1.00 47.17           O  
ANISOU 1322  O   HOH A 217     6287   5921   5712    985  -1172   2735       O  
HETATM 1323  O   HOH A 218      -8.650   3.706  15.776  1.00 32.10           O  
ANISOU 1323  O   HOH A 218     4985   4017   3192  -1056   -108   1044       O  
HETATM 1324  O   HOH A 219       1.697   5.781   0.157  1.00 15.59           O  
ANISOU 1324  O   HOH A 219     3295   1422   1205   -288    -64   -435       O  
HETATM 1325  O   HOH A 220       2.594  -6.452  11.705  1.00 36.19           O  
ANISOU 1325  O   HOH A 220     5226   3025   5499  -1376   -366    878       O  
HETATM 1326  O   HOH A 221      11.217   3.730  33.575  1.00 45.16           O  
ANISOU 1326  O   HOH A 221     7846   4754   4556   -845    -52  -1060       O  
HETATM 1327  O   HOH A 222      -5.106  13.082   5.943  1.00 44.64           O  
ANISOU 1327  O   HOH A 222     5302   4762   6893   -267  -1287  -1455       O  
HETATM 1328  O   HOH A 223       8.864  -2.982  20.095  1.00 15.39           O  
ANISOU 1328  O   HOH A 223     2852   1510   1483     49   -165   -261       O  
HETATM 1329  O   HOH A 224      13.758  -1.702   4.185  1.00 40.91           O  
ANISOU 1329  O   HOH A 224     6496   4369   4676   -333    371   2304       O  
HETATM 1330  O   HOH A 225       6.440  11.381  19.542  1.00 13.58           O  
ANISOU 1330  O   HOH A 225     2480   1161   1518    -86     96    108       O  
HETATM 1331  O   HOH A 226      15.991  16.745  33.204  1.00 43.58           O  
ANISOU 1331  O   HOH A 226     7080   4547   4930   -522   -979  -1382       O  
HETATM 1332  O   HOH A 227      -3.016  13.911   5.474  1.00 61.25           O  
ANISOU 1332  O   HOH A 227     6423   5218  11631  -2130  -3055   4999       O  
HETATM 1333  O   HOH A 228      17.737   2.307  31.403  1.00 46.07           O  
ANISOU 1333  O   HOH A 228     4687   7102   5715    923   -915   2537       O  
HETATM 1334  O   HOH A 229      -4.896   2.643   5.101  1.00 58.90           O  
ANISOU 1334  O   HOH A 229     5467  13223   3689   -124   -687   -863       O  
HETATM 1335  O   HOH A 230      -8.584  11.834  18.065  1.00 37.95           O  
ANISOU 1335  O   HOH A 230     3659   4839   5921    581    119  -1579       O  
HETATM 1336  O   HOH A 231       8.879  10.546  21.425  1.00 12.88           O  
ANISOU 1336  O   HOH A 231     2723   1059   1110   -158     44     -8       O  
HETATM 1337  O   HOH A 232       3.612  11.295  19.359  1.00 13.91           O  
ANISOU 1337  O   HOH A 232     2475   1467   1341   -223    192     15       O  
HETATM 1338  O   HOH A 233      19.214  20.520   7.222  1.00 34.47           O  
ANISOU 1338  O   HOH A 233     5427   3030   4637  -1439   1483  -1237       O  
HETATM 1339  O   HOH A 234      18.200   2.988  33.671  1.00 46.34           O  
ANISOU 1339  O   HOH A 234     7012   6891   3702   -621  -1247   1184       O  
HETATM 1340  O   HOH A 235      12.687  20.754  33.909  1.00125.61           O  
ANISOU 1340  O   HOH A 235    25522  13238   8964  -4685   4727  -4217       O  
HETATM 1341  O   HOH A 236       1.954  12.747  14.321  1.00 18.33           O  
ANISOU 1341  O   HOH A 236     3046   2303   1614     66    125   1156       O  
HETATM 1342  O   HOH A 237      21.089  10.823  10.556  1.00 41.77           O  
ANISOU 1342  O   HOH A 237     4556   6777   4536   -232   1187   1827       O  
HETATM 1343  O   HOH A 238       7.494  25.923  -0.924  1.00 37.27           O  
ANISOU 1343  O   HOH A 238     6255   5103   2800  -1978    743    412       O  
HETATM 1344  O   HOH A 239      20.401   5.083  28.393  0.50 12.51           O  
ANISOU 1344  O   HOH A 239     2746    827   1181    243   -222     59       O  
HETATM 1345  O   HOH A 240      13.022  21.809  19.854  1.00 16.77           O  
ANISOU 1345  O   HOH A 240     2685   2618   1068   -430   -159      6       O  
HETATM 1346  O   HOH A 241      11.263  -2.726   0.868  1.00 18.41           O  
ANISOU 1346  O   HOH A 241     3945   1359   1691   -431   -212    -57       O  
HETATM 1347  O   HOH A 242      13.165  -7.086   6.635  1.00 35.78           O  
ANISOU 1347  O   HOH A 242     5303   4726   3565    982  -1268     44       O  
HETATM 1348  O   HOH A 243       2.266   9.745  17.424  1.00 14.21           O  
ANISOU 1348  O   HOH A 243     2675   1370   1351   -162    -58     80       O  
HETATM 1349  O   HOH A 244      17.575  -1.496  20.185  1.00 15.56           O  
ANISOU 1349  O   HOH A 244     2615   1308   1987    137   -317     47       O  
HETATM 1350  O   HOH A 245       4.470  -4.486  26.317  1.00 40.06           O  
ANISOU 1350  O   HOH A 245     6100   5957   3163   -126    516   -166       O  
HETATM 1351  O   HOH A 246       1.638  26.182   2.233  1.00 17.65           O  
ANISOU 1351  O   HOH A 246     3462   1109   2133     -1     54   -244       O  
HETATM 1352  O   HOH A 247       2.583   6.868  13.713  1.00 20.30           O  
ANISOU 1352  O   HOH A 247     2954   1756   3001   -248    839   -600       O  
HETATM 1353  O   HOH A 248       3.053  13.750  18.319  1.00 16.95           O  
ANISOU 1353  O   HOH A 248     2966   1422   2052   -161     33    -65       O  
HETATM 1354  O   HOH A 249      24.275  14.382   6.341  1.00 43.35           O  
ANISOU 1354  O   HOH A 249     5261   4780   6428   1590    480  -1575       O  
HETATM 1355  O   HOH A 250       7.035  27.735  11.942  1.00 18.62           O  
ANISOU 1355  O   HOH A 250     2501   1493   3077    424   -404   -426       O  
HETATM 1356  O   HOH A 251      16.209  18.875  14.214  1.00 17.86           O  
ANISOU 1356  O   HOH A 251     3416   1760   1608   -175   -347     67       O  
HETATM 1357  O   HOH A 252      11.478  -3.081  13.714  1.00 17.53           O  
ANISOU 1357  O   HOH A 252     3843   1345   1469    -62      3    -47       O  
HETATM 1358  O   HOH A 253      16.320  21.142   7.235  1.00 18.01           O  
ANISOU 1358  O   HOH A 253     3685   1026   2129   -391    126    261       O  
HETATM 1359  O   HOH A 254       5.538  -5.546  16.525  1.00 46.36           O  
ANISOU 1359  O   HOH A 254     8246   3127   6239   -651  -1176     78       O  
HETATM 1360  O   HOH A 255       5.340  -4.918  19.269  1.00 45.07           O  
ANISOU 1360  O   HOH A 255     6328   3025   7769  -1016     -4   -710       O  
HETATM 1361  O   HOH A 256      23.004  18.510  10.918  1.00 53.09           O  
ANISOU 1361  O   HOH A 256     7912   8734   3522   -756   1351  -1069       O  
HETATM 1362  O   HOH A 257       4.085  27.117   2.464  1.00 17.38           O  
ANISOU 1362  O   HOH A 257     3309   1450   1845     51   -223    -71       O  
HETATM 1363  O   HOH A 258      11.245  30.822  -7.898  1.00 48.24           O  
ANISOU 1363  O   HOH A 258     6978   4833   6518   1244   -126   1949       O  
HETATM 1364  O   HOH A 259       2.999  19.147  30.927  1.00 51.66           O  
ANISOU 1364  O   HOH A 259     5887   9266   4475   2462   -234   1028       O  
HETATM 1365  O   HOH A 260      11.983 -10.261  17.022  1.00 37.41           O  
ANISOU 1365  O   HOH A 260     5507   3624   5082   -739   -466     25       O  
HETATM 1366  O   HOH A 261      23.450   7.714  12.991  1.00 48.88           O  
ANISOU 1366  O   HOH A 261     4253   6545   7773  -1644   -454    929       O  
HETATM 1367  O   HOH A 262       9.172  10.770  -4.596  1.00 42.68           O  
ANISOU 1367  O   HOH A 262     6871   4806   4537   1653   1078    996       O  
HETATM 1368  O   HOH A 263      14.177  -3.558  13.075  1.00 37.67           O  
ANISOU 1368  O   HOH A 263     4959   2623   6730    433   1225   -750       O  
HETATM 1369  O   HOH A 264      11.079  22.307  26.495  1.00 25.68           O  
ANISOU 1369  O   HOH A 264     5343   2312   2099     31    181    -66       O  
HETATM 1370  O   HOH A 265      19.287  12.906  26.071  1.00 37.14           O  
ANISOU 1370  O   HOH A 265     7574   2547   3990   -371   -509   -241       O  
HETATM 1371  O   HOH A 266       5.168  22.696  24.090  1.00 22.69           O  
ANISOU 1371  O   HOH A 266     4199   2609   1814   1195    -13    199       O  
HETATM 1372  O   HOH A 267      -6.089   0.867  22.222  1.00 16.71           O  
ANISOU 1372  O   HOH A 267     2773   1148   2424   -179   -763    396       O  
HETATM 1373  O   HOH A 268      11.475  -5.739  21.015  1.00 21.09           O  
ANISOU 1373  O   HOH A 268     4042    982   2988   -160    271    657       O  
HETATM 1374  O   HOH A 269      17.737  13.878  21.738  1.00 19.85           O  
ANISOU 1374  O   HOH A 269     3328   2506   1707   -277   -178   -500       O  
HETATM 1375  O   HOH A 270       3.479   3.630  35.830  1.00 23.25           O  
ANISOU 1375  O   HOH A 270     5699   2221    912   -861   -197    173       O  
HETATM 1376  O   HOH A 271       6.329   9.159  -1.765  1.00 19.36           O  
ANISOU 1376  O   HOH A 271     3738   1722   1894   -248    384    -12       O  
HETATM 1377  O   HOH A 272      15.301  19.874  27.334  1.00 22.32           O  
ANISOU 1377  O   HOH A 272     5168   1683   1626   -386   -550   -139       O  
HETATM 1378  O   HOH A 273      14.771   1.622  29.197  1.00 20.98           O  
ANISOU 1378  O   HOH A 273     3216   3288   1468    573   -397    564       O  
HETATM 1379  O   HOH A 274      13.156  21.298  28.401  1.00 22.99           O  
ANISOU 1379  O   HOH A 274     5040   1744   1951      1   -548   -107       O  
HETATM 1380  O   HOH A 275       2.207  -3.750  24.750  1.00 21.25           O  
ANISOU 1380  O   HOH A 275     3176   2884   2010    641   -232   -581       O  
HETATM 1381  O   HOH A 276       6.268  -0.477   1.437  1.00 18.17           O  
ANISOU 1381  O   HOH A 276     2893   2145   1862     78    415   -191       O  
HETATM 1382  O   HOH A 277       0.698  18.241  18.753  1.00 27.94           O  
ANISOU 1382  O   HOH A 277     3373   3192   4048   -571   -797   2240       O  
HETATM 1383  O   HOH A 278       0.260   3.420  -0.221  1.00 21.14           O  
ANISOU 1383  O   HOH A 278     3407   1900   2726   -224   -822   -409       O  
HETATM 1384  O   HOH A 279       0.184   7.756  17.579  1.00 17.14           O  
ANISOU 1384  O   HOH A 279     2948   1938   1624    -68    236     -5       O  
HETATM 1385  O   HOH A 280      18.248  11.398  24.354  1.00 26.36           O  
ANISOU 1385  O   HOH A 280     4042   1418   4555    367    -25    834       O  
HETATM 1386  O   HOH A 281       6.521   8.391  12.922  1.00 19.55           O  
ANISOU 1386  O   HOH A 281     2784   3247   1397   -431     60    275       O  
HETATM 1387  O   HOH A 282      -0.683  18.688   3.764  1.00 18.50           O  
ANISOU 1387  O   HOH A 282     3543   1447   2037   -115   -885    354       O  
HETATM 1388  O   HOH A 283      -3.755   1.859  15.102  1.00 19.54           O  
ANISOU 1388  O   HOH A 283     3673   1347   2404    223    958    444       O  
HETATM 1389  O   HOH A 284       0.367   3.024  34.749  1.00 23.36           O  
ANISOU 1389  O   HOH A 284     5737   2018   1118    346    304   -104       O  
HETATM 1390  O   HOH A 285       8.951  -3.489  23.001  1.00 30.18           O  
ANISOU 1390  O   HOH A 285     6837   1673   2954   -919   1532   -344       O  
HETATM 1391  O   HOH A 286      17.541  13.461  27.895  1.00 25.69           O  
ANISOU 1391  O   HOH A 286     3909   2928   2922    638   -770    799       O  
HETATM 1392  O   HOH A 287       5.031  -1.681  25.549  1.00 21.98           O  
ANISOU 1392  O   HOH A 287     3407   2803   2140    615   -150   -623       O  
HETATM 1393  O   HOH A 288       0.551   5.026  32.382  1.00 20.38           O  
ANISOU 1393  O   HOH A 288     3948   2143   1650   -398    147   -371       O  
HETATM 1394  O   HOH A 289       6.264  11.800  16.607  1.00 26.25           O  
ANISOU 1394  O   HOH A 289     2386   5745   1842   -400    467    445       O  
HETATM 1395  O   HOH A 290      -8.083   6.465  15.258  1.00 26.91           O  
ANISOU 1395  O   HOH A 290     3329   3250   3646   -643   -582    572       O  
HETATM 1396  O   HOH A 291      -7.582   6.391  19.297  1.00 28.12           O  
ANISOU 1396  O   HOH A 291     4071   4118   2493    851   1011   -434       O  
HETATM 1397  O   HOH A 292      -7.062   9.368  19.765  1.00 26.81           O  
ANISOU 1397  O   HOH A 292     2958   4614   2613   -220    887   -274       O  
HETATM 1398  O   HOH A 293       2.890  -2.401  17.721  1.00 24.08           O  
ANISOU 1398  O   HOH A 293     3887   2801   2458    603   -493   -157       O  
HETATM 1399  O   HOH A 294       7.418  -6.312  15.590  1.00 24.54           O  
ANISOU 1399  O   HOH A 294     5279   1358   2686  -1078  -1011   1083       O  
HETATM 1400  O   HOH A 295       1.057  15.607  18.530  1.00 24.02           O  
ANISOU 1400  O   HOH A 295     4704   2546   1876   -526    404     18       O  
HETATM 1401  O   HOH A 296       5.203  10.088  29.263  1.00 24.16           O  
ANISOU 1401  O   HOH A 296     6054   1695   1431   -124   -270    355       O  
HETATM 1402  O  AHOH A 297       2.910   1.003  18.725  0.50 13.55           O  
ANISOU 1402  O  AHOH A 297     2225   1995    927   -457    234   -242       O  
HETATM 1403  O  BHOH A 297       2.132   2.464  18.693  0.50 18.80           O  
ANISOU 1403  O  BHOH A 297     2841   2745   1557   -252    133      7       O  
HETATM 1404  O   HOH A 298       7.104  -3.047  30.535  1.00 23.33           O  
ANISOU 1404  O   HOH A 298     5558   1433   1870   -389    719    275       O  
HETATM 1405  O   HOH A 299      14.402   0.696  31.734  1.00 29.21           O  
ANISOU 1405  O   HOH A 299     4429   4154   2513    287   -122   1336       O  
HETATM 1406  O   HOH A 300      17.147   7.191   2.227  1.00 25.41           O  
ANISOU 1406  O   HOH A 300     4624   2731   2298   -853   1101   -330       O  
HETATM 1407  O   HOH A 301      -4.847  11.455  13.514  1.00 28.52           O  
ANISOU 1407  O   HOH A 301     3574   5091   2169   1026     41    574       O  
HETATM 1408  O   HOH A 302       9.374  28.886  15.227  1.00 20.61           O  
ANISOU 1408  O   HOH A 302     3900   1385   2546    -78    749    -59       O  
HETATM 1409  O   HOH A 303       9.194  21.378  29.601  1.00 24.56           O  
ANISOU 1409  O   HOH A 303     4639   2284   2407    954    115   -483       O  
HETATM 1410  O   HOH A 304       2.563   9.392  -2.400  1.00 26.95           O  
ANISOU 1410  O   HOH A 304     4402   3166   2671   -187  -1284   -546       O  
HETATM 1411  O   HOH A 305       0.044   5.157  18.637  1.00 31.46           O  
ANISOU 1411  O   HOH A 305     4318   2905   4727   -948  -1467   2494       O  
HETATM 1412  O   HOH A 306       1.445   2.307  -2.385  1.00 34.23           O  
ANISOU 1412  O   HOH A 306     4780   5204   3023    893   -925   -833       O  
HETATM 1413  O   HOH A 307       9.031   4.891  32.699  1.00 22.33           O  
ANISOU 1413  O   HOH A 307     3663   2569   2250   -176   -818    127       O  
HETATM 1414  O   HOH A 308      20.594   4.404  17.562  1.00 25.77           O  
ANISOU 1414  O   HOH A 308     4385   2363   3044    312   1028    868       O  
HETATM 1415  O   HOH A 309       4.838  17.030  29.627  1.00 24.83           O  
ANISOU 1415  O   HOH A 309     5548   2302   1582    -25    485    263       O  
HETATM 1416  O   HOH A 310      17.256   9.046  16.407  1.00 22.80           O  
ANISOU 1416  O   HOH A 310     3956   2686   2020    497   -174    550       O  
HETATM 1417  O   HOH A 311      -1.802  20.200  11.649  1.00 29.25           O  
ANISOU 1417  O   HOH A 311     3760   2974   4376   -582   1662   -437       O  
HETATM 1418  O   HOH A 312       9.986  28.912  19.797  1.00 28.89           O  
ANISOU 1418  O   HOH A 312     4012   2711   4252   -359    988  -1311       O  
HETATM 1419  O   HOH A 313      -1.775  15.875  17.882  1.00 25.97           O  
ANISOU 1419  O   HOH A 313     5775   2016   2076   -688   1224   -756       O  
HETATM 1420  O   HOH A 314      -8.957   2.176  20.600  1.00 20.16           O  
ANISOU 1420  O   HOH A 314     3127   1294   3237     57    661    370       O  
HETATM 1421  O   HOH A 315      18.551   4.704   2.405  1.00 23.57           O  
ANISOU 1421  O   HOH A 315     4394   3264   1297    351   -117   -310       O  
HETATM 1422  O   HOH A 316      -0.590  -5.129  17.475  1.00 29.03           O  
ANISOU 1422  O   HOH A 316     3896   1398   5736    136    751    293       O  
HETATM 1423  O   HOH A 317      13.269  28.668   7.849  1.00 32.15           O  
ANISOU 1423  O   HOH A 317     6414   4092   1709  -1598   -558    -60       O  
HETATM 1424  O   HOH A 318      -9.281   4.114  20.786  1.00 20.25           O  
ANISOU 1424  O   HOH A 318     4458   1570   1664    512    853    530       O  
HETATM 1425  O   HOH A 319       4.392   9.394  15.675  1.00 23.99           O  
ANISOU 1425  O   HOH A 319     4230   1854   3030    791   1198    555       O  
HETATM 1426  O   HOH A 320      12.135  -3.142  24.927  1.00 26.66           O  
ANISOU 1426  O   HOH A 320     7173    917   2037    192    806    251       O  
HETATM 1427  O   HOH A 321      -2.260  19.426   6.675  1.00 28.05           O  
ANISOU 1427  O   HOH A 321     3359   3452   3844    168   -915    423       O  
HETATM 1428  O  AHOH A 322       4.238  13.324  15.658  0.50 17.25           O  
ANISOU 1428  O  AHOH A 322     3868   1370   1313    499    105    160       O  
HETATM 1429  O  BHOH A 322       4.396  11.684  14.785  0.50 18.85           O  
ANISOU 1429  O  BHOH A 322     3162   1893   2107   -216   -118    494       O  
HETATM 1430  O   HOH A 323      16.219  -1.008  17.710  1.00 31.02           O  
ANISOU 1430  O   HOH A 323     6673   2511   2601   1587  -1912   -757       O  
HETATM 1431  O   HOH A 324      -1.577   9.233  26.279  1.00 29.43           O  
ANISOU 1431  O   HOH A 324     4478   3420   3282   -274   1385    178       O  
HETATM 1432  O   HOH A 325      20.962   5.118  21.530  1.00 25.04           O  
ANISOU 1432  O   HOH A 325     4705   2743   2065    792   -107    490       O  
HETATM 1433  O   HOH A 326      -2.363  18.872  16.150  1.00 38.61           O  
ANISOU 1433  O   HOH A 326     3627   5454   5588    161   1014  -2851       O  
HETATM 1434  O   HOH A 327       5.282   7.790  34.324  1.00 36.30           O  
ANISOU 1434  O   HOH A 327     6442   4928   2421   -331   1059   -779       O  
HETATM 1435  O   HOH A 328       9.105  12.118  30.767  1.00 22.98           O  
ANISOU 1435  O   HOH A 328     4577   2201   1952    164    648    583       O  
HETATM 1436  O   HOH A 329       7.872  30.727   8.558  1.00 30.65           O  
ANISOU 1436  O   HOH A 329     3959   2157   5528    240  -1174   1296       O  
HETATM 1437  O   HOH A 330      19.612  14.719  18.235  1.00 26.05           O  
ANISOU 1437  O   HOH A 330     2736   3372   3788   -239    -58   1127       O  
HETATM 1438  O   HOH A 331       5.861  29.941  10.060  1.00 26.78           O  
ANISOU 1438  O   HOH A 331     3587   3094   3492    459   -222      5       O  
HETATM 1439  O   HOH A 332       0.191   8.935  29.302  1.00 44.97           O  
ANISOU 1439  O   HOH A 332    10564   2966   3555    613   2498   1209       O  
HETATM 1440  O   HOH A 333       2.882  -2.397   1.182  1.00 36.13           O  
ANISOU 1440  O   HOH A 333     5274   3304   5149    -38    198  -2011       O  
HETATM 1441  O   HOH A 334       2.384  -5.453  19.944  1.00 33.11           O  
ANISOU 1441  O   HOH A 334     5595   3163   3820   1198   1183   -268       O  
HETATM 1442  O   HOH A 335      -2.764   5.970  28.744  1.00 36.76           O  
ANISOU 1442  O   HOH A 335     4663   4085   5217   -187   -641  -1682       O  
HETATM 1443  O   HOH A 336      21.766  11.668   7.819  1.00 41.22           O  
ANISOU 1443  O   HOH A 336     4380   5163   6118  -1367  -1340   2336       O  
HETATM 1444  O   HOH A 337       3.163  12.193  29.933  1.00 29.66           O  
ANISOU 1444  O   HOH A 337     5391   3145   2730     13     78    359       O  
HETATM 1445  O   HOH A 338      19.938  10.069   1.923  1.00 27.07           O  
ANISOU 1445  O   HOH A 338     4333   3662   2288    741    253    122       O  
HETATM 1446  O   HOH A 339      -7.110   2.672  23.672  1.00 23.02           O  
ANISOU 1446  O   HOH A 339     4695   1868   2182     55    334    303       O  
HETATM 1447  O   HOH A 340      10.373  29.645   6.352  1.00 33.86           O  
ANISOU 1447  O   HOH A 340     6821   3198   2843  -1420  -1210    682       O  
HETATM 1448  O   HOH A 341       2.296  30.217  -7.261  1.00 29.65           O  
ANISOU 1448  O   HOH A 341     5753   2916   2593   -430   -239    427       O  
HETATM 1449  O   HOH A 342       5.326  -1.805  19.827  1.00 32.22           O  
ANISOU 1449  O   HOH A 342     4115   3514   4611  -1211   2115  -1472       O  
HETATM 1450  O   HOH A 343       6.194  23.500  -4.172  1.00 42.42           O  
ANISOU 1450  O   HOH A 343     4665   7201   4251   1172   -286   -364       O  
HETATM 1451  O  AHOH A 344      21.441  17.912   4.311  0.50 23.09           O  
ANISOU 1451  O  AHOH A 344     4470   1716   2585   -826   1563   -420       O  
HETATM 1452  O  BHOH A 344      22.064  17.923   5.908  0.50 25.64           O  
ANISOU 1452  O  BHOH A 344     3489   2872   3381   -484    699    549       O  
HETATM 1453  O   HOH A 345      19.334   4.416  31.968  1.00 50.63           O  
ANISOU 1453  O   HOH A 345     7512   7097   4625    179   -478    244       O  
HETATM 1454  O   HOH A 346      -2.976  14.229  19.811  1.00 28.92           O  
ANISOU 1454  O   HOH A 346     4496   3121   3368   -741   1256  -1096       O  
HETATM 1455  O   HOH A 347      18.133   0.808   1.721  1.00 34.63           O  
ANISOU 1455  O   HOH A 347     3553   6269   3332    487    720   -312       O  
HETATM 1456  O   HOH A 348      20.893   2.431  21.490  1.00 28.28           O  
ANISOU 1456  O   HOH A 348     3080   5325   2338     24    117   -887       O  
HETATM 1457  O   HOH A 349       7.716   3.288  -0.639  1.00 24.37           O  
ANISOU 1457  O   HOH A 349     4011   2710   2536    918    889    742       O  
HETATM 1458  O   HOH A 350      21.607   9.454  22.434  1.00 35.83           O  
ANISOU 1458  O   HOH A 350     5365   3697   4552   -859   -447   1644       O  
HETATM 1459  O   HOH A 351       8.603  21.722  26.693  1.00 34.47           O  
ANISOU 1459  O   HOH A 351     7071   3271   2752   1708  -1296  -1511       O  
HETATM 1460  O   HOH A 352      -2.627  13.595  24.584  1.00 40.06           O  
ANISOU 1460  O   HOH A 352     5730   4406   5085  -1897  -1208    501       O  
HETATM 1461  O   HOH A 353       0.657  -4.118  10.639  1.00 26.85           O  
ANISOU 1461  O   HOH A 353     4034   2940   3226  -1465   -226   -155       O  
HETATM 1462  O   HOH A 354      10.197  -7.229  15.108  1.00 35.88           O  
ANISOU 1462  O   HOH A 354     4740   2825   6066    172  -1203    826       O  
HETATM 1463  O   HOH A 355       8.724  -6.055  20.311  1.00 36.40           O  
ANISOU 1463  O   HOH A 355     4690   4874   4265    584   -527     33       O  
HETATM 1464  O   HOH A 356      10.490  22.346  -3.387  1.00 44.23           O  
ANISOU 1464  O   HOH A 356     6214   4574   6014     67   -402  -1627       O  
HETATM 1465  O   HOH A 357       9.593   3.135  -2.847  1.00 31.15           O  
ANISOU 1465  O   HOH A 357     5870   2611   3353    609    767   -761       O  
HETATM 1466  O   HOH A 358      -1.486  14.174  21.861  1.00 29.74           O  
ANISOU 1466  O   HOH A 358     3810   4840   2646   -391     95   -180       O  
HETATM 1467  O  AHOH A 359       2.479   7.291  31.745  0.50 21.87           O  
ANISOU 1467  O  AHOH A 359     3597   2734   1977    303    454     84       O  
HETATM 1468  O  BHOH A 359       3.109   8.316  31.025  0.50 19.96           O  
ANISOU 1468  O  BHOH A 359     3798   1743   2043    445    226    360       O  
HETATM 1469  O   HOH A 360       0.983  -0.689  -1.617  1.00 51.61           O  
ANISOU 1469  O   HOH A 360     9868   3870   5871    709  -3784  -2854       O  
HETATM 1470  O   HOH A 361      10.396  -5.161   9.368  1.00 28.54           O  
ANISOU 1470  O   HOH A 361     5611   2160   3071    539    457   -364       O  
HETATM 1471  O   HOH A 362      15.585   8.188  31.310  1.00 68.24           O  
ANISOU 1471  O   HOH A 362     7046  11124   7757   1638   -381  -4200       O  
HETATM 1472  O   HOH A 363      21.665  10.070   5.367  1.00 32.16           O  
ANISOU 1472  O   HOH A 363     3772   4800   3646   -718   1185  -1185       O  
CONECT 1209 1213                                                                
CONECT 1210 1214                                                                
CONECT 1211 1221 1223                                                           
CONECT 1212 1222 1224                                                           
CONECT 1213 1209 1217 1221                                                      
CONECT 1214 1210 1218 1222                                                      
CONECT 1215 1235                                                                
CONECT 1216 1236                                                                
CONECT 1217 1213 1229                                                           
CONECT 1218 1214 1230                                                           
CONECT 1219 1235                                                                
CONECT 1220 1236                                                                
CONECT 1221 1211 1213 1225                                                      
CONECT 1222 1212 1214 1226                                                      
CONECT 1223 1211                                                                
CONECT 1224 1212                                                                
CONECT 1225 1221 1227                                                           
CONECT 1226 1222 1228                                                           
CONECT 1227 1225 1229                                                           
CONECT 1228 1226 1230                                                           
CONECT 1229 1217 1227 1231                                                      
CONECT 1230 1218 1228 1232                                                      
CONECT 1231 1229 1233                                                           
CONECT 1232 1230 1234                                                           
CONECT 1233 1231 1235                                                           
CONECT 1234 1232 1236                                                           
CONECT 1235 1215 1219 1233                                                      
CONECT 1236 1216 1220 1234                                                      
MASTER      344    0    1    3   10    0    3    6 1316    1   28   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.