CNRS Nantes University UFIP UFIP
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***  Test 1  ***

elNémo ID: 22012513052293604

Job options:

ID        	=	 22012513052293604
JOBID     	=	 Test 1
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 Test 1

HEADER    LIPID BINDING PROTEIN                   11-OCT-10   3P6F              
TITLE     HUMAN ADIPOCYTE LIPID-BINDING PROTEIN FABP4 IN COMPLEX WITH (S)-3-    
TITLE    2 PHENYL BUTYRIC ACID                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FATTY ACID-BINDING PROTEIN, ADIPOCYTE;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ADIPOCYTE LIPID-BINDING PROTEIN, ALBP, ADIPOCYTE-TYPE FATTY 
COMPND   5 ACID-BINDING PROTEIN, A-FABP, AFABP, FATTY ACID-BINDING PROTEIN 4;   
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: FABP4;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    LIPOCALIN, BETA BARREL, FATTY ACID BINDING PROTEIN, LIPID BINDING     
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.GONZALEZ,E.POZHARSKI                                              
REVDAT   3   25-FEB-15 3P6F    1       JRNL                                     
REVDAT   2   11-FEB-15 3P6F    1       JRNL                                     
REVDAT   1   13-APR-11 3P6F    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.    1.20 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) : 1.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 40515                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.157                           
REMARK   3   R VALUE            (WORKING SET) : 0.155                           
REMARK   3   FREE R VALUE                     : 0.190                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2079                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.23                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2749                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.64                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1330                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 126                          
REMARK   3   BIN FREE R VALUE                    : 0.1660                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1063                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 202                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.06000                                             
REMARK   3    B22 (A**2) : -0.11000                                             
REMARK   3    B33 (A**2) : 1.16000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.026         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.227         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1211 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):   828 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1641 ; 1.995 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2019 ; 0.945 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   164 ; 6.006 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    48 ;35.646 ;25.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   230 ;14.780 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;16.615 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   186 ; 0.121 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1378 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   236 ; 0.003 ; 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):   752 ; 2.051 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   317 ; 0.617 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1227 ; 3.221 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   459 ; 4.416 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   408 ; 6.221 ; 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):  2039 ; 1.632 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL                                        
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   4                                                                      
REMARK   4 3P6F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-OCT-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062014.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52856                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.090                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.09                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.13                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
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       16.18200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.47200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.69450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.47200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.18200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.69450            
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 470     ARG A  -3    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A  98    CG   OD1  OD2                                       
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   274              1.93            
REMARK 500   O    HOH A   281     O    HOH A   299              2.16            
REMARK 500   O    HOH A   143     O    HOH A   272              2.16            
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   OD1  ASN A    15     O    HOH A   271     3645     1.57            
REMARK 500   O    HOH A   268     O    HOH A   317     3655     1.72            
REMARK 500   O    HOH A   272     O    HOH A   317     1455     1.93            
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    MET A   0   CA  -  CB  -  CG  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    MET A   0   CG  -  SD  -  CE  ANGL. DEV. = -13.8 DEGREES          
REMARK 500    ARG A 108   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 110     -133.53     54.84                                   
REMARK 500    LYS A 120       73.28     26.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 236        DISTANCE =  5.32 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FBZ A 133                 
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: 3P6G   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P6H   RELATED DB: PDB                                   
DBREF  3P6F A    0   131  UNP    P15090   FABP4_HUMAN      1    132             
SEQADV 3P6F GLN A   -7  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6F GLN A   -6  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6F MET A   -5  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6F GLY A   -4  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6F ARG A   -3  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6F GLY A   -2  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6F SER A   -1  UNP  P15090              EXPRESSION TAG                 
SEQRES   1 A  139  GLN GLN MET GLY ARG GLY SER MET CYS ASP ALA PHE VAL          
SEQRES   2 A  139  GLY THR TRP LYS LEU VAL SER SER GLU ASN PHE ASP ASP          
SEQRES   3 A  139  TYR MET LYS GLU VAL GLY VAL GLY PHE ALA THR ARG LYS          
SEQRES   4 A  139  VAL ALA GLY MET ALA LYS PRO ASN MET ILE ILE SER VAL          
SEQRES   5 A  139  ASN GLY ASP VAL ILE THR ILE LYS SER GLU SER THR PHE          
SEQRES   6 A  139  LYS ASN THR GLU ILE SER PHE ILE LEU GLY GLN GLU PHE          
SEQRES   7 A  139  ASP GLU VAL THR ALA ASP ASP ARG LYS VAL LYS SER THR          
SEQRES   8 A  139  ILE THR LEU ASP GLY GLY VAL LEU VAL HIS VAL GLN LYS          
SEQRES   9 A  139  TRP ASP GLY LYS SER THR THR ILE LYS ARG LYS ARG GLU          
SEQRES  10 A  139  ASP ASP LYS LEU VAL VAL GLU CYS VAL MET LYS GLY VAL          
SEQRES  11 A  139  THR SER THR ARG VAL TYR GLU ARG ALA                          
HET    FBZ  A 133      24                                                       
HETNAM     FBZ (3S)-3-PHENYLBUTANOIC ACID                                       
FORMUL   2  FBZ    C10 H12 O2                                                   
FORMUL   3  HOH   *202(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           
SITE     1 AC1  7 PHE A  16  TYR A  19  ASP A  76  ARG A 126                    
SITE     2 AC1  7 TYR A 128  HOH A 211  HOH A 334                               
CRYST1   32.364   53.389   74.944  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      0.030899  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018730  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013343        0.00000                         
ATOM      1  N   GLN A  -7      -2.458  31.207  -8.775  1.00 34.86           N  
ANISOU    1  N   GLN A  -7     4596   4663   3986     35   -134     70       N  
ATOM      2  CA  GLN A  -7      -1.581  30.103  -8.301  1.00 34.41           C  
ANISOU    2  CA  GLN A  -7     4476   4582   4016     62    -98    -17       C  
ATOM      3  C   GLN A  -7      -0.897  29.359  -9.449  1.00 33.42           C  
ANISOU    3  C   GLN A  -7     4373   4505   3819     69   -141     16       C  
ATOM      4  O   GLN A  -7      -1.409  29.282 -10.572  1.00 33.23           O  
ANISOU    4  O   GLN A  -7     4511   4540   3575     10   -153   -185       O  
ATOM      5  CB  GLN A  -7      -2.372  29.125  -7.423  1.00 35.18           C  
ANISOU    5  CB  GLN A  -7     4532   4683   4150     64   -160     39       C  
ATOM      6  N   GLN A  -6       0.289  28.837  -9.167  1.00 32.02           N  
ANISOU    6  N   GLN A  -6     4235   4297   3635     42   -101     64       N  
ATOM      7  CA  GLN A  -6       0.988  27.974 -10.107  1.00 30.87           C  
ANISOU    7  CA  GLN A  -6     4041   4015   3673     44    -73    188       C  
ATOM      8  C   GLN A  -6       1.258  26.661  -9.429  1.00 29.25           C  
ANISOU    8  C   GLN A  -6     3867   3795   3449     -8    -51    200       C  
ATOM      9  O   GLN A  -6       1.243  26.569  -8.188  1.00 30.14           O  
ANISOU    9  O   GLN A  -6     4050   3962   3438    -75   -136    264       O  
ATOM     10  CB  GLN A  -6       2.300  28.609 -10.544  1.00 31.62           C  
ANISOU   10  CB  GLN A  -6     4142   4083   3787      1    -41    240       C  
ATOM     11  N  AMET A  -5       1.521  25.652 -10.258  0.50 29.39           N  
ANISOU   11  N  AMET A  -5     3812   3731   3624    -48    -68    185       N  
ATOM     12  N  BMET A  -5       1.480  25.616 -10.208  0.50 27.69           N  
ANISOU   12  N  BMET A  -5     3650   3550   3321    -55    -76    187       N  
ATOM     13  CA AMET A  -5       1.998  24.350  -9.820  0.50 29.07           C  
ANISOU   13  CA AMET A  -5     3743   3671   3628    -29    -44    166       C  
ATOM     14  CA BMET A  -5       1.843  24.354  -9.603  0.50 25.97           C  
ANISOU   14  CA BMET A  -5     3480   3341   3044    -16    -46    102       C  
ATOM     15  C  AMET A  -5       3.404  24.508  -9.281  0.50 28.18           C  
ANISOU   15  C  AMET A  -5     3651   3517   3538     19    -21    148       C  
ATOM     16  C  BMET A  -5       3.331  24.351  -9.304  0.50 26.54           C  
ANISOU   16  C  BMET A  -5     3505   3341   3238     19     -6    126       C  
ATOM     17  O  AMET A  -5       4.293  25.003  -9.987  0.50 28.12           O  
ANISOU   17  O  AMET A  -5     3579   3518   3585     -6    -71    230       O  
ATOM     18  O  BMET A  -5       4.181  24.528 -10.194  0.50 26.41           O  
ANISOU   18  O  BMET A  -5     3544   3399   3090     34    -22    161       O  
ATOM     19  CB AMET A  -5       2.002  23.361 -11.000  0.50 30.03           C  
ANISOU   19  CB AMET A  -5     3875   3796   3739     -8    -13    171       C  
ATOM     20  CB BMET A  -5       1.458  23.150 -10.458  0.50 25.25           C  
ANISOU   20  CB BMET A  -5     3409   3290   2896    -22    -49    141       C  
ATOM     21  CG AMET A  -5       3.060  23.636 -12.081  0.50 32.55           C  
ANISOU   21  CG AMET A  -5     4247   4228   3890   -129     69    216       C  
ATOM     22  CG BMET A  -5       1.709  21.838  -9.704  0.50 20.36           C  
ANISOU   22  CG BMET A  -5     3267   3066   1401      0     66    -85       C  
ATOM     23  SD AMET A  -5       4.543  22.591 -12.034  0.50 37.07           S  
ANISOU   23  SD AMET A  -5     4720   4956   4407    -62    130    302       S  
ATOM     24  SD BMET A  -5       1.226  20.407 -10.633  0.50 20.94           S  
ANISOU   24  SD BMET A  -5     3504   2617   1833   -207    -87    -69       S  
ATOM     25  CE AMET A  -5       5.152  22.758 -13.712  0.50 36.12           C  
ANISOU   25  CE AMET A  -5     4330   5029   4362   -325     18    522       C  
ATOM     26  CE BMET A  -5      -0.502  20.695 -10.676  0.50 17.10           C  
ANISOU   26  CE BMET A  -5     3418   2787    290    -61    312    123       C  
ATOM     27  N   GLY A  -4       3.611  24.108  -8.034  1.00 26.95           N  
ANISOU   27  N   GLY A  -4     3535   3339   3362     50    -50     30       N  
ATOM     28  CA  GLY A  -4       4.924  24.175  -7.458  1.00 26.82           C  
ANISOU   28  CA  GLY A  -4     3472   3282   3434    121     13     52       C  
ATOM     29  C   GLY A  -4       5.721  22.963  -7.855  1.00 26.32           C  
ANISOU   29  C   GLY A  -4     3475   3170   3355    112    -32     75       C  
ATOM     30  O   GLY A  -4       5.201  21.963  -8.368  1.00 27.76           O  
ANISOU   30  O   GLY A  -4     3601   3337   3608    131    -60   -197       O  
ATOM     31  N   ARG A  -3       6.999  23.063  -7.567  1.00 26.18           N  
ANISOU   31  N   ARG A  -3     3429   3134   3383    148     10    179       N  
ATOM     32  CA  ARG A  -3       7.938  22.007  -7.783  1.00 25.02           C  
ANISOU   32  CA  ARG A  -3     3405   3007   3094    209     15    469       C  
ATOM     33  C   ARG A  -3       7.890  20.989  -6.641  1.00 23.63           C  
ANISOU   33  C   ARG A  -3     3333   2935   2710    159     34    534       C  
ATOM     34  O   ARG A  -3       7.306  21.238  -5.569  1.00 26.11           O  
ANISOU   34  O   ARG A  -3     3624   3168   3126    258     84    428       O  
ATOM     35  CB  ARG A  -3       9.331  22.628  -7.819  1.00 27.20           C  
ANISOU   35  CB  ARG A  -3     3513   3223   3596    142    102    451       C  
ATOM     36  N   GLY A  -2       8.524  19.849  -6.889  1.00 21.90           N  
ANISOU   36  N   GLY A  -2     3249   2733   2339     29     47    594       N  
ATOM     37  CA  GLY A  -2       8.680  18.822  -5.898  1.00 20.94           C  
ANISOU   37  CA  GLY A  -2     3130   2640   2184    -47   -114    600       C  
ATOM     38  C   GLY A  -2       9.841  19.129  -4.990  1.00 20.90           C  
ANISOU   38  C   GLY A  -2     3176   2513   2252   -122    -70    641       C  
ATOM     39  O   GLY A  -2      10.545  20.143  -5.094  1.00 22.91           O  
ANISOU   39  O   GLY A  -2     3555   2754   2395   -165   -275    694       O  
ATOM     40  N   SER A  -1      10.060  18.190  -4.095  1.00 20.63           N  
ANISOU   40  N   SER A  -1     3273   2621   1945   -186    -24    661       N  
ATOM     41  CA  SER A  -1      11.216  18.299  -3.212  1.00 20.73           C  
ANISOU   41  CA  SER A  -1     3364   2574   1936   -170     39    585       C  
ATOM     42  C   SER A  -1      11.674  16.918  -2.786  1.00 21.14           C  
ANISOU   42  C   SER A  -1     3346   2608   2075   -207     70    616       C  
ATOM     43  O   SER A  -1      11.014  15.926  -2.957  1.00 21.58           O  
ANISOU   43  O   SER A  -1     3518   2580   2098   -453    171   1085       O  
ATOM     44  CB  SER A  -1      10.899  19.145  -1.980  1.00 21.82           C  
ANISOU   44  CB  SER A  -1     3690   2602   1997      0     19    544       C  
ATOM     45  OG  SER A  -1      10.334  18.364  -0.986  1.00 28.88           O  
ANISOU   45  OG  SER A  -1     4276   3670   3027   -255    576    413       O  
ATOM     46  N   MET A   0      12.886  16.870  -2.300  1.00 21.27           N  
ANISOU   46  N   MET A   0     3417   2750   1912   -115    -31    513       N  
ATOM     47  CA  MET A   0      13.447  15.629  -1.799  1.00 21.06           C  
ANISOU   47  CA  MET A   0     3407   2739   1853    -88     34    449       C  
ATOM     48  C   MET A   0      12.451  14.977  -0.780  1.00 20.05           C  
ANISOU   48  C   MET A   0     3259   2514   1845   -119    -53    537       C  
ATOM     49  O   MET A   0      12.319  13.754  -0.812  1.00 20.49           O  
ANISOU   49  O   MET A   0     3460   2491   1832   -109    -38    413       O  
ATOM     50  CB  MET A   0      14.829  16.010  -1.200  1.00 21.95           C  
ANISOU   50  CB  MET A   0     3495   2950   1895     -6    -54    339       C  
ATOM     51  CG  MET A   0      16.072  15.076  -1.208  1.00 24.42           C  
ANISOU   51  CG  MET A   0     3837   3432   2010    297    -58     33       C  
ATOM     52  SD  MET A   0      16.740  14.524   0.330  1.00 32.43           S  
ANISOU   52  SD  MET A   0     4754   4704   2864    275   -219     93       S  
ATOM     53  CE  MET A   0      15.079  14.299   0.845  1.00 19.81           C  
ANISOU   53  CE  MET A   0     3858   3065    603    349    117    834       C  
ATOM     54  N  ACYS A   1      11.779  15.793   0.053  0.50 20.48           N  
ANISOU   54  N  ACYS A   1     3180   2574   2026   -173    -11    517       N  
ATOM     55  N  BCYS A   1      11.756  15.735   0.087  0.50 19.68           N  
ANISOU   55  N  BCYS A   1     3160   2439   1878   -206    -13    544       N  
ATOM     56  CA ACYS A   1      10.809  15.332   1.089  0.50 20.58           C  
ANISOU   56  CA ACYS A   1     3141   2610   2069   -103     18    483       C  
ATOM     57  CA BCYS A   1      10.835  15.087   1.084  0.50 18.98           C  
ANISOU   57  CA BCYS A   1     3141   2290   1778   -185    -35    491       C  
ATOM     58  C  ACYS A   1       9.616  14.557   0.470  0.50 18.36           C  
ANISOU   58  C  ACYS A   1     2930   2296   1750   -122    -28    697       C  
ATOM     59  C  BCYS A   1       9.607  14.451   0.450  0.50 17.13           C  
ANISOU   59  C  BCYS A   1     2901   2072   1533   -171     -3    788       C  
ATOM     60  O  ACYS A   1       8.889  13.873   1.201  0.50 19.39           O  
ANISOU   60  O  ACYS A   1     3009   2378   1979   -122     40    611       O  
ATOM     61  O  BCYS A   1       8.849  13.725   1.133  0.50 17.03           O  
ANISOU   61  O  BCYS A   1     3105   1839   1524   -133    169   1085       O  
ATOM     62  CB ACYS A   1      10.327  16.539   1.937  0.50 21.46           C  
ANISOU   62  CB ACYS A   1     3132   2734   2285   -107     68    392       C  
ATOM     63  CB BCYS A   1      10.384  16.019   2.194  0.50 18.90           C  
ANISOU   63  CB BCYS A   1     3134   2359   1687    -38     53    522       C  
ATOM     64  SG ACYS A   1      10.477  16.496   3.830  0.50 26.49           S  
ANISOU   64  SG ACYS A   1     3936   3564   2564    102    667    534       S  
ATOM     65  SG BCYS A   1      11.719  16.784   3.088  0.50 24.58           S  
ANISOU   65  SG BCYS A   1     3916   3366   2056   -263     19   -523       S  
ATOM     66  N   ASP A   2       9.467  14.575  -0.860  1.00 18.05           N  
ANISOU   66  N   ASP A   2     2859   2441   1555   -266   -131    820       N  
ATOM     67  CA  ASP A   2       8.416  13.853  -1.473  1.00 18.44           C  
ANISOU   67  CA  ASP A   2     3028   2499   1477   -351   -122    915       C  
ATOM     68  C   ASP A   2       8.594  12.336  -1.275  1.00 17.83           C  
ANISOU   68  C   ASP A   2     3102   2533   1140   -304    -27    830       C  
ATOM     69  O   ASP A   2       7.587  11.660  -1.364  1.00 19.15           O  
ANISOU   69  O   ASP A   2     3004   2855   1416   -441     31    662       O  
ATOM     70  CB  ASP A   2       8.220  14.232  -2.900  1.00 19.63           C  
ANISOU   70  CB  ASP A   2     3211   2608   1639   -445   -124    823       C  
ATOM     71  CG  ASP A   2       7.662  15.655  -3.078  1.00 21.34           C  
ANISOU   71  CG  ASP A   2     3322   2859   1926    -68   -516   1160       C  
ATOM     72  OD1 ASP A   2       6.970  16.176  -2.168  1.00 27.85           O  
ANISOU   72  OD1 ASP A   2     4028   3860   2692    381   -249   1139       O  
ATOM     73  OD2 ASP A   2       7.923  16.278  -4.088  1.00 25.97           O  
ANISOU   73  OD2 ASP A   2     3676   3570   2621   -429   -603   1071       O  
ATOM     74  N   ALA A   3       9.822  11.816  -1.047  1.00 16.97           N  
ANISOU   74  N   ALA A   3     3010   2458    980   -430    331    706       N  
ATOM     75  CA  ALA A   3      10.015  10.383  -0.794  1.00 17.47           C  
ANISOU   75  CA  ALA A   3     3122   2407   1109   -153    241    622       C  
ATOM     76  C   ALA A   3       9.287   9.911   0.449  1.00 13.97           C  
ANISOU   76  C   ALA A   3     3017   1785    503   -130    285    326       C  
ATOM     77  O   ALA A   3       9.019   8.724   0.591  1.00 15.18           O  
ANISOU   77  O   ALA A   3     3283   1748    736      6    510     31       O  
ATOM     78  CB  ALA A   3      11.465  10.076  -0.649  1.00 19.89           C  
ANISOU   78  CB  ALA A   3     3172   2583   1802   -203    246    819       C  
ATOM     79  N   PHE A   4       8.996  10.840   1.361  1.00 12.69           N  
ANISOU   79  N   PHE A   4     2769   1545    506   -161    133    318       N  
ATOM     80  CA  PHE A   4       8.264  10.487   2.581  1.00 11.93           C  
ANISOU   80  CA  PHE A   4     2680   1331    521    -16    138    162       C  
ATOM     81  C   PHE A   4       6.758  10.530   2.431  1.00 10.76           C  
ANISOU   81  C   PHE A   4     2567   1133    386    -49     91     42       C  
ATOM     82  O   PHE A   4       6.040   9.971   3.248  1.00 12.08           O  
ANISOU   82  O   PHE A   4     2748   1373    468   -214    135    247       O  
ATOM     83  CB  PHE A   4       8.645  11.433   3.727  1.00 12.73           C  
ANISOU   83  CB  PHE A   4     2603   1427    807    -52     27    -11       C  
ATOM     84  CG  PHE A   4      10.069  11.305   4.160  1.00 12.26           C  
ANISOU   84  CG  PHE A   4     2570   1396    691     11    -32    -65       C  
ATOM     85  CD1 PHE A   4      10.447  10.284   5.009  1.00 13.61           C  
ANISOU   85  CD1 PHE A   4     2782   1800    588    -93    -47    181       C  
ATOM     86  CD2 PHE A   4      11.022  12.214   3.759  1.00 15.76           C  
ANISOU   86  CD2 PHE A   4     2885   2139    963   -111   -328    402       C  
ATOM     87  CE1 PHE A   4      11.738  10.164   5.416  1.00 15.22           C  
ANISOU   87  CE1 PHE A   4     2826   2221    734    126   -112    108       C  
ATOM     88  CE2 PHE A   4      12.335  12.061   4.125  1.00 16.62           C  
ANISOU   88  CE2 PHE A   4     2725   2638    951   -366    139    249       C  
ATOM     89  CZ  PHE A   4      12.690  11.033   4.990  1.00 14.48           C  
ANISOU   89  CZ  PHE A   4     2489   2221    792    101   -116   -197       C  
ATOM     90  N   VAL A   5       6.278  11.249   1.424  1.00 11.20           N  
ANISOU   90  N   VAL A   5     2698   1250    306    -29     76    224       N  
ATOM     91  CA  VAL A   5       4.862  11.496   1.328  1.00 11.54           C  
ANISOU   91  CA  VAL A   5     2629   1227    528   -128    173    -31       C  
ATOM     92  C   VAL A   5       4.135  10.193   1.034  1.00 11.80           C  
ANISOU   92  C   VAL A   5     2735   1289    456   -257    110   -225       C  
ATOM     93  O   VAL A   5       4.523   9.396   0.166  1.00 15.61           O  
ANISOU   93  O   VAL A   5     3312   1658    961   -499    528   -510       O  
ATOM     94  CB  VAL A   5       4.607  12.579   0.295  1.00 12.55           C  
ANISOU   94  CB  VAL A   5     2774   1210    782     12     76    198       C  
ATOM     95  CG1 VAL A   5       3.152  12.606  -0.252  1.00 16.21           C  
ANISOU   95  CG1 VAL A   5     3416   1783    958   -100   -371    141       C  
ATOM     96  CG2 VAL A   5       5.141  13.916   0.796  1.00 14.35           C  
ANISOU   96  CG2 VAL A   5     3054   1278   1118   -221   -173    269       C  
ATOM     97  N   GLY A   6       2.988  10.031   1.653  1.00 11.59           N  
ANISOU   97  N   GLY A   6     2673   1303    427   -278     80   -133       N  
ATOM     98  CA  GLY A   6       2.165   8.885   1.426  1.00 12.62           C  
ANISOU   98  CA  GLY A   6     2700   1572    522   -234     77   -130       C  
ATOM     99  C   GLY A   6       1.499   8.402   2.667  1.00 10.77           C  
ANISOU   99  C   GLY A   6     2341   1318    434   -214   -132    -89       C  
ATOM    100  O   GLY A   6       1.442   9.081   3.668  1.00 12.82           O  
ANISOU  100  O   GLY A   6     2926   1391    551   -342    147   -194       O  
ATOM    101  N   THR A   7       0.980   7.201   2.550  1.00 11.21           N  
ANISOU  101  N   THR A   7     2530   1333    394   -174   -215    -58       N  
ATOM    102  CA  THR A   7       0.238   6.535   3.616  1.00 11.96           C  
ANISOU  102  CA  THR A   7     2563   1212    767    -39   -128    -78       C  
ATOM    103  C   THR A   7       1.011   5.279   3.974  1.00 11.23           C  
ANISOU  103  C   THR A   7     2419   1259    588    -98   -186     -1       C  
ATOM    104  O   THR A   7       1.261   4.449   3.110  1.00 13.32           O  
ANISOU  104  O   THR A   7     3028   1392    639     82   -363    -90       O  
ATOM    105  CB  THR A   7      -1.162   6.185   3.147  1.00 13.79           C  
ANISOU  105  CB  THR A   7     2542   1288   1407    -42    -93    150       C  
ATOM    106  OG1 THR A   7      -1.729   7.307   2.452  1.00 18.84           O  
ANISOU  106  OG1 THR A   7     2954   1840   2364    -90   -489    130       O  
ATOM    107  CG2 THR A   7      -2.042   5.761   4.247  1.00 17.93           C  
ANISOU  107  CG2 THR A   7     2876   2123   1814   -172     -5    -40       C  
ATOM    108  N   TRP A   8       1.350   5.157   5.249  1.00 10.74           N  
ANISOU  108  N   TRP A   8     2446   1295    336     42     21     82       N  
ATOM    109  CA  TRP A   8       2.259   4.155   5.759  1.00 10.97           C  
ANISOU  109  CA  TRP A   8     2552   1224    390    -71     76     96       C  
ATOM    110  C   TRP A   8       1.597   3.390   6.876  1.00 10.82           C  
ANISOU  110  C   TRP A   8     2622   1135    353   -133    176     -5       C  
ATOM    111  O   TRP A   8       0.761   3.944   7.601  1.00 14.92           O  
ANISOU  111  O   TRP A   8     3378   1369    922    -12    704    172       O  
ATOM    112  CB  TRP A   8       3.510   4.836   6.296  1.00 10.42           C  
ANISOU  112  CB  TRP A   8     2473   1177    309     38     97    220       C  
ATOM    113  CG  TRP A   8       4.243   5.666   5.273  1.00 10.22           C  
ANISOU  113  CG  TRP A   8     2453   1170    260     -7   -127     -1       C  
ATOM    114  CD1 TRP A   8       4.142   7.004   5.047  1.00 10.43           C  
ANISOU  114  CD1 TRP A   8     2412   1245    305    -77     24     62       C  
ATOM    115  CD2 TRP A   8       5.236   5.176   4.372  1.00 10.16           C  
ANISOU  115  CD2 TRP A   8     2380   1057    422    -30    -63    137       C  
ATOM    116  NE1 TRP A   8       5.005   7.378   4.030  1.00 11.16           N  
ANISOU  116  NE1 TRP A   8     2604   1226    408   -198    137     53       N  
ATOM    117  CE2 TRP A   8       5.682   6.267   3.609  1.00 10.34           C  
ANISOU  117  CE2 TRP A   8     2339   1321    267   -163     90   -113       C  
ATOM    118  CE3 TRP A   8       5.778   3.912   4.120  1.00 10.69           C  
ANISOU  118  CE3 TRP A   8     2470   1184    404   -192    -82    -38       C  
ATOM    119  CZ2 TRP A   8       6.660   6.125   2.627  1.00 11.66           C  
ANISOU  119  CZ2 TRP A   8     2558   1500    371   -296     22    -41       C  
ATOM    120  CZ3 TRP A   8       6.763   3.778   3.173  1.00 11.56           C  
ANISOU  120  CZ3 TRP A   8     2332   1273    786    -31    -69   -172       C  
ATOM    121  CH2 TRP A   8       7.163   4.866   2.406  1.00 12.21           C  
ANISOU  121  CH2 TRP A   8     2385   1588    666   -152    239   -385       C  
ATOM    122  N   LYS A   9       1.920   2.130   7.023  1.00 10.50           N  
ANISOU  122  N   LYS A   9     2493   1123    371   -150    -56    164       N  
ATOM    123  CA  LYS A   9       1.380   1.290   8.104  1.00 11.25           C  
ANISOU  123  CA  LYS A   9     2458   1381    433   -156    -51    195       C  
ATOM    124  C   LYS A   9       2.505   0.612   8.842  1.00 10.45           C  
ANISOU  124  C   LYS A   9     2299   1179    491   -179     29    194       C  
ATOM    125  O   LYS A   9       3.447   0.130   8.245  1.00 11.06           O  
ANISOU  125  O   LYS A   9     2425   1362    413    -97    -24     70       O  
ATOM    126  CB  LYS A   9       0.463   0.256   7.499  1.00 13.67           C  
ANISOU  126  CB  LYS A   9     2544   1663    988   -285    -51    565       C  
ATOM    127  CG  LYS A   9       1.056  -0.687   6.523  1.00 20.11           C  
ANISOU  127  CG  LYS A   9     3382   2446   1813   -317   -239    208       C  
ATOM    128  CD  LYS A   9       0.019  -1.643   5.988  1.00 25.34           C  
ANISOU  128  CD  LYS A   9     3891   3111   2623   -606   -309   -204       C  
ATOM    129  CE  LYS A   9       0.667  -2.635   5.032  1.00 27.06           C  
ANISOU  129  CE  LYS A   9     4027   3352   2901   -822   -280   -769       C  
ATOM    130  NZ  LYS A   9       0.484  -2.414   3.549  1.00 32.18           N  
ANISOU  130  NZ  LYS A   9     4567   4142   3516   -480   -449    -21       N  
ATOM    131  N   LEU A  10       2.422   0.612  10.175  1.00 11.73           N  
ANISOU  131  N   LEU A  10     2369   1560    527   -129    -42    266       N  
ATOM    132  CA  LEU A  10       3.468  -0.006  11.001  1.00 11.33           C  
ANISOU  132  CA  LEU A  10     2237   1530    536   -313    -90    192       C  
ATOM    133  C   LEU A  10       3.436  -1.501  10.785  1.00 12.05           C  
ANISOU  133  C   LEU A  10     2408   1571    599   -315   -127    317       C  
ATOM    134  O   LEU A  10       2.376  -2.096  10.992  1.00 14.46           O  
ANISOU  134  O   LEU A  10     2585   1794   1115   -471   -144    470       O  
ATOM    135  CB  LEU A  10       3.254   0.313  12.477  1.00 12.37           C  
ANISOU  135  CB  LEU A  10     2426   1850    421   -315     58    240       C  
ATOM    136  CG  LEU A  10       4.334  -0.246  13.396  1.00 12.95           C  
ANISOU  136  CG  LEU A  10     2568   1768    584   -306   -225    260       C  
ATOM    137  CD1 LEU A  10       5.653   0.444  13.213  1.00 13.42           C  
ANISOU  137  CD1 LEU A  10     2362   1950    787    -17    -20    137       C  
ATOM    138  CD2 LEU A  10       3.881  -0.178  14.887  1.00 15.73           C  
ANISOU  138  CD2 LEU A  10     2826   2632    517     11     33    283       C  
ATOM    139  N   VAL A  11       4.593  -2.078  10.473  1.00 11.83           N  
ANISOU  139  N   VAL A  11     2608   1172    716   -222   -365    132       N  
ATOM    140  CA  VAL A  11       4.713  -3.531  10.340  1.00 14.22           C  
ANISOU  140  CA  VAL A  11     3007   1390   1005   -106   -483    105       C  
ATOM    141  C   VAL A  11       5.633  -4.243  11.315  1.00 14.97           C  
ANISOU  141  C   VAL A  11     3076   1328   1284   -155   -586    459       C  
ATOM    142  O   VAL A  11       5.518  -5.445  11.488  1.00 19.17           O  
ANISOU  142  O   VAL A  11     3797   1425   2059   -291  -1008    609       O  
ATOM    143  CB  VAL A  11       5.074  -3.935   8.931  1.00 15.39           C  
ANISOU  143  CB  VAL A  11     3209   1258   1379     57   -429   -102       C  
ATOM    144  CG1 VAL A  11       3.989  -3.467   7.993  1.00 17.72           C  
ANISOU  144  CG1 VAL A  11     3577   1809   1345    164   -592    -69       C  
ATOM    145  CG2 VAL A  11       6.488  -3.468   8.493  1.00 16.81           C  
ANISOU  145  CG2 VAL A  11     3363   1906   1118    173    -55   -232       C  
ATOM    146  N   SER A  12       6.565  -3.539  11.949  1.00 13.74           N  
ANISOU  146  N   SER A  12     2994   1348    876   -176   -459    187       N  
ATOM    147  CA  SER A  12       7.390  -4.157  12.974  1.00 14.10           C  
ANISOU  147  CA  SER A  12     3045   1320    992    -11   -462    228       C  
ATOM    148  C   SER A  12       7.890  -3.096  13.912  1.00 12.27           C  
ANISOU  148  C   SER A  12     2601   1289    772    -41   -302    276       C  
ATOM    149  O   SER A  12       8.071  -1.931  13.540  1.00 12.69           O  
ANISOU  149  O   SER A  12     2812   1368    640   -183   -210    445       O  
ATOM    150  CB  SER A  12       8.522  -4.928  12.349  1.00 17.16           C  
ANISOU  150  CB  SER A  12     3292   2042   1183    134   -438    189       C  
ATOM    151  OG  SER A  12       9.489  -4.078  11.805  1.00 17.97           O  
ANISOU  151  OG  SER A  12     3608   2082   1138    276   -278    188       O  
ATOM    152  N   SER A  13       8.180  -3.542  15.111  1.00 13.20           N  
ANISOU  152  N   SER A  13     2876   1263    873   -298   -436    512       N  
ATOM    153  CA  SER A  13       8.727  -2.701  16.134  1.00 13.68           C  
ANISOU  153  CA  SER A  13     2825   1457    915   -297   -483    439       C  
ATOM    154  C   SER A  13       9.685  -3.511  16.994  1.00 13.84           C  
ANISOU  154  C   SER A  13     2779   1567    909   -306   -233    639       C  
ATOM    155  O   SER A  13       9.368  -4.656  17.344  1.00 16.68           O  
ANISOU  155  O   SER A  13     3267   1603   1466   -494   -634    764       O  
ATOM    156  CB  SER A  13       7.531  -2.169  16.971  1.00 15.44           C  
ANISOU  156  CB  SER A  13     3141   1774    951   -329   -495    270       C  
ATOM    157  OG  SER A  13       7.893  -1.283  17.992  1.00 17.10           O  
ANISOU  157  OG  SER A  13     3655   2023    818   -269   -688    244       O  
ATOM    158  N   GLU A  14      10.824  -2.927  17.320  1.00 11.91           N  
ANISOU  158  N   GLU A  14     2688   1230    606   -144   -290    275       N  
ATOM    159  CA AGLU A  14      11.878  -3.514  18.147  0.50 12.88           C  
ANISOU  159  CA AGLU A  14     2784   1127    983      9   -235    105       C  
ATOM    160  CA BGLU A  14      11.738  -3.542  18.228  0.50 11.40           C  
ANISOU  160  CA BGLU A  14     2626    959    745     23   -201    -15       C  
ATOM    161  C   GLU A  14      12.147  -2.556  19.305  1.00 10.73           C  
ANISOU  161  C   GLU A  14     2416   1075    584     61    -78     82       C  
ATOM    162  O   GLU A  14      12.417  -1.379  19.033  1.00 11.44           O  
ANISOU  162  O   GLU A  14     2780   1064    502    -78   -255     83       O  
ATOM    163  CB AGLU A  14      13.236  -3.628  17.367  0.50 14.59           C  
ANISOU  163  CB AGLU A  14     2901   1268   1375      6   -281     87       C  
ATOM    164  CB BGLU A  14      12.975  -4.025  17.450  0.50 11.91           C  
ANISOU  164  CB BGLU A  14     2540   1130    852     74   -214   -211       C  
ATOM    165  CG AGLU A  14      13.383  -4.318  16.010  0.50 18.96           C  
ANISOU  165  CG AGLU A  14     3393   1734   2076    125   -147    -99       C  
ATOM    166  CG BGLU A  14      12.805  -5.143  16.500  0.50 13.49           C  
ANISOU  166  CG BGLU A  14     2730   1255   1139     29     53   -491       C  
ATOM    167  CD AGLU A  14      14.705  -3.846  15.331  0.50 23.07           C  
ANISOU  167  CD AGLU A  14     3796   2400   2570    325    143     -1       C  
ATOM    168  CD BGLU A  14      12.765  -6.504  17.158  0.50 14.19           C  
ANISOU  168  CD BGLU A  14     2728   1584   1076    231     56   -490       C  
ATOM    169  OE1AGLU A  14      15.703  -3.486  16.048  0.50 21.79           O  
ANISOU  169  OE1AGLU A  14     3798   1602   2876    691    250   -137       O  
ATOM    170  OE1BGLU A  14      13.014  -6.578  18.372  0.50 16.35           O  
ANISOU  170  OE1BGLU A  14     3057   1532   1621    150   -736   -562       O  
ATOM    171  OE2AGLU A  14      14.734  -3.769  14.075  0.50 23.71           O  
ANISOU  171  OE2AGLU A  14     4386   1911   2712    337    498    -48       O  
ATOM    172  OE2BGLU A  14      12.455  -7.485  16.469  0.50 17.79           O  
ANISOU  172  OE2BGLU A  14     3266   1786   1707    254     95   -870       O  
ATOM    173  N   ASN A  15      12.167  -3.058  20.527  1.00 10.64           N  
ANISOU  173  N   ASN A  15     2361   1146    533    -57   -145    225       N  
ATOM    174  CA AASN A  15      12.670  -2.335  21.699  0.50  9.72           C  
ANISOU  174  CA AASN A  15     2309   1062    323     75   -176    160       C  
ATOM    175  CA BASN A  15      12.615  -2.319  21.708  0.50 11.06           C  
ANISOU  175  CA BASN A  15     2445   1237    518     68   -160    102       C  
ATOM    176  C   ASN A  15      11.825  -1.109  22.058  1.00 10.22           C  
ANISOU  176  C   ASN A  15     2327   1141    415     15    -41    116       C  
ATOM    177  O   ASN A  15      12.305  -0.240  22.784  1.00 11.03           O  
ANISOU  177  O   ASN A  15     2435   1219    536      5   -115     64       O  
ATOM    178  CB AASN A  15      14.172  -1.996  21.542  0.50 10.16           C  
ANISOU  178  CB AASN A  15     2362   1094    402     78   -203    202       C  
ATOM    179  CB BASN A  15      14.063  -1.929  21.588  0.50 12.10           C  
ANISOU  179  CB BASN A  15     2579   1391    627     54   -134     67       C  
ATOM    180  CG AASN A  15      14.948  -2.010  22.862  0.50  8.63           C  
ANISOU  180  CG AASN A  15     2119    807    354    204   -149    189       C  
ATOM    181  CG BASN A  15      14.901  -3.086  21.382  0.50 16.49           C  
ANISOU  181  CG BASN A  15     2796   2095   1372    188   -142    -11       C  
ATOM    182  OD1AASN A  15      14.809  -2.935  23.662  0.50 10.02           O  
ANISOU  182  OD1AASN A  15     2321    862    624     -5   -153    346       O  
ATOM    183  OD1BASN A  15      14.954  -3.934  22.243  0.50 18.79           O  
ANISOU  183  OD1BASN A  15     3839   1557   1740    432    120    -23       O  
ATOM    184  ND2AASN A  15      15.777  -0.996  23.073  0.50  9.36           N  
ANISOU  184  ND2AASN A  15     2162   1006    387    133     26    153       N  
ATOM    185  ND2BASN A  15      15.502  -3.202  20.230  0.50 22.26           N  
ANISOU  185  ND2BASN A  15     3501   2965   1991    671    316    214       N  
ATOM    186  N   PHE A  16      10.586  -1.038  21.600  1.00 11.10           N  
ANISOU  186  N   PHE A  16     2358   1190    669    -46     -4    -13       N  
ATOM    187  CA  PHE A  16       9.770   0.140  21.861  1.00 11.60           C  
ANISOU  187  CA  PHE A  16     2364   1546    496      0    -81     31       C  
ATOM    188  C   PHE A  16       9.404   0.277  23.320  1.00 11.48           C  
ANISOU  188  C   PHE A  16     2379   1360    621    -66   -120    117       C  
ATOM    189  O   PHE A  16       9.331   1.403  23.828  1.00 11.02           O  
ANISOU  189  O   PHE A  16     2445   1215    524   -181    -13     50       O  
ATOM    190  CB  PHE A  16       8.539   0.145  20.934  1.00 12.43           C  
ANISOU  190  CB  PHE A  16     2355   1689    675    120   -126     -6       C  
ATOM    191  CG  PHE A  16       7.790   1.457  20.912  1.00 13.17           C  
ANISOU  191  CG  PHE A  16     2549   2132    320    226    -37     -2       C  
ATOM    192  CD1 PHE A  16       8.434   2.638  20.570  1.00 13.46           C  
ANISOU  192  CD1 PHE A  16     2587   1789    736    384   -115   -106       C  
ATOM    193  CD2 PHE A  16       6.439   1.482  21.144  1.00 14.47           C  
ANISOU  193  CD2 PHE A  16     2739   2157    600    344    -27   -249       C  
ATOM    194  CE1 PHE A  16       7.721   3.845  20.477  1.00 14.75           C  
ANISOU  194  CE1 PHE A  16     2968   1805    830    253   -159      2       C  
ATOM    195  CE2 PHE A  16       5.724   2.660  21.038  1.00 15.15           C  
ANISOU  195  CE2 PHE A  16     2712   2396    648    473     44   -122       C  
ATOM    196  CZ  PHE A  16       6.374   3.813  20.730  1.00 14.50           C  
ANISOU  196  CZ  PHE A  16     2980   1997    529    595   -276   -115       C  
ATOM    197  N   ASP A  17       9.128  -0.812  24.023  1.00 11.92           N  
ANISOU  197  N   ASP A  17     2590   1164    772    -96    137     -7       N  
ATOM    198  CA  ASP A  17       8.817  -0.719  25.447  1.00 12.07           C  
ANISOU  198  CA  ASP A  17     2644   1314    625   -113    206    172       C  
ATOM    199  C   ASP A  17      10.004  -0.114  26.192  1.00 12.00           C  
ANISOU  199  C   ASP A  17     2535   1264    759    -83     30    449       C  
ATOM    200  O   ASP A  17       9.822   0.782  27.021  1.00 12.36           O  
ANISOU  200  O   ASP A  17     2867   1281    547    -86     77    123       O  
ATOM    201  CB  ASP A  17       8.424  -2.080  25.988  1.00 14.58           C  
ANISOU  201  CB  ASP A  17     2892   1550   1097   -119    229    249       C  
ATOM    202  CG  ASP A  17       7.882  -1.990  27.377  1.00 16.68           C  
ANISOU  202  CG  ASP A  17     3061   1929   1347   -352    279    632       C  
ATOM    203  OD1 ASP A  17       8.504  -2.522  28.287  1.00 22.59           O  
ANISOU  203  OD1 ASP A  17     3571   3517   1495   -145     62    704       O  
ATOM    204  OD2 ASP A  17       6.845  -1.378  27.579  1.00 18.00           O  
ANISOU  204  OD2 ASP A  17     3413   2346   1077    -59    447    434       O  
ATOM    205  N   ASP A  18      11.213  -0.572  25.910  1.00 11.99           N  
ANISOU  205  N   ASP A  18     2584   1233    739     25    128    304       N  
ATOM    206  CA AASP A  18      12.373  -0.051  26.577  0.50 13.22           C  
ANISOU  206  CA AASP A  18     2577   1563    881     12     27    438       C  
ATOM    207  CA BASP A  18      12.403  -0.043  26.577  0.50 13.30           C  
ANISOU  207  CA BASP A  18     2600   1582    869     47     -5    442       C  
ATOM    208  C   ASP A  18      12.607   1.430  26.252  1.00 11.80           C  
ANISOU  208  C   ASP A  18     2381   1396    703      7     44    239       C  
ATOM    209  O   ASP A  18      12.964   2.232  27.122  1.00 12.68           O  
ANISOU  209  O   ASP A  18     2644   1597    576     54   -121    148       O  
ATOM    210  CB AASP A  18      13.583  -0.905  26.251  0.50 14.84           C  
ANISOU  210  CB AASP A  18     2650   1793   1193     39    108    394       C  
ATOM    211  CB BASP A  18      13.686  -0.806  26.234  0.50 15.11           C  
ANISOU  211  CB BASP A  18     2706   1731   1303     80     45    415       C  
ATOM    212  CG AASP A  18      13.614  -2.193  27.041  0.50 19.56           C  
ANISOU  212  CG AASP A  18     2995   1999   2436    -24    322    473       C  
ATOM    213  CG BASP A  18      14.000  -1.942  27.214  0.50 19.86           C  
ANISOU  213  CG BASP A  18     3091   2338   2114    293     25    529       C  
ATOM    214  OD1AASP A  18      12.834  -2.312  27.995  0.50 21.04           O  
ANISOU  214  OD1AASP A  18     4086   2208   1698    327    366    809       O  
ATOM    215  OD1BASP A  18      14.921  -1.843  28.057  0.50 23.66           O  
ANISOU  215  OD1BASP A  18     4031   2551   2407    534   -413    783       O  
ATOM    216  OD2AASP A  18      14.456  -3.055  26.750  0.50 22.13           O  
ANISOU  216  OD2AASP A  18     3424   2308   2676    146    335    235       O  
ATOM    217  OD2BASP A  18      13.350  -2.988  27.090  0.50 19.88           O  
ANISOU  217  OD2BASP A  18     3619   1721   2212    325    819    955       O  
ATOM    218  N   TYR A  19      12.400   1.822  25.004  1.00 10.73           N  
ANISOU  218  N   TYR A  19     2432   1235    410    -27    -69    216       N  
ATOM    219  CA  TYR A  19      12.433   3.241  24.646  1.00 10.44           C  
ANISOU  219  CA  TYR A  19     2257   1343    363    -64     -2    183       C  
ATOM    220  C   TYR A  19      11.427   4.049  25.450  1.00 10.49           C  
ANISOU  220  C   TYR A  19     2418   1166    400    -45     13    221       C  
ATOM    221  O   TYR A  19      11.774   5.104  26.031  1.00 11.09           O  
ANISOU  221  O   TYR A  19     2590   1328    295   -242    -85     82       O  
ATOM    222  CB  TYR A  19      12.208   3.410  23.123  1.00 10.35           C  
ANISOU  222  CB  TYR A  19     2294   1301    337      1      7    -55       C  
ATOM    223  CG  TYR A  19      11.996   4.856  22.720  1.00 10.11           C  
ANISOU  223  CG  TYR A  19     2283   1289    270    -87     76    -49       C  
ATOM    224  CD1 TYR A  19      13.066   5.736  22.628  1.00 10.39           C  
ANISOU  224  CD1 TYR A  19     2357   1322    265    -99     53     28       C  
ATOM    225  CD2 TYR A  19      10.714   5.358  22.495  1.00 11.06           C  
ANISOU  225  CD2 TYR A  19     2466   1480    256    -49     26     57       C  
ATOM    226  CE1 TYR A  19      12.862   7.084  22.328  1.00 10.14           C  
ANISOU  226  CE1 TYR A  19     2348   1148    356   -238    105     73       C  
ATOM    227  CE2 TYR A  19      10.516   6.703  22.184  1.00 10.66           C  
ANISOU  227  CE2 TYR A  19     2284   1398    368     91    -84      1       C  
ATOM    228  CZ  TYR A  19      11.586   7.549  22.096  1.00 10.54           C  
ANISOU  228  CZ  TYR A  19     2497   1240    268   -167    -36   -118       C  
ATOM    229  OH  TYR A  19      11.375   8.872  21.791  1.00 11.49           O  
ANISOU  229  OH  TYR A  19     2620   1204    541     50    -83    130       O  
ATOM    230  N   MET A  20      10.191   3.591  25.496  1.00 10.25           N  
ANISOU  230  N   MET A  20     2388   1190    316    -81     79     63       N  
ATOM    231  CA  MET A  20       9.182   4.310  26.225  1.00 10.47           C  
ANISOU  231  CA  MET A  20     2349   1371    258    -32     16     71       C  
ATOM    232  C   MET A  20       9.529   4.402  27.725  1.00 11.27           C  
ANISOU  232  C   MET A  20     2460   1354    467   -152     57    135       C  
ATOM    233  O   MET A  20       9.298   5.426  28.365  1.00 11.68           O  
ANISOU  233  O   MET A  20     2718   1397    321   -227     -1    -16       O  
ATOM    234  CB  MET A  20       7.788   3.693  26.047  1.00 10.79           C  
ANISOU  234  CB  MET A  20     2347   1495    257    -49     65     51       C  
ATOM    235  CG  MET A  20       7.193   3.944  24.686  1.00 11.80           C  
ANISOU  235  CG  MET A  20     2596   1570    318     13     40    162       C  
ATOM    236  SD  MET A  20       5.446   3.473  24.599  1.00 13.76           S  
ANISOU  236  SD  MET A  20     2553   2243    431    -64     -5     -9       S  
ATOM    237  CE  MET A  20       5.619   1.696  24.635  1.00 14.37           C  
ANISOU  237  CE  MET A  20     2616   2101    740   -303    -63   -226       C  
ATOM    238  N   LYS A  21      10.090   3.329  28.295  1.00 11.50           N  
ANISOU  238  N   LYS A  21     2621   1494    253   -168     22     -8       N  
ATOM    239  CA  LYS A  21      10.530   3.385  29.700  1.00 13.03           C  
ANISOU  239  CA  LYS A  21     2759   1886    305   -234     28    193       C  
ATOM    240  C   LYS A  21      11.567   4.475  29.865  1.00 13.48           C  
ANISOU  240  C   LYS A  21     2800   2030    292   -273   -167    128       C  
ATOM    241  O   LYS A  21      11.504   5.224  30.850  1.00 15.65           O  
ANISOU  241  O   LYS A  21     3242   2359    342   -445   -109    -89       O  
ATOM    242  CB  LYS A  21      11.151   2.052  30.142  1.00 14.47           C  
ANISOU  242  CB  LYS A  21     2880   2303    312    -99     -7    347       C  
ATOM    243  CG  LYS A  21      10.187   0.935  30.378  1.00 16.40           C  
ANISOU  243  CG  LYS A  21     3117   2357    757     67    -40    463       C  
ATOM    244  CD  LYS A  21      10.865  -0.265  30.980  1.00 19.47           C  
ANISOU  244  CD  LYS A  21     3474   2248   1676     38    -11   1018       C  
ATOM    245  CE  LYS A  21       9.901  -1.301  31.234  1.00 23.54           C  
ANISOU  245  CE  LYS A  21     3887   2688   2366     12   -256    960       C  
ATOM    246  NZ  LYS A  21      10.600  -2.408  31.872  1.00 27.40           N  
ANISOU  246  NZ  LYS A  21     4672   2379   3359    163   -258   1317       N  
ATOM    247  N   GLU A  22      12.523   4.583  28.957  1.00 14.08           N  
ANISOU  247  N   GLU A  22     2851   2140    359   -358   -165     56       N  
ATOM    248  CA  GLU A  22      13.580   5.561  29.050  1.00 15.23           C  
ANISOU  248  CA  GLU A  22     2993   2419    373   -420   -194     30       C  
ATOM    249  C   GLU A  22      13.002   6.960  28.993  1.00 14.67           C  
ANISOU  249  C   GLU A  22     3138   2121    312   -495   -110   -151       C  
ATOM    250  O   GLU A  22      13.446   7.881  29.686  1.00 17.43           O  
ANISOU  250  O   GLU A  22     3636   2497    488   -729   -291   -208       O  
ATOM    251  CB  GLU A  22      14.670   5.292  28.000  1.00 16.01           C  
ANISOU  251  CB  GLU A  22     2978   2412    693   -451   -123     75       C  
ATOM    252  CG  GLU A  22      16.055   5.731  28.251  1.00 19.25           C  
ANISOU  252  CG  GLU A  22     3191   2911   1212   -213   -380    -64       C  
ATOM    253  CD  GLU A  22      16.786   4.901  29.346  1.00 22.45           C  
ANISOU  253  CD  GLU A  22     3538   3089   1903   -362   -553    265       C  
ATOM    254  OE1 GLU A  22      16.247   3.898  29.849  1.00 24.82           O  
ANISOU  254  OE1 GLU A  22     3749   3390   2289   -449   -728    421       O  
ATOM    255  OE2 GLU A  22      17.949   5.241  29.693  1.00 25.26           O  
ANISOU  255  OE2 GLU A  22     4225   3136   2235    -20  -1017    -97       O  
ATOM    256  N   VAL A  23      11.977   7.149  28.147  1.00 13.91           N  
ANISOU  256  N   VAL A  23     3042   1885    355   -396    -42    -69       N  
ATOM    257  CA  VAL A  23      11.311   8.426  28.005  1.00 13.94           C  
ANISOU  257  CA  VAL A  23     3149   1872    274   -457      9   -162       C  
ATOM    258  C   VAL A  23      10.568   8.785  29.304  1.00 14.53           C  
ANISOU  258  C   VAL A  23     3335   1729    457   -478    151   -179       C  
ATOM    259  O   VAL A  23      10.423   9.942  29.589  1.00 17.08           O  
ANISOU  259  O   VAL A  23     4088   1712    691   -506    534   -282       O  
ATOM    260  CB  VAL A  23      10.383   8.353  26.762  1.00 14.93           C  
ANISOU  260  CB  VAL A  23     3299   1834    540   -339     86    -96       C  
ATOM    261  CG1 VAL A  23       9.428   9.509  26.742  1.00 15.61           C  
ANISOU  261  CG1 VAL A  23     3444   1484   1000   -121   -205     36       C  
ATOM    262  CG2 VAL A  23      11.211   8.333  25.497  1.00 15.37           C  
ANISOU  262  CG2 VAL A  23     3471   2011    356    -46    259     40       C  
ATOM    263  N   GLY A  24      10.078   7.809  30.026  1.00 13.42           N  
ANISOU  263  N   GLY A  24     3242   1578    279   -471    176    -66       N  
ATOM    264  CA  GLY A  24       9.322   8.018  31.271  1.00 14.36           C  
ANISOU  264  CA  GLY A  24     3123   1803    529   -391    189    -54       C  
ATOM    265  C   GLY A  24       7.840   7.674  31.143  1.00 13.58           C  
ANISOU  265  C   GLY A  24     2998   1643    517   -251    292    -46       C  
ATOM    266  O   GLY A  24       7.038   8.065  32.006  1.00 15.89           O  
ANISOU  266  O   GLY A  24     3172   2069    793   -375    313   -179       O  
ATOM    267  N   VAL A  25       7.448   6.907  30.126  1.00 12.33           N  
ANISOU  267  N   VAL A  25     2887   1240    556   -199     54     10       N  
ATOM    268  CA  VAL A  25       6.051   6.550  29.965  1.00 12.01           C  
ANISOU  268  CA  VAL A  25     2771   1321    470    -54      1     88       C  
ATOM    269  C   VAL A  25       5.663   5.510  31.018  1.00 11.97           C  
ANISOU  269  C   VAL A  25     2616   1521    411   -172    -65    -98       C  
ATOM    270  O   VAL A  25       6.417   4.557  31.260  1.00 13.04           O  
ANISOU  270  O   VAL A  25     2982   1637    335   -247   -125    216       O  
ATOM    271  CB  VAL A  25       5.832   5.972  28.552  1.00 11.89           C  
ANISOU  271  CB  VAL A  25     2723   1242    552     20    -34     12       C  
ATOM    272  CG1 VAL A  25       4.376   5.704  28.365  1.00 13.64           C  
ANISOU  272  CG1 VAL A  25     2832   1826    524   -155   -116    116       C  
ATOM    273  CG2 VAL A  25       6.399   6.929  27.439  1.00 13.83           C  
ANISOU  273  CG2 VAL A  25     3209   1573    472   -126    -76    429       C  
ATOM    274  N   GLY A  26       4.496   5.708  31.631  1.00 13.16           N  
ANISOU  274  N   GLY A  26     2771   1807    420   -174     40     67       N  
ATOM    275  CA  GLY A  26       4.044   4.797  32.660  1.00 13.49           C  
ANISOU  275  CA  GLY A  26     2627   2076    419   -300      1    -25       C  
ATOM    276  C   GLY A  26       3.516   3.477  32.141  1.00 12.70           C  
ANISOU  276  C   GLY A  26     2569   1912    344   -222     20     54       C  
ATOM    277  O   GLY A  26       3.271   3.306  30.962  1.00 13.37           O  
ANISOU  277  O   GLY A  26     2810   2012    256   -360    -51    -57       O  
ATOM    278  N   PHE A  27       3.312   2.539  33.052  1.00 12.98           N  
ANISOU  278  N   PHE A  27     2817   1842    270   -227   -127     27       N  
ATOM    279  CA  PHE A  27       3.019   1.164  32.678  1.00 12.73           C  
ANISOU  279  CA  PHE A  27     2579   1802    455   -245    -51    151       C  
ATOM    280  C   PHE A  27       1.808   1.033  31.769  1.00 12.01           C  
ANISOU  280  C   PHE A  27     2471   1573    518   -324      4    213       C  
ATOM    281  O   PHE A  27       1.891   0.417  30.706  1.00 12.82           O  
ANISOU  281  O   PHE A  27     2802   1756    314   -345    -97     70       O  
ATOM    282  CB  PHE A  27       2.776   0.349  33.985  1.00 13.49           C  
ANISOU  282  CB  PHE A  27     2697   1929    498   -243    -30    220       C  
ATOM    283  CG  PHE A  27       2.389  -1.077  33.702  1.00 14.03           C  
ANISOU  283  CG  PHE A  27     2922   1970    437   -309   -367    433       C  
ATOM    284  CD1 PHE A  27       3.341  -2.087  33.593  1.00 16.44           C  
ANISOU  284  CD1 PHE A  27     3412   2274    557   -459    -83    326       C  
ATOM    285  CD2 PHE A  27       1.083  -1.400  33.586  1.00 16.06           C  
ANISOU  285  CD2 PHE A  27     3110   2001    990   -225   -435    709       C  
ATOM    286  CE1 PHE A  27       2.945  -3.403  33.331  1.00 18.94           C  
ANISOU  286  CE1 PHE A  27     3672   2220   1301   -254     87    352       C  
ATOM    287  CE2 PHE A  27       0.688  -2.718  33.314  1.00 17.27           C  
ANISOU  287  CE2 PHE A  27     3445   2248    869   -608   -458    764       C  
ATOM    288  CZ  PHE A  27       1.610  -3.691  33.184  1.00 18.12           C  
ANISOU  288  CZ  PHE A  27     3786   2236    860   -448   -408    213       C  
ATOM    289  N   ALA A  28       0.652   1.549  32.171  1.00 12.82           N  
ANISOU  289  N   ALA A  28     2626   1785    459   -260     59     79       N  
ATOM    290  CA  ALA A  28      -0.589   1.308  31.402  1.00 13.32           C  
ANISOU  290  CA  ALA A  28     2548   1857    655   -219    -15    338       C  
ATOM    291  C   ALA A  28      -0.489   1.943  30.036  1.00 12.79           C  
ANISOU  291  C   ALA A  28     2548   1680    632   -248    -60    190       C  
ATOM    292  O   ALA A  28      -0.913   1.350  29.040  1.00 14.25           O  
ANISOU  292  O   ALA A  28     2749   1917    747   -382   -194     28       O  
ATOM    293  CB  ALA A  28      -1.792   1.838  32.162  1.00 15.40           C  
ANISOU  293  CB  ALA A  28     2641   2030   1178   -138    300    297       C  
ATOM    294  N   THR A  29       0.093   3.143  29.944  1.00 12.77           N  
ANISOU  294  N   THR A  29     2687   1707    456   -287    -82     83       N  
ATOM    295  CA  THR A  29       0.284   3.793  28.662  1.00 12.17           C  
ANISOU  295  CA  THR A  29     2455   1667    502   -141   -117    250       C  
ATOM    296  C   THR A  29       1.222   2.964  27.812  1.00 12.22           C  
ANISOU  296  C   THR A  29     2444   1641    555   -193    -13     48       C  
ATOM    297  O   THR A  29       0.959   2.789  26.597  1.00 12.78           O  
ANISOU  297  O   THR A  29     2705   1814    335   -224   -216     31       O  
ATOM    298  CB  THR A  29       0.743   5.234  28.835  1.00 13.70           C  
ANISOU  298  CB  THR A  29     2716   1578    909   -176    -57    314       C  
ATOM    299  OG1 THR A  29      -0.249   5.958  29.574  1.00 16.63           O  
ANISOU  299  OG1 THR A  29     3001   2012   1303    107      0    226       O  
ATOM    300  CG2 THR A  29       0.916   5.905  27.494  1.00 15.00           C  
ANISOU  300  CG2 THR A  29     2760   1613   1326   -128   -141    568       C  
ATOM    301  N   ARG A  30       2.326   2.457  28.347  1.00 11.99           N  
ANISOU  301  N   ARG A  30     2545   1746    264   -227   -112    101       N  
ATOM    302  CA  ARG A  30       3.228   1.629  27.543  1.00 11.70           C  
ANISOU  302  CA  ARG A  30     2407   1762    275   -162     90    159       C  
ATOM    303  C   ARG A  30       2.554   0.428  27.006  1.00 11.96           C  
ANISOU  303  C   ARG A  30     2337   1906    300   -189    -57    278       C  
ATOM    304  O   ARG A  30       2.775   0.057  25.849  1.00 12.84           O  
ANISOU  304  O   ARG A  30     2500   2105    272   -180      0    188       O  
ATOM    305  CB  ARG A  30       4.495   1.133  28.314  1.00 12.50           C  
ANISOU  305  CB  ARG A  30     2638   1810    299   -254    -41    260       C  
ATOM    306  CG  ARG A  30       5.449   2.228  28.696  1.00 12.52           C  
ANISOU  306  CG  ARG A  30     2727   1630    396    -79      7    171       C  
ATOM    307  CD  ARG A  30       6.827   1.679  28.975  1.00 11.86           C  
ANISOU  307  CD  ARG A  30     2564   1680    259   -144      2     91       C  
ATOM    308  NE  ARG A  30       6.764   0.510  29.877  1.00 12.22           N  
ANISOU  308  NE  ARG A  30     2717   1577    348    -97     37     28       N  
ATOM    309  CZ  ARG A  30       6.631   0.549  31.184  1.00 12.31           C  
ANISOU  309  CZ  ARG A  30     2629   1491    555   -109     13    214       C  
ATOM    310  NH1 ARG A  30       6.508   1.701  31.846  1.00 12.80           N  
ANISOU  310  NH1 ARG A  30     3017   1507    336   -170    -86    224       N  
ATOM    311  NH2 ARG A  30       6.588  -0.596  31.866  1.00 13.87           N  
ANISOU  311  NH2 ARG A  30     3270   1697    300     32    147     95       N  
ATOM    312  N   LYS A  31       1.754  -0.250  27.810  1.00 12.58           N  
ANISOU  312  N   LYS A  31     2537   1942    300   -264      9     94       N  
ATOM    313  CA  LYS A  31       1.110  -1.472  27.353  1.00 12.96           C  
ANISOU  313  CA  LYS A  31     2578   1774    570   -193      0    -49       C  
ATOM    314  C   LYS A  31       0.150  -1.187  26.198  1.00 12.97           C  
ANISOU  314  C   LYS A  31     2406   2031    489   -175    -62   -100       C  
ATOM    315  O   LYS A  31       0.150  -1.905  25.177  1.00 14.42           O  
ANISOU  315  O   LYS A  31     2657   2164    658   -122    -31   -333       O  
ATOM    316  CB  LYS A  31       0.358  -2.184  28.486  1.00 14.24           C  
ANISOU  316  CB  LYS A  31     2898   1814    698   -273   -103    -13       C  
ATOM    317  CG  LYS A  31       1.294  -2.725  29.572  1.00 17.39           C  
ANISOU  317  CG  LYS A  31     3240   2388    980   -371   -110    414       C  
ATOM    318  CD  LYS A  31       2.302  -3.755  29.049  1.00 22.75           C  
ANISOU  318  CD  LYS A  31     3871   3068   1703    279   -306    625       C  
ATOM    319  CE  LYS A  31       3.511  -4.034  29.929  1.00 26.27           C  
ANISOU  319  CE  LYS A  31     3930   3910   2141    387   -167    -69       C  
ATOM    320  NZ  LYS A  31       4.716  -4.348  29.079  1.00 28.30           N  
ANISOU  320  NZ  LYS A  31     4070   4126   2557    615   -115    -32       N  
ATOM    321  N   VAL A  32      -0.676  -0.175  26.325  1.00 12.62           N  
ANISOU  321  N   VAL A  32     2400   2011    381   -128    -67   -176       N  
ATOM    322  CA AVAL A  32      -1.652   0.161  25.269  0.50 13.49           C  
ANISOU  322  CA AVAL A  32     2415   2108    601   -137    -80   -256       C  
ATOM    323  CA BVAL A  32      -1.641   0.092  25.241  0.50 13.53           C  
ANISOU  323  CA BVAL A  32     2410   2150    578   -152    -97   -256       C  
ATOM    324  C   VAL A  32      -0.964   0.765  24.058  1.00 12.95           C  
ANISOU  324  C   VAL A  32     2273   2140    507   -178   -111   -152       C  
ATOM    325  O   VAL A  32      -1.309   0.476  22.909  1.00 13.63           O  
ANISOU  325  O   VAL A  32     2350   2409    417   -246    -50   -292       O  
ATOM    326  CB AVAL A  32      -2.735   1.158  25.852  0.50 13.38           C  
ANISOU  326  CB AVAL A  32     2437   2093    554    -87    -30   -426       C  
ATOM    327  CB BVAL A  32      -2.899   0.882  25.781  0.50 13.95           C  
ANISOU  327  CB BVAL A  32     2421   2290    588    -96    -24   -253       C  
ATOM    328  CG1AVAL A  32      -3.683   1.596  24.756  0.50 13.72           C  
ANISOU  328  CG1AVAL A  32     2288   2109    814     27   -134   -137       C  
ATOM    329  CG1BVAL A  32      -3.686   0.015  26.784  0.50 14.03           C  
ANISOU  329  CG1BVAL A  32     2310   2326    692   -326   -109   -200       C  
ATOM    330  CG2AVAL A  32      -3.519   0.518  27.035  0.50 15.00           C  
ANISOU  330  CG2AVAL A  32     2680   2209    808   -331    104   -273       C  
ATOM    331  CG2BVAL A  32      -2.484   2.236  26.353  0.50 15.57           C  
ANISOU  331  CG2BVAL A  32     2705   2139   1069     26     75   -274       C  
ATOM    332  N   ALA A  33       0.025   1.621  24.274  1.00 12.99           N  
ANISOU  332  N   ALA A  33     2418   2150    367   -106   -202    -79       N  
ATOM    333  CA  ALA A  33       0.724   2.241  23.145  1.00 13.95           C  
ANISOU  333  CA  ALA A  33     2526   2335    437   -130   -127    253       C  
ATOM    334  C   ALA A  33       1.503   1.183  22.395  1.00 13.95           C  
ANISOU  334  C   ALA A  33     2435   2476    386    -99   -114    284       C  
ATOM    335  O   ALA A  33       1.617   1.265  21.168  1.00 14.87           O  
ANISOU  335  O   ALA A  33     2682   2631    334   -200     18    435       O  
ATOM    336  CB  ALA A  33       1.627   3.373  23.627  1.00 14.55           C  
ANISOU  336  CB  ALA A  33     2483   2415    628   -221    -61    269       C  
ATOM    337  N   GLY A  34       2.070   0.192  23.064  1.00 14.21           N  
ANISOU  337  N   GLY A  34     2506   2529    362     98     -9    247       N  
ATOM    338  CA  GLY A  34       2.851  -0.833  22.415  1.00 14.96           C  
ANISOU  338  CA  GLY A  34     2406   2641    636    212    -11    247       C  
ATOM    339  C   GLY A  34       2.044  -1.746  21.505  1.00 14.74           C  
ANISOU  339  C   GLY A  34     2516   2570    514    200     55    250       C  
ATOM    340  O   GLY A  34       2.600  -2.272  20.560  1.00 16.58           O  
ANISOU  340  O   GLY A  34     2547   2980    773    235    284     51       O  
ATOM    341  N   MET A  35       0.745  -1.910  21.760  1.00 13.97           N  
ANISOU  341  N   MET A  35     2539   2179    587    119    324    446       N  
ATOM    342  CA  MET A  35      -0.124  -2.725  20.910  1.00 14.13           C  
ANISOU  342  CA  MET A  35     2542   2007    819     40    299    509       C  
ATOM    343  C   MET A  35      -0.450  -2.053  19.558  1.00 13.25           C  
ANISOU  343  C   MET A  35     2519   1789    725    -10    268    551       C  
ATOM    344  O   MET A  35      -0.730  -2.729  18.547  1.00 15.27           O  
ANISOU  344  O   MET A  35     2717   1878   1206   -166     55    434       O  
ATOM    345  CB  MET A  35      -1.434  -3.043  21.584  1.00 14.86           C  
ANISOU  345  CB  MET A  35     2650   1709   1287     81    448    575       C  
ATOM    346  CG  MET A  35      -1.304  -3.950  22.773  1.00 14.18           C  
ANISOU  346  CG  MET A  35     3183   1578    627   -211    563    129       C  
ATOM    347  SD  MET A  35      -0.669  -5.547  22.430  1.00 14.44           S  
ANISOU  347  SD  MET A  35     3065   1555    865     49    224    230       S  
ATOM    348  CE  MET A  35      -1.749  -6.264  21.252  1.00 20.72           C  
ANISOU  348  CE  MET A  35     4571   2249   1050    -61   -436    524       C  
ATOM    349  N   ALA A  36      -0.390  -0.727  19.511  1.00 13.36           N  
ANISOU  349  N   ALA A  36     2392   1789    894    -80     92    524       N  
ATOM    350  CA  ALA A  36      -0.896  -0.027  18.347  1.00 13.21           C  
ANISOU  350  CA  ALA A  36     2339   1900    780    -21    154    417       C  
ATOM    351  C   ALA A  36      -0.095  -0.295  17.102  1.00 12.35           C  
ANISOU  351  C   ALA A  36     2362   1634    695   -233     51    277       C  
ATOM    352  O   ALA A  36       1.112  -0.426  17.140  1.00 13.23           O  
ANISOU  352  O   ALA A  36     2352   2035    639   -134     22    288       O  
ATOM    353  CB  ALA A  36      -0.911   1.473  18.649  1.00 14.87           C  
ANISOU  353  CB  ALA A  36     2834   1934    882    147    259    329       C  
ATOM    354  N   LYS A  37      -0.809  -0.356  16.005  1.00 13.09           N  
ANISOU  354  N   LYS A  37     2407   1757    807   -290    -31    305       N  
ATOM    355  CA  LYS A  37      -0.252  -0.521  14.676  1.00 13.23           C  
ANISOU  355  CA  LYS A  37     2585   1640    801   -274     46    115       C  
ATOM    356  C   LYS A  37      -0.730   0.663  13.852  1.00 12.35           C  
ANISOU  356  C   LYS A  37     2523   1714    455   -321    124     53       C  
ATOM    357  O   LYS A  37      -1.652   0.557  13.042  1.00 14.00           O  
ANISOU  357  O   LYS A  37     2549   2092    675   -454   -121    262       O  
ATOM    358  CB  LYS A  37      -0.644  -1.856  14.049  1.00 15.55           C  
ANISOU  358  CB  LYS A  37     2869   1931   1105   -285     80    104       C  
ATOM    359  CG  LYS A  37      -0.037  -3.066  14.748  1.00 19.68           C  
ANISOU  359  CG  LYS A  37     3155   1978   2345   -363    -76    188       C  
ATOM    360  CD  LYS A  37       1.428  -3.201  14.383  1.00 21.59           C  
ANISOU  360  CD  LYS A  37     3429   2854   1918     16   -100    411       C  
ATOM    361  CE  LYS A  37       2.008  -4.530  14.735  1.00 24.71           C  
ANISOU  361  CE  LYS A  37     3933   3160   2293     63    -26    345       C  
ATOM    362  NZ  LYS A  37       1.812  -4.835  16.144  1.00 26.50           N  
ANISOU  362  NZ  LYS A  37     4678   2954   2436    383    149    748       N  
ATOM    363  N   PRO A  38      -0.154   1.835  14.037  1.00 12.03           N  
ANISOU  363  N   PRO A  38     2459   1568    541   -189     69     59       N  
ATOM    364  CA  PRO A  38      -0.699   3.027  13.435  1.00 12.50           C  
ANISOU  364  CA  PRO A  38     2630   1613    506   -118    217    145       C  
ATOM    365  C   PRO A  38      -0.517   3.103  11.943  1.00 12.59           C  
ANISOU  365  C   PRO A  38     2540   1470    770   -160    353     32       C  
ATOM    366  O   PRO A  38       0.383   2.496  11.358  1.00 13.09           O  
ANISOU  366  O   PRO A  38     2797   1630    544   -175    373    143       O  
ATOM    367  CB  PRO A  38       0.119   4.159  14.048  1.00 15.08           C  
ANISOU  367  CB  PRO A  38     2974   1842    912    -64    177    -13       C  
ATOM    368  CG  PRO A  38       1.263   3.493  14.682  1.00 18.40           C  
ANISOU  368  CG  PRO A  38     2877   2189   1925   -552   -182    152       C  
ATOM    369  CD  PRO A  38       0.917   2.149  14.985  1.00 12.61           C  
ANISOU  369  CD  PRO A  38     2472   1660    658   -289     19   -131       C  
ATOM    370  N   ASN A  39      -1.376   3.915  11.356  1.00 12.33           N  
ANISOU  370  N   ASN A  39     2772   1498    413    -82    362     98       N  
ATOM    371  CA  ASN A  39      -1.157   4.434  10.016  1.00 13.93           C  
ANISOU  371  CA  ASN A  39     3136   1490    666    -91    407     99       C  
ATOM    372  C   ASN A  39      -0.620   5.819  10.120  1.00 14.61           C  
ANISOU  372  C   ASN A  39     3433   1405    711   -143    571    -86       C  
ATOM    373  O   ASN A  39      -1.069   6.623  10.906  1.00 19.55           O  
ANISOU  373  O   ASN A  39     4155   1620   1650   -483   1386   -328       O  
ATOM    374  CB  ASN A  39      -2.453   4.428   9.266  1.00 16.71           C  
ANISOU  374  CB  ASN A  39     3520   1876    953     51    -20    242       C  
ATOM    375  CG  ASN A  39      -2.657   3.157   8.506  1.00 19.85           C  
ANISOU  375  CG  ASN A  39     3635   2239   1665    -34   -119    234       C  
ATOM    376  OD1 ASN A  39      -2.347   2.071   9.023  1.00 26.09           O  
ANISOU  376  OD1 ASN A  39     5225   2721   1963   -145   -802    258       O  
ATOM    377  ND2 ASN A  39      -3.140   3.278   7.273  1.00 27.04           N  
ANISOU  377  ND2 ASN A  39     4488   3835   1949    260   -295   -204       N  
ATOM    378  N   MET A  40       0.388   6.105   9.325  1.00 13.65           N  
ANISOU  378  N   MET A  40     3323   1274    586   -157    511    109       N  
ATOM    379  CA  MET A  40       0.983   7.404   9.324  1.00 13.42           C  
ANISOU  379  CA  MET A  40     3103   1348    648    -98    380     -8       C  
ATOM    380  C   MET A  40       0.822   7.991   7.932  1.00 12.45           C  
ANISOU  380  C   MET A  40     2912   1311    504    -91    432    137       C  
ATOM    381  O   MET A  40       1.153   7.364   6.944  1.00 13.84           O  
ANISOU  381  O   MET A  40     3407   1293    556    156    482    147       O  
ATOM    382  CB  MET A  40       2.453   7.261   9.702  1.00 14.63           C  
ANISOU  382  CB  MET A  40     3339   1469    750    -45    268     -2       C  
ATOM    383  CG  MET A  40       3.242   8.567   9.584  1.00 15.43           C  
ANISOU  383  CG  MET A  40     3414   1299   1147     47      1    201       C  
ATOM    384  SD  MET A  40       4.897   8.428  10.218  1.00 17.10           S  
ANISOU  384  SD  MET A  40     3724   1585   1187    -90   -232    -63       S  
ATOM    385  CE  MET A  40       5.583   7.094   9.262  1.00 19.34           C  
ANISOU  385  CE  MET A  40     3726   2671    949   -190    196     38       C  
ATOM    386  N   ILE A  41       0.292   9.200   7.871  1.00 12.38           N  
ANISOU  386  N   ILE A  41     2773   1308    621    -84    272    -40       N  
ATOM    387  CA  ILE A  41       0.072   9.899   6.623  1.00 11.80           C  
ANISOU  387  CA  ILE A  41     2701   1313    467   -172    132     -3       C  
ATOM    388  C   ILE A  41       0.952  11.115   6.620  1.00 10.73           C  
ANISOU  388  C   ILE A  41     2639   1031    406   -132     99     -4       C  
ATOM    389  O   ILE A  41       0.860  11.987   7.511  1.00 12.18           O  
ANISOU  389  O   ILE A  41     2929   1194    503   -257    229    -47       O  
ATOM    390  CB  ILE A  41      -1.410  10.356   6.479  1.00 14.32           C  
ANISOU  390  CB  ILE A  41     2725   1579   1134   -181    128   -165       C  
ATOM    391  CG1 ILE A  41      -2.367   9.147   6.596  1.00 18.60           C  
ANISOU  391  CG1 ILE A  41     2990   2063   2012   -360    205   -408       C  
ATOM    392  CG2 ILE A  41      -1.634  11.092   5.129  1.00 18.36           C  
ANISOU  392  CG2 ILE A  41     3168   2285   1524   -191   -278    -50       C  
ATOM    393  CD1 ILE A  41      -3.838   9.601   6.651  1.00 23.91           C  
ANISOU  393  CD1 ILE A  41     3215   2862   3005   -460   -124   -404       C  
ATOM    394  N   ILE A  42       1.821  11.205   5.622  1.00 10.51           N  
ANISOU  394  N   ILE A  42     2642   1090    260   -126     97    -17       N  
ATOM    395  CA  ILE A  42       2.776  12.317   5.496  1.00 10.38           C  
ANISOU  395  CA  ILE A  42     2565   1125    254    -12     45     -5       C  
ATOM    396  C   ILE A  42       2.428  13.057   4.235  1.00 10.50           C  
ANISOU  396  C   ILE A  42     2457   1275    258    -74   -104      5       C  
ATOM    397  O   ILE A  42       2.271  12.467   3.168  1.00 11.34           O  
ANISOU  397  O   ILE A  42     2858   1166    284    -87   -178     13       O  
ATOM    398  CB  ILE A  42       4.225  11.813   5.485  1.00 10.74           C  
ANISOU  398  CB  ILE A  42     2603   1220    255    -62     76    -12       C  
ATOM    399  CG1 ILE A  42       4.521  11.039   6.778  1.00 11.28           C  
ANISOU  399  CG1 ILE A  42     2727   1295    264    -30    -75     94       C  
ATOM    400  CG2 ILE A  42       5.199  12.955   5.295  1.00 11.26           C  
ANISOU  400  CG2 ILE A  42     2565   1285    426    -93     -4     52       C  
ATOM    401  CD1 ILE A  42       5.930  10.440   6.831  1.00 13.68           C  
ANISOU  401  CD1 ILE A  42     3063   1536    597    318   -223     79       C  
ATOM    402  N   SER A  43       2.274  14.378   4.359  1.00 10.64           N  
ANISOU  402  N   SER A  43     2668   1099    274     -7   -221     23       N  
ATOM    403  CA  SER A  43       1.968  15.201   3.209  1.00 11.09           C  
ANISOU  403  CA  SER A  43     2612   1203    397     -3   -184     44       C  
ATOM    404  C   SER A  43       2.746  16.492   3.287  1.00 10.81           C  
ANISOU  404  C   SER A  43     2791   1055    259    -12   -115    -23       C  
ATOM    405  O   SER A  43       3.227  16.891   4.359  1.00 11.20           O  
ANISOU  405  O   SER A  43     2795   1202    258     16   -103    -28       O  
ATOM    406  CB  SER A  43       0.479  15.473   3.171  1.00 13.33           C  
ANISOU  406  CB  SER A  43     2884   1292    886    -13   -293    296       C  
ATOM    407  OG  SER A  43       0.015  16.126   4.312  1.00 16.35           O  
ANISOU  407  OG  SER A  43     3014   1920   1277    202   -151    232       O  
ATOM    408  N   VAL A  44       2.869  17.136   2.135  1.00 10.99           N  
ANISOU  408  N   VAL A  44     2814   1086    272    -67   -148     98       N  
ATOM    409  CA  VAL A  44       3.574  18.395   2.035  1.00 11.44           C  
ANISOU  409  CA  VAL A  44     2914   1127    304    -60   -235    167       C  
ATOM    410  C   VAL A  44       2.737  19.372   1.244  1.00 11.86           C  
ANISOU  410  C   VAL A  44     3004   1232    270    -20   -138     98       C  
ATOM    411  O   VAL A  44       2.152  19.010   0.210  1.00 15.69           O  
ANISOU  411  O   VAL A  44     4159   1402    399     17   -743     69       O  
ATOM    412  CB  VAL A  44       4.963  18.251   1.369  1.00 13.36           C  
ANISOU  412  CB  VAL A  44     2998   1386    691    -54   -264     54       C  
ATOM    413  CG1 VAL A  44       5.663  19.584   1.298  1.00 19.69           C  
ANISOU  413  CG1 VAL A  44     3283   1716   2481   -356     11    366       C  
ATOM    414  CG2 VAL A  44       5.799  17.240   2.082  1.00 16.18           C  
ANISOU  414  CG2 VAL A  44     3003   1956   1187    -67   -357     -9       C  
ATOM    415  N   ASN A  45       2.686  20.600   1.695  1.00 11.46           N  
ANISOU  415  N   ASN A  45     2843   1240    269    -45   -201     21       N  
ATOM    416  CA  ASN A  45       1.982  21.684   1.014  1.00 11.12           C  
ANISOU  416  CA  ASN A  45     2714   1226    285    -88   -271     28       C  
ATOM    417  C   ASN A  45       2.850  22.908   1.170  1.00 11.76           C  
ANISOU  417  C   ASN A  45     2781   1319    368     -6   -136    225       C  
ATOM    418  O   ASN A  45       2.956  23.496   2.241  1.00 11.55           O  
ANISOU  418  O   ASN A  45     2727   1332    329    -43   -210     76       O  
ATOM    419  CB  ASN A  45       0.589  21.821   1.589  1.00 12.16           C  
ANISOU  419  CB  ASN A  45     2707   1347    563    -68   -245     89       C  
ATOM    420  CG  ASN A  45      -0.276  22.849   0.913  1.00 12.72           C  
ANISOU  420  CG  ASN A  45     2661   1710    461    -85   -313     52       C  
ATOM    421  OD1 ASN A  45      -1.533  22.657   0.829  1.00 14.61           O  
ANISOU  421  OD1 ASN A  45     2757   1877    914   -269   -142   -111       O  
ATOM    422  ND2 ASN A  45       0.329  23.893   0.416  1.00 12.39           N  
ANISOU  422  ND2 ASN A  45     2626   1496    584   -258   -428    301       N  
ATOM    423  N   GLY A  46       3.513  23.267   0.091  1.00 12.82           N  
ANISOU  423  N   GLY A  46     3113   1481    275   -257   -129    149       N  
ATOM    424  CA  GLY A  46       4.466  24.358   0.166  1.00 13.60           C  
ANISOU  424  CA  GLY A  46     2903   1673    590   -246    -53    274       C  
ATOM    425  C   GLY A  46       5.601  24.018   1.117  1.00 13.46           C  
ANISOU  425  C   GLY A  46     2755   1752    605   -259     76    293       C  
ATOM    426  O   GLY A  46       6.216  22.956   1.008  1.00 15.61           O  
ANISOU  426  O   GLY A  46     2943   1973   1015    -72     64     47       O  
ATOM    427  N   ASP A  47       5.841  24.878   2.094  1.00 13.22           N  
ANISOU  427  N   ASP A  47     2791   1610    621   -258    -51    270       N  
ATOM    428  CA  ASP A  47       6.874  24.640   3.104  1.00 13.92           C  
ANISOU  428  CA  ASP A  47     2668   1795    827   -190    -52    342       C  
ATOM    429  C   ASP A  47       6.381  23.802   4.278  1.00 11.72           C  
ANISOU  429  C   ASP A  47     2491   1431    528    -50    -45    191       C  
ATOM    430  O   ASP A  47       7.183  23.495   5.165  1.00 12.76           O  
ANISOU  430  O   ASP A  47     2432   1791    622    -56    -75    198       O  
ATOM    431  CB  ASP A  47       7.405  25.991   3.620  1.00 15.29           C  
ANISOU  431  CB  ASP A  47     2842   1985    982   -375   -222    376       C  
ATOM    432  CG  ASP A  47       8.104  26.788   2.587  1.00 21.56           C  
ANISOU  432  CG  ASP A  47     3353   2667   2170   -504   -186    415       C  
ATOM    433  OD1 ASP A  47       8.684  26.187   1.675  1.00 27.03           O  
ANISOU  433  OD1 ASP A  47     3831   4239   2197  -1028    814    730       O  
ATOM    434  OD2 ASP A  47       8.102  28.027   2.730  1.00 28.42           O  
ANISOU  434  OD2 ASP A  47     4802   2998   2995   -840   -554    792       O  
ATOM    435  N   VAL A  48       5.098  23.537   4.319  1.00 10.38           N  
ANISOU  435  N   VAL A  48     2376   1257    311    -42    -88    235       N  
ATOM    436  CA  VAL A  48       4.520  22.886   5.503  1.00  9.87           C  
ANISOU  436  CA  VAL A  48     2284   1194    271    -36    -46    127       C  
ATOM    437  C   VAL A  48       4.420  21.394   5.305  1.00  9.73           C  
ANISOU  437  C   VAL A  48     2243   1185    267    -70   -162     36       C  
ATOM    438  O   VAL A  48       3.766  20.911   4.375  1.00 11.03           O  
ANISOU  438  O   VAL A  48     2568   1302    317    -46   -267     83       O  
ATOM    439  CB  VAL A  48       3.129  23.433   5.798  1.00 11.16           C  
ANISOU  439  CB  VAL A  48     2382   1443    412      0   -110    138       C  
ATOM    440  CG1 VAL A  48       2.589  22.794   7.103  1.00 12.50           C  
ANISOU  440  CG1 VAL A  48     2625   1560    562    -54    167    270       C  
ATOM    441  CG2 VAL A  48       3.194  24.988   6.008  1.00 13.64           C  
ANISOU  441  CG2 VAL A  48     2904   1263   1015    204     94    139       C  
ATOM    442  N   ILE A  49       5.034  20.639   6.223  1.00  9.40           N  
ANISOU  442  N   ILE A  49     2269   1036    265   -151   -113     75       N  
ATOM    443  CA  ILE A  49       4.950  19.192   6.253  1.00  9.38           C  
ANISOU  443  CA  ILE A  49     2154   1153    255   -145    -47    -29       C  
ATOM    444  C   ILE A  49       3.947  18.818   7.331  1.00  9.30           C  
ANISOU  444  C   ILE A  49     2182   1096    254    -70    -42     26       C  
ATOM    445  O   ILE A  49       3.997  19.404   8.450  1.00  9.68           O  
ANISOU  445  O   ILE A  49     2247   1170    261   -141    -42    -78       O  
ATOM    446  CB  ILE A  49       6.320  18.585   6.523  1.00 10.41           C  
ANISOU  446  CB  ILE A  49     2357   1337    261    -72     86    -69       C  
ATOM    447  CG1 ILE A  49       7.337  19.004   5.475  1.00 11.25           C  
ANISOU  447  CG1 ILE A  49     2347   1554    372    -67    196    -51       C  
ATOM    448  CG2 ILE A  49       6.271  17.053   6.629  1.00 11.59           C  
ANISOU  448  CG2 ILE A  49     2550   1193    658     92   -160    -65       C  
ATOM    449  CD1 ILE A  49       8.788  18.773   5.893  1.00 16.87           C  
ANISOU  449  CD1 ILE A  49     2642   2717   1050    -46    123    248       C  
ATOM    450  N   THR A  50       3.095  17.861   7.049  1.00  9.55           N  
ANISOU  450  N   THR A  50     2178   1193    255   -133      8    -47       N  
ATOM    451  CA  THR A  50       2.175  17.332   8.062  1.00  9.79           C  
ANISOU  451  CA  THR A  50     2233   1224    263   -189    121     35       C  
ATOM    452  C   THR A  50       2.417  15.845   8.197  1.00  9.46           C  
ANISOU  452  C   THR A  50     2080   1258    253   -142      7    -25       C  
ATOM    453  O   THR A  50       2.531  15.087   7.218  1.00 10.55           O  
ANISOU  453  O   THR A  50     2613   1140    254   -162    -24     23       O  
ATOM    454  CB  THR A  50       0.690  17.591   7.659  1.00 10.58           C  
ANISOU  454  CB  THR A  50     2348   1262    408   -298      5    -94       C  
ATOM    455  OG1 THR A  50       0.499  18.994   7.533  1.00 11.69           O  
ANISOU  455  OG1 THR A  50     2351   1480    609    -48    -29     31       O  
ATOM    456  CG2 THR A  50      -0.298  17.046   8.633  1.00 12.81           C  
ANISOU  456  CG2 THR A  50     2510   1566    788   -368    194     26       C  
ATOM    457  N   ILE A  51       2.528  15.395   9.465  1.00  9.56           N  
ANISOU  457  N   ILE A  51     2270   1105    256   -113      4     48       N  
ATOM    458  CA  ILE A  51       2.617  13.991   9.810  1.00  9.90           C  
ANISOU  458  CA  ILE A  51     2354   1139    269   -191     29    -36       C  
ATOM    459  C   ILE A  51       1.428  13.665  10.724  1.00 10.10           C  
ANISOU  459  C   ILE A  51     2349   1222    265   -166     90     81       C  
ATOM    460  O   ILE A  51       1.346  14.194  11.843  1.00 11.30           O  
ANISOU  460  O   ILE A  51     2684   1349    259    -40     55    -24       O  
ATOM    461  CB  ILE A  51       3.942  13.622  10.507  1.00  9.83           C  
ANISOU  461  CB  ILE A  51     2334   1139    260   -156     57    -75       C  
ATOM    462  CG1 ILE A  51       5.130  13.995   9.615  1.00 11.15           C  
ANISOU  462  CG1 ILE A  51     2376   1324    535   -124    141   -214       C  
ATOM    463  CG2 ILE A  51       3.955  12.168  10.906  1.00 12.16           C  
ANISOU  463  CG2 ILE A  51     2765   1126    727     22     98    106       C  
ATOM    464  CD1 ILE A  51       6.467  13.736  10.226  1.00 13.59           C  
ANISOU  464  CD1 ILE A  51     2493   1801    870     59    -59    -91       C  
ATOM    465  N   LYS A  52       0.508  12.854  10.244  1.00 10.57           N  
ANISOU  465  N   LYS A  52     2427   1286    304   -223    130    -16       N  
ATOM    466  CA  LYS A  52      -0.641  12.390  10.989  1.00 12.22           C  
ANISOU  466  CA  LYS A  52     2617   1332    693   -195    309    -64       C  
ATOM    467  C   LYS A  52      -0.438  10.941  11.350  1.00 12.71           C  
ANISOU  467  C   LYS A  52     2725   1397    706   -288    373   -251       C  
ATOM    468  O   LYS A  52      -0.054  10.145  10.506  1.00 15.39           O  
ANISOU  468  O   LYS A  52     3700   1270    878   -272    737    -33       O  
ATOM    469  CB  LYS A  52      -1.894  12.529  10.138  1.00 15.27           C  
ANISOU  469  CB  LYS A  52     2543   2072   1187   -149    341   -326       C  
ATOM    470  CG  LYS A  52      -3.232  12.322  10.743  1.00 20.28           C  
ANISOU  470  CG  LYS A  52     3220   2642   1842   -369    104    299       C  
ATOM    471  CD  LYS A  52      -4.297  12.670   9.705  1.00 26.04           C  
ANISOU  471  CD  LYS A  52     3465   3717   2709   -150   -241    113       C  
ATOM    472  CE  LYS A  52      -4.211  14.142   9.323  1.00 32.14           C  
ANISOU  472  CE  LYS A  52     4015   4129   4068   -310   -430    -67       C  
ATOM    473  NZ  LYS A  52      -3.347  14.503   8.155  1.00 35.98           N  
ANISOU  473  NZ  LYS A  52     4349   4783   4537   -245   -270   -324       N  
ATOM    474  N   SER A  53      -0.767  10.597  12.579  1.00 12.19           N  
ANISOU  474  N   SER A  53     2761   1288    582   -258    315   -108       N  
ATOM    475  CA  SER A  53      -0.774   9.201  13.040  1.00 12.51           C  
ANISOU  475  CA  SER A  53     2709   1400    642   -226    316     49       C  
ATOM    476  C   SER A  53      -2.209   8.853  13.453  1.00 12.23           C  
ANISOU  476  C   SER A  53     2680   1519    446   -328    330    -48       C  
ATOM    477  O   SER A  53      -2.772   9.518  14.298  1.00 14.50           O  
ANISOU  477  O   SER A  53     3030   1630    847   -440    522   -178       O  
ATOM    478  CB  SER A  53       0.154   9.024  14.213  1.00 14.18           C  
ANISOU  478  CB  SER A  53     2745   1635   1006   -203    301     15       C  
ATOM    479  OG  SER A  53       0.188   7.670  14.671  1.00 16.98           O  
ANISOU  479  OG  SER A  53     3485   1793   1173   -227    109    332       O  
ATOM    480  N   GLU A  54      -2.748   7.843  12.783  1.00 13.04           N  
ANISOU  480  N   GLU A  54     2720   1694    540   -363    248    -24       N  
ATOM    481  CA  GLU A  54      -4.066   7.326  13.074  1.00 14.03           C  
ANISOU  481  CA  GLU A  54     2742   1764    825   -353    171     18       C  
ATOM    482  C   GLU A  54      -3.865   6.014  13.803  1.00 13.56           C  
ANISOU  482  C   GLU A  54     2630   1776    744   -294    327     86       C  
ATOM    483  O   GLU A  54      -3.309   5.070  13.221  1.00 13.62           O  
ANISOU  483  O   GLU A  54     2828   1756    591   -165    261    112       O  
ATOM    484  CB  GLU A  54      -4.848   7.099  11.804  1.00 16.04           C  
ANISOU  484  CB  GLU A  54     2949   1918   1225   -373     47    130       C  
ATOM    485  CG  GLU A  54      -5.049   8.356  10.985  1.00 21.64           C  
ANISOU  485  CG  GLU A  54     3500   2526   2194   -377     75    374       C  
ATOM    486  CD  GLU A  54      -5.991   8.170   9.872  1.00 27.44           C  
ANISOU  486  CD  GLU A  54     4028   3383   3012   -169   -407    423       C  
ATOM    487  OE1 GLU A  54      -5.846   7.171   9.169  1.00 29.86           O  
ANISOU  487  OE1 GLU A  54     4922   4364   2057   -449  -1033      4       O  
ATOM    488  OE2 GLU A  54      -6.856   9.046   9.676  1.00 35.75           O  
ANISOU  488  OE2 GLU A  54     4641   4534   4407    232   -391    267       O  
ATOM    489  N  ASER A  55      -4.334   5.863  15.042  0.50 15.07           N  
ANISOU  489  N  ASER A  55     2719   2066    940   -154    327    139       N  
ATOM    490  N  BSER A  55      -4.268   6.043  15.053  0.50 13.51           N  
ANISOU  490  N  BSER A  55     2705   1784    643    -86    249    154       N  
ATOM    491  CA ASER A  55      -4.315   4.516  15.684  0.50 15.37           C  
ANISOU  491  CA ASER A  55     2640   2207    992    -73    398    318       C  
ATOM    492  CA BSER A  55      -3.808   5.080  15.985  0.50 13.06           C  
ANISOU  492  CA BSER A  55     2678   1505    777     52    203    217       C  
ATOM    493  C  ASER A  55      -5.434   4.308  16.667  0.50 14.74           C  
ANISOU  493  C  ASER A  55     2744   1888    968   -109    506    276       C  
ATOM    494  C  BSER A  55      -4.924   4.690  16.910  0.50 12.89           C  
ANISOU  494  C  BSER A  55     2929   1427    538     26    287    246       C  
ATOM    495  O  ASER A  55      -6.253   5.169  16.922  0.50 14.71           O  
ANISOU  495  O  ASER A  55     2719   1705   1163   -138    370    357       O  
ATOM    496  O  BSER A  55      -5.666   5.514  17.410  0.50 13.92           O  
ANISOU  496  O  BSER A  55     3096   1364    827    269    399    290       O  
ATOM    497  CB ASER A  55      -2.974   4.219  16.393  0.50 17.49           C  
ANISOU  497  CB ASER A  55     2785   2375   1483      9    365    218       C  
ATOM    498  CB BSER A  55      -2.660   5.643  16.784  0.50 13.33           C  
ANISOU  498  CB BSER A  55     2730   1500    832     19    167    253       C  
ATOM    499  OG ASER A  55      -2.986   4.608  17.740  0.50 16.04           O  
ANISOU  499  OG ASER A  55     2370   2293   1429    -40    589    685       O  
ATOM    500  OG BSER A  55      -2.207   4.707  17.735  0.50 14.76           O  
ANISOU  500  OG BSER A  55     2486   2259    861    230    313    622       O  
ATOM    501  N  ATHR A  56      -5.453   3.096  17.183  0.50 14.80           N  
ANISOU  501  N  ATHR A  56     2977   1803    844      1    532    254       N  
ATOM    502  N  BTHR A  56      -5.050   3.415  17.133  0.50 14.08           N  
ANISOU  502  N  BTHR A  56     3092   1479    778     90    202    229       N  
ATOM    503  CA ATHR A  56      -6.202   2.726  18.346  0.50 14.70           C  
ANISOU  503  CA ATHR A  56     3226   1737    620    -94    589    223       C  
ATOM    504  CA BTHR A  56      -6.101   2.881  17.971  0.50 15.49           C  
ANISOU  504  CA BTHR A  56     3336   1588    960     -5    155    365       C  
ATOM    505  C  ATHR A  56      -5.652   3.238  19.684  0.50 15.06           C  
ANISOU  505  C  ATHR A  56     3203   1726    792    -32    521    173       C  
ATOM    506  C  BTHR A  56      -5.947   3.391  19.424  0.50 15.82           C  
ANISOU  506  C  BTHR A  56     3383   1587   1038   -102    240    301       C  
ATOM    507  O  ATHR A  56      -6.333   3.072  20.661  0.50 15.13           O  
ANISOU  507  O  ATHR A  56     3463   1813    472   -146    570    339       O  
ATOM    508  O  BTHR A  56      -6.946   3.574  20.180  0.50 17.81           O  
ANISOU  508  O  BTHR A  56     3604   1942   1221   -294    228    502       O  
ATOM    509  CB ATHR A  56      -6.102   1.199  18.438  0.50 14.88           C  
ANISOU  509  CB ATHR A  56     3178   1713    763    -72    572    287       C  
ATOM    510  CB BTHR A  56      -5.917   1.360  17.771  0.50 15.14           C  
ANISOU  510  CB BTHR A  56     3273   1607    872     56    131    327       C  
ATOM    511  OG1ATHR A  56      -4.716   0.799  18.185  0.50 11.67           O  
ANISOU  511  OG1ATHR A  56     2807   1326    297    228    220      8       O  
ATOM    512  OG1BTHR A  56      -6.837   0.855  16.773  0.50 17.78           O  
ANISOU  512  OG1BTHR A  56     3769   2250    737     44   -216    165       O  
ATOM    513  CG2ATHR A  56      -7.066   0.542  17.407  0.50 17.49           C  
ANISOU  513  CG2ATHR A  56     3878   1723   1041   -244    523    417       C  
ATOM    514  CG2BTHR A  56      -5.919   0.598  18.984  0.50 14.88           C  
ANISOU  514  CG2BTHR A  56     3277   1488    887    173    190    680       C  
ATOM    515  N  APHE A  57      -4.402   3.717  19.736  0.50 16.00           N  
ANISOU  515  N  APHE A  57     3437   1797    845    -47    460    173       N  
ATOM    516  N  BPHE A  57      -4.680   3.605  19.781  0.50 15.88           N  
ANISOU  516  N  BPHE A  57     3455   1604    974    -99    233    267       N  
ATOM    517  CA APHE A  57      -3.819   4.236  21.000  0.50 16.58           C  
ANISOU  517  CA APHE A  57     3378   1943    979    -51    411    130       C  
ATOM    518  CA BPHE A  57      -4.274   4.262  21.026  0.50 15.66           C  
ANISOU  518  CA BPHE A  57     3384   1719    844   -132    292    247       C  
ATOM    519  C  APHE A  57      -4.154   5.721  21.163  0.50 16.50           C  
ANISOU  519  C  APHE A  57     3389   1874   1003    -26    534    195       C  
ATOM    520  C  BPHE A  57      -4.595   5.750  20.979  0.50 15.27           C  
ANISOU  520  C  BPHE A  57     3275   1757    770    -55    333    275       C  
ATOM    521  O  APHE A  57      -4.810   6.133  22.129  0.50 16.78           O  
ANISOU  521  O  APHE A  57     3581   1976    817    -58    583    108       O  
ATOM    522  O  BPHE A  57      -5.631   6.154  21.484  0.50 16.74           O  
ANISOU  522  O  BPHE A  57     3233   1875   1249    -45    363    498       O  
ATOM    523  CB APHE A  57      -2.278   4.025  21.086  0.50 17.06           C  
ANISOU  523  CB APHE A  57     3483   1997   1001     -4    362    175       C  
ATOM    524  CB BPHE A  57      -2.764   4.055  21.300  0.50 15.93           C  
ANISOU  524  CB BPHE A  57     3479   1747    825     10    322    299       C  
ATOM    525  CG APHE A  57      -1.599   4.801  22.199  0.50 18.62           C  
ANISOU  525  CG APHE A  57     3407   2151   1514     58    255    176       C  
ATOM    526  CG BPHE A  57      -2.217   4.883  22.451  0.50 17.75           C  
ANISOU  526  CG BPHE A  57     3702   2160    881     48    103    426       C  
ATOM    527  CD1APHE A  57      -2.050   4.732  23.497  0.50 18.03           C  
ANISOU  527  CD1APHE A  57     3130   2152   1568      5    209    160       C  
ATOM    528  CD1BPHE A  57      -2.856   4.919  23.662  0.50 18.26           C  
ANISOU  528  CD1BPHE A  57     3848   2218    872     44     24    223       C  
ATOM    529  CD2APHE A  57      -0.505   5.609  21.920  0.50 19.66           C  
ANISOU  529  CD2APHE A  57     3547   2203   1718    -32    306    347       C  
ATOM    530  CD2BPHE A  57      -1.051   5.637  22.292  0.50 19.16           C  
ANISOU  530  CD2BPHE A  57     3499   2453   1324     67   -111    278       C  
ATOM    531  CE1APHE A  57      -1.419   5.449  24.486  0.50 19.24           C  
ANISOU  531  CE1APHE A  57     3162   2526   1620    -64    138    147       C  
ATOM    532  CE1BPHE A  57      -2.353   5.707  24.713  0.50 20.84           C  
ANISOU  532  CE1BPHE A  57     3745   2675   1497     56   -470    181       C  
ATOM    533  CE2APHE A  57       0.133   6.325  22.910  0.50 19.25           C  
ANISOU  533  CE2APHE A  57     3520   2272   1520    -27    378    783       C  
ATOM    534  CE2BPHE A  57      -0.556   6.411  23.330  0.50 20.63           C  
ANISOU  534  CE2BPHE A  57     3716   2584   1538    307   -320    493       C  
ATOM    535  CZ APHE A  57      -0.332   6.257  24.189  0.50 19.24           C  
ANISOU  535  CZ APHE A  57     3340   2465   1503     72    241    357       C  
ATOM    536  CZ BPHE A  57      -1.209   6.441  24.529  0.50 20.42           C  
ANISOU  536  CZ BPHE A  57     3841   2379   1539    187   -357    555       C  
ATOM    537  N  ALYS A  58      -3.709   6.541  20.224  0.50 16.85           N  
ANISOU  537  N  ALYS A  58     3292   1781   1327    -31    580    250       N  
ATOM    538  N  BLYS A  58      -3.698   6.572  20.418  0.50 15.79           N  
ANISOU  538  N  BLYS A  58     3131   1708   1159    -56    349    264       N  
ATOM    539  CA ALYS A  58      -3.938   7.993  20.304  0.50 16.58           C  
ANISOU  539  CA ALYS A  58     3047   1836   1416    -63    503    229       C  
ATOM    540  CA BLYS A  58      -3.912   8.053  20.355  0.50 16.04           C  
ANISOU  540  CA BLYS A  58     2960   1877   1255   -106    320    111       C  
ATOM    541  C  ALYS A  58      -3.593   8.565  18.939  0.50 16.64           C  
ANISOU  541  C  ALYS A  58     2954   1907   1458    -93    615    202       C  
ATOM    542  C  BLYS A  58      -3.557   8.673  19.013  0.50 15.63           C  
ANISOU  542  C  BLYS A  58     2837   1912   1189   -205    414     43       C  
ATOM    543  O  ALYS A  58      -2.519   8.291  18.420  0.50 19.47           O  
ANISOU  543  O  ALYS A  58     3279   2200   1916    164    621    405       O  
ATOM    544  O  BLYS A  58      -2.384   8.680  18.673  0.50 14.74           O  
ANISOU  544  O  BLYS A  58     2917   1861    823   -376     94   -172       O  
ATOM    545  CB ALYS A  58      -3.113   8.620  21.467  0.50 16.71           C  
ANISOU  545  CB ALYS A  58     2996   1828   1525   -154    389    238       C  
ATOM    546  CB BLYS A  58      -3.066   8.786  21.411  0.50 17.19           C  
ANISOU  546  CB BLYS A  58     2948   1991   1592   -146    223     85       C  
ATOM    547  CG ALYS A  58      -3.220  10.144  21.607  0.50 15.35           C  
ANISOU  547  CG ALYS A  58     2902   1717   1213   -238    268    191       C  
ATOM    548  CG BLYS A  58      -3.164   8.273  22.779  0.50 20.95           C  
ANISOU  548  CG BLYS A  58     3311   2724   1925    -79    160     72       C  
ATOM    549  CD ALYS A  58      -4.602  10.495  22.071  0.50 17.30           C  
ANISOU  549  CD ALYS A  58     3003   2039   1529   -143     90   -215       C  
ATOM    550  CD BLYS A  58      -4.383   8.792  23.448  0.50 23.29           C  
ANISOU  550  CD BLYS A  58     3380   3199   2269    -79    178    -53       C  
ATOM    551  CE ALYS A  58      -4.901  11.990  21.946  0.50 19.71           C  
ANISOU  551  CE ALYS A  58     3137   2365   1984    -74     61     -9       C  
ATOM    552  CE BLYS A  58      -4.622   8.013  24.713  0.50 23.47           C  
ANISOU  552  CE BLYS A  58     3273   3664   1979     24    272    -54       C  
ATOM    553  NZ ALYS A  58      -5.358  12.327  20.539  0.50 22.60           N  
ANISOU  553  NZ ALYS A  58     3782   2813   1991     88    194     79       N  
ATOM    554  NZ BLYS A  58      -4.757   8.948  25.862  0.50 25.11           N  
ANISOU  554  NZ BLYS A  58     3812   4064   1663    -24    305      8       N  
ATOM    555  N   ASN A  59      -4.549   9.292  18.350  1.00 15.05           N  
ANISOU  555  N   ASN A  59     2689   1755   1271   -204    688    179       N  
ATOM    556  CA  ASN A  59      -4.318   9.981  17.084  1.00 14.87           C  
ANISOU  556  CA  ASN A  59     2749   1609   1293   -188    695    -17       C  
ATOM    557  C   ASN A  59      -3.531  11.225  17.364  1.00 15.15           C  
ANISOU  557  C   ASN A  59     3054   1519   1181   -220    647    -62       C  
ATOM    558  O   ASN A  59      -3.755  11.918  18.363  1.00 17.57           O  
ANISOU  558  O   ASN A  59     3400   1750   1526   -311    964   -276       O  
ATOM    559  CB  ASN A  59      -5.638  10.367  16.456  1.00 15.99           C  
ANISOU  559  CB  ASN A  59     2998   1731   1344    -40    504    232       C  
ATOM    560  CG  ASN A  59      -6.538   9.185  16.121  1.00 18.22           C  
ANISOU  560  CG  ASN A  59     2607   2433   1882    -19    199     85       C  
ATOM    561  OD1 ASN A  59      -6.105   8.214  15.557  1.00 16.55           O  
ANISOU  561  OD1 ASN A  59     2744   1935   1609     -4    403    237       O  
ATOM    562  ND2 ASN A  59      -7.834   9.283  16.486  1.00 24.00           N  
ANISOU  562  ND2 ASN A  59     3035   3122   2962     41    561     11       N  
ATOM    563  N   THR A  60      -2.604  11.526  16.462  1.00 13.31           N  
ANISOU  563  N   THR A  60     2839   1429    788   -246    578     50       N  
ATOM    564  CA  THR A  60      -1.828  12.732  16.582  1.00 13.23           C  
ANISOU  564  CA  THR A  60     2852   1494    679   -184    507     -5       C  
ATOM    565  C   THR A  60      -1.709  13.365  15.210  1.00 11.87           C  
ANISOU  565  C   THR A  60     2572   1318    619   -145    402     34       C  
ATOM    566  O   THR A  60      -1.765  12.679  14.184  1.00 12.53           O  
ANISOU  566  O   THR A  60     2774   1333    651   -188    343    -29       O  
ATOM    567  CB  THR A  60      -0.385  12.458  17.148  1.00 13.70           C  
ANISOU  567  CB  THR A  60     2911   1586    707   -194    344     -3       C  
ATOM    568  OG1 THR A  60       0.369  11.624  16.281  1.00 14.42           O  
ANISOU  568  OG1 THR A  60     2838   1750    888    -56    242    130       O  
ATOM    569  CG2 THR A  60      -0.378  11.897  18.598  1.00 16.21           C  
ANISOU  569  CG2 THR A  60     3386   1872    898   -217    350    149       C  
ATOM    570  N   GLU A  61      -1.412  14.654  15.189  1.00 12.20           N  
ANISOU  570  N   GLU A  61     2752   1195    687   -217    353    -26       N  
ATOM    571  CA  GLU A  61      -1.105  15.359  13.933  1.00 12.38           C  
ANISOU  571  CA  GLU A  61     2558   1381    764   -158    285    -13       C  
ATOM    572  C   GLU A  61      -0.200  16.509  14.237  1.00 12.23           C  
ANISOU  572  C   GLU A  61     2663   1310    672   -114    275    -76       C  
ATOM    573  O   GLU A  61      -0.477  17.285  15.187  1.00 14.29           O  
ANISOU  573  O   GLU A  61     2978   1504    945   -143    573   -259       O  
ATOM    574  CB  GLU A  61      -2.395  15.811  13.274  1.00 15.10           C  
ANISOU  574  CB  GLU A  61     2769   1719   1249   -193    222    128       C  
ATOM    575  CG  GLU A  61      -2.246  16.495  11.993  1.00 18.90           C  
ANISOU  575  CG  GLU A  61     2861   2565   1754   -156     10    752       C  
ATOM    576  CD  GLU A  61      -3.544  17.039  11.453  1.00 25.91           C  
ANISOU  576  CD  GLU A  61     2978   3753   3112   -146     19   1062       C  
ATOM    577  OE1 GLU A  61      -3.485  18.099  10.840  1.00 29.53           O  
ANISOU  577  OE1 GLU A  61     3026   4271   3920   -407   -397   1361       O  
ATOM    578  OE2 GLU A  61      -4.604  16.426  11.649  1.00 31.17           O  
ANISOU  578  OE2 GLU A  61     3257   4654   3932   -416   -304    931       O  
ATOM    579  N   ILE A  62       0.928  16.600  13.536  1.00 10.31           N  
ANISOU  579  N   ILE A  62     2454   1181    281   -230    166    -36       N  
ATOM    580  CA  ILE A  62       1.799  17.727  13.612  1.00 10.26           C  
ANISOU  580  CA  ILE A  62     2451   1165    282   -151     74    -27       C  
ATOM    581  C   ILE A  62       1.997  18.325  12.226  1.00  9.90           C  
ANISOU  581  C   ILE A  62     2270   1230    260   -264     97     38       C  
ATOM    582  O   ILE A  62       2.100  17.589  11.240  1.00 11.35           O  
ANISOU  582  O   ILE A  62     2833   1215    264   -294     90    -96       O  
ATOM    583  CB  ILE A  62       3.154  17.362  14.245  1.00 10.78           C  
ANISOU  583  CB  ILE A  62     2557   1283    254   -278    -39    -24       C  
ATOM    584  CG1 ILE A  62       3.910  16.276  13.506  1.00 11.87           C  
ANISOU  584  CG1 ILE A  62     2459   1515    536   -218    -57     12       C  
ATOM    585  CG2 ILE A  62       2.949  16.932  15.734  1.00 13.36           C  
ANISOU  585  CG2 ILE A  62     2884   1899    290      6     91    238       C  
ATOM    586  CD1 ILE A  62       5.323  16.051  13.976  1.00 13.97           C  
ANISOU  586  CD1 ILE A  62     2434   1856   1018    -51   -282    -81       C  
ATOM    587  N   SER A  63       2.040  19.644  12.176  1.00  9.83           N  
ANISOU  587  N   SER A  63     2343   1128    262    -56    131     22       N  
ATOM    588  CA  SER A  63       2.407  20.388  10.962  1.00  9.10           C  
ANISOU  588  CA  SER A  63     2098   1105    253    -74     27     -4       C  
ATOM    589  C   SER A  63       3.513  21.336  11.294  1.00  9.52           C  
ANISOU  589  C   SER A  63     2117   1010    488    -31     39    -28       C  
ATOM    590  O   SER A  63       3.498  21.955  12.388  1.00 10.67           O  
ANISOU  590  O   SER A  63     2362   1167    524   -122    167   -233       O  
ATOM    591  CB  SER A  63       1.238  21.164  10.404  1.00 10.21           C  
ANISOU  591  CB  SER A  63     2234   1349    296     24     61    -74       C  
ATOM    592  OG  SER A  63       0.205  20.311   9.912  1.00 12.87           O  
ANISOU  592  OG  SER A  63     2493   1698    696    -46   -189    -47       O  
ATOM    593  N   PHE A  64       4.508  21.453  10.429  1.00  9.04           N  
ANISOU  593  N   PHE A  64     2110   1067    256   -165     13    -54       N  
ATOM    594  CA  PHE A  64       5.706  22.172  10.763  1.00  9.35           C  
ANISOU  594  CA  PHE A  64     2175   1123    255    -99    -13    -46       C  
ATOM    595  C   PHE A  64       6.435  22.606   9.496  1.00  8.77           C  
ANISOU  595  C   PHE A  64     2186    891    255   -111    -40     29       C  
ATOM    596  O   PHE A  64       6.206  22.058   8.402  1.00  9.65           O  
ANISOU  596  O   PHE A  64     2239   1161    263   -124   -107    -58       O  
ATOM    597  CB  PHE A  64       6.618  21.331  11.673  1.00  9.96           C  
ANISOU  597  CB  PHE A  64     2252   1178    354   -205    -35    118       C  
ATOM    598  CG  PHE A  64       6.968  20.016  11.051  1.00  9.44           C  
ANISOU  598  CG  PHE A  64     2185   1132    267    -23   -152    -10       C  
ATOM    599  CD1 PHE A  64       6.181  18.887  11.191  1.00  9.75           C  
ANISOU  599  CD1 PHE A  64     2156   1230    317    -65   -108     19       C  
ATOM    600  CD2 PHE A  64       8.100  19.879  10.295  1.00  9.85           C  
ANISOU  600  CD2 PHE A  64     2237   1108    397     21    -78    134       C  
ATOM    601  CE1 PHE A  64       6.459  17.712  10.590  1.00 11.29           C  
ANISOU  601  CE1 PHE A  64     2460   1373    457    -80   -315    -15       C  
ATOM    602  CE2 PHE A  64       8.388  18.670   9.691  1.00 11.32           C  
ANISOU  602  CE2 PHE A  64     2351   1663    287    125     16    220       C  
ATOM    603  CZ  PHE A  64       7.586  17.584   9.838  1.00 11.37           C  
ANISOU  603  CZ  PHE A  64     2603   1374    340      9   -231      4       C  
ATOM    604  N   ILE A  65       7.341  23.528   9.695  1.00  9.17           N  
ANISOU  604  N   ILE A  65     2159   1069    253   -124      3      4       N  
ATOM    605  CA  ILE A  65       8.299  23.992   8.711  1.00  9.29           C  
ANISOU  605  CA  ILE A  65     2183   1071    274    -40     20    -34       C  
ATOM    606  C   ILE A  65       9.702  23.561   9.171  1.00  9.02           C  
ANISOU  606  C   ILE A  65     2119   1025    281      5    -26    103       C  
ATOM    607  O   ILE A  65      10.010  23.665  10.369  1.00  9.48           O  
ANISOU  607  O   ILE A  65     2242   1048    311    -58    -63     -2       O  
ATOM    608  CB  ILE A  65       8.222  25.532   8.501  1.00  9.88           C  
ANISOU  608  CB  ILE A  65     2193   1023    536     -9     -6     -9       C  
ATOM    609  CG1 ILE A  65       6.829  25.836   7.940  1.00 11.43           C  
ANISOU  609  CG1 ILE A  65     2385   1268    690    -25   -102    216       C  
ATOM    610  CG2 ILE A  65       9.347  26.020   7.639  1.00 11.05           C  
ANISOU  610  CG2 ILE A  65     2510   1214    474     33    100    172       C  
ATOM    611  CD1 ILE A  65       6.511  27.361   7.880  1.00 15.94           C  
ANISOU  611  CD1 ILE A  65     2877   1413   1764    211   -107     56       C  
ATOM    612  N   LEU A  66      10.508  22.982   8.284  1.00  9.22           N  
ANISOU  612  N   LEU A  66     2184   1046    270     44    153     61       N  
ATOM    613  CA  LEU A  66      11.801  22.513   8.672  1.00  9.55           C  
ANISOU  613  CA  LEU A  66     2207   1057    364     18    136    131       C  
ATOM    614  C   LEU A  66      12.569  23.643   9.339  1.00  9.26           C  
ANISOU  614  C   LEU A  66     2156   1016    344     10     12     95       C  
ATOM    615  O   LEU A  66      12.643  24.766   8.831  1.00 10.37           O  
ANISOU  615  O   LEU A  66     2276   1071    594    -60    -28    164       O  
ATOM    616  CB  LEU A  66      12.574  21.950   7.467  1.00 10.34           C  
ANISOU  616  CB  LEU A  66     2199   1327    402     45    153     99       C  
ATOM    617  CG  LEU A  66      11.945  20.694   6.818  1.00 10.78           C  
ANISOU  617  CG  LEU A  66     2497   1201    398     16    -34   -222       C  
ATOM    618  CD1 LEU A  66      12.640  20.425   5.481  1.00 15.08           C  
ANISOU  618  CD1 LEU A  66     3338   1590    802    204    310   -277       C  
ATOM    619  CD2 LEU A  66      12.054  19.533   7.745  1.00 12.90           C  
ANISOU  619  CD2 LEU A  66     2865   1094    939   -125   -109     64       C  
ATOM    620  N   GLY A  67      13.235  23.300  10.426  1.00  9.74           N  
ANISOU  620  N   GLY A  67     2196   1103    402    -82    -76     87       N  
ATOM    621  CA  GLY A  67      14.079  24.209  11.158  1.00 10.16           C  
ANISOU  621  CA  GLY A  67     2156   1240    461    -17    -92     45       C  
ATOM    622  C   GLY A  67      13.396  25.151  12.123  1.00  9.61           C  
ANISOU  622  C   GLY A  67     2112   1088    448    -49   -123     25       C  
ATOM    623  O   GLY A  67      14.083  25.884  12.830  1.00 10.65           O  
ANISOU  623  O   GLY A  67     2161   1358    524   -122   -158   -101       O  
ATOM    624  N   GLN A  68      12.076  25.106  12.197  1.00  9.30           N  
ANISOU  624  N   GLN A  68     2148    961    424   -122   -122   -113       N  
ATOM    625  CA  GLN A  68      11.268  26.063  12.961  1.00  9.93           C  
ANISOU  625  CA  GLN A  68     2200   1004    568   -116   -156   -124       C  
ATOM    626  C   GLN A  68      10.540  25.370  14.128  1.00  9.96           C  
ANISOU  626  C   GLN A  68     2233    948    602     25    -83    -99       C  
ATOM    627  O   GLN A  68       9.657  24.515  13.910  1.00  9.80           O  
ANISOU  627  O   GLN A  68     2189   1027    507    -65    -25   -164       O  
ATOM    628  CB  GLN A  68      10.273  26.752  12.035  1.00 10.29           C  
ANISOU  628  CB  GLN A  68     2383    889    636    -74   -158    -59       C  
ATOM    629  CG  GLN A  68      11.017  27.465  10.925  1.00 13.30           C  
ANISOU  629  CG  GLN A  68     2811   1369    872   -190   -495    154       C  
ATOM    630  CD  GLN A  68      10.270  28.457  10.131  1.00 15.44           C  
ANISOU  630  CD  GLN A  68     3368   1306   1190    -75   -639    217       C  
ATOM    631  OE1 GLN A  68       9.091  28.743  10.407  1.00 18.75           O  
ANISOU  631  OE1 GLN A  68     3440   1372   2311    137  -1054    371       O  
ATOM    632  NE2 GLN A  68      10.966  29.016   9.150  1.00 16.72           N  
ANISOU  632  NE2 GLN A  68     4059   1303    991   -312   -563    406       N  
ATOM    633  N   GLU A  69      10.934  25.715  15.335  1.00  9.35           N  
ANISOU  633  N   GLU A  69     2215    980    357    -90   -101   -131       N  
ATOM    634  CA  GLU A  69      10.432  25.059  16.536  1.00 10.30           C  
ANISOU  634  CA  GLU A  69     2361   1050    502      6      6    179       C  
ATOM    635  C   GLU A  69       8.936  25.208  16.677  1.00  9.61           C  
ANISOU  635  C   GLU A  69     2370    987    295     14     68    -78       C  
ATOM    636  O   GLU A  69       8.388  26.273  16.321  1.00 10.57           O  
ANISOU  636  O   GLU A  69     2309    910    796     65    -66    -25       O  
ATOM    637  CB  GLU A  69      11.140  25.640  17.776  1.00 12.46           C  
ANISOU  637  CB  GLU A  69     2446   1786    502    -15    -61    173       C  
ATOM    638  CG  GLU A  69      10.837  25.032  19.080  1.00 15.74           C  
ANISOU  638  CG  GLU A  69     3382   1786    812   -299   -157    179       C  
ATOM    639  CD  GLU A  69      11.775  25.499  20.099  1.00 24.08           C  
ANISOU  639  CD  GLU A  69     4365   3400   1384   -169   -669    -68       C  
ATOM    640  OE1 GLU A  69      11.717  26.713  20.399  1.00 31.87           O  
ANISOU  640  OE1 GLU A  69     5206   4493   2409  -1043  -1098  -1144       O  
ATOM    641  OE2 GLU A  69      12.566  24.630  20.597  1.00 26.40           O  
ANISOU  641  OE2 GLU A  69     4681   3721   1625     48  -1029   -309       O  
ATOM    642  N   PHE A  70       8.296  24.185  17.219  1.00  9.52           N  
ANISOU  642  N   PHE A  70     2299    933    384    -29    102    -16       N  
ATOM    643  CA  PHE A  70       6.880  24.191  17.455  1.00  9.76           C  
ANISOU  643  CA  PHE A  70     2297    993    418     50    136    -50       C  
ATOM    644  C   PHE A  70       6.559  23.415  18.724  1.00  9.88           C  
ANISOU  644  C   PHE A  70     2341    918    491    147    248    -53       C  
ATOM    645  O   PHE A  70       7.344  22.627  19.215  1.00 10.78           O  
ANISOU  645  O   PHE A  70     2370   1263    460    365    133     46       O  
ATOM    646  CB  PHE A  70       6.123  23.598  16.254  1.00  9.57           C  
ANISOU  646  CB  PHE A  70     2173   1060    403    117     59    -37       C  
ATOM    647  CG  PHE A  70       6.475  22.174  15.908  1.00  9.86           C  
ANISOU  647  CG  PHE A  70     2317   1172    255    -38      0     46       C  
ATOM    648  CD1 PHE A  70       7.584  21.875  15.133  1.00  9.16           C  
ANISOU  648  CD1 PHE A  70     2127   1093    258     29     54    -57       C  
ATOM    649  CD2 PHE A  70       5.687  21.133  16.318  1.00 11.31           C  
ANISOU  649  CD2 PHE A  70     2371   1412    514    -29    277   -187       C  
ATOM    650  CE1 PHE A  70       7.870  20.594  14.765  1.00  9.82           C  
ANISOU  650  CE1 PHE A  70     2321   1140    269     36    -14    -52       C  
ATOM    651  CE2 PHE A  70       5.998  19.838  15.966  1.00 11.83           C  
ANISOU  651  CE2 PHE A  70     2626   1410    457   -207    195   -110       C  
ATOM    652  CZ  PHE A  70       7.079  19.553  15.210  1.00 10.49           C  
ANISOU  652  CZ  PHE A  70     2431   1268    287    137    -22   -184       C  
ATOM    653  N   ASP A  71       5.346  23.631  19.217  1.00 10.87           N  
ANISOU  653  N   ASP A  71     2315   1093    720    339    269    186       N  
ATOM    654  CA  ASP A  71       4.788  22.904  20.382  1.00 11.52           C  
ANISOU  654  CA  ASP A  71     2562   1369    444    204    430     74       C  
ATOM    655  C   ASP A  71       4.111  21.657  19.906  1.00 12.04           C  
ANISOU  655  C   ASP A  71     2577   1534    461     43    289     97       C  
ATOM    656  O   ASP A  71       3.398  21.623  18.860  1.00 14.01           O  
ANISOU  656  O   ASP A  71     2741   1625    954    167    139    337       O  
ATOM    657  CB  ASP A  71       3.702  23.741  21.037  1.00 12.78           C  
ANISOU  657  CB  ASP A  71     2598   1667    590    313    278     47       C  
ATOM    658  CG  ASP A  71       4.222  24.948  21.649  1.00 14.19           C  
ANISOU  658  CG  ASP A  71     2834   2108    450    226   -234   -306       C  
ATOM    659  OD1 ASP A  71       5.202  24.813  22.442  1.00 14.99           O  
ANISOU  659  OD1 ASP A  71     3161   1795    738    308   -223   -297       O  
ATOM    660  OD2 ASP A  71       3.634  26.040  21.445  1.00 14.87           O  
ANISOU  660  OD2 ASP A  71     2880   1854    916    259   -152    -15       O  
ATOM    661  N   GLU A  72       4.363  20.554  20.633  1.00 12.19           N  
ANISOU  661  N   GLU A  72     2577   1409    645    129    354    298       N  
ATOM    662  CA  GLU A  72       3.807  19.239  20.276  1.00 12.71           C  
ANISOU  662  CA  GLU A  72     2417   1504    906    107    250    322       C  
ATOM    663  C   GLU A  72       3.315  18.572  21.545  1.00 12.97           C  
ANISOU  663  C   GLU A  72     2573   1383    971    161    158    367       C  
ATOM    664  O   GLU A  72       3.995  18.597  22.566  1.00 14.84           O  
ANISOU  664  O   GLU A  72     2865   2017    754    -58    346    387       O  
ATOM    665  CB  GLU A  72       4.900  18.373  19.581  1.00 12.12           C  
ANISOU  665  CB  GLU A  72     2479   1425    698     94    321    254       C  
ATOM    666  CG  GLU A  72       4.498  16.939  19.298  1.00 12.61           C  
ANISOU  666  CG  GLU A  72     2695   1578    517    100     59    345       C  
ATOM    667  CD  GLU A  72       5.544  16.120  18.600  1.00 12.45           C  
ANISOU  667  CD  GLU A  72     2747   1548    436     85    239     91       C  
ATOM    668  OE1 GLU A  72       6.688  16.541  18.514  1.00 12.73           O  
ANISOU  668  OE1 GLU A  72     2549   1513    774    -30    144    -26       O  
ATOM    669  OE2 GLU A  72       5.210  14.990  18.154  1.00 14.37           O  
ANISOU  669  OE2 GLU A  72     2844   1593   1021      1    108    -18       O  
ATOM    670  N   VAL A  73       2.130  18.000  21.505  1.00 14.77           N  
ANISOU  670  N   VAL A  73     2617   1739   1256     57    289    583       N  
ATOM    671  CA  VAL A  73       1.686  17.151  22.613  1.00 15.39           C  
ANISOU  671  CA  VAL A  73     2474   1839   1532     67    384    539       C  
ATOM    672  C   VAL A  73       1.766  15.719  22.043  1.00 14.89           C  
ANISOU  672  C   VAL A  73     2514   1915   1228     64    241    534       C  
ATOM    673  O   VAL A  73       1.071  15.362  21.106  1.00 15.98           O  
ANISOU  673  O   VAL A  73     2751   1820   1497    -59    -70    534       O  
ATOM    674  CB  VAL A  73       0.277  17.522  23.083  1.00 16.57           C  
ANISOU  674  CB  VAL A  73     2703   2044   1548     64    610    432       C  
ATOM    675  CG1 VAL A  73      -0.170  16.563  24.194  1.00 18.94           C  
ANISOU  675  CG1 VAL A  73     2882   2429   1885    118    803    575       C  
ATOM    676  CG2 VAL A  73       0.221  18.957  23.605  1.00 18.86           C  
ANISOU  676  CG2 VAL A  73     2871   1944   2350    359    650    243       C  
ATOM    677  N   THR A  74       2.649  14.912  22.582  1.00 13.43           N  
ANISOU  677  N   THR A  74     2498   1994    608    230    216    398       N  
ATOM    678  CA  THR A  74       2.939  13.606  22.039  1.00 13.31           C  
ANISOU  678  CA  THR A  74     2541   1890    624     96    284    318       C  
ATOM    679  C   THR A  74       1.811  12.611  22.353  1.00 13.92           C  
ANISOU  679  C   THR A  74     2562   1961    765    132    189    373       C  
ATOM    680  O   THR A  74       0.969  12.889  23.172  1.00 14.74           O  
ANISOU  680  O   THR A  74     2828   1817    954    103    437    441       O  
ATOM    681  CB  THR A  74       4.263  13.045  22.561  1.00 12.09           C  
ANISOU  681  CB  THR A  74     2401   1867    325    111    303    222       C  
ATOM    682  OG1 THR A  74       4.122  12.814  23.969  1.00 13.17           O  
ANISOU  682  OG1 THR A  74     2627   1909    465    239    222    337       O  
ATOM    683  CG2 THR A  74       5.378  14.012  22.348  1.00 13.24           C  
ANISOU  683  CG2 THR A  74     2760   1648    620     52    278    233       C  
ATOM    684  N   ALA A  75       1.848  11.450  21.707  1.00 14.54           N  
ANISOU  684  N   ALA A  75     2682   2025    818    -46    311    333       N  
ATOM    685  CA  ALA A  75       0.801  10.416  21.869  1.00 14.45           C  
ANISOU  685  CA  ALA A  75     2667   1955    867    -74    126    279       C  
ATOM    686  C   ALA A  75       0.683  10.021  23.367  1.00 15.56           C  
ANISOU  686  C   ALA A  75     2695   2060   1157   -180    235    273       C  
ATOM    687  O   ALA A  75      -0.417   9.758  23.835  1.00 17.13           O  
ANISOU  687  O   ALA A  75     3020   2321   1165   -229    369    376       O  
ATOM    688  CB  ALA A  75       1.066   9.203  21.029  1.00 15.31           C  
ANISOU  688  CB  ALA A  75     2761   1958   1099   -160     78    169       C  
ATOM    689  N   ASP A  76       1.812   9.961  24.064  1.00 14.96           N  
ANISOU  689  N   ASP A  76     2867   1865    950    -94    257    436       N  
ATOM    690  CA  ASP A  76       1.854   9.635  25.520  1.00 15.20           C  
ANISOU  690  CA  ASP A  76     2905   2004    867   -220    221    426       C  
ATOM    691  C   ASP A  76       1.630  10.854  26.427  1.00 16.03           C  
ANISOU  691  C   ASP A  76     3145   2057    888   -190    425    448       C  
ATOM    692  O   ASP A  76       1.766  10.757  27.627  1.00 18.58           O  
ANISOU  692  O   ASP A  76     3650   2642    767    -19    360    492       O  
ATOM    693  CB  ASP A  76       3.180   8.927  25.824  1.00 15.92           C  
ANISOU  693  CB  ASP A  76     3059   1958   1029   -175    244    343       C  
ATOM    694  CG  ASP A  76       4.395   9.772  25.538  1.00 14.71           C  
ANISOU  694  CG  ASP A  76     2960   1830    798     -6   -219    268       C  
ATOM    695  OD1 ASP A  76       4.582  10.204  24.365  1.00 14.41           O  
ANISOU  695  OD1 ASP A  76     3149   1843    482    -92    -89    421       O  
ATOM    696  OD2 ASP A  76       5.152  10.002  26.490  1.00 14.80           O  
ANISOU  696  OD2 ASP A  76     3410   1618    595    -42     -2    336       O  
ATOM    697  N   ASP A  77       1.288  11.997  25.843  1.00 15.94           N  
ANISOU  697  N   ASP A  77     3142   2066    847   -122    626    338       N  
ATOM    698  CA  ASP A  77       0.864  13.190  26.577  1.00 17.86           C  
ANISOU  698  CA  ASP A  77     3232   2357   1198    -96    767    226       C  
ATOM    699  C   ASP A  77       2.000  14.008  27.174  1.00 17.68           C  
ANISOU  699  C   ASP A  77     3318   2283   1117    -36    644    159       C  
ATOM    700  O   ASP A  77       1.780  14.758  28.123  1.00 20.25           O  
ANISOU  700  O   ASP A  77     3525   2606   1563    -19    852   -322       O  
ATOM    701  CB  ASP A  77      -0.271  12.944  27.589  1.00 19.18           C  
ANISOU  701  CB  ASP A  77     3389   2486   1411   -175    937    273       C  
ATOM    702  CG  ASP A  77      -1.167  14.156  27.791  1.00 23.75           C  
ANISOU  702  CG  ASP A  77     3774   3211   2037    -54   1089    228       C  
ATOM    703  OD1 ASP A  77      -1.694  14.273  28.912  1.00 30.29           O  
ANISOU  703  OD1 ASP A  77     4566   4191   2752    252   1686   -157       O  
ATOM    704  OD2 ASP A  77      -1.393  14.961  26.859  1.00 29.24           O  
ANISOU  704  OD2 ASP A  77     4453   3955   2698    -35   1229    585       O  
ATOM    705  N   ARG A  78       3.192  13.946  26.604  1.00 15.25           N  
ANISOU  705  N   ARG A  78     3199   1853    743     53    590    329       N  
ATOM    706  CA  ARG A  78       4.213  14.896  26.948  1.00 14.82           C  
ANISOU  706  CA  ARG A  78     3165   1873    592     72    460    217       C  
ATOM    707  C   ARG A  78       3.967  16.176  26.178  1.00 14.42           C  
ANISOU  707  C   ARG A  78     3212   1782    485    152    472    215       C  
ATOM    708  O   ARG A  78       3.609  16.142  25.014  1.00 15.50           O  
ANISOU  708  O   ARG A  78     3487   1624    777    186    314    169       O  
ATOM    709  CB  ARG A  78       5.615  14.410  26.654  1.00 13.78           C  
ANISOU  709  CB  ARG A  78     3176   1521    538     55    319    266       C  
ATOM    710  CG  ARG A  78       6.119  13.312  27.534  1.00 13.52           C  
ANISOU  710  CG  ARG A  78     3091   1396    649     51    307    127       C  
ATOM    711  CD  ARG A  78       7.422  12.710  27.025  1.00 13.57           C  
ANISOU  711  CD  ARG A  78     3195   1554    407      4     10    168       C  
ATOM    712  NE  ARG A  78       7.150  11.854  25.887  1.00 12.99           N  
ANISOU  712  NE  ARG A  78     3058   1398    477    119   -121    158       N  
ATOM    713  CZ  ARG A  78       7.715  11.914  24.678  1.00 12.77           C  
ANISOU  713  CZ  ARG A  78     2650   1485    714    231    -66     45       C  
ATOM    714  NH1 ARG A  78       8.775  12.686  24.439  1.00 13.13           N  
ANISOU  714  NH1 ARG A  78     2869   1629    488    -73    -86    127       N  
ATOM    715  NH2 ARG A  78       7.286  11.086  23.732  1.00 12.38           N  
ANISOU  715  NH2 ARG A  78     2734   1314    654    -33   -121     21       N  
ATOM    716  N   LYS A  79       4.207  17.309  26.811  1.00 14.87           N  
ANISOU  716  N   LYS A  79     3327   1817    505    214    593    166       N  
ATOM    717  CA  LYS A  79       4.179  18.623  26.180  1.00 15.03           C  
ANISOU  717  CA  LYS A  79     3104   1772    833    355    521    138       C  
ATOM    718  C   LYS A  79       5.618  18.991  25.888  1.00 13.93           C  
ANISOU  718  C   LYS A  79     3028   1503    761    320    329    125       C  
ATOM    719  O   LYS A  79       6.417  19.269  26.792  1.00 16.10           O  
ANISOU  719  O   LYS A  79     3473   2222    421    309    523    -43       O  
ATOM    720  CB  LYS A  79       3.473  19.640  27.055  1.00 16.85           C  
ANISOU  720  CB  LYS A  79     3434   1944   1022    371    521    207       C  
ATOM    721  CG  LYS A  79       2.121  19.214  27.572  1.00 22.73           C  
ANISOU  721  CG  LYS A  79     3543   2705   2388    593    711    -29       C  
ATOM    722  CD  LYS A  79       1.041  18.792  26.626  1.00 28.57           C  
ANISOU  722  CD  LYS A  79     4101   3442   3311    393    573    -66       C  
ATOM    723  CE  LYS A  79      -0.304  18.536  27.357  1.00 31.76           C  
ANISOU  723  CE  LYS A  79     4325   3850   3892    289    550     49       C  
ATOM    724  NZ  LYS A  79      -0.289  17.377  28.302  1.00 33.42           N  
ANISOU  724  NZ  LYS A  79     4837   4131   3729    309    511    157       N  
ATOM    725  N   VAL A  80       5.991  18.955  24.608  1.00 12.54           N  
ANISOU  725  N   VAL A  80     2873   1538    353    243    242     46       N  
ATOM    726  CA  VAL A  80       7.372  19.084  24.226  1.00 11.96           C  
ANISOU  726  CA  VAL A  80     2807   1395    339    216    102     69       C  
ATOM    727  C   VAL A  80       7.545  20.244  23.221  1.00 11.33           C  
ANISOU  727  C   VAL A  80     2755   1254    294    301    181   -137       C  
ATOM    728  O   VAL A  80       6.575  20.684  22.593  1.00 12.65           O  
ANISOU  728  O   VAL A  80     2866   1377    561    313    311    132       O  
ATOM    729  CB  VAL A  80       7.909  17.746  23.579  1.00 12.12           C  
ANISOU  729  CB  VAL A  80     2855   1184    564    184    168     30       C  
ATOM    730  CG1 VAL A  80       7.606  16.543  24.482  1.00 13.28           C  
ANISOU  730  CG1 VAL A  80     3409   1184    450    237    110    236       C  
ATOM    731  CG2 VAL A  80       7.304  17.490  22.194  1.00 12.63           C  
ANISOU  731  CG2 VAL A  80     3213   1327    259     68    128    -14       C  
ATOM    732  N   LYS A  81       8.782  20.681  23.119  1.00 11.33           N  
ANISOU  732  N   LYS A  81     2840   1139    326    175     83    -24       N  
ATOM    733  CA  LYS A  81       9.180  21.655  22.095  1.00 11.42           C  
ANISOU  733  CA  LYS A  81     2920    969    450    269     48      5       C  
ATOM    734  C   LYS A  81       9.975  20.875  21.077  1.00 10.67           C  
ANISOU  734  C   LYS A  81     2651   1004    398    111     94   -128       C  
ATOM    735  O   LYS A  81      10.993  20.274  21.420  1.00 11.39           O  
ANISOU  735  O   LYS A  81     2719   1295    310    247   -143   -125       O  
ATOM    736  CB  LYS A  81      10.049  22.733  22.728  1.00 13.42           C  
ANISOU  736  CB  LYS A  81     3275   1149    674     46    221     14       C  
ATOM    737  CG  LYS A  81       9.405  23.579  23.735  1.00 19.38           C  
ANISOU  737  CG  LYS A  81     3782   1992   1588    162    -25   -552       C  
ATOM    738  CD  LYS A  81       8.374  24.486  23.195  1.00 22.36           C  
ANISOU  738  CD  LYS A  81     4020   2569   1907    180      0   -355       C  
ATOM    739  CE  LYS A  81       7.785  25.347  24.308  1.00 25.14           C  
ANISOU  739  CE  LYS A  81     4151   2897   2505    187   -452   -602       C  
ATOM    740  NZ  LYS A  81       6.954  26.479  23.827  1.00 26.85           N  
ANISOU  740  NZ  LYS A  81     4905   2900   2394    135  -1090   -524       N  
ATOM    741  N   SER A  82       9.515  20.934  19.831  1.00 10.31           N  
ANISOU  741  N   SER A  82     2580   1082    255    179     68     14       N  
ATOM    742  CA  SER A  82      10.050  20.090  18.771  1.00  9.26           C  
ANISOU  742  CA  SER A  82     2357    890    269     64     62    -22       C  
ATOM    743  C   SER A  82      10.652  20.923  17.654  1.00  9.38           C  
ANISOU  743  C   SER A  82     2339    955    267     67    -44     91       C  
ATOM    744  O   SER A  82      10.143  21.974  17.296  1.00  9.80           O  
ANISOU  744  O   SER A  82     2376    982    366    168    115     98       O  
ATOM    745  CB  SER A  82       8.938  19.256  18.206  1.00 10.23           C  
ANISOU  745  CB  SER A  82     2420   1193    271     20    127     62       C  
ATOM    746  OG  SER A  82       8.568  18.274  19.144  1.00 11.88           O  
ANISOU  746  OG  SER A  82     2710   1088    715     45    251    287       O  
ATOM    747  N   THR A  83      11.759  20.406  17.086  1.00  8.94           N  
ANISOU  747  N   THR A  83     2163    972    259    145    -10     64       N  
ATOM    748  CA  THR A  83      12.327  20.979  15.898  1.00  9.30           C  
ANISOU  748  CA  THR A  83     2328    940    264     10     89     69       C  
ATOM    749  C   THR A  83      12.663  19.835  14.970  1.00  9.54           C  
ANISOU  749  C   THR A  83     2377    990    257     83    -28     51       C  
ATOM    750  O   THR A  83      13.293  18.863  15.371  1.00 10.36           O  
ANISOU  750  O   THR A  83     2646   1032    257    258    -26    -55       O  
ATOM    751  CB  THR A  83      13.608  21.776  16.209  1.00 10.75           C  
ANISOU  751  CB  THR A  83     2254   1041    789    162    143     32       C  
ATOM    752  OG1 THR A  83      13.353  22.700  17.260  1.00 12.44           O  
ANISOU  752  OG1 THR A  83     2706   1222    795   -101   -165   -229       O  
ATOM    753  CG2 THR A  83      14.057  22.519  14.964  1.00 13.66           C  
ANISOU  753  CG2 THR A  83     2745   1225   1218   -125    199    132       C  
ATOM    754  N   ILE A  84      12.212  19.951  13.697  1.00  9.62           N  
ANISOU  754  N   ILE A  84     2383   1014    258    115    -60     49       N  
ATOM    755  CA  ILE A  84      12.430  18.928  12.698  1.00  9.16           C  
ANISOU  755  CA  ILE A  84     2270    951    257    101     92     -3       C  
ATOM    756  C   ILE A  84      13.234  19.533  11.591  1.00  9.49           C  
ANISOU  756  C   ILE A  84     2456    885    261      1     70     60       C  
ATOM    757  O   ILE A  84      12.904  20.594  11.051  1.00 10.10           O  
ANISOU  757  O   ILE A  84     2594    969    273     87    110    106       O  
ATOM    758  CB  ILE A  84      11.116  18.310  12.197  1.00  9.51           C  
ANISOU  758  CB  ILE A  84     2334    980    298    182     28    180       C  
ATOM    759  CG1 ILE A  84      10.353  17.720  13.403  1.00  9.59           C  
ANISOU  759  CG1 ILE A  84     2217   1139    285     75    -16    168       C  
ATOM    760  CG2 ILE A  84      11.420  17.229  11.154  1.00 10.98           C  
ANISOU  760  CG2 ILE A  84     2608   1087    474     20    215   -209       C  
ATOM    761  CD1 ILE A  84       9.035  17.163  13.072  1.00 10.64           C  
ANISOU  761  CD1 ILE A  84     2389   1274    380    100     90    109       C  
ATOM    762  N   THR A  85      14.329  18.854  11.215  1.00  9.77           N  
ANISOU  762  N   THR A  85     2377   1055    278    115    225     43       N  
ATOM    763  CA  THR A  85      15.189  19.262  10.127  1.00 10.49           C  
ANISOU  763  CA  THR A  85     2444   1081    457     76    179    -56       C  
ATOM    764  C   THR A  85      15.436  18.086   9.228  1.00 10.82           C  
ANISOU  764  C   THR A  85     2659   1103    346    -74    313    126       C  
ATOM    765  O   THR A  85      15.122  16.948   9.536  1.00 11.57           O  
ANISOU  765  O   THR A  85     2961   1124    312     80    382     76       O  
ATOM    766  CB  THR A  85      16.516  19.806  10.668  1.00 11.90           C  
ANISOU  766  CB  THR A  85     2349   1282    890     67    190     68       C  
ATOM    767  OG1 THR A  85      17.107  18.788  11.482  1.00 14.64           O  
ANISOU  767  OG1 THR A  85     2938   1672    949    247   -108   -146       O  
ATOM    768  CG2 THR A  85      16.310  21.130  11.430  1.00 13.66           C  
ANISOU  768  CG2 THR A  85     2763   1377   1048    -13     34   -533       C  
ATOM    769  N   LEU A  86      15.995  18.354   8.051  1.00 12.86           N  
ANISOU  769  N   LEU A  86     3125   1246    513   -154    504    -70       N  
ATOM    770  CA  LEU A  86      16.601  17.316   7.169  1.00 15.17           C  
ANISOU  770  CA  LEU A  86     3254   1450   1057   -287    491   -136       C  
ATOM    771  C   LEU A  86      18.143  17.221   7.410  1.00 17.41           C  
ANISOU  771  C   LEU A  86     3134   1749   1730   -343    742   -138       C  
ATOM    772  O   LEU A  86      18.871  18.272   7.516  1.00 20.25           O  
ANISOU  772  O   LEU A  86     3281   2086   2325   -447    440   -343       O  
ATOM    773  CB  LEU A  86      16.293  17.555   5.747  1.00 16.96           C  
ANISOU  773  CB  LEU A  86     3751   1829    862   -284    625     65       C  
ATOM    774  CG  LEU A  86      14.918  17.177   5.324  1.00 18.07           C  
ANISOU  774  CG  LEU A  86     3407   2113   1346     44    451    552       C  
ATOM    775  CD1 LEU A  86      14.660  17.746   3.919  1.00 19.24           C  
ANISOU  775  CD1 LEU A  86     4077   2199   1032    610    821    508       C  
ATOM    776  CD2 LEU A  86      14.770  15.554   5.177  1.00 16.85           C  
ANISOU  776  CD2 LEU A  86     3522   1860   1017   -150    101    118       C  
ATOM    777  N   ASP A  87      18.658  16.021   7.521  1.00 16.96           N  
ANISOU  777  N   ASP A  87     3047   1974   1420   -378    612   -589       N  
ATOM    778  CA  ASP A  87      20.109  15.792   7.622  1.00 18.78           C  
ANISOU  778  CA  ASP A  87     2972   2385   1778   -416    424   -433       C  
ATOM    779  C   ASP A  87      20.312  14.835   6.510  1.00 15.93           C  
ANISOU  779  C   ASP A  87     2729   2161   1161   -293    409   -390       C  
ATOM    780  O   ASP A  87      20.025  13.679   6.690  1.00 16.93           O  
ANISOU  780  O   ASP A  87     2936   2199   1297   -459    338   -176       O  
ATOM    781  CB  ASP A  87      20.498  15.183   9.009  1.00 21.62           C  
ANISOU  781  CB  ASP A  87     3135   2985   2093   -424    324   -312       C  
ATOM    782  CG  ASP A  87      21.985  14.785   9.120  1.00 26.45           C  
ANISOU  782  CG  ASP A  87     3615   3759   2675   -205    134     16       C  
ATOM    783  OD1 ASP A  87      22.798  15.121   8.236  1.00 31.83           O  
ANISOU  783  OD1 ASP A  87     3504   5031   3557   -408    130    116       O  
ATOM    784  OD2 ASP A  87      22.354  14.104  10.110  1.00 34.08           O  
ANISOU  784  OD2 ASP A  87     4305   4996   3648     32   -219    154       O  
ATOM    785  N  AGLY A  88      20.885  15.261   5.390  0.50 15.92           N  
ANISOU  785  N  AGLY A  88     2675   1893   1481   -285    419   -251       N  
ATOM    786  N  BGLY A  88      20.750  15.332   5.351  0.50 15.56           N  
ANISOU  786  N  BGLY A  88     2706   1866   1340   -356    490   -270       N  
ATOM    787  CA AGLY A  88      21.243  14.306   4.386  0.50 15.05           C  
ANISOU  787  CA AGLY A  88     2533   1956   1229   -141    320   -233       C  
ATOM    788  CA BGLY A  88      20.770  14.540   4.168  0.50 14.37           C  
ANISOU  788  CA BGLY A  88     2548   1891   1020   -225    597   -269       C  
ATOM    789  C  AGLY A  88      20.099  13.371   4.053  0.50 13.93           C  
ANISOU  789  C  AGLY A  88     2456   1899    937    -42    272   -197       C  
ATOM    790  C  BGLY A  88      19.362  14.193   3.813  0.50 13.72           C  
ANISOU  790  C  BGLY A  88     2544   1947    721   -159    535   -337       C  
ATOM    791  O  AGLY A  88      20.281  12.171   4.045  0.50 14.78           O  
ANISOU  791  O  AGLY A  88     2679   1847   1089    112    208   -312       O  
ATOM    792  O  BGLY A  88      18.515  15.057   3.727  0.50 14.73           O  
ANISOU  792  O  BGLY A  88     2874   1910    811   -129    472   -160       O  
ATOM    793  N  AGLY A  89      18.909  13.911   3.830  0.50 13.36           N  
ANISOU  793  N  AGLY A  89     2517   1899    659    133    361   -100       N  
ATOM    794  N  BGLY A  89      19.111  12.897   3.673  0.50 12.92           N  
ANISOU  794  N  BGLY A  89     2418   1948    543   -286    603   -274       N  
ATOM    795  CA AGLY A  89      17.786  13.110   3.450  0.50 12.64           C  
ANISOU  795  CA AGLY A  89     2616   1823    364     75    329   -159       C  
ATOM    796  CA BGLY A  89      17.805  12.342   3.417  0.50 13.66           C  
ANISOU  796  CA BGLY A  89     2604   1968    615   -237    315   -493       C  
ATOM    797  C  AGLY A  89      17.002  12.388   4.580  0.50 13.03           C  
ANISOU  797  C  AGLY A  89     2618   1883    448    -76    197   -110       C  
ATOM    798  C  BGLY A  89      17.115  11.873   4.672  0.50 13.01           C  
ANISOU  798  C  BGLY A  89     2505   1780    657   -196    291   -522       C  
ATOM    799  O  AGLY A  89      15.918  11.877   4.306  0.50 12.76           O  
ANISOU  799  O  AGLY A  89     2723   1811    311   -177    -19    -57       O  
ATOM    800  O  BGLY A  89      16.194  11.059   4.605  0.50 14.06           O  
ANISOU  800  O  BGLY A  89     2626   1756    959   -106     93   -850       O  
ATOM    801  N   VAL A  90      17.485  12.388   5.845  1.00 12.85           N  
ANISOU  801  N   VAL A  90     2588   1887    407   -305    314   -274       N  
ATOM    802  CA  VAL A  90      16.844  11.877   7.041  1.00 11.91           C  
ANISOU  802  CA  VAL A  90     2527   1494    503   -199    360   -257       C  
ATOM    803  C   VAL A  90      16.122  13.008   7.730  1.00 10.20           C  
ANISOU  803  C   VAL A  90     2335   1260    278   -129      2   -158       C  
ATOM    804  O   VAL A  90      16.681  14.078   7.957  1.00 11.49           O  
ANISOU  804  O   VAL A  90     2687   1293    386   -241    211    -57       O  
ATOM    805  CB  VAL A  90      17.905  11.318   7.985  1.00 13.19           C  
ANISOU  805  CB  VAL A  90     2715   1481    814    -51    457   -119       C  
ATOM    806  CG1 VAL A  90      17.294  10.815   9.299  1.00 12.81           C  
ANISOU  806  CG1 VAL A  90     2504   1597    765    185    200    126       C  
ATOM    807  CG2 VAL A  90      18.730  10.204   7.371  1.00 16.28           C  
ANISOU  807  CG2 VAL A  90     2897   1632   1655    129    612   -274       C  
ATOM    808  N   LEU A  91      14.845  12.790   8.036  1.00 10.13           N  
ANISOU  808  N   LEU A  91     2329   1252    265   -226     72   -106       N  
ATOM    809  CA  LEU A  91      14.115  13.753   8.850  1.00 10.08           C  
ANISOU  809  CA  LEU A  91     2431   1105    292    -10     94    173       C  
ATOM    810  C   LEU A  91      14.498  13.524  10.301  1.00  9.40           C  
ANISOU  810  C   LEU A  91     2351    928    293    138    230    114       C  
ATOM    811  O   LEU A  91      14.336  12.412  10.813  1.00 10.22           O  
ANISOU  811  O   LEU A  91     2645    969    267    122    183      4       O  
ATOM    812  CB  LEU A  91      12.601  13.570   8.708  1.00 12.48           C  
ANISOU  812  CB  LEU A  91     2736   1381    624   -147     74    284       C  
ATOM    813  CG  LEU A  91      11.964  14.174   7.449  1.00 13.17           C  
ANISOU  813  CG  LEU A  91     2834   1722    446     29     41    -64       C  
ATOM    814  CD1 LEU A  91      10.578  13.621   7.325  1.00 16.74           C  
ANISOU  814  CD1 LEU A  91     2881   2401   1077     -1   -158    -26       C  
ATOM    815  CD2 LEU A  91      11.948  15.694   7.605  1.00 13.25           C  
ANISOU  815  CD2 LEU A  91     3004   1071    957    227     18    255       C  
ATOM    816  N   VAL A  92      15.014  14.556  10.946  1.00  9.66           N  
ANISOU  816  N   VAL A  92     2405   1005    258    149     75     48       N  
ATOM    817  CA  VAL A  92      15.483  14.459  12.351  1.00  9.76           C  
ANISOU  817  CA  VAL A  92     2419   1032    254    261    -20     23       C  
ATOM    818  C   VAL A  92      14.595  15.313  13.206  1.00  9.83           C  
ANISOU  818  C   VAL A  92     2528    921    285    220     11     34       C  
ATOM    819  O   VAL A  92      14.541  16.539  13.011  1.00 10.95           O  
ANISOU  819  O   VAL A  92     2792   1015    351    171    220     48       O  
ATOM    820  CB  VAL A  92      16.955  14.929  12.419  1.00 11.03           C  
ANISOU  820  CB  VAL A  92     2488   1343    360    227      4   -120       C  
ATOM    821  CG1 VAL A  92      17.476  14.826  13.868  1.00 13.01           C  
ANISOU  821  CG1 VAL A  92     2786   1735    420    180    -60    -44       C  
ATOM    822  CG2 VAL A  92      17.876  14.098  11.497  1.00 13.47           C  
ANISOU  822  CG2 VAL A  92     2646   1753    719     68     68   -237       C  
ATOM    823  N   HIS A  93      13.929  14.671  14.149  1.00  9.82           N  
ANISOU  823  N   HIS A  93     2567    868    294    255    185    116       N  
ATOM    824  CA  HIS A  93      12.891  15.311  14.989  1.00  9.58           C  
ANISOU  824  CA  HIS A  93     2393    947    298    360    124    175       C  
ATOM    825  C   HIS A  93      13.346  15.258  16.416  1.00  9.68           C  
ANISOU  825  C   HIS A  93     2493    919    266    338    -23     85       C  
ATOM    826  O   HIS A  93      13.465  14.185  17.007  1.00 10.49           O  
ANISOU  826  O   HIS A  93     2784    939    259    211    -89     40       O  
ATOM    827  CB  HIS A  93      11.628  14.553  14.802  1.00 10.07           C  
ANISOU  827  CB  HIS A  93     2390   1161    272    484     98    132       C  
ATOM    828  CG  HIS A  93      10.444  14.969  15.564  1.00 10.27           C  
ANISOU  828  CG  HIS A  93     2296   1214    390    385      4    251       C  
ATOM    829  ND1 HIS A  93       9.252  14.318  15.363  1.00 13.49           N  
ANISOU  829  ND1 HIS A  93     2471   1830    823    479    254    561       N  
ATOM    830  CD2 HIS A  93      10.221  15.937  16.510  1.00 11.87           C  
ANISOU  830  CD2 HIS A  93     2663   1340    505    516    120    367       C  
ATOM    831  CE1 HIS A  93       8.350  14.848  16.162  1.00 13.77           C  
ANISOU  831  CE1 HIS A  93     2271   2135    825    417    484    849       C  
ATOM    832  NE2 HIS A  93       8.898  15.854  16.843  1.00 14.78           N  
ANISOU  832  NE2 HIS A  93     2844   1929    840    492    414    716       N  
ATOM    833  N   VAL A  94      13.710  16.410  16.988  1.00  9.83           N  
ANISOU  833  N   VAL A  94     2547    904    284    229    -22    116       N  
ATOM    834  CA  VAL A  94      14.165  16.495  18.374  1.00  9.97           C  
ANISOU  834  CA  VAL A  94     2385   1126    274    227    -30    113       C  
ATOM    835  C   VAL A  94      13.052  17.057  19.201  1.00  9.51           C  
ANISOU  835  C   VAL A  94     2427    904    281    118    -63    127       C  
ATOM    836  O   VAL A  94      12.511  18.106  18.892  1.00 11.10           O  
ANISOU  836  O   VAL A  94     2791   1115    309    419    185    214       O  
ATOM    837  CB  VAL A  94      15.460  17.335  18.492  1.00 11.50           C  
ANISOU  837  CB  VAL A  94     2489   1393    488    248     -3     37       C  
ATOM    838  CG1 VAL A  94      15.948  17.367  19.905  1.00 15.55           C  
ANISOU  838  CG1 VAL A  94     2912   2191    802   -123   -406     -1       C  
ATOM    839  CG2 VAL A  94      16.522  16.855  17.524  1.00 16.17           C  
ANISOU  839  CG2 VAL A  94     3008   2187    948    469    203    131       C  
ATOM    840  N   GLN A  95      12.762  16.372  20.309  1.00  9.78           N  
ANISOU  840  N   GLN A  95     2535    913    265    153    -35     84       N  
ATOM    841  CA  GLN A  95      11.742  16.791  21.294  1.00 10.47           C  
ANISOU  841  CA  GLN A  95     2598   1123    256    148    -29     43       C  
ATOM    842  C   GLN A  95      12.420  17.121  22.609  1.00 10.42           C  
ANISOU  842  C   GLN A  95     2735    950    273    148   -199     44       C  
ATOM    843  O   GLN A  95      13.173  16.295  23.145  1.00 11.59           O  
ANISOU  843  O   GLN A  95     2943   1193    268    214   -114    -50       O  
ATOM    844  CB  GLN A  95      10.775  15.656  21.546  1.00 10.58           C  
ANISOU  844  CB  GLN A  95     2574   1185    260    170     -1     82       C  
ATOM    845  CG  GLN A  95       9.942  15.272  20.340  1.00 10.51           C  
ANISOU  845  CG  GLN A  95     2694   1042    256     94    -28    -49       C  
ATOM    846  CD  GLN A  95       8.994  14.100  20.537  1.00 10.33           C  
ANISOU  846  CD  GLN A  95     2399   1097    428    145    159     15       C  
ATOM    847  OE1 GLN A  95       7.956  13.979  19.793  1.00 13.11           O  
ANISOU  847  OE1 GLN A  95     2524   1729    726     62    -15    143       O  
ATOM    848  NE2 GLN A  95       9.313  13.218  21.425  1.00 10.30           N  
ANISOU  848  NE2 GLN A  95     2550   1076    284     -6    -80    152       N  
ATOM    849  N   LYS A  96      12.129  18.263  23.160  1.00 10.91           N  
ANISOU  849  N   LYS A  96     2844   1033    268    111   -195    -10       N  
ATOM    850  CA  LYS A  96      12.683  18.747  24.440  1.00 12.23           C  
ANISOU  850  CA  LYS A  96     2951   1323    374    168   -148   -120       C  
ATOM    851  C   LYS A  96      11.547  18.967  25.438  1.00 12.13           C  
ANISOU  851  C   LYS A  96     3038   1286    285    161    -86    -87       C  
ATOM    852  O   LYS A  96      10.559  19.630  25.130  1.00 13.18           O  
ANISOU  852  O   LYS A  96     3392   1359    254    280    -23    -41       O  
ATOM    853  CB  LYS A  96      13.368  20.080  24.241  1.00 13.53           C  
ANISOU  853  CB  LYS A  96     2815   1738    588    -16   -188   -113       C  
ATOM    854  CG  LYS A  96      14.486  20.154  23.275  1.00 15.82           C  
ANISOU  854  CG  LYS A  96     3255   1819    936     43   -147   -125       C  
ATOM    855  CD  LYS A  96      15.654  19.275  23.580  1.00 17.26           C  
ANISOU  855  CD  LYS A  96     3263   1928   1365    -27   -195    -68       C  
ATOM    856  CE  LYS A  96      16.811  19.555  22.670  1.00 17.81           C  
ANISOU  856  CE  LYS A  96     2944   1969   1851   -331   -232   -263       C  
ATOM    857  NZ  LYS A  96      17.987  18.698  22.917  1.00 18.81           N  
ANISOU  857  NZ  LYS A  96     3027   2029   2089   -242     -7    -21       N  
ATOM    858  N   TRP A  97      11.729  18.452  26.651  1.00 13.11           N  
ANISOU  858  N   TRP A  97     3323   1391    265    290    -45    -70       N  
ATOM    859  CA  TRP A  97      10.763  18.681  27.722  1.00 14.56           C  
ANISOU  859  CA  TRP A  97     3467   1741    322    297    -36   -181       C  
ATOM    860  C   TRP A  97      11.409  18.362  29.051  1.00 15.62           C  
ANISOU  860  C   TRP A  97     3777   1875    280    284   -150   -195       C  
ATOM    861  O   TRP A  97      12.221  17.438  29.136  1.00 16.75           O  
ANISOU  861  O   TRP A  97     4067   2023    274    451   -250   -124       O  
ATOM    862  CB  TRP A  97       9.472  17.836  27.554  1.00 14.80           C  
ANISOU  862  CB  TRP A  97     3454   1772    397    280    142    -67       C  
ATOM    863  CG  TRP A  97       9.661  16.387  27.939  1.00 14.34           C  
ANISOU  863  CG  TRP A  97     3378   1524    547    150    372   -118       C  
ATOM    864  CD1 TRP A  97       9.152  15.778  29.026  1.00 16.04           C  
ANISOU  864  CD1 TRP A  97     3706   1828    558    263    612     20       C  
ATOM    865  CD2 TRP A  97      10.432  15.377  27.246  1.00 13.52           C  
ANISOU  865  CD2 TRP A  97     3209   1527    401     97     98    -64       C  
ATOM    866  NE1 TRP A  97       9.541  14.479  29.091  1.00 15.14           N  
ANISOU  866  NE1 TRP A  97     3657   1724    372    200    366     24       N  
ATOM    867  CE2 TRP A  97      10.332  14.205  28.009  1.00 13.80           C  
ANISOU  867  CE2 TRP A  97     3338   1376    527    -86    175     44       C  
ATOM    868  CE3 TRP A  97      11.191  15.347  26.076  1.00 13.55           C  
ANISOU  868  CE3 TRP A  97     3414   1350    384    -60    144   -126       C  
ATOM    869  CZ2 TRP A  97      10.982  13.044  27.666  1.00 13.99           C  
ANISOU  869  CZ2 TRP A  97     3213   1415    688   -153    -18    164       C  
ATOM    870  CZ3 TRP A  97      11.804  14.185  25.736  1.00 13.42           C  
ANISOU  870  CZ3 TRP A  97     3114   1533    450   -176     96   -117       C  
ATOM    871  CH2 TRP A  97      11.715  13.048  26.536  1.00 14.06           C  
ANISOU  871  CH2 TRP A  97     3203   1408    729   -109    148   -344       C  
ATOM    872  N   ASP A  98      11.101  19.161  30.055  1.00 17.52           N  
ANISOU  872  N   ASP A  98     4167   2126    362    288    -75   -327       N  
ATOM    873  CA  ASP A  98      11.525  18.836  31.427  1.00 19.29           C  
ANISOU  873  CA  ASP A  98     4374   2505    450    191   -204   -263       C  
ATOM    874  C   ASP A  98      13.024  18.581  31.533  1.00 19.43           C  
ANISOU  874  C   ASP A  98     4417   2498    467    140   -322   -486       C  
ATOM    875  O   ASP A  98      13.461  17.702  32.307  1.00 22.28           O  
ANISOU  875  O   ASP A  98     4929   2959    578    368   -374   -271       O  
ATOM    876  CB  ASP A  98      10.788  17.591  31.928  1.00 21.97           C  
ANISOU  876  CB  ASP A  98     4716   3010    619     42   -217     59       C  
ATOM    877  N   GLY A  99      13.812  19.314  30.764  1.00 19.49           N  
ANISOU  877  N   GLY A  99     4234   2248    920    168   -432   -522       N  
ATOM    878  CA  GLY A  99      15.246  19.144  30.743  1.00 19.44           C  
ANISOU  878  CA  GLY A  99     4031   2186   1166    -15   -630   -637       C  
ATOM    879  C   GLY A  99      15.768  17.870  30.068  1.00 19.18           C  
ANISOU  879  C   GLY A  99     3883   2237   1166     41   -668   -544       C  
ATOM    880  O   GLY A  99      16.986  17.598  30.095  1.00 22.62           O  
ANISOU  880  O   GLY A  99     3981   2827   1786      6   -943   -741       O  
ATOM    881  N   LYS A 100      14.893  17.116  29.398  1.00 16.96           N  
ANISOU  881  N   LYS A 100     3785   2007    651      0   -651   -373       N  
ATOM    882  CA  LYS A 100      15.170  15.873  28.689  1.00 15.51           C  
ANISOU  882  CA  LYS A 100     3437   1911    543     84   -509   -252       C  
ATOM    883  C   LYS A 100      15.098  16.122  27.192  1.00 13.62           C  
ANISOU  883  C   LYS A 100     3243   1512    419    126   -629    -43       C  
ATOM    884  O   LYS A 100      14.536  17.105  26.740  1.00 14.11           O  
ANISOU  884  O   LYS A 100     3489   1441    431    142   -490    -84       O  
ATOM    885  CB  LYS A 100      14.121  14.852  29.089  1.00 14.92           C  
ANISOU  885  CB  LYS A 100     3577   1781    309    202   -248    -76       C  
ATOM    886  CG  LYS A 100      14.097  14.520  30.641  1.00 19.78           C  
ANISOU  886  CG  LYS A 100     4042   2690    785     22   -313     70       C  
ATOM    887  CD  LYS A 100      12.877  13.656  31.001  1.00 22.24           C  
ANISOU  887  CD  LYS A 100     4151   3198   1100    135    127    399       C  
ATOM    888  CE  LYS A 100      12.645  13.366  32.464  1.00 26.13           C  
ANISOU  888  CE  LYS A 100     4601   3567   1760      3    257    464       C  
ATOM    889  NZ  LYS A 100      11.306  12.728  32.573  1.00 32.12           N  
ANISOU  889  NZ  LYS A 100     4821   4786   2597     10    116    716       N  
ATOM    890  N   SER A 101      15.602  15.152  26.436  1.00 12.96           N  
ANISOU  890  N   SER A 101     3234   1198    492     44   -507    -92       N  
ATOM    891  CA  SER A 101      15.579  15.254  24.970  1.00 12.11           C  
ANISOU  891  CA  SER A 101     2864   1340    394     -3   -350     -5       C  
ATOM    892  C   SER A 101      15.509  13.858  24.412  1.00 11.63           C  
ANISOU  892  C   SER A 101     2864   1231    323     46   -309    176       C  
ATOM    893  O   SER A 101      16.111  12.936  24.933  1.00 12.94           O  
ANISOU  893  O   SER A 101     3044   1355    515    119   -486     36       O  
ATOM    894  CB  SER A 101      16.858  15.897  24.513  1.00 13.83           C  
ANISOU  894  CB  SER A 101     3086   1484    684   -176   -287     28       C  
ATOM    895  OG  SER A 101      16.884  16.098  23.152  1.00 15.40           O  
ANISOU  895  OG  SER A 101     3448   1433    968   -278   -174     26       O  
ATOM    896  N   THR A 102      14.758  13.686  23.323  1.00 10.26           N  
ANISOU  896  N   THR A 102     2503   1096    296     24   -291     52       N  
ATOM    897  CA  THR A 102      14.732  12.453  22.544  1.00  9.56           C  
ANISOU  897  CA  THR A 102     2320   1038    271     95   -170     50       C  
ATOM    898  C   THR A 102      14.722  12.839  21.085  1.00  9.54           C  
ANISOU  898  C   THR A 102     2233   1059    331    168   -142     20       C  
ATOM    899  O   THR A 102      14.230  13.899  20.713  1.00 10.45           O  
ANISOU  899  O   THR A 102     2642   1063    263    206    -70     73       O  
ATOM    900  CB  THR A 102      13.528  11.601  22.914  1.00 10.29           C  
ANISOU  900  CB  THR A 102     2501   1133    272    -31   -157    -85       C  
ATOM    901  OG1 THR A 102      13.615  10.341  22.288  1.00 11.55           O  
ANISOU  901  OG1 THR A 102     2650   1066    672    -51    -53     21       O  
ATOM    902  CG2 THR A 102      12.213  12.195  22.604  1.00 11.61           C  
ANISOU  902  CG2 THR A 102     2771   1192    446    105   -122     24       C  
ATOM    903  N   THR A 103      15.314  11.983  20.244  1.00 10.04           N  
ANISOU  903  N   THR A 103     2516    942    354    259   -120     85       N  
ATOM    904  CA  THR A 103      15.401  12.212  18.803  1.00 10.19           C  
ANISOU  904  CA  THR A 103     2541   1069    259    163     25     68       C  
ATOM    905  C   THR A 103      14.776  11.055  18.055  1.00 10.18           C  
ANISOU  905  C   THR A 103     2667    942    259    247    -49     51       C  
ATOM    906  O   THR A 103      15.020   9.889  18.333  1.00 11.52           O  
ANISOU  906  O   THR A 103     3104    910    361    262   -251     38       O  
ATOM    907  CB  THR A 103      16.868  12.400  18.394  1.00 11.80           C  
ANISOU  907  CB  THR A 103     2666   1179    637    150      5    -81       C  
ATOM    908  OG1 THR A 103      17.395  13.536  19.051  1.00 15.15           O  
ANISOU  908  OG1 THR A 103     2914   1899    941   -222     60     48       O  
ATOM    909  CG2 THR A 103      16.983  12.631  16.900  1.00 13.89           C  
ANISOU  909  CG2 THR A 103     3030   1749    496     45    303     70       C  
ATOM    910  N   ILE A 104      13.894  11.429  17.122  1.00  9.95           N  
ANISOU  910  N   ILE A 104     2656    840    284    180   -114    113       N  
ATOM    911  CA  ILE A 104      13.209  10.487  16.255  1.00 10.13           C  
ANISOU  911  CA  ILE A 104     2661    920    266     94     83     87       C  
ATOM    912  C   ILE A 104      13.715  10.741  14.839  1.00  9.55           C  
ANISOU  912  C   ILE A 104     2550    807    271    270     80     97       C  
ATOM    913  O   ILE A 104      13.578  11.839  14.339  1.00 10.37           O  
ANISOU  913  O   ILE A 104     2722    963    255    374     46     38       O  
ATOM    914  CB  ILE A 104      11.701  10.675  16.292  1.00 10.65           C  
ANISOU  914  CB  ILE A 104     2711   1054    280    115     42    148       C  
ATOM    915  CG1 ILE A 104      11.170  10.513  17.721  1.00 12.49           C  
ANISOU  915  CG1 ILE A 104     2740   1527    478     77    345    169       C  
ATOM    916  CG2 ILE A 104      11.001   9.668  15.341  1.00 13.18           C  
ANISOU  916  CG2 ILE A 104     2901   1625    479     52    -35     -6       C  
ATOM    917  CD1 ILE A 104       9.922  11.280  17.918  1.00 18.56           C  
ANISOU  917  CD1 ILE A 104     3063   2828   1161    314    670    314       C  
ATOM    918  N   LYS A 105      14.333   9.759  14.223  1.00  9.15           N  
ANISOU  918  N   LYS A 105     2409    805    261    154     63     63       N  
ATOM    919  CA  LYS A 105      14.793   9.846  12.851  1.00  9.58           C  
ANISOU  919  CA  LYS A 105     2415    970    253     89     27    -13       C  
ATOM    920  C   LYS A 105      13.902   9.041  11.949  1.00  9.50           C  
ANISOU  920  C   LYS A 105     2419    930    259    -25    -17     54       C  
ATOM    921  O   LYS A 105      13.518   7.928  12.286  1.00 11.20           O  
ANISOU  921  O   LYS A 105     3044    936    274   -126   -161     53       O  
ATOM    922  CB  LYS A 105      16.242   9.382  12.725  1.00 10.88           C  
ANISOU  922  CB  LYS A 105     2509   1369    254     59    -32     19       C  
ATOM    923  CG  LYS A 105      17.256  10.368  13.422  1.00 14.79           C  
ANISOU  923  CG  LYS A 105     2591   1945   1083    182   -168   -139       C  
ATOM    924  CD  LYS A 105      18.697  10.013  13.246  1.00 20.24           C  
ANISOU  924  CD  LYS A 105     2680   3003   2005    -86   -144     18       C  
ATOM    925  CE  LYS A 105      19.624  11.020  13.881  1.00 23.24           C  
ANISOU  925  CE  LYS A 105     3009   3060   2761   -164   -270    312       C  
ATOM    926  NZ  LYS A 105      21.053  10.597  13.664  1.00 28.01           N  
ANISOU  926  NZ  LYS A 105     3406   3683   3550   -195    -53    201       N  
ATOM    927  N   ARG A 106      13.590   9.594  10.786  1.00  9.67           N  
ANISOU  927  N   ARG A 106     2438    962    272    -14     23    116       N  
ATOM    928  CA  ARG A 106      12.744   8.911   9.783  1.00 10.19           C  
ANISOU  928  CA  ARG A 106     2426   1177    266   -212    119     68       C  
ATOM    929  C   ARG A 106      13.537   8.894   8.458  1.00 10.01           C  
ANISOU  929  C   ARG A 106     2436   1021    345   -172     42     33       C  
ATOM    930  O   ARG A 106      13.987   9.930   8.011  1.00 10.19           O  
ANISOU  930  O   ARG A 106     2564   1051    255   -146     69     -4       O  
ATOM    931  CB  ARG A 106      11.405   9.622   9.663  1.00 11.07           C  
ANISOU  931  CB  ARG A 106     2525   1417    262   -246     51     88       C  
ATOM    932  CG  ARG A 106      10.625   9.606  10.962  1.00 12.10           C  
ANISOU  932  CG  ARG A 106     2550   1684    363    -69    138    148       C  
ATOM    933  CD  ARG A 106       9.345  10.379  10.922  1.00 15.46           C  
ANISOU  933  CD  ARG A 106     2698   2704    470   -222    142     82       C  
ATOM    934  NE  ARG A 106       8.519  10.310  12.123  1.00 15.77           N  
ANISOU  934  NE  ARG A 106     2728   2724    537   -187    180    176       N  
ATOM    935  CZ  ARG A 106       8.440  11.241  13.061  1.00 15.21           C  
ANISOU  935  CZ  ARG A 106     2414   2708    655     89    202    252       C  
ATOM    936  NH1 ARG A 106       9.258  12.257  13.098  1.00 14.73           N  
ANISOU  936  NH1 ARG A 106     2681   2127    787    276    215    267       N  
ATOM    937  NH2 ARG A 106       7.574  11.093  14.032  1.00 17.19           N  
ANISOU  937  NH2 ARG A 106     2660   3233    635   -150    441    -15       N  
ATOM    938  N   LYS A 107      13.664   7.714   7.894  1.00 10.02           N  
ANISOU  938  N   LYS A 107     2510    998    298   -201    134     19       N  
ATOM    939  CA  LYS A 107      14.490   7.555   6.670  1.00 11.22           C  
ANISOU  939  CA  LYS A 107     2513   1292    457   -217    174   -122       C  
ATOM    940  C   LYS A 107      13.873   6.520   5.783  1.00 10.78           C  
ANISOU  940  C   LYS A 107     2516   1308    269   -299    135     70       C  
ATOM    941  O   LYS A 107      13.360   5.506   6.213  1.00 13.52           O  
ANISOU  941  O   LYS A 107     3326   1549    259   -573    131    -42       O  
ATOM    942  CB  LYS A 107      15.925   7.157   7.018  1.00 14.04           C  
ANISOU  942  CB  LYS A 107     2685   1884    763   -107    167   -412       C  
ATOM    943  CG  LYS A 107      16.926   7.188   5.891  1.00 17.03           C  
ANISOU  943  CG  LYS A 107     2983   2249   1238   -163     50   -534       C  
ATOM    944  CD  LYS A 107      18.336   6.788   6.317  1.00 20.32           C  
ANISOU  944  CD  LYS A 107     3135   2810   1774     76    129   -756       C  
ATOM    945  CE  LYS A 107      19.383   7.281   5.294  1.00 23.25           C  
ANISOU  945  CE  LYS A 107     3561   3243   2028   -146    313  -1019       C  
ATOM    946  NZ  LYS A 107      18.827   7.316   3.942  1.00 31.66           N  
ANISOU  946  NZ  LYS A 107     4459   4633   2938   -166    -27   -285       N  
ATOM    947  N   ARG A 108      13.927   6.760   4.481  1.00 10.87           N  
ANISOU  947  N   ARG A 108     2462   1394    274   -222    190    -25       N  
ATOM    948  CA  ARG A 108      13.528   5.764   3.492  1.00 11.79           C  
ANISOU  948  CA  ARG A 108     2481   1675    322   -180    160     33       C  
ATOM    949  C   ARG A 108      14.614   4.709   3.329  1.00 12.80           C  
ANISOU  949  C   ARG A 108     2481   1868    512   -223    179   -211       C  
ATOM    950  O   ARG A 108      15.775   5.041   3.091  1.00 14.69           O  
ANISOU  950  O   ARG A 108     2759   1798   1021   -139    279   -639       O  
ATOM    951  CB  ARG A 108      13.243   6.412   2.160  1.00 13.65           C  
ANISOU  951  CB  ARG A 108     2745   2054    385   -218    191    147       C  
ATOM    952  CG  ARG A 108      11.922   7.092   2.131  1.00 15.19           C  
ANISOU  952  CG  ARG A 108     3083   2072    615      5    -52    571       C  
ATOM    953  CD  ARG A 108      10.726   6.146   2.215  1.00 17.77           C  
ANISOU  953  CD  ARG A 108     2739   2895   1118    -81   -172    996       C  
ATOM    954  NE  ARG A 108      10.849   5.056   1.209  1.00 20.48           N  
ANISOU  954  NE  ARG A 108     2966   2882   1932    -81   -360    807       N  
ATOM    955  CZ  ARG A 108      10.547   5.192  -0.079  1.00 17.57           C  
ANISOU  955  CZ  ARG A 108     2872   1611   2192    -92   -456    126       C  
ATOM    956  NH1 ARG A 108      10.015   6.289  -0.615  1.00 18.23           N  
ANISOU  956  NH1 ARG A 108     3305   2548   1070    -88   -659    369       N  
ATOM    957  NH2 ARG A 108      10.757   4.177  -0.887  1.00 21.70           N  
ANISOU  957  NH2 ARG A 108     3199   2711   2334    202   -399   -369       N  
ATOM    958  N   GLU A 109      14.210   3.444   3.354  1.00 11.97           N  
ANISOU  958  N   GLU A 109     2465   1685    396    -72    170   -292       N  
ATOM    959  CA  GLU A 109      15.117   2.317   3.099  1.00 12.87           C  
ANISOU  959  CA  GLU A 109     2596   1835    456    -60     61   -237       C  
ATOM    960  C   GLU A 109      14.358   1.338   2.232  1.00 12.42           C  
ANISOU  960  C   GLU A 109     2538   1580    598     18    160   -183       C  
ATOM    961  O   GLU A 109      13.355   0.774   2.684  1.00 12.35           O  
ANISOU  961  O   GLU A 109     2674   1729    288   -209    198   -182       O  
ATOM    962  CB  GLU A 109      15.503   1.627   4.418  1.00 14.27           C  
ANISOU  962  CB  GLU A 109     2728   2009    685     89    -70    -47       C  
ATOM    963  CG  GLU A 109      16.238   2.535   5.396  1.00 18.33           C  
ANISOU  963  CG  GLU A 109     3081   2663   1219    106   -376   -171       C  
ATOM    964  CD  GLU A 109      17.654   2.778   5.022  1.00 22.49           C  
ANISOU  964  CD  GLU A 109     3567   3407   1569    -69     44   -439       C  
ATOM    965  OE1 GLU A 109      18.355   3.467   5.780  1.00 26.66           O  
ANISOU  965  OE1 GLU A 109     3759   3946   2422   -383    149   -759       O  
ATOM    966  OE2 GLU A 109      18.095   2.284   3.983  1.00 28.36           O  
ANISOU  966  OE2 GLU A 109     4269   4024   2481    162    549   -734       O  
ATOM    967  N   ASP A 110      14.789   1.170   0.989  1.00 11.55           N  
ANISOU  967  N   ASP A 110     2568   1523    296    -10    249   -111       N  
ATOM    968  CA  ASP A 110      14.044   0.357   0.047  1.00 11.42           C  
ANISOU  968  CA  ASP A 110     2659   1404    276   -110    230    -41       C  
ATOM    969  C   ASP A 110      12.632   0.877  -0.021  1.00 10.90           C  
ANISOU  969  C   ASP A 110     2404   1469    267   -111    146    -82       C  
ATOM    970  O   ASP A 110      12.471   2.109  -0.129  1.00 11.77           O  
ANISOU  970  O   ASP A 110     2666   1540    264    -16    156    -31       O  
ATOM    971  CB  ASP A 110      14.178  -1.131   0.354  1.00 11.93           C  
ANISOU  971  CB  ASP A 110     2720   1454    358     62    248   -113       C  
ATOM    972  CG  ASP A 110      15.592  -1.611   0.303  1.00 15.41           C  
ANISOU  972  CG  ASP A 110     2997   1978    877     46    258    163       C  
ATOM    973  OD1 ASP A 110      16.326  -1.157  -0.565  1.00 18.50           O  
ANISOU  973  OD1 ASP A 110     3141   2338   1548    386    532    177       O  
ATOM    974  OD2 ASP A 110      15.967  -2.490   1.110  1.00 23.23           O  
ANISOU  974  OD2 ASP A 110     3586   2983   2255    625     50   1115       O  
ATOM    975  N   ASP A 111      11.595   0.079   0.032  1.00 11.98           N  
ANISOU  975  N   ASP A 111     2690   1571    290    -20    115   -204       N  
ATOM    976  CA  ASP A 111      10.235   0.559  -0.024  1.00 12.40           C  
ANISOU  976  CA  ASP A 111     2679   1731    298   -101     57   -149       C  
ATOM    977  C   ASP A 111       9.658   0.901   1.356  1.00 12.58           C  
ANISOU  977  C   ASP A 111     2594   1660    526    -44     73   -299       C  
ATOM    978  O   ASP A 111       8.456   1.137   1.464  1.00 15.60           O  
ANISOU  978  O   ASP A 111     2750   2487    686     66     32   -688       O  
ATOM    979  CB  ASP A 111       9.345  -0.446  -0.760  1.00 12.60           C  
ANISOU  979  CB  ASP A 111     2627   1887    272    -64    -19   -174       C  
ATOM    980  CG  ASP A 111       9.665  -0.523  -2.240  1.00 13.54           C  
ANISOU  980  CG  ASP A 111     2953   1753    438    -63     37   -187       C  
ATOM    981  OD1 ASP A 111       9.894   0.535  -2.843  1.00 15.32           O  
ANISOU  981  OD1 ASP A 111     3512   1809    498   -220      9    -69       O  
ATOM    982  OD2 ASP A 111       9.669  -1.615  -2.781  1.00 16.36           O  
ANISOU  982  OD2 ASP A 111     3936   1791    487   -187    268   -304       O  
ATOM    983  N   LYS A 112      10.485   0.874   2.390  1.00 11.44           N  
ANISOU  983  N   LYS A 112     2577   1495    275    -43    198    -85       N  
ATOM    984  CA  LYS A 112      10.046   1.104   3.739  1.00 11.22           C  
ANISOU  984  CA  LYS A 112     2613   1355    295    -52    306    -55       C  
ATOM    985  C   LYS A 112      10.371   2.489   4.192  1.00 10.62           C  
ANISOU  985  C   LYS A 112     2399   1349    286    -72    254     49       C  
ATOM    986  O   LYS A 112      11.232   3.161   3.661  1.00 11.21           O  
ANISOU  986  O   LYS A 112     2523   1432    302   -182    173    -39       O  
ATOM    987  CB  LYS A 112      10.714   0.080   4.654  1.00 12.86           C  
ANISOU  987  CB  LYS A 112     2999   1546    342    100    443   -122       C  
ATOM    988  CG  LYS A 112      10.359  -1.334   4.263  1.00 17.60           C  
ANISOU  988  CG  LYS A 112     3575   1908   1202    221    640   -166       C  
ATOM    989  CD  LYS A 112      11.010  -2.390   5.006  1.00 23.96           C  
ANISOU  989  CD  LYS A 112     4323   2956   1824    553    519   -310       C  
ATOM    990  CE  LYS A 112      10.685  -3.763   4.368  1.00 28.47           C  
ANISOU  990  CE  LYS A 112     4782   3188   2845    284    212   -342       C  
ATOM    991  NZ  LYS A 112      11.634  -4.794   4.775  1.00 31.43           N  
ANISOU  991  NZ  LYS A 112     5314   4009   2615    382   -224    -86       N  
ATOM    992  N   LEU A 113       9.712   2.878   5.264  1.00 10.00           N  
ANISOU  992  N   LEU A 113     2377   1159    264   -107    154      2       N  
ATOM    993  CA  LEU A 113      10.030   4.088   6.007  1.00  9.84           C  
ANISOU  993  CA  LEU A 113     2300   1183    255   -132     61     23       C  
ATOM    994  C   LEU A 113      10.395   3.619   7.434  1.00 10.08           C  
ANISOU  994  C   LEU A 113     2391   1119    317   -191    271     29       C  
ATOM    995  O   LEU A 113       9.586   3.006   8.107  1.00 11.11           O  
ANISOU  995  O   LEU A 113     2476   1480    263   -269    125     42       O  
ATOM    996  CB  LEU A 113       8.840   5.046   5.983  1.00 11.19           C  
ANISOU  996  CB  LEU A 113     2530   1364    357   -241     69   -103       C  
ATOM    997  CG  LEU A 113       9.049   6.444   6.662  1.00 14.06           C  
ANISOU  997  CG  LEU A 113     2786   1843    713    -90    -89   -415       C  
ATOM    998  CD1 LEU A 113       7.884   7.345   6.237  1.00 16.70           C  
ANISOU  998  CD1 LEU A 113     3025   2001   1317    329   -184   -101       C  
ATOM    999  CD2 LEU A 113       9.253   6.482   8.054  1.00 17.47           C  
ANISOU  999  CD2 LEU A 113     3172   2423   1042    108     95    108       C  
ATOM   1000  N   VAL A 114      11.669   3.797   7.774  1.00  9.88           N  
ANISOU 1000  N   VAL A 114     2257   1234    261   -169     65     70       N  
ATOM   1001  CA  VAL A 114      12.188   3.326   9.083  1.00 10.41           C  
ANISOU 1001  CA  VAL A 114     2414   1229    309   -177    -29    207       C  
ATOM   1002  C   VAL A 114      12.225   4.513  10.021  1.00 11.18           C  
ANISOU 1002  C   VAL A 114     2542   1396    310   -308     86    205       C  
ATOM   1003  O   VAL A 114      12.707   5.602   9.685  1.00 11.79           O  
ANISOU 1003  O   VAL A 114     2723   1449    306   -372    140     14       O  
ATOM   1004  CB  VAL A 114      13.574   2.730   8.892  1.00 12.47           C  
ANISOU 1004  CB  VAL A 114     2607   1487    645   -122     -7    268       C  
ATOM   1005  CG1 VAL A 114      14.142   2.208  10.181  1.00 13.88           C  
ANISOU 1005  CG1 VAL A 114     2856   1799    615    138    -79    350       C  
ATOM   1006  CG2 VAL A 114      13.547   1.568   7.854  1.00 14.86           C  
ANISOU 1006  CG2 VAL A 114     2968   1661   1017    256    258   -202       C  
ATOM   1007  N   VAL A 115      11.711   4.270  11.227  1.00 11.20           N  
ANISOU 1007  N   VAL A 115     2772   1194    288   -287    -52    182       N  
ATOM   1008  CA  VAL A 115      11.635   5.259  12.301  1.00 10.92           C  
ANISOU 1008  CA  VAL A 115     2696   1117    335   -270   -209     24       C  
ATOM   1009  C   VAL A 115      12.514   4.775  13.440  1.00 10.70           C  
ANISOU 1009  C   VAL A 115     2677   1102    283   -235   -170    138       C  
ATOM   1010  O   VAL A 115      12.264   3.721  14.020  1.00 13.93           O  
ANISOU 1010  O   VAL A 115     3270   1458    563   -576   -462    358       O  
ATOM   1011  CB  VAL A 115      10.194   5.472  12.730  1.00 11.60           C  
ANISOU 1011  CB  VAL A 115     2764   1349    293   -292   -169     30       C  
ATOM   1012  CG1 VAL A 115      10.068   6.582  13.782  1.00 13.97           C  
ANISOU 1012  CG1 VAL A 115     3063   1901    342   -112   -287   -122       C  
ATOM   1013  CG2 VAL A 115       9.310   5.790  11.537  1.00 13.12           C  
ANISOU 1013  CG2 VAL A 115     2779   1565    641   -445   -209    193       C  
ATOM   1014  N   GLU A 116      13.548   5.534  13.759  1.00 10.15           N  
ANISOU 1014  N   GLU A 116     2608    978    270   -199    -83    106       N  
ATOM   1015  CA AGLU A 116      14.484   5.206  14.857  0.50 10.37           C  
ANISOU 1015  CA AGLU A 116     2650    908    380     24    -98    117       C  
ATOM   1016  CA BGLU A 116      14.458   5.210  14.866  0.50 10.92           C  
ANISOU 1016  CA BGLU A 116     2672    956    521    -34   -112     87       C  
ATOM   1017  C   GLU A 116      14.266   6.222  15.961  1.00  9.95           C  
ANISOU 1017  C   GLU A 116     2554    941    285     44   -219     18       C  
ATOM   1018  O   GLU A 116      14.465   7.409  15.739  1.00 11.58           O  
ANISOU 1018  O   GLU A 116     3145    982    271     97    -71     34       O  
ATOM   1019  CB AGLU A 116      15.938   5.242  14.337  0.50 12.43           C  
ANISOU 1019  CB AGLU A 116     2820   1074    826    128    -58     17       C  
ATOM   1020  CB BGLU A 116      15.902   5.297  14.411  0.50 13.33           C  
ANISOU 1020  CB BGLU A 116     2839   1227    995     22    -99     19       C  
ATOM   1021  CG AGLU A 116      17.017   4.875  15.363  0.50 13.22           C  
ANISOU 1021  CG AGLU A 116     2807   1571    645    442    169    418       C  
ATOM   1022  CG BGLU A 116      16.502   4.098  13.766  0.50 16.39           C  
ANISOU 1022  CG BGLU A 116     2924   1612   1689    -12    102    150       C  
ATOM   1023  CD AGLU A 116      18.407   5.538  15.141  0.50 18.16           C  
ANISOU 1023  CD AGLU A 116     3208   2229   1460    156     26    132       C  
ATOM   1024  CD BGLU A 116      18.013   4.073  14.066  0.50 20.78           C  
ANISOU 1024  CD BGLU A 116     3073   2657   2163    137    -62    -73       C  
ATOM   1025  OE1AGLU A 116      18.536   6.798  15.082  0.50 19.19           O  
ANISOU 1025  OE1AGLU A 116     3237   2377   1675    179    291    483       O  
ATOM   1026  OE1BGLU A 116      18.579   5.084  14.547  0.50 22.55           O  
ANISOU 1026  OE1BGLU A 116     2967   3444   2154    393   -580   -322       O  
ATOM   1027  OE2AGLU A 116      19.399   4.788  15.041  0.50 19.99           O  
ANISOU 1027  OE2AGLU A 116     3224   3091   1280    219    310    422       O  
ATOM   1028  OE2BGLU A 116      18.637   3.045  13.805  0.50 22.11           O  
ANISOU 1028  OE2BGLU A 116     3369   2867   2162    540   -131    345       O  
ATOM   1029  N   CYS A 117      13.872   5.744  17.136  1.00 10.08           N  
ANISOU 1029  N   CYS A 117     2572    945    313     98   -130    152       N  
ATOM   1030  CA  CYS A 117      13.590   6.569  18.288  1.00 10.43           C  
ANISOU 1030  CA  CYS A 117     2585    947    429    220   -148    -42       C  
ATOM   1031  C   CYS A 117      14.719   6.344  19.289  1.00 10.43           C  
ANISOU 1031  C   CYS A 117     2610   1015    336    220   -160     38       C  
ATOM   1032  O   CYS A 117      14.939   5.214  19.697  1.00 11.37           O  
ANISOU 1032  O   CYS A 117     2867   1009    442    131   -389     66       O  
ATOM   1033  CB  CYS A 117      12.231   6.141  18.917  1.00 12.20           C  
ANISOU 1033  CB  CYS A 117     2701   1616    317    404   -291    -46       C  
ATOM   1034  SG  CYS A 117      10.844   6.160  17.765  1.00 16.58           S  
ANISOU 1034  SG  CYS A 117     2916   2711    673    272   -204    328       S  
ATOM   1035  N   VAL A 118      15.369   7.402  19.714  1.00 10.58           N  
ANISOU 1035  N   VAL A 118     2549   1036    434    200   -151     42       N  
ATOM   1036  CA  VAL A 118      16.542   7.307  20.563  1.00 11.24           C  
ANISOU 1036  CA  VAL A 118     2533   1014    723    171    -89    -70       C  
ATOM   1037  C   VAL A 118      16.374   8.159  21.810  1.00 11.61           C  
ANISOU 1037  C   VAL A 118     2530   1047    833    225   -214     28       C  
ATOM   1038  O   VAL A 118      16.043   9.346  21.731  1.00 11.70           O  
ANISOU 1038  O   VAL A 118     2879   1052    513    231   -155    -13       O  
ATOM   1039  CB  VAL A 118      17.839   7.702  19.796  1.00 13.96           C  
ANISOU 1039  CB  VAL A 118     2644   1354   1304     15      0    -80       C  
ATOM   1040  CG1 VAL A 118      19.018   7.678  20.700  1.00 18.35           C  
ANISOU 1040  CG1 VAL A 118     2722   2030   2219    -55      6   -280       C  
ATOM   1041  CG2 VAL A 118      18.056   6.805  18.593  1.00 16.06           C  
ANISOU 1041  CG2 VAL A 118     2921   1741   1438    -47    506   -258       C  
ATOM   1042  N   MET A 119      16.604   7.552  22.971  1.00 12.29           N  
ANISOU 1042  N   MET A 119     2737   1113    819    280   -361     88       N  
ATOM   1043  CA  MET A 119      16.628   8.307  24.252  1.00 13.64           C  
ANISOU 1043  CA  MET A 119     2958   1282    940    216   -500     46       C  
ATOM   1044  C   MET A 119      17.831   7.706  24.966  1.00 14.41           C  
ANISOU 1044  C   MET A 119     2835   1558   1079    184   -441   -103       C  
ATOM   1045  O   MET A 119      17.846   6.546  25.355  1.00 13.94           O  
ANISOU 1045  O   MET A 119     2950   1400    944    279   -560    -51       O  
ATOM   1046  CB  MET A 119      15.299   8.034  25.010  1.00 14.83           C  
ANISOU 1046  CB  MET A 119     3090   1848    695    459   -468   -181       C  
ATOM   1047  CG  MET A 119      15.181   8.461  26.442  1.00 17.07           C  
ANISOU 1047  CG  MET A 119     3742   1802    941     18   -380     38       C  
ATOM   1048  SD  MET A 119      14.822  10.194  26.368  1.00 23.10           S  
ANISOU 1048  SD  MET A 119     5376   1873   1528    865  -1441   -468       S  
ATOM   1049  CE  MET A 119      14.873  10.868  27.989  1.00 18.84           C  
ANISOU 1049  CE  MET A 119     4256   1561   1340    -55   -342   -102       C  
ATOM   1050  N  ALYS A 120      18.860   8.502  25.253  0.50 17.56           N  
ANISOU 1050  N  ALYS A 120     3014   1852   1805    110   -372     11       N  
ATOM   1051  N  BLYS A 120      18.833   8.561  25.058  0.50 15.24           N  
ANISOU 1051  N  BLYS A 120     2793   1578   1420    140   -398     -7       N  
ATOM   1052  CA ALYS A 120      20.056   8.077  26.030  0.50 19.93           C  
ANISOU 1052  CA ALYS A 120     2998   2353   2221     54   -254     -5       C  
ATOM   1053  CA BLYS A 120      20.072   8.244  25.612  0.50 15.06           C  
ANISOU 1053  CA BLYS A 120     2619   1693   1408     54   -336    151       C  
ATOM   1054  C  ALYS A 120      20.472   6.617  26.031  0.50 19.32           C  
ANISOU 1054  C  ALYS A 120     2917   2311   2111     25   -221    -33       C  
ATOM   1055  C  BLYS A 120      20.636   7.019  24.885  0.50 12.36           C  
ANISOU 1055  C  BLYS A 120     2378   1323    992     36   -362    188       C  
ATOM   1056  O  ALYS A 120      20.377   5.919  27.042  0.50 21.04           O  
ANISOU 1056  O  ALYS A 120     3176   2582   2236   -105   -246   -181       O  
ATOM   1057  O  BLYS A 120      20.775   6.992  23.650  0.50 13.32           O  
ANISOU 1057  O  BLYS A 120     2488   1339   1232    107    -98    490       O  
ATOM   1058  CB ALYS A 120      19.939   8.467  27.484  0.50 20.55           C  
ANISOU 1058  CB ALYS A 120     3049   2409   2350    136   -273    -44       C  
ATOM   1059  CB BLYS A 120      19.872   8.015  27.130  0.50 13.94           C  
ANISOU 1059  CB BLYS A 120     2646   1381   1269     45   -520      2       C  
ATOM   1060  CG ALYS A 120      18.722   8.034  28.195  0.50 20.92           C  
ANISOU 1060  CG ALYS A 120     3073   2522   2351    131   -415     63       C  
ATOM   1061  CG BLYS A 120      19.397   9.311  27.931  0.50 16.02           C  
ANISOU 1061  CG BLYS A 120     2633   2077   1376    262   -679   -234       C  
ATOM   1062  CD ALYS A 120      18.245   9.251  28.926  0.50 23.16           C  
ANISOU 1062  CD ALYS A 120     3308   2783   2708    201   -323    -63       C  
ATOM   1063  CD BLYS A 120      19.145   8.908  29.380  0.50 19.90           C  
ANISOU 1063  CD BLYS A 120     3125   2627   1807     73   -571   -354       C  
ATOM   1064  CE ALYS A 120      19.447   9.927  29.526  0.50 25.15           C  
ANISOU 1064  CE ALYS A 120     3477   3126   2951    -10   -225    108       C  
ATOM   1065  CE BLYS A 120      18.698  10.057  30.253  0.50 22.72           C  
ANISOU 1065  CE BLYS A 120     3304   3156   2172     12   -129   -378       C  
ATOM   1066  NZ ALYS A 120      20.101   9.020  30.501  0.50 26.28           N  
ANISOU 1066  NZ ALYS A 120     3899   3398   2686    -34   -268    258       N  
ATOM   1067  NZ BLYS A 120      19.715  10.422  31.270  0.50 24.58           N  
ANISOU 1067  NZ BLYS A 120     3601   3076   2661    -73   -421   -193       N  
ATOM   1068  N  AGLY A 121      21.022   6.189  24.912  0.50 18.52           N  
ANISOU 1068  N  AGLY A 121     2763   2329   1943     48   -164     -2       N  
ATOM   1069  N  BGLY A 121      20.935   5.940  25.615  0.50 13.01           N  
ANISOU 1069  N  BGLY A 121     2299   1582   1061    104   -239    333       N  
ATOM   1070  CA AGLY A 121      21.542   4.864  24.769  0.50 17.31           C  
ANISOU 1070  CA AGLY A 121     2620   2085   1868     36   -122    114       C  
ATOM   1071  CA BGLY A 121      21.525   4.784  25.004  0.50 14.87           C  
ANISOU 1071  CA BGLY A 121     2401   1765   1483     60   -173    242       C  
ATOM   1072  C   GLY A 121      20.507   3.822  24.406  1.00 13.86           C  
ANISOU 1072  C   GLY A 121     2363   1801   1101     85   -206    188       C  
ATOM   1073  O   GLY A 121      20.877   2.763  23.972  1.00 14.92           O  
ANISOU 1073  O   GLY A 121     2485   1831   1352    287     57    351       O  
ATOM   1074  N   VAL A 122      19.215   4.133  24.519  1.00 12.64           N  
ANISOU 1074  N   VAL A 122     2479   1478    846     99   -205    262       N  
ATOM   1075  CA  VAL A 122      18.141   3.196  24.132  1.00 11.27           C  
ANISOU 1075  CA  VAL A 122     2367   1253    663    262   -153    216       C  
ATOM   1076  C   VAL A 122      17.535   3.591  22.808  1.00 11.35           C  
ANISOU 1076  C   VAL A 122     2343   1167    800    157   -209    161       C  
ATOM   1077  O   VAL A 122      17.065   4.728  22.658  1.00 12.27           O  
ANISOU 1077  O   VAL A 122     2793   1184    684    322   -405     85       O  
ATOM   1078  CB  VAL A 122      17.055   3.116  25.223  1.00 12.33           C  
ANISOU 1078  CB  VAL A 122     2416   1473    796    234   -122    164       C  
ATOM   1079  CG1 VAL A 122      16.000   2.173  24.790  1.00 14.92           C  
ANISOU 1079  CG1 VAL A 122     2501   1906   1260     82     82    262       C  
ATOM   1080  CG2 VAL A 122      17.661   2.699  26.559  1.00 14.98           C  
ANISOU 1080  CG2 VAL A 122     2864   1989    836    391    -19    471       C  
ATOM   1081  N   THR A 123      17.552   2.669  21.850  1.00 11.41           N  
ANISOU 1081  N   THR A 123     2413   1134    786    172   -264    128       N  
ATOM   1082  CA  THR A 123      16.997   2.850  20.536  1.00 11.34           C  
ANISOU 1082  CA  THR A 123     2431   1270    606    200   -243    116       C  
ATOM   1083  C   THR A 123      15.821   1.906  20.315  1.00 10.97           C  
ANISOU 1083  C   THR A 123     2441    930    794    134   -351      5       C  
ATOM   1084  O   THR A 123      15.891   0.738  20.678  1.00 14.84           O  
ANISOU 1084  O   THR A 123     2887   1161   1587     39   -555    383       O  
ATOM   1085  CB  THR A 123      18.046   2.603  19.494  1.00 13.52           C  
ANISOU 1085  CB  THR A 123     2663   1628    844    139    -62     63       C  
ATOM   1086  OG1 THR A 123      19.104   3.528  19.695  1.00 17.28           O  
ANISOU 1086  OG1 THR A 123     3197   2035   1333   -135    493    -58       O  
ATOM   1087  CG2 THR A 123      17.482   2.772  18.064  1.00 15.20           C  
ANISOU 1087  CG2 THR A 123     2980   2083    709    196    123    142       C  
ATOM   1088  N   SER A 124      14.796   2.392  19.690  1.00 11.18           N  
ANISOU 1088  N   SER A 124     2547   1163    536     25   -371    220       N  
ATOM   1089  CA  SER A 124      13.762   1.572  19.133  1.00 11.24           C  
ANISOU 1089  CA  SER A 124     2525   1115    627    -22   -330    334       C  
ATOM   1090  C   SER A 124      13.669   1.784  17.651  1.00 10.51           C  
ANISOU 1090  C   SER A 124     2395   1092    506     79   -154    161       C  
ATOM   1091  O   SER A 124      13.704   2.910  17.172  1.00 12.38           O  
ANISOU 1091  O   SER A 124     3198   1046    460    -70   -172    188       O  
ATOM   1092  CB  SER A 124      12.394   1.871  19.770  1.00 11.30           C  
ANISOU 1092  CB  SER A 124     2575   1222    493    -78   -212    313       C  
ATOM   1093  OG  SER A 124      11.311   1.208  19.171  1.00 12.17           O  
ANISOU 1093  OG  SER A 124     2614   1447    561    -16    -85    114       O  
ATOM   1094  N   THR A 125      13.514   0.719  16.893  1.00 10.09           N  
ANISOU 1094  N   THR A 125     2436    953    443    -67   -222    249       N  
ATOM   1095  CA  THR A 125      13.347   0.749  15.450  1.00  9.95           C  
ANISOU 1095  CA  THR A 125     2232   1237    308     79    -34    230       C  
ATOM   1096  C   THR A 125      11.961   0.282  15.085  1.00 10.22           C  
ANISOU 1096  C   THR A 125     2379   1212    291   -110   -141    134       C  
ATOM   1097  O   THR A 125      11.562  -0.839  15.438  1.00 12.01           O  
ANISOU 1097  O   THR A 125     2743   1198    621   -277   -224    210       O  
ATOM   1098  CB  THR A 125      14.425  -0.093  14.777  1.00 12.87           C  
ANISOU 1098  CB  THR A 125     2513   1616    759    223    -25     18       C  
ATOM   1099  OG1 THR A 125      15.733   0.388  15.139  1.00 15.31           O  
ANISOU 1099  OG1 THR A 125     2508   1965   1344    270    265    -49       O  
ATOM   1100  CG2 THR A 125      14.275  -0.064  13.230  1.00 15.67           C  
ANISOU 1100  CG2 THR A 125     3010   2168    776    281    182    163       C  
ATOM   1101  N   ARG A 126      11.251   1.134  14.352  1.00 10.26           N  
ANISOU 1101  N   ARG A 126     2249   1292    356   -188    -24    192       N  
ATOM   1102  CA  ARG A 126       9.885   0.878  13.931  1.00 10.42           C  
ANISOU 1102  CA  ARG A 126     2333   1304    321   -326     -3    261       C  
ATOM   1103  C   ARG A 126       9.836   0.987  12.408  1.00 10.61           C  
ANISOU 1103  C   ARG A 126     2346   1396    288   -335    -34    199       C  
ATOM   1104  O   ARG A 126      10.283   1.969  11.843  1.00 13.91           O  
ANISOU 1104  O   ARG A 126     3278   1676    330   -784   -147    275       O  
ATOM   1105  CB  ARG A 126       8.943   1.868  14.601  1.00 12.07           C  
ANISOU 1105  CB  ARG A 126     2311   1862    410   -216    -94    232       C  
ATOM   1106  CG  ARG A 126       8.895   1.533  16.090  1.00 14.77           C  
ANISOU 1106  CG  ARG A 126     2755   2318    539     44    -75      6       C  
ATOM   1107  CD  ARG A 126       8.177   2.447  16.934  1.00 16.54           C  
ANISOU 1107  CD  ARG A 126     2918   2586    778     75   -147    380       C  
ATOM   1108  NE  ARG A 126       6.766   2.736  16.699  1.00 16.96           N  
ANISOU 1108  NE  ARG A 126     2851   2920    671    -72     62    -42       N  
ATOM   1109  CZ  ARG A 126       5.719   2.121  17.266  1.00 15.41           C  
ANISOU 1109  CZ  ARG A 126     2713   2500    640   -399    -77    -33       C  
ATOM   1110  NH1 ARG A 126       5.819   0.955  17.900  1.00 16.40           N  
ANISOU 1110  NH1 ARG A 126     3112   2645    470   -186   -222     46       N  
ATOM   1111  NH2 ARG A 126       4.547   2.646  17.143  1.00 16.99           N  
ANISOU 1111  NH2 ARG A 126     2899   2580    973   -502     65    136       N  
ATOM   1112  N   VAL A 127       9.312  -0.027  11.752  1.00  9.75           N  
ANISOU 1112  N   VAL A 127     2312   1122    268   -198     37    106       N  
ATOM   1113  CA  VAL A 127       9.348  -0.107  10.283  1.00 10.20           C  
ANISOU 1113  CA  VAL A 127     2190   1409    277    -48    168     98       C  
ATOM   1114  C   VAL A 127       7.941  -0.001   9.785  1.00  9.62           C  
ANISOU 1114  C   VAL A 127     2177   1181    296      3    174    -12       C  
ATOM   1115  O   VAL A 127       7.038  -0.720  10.210  1.00 10.80           O  
ANISOU 1115  O   VAL A 127     2358   1467    278   -148     43    106       O  
ATOM   1116  CB  VAL A 127       9.971  -1.414   9.841  1.00 11.77           C  
ANISOU 1116  CB  VAL A 127     2459   1513    500    131    -92    104       C  
ATOM   1117  CG1 VAL A 127       9.937  -1.494   8.284  1.00 14.40           C  
ANISOU 1117  CG1 VAL A 127     2989   1992    487    267     14   -167       C  
ATOM   1118  CG2 VAL A 127      11.368  -1.545  10.373  1.00 15.59           C  
ANISOU 1118  CG2 VAL A 127     2743   2174   1004    301    -53     32       C  
ATOM   1119  N   TYR A 128       7.754   0.946   8.863  1.00 10.02           N  
ANISOU 1119  N   TYR A 128     2303   1183    321    -85     19     68       N  
ATOM   1120  CA  TYR A 128       6.483   1.159   8.180  1.00  9.65           C  
ANISOU 1120  CA  TYR A 128     2143   1253    268   -104     80    102       C  
ATOM   1121  C   TYR A 128       6.609   0.760   6.696  1.00 10.56           C  
ANISOU 1121  C   TYR A 128     2261   1256    494    -59    -45    -18       C  
ATOM   1122  O   TYR A 128       7.657   0.957   6.078  1.00 11.48           O  
ANISOU 1122  O   TYR A 128     2462   1563    334   -165     91   -164       O  
ATOM   1123  CB  TYR A 128       6.074   2.622   8.233  1.00  9.59           C  
ANISOU 1123  CB  TYR A 128     2158   1199    286   -112      9    175       C  
ATOM   1124  CG  TYR A 128       5.661   3.134   9.616  1.00  9.71           C  
ANISOU 1124  CG  TYR A 128     2354   1071    263   -126    -34     89       C  
ATOM   1125  CD1 TYR A 128       6.600   3.405  10.595  1.00 11.15           C  
ANISOU 1125  CD1 TYR A 128     2393   1293    551    -72   -133     26       C  
ATOM   1126  CD2 TYR A 128       4.329   3.352   9.919  1.00 10.31           C  
ANISOU 1126  CD2 TYR A 128     2272   1069    574    -43     22    191       C  
ATOM   1127  CE1 TYR A 128       6.190   3.911  11.861  1.00 11.83           C  
ANISOU 1127  CE1 TYR A 128     2604   1552    337   -127   -141   -150       C  
ATOM   1128  CE2 TYR A 128       3.917   3.849  11.134  1.00 11.43           C  
ANISOU 1128  CE2 TYR A 128     2375   1391    575    -80    248      3       C  
ATOM   1129  CZ  TYR A 128       4.838   4.126  12.092  1.00 11.26           C  
ANISOU 1129  CZ  TYR A 128     2496   1329    453   -169     78     63       C  
ATOM   1130  OH  TYR A 128       4.402   4.599  13.311  1.00 14.08           O  
ANISOU 1130  OH  TYR A 128     2821   2107    422     63    186   -180       O  
ATOM   1131  N   GLU A 129       5.534   0.219   6.171  1.00 11.31           N  
ANISOU 1131  N   GLU A 129     2391   1456    447   -273    -28   -147       N  
ATOM   1132  CA AGLU A 129       5.380  -0.132   4.759  0.50 11.39           C  
ANISOU 1132  CA AGLU A 129     2382   1423    522    -79    -60   -399       C  
ATOM   1133  CA BGLU A 129       5.485   0.000   4.718  0.50 11.97           C  
ANISOU 1133  CA BGLU A 129     2481   1525    539    -72   -106   -373       C  
ATOM   1134  C   GLU A 129       4.289   0.727   4.166  1.00 10.98           C  
ANISOU 1134  C   GLU A 129     2353   1453    365   -158    -63   -246       C  
ATOM   1135  O   GLU A 129       3.444   1.205   4.857  1.00 11.46           O  
ANISOU 1135  O   GLU A 129     2522   1298    533    -38   -108    -76       O  
ATOM   1136  CB AGLU A 129       5.016  -1.616   4.649  0.50 12.45           C  
ANISOU 1136  CB AGLU A 129     2445   1543    742   -105    -68   -362       C  
ATOM   1137  CB BGLU A 129       5.483  -1.483   4.358  0.50 13.55           C  
ANISOU 1137  CB BGLU A 129     2731   1639    778     23   -208   -247       C  
ATOM   1138  CG AGLU A 129       6.234  -2.518   4.929  0.50 16.98           C  
ANISOU 1138  CG AGLU A 129     3152   2085   1213    151   -371   -418       C  
ATOM   1139  CG BGLU A 129       4.223  -2.207   4.799  0.50 17.95           C  
ANISOU 1139  CG BGLU A 129     3138   2260   1421   -229   -288   -394       C  
ATOM   1140  CD AGLU A 129       5.995  -3.950   4.588  0.50 21.61           C  
ANISOU 1140  CD AGLU A 129     3957   2285   1968     53   -396   -444       C  
ATOM   1141  CD BGLU A 129       4.238  -3.738   4.509  0.50 22.48           C  
ANISOU 1141  CD BGLU A 129     3890   2520   2132   -204   -427   -458       C  
ATOM   1142  OE1AGLU A 129       5.208  -4.198   3.644  0.50 24.00           O  
ANISOU 1142  OE1AGLU A 129     4700   2393   2025     -8   -629   -481       O  
ATOM   1143  OE1BGLU A 129       3.164  -4.296   4.248  0.50 24.75           O  
ANISOU 1143  OE1BGLU A 129     4267   2436   2701   -416   -332   -252       O  
ATOM   1144  OE2AGLU A 129       6.574  -4.808   5.285  0.50 25.35           O  
ANISOU 1144  OE2AGLU A 129     4717   2766   2149    244   -558   -575       O  
ATOM   1145  OE2BGLU A 129       5.311  -4.378   4.557  0.50 23.84           O  
ANISOU 1145  OE2BGLU A 129     4338   2440   2279   -105   -571   -698       O  
ATOM   1146  N   ARG A 130       4.247   0.845   2.841  1.00 12.39           N  
ANISOU 1146  N   ARG A 130     2664   1652    389    -92   -141   -352       N  
ATOM   1147  CA  ARG A 130       3.153   1.551   2.203  1.00 12.69           C  
ANISOU 1147  CA  ARG A 130     2665   1660    494    -64   -143   -153       C  
ATOM   1148  C   ARG A 130       1.843   0.883   2.486  1.00 13.49           C  
ANISOU 1148  C   ARG A 130     2664   1720    739   -145   -343   -210       C  
ATOM   1149  O   ARG A 130       1.722  -0.356   2.378  1.00 15.91           O  
ANISOU 1149  O   ARG A 130     3167   1460   1418    -55   -649   -226       O  
ATOM   1150  CB  ARG A 130       3.357   1.634   0.711  1.00 14.77           C  
ANISOU 1150  CB  ARG A 130     2784   2411    418   -130   -225   -146       C  
ATOM   1151  CG  ARG A 130       4.555   2.356   0.336  1.00 16.70           C  
ANISOU 1151  CG  ARG A 130     3200   2524    621   -209    -20    352       C  
ATOM   1152  CD  ARG A 130       4.264   3.781   0.216  1.00 19.29           C  
ANISOU 1152  CD  ARG A 130     3263   2415   1650   -185   -320   -214       C  
ATOM   1153  NE  ARG A 130       5.418   4.476  -0.342  1.00 20.01           N  
ANISOU 1153  NE  ARG A 130     3363   2054   2183    -84   -337    312       N  
ATOM   1154  CZ  ARG A 130       5.490   5.782  -0.530  1.00 16.19           C  
ANISOU 1154  CZ  ARG A 130     3076   1983   1092    -71   -273    133       C  
ATOM   1155  NH1 ARG A 130       4.450   6.504  -0.351  1.00 16.77           N  
ANISOU 1155  NH1 ARG A 130     3245   2213    913    -69   -165     70       N  
ATOM   1156  NH2 ARG A 130       6.626   6.322  -0.899  1.00 19.62           N  
ANISOU 1156  NH2 ARG A 130     3530   2656   1265   -115    244    500       N  
ATOM   1157  N   ALA A 131       0.815   1.660   2.769  1.00 15.10           N  
ANISOU 1157  N   ALA A 131     2719   1744   1274   -197   -385   -224       N  
ATOM   1158  CA  ALA A 131      -0.490   1.075   3.058  1.00 18.72           C  
ANISOU 1158  CA  ALA A 131     2899   2130   2083   -258   -336   -128       C  
ATOM   1159  C   ALA A 131      -1.124   0.543   1.782  1.00 21.44           C  
ANISOU 1159  C   ALA A 131     3196   2358   2590   -340   -350   -139       C  
ATOM   1160  O   ALA A 131      -0.721   0.956   0.699  1.00 22.42           O  
ANISOU 1160  O   ALA A 131     3348   2640   2530   -369   -808    -41       O  
ATOM   1161  CB  ALA A 131      -1.377   2.088   3.806  1.00 21.27           C  
ANISOU 1161  CB  ALA A 131     3064   2482   2533   -292    -95   -144       C  
TER    1162      ALA A 131                                                      
HETATM 1163  CAAAFBZ A 133       7.319   8.707  17.358  0.50 19.36           C  
ANISOU 1163  CAAAFBZ A 133     3012   2713   1631    150    -18   1043       C  
HETATM 1164  CAABFBZ A 133       7.670   8.115  17.789  0.50 17.24           C  
ANISOU 1164  CAABFBZ A 133     3225   1893   1431    253   -353   -716       C  
HETATM 1165  OABAFBZ A 133       5.635   7.109  15.177  0.50 18.90           O  
ANISOU 1165  OABAFBZ A 133     3578   1772   1828     60    219    283       O  
HETATM 1166  OABBFBZ A 133       5.676   7.157  15.235  0.50 17.64           O  
ANISOU 1166  OABBFBZ A 133     3420   2075   1207    274    -84   -257       O  
HETATM 1167  OACAFBZ A 133       5.926   4.939  15.490  0.50 19.29           O  
ANISOU 1167  OACAFBZ A 133     3884   1939   1503    297     93     -5       O  
HETATM 1168  OACBFBZ A 133       6.126   5.002  15.267  0.50 16.26           O  
ANISOU 1168  OACBFBZ A 133     3781   1949    448    709   -541   -494       O  
HETATM 1169  CADAFBZ A 133       6.004   7.792  22.273  0.50 20.69           C  
ANISOU 1169  CADAFBZ A 133     2930   2673   2255    130    189   -210       C  
HETATM 1170  CADBFBZ A 133       5.407   7.397  22.237  0.50 17.14           C  
ANISOU 1170  CADBFBZ A 133     3194   2117   1199    421   -295   -579       C  
HETATM 1171  CAEAFBZ A 133       5.131   8.523  21.468  0.50 21.30           C  
ANISOU 1171  CAEAFBZ A 133     3075   2862   2155    117    219     -2       C  
HETATM 1172  CAEBFBZ A 133       4.440   7.066  21.291  0.50 17.59           C  
ANISOU 1172  CAEBFBZ A 133     3120   2252   1310    451   -230   -420       C  
HETATM 1173  CAFAFBZ A 133       6.979   7.028  21.642  0.50 20.05           C  
ANISOU 1173  CAFAFBZ A 133     2984   2874   1760    290   -144   -268       C  
HETATM 1174  CAFBFBZ A 133       6.672   7.775  21.776  0.50 17.72           C  
ANISOU 1174  CAFBFBZ A 133     3163   2376   1192    196   -531   -857       C  
HETATM 1175  CAGAFBZ A 133       5.206   8.521  20.079  0.50 20.59           C  
ANISOU 1175  CAGAFBZ A 133     3099   2590   2134    167     58   -167       C  
HETATM 1176  CAGBFBZ A 133       4.700   7.125  19.931  0.50 17.27           C  
ANISOU 1176  CAGBFBZ A 133     2999   2270   1289    374   -324   -275       C  
HETATM 1177  CAHAFBZ A 133       7.051   7.021  20.243  0.50 20.23           C  
ANISOU 1177  CAHAFBZ A 133     3111   2835   1738    151   -156   -511       C  
HETATM 1178  CAHBFBZ A 133       6.941   7.835  20.406  0.50 18.60           C  
ANISOU 1178  CAHBFBZ A 133     3253   2568   1244    361   -582   -615       C  
HETATM 1179  CAIAFBZ A 133       6.523   6.357  17.312  0.50 19.46           C  
ANISOU 1179  CAIAFBZ A 133     3373   2155   1863    184    168    228       C  
HETATM 1180  CAIBFBZ A 133       6.179   6.138  17.358  0.50 16.08           C  
ANISOU 1180  CAIBFBZ A 133     3130   2063    916    351   -325   -576       C  
HETATM 1181  CAJAFBZ A 133       5.988   6.129  15.874  0.50 18.80           C  
ANISOU 1181  CAJAFBZ A 133     3635   1802   1703     51    173    480       C  
HETATM 1182  CAJBFBZ A 133       6.014   6.112  15.824  0.50 15.91           C  
ANISOU 1182  CAJBFBZ A 133     3290   1898    855    277   -295   -517       C  
HETATM 1183  CAKAFBZ A 133       6.184   7.770  19.438  0.50 20.10           C  
ANISOU 1183  CAKAFBZ A 133     3134   2494   2006    179     -6   -143       C  
HETATM 1184  CAKBFBZ A 133       5.960   7.510  19.488  0.50 16.42           C  
ANISOU 1184  CAKBFBZ A 133     2972   2233   1032    427   -415   -613       C  
HETATM 1185  CALAFBZ A 133       6.241   7.766  17.885  0.50 20.53           C  
ANISOU 1185  CALAFBZ A 133     3282   2401   2117     73    249     88       C  
HETATM 1186  CALBFBZ A 133       6.267   7.554  18.001  0.50 16.96           C  
ANISOU 1186  CALBFBZ A 133     3272   2246    927    322   -177   -853       C  
HETATM 1187  O   HOH A 134      10.455  22.054  12.801  1.00  9.68           O  
ANISOU 1187  O   HOH A 134     2346   1032    298     45     18     73       O  
HETATM 1188  O   HOH A 135      18.691   0.008  22.066  1.00 11.73           O  
ANISOU 1188  O   HOH A 135     2394   1239    823    208    -75     84       O  
HETATM 1189  O   HOH A 136       2.745  -7.735  16.893  1.00 39.72           O  
ANISOU 1189  O   HOH A 136     6034   4803   4253   1312   -836  -1828       O  
HETATM 1190  O   HOH A 137       6.281  23.748  -4.014  1.00 42.77           O  
ANISOU 1190  O   HOH A 137     4664   6272   5315    424   -230    801       O  
HETATM 1191  O   HOH A 138       7.220  24.848  12.379  1.00 11.52           O  
ANISOU 1191  O   HOH A 138     2225   1593    556    -37     48   -320       O  
HETATM 1192  O   HOH A 139      20.117  16.981  24.217  1.00 45.36           O  
ANISOU 1192  O   HOH A 139     5173   4090   7971   -240  -1532    969       O  
HETATM 1193  O   HOH A 140      -3.785  -0.601  22.289  1.00 12.93           O  
ANISOU 1193  O   HOH A 140     2556   1621    733   -248    -88    246       O  
HETATM 1194  O   HOH A 141       1.107  20.239   5.139  1.00 14.89           O  
ANISOU 1194  O   HOH A 141     2782   2004    870   -116   -207    314       O  
HETATM 1195  O   HOH A 142      -3.731  -1.145  19.583  1.00 13.97           O  
ANISOU 1195  O   HOH A 142     2408   1806   1092   -441     74    246       O  
HETATM 1196  O   HOH A 143      -8.225   5.546  21.604  1.00 45.80           O  
ANISOU 1196  O   HOH A 143     3725   7987   5688  -1237    405   1498       O  
HETATM 1197  O   HOH A 144       8.595  21.595  26.655  1.00 68.64           O  
ANISOU 1197  O   HOH A 144    16849   5599   3630   2524  -2319  -1690       O  
HETATM 1198  O   HOH A 145       6.313  19.934  29.712  1.00105.05           O  
ANISOU 1198  O   HOH A 145    18034  17780   4099   5741   1291    523       O  
HETATM 1199  O   HOH A 146      11.877  12.407  12.160  1.00 11.51           O  
ANISOU 1199  O   HOH A 146     2748   1231    393    123    233     60       O  
HETATM 1200  O   HOH A 147       1.800   3.883  19.630  1.00 34.68           O  
ANISOU 1200  O   HOH A 147     5302   4951   2923    257    258   1324       O  
HETATM 1201  O   HOH A 148      -6.866   5.144  23.866  1.00 88.16           O  
ANISOU 1201  O   HOH A 148    18241   8832   6422  -5580   3262  -3958       O  
HETATM 1202  O   HOH A 149      -3.562   3.185  28.808  1.00 30.99           O  
ANISOU 1202  O   HOH A 149     4917   3846   3008     28  -1140    135       O  
HETATM 1203  O   HOH A 150       9.781  23.013   5.438  1.00 13.95           O  
ANISOU 1203  O   HOH A 150     2600   2210    490    315    -50     42       O  
HETATM 1204  O   HOH A 151       0.049  -2.559   9.802  1.00 32.86           O  
ANISOU 1204  O   HOH A 151     3717   4612   4156  -1244   -745   1379       O  
HETATM 1205  O   HOH A 152      -4.667  -2.372  24.206  1.00 11.83           O  
ANISOU 1205  O   HOH A 152     2446   1503    545    -64    -81    240       O  
HETATM 1206  O   HOH A 153       1.710   5.759   0.130  1.00 16.90           O  
ANISOU 1206  O   HOH A 153     3593   2000    827   -349   -194   -246       O  
HETATM 1207  O   HOH A 154      -4.982   3.751  30.948  1.00 36.04           O  
ANISOU 1207  O   HOH A 154     6273   3634   3786    261    997    466       O  
HETATM 1208  O   HOH A 155       4.704  -3.545  16.263  1.00 53.00           O  
ANISOU 1208  O   HOH A 155     5425   4837   9873   1097  -2017   1278       O  
HETATM 1209  O   HOH A 156       3.114   8.276  30.910  1.00 25.74           O  
ANISOU 1209  O   HOH A 156     4468   2662   2650    436    512    553       O  
HETATM 1210  O   HOH A 157       3.521  11.395  19.314  1.00 16.02           O  
ANISOU 1210  O   HOH A 157     2856   2219   1010   -187    270    197       O  
HETATM 1211  O   HOH A 158       8.872  10.506  21.424  1.00 14.52           O  
ANISOU 1211  O   HOH A 158     3166   1609    741   -185    258    124       O  
HETATM 1212  O   HOH A 159       8.845  -3.027  20.091  1.00 17.71           O  
ANISOU 1212  O   HOH A 159     3454   2242   1030     88    -20   -322       O  
HETATM 1213  O   HOH A 160      -0.597  14.332   6.411  1.00 15.73           O  
ANISOU 1213  O   HOH A 160     3253   1653   1070      1   -225     27       O  
HETATM 1214  O   HOH A 161      21.846   9.918   5.449  1.00 33.20           O  
ANISOU 1214  O   HOH A 161     3712   5216   3683    299   1009   -633       O  
HETATM 1215  O   HOH A 162      12.453  10.484  31.531  1.00140.81           O  
ANISOU 1215  O   HOH A 162    30132  15157   8212 -11415   -858  -1690       O  
HETATM 1216  O   HOH A 163       1.703  15.760  -0.147  1.00 18.93           O  
ANISOU 1216  O   HOH A 163     4462   2096    636   -169   -683   -221       O  
HETATM 1217  O   HOH A 164       5.886  -7.408  13.349  1.00 38.42           O  
ANISOU 1217  O   HOH A 164     5616   2630   6351   -947  -2048   1162       O  
HETATM 1218  O   HOH A 165      18.177   0.833   1.685  1.00 37.98           O  
ANISOU 1218  O   HOH A 165     3872   8216   2342    -62    673   -448       O  
HETATM 1219  O   HOH A 166       4.406  -4.502  26.339  1.00 44.34           O  
ANISOU 1219  O   HOH A 166     7158   7231   2457   1185   1131    281       O  
HETATM 1220  O   HOH A 167      16.210  18.837  14.202  1.00 17.80           O  
ANISOU 1220  O   HOH A 167     3592   2059   1111   -140   -233    -62       O  
HETATM 1221  O   HOH A 168      13.106  21.646  19.888  1.00 17.62           O  
ANISOU 1221  O   HOH A 168     3297   2814    583   -253    -89     27       O  
HETATM 1222  O   HOH A 169       6.396  11.418  19.573  1.00 15.88           O  
ANISOU 1222  O   HOH A 169     2864   1791   1377   -144    148     56       O  
HETATM 1223  O   HOH A 170      13.100  12.122  -3.273  1.00 63.91           O  
ANISOU 1223  O   HOH A 170    11696   7126   5460  -1740   -757    145       O  
HETATM 1224  O   HOH A 171      16.389  21.123   7.295  1.00 18.19           O  
ANISOU 1224  O   HOH A 171     3855   1614   1442   -412     78    207       O  
HETATM 1225  O   HOH A 172      15.233   9.057   3.243  1.00 18.25           O  
ANISOU 1225  O   HOH A 172     3906   1883   1145   -558    488    118       O  
HETATM 1226  O   HOH A 173       4.141  27.136   2.505  1.00 17.62           O  
ANISOU 1226  O   HOH A 173     3271   2043   1381     51   -209     17       O  
HETATM 1227  O   HOH A 174      14.490   0.676  31.721  1.00 29.44           O  
ANISOU 1227  O   HOH A 174     4880   4072   2233   -133   -265    932       O  
HETATM 1228  O   HOH A 175      20.161  20.241  14.212  1.00 25.36           O  
ANISOU 1228  O   HOH A 175     4523   2671   2441     53    116   -326       O  
HETATM 1229  O   HOH A 176       1.429   2.512  -2.579  1.00 39.05           O  
ANISOU 1229  O   HOH A 176     6417   6156   2263    787   -471  -1260       O  
HETATM 1230  O   HOH A 177      -5.951   3.201  27.293  1.00 29.56           O  
ANISOU 1230  O   HOH A 177     3773   3339   4117   -360   -237   -523       O  
HETATM 1231  O   HOH A 178      11.465  -3.105  13.710  1.00 19.03           O  
ANISOU 1231  O   HOH A 178     4403   1803   1023   -232    -49     84       O  
HETATM 1232  O   HOH A 179      14.045  -2.182  31.402  1.00 35.61           O  
ANISOU 1232  O   HOH A 179     5368   4648   3513   1101   1456    554       O  
HETATM 1233  O   HOH A 180       2.902  13.842  18.210  1.00 19.96           O  
ANISOU 1233  O   HOH A 180     3123   2095   2365   -285     50    275       O  
HETATM 1234  O   HOH A 181      18.960  17.860  14.834  1.00 30.91           O  
ANISOU 1234  O   HOH A 181     4741   3266   3736   -324   -871    201       O  
HETATM 1235  O   HOH A 182       2.622   6.759  13.707  1.00 20.31           O  
ANISOU 1235  O   HOH A 182     3374   1935   2408   -330    882   -275       O  
HETATM 1236  O   HOH A 183      19.778  20.030   4.928  1.00 46.93           O  
ANISOU 1236  O   HOH A 183     7244   3389   7196   -726  -1552   -203       O  
HETATM 1237  O   HOH A 184       2.882   0.886  18.682  1.00 20.72           O  
ANISOU 1237  O   HOH A 184     3034   3932    906  -1233    208   -122       O  
HETATM 1238  O   HOH A 185       1.898  12.695  14.263  1.00 21.31           O  
ANISOU 1238  O   HOH A 185     3925   2828   1343    -98    248   1191       O  
HETATM 1239  O   HOH A 186       1.674  26.185   2.278  1.00 18.15           O  
ANISOU 1239  O   HOH A 186     3239   1843   1813    111    -88   -229       O  
HETATM 1240  O   HOH A 187       7.028  27.670  11.942  1.00 20.26           O  
ANISOU 1240  O   HOH A 187     2962   2669   2065    773   -511   -485       O  
HETATM 1241  O   HOH A 188      -0.644  18.705   3.772  1.00 19.74           O  
ANISOU 1241  O   HOH A 188     3796   1877   1826     73  -1038    105       O  
HETATM 1242  O   HOH A 189       2.973   5.839  16.790  1.00 73.20           O  
ANISOU 1242  O   HOH A 189    13250  10320   4240  -2967   -116  -1820       O  
HETATM 1243  O   HOH A 190      14.722  25.125  17.374  1.00 16.90           O  
ANISOU 1243  O   HOH A 190     2945   1889   1585     -9   -601   -138       O  
HETATM 1244  O   HOH A 191      11.381  -2.746   0.864  1.00 18.74           O  
ANISOU 1244  O   HOH A 191     4166   1762   1193   -260    -44      2       O  
HETATM 1245  O   HOH A 192       2.225   9.807  17.398  1.00 17.93           O  
ANISOU 1245  O   HOH A 192     3281   2407   1123   -220    278     -7       O  
HETATM 1246  O   HOH A 193      11.517  -5.762  21.044  1.00 23.78           O  
ANISOU 1246  O   HOH A 193     4663   1204   3165     74    297    618       O  
HETATM 1247  O   HOH A 194      -6.097   0.823  22.091  1.00 18.77           O  
ANISOU 1247  O   HOH A 194     3086   1637   2405   -265   -867    519       O  
HETATM 1248  O   HOH A 195       0.232   3.005  34.679  1.00 23.81           O  
ANISOU 1248  O   HOH A 195     5753   2599    694    555    216    -73       O  
HETATM 1249  O   HOH A 196      20.255  11.058  20.158  1.00 39.89           O  
ANISOU 1249  O   HOH A 196     5678   3992   5486   -922   -501  -1088       O  
HETATM 1250  O   HOH A 197       6.306  -0.507   1.379  1.00 20.23           O  
ANISOU 1250  O   HOH A 197     3211   2989   1486   -116    412   -605       O  
HETATM 1251  O   HOH A 198       3.500   3.676  35.727  1.00 25.23           O  
ANISOU 1251  O   HOH A 198     5940   2600   1047  -1136   -297    165       O  
HETATM 1252  O   HOH A 199      22.695   6.191  29.193  1.00 43.53           O  
ANISOU 1252  O   HOH A 199     7814   2936   5788    296  -2537    993       O  
HETATM 1253  O  AHOH A 200       1.027  15.694  18.510  0.50 17.42           O  
ANISOU 1253  O  AHOH A 200     3981   2159    479   -410    434    118       O  
HETATM 1254  O  BHOH A 200       0.482  18.580  19.254  0.50 24.34           O  
ANISOU 1254  O  BHOH A 200     3661   2540   3047  -1077  -1852   1651       O  
HETATM 1255  O   HOH A 201      14.779   1.567  29.188  1.00 24.77           O  
ANISOU 1255  O   HOH A 201     3790   4471   1149   1031   -585    595       O  
HETATM 1256  O   HOH A 202       2.196  -3.676  24.702  1.00 23.80           O  
ANISOU 1256  O   HOH A 202     3329   4081   1630    581   -198   -158       O  
HETATM 1257  O   HOH A 203       8.675  -3.499  22.947  1.00 29.18           O  
ANISOU 1257  O   HOH A 203     6296   2266   2525   -841   1128   -488       O  
HETATM 1258  O   HOH A 204       5.171  22.595  24.114  1.00 24.32           O  
ANISOU 1258  O   HOH A 204     4725   2677   1838   1057    210    -22       O  
HETATM 1259  O   HOH A 205      15.406  19.770  27.364  1.00 24.31           O  
ANISOU 1259  O   HOH A 205     5891   2146   1199   -710   -789   -196       O  
HETATM 1260  O   HOH A 206       0.496   5.041  32.287  1.00 22.73           O  
ANISOU 1260  O   HOH A 206     4770   2785   1081   -279    234    -82       O  
HETATM 1261  O   HOH A 207       0.276   3.416  -0.275  1.00 21.46           O  
ANISOU 1261  O   HOH A 207     3585   2297   2268   -183   -773   -487       O  
HETATM 1262  O   HOH A 208      -1.902  15.884  17.808  1.00 24.41           O  
ANISOU 1262  O   HOH A 208     5391   2321   1560   -276    862   -669       O  
HETATM 1263  O   HOH A 209      17.845  13.911  21.772  1.00 20.67           O  
ANISOU 1263  O   HOH A 209     3594   3068   1192   -228   -111   -433       O  
HETATM 1264  O   HOH A 210      11.324  13.592  -5.357  1.00 45.18           O  
ANISOU 1264  O   HOH A 210     4984   3635   8545   -544   2100  -1355       O  
HETATM 1265  O   HOH A 211       6.576   8.372  12.992  1.00 21.00           O  
ANISOU 1265  O   HOH A 211     3325   3779    874   -575     47    159       O  
HETATM 1266  O   HOH A 212      -2.673  20.049   1.501  1.00 26.72           O  
ANISOU 1266  O   HOH A 212     4875   3601   1676  -2132    204    -53       O  
HETATM 1267  O   HOH A 213      15.386  -2.645   3.840  1.00 38.63           O  
ANISOU 1267  O   HOH A 213     8441   2451   3783    -36   1154   -128       O  
HETATM 1268  O   HOH A 214       2.851  -2.549  17.656  1.00 25.53           O  
ANISOU 1268  O   HOH A 214     4868   3150   1680    656   -754    199       O  
HETATM 1269  O   HOH A 215       7.012  -3.033  30.534  1.00 24.64           O  
ANISOU 1269  O   HOH A 215     6193   1802   1366   -370    955    -12       O  
HETATM 1270  O   HOH A 216       5.016  -1.572  25.409  1.00 23.14           O  
ANISOU 1270  O   HOH A 216     3820   3373   1600    459   -117   -471       O  
HETATM 1271  O   HOH A 217      13.187  21.173  28.471  1.00 25.65           O  
ANISOU 1271  O   HOH A 217     5384   2790   1569    228   -407   -275       O  
HETATM 1272  O   HOH A 218      18.327  11.294  24.301  1.00 31.54           O  
ANISOU 1272  O   HOH A 218     4228   1744   6009    386   -604    296       O  
HETATM 1273  O   HOH A 219       9.022  12.051  30.743  1.00 23.96           O  
ANISOU 1273  O   HOH A 219     5086   2753   1265    -23    643    344       O  
HETATM 1274  O   HOH A 220      17.543  13.416  28.020  1.00 26.60           O  
ANISOU 1274  O   HOH A 220     4312   2814   2980    442  -1092    572       O  
HETATM 1275  O   HOH A 221       4.823  10.044  29.236  1.00 24.29           O  
ANISOU 1275  O   HOH A 221     5723   2548    955   -271    113    504       O  
HETATM 1276  O   HOH A 222      18.765   4.770   2.368  1.00 27.39           O  
ANISOU 1276  O   HOH A 222     6869   3071    464    796   -554   -651       O  
HETATM 1277  O   HOH A 223      17.382   9.039  16.433  1.00 25.12           O  
ANISOU 1277  O   HOH A 223     4397   3151   1995    576     20    637       O  
HETATM 1278  O   HOH A 224      -7.181   9.454  19.644  1.00 33.25           O  
ANISOU 1278  O   HOH A 224     3400   7454   1777     74    429    -49       O  
HETATM 1279  O   HOH A 225      -1.888  20.176  11.480  1.00 35.86           O  
ANISOU 1279  O   HOH A 225     5466   2449   5710   -715   3383   -332       O  
HETATM 1280  O   HOH A 226      18.598  17.341   2.345  1.00 31.17           O  
ANISOU 1280  O   HOH A 226     5497   3667   2679   -220   1450   -733       O  
HETATM 1281  O   HOH A 227      -7.973   6.294  14.894  1.00 38.78           O  
ANISOU 1281  O   HOH A 227     5038   3190   6504  -1106  -1770    837       O  
HETATM 1282  O   HOH A 228       0.186   4.987  18.323  1.00 45.69           O  
ANISOU 1282  O   HOH A 228     6180   5501   5678  -2024  -1767   2338       O  
HETATM 1283  O   HOH A 229       2.408  -5.352  19.808  1.00 34.98           O  
ANISOU 1283  O   HOH A 229     5308   4919   3063    497   -193  -1205       O  
HETATM 1284  O   HOH A 230      -0.562  -5.133  17.441  1.00 33.60           O  
ANISOU 1284  O   HOH A 230     3772   2570   6422    352    968   1176       O  
HETATM 1285  O   HOH A 231      -4.800  11.591  13.359  1.00 33.49           O  
ANISOU 1285  O   HOH A 231     3963   6547   2214   1486    139   1259       O  
HETATM 1286  O   HOH A 232       7.530  -5.977  15.286  1.00 80.48           O  
ANISOU 1286  O   HOH A 232    10538  12355   7686  -6170  -7045   -452       O  
HETATM 1287  O   HOH A 233      19.735  10.033  17.639  1.00 30.90           O  
ANISOU 1287  O   HOH A 233     4804   3603   3332    846   1114    564       O  
HETATM 1288  O   HOH A 234      -7.692   6.520  19.026  1.00 31.28           O  
ANISOU 1288  O   HOH A 234     4084   3847   3953    364    576   -736       O  
HETATM 1289  O   HOH A 235      20.076  16.550  20.290  1.00 52.78           O  
ANISOU 1289  O   HOH A 235     5700   5686   8665    661   -123  -3854       O  
HETATM 1290  O   HOH A 236      23.782  11.638  18.115  1.00 42.02           O  
ANISOU 1290  O   HOH A 236     3294   6129   6542   -283    416  -1169       O  
HETATM 1291  O   HOH A 237       8.726  -6.070  20.158  1.00 34.62           O  
ANISOU 1291  O   HOH A 237     4693   4189   4272    786    664    -11       O  
HETATM 1292  O   HOH A 238       5.338  -1.772  19.859  1.00 36.95           O  
ANISOU 1292  O   HOH A 238     4304   4969   4765  -1778   2222  -2405       O  
HETATM 1293  O   HOH A 239      21.042   5.142  21.515  1.00 30.13           O  
ANISOU 1293  O   HOH A 239     6246   3234   1968   1457   -306    280       O  
HETATM 1294  O   HOH A 240      -6.869  13.782  18.029  1.00 47.09           O  
ANISOU 1294  O   HOH A 240     6348   4508   7036  -1096   2167  -2747       O  
HETATM 1295  O   HOH A 241       9.184  21.238  29.603  1.00 26.02           O  
ANISOU 1295  O   HOH A 241     5215   2969   1702   1136     56   -459       O  
HETATM 1296  O   HOH A 242       0.039   7.893  17.515  1.00 25.91           O  
ANISOU 1296  O   HOH A 242     3869   4367   1608    277    422    489       O  
HETATM 1297  O   HOH A 243      17.722   0.847  13.302  1.00 29.71           O  
ANISOU 1297  O   HOH A 243     3747   3458   4082   -122   1083   -608       O  
HETATM 1298  O   HOH A 244       0.880   7.214  -1.985  1.00 25.47           O  
ANISOU 1298  O   HOH A 244     4313   4119   1245   -197   -529    566       O  
HETATM 1299  O   HOH A 245      15.123   8.320  -0.936  1.00 24.67           O  
ANISOU 1299  O   HOH A 245     4940   2424   2008   -697    439   -116       O  
HETATM 1300  O   HOH A 246      21.160   7.942  15.070  1.00 45.14           O  
ANISOU 1300  O   HOH A 246     3754   5927   7469    618    999   2266       O  
HETATM 1301  O   HOH A 247      -2.215   4.503  -0.412  1.00 36.07           O  
ANISOU 1301  O   HOH A 247     4863   4499   4343   -855   -778   1421       O  
HETATM 1302  O   HOH A 248       5.842  -2.611  22.983  1.00 38.56           O  
ANISOU 1302  O   HOH A 248     5494   6846   2309   2244   -674   -905       O  
HETATM 1303  O   HOH A 249      16.473  -5.617  17.875  1.00 31.29           O  
ANISOU 1303  O   HOH A 249     4605   1957   5325    626  -1946  -1006       O  
HETATM 1304  O   HOH A 250       5.087  29.029   4.242  1.00 29.35           O  
ANISOU 1304  O   HOH A 250     4255   2724   4170   -633   -326  -1303       O  
HETATM 1305  O   HOH A 251      15.625   9.803   1.009  1.00 94.35           O  
ANISOU 1305  O   HOH A 251     7168  24866   3812  -5015   1799   5203       O  
HETATM 1306  O   HOH A 252      15.918  22.196   4.736  1.00 63.02           O  
ANISOU 1306  O   HOH A 252    13743   6233   3967  -4413  -1817   4561       O  
HETATM 1307  O   HOH A 253       5.194  19.261  -8.206  1.00 33.15           O  
ANISOU 1307  O   HOH A 253     3920   5609   3065    -26    116    303       O  
HETATM 1308  O   HOH A 254      19.681  14.785  18.344  1.00 26.87           O  
ANISOU 1308  O   HOH A 254     3078   3293   3837   -303    -87   1363       O  
HETATM 1309  O   HOH A 255       9.004  -3.969  -1.933  1.00 34.94           O  
ANISOU 1309  O   HOH A 255     7768   3388   2119  -1319    768   -196       O  
HETATM 1310  O   HOH A 256      11.184  22.268  26.602  1.00 32.10           O  
ANISOU 1310  O   HOH A 256     7341   3028   1827    -94    398   -315       O  
HETATM 1311  O   HOH A 257       6.189  19.155  -2.709  1.00 46.40           O  
ANISOU 1311  O   HOH A 257     8440   5739   3451   2690   2087   1249       O  
HETATM 1312  O   HOH A 258       8.824   4.952  32.755  1.00 26.93           O  
ANISOU 1312  O   HOH A 258     4575   2836   2821   -608  -1559    453       O  
HETATM 1313  O   HOH A 259      -7.859   9.805  22.474  1.00 52.62           O  
ANISOU 1313  O   HOH A 259     6816  10333   2842    552  -1183    856       O  
HETATM 1314  O   HOH A 260      20.724   4.395  17.579  1.00 33.71           O  
ANISOU 1314  O   HOH A 260     4561   4221   4025    669   1688   1968       O  
HETATM 1315  O   HOH A 261      10.741  -3.859  28.323  1.00 77.55           O  
ANISOU 1315  O   HOH A 261     7744   9496  12223   3430   1318   4660       O  
HETATM 1316  O   HOH A 262       6.249  12.303  16.699  1.00 31.04           O  
ANISOU 1316  O   HOH A 262     2701   7111   1982   -399    338   1449       O  
HETATM 1317  O   HOH A 263       9.329  14.977  -5.866  1.00 39.76           O  
ANISOU 1317  O   HOH A 263     5929   5082   4093      3   -158   1783       O  
HETATM 1318  O   HOH A 264      18.349  11.628  21.882  1.00 41.47           O  
ANISOU 1318  O   HOH A 264     3838   7289   4629   1650  -1235  -2723       O  
HETATM 1319  O   HOH A 265       2.530  -6.395  11.756  1.00 34.26           O  
ANISOU 1319  O   HOH A 265     5386   3945   3686   -525   1086    441       O  
HETATM 1320  O   HOH A 266       4.583  28.303   0.134  1.00 38.68           O  
ANISOU 1320  O   HOH A 266     8147   3725   2825   -943   -825   1111       O  
HETATM 1321  O  AHOH A 267       7.889   2.352  -2.875  0.50 24.99           O  
ANISOU 1321  O  AHOH A 267     4730   3034   1732   -290   -226    181       O  
HETATM 1322  O  BHOH A 267       9.611   3.093  -2.738  0.50 22.68           O  
ANISOU 1322  O  BHOH A 267     5258   1765   1595    292   -453   -494       O  
HETATM 1323  O   HOH A 268       9.421  28.808  15.294  1.00 23.05           O  
ANISOU 1323  O   HOH A 268     4149   2018   2589     66    357     83       O  
HETATM 1324  O   HOH A 269       3.218  21.290  23.989  1.00 35.06           O  
ANISOU 1324  O   HOH A 269     7662   3086   2571   1575   1794     40       O  
HETATM 1325  O   HOH A 270       3.972  16.612  -2.007  1.00 29.91           O  
ANISOU 1325  O   HOH A 270     5980   3533   1850   -959    413    173       O  
HETATM 1326  O   HOH A 271      17.666  21.238  14.942  1.00 23.86           O  
ANISOU 1326  O   HOH A 271     5029   2625   1411   -184   -638   -346       O  
HETATM 1327  O   HOH A 272      -9.448   4.024  20.676  1.00 22.88           O  
ANISOU 1327  O   HOH A 272     4855   2166   1671    500   1072    337       O  
HETATM 1328  O   HOH A 273      -3.765   1.768  15.050  1.00 23.02           O  
ANISOU 1328  O   HOH A 273     4091   2132   2521    420   1189    258       O  
HETATM 1329  O   HOH A 274      13.002  -7.467  20.088  1.00 43.08           O  
ANISOU 1329  O   HOH A 274     5732   2404   8230    813  -1166   -713       O  
HETATM 1330  O  AHOH A 275       4.484  11.673  14.838  0.50 23.95           O  
ANISOU 1330  O  AHOH A 275     4000   3413   1685    658   -800   -816       O  
HETATM 1331  O  BHOH A 275       4.123  13.245  15.571  0.50 25.30           O  
ANISOU 1331  O  BHOH A 275     5706   3019    888   -351   -240   -217       O  
HETATM 1332  O   HOH A 276      20.843   2.493  21.395  1.00 35.83           O  
ANISOU 1332  O   HOH A 276     4158   7085   2368   -150   -416  -1456       O  
HETATM 1333  O   HOH A 277      -3.663  17.977  23.869  1.00108.93           O  
ANISOU 1333  O   HOH A 277     3508  13818  24062   5342    906  -9142       O  
HETATM 1334  O   HOH A 278      20.488   4.934  28.349  0.50 16.76           O  
ANISOU 1334  O   HOH A 278     3462   2050    853     66   -205    335       O  
HETATM 1335  O   HOH A 279      17.221  21.153  17.700  1.00 30.20           O  
ANISOU 1335  O   HOH A 279     4475   5314   1685   -204   -348    129       O  
HETATM 1336  O  AHOH A 280      11.478  24.741   4.310  0.50 27.35           O  
ANISOU 1336  O  AHOH A 280     3455   5045   1891  -1618    581   1843       O  
HETATM 1337  O  BHOH A 280      12.706  25.401   6.083  0.50 23.12           O  
ANISOU 1337  O  BHOH A 280     6067   2161    555   -502     79    420       O  
HETATM 1338  O   HOH A 281      -1.531  14.222  21.851  1.00 31.26           O  
ANISOU 1338  O   HOH A 281     4224   5200   2452   -366    170   -404       O  
HETATM 1339  O   HOH A 282      18.341  -2.172  14.333  1.00 31.30           O  
ANISOU 1339  O   HOH A 282     4596   4143   3153   -190     25   1316       O  
HETATM 1340  O   HOH A 283      19.209  20.523   7.253  1.00 36.27           O  
ANISOU 1340  O   HOH A 283     6135   3405   4239  -1275   1764  -1675       O  
HETATM 1341  O   HOH A 284      -1.652   9.272  26.208  1.00 43.27           O  
ANISOU 1341  O   HOH A 284     6805   4642   4991    -80   2437     68       O  
HETATM 1342  O   HOH A 285       0.394   9.025  29.392  1.00 38.87           O  
ANISOU 1342  O   HOH A 285     7352   4468   2950   -994   1533    936       O  
HETATM 1343  O   HOH A 286      13.304  28.441   7.857  1.00 33.83           O  
ANISOU 1343  O   HOH A 286     5952   5175   1727   -441   -484   -743       O  
HETATM 1344  O   HOH A 287      11.822  -3.130  24.855  1.00 28.39           O  
ANISOU 1344  O   HOH A 287     6580   1965   2241   -230   1418    385       O  
HETATM 1345  O   HOH A 288       3.044  -2.319   1.125  1.00 33.38           O  
ANISOU 1345  O   HOH A 288     5236   3165   4282     81    102  -1973       O  
HETATM 1346  O   HOH A 289      12.340  -1.430  34.233  1.00 42.37           O  
ANISOU 1346  O   HOH A 289     6520   6621   2956   1741    428   2556       O  
HETATM 1347  O   HOH A 290      21.861  11.619   7.681  1.00 38.58           O  
ANISOU 1347  O   HOH A 290     4208   4608   5842   -556   -973   1615       O  
HETATM 1348  O   HOH A 291       6.543  21.653  -1.448  1.00 33.87           O  
ANISOU 1348  O   HOH A 291     6646   4162   2058   -344   1430   -436       O  
HETATM 1349  O   HOH A 292      12.823   6.160  32.965  1.00 63.17           O  
ANISOU 1349  O   HOH A 292     8834  12935   2231    -77  -3449  -2709       O  
HETATM 1350  O   HOH A 293      -4.078  11.781  25.808  1.00 41.59           O  
ANISOU 1350  O   HOH A 293     6129   5286   4385   -405    519    271       O  
HETATM 1351  O   HOH A 294      -2.719  -1.920   3.826  1.00 44.12           O  
ANISOU 1351  O   HOH A 294     5346   4798   6617  -2008   -477   -108       O  
HETATM 1352  O   HOH A 295      -2.362  18.880  16.062  1.00 41.50           O  
ANISOU 1352  O   HOH A 295     4039   5474   6252    766   1082  -1861       O  
HETATM 1353  O   HOH A 296      15.113   4.118  32.592  1.00 40.75           O  
ANISOU 1353  O   HOH A 296     7333   4978   3172   -527  -1145    227       O  
HETATM 1354  O   HOH A 297      17.167  12.467  30.593  1.00 37.09           O  
ANISOU 1354  O   HOH A 297     6074   5612   2406    970   -945    299       O  
HETATM 1355  O   HOH A 298      11.709  27.883   5.387  1.00 35.46           O  
ANISOU 1355  O   HOH A 298     6601   3820   3049      0    835    901       O  
HETATM 1356  O   HOH A 299      -2.052  12.843  23.427  1.00 39.97           O  
ANISOU 1356  O   HOH A 299     3648   5358   6180   -208    656   -437       O  
HETATM 1357  O   HOH A 300      10.106  -0.757  34.531  1.00 42.86           O  
ANISOU 1357  O   HOH A 300     5975   6819   3489    -27    -76   1404       O  
HETATM 1358  O   HOH A 301      12.908   2.673  33.505  1.00 43.36           O  
ANISOU 1358  O   HOH A 301     7265   6683   2524  -1122   -737    713       O  
HETATM 1359  O   HOH A 302      -4.585  11.790  28.960  1.00 55.41           O  
ANISOU 1359  O   HOH A 302     7743   7344   5964   1095  -1414  -1083       O  
HETATM 1360  O   HOH A 303       7.558  25.947  -0.868  1.00 36.34           O  
ANISOU 1360  O   HOH A 303     5360   6128   2317  -1373    259     67       O  
HETATM 1361  O   HOH A 304      10.159  -7.236  15.244  1.00 36.75           O  
ANISOU 1361  O   HOH A 304     5176   2765   6022    -79    -85    572       O  
HETATM 1362  O   HOH A 305       8.651  -4.143  32.601  1.00 39.83           O  
ANISOU 1362  O   HOH A 305     6942   4905   3287   -347   1956   -309       O  
HETATM 1363  O   HOH A 306      19.107  12.635  26.198  1.00 39.26           O  
ANISOU 1363  O   HOH A 306     6293   5476   3147     74    374    654       O  
HETATM 1364  O   HOH A 307      19.708  18.963  11.732  1.00 43.45           O  
ANISOU 1364  O   HOH A 307     4161   5659   6686   1804    463   1256       O  
HETATM 1365  O   HOH A 308       0.156  17.543  17.998  1.00 38.66           O  
ANISOU 1365  O   HOH A 308     5633   5739   3315    733   1674    662       O  
HETATM 1366  O   HOH A 309      13.435  -3.953   2.405  1.00 36.15           O  
ANISOU 1366  O   HOH A 309     6307   3359   4069   1299   -263   1241       O  
HETATM 1367  O   HOH A 310      10.800  18.261  34.067  1.00 35.93           O  
ANISOU 1367  O   HOH A 310     6500   5533   1615   -225    446    616       O  
HETATM 1368  O   HOH A 311      15.659  -5.277   4.676  1.00 42.89           O  
ANISOU 1368  O   HOH A 311     8228   4551   3515   1666    242   1169       O  
HETATM 1369  O   HOH A 312      -5.523  11.006  31.351  1.00 44.60           O  
ANISOU 1369  O   HOH A 312     6179   6127   4638    510   -967   1050       O  
HETATM 1370  O   HOH A 313       8.578  17.282  32.212  1.00 44.69           O  
ANISOU 1370  O   HOH A 313     6017   9342   1621   1419     68   -944       O  
HETATM 1371  O   HOH A 314      16.412  -1.008  17.606  1.00 29.12           O  
ANISOU 1371  O   HOH A 314     5970   3196   1895   1060  -1464   -134       O  
HETATM 1372  O   HOH A 315      -1.543   7.605  -0.427  1.00 29.25           O  
ANISOU 1372  O   HOH A 315     4938   4794   1380  -1362    157     46       O  
HETATM 1373  O   HOH A 316      10.113  21.406   2.977  1.00 41.62           O  
ANISOU 1373  O   HOH A 316     7265   5866   2683    759   1300   -711       O  
HETATM 1374  O   HOH A 317      23.326   2.144  20.506  1.00 23.04           O  
ANISOU 1374  O   HOH A 317     3482   2064   3208    110    687     99       O  
HETATM 1375  O   HOH A 318      10.384  -5.220   9.401  1.00 32.59           O  
ANISOU 1375  O   HOH A 318     7608   2904   1869    848    602   -230       O  
HETATM 1376  O   HOH A 319      -3.232  14.286  19.692  1.00 29.49           O  
ANISOU 1376  O   HOH A 319     4923   2933   3348   -440   1088   -555       O  
HETATM 1377  O   HOH A 320      10.175  28.742  19.922  1.00 41.24           O  
ANISOU 1377  O   HOH A 320     5169   6592   3908  -1140   -187  -2991       O  
HETATM 1378  O   HOH A 321      17.160   7.095   2.158  1.00 32.39           O  
ANISOU 1378  O   HOH A 321     6372   3297   2637  -1742   1604    -30       O  
HETATM 1379  O   HOH A 322       7.705   3.207  -0.669  1.00 31.76           O  
ANISOU 1379  O   HOH A 322     5619   4014   2435   1866   1528    995       O  
HETATM 1380  O   HOH A 323      -2.728   5.921  28.670  1.00 40.71           O  
ANISOU 1380  O   HOH A 323     5377   4367   5722    929  -1905  -1700       O  
HETATM 1381  O   HOH A 324       2.064  22.845  25.930  1.00 53.74           O  
ANISOU 1381  O   HOH A 324    10158   6457   3801   2778    279   4461       O  
HETATM 1382  O   HOH A 325       7.140  29.303  13.869  1.00 24.23           O  
ANISOU 1382  O   HOH A 325     4680   2618   1906    -65    122   -335       O  
HETATM 1383  O   HOH A 326       6.383   9.135  -1.784  1.00 21.50           O  
ANISOU 1383  O   HOH A 326     3757   2275   2135   -393    713   -455       O  
HETATM 1384  O   HOH A 327       4.918  16.969  29.671  1.00 28.32           O  
ANISOU 1384  O   HOH A 327     6569   2938   1252   -380    636    -89       O  
HETATM 1385  O   HOH A 328      21.630  17.943   4.649  1.00 43.28           O  
ANISOU 1385  O   HOH A 328     5778   2639   8027   -638   3777   -136       O  
HETATM 1386  O   HOH A 329      -2.286  19.497   6.726  1.00 33.31           O  
ANISOU 1386  O   HOH A 329     3941   4199   4515    154  -1369   1294       O  
HETATM 1387  O   HOH A 330       7.855  -6.494  17.894  1.00 36.04           O  
ANISOU 1387  O   HOH A 330     6429   3048   4216   -961  -1948   1500       O  
HETATM 1388  O   HOH A 331      15.761  26.181   8.680  1.00 31.63           O  
ANISOU 1388  O   HOH A 331     5455   4974   1586  -1642    -11   -166       O  
HETATM 1389  O   HOH A 332       2.991  12.169  29.996  1.00 33.64           O  
ANISOU 1389  O   HOH A 332     6394   4023   2363    665    -76    -46       O  
HETATM 1390  O   HOH A 333      16.031  23.272   8.578  1.00 35.14           O  
ANISOU 1390  O   HOH A 333     4336   3477   5538   -250   1483   -892       O  
HETATM 1391  O   HOH A 334       4.074   9.313  15.359  1.00 30.37           O  
ANISOU 1391  O   HOH A 334     6289   3022   2227   1409   1970    738       O  
HETATM 1392  O   HOH A 335       3.077  -4.636  22.477  1.00 33.30           O  
ANISOU 1392  O   HOH A 335     6209   3859   2583    583    341    686       O  
CONECT 1163 1185                                                                
CONECT 1164 1186                                                                
CONECT 1165 1181                                                                
CONECT 1166 1182                                                                
CONECT 1167 1181                                                                
CONECT 1168 1182                                                                
CONECT 1169 1171 1173                                                           
CONECT 1170 1172 1174                                                           
CONECT 1171 1169 1175                                                           
CONECT 1172 1170 1176                                                           
CONECT 1173 1169 1177                                                           
CONECT 1174 1170 1178                                                           
CONECT 1175 1171 1183                                                           
CONECT 1176 1172 1184                                                           
CONECT 1177 1173 1183                                                           
CONECT 1178 1174 1184                                                           
CONECT 1179 1181 1185                                                           
CONECT 1180 1182 1186                                                           
CONECT 1181 1165 1167 1179                                                      
CONECT 1182 1166 1168 1180                                                      
CONECT 1183 1175 1177 1185                                                      
CONECT 1184 1176 1178 1186                                                      
CONECT 1185 1163 1179 1183                                                      
CONECT 1186 1164 1180 1184                                                      
MASTER      342    0    1    3   10    0    2    6 1277    1   24   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.