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

elNémo ID: 2002141232585375

Job options:

ID        	=	 2002141232585375
JOBID     	=	 LIPID BINDING PROTEIN 12-MAY-11 3RZY
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    LIPID BINDING PROTEIN                   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 SER A   -1  VAL A    5  5                                   7    
HELIX    2   2 ASN A   15  GLY A   24  1                                  10    
HELIX    3   3 GLY A   26  ALA A   36  1                                  11    
SHEET    1   A10 THR A  60  PHE A  64  0                                        
SHEET    2   A10 VAL A  48  GLU A  54 -1  N  ILE A  49   O  PHE A  64           
SHEET    3   A10 ASN A  39  ASN A  45 -1  N  ASN A  39   O  GLU A  54           
SHEET    4   A10 GLY A   6  GLU A  14 -1  N  TRP A   8   O  MET A  40           
SHEET    5   A10 VAL A 122  ARG A 130 -1  O  VAL A 127   N  VAL A  11           
SHEET    6   A10 LYS A 112  MET A 119 -1  N  VAL A 115   O  ARG A 126           
SHEET    7   A10 LYS A 100  GLU A 109 -1  N  LYS A 105   O  GLU A 116           
SHEET    8   A10 VAL A  90  TRP A  97 -1  N  TRP A  97   O  LYS A 100           
SHEET    9   A10 LYS A  79  ASP A  87 -1  N  THR A  85   O  VAL A  92           
SHEET   10   A10 PHE A  70  VAL A  73 -1  N  PHE A  70   O  SER A  82           
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   GLN A  -7      -2.412  31.391  -8.556  1.00 43.64           N  
ANISOU    1  N   GLN A  -7     5542   5508   5530    114    -18     44       N  
ATOM      2  CA  GLN A  -7      -1.552  30.237  -8.137  1.00 43.33           C  
ANISOU    2  CA  GLN A  -7     5505   5435   5521     34     33     40       C  
ATOM      3  C   GLN A  -7      -0.932  29.485  -9.335  1.00 44.70           C  
ANISOU    3  C   GLN A  -7     5626   5633   5724    101    -27    -59       C  
ATOM      4  O   GLN A  -7      -1.519  29.456 -10.429  1.00 47.02           O  
ANISOU    4  O   GLN A  -7     5963   5934   5969     97    -87   -102       O  
ATOM      5  CB  GLN A  -7      -2.364  29.268  -7.252  1.00 37.43           C  
ANISOU    5  CB  GLN A  -7     4692   4648   4879    153   -149    -17       C  
ATOM      6  N   GLN A  -6       0.259  28.904  -9.116  1.00 44.05           N  
ANISOU    6  N   GLN A  -6     5533   5552   5649     29    -29    -91       N  
ATOM      7  CA  GLN A  -6       0.927  28.013 -10.097  1.00 41.51           C  
ANISOU    7  CA  GLN A  -6     5066   5255   5450    -51     11      2       C  
ATOM      8  C   GLN A  -6       1.343  26.732  -9.383  1.00 41.60           C  
ANISOU    8  C   GLN A  -6     5092   5228   5483    -43    -59    -28       C  
ATOM      9  O   GLN A  -6       1.406  26.701  -8.142  1.00 42.27           O  
ANISOU    9  O   GLN A  -6     5216   5217   5626   -104   -149   -124       O  
ATOM     10  CB  GLN A  -6       2.155  28.693 -10.732  1.00 36.99           C  
ANISOU   10  CB  GLN A  -6     4510   4790   4751     56    -53    -29       C  
ATOM     11  N   MET A  -5       1.613  25.674 -10.154  1.00 41.40           N  
ANISOU   11  N   MET A  -5     5045   5197   5486    -90   -120      0       N  
ATOM     12  CA  MET A  -5       2.048  24.397  -9.552  1.00 40.14           C  
ANISOU   12  CA  MET A  -5     4856   5072   5324    -89   -139     -3       C  
ATOM     13  C   MET A  -5       3.484  24.401  -9.061  1.00 40.23           C  
ANISOU   13  C   MET A  -5     4864   5114   5307    -14   -147     69       C  
ATOM     14  O   MET A  -5       4.411  24.677  -9.836  1.00 40.41           O  
ANISOU   14  O   MET A  -5     4653   5265   5435      0   -182    149       O  
ATOM     15  CB  MET A  -5       1.884  23.221 -10.516  1.00 40.28           C  
ANISOU   15  CB  MET A  -5     4879   5051   5373    -87   -137     27       C  
ATOM     16  CG  MET A  -5       1.903  21.894  -9.748  1.00 37.34           C  
ANISOU   16  CG  MET A  -5     4432   4659   5095   -326   -245   -219       C  
ATOM     17  SD  MET A  -5       1.239  20.424 -10.529  1.00 35.53           S  
ANISOU   17  SD  MET A  -5     3899   4404   5195  -1008    -37     23       S  
ATOM     18  CE  MET A  -5      -0.496  20.750 -10.654  1.00 25.54           C  
ANISOU   18  CE  MET A  -5     1386   4716   3601  -1120    240   -659       C  
ATOM     19  N   GLY A  -4       3.652  24.014  -7.796  1.00 39.38           N  
ANISOU   19  N   GLY A  -4     4693   5059   5209     16   -177     11       N  
ATOM     20  CA  GLY A  -4       4.979  23.858  -7.183  1.00 39.21           C  
ANISOU   20  CA  GLY A  -4     4675   5064   5159     56   -186     62       C  
ATOM     21  C   GLY A  -4       5.752  22.672  -7.762  1.00 38.66           C  
ANISOU   21  C   GLY A  -4     4609   4986   5094     14   -180     87       C  
ATOM     22  O   GLY A  -4       5.171  21.646  -8.159  1.00 37.75           O  
ANISOU   22  O   GLY A  -4     4319   5052   4971     30   -385     23       O  
ATOM     23  N   ARG A  -3       7.075  22.800  -7.791  1.00 38.01           N  
ANISOU   23  N   ARG A  -3     4543   4889   5008     36   -111    196       N  
ATOM     24  CA  ARG A  -3       7.910  21.679  -8.152  1.00 37.30           C  
ANISOU   24  CA  ARG A  -3     4576   4756   4839     58    -83    308       C  
ATOM     25  C   ARG A  -3       8.108  20.774  -6.926  1.00 35.15           C  
ANISOU   25  C   ARG A  -3     4232   4494   4627     93   -137    368       C  
ATOM     26  O   ARG A  -3       7.703  21.110  -5.800  1.00 34.80           O  
ANISOU   26  O   ARG A  -3     4154   4467   4599    255   -225    396       O  
ATOM     27  CB  ARG A  -3       9.259  22.127  -8.736  1.00 38.91           C  
ANISOU   27  CB  ARG A  -3     4773   4947   5064     14    -55    302       C  
ATOM     28  CG  ARG A  -3       9.237  22.297 -10.270  1.00 42.20           C  
ANISOU   28  CG  ARG A  -3     5307   5465   5258     20     46    276       C  
ATOM     29  CD  ARG A  -3       9.138  23.771 -10.679  1.00 47.54           C  
ANISOU   29  CD  ARG A  -3     6058   5913   6090    -90    176    270       C  
ATOM     30  NE  ARG A  -3      10.468  24.326 -10.958  1.00 50.65           N  
ANISOU   30  NE  ARG A  -3     6170   6593   6479   -196    213    144       N  
ATOM     31  CZ  ARG A  -3      10.964  24.606 -12.175  1.00 51.89           C  
ANISOU   31  CZ  ARG A  -3     6464   6773   6478   -109    271     25       C  
ATOM     32  NH1 ARG A  -3      12.198  25.097 -12.267  1.00 51.13           N  
ANISOU   32  NH1 ARG A  -3     6276   6721   6429    -65    404    -76       N  
ATOM     33  NH2 ARG A  -3      10.248  24.422 -13.300  1.00 52.83           N  
ANISOU   33  NH2 ARG A  -3     6711   6880   6480     30    321   -119       N  
ATOM     34  N   GLY A  -2       8.671  19.599  -7.184  1.00 32.38           N  
ANISOU   34  N   GLY A  -2     3847   4104   4350     -1   -141    503       N  
ATOM     35  CA  GLY A  -2       8.901  18.609  -6.139  1.00 29.55           C  
ANISOU   35  CA  GLY A  -2     3329   3829   4069   -100   -189    513       C  
ATOM     36  C   GLY A  -2      10.085  18.967  -5.257  1.00 27.98           C  
ANISOU   36  C   GLY A  -2     3023   3565   4040   -183   -153    662       C  
ATOM     37  O   GLY A  -2      10.833  19.944  -5.493  1.00 26.50           O  
ANISOU   37  O   GLY A  -2     2336   3488   4244   -192   -300    822       O  
ATOM     38  N   SER A  -1      10.245  18.144  -4.234  1.00 26.24           N  
ANISOU   38  N   SER A  -1     2808   3384   3777   -307      8    652       N  
ATOM     39  CA  SER A  -1      11.368  18.280  -3.357  1.00 26.22           C  
ANISOU   39  CA  SER A  -1     2848   3362   3752   -300     61    557       C  
ATOM     40  C   SER A  -1      11.804  16.916  -2.910  1.00 25.64           C  
ANISOU   40  C   SER A  -1     2594   3368   3779   -334     34    612       C  
ATOM     41  O   SER A  -1      11.180  15.870  -3.149  1.00 24.12           O  
ANISOU   41  O   SER A  -1     2236   3216   3712   -813     -7    978       O  
ATOM     42  CB  SER A  -1      11.022  19.165  -2.152  1.00 27.98           C  
ANISOU   42  CB  SER A  -1     3110   3554   3964   -287    170    564       C  
ATOM     43  OG  SER A  -1      10.131  18.507  -1.271  1.00 33.61           O  
ANISOU   43  OG  SER A  -1     3729   4290   4752   -244    655    446       O  
ATOM     44  N   MET A   0      12.916  16.931  -2.227  1.00 26.87           N  
ANISOU   44  N   MET A   0     2831   3380   3997   -217   -208    628       N  
ATOM     45  CA  MET A   0      13.487  15.683  -1.807  1.00 27.68           C  
ANISOU   45  CA  MET A   0     3025   3443   4049     33   -229    572       C  
ATOM     46  C   MET A   0      12.522  14.997  -0.809  1.00 28.14           C  
ANISOU   46  C   MET A   0     3273   3296   4123   -144   -263    646       C  
ATOM     47  O   MET A   0      12.389  13.751  -0.860  1.00 28.76           O  
ANISOU   47  O   MET A   0     3461   3007   4457   -334   -253    885       O  
ATOM     48  CB  MET A   0      14.901  15.984  -1.263  1.00 27.56           C  
ANISOU   48  CB  MET A   0     2764   3669   4035    138   -183    415       C  
ATOM     49  CG  MET A   0      16.024  14.906  -1.409  1.00 28.44           C  
ANISOU   49  CG  MET A   0     2921   3584   4301    999   -237    302       C  
ATOM     50  SD  MET A   0      16.799  14.505   0.185  1.00 40.60           S  
ANISOU   50  SD  MET A   0     4501   5525   5399    811   -216    195       S  
ATOM     51  CE  MET A   0      15.261  14.271   1.016  1.00 34.61           C  
ANISOU   51  CE  MET A   0     3426   5013   4708   2513    246   -237       C  
ATOM     52  N   CYS A   1      11.827  15.812   0.028  1.00 29.14           N  
ANISOU   52  N   CYS A   1     3692   3310   4067   -268    -97    679       N  
ATOM     53  CA  CYS A   1      10.737  15.453   0.958  1.00 31.06           C  
ANISOU   53  CA  CYS A   1     4021   3698   4080   -194    -93    508       C  
ATOM     54  C   CYS A   1       9.691  14.527   0.350  1.00 27.59           C  
ANISOU   54  C   CYS A   1     3658   3255   3569   -366    155    773       C  
ATOM     55  O   CYS A   1       9.003  13.796   1.071  1.00 27.03           O  
ANISOU   55  O   CYS A   1     4190   2647   3433   -344    516    930       O  
ATOM     56  CB  CYS A   1       9.981  16.727   1.371  1.00 33.26           C  
ANISOU   56  CB  CYS A   1     4275   4011   4349    -99    -97    517       C  
ATOM     57  SG  CYS A   1      10.888  17.987   2.247  1.00 44.59           S  
ANISOU   57  SG  CYS A   1     5716   5511   5713   -341   -429    250       S  
ATOM     58  N   ASP A   2       9.535  14.577  -0.969  1.00 25.35           N  
ANISOU   58  N   ASP A   2     3214   3156   3261   -452      5    900       N  
ATOM     59  CA  ASP A   2       8.553  13.755  -1.649  1.00 25.36           C  
ANISOU   59  CA  ASP A   2     3066   3291   3279   -472     11    840       C  
ATOM     60  C   ASP A   2       8.687  12.235  -1.462  1.00 22.68           C  
ANISOU   60  C   ASP A   2     2585   3185   2847   -521    157    806       C  
ATOM     61  O   ASP A   2       7.628  11.614  -1.453  1.00 22.07           O  
ANISOU   61  O   ASP A   2     2080   3429   2874   -647    142    857       O  
ATOM     62  CB  ASP A   2       8.373  14.175  -3.116  1.00 26.94           C  
ANISOU   62  CB  ASP A   2     3193   3535   3509   -549    -97    765       C  
ATOM     63  CG  ASP A   2       7.808  15.610  -3.260  1.00 30.54           C  
ANISOU   63  CG  ASP A   2     3340   4173   4089   -343   -351    885       C  
ATOM     64  OD1 ASP A   2       7.163  16.151  -2.331  1.00 36.86           O  
ANISOU   64  OD1 ASP A   2     3560   5321   5122   -352    560   1192       O  
ATOM     65  OD2 ASP A   2       8.112  16.231  -4.289  1.00 33.47           O  
ANISOU   65  OD2 ASP A   2     2830   5192   4694   -983   -759    980       O  
ATOM     66  N   ALA A   3       9.896  11.676  -1.231  1.00 20.43           N  
ANISOU   66  N   ALA A   3     2343   3059   2359   -539    327    768       N  
ATOM     67  CA  ALA A   3      10.068  10.261  -0.927  1.00 19.88           C  
ANISOU   67  CA  ALA A   3     2124   2984   2442   -150    372    334       C  
ATOM     68  C   ALA A   3       9.363   9.852   0.371  1.00 16.97           C  
ANISOU   68  C   ALA A   3     2139   2310   1995    -90    336    347       C  
ATOM     69  O   ALA A   3       9.046   8.679   0.536  1.00 17.02           O  
ANISOU   69  O   ALA A   3     2128   2051   2287    -42    670    -88       O  
ATOM     70  CB  ALA A   3      11.469   9.877  -0.846  1.00 21.64           C  
ANISOU   70  CB  ALA A   3     2232   3228   2760   -227    346    638       C  
ATOM     71  N   PHE A   4       9.082  10.812   1.258  1.00 13.27           N  
ANISOU   71  N   PHE A   4     1316   1718   2007   -207    136    209       N  
ATOM     72  CA  PHE A   4       8.348  10.510   2.482  1.00 12.33           C  
ANISOU   72  CA  PHE A   4     1528   1480   1675    -79    208    132       C  
ATOM     73  C   PHE A   4       6.863  10.566   2.352  1.00 10.70           C  
ANISOU   73  C   PHE A   4      966   1444   1655   -121    144     78       C  
ATOM     74  O   PHE A   4       6.168  10.024   3.187  1.00 12.85           O  
ANISOU   74  O   PHE A   4     1625   1594   1663   -137    149    245       O  
ATOM     75  CB  PHE A   4       8.761  11.492   3.585  1.00 13.15           C  
ANISOU   75  CB  PHE A   4     1182   1763   2051    -86     55     66       C  
ATOM     76  CG  PHE A   4      10.168  11.342   4.035  1.00 14.39           C  
ANISOU   76  CG  PHE A   4     1463   1961   2041     78     66    -91       C  
ATOM     77  CD1 PHE A   4      10.516  10.331   4.950  1.00 14.95           C  
ANISOU   77  CD1 PHE A   4     1338   2298   2043   -330   -281    117       C  
ATOM     78  CD2 PHE A   4      11.177  12.176   3.614  1.00 20.07           C  
ANISOU   78  CD2 PHE A   4     1723   2756   3146   -252   -343    451       C  
ATOM     79  CE1 PHE A   4      11.760  10.164   5.367  1.00 17.90           C  
ANISOU   79  CE1 PHE A   4     1831   3033   1938    -52   -128    212       C  
ATOM     80  CE2 PHE A   4      12.498  11.955   4.055  1.00 19.18           C  
ANISOU   80  CE2 PHE A   4     1711   2652   2925   -482    -44    445       C  
ATOM     81  CZ  PHE A   4      12.769  10.962   4.936  1.00 16.07           C  
ANISOU   81  CZ  PHE A   4     1331   2462   2313    -96   -119   -207       C  
ATOM     82  N   VAL A   5       6.379  11.299   1.378  1.00 12.11           N  
ANISOU   82  N   VAL A   5     1444   1558   1598   -149    140    146       N  
ATOM     83  CA  VAL A   5       4.942  11.548   1.295  1.00 12.70           C  
ANISOU   83  CA  VAL A   5     1599   1521   1702   -230    122    104       C  
ATOM     84  C   VAL A   5       4.206  10.266   1.000  1.00 12.61           C  
ANISOU   84  C   VAL A   5     1327   1644   1820   -279    -37   -134       C  
ATOM     85  O   VAL A   5       4.605   9.450   0.168  1.00 16.08           O  
ANISOU   85  O   VAL A   5     1996   1922   2189   -454    376   -447       O  
ATOM     86  CB  VAL A   5       4.673  12.604   0.245  1.00 13.97           C  
ANISOU   86  CB  VAL A   5     1389   1695   2222    -87   -158    164       C  
ATOM     87  CG1 VAL A   5       3.232  12.676  -0.179  1.00 18.31           C  
ANISOU   87  CG1 VAL A   5     2225   2147   2585   -177   -230    395       C  
ATOM     88  CG2 VAL A   5       5.171  13.996   0.792  1.00 15.83           C  
ANISOU   88  CG2 VAL A   5     2092   1618   2302   -376   -385     39       C  
ATOM     89  N   GLY A   6       3.098  10.098   1.688  1.00 12.81           N  
ANISOU   89  N   GLY A   6     1636   1623   1606   -351     49   -162       N  
ATOM     90  CA  GLY A   6       2.227   8.969   1.459  1.00 12.52           C  
ANISOU   90  CA  GLY A   6      918   1891   1947   -385    -24   -190       C  
ATOM     91  C   GLY A   6       1.613   8.471   2.711  1.00 11.96           C  
ANISOU   91  C   GLY A   6     1296   1711   1535   -264   -159    -99       C  
ATOM     92  O   GLY A   6       1.607   9.132   3.720  1.00 12.96           O  
ANISOU   92  O   GLY A   6     1563   1599   1761   -276    150   -121       O  
ATOM     93  N   THR A   7       1.028   7.294   2.594  1.00 11.53           N  
ANISOU   93  N   THR A   7      944   1752   1683   -165   -330    -51       N  
ATOM     94  CA  THR A   7       0.379   6.634   3.671  1.00 12.90           C  
ANISOU   94  CA  THR A   7     1382   1622   1898    -77   -116    -40       C  
ATOM     95  C   THR A   7       1.117   5.384   3.996  1.00 12.66           C  
ANISOU   95  C   THR A   7     1486   1505   1819   -103    -45    -14       C  
ATOM     96  O   THR A   7       1.355   4.544   3.121  1.00 14.04           O  
ANISOU   96  O   THR A   7     1642   1789   1902    124   -279   -153       O  
ATOM     97  CB  THR A   7      -1.057   6.253   3.228  1.00 14.12           C  
ANISOU   97  CB  THR A   7     1191   1637   2535    -60    -68    150       C  
ATOM     98  OG1 THR A   7      -1.708   7.398   2.659  1.00 20.97           O  
ANISOU   98  OG1 THR A   7     1574   2267   4126   -337   -609    414       O  
ATOM     99  CG2 THR A   7      -1.881   5.733   4.406  1.00 19.15           C  
ANISOU   99  CG2 THR A   7     1986   2402   2885   -588    187     23       C  
ATOM    100  N   TRP A   8       1.486   5.252   5.257  1.00 11.57           N  
ANISOU  100  N   TRP A   8     1214   1530   1651     36    143     -3       N  
ATOM    101  CA  TRP A   8       2.393   4.219   5.731  1.00 11.55           C  
ANISOU  101  CA  TRP A   8     1157   1543   1687     -2     41     53       C  
ATOM    102  C   TRP A   8       1.722   3.461   6.858  1.00 12.23           C  
ANISOU  102  C   TRP A   8     1448   1547   1652   -193    323     -3       C  
ATOM    103  O   TRP A   8       0.910   4.018   7.608  1.00 16.07           O  
ANISOU  103  O   TRP A   8     2366   1658   2080    -64    672     97       O  
ATOM    104  CB  TRP A   8       3.654   4.904   6.271  1.00 11.18           C  
ANISOU  104  CB  TRP A   8     1189   1537   1521      4     29    217       C  
ATOM    105  CG  TRP A   8       4.358   5.710   5.256  1.00 11.25           C  
ANISOU  105  CG  TRP A   8     1390   1501   1383    -48   -105     45       C  
ATOM    106  CD1 TRP A   8       4.254   7.047   5.041  1.00 11.89           C  
ANISOU  106  CD1 TRP A   8     1439   1516   1560   -109     52     49       C  
ATOM    107  CD2 TRP A   8       5.324   5.223   4.331  1.00 10.44           C  
ANISOU  107  CD2 TRP A   8      930   1437   1597     82     36     11       C  
ATOM    108  NE1 TRP A   8       5.115   7.425   4.024  1.00 11.71           N  
ANISOU  108  NE1 TRP A   8     1473   1279   1695   -152    116    104       N  
ATOM    109  CE2 TRP A   8       5.766   6.323   3.562  1.00 10.33           C  
ANISOU  109  CE2 TRP A   8      620   1673   1629   -179      4    -38       C  
ATOM    110  CE3 TRP A   8       5.854   3.962   4.076  1.00 11.16           C  
ANISOU  110  CE3 TRP A   8     1154   1595   1488    -53   -138   -154       C  
ATOM    111  CZ2 TRP A   8       6.746   6.173   2.581  1.00 11.98           C  
ANISOU  111  CZ2 TRP A   8     1001   1660   1889   -308    195     97       C  
ATOM    112  CZ3 TRP A   8       6.802   3.817   3.094  1.00 11.43           C  
ANISOU  112  CZ3 TRP A   8      894   1634   1813    154    -92   -217       C  
ATOM    113  CH2 TRP A   8       7.193   4.905   2.351  1.00 12.23           C  
ANISOU  113  CH2 TRP A   8      815   2044   1786   -135    254   -196       C  
ATOM    114  N   LYS A   9       2.025   2.184   6.981  1.00 11.25           N  
ANISOU  114  N   LYS A   9      983   1662   1627   -194     15    187       N  
ATOM    115  CA  LYS A   9       1.442   1.315   8.030  1.00 12.94           C  
ANISOU  115  CA  LYS A   9     1239   1878   1799   -190    -83    140       C  
ATOM    116  C   LYS A   9       2.553   0.632   8.767  1.00 11.13           C  
ANISOU  116  C   LYS A   9      682   1804   1740   -259    -99    117       C  
ATOM    117  O   LYS A   9       3.491   0.156   8.176  1.00 11.76           O  
ANISOU  117  O   LYS A   9     1190   1577   1701   -155     15    166       O  
ATOM    118  CB  LYS A   9       0.465   0.289   7.440  1.00 14.61           C  
ANISOU  118  CB  LYS A   9     1207   2218   2127   -332   -294    473       C  
ATOM    119  CG  LYS A   9       0.992  -0.662   6.446  1.00 23.00           C  
ANISOU  119  CG  LYS A   9     2633   3125   2981   -411    -40    290       C  
ATOM    120  CD  LYS A   9      -0.028  -1.672   5.997  1.00 28.81           C  
ANISOU  120  CD  LYS A   9     3402   3461   4083   -596   -190    -35       C  
ATOM    121  CE  LYS A   9       0.604  -2.625   5.026  1.00 31.40           C  
ANISOU  121  CE  LYS A   9     3959   3859   4110   -389     52    -76       C  
ATOM    122  NZ  LYS A   9       0.497  -2.153   3.594  1.00 35.42           N  
ANISOU  122  NZ  LYS A   9     4644   3925   4887    152   -194    626       N  
ATOM    123  N   LEU A  10       2.458   0.625  10.093  1.00 12.14           N  
ANISOU  123  N   LEU A  10      959   1942   1710   -165    -51    184       N  
ATOM    124  CA  LEU A  10       3.493  -0.019  10.918  1.00 11.39           C  
ANISOU  124  CA  LEU A  10      256   2116   1953    -80     10    165       C  
ATOM    125  C   LEU A  10       3.453  -1.505  10.679  1.00 13.02           C  
ANISOU  125  C   LEU A  10      922   1975   2048   -268   -250    359       C  
ATOM    126  O   LEU A  10       2.403  -2.132  10.857  1.00 15.99           O  
ANISOU  126  O   LEU A  10     1105   2240   2728   -540   -279    463       O  
ATOM    127  CB  LEU A  10       3.301   0.230  12.408  1.00 13.04           C  
ANISOU  127  CB  LEU A  10      777   2234   1944    -98     28    169       C  
ATOM    128  CG  LEU A  10       4.370  -0.303  13.326  1.00 13.75           C  
ANISOU  128  CG  LEU A  10      930   2319   1974    -40   -156    247       C  
ATOM    129  CD1 LEU A  10       5.594   0.446  13.181  1.00 15.21           C  
ANISOU  129  CD1 LEU A  10     1121   2682   1973   -238   -240    298       C  
ATOM    130  CD2 LEU A  10       3.888  -0.240  14.790  1.00 19.54           C  
ANISOU  130  CD2 LEU A  10     1977   3826   1620    437    -38    330       C  
ATOM    131  N   VAL A  11       4.616  -2.067  10.378  1.00 13.03           N  
ANISOU  131  N   VAL A  11     1386   1403   2161   -395   -453    216       N  
ATOM    132  CA  VAL A  11       4.782  -3.496  10.212  1.00 16.39           C  
ANISOU  132  CA  VAL A  11     2198   1659   2368   -318   -760    138       C  
ATOM    133  C   VAL A  11       5.677  -4.201  11.188  1.00 17.22           C  
ANISOU  133  C   VAL A  11     2414   1742   2387   -216   -773    264       C  
ATOM    134  O   VAL A  11       5.539  -5.421  11.334  1.00 21.12           O  
ANISOU  134  O   VAL A  11     3098   1740   3184   -410  -1310    472       O  
ATOM    135  CB  VAL A  11       5.214  -3.867   8.793  1.00 18.17           C  
ANISOU  135  CB  VAL A  11     2446   1785   2671     38   -577      5       C  
ATOM    136  CG1 VAL A  11       4.137  -3.482   7.798  1.00 21.56           C  
ANISOU  136  CG1 VAL A  11     2862   2462   2866   -373   -902    139       C  
ATOM    137  CG2 VAL A  11       6.628  -3.397   8.375  1.00 19.50           C  
ANISOU  137  CG2 VAL A  11     2554   2319   2535      8   -110   -172       C  
ATOM    138  N   SER A  12       6.596  -3.512  11.847  1.00 15.44           N  
ANISOU  138  N   SER A  12     2178   1517   2171    -89   -730    122       N  
ATOM    139  CA  SER A  12       7.450  -4.149  12.836  1.00 16.19           C  
ANISOU  139  CA  SER A  12     2257   1675   2219    -60   -610    186       C  
ATOM    140  C   SER A  12       7.975  -3.093  13.785  1.00 14.41           C  
ANISOU  140  C   SER A  12     1721   1647   2107   -210   -512    181       C  
ATOM    141  O   SER A  12       8.103  -1.921  13.446  1.00 12.55           O  
ANISOU  141  O   SER A  12     1269   1529   1968   -240   -168    355       O  
ATOM    142  CB  SER A  12       8.571  -4.907  12.195  1.00 19.50           C  
ANISOU  142  CB  SER A  12     2690   2191   2526     23   -650    138       C  
ATOM    143  OG  SER A  12       9.560  -4.114  11.649  1.00 21.77           O  
ANISOU  143  OG  SER A  12     3068   2474   2730    334   -450    365       O  
ATOM    144  N   SER A  13       8.284  -3.570  14.968  1.00 14.68           N  
ANISOU  144  N   SER A  13     1890   1616   2070   -490   -480    298       N  
ATOM    145  CA  SER A  13       8.802  -2.738  16.027  1.00 15.58           C  
ANISOU  145  CA  SER A  13     2175   1718   2027   -414   -474    298       C  
ATOM    146  C   SER A  13       9.759  -3.538  16.859  1.00 15.08           C  
ANISOU  146  C   SER A  13     2022   1818   1888   -336   -484    384       C  
ATOM    147  O   SER A  13       9.515  -4.727  17.172  1.00 18.26           O  
ANISOU  147  O   SER A  13     2522   1793   2622   -572   -719    624       O  
ATOM    148  CB  SER A  13       7.607  -2.227  16.852  1.00 17.57           C  
ANISOU  148  CB  SER A  13     2494   2051   2129   -580   -495     52       C  
ATOM    149  OG  SER A  13       7.970  -1.378  17.868  1.00 19.74           O  
ANISOU  149  OG  SER A  13     3011   2255   2233   -241   -643    182       O  
ATOM    150  N   GLU A  14      10.849  -2.925  17.241  1.00 13.15           N  
ANISOU  150  N   GLU A  14     1705   1474   1816   -149   -501     91       N  
ATOM    151  CA  GLU A  14      11.851  -3.540  18.119  1.00 14.05           C  
ANISOU  151  CA  GLU A  14     1739   1521   2075     68   -333     41       C  
ATOM    152  C   GLU A  14      12.217  -2.566  19.206  1.00 12.53           C  
ANISOU  152  C   GLU A  14     1606   1350   1803    110   -210     74       C  
ATOM    153  O   GLU A  14      12.516  -1.412  18.934  1.00 12.86           O  
ANISOU  153  O   GLU A  14     1684   1414   1788     12   -262    116       O  
ATOM    154  CB  GLU A  14      13.154  -3.934  17.356  1.00 16.70           C  
ANISOU  154  CB  GLU A  14     1988   1987   2368    194   -239   -243       C  
ATOM    155  CG  GLU A  14      12.959  -5.092  16.346  1.00 25.80           C  
ANISOU  155  CG  GLU A  14     3493   2729   3578    -19   -153   -406       C  
ATOM    156  CD  GLU A  14      12.831  -6.496  17.017  1.00 30.97           C  
ANISOU  156  CD  GLU A  14     4520   2897   4348   -244   -225   -425       C  
ATOM    157  OE1 GLU A  14      13.237  -6.685  18.188  1.00 36.18           O  
ANISOU  157  OE1 GLU A  14     4823   3895   5027    110   -954   -385       O  
ATOM    158  OE2 GLU A  14      12.308  -7.430  16.370  1.00 37.25           O  
ANISOU  158  OE2 GLU A  14     5758   3428   4967   -478    171  -1231       O  
ATOM    159  N  AASN A  15      12.348  -3.101  20.402  0.50 11.43           N  
ANISOU  159  N  AASN A  15     1374   1226   1741      0   -178    153       N  
ATOM    160  N  BASN A  15      12.062  -2.991  20.451  0.50 12.69           N  
ANISOU  160  N  BASN A  15     1593   1433   1796   -172   -198    225       N  
ATOM    161  CA AASN A  15      12.797  -2.348  21.564  0.50 10.51           C  
ANISOU  161  CA AASN A  15      898   1433   1660    -12   -225    113       C  
ATOM    162  CA BASN A  15      12.607  -2.304  21.640  0.50 13.44           C  
ANISOU  162  CA BASN A  15     1681   1582   1842    -73   -163    150       C  
ATOM    163  C  AASN A  15      11.946  -1.104  21.936  0.50  9.50           C  
ANISOU  163  C  AASN A  15      361   1616   1632      0   -227    153       C  
ATOM    164  C  BASN A  15      11.870  -1.091  22.043  0.50 11.97           C  
ANISOU  164  C  BASN A  15     1201   1656   1690    -91   -125    248       C  
ATOM    165  O  AASN A  15      12.417  -0.223  22.608  0.50 11.38           O  
ANISOU  165  O  AASN A  15     1003   1578   1741   -152   -173    -82       O  
ATOM    166  O  BASN A  15      12.324  -0.233  22.784  0.50 12.29           O  
ANISOU  166  O  BASN A  15     1294   1626   1748    -28   -128    189       O  
ATOM    167  CB AASN A  15      14.282  -2.002  21.428  0.50 10.67           C  
ANISOU  167  CB AASN A  15      936   1366   1751    180   -230     53       C  
ATOM    168  CB BASN A  15      14.067  -1.979  21.499  0.50 14.01           C  
ANISOU  168  CB BASN A  15     1722   1650   1948    -34    -27    165       C  
ATOM    169  CG AASN A  15      15.023  -2.043  22.739  0.50 10.32           C  
ANISOU  169  CG AASN A  15      638   1654   1627    -71   -350    342       C  
ATOM    170  CG BASN A  15      14.871  -3.172  21.329  0.50 18.50           C  
ANISOU  170  CG BASN A  15     2426   2370   2232    412     70     67       C  
ATOM    171  OD1AASN A  15      14.800  -2.965  23.551  0.50 12.17           O  
ANISOU  171  OD1AASN A  15      785   1880   1957   -131   -550    250       O  
ATOM    172  OD1BASN A  15      14.860  -4.037  22.177  0.50 21.45           O  
ANISOU  172  OD1BASN A  15     3279   2005   2866    690    341    172       O  
ATOM    173  ND2AASN A  15      15.870  -1.065  22.980  0.50 10.48           N  
ANISOU  173  ND2AASN A  15      760   1620   1600     75    -86    141       N  
ATOM    174  ND2BASN A  15      15.621  -3.243  20.256  0.50 21.18           N  
ANISOU  174  ND2BASN A  15     2599   3122   2325    599    226    208       N  
ATOM    175  N   PHE A  16      10.706  -1.023  21.514  1.00 11.12           N  
ANISOU  175  N   PHE A  16      922   1492   1810     -4   -200      4       N  
ATOM    176  CA  PHE A  16       9.815   0.153  21.754  1.00 11.45           C  
ANISOU  176  CA  PHE A  16      603   1777   1967     27   -166    104       C  
ATOM    177  C   PHE A  16       9.478   0.283  23.210  1.00 11.84           C  
ANISOU  177  C   PHE A  16      982   1605   1911    138    -70    114       C  
ATOM    178  O   PHE A  16       9.383   1.394  23.744  1.00 12.43           O  
ANISOU  178  O   PHE A  16     1657   1315   1751   -210    -89     18       O  
ATOM    179  CB  PHE A  16       8.641   0.141  20.827  1.00 12.75           C  
ANISOU  179  CB  PHE A  16      949   1779   2114    259    -34   -104       C  
ATOM    180  CG  PHE A  16       7.870   1.461  20.786  1.00 14.68           C  
ANISOU  180  CG  PHE A  16     1670   2368   1541     40   -116   -191       C  
ATOM    181  CD1 PHE A  16       8.470   2.628  20.480  1.00 14.47           C  
ANISOU  181  CD1 PHE A  16      808   2275   2413    278   -220    -63       C  
ATOM    182  CD2 PHE A  16       6.566   1.498  20.992  1.00 16.69           C  
ANISOU  182  CD2 PHE A  16     2050   2386   1905    377   -242   -256       C  
ATOM    183  CE1 PHE A  16       7.795   3.826  20.377  1.00 17.48           C  
ANISOU  183  CE1 PHE A  16     1961   2306   2375    691   -507   -169       C  
ATOM    184  CE2 PHE A  16       5.864   2.700  20.895  1.00 16.40           C  
ANISOU  184  CE2 PHE A  16     1599   2660   1968    544    -85     35       C  
ATOM    185  CZ  PHE A  16       6.496   3.848  20.629  1.00 17.21           C  
ANISOU  185  CZ  PHE A  16     2168   2253   2115   1036   -377   -103       C  
ATOM    186  N   ASP A  17       9.212  -0.829  23.885  1.00 12.98           N  
ANISOU  186  N   ASP A  17     1472   1425   2034   -254     62     88       N  
ATOM    187  CA  ASP A  17       8.880  -0.709  25.334  1.00 14.35           C  
ANISOU  187  CA  ASP A  17     1709   1758   1982   -198     91    231       C  
ATOM    188  C   ASP A  17      10.071  -0.135  26.136  1.00 12.58           C  
ANISOU  188  C   ASP A  17      980   1863   1937   -243     10    458       C  
ATOM    189  O   ASP A  17       9.868   0.751  26.951  1.00 14.02           O  
ANISOU  189  O   ASP A  17     1928   1674   1725   -349    150    135       O  
ATOM    190  CB  ASP A  17       8.448  -2.075  25.878  1.00 16.48           C  
ANISOU  190  CB  ASP A  17     1819   2018   2425   -161    111    369       C  
ATOM    191  CG  ASP A  17       7.882  -2.010  27.275  1.00 19.88           C  
ANISOU  191  CG  ASP A  17     2569   2362   2622   -346    174    545       C  
ATOM    192  OD1 ASP A  17       8.460  -2.637  28.165  1.00 26.47           O  
ANISOU  192  OD1 ASP A  17     2907   4078   3070    274   -145    917       O  
ATOM    193  OD2 ASP A  17       6.937  -1.291  27.526  1.00 22.04           O  
ANISOU  193  OD2 ASP A  17     2918   2741   2713    139    747    437       O  
ATOM    194  N   ASP A  18      11.271  -0.589  25.848  1.00 12.97           N  
ANISOU  194  N   ASP A  18     1133   1866   1926    -43    -20    340       N  
ATOM    195  CA  ASP A  18      12.466  -0.080  26.475  1.00 14.07           C  
ANISOU  195  CA  ASP A  18     1542   1886   1915     60   -159    331       C  
ATOM    196  C   ASP A  18      12.639   1.397  26.161  1.00 14.09           C  
ANISOU  196  C   ASP A  18     1733   1768   1851    129     28    152       C  
ATOM    197  O   ASP A  18      13.014   2.173  27.055  1.00 13.20           O  
ANISOU  197  O   ASP A  18     1303   1839   1873      5   -294    170       O  
ATOM    198  CB  ASP A  18      13.716  -0.892  26.128  1.00 16.75           C  
ANISOU  198  CB  ASP A  18     1786   2252   2325    252    -88    263       C  
ATOM    199  CG  ASP A  18      13.753  -2.248  26.857  1.00 25.08           C  
ANISOU  199  CG  ASP A  18     2687   3248   3593    224     17    526       C  
ATOM    200  OD1 ASP A  18      12.964  -2.495  27.766  1.00 31.89           O  
ANISOU  200  OD1 ASP A  18     3489   4099   4525    146   -218   1519       O  
ATOM    201  OD2 ASP A  18      14.695  -3.023  26.567  1.00 34.12           O  
ANISOU  201  OD2 ASP A  18     3690   3848   5424    780    -99    344       O  
ATOM    202  N   TYR A  19      12.388   1.808  24.922  1.00 12.02           N  
ANISOU  202  N   TYR A  19     1390   1573   1602      2    -24     49       N  
ATOM    203  CA  TYR A  19      12.498   3.236  24.581  1.00 10.86           C  
ANISOU  203  CA  TYR A  19      834   1609   1682   -118    -65     95       C  
ATOM    204  C   TYR A  19      11.478   4.036  25.381  1.00 10.49           C  
ANISOU  204  C   TYR A  19      794   1691   1498    123    -32    224       C  
ATOM    205  O   TYR A  19      11.825   5.054  25.981  1.00 11.43           O  
ANISOU  205  O   TYR A  19     1279   1573   1488   -173    -89     39       O  
ATOM    206  CB  TYR A  19      12.314   3.394  23.074  1.00 11.46           C  
ANISOU  206  CB  TYR A  19      944   1849   1560   -180   -109      1       C  
ATOM    207  CG  TYR A  19      12.048   4.873  22.665  1.00 10.68           C  
ANISOU  207  CG  TYR A  19      772   1788   1496   -441    -38    -61       C  
ATOM    208  CD1 TYR A  19      13.085   5.704  22.573  1.00 10.48           C  
ANISOU  208  CD1 TYR A  19      258   1930   1792     11    -89    -91       C  
ATOM    209  CD2 TYR A  19      10.832   5.338  22.425  1.00 11.53           C  
ANISOU  209  CD2 TYR A  19      615   2081   1684   -365   -237    172       C  
ATOM    210  CE1 TYR A  19      12.944   7.035  22.284  1.00 10.71           C  
ANISOU  210  CE1 TYR A  19      650   1714   1702   -448     41    -12       C  
ATOM    211  CE2 TYR A  19      10.640   6.670  22.110  1.00 12.43           C  
ANISOU  211  CE2 TYR A  19      728   2184   1808   -158   -183    237       C  
ATOM    212  CZ  TYR A  19      11.701   7.506  22.046  1.00 11.46           C  
ANISOU  212  CZ  TYR A  19      962   1880   1511   -322   -104    -14       C  
ATOM    213  OH  TYR A  19      11.495   8.860  21.725  1.00 13.37           O  
ANISOU  213  OH  TYR A  19     1621   1665   1794    -55   -195    215       O  
ATOM    214  N   MET A  20      10.250   3.582  25.426  1.00 10.30           N  
ANISOU  214  N   MET A  20      778   1668   1467   -141     24     23       N  
ATOM    215  CA  MET A  20       9.255   4.291  26.159  1.00 11.26           C  
ANISOU  215  CA  MET A  20     1216   1591   1471    -94     52     78       C  
ATOM    216  C   MET A  20       9.660   4.355  27.655  1.00 11.27           C  
ANISOU  216  C   MET A  20     1007   1728   1546   -278     -8     82       C  
ATOM    217  O   MET A  20       9.344   5.367  28.297  1.00 13.16           O  
ANISOU  217  O   MET A  20     1737   1675   1585   -298   -151    -75       O  
ATOM    218  CB  MET A  20       7.867   3.653  25.958  1.00 11.67           C  
ANISOU  218  CB  MET A  20     1200   1915   1317   -156     66     51       C  
ATOM    219  CG  MET A  20       7.283   3.911  24.613  1.00 12.38           C  
ANISOU  219  CG  MET A  20     1245   1714   1743    108    119     90       C  
ATOM    220  SD  MET A  20       5.535   3.414  24.515  1.00 14.72           S  
ANISOU  220  SD  MET A  20     1201   2554   1838   -155     32     15       S  
ATOM    221  CE  MET A  20       5.779   1.617  24.531  1.00 16.51           C  
ANISOU  221  CE  MET A  20     1347   2520   2405   -486     23   -142       C  
ATOM    222  N   LYS A  21      10.188   3.264  28.220  1.00 12.21           N  
ANISOU  222  N   LYS A  21     1302   1784   1553   -260     80    137       N  
ATOM    223  CA  LYS A  21      10.554   3.329  29.631  1.00 14.42           C  
ANISOU  223  CA  LYS A  21     1628   2237   1611   -118     82    180       C  
ATOM    224  C   LYS A  21      11.596   4.426  29.818  1.00 15.11           C  
ANISOU  224  C   LYS A  21     1825   2282   1634   -208   -118     78       C  
ATOM    225  O   LYS A  21      11.516   5.191  30.786  1.00 17.76           O  
ANISOU  225  O   LYS A  21     2526   2546   1676   -355   -205    -20       O  
ATOM    226  CB  LYS A  21      11.180   1.979  30.073  1.00 15.84           C  
ANISOU  226  CB  LYS A  21     1732   2491   1792   -110    -64    262       C  
ATOM    227  CG  LYS A  21      10.180   0.889  30.244  1.00 18.18           C  
ANISOU  227  CG  LYS A  21     1785   2903   2220   -266    -30    425       C  
ATOM    228  CD  LYS A  21      10.816  -0.351  30.866  1.00 20.41           C  
ANISOU  228  CD  LYS A  21     1817   3004   2932    278   -109    646       C  
ATOM    229  CE  LYS A  21       9.857  -1.374  31.196  1.00 26.64           C  
ANISOU  229  CE  LYS A  21     2549   3680   3893    225   -276    712       C  
ATOM    230  NZ  LYS A  21      10.432  -2.474  31.925  1.00 32.98           N  
ANISOU  230  NZ  LYS A  21     2764   4664   5101    868   -674    961       N  
ATOM    231  N   GLU A  22      12.591   4.508  28.903  1.00 14.62           N  
ANISOU  231  N   GLU A  22     1516   2398   1638   -270   -279    124       N  
ATOM    232  CA  GLU A  22      13.652   5.513  28.994  1.00 15.60           C  
ANISOU  232  CA  GLU A  22     1531   2426   1970   -319   -386    -35       C  
ATOM    233  C   GLU A  22      13.065   6.909  28.950  1.00 15.26           C  
ANISOU  233  C   GLU A  22     1931   2214   1651   -656   -403    -36       C  
ATOM    234  O   GLU A  22      13.540   7.813  29.641  1.00 18.05           O  
ANISOU  234  O   GLU A  22     2215   2788   1854   -768   -300   -155       O  
ATOM    235  CB  GLU A  22      14.782   5.177  27.972  1.00 15.11           C  
ANISOU  235  CB  GLU A  22     1010   2584   2146    -80   -196    109       C  
ATOM    236  CG  GLU A  22      16.088   5.582  28.238  1.00 19.18           C  
ANISOU  236  CG  GLU A  22      690   3391   3207    450   -253   -202       C  
ATOM    237  CD  GLU A  22      16.883   4.777  29.322  1.00 24.30           C  
ANISOU  237  CD  GLU A  22      441   4724   4067   -128   -845    324       C  
ATOM    238  OE1 GLU A  22      16.214   3.868  29.874  1.00 27.84           O  
ANISOU  238  OE1 GLU A  22     2308   4734   3534   -600   -378    183       O  
ATOM    239  OE2 GLU A  22      17.990   5.084  29.648  1.00 29.38           O  
ANISOU  239  OE2 GLU A  22     1714   5223   4223    167  -1027   -124       O  
ATOM    240  N   VAL A  23      12.059   7.118  28.100  1.00 14.16           N  
ANISOU  240  N   VAL A  23     1812   1861   1707   -505   -135     36       N  
ATOM    241  CA  VAL A  23      11.394   8.379  27.989  1.00 14.83           C  
ANISOU  241  CA  VAL A  23     2149   1880   1606   -623    -47    -27       C  
ATOM    242  C   VAL A  23      10.600   8.743  29.222  1.00 16.37           C  
ANISOU  242  C   VAL A  23     2442   1968   1808   -536   -121    -86       C  
ATOM    243  O   VAL A  23      10.406   9.908  29.495  1.00 20.26           O  
ANISOU  243  O   VAL A  23     3600   1961   2136   -581    512   -164       O  
ATOM    244  CB  VAL A  23      10.488   8.336  26.723  1.00 15.09           C  
ANISOU  244  CB  VAL A  23     1893   2051   1790   -198     53      1       C  
ATOM    245  CG1 VAL A  23       9.494   9.522  26.659  1.00 17.77           C  
ANISOU  245  CG1 VAL A  23     2749   1965   2038    -73   -218    -56       C  
ATOM    246  CG2 VAL A  23      11.331   8.309  25.463  1.00 17.28           C  
ANISOU  246  CG2 VAL A  23     2632   2099   1831   -289    126     35       C  
ATOM    247  N   GLY A  24      10.180   7.748  29.989  1.00 15.63           N  
ANISOU  247  N   GLY A  24     2417   1940   1581   -432     -1    -89       N  
ATOM    248  CA  GLY A  24       9.392   7.960  31.192  1.00 15.89           C  
ANISOU  248  CA  GLY A  24     2157   2116   1765   -411     27   -133       C  
ATOM    249  C   GLY A  24       7.912   7.662  31.085  1.00 14.91           C  
ANISOU  249  C   GLY A  24     2156   1925   1582   -366     33   -165       C  
ATOM    250  O   GLY A  24       7.117   8.032  31.953  1.00 16.74           O  
ANISOU  250  O   GLY A  24     2214   2352   1794   -377    140   -274       O  
ATOM    251  N   VAL A  25       7.491   6.936  30.074  1.00 13.35           N  
ANISOU  251  N   VAL A  25     1751   1705   1615   -359     99    -36       N  
ATOM    252  CA  VAL A  25       6.098   6.581  29.889  1.00 13.56           C  
ANISOU  252  CA  VAL A  25     1871   1607   1671   -315     36    -23       C  
ATOM    253  C   VAL A  25       5.711   5.514  30.940  1.00 13.65           C  
ANISOU  253  C   VAL A  25     1834   1730   1620   -247    149    -47       C  
ATOM    254  O   VAL A  25       6.441   4.569  31.173  1.00 14.96           O  
ANISOU  254  O   VAL A  25     2150   1820   1715   -343    -54    197       O  
ATOM    255  CB  VAL A  25       5.907   5.991  28.480  1.00 12.27           C  
ANISOU  255  CB  VAL A  25     1326   1673   1663   -319     88     88       C  
ATOM    256  CG1 VAL A  25       4.494   5.706  28.232  1.00 13.90           C  
ANISOU  256  CG1 VAL A  25     1666   1915   1697   -329    -33     45       C  
ATOM    257  CG2 VAL A  25       6.444   6.945  27.368  1.00 14.49           C  
ANISOU  257  CG2 VAL A  25     2276   1601   1626   -304      3    327       C  
ATOM    258  N   GLY A  26       4.550   5.735  31.545  1.00 15.59           N  
ANISOU  258  N   GLY A  26     2133   2092   1695   -475     98      4       N  
ATOM    259  CA  GLY A  26       4.015   4.847  32.553  1.00 15.64           C  
ANISOU  259  CA  GLY A  26     2044   2368   1529   -429    168   -143       C  
ATOM    260  C   GLY A  26       3.574   3.510  32.015  1.00 14.73           C  
ANISOU  260  C   GLY A  26     1878   2139   1577   -468    200     23       C  
ATOM    261  O   GLY A  26       3.300   3.335  30.855  1.00 14.41           O  
ANISOU  261  O   GLY A  26     1801   2234   1437   -606     34     45       O  
ATOM    262  N   PHE A  27       3.363   2.594  32.930  1.00 14.51           N  
ANISOU  262  N   PHE A  27     1842   2164   1506   -514   -110     36       N  
ATOM    263  CA  PHE A  27       3.059   1.236  32.594  1.00 14.40           C  
ANISOU  263  CA  PHE A  27     1683   2190   1596   -433     64     64       C  
ATOM    264  C   PHE A  27       1.845   1.105  31.673  1.00 13.30           C  
ANISOU  264  C   PHE A  27     1629   1802   1622   -353     16    228       C  
ATOM    265  O   PHE A  27       1.948   0.473  30.632  1.00 13.94           O  
ANISOU  265  O   PHE A  27     1852   1934   1508   -456    -22    142       O  
ATOM    266  CB  PHE A  27       2.799   0.427  33.894  1.00 15.05           C  
ANISOU  266  CB  PHE A  27     1678   2352   1688   -366   -110    209       C  
ATOM    267  CG  PHE A  27       2.426  -1.019  33.627  1.00 14.54           C  
ANISOU  267  CG  PHE A  27     1162   2650   1711   -520   -178    338       C  
ATOM    268  CD1 PHE A  27       3.394  -2.012  33.505  1.00 18.43           C  
ANISOU  268  CD1 PHE A  27     2514   2486   2001   -306    143    389       C  
ATOM    269  CD2 PHE A  27       1.148  -1.372  33.525  1.00 16.28           C  
ANISOU  269  CD2 PHE A  27     1611   2314   2257   -188   -338    770       C  
ATOM    270  CE1 PHE A  27       3.015  -3.345  33.252  1.00 20.45           C  
ANISOU  270  CE1 PHE A  27     2926   2611   2231   -204     88    582       C  
ATOM    271  CE2 PHE A  27       0.769  -2.685  33.256  1.00 17.95           C  
ANISOU  271  CE2 PHE A  27     2092   2557   2168   -577   -274    670       C  
ATOM    272  CZ  PHE A  27       1.690  -3.655  33.114  1.00 21.26           C  
ANISOU  272  CZ  PHE A  27     3084   2619   2372   -383   -398    219       C  
ATOM    273  N   ALA A  28       0.684   1.636  32.067  1.00 14.58           N  
ANISOU  273  N   ALA A  28     1816   2026   1696   -307     98     43       N  
ATOM    274  CA  ALA A  28      -0.535   1.396  31.297  1.00 14.11           C  
ANISOU  274  CA  ALA A  28     1463   1977   1920   -395    -78     85       C  
ATOM    275  C   ALA A  28      -0.428   2.002  29.931  1.00 13.46           C  
ANISOU  275  C   ALA A  28     1461   1708   1943   -300     -9     52       C  
ATOM    276  O   ALA A  28      -0.883   1.400  28.944  1.00 14.50           O  
ANISOU  276  O   ALA A  28     1291   2120   2095   -408   -217    141       O  
ATOM    277  CB  ALA A  28      -1.775   1.874  32.044  1.00 15.54           C  
ANISOU  277  CB  ALA A  28     1865   2046   1992   -113    280    134       C  
ATOM    278  N   THR A  29       0.121   3.193  29.823  1.00 14.14           N  
ANISOU  278  N   THR A  29     1786   1857   1727   -365   -161      0       N  
ATOM    279  CA  THR A  29       0.347   3.809  28.558  1.00 13.75           C  
ANISOU  279  CA  THR A  29     1615   1883   1725   -252   -149    195       C  
ATOM    280  C   THR A  29       1.305   2.983  27.700  1.00 13.37           C  
ANISOU  280  C   THR A  29     1555   1886   1636   -380   -103    132       C  
ATOM    281  O   THR A  29       1.008   2.814  26.501  1.00 14.22           O  
ANISOU  281  O   THR A  29     1769   2055   1577   -368   -159     38       O  
ATOM    282  CB  THR A  29       0.797   5.264  28.713  1.00 15.39           C  
ANISOU  282  CB  THR A  29     2079   1859   1907   -404   -225    152       C  
ATOM    283  OG1 THR A  29      -0.175   6.009  29.442  1.00 19.70           O  
ANISOU  283  OG1 THR A  29     2727   2182   2574   -136     86    114       O  
ATOM    284  CG2 THR A  29       1.029   5.957  27.356  1.00 17.26           C  
ANISOU  284  CG2 THR A  29     2248   2155   2155    -50   -332    312       C  
ATOM    285  N   ARG A  30       2.393   2.489  28.254  1.00 13.52           N  
ANISOU  285  N   ARG A  30     1777   1849   1508   -413   -327    198       N  
ATOM    286  CA  ARG A  30       3.274   1.673  27.457  1.00 13.10           C  
ANISOU  286  CA  ARG A  30     1525   2009   1441   -414    -78    146       C  
ATOM    287  C   ARG A  30       2.600   0.463  26.880  1.00 14.13           C  
ANISOU  287  C   ARG A  30     1732   2085   1552   -352   -178    184       C  
ATOM    288  O   ARG A  30       2.881   0.080  25.767  1.00 13.63           O  
ANISOU  288  O   ARG A  30     1471   2247   1459   -268    -29     96       O  
ATOM    289  CB  ARG A  30       4.553   1.195  28.222  1.00 14.51           C  
ANISOU  289  CB  ARG A  30     1785   2182   1546   -509   -215    243       C  
ATOM    290  CG  ARG A  30       5.516   2.259  28.594  1.00 14.28           C  
ANISOU  290  CG  ARG A  30     1707   2089   1629   -193     34    131       C  
ATOM    291  CD  ARG A  30       6.849   1.671  28.908  1.00 13.72           C  
ANISOU  291  CD  ARG A  30     1269   2226   1716    -58   -217    207       C  
ATOM    292  NE  ARG A  30       6.801   0.497  29.796  1.00 13.77           N  
ANISOU  292  NE  ARG A  30     1529   2022   1681   -175     15    127       N  
ATOM    293  CZ  ARG A  30       6.631   0.562  31.113  1.00 14.81           C  
ANISOU  293  CZ  ARG A  30     1670   2041   1917    -58    -15    147       C  
ATOM    294  NH1 ARG A  30       6.525   1.706  31.762  1.00 16.20           N  
ANISOU  294  NH1 ARG A  30     2584   1964   1607   -346    -11    418       N  
ATOM    295  NH2 ARG A  30       6.624  -0.587  31.808  1.00 16.65           N  
ANISOU  295  NH2 ARG A  30     2684   1927   1712   -108    249    197       N  
ATOM    296  N   LYS A  31       1.796  -0.208  27.711  1.00 12.99           N  
ANISOU  296  N   LYS A  31     1393   2053   1490   -415    -70     91       N  
ATOM    297  CA  LYS A  31       1.134  -1.409  27.255  1.00 13.24           C  
ANISOU  297  CA  LYS A  31     1430   1966   1634   -327      7     -1       C  
ATOM    298  C   LYS A  31       0.231  -1.138  26.103  1.00 13.02           C  
ANISOU  298  C   LYS A  31     1196   2066   1682   -238    101    -92       C  
ATOM    299  O   LYS A  31       0.231  -1.848  25.102  1.00 14.52           O  
ANISOU  299  O   LYS A  31     1392   2259   1865   -156    -72   -260       O  
ATOM    300  CB  LYS A  31       0.448  -2.131  28.375  1.00 14.09           C  
ANISOU  300  CB  LYS A  31     1232   2054   2066   -365     51     58       C  
ATOM    301  CG  LYS A  31       1.392  -2.651  29.438  1.00 17.34           C  
ANISOU  301  CG  LYS A  31     1934   2408   2246   -395    -68    146       C  
ATOM    302  CD  LYS A  31       2.312  -3.727  28.902  1.00 25.32           C  
ANISOU  302  CD  LYS A  31     3648   2894   3077    291    -96    297       C  
ATOM    303  CE  LYS A  31       3.440  -4.115  29.881  1.00 29.03           C  
ANISOU  303  CE  LYS A  31     3701   3851   3477    328    -74    -78       C  
ATOM    304  NZ  LYS A  31       4.750  -4.307  29.186  1.00 34.49           N  
ANISOU  304  NZ  LYS A  31     4191   4761   4152     17    140   -138       N  
ATOM    305  N   VAL A  32      -0.628  -0.151  26.271  1.00 12.24           N  
ANISOU  305  N   VAL A  32      952   2028   1670   -149      8   -115       N  
ATOM    306  CA  VAL A  32      -1.580   0.151  25.190  1.00 13.25           C  
ANISOU  306  CA  VAL A  32      873   2357   1802   -294     21   -242       C  
ATOM    307  C   VAL A  32      -0.901   0.740  23.975  1.00 12.89           C  
ANISOU  307  C   VAL A  32      926   2243   1726   -392      1    -87       C  
ATOM    308  O   VAL A  32      -1.263   0.424  22.836  1.00 13.60           O  
ANISOU  308  O   VAL A  32     1039   2409   1720   -266    -62   -168       O  
ATOM    309  CB  VAL A  32      -2.736   1.045  25.759  1.00 15.08           C  
ANISOU  309  CB  VAL A  32      980   2710   2038   -314   -143   -237       C  
ATOM    310  CG1 VAL A  32      -3.670   1.557  24.669  1.00 18.82           C  
ANISOU  310  CG1 VAL A  32     1397   3190   2561    285     96   -155       C  
ATOM    311  CG2 VAL A  32      -3.481   0.298  26.860  1.00 17.31           C  
ANISOU  311  CG2 VAL A  32      496   3309   2772   -121    468   -128       C  
ATOM    312  N   ALA A  33       0.022   1.641  24.170  1.00 12.67           N  
ANISOU  312  N   ALA A  33     1095   2064   1653   -177   -142      9       N  
ATOM    313  CA  ALA A  33       0.779   2.232  23.065  1.00 14.03           C  
ANISOU  313  CA  ALA A  33     1560   2192   1579   -340   -194    182       C  
ATOM    314  C   ALA A  33       1.525   1.186  22.304  1.00 13.54           C  
ANISOU  314  C   ALA A  33     1302   2256   1586   -298   -211    248       C  
ATOM    315  O   ALA A  33       1.684   1.246  21.091  1.00 15.22           O  
ANISOU  315  O   ALA A  33     1717   2450   1612   -200   -146    363       O  
ATOM    316  CB  ALA A  33       1.662   3.351  23.541  1.00 15.79           C  
ANISOU  316  CB  ALA A  33     1829   2284   1885   -533   -201    282       C  
ATOM    317  N   GLY A  34       2.132   0.242  23.017  1.00 14.68           N  
ANISOU  317  N   GLY A  34     1587   2471   1517     67    -35    213       N  
ATOM    318  CA  GLY A  34       2.913  -0.775  22.368  1.00 15.02           C  
ANISOU  318  CA  GLY A  34     1430   2536   1738    188    112    283       C  
ATOM    319  C   GLY A  34       2.096  -1.722  21.495  1.00 15.73           C  
ANISOU  319  C   GLY A  34     1884   2496   1594    226    338    239       C  
ATOM    320  O   GLY A  34       2.675  -2.274  20.578  1.00 18.00           O  
ANISOU  320  O   GLY A  34     1643   3151   2044    295    371   -132       O  
ATOM    321  N   MET A  35       0.804  -1.900  21.753  1.00 15.26           N  
ANISOU  321  N   MET A  35     1939   2131   1725     64    458    262       N  
ATOM    322  CA  MET A  35      -0.069  -2.689  20.903  1.00 14.85           C  
ANISOU  322  CA  MET A  35     1555   2039   2047     46    371    346       C  
ATOM    323  C   MET A  35      -0.427  -2.008  19.588  1.00 13.73           C  
ANISOU  323  C   MET A  35     1221   1909   2087    -85    428    310       C  
ATOM    324  O   MET A  35      -0.779  -2.689  18.636  1.00 16.83           O  
ANISOU  324  O   MET A  35     1797   2194   2403   -336   -165    395       O  
ATOM    325  CB  MET A  35      -1.369  -2.997  21.634  1.00 16.63           C  
ANISOU  325  CB  MET A  35     1850   2000   2466    -31    685    465       C  
ATOM    326  CG  MET A  35      -1.246  -3.961  22.751  1.00 16.95           C  
ANISOU  326  CG  MET A  35     2086   2117   2235    -58    658    111       C  
ATOM    327  SD  MET A  35      -0.732  -5.580  22.285  1.00 16.25           S  
ANISOU  327  SD  MET A  35     1938   1921   2313    117    280    326       S  
ATOM    328  CE  MET A  35      -2.161  -6.080  21.420  1.00 23.73           C  
ANISOU  328  CE  MET A  35     3877   2769   2368   -637   -984    509       C  
ATOM    329  N   ALA A  36      -0.338  -0.699  19.530  1.00 13.55           N  
ANISOU  329  N   ALA A  36     1196   1991   1959    -50    210    365       N  
ATOM    330  CA  ALA A  36      -0.926   0.008  18.402  1.00 13.64           C  
ANISOU  330  CA  ALA A  36      971   2216   1994   -114    158    447       C  
ATOM    331  C   ALA A  36      -0.099  -0.269  17.107  1.00 12.99           C  
ANISOU  331  C   ALA A  36      942   2031   1962   -390    -39    371       C  
ATOM    332  O   ALA A  36       1.107  -0.468  17.136  1.00 13.54           O  
ANISOU  332  O   ALA A  36      760   2449   1934   -246   -196    214       O  
ATOM    333  CB  ALA A  36      -0.946   1.477  18.674  1.00 16.15           C  
ANISOU  333  CB  ALA A  36     1654   2253   2229     72    304    282       C  
ATOM    334  N   LYS A  37      -0.871  -0.273  16.035  1.00 14.06           N  
ANISOU  334  N   LYS A  37     1096   2101   2145   -378    -41    403       N  
ATOM    335  CA  LYS A  37      -0.296  -0.454  14.694  1.00 15.89           C  
ANISOU  335  CA  LYS A  37     1896   2033   2107   -291     -1    120       C  
ATOM    336  C   LYS A  37      -0.729   0.721  13.853  1.00 14.40           C  
ANISOU  336  C   LYS A  37     1595   1992   1882   -380     13    240       C  
ATOM    337  O   LYS A  37      -1.609   0.638  13.047  1.00 15.79           O  
ANISOU  337  O   LYS A  37     1561   2306   2131   -373   -174    382       O  
ATOM    338  CB  LYS A  37      -0.730  -1.789  14.064  1.00 18.40           C  
ANISOU  338  CB  LYS A  37     2496   2084   2412   -294   -201    111       C  
ATOM    339  CG  LYS A  37      -0.159  -3.020  14.775  1.00 22.51           C  
ANISOU  339  CG  LYS A  37     2893   2498   3160   -422   -217     38       C  
ATOM    340  CD  LYS A  37       1.346  -3.071  14.573  1.00 28.39           C  
ANISOU  340  CD  LYS A  37     3558   3603   3625     80   -190    -26       C  
ATOM    341  CE  LYS A  37       1.889  -4.428  14.100  1.00 34.48           C  
ANISOU  341  CE  LYS A  37     4393   4145   4561      8     -5   -179       C  
ATOM    342  NZ  LYS A  37       1.737  -4.590  12.554  1.00 35.89           N  
ANISOU  342  NZ  LYS A  37     4821   4502   4313    -62    318    331       N  
ATOM    343  N   PRO A  38      -0.114   1.873  14.055  1.00 13.62           N  
ANISOU  343  N   PRO A  38     1519   1895   1760   -162    187    212       N  
ATOM    344  CA  PRO A  38      -0.643   3.070  13.444  1.00 15.49           C  
ANISOU  344  CA  PRO A  38     2145   1886   1854    -97    303    190       C  
ATOM    345  C   PRO A  38      -0.413   3.125  11.954  1.00 14.79           C  
ANISOU  345  C   PRO A  38     2147   1692   1778   -250    525     86       C  
ATOM    346  O   PRO A  38       0.467   2.510  11.402  1.00 14.92           O  
ANISOU  346  O   PRO A  38     1896   1881   1890   -145    531     72       O  
ATOM    347  CB  PRO A  38       0.166   4.191  14.101  1.00 16.65           C  
ANISOU  347  CB  PRO A  38     2362   1896   2067    -31    207     92       C  
ATOM    348  CG  PRO A  38       1.333   3.522  14.636  1.00 18.79           C  
ANISOU  348  CG  PRO A  38     2027   2350   2761   -552    -93     87       C  
ATOM    349  CD  PRO A  38       0.969   2.145  14.985  1.00 15.73           C  
ANISOU  349  CD  PRO A  38     2010   2091   1874   -233    220     -4       C  
ATOM    350  N   ASN A  39      -1.242   3.941  11.345  1.00 14.44           N  
ANISOU  350  N   ASN A  39     1866   1876   1741   -195    582    176       N  
ATOM    351  CA  ASN A  39      -1.010   4.495  10.013  1.00 15.84           C  
ANISOU  351  CA  ASN A  39     2301   1762   1955   -258    645     28       C  
ATOM    352  C   ASN A  39      -0.437   5.857  10.164  1.00 17.18           C  
ANISOU  352  C   ASN A  39     2932   1632   1962   -241    884    -96       C  
ATOM    353  O   ASN A  39      -0.897   6.662  10.947  1.00 21.94           O  
ANISOU  353  O   ASN A  39     3844   1862   2630   -517   1441   -194       O  
ATOM    354  CB  ASN A  39      -2.232   4.542   9.169  1.00 19.42           C  
ANISOU  354  CB  ASN A  39     2848   2143   2385     65    317     27       C  
ATOM    355  CG  ASN A  39      -2.499   3.241   8.466  1.00 23.88           C  
ANISOU  355  CG  ASN A  39     3125   2896   3051   -422   -128     49       C  
ATOM    356  OD1 ASN A  39      -2.080   2.168   8.893  1.00 30.08           O  
ANISOU  356  OD1 ASN A  39     4139   3301   3988   -431   -319   -119       O  
ATOM    357  ND2 ASN A  39      -3.129   3.359   7.315  1.00 30.82           N  
ANISOU  357  ND2 ASN A  39     2843   4939   3925    -99   -869    156       N  
ATOM    358  N   MET A  40       0.564   6.147   9.374  1.00 16.00           N  
ANISOU  358  N   MET A  40     2665   1590   1822   -220    619    -44       N  
ATOM    359  CA  MET A  40       1.186   7.430   9.373  1.00 15.69           C  
ANISOU  359  CA  MET A  40     2494   1582   1882   -191    543    -76       C  
ATOM    360  C   MET A  40       1.010   8.053   7.998  1.00 15.11           C  
ANISOU  360  C   MET A  40     2467   1547   1726    -78    459      6       C  
ATOM    361  O   MET A  40       1.378   7.436   7.006  1.00 15.71           O  
ANISOU  361  O   MET A  40     2607   1562   1799    187    493    134       O  
ATOM    362  CB  MET A  40       2.649   7.273   9.657  1.00 17.57           C  
ANISOU  362  CB  MET A  40     2812   1845   2018   -465    334     70       C  
ATOM    363  CG  MET A  40       3.392   8.554   9.657  1.00 19.44           C  
ANISOU  363  CG  MET A  40     2987   2075   2321   -500    266    -71       C  
ATOM    364  SD  MET A  40       5.065   8.423  10.170  1.00 25.01           S  
ANISOU  364  SD  MET A  40     3825   2304   3371   -613   -826    113       S  
ATOM    365  CE  MET A  40       5.603   7.016   9.287  1.00 25.84           C  
ANISOU  365  CE  MET A  40     2243   3592   3983   -360    362     50       C  
ATOM    366  N   ILE A  41       0.481   9.261   7.935  1.00 13.24           N  
ANISOU  366  N   ILE A  41     1807   1472   1751   -127    415    -17       N  
ATOM    367  CA  ILE A  41       0.229   9.940   6.696  1.00 13.24           C  
ANISOU  367  CA  ILE A  41     1577   1537   1915   -323    231   -104       C  
ATOM    368  C   ILE A  41       1.115  11.169   6.684  1.00 11.97           C  
ANISOU  368  C   ILE A  41     1518   1284   1745   -262     83    -42       C  
ATOM    369  O   ILE A  41       1.016  12.006   7.573  1.00 13.71           O  
ANISOU  369  O   ILE A  41     1956   1483   1768   -466    420    -80       O  
ATOM    370  CB  ILE A  41      -1.263  10.371   6.532  1.00 15.94           C  
ANISOU  370  CB  ILE A  41     1772   1847   2437   -349    193   -309       C  
ATOM    371  CG1 ILE A  41      -2.230   9.194   6.702  1.00 20.39           C  
ANISOU  371  CG1 ILE A  41     1643   2699   3404   -552    148   -392       C  
ATOM    372  CG2 ILE A  41      -1.479  11.067   5.217  1.00 22.15           C  
ANISOU  372  CG2 ILE A  41     2976   2443   2997   -247   -300   -142       C  
ATOM    373  CD1 ILE A  41      -3.668   9.677   7.062  1.00 27.77           C  
ANISOU  373  CD1 ILE A  41     1278   4197   5073   -893    617   -169       C  
ATOM    374  N   ILE A  42       1.974  11.272   5.690  1.00 10.65           N  
ANISOU  374  N   ILE A  42     1155   1391   1500   -136     14    -59       N  
ATOM    375  CA  ILE A  42       2.931  12.383   5.540  1.00  9.65           C  
ANISOU  375  CA  ILE A  42      778   1416   1471   -133     50     -2       C  
ATOM    376  C   ILE A  42       2.550  13.119   4.285  1.00 10.42           C  
ANISOU  376  C   ILE A  42      990   1456   1513   -259     28      5       C  
ATOM    377  O   ILE A  42       2.409  12.519   3.231  1.00 12.13           O  
ANISOU  377  O   ILE A  42     1692   1440   1474    -83    -90    -56       O  
ATOM    378  CB  ILE A  42       4.325  11.874   5.494  1.00 10.75           C  
ANISOU  378  CB  ILE A  42     1277   1464   1344   -145     84    -10       C  
ATOM    379  CG1 ILE A  42       4.696  11.081   6.779  1.00 11.43           C  
ANISOU  379  CG1 ILE A  42     1029   1631   1683    210    159    -47       C  
ATOM    380  CG2 ILE A  42       5.289  13.055   5.274  1.00 11.07           C  
ANISOU  380  CG2 ILE A  42      309   1894   2000    -90    164   -127       C  
ATOM    381  CD1 ILE A  42       6.044  10.526   6.808  1.00 13.86           C  
ANISOU  381  CD1 ILE A  42     1433   1989   1844    164    -99     62       C  
ATOM    382  N   SER A  43       2.336  14.424   4.404  1.00 10.68           N  
ANISOU  382  N   SER A  43     1232   1463   1360   -143   -106     36       N  
ATOM    383  CA  SER A  43       2.007  15.251   3.288  1.00 11.53           C  
ANISOU  383  CA  SER A  43     1302   1503   1574     27   -215     77       C  
ATOM    384  C   SER A  43       2.759  16.557   3.362  1.00 11.60           C  
ANISOU  384  C   SER A  43     1511   1397   1499     99   -114     16       C  
ATOM    385  O   SER A  43       3.277  16.952   4.416  1.00 11.32           O  
ANISOU  385  O   SER A  43     1631   1370   1300   -123    -28     57       O  
ATOM    386  CB  SER A  43       0.548  15.489   3.249  1.00 14.48           C  
ANISOU  386  CB  SER A  43     1436   1784   2280      4   -185    284       C  
ATOM    387  OG  SER A  43       0.097  16.150   4.372  1.00 18.94           O  
ANISOU  387  OG  SER A  43     2176   2509   2509    449   -261    172       O  
ATOM    388  N   VAL A  44       2.870  17.205   2.220  1.00 12.01           N  
ANISOU  388  N   VAL A  44     1825   1334   1403    -27   -293     67       N  
ATOM    389  CA  VAL A  44       3.557  18.471   2.094  1.00 12.10           C  
ANISOU  389  CA  VAL A  44     1552   1412   1632    -59   -357     94       C  
ATOM    390  C   VAL A  44       2.686  19.447   1.329  1.00 13.18           C  
ANISOU  390  C   VAL A  44     1797   1665   1546    -67   -355    180       C  
ATOM    391  O   VAL A  44       2.089  19.074   0.323  1.00 17.17           O  
ANISOU  391  O   VAL A  44     3168   1604   1750     64   -799     56       O  
ATOM    392  CB  VAL A  44       4.881  18.316   1.436  1.00 14.04           C  
ANISOU  392  CB  VAL A  44     1359   1793   2182     35     18    187       C  
ATOM    393  CG1 VAL A  44       5.633  19.673   1.459  1.00 19.80           C  
ANISOU  393  CG1 VAL A  44     2034   2014   3474   -296    114    251       C  
ATOM    394  CG2 VAL A  44       5.818  17.351   2.180  1.00 18.12           C  
ANISOU  394  CG2 VAL A  44     1910   2348   2623    -88   -346     17       C  
ATOM    395  N   ASN A  45       2.610  20.666   1.774  1.00 11.86           N  
ANISOU  395  N   ASN A  45     1450   1601   1454    -32   -281    105       N  
ATOM    396  CA  ASN A  45       1.881  21.763   1.050  1.00 11.91           C  
ANISOU  396  CA  ASN A  45     1256   1727   1540     34   -312    177       C  
ATOM    397  C   ASN A  45       2.773  22.977   1.213  1.00 11.53           C  
ANISOU  397  C   ASN A  45     1196   1633   1552    -36   -204    138       C  
ATOM    398  O   ASN A  45       2.876  23.530   2.287  1.00 11.86           O  
ANISOU  398  O   ASN A  45     1339   1626   1540    -22   -115    194       O  
ATOM    399  CB  ASN A  45       0.530  21.901   1.644  1.00 12.09           C  
ANISOU  399  CB  ASN A  45     1216   1655   1721   -120   -216     28       C  
ATOM    400  CG  ASN A  45      -0.357  22.930   0.948  1.00 12.82           C  
ANISOU  400  CG  ASN A  45     1495   1682   1692    185   -578     65       C  
ATOM    401  OD1 ASN A  45      -1.627  22.738   0.866  1.00 14.87           O  
ANISOU  401  OD1 ASN A  45     1648   2102   1898     -7   -426   -203       O  
ATOM    402  ND2 ASN A  45       0.226  23.950   0.478  1.00 12.31           N  
ANISOU  402  ND2 ASN A  45     1166   1508   2003     80   -470    340       N  
ATOM    403  N   GLY A  46       3.446  23.326   0.136  1.00 14.23           N  
ANISOU  403  N   GLY A  46     1963   1861   1581   -252   -267    211       N  
ATOM    404  CA  GLY A  46       4.402  24.404   0.220  1.00 15.84           C  
ANISOU  404  CA  GLY A  46     2128   2037   1852   -320    -88    301       C  
ATOM    405  C   GLY A  46       5.502  24.068   1.163  1.00 14.30           C  
ANISOU  405  C   GLY A  46     1621   2001   1809   -433     39    353       C  
ATOM    406  O   GLY A  46       6.122  23.028   1.027  1.00 17.38           O  
ANISOU  406  O   GLY A  46     2336   2091   2176   -177    235    146       O  
ATOM    407  N   ASP A  47       5.774  24.921   2.131  1.00 14.68           N  
ANISOU  407  N   ASP A  47     1776   1939   1861   -308     90    379       N  
ATOM    408  CA  ASP A  47       6.817  24.658   3.148  1.00 14.17           C  
ANISOU  408  CA  ASP A  47     1223   2129   2032    -81   -112    450       C  
ATOM    409  C   ASP A  47       6.322  23.867   4.335  1.00 11.18           C  
ANISOU  409  C   ASP A  47      639   1767   1839    -68   -131    216       C  
ATOM    410  O   ASP A  47       7.135  23.591   5.210  1.00 13.38           O  
ANISOU  410  O   ASP A  47      723   2299   2059      4    -28    249       O  
ATOM    411  CB  ASP A  47       7.343  25.997   3.667  1.00 18.17           C  
ANISOU  411  CB  ASP A  47     2276   2393   2234   -313   -263    482       C  
ATOM    412  CG  ASP A  47       8.007  26.816   2.626  1.00 23.43           C  
ANISOU  412  CG  ASP A  47     2491   3167   3243   -626   -282    331       C  
ATOM    413  OD1 ASP A  47       8.519  26.271   1.630  1.00 29.60           O  
ANISOU  413  OD1 ASP A  47     3180   4646   3418  -1110    959    714       O  
ATOM    414  OD2 ASP A  47       7.983  28.058   2.792  1.00 33.81           O  
ANISOU  414  OD2 ASP A  47     4692   3316   4836   -809   -175    544       O  
ATOM    415  N   VAL A  48       5.062  23.600   4.378  1.00 10.37           N  
ANISOU  415  N   VAL A  48      596   1708   1634     32   -251    179       N  
ATOM    416  CA  VAL A  48       4.490  22.950   5.564  1.00 10.27           C  
ANISOU  416  CA  VAL A  48      824   1548   1529    -48     21    148       C  
ATOM    417  C   VAL A  48       4.367  21.467   5.355  1.00 10.03           C  
ANISOU  417  C   VAL A  48      805   1613   1393    -73      8     17       C  
ATOM    418  O   VAL A  48       3.699  20.993   4.441  1.00 11.48           O  
ANISOU  418  O   VAL A  48     1279   1584   1499   -171   -312    125       O  
ATOM    419  CB  VAL A  48       3.067  23.532   5.907  1.00 13.12           C  
ANISOU  419  CB  VAL A  48     1556   1755   1673   -133     12    122       C  
ATOM    420  CG1 VAL A  48       2.473  22.899   7.140  1.00 14.29           C  
ANISOU  420  CG1 VAL A  48     1801   1816   1811     96    345    125       C  
ATOM    421  CG2 VAL A  48       3.129  25.079   6.058  1.00 14.85           C  
ANISOU  421  CG2 VAL A  48     1661   1719   2262    276    426     23       C  
ATOM    422  N   ILE A  49       4.962  20.740   6.273  1.00  9.35           N  
ANISOU  422  N   ILE A  49      773   1457   1319   -232    -40      7       N  
ATOM    423  CA  ILE A  49       4.908  19.264   6.299  1.00  9.13           C  
ANISOU  423  CA  ILE A  49      386   1670   1411   -218     14     10       C  
ATOM    424  C   ILE A  49       3.926  18.871   7.381  1.00  9.15           C  
ANISOU  424  C   ILE A  49      417   1657   1403    -38      0    123       C  
ATOM    425  O   ILE A  49       3.938  19.478   8.478  1.00 10.04           O  
ANISOU  425  O   ILE A  49      802   1553   1456   -193     72     -7       O  
ATOM    426  CB  ILE A  49       6.262  18.678   6.585  1.00 10.28           C  
ANISOU  426  CB  ILE A  49      294   1909   1701   -262     26    -94       C  
ATOM    427  CG1 ILE A  49       7.346  19.111   5.612  1.00 11.42           C  
ANISOU  427  CG1 ILE A  49      311   2112   1913   -324     93   -275       C  
ATOM    428  CG2 ILE A  49       6.221  17.151   6.716  1.00 12.76           C  
ANISOU  428  CG2 ILE A  49     1943   1285   1619      4   -247     44       C  
ATOM    429  CD1 ILE A  49       8.668  18.898   6.021  1.00 15.42           C  
ANISOU  429  CD1 ILE A  49      348   3171   2337   -484    198   -148       C  
ATOM    430  N   THR A  50       3.020  17.957   7.093  1.00  9.20           N  
ANISOU  430  N   THR A  50      277   1758   1461   -189     18     68       N  
ATOM    431  CA  THR A  50       2.108  17.387   8.078  1.00  9.80           C  
ANISOU  431  CA  THR A  50      647   1522   1553   -433    152    -74       C  
ATOM    432  C   THR A  50       2.394  15.922   8.240  1.00 10.23           C  
ANISOU  432  C   THR A  50      845   1527   1513   -237    147    -63       C  
ATOM    433  O   THR A  50       2.539  15.159   7.258  1.00 11.77           O  
ANISOU  433  O   THR A  50     1619   1439   1414   -318     57     12       O  
ATOM    434  CB  THR A  50       0.682  17.638   7.690  1.00 11.08           C  
ANISOU  434  CB  THR A  50      614   1734   1861   -463    146     19       C  
ATOM    435  OG1 THR A  50       0.447  19.079   7.591  1.00 13.34           O  
ANISOU  435  OG1 THR A  50      995   2114   1957    -41   -164     11       O  
ATOM    436  CG2 THR A  50      -0.251  17.093   8.677  1.00 13.98           C  
ANISOU  436  CG2 THR A  50      667   2192   2451   -286     90   -149       C  
ATOM    437  N   ILE A  51       2.512  15.480   9.492  1.00  9.93           N  
ANISOU  437  N   ILE A  51     1036   1306   1432   -218    149    -57       N  
ATOM    438  CA  ILE A  51       2.626  14.031   9.856  1.00  9.56           C  
ANISOU  438  CA  ILE A  51      387   1527   1715   -175    179    -75       C  
ATOM    439  C   ILE A  51       1.441  13.711  10.763  1.00 10.48           C  
ANISOU  439  C   ILE A  51      398   1723   1858      7    -82    -69       C  
ATOM    440  O   ILE A  51       1.307  14.265  11.858  1.00 12.16           O  
ANISOU  440  O   ILE A  51     1533   1499   1587   -130    204    -81       O  
ATOM    441  CB  ILE A  51       3.893  13.731  10.504  1.00 10.28           C  
ANISOU  441  CB  ILE A  51      288   1769   1847    -47    231    -30       C  
ATOM    442  CG1 ILE A  51       5.144  14.077   9.645  1.00 12.83           C  
ANISOU  442  CG1 ILE A  51     1338   1496   2040    -96     63   -315       C  
ATOM    443  CG2 ILE A  51       3.965  12.216  10.855  1.00 12.94           C  
ANISOU  443  CG2 ILE A  51     1326   1565   2023    -72     -2    204       C  
ATOM    444  CD1 ILE A  51       6.474  13.787  10.290  1.00 14.53           C  
ANISOU  444  CD1 ILE A  51      814   2183   2522    128    -74   -173       C  
ATOM    445  N   LYS A  52       0.519  12.902  10.269  1.00 11.88           N  
ANISOU  445  N   LYS A  52     1143   1777   1591   -171    337     21       N  
ATOM    446  CA  LYS A  52      -0.629  12.406  11.033  1.00 14.14           C  
ANISOU  446  CA  LYS A  52     1857   1604   1909   -240    497   -135       C  
ATOM    447  C   LYS A  52      -0.357  10.939  11.379  1.00 15.63           C  
ANISOU  447  C   LYS A  52     2252   1627   2060   -407    593   -246       C  
ATOM    448  O   LYS A  52       0.055  10.167  10.559  1.00 18.38           O  
ANISOU  448  O   LYS A  52     3297   1526   2159   -379   1072    -71       O  
ATOM    449  CB  LYS A  52      -1.864  12.568  10.152  1.00 17.35           C  
ANISOU  449  CB  LYS A  52     1925   2309   2358   -356    382   -238       C  
ATOM    450  CG  LYS A  52      -3.166  12.341  10.701  1.00 24.19           C  
ANISOU  450  CG  LYS A  52     2928   3147   3116   -174    256    340       C  
ATOM    451  CD  LYS A  52      -4.197  12.802   9.665  1.00 27.77           C  
ANISOU  451  CD  LYS A  52     2444   4149   3956    123   -573    294       C  
ATOM    452  CE  LYS A  52      -5.602  13.036  10.342  1.00 31.75           C  
ANISOU  452  CE  LYS A  52     2862   4591   4608    440   -375    276       C  
ATOM    453  NZ  LYS A  52      -6.849  13.285   9.473  1.00 34.11           N  
ANISOU  453  NZ  LYS A  52     1706   5584   5668    132   -472    236       N  
ATOM    454  N   SER A  53      -0.716  10.575  12.595  1.00 14.74           N  
ANISOU  454  N   SER A  53     2034   1565   2001   -389    744   -163       N  
ATOM    455  CA  SER A  53      -0.677   9.208  13.031  1.00 15.90           C  
ANISOU  455  CA  SER A  53     2053   1795   2191   -500    809    -37       C  
ATOM    456  C   SER A  53      -2.078   8.844  13.476  1.00 15.98           C  
ANISOU  456  C   SER A  53     2108   1858   2105   -427    842   -212       C  
ATOM    457  O   SER A  53      -2.675   9.502  14.325  1.00 19.24           O  
ANISOU  457  O   SER A  53     2866   1952   2490   -717   1203   -285       O  
ATOM    458  CB  SER A  53       0.273   9.036  14.172  1.00 17.74           C  
ANISOU  458  CB  SER A  53     2306   1885   2547   -207    674     65       C  
ATOM    459  OG  SER A  53       0.345   7.658  14.622  1.00 24.19           O  
ANISOU  459  OG  SER A  53     3775   2463   2951   -194    430    240       O  
ATOM    460  N   GLU A  54      -2.596   7.817  12.880  1.00 16.04           N  
ANISOU  460  N   GLU A  54     2028   1945   2119   -598    837   -166       N  
ATOM    461  CA  GLU A  54      -3.964   7.322  13.211  1.00 17.42           C  
ANISOU  461  CA  GLU A  54     2145   2137   2334   -369    672   -107       C  
ATOM    462  C   GLU A  54      -3.792   5.935  13.836  1.00 15.25           C  
ANISOU  462  C   GLU A  54     1763   1946   2084   -479    462    -34       C  
ATOM    463  O   GLU A  54      -3.231   5.045  13.213  1.00 15.00           O  
ANISOU  463  O   GLU A  54     1932   1849   1917   -163    459    180       O  
ATOM    464  CB  GLU A  54      -4.783   7.215  11.926  1.00 20.95           C  
ANISOU  464  CB  GLU A  54     2586   2546   2827   -276    523    147       C  
ATOM    465  CG  GLU A  54      -5.025   8.516  11.171  1.00 27.57           C  
ANISOU  465  CG  GLU A  54     3497   3478   3497   -194    331    297       C  
ATOM    466  CD  GLU A  54      -5.974   8.283  10.016  1.00 35.22           C  
ANISOU  466  CD  GLU A  54     4184   4875   4322    125    -66    165       C  
ATOM    467  OE1 GLU A  54      -5.685   7.398   9.147  1.00 35.72           O  
ANISOU  467  OE1 GLU A  54     4341   5170   4058    -57   -288   -142       O  
ATOM    468  OE2 GLU A  54      -7.015   8.982   9.981  1.00 42.05           O  
ANISOU  468  OE2 GLU A  54     4787   5532   5658    658    438    152       O  
ATOM    469  N   SER A  55      -4.259   5.732  15.064  1.00 15.58           N  
ANISOU  469  N   SER A  55     1322   2455   2141   -273    573   -118       N  
ATOM    470  CA  SER A  55      -4.204   4.393  15.695  1.00 16.83           C  
ANISOU  470  CA  SER A  55     1602   2600   2193    168    355    206       C  
ATOM    471  C   SER A  55      -5.309   4.256  16.666  1.00 16.08           C  
ANISOU  471  C   SER A  55     1594   2416   2099      3    457     90       C  
ATOM    472  O   SER A  55      -5.985   5.195  17.037  1.00 16.92           O  
ANISOU  472  O   SER A  55     1907   2026   2496    216    665    440       O  
ATOM    473  CB  SER A  55      -2.888   3.916  16.392  1.00 18.81           C  
ANISOU  473  CB  SER A  55     2051   2543   2551     21    359    223       C  
ATOM    474  OG  SER A  55      -2.693   4.472  17.668  1.00 17.25           O  
ANISOU  474  OG  SER A  55     1484   2955   2116     43     82    566       O  
ATOM    475  N   THR A  56      -5.409   3.057  17.137  1.00 16.75           N  
ANISOU  475  N   THR A  56     1920   2152   2292    245    131     74       N  
ATOM    476  CA  THR A  56      -6.383   2.766  18.155  1.00 17.51           C  
ANISOU  476  CA  THR A  56     2550   1973   2130   -235    213    171       C  
ATOM    477  C   THR A  56      -5.944   3.303  19.503  1.00 17.94           C  
ANISOU  477  C   THR A  56     2666   2045   2104   -459    453    179       C  
ATOM    478  O   THR A  56      -6.773   3.423  20.382  1.00 22.76           O  
ANISOU  478  O   THR A  56     3271   3151   2225   -877    972     60       O  
ATOM    479  CB  THR A  56      -6.538   1.214  18.314  1.00 19.92           C  
ANISOU  479  CB  THR A  56     2846   1970   2751   -206     59    -54       C  
ATOM    480  OG1 THR A  56      -5.225   0.639  18.466  1.00 26.36           O  
ANISOU  480  OG1 THR A  56     4423   2225   3368    572  -1359   -263       O  
ATOM    481  CG2 THR A  56      -7.196   0.629  17.088  1.00 21.06           C  
ANISOU  481  CG2 THR A  56     3209   2187   2603    -99   -585   -129       C  
ATOM    482  N   PHE A  57      -4.685   3.654  19.670  1.00 17.48           N  
ANISOU  482  N   PHE A  57     2755   2049   1834   -238    342    238       N  
ATOM    483  CA  PHE A  57      -4.240   4.252  20.917  1.00 18.10           C  
ANISOU  483  CA  PHE A  57     2766   2061   2050   -251    419    256       C  
ATOM    484  C   PHE A  57      -4.535   5.741  20.947  1.00 18.33           C  
ANISOU  484  C   PHE A  57     2551   2090   2323   -174    585    252       C  
ATOM    485  O   PHE A  57      -5.218   6.213  21.805  1.00 20.80           O  
ANISOU  485  O   PHE A  57     3040   2165   2695   -171    969    142       O  
ATOM    486  CB  PHE A  57      -2.746   3.935  21.120  1.00 19.31           C  
ANISOU  486  CB  PHE A  57     2995   2296   2043    -80    306    316       C  
ATOM    487  CG  PHE A  57      -2.057   4.763  22.158  1.00 22.51           C  
ANISOU  487  CG  PHE A  57     3329   2401   2821    -77     21    529       C  
ATOM    488  CD1 PHE A  57      -2.496   4.777  23.446  1.00 23.27           C  
ANISOU  488  CD1 PHE A  57     3552   2532   2756   -161    130    -86       C  
ATOM    489  CD2 PHE A  57      -0.956   5.534  21.829  1.00 22.95           C  
ANISOU  489  CD2 PHE A  57     3094   2533   3093    137    -55    356       C  
ATOM    490  CE1 PHE A  57      -1.869   5.576  24.409  1.00 23.71           C  
ANISOU  490  CE1 PHE A  57     2986   3003   3018   -199   -256     99       C  
ATOM    491  CE2 PHE A  57      -0.321   6.308  22.786  1.00 25.49           C  
ANISOU  491  CE2 PHE A  57     3522   2751   3411     30   -109    453       C  
ATOM    492  CZ  PHE A  57      -0.796   6.326  24.053  1.00 23.49           C  
ANISOU  492  CZ  PHE A  57     2904   2866   3154    210   -288    -27       C  
ATOM    493  N  ALYS A  58      -3.909   6.504  20.062  0.50 17.94           N  
ANISOU  493  N  ALYS A  58     2448   1969   2396     -6    750    306       N  
ATOM    494  N  BLYS A  58      -4.067   6.510  19.967  0.50 18.93           N  
ANISOU  494  N  BLYS A  58     2474   2150   2568    -77    750    309       N  
ATOM    495  CA ALYS A  58      -4.187   7.905  19.954  0.50 17.88           C  
ANISOU  495  CA ALYS A  58     2254   1941   2598    -49    625    175       C  
ATOM    496  CA BLYS A  58      -4.084   7.966  20.089  0.50 19.33           C  
ANISOU  496  CA BLYS A  58     2369   2199   2774   -112    596    187       C  
ATOM    497  C  ALYS A  58      -4.041   8.290  18.473  0.50 16.97           C  
ANISOU  497  C  ALYS A  58     1983   1836   2627   -187    778    178       C  
ATOM    498  C  BLYS A  58      -3.747   8.641  18.782  0.50 17.71           C  
ANISOU  498  C  BLYS A  58     1990   1986   2753   -209    881    229       C  
ATOM    499  O  ALYS A  58      -3.442   7.626  17.625  0.50 16.60           O  
ANISOU  499  O  ALYS A  58     2005   1588   2713   -108    828    220       O  
ATOM    500  O  BLYS A  58      -2.565   8.578  18.406  0.50 15.93           O  
ANISOU  500  O  BLYS A  58     1424   1773   2854      4    977    133       O  
ATOM    501  CB ALYS A  58      -3.231   8.673  20.899  0.50 18.83           C  
ANISOU  501  CB ALYS A  58     2133   2005   3015    -45    499    137       C  
ATOM    502  CB BLYS A  58      -2.974   8.372  21.061  0.50 21.59           C  
ANISOU  502  CB BLYS A  58     2557   2389   3257   -202    407    227       C  
ATOM    503  CG ALYS A  58      -3.461  10.147  21.142  0.50 21.21           C  
ANISOU  503  CG ALYS A  58     2778   2377   2904    -71    108    -59       C  
ATOM    504  CG BLYS A  58      -3.415   9.049  22.291  0.50 24.48           C  
ANISOU  504  CG BLYS A  58     2801   2987   3511   -361    173      9       C  
ATOM    505  CD ALYS A  58      -4.657  10.448  22.013  0.50 23.66           C  
ANISOU  505  CD ALYS A  58     2681   2975   3334   -227    -11   -159       C  
ATOM    506  CD BLYS A  58      -3.639  10.532  21.975  0.50 27.30           C  
ANISOU  506  CD BLYS A  58     3316   3393   3660    -57     94    138       C  
ATOM    507  CE ALYS A  58      -4.988  11.945  21.939  0.50 25.87           C  
ANISOU  507  CE ALYS A  58     3057   3143   3630     48    -13   -210       C  
ATOM    508  CE BLYS A  58      -4.346  11.280  23.107  0.50 29.86           C  
ANISOU  508  CE BLYS A  58     3776   3553   4016    -36     54    -88       C  
ATOM    509  NZ ALYS A  58      -6.456  12.284  22.077  0.50 28.07           N  
ANISOU  509  NZ ALYS A  58     3227   3295   4143    334     -5   -149       N  
ATOM    510  NZ BLYS A  58      -4.653  12.683  22.701  0.50 31.45           N  
ANISOU  510  NZ BLYS A  58     3824   3526   4596   -300    124   -115       N  
ATOM    511  N   ASN A  59      -4.719   9.336  18.151  1.00 15.87           N  
ANISOU  511  N   ASN A  59     1680   1824   2525   -163    918     78       N  
ATOM    512  CA  ASN A  59      -4.512  10.027  16.886  1.00 15.04           C  
ANISOU  512  CA  ASN A  59     1174   1946   2593   -456    795    -28       C  
ATOM    513  C   ASN A  59      -3.732  11.266  17.226  1.00 16.55           C  
ANISOU  513  C   ASN A  59     2141   1949   2198   -383    741   -118       C  
ATOM    514  O   ASN A  59      -4.061  11.993  18.169  1.00 20.32           O  
ANISOU  514  O   ASN A  59     2826   2179   2716   -433   1239   -327       O  
ATOM    515  CB  ASN A  59      -5.814  10.331  16.286  1.00 15.87           C  
ANISOU  515  CB  ASN A  59      758   2350   2921   -317    515    135       C  
ATOM    516  CG  ASN A  59      -6.655   9.109  16.008  1.00 19.81           C  
ANISOU  516  CG  ASN A  59     1740   2904   2880   -440    350    -86       C  
ATOM    517  OD1 ASN A  59      -6.154   8.136  15.466  1.00 17.92           O  
ANISOU  517  OD1 ASN A  59     1315   2584   2907   -125    295     48       O  
ATOM    518  ND2 ASN A  59      -7.956   9.142  16.386  1.00 25.48           N  
ANISOU  518  ND2 ASN A  59     1834   4276   3570   -207    722    174       N  
ATOM    519  N   THR A  60      -2.772  11.548  16.392  1.00 15.21           N  
ANISOU  519  N   THR A  60     2020   1762   1994   -282    574    -86       N  
ATOM    520  CA  THR A  60      -1.967  12.745  16.530  1.00 15.79           C  
ANISOU  520  CA  THR A  60     2128   1924   1944   -247    420     -1       C  
ATOM    521  C   THR A  60      -1.751  13.377  15.152  1.00 14.44           C  
ANISOU  521  C   THR A  60     1905   1737   1842   -132    575    -22       C  
ATOM    522  O   THR A  60      -1.825  12.715  14.136  1.00 13.68           O  
ANISOU  522  O   THR A  60     1778   1563   1854   -169    460      2       O  
ATOM    523  CB  THR A  60      -0.581  12.466  17.134  1.00 16.62           C  
ANISOU  523  CB  THR A  60     2311   1978   2025    -65    232     30       C  
ATOM    524  OG1 THR A  60       0.182  11.631  16.271  1.00 18.78           O  
ANISOU  524  OG1 THR A  60     2059   2425   2650     95    153    275       O  
ATOM    525  CG2 THR A  60      -0.670  11.890  18.528  1.00 21.58           C  
ANISOU  525  CG2 THR A  60     2972   2684   2542    -57    134    477       C  
ATOM    526  N   GLU A  61      -1.505  14.669  15.154  1.00 14.11           N  
ANISOU  526  N   GLU A  61     1975   1620   1764   -251    604   -129       N  
ATOM    527  CA  GLU A  61      -1.122  15.358  13.927  1.00 13.57           C  
ANISOU  527  CA  GLU A  61     1681   1686   1789   -263    291   -102       C  
ATOM    528  C   GLU A  61      -0.244  16.502  14.273  1.00 12.48           C  
ANISOU  528  C   GLU A  61     1531   1500   1709   -163    235   -166       C  
ATOM    529  O   GLU A  61      -0.573  17.279  15.179  1.00 14.50           O  
ANISOU  529  O   GLU A  61     1515   1835   2156   -343    467   -209       O  
ATOM    530  CB  GLU A  61      -2.394  15.881  13.253  1.00 16.23           C  
ANISOU  530  CB  GLU A  61     1860   2069   2236   -295    194    -23       C  
ATOM    531  CG  GLU A  61      -2.178  16.680  11.993  1.00 21.15           C  
ANISOU  531  CG  GLU A  61     2307   2877   2849   -562    -78    286       C  
ATOM    532  CD  GLU A  61      -3.512  17.246  11.441  1.00 28.90           C  
ANISOU  532  CD  GLU A  61     2627   4015   4339   -655   -107    681       C  
ATOM    533  OE1 GLU A  61      -3.465  18.376  10.884  1.00 35.98           O  
ANISOU  533  OE1 GLU A  61     4100   4327   5244   -859    163   1194       O  
ATOM    534  OE2 GLU A  61      -4.606  16.625  11.630  1.00 35.99           O  
ANISOU  534  OE2 GLU A  61     3378   5011   5283  -1258   -323    638       O  
ATOM    535  N   ILE A  62       0.863  16.621  13.542  1.00 11.39           N  
ANISOU  535  N   ILE A  62     1419   1437   1470   -185    219   -150       N  
ATOM    536  CA  ILE A  62       1.765  17.758  13.658  1.00 12.26           C  
ANISOU  536  CA  ILE A  62     1739   1439   1477   -452     82   -210       C  
ATOM    537  C   ILE A  62       1.916  18.399  12.278  1.00 11.51           C  
ANISOU  537  C   ILE A  62     1472   1437   1462   -224    269     57       C  
ATOM    538  O   ILE A  62       1.978  17.672  11.277  1.00 13.22           O  
ANISOU  538  O   ILE A  62     2258   1324   1439   -262    199    -39       O  
ATOM    539  CB  ILE A  62       3.120  17.410  14.316  1.00 12.22           C  
ANISOU  539  CB  ILE A  62     1588   1643   1412   -449     -9    -20       C  
ATOM    540  CG1 ILE A  62       3.879  16.364  13.541  1.00 13.93           C  
ANISOU  540  CG1 ILE A  62     1803   1816   1671   -418   -369    111       C  
ATOM    541  CG2 ILE A  62       2.856  16.966  15.763  1.00 17.05           C  
ANISOU  541  CG2 ILE A  62     2661   2118   1699   -240     35    173       C  
ATOM    542  CD1 ILE A  62       5.303  16.129  13.989  1.00 16.43           C  
ANISOU  542  CD1 ILE A  62     1900   2280   2060   -164   -485     16       C  
ATOM    543  N   SER A  63       2.009  19.696  12.246  1.00 10.11           N  
ANISOU  543  N   SER A  63      961   1490   1389   -121    113   -101       N  
ATOM    544  CA  SER A  63       2.341  20.457  11.051  1.00  9.60           C  
ANISOU  544  CA  SER A  63      633   1591   1423    -76     10    -28       C  
ATOM    545  C   SER A  63       3.494  21.380  11.411  1.00  9.51           C  
ANISOU  545  C   SER A  63      708   1358   1547     19     16      3       C  
ATOM    546  O   SER A  63       3.496  21.986  12.469  1.00 11.24           O  
ANISOU  546  O   SER A  63     1067   1515   1686   -281    268   -231       O  
ATOM    547  CB  SER A  63       1.178  21.238  10.481  1.00 11.53           C  
ANISOU  547  CB  SER A  63      955   1810   1616    -52    -87      1       C  
ATOM    548  OG  SER A  63       0.174  20.371  10.026  1.00 13.78           O  
ANISOU  548  OG  SER A  63     1019   2084   2130     70   -294   -168       O  
ATOM    549  N   PHE A  64       4.458  21.508  10.522  1.00  9.41           N  
ANISOU  549  N   PHE A  64      825   1429   1318    -34     36      7       N  
ATOM    550  CA  PHE A  64       5.690  22.217  10.844  1.00  8.59           C  
ANISOU  550  CA  PHE A  64      445   1343   1477   -109    -63    -28       C  
ATOM    551  C   PHE A  64       6.355  22.644   9.565  1.00  9.52           C  
ANISOU  551  C   PHE A  64      718   1398   1498     21    -50     83       C  
ATOM    552  O   PHE A  64       6.122  22.110   8.486  1.00  9.19           O  
ANISOU  552  O   PHE A  64      646   1445   1401   -134     21     39       O  
ATOM    553  CB  PHE A  64       6.556  21.361  11.734  1.00  9.97           C  
ANISOU  553  CB  PHE A  64      830   1505   1451   -287    -41     70       C  
ATOM    554  CG  PHE A  64       6.928  20.059  11.105  1.00  9.72           C  
ANISOU  554  CG  PHE A  64      313   1717   1663   -254   -170    117       C  
ATOM    555  CD1 PHE A  64       6.099  18.952  11.246  1.00 10.33           C  
ANISOU  555  CD1 PHE A  64      656   1730   1537   -108    -81     32       C  
ATOM    556  CD2 PHE A  64       8.051  19.930  10.397  1.00  9.46           C  
ANISOU  556  CD2 PHE A  64      259   1524   1811    -28    -93    148       C  
ATOM    557  CE1 PHE A  64       6.438  17.759  10.626  1.00 12.38           C  
ANISOU  557  CE1 PHE A  64     1420   1609   1674      9   -287     52       C  
ATOM    558  CE2 PHE A  64       8.322  18.736   9.742  1.00 11.52           C  
ANISOU  558  CE2 PHE A  64      907   1698   1772    210   -101    147       C  
ATOM    559  CZ  PHE A  64       7.518  17.659   9.873  1.00 12.47           C  
ANISOU  559  CZ  PHE A  64     1743   1512   1480     31   -194    -95       C  
ATOM    560  N   ILE A  65       7.318  23.560   9.765  1.00  9.34           N  
ANISOU  560  N   ILE A  65      485   1673   1388    -47    120   -100       N  
ATOM    561  CA  ILE A  65       8.259  23.977   8.768  1.00  9.74           C  
ANISOU  561  CA  ILE A  65      769   1380   1552     30    198    -53       C  
ATOM    562  C   ILE A  65       9.628  23.541   9.224  1.00  8.95           C  
ANISOU  562  C   ILE A  65      390   1381   1629     96    291    294       C  
ATOM    563  O   ILE A  65       9.964  23.673  10.408  1.00  9.40           O  
ANISOU  563  O   ILE A  65      767   1336   1467     33     19     54       O  
ATOM    564  CB  ILE A  65       8.193  25.528   8.572  1.00 11.09           C  
ANISOU  564  CB  ILE A  65     1181   1310   1720     15   -127     23       C  
ATOM    565  CG1 ILE A  65       6.756  25.874   8.049  1.00 13.66           C  
ANISOU  565  CG1 ILE A  65     1582   1504   2102   -159    -59    320       C  
ATOM    566  CG2 ILE A  65       9.211  26.016   7.632  1.00 10.60           C  
ANISOU  566  CG2 ILE A  65      515   1613   1900    -18     55    248       C  
ATOM    567  CD1 ILE A  65       6.385  27.348   7.960  1.00 15.62           C  
ANISOU  567  CD1 ILE A  65     1183   1786   2963    133   -250    220       C  
ATOM    568  N   LEU A  66      10.455  22.996   8.341  1.00  8.70           N  
ANISOU  568  N   LEU A  66      314   1492   1497   -239    124     62       N  
ATOM    569  CA  LEU A  66      11.755  22.548   8.698  1.00  9.23           C  
ANISOU  569  CA  LEU A  66      276   1591   1637    -72    153    173       C  
ATOM    570  C   LEU A  66      12.563  23.631   9.350  1.00  9.48           C  
ANISOU  570  C   LEU A  66      532   1442   1625   -132   -130    175       C  
ATOM    571  O   LEU A  66      12.595  24.762   8.880  1.00 10.79           O  
ANISOU  571  O   LEU A  66      641   1606   1850    -74     28    229       O  
ATOM    572  CB  LEU A  66      12.489  21.981   7.454  1.00 10.83           C  
ANISOU  572  CB  LEU A  66      723   1596   1793     83    241     50       C  
ATOM    573  CG  LEU A  66      11.864  20.698   6.839  1.00 11.11           C  
ANISOU  573  CG  LEU A  66      297   1900   2023    224    121   -232       C  
ATOM    574  CD1 LEU A  66      12.644  20.503   5.484  1.00 17.28           C  
ANISOU  574  CD1 LEU A  66     2122   2244   2198    546    447   -350       C  
ATOM    575  CD2 LEU A  66      12.020  19.513   7.753  1.00 14.07           C  
ANISOU  575  CD2 LEU A  66     1664   1582   2098     10      4    138       C  
ATOM    576  N   GLY A  67      13.206  23.291  10.437  1.00 10.14           N  
ANISOU  576  N   GLY A  67      791   1356   1706    -58     30    116       N  
ATOM    577  CA  GLY A  67      14.066  24.184  11.186  1.00 10.36           C  
ANISOU  577  CA  GLY A  67      671   1612   1651     19     89     68       C  
ATOM    578  C   GLY A  67      13.371  25.109  12.150  1.00  9.51           C  
ANISOU  578  C   GLY A  67      298   1514   1800   -187     39    143       C  
ATOM    579  O   GLY A  67      14.102  25.853  12.848  1.00 11.51           O  
ANISOU  579  O   GLY A  67      820   1604   1945   -223   -149    -42       O  
ATOM    580  N   GLN A  68      12.084  25.075  12.204  1.00  9.12           N  
ANISOU  580  N   GLN A  68      763   1170   1532   -243     10    -14       N  
ATOM    581  CA  GLN A  68      11.294  26.061  12.958  1.00  9.94           C  
ANISOU  581  CA  GLN A  68      731   1329   1715   -154    -33    -40       C  
ATOM    582  C   GLN A  68      10.587  25.383  14.141  1.00  9.62           C  
ANISOU  582  C   GLN A  68      370   1529   1756   -133    -76    -34       C  
ATOM    583  O   GLN A  68       9.689  24.544  13.935  1.00  9.84           O  
ANISOU  583  O   GLN A  68      535   1431   1770    -57     32    -64       O  
ATOM    584  CB  GLN A  68      10.285  26.784  12.049  1.00  9.87           C  
ANISOU  584  CB  GLN A  68      619   1321   1809    -20    -99    -37       C  
ATOM    585  CG  GLN A  68      11.045  27.490  10.982  1.00 14.08           C  
ANISOU  585  CG  GLN A  68     1777   1642   1931   -376   -527    177       C  
ATOM    586  CD  GLN A  68      10.278  28.429  10.198  1.00 15.74           C  
ANISOU  586  CD  GLN A  68     1680   1644   2652   -229   -541    300       C  
ATOM    587  OE1 GLN A  68       9.093  28.745  10.440  1.00 20.04           O  
ANISOU  587  OE1 GLN A  68     2006   2137   3470    261  -1144    242       O  
ATOM    588  NE2 GLN A  68      11.046  28.998   9.202  1.00 18.02           N  
ANISOU  588  NE2 GLN A  68     2535   1822   2489   -202   -567    593       N  
ATOM    589  N  AGLU A  69      10.967  25.716  15.350  0.50  9.83           N  
ANISOU  589  N  AGLU A  69      783   1214   1737   -191     70     -4       N  
ATOM    590  N  BGLU A  69      10.994  25.732  15.357  0.50 10.33           N  
ANISOU  590  N  BGLU A  69      790   1340   1795   -173     35     27       N  
ATOM    591  CA AGLU A  69      10.487  24.970  16.510  0.50 10.43           C  
ANISOU  591  CA AGLU A  69     1109   1277   1574   -168     27    -32       C  
ATOM    592  CA BGLU A  69      10.495  25.137  16.620  0.50 11.74           C  
ANISOU  592  CA BGLU A  69     1091   1564   1806    -82     25     31       C  
ATOM    593  C  AGLU A  69       9.008  25.192  16.716  0.50 10.53           C  
ANISOU  593  C  AGLU A  69     1213   1300   1486     14    156      7       C  
ATOM    594  C  BGLU A  69       8.999  25.209  16.709  0.50 11.04           C  
ANISOU  594  C  BGLU A  69     1190   1439   1562      8    142     52       C  
ATOM    595  O  AGLU A  69       8.441  26.253  16.375  0.50 10.88           O  
ANISOU  595  O  AGLU A  69     1081   1146   1905     70    -22     78       O  
ATOM    596  O  BGLU A  69       8.418  26.244  16.345  0.50 10.98           O  
ANISOU  596  O  BGLU A  69     1038   1202   1929     67    -53     76       O  
ATOM    597  CB AGLU A  69      11.330  25.363  17.733  0.50 11.52           C  
ANISOU  597  CB AGLU A  69     1334   1407   1634    -69      9     68       C  
ATOM    598  CB BGLU A  69      11.041  25.942  17.839  0.50 13.04           C  
ANISOU  598  CB BGLU A  69      977   2165   1809   -227   -116    281       C  
ATOM    599  CG AGLU A  69      10.813  24.990  19.184  0.50 14.44           C  
ANISOU  599  CG AGLU A  69     1842   1933   1712     32   -300     70       C  
ATOM    600  CG BGLU A  69      10.630  27.393  17.833  0.50 18.44           C  
ANISOU  600  CG BGLU A  69     1484   2710   2812   -158    -81   -134       C  
ATOM    601  CD AGLU A  69      11.613  25.666  20.296  0.50 21.60           C  
ANISOU  601  CD AGLU A  69     2356   3275   2575     88   -666    -44       C  
ATOM    602  CD BGLU A  69      10.715  28.140  19.197  0.50 21.69           C  
ANISOU  602  CD BGLU A  69     1466   3286   3486    463   -551   -137       C  
ATOM    603  OE1AGLU A  69      11.475  26.878  20.515  0.50 27.77           O  
ANISOU  603  OE1AGLU A  69     3750   3527   3275   -300   -727    -81       O  
ATOM    604  OE1BGLU A  69       9.869  29.081  19.469  0.50 25.12           O  
ANISOU  604  OE1BGLU A  69     2326   3405   3813    542    130   -433       O  
ATOM    605  OE2AGLU A  69      12.410  24.976  20.919  0.50 24.81           O  
ANISOU  605  OE2AGLU A  69      687   4833   3903    204  -1027   -146       O  
ATOM    606  OE2BGLU A  69      11.643  27.785  19.958  0.50 24.07           O  
ANISOU  606  OE2BGLU A  69     2238   3286   3620   -119  -1167    418       O  
ATOM    607  N   PHE A  70       8.346  24.191  17.280  1.00  9.18           N  
ANISOU  607  N   PHE A  70      741   1208   1540    196     94    -29       N  
ATOM    608  CA  PHE A  70       6.970  24.189  17.547  1.00  9.47           C  
ANISOU  608  CA  PHE A  70      688   1235   1673    219    263      0       C  
ATOM    609  C   PHE A  70       6.679  23.396  18.829  1.00 11.06           C  
ANISOU  609  C   PHE A  70     1209   1345   1646    248    310    -78       C  
ATOM    610  O   PHE A  70       7.473  22.623  19.320  1.00 12.67           O  
ANISOU  610  O   PHE A  70     1498   1706   1609    545    221    136       O  
ATOM    611  CB  PHE A  70       6.149  23.632  16.352  1.00 10.95           C  
ANISOU  611  CB  PHE A  70     1202   1368   1589     60    254     42       C  
ATOM    612  CG  PHE A  70       6.494  22.221  15.991  1.00 10.34           C  
ANISOU  612  CG  PHE A  70      535   1642   1751      7     54    179       C  
ATOM    613  CD1 PHE A  70       7.585  21.902  15.205  1.00  9.61           C  
ANISOU  613  CD1 PHE A  70      663   1397   1590     20      0      5       C  
ATOM    614  CD2 PHE A  70       5.713  21.194  16.429  1.00 12.76           C  
ANISOU  614  CD2 PHE A  70     1408   1466   1972     15    297    -67       C  
ATOM    615  CE1 PHE A  70       7.906  20.604  14.864  1.00 10.76           C  
ANISOU  615  CE1 PHE A  70     1085   1540   1462   -179    -11     -2       C  
ATOM    616  CE2 PHE A  70       6.031  19.886  16.079  1.00 12.77           C  
ANISOU  616  CE2 PHE A  70      912   1807   2133   -400    298     37       C  
ATOM    617  CZ  PHE A  70       7.082  19.608  15.310  1.00 11.27           C  
ANISOU  617  CZ  PHE A  70     1048   1556   1677     35    -20   -136       C  
ATOM    618  N   ASP A  71       5.497  23.649  19.368  1.00 12.91           N  
ANISOU  618  N   ASP A  71     1551   1446   1909    276    536    275       N  
ATOM    619  CA  ASP A  71       4.918  22.880  20.503  1.00 15.38           C  
ANISOU  619  CA  ASP A  71     2009   1859   1973    338    684     47       C  
ATOM    620  C   ASP A  71       4.206  21.675  20.061  1.00 14.37           C  
ANISOU  620  C   ASP A  71     1589   1960   1909    214    504    199       C  
ATOM    621  O   ASP A  71       3.457  21.700  19.053  1.00 16.28           O  
ANISOU  621  O   ASP A  71     1465   2238   2481    221    352    630       O  
ATOM    622  CB  ASP A  71       3.801  23.713  21.192  1.00 16.76           C  
ANISOU  622  CB  ASP A  71     1993   2207   2165    516    731     70       C  
ATOM    623  CG  ASP A  71       4.289  24.934  21.745  1.00 19.92           C  
ANISOU  623  CG  ASP A  71     2585   2713   2268    390     41     35       C  
ATOM    624  OD1 ASP A  71       5.274  24.816  22.484  1.00 21.57           O  
ANISOU  624  OD1 ASP A  71     2825   2963   2407    709   -292    109       O  
ATOM    625  OD2 ASP A  71       3.666  26.031  21.527  1.00 21.12           O  
ANISOU  625  OD2 ASP A  71     2473   2922   2630    619   -161   -198       O  
ATOM    626  N   GLU A  72       4.443  20.581  20.766  1.00 13.72           N  
ANISOU  626  N   GLU A  72     1399   1877   1934     83    304    370       N  
ATOM    627  CA  GLU A  72       3.859  19.302  20.414  1.00 16.20           C  
ANISOU  627  CA  GLU A  72     1915   2085   2155    -46    260    459       C  
ATOM    628  C   GLU A  72       3.366  18.645  21.732  1.00 15.24           C  
ANISOU  628  C   GLU A  72     1529   2112   2148    -39    381    473       C  
ATOM    629  O   GLU A  72       4.047  18.705  22.728  1.00 18.04           O  
ANISOU  629  O   GLU A  72     2019   2700   2133   -223    310    597       O  
ATOM    630  CB  GLU A  72       4.893  18.400  19.675  1.00 16.12           C  
ANISOU  630  CB  GLU A  72     2191   2024   1907    -76    334    298       C  
ATOM    631  CG  GLU A  72       4.522  17.000  19.397  1.00 18.42           C  
ANISOU  631  CG  GLU A  72     2478   2318   2201    -29    124    494       C  
ATOM    632  CD  GLU A  72       5.531  16.155  18.680  1.00 19.96           C  
ANISOU  632  CD  GLU A  72     3414   2232   1935    -96    448    348       C  
ATOM    633  OE1 GLU A  72       6.714  16.551  18.606  1.00 19.20           O  
ANISOU  633  OE1 GLU A  72     2949   1951   2393    -54    603     59       O  
ATOM    634  OE2 GLU A  72       5.163  15.017  18.237  1.00 22.86           O  
ANISOU  634  OE2 GLU A  72     3543   2446   2694     91    233    -14       O  
ATOM    635  N   VAL A  73       2.181  18.094  21.713  1.00 15.73           N  
ANISOU  635  N   VAL A  73     1586   2134   2255     67    269    634       N  
ATOM    636  CA  VAL A  73       1.726  17.210  22.808  1.00 16.39           C  
ANISOU  636  CA  VAL A  73     1592   2239   2394     38    424    432       C  
ATOM    637  C   VAL A  73       1.818  15.822  22.216  1.00 16.13           C  
ANISOU  637  C   VAL A  73     1839   2127   2160    -35    281    536       C  
ATOM    638  O   VAL A  73       1.118  15.491  21.272  1.00 17.60           O  
ANISOU  638  O   VAL A  73     1985   2258   2444    -52      6    575       O  
ATOM    639  CB  VAL A  73       0.373  17.563  23.285  1.00 18.95           C  
ANISOU  639  CB  VAL A  73     2059   2401   2740    190    646    387       C  
ATOM    640  CG1 VAL A  73      -0.134  16.571  24.346  1.00 20.25           C  
ANISOU  640  CG1 VAL A  73     1267   3221   3204    152    789    524       C  
ATOM    641  CG2 VAL A  73       0.400  19.030  23.852  1.00 20.40           C  
ANISOU  641  CG2 VAL A  73     1484   2696   3570    164    995    116       C  
ATOM    642  N   THR A  74       2.688  14.999  22.748  1.00 15.35           N  
ANISOU  642  N   THR A  74     1527   2119   2185    -25    228    459       N  
ATOM    643  CA  THR A  74       3.000  13.687  22.173  1.00 16.76           C  
ANISOU  643  CA  THR A  74     1956   2227   2185   -211    289    496       C  
ATOM    644  C   THR A  74       1.879  12.685  22.510  1.00 17.14           C  
ANISOU  644  C   THR A  74     1721   2345   2445    -62    194    526       C  
ATOM    645  O   THR A  74       1.010  12.932  23.332  1.00 18.32           O  
ANISOU  645  O   THR A  74     1908   2366   2683   -180    366    592       O  
ATOM    646  CB  THR A  74       4.340  13.152  22.678  1.00 16.03           C  
ANISOU  646  CB  THR A  74     1810   2334   1946    -89     58    384       C  
ATOM    647  OG1 THR A  74       4.159  12.883  24.063  1.00 17.17           O  
ANISOU  647  OG1 THR A  74     2030   2444   2049    101    227    333       O  
ATOM    648  CG2 THR A  74       5.423  14.164  22.412  1.00 17.06           C  
ANISOU  648  CG2 THR A  74     2044   2177   2260   -156    345    489       C  
ATOM    649  N   ALA A  75       1.917  11.535  21.841  1.00 17.54           N  
ANISOU  649  N   ALA A  75     1738   2259   2666   -315    159    419       N  
ATOM    650  CA  ALA A  75       0.875  10.529  22.030  1.00 20.13           C  
ANISOU  650  CA  ALA A  75     2236   2475   2938   -415    144    465       C  
ATOM    651  C   ALA A  75       0.805  10.119  23.491  1.00 20.19           C  
ANISOU  651  C   ALA A  75     2185   2472   3012   -715    151    629       C  
ATOM    652  O   ALA A  75      -0.286   9.785  23.986  1.00 23.24           O  
ANISOU  652  O   ALA A  75     2215   2950   3664   -751    290    647       O  
ATOM    653  CB  ALA A  75       1.119   9.289  21.105  1.00 21.38           C  
ANISOU  653  CB  ALA A  75     2453   2559   3109   -398    192    490       C  
ATOM    654  N   ASP A  76       1.928  10.059  24.165  1.00 20.58           N  
ANISOU  654  N   ASP A  76     2597   2526   2695   -320    255    645       N  
ATOM    655  CA  ASP A  76       1.976   9.684  25.588  1.00 21.51           C  
ANISOU  655  CA  ASP A  76     2883   2660   2627   -215    273    689       C  
ATOM    656  C   ASP A  76       1.799  10.884  26.528  1.00 22.93           C  
ANISOU  656  C   ASP A  76     3091   2944   2676   -155    551    639       C  
ATOM    657  O   ASP A  76       2.034  10.785  27.730  1.00 26.28           O  
ANISOU  657  O   ASP A  76     3719   3580   2685     60    446    589       O  
ATOM    658  CB  ASP A  76       3.287   8.977  25.925  1.00 21.36           C  
ANISOU  658  CB  ASP A  76     2808   2448   2858   -261    246    732       C  
ATOM    659  CG  ASP A  76       4.506   9.834  25.609  1.00 20.41           C  
ANISOU  659  CG  ASP A  76     2454   2493   2806    -50    -35    858       C  
ATOM    660  OD1 ASP A  76       4.682  10.253  24.434  1.00 19.45           O  
ANISOU  660  OD1 ASP A  76     1921   2661   2806     51     68    826       O  
ATOM    661  OD2 ASP A  76       5.305  10.098  26.520  1.00 20.29           O  
ANISOU  661  OD2 ASP A  76     2710   2209   2789   -180     74    675       O  
ATOM    662  N   ASP A  77       1.344  12.005  25.988  1.00 22.44           N  
ANISOU  662  N   ASP A  77     3051   2865   2610   -239    743    627       N  
ATOM    663  CA  ASP A  77       0.994  13.196  26.741  1.00 23.58           C  
ANISOU  663  CA  ASP A  77     2953   3249   2758   -157    813    447       C  
ATOM    664  C   ASP A  77       2.121  14.032  27.343  1.00 23.25           C  
ANISOU  664  C   ASP A  77     3118   3155   2562    -76    782    316       C  
ATOM    665  O   ASP A  77       1.884  14.758  28.327  1.00 26.28           O  
ANISOU  665  O   ASP A  77     3216   3753   3014   -112   1131     83       O  
ATOM    666  CB  ASP A  77      -0.074  12.904  27.808  1.00 25.22           C  
ANISOU  666  CB  ASP A  77     3095   3484   3003   -312    882    415       C  
ATOM    667  CG  ASP A  77      -1.044  14.027  27.936  1.00 31.44           C  
ANISOU  667  CG  ASP A  77     3527   4665   3751    -54   1058    458       C  
ATOM    668  OD1 ASP A  77      -1.584  14.204  29.058  1.00 39.25           O  
ANISOU  668  OD1 ASP A  77     4903   5940   4067   -339   1582    580       O  
ATOM    669  OD2 ASP A  77      -1.271  14.760  26.930  1.00 39.60           O  
ANISOU  669  OD2 ASP A  77     4542   5937   4567   -182   1088    933       O  
ATOM    670  N   ARG A  78       3.320  13.987  26.759  1.00 19.75           N  
ANISOU  670  N   ARG A  78     2783   2548   2173     46    779    411       N  
ATOM    671  CA  ARG A  78       4.342  14.975  27.092  1.00 17.82           C  
ANISOU  671  CA  ARG A  78     2557   2311   1903    195    553    329       C  
ATOM    672  C   ARG A  78       4.135  16.246  26.293  1.00 16.17           C  
ANISOU  672  C   ARG A  78     2095   2226   1820    157    723    318       C  
ATOM    673  O   ARG A  78       3.779  16.192  25.115  1.00 17.98           O  
ANISOU  673  O   ARG A  78     2411   2252   2169    200    465    301       O  
ATOM    674  CB  ARG A  78       5.704  14.454  26.748  1.00 17.88           C  
ANISOU  674  CB  ARG A  78     2625   2101   2066    163    416    264       C  
ATOM    675  CG  ARG A  78       6.205  13.364  27.670  1.00 17.43           C  
ANISOU  675  CG  ARG A  78     2511   2118   1992    314    268    351       C  
ATOM    676  CD  ARG A  78       7.481  12.770  27.103  1.00 16.89           C  
ANISOU  676  CD  ARG A  78     2185   2196   2036     88    -42    308       C  
ATOM    677  NE  ARG A  78       7.226  11.966  25.932  1.00 16.40           N  
ANISOU  677  NE  ARG A  78     1902   2062   2267    337     94    314       N  
ATOM    678  CZ  ARG A  78       7.848  12.026  24.752  1.00 16.94           C  
ANISOU  678  CZ  ARG A  78     2155   2085   2194     31    100    194       C  
ATOM    679  NH1 ARG A  78       8.935  12.784  24.545  1.00 15.61           N  
ANISOU  679  NH1 ARG A  78     1757   2246   1926    196    195    156       N  
ATOM    680  NH2 ARG A  78       7.383  11.244  23.778  1.00 17.49           N  
ANISOU  680  NH2 ARG A  78     2291   2054   2299     11    130     10       N  
ATOM    681  N   LYS A  79       4.357  17.370  26.939  1.00 17.04           N  
ANISOU  681  N   LYS A  79     2266   2358   1850    244    558    211       N  
ATOM    682  CA  LYS A  79       4.380  18.674  26.294  1.00 17.05           C  
ANISOU  682  CA  LYS A  79     2154   2304   2018    423    473    148       C  
ATOM    683  C   LYS A  79       5.812  18.987  25.986  1.00 16.79           C  
ANISOU  683  C   LYS A  79     2245   2210   1923    196    485     16       C  
ATOM    684  O   LYS A  79       6.578  19.214  26.888  1.00 19.10           O  
ANISOU  684  O   LYS A  79     2849   2631   1778    172    549   -105       O  
ATOM    685  CB  LYS A  79       3.765  19.716  27.222  1.00 19.69           C  
ANISOU  685  CB  LYS A  79     2591   2502   2388    435    618    129       C  
ATOM    686  CG  LYS A  79       2.244  19.566  27.445  1.00 27.31           C  
ANISOU  686  CG  LYS A  79     3350   3485   3539    349    553    -51       C  
ATOM    687  CD  LYS A  79       1.694  18.211  27.809  1.00 34.90           C  
ANISOU  687  CD  LYS A  79     4280   4377   4602    -38    405     86       C  
ATOM    688  CE  LYS A  79       0.264  18.339  28.400  1.00 38.35           C  
ANISOU  688  CE  LYS A  79     4546   5006   5016      1    423    140       C  
ATOM    689  NZ  LYS A  79      -0.560  17.071  28.254  1.00 40.14           N  
ANISOU  689  NZ  LYS A  79     5086   4934   5231     80    484     36       N  
ATOM    690  N   VAL A  80       6.152  18.952  24.706  1.00 14.74           N  
ANISOU  690  N   VAL A  80     2168   1857   1572    129    351    100       N  
ATOM    691  CA  VAL A  80       7.515  19.086  24.293  1.00 14.09           C  
ANISOU  691  CA  VAL A  80     2042   1674   1634     16    209     21       C  
ATOM    692  C   VAL A  80       7.650  20.242  23.302  1.00 13.90           C  
ANISOU  692  C   VAL A  80     2029   1677   1573    285    274    -20       C  
ATOM    693  O   VAL A  80       6.693  20.727  22.702  1.00 14.94           O  
ANISOU  693  O   VAL A  80     2081   1763   1831    187    355    220       O  
ATOM    694  CB  VAL A  80       8.019  17.780  23.641  1.00 13.09           C  
ANISOU  694  CB  VAL A  80     1610   1588   1773    153    247    124       C  
ATOM    695  CG1 VAL A  80       7.769  16.547  24.577  1.00 16.49           C  
ANISOU  695  CG1 VAL A  80     2823   1538   1903      1    288    278       C  
ATOM    696  CG2 VAL A  80       7.380  17.515  22.278  1.00 14.00           C  
ANISOU  696  CG2 VAL A  80     1932   1753   1632     55    326     98       C  
ATOM    697  N   LYS A  81       8.889  20.669  23.175  1.00 12.87           N  
ANISOU  697  N   LYS A  81     2055   1383   1453    106    125      1       N  
ATOM    698  CA  LYS A  81       9.293  21.614  22.139  1.00 12.90           C  
ANISOU  698  CA  LYS A  81     1803   1468   1628    167     36    -22       C  
ATOM    699  C   LYS A  81      10.079  20.841  21.095  1.00 11.15           C  
ANISOU  699  C   LYS A  81     1401   1251   1583    285    113    -31       C  
ATOM    700  O   LYS A  81      11.019  20.163  21.425  1.00 12.61           O  
ANISOU  700  O   LYS A  81     1571   1726   1492    382    -39     16       O  
ATOM    701  CB  LYS A  81      10.129  22.721  22.750  1.00 15.24           C  
ANISOU  701  CB  LYS A  81     2244   1762   1782     27    171    -41       C  
ATOM    702  CG  LYS A  81       9.496  23.555  23.767  1.00 21.92           C  
ANISOU  702  CG  LYS A  81     3059   2432   2836     33     -8   -187       C  
ATOM    703  CD  LYS A  81       8.391  24.428  23.242  1.00 27.79           C  
ANISOU  703  CD  LYS A  81     3687   3412   3457    229   -273   -190       C  
ATOM    704  CE  LYS A  81       7.990  25.417  24.340  1.00 30.70           C  
ANISOU  704  CE  LYS A  81     4116   3686   3863    217   -263   -373       C  
ATOM    705  NZ  LYS A  81       7.056  26.426  23.814  1.00 32.67           N  
ANISOU  705  NZ  LYS A  81     4716   3743   3953     46   -910   -249       N  
ATOM    706  N   SER A  82       9.579  20.873  19.876  1.00 11.22           N  
ANISOU  706  N   SER A  82     1578   1342   1341    261    108     61       N  
ATOM    707  CA  SER A  82      10.084  20.060  18.802  1.00  9.67           C  
ANISOU  707  CA  SER A  82      853   1321   1500    211    -14     56       C  
ATOM    708  C   SER A  82      10.714  20.879  17.712  1.00  9.94           C  
ANISOU  708  C   SER A  82     1129   1314   1334    208    -71     53       C  
ATOM    709  O   SER A  82      10.212  21.956  17.367  1.00 10.28           O  
ANISOU  709  O   SER A  82     1065   1285   1554    203    129     99       O  
ATOM    710  CB  SER A  82       8.953  19.264  18.233  1.00 11.43           C  
ANISOU  710  CB  SER A  82      951   1715   1676     59    244     38       C  
ATOM    711  OG  SER A  82       8.585  18.255  19.158  1.00 13.92           O  
ANISOU  711  OG  SER A  82     1890   1458   1940    109    396    319       O  
ATOM    712  N   THR A  83      11.777  20.352  17.107  1.00  9.44           N  
ANISOU  712  N   THR A  83      971   1222   1391    163     46     51       N  
ATOM    713  CA  THR A  83      12.356  20.968  15.902  1.00  9.92           C  
ANISOU  713  CA  THR A  83      810   1428   1528    120     -7     93       C  
ATOM    714  C   THR A  83      12.634  19.802  14.955  1.00 10.55           C  
ANISOU  714  C   THR A  83     1319   1275   1412    302    133    201       C  
ATOM    715  O   THR A  83      13.251  18.820  15.374  1.00 11.67           O  
ANISOU  715  O   THR A  83     1682   1365   1385    395     47     81       O  
ATOM    716  CB  THR A  83      13.584  21.755  16.187  1.00 11.34           C  
ANISOU  716  CB  THR A  83      590   1679   2040      4    -33    -22       C  
ATOM    717  OG1 THR A  83      13.358  22.662  17.271  1.00 15.06           O  
ANISOU  717  OG1 THR A  83     1846   1670   2205     24   -128   -243       O  
ATOM    718  CG2 THR A  83      13.940  22.489  14.931  1.00 14.44           C  
ANISOU  718  CG2 THR A  83     1538   1666   2280   -217    327     43       C  
ATOM    719  N   ILE A  84      12.175  19.914  13.720  1.00  9.47           N  
ANISOU  719  N   ILE A  84      899   1256   1443    334    127    147       N  
ATOM    720  CA  ILE A  84      12.365  18.890  12.691  1.00  9.55           C  
ANISOU  720  CA  ILE A  84      901   1273   1453    182    269    182       C  
ATOM    721  C   ILE A  84      13.176  19.514  11.576  1.00 10.36           C  
ANISOU  721  C   ILE A  84     1099   1392   1443     21    133     86       C  
ATOM    722  O   ILE A  84      12.846  20.573  11.068  1.00 10.41           O  
ANISOU  722  O   ILE A  84     1110   1441   1403    143    186    183       O  
ATOM    723  CB  ILE A  84      11.020  18.306  12.237  1.00  9.42           C  
ANISOU  723  CB  ILE A  84      767   1323   1489    214    133    128       C  
ATOM    724  CG1 ILE A  84      10.316  17.705  13.423  1.00 10.10           C  
ANISOU  724  CG1 ILE A  84      853   1539   1442    148     12    300       C  
ATOM    725  CG2 ILE A  84      11.282  17.225  11.158  1.00 12.00           C  
ANISOU  725  CG2 ILE A  84     1696   1347   1515     50    191    -93       C  
ATOM    726  CD1 ILE A  84       8.984  17.151  13.120  1.00 11.41           C  
ANISOU  726  CD1 ILE A  84      838   1844   1650     97    161    232       C  
ATOM    727  N   THR A  85      14.269  18.838  11.188  1.00 10.18           N  
ANISOU  727  N   THR A  85      999   1361   1507    -48    174    170       N  
ATOM    728  CA  THR A  85      15.153  19.245  10.124  1.00 11.80           C  
ANISOU  728  CA  THR A  85     1353   1378   1751    -25    251     57       C  
ATOM    729  C   THR A  85      15.368  18.038   9.199  1.00 11.30           C  
ANISOU  729  C   THR A  85     1212   1438   1643    -55    393     64       C  
ATOM    730  O   THR A  85      15.099  16.903   9.526  1.00 12.33           O  
ANISOU  730  O   THR A  85     1601   1473   1610    -31    460    106       O  
ATOM    731  CB  THR A  85      16.468  19.771  10.676  1.00 12.74           C  
ANISOU  731  CB  THR A  85     1232   1641   1966      5    317    -42       C  
ATOM    732  OG1 THR A  85      17.015  18.741  11.494  1.00 16.00           O  
ANISOU  732  OG1 THR A  85     1626   2135   2317    202   -299    -89       O  
ATOM    733  CG2 THR A  85      16.267  21.044  11.442  1.00 16.03           C  
ANISOU  733  CG2 THR A  85     1584   1952   2552   -393    279   -514       C  
ATOM    734  N  ALEU A  86      15.658  18.351   7.945  0.50 12.53           N  
ANISOU  734  N  ALEU A  86     1616   1474   1669   -122    235    123       N  
ATOM    735  N  BLEU A  86      16.136  18.308   8.147  0.50 11.18           N  
ANISOU  735  N  BLEU A  86      965   1461   1818    -17    538     34       N  
ATOM    736  CA ALEU A  86      16.017  17.365   6.929  0.50 12.45           C  
ANISOU  736  CA ALEU A  86     1255   1709   1765   -224    334    115       C  
ATOM    737  CA BLEU A  86      16.734  17.255   7.296  0.50 12.49           C  
ANISOU  737  CA BLEU A  86     1513   1453   1779    -80    318    -22       C  
ATOM    738  C  ALEU A  86      17.533  17.400   6.726  0.50 13.51           C  
ANISOU  738  C  ALEU A  86     1504   1812   1814   -246    406    146       C  
ATOM    739  C  BLEU A  86      18.234  17.213   7.477  0.50 13.62           C  
ANISOU  739  C  BLEU A  86     1284   1800   2089   -209    373     42       C  
ATOM    740  O  ALEU A  86      18.086  18.420   6.283  0.50 16.44           O  
ANISOU  740  O  ALEU A  86     1997   1930   2318    -87    743     32       O  
ATOM    741  O  BLEU A  86      18.849  18.273   7.438  0.50 14.70           O  
ANISOU  741  O  BLEU A  86     1511   1602   2473   -515    389    -65       O  
ATOM    742  CB ALEU A  86      15.359  17.722   5.626  0.50 14.37           C  
ANISOU  742  CB ALEU A  86     1720   1898   1839   -245    197     93       C  
ATOM    743  CB BLEU A  86      16.440  17.443   5.800  0.50 14.34           C  
ANISOU  743  CB BLEU A  86     1769   1854   1824    -23    229    232       C  
ATOM    744  CG ALEU A  86      14.157  16.998   5.041  0.50 19.81           C  
ANISOU  744  CG ALEU A  86     2331   2679   2514   -387     33    116       C  
ATOM    745  CG BLEU A  86      15.052  17.078   5.289  0.50 14.51           C  
ANISOU  745  CG BLEU A  86     1481   1793   2237   -123   -155    569       C  
ATOM    746  CD1ALEU A  86      14.088  17.401   3.587  0.50 18.06           C  
ANISOU  746  CD1ALEU A  86     2213   2613   2036   -475    -28    -56       C  
ATOM    747  CD1BLEU A  86      14.697  17.785   3.983  0.50 18.68           C  
ANISOU  747  CD1BLEU A  86     2446   2653   1996    -36    186    336       C  
ATOM    748  CD2ALEU A  86      14.168  15.462   5.103  0.50 18.03           C  
ANISOU  748  CD2ALEU A  86     2519   2329   2002   -922    177    -86       C  
ATOM    749  CD2BLEU A  86      14.906  15.566   5.139  0.50 13.31           C  
ANISOU  749  CD2BLEU A  86      305   2277   2472   -312   -106    119       C  
ATOM    750  N  AASP A  87      18.209  16.319   7.115  0.50 15.11           N  
ANISOU  750  N  AASP A  87     1735   1968   2036   -176    353     47       N  
ATOM    751  N  BASP A  87      18.774  16.005   7.667  0.50 13.63           N  
ANISOU  751  N  BASP A  87     1137   1903   2138   -406    308     54       N  
ATOM    752  CA AASP A  87      19.678  16.232   7.198  0.50 17.53           C  
ANISOU  752  CA AASP A  87     1958   2363   2340   -189    364    -16       C  
ATOM    753  CA BASP A  87      20.193  15.709   7.683  0.50 15.11           C  
ANISOU  753  CA BASP A  87     1229   2153   2359   -141    150     95       C  
ATOM    754  C  AASP A  87      20.079  15.129   6.268  0.50 16.09           C  
ANISOU  754  C  AASP A  87     1588   2300   2225   -183    434    -45       C  
ATOM    755  C  BASP A  87      20.320  14.711   6.574  0.50 14.63           C  
ANISOU  755  C  BASP A  87     1358   1995   2203   -238    141    150       C  
ATOM    756  O  AASP A  87      20.000  13.959   6.612  0.50 16.86           O  
ANISOU  756  O  AASP A  87     1576   2392   2437   -381    380    -32       O  
ATOM    757  O  BASP A  87      19.926  13.559   6.715  0.50 17.22           O  
ANISOU  757  O  BASP A  87     1790   2125   2627   -553    329    126       O  
ATOM    758  CB AASP A  87      20.113  15.885   8.645  0.50 18.07           C  
ANISOU  758  CB AASP A  87     1796   2652   2417   -281    287    -11       C  
ATOM    759  CB BASP A  87      20.662  15.019   8.965  0.50 16.49           C  
ANISOU  759  CB BASP A  87     1308   2303   2654   -123    115    106       C  
ATOM    760  CG AASP A  87      21.589  15.377   8.775  0.50 24.14           C  
ANISOU  760  CG AASP A  87     2381   3619   3172   -270    516    149       C  
ATOM    761  CG BASP A  87      22.225  15.176   9.216  0.50 20.95           C  
ANISOU  761  CG BASP A  87     1555   3082   3320    140   -114    307       C  
ATOM    762  OD1AASP A  87      22.439  15.653   7.899  0.50 30.61           O  
ANISOU  762  OD1AASP A  87     3429   4849   3350   -888    740    254       O  
ATOM    763  OD1BASP A  87      22.980  14.177   9.206  0.50 27.99           O  
ANISOU  763  OD1BASP A  87     1265   4041   5327    -36    118   -477       O  
ATOM    764  OD2AASP A  87      21.933  14.731   9.816  0.50 27.93           O  
ANISOU  764  OD2AASP A  87     2096   4591   3925   -363    892    621       O  
ATOM    765  OD2BASP A  87      22.664  16.317   9.462  0.50 30.96           O  
ANISOU  765  OD2BASP A  87     3146   3740   4877   -166    207   -101       O  
ATOM    766  N  AGLY A  88      20.543  15.507   5.086  0.50 16.44           N  
ANISOU  766  N  AGLY A  88     1969   2086   2191   -103    308     26       N  
ATOM    767  N  BGLY A  88      20.941  15.115   5.477  0.50 16.04           N  
ANISOU  767  N  BGLY A  88     1567   2194   2330   -191    237    119       N  
ATOM    768  CA AGLY A  88      20.618  14.568   4.026  0.50 16.16           C  
ANISOU  768  CA AGLY A  88     1942   2121   2074    -20    352     17       C  
ATOM    769  CA BGLY A  88      21.264  14.135   4.481  0.50 15.76           C  
ANISOU  769  CA BGLY A  88     1557   2276   2152    -79    123     93       C  
ATOM    770  C  AGLY A  88      19.220  14.139   3.732  0.50 16.21           C  
ANISOU  770  C  AGLY A  88     1984   2225   1947   -125    419      9       C  
ATOM    771  C  BGLY A  88      20.106  13.231   4.097  0.50 15.70           C  
ANISOU  771  C  BGLY A  88     1610   2336   2018   -100    245     11       C  
ATOM    772  O  AGLY A  88      18.318  14.972   3.587  0.50 18.26           O  
ANISOU  772  O  AGLY A  88     2285   2448   2202   -141    509     64       O  
ATOM    773  O  BGLY A  88      20.242  12.031   4.018  0.50 15.88           O  
ANISOU  773  O  BGLY A  88     1422   2293   2317   -121    173     91       O  
ATOM    774  N  AGLY A  89      19.072  12.827   3.630  0.50 14.09           N  
ANISOU  774  N  AGLY A  89     1664   2005   1684   -189    309    -85       N  
ATOM    775  N  BGLY A  89      18.950  13.800   3.834  0.50 15.08           N  
ANISOU  775  N  BGLY A  89     1648   2284   1795    -17    452     54       N  
ATOM    776  CA AGLY A  89      17.804  12.154   3.409  0.50 14.86           C  
ANISOU  776  CA AGLY A  89     1784   2081   1780   -171    217   -137       C  
ATOM    777  CA BGLY A  89      17.814  13.005   3.448  0.50 15.16           C  
ANISOU  777  CA BGLY A  89     1820   2165   1773    -34    238    -56       C  
ATOM    778  C  AGLY A  89      17.108  11.754   4.681  0.50 13.13           C  
ANISOU  778  C  AGLY A  89     1363   1950   1673   -196    274   -147       C  
ATOM    779  C  BGLY A  89      17.034  12.251   4.566  0.50 13.83           C  
ANISOU  779  C  BGLY A  89     1423   2126   1703   -266    232      2       C  
ATOM    780  O  AGLY A  89      16.182  10.930   4.650  0.50 14.42           O  
ANISOU  780  O  AGLY A  89     1892   1775   1812    -85     69   -303       O  
ATOM    781  O  BGLY A  89      16.025  11.614   4.275  0.50 14.82           O  
ANISOU  781  O  BGLY A  89     1777   2174   1678   -363   -143    -77       O  
ATOM    782  N   VAL A  90      17.502  12.334   5.815  1.00 13.52           N  
ANISOU  782  N   VAL A  90     1423   2064   1647   -378    344   -157       N  
ATOM    783  CA  VAL A  90      16.888  11.835   7.041  1.00 12.90           C  
ANISOU  783  CA  VAL A  90     1577   1626   1698   -302    280   -171       C  
ATOM    784  C   VAL A  90      16.131  12.966   7.687  1.00 11.10           C  
ANISOU  784  C   VAL A  90     1155   1611   1450    -54    209    -47       C  
ATOM    785  O   VAL A  90      16.660  14.051   7.919  1.00 12.30           O  
ANISOU  785  O   VAL A  90     1484   1465   1725   -253    362   -116       O  
ATOM    786  CB  VAL A  90      17.928  11.265   8.028  1.00 13.75           C  
ANISOU  786  CB  VAL A  90     1475   1690   2058    -30    390   -154       C  
ATOM    787  CG1 VAL A  90      17.342  10.734   9.291  1.00 14.48           C  
ANISOU  787  CG1 VAL A  90     1530   1986   1983   -101    395     35       C  
ATOM    788  CG2 VAL A  90      18.838  10.186   7.382  1.00 16.73           C  
ANISOU  788  CG2 VAL A  90     1417   2088   2851    460    568    -34       C  
ATOM    789  N  ALEU A  91      14.843  12.770   7.944  0.50 10.91           N  
ANISOU  789  N  ALEU A  91     1236   1423   1487    -88     71    -43       N  
ATOM    790  N  BLEU A  91      14.913  12.678   8.038  0.50 10.55           N  
ANISOU  790  N  BLEU A  91     1011   1532   1465   -134    217      8       N  
ATOM    791  CA ALEU A  91      14.060  13.697   8.835  0.50 11.12           C  
ANISOU  791  CA ALEU A  91     1378   1328   1518     55    -15     39       C  
ATOM    792  CA BLEU A  91      14.055  13.635   8.710  0.50 10.85           C  
ANISOU  792  CA BLEU A  91     1196   1400   1527      7    209    166       C  
ATOM    793  C  ALEU A  91      14.511  13.426  10.253  0.50 11.20           C  
ANISOU  793  C  ALEU A  91     1482   1386   1385    205    166    -52       C  
ATOM    794  C  BLEU A  91      14.346  13.462  10.229  0.50 11.55           C  
ANISOU  794  C  BLEU A  91     1545   1416   1427    105    332     11       C  
ATOM    795  O  ALEU A  91      14.450  12.313  10.760  0.50 11.09           O  
ANISOU  795  O  ALEU A  91     1648   1209   1356    154     80     56       O  
ATOM    796  O  BLEU A  91      14.059  12.394  10.763  0.50 10.87           O  
ANISOU  796  O  BLEU A  91     1295   1263   1570     11    412    180       O  
ATOM    797  CB ALEU A  91      12.515  13.575   8.745  0.50 11.44           C  
ANISOU  797  CB ALEU A  91     1175   1611   1557     81    -97    -45       C  
ATOM    798  CB BLEU A  91      12.606  13.342   8.316  0.50 10.80           C  
ANISOU  798  CB BLEU A  91      882   1616   1602   -129    214    183       C  
ATOM    799  CG ALEU A  91      11.954  14.121   7.422  0.50 12.88           C  
ANISOU  799  CG ALEU A  91     1577   1591   1726     36   -153     -8       C  
ATOM    800  CG BLEU A  91      11.730  14.446   8.865  0.50 11.37           C  
ANISOU  800  CG BLEU A  91     1027   1673   1618    234    376    188       C  
ATOM    801  CD1ALEU A  91      10.572  13.556   7.243  0.50 15.14           C  
ANISOU  801  CD1ALEU A  91     1682   1837   2232    -97    166     77       C  
ATOM    802  CD1BLEU A  91      11.882  15.726   8.091  0.50 10.91           C  
ANISOU  802  CD1BLEU A  91      855   1866   1422    207    216    143       C  
ATOM    803  CD2ALEU A  91      11.908  15.668   7.398  0.50 13.04           C  
ANISOU  803  CD2ALEU A  91     2378   1193   1382    434    206     81       C  
ATOM    804  CD2BLEU A  91      10.387  13.930   8.830  0.50 16.38           C  
ANISOU  804  CD2BLEU A  91      718   2505   2998    -50    820    369       C  
ATOM    805  N   VAL A  92      14.942  14.480  10.894  1.00  9.82           N  
ANISOU  805  N   VAL A  92     1036   1198   1497    135    223     74       N  
ATOM    806  CA  VAL A  92      15.449  14.413  12.265  1.00  9.95           C  
ANISOU  806  CA  VAL A  92      933   1415   1431    283    223     89       C  
ATOM    807  C   VAL A  92      14.538  15.275  13.141  1.00 10.14           C  
ANISOU  807  C   VAL A  92     1073   1392   1385    315     50     10       C  
ATOM    808  O   VAL A  92      14.448  16.485  12.954  1.00 11.88           O  
ANISOU  808  O   VAL A  92     1765   1186   1559    270    282    136       O  
ATOM    809  CB  VAL A  92      16.863  14.836  12.374  1.00 11.38           C  
ANISOU  809  CB  VAL A  92      877   1708   1736    220    169     42       C  
ATOM    810  CG1 VAL A  92      17.393  14.762  13.817  1.00 14.05           C  
ANISOU  810  CG1 VAL A  92     1315   2235   1788    297    -82   -117       C  
ATOM    811  CG2 VAL A  92      17.767  14.070  11.402  1.00 13.94           C  
ANISOU  811  CG2 VAL A  92      660   2271   2366    335    304   -266       C  
ATOM    812  N   HIS A  93      13.831  14.626  14.072  1.00  9.68           N  
ANISOU  812  N   HIS A  93      977   1293   1405    261    138     63       N  
ATOM    813  CA  HIS A  93      12.812  15.229  14.965  1.00  9.89           C  
ANISOU  813  CA  HIS A  93     1002   1308   1447    249    153    186       C  
ATOM    814  C   HIS A  93      13.362  15.191  16.387  1.00 10.22           C  
ANISOU  814  C   HIS A  93     1298   1173   1411    278     76     43       C  
ATOM    815  O   HIS A  93      13.454  14.131  16.954  1.00 11.96           O  
ANISOU  815  O   HIS A  93     2059   1110   1372    178    -47     36       O  
ATOM    816  CB  HIS A  93      11.511  14.490  14.776  1.00  9.77           C  
ANISOU  816  CB  HIS A  93      619   1563   1526    111    195    226       C  
ATOM    817  CG  HIS A  93      10.395  14.931  15.593  1.00 10.73           C  
ANISOU  817  CG  HIS A  93      926   1581   1570    147    -11    406       C  
ATOM    818  ND1 HIS A  93       9.178  14.321  15.469  1.00 14.45           N  
ANISOU  818  ND1 HIS A  93      757   2271   2460     71    103    767       N  
ATOM    819  CD2 HIS A  93      10.238  15.925  16.514  1.00 13.66           C  
ANISOU  819  CD2 HIS A  93     1725   1891   1574    340    307    394       C  
ATOM    820  CE1 HIS A  93       8.333  14.906  16.276  1.00 15.95           C  
ANISOU  820  CE1 HIS A  93      609   2447   3002    148    525   1053       C  
ATOM    821  NE2 HIS A  93       8.939  15.876  16.932  1.00 16.64           N  
ANISOU  821  NE2 HIS A  93     1666   2318   2338    341    596    892       N  
ATOM    822  N   VAL A  94      13.726  16.345  16.939  1.00  9.70           N  
ANISOU  822  N   VAL A  94     1269   1132   1284    248     -3     99       N  
ATOM    823  CA  VAL A  94      14.181  16.449  18.298  1.00  9.89           C  
ANISOU  823  CA  VAL A  94      867   1377   1513     97    -33    102       C  
ATOM    824  C   VAL A  94      13.110  17.012  19.179  1.00 10.80           C  
ANISOU  824  C   VAL A  94     1314   1364   1425    199     -4     -3       C  
ATOM    825  O   VAL A  94      12.506  18.035  18.841  1.00 13.11           O  
ANISOU  825  O   VAL A  94     2006   1503   1469    606    248    214       O  
ATOM    826  CB  VAL A  94      15.417  17.287  18.387  1.00 12.41           C  
ANISOU  826  CB  VAL A  94     1113   1725   1877    133    -60      7       C  
ATOM    827  CG1 VAL A  94      16.002  17.383  19.805  1.00 15.90           C  
ANISOU  827  CG1 VAL A  94     1795   2241   2004   -280   -394    -33       C  
ATOM    828  CG2 VAL A  94      16.482  16.802  17.410  1.00 15.49           C  
ANISOU  828  CG2 VAL A  94     1134   2440   2311   -238    190    -83       C  
ATOM    829  N   GLN A  95      12.841  16.354  20.293  1.00 10.61           N  
ANISOU  829  N   GLN A  95     1502   1180   1348    155    -25     13       N  
ATOM    830  CA  GLN A  95      11.872  16.765  21.276  1.00 11.29           C  
ANISOU  830  CA  GLN A  95     1555   1381   1352    147     -7     69       C  
ATOM    831  C   GLN A  95      12.569  17.078  22.571  1.00 12.07           C  
ANISOU  831  C   GLN A  95     1843   1354   1387     51    -52     66       C  
ATOM    832  O   GLN A  95      13.315  16.231  23.089  1.00 13.00           O  
ANISOU  832  O   GLN A  95     2018   1416   1503    204   -230     17       O  
ATOM    833  CB  GLN A  95      10.895  15.626  21.543  1.00 11.94           C  
ANISOU  833  CB  GLN A  95     1585   1506   1445    144    -25     42       C  
ATOM    834  CG  GLN A  95      10.051  15.244  20.368  1.00 11.96           C  
ANISOU  834  CG  GLN A  95     1295   1435   1811    -13      9    144       C  
ATOM    835  CD  GLN A  95       9.053  14.130  20.633  1.00 13.16           C  
ANISOU  835  CD  GLN A  95     1476   1632   1892    -54    -48     38       C  
ATOM    836  OE1 GLN A  95       8.031  14.005  19.893  1.00 16.51           O  
ANISOU  836  OE1 GLN A  95     1861   2288   2125   -183   -126    164       O  
ATOM    837  NE2 GLN A  95       9.395  13.242  21.510  1.00 14.90           N  
ANISOU  837  NE2 GLN A  95     2156   1483   2021   -161   -241    334       N  
ATOM    838  N   LYS A  96      12.237  18.206  23.166  1.00 12.50           N  
ANISOU  838  N   LYS A  96     1881   1411   1457    119   -244    -15       N  
ATOM    839  CA  LYS A  96      12.835  18.675  24.432  1.00 13.21           C  
ANISOU  839  CA  LYS A  96     1749   1663   1606     82   -249    -69       C  
ATOM    840  C   LYS A  96      11.729  18.933  25.440  1.00 14.14           C  
ANISOU  840  C   LYS A  96     2283   1516   1570    166   -146   -163       C  
ATOM    841  O   LYS A  96      10.763  19.585  25.143  1.00 14.98           O  
ANISOU  841  O   LYS A  96     2488   1670   1533    361     44   -151       O  
ATOM    842  CB  LYS A  96      13.549  19.990  24.217  1.00 15.30           C  
ANISOU  842  CB  LYS A  96     1763   2056   1991   -142   -189   -319       C  
ATOM    843  CG  LYS A  96      14.638  19.961  23.237  1.00 19.09           C  
ANISOU  843  CG  LYS A  96     1824   2734   2693   -154    -67   -261       C  
ATOM    844  CD  LYS A  96      15.848  19.161  23.546  1.00 21.31           C  
ANISOU  844  CD  LYS A  96     1798   2963   3334    161    142   -292       C  
ATOM    845  CE  LYS A  96      17.020  19.370  22.604  1.00 21.34           C  
ANISOU  845  CE  LYS A  96      742   3494   3870   -466    -92   -199       C  
ATOM    846  NZ  LYS A  96      18.198  18.595  22.755  1.00 24.19           N  
ANISOU  846  NZ  LYS A  96     1413   3785   3993   -763   -180    -19       N  
ATOM    847  N   TRP A  97      11.932  18.422  26.651  1.00 15.03           N  
ANISOU  847  N   TRP A  97     2444   1728   1537    242    -75   -154       N  
ATOM    848  CA  TRP A  97      10.945  18.621  27.714  1.00 16.21           C  
ANISOU  848  CA  TRP A  97     2681   1863   1614    338    -19    -73       C  
ATOM    849  C   TRP A  97      11.636  18.324  29.032  1.00 19.15           C  
ANISOU  849  C   TRP A  97     3383   2185   1705    343   -131   -187       C  
ATOM    850  O   TRP A  97      12.485  17.459  29.103  1.00 20.14           O  
ANISOU  850  O   TRP A  97     3715   2397   1538    560   -258    -58       O  
ATOM    851  CB  TRP A  97       9.668  17.754  27.561  1.00 17.20           C  
ANISOU  851  CB  TRP A  97     2850   1954   1730    198    159    -68       C  
ATOM    852  CG  TRP A  97       9.866  16.337  27.947  1.00 16.16           C  
ANISOU  852  CG  TRP A  97     2668   1691   1778     19    360     85       C  
ATOM    853  CD1 TRP A  97       9.345  15.727  29.031  1.00 18.75           C  
ANISOU  853  CD1 TRP A  97     2890   2432   1801    -90    445    228       C  
ATOM    854  CD2 TRP A  97      10.612  15.335  27.252  1.00 15.29           C  
ANISOU  854  CD2 TRP A  97     2412   1750   1645   -272    212   -191       C  
ATOM    855  NE1 TRP A  97       9.726  14.431  29.084  1.00 17.80           N  
ANISOU  855  NE1 TRP A  97     2853   2149   1760     27    231    197       N  
ATOM    856  CE2 TRP A  97      10.512  14.153  28.006  1.00 16.08           C  
ANISOU  856  CE2 TRP A  97     2647   1829   1633     48     98     71       C  
ATOM    857  CE3 TRP A  97      11.363  15.301  26.060  1.00 15.09           C  
ANISOU  857  CE3 TRP A  97     2321   1731   1679   -156     51    -62       C  
ATOM    858  CZ2 TRP A  97      11.170  12.987  27.635  1.00 16.32           C  
ANISOU  858  CZ2 TRP A  97     2557   1665   1976   -247     62    221       C  
ATOM    859  CZ3 TRP A  97      11.986  14.134  25.721  1.00 13.86           C  
ANISOU  859  CZ3 TRP A  97     1412   1951   1904      5    -45    -62       C  
ATOM    860  CH2 TRP A  97      11.855  13.005  26.487  1.00 16.39           C  
ANISOU  860  CH2 TRP A  97     2599   1589   2039     52     46   -186       C  
ATOM    861  N   ASP A  98      11.333  19.115  30.059  1.00 21.91           N  
ANISOU  861  N   ASP A  98     3932   2611   1780    384    -87   -252       N  
ATOM    862  CA  ASP A  98      11.800  18.812  31.429  1.00 24.86           C  
ANISOU  862  CA  ASP A  98     4165   3071   2210    194   -253   -250       C  
ATOM    863  C   ASP A  98      13.298  18.555  31.514  1.00 24.55           C  
ANISOU  863  C   ASP A  98     4271   2917   2139    114   -332   -457       C  
ATOM    864  O   ASP A  98      13.758  17.683  32.259  1.00 27.61           O  
ANISOU  864  O   ASP A  98     4785   3376   2328    165   -482   -268       O  
ATOM    865  CB  ASP A  98      11.002  17.608  31.957  1.00 27.82           C  
ANISOU  865  CB  ASP A  98     4517   3444   2607    201   -317   -154       C  
ATOM    866  CG  ASP A  98      10.990  17.496  33.478  1.00 33.77           C  
ANISOU  866  CG  ASP A  98     5286   4217   3327    167   -275    -49       C  
ATOM    867  OD1 ASP A  98      11.029  18.543  34.150  1.00 39.07           O  
ANISOU  867  OD1 ASP A  98     6067   4654   4122    544   -259   -465       O  
ATOM    868  OD2 ASP A  98      10.875  16.346  33.985  1.00 43.35           O  
ANISOU  868  OD2 ASP A  98     6846   4998   4627    343   -211    582       O  
ATOM    869  N   GLY A  99      14.086  19.291  30.744  1.00 24.40           N  
ANISOU  869  N   GLY A  99     4021   2899   2350    -64   -394   -608       N  
ATOM    870  CA  GLY A  99      15.540  19.053  30.706  1.00 24.43           C  
ANISOU  870  CA  GLY A  99     3769   2874   2638   -105   -464   -516       C  
ATOM    871  C   GLY A  99      16.021  17.777  30.009  1.00 24.36           C  
ANISOU  871  C   GLY A  99     3699   2896   2660    -41   -541   -446       C  
ATOM    872  O   GLY A  99      17.219  17.502  29.956  1.00 27.26           O  
ANISOU  872  O   GLY A  99     3828   3355   3173   -209  -1056   -611       O  
ATOM    873  N   LYS A 100      15.106  17.036  29.391  1.00 20.61           N  
ANISOU  873  N   LYS A 100     3369   2432   2030    -40   -730   -307       N  
ATOM    874  CA  LYS A 100      15.362  15.794  28.654  1.00 19.69           C  
ANISOU  874  CA  LYS A 100     3227   2373   1878    132   -639   -114       C  
ATOM    875  C   LYS A 100      15.242  16.051  27.135  1.00 16.95           C  
ANISOU  875  C   LYS A 100     2664   2084   1691     67   -739     -2       C  
ATOM    876  O   LYS A 100      14.686  17.060  26.705  1.00 17.08           O  
ANISOU  876  O   LYS A 100     3081   1649   1760    -77   -712    -69       O  
ATOM    877  CB  LYS A 100      14.340  14.760  29.069  1.00 19.34           C  
ANISOU  877  CB  LYS A 100     3290   2194   1865    327   -557     19       C  
ATOM    878  CG  LYS A 100      14.364  14.373  30.539  1.00 24.46           C  
ANISOU  878  CG  LYS A 100     3682   3317   2293    120   -445     74       C  
ATOM    879  CD  LYS A 100      13.120  13.582  30.935  1.00 30.09           C  
ANISOU  879  CD  LYS A 100     4340   3858   3235    103    -12    438       C  
ATOM    880  CE  LYS A 100      12.851  13.532  32.426  1.00 34.65           C  
ANISOU  880  CE  LYS A 100     4764   4569   3831     62     95    220       C  
ATOM    881  NZ  LYS A 100      11.349  13.683  32.706  1.00 39.14           N  
ANISOU  881  NZ  LYS A 100     4920   5314   4637     77    134    485       N  
ATOM    882  N   SER A 101      15.773  15.114  26.364  1.00 16.87           N  
ANISOU  882  N   SER A 101     2851   1842   1715     92   -625    -35       N  
ATOM    883  CA  SER A 101      15.713  15.182  24.908  1.00 16.07           C  
ANISOU  883  CA  SER A 101     2655   1659   1790    -21   -508     32       C  
ATOM    884  C   SER A 101      15.639  13.803  24.330  1.00 13.81           C  
ANISOU  884  C   SER A 101     2018   1564   1662    143   -448     55       C  
ATOM    885  O   SER A 101      16.267  12.898  24.838  1.00 13.85           O  
ANISOU  885  O   SER A 101     1444   1798   2019    116   -557     31       O  
ATOM    886  CB  SER A 101      16.997  15.847  24.436  1.00 18.60           C  
ANISOU  886  CB  SER A 101     3082   1955   2027   -269   -394     65       C  
ATOM    887  OG  SER A 101      17.000  16.027  23.069  1.00 22.15           O  
ANISOU  887  OG  SER A 101     3470   2415   2530   -557   -415     33       O  
ATOM    888  N   THR A 102      14.854  13.657  23.262  1.00 11.58           N  
ANISOU  888  N   THR A 102     1417   1474   1506     47   -407     32       N  
ATOM    889  CA  THR A 102      14.866  12.434  22.495  1.00 11.47           C  
ANISOU  889  CA  THR A 102     1334   1400   1622    201   -270    -41       C  
ATOM    890  C   THR A 102      14.859  12.844  21.010  1.00 10.95           C  
ANISOU  890  C   THR A 102     1492   1282   1383     89    -75     67       C  
ATOM    891  O   THR A 102      14.393  13.906  20.659  1.00 11.48           O  
ANISOU  891  O   THR A 102     1489   1277   1594    123   -159     36       O  
ATOM    892  CB  THR A 102      13.640  11.573  22.898  1.00 12.29           C  
ANISOU  892  CB  THR A 102     1385   1610   1675     -8    -93   -132       C  
ATOM    893  OG1 THR A 102      13.755  10.279  22.274  1.00 13.53           O  
ANISOU  893  OG1 THR A 102     1640   1396   2103      8    -91     11       O  
ATOM    894  CG2 THR A 102      12.350  12.171  22.550  1.00 13.10           C  
ANISOU  894  CG2 THR A 102     1335   1739   1900     59   -155    -38       C  
ATOM    895  N   THR A 103      15.369  11.938  20.177  1.00 10.94           N  
ANISOU  895  N   THR A 103     1264   1271   1619    202   -236     46       N  
ATOM    896  CA  THR A 103      15.421  12.141  18.755  1.00 12.13           C  
ANISOU  896  CA  THR A 103     1866   1284   1458    260     -8     86       C  
ATOM    897  C   THR A 103      14.746  11.014  18.027  1.00 12.35           C  
ANISOU  897  C   THR A 103     1971   1275   1444    187   -135    -45       C  
ATOM    898  O   THR A 103      15.003   9.846  18.309  1.00 14.18           O  
ANISOU  898  O   THR A 103     2565   1203   1618    297   -474     11       O  
ATOM    899  CB  THR A 103      16.870  12.311  18.289  1.00 14.06           C  
ANISOU  899  CB  THR A 103     1861   1697   1784     -1      4    -82       C  
ATOM    900  OG1 THR A 103      17.470  13.432  18.976  1.00 18.83           O  
ANISOU  900  OG1 THR A 103     2528   2357   2266   -333    -91     30       O  
ATOM    901  CG2 THR A 103      16.927  12.620  16.825  1.00 17.57           C  
ANISOU  901  CG2 THR A 103     2500   2254   1920     50     51   -110       C  
ATOM    902  N   ILE A 104      13.907  11.345  17.062  1.00 10.66           N  
ANISOU  902  N   ILE A 104     1489   1159   1403    194    -51     13       N  
ATOM    903  CA  ILE A 104      13.209  10.424  16.185  1.00 10.97           C  
ANISOU  903  CA  ILE A 104     1549   1222   1398    123    -58     37       C  
ATOM    904  C   ILE A 104      13.685  10.713  14.775  1.00  9.88           C  
ANISOU  904  C   ILE A 104     1121   1332   1298     59    -52     45       C  
ATOM    905  O   ILE A 104      13.545  11.803  14.276  1.00 11.74           O  
ANISOU  905  O   ILE A 104     1802   1324   1334    259     90     66       O  
ATOM    906  CB  ILE A 104      11.661  10.595  16.256  1.00 12.19           C  
ANISOU  906  CB  ILE A 104     1669   1572   1391     58    109    135       C  
ATOM    907  CG1 ILE A 104      11.173  10.434  17.698  1.00 13.52           C  
ANISOU  907  CG1 ILE A 104     1605   1738   1792   -132    347    -94       C  
ATOM    908  CG2 ILE A 104      10.961   9.651  15.335  1.00 14.48           C  
ANISOU  908  CG2 ILE A 104     1799   2106   1595   -173    -41   -105       C  
ATOM    909  CD1 ILE A 104       9.793  10.910  17.880  1.00 23.88           C  
ANISOU  909  CD1 ILE A 104     2780   3742   2551    491    624    -63       C  
ATOM    910  N   LYS A 105      14.283   9.729  14.140  1.00 10.12           N  
ANISOU  910  N   LYS A 105     1381   1126   1336     18    -11     48       N  
ATOM    911  CA  LYS A 105      14.798   9.833  12.790  1.00 10.46           C  
ANISOU  911  CA  LYS A 105     1279   1266   1427     32     53     83       C  
ATOM    912  C   LYS A 105      13.955   8.997  11.874  1.00 10.53           C  
ANISOU  912  C   LYS A 105     1340   1287   1373   -111     -1     47       C  
ATOM    913  O   LYS A 105      13.585   7.883  12.200  1.00 13.38           O  
ANISOU  913  O   LYS A 105     2284   1304   1493   -273   -222    128       O  
ATOM    914  CB  LYS A 105      16.199   9.334  12.707  1.00 12.29           C  
ANISOU  914  CB  LYS A 105     1437   1735   1497    -26     -7    -64       C  
ATOM    915  CG  LYS A 105      17.205  10.229  13.465  1.00 15.84           C  
ANISOU  915  CG  LYS A 105     1329   2456   2232    203   -176   -125       C  
ATOM    916  CD  LYS A 105      18.654   9.930  13.291  1.00 19.64           C  
ANISOU  916  CD  LYS A 105     1305   3310   2845    -25   -203   -132       C  
ATOM    917  CE  LYS A 105      19.536  11.055  14.012  1.00 24.72           C  
ANISOU  917  CE  LYS A 105     1920   3700   3772    281   -598   -182       C  
ATOM    918  NZ  LYS A 105      21.000  10.834  14.040  1.00 32.22           N  
ANISOU  918  NZ  LYS A 105     2571   4673   4996    605   -595     46       N  
ATOM    919  N   ARG A 106      13.592   9.537  10.731  1.00 10.23           N  
ANISOU  919  N   ARG A 106     1262   1254   1370    -92     75     61       N  
ATOM    920  CA  ARG A 106      12.794   8.834   9.721  1.00 11.54           C  
ANISOU  920  CA  ARG A 106     1456   1494   1431   -350     37     69       C  
ATOM    921  C   ARG A 106      13.627   8.834   8.434  1.00 10.50           C  
ANISOU  921  C   ARG A 106     1345   1281   1363   -136   -103    -10       C  
ATOM    922  O   ARG A 106      14.073   9.872   7.962  1.00 11.67           O  
ANISOU  922  O   ARG A 106     1674   1324   1433   -283     30     24       O  
ATOM    923  CB  ARG A 106      11.443   9.527   9.523  1.00 12.90           C  
ANISOU  923  CB  ARG A 106     1283   1943   1673   -464     80     57       C  
ATOM    924  CG  ARG A 106      10.583   9.515  10.798  1.00 14.55           C  
ANISOU  924  CG  ARG A 106     1448   2065   2015   -272    325    160       C  
ATOM    925  CD  ARG A 106       9.322  10.311  10.669  1.00 20.07           C  
ANISOU  925  CD  ARG A 106     1569   3302   2756   -107    659     97       C  
ATOM    926  NE  ARG A 106       8.437  10.240  11.847  1.00 25.51           N  
ANISOU  926  NE  ARG A 106     2315   3919   3458   -311   1204    183       N  
ATOM    927  CZ  ARG A 106       8.414  11.090  12.857  1.00 24.38           C  
ANISOU  927  CZ  ARG A 106     2366   3911   2987     16    813    455       C  
ATOM    928  NH1 ARG A 106       9.215  12.097  12.970  1.00 20.91           N  
ANISOU  928  NH1 ARG A 106     1972   3507   2463    741    360    757       N  
ATOM    929  NH2 ARG A 106       7.545  10.887  13.842  1.00 26.79           N  
ANISOU  929  NH2 ARG A 106     2578   4509   3091   -299   1218    314       N  
ATOM    930  N   LYS A 107      13.732   7.671   7.809  1.00 11.16           N  
ANISOU  930  N   LYS A 107     1413   1434   1392   -404    152     17       N  
ATOM    931  CA  LYS A 107      14.488   7.498   6.594  1.00 12.65           C  
ANISOU  931  CA  LYS A 107     1491   1750   1563   -155     -8    -45       C  
ATOM    932  C   LYS A 107      13.871   6.467   5.680  1.00 13.44           C  
ANISOU  932  C   LYS A 107     1869   1741   1497   -499     76    -43       C  
ATOM    933  O   LYS A 107      13.347   5.494   6.124  1.00 15.15           O  
ANISOU  933  O   LYS A 107     2326   2006   1421   -813     93    -13       O  
ATOM    934  CB  LYS A 107      15.911   7.161   6.892  1.00 15.87           C  
ANISOU  934  CB  LYS A 107     1979   2316   1734   -190    118   -319       C  
ATOM    935  CG  LYS A 107      16.241   5.920   7.230  1.00 24.30           C  
ANISOU  935  CG  LYS A 107     2929   3051   3251   -166   -149   -170       C  
ATOM    936  CD  LYS A 107      17.672   5.606   6.562  1.00 28.61           C  
ANISOU  936  CD  LYS A 107     2904   3852   4114    500     -6    -48       C  
ATOM    937  CE  LYS A 107      18.639   6.779   6.385  1.00 25.78           C  
ANISOU  937  CE  LYS A 107     3009   3235   3551    468    158    -53       C  
ATOM    938  NZ  LYS A 107      19.327   7.049   5.060  1.00 29.45           N  
ANISOU  938  NZ  LYS A 107     3014   4265   3908   -275    743   -304       N  
ATOM    939  N   ARG A 108      13.988   6.697   4.401  1.00 12.23           N  
ANISOU  939  N   ARG A 108     1496   1642   1508   -428     57    -61       N  
ATOM    940  CA  ARG A 108      13.575   5.702   3.418  1.00 11.69           C  
ANISOU  940  CA  ARG A 108      972   1894   1576   -340    224      1       C  
ATOM    941  C   ARG A 108      14.678   4.654   3.249  1.00 12.65           C  
ANISOU  941  C   ARG A 108     1120   2072   1613   -202    238   -267       C  
ATOM    942  O   ARG A 108      15.840   4.974   3.024  1.00 15.30           O  
ANISOU  942  O   ARG A 108     1239   2149   2422   -280    455   -500       O  
ATOM    943  CB  ARG A 108      13.296   6.374   2.095  1.00 14.26           C  
ANISOU  943  CB  ARG A 108     1406   2364   1645   -458    156     60       C  
ATOM    944  CG  ARG A 108      11.960   7.077   2.049  1.00 16.76           C  
ANISOU  944  CG  ARG A 108     2038   2422   1905   -188     48    395       C  
ATOM    945  CD  ARG A 108      10.806   6.100   2.157  1.00 18.03           C  
ANISOU  945  CD  ARG A 108     1703   3065   2082   -391    132    563       C  
ATOM    946  NE  ARG A 108      10.861   4.995   1.154  1.00 18.91           N  
ANISOU  946  NE  ARG A 108     1075   3270   2837   -281    -95    507       N  
ATOM    947  CZ  ARG A 108      10.580   5.134  -0.125  1.00 17.10           C  
ANISOU  947  CZ  ARG A 108     1048   2218   3229   -131   -256     74       C  
ATOM    948  NH1 ARG A 108      10.052   6.240  -0.618  1.00 19.05           N  
ANISOU  948  NH1 ARG A 108     1888   2613   2735    196     46    274       N  
ATOM    949  NH2 ARG A 108      10.729   4.105  -0.935  1.00 23.19           N  
ANISOU  949  NH2 ARG A 108     2291   2934   3583    -12   -208   -348       N  
ATOM    950  N   GLU A 109      14.226   3.374   3.271  1.00 11.86           N  
ANISOU  950  N   GLU A 109     1078   1796   1631   -248    275   -292       N  
ATOM    951  CA  GLU A 109      15.129   2.263   3.026  1.00 13.93           C  
ANISOU  951  CA  GLU A 109     1521   2171   1599     49    111   -216       C  
ATOM    952  C   GLU A 109      14.371   1.299   2.166  1.00 12.65           C  
ANISOU  952  C   GLU A 109     1308   1886   1613    -82    249   -136       C  
ATOM    953  O   GLU A 109      13.403   0.714   2.628  1.00 13.76           O  
ANISOU  953  O   GLU A 109     1666   2065   1495   -243    254   -125       O  
ATOM    954  CB  GLU A 109      15.547   1.550   4.352  1.00 16.55           C  
ANISOU  954  CB  GLU A 109     1896   2456   1935     25    -39   -219       C  
ATOM    955  CG  GLU A 109      16.306   2.423   5.316  1.00 20.86           C  
ANISOU  955  CG  GLU A 109     2856   2683   2383    -27    -66   -190       C  
ATOM    956  CD  GLU A 109      17.713   2.679   4.857  1.00 29.23           C  
ANISOU  956  CD  GLU A 109     3624   4138   3342   -189    205   -494       C  
ATOM    957  OE1 GLU A 109      18.459   3.421   5.546  1.00 36.45           O  
ANISOU  957  OE1 GLU A 109     5208   4430   4210   -452   -475   -732       O  
ATOM    958  OE2 GLU A 109      18.119   2.162   3.780  1.00 38.20           O  
ANISOU  958  OE2 GLU A 109     5393   4965   4157    127    518   -620       O  
ATOM    959  N   ASP A 110      14.833   1.094   0.951  1.00 12.32           N  
ANISOU  959  N   ASP A 110     1368   1785   1526      8    137    -75       N  
ATOM    960  CA  ASP A 110      14.086   0.303  -0.012  1.00 12.46           C  
ANISOU  960  CA  ASP A 110     1423   1829   1480   -112    329    -15       C  
ATOM    961  C   ASP A 110      12.687   0.847  -0.071  1.00 11.09           C  
ANISOU  961  C   ASP A 110      875   2020   1315   -261    155   -184       C  
ATOM    962  O   ASP A 110      12.529   2.074  -0.188  1.00 12.12           O  
ANISOU  962  O   ASP A 110     1205   1735   1663   -213    245    -89       O  
ATOM    963  CB  ASP A 110      14.189  -1.181   0.259  1.00 14.71           C  
ANISOU  963  CB  ASP A 110     1892   1952   1743    -81    421   -185       C  
ATOM    964  CG  ASP A 110      15.589  -1.670   0.222  1.00 18.80           C  
ANISOU  964  CG  ASP A 110     2405   2296   2442    346    607    147       C  
ATOM    965  OD1 ASP A 110      16.391  -1.275  -0.698  1.00 22.73           O  
ANISOU  965  OD1 ASP A 110     2838   3012   2784    452    770   -102       O  
ATOM    966  OD2 ASP A 110      15.966  -2.508   1.071  1.00 28.92           O  
ANISOU  966  OD2 ASP A 110     4105   3290   3591    759    188    949       O  
ATOM    967  N   ASP A 111      11.631   0.040  -0.046  1.00 12.48           N  
ANISOU  967  N   ASP A 111     1040   2119   1582   -274     70   -382       N  
ATOM    968  CA  ASP A 111      10.289   0.519  -0.118  1.00 12.92           C  
ANISOU  968  CA  ASP A 111     1033   2288   1585   -486     51   -162       C  
ATOM    969  C   ASP A 111       9.694   0.862   1.257  1.00 12.35           C  
ANISOU  969  C   ASP A 111      740   2105   1845     -9    -77   -361       C  
ATOM    970  O   ASP A 111       8.548   1.190   1.313  1.00 15.37           O  
ANISOU  970  O   ASP A 111     1086   2743   2007     37   -134   -697       O  
ATOM    971  CB  ASP A 111       9.417  -0.495  -0.832  1.00 13.05           C  
ANISOU  971  CB  ASP A 111      802   2339   1815   -438     67   -192       C  
ATOM    972  CG  ASP A 111       9.706  -0.567  -2.317  1.00 15.36           C  
ANISOU  972  CG  ASP A 111     1409   2636   1789   -348     38   -397       C  
ATOM    973  OD1 ASP A 111       9.881   0.503  -2.923  1.00 18.20           O  
ANISOU  973  OD1 ASP A 111     2595   2519   1798   -509    158   -124       O  
ATOM    974  OD2 ASP A 111       9.737  -1.666  -2.847  1.00 19.77           O  
ANISOU  974  OD2 ASP A 111     3305   2418   1789   -310    261   -548       O  
ATOM    975  N   LYS A 112      10.565   0.857   2.276  1.00 12.84           N  
ANISOU  975  N   LYS A 112     1370   1771   1736   -175    181   -107       N  
ATOM    976  CA  LYS A 112      10.068   1.086   3.652  1.00 12.91           C  
ANISOU  976  CA  LYS A 112     1671   1768   1467    -94    333    -85       C  
ATOM    977  C   LYS A 112      10.429   2.464   4.129  1.00 10.92           C  
ANISOU  977  C   LYS A 112     1010   1637   1502   -248     59    -76       C  
ATOM    978  O   LYS A 112      11.301   3.132   3.606  1.00 11.69           O  
ANISOU  978  O   LYS A 112     1054   1788   1597   -383    225    -93       O  
ATOM    979  CB  LYS A 112      10.717   0.062   4.565  1.00 13.84           C  
ANISOU  979  CB  LYS A 112     1894   1718   1644     35    465   -135       C  
ATOM    980  CG  LYS A 112      10.417  -1.372   4.203  1.00 18.80           C  
ANISOU  980  CG  LYS A 112     2731   1991   2421     12    444   -163       C  
ATOM    981  CD  LYS A 112      11.351  -2.242   4.970  1.00 27.62           C  
ANISOU  981  CD  LYS A 112     3951   3074   3468    358    261   -173       C  
ATOM    982  CE  LYS A 112      12.666  -2.631   4.162  1.00 32.68           C  
ANISOU  982  CE  LYS A 112     4076   3910   4427     33    362     83       C  
ATOM    983  NZ  LYS A 112      13.811  -1.627   4.287  1.00 30.04           N  
ANISOU  983  NZ  LYS A 112     3916   3351   4145    -15    729    900       N  
ATOM    984  N  ALEU A 113       9.757   2.891   5.181  0.50 10.47           N  
ANISOU  984  N  ALEU A 113     1113   1448   1416   -173     97    -59       N  
ATOM    985  N  BLEU A 113       9.754   2.817   5.201  0.50 10.87           N  
ANISOU  985  N  BLEU A 113     1178   1536   1416   -213    141   -120       N  
ATOM    986  CA ALEU A 113      10.118   4.086   5.927  0.50 10.69           C  
ANISOU  986  CA ALEU A 113     1189   1509   1365    -76     20    -49       C  
ATOM    987  CA BLEU A 113      10.073   3.953   6.006  0.50 10.91           C  
ANISOU  987  CA BLEU A 113     1190   1548   1405   -232    172    -27       C  
ATOM    988  C  ALEU A 113      10.450   3.614   7.328  0.50  9.61           C  
ANISOU  988  C  ALEU A 113      895   1373   1382     94    104    -91       C  
ATOM    989  C  BLEU A 113      10.510   3.416   7.346  0.50 10.22           C  
ANISOU  989  C  BLEU A 113     1034   1455   1395    -79    182   -115       C  
ATOM    990  O  ALEU A 113       9.579   3.127   8.041  0.50 10.25           O  
ANISOU  990  O  ALEU A 113     1295   1177   1420     99    135   -104       O  
ATOM    991  O  BLEU A 113       9.849   2.639   8.003  0.50  9.57           O  
ANISOU  991  O  BLEU A 113      887   1237   1510    -29    232     61       O  
ATOM    992  CB ALEU A 113       8.955   5.060   5.893  0.50 12.03           C  
ANISOU  992  CB ALEU A 113     1537   1628   1406   -253     27     31       C  
ATOM    993  CB BLEU A 113       8.873   4.853   6.090  0.50 12.75           C  
ANISOU  993  CB BLEU A 113     1674   1664   1506   -313    124    -77       C  
ATOM    994  CG ALEU A 113       9.237   6.440   6.497  0.50 11.72           C  
ANISOU  994  CG ALEU A 113      694   1905   1851    174    -75    -92       C  
ATOM    995  CG BLEU A 113       9.203   6.109   6.873  0.50 14.35           C  
ANISOU  995  CG BLEU A 113     1677   1974   1798   -376    -69   -113       C  
ATOM    996  CD1ALEU A 113       8.100   7.289   6.099  0.50 12.51           C  
ANISOU  996  CD1ALEU A 113     1263   1856   1634     -6   -133   -184       C  
ATOM    997  CD1BLEU A 113      10.325   6.958   6.167  0.50 15.52           C  
ANISOU  997  CD1BLEU A 113     1376   1975   2545   -421    220   -236       C  
ATOM    998  CD2ALEU A 113       9.281   6.442   7.985  0.50 15.21           C  
ANISOU  998  CD2ALEU A 113     1635   2211   1931    248    210    121       C  
ATOM    999  CD2BLEU A 113       7.972   6.913   6.981  0.50 17.73           C  
ANISOU  999  CD2BLEU A 113     1831   2503   2402   -109   -145   -386       C  
ATOM   1000  N   VAL A 114      11.731   3.737   7.702  1.00 10.68           N  
ANISOU 1000  N   VAL A 114     1258   1458   1343    -94     13     37       N  
ATOM   1001  CA  VAL A 114      12.274   3.257   8.958  1.00 12.21           C  
ANISOU 1001  CA  VAL A 114     1693   1462   1481   -139      9     91       C  
ATOM   1002  C   VAL A 114      12.392   4.423   9.921  1.00 12.42           C  
ANISOU 1002  C   VAL A 114     1771   1592   1355   -416   -114    134       C  
ATOM   1003  O   VAL A 114      12.837   5.507   9.584  1.00 12.56           O  
ANISOU 1003  O   VAL A 114     1794   1548   1428   -462     70     -9       O  
ATOM   1004  CB  VAL A 114      13.634   2.646   8.728  1.00 14.16           C  
ANISOU 1004  CB  VAL A 114     1968   1763   1650   -210    113    233       C  
ATOM   1005  CG1 VAL A 114      14.245   2.163  10.029  1.00 15.54           C  
ANISOU 1005  CG1 VAL A 114     1325   2410   2166    -64   -100    189       C  
ATOM   1006  CG2 VAL A 114      13.508   1.473   7.676  1.00 17.04           C  
ANISOU 1006  CG2 VAL A 114     2469   1985   2017     59    153   -145       C  
ATOM   1007  N   VAL A 115      11.877   4.200  11.111  1.00 12.62           N  
ANISOU 1007  N   VAL A 115     1983   1421   1388   -448   -151     64       N  
ATOM   1008  CA  VAL A 115      11.820   5.173  12.181  1.00 12.33           C  
ANISOU 1008  CA  VAL A 115     1903   1352   1427   -393   -150     62       C  
ATOM   1009  C   VAL A 115      12.719   4.692  13.314  1.00 12.17           C  
ANISOU 1009  C   VAL A 115     1875   1417   1331   -240   -185    195       C  
ATOM   1010  O   VAL A 115      12.486   3.637  13.874  1.00 16.01           O  
ANISOU 1010  O   VAL A 115     2527   1767   1787   -581   -583    373       O  
ATOM   1011  CB  VAL A 115      10.398   5.426  12.648  1.00 13.33           C  
ANISOU 1011  CB  VAL A 115     1952   1549   1562   -321     14     71       C  
ATOM   1012  CG1 VAL A 115      10.403   6.533  13.683  1.00 16.13           C  
ANISOU 1012  CG1 VAL A 115     2316   1989   1822   -106    127     -2       C  
ATOM   1013  CG2 VAL A 115       9.462   5.738  11.457  1.00 16.62           C  
ANISOU 1013  CG2 VAL A 115     2221   1972   2119   -573   -413    306       C  
ATOM   1014  N  AGLU A 116      13.694   5.489  13.706  0.50 11.10           N  
ANISOU 1014  N  AGLU A 116     1552   1282   1383   -104   -129     67       N  
ATOM   1015  N  BGLU A 116      13.711   5.468  13.694  0.50 11.53           N  
ANISOU 1015  N  BGLU A 116     1644   1315   1422   -141   -100     79       N  
ATOM   1016  CA AGLU A 116      14.631   5.181  14.789  0.50 10.94           C  
ANISOU 1016  CA AGLU A 116     1333   1207   1616     44   -128    100       C  
ATOM   1017  CA BGLU A 116      14.556   5.122  14.829  0.50 11.78           C  
ANISOU 1017  CA BGLU A 116     1511   1327   1636    -22     -1    120       C  
ATOM   1018  C  AGLU A 116      14.363   6.188  15.873  0.50 11.62           C  
ANISOU 1018  C  AGLU A 116     1674   1248   1490     -2   -273    -27       C  
ATOM   1019  C  BGLU A 116      14.374   6.172  15.875  0.50 12.10           C  
ANISOU 1019  C  BGLU A 116     1760   1298   1539    -57   -225      0       C  
ATOM   1020  O  AGLU A 116      14.526   7.385  15.661  0.50 12.60           O  
ANISOU 1020  O  AGLU A 116     2066   1163   1557    -32   -219     81       O  
ATOM   1021  O  BGLU A 116      14.569   7.364  15.639  0.50 12.86           O  
ANISOU 1021  O  BGLU A 116     2105   1172   1609    -65   -220     84       O  
ATOM   1022  CB AGLU A 116      16.073   5.323  14.275  0.50 11.90           C  
ANISOU 1022  CB AGLU A 116     1252   1265   2002    289   -186     20       C  
ATOM   1023  CB BGLU A 116      16.014   4.942  14.426  0.50 13.59           C  
ANISOU 1023  CB BGLU A 116     1581   1518   2065      5    -61    208       C  
ATOM   1024  CG AGLU A 116      17.178   4.865  15.242  0.50 15.38           C  
ANISOU 1024  CG AGLU A 116     1445   2293   2104     80   -163    309       C  
ATOM   1025  CG BGLU A 116      16.201   3.797  13.420  0.50 17.46           C  
ANISOU 1025  CG BGLU A 116     1717   2380   2536    153    297     96       C  
ATOM   1026  CD AGLU A 116      18.563   5.535  15.013  0.50 22.37           C  
ANISOU 1026  CD AGLU A 116     2309   3037   3151   -300   -325    462       C  
ATOM   1027  CD BGLU A 116      17.498   3.017  13.527  0.50 26.37           C  
ANISOU 1027  CD BGLU A 116     1960   3890   4167      0     29     90       C  
ATOM   1028  OE1AGLU A 116      18.689   6.794  14.951  0.50 24.62           O  
ANISOU 1028  OE1AGLU A 116     2486   3374   3494   -729     -9   1034       O  
ATOM   1029  OE1BGLU A 116      18.495   3.600  14.031  0.50 29.72           O  
ANISOU 1029  OE1BGLU A 116      469   5858   4965    472   -112    582       O  
ATOM   1030  OE2AGLU A 116      19.555   4.794  14.952  0.50 25.52           O  
ANISOU 1030  OE2AGLU A 116     3078   3264   3353     97   -117    804       O  
ATOM   1031  OE2BGLU A 116      17.557   1.814  13.057  0.50 30.21           O  
ANISOU 1031  OE2BGLU A 116     2701   4170   4606   -426    630     55       O  
ATOM   1032  N   CYS A 117      14.010   5.709  17.055  1.00 11.47           N  
ANISOU 1032  N   CYS A 117     1522   1348   1488     33   -207     43       N  
ATOM   1033  CA  CYS A 117      13.767   6.558  18.203  1.00 11.94           C  
ANISOU 1033  CA  CYS A 117     1468   1486   1581    184   -232     96       C  
ATOM   1034  C   CYS A 117      14.847   6.303  19.223  1.00 11.83           C  
ANISOU 1034  C   CYS A 117     1480   1405   1610    147   -248     28       C  
ATOM   1035  O   CYS A 117      15.068   5.181  19.617  1.00 12.55           O  
ANISOU 1035  O   CYS A 117     1786   1205   1774    -10   -526    175       O  
ATOM   1036  CB  CYS A 117      12.398   6.142  18.823  1.00 14.99           C  
ANISOU 1036  CB  CYS A 117     1639   2391   1663    627   -230    -56       C  
ATOM   1037  SG  CYS A 117      11.036   6.149  17.675  1.00 21.00           S  
ANISOU 1037  SG  CYS A 117     1681   4207   2089    191   -367    322       S  
ATOM   1038  N   VAL A 118      15.514   7.368  19.669  1.00 10.49           N  
ANISOU 1038  N   VAL A 118      833   1321   1829    155   -184     48       N  
ATOM   1039  CA  VAL A 118      16.676   7.250  20.512  1.00 11.60           C  
ANISOU 1039  CA  VAL A 118      700   1597   2109    164   -299    -73       C  
ATOM   1040  C   VAL A 118      16.502   8.113  21.769  1.00 11.82           C  
ANISOU 1040  C   VAL A 118     1055   1330   2106    172   -316    -39       C  
ATOM   1041  O   VAL A 118      16.192   9.318  21.691  1.00 13.25           O  
ANISOU 1041  O   VAL A 118     1857   1277   1898    198   -449    -50       O  
ATOM   1042  CB  VAL A 118      18.003   7.701  19.842  1.00 14.63           C  
ANISOU 1042  CB  VAL A 118      691   2024   2841    286   -111   -106       C  
ATOM   1043  CG1 VAL A 118      19.151   7.748  20.754  1.00 19.95           C  
ANISOU 1043  CG1 VAL A 118      570   3028   3983    148   -113   -112       C  
ATOM   1044  CG2 VAL A 118      18.340   6.822  18.660  1.00 19.64           C  
ANISOU 1044  CG2 VAL A 118     2369   2205   2888      1    525    -69       C  
ATOM   1045  N   MET A 119      16.714   7.512  22.917  1.00 13.52           N  
ANISOU 1045  N   MET A 119     1781   1424   1932    296   -607     -8       N  
ATOM   1046  CA  MET A 119      16.767   8.246  24.176  1.00 14.78           C  
ANISOU 1046  CA  MET A 119     1935   1674   2006    239   -560     67       C  
ATOM   1047  C   MET A 119      17.935   7.655  24.915  1.00 16.45           C  
ANISOU 1047  C   MET A 119     2073   1936   2238     52   -686     -9       C  
ATOM   1048  O   MET A 119      17.945   6.498  25.298  1.00 15.28           O  
ANISOU 1048  O   MET A 119     1973   1799   2033    228   -736    -67       O  
ATOM   1049  CB  MET A 119      15.472   7.991  24.924  1.00 16.51           C  
ANISOU 1049  CB  MET A 119     2139   2151   1980    668   -580    -40       C  
ATOM   1050  CG  MET A 119      15.285   8.483  26.386  1.00 20.94           C  
ANISOU 1050  CG  MET A 119     3003   2468   2483    332   -614    -82       C  
ATOM   1051  SD  MET A 119      14.992  10.172  26.332  1.00 26.57           S  
ANISOU 1051  SD  MET A 119     4648   2439   3006   1038  -1528   -485       S  
ATOM   1052  CE  MET A 119      15.037  10.809  27.961  1.00 20.96           C  
ANISOU 1052  CE  MET A 119     3026   2201   2735   -341   -438   -343       C  
ATOM   1053  N  ALYS A 120      18.970   8.457  25.165  0.50 19.92           N  
ANISOU 1053  N  ALYS A 120     2310   2420   2837     76   -470     31       N  
ATOM   1054  N  BLYS A 120      18.926   8.530  25.036  0.50 16.73           N  
ANISOU 1054  N  BLYS A 120     1712   2100   2542    125   -478     33       N  
ATOM   1055  CA ALYS A 120      20.250   7.991  25.779  0.50 22.21           C  
ANISOU 1055  CA ALYS A 120     2535   2824   3079      4   -345     12       C  
ATOM   1056  CA BLYS A 120      20.167   8.198  25.627  0.50 16.79           C  
ANISOU 1056  CA BLYS A 120     1729   2093   2557      2   -388     70       C  
ATOM   1057  C  ALYS A 120      20.561   6.475  25.846  0.50 20.95           C  
ANISOU 1057  C  ALYS A 120     2243   2730   2984    -68   -280    -27       C  
ATOM   1058  C  BLYS A 120      20.726   6.958  24.866  0.50 14.39           C  
ANISOU 1058  C  BLYS A 120     1330   1913   2224     56   -389    119       C  
ATOM   1059  O  ALYS A 120      20.331   5.797  26.863  0.50 22.60           O  
ANISOU 1059  O  ALYS A 120     2448   2952   3186   -103   -490   -183       O  
ATOM   1060  O  BLYS A 120      20.925   6.974  23.622  0.50 15.14           O  
ANISOU 1060  O  BLYS A 120     1263   1926   2561    295   -186    263       O  
ATOM   1061  CB ALYS A 120      20.361   8.531  27.186  0.50 23.93           C  
ANISOU 1061  CB ALYS A 120     2877   3006   3207     58   -338      4       C  
ATOM   1062  CB BLYS A 120      19.905   7.948  27.138  0.50 16.10           C  
ANISOU 1062  CB BLYS A 120     1830   1840   2443      7   -520     -9       C  
ATOM   1063  CG ALYS A 120      19.188   8.193  28.068  0.50 25.66           C  
ANISOU 1063  CG ALYS A 120     3127   3352   3267    171   -307    110       C  
ATOM   1064  CG BLYS A 120      19.462   9.250  27.890  0.50 18.68           C  
ANISOU 1064  CG BLYS A 120     2198   2154   2744     39   -467   -227       C  
ATOM   1065  CD ALYS A 120      18.845   9.438  28.880  0.50 29.59           C  
ANISOU 1065  CD ALYS A 120     3819   3581   3842    164    -68    -34       C  
ATOM   1066  CD BLYS A 120      18.762   8.915  29.194  0.50 25.58           C  
ANISOU 1066  CD BLYS A 120     3342   3206   3170    227   -177   -194       C  
ATOM   1067  CE ALYS A 120      19.051   9.267  30.374  0.50 32.57           C  
ANISOU 1067  CE ALYS A 120     4159   4085   4129    136   -137     33       C  
ATOM   1068  CE BLYS A 120      19.720   8.824  30.362  0.50 29.71           C  
ANISOU 1068  CE BLYS A 120     3665   3870   3753    126   -251    -66       C  
ATOM   1069  NZ ALYS A 120      17.933   8.492  30.996  0.50 33.98           N  
ANISOU 1069  NZ ALYS A 120     4030   4302   4578    -36    -80    -89       N  
ATOM   1070  NZ BLYS A 120      18.898   8.779  31.608  0.50 32.07           N  
ANISOU 1070  NZ BLYS A 120     4095   4363   3725    215   -134     14       N  
ATOM   1071  N  AGLY A 121      21.176   5.986  24.772  0.50 19.50           N  
ANISOU 1071  N  AGLY A 121     1954   2604   2849   -168   -242    -11       N  
ATOM   1072  N  BGLY A 121      21.041   5.868  25.574  0.50 13.81           N  
ANISOU 1072  N  BGLY A 121     1302   1865   2077   -132   -278    162       N  
ATOM   1073  CA AGLY A 121      21.637   4.620  24.654  0.50 17.20           C  
ANISOU 1073  CA AGLY A 121     1129   2636   2766   -154    -82     63       C  
ATOM   1074  CA BGLY A 121      21.599   4.746  24.875  0.50 14.28           C  
ANISOU 1074  CA BGLY A 121      735   2282   2406   -103   -189    168       C  
ATOM   1075  C  AGLY A 121      20.554   3.658  24.271  0.50 13.81           C  
ANISOU 1075  C  AGLY A 121      282   2431   2532   -217   -140    118       C  
ATOM   1076  C  BGLY A 121      20.599   3.739  24.362  0.50 12.39           C  
ANISOU 1076  C  BGLY A 121      303   2201   2204   -185   -267    175       C  
ATOM   1077  O  AGLY A 121      20.845   2.562  23.783  0.50 15.22           O  
ANISOU 1077  O  AGLY A 121      494   2449   2840   -352    131    225       O  
ATOM   1078  O  BGLY A 121      21.074   2.708  23.870  0.50 15.41           O  
ANISOU 1078  O  BGLY A 121     1411   2101   2342    361   -257    433       O  
ATOM   1079  N   VAL A 122      19.316   4.025  24.448  1.00 11.93           N  
ANISOU 1079  N   VAL A 122      616   1828   2089     -2   -164    248       N  
ATOM   1080  CA  VAL A 122      18.242   3.127  24.080  1.00 11.40           C  
ANISOU 1080  CA  VAL A 122      262   1919   2151     54    -59    193       C  
ATOM   1081  C   VAL A 122      17.625   3.553  22.747  1.00 12.05           C  
ANISOU 1081  C   VAL A 122     1070   1654   1852    157   -214    174       C  
ATOM   1082  O   VAL A 122      17.182   4.705  22.606  1.00 14.53           O  
ANISOU 1082  O   VAL A 122     2088   1362   2068    419   -674     26       O  
ATOM   1083  CB  VAL A 122      17.198   3.047  25.139  1.00 12.45           C  
ANISOU 1083  CB  VAL A 122      265   2039   2425    137    -37    317       C  
ATOM   1084  CG1 VAL A 122      16.110   2.169  24.749  1.00 15.83           C  
ANISOU 1084  CG1 VAL A 122      311   3010   2693    311    278    368       C  
ATOM   1085  CG2 VAL A 122      17.747   2.584  26.510  1.00 14.40           C  
ANISOU 1085  CG2 VAL A 122      736   2517   2217    152    277    315       C  
ATOM   1086  N   THR A 123      17.642   2.629  21.802  1.00 12.24           N  
ANISOU 1086  N   THR A 123     1237   1406   2007    173   -317    164       N  
ATOM   1087  CA  THR A 123      17.080   2.847  20.489  1.00 12.90           C  
ANISOU 1087  CA  THR A 123     1448   1562   1889    158   -243     84       C  
ATOM   1088  C   THR A 123      15.947   1.877  20.228  1.00 12.72           C  
ANISOU 1088  C   THR A 123     1624   1291   1917     39   -458    101       C  
ATOM   1089  O   THR A 123      16.048   0.686  20.515  1.00 16.22           O  
ANISOU 1089  O   THR A 123     1894   1372   2896     56   -592    359       O  
ATOM   1090  CB  THR A 123      18.107   2.621  19.439  1.00 15.62           C  
ANISOU 1090  CB  THR A 123     1812   2052   2068   -154   -215    -39       C  
ATOM   1091  OG1 THR A 123      19.151   3.511  19.663  1.00 19.54           O  
ANISOU 1091  OG1 THR A 123     2097   2645   2682    -39    364      0       O  
ATOM   1092  CG2 THR A 123      17.541   2.872  18.022  1.00 16.59           C  
ANISOU 1092  CG2 THR A 123      717   3240   2343     83    225    243       C  
ATOM   1093  N   SER A 124      14.941   2.360  19.592  1.00 12.35           N  
ANISOU 1093  N   SER A 124     1639   1328   1725   -144   -492    153       N  
ATOM   1094  CA  SER A 124      13.867   1.547  19.046  1.00 12.33           C  
ANISOU 1094  CA  SER A 124     1450   1434   1800   -131   -282    299       C  
ATOM   1095  C   SER A 124      13.762   1.762  17.584  1.00 10.63           C  
ANISOU 1095  C   SER A 124      958   1429   1651     34   -165    204       C  
ATOM   1096  O   SER A 124      13.883   2.868  17.111  1.00 13.98           O  
ANISOU 1096  O   SER A 124     2286   1353   1674   -147   -235    178       O  
ATOM   1097  CB  SER A 124      12.536   1.843  19.736  1.00 12.48           C  
ANISOU 1097  CB  SER A 124     1084   1755   1904   -265   -306    247       C  
ATOM   1098  OG  SER A 124      11.443   1.205  19.106  1.00 14.29           O  
ANISOU 1098  OG  SER A 124     1371   2072   1986   -158   -118     90       O  
ATOM   1099  N   THR A 125      13.559   0.694  16.818  1.00 11.85           N  
ANISOU 1099  N   THR A 125     1576   1275   1650    -96   -205    199       N  
ATOM   1100  CA  THR A 125      13.367   0.741  15.381  1.00 12.27           C  
ANISOU 1100  CA  THR A 125     1417   1512   1733    -30    -43    234       C  
ATOM   1101  C   THR A 125      11.994   0.278  15.021  1.00 11.43           C  
ANISOU 1101  C   THR A 125     1159   1571   1609   -313   -160    138       C  
ATOM   1102  O   THR A 125      11.630  -0.831  15.382  1.00 13.97           O  
ANISOU 1102  O   THR A 125     1861   1536   1911   -426   -295    310       O  
ATOM   1103  CB  THR A 125      14.453  -0.112  14.670  1.00 15.13           C  
ANISOU 1103  CB  THR A 125     1669   1936   2144    280    -46    -83       C  
ATOM   1104  OG1 THR A 125      15.756   0.389  15.015  1.00 19.97           O  
ANISOU 1104  OG1 THR A 125     1705   2783   3097    477    -67   -255       O  
ATOM   1105  CG2 THR A 125      14.326  -0.039  13.174  1.00 18.38           C  
ANISOU 1105  CG2 THR A 125     2166   2661   2157    321    342   -195       C  
ATOM   1106  N   ARG A 126      11.277   1.112  14.295  1.00 12.09           N  
ANISOU 1106  N   ARG A 126     1567   1479   1546   -344   -169    214       N  
ATOM   1107  CA  ARG A 126       9.935   0.853  13.824  1.00 12.19           C  
ANISOU 1107  CA  ARG A 126     1424   1667   1539   -425   -221    270       C  
ATOM   1108  C   ARG A 126       9.949   0.920  12.313  1.00 12.79           C  
ANISOU 1108  C   ARG A 126     1514   1783   1562   -401   -125    290       C  
ATOM   1109  O   ARG A 126      10.500   1.846  11.732  1.00 16.21           O  
ANISOU 1109  O   ARG A 126     2412   2185   1561   -962   -215    230       O  
ATOM   1110  CB  ARG A 126       8.982   1.838  14.447  1.00 13.62           C  
ANISOU 1110  CB  ARG A 126     1529   2056   1589   -343    -48    132       C  
ATOM   1111  CG  ARG A 126       8.829   1.494  15.966  1.00 19.67           C  
ANISOU 1111  CG  ARG A 126     2503   2844   2125     85    125     15       C  
ATOM   1112  CD  ARG A 126       8.154   2.440  16.796  1.00 21.93           C  
ANISOU 1112  CD  ARG A 126     2449   3553   2329    -62     25    -89       C  
ATOM   1113  NE  ARG A 126       6.743   2.668  16.604  1.00 22.77           N  
ANISOU 1113  NE  ARG A 126     2228   3929   2492    -34     83   -166       N  
ATOM   1114  CZ  ARG A 126       5.717   2.037  17.193  1.00 22.62           C  
ANISOU 1114  CZ  ARG A 126     2683   3926   1986   -456     83   -124       C  
ATOM   1115  NH1 ARG A 126       5.847   0.849  17.766  1.00 23.88           N  
ANISOU 1115  NH1 ARG A 126     2760   4217   2093    -94   -411   -234       N  
ATOM   1116  NH2 ARG A 126       4.517   2.489  17.006  1.00 26.51           N  
ANISOU 1116  NH2 ARG A 126     3323   3769   2978   -200    195     45       N  
ATOM   1117  N   VAL A 127       9.295  -0.022  11.655  1.00 11.28           N  
ANISOU 1117  N   VAL A 127     1363   1492   1431   -254    -17     97       N  
ATOM   1118  CA  VAL A 127       9.357  -0.096  10.208  1.00 11.79           C  
ANISOU 1118  CA  VAL A 127     1347   1563   1568     21     10     78       C  
ATOM   1119  C   VAL A 127       7.930  -0.011   9.700  1.00 10.45           C  
ANISOU 1119  C   VAL A 127     1162   1410   1398     38    -49    -30       C  
ATOM   1120  O   VAL A 127       7.067  -0.732  10.161  1.00 11.23           O  
ANISOU 1120  O   VAL A 127     1196   1524   1545   -217     63    112       O  
ATOM   1121  CB  VAL A 127      10.034  -1.416   9.716  1.00 12.32           C  
ANISOU 1121  CB  VAL A 127      688   2013   1980     84      0     77       C  
ATOM   1122  CG1 VAL A 127      10.021  -1.520   8.194  1.00 15.65           C  
ANISOU 1122  CG1 VAL A 127     1807   2364   1773    343     38   -215       C  
ATOM   1123  CG2 VAL A 127      11.336  -1.564  10.312  1.00 14.84           C  
ANISOU 1123  CG2 VAL A 127      545   2523   2567    264    158    -71       C  
ATOM   1124  N   TYR A 128       7.742   0.907   8.750  1.00 10.67           N  
ANISOU 1124  N   TYR A 128     1157   1406   1491   -168     30    -33       N  
ATOM   1125  CA  TYR A 128       6.494   1.141   8.046  1.00 10.56           C  
ANISOU 1125  CA  TYR A 128     1157   1471   1381    -64    -70      9       C  
ATOM   1126  C   TYR A 128       6.611   0.759   6.599  1.00 11.62           C  
ANISOU 1126  C   TYR A 128     1234   1539   1640   -117    -46     10       C  
ATOM   1127  O   TYR A 128       7.662   0.956   5.974  1.00 11.81           O  
ANISOU 1127  O   TYR A 128     1389   1603   1494   -227     12   -128       O  
ATOM   1128  CB  TYR A 128       6.107   2.578   8.150  1.00 10.50           C  
ANISOU 1128  CB  TYR A 128      969   1617   1400   -107    -42     20       C  
ATOM   1129  CG  TYR A 128       5.723   3.095   9.520  1.00 10.59           C  
ANISOU 1129  CG  TYR A 128      914   1345   1764   -221   -181     94       C  
ATOM   1130  CD1 TYR A 128       6.709   3.349  10.473  1.00 12.29           C  
ANISOU 1130  CD1 TYR A 128     1177   1605   1885    -88    -49    -57       C  
ATOM   1131  CD2 TYR A 128       4.406   3.337   9.854  1.00 11.60           C  
ANISOU 1131  CD2 TYR A 128      937   1699   1768   -222    -89    132       C  
ATOM   1132  CE1 TYR A 128       6.319   3.866  11.753  1.00 14.17           C  
ANISOU 1132  CE1 TYR A 128     1543   2028   1811    -24    -44   -170       C  
ATOM   1133  CE2 TYR A 128       4.050   3.833  11.088  1.00 13.54           C  
ANISOU 1133  CE2 TYR A 128     1386   1902   1856   -250    183    -16       C  
ATOM   1134  CZ  TYR A 128       4.999   4.085  12.020  1.00 14.33           C  
ANISOU 1134  CZ  TYR A 128     1657   2108   1679   -138    360    -76       C  
ATOM   1135  OH  TYR A 128       4.592   4.575  13.257  1.00 19.12           O  
ANISOU 1135  OH  TYR A 128     2968   2596   1697    285    251   -280       O  
ATOM   1136  N   GLU A 129       5.497   0.257   6.061  1.00 11.89           N  
ANISOU 1136  N   GLU A 129     1283   1638   1594   -166    -92   -202       N  
ATOM   1137  CA  GLU A 129       5.388  -0.031   4.655  1.00 13.72           C  
ANISOU 1137  CA  GLU A 129     1692   1769   1752     84   -187   -190       C  
ATOM   1138  C   GLU A 129       4.268   0.790   4.079  1.00 12.49           C  
ANISOU 1138  C   GLU A 129     1593   1642   1508   -136   -192   -321       C  
ATOM   1139  O   GLU A 129       3.424   1.270   4.778  1.00 12.66           O  
ANISOU 1139  O   GLU A 129     1620   1555   1634    -14    -88    -61       O  
ATOM   1140  CB  GLU A 129       5.154  -1.522   4.409  1.00 16.55           C  
ANISOU 1140  CB  GLU A 129     2211   1924   2151    305   -318   -196       C  
ATOM   1141  CG  GLU A 129       6.421  -2.283   4.822  1.00 25.12           C  
ANISOU 1141  CG  GLU A 129     3309   3015   3220    587   -346   -176       C  
ATOM   1142  CD  GLU A 129       6.624  -3.668   4.239  1.00 34.16           C  
ANISOU 1142  CD  GLU A 129     4754   3747   4475    624   -560   -627       C  
ATOM   1143  OE1 GLU A 129       5.643  -4.235   3.676  1.00 40.20           O  
ANISOU 1143  OE1 GLU A 129     5656   4025   5593    -83   -809   -797       O  
ATOM   1144  OE2 GLU A 129       7.792  -4.170   4.371  1.00 38.86           O  
ANISOU 1144  OE2 GLU A 129     5427   3945   5392   1193   -762   -674       O  
ATOM   1145  N   ARG A 130       4.238   0.921   2.768  1.00 13.79           N  
ANISOU 1145  N   ARG A 130     1773   1837   1627      7   -165   -323       N  
ATOM   1146  CA  ARG A 130       3.142   1.663   2.122  1.00 14.33           C  
ANISOU 1146  CA  ARG A 130     1808   1949   1688     -8   -195   -208       C  
ATOM   1147  C   ARG A 130       1.839   0.994   2.360  1.00 15.76           C  
ANISOU 1147  C   ARG A 130     1746   2118   2124   -229   -441   -460       C  
ATOM   1148  O   ARG A 130       1.734  -0.233   2.219  1.00 17.42           O  
ANISOU 1148  O   ARG A 130     1533   2198   2887     36   -790   -561       O  
ATOM   1149  CB  ARG A 130       3.367   1.714   0.647  1.00 17.61           C  
ANISOU 1149  CB  ARG A 130     2352   2450   1887     74   -370    -27       C  
ATOM   1150  CG  ARG A 130       4.496   2.465   0.244  1.00 18.18           C  
ANISOU 1150  CG  ARG A 130     2268   2678   1962    290   -216    192       C  
ATOM   1151  CD  ARG A 130       4.230   3.873   0.081  1.00 22.01           C  
ANISOU 1151  CD  ARG A 130     2081   2704   3578   -122   -285     80       C  
ATOM   1152  NE  ARG A 130       5.377   4.589  -0.463  1.00 20.88           N  
ANISOU 1152  NE  ARG A 130     2273   2182   3475    -81   -199    136       N  
ATOM   1153  CZ  ARG A 130       5.439   5.910  -0.601  1.00 16.20           C  
ANISOU 1153  CZ  ARG A 130     1368   2201   2586   -277   -388    252       C  
ATOM   1154  NH1 ARG A 130       4.415   6.636  -0.377  1.00 18.64           N  
ANISOU 1154  NH1 ARG A 130     2096   2655   2329    239   -292     95       N  
ATOM   1155  NH2 ARG A 130       6.595   6.443  -0.961  1.00 19.51           N  
ANISOU 1155  NH2 ARG A 130     1941   2883   2587      4    153    166       N  
ATOM   1156  N   ALA A 131       0.865   1.774   2.708  1.00 17.30           N  
ANISOU 1156  N   ALA A 131     1799   2204   2569   -336   -471   -382       N  
ATOM   1157  CA  ALA A 131      -0.447   1.201   2.989  1.00 21.39           C  
ANISOU 1157  CA  ALA A 131     2024   2754   3346   -383   -440   -103       C  
ATOM   1158  C   ALA A 131      -1.132   0.691   1.707  1.00 24.33           C  
ANISOU 1158  C   ALA A 131     2419   3067   3755   -527   -462    -69       C  
ATOM   1159  O   ALA A 131      -0.707   1.097   0.603  1.00 27.60           O  
ANISOU 1159  O   ALA A 131     2839   3765   3880   -534   -947      9       O  
ATOM   1160  CB  ALA A 131      -1.269   2.194   3.760  1.00 23.65           C  
ANISOU 1160  CB  ALA A 131     2259   2901   3824   -477     25   -198       C  
ATOM   1161  OXT ALA A 131      -2.046  -0.189   1.711  1.00 28.95           O  
ANISOU 1161  OXT ALA A 131     3224   3449   4325   -778   -455     47       O  
TER    1162      ALA A 131                                                      
HETATM 1163  O   HOH A 132       4.795  28.336   0.125  1.00 34.67           O  
ANISOU 1163  O   HOH A 132     2973   4917   5281   -720    265   1439       O  
HETATM 1164  O   HOH A 133      16.168  21.669  32.708  1.00 47.11           O  
ANISOU 1164  O   HOH A 133     8901   3980   5019  -2336    981  -1362       O  
HETATM 1165  O   HOH A 134       8.309   7.699  18.964  1.00 43.74           O  
ANISOU 1165  O   HOH A 134     2172   9002   5443   1010   -273   -454       O  
HETATM 1166  O   HOH A 135       4.077  13.326  15.489  1.00 53.68           O  
ANISOU 1166  O   HOH A 135    10002   3629   6764   -649   3272     17       O  
HETATM 1167  O   HOH A 136      11.582  30.678   2.450  1.00 44.40           O  
ANISOU 1167  O   HOH A 136     4435   7018   5415  -1451   -361    627       O  
HETATM 1168  O   HOH A 137       9.011  -3.989   0.941  1.00 36.55           O  
ANISOU 1168  O   HOH A 137     1838   5371   6678   -139    543   2310       O  
HETATM 1169  O   HOH A 138       5.759  14.677  31.040  1.00 45.94           O  
ANISOU 1169  O   HOH A 138     9591   4034   3828   1083    419   -258       O  
HETATM 1170  O   HOH A 139      19.672  20.035   8.359  1.00126.19           O  
ANISOU 1170  O   HOH A 139    12732  14821  20392  -7585   6939  -7171       O  
HETATM 1171  O   HOH A 140      10.437  22.065  12.821  1.00 10.34           O  
ANISOU 1171  O   HOH A 140     1122   1259   1546     97    107     99       O  
HETATM 1172  O   HOH A 141      13.268  27.523   8.366  1.00 37.90           O  
ANISOU 1172  O   HOH A 141     3711   5070   5619    167   1323  -1857       O  
HETATM 1173  O   HOH A 142      18.844  17.898  14.852  1.00 39.29           O  
ANISOU 1173  O   HOH A 142     2581   4173   8172   -529  -1097      1       O  
HETATM 1174  O   HOH A 143      10.039  16.224   4.262  1.00 45.18           O  
ANISOU 1174  O   HOH A 143     5836   6897   4433   2295   -884  -1106       O  
HETATM 1175  O   HOH A 144       7.200  24.888  12.435  1.00 11.00           O  
ANISOU 1175  O   HOH A 144      639   1811   1730   -123      0   -362       O  
HETATM 1176  O   HOH A 145       3.237  -4.169   4.312  1.00 39.35           O  
ANISOU 1176  O   HOH A 145     4794   4732   5425   -120     62   -601       O  
HETATM 1177  O   HOH A 146      13.421  -7.454  20.030  1.00 42.40           O  
ANISOU 1177  O   HOH A 146     3136   5934   7039    746  -1086   -400       O  
HETATM 1178  O   HOH A 147      14.880  -5.527  22.437  0.50 24.55           O  
ANISOU 1178  O   HOH A 147     4242   1884   3199     -8  -1430     73       O  
HETATM 1179  O   HOH A 148      18.248   0.820   1.630  1.00 46.81           O  
ANISOU 1179  O   HOH A 148     2345   9835   5604    800    534   1378       O  
HETATM 1180  O   HOH A 149       3.313  21.342  24.105  1.00 42.14           O  
ANISOU 1180  O   HOH A 149     7698   4666   3645   2468   1382    247       O  
HETATM 1181  O   HOH A 150       3.838   5.298  16.427  1.00 45.29           O  
ANISOU 1181  O   HOH A 150     4721   6896   5589  -1619  -1035   1738       O  
HETATM 1182  O   HOH A 151       3.982   8.963  13.251  1.00 48.50           O  
ANISOU 1182  O   HOH A 151     5909   7875   4642  -1856   2100    663       O  
HETATM 1183  O   HOH A 152       5.328  -1.543  19.637  1.00 39.48           O  
ANISOU 1183  O   HOH A 152     3125   6145   5728  -1052   1155  -1969       O  
HETATM 1184  O   HOH A 153      -5.494  13.945  14.919  1.00 44.87           O  
ANISOU 1184  O   HOH A 153     4199   3335   9511   1958    625    441       O  
HETATM 1185  O   HOH A 154       2.271  -5.434  19.717  1.00 45.13           O  
ANISOU 1185  O   HOH A 154     6690   5853   4603   1419    781  -1638       O  
HETATM 1186  O   HOH A 155       6.868  -1.740  -3.655  1.00 50.14           O  
ANISOU 1186  O   HOH A 155     3367   9914   5767   -727    -38  -1346       O  
HETATM 1187  O   HOH A 156      10.870  -6.563  14.583  1.00 55.51           O  
ANISOU 1187  O   HOH A 156     6044   6230   8817   3472  -1708  -3830       O  
HETATM 1188  O   HOH A 157       0.350  -3.984  10.266  1.00 78.27           O  
ANISOU 1188  O   HOH A 157     6393  11546  11798  -3343   2394   -566       O  
HETATM 1189  O   HOH A 158       7.443  -6.283  15.510  1.00 28.33           O  
ANISOU 1189  O   HOH A 158     4227   2713   3822  -1108  -1195   1075       O  
HETATM 1190  O   HOH A 159      -7.187   9.577  19.664  1.00 32.85           O  
ANISOU 1190  O   HOH A 159     2898   5744   3839    562   1352    316       O  
HETATM 1191  O   HOH A 160      12.225  25.108 -14.809  1.00 34.78           O  
ANISOU 1191  O   HOH A 160     3813   4039   5360  -1021  -1291    539       O  
HETATM 1192  O   HOH A 161      -0.174   7.634  17.388  1.00 36.03           O  
ANISOU 1192  O   HOH A 161     4202   5227   4258   1305   1725   1024       O  
HETATM 1193  O   HOH A 162      12.527  -3.669  -1.861  1.00 27.13           O  
ANISOU 1193  O   HOH A 162     4719   3066   2521   -888    306   -107       O  
HETATM 1194  O   HOH A 163       0.997  20.248   5.153  1.00 15.57           O  
ANISOU 1194  O   HOH A 163     1351   2388   2175   -241   -262    393       O  
HETATM 1195  O   HOH A 164      13.759  26.668  15.418  1.00 13.56           O  
ANISOU 1195  O   HOH A 164     1575   1494   2082   -342   -402   -121       O  
HETATM 1196  O   HOH A 165       9.673  23.017   5.459  1.00 15.37           O  
ANISOU 1196  O   HOH A 165     1282   2846   1710    316    -13    178       O  
HETATM 1197  O   HOH A 166      16.183  18.691  14.170  1.00 20.71           O  
ANISOU 1197  O   HOH A 166     2571   2845   2450   -121   -286    106       O  
HETATM 1198  O   HOH A 167      -3.735  -0.636  22.106  1.00 14.07           O  
ANISOU 1198  O   HOH A 167     1313   1782   2250   -297   -352    322       O  
HETATM 1199  O   HOH A 168      11.785  12.324  12.111  1.00 13.40           O  
ANISOU 1199  O   HOH A 168     1759   1693   1639    205    170     55       O  
HETATM 1200  O   HOH A 169       1.762  12.848  14.281  1.00 23.67           O  
ANISOU 1200  O   HOH A 169     2744   3480   2766   -103    459   1333       O  
HETATM 1201  O   HOH A 170      15.475   8.911   3.223  1.00 19.86           O  
ANISOU 1201  O   HOH A 170     2489   2192   2864   -636    822      0       O  
HETATM 1202  O   HOH A 171       3.731  25.424  18.058  1.00 16.62           O  
ANISOU 1202  O   HOH A 171     1397   2648   2267    781    -92   -461       O  
HETATM 1203  O   HOH A 172       1.747  15.864  -0.123  1.00 22.89           O  
ANISOU 1203  O   HOH A 172     4629   2292   1774     54   -958   -151       O  
HETATM 1204  O   HOH A 173       4.056  27.190   2.550  1.00 18.26           O  
ANISOU 1204  O   HOH A 173     1459   2456   3021    109   -216    -34       O  
HETATM 1205  O   HOH A 174      13.280  21.532  19.910  1.00 19.99           O  
ANISOU 1205  O   HOH A 174     1881   3455   2257   -859    -89    -13       O  
HETATM 1206  O   HOH A 175       6.383  -0.339   1.278  1.00 21.27           O  
ANISOU 1206  O   HOH A 175     1471   3367   3243   -193    332  -1037       O  
HETATM 1207  O   HOH A 176       8.908  -3.083  19.991  1.00 18.65           O  
ANISOU 1207  O   HOH A 176     2437   2352   2297    -35   -401   -182       O  
HETATM 1208  O   HOH A 177       6.007  27.476  15.548  1.00 18.97           O  
ANISOU 1208  O   HOH A 177     1904   1985   3320     49   -675   -173       O  
HETATM 1209  O   HOH A 178       1.687   5.887   0.087  1.00 17.93           O  
ANISOU 1209  O   HOH A 178     2028   2514   2268   -112   -165   -292       O  
HETATM 1210  O   HOH A 179      -0.572  14.333   6.447  1.00 18.58           O  
ANISOU 1210  O   HOH A 179     2243   2116   2699    -16   -146     75       O  
HETATM 1211  O   HOH A 180      16.310  21.154   7.360  1.00 19.73           O  
ANISOU 1211  O   HOH A 180     2818   1808   2871   -374    364    327       O  
HETATM 1212  O   HOH A 181       2.684   6.692  13.453  1.00 25.25           O  
ANISOU 1212  O   HOH A 181     2752   2907   3931    -76    562    276       O  
HETATM 1213  O   HOH A 182       9.171  10.446  21.592  1.00 20.46           O  
ANISOU 1213  O   HOH A 182     2678   2606   2489   -276    383    336       O  
HETATM 1214  O   HOH A 183       7.117  27.732  11.909  1.00 17.89           O  
ANISOU 1214  O   HOH A 183     1194   2607   2995    207   -370   -413       O  
HETATM 1215  O   HOH A 184      17.804  -1.622  20.014  1.00 20.85           O  
ANISOU 1215  O   HOH A 184     2117   2345   3458    -70   -834   -144       O  
HETATM 1216  O   HOH A 185       6.361   9.252  -1.812  1.00 22.48           O  
ANISOU 1216  O   HOH A 185     2734   2571   3236   -455    766   -426       O  
HETATM 1217  O   HOH A 186       1.602  26.236   2.255  1.00 24.25           O  
ANISOU 1217  O   HOH A 186     2002   2103   5105   -333    529   -440       O  
HETATM 1218  O   HOH A 187      11.387  -2.789   0.739  1.00 20.92           O  
ANISOU 1218  O   HOH A 187     3272   2013   2664   -477     86    -35       O  
HETATM 1219  O   HOH A 188      15.953  -3.031  -2.876  1.00 27.96           O  
ANISOU 1219  O   HOH A 188     5673   2808   2139    542    -51    199       O  
HETATM 1220  O   HOH A 189      11.609  -5.788  20.936  1.00 26.21           O  
ANISOU 1220  O   HOH A 189     4031   1610   4318   -240    216    770       O  
HETATM 1221  O   HOH A 190       2.935   0.891  18.637  1.00 22.21           O  
ANISOU 1221  O   HOH A 190     1792   4330   2315   -746    209    -32       O  
HETATM 1222  O   HOH A 191      11.513  -3.079  13.603  1.00 24.17           O  
ANISOU 1222  O   HOH A 191     4045   2292   2847   -112     85   -146       O  
HETATM 1223  O   HOH A 192      -2.004  15.869  17.786  1.00 28.71           O  
ANISOU 1223  O   HOH A 192     5722   2585   2600   -859   1172   -607       O  
HETATM 1224  O   HOH A 193       2.760  14.020  18.164  1.00 30.13           O  
ANISOU 1224  O   HOH A 193     3834   3335   4276   -601   -287    662       O  
HETATM 1225  O   HOH A 194       4.964  29.088   4.408  1.00 30.78           O  
ANISOU 1225  O   HOH A 194     2907   3268   5518   -585   -735  -1111       O  
HETATM 1226  O   HOH A 195       8.708  -3.492  22.823  1.00 32.20           O  
ANISOU 1226  O   HOH A 195     6644   2518   3070  -1230   1176   -487       O  
HETATM 1227  O   HOH A 196      14.744   1.443  29.153  1.00 24.88           O  
ANISOU 1227  O   HOH A 196     2661   4043   2746   1052   -605    265       O  
HETATM 1228  O   HOH A 197      20.530   4.893  28.321  0.50 17.76           O  
ANISOU 1228  O   HOH A 197     2218   2040   2490    300    -15      5       O  
HETATM 1229  O   HOH A 198      17.603  13.243  27.860  1.00 26.96           O  
ANISOU 1229  O   HOH A 198     2622   3903   3718    510   -773   1062       O  
HETATM 1230  O   HOH A 199       2.191  -3.688  24.644  1.00 23.60           O  
ANISOU 1230  O   HOH A 199     2309   3503   3155    847   -180   -514       O  
HETATM 1231  O   HOH A 200      17.927  13.847  21.658  1.00 24.30           O  
ANISOU 1231  O   HOH A 200     2169   4265   2796  -1015   -200   -258       O  
HETATM 1232  O   HOH A 201      15.638  19.647  27.332  1.00 30.89           O  
ANISOU 1232  O   HOH A 201     6278   2464   2994  -1282  -1576   -223       O  
HETATM 1233  O   HOH A 202       8.769   4.913  32.734  1.00 31.27           O  
ANISOU 1233  O   HOH A 202     4329   3656   3896   -500  -1992    311       O  
HETATM 1234  O   HOH A 203       9.331  21.198  29.647  1.00 35.15           O  
ANISOU 1234  O   HOH A 203     6194   3420   3739   1575    330   -759       O  
HETATM 1235  O   HOH A 204      18.485   4.534   2.416  1.00 26.00           O  
ANISOU 1235  O   HOH A 204     3171   4338   2367   -147   -323   -242       O  
HETATM 1236  O   HOH A 205       0.443   5.078  32.157  1.00 26.11           O  
ANISOU 1236  O   HOH A 205     4131   3233   2557    -38    125   -206       O  
HETATM 1237  O  AHOH A 206       9.438  28.738  15.378  0.50 12.95           O  
ANISOU 1237  O  AHOH A 206      979   1831   2109   -296    427    -42       O  
HETATM 1238  O  BHOH A 206       9.043  28.761  16.837  0.50 22.39           O  
ANISOU 1238  O  BHOH A 206     2087   1758   4662   -111    306     13       O  
HETATM 1239  O   HOH A 207      -7.633   6.565  18.945  1.00 34.26           O  
ANISOU 1239  O   HOH A 207     3601   4089   5324    851   1867    -59       O  
HETATM 1240  O   HOH A 208       9.236  12.000  30.738  1.00 30.91           O  
ANISOU 1240  O   HOH A 208     5507   2933   3304    354   1745    617       O  
HETATM 1241  O   HOH A 209       6.671   5.673  14.928  1.00 30.31           O  
ANISOU 1241  O   HOH A 209     1498   6273   3742   -609     18  -1171       O  
HETATM 1242  O   HOH A 210      -0.705  18.669   3.818  1.00 23.04           O  
ANISOU 1242  O   HOH A 210     3128   2543   3083   -235  -1541    123       O  
HETATM 1243  O   HOH A 211       0.979  15.709  18.525  1.00 38.60           O  
ANISOU 1243  O   HOH A 211     7117   4851   2696  -2233   1236   -533       O  
HETATM 1244  O   HOH A 212       3.426  11.495  19.447  1.00 24.42           O  
ANISOU 1244  O   HOH A 212     1981   3717   3579   -554    551   -107       O  
HETATM 1245  O   HOH A 213       4.910  10.084  29.298  1.00 31.77           O  
ANISOU 1245  O   HOH A 213     5621   3094   3354    677    519   1471       O  
HETATM 1246  O   HOH A 214      -1.885  20.300  11.689  1.00 33.96           O  
ANISOU 1246  O   HOH A 214     3343   3431   6126   -791   2870      7       O  
HETATM 1247  O   HOH A 215      13.436  21.297  28.302  1.00 56.97           O  
ANISOU 1247  O   HOH A 215    12023   4892   4732   -204   -648   1448       O  
HETATM 1248  O   HOH A 216      12.019  -3.077  24.663  1.00 66.37           O  
ANISOU 1248  O   HOH A 216    20247   1591   3377  -3269   -341   1085       O  
HETATM 1249  O   HOH A 217       5.354  22.581  24.352  1.00 30.41           O  
ANISOU 1249  O   HOH A 217     4373   3271   3909    945   1619   -106       O  
HETATM 1250  O   HOH A 218       0.745  19.525  -1.762  1.00 54.24           O  
ANISOU 1250  O   HOH A 218     7066   6244   7298   4071  -3020  -4534       O  
HETATM 1251  O   HOH A 219      -7.202   2.564  23.459  1.00 24.69           O  
ANISOU 1251  O   HOH A 219     3455   2434   3490   -432    429   -410       O  
HETATM 1252  O   HOH A 220      18.536  11.354  24.264  1.00 87.96           O  
ANISOU 1252  O   HOH A 220     9372   4778  19269    157  -2320   2893       O  
HETATM 1253  O   HOH A 221       3.243  -2.292   1.083  1.00 34.84           O  
ANISOU 1253  O   HOH A 221     2979   4068   6190   -292    432  -1692       O  
HETATM 1254  O   HOH A 222       9.824  21.198   3.005  1.00 40.96           O  
ANISOU 1254  O   HOH A 222     7751   4530   3281    603    685   -474       O  
HETATM 1255  O   HOH A 223      -6.664   5.032  23.756  1.00 43.60           O  
ANISOU 1255  O   HOH A 223     6770   5611   4184  -1835    435   -993       O  
HETATM 1256  O   HOH A 224      11.336  24.946   4.402  1.00 36.30           O  
ANISOU 1256  O   HOH A 224     3316   6228   4247   -860    232   1530       O  
HETATM 1257  O   HOH A 225      -0.683  -5.053  17.525  1.00 32.67           O  
ANISOU 1257  O   HOH A 225     3734   2946   5733    100    905    428       O  
HETATM 1258  O   HOH A 226      20.729   4.608  17.613  1.00 50.20           O  
ANISOU 1258  O   HOH A 226     5494   6534   7044    544   3845   -761       O  
HETATM 1259  O   HOH A 227      -4.659  -2.380  24.090  1.00 12.15           O  
ANISOU 1259  O   HOH A 227     1049   1737   1828     36    -32    300       O  
HETATM 1260  O   HOH A 228      -0.357  -8.053  17.995  1.00 41.03           O  
ANISOU 1260  O   HOH A 228     4136   3897   7556    -45  -2378  -2159       O  
HETATM 1261  O   HOH A 229       0.252   3.599  -0.343  1.00 33.98           O  
ANISOU 1261  O   HOH A 229     2959   3358   6593     84  -2267   -128       O  
HETATM 1262  O   HOH A 230       3.058   8.167  31.031  1.00 33.92           O  
ANISOU 1262  O   HOH A 230     3133   4902   4852   1856   -510  -1266       O  
HETATM 1263  O   HOH A 231       3.122  12.288  30.073  1.00 40.05           O  
ANISOU 1263  O   HOH A 231     6024   4898   4295    267   -654   1457       O  
HETATM 1264  O   HOH A 232      15.451  -5.826  19.490  1.00 29.93           O  
ANISOU 1264  O   HOH A 232     1869   4469   5032   -102   -635   1172       O  
HETATM 1265  O   HOH A 233       6.252  11.502  19.695  1.00 32.77           O  
ANISOU 1265  O   HOH A 233     2255   4090   6103   -950    429   -892       O  
HETATM 1266  O   HOH A 234      10.503  -4.066  27.937  1.00 43.35           O  
ANISOU 1266  O   HOH A 234     4737   7202   4529   3108    844   2439       O  
HETATM 1267  O   HOH A 235      15.925  -1.244  17.812  1.00 32.05           O  
ANISOU 1267  O   HOH A 235     4768   3937   3472   2096   -747   -599       O  
HETATM 1268  O   HOH A 236       7.165  -3.072  30.410  1.00 30.09           O  
ANISOU 1268  O   HOH A 236     5886   2395   3152   -159    675     91       O  
HETATM 1269  O   HOH A 237      -4.304  12.446  13.343  1.00 56.28           O  
ANISOU 1269  O   HOH A 237     2969  11674   6740    450  -2270    567       O  
HETATM 1270  O   HOH A 238      -0.021   4.953  18.129  1.00 36.40           O  
ANISOU 1270  O   HOH A 238     3264   4896   5668  -1252  -1360   2636       O  
HETATM 1271  O   HOH A 239      15.935  -3.402  15.842  1.00 44.56           O  
ANISOU 1271  O   HOH A 239     5513   3648   7767   -778    262    393       O  
HETATM 1272  O   HOH A 240      12.645  25.501   6.136  1.00 36.15           O  
ANISOU 1272  O   HOH A 240     6353   3586   3795   -296    400   1565       O  
HETATM 1273  O   HOH A 241       7.621   3.040  -0.868  1.00 31.01           O  
ANISOU 1273  O   HOH A 241     3910   4010   3861   1728   1192   1182       O  
HETATM 1274  O   HOH A 242       2.230   9.927  17.431  1.00 27.15           O  
ANISOU 1274  O   HOH A 242     3775   3728   2810    598     65    121       O  
HETATM 1275  O   HOH A 243      21.367   5.234  21.367  1.00 44.20           O  
ANISOU 1275  O   HOH A 243     7841   5006   3946   3024  -1005    235       O  
HETATM 1276  O   HOH A 244      20.118  10.127   2.179  1.00 36.18           O  
ANISOU 1276  O   HOH A 244     4424   4660   4664   1492    555    490       O  
HETATM 1277  O   HOH A 245      19.640  14.751  18.040  1.00 64.60           O  
ANISOU 1277  O   HOH A 245     3556   8775  12213    212   1819   1313       O  
HETATM 1278  O   HOH A 246      -8.775  11.498  17.991  1.00 79.90           O  
ANISOU 1278  O   HOH A 246     5814  10489  14054    289  -2567  -1536       O  
HETATM 1279  O   HOH A 247       2.711  -2.639  17.704  1.00 32.88           O  
ANISOU 1279  O   HOH A 247     4567   4787   3136   2369   -270    212       O  
HETATM 1280  O   HOH A 248       6.302  22.155  -1.177  1.00 73.61           O  
ANISOU 1280  O   HOH A 248    16031   6222   5715   -479   -590   1326       O  
HETATM 1281  O   HOH A 249      17.245   8.802  16.381  1.00 30.47           O  
ANISOU 1281  O   HOH A 249     4589   3358   3630    590   -319    436       O  
HETATM 1282  O   HOH A 250       5.002  17.005  29.807  1.00 37.54           O  
ANISOU 1282  O   HOH A 250     7550   4086   2626   -625    215   -165       O  
HETATM 1283  O   HOH A 251      -2.811  20.272   1.661  1.00 24.70           O  
ANISOU 1283  O   HOH A 251     2860   3127   3395  -1447   -359    272       O  
HETATM 1284  O   HOH A 252      -1.146  18.377   1.015  1.00 26.35           O  
ANISOU 1284  O   HOH A 252     3045   3119   3846    583   -619    -82       O  
HETATM 1285  O   HOH A 253       0.638   7.618  -1.808  1.00 33.47           O  
ANISOU 1285  O   HOH A 253     4695   4344   3677    257  -1707    669       O  
HETATM 1286  O   HOH A 254       5.860  29.945  10.323  1.00 32.52           O  
ANISOU 1286  O   HOH A 254     3148   3467   5738   -217    318    413       O  
HETATM 1287  O   HOH A 255      -3.690   0.608  16.739  1.00 22.83           O  
ANISOU 1287  O   HOH A 255     3214   2739   2721   -138    361     40       O  
HETATM 1288  O   HOH A 256      18.607  17.084   2.489  1.00 38.30           O  
ANISOU 1288  O   HOH A 256     4851   5853   3847   1546    787  -1594       O  
HETATM 1289  O   HOH A 257      15.047  10.345   0.679  1.00 39.06           O  
ANISOU 1289  O   HOH A 257     6570   3590   4680   1504   -973   -152       O  
HETATM 1290  O   HOH A 258       9.275   3.019  -2.963  1.00 38.50           O  
ANISOU 1290  O   HOH A 258     7283   3307   4039   1995    136    -90       O  
HETATM 1291  O   HOH A 259      10.300  -5.164   9.436  1.00 38.86           O  
ANISOU 1291  O   HOH A 259     8021   2966   3776     40   1279   -165       O  
HETATM 1292  O   HOH A 260       5.099  -1.728  25.455  1.00 32.38           O  
ANISOU 1292  O   HOH A 260     3578   4814   3908   1774    248   -464       O  
HETATM 1293  O   HOH A 261      -1.958   7.967  -0.358  1.00 74.47           O  
ANISOU 1293  O   HOH A 261    16725   5714   5856  -2121   1698   2236       O  
HETATM 1294  O   HOH A 262      10.811  22.114  26.500  1.00121.38           O  
ANISOU 1294  O   HOH A 262    33126   6421   6572   3830  -3305  -4837       O  
HETATM 1295  O   HOH A 263       0.695   8.933  29.598  1.00 97.83           O  
ANISOU 1295  O   HOH A 263    18179   7726  11263  -1801   4417   -743       O  
HETATM 1296  O   HOH A 264      -9.397   3.985  20.554  1.00 23.85           O  
ANISOU 1296  O   HOH A 264     3569   2148   3345    516    776    430       O  
HETATM 1297  O   HOH A 265      12.781  10.270  31.413  1.00 67.67           O  
ANISOU 1297  O   HOH A 265     9169   9196   7343   1117    703   -867       O  
HETATM 1298  O   HOH A 266      11.713   6.309  -3.426  1.00 53.52           O  
ANISOU 1298  O   HOH A 266     9414   6899   4020  -3125  -1081    611       O  
HETATM 1299  O   HOH A 267       5.363   7.957  33.986  1.00 68.35           O  
ANISOU 1299  O   HOH A 267     8014  10405   7551  -6666   2788  -6055       O  
HETATM 1300  O   HOH A 268       1.951   3.744  19.548  1.00 36.37           O  
ANISOU 1300  O   HOH A 268     4037   4908   4874    671   -203   1298       O  
HETATM 1301  O   HOH A 269      -1.385  14.164  21.818  1.00 42.09           O  
ANISOU 1301  O   HOH A 269     5110   5745   5135   -796   -649  -1497       O  
HETATM 1302  O   HOH A 270      18.428  11.310  21.718  1.00 38.85           O  
ANISOU 1302  O   HOH A 270     4288   4272   6200    224  -2144  -1155       O  
HETATM 1303  O   HOH A 271      21.314  18.049   4.459  1.00 65.05           O  
ANISOU 1303  O   HOH A 271     5517   2285  16913  -1134   7667   1480       O  
HETATM 1304  O   HOH A 272       6.076  -2.389  22.817  1.00 39.30           O  
ANISOU 1304  O   HOH A 272     5990   4577   4364    520  -1141   -786       O  
HETATM 1305  O   HOH A 273      10.941   3.686  16.695  1.00 33.23           O  
ANISOU 1305  O   HOH A 273     5099   3710   3813    493   -554    224       O  
HETATM 1306  O   HOH A 274       7.948  30.665   8.504  1.00 50.10           O  
ANISOU 1306  O   HOH A 274     5017   3309  10709  -1473  -1161    477       O  
HETATM 1307  O   HOH A 275      -1.347   0.014  10.403  1.00 39.91           O  
ANISOU 1307  O   HOH A 275     6508   5434   3219   1638   -377    151       O  
HETATM 1308  O   HOH A 276       5.057  30.397   6.753  1.00 36.93           O  
ANISOU 1308  O   HOH A 276     4666   5322   4043    450    542    924       O  
HETATM 1309  O   HOH A 277       3.541  29.845   8.632  1.00 31.23           O  
ANISOU 1309  O   HOH A 277     4203   3075   4585   -409  -1380    493       O  
HETATM 1310  O   HOH A 278      16.824  -0.543  28.750  1.00 33.94           O  
ANISOU 1310  O   HOH A 278     3959   5329   3604   2056    -82   -374       O  
MASTER      341    0    0    3   10    0    0    6 1220    1    0   11          
END                                                                             



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