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***  LIPID BINDING PROTEIN 12-MAY-11 3RZY  ***

elNémo ID: 220125132214134349

Job options:

ID        	=	 220125132214134349
JOBID     	=	 LIPID BINDING PROTEIN 12-MAY-11 3RZY
USERID    	=	 test2
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                   12-MAY-11   3RZY              
TITLE     HUMAN ADIPOCYTE LIPID-BINDING PROTEIN FABP4, APO FORM AT 1.08 ANG     
TITLE    2 RESOLUTION.                                                          
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 3RZY    1       JRNL                                     
REVDAT   2   11-FEB-15 3RZY    1       JRNL                                     
REVDAT   1   29-JUN-11 3RZY    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.    1.08 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) : 1.08                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 50942                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.154                           
REMARK   3   R VALUE            (WORKING SET) : 0.152                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2728                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.08                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2691                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 67.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2600                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 144                          
REMARK   3   BIN FREE R VALUE                    : 0.2960                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1073                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 147                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.24                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.66000                                              
REMARK   3    B22 (A**2) : -0.61000                                             
REMARK   3    B33 (A**2) : -1.04000                                             
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): 0.031         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.034         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.031         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.492         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.976                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.960                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1182 ; 0.025 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):   811 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1598 ; 2.172 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  1994 ; 1.188 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   158 ; 6.172 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    48 ;34.193 ;24.792       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   230 ;16.168 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;18.220 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   181 ; 0.130 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1350 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   235 ; 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):   749 ; 2.654 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   315 ; 1.002 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1218 ; 4.149 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   433 ; 5.844 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   380 ; 8.428 ; 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):  1993 ; 2.552 ; 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 WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3RZY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065586.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-APR-11                          
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                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.94312                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53794                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.080                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04900                            
REMARK 200   FOR THE DATA SET  : 11.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.08                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.13                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.43700                            
REMARK 200   FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
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       16.26250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.47550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.71150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.47550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.26250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.71150            
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   OE1  GLU A    14     O    HOH A   146              2.00            
REMARK 500   O    LEU A    86     O    HOH A   139              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   OD2  ASP A    71     O    HOH A   255     3555     1.51            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  22   CB    GLU A  22   CG     -0.124                       
REMARK 500    LYS A 107   CB    LYS A 107   CG     -0.193                       
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    SER A  55   N   -  CA  -  CB  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ARG A  78   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 110     -134.18     51.62                                   
REMARK 500    LYS A 120       87.98     14.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3P6C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P6D   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P6E   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P6F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P6G   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P6H   RELATED DB: PDB                                   
DBREF  3RZY A    0   131  UNP    P15090   FABP4_HUMAN      1    132             
SEQADV 3RZY GLN A   -7  UNP  P15090              EXPRESSION TAG                 
SEQADV 3RZY GLN A   -6  UNP  P15090              EXPRESSION TAG                 
SEQADV 3RZY MET A   -5  UNP  P15090              EXPRESSION TAG                 
SEQADV 3RZY GLY A   -4  UNP  P15090              EXPRESSION TAG                 
SEQADV 3RZY ARG A   -3  UNP  P15090              EXPRESSION TAG                 
SEQADV 3RZY GLY A   -2  UNP  P15090              EXPRESSION TAG                 
SEQADV 3RZY 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                          
FORMUL   2  HOH   *147(H2 O)                                                    
HELIX    1   1 VAL A    5  VAL A    5  1                                   1
HELIX    2   2 ASN A   15  GLY A   24  1                                  10
HELIX    3   3 GLY A   26  ALA A   36  1                                  11
SHEET    1   1 1 GLY A   6  GLU A  14  0
SHEET    2   2 1 ASN A  39  ASN A  45  0
SHEET    3   3 1 VAL A  48  GLU A  54  0
SHEET    4   4 1 THR A  60  PHE A  64  0
SHEET    5   5 1 PHE A  70  VAL A  73  0
SHEET    6   6 1 LYS A  79  ASP A  87  0
SHEET    7   7 1 VAL A  90  TRP A  97  0
SHEET    8   8 1 LYS A 100  GLU A 109  0
SHEET    9   9 1 LYS A 112  MET A 119  0
SHEET   10  10 1 VAL A 122  ARG A 130  0
CRYST1   32.525   53.423   74.951  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      0.030746  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018719  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013342        0.00000                         
ATOM      1  N   VAL A   5       6.379  11.299   1.378  1.00 12.11           N
ANISOU    1  N   VAL A   5     1444   1558   1598   -149    140    146       N
ATOM      2  CA  VAL A   5       4.942  11.548   1.295  1.00 12.70           C
ANISOU    2  CA  VAL A   5     1599   1521   1702   -230    122    104       C
ATOM      3  C   VAL A   5       4.206  10.266   1.000  1.00 12.61           C
ANISOU    3  C   VAL A   5     1327   1644   1820   -279    -37   -134       C
ATOM      4  O   VAL A   5       4.605   9.450   0.168  1.00 16.08           O
ANISOU    4  O   VAL A   5     1996   1922   2189   -454    376   -447       O
ATOM      5  CB  VAL A   5       4.673  12.604   0.245  1.00 13.97           C
ANISOU    5  CB  VAL A   5     1389   1695   2222    -87   -158    164       C
ATOM      6  CG1 VAL A   5       3.232  12.676  -0.179  1.00 18.31           C
ANISOU    6  CG1 VAL A   5     2225   2147   2585   -177   -230    395       C
ATOM      7  CG2 VAL A   5       5.171  13.996   0.792  1.00 15.83           C
ANISOU    7  CG2 VAL A   5     2092   1618   2302   -376   -385     39       C
ATOM      8  N   GLY A   6       3.098  10.098   1.688  1.00 12.81           N
ANISOU    8  N   GLY A   6     1636   1623   1606   -351     49   -162       N
ATOM      9  CA  GLY A   6       2.227   8.969   1.459  1.00 12.52           C
ANISOU    9  CA  GLY A   6      918   1891   1947   -385    -24   -190       C
ATOM     10  C   GLY A   6       1.613   8.471   2.711  1.00 11.96           C
ANISOU   10  C   GLY A   6     1296   1711   1535   -264   -159    -99       C
ATOM     11  O   GLY A   6       1.607   9.132   3.720  1.00 12.96           O
ANISOU   11  O   GLY A   6     1563   1599   1761   -276    150   -121       O
ATOM     12  N   THR A   7       1.028   7.294   2.594  1.00 11.53           N
ANISOU   12  N   THR A   7      944   1752   1683   -165   -330    -51       N
ATOM     13  CA  THR A   7       0.379   6.634   3.671  1.00 12.90           C
ANISOU   13  CA  THR A   7     1382   1622   1898    -77   -116    -40       C
ATOM     14  C   THR A   7       1.117   5.384   3.996  1.00 12.66           C
ANISOU   14  C   THR A   7     1486   1505   1819   -103    -45    -14       C
ATOM     15  O   THR A   7       1.355   4.544   3.121  1.00 14.04           O
ANISOU   15  O   THR A   7     1642   1789   1902    124   -279   -153       O
ATOM     16  CB  THR A   7      -1.057   6.253   3.228  1.00 14.12           C
ANISOU   16  CB  THR A   7     1191   1637   2535    -60    -68    150       C
ATOM     17  OG1 THR A   7      -1.708   7.398   2.659  1.00 20.97           O
ANISOU   17  OG1 THR A   7     1574   2267   4126   -337   -609    414       O
ATOM     18  CG2 THR A   7      -1.881   5.733   4.406  1.00 19.15           C
ANISOU   18  CG2 THR A   7     1986   2402   2885   -588    187     23       C
ATOM     19  N   TRP A   8       1.486   5.252   5.257  1.00 11.57           N
ANISOU   19  N   TRP A   8     1214   1530   1651     36    143     -3       N
ATOM     20  CA  TRP A   8       2.393   4.219   5.731  1.00 11.55           C
ANISOU   20  CA  TRP A   8     1157   1543   1687     -2     41     53       C
ATOM     21  C   TRP A   8       1.722   3.461   6.858  1.00 12.23           C
ANISOU   21  C   TRP A   8     1448   1547   1652   -193    323     -3       C
ATOM     22  O   TRP A   8       0.910   4.018   7.608  1.00 16.07           O
ANISOU   22  O   TRP A   8     2366   1658   2080    -64    672     97       O
ATOM     23  CB  TRP A   8       3.654   4.904   6.271  1.00 11.18           C
ANISOU   23  CB  TRP A   8     1189   1537   1521      4     29    217       C
ATOM     24  CG  TRP A   8       4.358   5.710   5.256  1.00 11.25           C
ANISOU   24  CG  TRP A   8     1390   1501   1383    -48   -105     45       C
ATOM     25  CD1 TRP A   8       4.254   7.047   5.041  1.00 11.89           C
ANISOU   25  CD1 TRP A   8     1439   1516   1560   -109     52     49       C
ATOM     26  CD2 TRP A   8       5.324   5.223   4.331  1.00 10.44           C
ANISOU   26  CD2 TRP A   8      930   1437   1597     82     36     11       C
ATOM     27  NE1 TRP A   8       5.115   7.425   4.024  1.00 11.71           N
ANISOU   27  NE1 TRP A   8     1473   1279   1695   -152    116    104       N
ATOM     28  CE2 TRP A   8       5.766   6.323   3.562  1.00 10.33           C
ANISOU   28  CE2 TRP A   8      620   1673   1629   -179      4    -38       C
ATOM     29  CE3 TRP A   8       5.854   3.962   4.076  1.00 11.16           C
ANISOU   29  CE3 TRP A   8     1154   1595   1488    -53   -138   -154       C
ATOM     30  CZ2 TRP A   8       6.746   6.173   2.581  1.00 11.98           C
ANISOU   30  CZ2 TRP A   8     1001   1660   1889   -308    195     97       C
ATOM     31  CZ3 TRP A   8       6.802   3.817   3.094  1.00 11.43           C
ANISOU   31  CZ3 TRP A   8      894   1634   1813    154    -92   -217       C
ATOM     32  CH2 TRP A   8       7.193   4.905   2.351  1.00 12.23           C
ANISOU   32  CH2 TRP A   8      815   2044   1786   -135    254   -196       C
ATOM     33  N   LYS A   9       2.025   2.184   6.981  1.00 11.25           N
ANISOU   33  N   LYS A   9      983   1662   1627   -194     15    187       N
ATOM     34  CA  LYS A   9       1.442   1.315   8.030  1.00 12.94           C
ANISOU   34  CA  LYS A   9     1239   1878   1799   -190    -83    140       C
ATOM     35  C   LYS A   9       2.553   0.632   8.767  1.00 11.13           C
ANISOU   35  C   LYS A   9      682   1804   1740   -259    -99    117       C
ATOM     36  O   LYS A   9       3.491   0.156   8.176  1.00 11.76           O
ANISOU   36  O   LYS A   9     1190   1577   1701   -155     15    166       O
ATOM     37  CB  LYS A   9       0.465   0.289   7.440  1.00 14.61           C
ANISOU   37  CB  LYS A   9     1207   2218   2127   -332   -294    473       C
ATOM     38  CG  LYS A   9       0.992  -0.662   6.446  1.00 23.00           C
ANISOU   38  CG  LYS A   9     2633   3125   2981   -411    -40    290       C
ATOM     39  CD  LYS A   9      -0.028  -1.672   5.997  1.00 28.81           C
ANISOU   39  CD  LYS A   9     3402   3461   4083   -596   -190    -35       C
ATOM     40  CE  LYS A   9       0.604  -2.625   5.026  1.00 31.40           C
ANISOU   40  CE  LYS A   9     3959   3859   4110   -389     52    -76       C
ATOM     41  NZ  LYS A   9       0.497  -2.153   3.594  1.00 35.42           N
ANISOU   41  NZ  LYS A   9     4644   3925   4887    152   -194    626       N
ATOM     42  N   LEU A  10       2.458   0.625  10.093  1.00 12.14           N
ANISOU   42  N   LEU A  10      959   1942   1710   -165    -51    184       N
ATOM     43  CA  LEU A  10       3.493  -0.019  10.918  1.00 11.39           C
ANISOU   43  CA  LEU A  10      256   2116   1953    -80     10    165       C
ATOM     44  C   LEU A  10       3.453  -1.505  10.679  1.00 13.02           C
ANISOU   44  C   LEU A  10      922   1975   2048   -268   -250    359       C
ATOM     45  O   LEU A  10       2.403  -2.132  10.857  1.00 15.99           O
ANISOU   45  O   LEU A  10     1105   2240   2728   -540   -279    463       O
ATOM     46  CB  LEU A  10       3.301   0.230  12.408  1.00 13.04           C
ANISOU   46  CB  LEU A  10      777   2234   1944    -98     28    169       C
ATOM     47  CG  LEU A  10       4.370  -0.303  13.326  1.00 13.75           C
ANISOU   47  CG  LEU A  10      930   2319   1974    -40   -156    247       C
ATOM     48  CD1 LEU A  10       5.594   0.446  13.181  1.00 15.21           C
ANISOU   48  CD1 LEU A  10     1121   2682   1973   -238   -240    298       C
ATOM     49  CD2 LEU A  10       3.888  -0.240  14.790  1.00 19.54           C
ANISOU   49  CD2 LEU A  10     1977   3826   1620    437    -38    330       C
ATOM     50  N   VAL A  11       4.616  -2.067  10.378  1.00 13.03           N
ANISOU   50  N   VAL A  11     1386   1403   2161   -395   -453    216       N
ATOM     51  CA  VAL A  11       4.782  -3.496  10.212  1.00 16.39           C
ANISOU   51  CA  VAL A  11     2198   1659   2368   -318   -760    138       C
ATOM     52  C   VAL A  11       5.677  -4.201  11.188  1.00 17.22           C
ANISOU   52  C   VAL A  11     2414   1742   2387   -216   -773    264       C
ATOM     53  O   VAL A  11       5.539  -5.421  11.334  1.00 21.12           O
ANISOU   53  O   VAL A  11     3098   1740   3184   -410  -1310    472       O
ATOM     54  CB  VAL A  11       5.214  -3.867   8.793  1.00 18.17           C
ANISOU   54  CB  VAL A  11     2446   1785   2671     38   -577      5       C
ATOM     55  CG1 VAL A  11       4.137  -3.482   7.798  1.00 21.56           C
ANISOU   55  CG1 VAL A  11     2862   2462   2866   -373   -902    139       C
ATOM     56  CG2 VAL A  11       6.628  -3.397   8.375  1.00 19.50           C
ANISOU   56  CG2 VAL A  11     2554   2319   2535      8   -110   -172       C
ATOM     57  N   SER A  12       6.596  -3.512  11.847  1.00 15.44           N
ANISOU   57  N   SER A  12     2178   1517   2171    -89   -730    122       N
ATOM     58  CA  SER A  12       7.450  -4.149  12.836  1.00 16.19           C
ANISOU   58  CA  SER A  12     2257   1675   2219    -60   -610    186       C
ATOM     59  C   SER A  12       7.975  -3.093  13.785  1.00 14.41           C
ANISOU   59  C   SER A  12     1721   1647   2107   -210   -512    181       C
ATOM     60  O   SER A  12       8.103  -1.921  13.446  1.00 12.55           O
ANISOU   60  O   SER A  12     1269   1529   1968   -240   -168    355       O
ATOM     61  CB  SER A  12       8.571  -4.907  12.195  1.00 19.50           C
ANISOU   61  CB  SER A  12     2690   2191   2526     23   -650    138       C
ATOM     62  OG  SER A  12       9.560  -4.114  11.649  1.00 21.77           O
ANISOU   62  OG  SER A  12     3068   2474   2730    334   -450    365       O
ATOM     63  N   SER A  13       8.284  -3.570  14.968  1.00 14.68           N
ANISOU   63  N   SER A  13     1890   1616   2070   -490   -480    298       N
ATOM     64  CA  SER A  13       8.802  -2.738  16.027  1.00 15.58           C
ANISOU   64  CA  SER A  13     2175   1718   2027   -414   -474    298       C
ATOM     65  C   SER A  13       9.759  -3.538  16.859  1.00 15.08           C
ANISOU   65  C   SER A  13     2022   1818   1888   -336   -484    384       C
ATOM     66  O   SER A  13       9.515  -4.727  17.172  1.00 18.26           O
ANISOU   66  O   SER A  13     2522   1793   2622   -572   -719    624       O
ATOM     67  CB  SER A  13       7.607  -2.227  16.852  1.00 17.57           C
ANISOU   67  CB  SER A  13     2494   2051   2129   -580   -495     52       C
ATOM     68  OG  SER A  13       7.970  -1.378  17.868  1.00 19.74           O
ANISOU   68  OG  SER A  13     3011   2255   2233   -241   -643    182       O
ATOM     69  N   GLU A  14      10.849  -2.925  17.241  1.00 13.15           N
ANISOU   69  N   GLU A  14     1705   1474   1816   -149   -501     91       N
ATOM     70  CA  GLU A  14      11.851  -3.540  18.119  1.00 14.05           C
ANISOU   70  CA  GLU A  14     1739   1521   2075     68   -333     41       C
ATOM     71  C   GLU A  14      12.217  -2.566  19.206  1.00 12.53           C
ANISOU   71  C   GLU A  14     1606   1350   1803    110   -210     74       C
ATOM     72  O   GLU A  14      12.516  -1.412  18.934  1.00 12.86           O
ANISOU   72  O   GLU A  14     1684   1414   1788     12   -262    116       O
ATOM     73  CB  GLU A  14      13.154  -3.934  17.356  1.00 16.70           C
ANISOU   73  CB  GLU A  14     1988   1987   2368    194   -239   -243       C
ATOM     74  CG  GLU A  14      12.959  -5.092  16.346  1.00 25.80           C
ANISOU   74  CG  GLU A  14     3493   2729   3578    -19   -153   -406       C
ATOM     75  CD  GLU A  14      12.831  -6.496  17.017  1.00 30.97           C
ANISOU   75  CD  GLU A  14     4520   2897   4348   -244   -225   -425       C
ATOM     76  OE1 GLU A  14      13.237  -6.685  18.188  1.00 36.18           O
ANISOU   76  OE1 GLU A  14     4823   3895   5027    110   -954   -385       O
ATOM     77  OE2 GLU A  14      12.308  -7.430  16.370  1.00 37.25           O
ANISOU   77  OE2 GLU A  14     5758   3428   4967   -478    171  -1231       O
ATOM     78  N  AASN A  15      12.348  -3.101  20.402  0.50 11.43           N
ANISOU   78  N  AASN A  15     1374   1226   1741      0   -178    153       N
ATOM     79  N  BASN A  15      12.062  -2.991  20.451  0.50 12.69           N
ANISOU   79  N  BASN A  15     1593   1433   1796   -172   -198    225       N
ATOM     80  CA AASN A  15      12.797  -2.348  21.564  0.50 10.51           C
ANISOU   80  CA AASN A  15      898   1433   1660    -12   -225    113       C
ATOM     81  CA BASN A  15      12.607  -2.304  21.640  0.50 13.44           C
ANISOU   81  CA BASN A  15     1681   1582   1842    -73   -163    150       C
ATOM     82  C  AASN A  15      11.946  -1.104  21.936  0.50  9.50           C
ANISOU   82  C  AASN A  15      361   1616   1632      0   -227    153       C
ATOM     83  C  BASN A  15      11.870  -1.091  22.043  0.50 11.97           C
ANISOU   83  C  BASN A  15     1201   1656   1690    -91   -125    248       C
ATOM     84  O  AASN A  15      12.417  -0.223  22.608  0.50 11.38           O
ANISOU   84  O  AASN A  15     1003   1578   1741   -152   -173    -82       O
ATOM     85  O  BASN A  15      12.324  -0.233  22.784  0.50 12.29           O
ANISOU   85  O  BASN A  15     1294   1626   1748    -28   -128    189       O
ATOM     86  CB AASN A  15      14.282  -2.002  21.428  0.50 10.67           C
ANISOU   86  CB AASN A  15      936   1366   1751    180   -230     53       C
ATOM     87  CB BASN A  15      14.067  -1.979  21.499  0.50 14.01           C
ANISOU   87  CB BASN A  15     1722   1650   1948    -34    -27    165       C
ATOM     88  CG AASN A  15      15.023  -2.043  22.739  0.50 10.32           C
ANISOU   88  CG AASN A  15      638   1654   1627    -71   -350    342       C
ATOM     89  CG BASN A  15      14.871  -3.172  21.329  0.50 18.50           C
ANISOU   89  CG BASN A  15     2426   2370   2232    412     70     67       C
ATOM     90  OD1AASN A  15      14.800  -2.965  23.551  0.50 12.17           O
ANISOU   90  OD1AASN A  15      785   1880   1957   -131   -550    250       O
ATOM     91  OD1BASN A  15      14.860  -4.037  22.177  0.50 21.45           O
ANISOU   91  OD1BASN A  15     3279   2005   2866    690    341    172       O
ATOM     92  ND2AASN A  15      15.870  -1.065  22.980  0.50 10.48           N
ANISOU   92  ND2AASN A  15      760   1620   1600     75    -86    141       N
ATOM     93  ND2BASN A  15      15.621  -3.243  20.256  0.50 21.18           N
ANISOU   93  ND2BASN A  15     2599   3122   2325    599    226    208       N
ATOM     94  N   PHE A  16      10.706  -1.023  21.514  1.00 11.12           N
ANISOU   94  N   PHE A  16      922   1492   1810     -4   -200      4       N
ATOM     95  CA  PHE A  16       9.815   0.153  21.754  1.00 11.45           C
ANISOU   95  CA  PHE A  16      603   1777   1967     27   -166    104       C
ATOM     96  C   PHE A  16       9.478   0.283  23.210  1.00 11.84           C
ANISOU   96  C   PHE A  16      982   1605   1911    138    -70    114       C
ATOM     97  O   PHE A  16       9.383   1.394  23.744  1.00 12.43           O
ANISOU   97  O   PHE A  16     1657   1315   1751   -210    -89     18       O
ATOM     98  CB  PHE A  16       8.641   0.141  20.827  1.00 12.75           C
ANISOU   98  CB  PHE A  16      949   1779   2114    259    -34   -104       C
ATOM     99  CG  PHE A  16       7.870   1.461  20.786  1.00 14.68           C
ANISOU   99  CG  PHE A  16     1670   2368   1541     40   -116   -191       C
ATOM    100  CD1 PHE A  16       8.470   2.628  20.480  1.00 14.47           C
ANISOU  100  CD1 PHE A  16      808   2275   2413    278   -220    -63       C
ATOM    101  CD2 PHE A  16       6.566   1.498  20.992  1.00 16.69           C
ANISOU  101  CD2 PHE A  16     2050   2386   1905    377   -242   -256       C
ATOM    102  CE1 PHE A  16       7.795   3.826  20.377  1.00 17.48           C
ANISOU  102  CE1 PHE A  16     1961   2306   2375    691   -507   -169       C
ATOM    103  CE2 PHE A  16       5.864   2.700  20.895  1.00 16.40           C
ANISOU  103  CE2 PHE A  16     1599   2660   1968    544    -85     35       C
ATOM    104  CZ  PHE A  16       6.496   3.848  20.629  1.00 17.21           C
ANISOU  104  CZ  PHE A  16     2168   2253   2115   1036   -377   -103       C
ATOM    105  N   ASP A  17       9.212  -0.829  23.885  1.00 12.98           N
ANISOU  105  N   ASP A  17     1472   1425   2034   -254     62     88       N
ATOM    106  CA  ASP A  17       8.880  -0.709  25.334  1.00 14.35           C
ANISOU  106  CA  ASP A  17     1709   1758   1982   -198     91    231       C
ATOM    107  C   ASP A  17      10.071  -0.135  26.136  1.00 12.58           C
ANISOU  107  C   ASP A  17      980   1863   1937   -243     10    458       C
ATOM    108  O   ASP A  17       9.868   0.751  26.951  1.00 14.02           O
ANISOU  108  O   ASP A  17     1928   1674   1725   -349    150    135       O
ATOM    109  CB  ASP A  17       8.448  -2.075  25.878  1.00 16.48           C
ANISOU  109  CB  ASP A  17     1819   2018   2425   -161    111    369       C
ATOM    110  CG  ASP A  17       7.882  -2.010  27.275  1.00 19.88           C
ANISOU  110  CG  ASP A  17     2569   2362   2622   -346    174    545       C
ATOM    111  OD1 ASP A  17       8.460  -2.637  28.165  1.00 26.47           O
ANISOU  111  OD1 ASP A  17     2907   4078   3070    274   -145    917       O
ATOM    112  OD2 ASP A  17       6.937  -1.291  27.526  1.00 22.04           O
ANISOU  112  OD2 ASP A  17     2918   2741   2713    139    747    437       O
ATOM    113  N   ASP A  18      11.271  -0.589  25.848  1.00 12.97           N
ANISOU  113  N   ASP A  18     1133   1866   1926    -43    -20    340       N
ATOM    114  CA  ASP A  18      12.466  -0.080  26.475  1.00 14.07           C
ANISOU  114  CA  ASP A  18     1542   1886   1915     60   -159    331       C
ATOM    115  C   ASP A  18      12.639   1.397  26.161  1.00 14.09           C
ANISOU  115  C   ASP A  18     1733   1768   1851    129     28    152       C
ATOM    116  O   ASP A  18      13.014   2.173  27.055  1.00 13.20           O
ANISOU  116  O   ASP A  18     1303   1839   1873      5   -294    170       O
ATOM    117  CB  ASP A  18      13.716  -0.892  26.128  1.00 16.75           C
ANISOU  117  CB  ASP A  18     1786   2252   2325    252    -88    263       C
ATOM    118  CG  ASP A  18      13.753  -2.248  26.857  1.00 25.08           C
ANISOU  118  CG  ASP A  18     2687   3248   3593    224     17    526       C
ATOM    119  OD1 ASP A  18      12.964  -2.495  27.766  1.00 31.89           O
ANISOU  119  OD1 ASP A  18     3489   4099   4525    146   -218   1519       O
ATOM    120  OD2 ASP A  18      14.695  -3.023  26.567  1.00 34.12           O
ANISOU  120  OD2 ASP A  18     3690   3848   5424    780    -99    344       O
ATOM    121  N   TYR A  19      12.388   1.808  24.922  1.00 12.02           N
ANISOU  121  N   TYR A  19     1390   1573   1602      2    -24     49       N
ATOM    122  CA  TYR A  19      12.498   3.236  24.581  1.00 10.86           C
ANISOU  122  CA  TYR A  19      834   1609   1682   -118    -65     95       C
ATOM    123  C   TYR A  19      11.478   4.036  25.381  1.00 10.49           C
ANISOU  123  C   TYR A  19      794   1691   1498    123    -32    224       C
ATOM    124  O   TYR A  19      11.825   5.054  25.981  1.00 11.43           O
ANISOU  124  O   TYR A  19     1279   1573   1488   -173    -89     39       O
ATOM    125  CB  TYR A  19      12.314   3.394  23.074  1.00 11.46           C
ANISOU  125  CB  TYR A  19      944   1849   1560   -180   -109      1       C
ATOM    126  CG  TYR A  19      12.048   4.873  22.665  1.00 10.68           C
ANISOU  126  CG  TYR A  19      772   1788   1496   -441    -38    -61       C
ATOM    127  CD1 TYR A  19      13.085   5.704  22.573  1.00 10.48           C
ANISOU  127  CD1 TYR A  19      258   1930   1792     11    -89    -91       C
ATOM    128  CD2 TYR A  19      10.832   5.338  22.425  1.00 11.53           C
ANISOU  128  CD2 TYR A  19      615   2081   1684   -365   -237    172       C
ATOM    129  CE1 TYR A  19      12.944   7.035  22.284  1.00 10.71           C
ANISOU  129  CE1 TYR A  19      650   1714   1702   -448     41    -12       C
ATOM    130  CE2 TYR A  19      10.640   6.670  22.110  1.00 12.43           C
ANISOU  130  CE2 TYR A  19      728   2184   1808   -158   -183    237       C
ATOM    131  CZ  TYR A  19      11.701   7.506  22.046  1.00 11.46           C
ANISOU  131  CZ  TYR A  19      962   1880   1511   -322   -104    -14       C
ATOM    132  OH  TYR A  19      11.495   8.860  21.725  1.00 13.37           O
ANISOU  132  OH  TYR A  19     1621   1665   1794    -55   -195    215       O
ATOM    133  N   MET A  20      10.250   3.582  25.426  1.00 10.30           N
ANISOU  133  N   MET A  20      778   1668   1467   -141     24     23       N
ATOM    134  CA  MET A  20       9.255   4.291  26.159  1.00 11.26           C
ANISOU  134  CA  MET A  20     1216   1591   1471    -94     52     78       C
ATOM    135  C   MET A  20       9.660   4.355  27.655  1.00 11.27           C
ANISOU  135  C   MET A  20     1007   1728   1546   -278     -8     82       C
ATOM    136  O   MET A  20       9.344   5.367  28.297  1.00 13.16           O
ANISOU  136  O   MET A  20     1737   1675   1585   -298   -151    -75       O
ATOM    137  CB  MET A  20       7.867   3.653  25.958  1.00 11.67           C
ANISOU  137  CB  MET A  20     1200   1915   1317   -156     66     51       C
ATOM    138  CG  MET A  20       7.283   3.911  24.613  1.00 12.38           C
ANISOU  138  CG  MET A  20     1245   1714   1743    108    119     90       C
ATOM    139  SD  MET A  20       5.535   3.414  24.515  1.00 14.72           S
ANISOU  139  SD  MET A  20     1201   2554   1838   -155     32     15       S
ATOM    140  CE  MET A  20       5.779   1.617  24.531  1.00 16.51           C
ANISOU  140  CE  MET A  20     1347   2520   2405   -486     23   -142       C
ATOM    141  N   LYS A  21      10.188   3.264  28.220  1.00 12.21           N
ANISOU  141  N   LYS A  21     1302   1784   1553   -260     80    137       N
ATOM    142  CA  LYS A  21      10.554   3.329  29.631  1.00 14.42           C
ANISOU  142  CA  LYS A  21     1628   2237   1611   -118     82    180       C
ATOM    143  C   LYS A  21      11.596   4.426  29.818  1.00 15.11           C
ANISOU  143  C   LYS A  21     1825   2282   1634   -208   -118     78       C
ATOM    144  O   LYS A  21      11.516   5.191  30.786  1.00 17.76           O
ANISOU  144  O   LYS A  21     2526   2546   1676   -355   -205    -20       O
ATOM    145  CB  LYS A  21      11.180   1.979  30.073  1.00 15.84           C
ANISOU  145  CB  LYS A  21     1732   2491   1792   -110    -64    262       C
ATOM    146  CG  LYS A  21      10.180   0.889  30.244  1.00 18.18           C
ANISOU  146  CG  LYS A  21     1785   2903   2220   -266    -30    425       C
ATOM    147  CD  LYS A  21      10.816  -0.351  30.866  1.00 20.41           C
ANISOU  147  CD  LYS A  21     1817   3004   2932    278   -109    646       C
ATOM    148  CE  LYS A  21       9.857  -1.374  31.196  1.00 26.64           C
ANISOU  148  CE  LYS A  21     2549   3680   3893    225   -276    712       C
ATOM    149  NZ  LYS A  21      10.432  -2.474  31.925  1.00 32.98           N
ANISOU  149  NZ  LYS A  21     2764   4664   5101    868   -674    961       N
ATOM    150  N   GLU A  22      12.591   4.508  28.903  1.00 14.62           N
ANISOU  150  N   GLU A  22     1516   2398   1638   -270   -279    124       N
ATOM    151  CA  GLU A  22      13.652   5.513  28.994  1.00 15.60           C
ANISOU  151  CA  GLU A  22     1531   2426   1970   -319   -386    -35       C
ATOM    152  C   GLU A  22      13.065   6.909  28.950  1.00 15.26           C
ANISOU  152  C   GLU A  22     1931   2214   1651   -656   -403    -36       C
ATOM    153  O   GLU A  22      13.540   7.813  29.641  1.00 18.05           O
ANISOU  153  O   GLU A  22     2215   2788   1854   -768   -300   -155       O
ATOM    154  CB  GLU A  22      14.782   5.177  27.972  1.00 15.11           C
ANISOU  154  CB  GLU A  22     1010   2584   2146    -80   -196    109       C
ATOM    155  CG  GLU A  22      16.088   5.582  28.238  1.00 19.18           C
ANISOU  155  CG  GLU A  22      690   3391   3207    450   -253   -202       C
ATOM    156  CD  GLU A  22      16.883   4.777  29.322  1.00 24.30           C
ANISOU  156  CD  GLU A  22      441   4724   4067   -128   -845    324       C
ATOM    157  OE1 GLU A  22      16.214   3.868  29.874  1.00 27.84           O
ANISOU  157  OE1 GLU A  22     2308   4734   3534   -600   -378    183       O
ATOM    158  OE2 GLU A  22      17.990   5.084  29.648  1.00 29.38           O
ANISOU  158  OE2 GLU A  22     1714   5223   4223    167  -1027   -124       O
ATOM    159  N   VAL A  23      12.059   7.118  28.100  1.00 14.16           N
ANISOU  159  N   VAL A  23     1812   1861   1707   -505   -135     36       N
ATOM    160  CA  VAL A  23      11.394   8.379  27.989  1.00 14.83           C
ANISOU  160  CA  VAL A  23     2149   1880   1606   -623    -47    -27       C
ATOM    161  C   VAL A  23      10.600   8.743  29.222  1.00 16.37           C
ANISOU  161  C   VAL A  23     2442   1968   1808   -536   -121    -86       C
ATOM    162  O   VAL A  23      10.406   9.908  29.495  1.00 20.26           O
ANISOU  162  O   VAL A  23     3600   1961   2136   -581    512   -164       O
ATOM    163  CB  VAL A  23      10.488   8.336  26.723  1.00 15.09           C
ANISOU  163  CB  VAL A  23     1893   2051   1790   -198     53      1       C
ATOM    164  CG1 VAL A  23       9.494   9.522  26.659  1.00 17.77           C
ANISOU  164  CG1 VAL A  23     2749   1965   2038    -73   -218    -56       C
ATOM    165  CG2 VAL A  23      11.331   8.309  25.463  1.00 17.28           C
ANISOU  165  CG2 VAL A  23     2632   2099   1831   -289    126     35       C
ATOM    166  N   GLY A  24      10.180   7.748  29.989  1.00 15.63           N
ANISOU  166  N   GLY A  24     2417   1940   1581   -432     -1    -89       N
ATOM    167  CA  GLY A  24       9.392   7.960  31.192  1.00 15.89           C
ANISOU  167  CA  GLY A  24     2157   2116   1765   -411     27   -133       C
ATOM    168  C   GLY A  24       7.912   7.662  31.085  1.00 14.91           C
ANISOU  168  C   GLY A  24     2156   1925   1582   -366     33   -165       C
ATOM    169  O   GLY A  24       7.117   8.032  31.953  1.00 16.74           O
ANISOU  169  O   GLY A  24     2214   2352   1794   -377    140   -274       O
ATOM    170  N   VAL A  25       7.491   6.936  30.074  1.00 13.35           N
ANISOU  170  N   VAL A  25     1751   1705   1615   -359     99    -36       N
ATOM    171  CA  VAL A  25       6.098   6.581  29.889  1.00 13.56           C
ANISOU  171  CA  VAL A  25     1871   1607   1671   -315     36    -23       C
ATOM    172  C   VAL A  25       5.711   5.514  30.940  1.00 13.65           C
ANISOU  172  C   VAL A  25     1834   1730   1620   -247    149    -47       C
ATOM    173  O   VAL A  25       6.441   4.569  31.173  1.00 14.96           O
ANISOU  173  O   VAL A  25     2150   1820   1715   -343    -54    197       O
ATOM    174  CB  VAL A  25       5.907   5.991  28.480  1.00 12.27           C
ANISOU  174  CB  VAL A  25     1326   1673   1663   -319     88     88       C
ATOM    175  CG1 VAL A  25       4.494   5.706  28.232  1.00 13.90           C
ANISOU  175  CG1 VAL A  25     1666   1915   1697   -329    -33     45       C
ATOM    176  CG2 VAL A  25       6.444   6.945  27.368  1.00 14.49           C
ANISOU  176  CG2 VAL A  25     2276   1601   1626   -304      3    327       C
ATOM    177  N   GLY A  26       4.550   5.735  31.545  1.00 15.59           N
ANISOU  177  N   GLY A  26     2133   2092   1695   -475     98      4       N
ATOM    178  CA  GLY A  26       4.015   4.847  32.553  1.00 15.64           C
ANISOU  178  CA  GLY A  26     2044   2368   1529   -429    168   -143       C
ATOM    179  C   GLY A  26       3.574   3.510  32.015  1.00 14.73           C
ANISOU  179  C   GLY A  26     1878   2139   1577   -468    200     23       C
ATOM    180  O   GLY A  26       3.300   3.335  30.855  1.00 14.41           O
ANISOU  180  O   GLY A  26     1801   2234   1437   -606     34     45       O
ATOM    181  N   PHE A  27       3.363   2.594  32.930  1.00 14.51           N
ANISOU  181  N   PHE A  27     1842   2164   1506   -514   -110     36       N
ATOM    182  CA  PHE A  27       3.059   1.236  32.594  1.00 14.40           C
ANISOU  182  CA  PHE A  27     1683   2190   1596   -433     64     64       C
ATOM    183  C   PHE A  27       1.845   1.105  31.673  1.00 13.30           C
ANISOU  183  C   PHE A  27     1629   1802   1622   -353     16    228       C
ATOM    184  O   PHE A  27       1.948   0.473  30.632  1.00 13.94           O
ANISOU  184  O   PHE A  27     1852   1934   1508   -456    -22    142       O
ATOM    185  CB  PHE A  27       2.799   0.427  33.894  1.00 15.05           C
ANISOU  185  CB  PHE A  27     1678   2352   1688   -366   -110    209       C
ATOM    186  CG  PHE A  27       2.426  -1.019  33.627  1.00 14.54           C
ANISOU  186  CG  PHE A  27     1162   2650   1711   -520   -178    338       C
ATOM    187  CD1 PHE A  27       3.394  -2.012  33.505  1.00 18.43           C
ANISOU  187  CD1 PHE A  27     2514   2486   2001   -306    143    389       C
ATOM    188  CD2 PHE A  27       1.148  -1.372  33.525  1.00 16.28           C
ANISOU  188  CD2 PHE A  27     1611   2314   2257   -188   -338    770       C
ATOM    189  CE1 PHE A  27       3.015  -3.345  33.252  1.00 20.45           C
ANISOU  189  CE1 PHE A  27     2926   2611   2231   -204     88    582       C
ATOM    190  CE2 PHE A  27       0.769  -2.685  33.256  1.00 17.95           C
ANISOU  190  CE2 PHE A  27     2092   2557   2168   -577   -274    670       C
ATOM    191  CZ  PHE A  27       1.690  -3.655  33.114  1.00 21.26           C
ANISOU  191  CZ  PHE A  27     3084   2619   2372   -383   -398    219       C
ATOM    192  N   ALA A  28       0.684   1.636  32.067  1.00 14.58           N
ANISOU  192  N   ALA A  28     1816   2026   1696   -307     98     43       N
ATOM    193  CA  ALA A  28      -0.535   1.396  31.297  1.00 14.11           C
ANISOU  193  CA  ALA A  28     1463   1977   1920   -395    -78     85       C
ATOM    194  C   ALA A  28      -0.428   2.002  29.931  1.00 13.46           C
ANISOU  194  C   ALA A  28     1461   1708   1943   -300     -9     52       C
ATOM    195  O   ALA A  28      -0.883   1.400  28.944  1.00 14.50           O
ANISOU  195  O   ALA A  28     1291   2120   2095   -408   -217    141       O
ATOM    196  CB  ALA A  28      -1.775   1.874  32.044  1.00 15.54           C
ANISOU  196  CB  ALA A  28     1865   2046   1992   -113    280    134       C
ATOM    197  N   THR A  29       0.121   3.193  29.823  1.00 14.14           N
ANISOU  197  N   THR A  29     1786   1857   1727   -365   -161      0       N
ATOM    198  CA  THR A  29       0.347   3.809  28.558  1.00 13.75           C
ANISOU  198  CA  THR A  29     1615   1883   1725   -252   -149    195       C
ATOM    199  C   THR A  29       1.305   2.983  27.700  1.00 13.37           C
ANISOU  199  C   THR A  29     1555   1886   1636   -380   -103    132       C
ATOM    200  O   THR A  29       1.008   2.814  26.501  1.00 14.22           O
ANISOU  200  O   THR A  29     1769   2055   1577   -368   -159     38       O
ATOM    201  CB  THR A  29       0.797   5.264  28.713  1.00 15.39           C
ANISOU  201  CB  THR A  29     2079   1859   1907   -404   -225    152       C
ATOM    202  OG1 THR A  29      -0.175   6.009  29.442  1.00 19.70           O
ANISOU  202  OG1 THR A  29     2727   2182   2574   -136     86    114       O
ATOM    203  CG2 THR A  29       1.029   5.957  27.356  1.00 17.26           C
ANISOU  203  CG2 THR A  29     2248   2155   2155    -50   -332    312       C
ATOM    204  N   ARG A  30       2.393   2.489  28.254  1.00 13.52           N
ANISOU  204  N   ARG A  30     1777   1849   1508   -413   -327    198       N
ATOM    205  CA  ARG A  30       3.274   1.673  27.457  1.00 13.10           C
ANISOU  205  CA  ARG A  30     1525   2009   1441   -414    -78    146       C
ATOM    206  C   ARG A  30       2.600   0.463  26.880  1.00 14.13           C
ANISOU  206  C   ARG A  30     1732   2085   1552   -352   -178    184       C
ATOM    207  O   ARG A  30       2.881   0.080  25.767  1.00 13.63           O
ANISOU  207  O   ARG A  30     1471   2247   1459   -268    -29     96       O
ATOM    208  CB  ARG A  30       4.553   1.195  28.222  1.00 14.51           C
ANISOU  208  CB  ARG A  30     1785   2182   1546   -509   -215    243       C
ATOM    209  CG  ARG A  30       5.516   2.259  28.594  1.00 14.28           C
ANISOU  209  CG  ARG A  30     1707   2089   1629   -193     34    131       C
ATOM    210  CD  ARG A  30       6.849   1.671  28.908  1.00 13.72           C
ANISOU  210  CD  ARG A  30     1269   2226   1716    -58   -217    207       C
ATOM    211  NE  ARG A  30       6.801   0.497  29.796  1.00 13.77           N
ANISOU  211  NE  ARG A  30     1529   2022   1681   -175     15    127       N
ATOM    212  CZ  ARG A  30       6.631   0.562  31.113  1.00 14.81           C
ANISOU  212  CZ  ARG A  30     1670   2041   1917    -58    -15    147       C
ATOM    213  NH1 ARG A  30       6.525   1.706  31.762  1.00 16.20           N
ANISOU  213  NH1 ARG A  30     2584   1964   1607   -346    -11    418       N
ATOM    214  NH2 ARG A  30       6.624  -0.587  31.808  1.00 16.65           N
ANISOU  214  NH2 ARG A  30     2684   1927   1712   -108    249    197       N
ATOM    215  N   LYS A  31       1.796  -0.208  27.711  1.00 12.99           N
ANISOU  215  N   LYS A  31     1393   2053   1490   -415    -70     91       N
ATOM    216  CA  LYS A  31       1.134  -1.409  27.255  1.00 13.24           C
ANISOU  216  CA  LYS A  31     1430   1966   1634   -327      7     -1       C
ATOM    217  C   LYS A  31       0.231  -1.138  26.103  1.00 13.02           C
ANISOU  217  C   LYS A  31     1196   2066   1682   -238    101    -92       C
ATOM    218  O   LYS A  31       0.231  -1.848  25.102  1.00 14.52           O
ANISOU  218  O   LYS A  31     1392   2259   1865   -156    -72   -260       O
ATOM    219  CB  LYS A  31       0.448  -2.131  28.375  1.00 14.09           C
ANISOU  219  CB  LYS A  31     1232   2054   2066   -365     51     58       C
ATOM    220  CG  LYS A  31       1.392  -2.651  29.438  1.00 17.34           C
ANISOU  220  CG  LYS A  31     1934   2408   2246   -395    -68    146       C
ATOM    221  CD  LYS A  31       2.312  -3.727  28.902  1.00 25.32           C
ANISOU  221  CD  LYS A  31     3648   2894   3077    291    -96    297       C
ATOM    222  CE  LYS A  31       3.440  -4.115  29.881  1.00 29.03           C
ANISOU  222  CE  LYS A  31     3701   3851   3477    328    -74    -78       C
ATOM    223  NZ  LYS A  31       4.750  -4.307  29.186  1.00 34.49           N
ANISOU  223  NZ  LYS A  31     4191   4761   4152     17    140   -138       N
ATOM    224  N   VAL A  32      -0.628  -0.151  26.271  1.00 12.24           N
ANISOU  224  N   VAL A  32      952   2028   1670   -149      8   -115       N
ATOM    225  CA  VAL A  32      -1.580   0.151  25.190  1.00 13.25           C
ANISOU  225  CA  VAL A  32      873   2357   1802   -294     21   -242       C
ATOM    226  C   VAL A  32      -0.901   0.740  23.975  1.00 12.89           C
ANISOU  226  C   VAL A  32      926   2243   1726   -392      1    -87       C
ATOM    227  O   VAL A  32      -1.263   0.424  22.836  1.00 13.60           O
ANISOU  227  O   VAL A  32     1039   2409   1720   -266    -62   -168       O
ATOM    228  CB  VAL A  32      -2.736   1.045  25.759  1.00 15.08           C
ANISOU  228  CB  VAL A  32      980   2710   2038   -314   -143   -237       C
ATOM    229  CG1 VAL A  32      -3.670   1.557  24.669  1.00 18.82           C
ANISOU  229  CG1 VAL A  32     1397   3190   2561    285     96   -155       C
ATOM    230  CG2 VAL A  32      -3.481   0.298  26.860  1.00 17.31           C
ANISOU  230  CG2 VAL A  32      496   3309   2772   -121    468   -128       C
ATOM    231  N   ALA A  33       0.022   1.641  24.170  1.00 12.67           N
ANISOU  231  N   ALA A  33     1095   2064   1653   -177   -142      9       N
ATOM    232  CA  ALA A  33       0.779   2.232  23.065  1.00 14.03           C
ANISOU  232  CA  ALA A  33     1560   2192   1579   -340   -194    182       C
ATOM    233  C   ALA A  33       1.525   1.186  22.304  1.00 13.54           C
ANISOU  233  C   ALA A  33     1302   2256   1586   -298   -211    248       C
ATOM    234  O   ALA A  33       1.684   1.246  21.091  1.00 15.22           O
ANISOU  234  O   ALA A  33     1717   2450   1612   -200   -146    363       O
ATOM    235  CB  ALA A  33       1.662   3.351  23.541  1.00 15.79           C
ANISOU  235  CB  ALA A  33     1829   2284   1885   -533   -201    282       C
ATOM    236  N   GLY A  34       2.132   0.242  23.017  1.00 14.68           N
ANISOU  236  N   GLY A  34     1587   2471   1517     67    -35    213       N
ATOM    237  CA  GLY A  34       2.913  -0.775  22.368  1.00 15.02           C
ANISOU  237  CA  GLY A  34     1430   2536   1738    188    112    283       C
ATOM    238  C   GLY A  34       2.096  -1.722  21.495  1.00 15.73           C
ANISOU  238  C   GLY A  34     1884   2496   1594    226    338    239       C
ATOM    239  O   GLY A  34       2.675  -2.274  20.578  1.00 18.00           O
ANISOU  239  O   GLY A  34     1643   3151   2044    295    371   -132       O
ATOM    240  N   MET A  35       0.804  -1.900  21.753  1.00 15.26           N
ANISOU  240  N   MET A  35     1939   2131   1725     64    458    262       N
ATOM    241  CA  MET A  35      -0.069  -2.689  20.903  1.00 14.85           C
ANISOU  241  CA  MET A  35     1555   2039   2047     46    371    346       C
ATOM    242  C   MET A  35      -0.427  -2.008  19.588  1.00 13.73           C
ANISOU  242  C   MET A  35     1221   1909   2087    -85    428    310       C
ATOM    243  O   MET A  35      -0.779  -2.689  18.636  1.00 16.83           O
ANISOU  243  O   MET A  35     1797   2194   2403   -336   -165    395       O
ATOM    244  CB  MET A  35      -1.369  -2.997  21.634  1.00 16.63           C
ANISOU  244  CB  MET A  35     1850   2000   2466    -31    685    465       C
ATOM    245  CG  MET A  35      -1.246  -3.961  22.751  1.00 16.95           C
ANISOU  245  CG  MET A  35     2086   2117   2235    -58    658    111       C
ATOM    246  SD  MET A  35      -0.732  -5.580  22.285  1.00 16.25           S
ANISOU  246  SD  MET A  35     1938   1921   2313    117    280    326       S
ATOM    247  CE  MET A  35      -2.161  -6.080  21.420  1.00 23.73           C
ANISOU  247  CE  MET A  35     3877   2769   2368   -637   -984    509       C
ATOM    248  N   ALA A  36      -0.338  -0.699  19.530  1.00 13.55           N
ANISOU  248  N   ALA A  36     1196   1991   1959    -50    210    365       N
ATOM    249  CA  ALA A  36      -0.926   0.008  18.402  1.00 13.64           C
ANISOU  249  CA  ALA A  36      971   2216   1994   -114    158    447       C
ATOM    250  C   ALA A  36      -0.099  -0.269  17.107  1.00 12.99           C
ANISOU  250  C   ALA A  36      942   2031   1962   -390    -39    371       C
ATOM    251  O   ALA A  36       1.107  -0.468  17.136  1.00 13.54           O
ANISOU  251  O   ALA A  36      760   2449   1934   -246   -196    214       O
ATOM    252  CB  ALA A  36      -0.946   1.477  18.674  1.00 16.15           C
ANISOU  252  CB  ALA A  36     1654   2253   2229     72    304    282       C
ATOM    253  N   LYS A  37      -0.871  -0.273  16.035  1.00 14.06           N
ANISOU  253  N   LYS A  37     1096   2101   2145   -378    -41    403       N
ATOM    254  CA  LYS A  37      -0.296  -0.454  14.694  1.00 15.89           C
ANISOU  254  CA  LYS A  37     1896   2033   2107   -291     -1    120       C
ATOM    255  C   LYS A  37      -0.729   0.721  13.853  1.00 14.40           C
ANISOU  255  C   LYS A  37     1595   1992   1882   -380     13    240       C
ATOM    256  O   LYS A  37      -1.609   0.638  13.047  1.00 15.79           O
ANISOU  256  O   LYS A  37     1561   2306   2131   -373   -174    382       O
ATOM    257  CB  LYS A  37      -0.730  -1.789  14.064  1.00 18.40           C
ANISOU  257  CB  LYS A  37     2496   2084   2412   -294   -201    111       C
ATOM    258  CG  LYS A  37      -0.159  -3.020  14.775  1.00 22.51           C
ANISOU  258  CG  LYS A  37     2893   2498   3160   -422   -217     38       C
ATOM    259  CD  LYS A  37       1.346  -3.071  14.573  1.00 28.39           C
ANISOU  259  CD  LYS A  37     3558   3603   3625     80   -190    -26       C
ATOM    260  CE  LYS A  37       1.889  -4.428  14.100  1.00 34.48           C
ANISOU  260  CE  LYS A  37     4393   4145   4561      8     -5   -179       C
ATOM    261  NZ  LYS A  37       1.737  -4.590  12.554  1.00 35.89           N
ANISOU  261  NZ  LYS A  37     4821   4502   4313    -62    318    331       N
ATOM    262  N   PRO A  38      -0.114   1.873  14.055  1.00 13.62           N
ANISOU  262  N   PRO A  38     1519   1895   1760   -162    187    212       N
ATOM    263  CA  PRO A  38      -0.643   3.070  13.444  1.00 15.49           C
ANISOU  263  CA  PRO A  38     2145   1886   1854    -97    303    190       C
ATOM    264  C   PRO A  38      -0.413   3.125  11.954  1.00 14.79           C
ANISOU  264  C   PRO A  38     2147   1692   1778   -250    525     86       C
ATOM    265  O   PRO A  38       0.467   2.510  11.402  1.00 14.92           O
ANISOU  265  O   PRO A  38     1896   1881   1890   -145    531     72       O
ATOM    266  CB  PRO A  38       0.166   4.191  14.101  1.00 16.65           C
ANISOU  266  CB  PRO A  38     2362   1896   2067    -31    207     92       C
ATOM    267  CG  PRO A  38       1.333   3.522  14.636  1.00 18.79           C
ANISOU  267  CG  PRO A  38     2027   2350   2761   -552    -93     87       C
ATOM    268  CD  PRO A  38       0.969   2.145  14.985  1.00 15.73           C
ANISOU  268  CD  PRO A  38     2010   2091   1874   -233    220     -4       C
ATOM    269  N   ASN A  39      -1.242   3.941  11.345  1.00 14.44           N
ANISOU  269  N   ASN A  39     1866   1876   1741   -195    582    176       N
ATOM    270  CA  ASN A  39      -1.010   4.495  10.013  1.00 15.84           C
ANISOU  270  CA  ASN A  39     2301   1762   1955   -258    645     28       C
ATOM    271  C   ASN A  39      -0.437   5.857  10.164  1.00 17.18           C
ANISOU  271  C   ASN A  39     2932   1632   1962   -241    884    -96       C
ATOM    272  O   ASN A  39      -0.897   6.662  10.947  1.00 21.94           O
ANISOU  272  O   ASN A  39     3844   1862   2630   -517   1441   -194       O
ATOM    273  CB  ASN A  39      -2.232   4.542   9.169  1.00 19.42           C
ANISOU  273  CB  ASN A  39     2848   2143   2385     65    317     27       C
ATOM    274  CG  ASN A  39      -2.499   3.241   8.466  1.00 23.88           C
ANISOU  274  CG  ASN A  39     3125   2896   3051   -422   -128     49       C
ATOM    275  OD1 ASN A  39      -2.080   2.168   8.893  1.00 30.08           O
ANISOU  275  OD1 ASN A  39     4139   3301   3988   -431   -319   -119       O
ATOM    276  ND2 ASN A  39      -3.129   3.359   7.315  1.00 30.82           N
ANISOU  276  ND2 ASN A  39     2843   4939   3925    -99   -869    156       N
ATOM    277  N   MET A  40       0.564   6.147   9.374  1.00 16.00           N
ANISOU  277  N   MET A  40     2665   1590   1822   -220    619    -44       N
ATOM    278  CA  MET A  40       1.186   7.430   9.373  1.00 15.69           C
ANISOU  278  CA  MET A  40     2494   1582   1882   -191    543    -76       C
ATOM    279  C   MET A  40       1.010   8.053   7.998  1.00 15.11           C
ANISOU  279  C   MET A  40     2467   1547   1726    -78    459      6       C
ATOM    280  O   MET A  40       1.378   7.436   7.006  1.00 15.71           O
ANISOU  280  O   MET A  40     2607   1562   1799    187    493    134       O
ATOM    281  CB  MET A  40       2.649   7.273   9.657  1.00 17.57           C
ANISOU  281  CB  MET A  40     2812   1845   2018   -465    334     70       C
ATOM    282  CG  MET A  40       3.392   8.554   9.657  1.00 19.44           C
ANISOU  282  CG  MET A  40     2987   2075   2321   -500    266    -71       C
ATOM    283  SD  MET A  40       5.065   8.423  10.170  1.00 25.01           S
ANISOU  283  SD  MET A  40     3825   2304   3371   -613   -826    113       S
ATOM    284  CE  MET A  40       5.603   7.016   9.287  1.00 25.84           C
ANISOU  284  CE  MET A  40     2243   3592   3983   -360    362     50       C
ATOM    285  N   ILE A  41       0.481   9.261   7.935  1.00 13.24           N
ANISOU  285  N   ILE A  41     1807   1472   1751   -127    415    -17       N
ATOM    286  CA  ILE A  41       0.229   9.940   6.696  1.00 13.24           C
ANISOU  286  CA  ILE A  41     1577   1537   1915   -323    231   -104       C
ATOM    287  C   ILE A  41       1.115  11.169   6.684  1.00 11.97           C
ANISOU  287  C   ILE A  41     1518   1284   1745   -262     83    -42       C
ATOM    288  O   ILE A  41       1.016  12.006   7.573  1.00 13.71           O
ANISOU  288  O   ILE A  41     1956   1483   1768   -466    420    -80       O
ATOM    289  CB  ILE A  41      -1.263  10.371   6.532  1.00 15.94           C
ANISOU  289  CB  ILE A  41     1772   1847   2437   -349    193   -309       C
ATOM    290  CG1 ILE A  41      -2.230   9.194   6.702  1.00 20.39           C
ANISOU  290  CG1 ILE A  41     1643   2699   3404   -552    148   -392       C
ATOM    291  CG2 ILE A  41      -1.479  11.067   5.217  1.00 22.15           C
ANISOU  291  CG2 ILE A  41     2976   2443   2997   -247   -300   -142       C
ATOM    292  CD1 ILE A  41      -3.668   9.677   7.062  1.00 27.77           C
ANISOU  292  CD1 ILE A  41     1278   4197   5073   -893    617   -169       C
ATOM    293  N   ILE A  42       1.974  11.272   5.690  1.00 10.65           N
ANISOU  293  N   ILE A  42     1155   1391   1500   -136     14    -59       N
ATOM    294  CA  ILE A  42       2.931  12.383   5.540  1.00  9.65           C
ANISOU  294  CA  ILE A  42      778   1416   1471   -133     50     -2       C
ATOM    295  C   ILE A  42       2.550  13.119   4.285  1.00 10.42           C
ANISOU  295  C   ILE A  42      990   1456   1513   -259     28      5       C
ATOM    296  O   ILE A  42       2.409  12.519   3.231  1.00 12.13           O
ANISOU  296  O   ILE A  42     1692   1440   1474    -83    -90    -56       O
ATOM    297  CB  ILE A  42       4.325  11.874   5.494  1.00 10.75           C
ANISOU  297  CB  ILE A  42     1277   1464   1344   -145     84    -10       C
ATOM    298  CG1 ILE A  42       4.696  11.081   6.779  1.00 11.43           C
ANISOU  298  CG1 ILE A  42     1029   1631   1683    210    159    -47       C
ATOM    299  CG2 ILE A  42       5.289  13.055   5.274  1.00 11.07           C
ANISOU  299  CG2 ILE A  42      309   1894   2000    -90    164   -127       C
ATOM    300  CD1 ILE A  42       6.044  10.526   6.808  1.00 13.86           C
ANISOU  300  CD1 ILE A  42     1433   1989   1844    164    -99     62       C
ATOM    301  N   SER A  43       2.336  14.424   4.404  1.00 10.68           N
ANISOU  301  N   SER A  43     1232   1463   1360   -143   -106     36       N
ATOM    302  CA  SER A  43       2.007  15.251   3.288  1.00 11.53           C
ANISOU  302  CA  SER A  43     1302   1503   1574     27   -215     77       C
ATOM    303  C   SER A  43       2.759  16.557   3.362  1.00 11.60           C
ANISOU  303  C   SER A  43     1511   1397   1499     99   -114     16       C
ATOM    304  O   SER A  43       3.277  16.952   4.416  1.00 11.32           O
ANISOU  304  O   SER A  43     1631   1370   1300   -123    -28     57       O
ATOM    305  CB  SER A  43       0.548  15.489   3.249  1.00 14.48           C
ANISOU  305  CB  SER A  43     1436   1784   2280      4   -185    284       C
ATOM    306  OG  SER A  43       0.097  16.150   4.372  1.00 18.94           O
ANISOU  306  OG  SER A  43     2176   2509   2509    449   -261    172       O
ATOM    307  N   VAL A  44       2.870  17.205   2.220  1.00 12.01           N
ANISOU  307  N   VAL A  44     1825   1334   1403    -27   -293     67       N
ATOM    308  CA  VAL A  44       3.557  18.471   2.094  1.00 12.10           C
ANISOU  308  CA  VAL A  44     1552   1412   1632    -59   -357     94       C
ATOM    309  C   VAL A  44       2.686  19.447   1.329  1.00 13.18           C
ANISOU  309  C   VAL A  44     1797   1665   1546    -67   -355    180       C
ATOM    310  O   VAL A  44       2.089  19.074   0.323  1.00 17.17           O
ANISOU  310  O   VAL A  44     3168   1604   1750     64   -799     56       O
ATOM    311  CB  VAL A  44       4.881  18.316   1.436  1.00 14.04           C
ANISOU  311  CB  VAL A  44     1359   1793   2182     35     18    187       C
ATOM    312  CG1 VAL A  44       5.633  19.673   1.459  1.00 19.80           C
ANISOU  312  CG1 VAL A  44     2034   2014   3474   -296    114    251       C
ATOM    313  CG2 VAL A  44       5.818  17.351   2.180  1.00 18.12           C
ANISOU  313  CG2 VAL A  44     1910   2348   2623    -88   -346     17       C
ATOM    314  N   ASN A  45       2.610  20.666   1.774  1.00 11.86           N
ANISOU  314  N   ASN A  45     1450   1601   1454    -32   -281    105       N
ATOM    315  CA  ASN A  45       1.881  21.763   1.050  1.00 11.91           C
ANISOU  315  CA  ASN A  45     1256   1727   1540     34   -312    177       C
ATOM    316  C   ASN A  45       2.773  22.977   1.213  1.00 11.53           C
ANISOU  316  C   ASN A  45     1196   1633   1552    -36   -204    138       C
ATOM    317  O   ASN A  45       2.876  23.530   2.287  1.00 11.86           O
ANISOU  317  O   ASN A  45     1339   1626   1540    -22   -115    194       O
ATOM    318  CB  ASN A  45       0.530  21.901   1.644  1.00 12.09           C
ANISOU  318  CB  ASN A  45     1216   1655   1721   -120   -216     28       C
ATOM    319  CG  ASN A  45      -0.357  22.930   0.948  1.00 12.82           C
ANISOU  319  CG  ASN A  45     1495   1682   1692    185   -578     65       C
ATOM    320  OD1 ASN A  45      -1.627  22.738   0.866  1.00 14.87           O
ANISOU  320  OD1 ASN A  45     1648   2102   1898     -7   -426   -203       O
ATOM    321  ND2 ASN A  45       0.226  23.950   0.478  1.00 12.31           N
ANISOU  321  ND2 ASN A  45     1166   1508   2003     80   -470    340       N
ATOM    322  N   GLY A  46       3.446  23.326   0.136  1.00 14.23           N
ANISOU  322  N   GLY A  46     1963   1861   1581   -252   -267    211       N
ATOM    323  CA  GLY A  46       4.402  24.404   0.220  1.00 15.84           C
ANISOU  323  CA  GLY A  46     2128   2037   1852   -320    -88    301       C
ATOM    324  C   GLY A  46       5.502  24.068   1.163  1.00 14.30           C
ANISOU  324  C   GLY A  46     1621   2001   1809   -433     39    353       C
ATOM    325  O   GLY A  46       6.122  23.028   1.027  1.00 17.38           O
ANISOU  325  O   GLY A  46     2336   2091   2176   -177    235    146       O
ATOM    326  N   ASP A  47       5.774  24.921   2.131  1.00 14.68           N
ANISOU  326  N   ASP A  47     1776   1939   1861   -308     90    379       N
ATOM    327  CA  ASP A  47       6.817  24.658   3.148  1.00 14.17           C
ANISOU  327  CA  ASP A  47     1223   2129   2032    -81   -112    450       C
ATOM    328  C   ASP A  47       6.322  23.867   4.335  1.00 11.18           C
ANISOU  328  C   ASP A  47      639   1767   1839    -68   -131    216       C
ATOM    329  O   ASP A  47       7.135  23.591   5.210  1.00 13.38           O
ANISOU  329  O   ASP A  47      723   2299   2059      4    -28    249       O
ATOM    330  CB  ASP A  47       7.343  25.997   3.667  1.00 18.17           C
ANISOU  330  CB  ASP A  47     2276   2393   2234   -313   -263    482       C
ATOM    331  CG  ASP A  47       8.007  26.816   2.626  1.00 23.43           C
ANISOU  331  CG  ASP A  47     2491   3167   3243   -626   -282    331       C
ATOM    332  OD1 ASP A  47       8.519  26.271   1.630  1.00 29.60           O
ANISOU  332  OD1 ASP A  47     3180   4646   3418  -1110    959    714       O
ATOM    333  OD2 ASP A  47       7.983  28.058   2.792  1.00 33.81           O
ANISOU  333  OD2 ASP A  47     4692   3316   4836   -809   -175    544       O
ATOM    334  N   VAL A  48       5.062  23.600   4.378  1.00 10.37           N
ANISOU  334  N   VAL A  48      596   1708   1634     32   -251    179       N
ATOM    335  CA  VAL A  48       4.490  22.950   5.564  1.00 10.27           C
ANISOU  335  CA  VAL A  48      824   1548   1529    -48     21    148       C
ATOM    336  C   VAL A  48       4.367  21.467   5.355  1.00 10.03           C
ANISOU  336  C   VAL A  48      805   1613   1393    -73      8     17       C
ATOM    337  O   VAL A  48       3.699  20.993   4.441  1.00 11.48           O
ANISOU  337  O   VAL A  48     1279   1584   1499   -171   -312    125       O
ATOM    338  CB  VAL A  48       3.067  23.532   5.907  1.00 13.12           C
ANISOU  338  CB  VAL A  48     1556   1755   1673   -133     12    122       C
ATOM    339  CG1 VAL A  48       2.473  22.899   7.140  1.00 14.29           C
ANISOU  339  CG1 VAL A  48     1801   1816   1811     96    345    125       C
ATOM    340  CG2 VAL A  48       3.129  25.079   6.058  1.00 14.85           C
ANISOU  340  CG2 VAL A  48     1661   1719   2262    276    426     23       C
ATOM    341  N   ILE A  49       4.962  20.740   6.273  1.00  9.35           N
ANISOU  341  N   ILE A  49      773   1457   1319   -232    -40      7       N
ATOM    342  CA  ILE A  49       4.908  19.264   6.299  1.00  9.13           C
ANISOU  342  CA  ILE A  49      386   1670   1411   -218     14     10       C
ATOM    343  C   ILE A  49       3.926  18.871   7.381  1.00  9.15           C
ANISOU  343  C   ILE A  49      417   1657   1403    -38      0    123       C
ATOM    344  O   ILE A  49       3.938  19.478   8.478  1.00 10.04           O
ANISOU  344  O   ILE A  49      802   1553   1456   -193     72     -7       O
ATOM    345  CB  ILE A  49       6.262  18.678   6.585  1.00 10.28           C
ANISOU  345  CB  ILE A  49      294   1909   1701   -262     26    -94       C
ATOM    346  CG1 ILE A  49       7.346  19.111   5.612  1.00 11.42           C
ANISOU  346  CG1 ILE A  49      311   2112   1913   -324     93   -275       C
ATOM    347  CG2 ILE A  49       6.221  17.151   6.716  1.00 12.76           C
ANISOU  347  CG2 ILE A  49     1943   1285   1619      4   -247     44       C
ATOM    348  CD1 ILE A  49       8.668  18.898   6.021  1.00 15.42           C
ANISOU  348  CD1 ILE A  49      348   3171   2337   -484    198   -148       C
ATOM    349  N   THR A  50       3.020  17.957   7.093  1.00  9.20           N
ANISOU  349  N   THR A  50      277   1758   1461   -189     18     68       N
ATOM    350  CA  THR A  50       2.108  17.387   8.078  1.00  9.80           C
ANISOU  350  CA  THR A  50      647   1522   1553   -433    152    -74       C
ATOM    351  C   THR A  50       2.394  15.922   8.240  1.00 10.23           C
ANISOU  351  C   THR A  50      845   1527   1513   -237    147    -63       C
ATOM    352  O   THR A  50       2.539  15.159   7.258  1.00 11.77           O
ANISOU  352  O   THR A  50     1619   1439   1414   -318     57     12       O
ATOM    353  CB  THR A  50       0.682  17.638   7.690  1.00 11.08           C
ANISOU  353  CB  THR A  50      614   1734   1861   -463    146     19       C
ATOM    354  OG1 THR A  50       0.447  19.079   7.591  1.00 13.34           O
ANISOU  354  OG1 THR A  50      995   2114   1957    -41   -164     11       O
ATOM    355  CG2 THR A  50      -0.251  17.093   8.677  1.00 13.98           C
ANISOU  355  CG2 THR A  50      667   2192   2451   -286     90   -149       C
ATOM    356  N   ILE A  51       2.512  15.480   9.492  1.00  9.93           N
ANISOU  356  N   ILE A  51     1036   1306   1432   -218    149    -57       N
ATOM    357  CA  ILE A  51       2.626  14.031   9.856  1.00  9.56           C
ANISOU  357  CA  ILE A  51      387   1527   1715   -175    179    -75       C
ATOM    358  C   ILE A  51       1.441  13.711  10.763  1.00 10.48           C
ANISOU  358  C   ILE A  51      398   1723   1858      7    -82    -69       C
ATOM    359  O   ILE A  51       1.307  14.265  11.858  1.00 12.16           O
ANISOU  359  O   ILE A  51     1533   1499   1587   -130    204    -81       O
ATOM    360  CB  ILE A  51       3.893  13.731  10.504  1.00 10.28           C
ANISOU  360  CB  ILE A  51      288   1769   1847    -47    231    -30       C
ATOM    361  CG1 ILE A  51       5.144  14.077   9.645  1.00 12.83           C
ANISOU  361  CG1 ILE A  51     1338   1496   2040    -96     63   -315       C
ATOM    362  CG2 ILE A  51       3.965  12.216  10.855  1.00 12.94           C
ANISOU  362  CG2 ILE A  51     1326   1565   2023    -72     -2    204       C
ATOM    363  CD1 ILE A  51       6.474  13.787  10.290  1.00 14.53           C
ANISOU  363  CD1 ILE A  51      814   2183   2522    128    -74   -173       C
ATOM    364  N   LYS A  52       0.519  12.902  10.269  1.00 11.88           N
ANISOU  364  N   LYS A  52     1143   1777   1591   -171    337     21       N
ATOM    365  CA  LYS A  52      -0.629  12.406  11.033  1.00 14.14           C
ANISOU  365  CA  LYS A  52     1857   1604   1909   -240    497   -135       C
ATOM    366  C   LYS A  52      -0.357  10.939  11.379  1.00 15.63           C
ANISOU  366  C   LYS A  52     2252   1627   2060   -407    593   -246       C
ATOM    367  O   LYS A  52       0.055  10.167  10.559  1.00 18.38           O
ANISOU  367  O   LYS A  52     3297   1526   2159   -379   1072    -71       O
ATOM    368  CB  LYS A  52      -1.864  12.568  10.152  1.00 17.35           C
ANISOU  368  CB  LYS A  52     1925   2309   2358   -356    382   -238       C
ATOM    369  CG  LYS A  52      -3.166  12.341  10.701  1.00 24.19           C
ANISOU  369  CG  LYS A  52     2928   3147   3116   -174    256    340       C
ATOM    370  CD  LYS A  52      -4.197  12.802   9.665  1.00 27.77           C
ANISOU  370  CD  LYS A  52     2444   4149   3956    123   -573    294       C
ATOM    371  CE  LYS A  52      -5.602  13.036  10.342  1.00 31.75           C
ANISOU  371  CE  LYS A  52     2862   4591   4608    440   -375    276       C
ATOM    372  NZ  LYS A  52      -6.849  13.285   9.473  1.00 34.11           N
ANISOU  372  NZ  LYS A  52     1706   5584   5668    132   -472    236       N
ATOM    373  N   SER A  53      -0.716  10.575  12.595  1.00 14.74           N
ANISOU  373  N   SER A  53     2034   1565   2001   -389    744   -163       N
ATOM    374  CA  SER A  53      -0.677   9.208  13.031  1.00 15.90           C
ANISOU  374  CA  SER A  53     2053   1795   2191   -500    809    -37       C
ATOM    375  C   SER A  53      -2.078   8.844  13.476  1.00 15.98           C
ANISOU  375  C   SER A  53     2108   1858   2105   -427    842   -212       C
ATOM    376  O   SER A  53      -2.675   9.502  14.325  1.00 19.24           O
ANISOU  376  O   SER A  53     2866   1952   2490   -717   1203   -285       O
ATOM    377  CB  SER A  53       0.273   9.036  14.172  1.00 17.74           C
ANISOU  377  CB  SER A  53     2306   1885   2547   -207    674     65       C
ATOM    378  OG  SER A  53       0.345   7.658  14.622  1.00 24.19           O
ANISOU  378  OG  SER A  53     3775   2463   2951   -194    430    240       O
ATOM    379  N   GLU A  54      -2.596   7.817  12.880  1.00 16.04           N
ANISOU  379  N   GLU A  54     2028   1945   2119   -598    837   -166       N
ATOM    380  CA  GLU A  54      -3.964   7.322  13.211  1.00 17.42           C
ANISOU  380  CA  GLU A  54     2145   2137   2334   -369    672   -107       C
ATOM    381  C   GLU A  54      -3.792   5.935  13.836  1.00 15.25           C
ANISOU  381  C   GLU A  54     1763   1946   2084   -479    462    -34       C
ATOM    382  O   GLU A  54      -3.231   5.045  13.213  1.00 15.00           O
ANISOU  382  O   GLU A  54     1932   1849   1917   -163    459    180       O
ATOM    383  CB  GLU A  54      -4.783   7.215  11.926  1.00 20.95           C
ANISOU  383  CB  GLU A  54     2586   2546   2827   -276    523    147       C
ATOM    384  CG  GLU A  54      -5.025   8.516  11.171  1.00 27.57           C
ANISOU  384  CG  GLU A  54     3497   3478   3497   -194    331    297       C
ATOM    385  CD  GLU A  54      -5.974   8.283  10.016  1.00 35.22           C
ANISOU  385  CD  GLU A  54     4184   4875   4322    125    -66    165       C
ATOM    386  OE1 GLU A  54      -5.685   7.398   9.147  1.00 35.72           O
ANISOU  386  OE1 GLU A  54     4341   5170   4058    -57   -288   -142       O
ATOM    387  OE2 GLU A  54      -7.015   8.982   9.981  1.00 42.05           O
ANISOU  387  OE2 GLU A  54     4787   5532   5658    658    438    152       O
ATOM    388  N   SER A  55      -4.259   5.732  15.064  1.00 15.58           N
ANISOU  388  N   SER A  55     1322   2455   2141   -273    573   -118       N
ATOM    389  CA  SER A  55      -4.204   4.393  15.695  1.00 16.83           C
ANISOU  389  CA  SER A  55     1602   2600   2193    168    355    206       C
ATOM    390  C   SER A  55      -5.309   4.256  16.666  1.00 16.08           C
ANISOU  390  C   SER A  55     1594   2416   2099      3    457     90       C
ATOM    391  O   SER A  55      -5.985   5.195  17.037  1.00 16.92           O
ANISOU  391  O   SER A  55     1907   2026   2496    216    665    440       O
ATOM    392  CB  SER A  55      -2.888   3.916  16.392  1.00 18.81           C
ANISOU  392  CB  SER A  55     2051   2543   2551     21    359    223       C
ATOM    393  OG  SER A  55      -2.693   4.472  17.668  1.00 17.25           O
ANISOU  393  OG  SER A  55     1484   2955   2116     43     82    566       O
ATOM    394  N   THR A  56      -5.409   3.057  17.137  1.00 16.75           N
ANISOU  394  N   THR A  56     1920   2152   2292    245    131     74       N
ATOM    395  CA  THR A  56      -6.383   2.766  18.155  1.00 17.51           C
ANISOU  395  CA  THR A  56     2550   1973   2130   -235    213    171       C
ATOM    396  C   THR A  56      -5.944   3.303  19.503  1.00 17.94           C
ANISOU  396  C   THR A  56     2666   2045   2104   -459    453    179       C
ATOM    397  O   THR A  56      -6.773   3.423  20.382  1.00 22.76           O
ANISOU  397  O   THR A  56     3271   3151   2225   -877    972     60       O
ATOM    398  CB  THR A  56      -6.538   1.214  18.314  1.00 19.92           C
ANISOU  398  CB  THR A  56     2846   1970   2751   -206     59    -54       C
ATOM    399  OG1 THR A  56      -5.225   0.639  18.466  1.00 26.36           O
ANISOU  399  OG1 THR A  56     4423   2225   3368    572  -1359   -263       O
ATOM    400  CG2 THR A  56      -7.196   0.629  17.088  1.00 21.06           C
ANISOU  400  CG2 THR A  56     3209   2187   2603    -99   -585   -129       C
ATOM    401  N   PHE A  57      -4.685   3.654  19.670  1.00 17.48           N
ANISOU  401  N   PHE A  57     2755   2049   1834   -238    342    238       N
ATOM    402  CA  PHE A  57      -4.240   4.252  20.917  1.00 18.10           C
ANISOU  402  CA  PHE A  57     2766   2061   2050   -251    419    256       C
ATOM    403  C   PHE A  57      -4.535   5.741  20.947  1.00 18.33           C
ANISOU  403  C   PHE A  57     2551   2090   2323   -174    585    252       C
ATOM    404  O   PHE A  57      -5.218   6.213  21.805  1.00 20.80           O
ANISOU  404  O   PHE A  57     3040   2165   2695   -171    969    142       O
ATOM    405  CB  PHE A  57      -2.746   3.935  21.120  1.00 19.31           C
ANISOU  405  CB  PHE A  57     2995   2296   2043    -80    306    316       C
ATOM    406  CG  PHE A  57      -2.057   4.763  22.158  1.00 22.51           C
ANISOU  406  CG  PHE A  57     3329   2401   2821    -77     21    529       C
ATOM    407  CD1 PHE A  57      -2.496   4.777  23.446  1.00 23.27           C
ANISOU  407  CD1 PHE A  57     3552   2532   2756   -161    130    -86       C
ATOM    408  CD2 PHE A  57      -0.956   5.534  21.829  1.00 22.95           C
ANISOU  408  CD2 PHE A  57     3094   2533   3093    137    -55    356       C
ATOM    409  CE1 PHE A  57      -1.869   5.576  24.409  1.00 23.71           C
ANISOU  409  CE1 PHE A  57     2986   3003   3018   -199   -256     99       C
ATOM    410  CE2 PHE A  57      -0.321   6.308  22.786  1.00 25.49           C
ANISOU  410  CE2 PHE A  57     3522   2751   3411     30   -109    453       C
ATOM    411  CZ  PHE A  57      -0.796   6.326  24.053  1.00 23.49           C
ANISOU  411  CZ  PHE A  57     2904   2866   3154    210   -288    -27       C
ATOM    412  N  ALYS A  58      -3.909   6.504  20.062  0.50 17.94           N
ANISOU  412  N  ALYS A  58     2448   1969   2396     -6    750    306       N
ATOM    413  N  BLYS A  58      -4.067   6.510  19.967  0.50 18.93           N
ANISOU  413  N  BLYS A  58     2474   2150   2568    -77    750    309       N
ATOM    414  CA ALYS A  58      -4.187   7.905  19.954  0.50 17.88           C
ANISOU  414  CA ALYS A  58     2254   1941   2598    -49    625    175       C
ATOM    415  CA BLYS A  58      -4.084   7.966  20.089  0.50 19.33           C
ANISOU  415  CA BLYS A  58     2369   2199   2774   -112    596    187       C
ATOM    416  C  ALYS A  58      -4.041   8.290  18.473  0.50 16.97           C
ANISOU  416  C  ALYS A  58     1983   1836   2627   -187    778    178       C
ATOM    417  C  BLYS A  58      -3.747   8.641  18.782  0.50 17.71           C
ANISOU  417  C  BLYS A  58     1990   1986   2753   -209    881    229       C
ATOM    418  O  ALYS A  58      -3.442   7.626  17.625  0.50 16.60           O
ANISOU  418  O  ALYS A  58     2005   1588   2713   -108    828    220       O
ATOM    419  O  BLYS A  58      -2.565   8.578  18.406  0.50 15.93           O
ANISOU  419  O  BLYS A  58     1424   1773   2854      4    977    133       O
ATOM    420  CB ALYS A  58      -3.231   8.673  20.899  0.50 18.83           C
ANISOU  420  CB ALYS A  58     2133   2005   3015    -45    499    137       C
ATOM    421  CB BLYS A  58      -2.974   8.372  21.061  0.50 21.59           C
ANISOU  421  CB BLYS A  58     2557   2389   3257   -202    407    227       C
ATOM    422  CG ALYS A  58      -3.461  10.147  21.142  0.50 21.21           C
ANISOU  422  CG ALYS A  58     2778   2377   2904    -71    108    -59       C
ATOM    423  CG BLYS A  58      -3.415   9.049  22.291  0.50 24.48           C
ANISOU  423  CG BLYS A  58     2801   2987   3511   -361    173      9       C
ATOM    424  CD ALYS A  58      -4.657  10.448  22.013  0.50 23.66           C
ANISOU  424  CD ALYS A  58     2681   2975   3334   -227    -11   -159       C
ATOM    425  CD BLYS A  58      -3.639  10.532  21.975  0.50 27.30           C
ANISOU  425  CD BLYS A  58     3316   3393   3660    -57     94    138       C
ATOM    426  CE ALYS A  58      -4.988  11.945  21.939  0.50 25.87           C
ANISOU  426  CE ALYS A  58     3057   3143   3630     48    -13   -210       C
ATOM    427  CE BLYS A  58      -4.346  11.280  23.107  0.50 29.86           C
ANISOU  427  CE BLYS A  58     3776   3553   4016    -36     54    -88       C
ATOM    428  NZ ALYS A  58      -6.456  12.284  22.077  0.50 28.07           N
ANISOU  428  NZ ALYS A  58     3227   3295   4143    334     -5   -149       N
ATOM    429  NZ BLYS A  58      -4.653  12.683  22.701  0.50 31.45           N
ANISOU  429  NZ BLYS A  58     3824   3526   4596   -300    124   -115       N
ATOM    430  N   ASN A  59      -4.719   9.336  18.151  1.00 15.87           N
ANISOU  430  N   ASN A  59     1680   1824   2525   -163    918     78       N
ATOM    431  CA  ASN A  59      -4.512  10.027  16.886  1.00 15.04           C
ANISOU  431  CA  ASN A  59     1174   1946   2593   -456    795    -28       C
ATOM    432  C   ASN A  59      -3.732  11.266  17.226  1.00 16.55           C
ANISOU  432  C   ASN A  59     2141   1949   2198   -383    741   -118       C
ATOM    433  O   ASN A  59      -4.061  11.993  18.169  1.00 20.32           O
ANISOU  433  O   ASN A  59     2826   2179   2716   -433   1239   -327       O
ATOM    434  CB  ASN A  59      -5.814  10.331  16.286  1.00 15.87           C
ANISOU  434  CB  ASN A  59      758   2350   2921   -317    515    135       C
ATOM    435  CG  ASN A  59      -6.655   9.109  16.008  1.00 19.81           C
ANISOU  435  CG  ASN A  59     1740   2904   2880   -440    350    -86       C
ATOM    436  OD1 ASN A  59      -6.154   8.136  15.466  1.00 17.92           O
ANISOU  436  OD1 ASN A  59     1315   2584   2907   -125    295     48       O
ATOM    437  ND2 ASN A  59      -7.956   9.142  16.386  1.00 25.48           N
ANISOU  437  ND2 ASN A  59     1834   4276   3570   -207    722    174       N
ATOM    438  N   THR A  60      -2.772  11.548  16.392  1.00 15.21           N
ANISOU  438  N   THR A  60     2020   1762   1994   -282    574    -86       N
ATOM    439  CA  THR A  60      -1.967  12.745  16.530  1.00 15.79           C
ANISOU  439  CA  THR A  60     2128   1924   1944   -247    420     -1       C
ATOM    440  C   THR A  60      -1.751  13.377  15.152  1.00 14.44           C
ANISOU  440  C   THR A  60     1905   1737   1842   -132    575    -22       C
ATOM    441  O   THR A  60      -1.825  12.715  14.136  1.00 13.68           O
ANISOU  441  O   THR A  60     1778   1563   1854   -169    460      2       O
ATOM    442  CB  THR A  60      -0.581  12.466  17.134  1.00 16.62           C
ANISOU  442  CB  THR A  60     2311   1978   2025    -65    232     30       C
ATOM    443  OG1 THR A  60       0.182  11.631  16.271  1.00 18.78           O
ANISOU  443  OG1 THR A  60     2059   2425   2650     95    153    275       O
ATOM    444  CG2 THR A  60      -0.670  11.890  18.528  1.00 21.58           C
ANISOU  444  CG2 THR A  60     2972   2684   2542    -57    134    477       C
ATOM    445  N   GLU A  61      -1.505  14.669  15.154  1.00 14.11           N
ANISOU  445  N   GLU A  61     1975   1620   1764   -251    604   -129       N
ATOM    446  CA  GLU A  61      -1.122  15.358  13.927  1.00 13.57           C
ANISOU  446  CA  GLU A  61     1681   1686   1789   -263    291   -102       C
ATOM    447  C   GLU A  61      -0.244  16.502  14.273  1.00 12.48           C
ANISOU  447  C   GLU A  61     1531   1500   1709   -163    235   -166       C
ATOM    448  O   GLU A  61      -0.573  17.279  15.179  1.00 14.50           O
ANISOU  448  O   GLU A  61     1515   1835   2156   -343    467   -209       O
ATOM    449  CB  GLU A  61      -2.394  15.881  13.253  1.00 16.23           C
ANISOU  449  CB  GLU A  61     1860   2069   2236   -295    194    -23       C
ATOM    450  CG  GLU A  61      -2.178  16.680  11.993  1.00 21.15           C
ANISOU  450  CG  GLU A  61     2307   2877   2849   -562    -78    286       C
ATOM    451  CD  GLU A  61      -3.512  17.246  11.441  1.00 28.90           C
ANISOU  451  CD  GLU A  61     2627   4015   4339   -655   -107    681       C
ATOM    452  OE1 GLU A  61      -3.465  18.376  10.884  1.00 35.98           O
ANISOU  452  OE1 GLU A  61     4100   4327   5244   -859    163   1194       O
ATOM    453  OE2 GLU A  61      -4.606  16.625  11.630  1.00 35.99           O
ANISOU  453  OE2 GLU A  61     3378   5011   5283  -1258   -323    638       O
ATOM    454  N   ILE A  62       0.863  16.621  13.542  1.00 11.39           N
ANISOU  454  N   ILE A  62     1419   1437   1470   -185    219   -150       N
ATOM    455  CA  ILE A  62       1.765  17.758  13.658  1.00 12.26           C
ANISOU  455  CA  ILE A  62     1739   1439   1477   -452     82   -210       C
ATOM    456  C   ILE A  62       1.916  18.399  12.278  1.00 11.51           C
ANISOU  456  C   ILE A  62     1472   1437   1462   -224    269     57       C
ATOM    457  O   ILE A  62       1.978  17.672  11.277  1.00 13.22           O
ANISOU  457  O   ILE A  62     2258   1324   1439   -262    199    -39       O
ATOM    458  CB  ILE A  62       3.120  17.410  14.316  1.00 12.22           C
ANISOU  458  CB  ILE A  62     1588   1643   1412   -449     -9    -20       C
ATOM    459  CG1 ILE A  62       3.879  16.364  13.541  1.00 13.93           C
ANISOU  459  CG1 ILE A  62     1803   1816   1671   -418   -369    111       C
ATOM    460  CG2 ILE A  62       2.856  16.966  15.763  1.00 17.05           C
ANISOU  460  CG2 ILE A  62     2661   2118   1699   -240     35    173       C
ATOM    461  CD1 ILE A  62       5.303  16.129  13.989  1.00 16.43           C
ANISOU  461  CD1 ILE A  62     1900   2280   2060   -164   -485     16       C
ATOM    462  N   SER A  63       2.009  19.696  12.246  1.00 10.11           N
ANISOU  462  N   SER A  63      961   1490   1389   -121    113   -101       N
ATOM    463  CA  SER A  63       2.341  20.457  11.051  1.00  9.60           C
ANISOU  463  CA  SER A  63      633   1591   1423    -76     10    -28       C
ATOM    464  C   SER A  63       3.494  21.380  11.411  1.00  9.51           C
ANISOU  464  C   SER A  63      708   1358   1547     19     16      3       C
ATOM    465  O   SER A  63       3.496  21.986  12.469  1.00 11.24           O
ANISOU  465  O   SER A  63     1067   1515   1686   -281    268   -231       O
ATOM    466  CB  SER A  63       1.178  21.238  10.481  1.00 11.53           C
ANISOU  466  CB  SER A  63      955   1810   1616    -52    -87      1       C
ATOM    467  OG  SER A  63       0.174  20.371  10.026  1.00 13.78           O
ANISOU  467  OG  SER A  63     1019   2084   2130     70   -294   -168       O
ATOM    468  N   PHE A  64       4.458  21.508  10.522  1.00  9.41           N
ANISOU  468  N   PHE A  64      825   1429   1318    -34     36      7       N
ATOM    469  CA  PHE A  64       5.690  22.217  10.844  1.00  8.59           C
ANISOU  469  CA  PHE A  64      445   1343   1477   -109    -63    -28       C
ATOM    470  C   PHE A  64       6.355  22.644   9.565  1.00  9.52           C
ANISOU  470  C   PHE A  64      718   1398   1498     21    -50     83       C
ATOM    471  O   PHE A  64       6.122  22.110   8.486  1.00  9.19           O
ANISOU  471  O   PHE A  64      646   1445   1401   -134     21     39       O
ATOM    472  CB  PHE A  64       6.556  21.361  11.734  1.00  9.97           C
ANISOU  472  CB  PHE A  64      830   1505   1451   -287    -41     70       C
ATOM    473  CG  PHE A  64       6.928  20.059  11.105  1.00  9.72           C
ANISOU  473  CG  PHE A  64      313   1717   1663   -254   -170    117       C
ATOM    474  CD1 PHE A  64       6.099  18.952  11.246  1.00 10.33           C
ANISOU  474  CD1 PHE A  64      656   1730   1537   -108    -81     32       C
ATOM    475  CD2 PHE A  64       8.051  19.930  10.397  1.00  9.46           C
ANISOU  475  CD2 PHE A  64      259   1524   1811    -28    -93    148       C
ATOM    476  CE1 PHE A  64       6.438  17.759  10.626  1.00 12.38           C
ANISOU  476  CE1 PHE A  64     1420   1609   1674      9   -287     52       C
ATOM    477  CE2 PHE A  64       8.322  18.736   9.742  1.00 11.52           C
ANISOU  477  CE2 PHE A  64      907   1698   1772    210   -101    147       C
ATOM    478  CZ  PHE A  64       7.518  17.659   9.873  1.00 12.47           C
ANISOU  478  CZ  PHE A  64     1743   1512   1480     31   -194    -95       C
ATOM    479  N   ILE A  65       7.318  23.560   9.765  1.00  9.34           N
ANISOU  479  N   ILE A  65      485   1673   1388    -47    120   -100       N
ATOM    480  CA  ILE A  65       8.259  23.977   8.768  1.00  9.74           C
ANISOU  480  CA  ILE A  65      769   1380   1552     30    198    -53       C
ATOM    481  C   ILE A  65       9.628  23.541   9.224  1.00  8.95           C
ANISOU  481  C   ILE A  65      390   1381   1629     96    291    294       C
ATOM    482  O   ILE A  65       9.964  23.673  10.408  1.00  9.40           O
ANISOU  482  O   ILE A  65      767   1336   1467     33     19     54       O
ATOM    483  CB  ILE A  65       8.193  25.528   8.572  1.00 11.09           C
ANISOU  483  CB  ILE A  65     1181   1310   1720     15   -127     23       C
ATOM    484  CG1 ILE A  65       6.756  25.874   8.049  1.00 13.66           C
ANISOU  484  CG1 ILE A  65     1582   1504   2102   -159    -59    320       C
ATOM    485  CG2 ILE A  65       9.211  26.016   7.632  1.00 10.60           C
ANISOU  485  CG2 ILE A  65      515   1613   1900    -18     55    248       C
ATOM    486  CD1 ILE A  65       6.385  27.348   7.960  1.00 15.62           C
ANISOU  486  CD1 ILE A  65     1183   1786   2963    133   -250    220       C
ATOM    487  N   LEU A  66      10.455  22.996   8.341  1.00  8.70           N
ANISOU  487  N   LEU A  66      314   1492   1497   -239    124     62       N
ATOM    488  CA  LEU A  66      11.755  22.548   8.698  1.00  9.23           C
ANISOU  488  CA  LEU A  66      276   1591   1637    -72    153    173       C
ATOM    489  C   LEU A  66      12.563  23.631   9.350  1.00  9.48           C
ANISOU  489  C   LEU A  66      532   1442   1625   -132   -130    175       C
ATOM    490  O   LEU A  66      12.595  24.762   8.880  1.00 10.79           O
ANISOU  490  O   LEU A  66      641   1606   1850    -74     28    229       O
ATOM    491  CB  LEU A  66      12.489  21.981   7.454  1.00 10.83           C
ANISOU  491  CB  LEU A  66      723   1596   1793     83    241     50       C
ATOM    492  CG  LEU A  66      11.864  20.698   6.839  1.00 11.11           C
ANISOU  492  CG  LEU A  66      297   1900   2023    224    121   -232       C
ATOM    493  CD1 LEU A  66      12.644  20.503   5.484  1.00 17.28           C
ANISOU  493  CD1 LEU A  66     2122   2244   2198    546    447   -350       C
ATOM    494  CD2 LEU A  66      12.020  19.513   7.753  1.00 14.07           C
ANISOU  494  CD2 LEU A  66     1664   1582   2098     10      4    138       C
ATOM    495  N   GLY A  67      13.206  23.291  10.437  1.00 10.14           N
ANISOU  495  N   GLY A  67      791   1356   1706    -58     30    116       N
ATOM    496  CA  GLY A  67      14.066  24.184  11.186  1.00 10.36           C
ANISOU  496  CA  GLY A  67      671   1612   1651     19     89     68       C
ATOM    497  C   GLY A  67      13.371  25.109  12.150  1.00  9.51           C
ANISOU  497  C   GLY A  67      298   1514   1800   -187     39    143       C
ATOM    498  O   GLY A  67      14.102  25.853  12.848  1.00 11.51           O
ANISOU  498  O   GLY A  67      820   1604   1945   -223   -149    -42       O
ATOM    499  N   GLN A  68      12.084  25.075  12.204  1.00  9.12           N
ANISOU  499  N   GLN A  68      763   1170   1532   -243     10    -14       N
ATOM    500  CA  GLN A  68      11.294  26.061  12.958  1.00  9.94           C
ANISOU  500  CA  GLN A  68      731   1329   1715   -154    -33    -40       C
ATOM    501  C   GLN A  68      10.587  25.383  14.141  1.00  9.62           C
ANISOU  501  C   GLN A  68      370   1529   1756   -133    -76    -34       C
ATOM    502  O   GLN A  68       9.689  24.544  13.935  1.00  9.84           O
ANISOU  502  O   GLN A  68      535   1431   1770    -57     32    -64       O
ATOM    503  CB  GLN A  68      10.285  26.784  12.049  1.00  9.87           C
ANISOU  503  CB  GLN A  68      619   1321   1809    -20    -99    -37       C
ATOM    504  CG  GLN A  68      11.045  27.490  10.982  1.00 14.08           C
ANISOU  504  CG  GLN A  68     1777   1642   1931   -376   -527    177       C
ATOM    505  CD  GLN A  68      10.278  28.429  10.198  1.00 15.74           C
ANISOU  505  CD  GLN A  68     1680   1644   2652   -229   -541    300       C
ATOM    506  OE1 GLN A  68       9.093  28.745  10.440  1.00 20.04           O
ANISOU  506  OE1 GLN A  68     2006   2137   3470    261  -1144    242       O
ATOM    507  NE2 GLN A  68      11.046  28.998   9.202  1.00 18.02           N
ANISOU  507  NE2 GLN A  68     2535   1822   2489   -202   -567    593       N
ATOM    508  N  AGLU A  69      10.967  25.716  15.350  0.50  9.83           N
ANISOU  508  N  AGLU A  69      783   1214   1737   -191     70     -4       N
ATOM    509  N  BGLU A  69      10.994  25.732  15.357  0.50 10.33           N
ANISOU  509  N  BGLU A  69      790   1340   1795   -173     35     27       N
ATOM    510  CA AGLU A  69      10.487  24.970  16.510  0.50 10.43           C
ANISOU  510  CA AGLU A  69     1109   1277   1574   -168     27    -32       C
ATOM    511  CA BGLU A  69      10.495  25.137  16.620  0.50 11.74           C
ANISOU  511  CA BGLU A  69     1091   1564   1806    -82     25     31       C
ATOM    512  C  AGLU A  69       9.008  25.192  16.716  0.50 10.53           C
ANISOU  512  C  AGLU A  69     1213   1300   1486     14    156      7       C
ATOM    513  C  BGLU A  69       8.999  25.209  16.709  0.50 11.04           C
ANISOU  513  C  BGLU A  69     1190   1439   1562      8    142     52       C
ATOM    514  O  AGLU A  69       8.441  26.253  16.375  0.50 10.88           O
ANISOU  514  O  AGLU A  69     1081   1146   1905     70    -22     78       O
ATOM    515  O  BGLU A  69       8.418  26.244  16.345  0.50 10.98           O
ANISOU  515  O  BGLU A  69     1038   1202   1929     67    -53     76       O
ATOM    516  CB AGLU A  69      11.330  25.363  17.733  0.50 11.52           C
ANISOU  516  CB AGLU A  69     1334   1407   1634    -69      9     68       C
ATOM    517  CB BGLU A  69      11.041  25.942  17.839  0.50 13.04           C
ANISOU  517  CB BGLU A  69      977   2165   1809   -227   -116    281       C
ATOM    518  CG AGLU A  69      10.813  24.990  19.184  0.50 14.44           C
ANISOU  518  CG AGLU A  69     1842   1933   1712     32   -300     70       C
ATOM    519  CG BGLU A  69      10.630  27.393  17.833  0.50 18.44           C
ANISOU  519  CG BGLU A  69     1484   2710   2812   -158    -81   -134       C
ATOM    520  CD AGLU A  69      11.613  25.666  20.296  0.50 21.60           C
ANISOU  520  CD AGLU A  69     2356   3275   2575     88   -666    -44       C
ATOM    521  CD BGLU A  69      10.715  28.140  19.197  0.50 21.69           C
ANISOU  521  CD BGLU A  69     1466   3286   3486    463   -551   -137       C
ATOM    522  OE1AGLU A  69      11.475  26.878  20.515  0.50 27.77           O
ANISOU  522  OE1AGLU A  69     3750   3527   3275   -300   -727    -81       O
ATOM    523  OE1BGLU A  69       9.869  29.081  19.469  0.50 25.12           O
ANISOU  523  OE1BGLU A  69     2326   3405   3813    542    130   -433       O
ATOM    524  OE2AGLU A  69      12.410  24.976  20.919  0.50 24.81           O
ANISOU  524  OE2AGLU A  69      687   4833   3903    204  -1027   -146       O
ATOM    525  OE2BGLU A  69      11.643  27.785  19.958  0.50 24.07           O
ANISOU  525  OE2BGLU A  69     2238   3286   3620   -119  -1167    418       O
ATOM    526  N   PHE A  70       8.346  24.191  17.280  1.00  9.18           N
ANISOU  526  N   PHE A  70      741   1208   1540    196     94    -29       N
ATOM    527  CA  PHE A  70       6.970  24.189  17.547  1.00  9.47           C
ANISOU  527  CA  PHE A  70      688   1235   1673    219    263      0       C
ATOM    528  C   PHE A  70       6.679  23.396  18.829  1.00 11.06           C
ANISOU  528  C   PHE A  70     1209   1345   1646    248    310    -78       C
ATOM    529  O   PHE A  70       7.473  22.623  19.320  1.00 12.67           O
ANISOU  529  O   PHE A  70     1498   1706   1609    545    221    136       O
ATOM    530  CB  PHE A  70       6.149  23.632  16.352  1.00 10.95           C
ANISOU  530  CB  PHE A  70     1202   1368   1589     60    254     42       C
ATOM    531  CG  PHE A  70       6.494  22.221  15.991  1.00 10.34           C
ANISOU  531  CG  PHE A  70      535   1642   1751      7     54    179       C
ATOM    532  CD1 PHE A  70       7.585  21.902  15.205  1.00  9.61           C
ANISOU  532  CD1 PHE A  70      663   1397   1590     20      0      5       C
ATOM    533  CD2 PHE A  70       5.713  21.194  16.429  1.00 12.76           C
ANISOU  533  CD2 PHE A  70     1408   1466   1972     15    297    -67       C
ATOM    534  CE1 PHE A  70       7.906  20.604  14.864  1.00 10.76           C
ANISOU  534  CE1 PHE A  70     1085   1540   1462   -179    -11     -2       C
ATOM    535  CE2 PHE A  70       6.031  19.886  16.079  1.00 12.77           C
ANISOU  535  CE2 PHE A  70      912   1807   2133   -400    298     37       C
ATOM    536  CZ  PHE A  70       7.082  19.608  15.310  1.00 11.27           C
ANISOU  536  CZ  PHE A  70     1048   1556   1677     35    -20   -136       C
ATOM    537  N   ASP A  71       5.497  23.649  19.368  1.00 12.91           N
ANISOU  537  N   ASP A  71     1551   1446   1909    276    536    275       N
ATOM    538  CA  ASP A  71       4.918  22.880  20.503  1.00 15.38           C
ANISOU  538  CA  ASP A  71     2009   1859   1973    338    684     47       C
ATOM    539  C   ASP A  71       4.206  21.675  20.061  1.00 14.37           C
ANISOU  539  C   ASP A  71     1589   1960   1909    214    504    199       C
ATOM    540  O   ASP A  71       3.457  21.700  19.053  1.00 16.28           O
ANISOU  540  O   ASP A  71     1465   2238   2481    221    352    630       O
ATOM    541  CB  ASP A  71       3.801  23.713  21.192  1.00 16.76           C
ANISOU  541  CB  ASP A  71     1993   2207   2165    516    731     70       C
ATOM    542  CG  ASP A  71       4.289  24.934  21.745  1.00 19.92           C
ANISOU  542  CG  ASP A  71     2585   2713   2268    390     41     35       C
ATOM    543  OD1 ASP A  71       5.274  24.816  22.484  1.00 21.57           O
ANISOU  543  OD1 ASP A  71     2825   2963   2407    709   -292    109       O
ATOM    544  OD2 ASP A  71       3.666  26.031  21.527  1.00 21.12           O
ANISOU  544  OD2 ASP A  71     2473   2922   2630    619   -161   -198       O
ATOM    545  N   GLU A  72       4.443  20.581  20.766  1.00 13.72           N
ANISOU  545  N   GLU A  72     1399   1877   1934     83    304    370       N
ATOM    546  CA  GLU A  72       3.859  19.302  20.414  1.00 16.20           C
ANISOU  546  CA  GLU A  72     1915   2085   2155    -46    260    459       C
ATOM    547  C   GLU A  72       3.366  18.645  21.732  1.00 15.24           C
ANISOU  547  C   GLU A  72     1529   2112   2148    -39    381    473       C
ATOM    548  O   GLU A  72       4.047  18.705  22.728  1.00 18.04           O
ANISOU  548  O   GLU A  72     2019   2700   2133   -223    310    597       O
ATOM    549  CB  GLU A  72       4.893  18.400  19.675  1.00 16.12           C
ANISOU  549  CB  GLU A  72     2191   2024   1907    -76    334    298       C
ATOM    550  CG  GLU A  72       4.522  17.000  19.397  1.00 18.42           C
ANISOU  550  CG  GLU A  72     2478   2318   2201    -29    124    494       C
ATOM    551  CD  GLU A  72       5.531  16.155  18.680  1.00 19.96           C
ANISOU  551  CD  GLU A  72     3414   2232   1935    -96    448    348       C
ATOM    552  OE1 GLU A  72       6.714  16.551  18.606  1.00 19.20           O
ANISOU  552  OE1 GLU A  72     2949   1951   2393    -54    603     59       O
ATOM    553  OE2 GLU A  72       5.163  15.017  18.237  1.00 22.86           O
ANISOU  553  OE2 GLU A  72     3543   2446   2694     91    233    -14       O
ATOM    554  N   VAL A  73       2.181  18.094  21.713  1.00 15.73           N
ANISOU  554  N   VAL A  73     1586   2134   2255     67    269    634       N
ATOM    555  CA  VAL A  73       1.726  17.210  22.808  1.00 16.39           C
ANISOU  555  CA  VAL A  73     1592   2239   2394     38    424    432       C
ATOM    556  C   VAL A  73       1.818  15.822  22.216  1.00 16.13           C
ANISOU  556  C   VAL A  73     1839   2127   2160    -35    281    536       C
ATOM    557  O   VAL A  73       1.118  15.491  21.272  1.00 17.60           O
ANISOU  557  O   VAL A  73     1985   2258   2444    -52      6    575       O
ATOM    558  CB  VAL A  73       0.373  17.563  23.285  1.00 18.95           C
ANISOU  558  CB  VAL A  73     2059   2401   2740    190    646    387       C
ATOM    559  CG1 VAL A  73      -0.134  16.571  24.346  1.00 20.25           C
ANISOU  559  CG1 VAL A  73     1267   3221   3204    152    789    524       C
ATOM    560  CG2 VAL A  73       0.400  19.030  23.852  1.00 20.40           C
ANISOU  560  CG2 VAL A  73     1484   2696   3570    164    995    116       C
ATOM    561  N   THR A  74       2.688  14.999  22.748  1.00 15.35           N
ANISOU  561  N   THR A  74     1527   2119   2185    -25    228    459       N
ATOM    562  CA  THR A  74       3.000  13.687  22.173  1.00 16.76           C
ANISOU  562  CA  THR A  74     1956   2227   2185   -211    289    496       C
ATOM    563  C   THR A  74       1.879  12.685  22.510  1.00 17.14           C
ANISOU  563  C   THR A  74     1721   2345   2445    -62    194    526       C
ATOM    564  O   THR A  74       1.010  12.932  23.332  1.00 18.32           O
ANISOU  564  O   THR A  74     1908   2366   2683   -180    366    592       O
ATOM    565  CB  THR A  74       4.340  13.152  22.678  1.00 16.03           C
ANISOU  565  CB  THR A  74     1810   2334   1946    -89     58    384       C
ATOM    566  OG1 THR A  74       4.159  12.883  24.063  1.00 17.17           O
ANISOU  566  OG1 THR A  74     2030   2444   2049    101    227    333       O
ATOM    567  CG2 THR A  74       5.423  14.164  22.412  1.00 17.06           C
ANISOU  567  CG2 THR A  74     2044   2177   2260   -156    345    489       C
ATOM    568  N   ALA A  75       1.917  11.535  21.841  1.00 17.54           N
ANISOU  568  N   ALA A  75     1738   2259   2666   -315    159    419       N
ATOM    569  CA  ALA A  75       0.875  10.529  22.030  1.00 20.13           C
ANISOU  569  CA  ALA A  75     2236   2475   2938   -415    144    465       C
ATOM    570  C   ALA A  75       0.805  10.119  23.491  1.00 20.19           C
ANISOU  570  C   ALA A  75     2185   2472   3012   -715    151    629       C
ATOM    571  O   ALA A  75      -0.286   9.785  23.986  1.00 23.24           O
ANISOU  571  O   ALA A  75     2215   2950   3664   -751    290    647       O
ATOM    572  CB  ALA A  75       1.119   9.289  21.105  1.00 21.38           C
ANISOU  572  CB  ALA A  75     2453   2559   3109   -398    192    490       C
ATOM    573  N   ASP A  76       1.928  10.059  24.165  1.00 20.58           N
ANISOU  573  N   ASP A  76     2597   2526   2695   -320    255    645       N
ATOM    574  CA  ASP A  76       1.976   9.684  25.588  1.00 21.51           C
ANISOU  574  CA  ASP A  76     2883   2660   2627   -215    273    689       C
ATOM    575  C   ASP A  76       1.799  10.884  26.528  1.00 22.93           C
ANISOU  575  C   ASP A  76     3091   2944   2676   -155    551    639       C
ATOM    576  O   ASP A  76       2.034  10.785  27.730  1.00 26.28           O
ANISOU  576  O   ASP A  76     3719   3580   2685     60    446    589       O
ATOM    577  CB  ASP A  76       3.287   8.977  25.925  1.00 21.36           C
ANISOU  577  CB  ASP A  76     2808   2448   2858   -261    246    732       C
ATOM    578  CG  ASP A  76       4.506   9.834  25.609  1.00 20.41           C
ANISOU  578  CG  ASP A  76     2454   2493   2806    -50    -35    858       C
ATOM    579  OD1 ASP A  76       4.682  10.253  24.434  1.00 19.45           O
ANISOU  579  OD1 ASP A  76     1921   2661   2806     51     68    826       O
ATOM    580  OD2 ASP A  76       5.305  10.098  26.520  1.00 20.29           O
ANISOU  580  OD2 ASP A  76     2710   2209   2789   -180     74    675       O
ATOM    581  N   ASP A  77       1.344  12.005  25.988  1.00 22.44           N
ANISOU  581  N   ASP A  77     3051   2865   2610   -239    743    627       N
ATOM    582  CA  ASP A  77       0.994  13.196  26.741  1.00 23.58           C
ANISOU  582  CA  ASP A  77     2953   3249   2758   -157    813    447       C
ATOM    583  C   ASP A  77       2.121  14.032  27.343  1.00 23.25           C
ANISOU  583  C   ASP A  77     3118   3155   2562    -76    782    316       C
ATOM    584  O   ASP A  77       1.884  14.758  28.327  1.00 26.28           O
ANISOU  584  O   ASP A  77     3216   3753   3014   -112   1131     83       O
ATOM    585  CB  ASP A  77      -0.074  12.904  27.808  1.00 25.22           C
ANISOU  585  CB  ASP A  77     3095   3484   3003   -312    882    415       C
ATOM    586  CG  ASP A  77      -1.044  14.027  27.936  1.00 31.44           C
ANISOU  586  CG  ASP A  77     3527   4665   3751    -54   1058    458       C
ATOM    587  OD1 ASP A  77      -1.584  14.204  29.058  1.00 39.25           O
ANISOU  587  OD1 ASP A  77     4903   5940   4067   -339   1582    580       O
ATOM    588  OD2 ASP A  77      -1.271  14.760  26.930  1.00 39.60           O
ANISOU  588  OD2 ASP A  77     4542   5937   4567   -182   1088    933       O
ATOM    589  N   ARG A  78       3.320  13.987  26.759  1.00 19.75           N
ANISOU  589  N   ARG A  78     2783   2548   2173     46    779    411       N
ATOM    590  CA  ARG A  78       4.342  14.975  27.092  1.00 17.82           C
ANISOU  590  CA  ARG A  78     2557   2311   1903    195    553    329       C
ATOM    591  C   ARG A  78       4.135  16.246  26.293  1.00 16.17           C
ANISOU  591  C   ARG A  78     2095   2226   1820    157    723    318       C
ATOM    592  O   ARG A  78       3.779  16.192  25.115  1.00 17.98           O
ANISOU  592  O   ARG A  78     2411   2252   2169    200    465    301       O
ATOM    593  CB  ARG A  78       5.704  14.454  26.748  1.00 17.88           C
ANISOU  593  CB  ARG A  78     2625   2101   2066    163    416    264       C
ATOM    594  CG  ARG A  78       6.205  13.364  27.670  1.00 17.43           C
ANISOU  594  CG  ARG A  78     2511   2118   1992    314    268    351       C
ATOM    595  CD  ARG A  78       7.481  12.770  27.103  1.00 16.89           C
ANISOU  595  CD  ARG A  78     2185   2196   2036     88    -42    308       C
ATOM    596  NE  ARG A  78       7.226  11.966  25.932  1.00 16.40           N
ANISOU  596  NE  ARG A  78     1902   2062   2267    337     94    314       N
ATOM    597  CZ  ARG A  78       7.848  12.026  24.752  1.00 16.94           C
ANISOU  597  CZ  ARG A  78     2155   2085   2194     31    100    194       C
ATOM    598  NH1 ARG A  78       8.935  12.784  24.545  1.00 15.61           N
ANISOU  598  NH1 ARG A  78     1757   2246   1926    196    195    156       N
ATOM    599  NH2 ARG A  78       7.383  11.244  23.778  1.00 17.49           N
ANISOU  599  NH2 ARG A  78     2291   2054   2299     11    130     10       N
ATOM    600  N   LYS A  79       4.357  17.370  26.939  1.00 17.04           N
ANISOU  600  N   LYS A  79     2266   2358   1850    244    558    211       N
ATOM    601  CA  LYS A  79       4.380  18.674  26.294  1.00 17.05           C
ANISOU  601  CA  LYS A  79     2154   2304   2018    423    473    148       C
ATOM    602  C   LYS A  79       5.812  18.987  25.986  1.00 16.79           C
ANISOU  602  C   LYS A  79     2245   2210   1923    196    485     16       C
ATOM    603  O   LYS A  79       6.578  19.214  26.888  1.00 19.10           O
ANISOU  603  O   LYS A  79     2849   2631   1778    172    549   -105       O
ATOM    604  CB  LYS A  79       3.765  19.716  27.222  1.00 19.69           C
ANISOU  604  CB  LYS A  79     2591   2502   2388    435    618    129       C
ATOM    605  CG  LYS A  79       2.244  19.566  27.445  1.00 27.31           C
ANISOU  605  CG  LYS A  79     3350   3485   3539    349    553    -51       C
ATOM    606  CD  LYS A  79       1.694  18.211  27.809  1.00 34.90           C
ANISOU  606  CD  LYS A  79     4280   4377   4602    -38    405     86       C
ATOM    607  CE  LYS A  79       0.264  18.339  28.400  1.00 38.35           C
ANISOU  607  CE  LYS A  79     4546   5006   5016      1    423    140       C
ATOM    608  NZ  LYS A  79      -0.560  17.071  28.254  1.00 40.14           N
ANISOU  608  NZ  LYS A  79     5086   4934   5231     80    484     36       N
ATOM    609  N   VAL A  80       6.152  18.952  24.706  1.00 14.74           N
ANISOU  609  N   VAL A  80     2168   1857   1572    129    351    100       N
ATOM    610  CA  VAL A  80       7.515  19.086  24.293  1.00 14.09           C
ANISOU  610  CA  VAL A  80     2042   1674   1634     16    209     21       C
ATOM    611  C   VAL A  80       7.650  20.242  23.302  1.00 13.90           C
ANISOU  611  C   VAL A  80     2029   1677   1573    285    274    -20       C
ATOM    612  O   VAL A  80       6.693  20.727  22.702  1.00 14.94           O
ANISOU  612  O   VAL A  80     2081   1763   1831    187    355    220       O
ATOM    613  CB  VAL A  80       8.019  17.780  23.641  1.00 13.09           C
ANISOU  613  CB  VAL A  80     1610   1588   1773    153    247    124       C
ATOM    614  CG1 VAL A  80       7.769  16.547  24.577  1.00 16.49           C
ANISOU  614  CG1 VAL A  80     2823   1538   1903      1    288    278       C
ATOM    615  CG2 VAL A  80       7.380  17.515  22.278  1.00 14.00           C
ANISOU  615  CG2 VAL A  80     1932   1753   1632     55    326     98       C
ATOM    616  N   LYS A  81       8.889  20.669  23.175  1.00 12.87           N
ANISOU  616  N   LYS A  81     2055   1383   1453    106    125      1       N
ATOM    617  CA  LYS A  81       9.293  21.614  22.139  1.00 12.90           C
ANISOU  617  CA  LYS A  81     1803   1468   1628    167     36    -22       C
ATOM    618  C   LYS A  81      10.079  20.841  21.095  1.00 11.15           C
ANISOU  618  C   LYS A  81     1401   1251   1583    285    113    -31       C
ATOM    619  O   LYS A  81      11.019  20.163  21.425  1.00 12.61           O
ANISOU  619  O   LYS A  81     1571   1726   1492    382    -39     16       O
ATOM    620  CB  LYS A  81      10.129  22.721  22.750  1.00 15.24           C
ANISOU  620  CB  LYS A  81     2244   1762   1782     27    171    -41       C
ATOM    621  CG  LYS A  81       9.496  23.555  23.767  1.00 21.92           C
ANISOU  621  CG  LYS A  81     3059   2432   2836     33     -8   -187       C
ATOM    622  CD  LYS A  81       8.391  24.428  23.242  1.00 27.79           C
ANISOU  622  CD  LYS A  81     3687   3412   3457    229   -273   -190       C
ATOM    623  CE  LYS A  81       7.990  25.417  24.340  1.00 30.70           C
ANISOU  623  CE  LYS A  81     4116   3686   3863    217   -263   -373       C
ATOM    624  NZ  LYS A  81       7.056  26.426  23.814  1.00 32.67           N
ANISOU  624  NZ  LYS A  81     4716   3743   3953     46   -910   -249       N
ATOM    625  N   SER A  82       9.579  20.873  19.876  1.00 11.22           N
ANISOU  625  N   SER A  82     1578   1342   1341    261    108     61       N
ATOM    626  CA  SER A  82      10.084  20.060  18.802  1.00  9.67           C
ANISOU  626  CA  SER A  82      853   1321   1500    211    -14     56       C
ATOM    627  C   SER A  82      10.714  20.879  17.712  1.00  9.94           C
ANISOU  627  C   SER A  82     1129   1314   1334    208    -71     53       C
ATOM    628  O   SER A  82      10.212  21.956  17.367  1.00 10.28           O
ANISOU  628  O   SER A  82     1065   1285   1554    203    129     99       O
ATOM    629  CB  SER A  82       8.953  19.264  18.233  1.00 11.43           C
ANISOU  629  CB  SER A  82      951   1715   1676     59    244     38       C
ATOM    630  OG  SER A  82       8.585  18.255  19.158  1.00 13.92           O
ANISOU  630  OG  SER A  82     1890   1458   1940    109    396    319       O
ATOM    631  N   THR A  83      11.777  20.352  17.107  1.00  9.44           N
ANISOU  631  N   THR A  83      971   1222   1391    163     46     51       N
ATOM    632  CA  THR A  83      12.356  20.968  15.902  1.00  9.92           C
ANISOU  632  CA  THR A  83      810   1428   1528    120     -7     93       C
ATOM    633  C   THR A  83      12.634  19.802  14.955  1.00 10.55           C
ANISOU  633  C   THR A  83     1319   1275   1412    302    133    201       C
ATOM    634  O   THR A  83      13.251  18.820  15.374  1.00 11.67           O
ANISOU  634  O   THR A  83     1682   1365   1385    395     47     81       O
ATOM    635  CB  THR A  83      13.584  21.755  16.187  1.00 11.34           C
ANISOU  635  CB  THR A  83      590   1679   2040      4    -33    -22       C
ATOM    636  OG1 THR A  83      13.358  22.662  17.271  1.00 15.06           O
ANISOU  636  OG1 THR A  83     1846   1670   2205     24   -128   -243       O
ATOM    637  CG2 THR A  83      13.940  22.489  14.931  1.00 14.44           C
ANISOU  637  CG2 THR A  83     1538   1666   2280   -217    327     43       C
ATOM    638  N   ILE A  84      12.175  19.914  13.720  1.00  9.47           N
ANISOU  638  N   ILE A  84      899   1256   1443    334    127    147       N
ATOM    639  CA  ILE A  84      12.365  18.890  12.691  1.00  9.55           C
ANISOU  639  CA  ILE A  84      901   1273   1453    182    269    182       C
ATOM    640  C   ILE A  84      13.176  19.514  11.576  1.00 10.36           C
ANISOU  640  C   ILE A  84     1099   1392   1443     21    133     86       C
ATOM    641  O   ILE A  84      12.846  20.573  11.068  1.00 10.41           O
ANISOU  641  O   ILE A  84     1110   1441   1403    143    186    183       O
ATOM    642  CB  ILE A  84      11.020  18.306  12.237  1.00  9.42           C
ANISOU  642  CB  ILE A  84      767   1323   1489    214    133    128       C
ATOM    643  CG1 ILE A  84      10.316  17.705  13.423  1.00 10.10           C
ANISOU  643  CG1 ILE A  84      853   1539   1442    148     12    300       C
ATOM    644  CG2 ILE A  84      11.282  17.225  11.158  1.00 12.00           C
ANISOU  644  CG2 ILE A  84     1696   1347   1515     50    191    -93       C
ATOM    645  CD1 ILE A  84       8.984  17.151  13.120  1.00 11.41           C
ANISOU  645  CD1 ILE A  84      838   1844   1650     97    161    232       C
ATOM    646  N   THR A  85      14.269  18.838  11.188  1.00 10.18           N
ANISOU  646  N   THR A  85      999   1361   1507    -48    174    170       N
ATOM    647  CA  THR A  85      15.153  19.245  10.124  1.00 11.80           C
ANISOU  647  CA  THR A  85     1353   1378   1751    -25    251     57       C
ATOM    648  C   THR A  85      15.368  18.038   9.199  1.00 11.30           C
ANISOU  648  C   THR A  85     1212   1438   1643    -55    393     64       C
ATOM    649  O   THR A  85      15.099  16.903   9.526  1.00 12.33           O
ANISOU  649  O   THR A  85     1601   1473   1610    -31    460    106       O
ATOM    650  CB  THR A  85      16.468  19.771  10.676  1.00 12.74           C
ANISOU  650  CB  THR A  85     1232   1641   1966      5    317    -42       C
ATOM    651  OG1 THR A  85      17.015  18.741  11.494  1.00 16.00           O
ANISOU  651  OG1 THR A  85     1626   2135   2317    202   -299    -89       O
ATOM    652  CG2 THR A  85      16.267  21.044  11.442  1.00 16.03           C
ANISOU  652  CG2 THR A  85     1584   1952   2552   -393    279   -514       C
ATOM    653  N  ALEU A  86      15.658  18.351   7.945  0.50 12.53           N
ANISOU  653  N  ALEU A  86     1616   1474   1669   -122    235    123       N
ATOM    654  N  BLEU A  86      16.136  18.308   8.147  0.50 11.18           N
ANISOU  654  N  BLEU A  86      965   1461   1818    -17    538     34       N
ATOM    655  CA ALEU A  86      16.017  17.365   6.929  0.50 12.45           C
ANISOU  655  CA ALEU A  86     1255   1709   1765   -224    334    115       C
ATOM    656  CA BLEU A  86      16.734  17.255   7.296  0.50 12.49           C
ANISOU  656  CA BLEU A  86     1513   1453   1779    -80    318    -22       C
ATOM    657  C  ALEU A  86      17.533  17.400   6.726  0.50 13.51           C
ANISOU  657  C  ALEU A  86     1504   1812   1814   -246    406    146       C
ATOM    658  C  BLEU A  86      18.234  17.213   7.477  0.50 13.62           C
ANISOU  658  C  BLEU A  86     1284   1800   2089   -209    373     42       C
ATOM    659  O  ALEU A  86      18.086  18.420   6.283  0.50 16.44           O
ANISOU  659  O  ALEU A  86     1997   1930   2318    -87    743     32       O
ATOM    660  O  BLEU A  86      18.849  18.273   7.438  0.50 14.70           O
ANISOU  660  O  BLEU A  86     1511   1602   2473   -515    389    -65       O
ATOM    661  CB ALEU A  86      15.359  17.722   5.626  0.50 14.37           C
ANISOU  661  CB ALEU A  86     1720   1898   1839   -245    197     93       C
ATOM    662  CB BLEU A  86      16.440  17.443   5.800  0.50 14.34           C
ANISOU  662  CB BLEU A  86     1769   1854   1824    -23    229    232       C
ATOM    663  CG ALEU A  86      14.157  16.998   5.041  0.50 19.81           C
ANISOU  663  CG ALEU A  86     2331   2679   2514   -387     33    116       C
ATOM    664  CG BLEU A  86      15.052  17.078   5.289  0.50 14.51           C
ANISOU  664  CG BLEU A  86     1481   1793   2237   -123   -155    569       C
ATOM    665  CD1ALEU A  86      14.088  17.401   3.587  0.50 18.06           C
ANISOU  665  CD1ALEU A  86     2213   2613   2036   -475    -28    -56       C
ATOM    666  CD1BLEU A  86      14.697  17.785   3.983  0.50 18.68           C
ANISOU  666  CD1BLEU A  86     2446   2653   1996    -36    186    336       C
ATOM    667  CD2ALEU A  86      14.168  15.462   5.103  0.50 18.03           C
ANISOU  667  CD2ALEU A  86     2519   2329   2002   -922    177    -86       C
ATOM    668  CD2BLEU A  86      14.906  15.566   5.139  0.50 13.31           C
ANISOU  668  CD2BLEU A  86      305   2277   2472   -312   -106    119       C
ATOM    669  N  AASP A  87      18.209  16.319   7.115  0.50 15.11           N
ANISOU  669  N  AASP A  87     1735   1968   2036   -176    353     47       N
ATOM    670  N  BASP A  87      18.774  16.005   7.667  0.50 13.63           N
ANISOU  670  N  BASP A  87     1137   1903   2138   -406    308     54       N
ATOM    671  CA AASP A  87      19.678  16.232   7.198  0.50 17.53           C
ANISOU  671  CA AASP A  87     1958   2363   2340   -189    364    -16       C
ATOM    672  CA BASP A  87      20.193  15.709   7.683  0.50 15.11           C
ANISOU  672  CA BASP A  87     1229   2153   2359   -141    150     95       C
ATOM    673  C  AASP A  87      20.079  15.129   6.268  0.50 16.09           C
ANISOU  673  C  AASP A  87     1588   2300   2225   -183    434    -45       C
ATOM    674  C  BASP A  87      20.320  14.711   6.574  0.50 14.63           C
ANISOU  674  C  BASP A  87     1358   1995   2203   -238    141    150       C
ATOM    675  O  AASP A  87      20.000  13.959   6.612  0.50 16.86           O
ANISOU  675  O  AASP A  87     1576   2392   2437   -381    380    -32       O
ATOM    676  O  BASP A  87      19.926  13.559   6.715  0.50 17.22           O
ANISOU  676  O  BASP A  87     1790   2125   2627   -553    329    126       O
ATOM    677  CB AASP A  87      20.113  15.885   8.645  0.50 18.07           C
ANISOU  677  CB AASP A  87     1796   2652   2417   -281    287    -11       C
ATOM    678  CB BASP A  87      20.662  15.019   8.965  0.50 16.49           C
ANISOU  678  CB BASP A  87     1308   2303   2654   -123    115    106       C
ATOM    679  CG AASP A  87      21.589  15.377   8.775  0.50 24.14           C
ANISOU  679  CG AASP A  87     2381   3619   3172   -270    516    149       C
ATOM    680  CG BASP A  87      22.225  15.176   9.216  0.50 20.95           C
ANISOU  680  CG BASP A  87     1555   3082   3320    140   -114    307       C
ATOM    681  OD1AASP A  87      22.439  15.653   7.899  0.50 30.61           O
ANISOU  681  OD1AASP A  87     3429   4849   3350   -888    740    254       O
ATOM    682  OD1BASP A  87      22.980  14.177   9.206  0.50 27.99           O
ANISOU  682  OD1BASP A  87     1265   4041   5327    -36    118   -477       O
ATOM    683  OD2AASP A  87      21.933  14.731   9.816  0.50 27.93           O
ANISOU  683  OD2AASP A  87     2096   4591   3925   -363    892    621       O
ATOM    684  OD2BASP A  87      22.664  16.317   9.462  0.50 30.96           O
ANISOU  684  OD2BASP A  87     3146   3740   4877   -166    207   -101       O
ATOM    685  N  AGLY A  88      20.543  15.507   5.086  0.50 16.44           N
ANISOU  685  N  AGLY A  88     1969   2086   2191   -103    308     26       N
ATOM    686  N  BGLY A  88      20.941  15.115   5.477  0.50 16.04           N
ANISOU  686  N  BGLY A  88     1567   2194   2330   -191    237    119       N
ATOM    687  CA AGLY A  88      20.618  14.568   4.026  0.50 16.16           C
ANISOU  687  CA AGLY A  88     1942   2121   2074    -20    352     17       C
ATOM    688  CA BGLY A  88      21.264  14.135   4.481  0.50 15.76           C
ANISOU  688  CA BGLY A  88     1557   2276   2152    -79    123     93       C
ATOM    689  C  AGLY A  88      19.220  14.139   3.732  0.50 16.21           C
ANISOU  689  C  AGLY A  88     1984   2225   1947   -125    419      9       C
ATOM    690  C  BGLY A  88      20.106  13.231   4.097  0.50 15.70           C
ANISOU  690  C  BGLY A  88     1610   2336   2018   -100    245     11       C
ATOM    691  O  AGLY A  88      18.318  14.972   3.587  0.50 18.26           O
ANISOU  691  O  AGLY A  88     2285   2448   2202   -141    509     64       O
ATOM    692  O  BGLY A  88      20.242  12.031   4.018  0.50 15.88           O
ANISOU  692  O  BGLY A  88     1422   2293   2317   -121    173     91       O
ATOM    693  N  AGLY A  89      19.072  12.827   3.630  0.50 14.09           N
ANISOU  693  N  AGLY A  89     1664   2005   1684   -189    309    -85       N
ATOM    694  N  BGLY A  89      18.950  13.800   3.834  0.50 15.08           N
ANISOU  694  N  BGLY A  89     1648   2284   1795    -17    452     54       N
ATOM    695  CA AGLY A  89      17.804  12.154   3.409  0.50 14.86           C
ANISOU  695  CA AGLY A  89     1784   2081   1780   -171    217   -137       C
ATOM    696  CA BGLY A  89      17.814  13.005   3.448  0.50 15.16           C
ANISOU  696  CA BGLY A  89     1820   2165   1773    -34    238    -56       C
ATOM    697  C  AGLY A  89      17.108  11.754   4.681  0.50 13.13           C
ANISOU  697  C  AGLY A  89     1363   1950   1673   -196    274   -147       C
ATOM    698  C  BGLY A  89      17.034  12.251   4.566  0.50 13.83           C
ANISOU  698  C  BGLY A  89     1423   2126   1703   -266    232      2       C
ATOM    699  O  AGLY A  89      16.182  10.930   4.650  0.50 14.42           O
ANISOU  699  O  AGLY A  89     1892   1775   1812    -85     69   -303       O
ATOM    700  O  BGLY A  89      16.025  11.614   4.275  0.50 14.82           O
ANISOU  700  O  BGLY A  89     1777   2174   1678   -363   -143    -77       O
ATOM    701  N   VAL A  90      17.502  12.334   5.815  1.00 13.52           N
ANISOU  701  N   VAL A  90     1423   2064   1647   -378    344   -157       N
ATOM    702  CA  VAL A  90      16.888  11.835   7.041  1.00 12.90           C
ANISOU  702  CA  VAL A  90     1577   1626   1698   -302    280   -171       C
ATOM    703  C   VAL A  90      16.131  12.966   7.687  1.00 11.10           C
ANISOU  703  C   VAL A  90     1155   1611   1450    -54    209    -47       C
ATOM    704  O   VAL A  90      16.660  14.051   7.919  1.00 12.30           O
ANISOU  704  O   VAL A  90     1484   1465   1725   -253    362   -116       O
ATOM    705  CB  VAL A  90      17.928  11.265   8.028  1.00 13.75           C
ANISOU  705  CB  VAL A  90     1475   1690   2058    -30    390   -154       C
ATOM    706  CG1 VAL A  90      17.342  10.734   9.291  1.00 14.48           C
ANISOU  706  CG1 VAL A  90     1530   1986   1983   -101    395     35       C
ATOM    707  CG2 VAL A  90      18.838  10.186   7.382  1.00 16.73           C
ANISOU  707  CG2 VAL A  90     1417   2088   2851    460    568    -34       C
ATOM    708  N  ALEU A  91      14.843  12.770   7.944  0.50 10.91           N
ANISOU  708  N  ALEU A  91     1236   1423   1487    -88     71    -43       N
ATOM    709  N  BLEU A  91      14.913  12.678   8.038  0.50 10.55           N
ANISOU  709  N  BLEU A  91     1011   1532   1465   -134    217      8       N
ATOM    710  CA ALEU A  91      14.060  13.697   8.835  0.50 11.12           C
ANISOU  710  CA ALEU A  91     1378   1328   1518     55    -15     39       C
ATOM    711  CA BLEU A  91      14.055  13.635   8.710  0.50 10.85           C
ANISOU  711  CA BLEU A  91     1196   1400   1527      7    209    166       C
ATOM    712  C  ALEU A  91      14.511  13.426  10.253  0.50 11.20           C
ANISOU  712  C  ALEU A  91     1482   1386   1385    205    166    -52       C
ATOM    713  C  BLEU A  91      14.346  13.462  10.229  0.50 11.55           C
ANISOU  713  C  BLEU A  91     1545   1416   1427    105    332     11       C
ATOM    714  O  ALEU A  91      14.450  12.313  10.760  0.50 11.09           O
ANISOU  714  O  ALEU A  91     1648   1209   1356    154     80     56       O
ATOM    715  O  BLEU A  91      14.059  12.394  10.763  0.50 10.87           O
ANISOU  715  O  BLEU A  91     1295   1263   1570     11    412    180       O
ATOM    716  CB ALEU A  91      12.515  13.575   8.745  0.50 11.44           C
ANISOU  716  CB ALEU A  91     1175   1611   1557     81    -97    -45       C
ATOM    717  CB BLEU A  91      12.606  13.342   8.316  0.50 10.80           C
ANISOU  717  CB BLEU A  91      882   1616   1602   -129    214    183       C
ATOM    718  CG ALEU A  91      11.954  14.121   7.422  0.50 12.88           C
ANISOU  718  CG ALEU A  91     1577   1591   1726     36   -153     -8       C
ATOM    719  CG BLEU A  91      11.730  14.446   8.865  0.50 11.37           C
ANISOU  719  CG BLEU A  91     1027   1673   1618    234    376    188       C
ATOM    720  CD1ALEU A  91      10.572  13.556   7.243  0.50 15.14           C
ANISOU  720  CD1ALEU A  91     1682   1837   2232    -97    166     77       C
ATOM    721  CD1BLEU A  91      11.882  15.726   8.091  0.50 10.91           C
ANISOU  721  CD1BLEU A  91      855   1866   1422    207    216    143       C
ATOM    722  CD2ALEU A  91      11.908  15.668   7.398  0.50 13.04           C
ANISOU  722  CD2ALEU A  91     2378   1193   1382    434    206     81       C
ATOM    723  CD2BLEU A  91      10.387  13.930   8.830  0.50 16.38           C
ANISOU  723  CD2BLEU A  91      718   2505   2998    -50    820    369       C
ATOM    724  N   VAL A  92      14.942  14.480  10.894  1.00  9.82           N
ANISOU  724  N   VAL A  92     1036   1198   1497    135    223     74       N
ATOM    725  CA  VAL A  92      15.449  14.413  12.265  1.00  9.95           C
ANISOU  725  CA  VAL A  92      933   1415   1431    283    223     89       C
ATOM    726  C   VAL A  92      14.538  15.275  13.141  1.00 10.14           C
ANISOU  726  C   VAL A  92     1073   1392   1385    315     50     10       C
ATOM    727  O   VAL A  92      14.448  16.485  12.954  1.00 11.88           O
ANISOU  727  O   VAL A  92     1765   1186   1559    270    282    136       O
ATOM    728  CB  VAL A  92      16.863  14.836  12.374  1.00 11.38           C
ANISOU  728  CB  VAL A  92      877   1708   1736    220    169     42       C
ATOM    729  CG1 VAL A  92      17.393  14.762  13.817  1.00 14.05           C
ANISOU  729  CG1 VAL A  92     1315   2235   1788    297    -82   -117       C
ATOM    730  CG2 VAL A  92      17.767  14.070  11.402  1.00 13.94           C
ANISOU  730  CG2 VAL A  92      660   2271   2366    335    304   -266       C
ATOM    731  N   HIS A  93      13.831  14.626  14.072  1.00  9.68           N
ANISOU  731  N   HIS A  93      977   1293   1405    261    138     63       N
ATOM    732  CA  HIS A  93      12.812  15.229  14.965  1.00  9.89           C
ANISOU  732  CA  HIS A  93     1002   1308   1447    249    153    186       C
ATOM    733  C   HIS A  93      13.362  15.191  16.387  1.00 10.22           C
ANISOU  733  C   HIS A  93     1298   1173   1411    278     76     43       C
ATOM    734  O   HIS A  93      13.454  14.131  16.954  1.00 11.96           O
ANISOU  734  O   HIS A  93     2059   1110   1372    178    -47     36       O
ATOM    735  CB  HIS A  93      11.511  14.490  14.776  1.00  9.77           C
ANISOU  735  CB  HIS A  93      619   1563   1526    111    195    226       C
ATOM    736  CG  HIS A  93      10.395  14.931  15.593  1.00 10.73           C
ANISOU  736  CG  HIS A  93      926   1581   1570    147    -11    406       C
ATOM    737  ND1 HIS A  93       9.178  14.321  15.469  1.00 14.45           N
ANISOU  737  ND1 HIS A  93      757   2271   2460     71    103    767       N
ATOM    738  CD2 HIS A  93      10.238  15.925  16.514  1.00 13.66           C
ANISOU  738  CD2 HIS A  93     1725   1891   1574    340    307    394       C
ATOM    739  CE1 HIS A  93       8.333  14.906  16.276  1.00 15.95           C
ANISOU  739  CE1 HIS A  93      609   2447   3002    148    525   1053       C
ATOM    740  NE2 HIS A  93       8.939  15.876  16.932  1.00 16.64           N
ANISOU  740  NE2 HIS A  93     1666   2318   2338    341    596    892       N
ATOM    741  N   VAL A  94      13.726  16.345  16.939  1.00  9.70           N
ANISOU  741  N   VAL A  94     1269   1132   1284    248     -3     99       N
ATOM    742  CA  VAL A  94      14.181  16.449  18.298  1.00  9.89           C
ANISOU  742  CA  VAL A  94      867   1377   1513     97    -33    102       C
ATOM    743  C   VAL A  94      13.110  17.012  19.179  1.00 10.80           C
ANISOU  743  C   VAL A  94     1314   1364   1425    199     -4     -3       C
ATOM    744  O   VAL A  94      12.506  18.035  18.841  1.00 13.11           O
ANISOU  744  O   VAL A  94     2006   1503   1469    606    248    214       O
ATOM    745  CB  VAL A  94      15.417  17.287  18.387  1.00 12.41           C
ANISOU  745  CB  VAL A  94     1113   1725   1877    133    -60      7       C
ATOM    746  CG1 VAL A  94      16.002  17.383  19.805  1.00 15.90           C
ANISOU  746  CG1 VAL A  94     1795   2241   2004   -280   -394    -33       C
ATOM    747  CG2 VAL A  94      16.482  16.802  17.410  1.00 15.49           C
ANISOU  747  CG2 VAL A  94     1134   2440   2311   -238    190    -83       C
ATOM    748  N   GLN A  95      12.841  16.354  20.293  1.00 10.61           N
ANISOU  748  N   GLN A  95     1502   1180   1348    155    -25     13       N
ATOM    749  CA  GLN A  95      11.872  16.765  21.276  1.00 11.29           C
ANISOU  749  CA  GLN A  95     1555   1381   1352    147     -7     69       C
ATOM    750  C   GLN A  95      12.569  17.078  22.571  1.00 12.07           C
ANISOU  750  C   GLN A  95     1843   1354   1387     51    -52     66       C
ATOM    751  O   GLN A  95      13.315  16.231  23.089  1.00 13.00           O
ANISOU  751  O   GLN A  95     2018   1416   1503    204   -230     17       O
ATOM    752  CB  GLN A  95      10.895  15.626  21.543  1.00 11.94           C
ANISOU  752  CB  GLN A  95     1585   1506   1445    144    -25     42       C
ATOM    753  CG  GLN A  95      10.051  15.244  20.368  1.00 11.96           C
ANISOU  753  CG  GLN A  95     1295   1435   1811    -13      9    144       C
ATOM    754  CD  GLN A  95       9.053  14.130  20.633  1.00 13.16           C
ANISOU  754  CD  GLN A  95     1476   1632   1892    -54    -48     38       C
ATOM    755  OE1 GLN A  95       8.031  14.005  19.893  1.00 16.51           O
ANISOU  755  OE1 GLN A  95     1861   2288   2125   -183   -126    164       O
ATOM    756  NE2 GLN A  95       9.395  13.242  21.510  1.00 14.90           N
ANISOU  756  NE2 GLN A  95     2156   1483   2021   -161   -241    334       N
ATOM    757  N   LYS A  96      12.237  18.206  23.166  1.00 12.50           N
ANISOU  757  N   LYS A  96     1881   1411   1457    119   -244    -15       N
ATOM    758  CA  LYS A  96      12.835  18.675  24.432  1.00 13.21           C
ANISOU  758  CA  LYS A  96     1749   1663   1606     82   -249    -69       C
ATOM    759  C   LYS A  96      11.729  18.933  25.440  1.00 14.14           C
ANISOU  759  C   LYS A  96     2283   1516   1570    166   -146   -163       C
ATOM    760  O   LYS A  96      10.763  19.585  25.143  1.00 14.98           O
ANISOU  760  O   LYS A  96     2488   1670   1533    361     44   -151       O
ATOM    761  CB  LYS A  96      13.549  19.990  24.217  1.00 15.30           C
ANISOU  761  CB  LYS A  96     1763   2056   1991   -142   -189   -319       C
ATOM    762  CG  LYS A  96      14.638  19.961  23.237  1.00 19.09           C
ANISOU  762  CG  LYS A  96     1824   2734   2693   -154    -67   -261       C
ATOM    763  CD  LYS A  96      15.848  19.161  23.546  1.00 21.31           C
ANISOU  763  CD  LYS A  96     1798   2963   3334    161    142   -292       C
ATOM    764  CE  LYS A  96      17.020  19.370  22.604  1.00 21.34           C
ANISOU  764  CE  LYS A  96      742   3494   3870   -466    -92   -199       C
ATOM    765  NZ  LYS A  96      18.198  18.595  22.755  1.00 24.19           N
ANISOU  765  NZ  LYS A  96     1413   3785   3993   -763   -180    -19       N
ATOM    766  N   TRP A  97      11.932  18.422  26.651  1.00 15.03           N
ANISOU  766  N   TRP A  97     2444   1728   1537    242    -75   -154       N
ATOM    767  CA  TRP A  97      10.945  18.621  27.714  1.00 16.21           C
ANISOU  767  CA  TRP A  97     2681   1863   1614    338    -19    -73       C
ATOM    768  C   TRP A  97      11.636  18.324  29.032  1.00 19.15           C
ANISOU  768  C   TRP A  97     3383   2185   1705    343   -131   -187       C
ATOM    769  O   TRP A  97      12.485  17.459  29.103  1.00 20.14           O
ANISOU  769  O   TRP A  97     3715   2397   1538    560   -258    -58       O
ATOM    770  CB  TRP A  97       9.668  17.754  27.561  1.00 17.20           C
ANISOU  770  CB  TRP A  97     2850   1954   1730    198    159    -68       C
ATOM    771  CG  TRP A  97       9.866  16.337  27.947  1.00 16.16           C
ANISOU  771  CG  TRP A  97     2668   1691   1778     19    360     85       C
ATOM    772  CD1 TRP A  97       9.345  15.727  29.031  1.00 18.75           C
ANISOU  772  CD1 TRP A  97     2890   2432   1801    -90    445    228       C
ATOM    773  CD2 TRP A  97      10.612  15.335  27.252  1.00 15.29           C
ANISOU  773  CD2 TRP A  97     2412   1750   1645   -272    212   -191       C
ATOM    774  NE1 TRP A  97       9.726  14.431  29.084  1.00 17.80           N
ANISOU  774  NE1 TRP A  97     2853   2149   1760     27    231    197       N
ATOM    775  CE2 TRP A  97      10.512  14.153  28.006  1.00 16.08           C
ANISOU  775  CE2 TRP A  97     2647   1829   1633     48     98     71       C
ATOM    776  CE3 TRP A  97      11.363  15.301  26.060  1.00 15.09           C
ANISOU  776  CE3 TRP A  97     2321   1731   1679   -156     51    -62       C
ATOM    777  CZ2 TRP A  97      11.170  12.987  27.635  1.00 16.32           C
ANISOU  777  CZ2 TRP A  97     2557   1665   1976   -247     62    221       C
ATOM    778  CZ3 TRP A  97      11.986  14.134  25.721  1.00 13.86           C
ANISOU  778  CZ3 TRP A  97     1412   1951   1904      5    -45    -62       C
ATOM    779  CH2 TRP A  97      11.855  13.005  26.487  1.00 16.39           C
ANISOU  779  CH2 TRP A  97     2599   1589   2039     52     46   -186       C
ATOM    780  N   ASP A  98      11.333  19.115  30.059  1.00 21.91           N
ANISOU  780  N   ASP A  98     3932   2611   1780    384    -87   -252       N
ATOM    781  CA  ASP A  98      11.800  18.812  31.429  1.00 24.86           C
ANISOU  781  CA  ASP A  98     4165   3071   2210    194   -253   -250       C
ATOM    782  C   ASP A  98      13.298  18.555  31.514  1.00 24.55           C
ANISOU  782  C   ASP A  98     4271   2917   2139    114   -332   -457       C
ATOM    783  O   ASP A  98      13.758  17.683  32.259  1.00 27.61           O
ANISOU  783  O   ASP A  98     4785   3376   2328    165   -482   -268       O
ATOM    784  CB  ASP A  98      11.002  17.608  31.957  1.00 27.82           C
ANISOU  784  CB  ASP A  98     4517   3444   2607    201   -317   -154       C
ATOM    785  CG  ASP A  98      10.990  17.496  33.478  1.00 33.77           C
ANISOU  785  CG  ASP A  98     5286   4217   3327    167   -275    -49       C
ATOM    786  OD1 ASP A  98      11.029  18.543  34.150  1.00 39.07           O
ANISOU  786  OD1 ASP A  98     6067   4654   4122    544   -259   -465       O
ATOM    787  OD2 ASP A  98      10.875  16.346  33.985  1.00 43.35           O
ANISOU  787  OD2 ASP A  98     6846   4998   4627    343   -211    582       O
ATOM    788  N   GLY A  99      14.086  19.291  30.744  1.00 24.40           N
ANISOU  788  N   GLY A  99     4021   2899   2350    -64   -394   -608       N
ATOM    789  CA  GLY A  99      15.540  19.053  30.706  1.00 24.43           C
ANISOU  789  CA  GLY A  99     3769   2874   2638   -105   -464   -516       C
ATOM    790  C   GLY A  99      16.021  17.777  30.009  1.00 24.36           C
ANISOU  790  C   GLY A  99     3699   2896   2660    -41   -541   -446       C
ATOM    791  O   GLY A  99      17.219  17.502  29.956  1.00 27.26           O
ANISOU  791  O   GLY A  99     3828   3355   3173   -209  -1056   -611       O
ATOM    792  N   LYS A 100      15.106  17.036  29.391  1.00 20.61           N
ANISOU  792  N   LYS A 100     3369   2432   2030    -40   -730   -307       N
ATOM    793  CA  LYS A 100      15.362  15.794  28.654  1.00 19.69           C
ANISOU  793  CA  LYS A 100     3227   2373   1878    132   -639   -114       C
ATOM    794  C   LYS A 100      15.242  16.051  27.135  1.00 16.95           C
ANISOU  794  C   LYS A 100     2664   2084   1691     67   -739     -2       C
ATOM    795  O   LYS A 100      14.686  17.060  26.705  1.00 17.08           O
ANISOU  795  O   LYS A 100     3081   1649   1760    -77   -712    -69       O
ATOM    796  CB  LYS A 100      14.340  14.760  29.069  1.00 19.34           C
ANISOU  796  CB  LYS A 100     3290   2194   1865    327   -557     19       C
ATOM    797  CG  LYS A 100      14.364  14.373  30.539  1.00 24.46           C
ANISOU  797  CG  LYS A 100     3682   3317   2293    120   -445     74       C
ATOM    798  CD  LYS A 100      13.120  13.582  30.935  1.00 30.09           C
ANISOU  798  CD  LYS A 100     4340   3858   3235    103    -12    438       C
ATOM    799  CE  LYS A 100      12.851  13.532  32.426  1.00 34.65           C
ANISOU  799  CE  LYS A 100     4764   4569   3831     62     95    220       C
ATOM    800  NZ  LYS A 100      11.349  13.683  32.706  1.00 39.14           N
ANISOU  800  NZ  LYS A 100     4920   5314   4637     77    134    485       N
ATOM    801  N   SER A 101      15.773  15.114  26.364  1.00 16.87           N
ANISOU  801  N   SER A 101     2851   1842   1715     92   -625    -35       N
ATOM    802  CA  SER A 101      15.713  15.182  24.908  1.00 16.07           C
ANISOU  802  CA  SER A 101     2655   1659   1790    -21   -508     32       C
ATOM    803  C   SER A 101      15.639  13.803  24.330  1.00 13.81           C
ANISOU  803  C   SER A 101     2018   1564   1662    143   -448     55       C
ATOM    804  O   SER A 101      16.267  12.898  24.838  1.00 13.85           O
ANISOU  804  O   SER A 101     1444   1798   2019    116   -557     31       O
ATOM    805  CB  SER A 101      16.997  15.847  24.436  1.00 18.60           C
ANISOU  805  CB  SER A 101     3082   1955   2027   -269   -394     65       C
ATOM    806  OG  SER A 101      17.000  16.027  23.069  1.00 22.15           O
ANISOU  806  OG  SER A 101     3470   2415   2530   -557   -415     33       O
ATOM    807  N   THR A 102      14.854  13.657  23.262  1.00 11.58           N
ANISOU  807  N   THR A 102     1417   1474   1506     47   -407     32       N
ATOM    808  CA  THR A 102      14.866  12.434  22.495  1.00 11.47           C
ANISOU  808  CA  THR A 102     1334   1400   1622    201   -270    -41       C
ATOM    809  C   THR A 102      14.859  12.844  21.010  1.00 10.95           C
ANISOU  809  C   THR A 102     1492   1282   1383     89    -75     67       C
ATOM    810  O   THR A 102      14.393  13.906  20.659  1.00 11.48           O
ANISOU  810  O   THR A 102     1489   1277   1594    123   -159     36       O
ATOM    811  CB  THR A 102      13.640  11.573  22.898  1.00 12.29           C
ANISOU  811  CB  THR A 102     1385   1610   1675     -8    -93   -132       C
ATOM    812  OG1 THR A 102      13.755  10.279  22.274  1.00 13.53           O
ANISOU  812  OG1 THR A 102     1640   1396   2103      8    -91     11       O
ATOM    813  CG2 THR A 102      12.350  12.171  22.550  1.00 13.10           C
ANISOU  813  CG2 THR A 102     1335   1739   1900     59   -155    -38       C
ATOM    814  N   THR A 103      15.369  11.938  20.177  1.00 10.94           N
ANISOU  814  N   THR A 103     1264   1271   1619    202   -236     46       N
ATOM    815  CA  THR A 103      15.421  12.141  18.755  1.00 12.13           C
ANISOU  815  CA  THR A 103     1866   1284   1458    260     -8     86       C
ATOM    816  C   THR A 103      14.746  11.014  18.027  1.00 12.35           C
ANISOU  816  C   THR A 103     1971   1275   1444    187   -135    -45       C
ATOM    817  O   THR A 103      15.003   9.846  18.309  1.00 14.18           O
ANISOU  817  O   THR A 103     2565   1203   1618    297   -474     11       O
ATOM    818  CB  THR A 103      16.870  12.311  18.289  1.00 14.06           C
ANISOU  818  CB  THR A 103     1861   1697   1784     -1      4    -82       C
ATOM    819  OG1 THR A 103      17.470  13.432  18.976  1.00 18.83           O
ANISOU  819  OG1 THR A 103     2528   2357   2266   -333    -91     30       O
ATOM    820  CG2 THR A 103      16.927  12.620  16.825  1.00 17.57           C
ANISOU  820  CG2 THR A 103     2500   2254   1920     50     51   -110       C
ATOM    821  N   ILE A 104      13.907  11.345  17.062  1.00 10.66           N
ANISOU  821  N   ILE A 104     1489   1159   1403    194    -51     13       N
ATOM    822  CA  ILE A 104      13.209  10.424  16.185  1.00 10.97           C
ANISOU  822  CA  ILE A 104     1549   1222   1398    123    -58     37       C
ATOM    823  C   ILE A 104      13.685  10.713  14.775  1.00  9.88           C
ANISOU  823  C   ILE A 104     1121   1332   1298     59    -52     45       C
ATOM    824  O   ILE A 104      13.545  11.803  14.276  1.00 11.74           O
ANISOU  824  O   ILE A 104     1802   1324   1334    259     90     66       O
ATOM    825  CB  ILE A 104      11.661  10.595  16.256  1.00 12.19           C
ANISOU  825  CB  ILE A 104     1669   1572   1391     58    109    135       C
ATOM    826  CG1 ILE A 104      11.173  10.434  17.698  1.00 13.52           C
ANISOU  826  CG1 ILE A 104     1605   1738   1792   -132    347    -94       C
ATOM    827  CG2 ILE A 104      10.961   9.651  15.335  1.00 14.48           C
ANISOU  827  CG2 ILE A 104     1799   2106   1595   -173    -41   -105       C
ATOM    828  CD1 ILE A 104       9.793  10.910  17.880  1.00 23.88           C
ANISOU  828  CD1 ILE A 104     2780   3742   2551    491    624    -63       C
ATOM    829  N   LYS A 105      14.283   9.729  14.140  1.00 10.12           N
ANISOU  829  N   LYS A 105     1381   1126   1336     18    -11     48       N
ATOM    830  CA  LYS A 105      14.798   9.833  12.790  1.00 10.46           C
ANISOU  830  CA  LYS A 105     1279   1266   1427     32     53     83       C
ATOM    831  C   LYS A 105      13.955   8.997  11.874  1.00 10.53           C
ANISOU  831  C   LYS A 105     1340   1287   1373   -111     -1     47       C
ATOM    832  O   LYS A 105      13.585   7.883  12.200  1.00 13.38           O
ANISOU  832  O   LYS A 105     2284   1304   1493   -273   -222    128       O
ATOM    833  CB  LYS A 105      16.199   9.334  12.707  1.00 12.29           C
ANISOU  833  CB  LYS A 105     1437   1735   1497    -26     -7    -64       C
ATOM    834  CG  LYS A 105      17.205  10.229  13.465  1.00 15.84           C
ANISOU  834  CG  LYS A 105     1329   2456   2232    203   -176   -125       C
ATOM    835  CD  LYS A 105      18.654   9.930  13.291  1.00 19.64           C
ANISOU  835  CD  LYS A 105     1305   3310   2845    -25   -203   -132       C
ATOM    836  CE  LYS A 105      19.536  11.055  14.012  1.00 24.72           C
ANISOU  836  CE  LYS A 105     1920   3700   3772    281   -598   -182       C
ATOM    837  NZ  LYS A 105      21.000  10.834  14.040  1.00 32.22           N
ANISOU  837  NZ  LYS A 105     2571   4673   4996    605   -595     46       N
ATOM    838  N   ARG A 106      13.592   9.537  10.731  1.00 10.23           N
ANISOU  838  N   ARG A 106     1262   1254   1370    -92     75     61       N
ATOM    839  CA  ARG A 106      12.794   8.834   9.721  1.00 11.54           C
ANISOU  839  CA  ARG A 106     1456   1494   1431   -350     37     69       C
ATOM    840  C   ARG A 106      13.627   8.834   8.434  1.00 10.50           C
ANISOU  840  C   ARG A 106     1345   1281   1363   -136   -103    -10       C
ATOM    841  O   ARG A 106      14.073   9.872   7.962  1.00 11.67           O
ANISOU  841  O   ARG A 106     1674   1324   1433   -283     30     24       O
ATOM    842  CB  ARG A 106      11.443   9.527   9.523  1.00 12.90           C
ANISOU  842  CB  ARG A 106     1283   1943   1673   -464     80     57       C
ATOM    843  CG  ARG A 106      10.583   9.515  10.798  1.00 14.55           C
ANISOU  843  CG  ARG A 106     1448   2065   2015   -272    325    160       C
ATOM    844  CD  ARG A 106       9.322  10.311  10.669  1.00 20.07           C
ANISOU  844  CD  ARG A 106     1569   3302   2756   -107    659     97       C
ATOM    845  NE  ARG A 106       8.437  10.240  11.847  1.00 25.51           N
ANISOU  845  NE  ARG A 106     2315   3919   3458   -311   1204    183       N
ATOM    846  CZ  ARG A 106       8.414  11.090  12.857  1.00 24.38           C
ANISOU  846  CZ  ARG A 106     2366   3911   2987     16    813    455       C
ATOM    847  NH1 ARG A 106       9.215  12.097  12.970  1.00 20.91           N
ANISOU  847  NH1 ARG A 106     1972   3507   2463    741    360    757       N
ATOM    848  NH2 ARG A 106       7.545  10.887  13.842  1.00 26.79           N
ANISOU  848  NH2 ARG A 106     2578   4509   3091   -299   1218    314       N
ATOM    849  N   LYS A 107      13.732   7.671   7.809  1.00 11.16           N
ANISOU  849  N   LYS A 107     1413   1434   1392   -404    152     17       N
ATOM    850  CA  LYS A 107      14.488   7.498   6.594  1.00 12.65           C
ANISOU  850  CA  LYS A 107     1491   1750   1563   -155     -8    -45       C
ATOM    851  C   LYS A 107      13.871   6.467   5.680  1.00 13.44           C
ANISOU  851  C   LYS A 107     1869   1741   1497   -499     76    -43       C
ATOM    852  O   LYS A 107      13.347   5.494   6.124  1.00 15.15           O
ANISOU  852  O   LYS A 107     2326   2006   1421   -813     93    -13       O
ATOM    853  CB  LYS A 107      15.911   7.161   6.892  1.00 15.87           C
ANISOU  853  CB  LYS A 107     1979   2316   1734   -190    118   -319       C
ATOM    854  CG  LYS A 107      16.241   5.920   7.230  1.00 24.30           C
ANISOU  854  CG  LYS A 107     2929   3051   3251   -166   -149   -170       C
ATOM    855  CD  LYS A 107      17.672   5.606   6.562  1.00 28.61           C
ANISOU  855  CD  LYS A 107     2904   3852   4114    500     -6    -48       C
ATOM    856  CE  LYS A 107      18.639   6.779   6.385  1.00 25.78           C
ANISOU  856  CE  LYS A 107     3009   3235   3551    468    158    -53       C
ATOM    857  NZ  LYS A 107      19.327   7.049   5.060  1.00 29.45           N
ANISOU  857  NZ  LYS A 107     3014   4265   3908   -275    743   -304       N
ATOM    858  N   ARG A 108      13.988   6.697   4.401  1.00 12.23           N
ANISOU  858  N   ARG A 108     1496   1642   1508   -428     57    -61       N
ATOM    859  CA  ARG A 108      13.575   5.702   3.418  1.00 11.69           C
ANISOU  859  CA  ARG A 108      972   1894   1576   -340    224      1       C
ATOM    860  C   ARG A 108      14.678   4.654   3.249  1.00 12.65           C
ANISOU  860  C   ARG A 108     1120   2072   1613   -202    238   -267       C
ATOM    861  O   ARG A 108      15.840   4.974   3.024  1.00 15.30           O
ANISOU  861  O   ARG A 108     1239   2149   2422   -280    455   -500       O
ATOM    862  CB  ARG A 108      13.296   6.374   2.095  1.00 14.26           C
ANISOU  862  CB  ARG A 108     1406   2364   1645   -458    156     60       C
ATOM    863  CG  ARG A 108      11.960   7.077   2.049  1.00 16.76           C
ANISOU  863  CG  ARG A 108     2038   2422   1905   -188     48    395       C
ATOM    864  CD  ARG A 108      10.806   6.100   2.157  1.00 18.03           C
ANISOU  864  CD  ARG A 108     1703   3065   2082   -391    132    563       C
ATOM    865  NE  ARG A 108      10.861   4.995   1.154  1.00 18.91           N
ANISOU  865  NE  ARG A 108     1075   3270   2837   -281    -95    507       N
ATOM    866  CZ  ARG A 108      10.580   5.134  -0.125  1.00 17.10           C
ANISOU  866  CZ  ARG A 108     1048   2218   3229   -131   -256     74       C
ATOM    867  NH1 ARG A 108      10.052   6.240  -0.618  1.00 19.05           N
ANISOU  867  NH1 ARG A 108     1888   2613   2735    196     46    274       N
ATOM    868  NH2 ARG A 108      10.729   4.105  -0.935  1.00 23.19           N
ANISOU  868  NH2 ARG A 108     2291   2934   3583    -12   -208   -348       N
ATOM    869  N   GLU A 109      14.226   3.374   3.271  1.00 11.86           N
ANISOU  869  N   GLU A 109     1078   1796   1631   -248    275   -292       N
ATOM    870  CA  GLU A 109      15.129   2.263   3.026  1.00 13.93           C
ANISOU  870  CA  GLU A 109     1521   2171   1599     49    111   -216       C
ATOM    871  C   GLU A 109      14.371   1.299   2.166  1.00 12.65           C
ANISOU  871  C   GLU A 109     1308   1886   1613    -82    249   -136       C
ATOM    872  O   GLU A 109      13.403   0.714   2.628  1.00 13.76           O
ANISOU  872  O   GLU A 109     1666   2065   1495   -243    254   -125       O
ATOM    873  CB  GLU A 109      15.547   1.550   4.352  1.00 16.55           C
ANISOU  873  CB  GLU A 109     1896   2456   1935     25    -39   -219       C
ATOM    874  CG  GLU A 109      16.306   2.423   5.316  1.00 20.86           C
ANISOU  874  CG  GLU A 109     2856   2683   2383    -27    -66   -190       C
ATOM    875  CD  GLU A 109      17.713   2.679   4.857  1.00 29.23           C
ANISOU  875  CD  GLU A 109     3624   4138   3342   -189    205   -494       C
ATOM    876  OE1 GLU A 109      18.459   3.421   5.546  1.00 36.45           O
ANISOU  876  OE1 GLU A 109     5208   4430   4210   -452   -475   -732       O
ATOM    877  OE2 GLU A 109      18.119   2.162   3.780  1.00 38.20           O
ANISOU  877  OE2 GLU A 109     5393   4965   4157    127    518   -620       O
ATOM    878  N   ASP A 110      14.833   1.094   0.951  1.00 12.32           N
ANISOU  878  N   ASP A 110     1368   1785   1526      8    137    -75       N
ATOM    879  CA  ASP A 110      14.086   0.303  -0.012  1.00 12.46           C
ANISOU  879  CA  ASP A 110     1423   1829   1480   -112    329    -15       C
ATOM    880  C   ASP A 110      12.687   0.847  -0.071  1.00 11.09           C
ANISOU  880  C   ASP A 110      875   2020   1315   -261    155   -184       C
ATOM    881  O   ASP A 110      12.529   2.074  -0.188  1.00 12.12           O
ANISOU  881  O   ASP A 110     1205   1735   1663   -213    245    -89       O
ATOM    882  CB  ASP A 110      14.189  -1.181   0.259  1.00 14.71           C
ANISOU  882  CB  ASP A 110     1892   1952   1743    -81    421   -185       C
ATOM    883  CG  ASP A 110      15.589  -1.670   0.222  1.00 18.80           C
ANISOU  883  CG  ASP A 110     2405   2296   2442    346    607    147       C
ATOM    884  OD1 ASP A 110      16.391  -1.275  -0.698  1.00 22.73           O
ANISOU  884  OD1 ASP A 110     2838   3012   2784    452    770   -102       O
ATOM    885  OD2 ASP A 110      15.966  -2.508   1.071  1.00 28.92           O
ANISOU  885  OD2 ASP A 110     4105   3290   3591    759    188    949       O
ATOM    886  N   ASP A 111      11.631   0.040  -0.046  1.00 12.48           N
ANISOU  886  N   ASP A 111     1040   2119   1582   -274     70   -382       N
ATOM    887  CA  ASP A 111      10.289   0.519  -0.118  1.00 12.92           C
ANISOU  887  CA  ASP A 111     1033   2288   1585   -486     51   -162       C
ATOM    888  C   ASP A 111       9.694   0.862   1.257  1.00 12.35           C
ANISOU  888  C   ASP A 111      740   2105   1845     -9    -77   -361       C
ATOM    889  O   ASP A 111       8.548   1.190   1.313  1.00 15.37           O
ANISOU  889  O   ASP A 111     1086   2743   2007     37   -134   -697       O
ATOM    890  CB  ASP A 111       9.417  -0.495  -0.832  1.00 13.05           C
ANISOU  890  CB  ASP A 111      802   2339   1815   -438     67   -192       C
ATOM    891  CG  ASP A 111       9.706  -0.567  -2.317  1.00 15.36           C
ANISOU  891  CG  ASP A 111     1409   2636   1789   -348     38   -397       C
ATOM    892  OD1 ASP A 111       9.881   0.503  -2.923  1.00 18.20           O
ANISOU  892  OD1 ASP A 111     2595   2519   1798   -509    158   -124       O
ATOM    893  OD2 ASP A 111       9.737  -1.666  -2.847  1.00 19.77           O
ANISOU  893  OD2 ASP A 111     3305   2418   1789   -310    261   -548       O
ATOM    894  N   LYS A 112      10.565   0.857   2.276  1.00 12.84           N
ANISOU  894  N   LYS A 112     1370   1771   1736   -175    181   -107       N
ATOM    895  CA  LYS A 112      10.068   1.086   3.652  1.00 12.91           C
ANISOU  895  CA  LYS A 112     1671   1768   1467    -94    333    -85       C
ATOM    896  C   LYS A 112      10.429   2.464   4.129  1.00 10.92           C
ANISOU  896  C   LYS A 112     1010   1637   1502   -248     59    -76       C
ATOM    897  O   LYS A 112      11.301   3.132   3.606  1.00 11.69           O
ANISOU  897  O   LYS A 112     1054   1788   1597   -383    225    -93       O
ATOM    898  CB  LYS A 112      10.717   0.062   4.565  1.00 13.84           C
ANISOU  898  CB  LYS A 112     1894   1718   1644     35    465   -135       C
ATOM    899  CG  LYS A 112      10.417  -1.372   4.203  1.00 18.80           C
ANISOU  899  CG  LYS A 112     2731   1991   2421     12    444   -163       C
ATOM    900  CD  LYS A 112      11.351  -2.242   4.970  1.00 27.62           C
ANISOU  900  CD  LYS A 112     3951   3074   3468    358    261   -173       C
ATOM    901  CE  LYS A 112      12.666  -2.631   4.162  1.00 32.68           C
ANISOU  901  CE  LYS A 112     4076   3910   4427     33    362     83       C
ATOM    902  NZ  LYS A 112      13.811  -1.627   4.287  1.00 30.04           N
ANISOU  902  NZ  LYS A 112     3916   3351   4145    -15    729    900       N
ATOM    903  N  ALEU A 113       9.757   2.891   5.181  0.50 10.47           N
ANISOU  903  N  ALEU A 113     1113   1448   1416   -173     97    -59       N
ATOM    904  N  BLEU A 113       9.754   2.817   5.201  0.50 10.87           N
ANISOU  904  N  BLEU A 113     1178   1536   1416   -213    141   -120       N
ATOM    905  CA ALEU A 113      10.118   4.086   5.927  0.50 10.69           C
ANISOU  905  CA ALEU A 113     1189   1509   1365    -76     20    -49       C
ATOM    906  CA BLEU A 113      10.073   3.953   6.006  0.50 10.91           C
ANISOU  906  CA BLEU A 113     1190   1548   1405   -232    172    -27       C
ATOM    907  C  ALEU A 113      10.450   3.614   7.328  0.50  9.61           C
ANISOU  907  C  ALEU A 113      895   1373   1382     94    104    -91       C
ATOM    908  C  BLEU A 113      10.510   3.416   7.346  0.50 10.22           C
ANISOU  908  C  BLEU A 113     1034   1455   1395    -79    182   -115       C
ATOM    909  O  ALEU A 113       9.579   3.127   8.041  0.50 10.25           O
ANISOU  909  O  ALEU A 113     1295   1177   1420     99    135   -104       O
ATOM    910  O  BLEU A 113       9.849   2.639   8.003  0.50  9.57           O
ANISOU  910  O  BLEU A 113      887   1237   1510    -29    232     61       O
ATOM    911  CB ALEU A 113       8.955   5.060   5.893  0.50 12.03           C
ANISOU  911  CB ALEU A 113     1537   1628   1406   -253     27     31       C
ATOM    912  CB BLEU A 113       8.873   4.853   6.090  0.50 12.75           C
ANISOU  912  CB BLEU A 113     1674   1664   1506   -313    124    -77       C
ATOM    913  CG ALEU A 113       9.237   6.440   6.497  0.50 11.72           C
ANISOU  913  CG ALEU A 113      694   1905   1851    174    -75    -92       C
ATOM    914  CG BLEU A 113       9.203   6.109   6.873  0.50 14.35           C
ANISOU  914  CG BLEU A 113     1677   1974   1798   -376    -69   -113       C
ATOM    915  CD1ALEU A 113       8.100   7.289   6.099  0.50 12.51           C
ANISOU  915  CD1ALEU A 113     1263   1856   1634     -6   -133   -184       C
ATOM    916  CD1BLEU A 113      10.325   6.958   6.167  0.50 15.52           C
ANISOU  916  CD1BLEU A 113     1376   1975   2545   -421    220   -236       C
ATOM    917  CD2ALEU A 113       9.281   6.442   7.985  0.50 15.21           C
ANISOU  917  CD2ALEU A 113     1635   2211   1931    248    210    121       C
ATOM    918  CD2BLEU A 113       7.972   6.913   6.981  0.50 17.73           C
ANISOU  918  CD2BLEU A 113     1831   2503   2402   -109   -145   -386       C
ATOM    919  N   VAL A 114      11.731   3.737   7.702  1.00 10.68           N
ANISOU  919  N   VAL A 114     1258   1458   1343    -94     13     37       N
ATOM    920  CA  VAL A 114      12.274   3.257   8.958  1.00 12.21           C
ANISOU  920  CA  VAL A 114     1693   1462   1481   -139      9     91       C
ATOM    921  C   VAL A 114      12.392   4.423   9.921  1.00 12.42           C
ANISOU  921  C   VAL A 114     1771   1592   1355   -416   -114    134       C
ATOM    922  O   VAL A 114      12.837   5.507   9.584  1.00 12.56           O
ANISOU  922  O   VAL A 114     1794   1548   1428   -462     70     -9       O
ATOM    923  CB  VAL A 114      13.634   2.646   8.728  1.00 14.16           C
ANISOU  923  CB  VAL A 114     1968   1763   1650   -210    113    233       C
ATOM    924  CG1 VAL A 114      14.245   2.163  10.029  1.00 15.54           C
ANISOU  924  CG1 VAL A 114     1325   2410   2166    -64   -100    189       C
ATOM    925  CG2 VAL A 114      13.508   1.473   7.676  1.00 17.04           C
ANISOU  925  CG2 VAL A 114     2469   1985   2017     59    153   -145       C
ATOM    926  N   VAL A 115      11.877   4.200  11.111  1.00 12.62           N
ANISOU  926  N   VAL A 115     1983   1421   1388   -448   -151     64       N
ATOM    927  CA  VAL A 115      11.820   5.173  12.181  1.00 12.33           C
ANISOU  927  CA  VAL A 115     1903   1352   1427   -393   -150     62       C
ATOM    928  C   VAL A 115      12.719   4.692  13.314  1.00 12.17           C
ANISOU  928  C   VAL A 115     1875   1417   1331   -240   -185    195       C
ATOM    929  O   VAL A 115      12.486   3.637  13.874  1.00 16.01           O
ANISOU  929  O   VAL A 115     2527   1767   1787   -581   -583    373       O
ATOM    930  CB  VAL A 115      10.398   5.426  12.648  1.00 13.33           C
ANISOU  930  CB  VAL A 115     1952   1549   1562   -321     14     71       C
ATOM    931  CG1 VAL A 115      10.403   6.533  13.683  1.00 16.13           C
ANISOU  931  CG1 VAL A 115     2316   1989   1822   -106    127     -2       C
ATOM    932  CG2 VAL A 115       9.462   5.738  11.457  1.00 16.62           C
ANISOU  932  CG2 VAL A 115     2221   1972   2119   -573   -413    306       C
ATOM    933  N  AGLU A 116      13.694   5.489  13.706  0.50 11.10           N
ANISOU  933  N  AGLU A 116     1552   1282   1383   -104   -129     67       N
ATOM    934  N  BGLU A 116      13.711   5.468  13.694  0.50 11.53           N
ANISOU  934  N  BGLU A 116     1644   1315   1422   -141   -100     79       N
ATOM    935  CA AGLU A 116      14.631   5.181  14.789  0.50 10.94           C
ANISOU  935  CA AGLU A 116     1333   1207   1616     44   -128    100       C
ATOM    936  CA BGLU A 116      14.556   5.122  14.829  0.50 11.78           C
ANISOU  936  CA BGLU A 116     1511   1327   1636    -22     -1    120       C
ATOM    937  C  AGLU A 116      14.363   6.188  15.873  0.50 11.62           C
ANISOU  937  C  AGLU A 116     1674   1248   1490     -2   -273    -27       C
ATOM    938  C  BGLU A 116      14.374   6.172  15.875  0.50 12.10           C
ANISOU  938  C  BGLU A 116     1760   1298   1539    -57   -225      0       C
ATOM    939  O  AGLU A 116      14.526   7.385  15.661  0.50 12.60           O
ANISOU  939  O  AGLU A 116     2066   1163   1557    -32   -219     81       O
ATOM    940  O  BGLU A 116      14.569   7.364  15.639  0.50 12.86           O
ANISOU  940  O  BGLU A 116     2105   1172   1609    -65   -220     84       O
ATOM    941  CB AGLU A 116      16.073   5.323  14.275  0.50 11.90           C
ANISOU  941  CB AGLU A 116     1252   1265   2002    289   -186     20       C
ATOM    942  CB BGLU A 116      16.014   4.942  14.426  0.50 13.59           C
ANISOU  942  CB BGLU A 116     1581   1518   2065      5    -61    208       C
ATOM    943  CG AGLU A 116      17.178   4.865  15.242  0.50 15.38           C
ANISOU  943  CG AGLU A 116     1445   2293   2104     80   -163    309       C
ATOM    944  CG BGLU A 116      16.201   3.797  13.420  0.50 17.46           C
ANISOU  944  CG BGLU A 116     1717   2380   2536    153    297     96       C
ATOM    945  CD AGLU A 116      18.563   5.535  15.013  0.50 22.37           C
ANISOU  945  CD AGLU A 116     2309   3037   3151   -300   -325    462       C
ATOM    946  CD BGLU A 116      17.498   3.017  13.527  0.50 26.37           C
ANISOU  946  CD BGLU A 116     1960   3890   4167      0     29     90       C
ATOM    947  OE1AGLU A 116      18.689   6.794  14.951  0.50 24.62           O
ANISOU  947  OE1AGLU A 116     2486   3374   3494   -729     -9   1034       O
ATOM    948  OE1BGLU A 116      18.495   3.600  14.031  0.50 29.72           O
ANISOU  948  OE1BGLU A 116      469   5858   4965    472   -112    582       O
ATOM    949  OE2AGLU A 116      19.555   4.794  14.952  0.50 25.52           O
ANISOU  949  OE2AGLU A 116     3078   3264   3353     97   -117    804       O
ATOM    950  OE2BGLU A 116      17.557   1.814  13.057  0.50 30.21           O
ANISOU  950  OE2BGLU A 116     2701   4170   4606   -426    630     55       O
ATOM    951  N   CYS A 117      14.010   5.709  17.055  1.00 11.47           N
ANISOU  951  N   CYS A 117     1522   1348   1488     33   -207     43       N
ATOM    952  CA  CYS A 117      13.767   6.558  18.203  1.00 11.94           C
ANISOU  952  CA  CYS A 117     1468   1486   1581    184   -232     96       C
ATOM    953  C   CYS A 117      14.847   6.303  19.223  1.00 11.83           C
ANISOU  953  C   CYS A 117     1480   1405   1610    147   -248     28       C
ATOM    954  O   CYS A 117      15.068   5.181  19.617  1.00 12.55           O
ANISOU  954  O   CYS A 117     1786   1205   1774    -10   -526    175       O
ATOM    955  CB  CYS A 117      12.398   6.142  18.823  1.00 14.99           C
ANISOU  955  CB  CYS A 117     1639   2391   1663    627   -230    -56       C
ATOM    956  SG  CYS A 117      11.036   6.149  17.675  1.00 21.00           S
ANISOU  956  SG  CYS A 117     1681   4207   2089    191   -367    322       S
ATOM    957  N   VAL A 118      15.514   7.368  19.669  1.00 10.49           N
ANISOU  957  N   VAL A 118      833   1321   1829    155   -184     48       N
ATOM    958  CA  VAL A 118      16.676   7.250  20.512  1.00 11.60           C
ANISOU  958  CA  VAL A 118      700   1597   2109    164   -299    -73       C
ATOM    959  C   VAL A 118      16.502   8.113  21.769  1.00 11.82           C
ANISOU  959  C   VAL A 118     1055   1330   2106    172   -316    -39       C
ATOM    960  O   VAL A 118      16.192   9.318  21.691  1.00 13.25           O
ANISOU  960  O   VAL A 118     1857   1277   1898    198   -449    -50       O
ATOM    961  CB  VAL A 118      18.003   7.701  19.842  1.00 14.63           C
ANISOU  961  CB  VAL A 118      691   2024   2841    286   -111   -106       C
ATOM    962  CG1 VAL A 118      19.151   7.748  20.754  1.00 19.95           C
ANISOU  962  CG1 VAL A 118      570   3028   3983    148   -113   -112       C
ATOM    963  CG2 VAL A 118      18.340   6.822  18.660  1.00 19.64           C
ANISOU  963  CG2 VAL A 118     2369   2205   2888      1    525    -69       C
ATOM    964  N   MET A 119      16.714   7.512  22.917  1.00 13.52           N
ANISOU  964  N   MET A 119     1781   1424   1932    296   -607     -8       N
ATOM    965  CA  MET A 119      16.767   8.246  24.176  1.00 14.78           C
ANISOU  965  CA  MET A 119     1935   1674   2006    239   -560     67       C
ATOM    966  C   MET A 119      17.935   7.655  24.915  1.00 16.45           C
ANISOU  966  C   MET A 119     2073   1936   2238     52   -686     -9       C
ATOM    967  O   MET A 119      17.945   6.498  25.298  1.00 15.28           O
ANISOU  967  O   MET A 119     1973   1799   2033    228   -736    -67       O
ATOM    968  CB  MET A 119      15.472   7.991  24.924  1.00 16.51           C
ANISOU  968  CB  MET A 119     2139   2151   1980    668   -580    -40       C
ATOM    969  CG  MET A 119      15.285   8.483  26.386  1.00 20.94           C
ANISOU  969  CG  MET A 119     3003   2468   2483    332   -614    -82       C
ATOM    970  SD  MET A 119      14.992  10.172  26.332  1.00 26.57           S
ANISOU  970  SD  MET A 119     4648   2439   3006   1038  -1528   -485       S
ATOM    971  CE  MET A 119      15.037  10.809  27.961  1.00 20.96           C
ANISOU  971  CE  MET A 119     3026   2201   2735   -341   -438   -343       C
ATOM    972  N  ALYS A 120      18.970   8.457  25.165  0.50 19.92           N
ANISOU  972  N  ALYS A 120     2310   2420   2837     76   -470     31       N
ATOM    973  N  BLYS A 120      18.926   8.530  25.036  0.50 16.73           N
ANISOU  973  N  BLYS A 120     1712   2100   2542    125   -478     33       N
ATOM    974  CA ALYS A 120      20.250   7.991  25.779  0.50 22.21           C
ANISOU  974  CA ALYS A 120     2535   2824   3079      4   -345     12       C
ATOM    975  CA BLYS A 120      20.167   8.198  25.627  0.50 16.79           C
ANISOU  975  CA BLYS A 120     1729   2093   2557      2   -388     70       C
ATOM    976  C  ALYS A 120      20.561   6.475  25.846  0.50 20.95           C
ANISOU  976  C  ALYS A 120     2243   2730   2984    -68   -280    -27       C
ATOM    977  C  BLYS A 120      20.726   6.958  24.866  0.50 14.39           C
ANISOU  977  C  BLYS A 120     1330   1913   2224     56   -389    119       C
ATOM    978  O  ALYS A 120      20.331   5.797  26.863  0.50 22.60           O
ANISOU  978  O  ALYS A 120     2448   2952   3186   -103   -490   -183       O
ATOM    979  O  BLYS A 120      20.925   6.974  23.622  0.50 15.14           O
ANISOU  979  O  BLYS A 120     1263   1926   2561    295   -186    263       O
ATOM    980  CB ALYS A 120      20.361   8.531  27.186  0.50 23.93           C
ANISOU  980  CB ALYS A 120     2877   3006   3207     58   -338      4       C
ATOM    981  CB BLYS A 120      19.905   7.948  27.138  0.50 16.10           C
ANISOU  981  CB BLYS A 120     1830   1840   2443      7   -520     -9       C
ATOM    982  CG ALYS A 120      19.188   8.193  28.068  0.50 25.66           C
ANISOU  982  CG ALYS A 120     3127   3352   3267    171   -307    110       C
ATOM    983  CG BLYS A 120      19.462   9.250  27.890  0.50 18.68           C
ANISOU  983  CG BLYS A 120     2198   2154   2744     39   -467   -227       C
ATOM    984  CD ALYS A 120      18.845   9.438  28.880  0.50 29.59           C
ANISOU  984  CD ALYS A 120     3819   3581   3842    164    -68    -34       C
ATOM    985  CD BLYS A 120      18.762   8.915  29.194  0.50 25.58           C
ANISOU  985  CD BLYS A 120     3342   3206   3170    227   -177   -194       C
ATOM    986  CE ALYS A 120      19.051   9.267  30.374  0.50 32.57           C
ANISOU  986  CE ALYS A 120     4159   4085   4129    136   -137     33       C
ATOM    987  CE BLYS A 120      19.720   8.824  30.362  0.50 29.71           C
ANISOU  987  CE BLYS A 120     3665   3870   3753    126   -251    -66       C
ATOM    988  NZ ALYS A 120      17.933   8.492  30.996  0.50 33.98           N
ANISOU  988  NZ ALYS A 120     4030   4302   4578    -36    -80    -89       N
ATOM    989  NZ BLYS A 120      18.898   8.779  31.608  0.50 32.07           N
ANISOU  989  NZ BLYS A 120     4095   4363   3725    215   -134     14       N
ATOM    990  N  AGLY A 121      21.176   5.986  24.772  0.50 19.50           N
ANISOU  990  N  AGLY A 121     1954   2604   2849   -168   -242    -11       N
ATOM    991  N  BGLY A 121      21.041   5.868  25.574  0.50 13.81           N
ANISOU  991  N  BGLY A 121     1302   1865   2077   -132   -278    162       N
ATOM    992  CA AGLY A 121      21.637   4.620  24.654  0.50 17.20           C
ANISOU  992  CA AGLY A 121     1129   2636   2766   -154    -82     63       C
ATOM    993  CA BGLY A 121      21.599   4.746  24.875  0.50 14.28           C
ANISOU  993  CA BGLY A 121      735   2282   2406   -103   -189    168       C
ATOM    994  C  AGLY A 121      20.554   3.658  24.271  0.50 13.81           C
ANISOU  994  C  AGLY A 121      282   2431   2532   -217   -140    118       C
ATOM    995  C  BGLY A 121      20.599   3.739  24.362  0.50 12.39           C
ANISOU  995  C  BGLY A 121      303   2201   2204   -185   -267    175       C
ATOM    996  O  AGLY A 121      20.845   2.562  23.783  0.50 15.22           O
ANISOU  996  O  AGLY A 121      494   2449   2840   -352    131    225       O
ATOM    997  O  BGLY A 121      21.074   2.708  23.870  0.50 15.41           O
ANISOU  997  O  BGLY A 121     1411   2101   2342    361   -257    433       O
ATOM    998  N   VAL A 122      19.316   4.025  24.448  1.00 11.93           N
ANISOU  998  N   VAL A 122      616   1828   2089     -2   -164    248       N
ATOM    999  CA  VAL A 122      18.242   3.127  24.080  1.00 11.40           C
ANISOU  999  CA  VAL A 122      262   1919   2151     54    -59    193       C
ATOM   1000  C   VAL A 122      17.625   3.553  22.747  1.00 12.05           C
ANISOU 1000  C   VAL A 122     1070   1654   1852    157   -214    174       C
ATOM   1001  O   VAL A 122      17.182   4.705  22.606  1.00 14.53           O
ANISOU 1001  O   VAL A 122     2088   1362   2068    419   -674     26       O
ATOM   1002  CB  VAL A 122      17.198   3.047  25.139  1.00 12.45           C
ANISOU 1002  CB  VAL A 122      265   2039   2425    137    -37    317       C
ATOM   1003  CG1 VAL A 122      16.110   2.169  24.749  1.00 15.83           C
ANISOU 1003  CG1 VAL A 122      311   3010   2693    311    278    368       C
ATOM   1004  CG2 VAL A 122      17.747   2.584  26.510  1.00 14.40           C
ANISOU 1004  CG2 VAL A 122      736   2517   2217    152    277    315       C
ATOM   1005  N   THR A 123      17.642   2.629  21.802  1.00 12.24           N
ANISOU 1005  N   THR A 123     1237   1406   2007    173   -317    164       N
ATOM   1006  CA  THR A 123      17.080   2.847  20.489  1.00 12.90           C
ANISOU 1006  CA  THR A 123     1448   1562   1889    158   -243     84       C
ATOM   1007  C   THR A 123      15.947   1.877  20.228  1.00 12.72           C
ANISOU 1007  C   THR A 123     1624   1291   1917     39   -458    101       C
ATOM   1008  O   THR A 123      16.048   0.686  20.515  1.00 16.22           O
ANISOU 1008  O   THR A 123     1894   1372   2896     56   -592    359       O
ATOM   1009  CB  THR A 123      18.107   2.621  19.439  1.00 15.62           C
ANISOU 1009  CB  THR A 123     1812   2052   2068   -154   -215    -39       C
ATOM   1010  OG1 THR A 123      19.151   3.511  19.663  1.00 19.54           O
ANISOU 1010  OG1 THR A 123     2097   2645   2682    -39    364      0       O
ATOM   1011  CG2 THR A 123      17.541   2.872  18.022  1.00 16.59           C
ANISOU 1011  CG2 THR A 123      717   3240   2343     83    225    243       C
ATOM   1012  N   SER A 124      14.941   2.360  19.592  1.00 12.35           N
ANISOU 1012  N   SER A 124     1639   1328   1725   -144   -492    153       N
ATOM   1013  CA  SER A 124      13.867   1.547  19.046  1.00 12.33           C
ANISOU 1013  CA  SER A 124     1450   1434   1800   -131   -282    299       C
ATOM   1014  C   SER A 124      13.762   1.762  17.584  1.00 10.63           C
ANISOU 1014  C   SER A 124      958   1429   1651     34   -165    204       C
ATOM   1015  O   SER A 124      13.883   2.868  17.111  1.00 13.98           O
ANISOU 1015  O   SER A 124     2286   1353   1674   -147   -235    178       O
ATOM   1016  CB  SER A 124      12.536   1.843  19.736  1.00 12.48           C
ANISOU 1016  CB  SER A 124     1084   1755   1904   -265   -306    247       C
ATOM   1017  OG  SER A 124      11.443   1.205  19.106  1.00 14.29           O
ANISOU 1017  OG  SER A 124     1371   2072   1986   -158   -118     90       O
ATOM   1018  N   THR A 125      13.559   0.694  16.818  1.00 11.85           N
ANISOU 1018  N   THR A 125     1576   1275   1650    -96   -205    199       N
ATOM   1019  CA  THR A 125      13.367   0.741  15.381  1.00 12.27           C
ANISOU 1019  CA  THR A 125     1417   1512   1733    -30    -43    234       C
ATOM   1020  C   THR A 125      11.994   0.278  15.021  1.00 11.43           C
ANISOU 1020  C   THR A 125     1159   1571   1609   -313   -160    138       C
ATOM   1021  O   THR A 125      11.630  -0.831  15.382  1.00 13.97           O
ANISOU 1021  O   THR A 125     1861   1536   1911   -426   -295    310       O
ATOM   1022  CB  THR A 125      14.453  -0.112  14.670  1.00 15.13           C
ANISOU 1022  CB  THR A 125     1669   1936   2144    280    -46    -83       C
ATOM   1023  OG1 THR A 125      15.756   0.389  15.015  1.00 19.97           O
ANISOU 1023  OG1 THR A 125     1705   2783   3097    477    -67   -255       O
ATOM   1024  CG2 THR A 125      14.326  -0.039  13.174  1.00 18.38           C
ANISOU 1024  CG2 THR A 125     2166   2661   2157    321    342   -195       C
ATOM   1025  N   ARG A 126      11.277   1.112  14.295  1.00 12.09           N
ANISOU 1025  N   ARG A 126     1567   1479   1546   -344   -169    214       N
ATOM   1026  CA  ARG A 126       9.935   0.853  13.824  1.00 12.19           C
ANISOU 1026  CA  ARG A 126     1424   1667   1539   -425   -221    270       C
ATOM   1027  C   ARG A 126       9.949   0.920  12.313  1.00 12.79           C
ANISOU 1027  C   ARG A 126     1514   1783   1562   -401   -125    290       C
ATOM   1028  O   ARG A 126      10.500   1.846  11.732  1.00 16.21           O
ANISOU 1028  O   ARG A 126     2412   2185   1561   -962   -215    230       O
ATOM   1029  CB  ARG A 126       8.982   1.838  14.447  1.00 13.62           C
ANISOU 1029  CB  ARG A 126     1529   2056   1589   -343    -48    132       C
ATOM   1030  CG  ARG A 126       8.829   1.494  15.966  1.00 19.67           C
ANISOU 1030  CG  ARG A 126     2503   2844   2125     85    125     15       C
ATOM   1031  CD  ARG A 126       8.154   2.440  16.796  1.00 21.93           C
ANISOU 1031  CD  ARG A 126     2449   3553   2329    -62     25    -89       C
ATOM   1032  NE  ARG A 126       6.743   2.668  16.604  1.00 22.77           N
ANISOU 1032  NE  ARG A 126     2228   3929   2492    -34     83   -166       N
ATOM   1033  CZ  ARG A 126       5.717   2.037  17.193  1.00 22.62           C
ANISOU 1033  CZ  ARG A 126     2683   3926   1986   -456     83   -124       C
ATOM   1034  NH1 ARG A 126       5.847   0.849  17.766  1.00 23.88           N
ANISOU 1034  NH1 ARG A 126     2760   4217   2093    -94   -411   -234       N
ATOM   1035  NH2 ARG A 126       4.517   2.489  17.006  1.00 26.51           N
ANISOU 1035  NH2 ARG A 126     3323   3769   2978   -200    195     45       N
ATOM   1036  N   VAL A 127       9.295  -0.022  11.655  1.00 11.28           N
ANISOU 1036  N   VAL A 127     1363   1492   1431   -254    -17     97       N
ATOM   1037  CA  VAL A 127       9.357  -0.096  10.208  1.00 11.79           C
ANISOU 1037  CA  VAL A 127     1347   1563   1568     21     10     78       C
ATOM   1038  C   VAL A 127       7.930  -0.011   9.700  1.00 10.45           C
ANISOU 1038  C   VAL A 127     1162   1410   1398     38    -49    -30       C
ATOM   1039  O   VAL A 127       7.067  -0.732  10.161  1.00 11.23           O
ANISOU 1039  O   VAL A 127     1196   1524   1545   -217     63    112       O
ATOM   1040  CB  VAL A 127      10.034  -1.416   9.716  1.00 12.32           C
ANISOU 1040  CB  VAL A 127      688   2013   1980     84      0     77       C
ATOM   1041  CG1 VAL A 127      10.021  -1.520   8.194  1.00 15.65           C
ANISOU 1041  CG1 VAL A 127     1807   2364   1773    343     38   -215       C
ATOM   1042  CG2 VAL A 127      11.336  -1.564  10.312  1.00 14.84           C
ANISOU 1042  CG2 VAL A 127      545   2523   2567    264    158    -71       C
ATOM   1043  N   TYR A 128       7.742   0.907   8.750  1.00 10.67           N
ANISOU 1043  N   TYR A 128     1157   1406   1491   -168     30    -33       N
ATOM   1044  CA  TYR A 128       6.494   1.141   8.046  1.00 10.56           C
ANISOU 1044  CA  TYR A 128     1157   1471   1381    -64    -70      9       C
ATOM   1045  C   TYR A 128       6.611   0.759   6.599  1.00 11.62           C
ANISOU 1045  C   TYR A 128     1234   1539   1640   -117    -46     10       C
ATOM   1046  O   TYR A 128       7.662   0.956   5.974  1.00 11.81           O
ANISOU 1046  O   TYR A 128     1389   1603   1494   -227     12   -128       O
ATOM   1047  CB  TYR A 128       6.107   2.578   8.150  1.00 10.50           C
ANISOU 1047  CB  TYR A 128      969   1617   1400   -107    -42     20       C
ATOM   1048  CG  TYR A 128       5.723   3.095   9.520  1.00 10.59           C
ANISOU 1048  CG  TYR A 128      914   1345   1764   -221   -181     94       C
ATOM   1049  CD1 TYR A 128       6.709   3.349  10.473  1.00 12.29           C
ANISOU 1049  CD1 TYR A 128     1177   1605   1885    -88    -49    -57       C
ATOM   1050  CD2 TYR A 128       4.406   3.337   9.854  1.00 11.60           C
ANISOU 1050  CD2 TYR A 128      937   1699   1768   -222    -89    132       C
ATOM   1051  CE1 TYR A 128       6.319   3.866  11.753  1.00 14.17           C
ANISOU 1051  CE1 TYR A 128     1543   2028   1811    -24    -44   -170       C
ATOM   1052  CE2 TYR A 128       4.050   3.833  11.088  1.00 13.54           C
ANISOU 1052  CE2 TYR A 128     1386   1902   1856   -250    183    -16       C
ATOM   1053  CZ  TYR A 128       4.999   4.085  12.020  1.00 14.33           C
ANISOU 1053  CZ  TYR A 128     1657   2108   1679   -138    360    -76       C
ATOM   1054  OH  TYR A 128       4.592   4.575  13.257  1.00 19.12           O
ANISOU 1054  OH  TYR A 128     2968   2596   1697    285    251   -280       O
ATOM   1055  N   GLU A 129       5.497   0.257   6.061  1.00 11.89           N
ANISOU 1055  N   GLU A 129     1283   1638   1594   -166    -92   -202       N
ATOM   1056  CA  GLU A 129       5.388  -0.031   4.655  1.00 13.72           C
ANISOU 1056  CA  GLU A 129     1692   1769   1752     84   -187   -190       C
ATOM   1057  C   GLU A 129       4.268   0.790   4.079  1.00 12.49           C
ANISOU 1057  C   GLU A 129     1593   1642   1508   -136   -192   -321       C
ATOM   1058  O   GLU A 129       3.424   1.270   4.778  1.00 12.66           O
ANISOU 1058  O   GLU A 129     1620   1555   1634    -14    -88    -61       O
ATOM   1059  CB  GLU A 129       5.154  -1.522   4.409  1.00 16.55           C
ANISOU 1059  CB  GLU A 129     2211   1924   2151    305   -318   -196       C
ATOM   1060  CG  GLU A 129       6.421  -2.283   4.822  1.00 25.12           C
ANISOU 1060  CG  GLU A 129     3309   3015   3220    587   -346   -176       C
ATOM   1061  CD  GLU A 129       6.624  -3.668   4.239  1.00 34.16           C
ANISOU 1061  CD  GLU A 129     4754   3747   4475    624   -560   -627       C
ATOM   1062  OE1 GLU A 129       5.643  -4.235   3.676  1.00 40.20           O
ANISOU 1062  OE1 GLU A 129     5656   4025   5593    -83   -809   -797       O
ATOM   1063  OE2 GLU A 129       7.792  -4.170   4.371  1.00 38.86           O
ANISOU 1063  OE2 GLU A 129     5427   3945   5392   1193   -762   -674       O
ATOM   1064  N   ARG A 130       4.238   0.921   2.768  1.00 13.79           N
ANISOU 1064  N   ARG A 130     1773   1837   1627      7   -165   -323       N
ATOM   1065  CA  ARG A 130       3.142   1.663   2.122  1.00 14.33           C
ANISOU 1065  CA  ARG A 130     1808   1949   1688     -8   -195   -208       C
ATOM   1066  C   ARG A 130       1.839   0.994   2.360  1.00 15.76           C
ANISOU 1066  C   ARG A 130     1746   2118   2124   -229   -441   -460       C
ATOM   1067  O   ARG A 130       1.734  -0.233   2.219  1.00 17.42           O
ANISOU 1067  O   ARG A 130     1533   2198   2887     36   -790   -561       O
ATOM   1068  CB  ARG A 130       3.367   1.714   0.647  1.00 17.61           C
ANISOU 1068  CB  ARG A 130     2352   2450   1887     74   -370    -27       C
ATOM   1069  CG  ARG A 130       4.496   2.465   0.244  1.00 18.18           C
ANISOU 1069  CG  ARG A 130     2268   2678   1962    290   -216    192       C
ATOM   1070  CD  ARG A 130       4.230   3.873   0.081  1.00 22.01           C
ANISOU 1070  CD  ARG A 130     2081   2704   3578   -122   -285     80       C
ATOM   1071  NE  ARG A 130       5.377   4.589  -0.463  1.00 20.88           N
ANISOU 1071  NE  ARG A 130     2273   2182   3475    -81   -199    136       N
ATOM   1072  CZ  ARG A 130       5.439   5.910  -0.601  1.00 16.20           C
ANISOU 1072  CZ  ARG A 130     1368   2201   2586   -277   -388    252       C
ATOM   1073  NH1 ARG A 130       4.415   6.636  -0.377  1.00 18.64           N
ANISOU 1073  NH1 ARG A 130     2096   2655   2329    239   -292     95       N
ATOM   1074  NH2 ARG A 130       6.595   6.443  -0.961  1.00 19.51           N
ANISOU 1074  NH2 ARG A 130     1941   2883   2587      4    153    166       N
ATOM   1075  N   ALA A 131       0.865   1.774   2.708  1.00 17.30           N
ANISOU 1075  N   ALA A 131     1799   2204   2569   -336   -471   -382       N
ATOM   1076  CA  ALA A 131      -0.447   1.201   2.989  1.00 21.39           C
ANISOU 1076  CA  ALA A 131     2024   2754   3346   -383   -440   -103       C
ATOM   1077  C   ALA A 131      -1.132   0.691   1.707  1.00 24.33           C
ANISOU 1077  C   ALA A 131     2419   3067   3755   -527   -462    -69       C
ATOM   1078  O   ALA A 131      -0.707   1.097   0.603  1.00 27.60           O
ANISOU 1078  O   ALA A 131     2839   3765   3880   -534   -947      9       O
ATOM   1079  CB  ALA A 131      -1.269   2.194   3.760  1.00 23.65           C
ANISOU 1079  CB  ALA A 131     2259   2901   3824   -477     25   -198       C
ATOM   1080  OXT ALA A 131      -2.046  -0.189   1.711  1.00 28.95           O
ANISOU 1080  OXT ALA A 131     3224   3449   4325   -778   -455     47       O
TER    1081      ALA A 131
HETATM 1082  O   HOH A 132       4.795  28.336   0.125  1.00 34.67           O
ANISOU 1082  O   HOH A 132     2973   4917   5281   -720    265   1439       O
HETATM 1083  O   HOH A 133      16.168  21.669  32.708  1.00 47.11           O
ANISOU 1083  O   HOH A 133     8901   3980   5019  -2336    981  -1362       O
HETATM 1084  O   HOH A 134       8.309   7.699  18.964  1.00 43.74           O
ANISOU 1084  O   HOH A 134     2172   9002   5443   1010   -273   -454       O
HETATM 1085  O   HOH A 135       4.077  13.326  15.489  1.00 53.68           O
ANISOU 1085  O   HOH A 135    10002   3629   6764   -649   3272     17       O
HETATM 1086  O   HOH A 136      11.582  30.678   2.450  1.00 44.40           O
ANISOU 1086  O   HOH A 136     4435   7018   5415  -1451   -361    627       O
HETATM 1087  O   HOH A 137       9.011  -3.989   0.941  1.00 36.55           O
ANISOU 1087  O   HOH A 137     1838   5371   6678   -139    543   2310       O
HETATM 1088  O   HOH A 138       5.759  14.677  31.040  1.00 45.94           O
ANISOU 1088  O   HOH A 138     9591   4034   3828   1083    419   -258       O
HETATM 1089  O   HOH A 139      19.672  20.035   8.359  1.00126.19           O
ANISOU 1089  O   HOH A 139    12732  14821  20392  -7585   6939  -7171       O
HETATM 1090  O   HOH A 140      10.437  22.065  12.821  1.00 10.34           O
ANISOU 1090  O   HOH A 140     1122   1259   1546     97    107     99       O
HETATM 1091  O   HOH A 141      13.268  27.523   8.366  1.00 37.90           O
ANISOU 1091  O   HOH A 141     3711   5070   5619    167   1323  -1857       O
HETATM 1092  O   HOH A 142      18.844  17.898  14.852  1.00 39.29           O
ANISOU 1092  O   HOH A 142     2581   4173   8172   -529  -1097      1       O
HETATM 1093  O   HOH A 143      10.039  16.224   4.262  1.00 45.18           O
ANISOU 1093  O   HOH A 143     5836   6897   4433   2295   -884  -1106       O
HETATM 1094  O   HOH A 144       7.200  24.888  12.435  1.00 11.00           O
ANISOU 1094  O   HOH A 144      639   1811   1730   -123      0   -362       O
HETATM 1095  O   HOH A 145       3.237  -4.169   4.312  1.00 39.35           O
ANISOU 1095  O   HOH A 145     4794   4732   5425   -120     62   -601       O
HETATM 1096  O   HOH A 146      13.421  -7.454  20.030  1.00 42.40           O
ANISOU 1096  O   HOH A 146     3136   5934   7039    746  -1086   -400       O
HETATM 1097  O   HOH A 147      14.880  -5.527  22.437  0.50 24.55           O
ANISOU 1097  O   HOH A 147     4242   1884   3199     -8  -1430     73       O
HETATM 1098  O   HOH A 148      18.248   0.820   1.630  1.00 46.81           O
ANISOU 1098  O   HOH A 148     2345   9835   5604    800    534   1378       O
HETATM 1099  O   HOH A 149       3.313  21.342  24.105  1.00 42.14           O
ANISOU 1099  O   HOH A 149     7698   4666   3645   2468   1382    247       O
HETATM 1100  O   HOH A 150       3.838   5.298  16.427  1.00 45.29           O
ANISOU 1100  O   HOH A 150     4721   6896   5589  -1619  -1035   1738       O
HETATM 1101  O   HOH A 151       3.982   8.963  13.251  1.00 48.50           O
ANISOU 1101  O   HOH A 151     5909   7875   4642  -1856   2100    663       O
HETATM 1102  O   HOH A 152       5.328  -1.543  19.637  1.00 39.48           O
ANISOU 1102  O   HOH A 152     3125   6145   5728  -1052   1155  -1969       O
HETATM 1103  O   HOH A 153      -5.494  13.945  14.919  1.00 44.87           O
ANISOU 1103  O   HOH A 153     4199   3335   9511   1958    625    441       O
HETATM 1104  O   HOH A 154       2.271  -5.434  19.717  1.00 45.13           O
ANISOU 1104  O   HOH A 154     6690   5853   4603   1419    781  -1638       O
HETATM 1105  O   HOH A 155       6.868  -1.740  -3.655  1.00 50.14           O
ANISOU 1105  O   HOH A 155     3367   9914   5767   -727    -38  -1346       O
HETATM 1106  O   HOH A 156      10.870  -6.563  14.583  1.00 55.51           O
ANISOU 1106  O   HOH A 156     6044   6230   8817   3472  -1708  -3830       O
HETATM 1107  O   HOH A 157       0.350  -3.984  10.266  1.00 78.27           O
ANISOU 1107  O   HOH A 157     6393  11546  11798  -3343   2394   -566       O
HETATM 1108  O   HOH A 158       7.443  -6.283  15.510  1.00 28.33           O
ANISOU 1108  O   HOH A 158     4227   2713   3822  -1108  -1195   1075       O
HETATM 1109  O   HOH A 159      -7.187   9.577  19.664  1.00 32.85           O
ANISOU 1109  O   HOH A 159     2898   5744   3839    562   1352    316       O
HETATM 1110  O   HOH A 160      12.225  25.108 -14.809  1.00 34.78           O
ANISOU 1110  O   HOH A 160     3813   4039   5360  -1021  -1291    539       O
HETATM 1111  O   HOH A 161      -0.174   7.634  17.388  1.00 36.03           O
ANISOU 1111  O   HOH A 161     4202   5227   4258   1305   1725   1024       O
HETATM 1112  O   HOH A 162      12.527  -3.669  -1.861  1.00 27.13           O
ANISOU 1112  O   HOH A 162     4719   3066   2521   -888    306   -107       O
HETATM 1113  O   HOH A 163       0.997  20.248   5.153  1.00 15.57           O
ANISOU 1113  O   HOH A 163     1351   2388   2175   -241   -262    393       O
HETATM 1114  O   HOH A 164      13.759  26.668  15.418  1.00 13.56           O
ANISOU 1114  O   HOH A 164     1575   1494   2082   -342   -402   -121       O
HETATM 1115  O   HOH A 165       9.673  23.017   5.459  1.00 15.37           O
ANISOU 1115  O   HOH A 165     1282   2846   1710    316    -13    178       O
HETATM 1116  O   HOH A 166      16.183  18.691  14.170  1.00 20.71           O
ANISOU 1116  O   HOH A 166     2571   2845   2450   -121   -286    106       O
HETATM 1117  O   HOH A 167      -3.735  -0.636  22.106  1.00 14.07           O
ANISOU 1117  O   HOH A 167     1313   1782   2250   -297   -352    322       O
HETATM 1118  O   HOH A 168      11.785  12.324  12.111  1.00 13.40           O
ANISOU 1118  O   HOH A 168     1759   1693   1639    205    170     55       O
HETATM 1119  O   HOH A 169       1.762  12.848  14.281  1.00 23.67           O
ANISOU 1119  O   HOH A 169     2744   3480   2766   -103    459   1333       O
HETATM 1120  O   HOH A 170      15.475   8.911   3.223  1.00 19.86           O
ANISOU 1120  O   HOH A 170     2489   2192   2864   -636    822      0       O
HETATM 1121  O   HOH A 171       3.731  25.424  18.058  1.00 16.62           O
ANISOU 1121  O   HOH A 171     1397   2648   2267    781    -92   -461       O
HETATM 1122  O   HOH A 172       1.747  15.864  -0.123  1.00 22.89           O
ANISOU 1122  O   HOH A 172     4629   2292   1774     54   -958   -151       O
HETATM 1123  O   HOH A 173       4.056  27.190   2.550  1.00 18.26           O
ANISOU 1123  O   HOH A 173     1459   2456   3021    109   -216    -34       O
HETATM 1124  O   HOH A 174      13.280  21.532  19.910  1.00 19.99           O
ANISOU 1124  O   HOH A 174     1881   3455   2257   -859    -89    -13       O
HETATM 1125  O   HOH A 175       6.383  -0.339   1.278  1.00 21.27           O
ANISOU 1125  O   HOH A 175     1471   3367   3243   -193    332  -1037       O
HETATM 1126  O   HOH A 176       8.908  -3.083  19.991  1.00 18.65           O
ANISOU 1126  O   HOH A 176     2437   2352   2297    -35   -401   -182       O
HETATM 1127  O   HOH A 177       6.007  27.476  15.548  1.00 18.97           O
ANISOU 1127  O   HOH A 177     1904   1985   3320     49   -675   -173       O
HETATM 1128  O   HOH A 178       1.687   5.887   0.087  1.00 17.93           O
ANISOU 1128  O   HOH A 178     2028   2514   2268   -112   -165   -292       O
HETATM 1129  O   HOH A 179      -0.572  14.333   6.447  1.00 18.58           O
ANISOU 1129  O   HOH A 179     2243   2116   2699    -16   -146     75       O
HETATM 1130  O   HOH A 180      16.310  21.154   7.360  1.00 19.73           O
ANISOU 1130  O   HOH A 180     2818   1808   2871   -374    364    327       O
HETATM 1131  O   HOH A 181       2.684   6.692  13.453  1.00 25.25           O
ANISOU 1131  O   HOH A 181     2752   2907   3931    -76    562    276       O
HETATM 1132  O   HOH A 182       9.171  10.446  21.592  1.00 20.46           O
ANISOU 1132  O   HOH A 182     2678   2606   2489   -276    383    336       O
HETATM 1133  O   HOH A 183       7.117  27.732  11.909  1.00 17.89           O
ANISOU 1133  O   HOH A 183     1194   2607   2995    207   -370   -413       O
HETATM 1134  O   HOH A 184      17.804  -1.622  20.014  1.00 20.85           O
ANISOU 1134  O   HOH A 184     2117   2345   3458    -70   -834   -144       O
HETATM 1135  O   HOH A 185       6.361   9.252  -1.812  1.00 22.48           O
ANISOU 1135  O   HOH A 185     2734   2571   3236   -455    766   -426       O
HETATM 1136  O   HOH A 186       1.602  26.236   2.255  1.00 24.25           O
ANISOU 1136  O   HOH A 186     2002   2103   5105   -333    529   -440       O
HETATM 1137  O   HOH A 187      11.387  -2.789   0.739  1.00 20.92           O
ANISOU 1137  O   HOH A 187     3272   2013   2664   -477     86    -35       O
HETATM 1138  O   HOH A 188      15.953  -3.031  -2.876  1.00 27.96           O
ANISOU 1138  O   HOH A 188     5673   2808   2139    542    -51    199       O
HETATM 1139  O   HOH A 189      11.609  -5.788  20.936  1.00 26.21           O
ANISOU 1139  O   HOH A 189     4031   1610   4318   -240    216    770       O
HETATM 1140  O   HOH A 190       2.935   0.891  18.637  1.00 22.21           O
ANISOU 1140  O   HOH A 190     1792   4330   2315   -746    209    -32       O
HETATM 1141  O   HOH A 191      11.513  -3.079  13.603  1.00 24.17           O
ANISOU 1141  O   HOH A 191     4045   2292   2847   -112     85   -146       O
HETATM 1142  O   HOH A 192      -2.004  15.869  17.786  1.00 28.71           O
ANISOU 1142  O   HOH A 192     5722   2585   2600   -859   1172   -607       O
HETATM 1143  O   HOH A 193       2.760  14.020  18.164  1.00 30.13           O
ANISOU 1143  O   HOH A 193     3834   3335   4276   -601   -287    662       O
HETATM 1144  O   HOH A 194       4.964  29.088   4.408  1.00 30.78           O
ANISOU 1144  O   HOH A 194     2907   3268   5518   -585   -735  -1111       O
HETATM 1145  O   HOH A 195       8.708  -3.492  22.823  1.00 32.20           O
ANISOU 1145  O   HOH A 195     6644   2518   3070  -1230   1176   -487       O
HETATM 1146  O   HOH A 196      14.744   1.443  29.153  1.00 24.88           O
ANISOU 1146  O   HOH A 196     2661   4043   2746   1052   -605    265       O
HETATM 1147  O   HOH A 197      20.530   4.893  28.321  0.50 17.76           O
ANISOU 1147  O   HOH A 197     2218   2040   2490    300    -15      5       O
HETATM 1148  O   HOH A 198      17.603  13.243  27.860  1.00 26.96           O
ANISOU 1148  O   HOH A 198     2622   3903   3718    510   -773   1062       O
HETATM 1149  O   HOH A 199       2.191  -3.688  24.644  1.00 23.60           O
ANISOU 1149  O   HOH A 199     2309   3503   3155    847   -180   -514       O
HETATM 1150  O   HOH A 200      17.927  13.847  21.658  1.00 24.30           O
ANISOU 1150  O   HOH A 200     2169   4265   2796  -1015   -200   -258       O
HETATM 1151  O   HOH A 201      15.638  19.647  27.332  1.00 30.89           O
ANISOU 1151  O   HOH A 201     6278   2464   2994  -1282  -1576   -223       O
HETATM 1152  O   HOH A 202       8.769   4.913  32.734  1.00 31.27           O
ANISOU 1152  O   HOH A 202     4329   3656   3896   -500  -1992    311       O
HETATM 1153  O   HOH A 203       9.331  21.198  29.647  1.00 35.15           O
ANISOU 1153  O   HOH A 203     6194   3420   3739   1575    330   -759       O
HETATM 1154  O   HOH A 204      18.485   4.534   2.416  1.00 26.00           O
ANISOU 1154  O   HOH A 204     3171   4338   2367   -147   -323   -242       O
HETATM 1155  O   HOH A 205       0.443   5.078  32.157  1.00 26.11           O
ANISOU 1155  O   HOH A 205     4131   3233   2557    -38    125   -206       O
HETATM 1156  O  AHOH A 206       9.438  28.738  15.378  0.50 12.95           O
ANISOU 1156  O  AHOH A 206      979   1831   2109   -296    427    -42       O
HETATM 1157  O  BHOH A 206       9.043  28.761  16.837  0.50 22.39           O
ANISOU 1157  O  BHOH A 206     2087   1758   4662   -111    306     13       O
HETATM 1158  O   HOH A 207      -7.633   6.565  18.945  1.00 34.26           O
ANISOU 1158  O   HOH A 207     3601   4089   5324    851   1867    -59       O
HETATM 1159  O   HOH A 208       9.236  12.000  30.738  1.00 30.91           O
ANISOU 1159  O   HOH A 208     5507   2933   3304    354   1745    617       O
HETATM 1160  O   HOH A 209       6.671   5.673  14.928  1.00 30.31           O
ANISOU 1160  O   HOH A 209     1498   6273   3742   -609     18  -1171       O
HETATM 1161  O   HOH A 210      -0.705  18.669   3.818  1.00 23.04           O
ANISOU 1161  O   HOH A 210     3128   2543   3083   -235  -1541    123       O
HETATM 1162  O   HOH A 211       0.979  15.709  18.525  1.00 38.60           O
ANISOU 1162  O   HOH A 211     7117   4851   2696  -2233   1236   -533       O
HETATM 1163  O   HOH A 212       3.426  11.495  19.447  1.00 24.42           O
ANISOU 1163  O   HOH A 212     1981   3717   3579   -554    551   -107       O
HETATM 1164  O   HOH A 213       4.910  10.084  29.298  1.00 31.77           O
ANISOU 1164  O   HOH A 213     5621   3094   3354    677    519   1471       O
HETATM 1165  O   HOH A 214      -1.885  20.300  11.689  1.00 33.96           O
ANISOU 1165  O   HOH A 214     3343   3431   6126   -791   2870      7       O
HETATM 1166  O   HOH A 215      13.436  21.297  28.302  1.00 56.97           O
ANISOU 1166  O   HOH A 215    12023   4892   4732   -204   -648   1448       O
HETATM 1167  O   HOH A 216      12.019  -3.077  24.663  1.00 66.37           O
ANISOU 1167  O   HOH A 216    20247   1591   3377  -3269   -341   1085       O
HETATM 1168  O   HOH A 217       5.354  22.581  24.352  1.00 30.41           O
ANISOU 1168  O   HOH A 217     4373   3271   3909    945   1619   -106       O
HETATM 1169  O   HOH A 218       0.745  19.525  -1.762  1.00 54.24           O
ANISOU 1169  O   HOH A 218     7066   6244   7298   4071  -3020  -4534       O
HETATM 1170  O   HOH A 219      -7.202   2.564  23.459  1.00 24.69           O
ANISOU 1170  O   HOH A 219     3455   2434   3490   -432    429   -410       O
HETATM 1171  O   HOH A 220      18.536  11.354  24.264  1.00 87.96           O
ANISOU 1171  O   HOH A 220     9372   4778  19269    157  -2320   2893       O
HETATM 1172  O   HOH A 221       3.243  -2.292   1.083  1.00 34.84           O
ANISOU 1172  O   HOH A 221     2979   4068   6190   -292    432  -1692       O
HETATM 1173  O   HOH A 222       9.824  21.198   3.005  1.00 40.96           O
ANISOU 1173  O   HOH A 222     7751   4530   3281    603    685   -474       O
HETATM 1174  O   HOH A 223      -6.664   5.032  23.756  1.00 43.60           O
ANISOU 1174  O   HOH A 223     6770   5611   4184  -1835    435   -993       O
HETATM 1175  O   HOH A 224      11.336  24.946   4.402  1.00 36.30           O
ANISOU 1175  O   HOH A 224     3316   6228   4247   -860    232   1530       O
HETATM 1176  O   HOH A 225      -0.683  -5.053  17.525  1.00 32.67           O
ANISOU 1176  O   HOH A 225     3734   2946   5733    100    905    428       O
HETATM 1177  O   HOH A 226      20.729   4.608  17.613  1.00 50.20           O
ANISOU 1177  O   HOH A 226     5494   6534   7044    544   3845   -761       O
HETATM 1178  O   HOH A 227      -4.659  -2.380  24.090  1.00 12.15           O
ANISOU 1178  O   HOH A 227     1049   1737   1828     36    -32    300       O
HETATM 1179  O   HOH A 228      -0.357  -8.053  17.995  1.00 41.03           O
ANISOU 1179  O   HOH A 228     4136   3897   7556    -45  -2378  -2159       O
HETATM 1180  O   HOH A 229       0.252   3.599  -0.343  1.00 33.98           O
ANISOU 1180  O   HOH A 229     2959   3358   6593     84  -2267   -128       O
HETATM 1181  O   HOH A 230       3.058   8.167  31.031  1.00 33.92           O
ANISOU 1181  O   HOH A 230     3133   4902   4852   1856   -510  -1266       O
HETATM 1182  O   HOH A 231       3.122  12.288  30.073  1.00 40.05           O
ANISOU 1182  O   HOH A 231     6024   4898   4295    267   -654   1457       O
HETATM 1183  O   HOH A 232      15.451  -5.826  19.490  1.00 29.93           O
ANISOU 1183  O   HOH A 232     1869   4469   5032   -102   -635   1172       O
HETATM 1184  O   HOH A 233       6.252  11.502  19.695  1.00 32.77           O
ANISOU 1184  O   HOH A 233     2255   4090   6103   -950    429   -892       O
HETATM 1185  O   HOH A 234      10.503  -4.066  27.937  1.00 43.35           O
ANISOU 1185  O   HOH A 234     4737   7202   4529   3108    844   2439       O
HETATM 1186  O   HOH A 235      15.925  -1.244  17.812  1.00 32.05           O
ANISOU 1186  O   HOH A 235     4768   3937   3472   2096   -747   -599       O
HETATM 1187  O   HOH A 236       7.165  -3.072  30.410  1.00 30.09           O
ANISOU 1187  O   HOH A 236     5886   2395   3152   -159    675     91       O
HETATM 1188  O   HOH A 237      -4.304  12.446  13.343  1.00 56.28           O
ANISOU 1188  O   HOH A 237     2969  11674   6740    450  -2270    567       O
HETATM 1189  O   HOH A 238      -0.021   4.953  18.129  1.00 36.40           O
ANISOU 1189  O   HOH A 238     3264   4896   5668  -1252  -1360   2636       O
HETATM 1190  O   HOH A 239      15.935  -3.402  15.842  1.00 44.56           O
ANISOU 1190  O   HOH A 239     5513   3648   7767   -778    262    393       O
HETATM 1191  O   HOH A 240      12.645  25.501   6.136  1.00 36.15           O
ANISOU 1191  O   HOH A 240     6353   3586   3795   -296    400   1565       O
HETATM 1192  O   HOH A 241       7.621   3.040  -0.868  1.00 31.01           O
ANISOU 1192  O   HOH A 241     3910   4010   3861   1728   1192   1182       O
HETATM 1193  O   HOH A 242       2.230   9.927  17.431  1.00 27.15           O
ANISOU 1193  O   HOH A 242     3775   3728   2810    598     65    121       O
HETATM 1194  O   HOH A 243      21.367   5.234  21.367  1.00 44.20           O
ANISOU 1194  O   HOH A 243     7841   5006   3946   3024  -1005    235       O
HETATM 1195  O   HOH A 244      20.118  10.127   2.179  1.00 36.18           O
ANISOU 1195  O   HOH A 244     4424   4660   4664   1492    555    490       O
HETATM 1196  O   HOH A 245      19.640  14.751  18.040  1.00 64.60           O
ANISOU 1196  O   HOH A 245     3556   8775  12213    212   1819   1313       O
HETATM 1197  O   HOH A 246      -8.775  11.498  17.991  1.00 79.90           O
ANISOU 1197  O   HOH A 246     5814  10489  14054    289  -2567  -1536       O
HETATM 1198  O   HOH A 247       2.711  -2.639  17.704  1.00 32.88           O
ANISOU 1198  O   HOH A 247     4567   4787   3136   2369   -270    212       O
HETATM 1199  O   HOH A 248       6.302  22.155  -1.177  1.00 73.61           O
ANISOU 1199  O   HOH A 248    16031   6222   5715   -479   -590   1326       O
HETATM 1200  O   HOH A 249      17.245   8.802  16.381  1.00 30.47           O
ANISOU 1200  O   HOH A 249     4589   3358   3630    590   -319    436       O
HETATM 1201  O   HOH A 250       5.002  17.005  29.807  1.00 37.54           O
ANISOU 1201  O   HOH A 250     7550   4086   2626   -625    215   -165       O
HETATM 1202  O   HOH A 251      -2.811  20.272   1.661  1.00 24.70           O
ANISOU 1202  O   HOH A 251     2860   3127   3395  -1447   -359    272       O
HETATM 1203  O   HOH A 252      -1.146  18.377   1.015  1.00 26.35           O
ANISOU 1203  O   HOH A 252     3045   3119   3846    583   -619    -82       O
HETATM 1204  O   HOH A 253       0.638   7.618  -1.808  1.00 33.47           O
ANISOU 1204  O   HOH A 253     4695   4344   3677    257  -1707    669       O
HETATM 1205  O   HOH A 254       5.860  29.945  10.323  1.00 32.52           O
ANISOU 1205  O   HOH A 254     3148   3467   5738   -217    318    413       O
HETATM 1206  O   HOH A 255      -3.690   0.608  16.739  1.00 22.83           O
ANISOU 1206  O   HOH A 255     3214   2739   2721   -138    361     40       O
HETATM 1207  O   HOH A 256      18.607  17.084   2.489  1.00 38.30           O
ANISOU 1207  O   HOH A 256     4851   5853   3847   1546    787  -1594       O
HETATM 1208  O   HOH A 257      15.047  10.345   0.679  1.00 39.06           O
ANISOU 1208  O   HOH A 257     6570   3590   4680   1504   -973   -152       O
HETATM 1209  O   HOH A 258       9.275   3.019  -2.963  1.00 38.50           O
ANISOU 1209  O   HOH A 258     7283   3307   4039   1995    136    -90       O
HETATM 1210  O   HOH A 259      10.300  -5.164   9.436  1.00 38.86           O
ANISOU 1210  O   HOH A 259     8021   2966   3776     40   1279   -165       O
HETATM 1211  O   HOH A 260       5.099  -1.728  25.455  1.00 32.38           O
ANISOU 1211  O   HOH A 260     3578   4814   3908   1774    248   -464       O
HETATM 1212  O   HOH A 261      -1.958   7.967  -0.358  1.00 74.47           O
ANISOU 1212  O   HOH A 261    16725   5714   5856  -2121   1698   2236       O
HETATM 1213  O   HOH A 262      10.811  22.114  26.500  1.00121.38           O
ANISOU 1213  O   HOH A 262    33126   6421   6572   3830  -3305  -4837       O
HETATM 1214  O   HOH A 263       0.695   8.933  29.598  1.00 97.83           O
ANISOU 1214  O   HOH A 263    18179   7726  11263  -1801   4417   -743       O
HETATM 1215  O   HOH A 264      -9.397   3.985  20.554  1.00 23.85           O
ANISOU 1215  O   HOH A 264     3569   2148   3345    516    776    430       O
HETATM 1216  O   HOH A 265      12.781  10.270  31.413  1.00 67.67           O
ANISOU 1216  O   HOH A 265     9169   9196   7343   1117    703   -867       O
HETATM 1217  O   HOH A 266      11.713   6.309  -3.426  1.00 53.52           O
ANISOU 1217  O   HOH A 266     9414   6899   4020  -3125  -1081    611       O
HETATM 1218  O   HOH A 267       5.363   7.957  33.986  1.00 68.35           O
ANISOU 1218  O   HOH A 267     8014  10405   7551  -6666   2788  -6055       O
HETATM 1219  O   HOH A 268       1.951   3.744  19.548  1.00 36.37           O
ANISOU 1219  O   HOH A 268     4037   4908   4874    671   -203   1298       O
HETATM 1220  O   HOH A 269      -1.385  14.164  21.818  1.00 42.09           O
ANISOU 1220  O   HOH A 269     5110   5745   5135   -796   -649  -1497       O
HETATM 1221  O   HOH A 270      18.428  11.310  21.718  1.00 38.85           O
ANISOU 1221  O   HOH A 270     4288   4272   6200    224  -2144  -1155       O
HETATM 1222  O   HOH A 271      21.314  18.049   4.459  1.00 65.05           O
ANISOU 1222  O   HOH A 271     5517   2285  16913  -1134   7667   1480       O
HETATM 1223  O   HOH A 272       6.076  -2.389  22.817  1.00 39.30           O
ANISOU 1223  O   HOH A 272     5990   4577   4364    520  -1141   -786       O
HETATM 1224  O   HOH A 273      10.941   3.686  16.695  1.00 33.23           O
ANISOU 1224  O   HOH A 273     5099   3710   3813    493   -554    224       O
HETATM 1225  O   HOH A 274       7.948  30.665   8.504  1.00 50.10           O
ANISOU 1225  O   HOH A 274     5017   3309  10709  -1473  -1161    477       O
HETATM 1226  O   HOH A 275      -1.347   0.014  10.403  1.00 39.91           O
ANISOU 1226  O   HOH A 275     6508   5434   3219   1638   -377    151       O
HETATM 1227  O   HOH A 276       5.057  30.397   6.753  1.00 36.93           O
ANISOU 1227  O   HOH A 276     4666   5322   4043    450    542    924       O
HETATM 1228  O   HOH A 277       3.541  29.845   8.632  1.00 31.23           O
ANISOU 1228  O   HOH A 277     4203   3075   4585   -409  -1380    493       O
HETATM 1229  O   HOH A 278      16.824  -0.543  28.750  1.00 33.94           O
ANISOU 1229  O   HOH A 278     3959   5329   3604   2056    -82   -374       O
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.