CNRS Nantes University UFIP UFIP
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***  notail_Alba  ***

elNémo ID: 220127100209143361

Job options:

ID        	=	 220127100209143361
JOBID     	=	 notail_Alba
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 notail_Alba

HEADER    LIPID BINDING PROTEIN                   11-OCT-10   3P6E              
TITLE     HUMAN ADIPOCYTE LIPID-BINDING PROTEIN FABP4 IN COMPLEX WITH 3-(4-     
TITLE    2 METHOXYPHENYL) PROPIONIC ACID                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FATTY ACID-BINDING PROTEIN, ADIPOCYTE;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ADIPOCYTE LIPID-BINDING PROTEIN, ALBP, ADIPOCYTE-TYPE FATTY 
COMPND   5 ACID-BINDING PROTEIN, A-FABP, AFABP, FATTY ACID-BINDING PROTEIN 4;   
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: FABP4;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    LIPOCALIN, BETA BARREL, FATTY ACID BINDING PROTEIN, LIPID BINDING     
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.GONZALEZ,E.POZHARSKI                                              
REVDAT   3   25-FEB-15 3P6E    1       JRNL                                     
REVDAT   2   11-FEB-15 3P6E    1       JRNL                                     
REVDAT   1   13-APR-11 3P6E    0                                                
JRNL        AUTH   J.M.GONZALEZ,S.Z.FISHER                                      
JRNL        TITL   STRUCTURAL ANALYSIS OF IBUPROFEN BINDING TO HUMAN ADIPOCYTE  
JRNL        TITL 2 FATTY-ACID BINDING PROTEIN (FABP4).                          
JRNL        REF    ACTA CRYSTALLOGR F STRUCT     V.  71   163 2015              
JRNL        REF  2 BIOL COMMUN                                                  
JRNL        REFN                                                                
JRNL        PMID   25664790                                                     
JRNL        DOI    10.1107/S2053230X14027897                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.08 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.08                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.39                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 53671                          
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) : 0.167                           
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2719                            
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) : 1.08                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.11                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2851                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 156                          
REMARK   3   BIN FREE R VALUE                    : 0.2600                       
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          : 13                                      
REMARK   3   SOLVENT ATOMS            : 196                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.63000                                              
REMARK   3    B22 (A**2) : -0.40000                                             
REMARK   3    B33 (A**2) : -2.24000                                             
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): 0.031         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.461         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1238 ; 0.022 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):   847 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1678 ; 2.020 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2071 ; 0.996 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   169 ; 6.450 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    49 ;35.155 ;25.102       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   239 ;13.899 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;18.116 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   188 ; 0.130 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1408 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   240 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   765 ; 2.254 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   321 ; 0.749 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1248 ; 3.368 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   473 ; 4.538 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   422 ; 6.255 ; 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):  2085 ; 2.187 ; 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 3P6E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062013.                                      
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   : 53739                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.080                              
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     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.12200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.08                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 76.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
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       16.03650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.48900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.60300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.48900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.03650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.60300            
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   O    HOH A   172     O    HOH A   276              1.49            
REMARK 500   OD1  ASN A    15     O    HOH A   212              1.59            
REMARK 500   O    HOH A   272     O    HOH A   309              1.80            
REMARK 500   O    LYS A   120     O    HOH A   207              1.91            
REMARK 500   O    HOH A   201     O    HOH A   237              2.00            
REMARK 500   O    HOH A   185     O    HOH A   233              2.02            
REMARK 500   O    HOH A   293     O    HOH A   304              2.12            
REMARK 500   O    HOH A   194     O    HOH A   311              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   149     O    HOH A   272     3655     1.77            
REMARK 500   OE1  GLU A    14     O    HOH A   182     3645     1.80            
REMARK 500   O    HOH A   149     O    HOH A   286     3655     2.03            
REMARK 500   O    HOH A   164     O    HOH A   298     4455     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  78   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 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     -132.35     56.25                                   
REMARK 500    LYS A 120     -123.63     50.89                                   
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 301        DISTANCE =  9.26 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZGC 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: 3P6F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P6G   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P6H   RELATED DB: PDB                                   
DBREF  3P6E A    0   131  UNP    P15090   FABP4_HUMAN      1    132             
SEQADV 3P6E GLN A   -7  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6E GLN A   -6  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6E MET A   -5  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6E GLY A   -4  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6E ARG A   -3  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6E GLY A   -2  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6E 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    ZGC  A 133      26                                                       
HETNAM     ZGC 3-(4-METHOXYPHENYL)PROPANOIC ACID                                
FORMUL   2  ZGC    C10 H12 O3                                                   
FORMUL   3  HOH   *196(H2 O)                                                    
HELIX    1   1 SER A   -1  VAL A    5  1                                   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   1 1 GLY A   6  GLU A  14  0
SHEET    2   2 1 ASN A  39  ASN A  45  0
SHEET    3   3 1 VAL A  48  GLU A  54  0
SHEET    4   4 1 THR A  60  ILE A  65  0
SHEET    5   5 1 PHE A  70  VAL A  73  0
SHEET    6   6 1 LYS A  79  ASP A  87  0
SHEET    7   7 1 VAL A  90  TRP A  97  0
SHEET    8   8 1 LYS A 100  GLU A 109  0
SHEET    9   9 1 LYS A 112  MET A 119  0
SHEET   10  10 1 VAL A 122  ARG A 130  0
SITE     1 AC1  9 PHE A  16  MET A  20  ALA A  75  ASP A  76                    
SITE     2 AC1  9 CYS A 117  ARG A 126  TYR A 128  HOH A 162                    
SITE     3 AC1  9 HOH A 270                                                     
CRYST1   32.073   53.206   74.978  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      0.031179  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018795  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013337        0.00000                         
ATOM      1  N   SER A  -1       9.928  18.184  -4.151  1.00 17.09           N
ANISOU    1  N   SER A  -1      589   2817   3086   -183    -60    399       N
ATOM      2  CA  SER A  -1      11.033  18.269  -3.312  1.00 17.15           C
ANISOU    2  CA  SER A  -1      817   2506   3193   -104    -14    331       C
ATOM      3  C   SER A  -1      11.525  16.891  -2.883  1.00 16.50           C
ANISOU    3  C   SER A  -1     1046   2406   2816   -191     34    439       C
ATOM      4  O   SER A  -1      10.851  15.873  -3.041  1.00 17.47           O
ANISOU    4  O   SER A  -1     1285   2469   2882   -454   -127    652       O
ATOM      5  CB  SER A  -1      10.738  19.108  -2.081  1.00 19.67           C
ANISOU    5  CB  SER A  -1     1409   2770   3294    -25     59    345       C
ATOM      6  OG  SER A  -1      10.000  18.365  -1.170  1.00 27.01           O
ANISOU    6  OG  SER A  -1     2686   3636   3938   -268    559    -10       O
ATOM      7  N   MET A   0      12.704  16.858  -2.320  1.00 17.24           N
ANISOU    7  N   MET A   0     1276   2414   2858   -119      8    337       N
ATOM      8  CA AMET A   0      13.225  15.568  -1.916  0.50 16.38           C
ANISOU    8  CA AMET A   0     1080   2376   2767   -265     24    321       C
ATOM      9  CA BMET A   0      13.275  15.607  -1.828  0.50 16.83           C
ANISOU    9  CA BMET A   0     1158   2425   2811   -189     24    312       C
ATOM     10  C   MET A   0      12.293  14.915  -0.880  1.00 16.76           C
ANISOU   10  C   MET A   0     1029   2460   2876   -149     31    287       C
ATOM     11  O   MET A   0      12.187  13.721  -0.859  1.00 17.16           O
ANISOU   11  O   MET A   0     1015   2472   3032   -211    174    481       O
ATOM     12  CB AMET A   0      14.672  15.677  -1.465  0.50 16.14           C
ANISOU   12  CB AMET A   0      879   2523   2728   -267    -62    209       C
ATOM     13  CB BMET A   0      14.610  15.874  -1.133  0.50 17.09           C
ANISOU   13  CB BMET A   0     1006   2619   2868   -144      4    183       C
ATOM     14  CG AMET A   0      15.218  14.379  -0.921  0.50 17.00           C
ANISOU   14  CG AMET A   0      891   2610   2958   -254   -184    158       C
ATOM     15  CG BMET A   0      15.509  14.648  -1.105  0.50 19.46           C
ANISOU   15  CG BMET A   0     1617   2729   3047    189    -96    231       C
ATOM     16  SD AMET A   0      14.934  14.269   0.838  0.50 19.20           S
ANISOU   16  SD AMET A   0     1406   2792   3097    384   -394    268       S
ATOM     17  SD BMET A   0      16.488  14.404   0.395  0.50 24.27           S
ANISOU   17  SD BMET A   0     2604   3082   3534    640   -745    -76       S
ATOM     18  CE AMET A   0      15.023  12.512   1.083  0.50 20.43           C
ANISOU   18  CE AMET A   0     1953   2616   3191   -129   -479    124       C
ATOM     19  CE BMET A   0      15.464  15.229   1.565  0.50 25.01           C
ANISOU   19  CE BMET A   0     2384   3237   3880    294   -542   -188       C
ATOM     20  N   CYS A   1      11.647  15.708  -0.038  1.00 17.25           N
ANISOU   20  N   CYS A   1     1326   2443   2783   -101     31    316       N
ATOM     21  CA ACYS A   1      10.692  15.212   0.988  0.50 17.46           C
ANISOU   21  CA ACYS A   1     1266   2612   2756    -52    110    287       C
ATOM     22  CA BCYS A   1      10.717  15.164   0.998  0.50 18.78           C
ANISOU   22  CA BCYS A   1     1536   2663   2937    -57    116    333       C
ATOM     23  C   CYS A   1       9.466  14.468   0.432  1.00 16.13           C
ANISOU   23  C   CYS A   1      930   2468   2729     85    220    385       C
ATOM     24  O   CYS A   1       8.758  13.741   1.150  1.00 16.46           O
ANISOU   24  O   CYS A   1     1411   2110   2731    130    350    538       O
ATOM     25  CB ACYS A   1      10.282  16.350   1.910  0.50 18.26           C
ANISOU   25  CB ACYS A   1     1316   2732   2888     45    -10    243       C
ATOM     26  CB BCYS A   1      10.330  16.218   2.033  0.50 20.41           C
ANISOU   26  CB BCYS A   1     1691   2922   3141    -39     66    234       C
ATOM     27  SG ACYS A   1      11.612  16.709   3.059  0.50 22.19           S
ANISOU   27  SG ACYS A   1     1377   3807   3247   -303     18   -325       S
ATOM     28  SG BCYS A   1       9.432  17.594   1.381  0.50 30.72           S
ANISOU   28  SG BCYS A   1     3348   3824   4501    202     48    119       S
ATOM     29  N   ASP A   2       9.277  14.590  -0.871  1.00 16.33           N
ANISOU   29  N   ASP A   2      857   2547   2799   -409    -78    497       N
ATOM     30  CA  ASP A   2       8.335  13.784  -1.539  1.00 17.32           C
ANISOU   30  CA  ASP A   2      978   2742   2861   -553    -30    549       C
ATOM     31  C   ASP A   2       8.524  12.279  -1.360  1.00 16.04           C
ANISOU   31  C   ASP A   2      628   2810   2657   -498    -79    356       C
ATOM     32  O   ASP A   2       7.528  11.605  -1.414  1.00 17.46           O
ANISOU   32  O   ASP A   2     1074   2794   2766   -634   -128    370       O
ATOM     33  CB  ASP A   2       8.175  14.146  -3.016  1.00 18.52           C
ANISOU   33  CB  ASP A   2     1110   2901   3023   -752   -174    440       C
ATOM     34  CG  ASP A   2       7.552  15.532  -3.229  1.00 22.90           C
ANISOU   34  CG  ASP A   2     1997   3506   3197   -181   -258    687       C
ATOM     35  OD1 ASP A   2       6.857  16.103  -2.358  1.00 27.50           O
ANISOU   35  OD1 ASP A   2     2380   4130   3939    171   -171   1145       O
ATOM     36  OD2 ASP A   2       7.752  16.059  -4.313  1.00 26.59           O
ANISOU   36  OD2 ASP A   2     1334   4662   4104   -718   -197    829       O
ATOM     37  N   ALA A   3       9.736  11.827  -1.079  1.00 16.33           N
ANISOU   37  N   ALA A   3      965   2678   2559   -381    126    349       N
ATOM     38  CA  ALA A   3       9.958  10.403  -0.813  1.00 17.33           C
ANISOU   38  CA  ALA A   3     1453   2586   2546    -52    194    219       C
ATOM     39  C   ALA A   3       9.212   9.916   0.418  1.00 15.04           C
ANISOU   39  C   ALA A   3     1177   2134   2402   -174    113    187       C
ATOM     40  O   ALA A   3       8.994   8.724   0.552  1.00 16.05           O
ANISOU   40  O   ALA A   3     1500   2037   2558     33    368    -25       O
ATOM     41  CB  ALA A   3      11.449  10.135  -0.639  1.00 19.24           C
ANISOU   41  CB  ALA A   3     1404   2916   2991   -181    389    459       C
ATOM     42  N   PHE A   4       8.863  10.823   1.340  1.00 13.25           N
ANISOU   42  N   PHE A   4      781   1879   2371   -130    131     74       N
ATOM     43  CA  PHE A   4       8.179  10.432   2.576  1.00 12.20           C
ANISOU   43  CA  PHE A   4      638   1722   2273    -30    174     47       C
ATOM     44  C   PHE A   4       6.666  10.495   2.399  1.00 11.59           C
ANISOU   44  C   PHE A   4      847   1378   2178    -62    135    -11       C
ATOM     45  O   PHE A   4       5.929   9.924   3.195  1.00 12.46           O
ANISOU   45  O   PHE A   4      785   1585   2364    -92     45    201       O
ATOM     46  CB  PHE A   4       8.568  11.409   3.703  1.00 11.77           C
ANISOU   46  CB  PHE A   4      355   1674   2443   -138     94    155       C
ATOM     47  CG  PHE A   4       9.947  11.304   4.123  1.00 12.75           C
ANISOU   47  CG  PHE A   4      400   2073   2371    -92     54   -100       C
ATOM     48  CD1 PHE A   4      10.354  10.229   4.965  1.00 14.34           C
ANISOU   48  CD1 PHE A   4      261   2455   2731   -129     35    151       C
ATOM     49  CD2 PHE A   4      10.914  12.208   3.765  1.00 14.41           C
ANISOU   49  CD2 PHE A   4      346   2394   2734   -131    -29   -175       C
ATOM     50  CE1 PHE A   4      11.588  10.101   5.328  1.00 15.34           C
ANISOU   50  CE1 PHE A   4      781   2551   2494    -96    272     22       C
ATOM     51  CE2 PHE A   4      12.151  12.056   4.111  1.00 15.52           C
ANISOU   51  CE2 PHE A   4      369   2684   2841   -484    214     56       C
ATOM     52  CZ  PHE A   4      12.530  10.976   4.942  1.00 15.54           C
ANISOU   52  CZ  PHE A   4      709   2538   2658     89    107   -164       C
ATOM     53  N   VAL A   5       6.142  11.178   1.370  1.00 11.36           N
ANISOU   53  N   VAL A   5      662   1482   2172   -101     38     77       N
ATOM     54  CA  VAL A   5       4.734  11.440   1.264  1.00 11.94           C
ANISOU   54  CA  VAL A   5      672   1528   2335    -53     46    -31       C
ATOM     55  C   VAL A   5       3.971  10.181   0.963  1.00 13.26           C
ANISOU   55  C   VAL A   5      942   1677   2420   -120     70   -155       C
ATOM     56  O   VAL A   5       4.364   9.394   0.089  1.00 15.74           O
ANISOU   56  O   VAL A   5     1267   1910   2804   -352    411   -404       O
ATOM     57  CB  VAL A   5       4.473  12.505   0.168  1.00 12.96           C
ANISOU   57  CB  VAL A   5      699   1490   2733     34     24    151       C
ATOM     58  CG1 VAL A   5       3.001  12.587  -0.211  1.00 15.23           C
ANISOU   58  CG1 VAL A   5     1251   1814   2721    129    132    198       C
ATOM     59  CG2 VAL A   5       5.023  13.878   0.740  1.00 14.03           C
ANISOU   59  CG2 VAL A   5      924   1602   2805     20    -57    -38       C
ATOM     60  N   GLY A   6       2.856   9.996   1.625  1.00 12.36           N
ANISOU   60  N   GLY A   6      884   1555   2254   -127    123   -180       N
ATOM     61  CA  GLY A   6       1.993   8.906   1.362  1.00 13.60           C
ANISOU   61  CA  GLY A   6     1063   1813   2291   -104    -92   -118       C
ATOM     62  C   GLY A   6       1.363   8.391   2.622  1.00 12.34           C
ANISOU   62  C   GLY A   6      845   1711   2132   -189    -35    -73       C
ATOM     63  O   GLY A   6       1.263   9.091   3.593  1.00 12.71           O
ANISOU   63  O   GLY A   6      749   1666   2413   -204    174    -64       O
ATOM     64  N   THR A   7       0.879   7.161   2.533  1.00 12.24           N
ANISOU   64  N   THR A   7      684   1619   2347   -102    -16    -72       N
ATOM     65  CA  THR A   7       0.137   6.488   3.574  1.00 12.81           C
ANISOU   65  CA  THR A   7      835   1627   2402     12     67     23       C
ATOM     66  C   THR A   7       0.932   5.224   3.959  1.00 11.96           C
ANISOU   66  C   THR A   7      795   1386   2361    -26    -37     66       C
ATOM     67  O   THR A   7       1.180   4.380   3.107  1.00 13.46           O
ANISOU   67  O   THR A   7      851   1770   2494     60   -233   -133       O
ATOM     68  CB  THR A   7      -1.291   6.161   3.127  1.00 13.65           C
ANISOU   68  CB  THR A   7      573   1643   2968    -52    -16    222       C
ATOM     69  OG1 THR A   7      -1.861   7.276   2.447  1.00 17.08           O
ANISOU   69  OG1 THR A   7     1101   2011   3378     77   -169    170       O
ATOM     70  CG2 THR A   7      -2.127   5.701   4.300  1.00 18.06           C
ANISOU   70  CG2 THR A   7     1303   2238   3321   -172    262    178       C
ATOM     71  N   TRP A   8       1.232   5.132   5.238  1.00 11.53           N
ANISOU   71  N   TRP A   8      544   1536   2299    -54    168     83       N
ATOM     72  CA  TRP A   8       2.152   4.130   5.756  1.00 12.28           C
ANISOU   72  CA  TRP A   8      858   1458   2348     36     25    127       C
ATOM     73  C   TRP A   8       1.499   3.373   6.899  1.00 12.35           C
ANISOU   73  C   TRP A   8      772   1525   2395      0    111     80       C
ATOM     74  O   TRP A   8       0.671   3.940   7.596  1.00 16.20           O
ANISOU   74  O   TRP A   8     1870   1597   2684     18    665    271       O
ATOM     75  CB  TRP A   8       3.393   4.819   6.299  1.00 12.14           C
ANISOU   75  CB  TRP A   8      914   1448   2247    -94      5    226       C
ATOM     76  CG  TRP A   8       4.142   5.635   5.266  1.00 12.11           C
ANISOU   76  CG  TRP A   8     1004   1339   2258    -18     53     97       C
ATOM     77  CD1 TRP A   8       4.013   6.964   4.999  1.00 12.14           C
ANISOU   77  CD1 TRP A   8      656   1495   2461     18     -3   -114       C
ATOM     78  CD2 TRP A   8       5.132   5.148   4.370  1.00 10.99           C
ANISOU   78  CD2 TRP A   8      503   1427   2243     26    -44    157       C
ATOM     79  NE1 TRP A   8       4.873   7.340   4.012  1.00 11.89           N
ANISOU   79  NE1 TRP A   8      637   1440   2441   -234    178     59       N
ATOM     80  CE2 TRP A   8       5.576   6.234   3.604  1.00 11.81           C
ANISOU   80  CE2 TRP A   8      546   1707   2233   -117    106     18       C
ATOM     81  CE3 TRP A   8       5.690   3.899   4.115  1.00 12.66           C
ANISOU   81  CE3 TRP A   8      920   1615   2276    -65   -126     34       C
ATOM     82  CZ2 TRP A   8       6.559   6.085   2.652  1.00 12.97           C
ANISOU   82  CZ2 TRP A   8      988   1606   2331   -158     87    198       C
ATOM     83  CZ3 TRP A   8       6.658   3.759   3.154  1.00 13.40           C
ANISOU   83  CZ3 TRP A   8      877   1715   2498    218    -71    -12       C
ATOM     84  CH2 TRP A   8       7.061   4.829   2.426  1.00 12.98           C
ANISOU   84  CH2 TRP A   8      903   1831   2196     -4    142     -7       C
ATOM     85  N   LYS A   9       1.800   2.110   7.032  1.00 11.95           N
ANISOU   85  N   LYS A   9      735   1532   2272   -100    -32    264       N
ATOM     86  CA  LYS A   9       1.274   1.271   8.130  1.00 12.54           C
ANISOU   86  CA  LYS A   9      603   1746   2415   -248    -18    284       C
ATOM     87  C   LYS A   9       2.399   0.596   8.890  1.00 11.89           C
ANISOU   87  C   LYS A   9      662   1597   2257   -175    108     89       C
ATOM     88  O   LYS A   9       3.316   0.094   8.303  1.00 12.57           O
ANISOU   88  O   LYS A   9     1021   1578   2173   -118     36    127       O
ATOM     89  CB  LYS A   9       0.347   0.224   7.549  1.00 14.50           C
ANISOU   89  CB  LYS A   9      659   2192   2656   -352     93    479       C
ATOM     90  CG  LYS A   9       0.860  -0.762   6.648  1.00 22.01           C
ANISOU   90  CG  LYS A   9     2274   2808   3282   -395    -55    181       C
ATOM     91  CD  LYS A   9      -0.196  -1.731   6.232  1.00 27.33           C
ANISOU   91  CD  LYS A   9     3361   3167   3855   -595   -112     69       C
ATOM     92  CE  LYS A   9       0.443  -2.768   5.363  1.00 30.07           C
ANISOU   92  CE  LYS A   9     3743   3433   4249   -472    -43   -123       C
ATOM     93  NZ  LYS A   9       0.463  -2.358   3.942  1.00 33.85           N
ANISOU   93  NZ  LYS A   9     4189   4020   4651   -200    211    269       N
ATOM     94  N   LEU A  10       2.331   0.646  10.222  1.00 12.20           N
ANISOU   94  N   LEU A  10      359   1858   2419    -39     37    190       N
ATOM     95  CA  LEU A  10       3.364   0.014  11.028  1.00 12.57           C
ANISOU   95  CA  LEU A  10      304   1936   2535   -290     43     46       C
ATOM     96  C   LEU A  10       3.376  -1.537  10.862  1.00 12.29           C
ANISOU   96  C   LEU A  10      542   1790   2337   -446    -16    303       C
ATOM     97  O   LEU A  10       2.354  -2.131  11.027  1.00 15.60           O
ANISOU   97  O   LEU A  10     1000   2006   2919   -544   -155    423       O
ATOM     98  CB  LEU A  10       3.181   0.350  12.512  1.00 13.80           C
ANISOU   98  CB  LEU A  10      478   2136   2625   -208     76    159       C
ATOM     99  CG  LEU A  10       4.261  -0.169  13.437  1.00 13.75           C
ANISOU   99  CG  LEU A  10      358   2301   2564    -41    -50     89       C
ATOM    100  CD1 LEU A  10       5.568   0.486  13.196  1.00 14.90           C
ANISOU  100  CD1 LEU A  10      698   2314   2648    -94   -129    121       C
ATOM    101  CD2 LEU A  10       3.918   0.015  14.901  1.00 19.86           C
ANISOU  101  CD2 LEU A  10     1246   3956   2344    179    -31     10       C
ATOM    102  N   VAL A  11       4.518  -2.106  10.523  1.00 13.46           N
ANISOU  102  N   VAL A  11     1033   1597   2484   -249   -189    273       N
ATOM    103  CA  VAL A  11       4.621  -3.566  10.386  1.00 16.14           C
ANISOU  103  CA  VAL A  11     1549   1733   2850   -309   -489    156       C
ATOM    104  C   VAL A  11       5.526  -4.247  11.352  1.00 16.15           C
ANISOU  104  C   VAL A  11     1497   1699   2940   -320   -508    368       C
ATOM    105  O   VAL A  11       5.426  -5.455  11.519  1.00 19.83           O
ANISOU  105  O   VAL A  11     2362   1773   3398   -326   -904    463       O
ATOM    106  CB  VAL A  11       4.969  -3.968   8.965  1.00 17.69           C
ANISOU  106  CB  VAL A  11     1819   1726   3175    -23   -483     16       C
ATOM    107  CG1 VAL A  11       3.865  -3.535   8.032  1.00 19.29           C
ANISOU  107  CG1 VAL A  11     1805   2239   3282     47   -449     16       C
ATOM    108  CG2 VAL A  11       6.387  -3.508   8.526  1.00 19.70           C
ANISOU  108  CG2 VAL A  11     2225   2136   3122   -129   -387   -178       C
ATOM    109  N   SER A  12       6.469  -3.527  11.961  1.00 15.19           N
ANISOU  109  N   SER A  12     1433   1576   2762   -171   -475    301       N
ATOM    110  CA  SER A  12       7.307  -4.116  12.976  1.00 16.58           C
ANISOU  110  CA  SER A  12     1726   1739   2831     35   -391    284       C
ATOM    111  C   SER A  12       7.792  -3.085  13.912  1.00 15.00           C
ANISOU  111  C   SER A  12     1195   1827   2675   -423   -471    334       C
ATOM    112  O   SER A  12       7.943  -1.901  13.571  1.00 14.86           O
ANISOU  112  O   SER A  12     1280   1703   2664   -328   -260    376       O
ATOM    113  CB  SER A  12       8.426  -4.878  12.332  1.00 18.82           C
ANISOU  113  CB  SER A  12     1883   2189   3076     43   -452    187       C
ATOM    114  OG  SER A  12       9.405  -4.069  11.761  1.00 21.52           O
ANISOU  114  OG  SER A  12     1974   2936   3264     64   -266    373       O
ATOM    115  N   SER A  13       8.070  -3.539  15.122  1.00 16.05           N
ANISOU  115  N   SER A  13     1694   1662   2740   -612   -416    380       N
ATOM    116  CA  SER A  13       8.626  -2.653  16.159  1.00 16.13           C
ANISOU  116  CA  SER A  13     1669   1849   2611   -485   -495    515       C
ATOM    117  C   SER A  13       9.591  -3.483  17.005  1.00 16.02           C
ANISOU  117  C   SER A  13     1518   1927   2639   -447   -465    477       C
ATOM    118  O   SER A  13       9.289  -4.654  17.325  1.00 19.47           O
ANISOU  118  O   SER A  13     2170   2068   3156   -684   -753    674       O
ATOM    119  CB  SER A  13       7.427  -2.216  17.023  1.00 17.62           C
ANISOU  119  CB  SER A  13     1715   2164   2814   -465   -571    363       C
ATOM    120  OG  SER A  13       7.730  -1.309  18.062  1.00 20.15           O
ANISOU  120  OG  SER A  13     2248   2455   2952   -678   -855    369       O
ATOM    121  N   GLU A  14      10.705  -2.898  17.337  1.00 14.40           N
ANISOU  121  N   GLU A  14     1481   1543   2445   -233   -326    260       N
ATOM    122  CA  GLU A  14      11.666  -3.494  18.238  1.00 14.66           C
ANISOU  122  CA  GLU A  14     1548   1511   2509     94   -313     50       C
ATOM    123  C   GLU A  14      12.047  -2.519  19.346  1.00 12.41           C
ANISOU  123  C   GLU A  14      962   1528   2222    117   -254    152       C
ATOM    124  O   GLU A  14      12.314  -1.349  19.068  1.00 12.52           O
ANISOU  124  O   GLU A  14     1072   1363   2320     65    -56     27       O
ATOM    125  CB  GLU A  14      12.931  -3.844  17.465  1.00 17.09           C
ANISOU  125  CB  GLU A  14     1962   1926   2603    217   -378     45       C
ATOM    126  CG  GLU A  14      12.755  -5.026  16.503  1.00 23.14           C
ANISOU  126  CG  GLU A  14     3025   2401   3366    178   -282   -266       C
ATOM    127  CD  GLU A  14      12.709  -6.405  17.176  1.00 26.42           C
ANISOU  127  CD  GLU A  14     3884   2433   3721    -90   -379   -408       C
ATOM    128  OE1 GLU A  14      12.945  -6.551  18.392  1.00 28.83           O
ANISOU  128  OE1 GLU A  14     4010   2636   4305    103   -750   -328       O
ATOM    129  OE2 GLU A  14      12.367  -7.390  16.493  1.00 30.74           O
ANISOU  129  OE2 GLU A  14     4283   3029   4367    -78    -54   -908       O
ATOM    130  N   ASN A  15      12.027  -3.003  20.559  1.00 12.06           N
ANISOU  130  N   ASN A  15      862   1453   2266     71    -96     81       N
ATOM    131  CA AASN A  15      12.534  -2.279  21.745  0.50 11.13           C
ANISOU  131  CA AASN A  15      489   1470   2268    144   -143    172       C
ATOM    132  CA BASN A  15      12.516  -2.267  21.735  0.50 12.36           C
ANISOU  132  CA BASN A  15      719   1613   2362    114    -76    133       C
ATOM    133  C   ASN A  15      11.714  -1.041  22.085  1.00 11.19           C
ANISOU  133  C   ASN A  15      300   1609   2342    245    116    202       C
ATOM    134  O   ASN A  15      12.166  -0.183  22.832  1.00 12.26           O
ANISOU  134  O   ASN A  15      639   1556   2463     55   -113     57       O
ATOM    135  CB AASN A  15      14.003  -1.940  21.607  0.50 11.01           C
ANISOU  135  CB AASN A  15      497   1411   2274    292   -201    108       C
ATOM    136  CB BASN A  15      13.977  -1.937  21.591  0.50 13.40           C
ANISOU  136  CB BASN A  15      925   1733   2432    124   -111     62       C
ATOM    137  CG AASN A  15      14.745  -1.950  22.930  0.50 11.53           C
ANISOU  137  CG AASN A  15      763   1403   2215    168   -272    265       C
ATOM    138  CG BASN A  15      14.790  -3.154  21.349  0.50 16.50           C
ANISOU  138  CG BASN A  15      848   2497   2921    173     97    -31       C
ATOM    139  OD1AASN A  15      14.563  -2.847  23.731  0.50 11.87           O
ANISOU  139  OD1AASN A  15     1022   1465   2022    -29   -332    253       O
ATOM    140  OD1BASN A  15      14.953  -3.941  22.256  0.50 21.20           O
ANISOU  140  OD1BASN A  15     2466   2230   3359    166   -104   -190       O
ATOM    141  ND2AASN A  15      15.566  -0.928  23.173  0.50 10.51           N
ANISOU  141  ND2AASN A  15      266   1422   2304    116    -21    285       N
ATOM    142  ND2BASN A  15      15.246  -3.368  20.126  0.50 22.55           N
ANISOU  142  ND2BASN A  15     2387   2799   3381     79    364   -323       N
ATOM    143  N   PHE A  16      10.493  -0.969  21.642  1.00 11.60           N
ANISOU  143  N   PHE A  16      388   1409   2610    134    141     44       N
ATOM    144  CA  PHE A  16       9.686   0.200  21.892  1.00 12.25           C
ANISOU  144  CA  PHE A  16      567   1657   2430     18   -135     33       C
ATOM    145  C   PHE A  16       9.307   0.347  23.354  1.00 12.83           C
ANISOU  145  C   PHE A  16      302   1868   2704   -191    -46     66       C
ATOM    146  O   PHE A  16       9.205   1.480  23.871  1.00 12.38           O
ANISOU  146  O   PHE A  16      823   1534   2344    -45     29     -1       O
ATOM    147  CB  PHE A  16       8.474   0.223  20.964  1.00 13.19           C
ANISOU  147  CB  PHE A  16      964   1544   2502    171     95    100       C
ATOM    148  CG  PHE A  16       7.690   1.551  20.930  1.00 13.44           C
ANISOU  148  CG  PHE A  16      988   2113   2004    241    -97    -16       C
ATOM    149  CD1 PHE A  16       8.320   2.711  20.573  1.00 14.25           C
ANISOU  149  CD1 PHE A  16      983   1859   2571    463     51    137       C
ATOM    150  CD2 PHE A  16       6.350   1.599  21.179  1.00 14.77           C
ANISOU  150  CD2 PHE A  16      862   2267   2483    361   -182    -93       C
ATOM    151  CE1 PHE A  16       7.646   3.920  20.451  1.00 17.01           C
ANISOU  151  CE1 PHE A  16     1952   2081   2430    477   -412    -10       C
ATOM    152  CE2 PHE A  16       5.645   2.838  21.073  1.00 16.11           C
ANISOU  152  CE2 PHE A  16      759   2689   2671    625   -454   -251       C
ATOM    153  CZ  PHE A  16       6.299   3.965  20.703  1.00 17.15           C
ANISOU  153  CZ  PHE A  16     2007   1924   2584    620   -503   -127       C
ATOM    154  N   ASP A  17       9.040  -0.758  24.040  1.00 13.09           N
ANISOU  154  N   ASP A  17      914   1533   2525     39     93    163       N
ATOM    155  CA  ASP A  17       8.763  -0.678  25.480  1.00 13.83           C
ANISOU  155  CA  ASP A  17      810   1755   2688   -132    204    321       C
ATOM    156  C   ASP A  17       9.922  -0.077  26.237  1.00 12.57           C
ANISOU  156  C   ASP A  17      450   1738   2587   -276    -86    337       C
ATOM    157  O   ASP A  17       9.705   0.795  27.080  1.00 13.98           O
ANISOU  157  O   ASP A  17     1093   1816   2401   -111    154    235       O
ATOM    158  CB  ASP A  17       8.320  -2.048  26.047  1.00 15.71           C
ANISOU  158  CB  ASP A  17     1351   1814   2801   -210    107    216       C
ATOM    159  CG  ASP A  17       7.803  -1.925  27.442  1.00 19.02           C
ANISOU  159  CG  ASP A  17     2019   2213   2993   -222    214    617       C
ATOM    160  OD1 ASP A  17       8.486  -2.473  28.311  1.00 24.41           O
ANISOU  160  OD1 ASP A  17     2670   3480   3121    119   -263    411       O
ATOM    161  OD2 ASP A  17       6.760  -1.314  27.642  1.00 20.83           O
ANISOU  161  OD2 ASP A  17     2720   2456   2735    229    246    319       O
ATOM    162  N   ASP A  18      11.135  -0.501  25.957  1.00 12.77           N
ANISOU  162  N   ASP A  18      297   1728   2824     29    125    478       N
ATOM    163  CA  ASP A  18      12.290   0.018  26.589  1.00 13.64           C
ANISOU  163  CA  ASP A  18      338   2113   2731   -223     10    465       C
ATOM    164  C   ASP A  18      12.506   1.506  26.272  1.00 12.89           C
ANISOU  164  C   ASP A  18      586   1751   2559    -75    -75    193       C
ATOM    165  O   ASP A  18      12.903   2.264  27.151  1.00 13.40           O
ANISOU  165  O   ASP A  18      715   1915   2459    -29    -48    193       O
ATOM    166  CB  ASP A  18      13.562  -0.742  26.272  1.00 15.53           C
ANISOU  166  CB  ASP A  18      275   2312   3313   -206   -109    386       C
ATOM    167  CG  ASP A  18      13.793  -1.918  27.273  1.00 24.43           C
ANISOU  167  CG  ASP A  18     1857   3616   3807     22     99    748       C
ATOM    168  OD1 ASP A  18      14.904  -2.021  27.837  1.00 32.80           O
ANISOU  168  OD1 ASP A  18     3494   4345   4622    523   -165   1109       O
ATOM    169  OD2 ASP A  18      12.879  -2.692  27.444  1.00 30.24           O
ANISOU  169  OD2 ASP A  18     3236   3602   4651    247      8   1654       O
ATOM    170  N   TYR A  19      12.275   1.902  25.031  1.00 12.01           N
ANISOU  170  N   TYR A  19      630   1549   2383      3     95     16       N
ATOM    171  CA  TYR A  19      12.282   3.326  24.683  1.00 11.60           C
ANISOU  171  CA  TYR A  19      594   1471   2340     29    -22    144       C
ATOM    172  C   TYR A  19      11.323   4.136  25.496  1.00 11.08           C
ANISOU  172  C   TYR A  19      504   1566   2139     75    -36    118       C
ATOM    173  O   TYR A  19      11.658   5.160  26.059  1.00 11.70           O
ANISOU  173  O   TYR A  19      586   1658   2200     37     58     32       O
ATOM    174  CB  TYR A  19      12.073   3.447  23.167  1.00 11.91           C
ANISOU  174  CB  TYR A  19      610   1634   2278    -75    116     13       C
ATOM    175  CG  TYR A  19      11.839   4.898  22.754  1.00 10.99           C
ANISOU  175  CG  TYR A  19      348   1614   2211   -239    325    -23       C
ATOM    176  CD1 TYR A  19      12.900   5.753  22.668  1.00 11.30           C
ANISOU  176  CD1 TYR A  19      439   1801   2051    -10     18     16       C
ATOM    177  CD2 TYR A  19      10.567   5.355  22.503  1.00 12.18           C
ANISOU  177  CD2 TYR A  19      296   2023   2307   -153    158    -98       C
ATOM    178  CE1 TYR A  19      12.719   7.120  22.357  1.00 11.45           C
ANISOU  178  CE1 TYR A  19      671   1655   2022    -10    -27     56       C
ATOM    179  CE2 TYR A  19      10.420   6.788  22.168  1.00 13.18           C
ANISOU  179  CE2 TYR A  19      788   1926   2294    114   -109     -3       C
ATOM    180  CZ  TYR A  19      11.489   7.595  22.117  1.00 11.98           C
ANISOU  180  CZ  TYR A  19      782   1746   2023   -246    -16    -76       C
ATOM    181  OH  TYR A  19      11.227   8.906  21.778  1.00 13.35           O
ANISOU  181  OH  TYR A  19     1313   1512   2246      9    -87     99       O
ATOM    182  N   MET A  20      10.088   3.694  25.542  1.00 11.65           N
ANISOU  182  N   MET A  20      774   1554   2096      8    -24    177       N
ATOM    183  CA  MET A  20       9.054   4.403  26.276  1.00 12.35           C
ANISOU  183  CA  MET A  20      592   1816   2283    -42    164    153       C
ATOM    184  C   MET A  20       9.436   4.463  27.773  1.00 12.08           C
ANISOU  184  C   MET A  20      521   1898   2168    -84    184    178       C
ATOM    185  O   MET A  20       9.204   5.494  28.413  1.00 13.19           O
ANISOU  185  O   MET A  20     1009   1802   2199     40     63    -37       O
ATOM    186  CB  MET A  20       7.693   3.743  26.105  1.00 12.61           C
ANISOU  186  CB  MET A  20      814   1851   2124     37     93    199       C
ATOM    187  CG  MET A  20       7.011   4.004  24.725  1.00 13.32           C
ANISOU  187  CG  MET A  20     1037   1775   2247    199    182     72       C
ATOM    188  SD  MET A  20       5.354   3.522  24.665  1.00 14.55           S
ANISOU  188  SD  MET A  20      715   2317   2495     60     33     52       S
ATOM    189  CE  MET A  20       5.567   1.719  24.683  1.00 15.78           C
ANISOU  189  CE  MET A  20     1176   2088   2729   -341     69     -5       C
ATOM    190  N   LYS A  21       9.994   3.391  28.356  1.00 13.08           N
ANISOU  190  N   LYS A  21      901   1911   2157    -15    139    123       N
ATOM    191  CA  LYS A  21      10.386   3.422  29.764  1.00 14.16           C
ANISOU  191  CA  LYS A  21      935   2232   2213      8    269    159       C
ATOM    192  C   LYS A  21      11.460   4.497  29.928  1.00 14.49           C
ANISOU  192  C   LYS A  21     1049   2211   2246    -83    -67    206       C
ATOM    193  O   LYS A  21      11.429   5.245  30.916  1.00 16.52           O
ANISOU  193  O   LYS A  21     1594   2520   2161   -376    126     19       O
ATOM    194  CB  LYS A  21      10.974   2.052  30.167  1.00 15.51           C
ANISOU  194  CB  LYS A  21     1238   2325   2329    117    113    295       C
ATOM    195  CG  LYS A  21      10.015   0.996  30.452  1.00 18.86           C
ANISOU  195  CG  LYS A  21     1969   2670   2526    -91    -53    239       C
ATOM    196  CD  LYS A  21      10.688  -0.279  30.949  1.00 23.01           C
ANISOU  196  CD  LYS A  21     2685   2976   3079    220    -15    325       C
ATOM    197  CE  LYS A  21       9.701  -1.331  31.334  1.00 26.35           C
ANISOU  197  CE  LYS A  21     2808   3418   3786    344   -307    544       C
ATOM    198  NZ  LYS A  21      10.267  -2.621  31.749  1.00 31.50           N
ANISOU  198  NZ  LYS A  21     3478   4059   4429    920   -565    860       N
ATOM    199  N   GLU A  22      12.410   4.616  29.001  1.00 14.73           N
ANISOU  199  N   GLU A  22     1027   2371   2199   -179    -91     63       N
ATOM    200  CA  GLU A  22      13.488   5.565  29.109  1.00 15.49           C
ANISOU  200  CA  GLU A  22     1086   2499   2301   -227   -138     91       C
ATOM    201  C   GLU A  22      12.962   6.978  29.027  1.00 14.53           C
ANISOU  201  C   GLU A  22     1048   2187   2285   -258   -137     -3       C
ATOM    202  O   GLU A  22      13.433   7.882  29.725  1.00 16.44           O
ANISOU  202  O   GLU A  22     1268   2462   2516   -446   -254    -42       O
ATOM    203  CB  GLU A  22      14.555   5.292  28.055  1.00 15.20           C
ANISOU  203  CB  GLU A  22      822   2462   2489     -8    -42    126       C
ATOM    204  CG  GLU A  22      15.928   5.815  28.337  1.00 18.24           C
ANISOU  204  CG  GLU A  22     1144   2864   2921   -174   -120    226       C
ATOM    205  CD  GLU A  22      16.676   5.031  29.441  1.00 20.76           C
ANISOU  205  CD  GLU A  22     1487   3281   3117    -36   -177    468       C
ATOM    206  OE1 GLU A  22      16.180   4.018  29.938  1.00 23.73           O
ANISOU  206  OE1 GLU A  22     1736   3853   3425    -60   -434    294       O
ATOM    207  OE2 GLU A  22      17.821   5.384  29.787  1.00 26.08           O
ANISOU  207  OE2 GLU A  22     2389   3957   3561      5   -570    140       O
ATOM    208  N   VAL A  23      11.930   7.199  28.213  1.00 14.28           N
ANISOU  208  N   VAL A  23     1215   1864   2346   -122    -86     14       N
ATOM    209  CA  VAL A  23      11.245   8.468  28.066  1.00 14.21           C
ANISOU  209  CA  VAL A  23     1203   1941   2254   -225     55     30       C
ATOM    210  C   VAL A  23      10.493   8.839  29.342  1.00 15.81           C
ANISOU  210  C   VAL A  23     1655   1973   2378   -229     89    -73       C
ATOM    211  O   VAL A  23      10.405   9.998  29.646  1.00 18.57           O
ANISOU  211  O   VAL A  23     2559   2082   2415   -205    232   -156       O
ATOM    212  CB  VAL A  23      10.316   8.440  26.822  1.00 14.69           C
ANISOU  212  CB  VAL A  23     1395   1877   2309    -28    131     95       C
ATOM    213  CG1 VAL A  23       9.344   9.589  26.741  1.00 16.31           C
ANISOU  213  CG1 VAL A  23     1845   1859   2491    145     -1     -7       C
ATOM    214  CG2 VAL A  23      11.132   8.388  25.556  1.00 15.24           C
ANISOU  214  CG2 VAL A  23     1739   1735   2314    -90    110     20       C
ATOM    215  N   GLY A  24      10.031   7.857  30.107  1.00 15.28           N
ANISOU  215  N   GLY A  24     1796   1861   2148   -196    -40    -77       N
ATOM    216  CA  GLY A  24       9.269   8.082  31.339  1.00 15.59           C
ANISOU  216  CA  GLY A  24     1619   1949   2356   -367     10    -76       C
ATOM    217  C   GLY A  24       7.804   7.753  31.233  1.00 14.65           C
ANISOU  217  C   GLY A  24     1455   1784   2327   -369     64    -99       C
ATOM    218  O   GLY A  24       7.017   8.168  32.081  1.00 17.74           O
ANISOU  218  O   GLY A  24     2057   2193   2491   -295    263   -220       O
ATOM    219  N   VAL A  25       7.377   6.996  30.223  1.00 14.28           N
ANISOU  219  N   VAL A  25     1510   1704   2210   -176     70    -47       N
ATOM    220  CA  VAL A  25       5.958   6.664  30.034  1.00 13.56           C
ANISOU  220  CA  VAL A  25     1256   1640   2256    -87    103     -3       C
ATOM    221  C   VAL A  25       5.598   5.651  31.106  1.00 14.07           C
ANISOU  221  C   VAL A  25     1271   1878   2196   -364     36    -50       C
ATOM    222  O   VAL A  25       6.310   4.674  31.353  1.00 15.40           O
ANISOU  222  O   VAL A  25     1769   1845   2238   -379    -88    164       O
ATOM    223  CB  VAL A  25       5.779   6.052  28.666  1.00 12.30           C
ANISOU  223  CB  VAL A  25      573   1728   2371   -205    -50    166       C
ATOM    224  CG1 VAL A  25       4.359   5.766  28.451  1.00 14.16           C
ANISOU  224  CG1 VAL A  25     1260   1691   2427    -80    104    162       C
ATOM    225  CG2 VAL A  25       6.234   6.981  27.510  1.00 13.77           C
ANISOU  225  CG2 VAL A  25      860   1865   2505     23     76    352       C
ATOM    226  N   GLY A  26       4.456   5.864  31.709  1.00 15.29           N
ANISOU  226  N   GLY A  26     1327   2235   2245   -524    142    -24       N
ATOM    227  CA  GLY A  26       3.959   4.949  32.738  1.00 15.91           C
ANISOU  227  CA  GLY A  26     1433   2301   2310   -459    181   -129       C
ATOM    228  C   GLY A  26       3.415   3.623  32.236  1.00 15.18           C
ANISOU  228  C   GLY A  26     1291   2214   2262   -437     94    -10       C
ATOM    229  O   GLY A  26       3.171   3.455  31.072  1.00 15.28           O
ANISOU  229  O   GLY A  26     1352   2220   2232   -541     -2   -103       O
ATOM    230  N   PHE A  27       3.309   2.671  33.139  1.00 15.99           N
ANISOU  230  N   PHE A  27     1785   2253   2036   -463    -26    -83       N
ATOM    231  CA  PHE A  27       2.968   1.295  32.798  1.00 14.90           C
ANISOU  231  CA  PHE A  27     1348   2157   2153   -378     81    114       C
ATOM    232  C   PHE A  27       1.752   1.153  31.922  1.00 13.89           C
ANISOU  232  C   PHE A  27     1195   1776   2307   -415    -21    183       C
ATOM    233  O   PHE A  27       1.836   0.558  30.847  1.00 14.01           O
ANISOU  233  O   PHE A  27     1234   1851   2236   -414     74     58       O
ATOM    234  CB  PHE A  27       2.790   0.467  34.078  1.00 16.06           C
ANISOU  234  CB  PHE A  27     1572   2345   2183   -194   -165    180       C
ATOM    235  CG  PHE A  27       2.423  -0.975  33.805  1.00 17.69           C
ANISOU  235  CG  PHE A  27     1984   2404   2334   -710   -141    298       C
ATOM    236  CD1 PHE A  27       3.345  -1.965  33.644  1.00 20.49           C
ANISOU  236  CD1 PHE A  27     2642   2692   2451   -694   -106    335       C
ATOM    237  CD2 PHE A  27       1.107  -1.317  33.677  1.00 18.66           C
ANISOU  237  CD2 PHE A  27     2409   2211   2470   -591   -319    583       C
ATOM    238  CE1 PHE A  27       2.901  -3.311  33.382  1.00 21.25           C
ANISOU  238  CE1 PHE A  27     2750   2689   2636   -705    -98    407       C
ATOM    239  CE2 PHE A  27       0.682  -2.611  33.434  1.00 20.71           C
ANISOU  239  CE2 PHE A  27     2567   2646   2653   -903   -311    723       C
ATOM    240  CZ  PHE A  27       1.550  -3.603  33.279  1.00 20.48           C
ANISOU  240  CZ  PHE A  27     2760   2435   2583   -912   -469    228       C
ATOM    241  N   ALA A  28       0.614   1.691  32.325  1.00 15.37           N
ANISOU  241  N   ALA A  28     1519   1999   2322   -266     63     56       N
ATOM    242  CA  ALA A  28      -0.624   1.428  31.580  1.00 15.38           C
ANISOU  242  CA  ALA A  28     1376   2060   2406   -240     67    158       C
ATOM    243  C   ALA A  28      -0.540   2.046  30.188  1.00 14.36           C
ANISOU  243  C   ALA A  28     1108   1924   2423   -287     -7     59       C
ATOM    244  O   ALA A  28      -0.966   1.447  29.207  1.00 15.81           O
ANISOU  244  O   ALA A  28     1530   2038   2436   -309    -31     14       O
ATOM    245  CB  ALA A  28      -1.820   1.926  32.298  1.00 17.58           C
ANISOU  245  CB  ALA A  28     1665   2379   2635    -28    176    146       C
ATOM    246  N   THR A  29       0.015   3.251  30.088  1.00 14.11           N
ANISOU  246  N   THR A  29     1147   1920   2292   -290     21    -77       N
ATOM    247  CA  THR A  29       0.175   3.899  28.825  1.00 14.67           C
ANISOU  247  CA  THR A  29     1315   1861   2399   -217   -211     73       C
ATOM    248  C   THR A  29       1.090   3.098  27.946  1.00 13.33           C
ANISOU  248  C   THR A  29      827   1863   2372   -438   -254     41       C
ATOM    249  O   THR A  29       0.858   2.962  26.710  1.00 14.78           O
ANISOU  249  O   THR A  29     1157   2092   2366   -321   -204    146       O
ATOM    250  CB  THR A  29       0.702   5.341  29.007  1.00 15.24           C
ANISOU  250  CB  THR A  29     1516   1713   2560    -79   -192     70       C
ATOM    251  OG1 THR A  29      -0.279   6.048  29.752  1.00 18.13           O
ANISOU  251  OG1 THR A  29     1667   2237   2982     78    -25     68       O
ATOM    252  CG2 THR A  29       0.848   6.039  27.677  1.00 16.45           C
ANISOU  252  CG2 THR A  29     1710   1954   2585   -119   -165    383       C
ATOM    253  N   ARG A  30       2.216   2.636  28.473  1.00 13.17           N
ANISOU  253  N   ARG A  30      946   1872   2185   -466   -199     93       N
ATOM    254  CA  ARG A  30       3.139   1.810  27.673  1.00 13.38           C
ANISOU  254  CA  ARG A  30      859   1966   2257   -222    -32    255       C
ATOM    255  C   ARG A  30       2.467   0.584  27.119  1.00 13.48           C
ANISOU  255  C   ARG A  30      953   1941   2227   -201   -156    238       C
ATOM    256  O   ARG A  30       2.699   0.183  25.961  1.00 13.73           O
ANISOU  256  O   ARG A  30      938   2008   2269   -122      1    173       O
ATOM    257  CB  ARG A  30       4.387   1.345  28.471  1.00 14.87           C
ANISOU  257  CB  ARG A  30      984   2219   2447   -273    -79    262       C
ATOM    258  CG  ARG A  30       5.437   2.328  28.718  1.00 14.28           C
ANISOU  258  CG  ARG A  30     1214   2086   2124   -341    304     48       C
ATOM    259  CD  ARG A  30       6.775   1.732  29.018  1.00 14.12           C
ANISOU  259  CD  ARG A  30      755   2347   2263    -85    -25    137       C
ATOM    260  NE  ARG A  30       6.687   0.569  29.920  1.00 14.85           N
ANISOU  260  NE  ARG A  30      975   2156   2510     43    -66    144       N
ATOM    261  CZ  ARG A  30       6.557   0.628  31.241  1.00 15.05           C
ANISOU  261  CZ  ARG A  30     1150   1928   2637     18    133    131       C
ATOM    262  NH1 ARG A  30       6.481   1.791  31.898  1.00 15.99           N
ANISOU  262  NH1 ARG A  30     1682   1981   2409    -78   -112    391       N
ATOM    263  NH2 ARG A  30       6.520  -0.526  31.920  1.00 17.62           N
ANISOU  263  NH2 ARG A  30     2104   2024   2565    187     72    257       N
ATOM    264  N   LYS A  31       1.692  -0.104  27.938  1.00 13.49           N
ANISOU  264  N   LYS A  31     1057   1877   2190   -166      8    149       N
ATOM    265  CA  LYS A  31       1.087  -1.349  27.472  1.00 14.31           C
ANISOU  265  CA  LYS A  31     1224   1826   2385   -199      0     10       C
ATOM    266  C   LYS A  31       0.128  -1.052  26.344  1.00 14.06           C
ANISOU  266  C   LYS A  31      824   2016   2499   -145    -12    -84       C
ATOM    267  O   LYS A  31       0.115  -1.774  25.331  1.00 15.62           O
ANISOU  267  O   LYS A  31      983   2291   2659   -131     69   -362       O
ATOM    268  CB  LYS A  31       0.343  -2.040  28.620  1.00 15.25           C
ANISOU  268  CB  LYS A  31     1135   2092   2567   -335     94     36       C
ATOM    269  CG  LYS A  31       1.220  -2.515  29.698  1.00 19.15           C
ANISOU  269  CG  LYS A  31     2092   2259   2923   -400   -121    203       C
ATOM    270  CD  LYS A  31       2.210  -3.520  29.251  1.00 24.45           C
ANISOU  270  CD  LYS A  31     3001   3054   3234    140    -42    475       C
ATOM    271  CE  LYS A  31       3.571  -2.934  29.060  1.00 28.31           C
ANISOU  271  CE  LYS A  31     3423   3435   3895     24     70     22       C
ATOM    272  NZ  LYS A  31       4.571  -4.057  28.993  1.00 32.27           N
ANISOU  272  NZ  LYS A  31     4322   3598   4340    359   -275    232       N
ATOM    273  N   VAL A  32      -0.736  -0.065  26.494  1.00 13.69           N
ANISOU  273  N   VAL A  32      629   2118   2454   -199   -212   -114       N
ATOM    274  CA AVAL A  32      -1.685   0.273  25.442  0.50 14.56           C
ANISOU  274  CA AVAL A  32      699   2169   2664   -285   -138   -193       C
ATOM    275  CA BVAL A  32      -1.663   0.167  25.419  0.50 14.54           C
ANISOU  275  CA BVAL A  32      626   2270   2626   -277   -143   -101       C
ATOM    276  C   VAL A  32      -0.983   0.855  24.200  1.00 13.15           C
ANISOU  276  C   VAL A  32      284   2292   2418    -70   -249    -25       C
ATOM    277  O   VAL A  32      -1.316   0.507  23.035  1.00 14.59           O
ANISOU  277  O   VAL A  32      605   2418   2519   -178   -216   -166       O
ATOM    278  CB AVAL A  32      -2.767   1.262  25.973  0.50 15.29           C
ANISOU  278  CB AVAL A  32     1017   2079   2712   -219   -167   -264       C
ATOM    279  CB BVAL A  32      -2.926   0.906  25.909  0.50 14.81           C
ANISOU  279  CB BVAL A  32      496   2565   2564   -218   -266     14       C
ATOM    280  CG1AVAL A  32      -3.746   1.653  24.854  0.50 14.11           C
ANISOU  280  CG1AVAL A  32      253   2123   2984     23     -1   -598       C
ATOM    281  CG1BVAL A  32      -3.731   0.054  26.979  0.50 15.13           C
ANISOU  281  CG1BVAL A  32      769   2187   2792   -337    290   -136       C
ATOM    282  CG2AVAL A  32      -3.556   0.599  27.130  0.50 17.21           C
ANISOU  282  CG2AVAL A  32     1288   2222   3026   -304     20   -346       C
ATOM    283  CG2BVAL A  32      -2.543   2.312  26.419  0.50 17.59           C
ANISOU  283  CG2BVAL A  32     1358   2431   2893     62   -198   -118       C
ATOM    284  N   ALA A  33      -0.022   1.732  24.407  1.00 13.48           N
ANISOU  284  N   ALA A  33      546   2265   2309   -241   -231    -28       N
ATOM    285  CA  ALA A  33       0.697   2.356  23.273  1.00 14.10           C
ANISOU  285  CA  ALA A  33      899   2273   2183    -46   -156    209       C
ATOM    286  C   ALA A  33       1.461   1.307  22.506  1.00 14.78           C
ANISOU  286  C   ALA A  33      960   2386   2268   -209     31    286       C
ATOM    287  O   ALA A  33       1.578   1.405  21.289  1.00 15.32           O
ANISOU  287  O   ALA A  33     1224   2394   2201   -110   -149    271       O
ATOM    288  CB  ALA A  33       1.638   3.461  23.776  1.00 15.26           C
ANISOU  288  CB  ALA A  33     1006   2246   2545   -286   -326    255       C
ATOM    289  N   GLY A  34       2.002   0.315  23.204  1.00 14.18           N
ANISOU  289  N   GLY A  34      902   2335   2149     13     52    225       N
ATOM    290  CA  GLY A  34       2.853  -0.679  22.522  1.00 15.34           C
ANISOU  290  CA  GLY A  34     1040   2349   2439    163    118    217       C
ATOM    291  C   GLY A  34       2.049  -1.613  21.653  1.00 15.32           C
ANISOU  291  C   GLY A  34     1348   2068   2402    400    138    117       C
ATOM    292  O   GLY A  34       2.620  -2.196  20.735  1.00 16.79           O
ANISOU  292  O   GLY A  34     1064   2608   2706    219    127   -145       O
ATOM    293  N   MET A  35       0.736  -1.744  21.872  1.00 14.18           N
ANISOU  293  N   MET A  35     1102   1975   2308    203    229    216       N
ATOM    294  CA  MET A  35      -0.112  -2.562  20.991  1.00 14.60           C
ANISOU  294  CA  MET A  35     1255   1885   2407     -4    208    166       C
ATOM    295  C   MET A  35      -0.461  -1.886  19.642  1.00 13.31           C
ANISOU  295  C   MET A  35      721   1919   2416    -73    297    232       C
ATOM    296  O   MET A  35      -0.737  -2.539  18.626  1.00 14.73           O
ANISOU  296  O   MET A  35      768   2133   2695    -89     60    229       O
ATOM    297  CB  MET A  35      -1.430  -2.920  21.639  1.00 14.77           C
ANISOU  297  CB  MET A  35     1299   1681   2631    -77    393    202       C
ATOM    298  CG  MET A  35      -1.257  -3.796  22.872  1.00 15.60           C
ANISOU  298  CG  MET A  35     1490   1825   2609   -103    381     79       C
ATOM    299  SD  MET A  35      -0.625  -5.414  22.512  1.00 15.63           S
ANISOU  299  SD  MET A  35     1423   1811   2702     74    198    281       S
ATOM    300  CE  MET A  35      -1.840  -6.108  21.395  1.00 22.31           C
ANISOU  300  CE  MET A  35     3030   2344   3102   -489   -539    529       C
ATOM    301  N   ALA A  36      -0.380  -0.570  19.609  1.00 13.83           N
ANISOU  301  N   ALA A  36      877   1871   2506    -39     66    326       N
ATOM    302  CA  ALA A  36      -0.908   0.131  18.439  1.00 14.32           C
ANISOU  302  CA  ALA A  36      967   1990   2482   -112      0    372       C
ATOM    303  C   ALA A  36      -0.110  -0.145  17.190  1.00 12.69           C
ANISOU  303  C   ALA A  36      393   1856   2571   -470     -9    294       C
ATOM    304  O   ALA A  36       1.119  -0.245  17.239  1.00 13.61           O
ANISOU  304  O   ALA A  36      550   2216   2403   -271    -93    261       O
ATOM    305  CB  ALA A  36      -1.002   1.633  18.686  1.00 16.22           C
ANISOU  305  CB  ALA A  36     1479   2028   2653    143     66     83       C
ATOM    306  N   LYS A  37      -0.811  -0.211  16.085  1.00 13.67           N
ANISOU  306  N   LYS A  37      707   1887   2599    -93   -115    272       N
ATOM    307  CA  LYS A  37      -0.235  -0.367  14.740  1.00 14.73           C
ANISOU  307  CA  LYS A  37     1114   1979   2503   -242     25    108       C
ATOM    308  C   LYS A  37      -0.714   0.785  13.885  1.00 13.66           C
ANISOU  308  C   LYS A  37      588   2105   2494   -394    116    248       C
ATOM    309  O   LYS A  37      -1.663   0.619  13.131  1.00 15.73           O
ANISOU  309  O   LYS A  37     1120   2304   2552   -579   -123    255       O
ATOM    310  CB  LYS A  37      -0.605  -1.722  14.118  1.00 15.82           C
ANISOU  310  CB  LYS A  37     1166   2073   2771   -154     -2    122       C
ATOM    311  CG  LYS A  37       0.021  -2.854  14.905  1.00 19.04           C
ANISOU  311  CG  LYS A  37     1410   2486   3335    158    -43     -5       C
ATOM    312  CD  LYS A  37       1.443  -2.971  14.621  1.00 22.55           C
ANISOU  312  CD  LYS A  37     2216   2874   3478    220   -219     44       C
ATOM    313  CE  LYS A  37       2.037  -4.312  14.944  1.00 25.17           C
ANISOU  313  CE  LYS A  37     2611   3206   3744    335    132    -72       C
ATOM    314  NZ  LYS A  37       2.086  -4.522  16.412  1.00 29.22           N
ANISOU  314  NZ  LYS A  37     3125   4268   3709    299     89    279       N
ATOM    315  N   PRO A  38      -0.149   1.988  14.106  1.00 13.33           N
ANISOU  315  N   PRO A  38      728   1939   2398   -313     90    202       N
ATOM    316  CA  PRO A  38      -0.734   3.142  13.458  1.00 14.64           C
ANISOU  316  CA  PRO A  38     1310   1925   2327   -218    222    277       C
ATOM    317  C   PRO A  38      -0.640   3.160  11.954  1.00 14.26           C
ANISOU  317  C   PRO A  38     1205   1875   2336   -351    399    228       C
ATOM    318  O   PRO A  38       0.290   2.567  11.382  1.00 14.51           O
ANISOU  318  O   PRO A  38     1090   1947   2476   -329    331    199       O
ATOM    319  CB  PRO A  38       0.008   4.316  14.062  1.00 17.08           C
ANISOU  319  CB  PRO A  38     1995   2054   2438   -193    174     65       C
ATOM    320  CG  PRO A  38       0.888   3.766  15.077  1.00 19.44           C
ANISOU  320  CG  PRO A  38     2157   2217   3011   -447   -120     49       C
ATOM    321  CD  PRO A  38       0.944   2.326  15.003  1.00 13.89           C
ANISOU  321  CD  PRO A  38      847   1952   2479   -449    182    237       C
ATOM    322  N  AASN A  39      -1.533   3.893  11.328  0.50 14.81           N
ANISOU  322  N  AASN A  39     1457   1930   2237   -290    275    197       N
ATOM    323  N  BASN A  39      -1.504   3.994  11.372  0.50 14.27           N
ANISOU  323  N  BASN A  39     1308   1837   2277   -304    320    183       N
ATOM    324  CA AASN A  39      -1.234   4.423  10.025  0.50 15.54           C
ANISOU  324  CA AASN A  39     1793   1839   2272   -162    238    154       C
ATOM    325  CA BASN A  39      -1.581   4.428   9.958  0.50 14.42           C
ANISOU  325  CA BASN A  39     1459   1694   2325   -119    362     89       C
ATOM    326  C  AASN A  39      -0.641   5.768  10.244  0.50 15.02           C
ANISOU  326  C  AASN A  39     1699   1756   2250   -172    263     97       C
ATOM    327  C  BASN A  39      -0.972   5.883   9.945  0.50 13.53           C
ANISOU  327  C  BASN A  39     1321   1561   2256   -178    286     63       C
ATOM    328  O  AASN A  39      -0.824   6.434  11.270  0.50 15.73           O
ANISOU  328  O  AASN A  39     1751   2024   2201   -118    163     89       O
ATOM    329  O  BASN A  39      -1.586   6.780  10.568  0.50 15.07           O
ANISOU  329  O  BASN A  39     2184   1585   1957    -37    484    199       O
ATOM    330  CB AASN A  39      -2.419   4.532   9.111  0.50 15.74           C
ANISOU  330  CB AASN A  39     1815   2019   2144   -182    221    193       C
ATOM    331  CB BASN A  39      -3.082   4.394   9.548  0.50 15.27           C
ANISOU  331  CB BASN A  39     1525   1800   2474    -76    384    157       C
ATOM    332  CG AASN A  39      -2.793   3.207   8.494  0.50 16.69           C
ANISOU  332  CG AASN A  39     1437   2215   2689   -504   -125    332       C
ATOM    333  CG BASN A  39      -3.339   4.780   8.080  0.50 19.75           C
ANISOU  333  CG BASN A  39     2164   2470   2868     48    151    169       C
ATOM    334  OD1AASN A  39      -2.468   2.136   9.032  0.50 22.71           O
ANISOU  334  OD1AASN A  39     3171   2536   2918   -522   -639     82       O
ATOM    335  OD1BASN A  39      -3.965   5.812   7.781  0.50 21.91           O
ANISOU  335  OD1BASN A  39     1646   2722   3958   -225    211    223       O
ATOM    336  ND2AASN A  39      -3.505   3.261   7.365  0.50 22.48           N
ANISOU  336  ND2AASN A  39     2361   3286   2892   -183    -85    264       N
ATOM    337  ND2BASN A  39      -2.851   3.958   7.165  0.50 19.56           N
ANISOU  337  ND2BASN A  39     2509   2344   2579   -265   -298    -42       N
ATOM    338  N   MET A  40       0.205   6.098   9.318  1.00 14.75           N
ANISOU  338  N   MET A  40     1535   1650   2418   -156    372    117       N
ATOM    339  CA  MET A  40       0.842   7.395   9.318  1.00 13.89           C
ANISOU  339  CA  MET A  40     1548   1503   2226   -159    233     31       C
ATOM    340  C   MET A  40       0.736   7.981   7.943  1.00 13.87           C
ANISOU  340  C   MET A  40     1310   1692   2268   -246    243     58       C
ATOM    341  O   MET A  40       1.060   7.334   6.951  1.00 15.01           O
ANISOU  341  O   MET A  40     1675   1624   2402     39    281    142       O
ATOM    342  CB  MET A  40       2.304   7.220   9.666  1.00 15.66           C
ANISOU  342  CB  MET A  40     2134   1516   2299   -229    118     86       C
ATOM    343  CG  MET A  40       3.161   8.525   9.620  1.00 15.51           C
ANISOU  343  CG  MET A  40     1584   1765   2545   -115    -48     27       C
ATOM    344  SD  MET A  40       4.813   8.422  10.154  1.00 20.18           S
ANISOU  344  SD  MET A  40     2842   1896   2930   -243   -213    -24       S
ATOM    345  CE  MET A  40       5.395   7.000   9.246  1.00 19.29           C
ANISOU  345  CE  MET A  40     1429   2642   3256   -195    177     54       C
ATOM    346  N   ILE A  41       0.197   9.186   7.891  1.00 13.39           N
ANISOU  346  N   ILE A  41     1240   1617   2231   -207    191    -31       N
ATOM    347  CA  ILE A  41      -0.056   9.884   6.648  1.00 12.37           C
ANISOU  347  CA  ILE A  41      639   1717   2342   -329    182     41       C
ATOM    348  C   ILE A  41       0.865  11.079   6.644  1.00 12.57           C
ANISOU  348  C   ILE A  41     1066   1549   2158    -82    166    -27       C
ATOM    349  O   ILE A  41       0.823  11.949   7.543  1.00 13.27           O
ANISOU  349  O   ILE A  41     1240   1611   2190   -328    247    -92       O
ATOM    350  CB  ILE A  41      -1.506  10.332   6.504  1.00 14.61           C
ANISOU  350  CB  ILE A  41      939   2089   2521   -245    205   -175       C
ATOM    351  CG1 ILE A  41      -2.476   9.177   6.637  1.00 17.77           C
ANISOU  351  CG1 ILE A  41      778   2941   3033   -651    151   -201       C
ATOM    352  CG2 ILE A  41      -1.733  11.052   5.188  1.00 18.49           C
ANISOU  352  CG2 ILE A  41     1276   2824   2924   -282    -69     46       C
ATOM    353  CD1 ILE A  41      -3.783   9.605   6.698  1.00 23.94           C
ANISOU  353  CD1 ILE A  41      735   4048   4312  -1107    146   -241       C
ATOM    354  N   ILE A  42       1.676  11.189   5.613  1.00 11.62           N
ANISOU  354  N   ILE A  42      998   1322   2095    -91    123   -116       N
ATOM    355  CA  ILE A  42       2.626  12.292   5.485  1.00 11.39           C
ANISOU  355  CA  ILE A  42      851   1524   1953     -7    -39    -73       C
ATOM    356  C   ILE A  42       2.274  13.032   4.221  1.00 11.34           C
ANISOU  356  C   ILE A  42      741   1439   2126     -4     30    -80       C
ATOM    357  O   ILE A  42       2.158  12.435   3.138  1.00 12.10           O
ANISOU  357  O   ILE A  42     1003   1494   2100    -90    -44     27       O
ATOM    358  CB  ILE A  42       4.090  11.768   5.429  1.00 11.56           C
ANISOU  358  CB  ILE A  42     1010   1505   1877   -127     45      4       C
ATOM    359  CG1 ILE A  42       4.419  11.006   6.707  1.00 12.30           C
ANISOU  359  CG1 ILE A  42     1009   1576   2088    190      8   -102       C
ATOM    360  CG2 ILE A  42       5.059  12.960   5.220  1.00 13.08           C
ANISOU  360  CG2 ILE A  42      870   1797   2301    133     76    -67       C
ATOM    361  CD1 ILE A  42       5.816  10.467   6.805  1.00 14.26           C
ANISOU  361  CD1 ILE A  42     1253   1940   2224    187    -80    119       C
ATOM    362  N   SER A  43       2.153  14.344   4.326  1.00 11.59           N
ANISOU  362  N   SER A  43      936   1416   2049   -170   -175    -65       N
ATOM    363  CA  SER A  43       1.836  15.198   3.173  1.00 12.76           C
ANISOU  363  CA  SER A  43     1273   1447   2128    -44   -174     23       C
ATOM    364  C   SER A  43       2.709  16.445   3.243  1.00 12.63           C
ANISOU  364  C   SER A  43     1258   1450   2089    187   -137    -48       C
ATOM    365  O   SER A  43       3.179  16.855   4.296  1.00 12.48           O
ANISOU  365  O   SER A  43     1207   1490   2043    -59    -29     28       O
ATOM    366  CB  SER A  43       0.372  15.501   3.124  1.00 15.16           C
ANISOU  366  CB  SER A  43     1371   1866   2522    -31   -310     65       C
ATOM    367  OG  SER A  43      -0.011  16.168   4.266  1.00 18.22           O
ANISOU  367  OG  SER A  43     1723   2305   2894    217   -134    -90       O
ATOM    368  N   VAL A  44       2.870  17.063   2.091  1.00 13.63           N
ANISOU  368  N   VAL A  44     1670   1476   2032    -12   -154    -67       N
ATOM    369  CA  VAL A  44       3.578  18.310   1.940  1.00 14.55           C
ANISOU  369  CA  VAL A  44     1645   1588   2294   -110   -231     80       C
ATOM    370  C   VAL A  44       2.732  19.306   1.143  1.00 15.44           C
ANISOU  370  C   VAL A  44     1957   1681   2226   -104   -327      5       C
ATOM    371  O   VAL A  44       2.094  18.953   0.174  1.00 19.38           O
ANISOU  371  O   VAL A  44     3335   1644   2383    -48   -679     68       O
ATOM    372  CB  VAL A  44       4.955  18.110   1.271  1.00 15.55           C
ANISOU  372  CB  VAL A  44     1852   1577   2476   -130   -199    104       C
ATOM    373  CG1 VAL A  44       5.720  19.430   1.153  1.00 20.56           C
ANISOU  373  CG1 VAL A  44     2083   2224   3503   -506    -53    163       C
ATOM    374  CG2 VAL A  44       5.828  17.152   2.015  1.00 18.78           C
ANISOU  374  CG2 VAL A  44     1899   2223   3011    -38   -173   -137       C
ATOM    375  N   ASN A  45       2.667  20.535   1.619  1.00 14.12           N
ANISOU  375  N   ASN A  45     1750   1505   2106   -126   -141     66       N
ATOM    376  CA  ASN A  45       1.957  21.625   0.940  1.00 13.89           C
ANISOU  376  CA  ASN A  45     1594   1609   2074   -139   -308     81       C
ATOM    377  C   ASN A  45       2.847  22.846   1.085  1.00 14.69           C
ANISOU  377  C   ASN A  45     1744   1635   2201    -58   -187    144       C
ATOM    378  O   ASN A  45       2.961  23.410   2.140  1.00 13.09           O
ANISOU  378  O   ASN A  45     1279   1514   2180     49   -155     39       O
ATOM    379  CB  ASN A  45       0.581  21.783   1.528  1.00 14.12           C
ANISOU  379  CB  ASN A  45     1464   1638   2261     17   -220      3       C
ATOM    380  CG  ASN A  45      -0.274  22.789   0.821  1.00 13.27           C
ANISOU  380  CG  ASN A  45     1099   1859   2081   -367   -429    -87       C
ATOM    381  OD1 ASN A  45      -1.513  22.593   0.745  1.00 15.25           O
ANISOU  381  OD1 ASN A  45     1342   1921   2529   -283   -185    -91       O
ATOM    382  ND2 ASN A  45       0.292  23.827   0.350  1.00 14.35           N
ANISOU  382  ND2 ASN A  45     1239   1571   2640   -313   -535    248       N
ATOM    383  N   GLY A  46       3.520  23.201   0.006  1.00 16.02           N
ANISOU  383  N   GLY A  46     2286   1709   2089   -177   -215    140       N
ATOM    384  CA  GLY A  46       4.486  24.271   0.075  1.00 16.63           C
ANISOU  384  CA  GLY A  46     2140   1979   2199   -215     82    199       C
ATOM    385  C   GLY A  46       5.621  23.927   1.042  1.00 15.57           C
ANISOU  385  C   GLY A  46     1599   1953   2361   -216    247    170       C
ATOM    386  O   GLY A  46       6.210  22.872   0.957  1.00 17.54           O
ANISOU  386  O   GLY A  46     1929   2034   2701   -203    174    -70       O
ATOM    387  N   ASP A  47       5.865  24.802   2.002  1.00 14.90           N
ANISOU  387  N   ASP A  47     1416   1819   2425   -177    160    206       N
ATOM    388  CA  ASP A  47       6.871  24.573   3.028  1.00 16.17           C
ANISOU  388  CA  ASP A  47     1511   2017   2614   -221    -96    225       C
ATOM    389  C   ASP A  47       6.359  23.758   4.208  1.00 13.72           C
ANISOU  389  C   ASP A  47     1151   1754   2308     85    109     58       C
ATOM    390  O   ASP A  47       7.177  23.441   5.088  1.00 14.86           O
ANISOU  390  O   ASP A  47      987   2063   2596     95   -166     81       O
ATOM    391  CB  ASP A  47       7.365  25.934   3.583  1.00 18.45           C
ANISOU  391  CB  ASP A  47     2113   2228   2666   -403   -100    212       C
ATOM    392  CG  ASP A  47       8.035  26.811   2.543  1.00 22.87           C
ANISOU  392  CG  ASP A  47     2687   2664   3337   -536   -133    177       C
ATOM    393  OD1 ASP A  47       8.619  26.282   1.592  1.00 26.78           O
ANISOU  393  OD1 ASP A  47     3089   3833   3251  -1059    603    437       O
ATOM    394  OD2 ASP A  47       8.021  28.047   2.716  1.00 30.52           O
ANISOU  394  OD2 ASP A  47     4176   3109   4311   -729   -139    598       O
ATOM    395  N   VAL A  48       5.059  23.472   4.244  1.00 11.63           N
ANISOU  395  N   VAL A  48      768   1525   2122    167    -73    128       N
ATOM    396  CA  VAL A  48       4.508  22.836   5.415  1.00 11.42           C
ANISOU  396  CA  VAL A  48      691   1571   2077     50    -90     66       C
ATOM    397  C   VAL A  48       4.424  21.325   5.200  1.00 11.52           C
ANISOU  397  C   VAL A  48      902   1459   2016   -143    -68     65       C
ATOM    398  O   VAL A  48       3.786  20.829   4.279  1.00 12.39           O
ANISOU  398  O   VAL A  48     1065   1491   2149     51   -236    100       O
ATOM    399  CB  VAL A  48       3.138  23.382   5.716  1.00 12.57           C
ANISOU  399  CB  VAL A  48      928   1646   2202     34    -51     91       C
ATOM    400  CG1 VAL A  48       2.605  22.715   6.990  1.00 14.57           C
ANISOU  400  CG1 VAL A  48     1440   1714   2382    144    355    133       C
ATOM    401  CG2 VAL A  48       3.185  24.925   5.885  1.00 15.12           C
ANISOU  401  CG2 VAL A  48     1307   1720   2715    309     29     55       C
ATOM    402  N   ILE A  49       4.978  20.598   6.130  1.00 10.79           N
ANISOU  402  N   ILE A  49      685   1446   1966   -136    -72      1       N
ATOM    403  CA  ILE A  49       4.886  19.148   6.154  1.00 10.70           C
ANISOU  403  CA  ILE A  49      263   1599   2203   -104     77   -100       C
ATOM    404  C   ILE A  49       3.942  18.792   7.264  1.00 10.43           C
ANISOU  404  C   ILE A  49      263   1457   2242    -88    -30     52       C
ATOM    405  O   ILE A  49       3.973  19.349   8.380  1.00 11.05           O
ANISOU  405  O   ILE A  49      429   1602   2166   -103     -2    -61       O
ATOM    406  CB  ILE A  49       6.254  18.506   6.428  1.00 11.76           C
ANISOU  406  CB  ILE A  49      332   1779   2358   -285    251   -111       C
ATOM    407  CG1 ILE A  49       7.318  18.955   5.482  1.00 12.28           C
ANISOU  407  CG1 ILE A  49      261   1833   2568   -110     48   -136       C
ATOM    408  CG2 ILE A  49       6.191  16.996   6.544  1.00 12.72           C
ANISOU  408  CG2 ILE A  49      974   1631   2226     87    -81     -6       C
ATOM    409  CD1 ILE A  49       8.656  18.721   5.843  1.00 17.03           C
ANISOU  409  CD1 ILE A  49      345   2968   3157   -490     34    408       C
ATOM    410  N   THR A  50       3.036  17.859   7.004  1.00 10.85           N
ANISOU  410  N   THR A  50      479   1516   2125    -28     86    -32       N
ATOM    411  CA  THR A  50       2.074  17.325   7.972  1.00 11.29           C
ANISOU  411  CA  THR A  50      633   1484   2173   -284     18    -72       C
ATOM    412  C   THR A  50       2.346  15.807   8.164  1.00 11.15           C
ANISOU  412  C   THR A  50      624   1469   2142    -61     72    -86       C
ATOM    413  O   THR A  50       2.434  15.064   7.188  1.00 12.41           O
ANISOU  413  O   THR A  50     1155   1443   2116   -193     19      5       O
ATOM    414  CB  THR A  50       0.638  17.596   7.609  1.00 12.16           C
ANISOU  414  CB  THR A  50      388   1717   2515   -444     -4    -36       C
ATOM    415  OG1 THR A  50       0.441  19.014   7.481  1.00 13.67           O
ANISOU  415  OG1 THR A  50      789   1812   2591    -62    -82    -27       O
ATOM    416  CG2 THR A  50      -0.347  17.044   8.598  1.00 14.93           C
ANISOU  416  CG2 THR A  50      370   2109   3194   -374    166   -294       C
ATOM    417  N   ILE A  51       2.444  15.391   9.407  1.00 10.76           N
ANISOU  417  N   ILE A  51      700   1312   2075   -177     24    -44       N
ATOM    418  CA  ILE A  51       2.579  13.958   9.788  1.00 11.41           C
ANISOU  418  CA  ILE A  51      580   1483   2271   -341     63    -82       C
ATOM    419  C   ILE A  51       1.393  13.653  10.704  1.00 11.36           C
ANISOU  419  C   ILE A  51      503   1532   2279   -127    -33    -16       C
ATOM    420  O   ILE A  51       1.300  14.213  11.830  1.00 12.48           O
ANISOU  420  O   ILE A  51     1103   1490   2148    -69    164   -111       O
ATOM    421  CB  ILE A  51       3.906  13.656  10.437  1.00 11.56           C
ANISOU  421  CB  ILE A  51      572   1377   2440    -83    -65   -157       C
ATOM    422  CG1 ILE A  51       5.100  14.039   9.595  1.00 13.19           C
ANISOU  422  CG1 ILE A  51      663   1609   2738   -411    267   -264       C
ATOM    423  CG2 ILE A  51       3.966  12.162  10.857  1.00 13.65           C
ANISOU  423  CG2 ILE A  51      905   1566   2713     55    142    137       C
ATOM    424  CD1 ILE A  51       6.461  13.786  10.189  1.00 14.63           C
ANISOU  424  CD1 ILE A  51      255   2263   3038    -61    -18   -181       C
ATOM    425  N   LYS A  52       0.450  12.837  10.245  1.00 11.62           N
ANISOU  425  N   LYS A  52      450   1667   2297   -249    199    -76       N
ATOM    426  CA ALYS A  52      -0.723  12.420  10.950  0.50 13.02           C
ANISOU  426  CA ALYS A  52      811   1663   2473   -173    271   -167       C
ATOM    427  CA BLYS A  52      -0.689  12.364  11.032  0.50 13.38           C
ANISOU  427  CA BLYS A  52      930   1697   2456   -141    347   -161       C
ATOM    428  C   LYS A  52      -0.499  10.931  11.347  1.00 13.96           C
ANISOU  428  C   LYS A  52     1271   1615   2417   -245    330   -105       C
ATOM    429  O   LYS A  52      -0.115  10.133  10.502  1.00 16.77           O
ANISOU  429  O   LYS A  52     2427   1623   2319   -359    483      3       O
ATOM    430  CB ALYS A  52      -1.958  12.635  10.055  0.50 14.10           C
ANISOU  430  CB ALYS A  52      745   1938   2671   -306    149    -30       C
ATOM    431  CB BLYS A  52      -2.035  12.377  10.338  0.50 13.65           C
ANISOU  431  CB BLYS A  52      568   2010   2605   -123    311    -60       C
ATOM    432  CG ALYS A  52      -3.305  12.395  10.693  0.50 14.93           C
ANISOU  432  CG ALYS A  52      581   2051   3039    -33    -36     22       C
ATOM    433  CG BLYS A  52      -2.409  13.649   9.822  0.50 17.38           C
ANISOU  433  CG BLYS A  52     1429   2201   2972    -68    327    -85       C
ATOM    434  CD ALYS A  52      -4.403  12.486   9.663  0.50 18.60           C
ANISOU  434  CD ALYS A  52     1133   2584   3348     98    -95    271       C
ATOM    435  CD BLYS A  52      -3.685  13.562   9.105  0.50 20.56           C
ANISOU  435  CD BLYS A  52     1906   2964   2941   -108    -52     26       C
ATOM    436  CE ALYS A  52      -5.765  12.558  10.304  0.50 20.42           C
ANISOU  436  CE ALYS A  52     1170   3100   3485    260    -16    226       C
ATOM    437  CE BLYS A  52      -3.936  14.878   8.469  0.50 22.45           C
ANISOU  437  CE BLYS A  52     2217   3195   3116   -147   -122    216       C
ATOM    438  NZ ALYS A  52      -6.823  12.603   9.287  0.50 24.12           N
ANISOU  438  NZ ALYS A  52      995   3844   4324     63   -266    201       N
ATOM    439  NZ BLYS A  52      -3.088  15.017   7.272  0.50 22.34           N
ANISOU  439  NZ BLYS A  52     1928   3436   3123     85     -2    385       N
ATOM    440  N   SER A  53      -0.766  10.595  12.601  1.00 13.40           N
ANISOU  440  N   SER A  53     1208   1604   2279   -251    286      3       N
ATOM    441  CA  SER A  53      -0.790   9.234  13.059  1.00 14.25           C
ANISOU  441  CA  SER A  53     1281   1742   2390   -226    433    -49       C
ATOM    442  C   SER A  53      -2.194   8.872  13.492  1.00 14.41           C
ANISOU  442  C   SER A  53     1374   1723   2376   -378    364    -79       C
ATOM    443  O   SER A  53      -2.751   9.519  14.362  1.00 17.03           O
ANISOU  443  O   SER A  53     1789   2031   2648   -556    622    -61       O
ATOM    444  CB  SER A  53       0.159   9.070  14.224  1.00 16.16           C
ANISOU  444  CB  SER A  53     1730   1782   2625   -260    333     33       C
ATOM    445  OG  SER A  53       0.128   7.725  14.700  1.00 17.99           O
ANISOU  445  OG  SER A  53     1961   2088   2784   -225    239     84       O
ATOM    446  N   GLU A  54      -2.741   7.852  12.850  1.00 15.35           N
ANISOU  446  N   GLU A  54     1420   2035   2375   -418    370   -142       N
ATOM    447  CA  GLU A  54      -4.116   7.376  13.120  1.00 15.22           C
ANISOU  447  CA  GLU A  54     1101   2108   2572   -232    318     63       C
ATOM    448  C   GLU A  54      -3.999   6.045  13.791  1.00 15.14           C
ANISOU  448  C   GLU A  54      902   2228   2622   -168    355    189       C
ATOM    449  O   GLU A  54      -3.388   5.096  13.257  1.00 15.09           O
ANISOU  449  O   GLU A  54     1150   2008   2573     14    207    347       O
ATOM    450  CB  GLU A  54      -4.899   7.225  11.822  1.00 17.48           C
ANISOU  450  CB  GLU A  54     1459   2364   2818   -278    299    132       C
ATOM    451  CG  GLU A  54      -5.103   8.496  11.033  1.00 22.65           C
ANISOU  451  CG  GLU A  54     2503   2814   3286   -204    257    332       C
ATOM    452  CD  GLU A  54      -6.147   8.336   9.949  1.00 27.27           C
ANISOU  452  CD  GLU A  54     2903   3557   3900    -19    -16    420       C
ATOM    453  OE1 GLU A  54      -6.123   7.301   9.257  1.00 29.08           O
ANISOU  453  OE1 GLU A  54     3178   4327   3542    -69   -585     33       O
ATOM    454  OE2 GLU A  54      -7.024   9.225   9.780  1.00 33.54           O
ANISOU  454  OE2 GLU A  54     3333   4209   5200    129    -72    225       O
ATOM    455  N   SER A  55      -4.410   6.010  15.039  1.00 15.09           N
ANISOU  455  N   SER A  55      545   2461   2728    -12     49    235       N
ATOM    456  CA  SER A  55      -4.103   4.958  15.942  1.00 16.94           C
ANISOU  456  CA  SER A  55      954   2513   2969     90    262    265       C
ATOM    457  C   SER A  55      -5.243   4.541  16.824  1.00 17.00           C
ANISOU  457  C   SER A  55     1327   2352   2779    231    346    291       C
ATOM    458  O   SER A  55      -6.061   5.320  17.166  1.00 16.69           O
ANISOU  458  O   SER A  55     1293   2228   2820    502    565    564       O
ATOM    459  CB  SER A  55      -2.970   5.523  16.782  1.00 18.30           C
ANISOU  459  CB  SER A  55     1249   2546   3155   -144    324    393       C
ATOM    460  OG  SER A  55      -2.639   4.584  17.764  1.00 17.67           O
ANISOU  460  OG  SER A  55     1059   2681   2973    168    174    691       O
ATOM    461  N   THR A  56      -5.297   3.271  17.184  1.00 17.32           N
ANISOU  461  N   THR A  56     1633   2142   2804    407    335    214       N
ATOM    462  CA  THR A  56      -6.181   2.781  18.224  1.00 18.81           C
ANISOU  462  CA  THR A  56     2187   2040   2919   -106    344     97       C
ATOM    463  C   THR A  56      -5.800   3.289  19.602  1.00 17.33           C
ANISOU  463  C   THR A  56     2124   1834   2627    -49    502    139       C
ATOM    464  O   THR A  56      -6.586   3.204  20.520  1.00 21.25           O
ANISOU  464  O   THR A  56     2501   2637   2934   -647    690    -10       O
ATOM    465  CB  THR A  56      -6.114   1.221  18.234  1.00 18.02           C
ANISOU  465  CB  THR A  56     1489   2268   3089   -131    353   -152       C
ATOM    466  OG1 THR A  56      -4.718   0.853  18.241  1.00 18.54           O
ANISOU  466  OG1 THR A  56     1988   2232   2821    -50    255    -20       O
ATOM    467  CG2 THR A  56      -6.837   0.685  16.944  1.00 20.24           C
ANISOU  467  CG2 THR A  56     1569   2721   3397   -288   -236   -297       C
ATOM    468  N  APHE A  57      -4.581   3.755  19.787  0.50 17.53           N
ANISOU  468  N  APHE A  57     2188   1890   2581    -53    468    214       N
ATOM    469  N  BPHE A  57      -4.577   3.760  19.780  0.50 17.48           N
ANISOU  469  N  BPHE A  57     2188   1893   2560    -68    441    190       N
ATOM    470  CA APHE A  57      -4.174   4.342  21.070  0.50 17.81           C
ANISOU  470  CA APHE A  57     2218   1939   2610     92    417    280       C
ATOM    471  CA BPHE A  57      -4.128   4.331  21.064  0.50 17.69           C
ANISOU  471  CA BPHE A  57     2214   1941   2564     51    358    238       C
ATOM    472  C  APHE A  57      -4.548   5.817  21.047  0.50 17.97           C
ANISOU  472  C  APHE A  57     2109   1952   2764    122    501    296       C
ATOM    473  C  BPHE A  57      -4.477   5.809  21.079  0.50 17.45           C
ANISOU  473  C  BPHE A  57     2087   1884   2657     49    408    192       C
ATOM    474  O  APHE A  57      -5.350   6.261  21.830  0.50 19.16           O
ANISOU  474  O  APHE A  57     2051   2157   3071     34    752    400       O
ATOM    475  O  BPHE A  57      -5.500   6.183  21.597  0.50 18.52           O
ANISOU  475  O  BPHE A  57     2035   2101   2901    -24    600    203       O
ATOM    476  CB APHE A  57      -2.673   4.131  21.303  0.50 18.22           C
ANISOU  476  CB APHE A  57     2310   1924   2685    267    326    362       C
ATOM    477  CB BPHE A  57      -2.627   4.091  21.262  0.50 18.46           C
ANISOU  477  CB BPHE A  57     2361   1989   2664    212    284    349       C
ATOM    478  CG APHE A  57      -2.109   4.900  22.449  0.50 20.99           C
ANISOU  478  CG APHE A  57     2913   2130   2931    251    102    397       C
ATOM    479  CG BPHE A  57      -1.990   4.944  22.311  0.50 21.40           C
ANISOU  479  CG BPHE A  57     2948   2252   2929    197     95    384       C
ATOM    480  CD1APHE A  57      -2.626   4.773  23.712  0.50 22.76           C
ANISOU  480  CD1APHE A  57     3554   2196   2896    131     89    349       C
ATOM    481  CD1BPHE A  57      -0.830   5.632  22.029  0.50 21.80           C
ANISOU  481  CD1BPHE A  57     3050   2267   2965    227    140    378       C
ATOM    482  CD2APHE A  57      -1.031   5.735  22.260  0.50 20.11           C
ANISOU  482  CD2APHE A  57     2665   2045   2931    352      2    421       C
ATOM    483  CD2BPHE A  57      -2.532   5.054  23.569  0.50 22.64           C
ANISOU  483  CD2BPHE A  57     3393   2374   2834    100     81    431       C
ATOM    484  CE1APHE A  57      -2.081   5.509  24.780  0.50 24.51           C
ANISOU  484  CE1APHE A  57     3646   2648   3016    -12    -82    343       C
ATOM    485  CE1BPHE A  57      -0.206   6.418  22.973  0.50 24.27           C
ANISOU  485  CE1BPHE A  57     3516   2534   3168    130     63    364       C
ATOM    486  CE2APHE A  57      -0.488   6.449  23.310  0.50 24.17           C
ANISOU  486  CE2APHE A  57     3515   2486   3183    291   -117    398       C
ATOM    487  CE2BPHE A  57      -1.919   5.869  24.539  0.50 23.00           C
ANISOU  487  CE2BPHE A  57     3408   2423   2908   -159    -22    502       C
ATOM    488  CZ APHE A  57      -1.023   6.342  24.563  0.50 24.60           C
ANISOU  488  CZ APHE A  57     3563   2607   3176    193   -166    393       C
ATOM    489  CZ BPHE A  57      -0.755   6.547  24.226  0.50 22.93           C
ANISOU  489  CZ BPHE A  57     3519   2227   2966     99     20    515       C
ATOM    490  N  ALYS A  58      -3.972   6.585  20.140  0.50 17.70           N
ANISOU  490  N  ALYS A  58     1959   2093   2674    151    620    303       N
ATOM    491  N  BLYS A  58      -3.637   6.666  20.518  0.50 16.19           N
ANISOU  491  N  BLYS A  58     1877   1886   2387     -5    314    117       N
ATOM    492  CA ALYS A  58      -4.166   8.045  20.116  0.50 17.23           C
ANISOU  492  CA ALYS A  58     1768   2137   2638    211    469    215       C
ATOM    493  CA BLYS A  58      -3.936   8.104  20.509  0.50 15.20           C
ANISOU  493  CA BLYS A  58     1543   1902   2329      9    233    -64       C
ATOM    494  C  ALYS A  58      -3.896   8.519  18.706  0.50 17.03           C
ANISOU  494  C  ALYS A  58     1649   2226   2592    195    611    256       C
ATOM    495  C  BLYS A  58      -3.596   8.739  19.168  0.50 14.48           C
ANISOU  495  C  BLYS A  58     1452   1748   2302    -87    225    -54       C
ATOM    496  O  ALYS A  58      -2.868   8.145  18.142  0.50 20.31           O
ANISOU  496  O  ALYS A  58     1875   2854   2988    362    569    292       O
ATOM    497  O  BLYS A  58      -2.465   8.645  18.726  0.50 13.37           O
ANISOU  497  O  BLYS A  58     1348   1739   1994   -186    165   -185       O
ATOM    498  CB ALYS A  58      -3.189   8.724  21.100  0.50 17.38           C
ANISOU  498  CB ALYS A  58     1638   2190   2773    142    387    172       C
ATOM    499  CB BLYS A  58      -3.193   8.798  21.668  0.50 14.72           C
ANISOU  499  CB BLYS A  58     1201   1878   2513      1    225   -169       C
ATOM    500  CG ALYS A  58      -3.413  10.214  21.435  0.50 17.96           C
ANISOU  500  CG ALYS A  58     1812   2250   2763      7    122    113       C
ATOM    501  CG BLYS A  58      -3.854   8.578  23.000  0.50 20.14           C
ANISOU  501  CG BLYS A  58     2078   2743   2827    -91    251     27       C
ATOM    502  CD ALYS A  58      -4.770  10.577  22.007  0.50 19.76           C
ANISOU  502  CD ALYS A  58     1743   2860   2904    114   -105    -63       C
ATOM    503  CD BLYS A  58      -3.375   9.549  24.051  0.50 23.04           C
ANISOU  503  CD BLYS A  58     2613   2930   3210     -4    408   -117       C
ATOM    504  CE ALYS A  58      -4.819  12.036  22.383  0.50 21.09           C
ANISOU  504  CE ALYS A  58     1848   3145   3018    230    136   -160       C
ATOM    505  CE BLYS A  58      -2.947   8.791  25.312  0.50 23.37           C
ANISOU  505  CE BLYS A  58     2608   3156   3114     -1    438   -127       C
ATOM    506  NZ ALYS A  58      -6.180  12.549  22.335  0.50 24.91           N
ANISOU  506  NZ ALYS A  58     2331   3684   3448    232    151   -112       N
ATOM    507  NZ BLYS A  58      -1.974   9.457  26.214  0.50 21.78           N
ANISOU  507  NZ BLYS A  58     2435   2730   3108   -277    869   -136       N
ATOM    508  N  AASN A  59      -4.763   9.363  18.157  0.50 16.28           N
ANISOU  508  N  AASN A  59     1456   2124   2603     67    635    202       N
ATOM    509  N  BASN A  59      -4.581   9.344  18.513  0.50 13.79           N
ANISOU  509  N  BASN A  59     1251   1731   2256    -35    341     70       N
ATOM    510  CA AASN A  59      -4.535  10.050  16.887  0.50 16.02           C
ANISOU  510  CA AASN A  59     1529   1930   2625    -23    558     75       C
ATOM    511  CA BASN A  59      -4.400  10.060  17.259  0.50 14.78           C
ANISOU  511  CA BASN A  59     1523   1663   2427     37    329    -31       C
ATOM    512  C  AASN A  59      -3.774  11.354  17.179  0.50 16.67           C
ANISOU  512  C  AASN A  59     1692   1930   2710    -87    453     21       C
ATOM    513  C  BASN A  59      -3.497  11.259  17.476  0.50 15.15           C
ANISOU  513  C  BASN A  59     1521   1730   2503     15    324     55       C
ATOM    514  O  AASN A  59      -4.201  12.134  18.045  0.50 17.25           O
ANISOU  514  O  AASN A  59     1753   1946   2853    -26    527    -65       O
ATOM    515  O  BASN A  59      -3.613  11.944  18.525  0.50 14.92           O
ANISOU  515  O  BASN A  59     1535   1674   2458    151    238     75       O
ATOM    516  CB AASN A  59      -5.856  10.308  16.167  0.50 16.66           C
ANISOU  516  CB AASN A  59     1685   1995   2648   -139    478    118       C
ATOM    517  CB BASN A  59      -5.737  10.583  16.748  0.50 15.16           C
ANISOU  517  CB BASN A  59     1686   1670   2402     46    195    112       C
ATOM    518  CG AASN A  59      -6.678   9.055  15.976  0.50 17.91           C
ANISOU  518  CG AASN A  59     1374   2320   3109   -226    483     83       C
ATOM    519  CG BASN A  59      -6.613   9.517  16.157  0.50 16.77           C
ANISOU  519  CG BASN A  59     1373   2116   2880    -28    283   -103       C
ATOM    520  OD1AASN A  59      -6.242   8.090  15.347  0.50 19.12           O
ANISOU  520  OD1AASN A  59     1648   2605   3010    278    448    153       O
ATOM    521  OD1BASN A  59      -6.162   8.416  15.842  0.50 14.70           O
ANISOU  521  OD1BASN A  59      869   1929   2787   -182    146    -16       O
ATOM    522  ND2AASN A  59      -7.906   9.075  16.495  0.50 19.33           N
ANISOU  522  ND2AASN A  59     1125   2931   3285   -679    351    517       N
ATOM    523  ND2BASN A  59      -7.892   9.838  15.996  0.50 21.16           N
ANISOU  523  ND2BASN A  59     1545   2641   3853    722    346      0       N
ATOM    524  N   THR A  60      -2.651  11.569  16.488  1.00 14.67           N
ANISOU  524  N   THR A  60     1327   1742   2503    -14    477    -27       N
ATOM    525  CA  THR A  60      -1.828  12.781  16.586  1.00 15.23           C
ANISOU  525  CA  THR A  60     1649   1653   2481    -67    369    -47       C
ATOM    526  C   THR A  60      -1.707  13.391  15.191  1.00 14.53           C
ANISOU  526  C   THR A  60     1379   1661   2480     13    410    -10       C
ATOM    527  O   THR A  60      -1.804  12.710  14.170  1.00 14.11           O
ANISOU  527  O   THR A  60     1098   1721   2542   -164    347     20       O
ATOM    528  CB  THR A  60      -0.440  12.526  17.150  1.00 15.74           C
ANISOU  528  CB  THR A  60     1676   1873   2431    -18    226     56       C
ATOM    529  OG1 THR A  60       0.291  11.680  16.281  1.00 16.41           O
ANISOU  529  OG1 THR A  60     1691   1885   2656    -73    214     84       O
ATOM    530  CG2 THR A  60      -0.444  11.948  18.576  1.00 16.95           C
ANISOU  530  CG2 THR A  60     1469   2359   2611    190    159    199       C
ATOM    531  N   GLU A  61      -1.432  14.685  15.148  1.00 14.45           N
ANISOU  531  N   GLU A  61     1458   1559   2470   -109    537    -56       N
ATOM    532  CA  GLU A  61      -1.190  15.394  13.869  1.00 13.96           C
ANISOU  532  CA  GLU A  61      945   1746   2611    -58    402    -19       C
ATOM    533  C   GLU A  61      -0.264  16.541  14.188  1.00 13.94           C
ANISOU  533  C   GLU A  61     1066   1607   2623   -249    355   -152       C
ATOM    534  O   GLU A  61      -0.509  17.342  15.156  1.00 16.28           O
ANISOU  534  O   GLU A  61     1671   1708   2805   -208    647   -221       O
ATOM    535  CB  GLU A  61      -2.482  15.863  13.285  1.00 15.15           C
ANISOU  535  CB  GLU A  61      902   1991   2862    -74    233    -55       C
ATOM    536  CG  GLU A  61      -2.340  16.632  11.999  1.00 19.49           C
ANISOU  536  CG  GLU A  61      758   3105   3540    -86    518    316       C
ATOM    537  CD  GLU A  61      -3.605  17.159  11.438  1.00 25.79           C
ANISOU  537  CD  GLU A  61      647   4501   4648     99    482    237       C
ATOM    538  OE1 GLU A  61      -3.498  18.001  10.530  1.00 33.86           O
ANISOU  538  OE1 GLU A  61     2671   4783   5410   -626    127    626       O
ATOM    539  OE2 GLU A  61      -4.688  16.778  11.877  1.00 31.84           O
ANISOU  539  OE2 GLU A  61     1209   5229   5659   -125   -163    553       O
ATOM    540  N   ILE A  62       0.844  16.630  13.481  1.00 12.11           N
ANISOU  540  N   ILE A  62      741   1520   2339   -143    195   -123       N
ATOM    541  CA  ILE A  62       1.761  17.745  13.570  1.00 12.25           C
ANISOU  541  CA  ILE A  62      854   1560   2237   -274    102   -145       C
ATOM    542  C   ILE A  62       1.915  18.327  12.171  1.00 12.04           C
ANISOU  542  C   ILE A  62      960   1573   2040   -190     51   -124       C
ATOM    543  O   ILE A  62       2.024  17.610  11.193  1.00 13.31           O
ANISOU  543  O   ILE A  62     1655   1391   2009   -200     88      4       O
ATOM    544  CB  ILE A  62       3.122  17.383  14.210  1.00 12.73           C
ANISOU  544  CB  ILE A  62      903   1741   2192   -349     66   -106       C
ATOM    545  CG1 ILE A  62       3.832  16.278  13.452  1.00 12.93           C
ANISOU  545  CG1 ILE A  62      780   1819   2311   -344    -23   -132       C
ATOM    546  CG2 ILE A  62       2.903  16.978  15.681  1.00 15.20           C
ANISOU  546  CG2 ILE A  62     1616   2020   2138     97     49    100       C
ATOM    547  CD1 ILE A  62       5.291  16.006  13.929  1.00 15.91           C
ANISOU  547  CD1 ILE A  62     1039   2169   2834   -349    -74   -223       C
ATOM    548  N   SER A  63       1.993  19.646  12.110  1.00 11.28           N
ANISOU  548  N   SER A  63      798   1475   2011    -22    -33    -75       N
ATOM    549  CA  SER A  63       2.323  20.383  10.898  1.00 11.06           C
ANISOU  549  CA  SER A  63      566   1550   2085    -63     49    -87       C
ATOM    550  C   SER A  63       3.456  21.333  11.229  1.00 10.88           C
ANISOU  550  C   SER A  63      261   1566   2305    -53    111   -109       C
ATOM    551  O   SER A  63       3.462  21.949  12.307  1.00 12.66           O
ANISOU  551  O   SER A  63      872   1658   2279   -212    306   -247       O
ATOM    552  CB  SER A  63       1.190  21.154  10.299  1.00 12.26           C
ANISOU  552  CB  SER A  63      918   1602   2137     91     15    -74       C
ATOM    553  OG  SER A  63       0.123  20.311   9.864  1.00 14.06           O
ANISOU  553  OG  SER A  63      795   1993   2553     47   -134     49       O
ATOM    554  N   PHE A  64       4.453  21.442  10.381  1.00 10.04           N
ANISOU  554  N   PHE A  64      332   1393   2088    -10    -88   -125       N
ATOM    555  CA  PHE A  64       5.657  22.143  10.686  1.00 10.64           C
ANISOU  555  CA  PHE A  64      294   1550   2195   -113    -10    -17       C
ATOM    556  C   PHE A  64       6.376  22.579   9.407  1.00 10.64           C
ANISOU  556  C   PHE A  64      378   1511   2153    178    -84     27       C
ATOM    557  O   PHE A  64       6.164  22.035   8.329  1.00 11.05           O
ANISOU  557  O   PHE A  64      623   1498   2077   -132     22    -20       O
ATOM    558  CB  PHE A  64       6.598  21.322  11.589  1.00 11.23           C
ANISOU  558  CB  PHE A  64      480   1521   2263    -82   -153      0       C
ATOM    559  CG  PHE A  64       6.945  19.989  10.967  1.00 11.39           C
ANISOU  559  CG  PHE A  64      568   1563   2193   -114   -190     39       C
ATOM    560  CD1 PHE A  64       6.164  18.912  11.134  1.00 11.61           C
ANISOU  560  CD1 PHE A  64      473   1710   2227   -141    -36    -20       C
ATOM    561  CD2 PHE A  64       8.081  19.862  10.232  1.00 11.38           C
ANISOU  561  CD2 PHE A  64      588   1624   2111   -119    -18     42       C
ATOM    562  CE1 PHE A  64       6.399  17.712  10.493  1.00 12.38           C
ANISOU  562  CE1 PHE A  64      579   1754   2371    -11   -200     81       C
ATOM    563  CE2 PHE A  64       8.343  18.657   9.613  1.00 12.87           C
ANISOU  563  CE2 PHE A  64      821   1837   2228    189     15     46       C
ATOM    564  CZ  PHE A  64       7.528  17.558   9.826  1.00 12.97           C
ANISOU  564  CZ  PHE A  64     1017   1500   2409    110   -357    -31       C
ATOM    565  N   ILE A  65       7.284  23.532   9.573  1.00 11.18           N
ANISOU  565  N   ILE A  65      313   1542   2393   -188    -89   -191       N
ATOM    566  CA  ILE A  65       8.267  23.958   8.594  1.00 11.23           C
ANISOU  566  CA  ILE A  65      258   1468   2541    -38     95   -142       C
ATOM    567  C   ILE A  65       9.641  23.535   9.074  1.00 10.73           C
ANISOU  567  C   ILE A  65      421   1296   2359   -103    271      5       C
ATOM    568  O   ILE A  65       9.918  23.658  10.263  1.00 10.75           O
ANISOU  568  O   ILE A  65      466   1385   2232   -109     -8    -57       O
ATOM    569  CB  ILE A  65       8.149  25.471   8.358  1.00 12.32           C
ANISOU  569  CB  ILE A  65      706   1428   2544    -75     81    -54       C
ATOM    570  CG1 ILE A  65       6.743  25.795   7.801  1.00 13.37           C
ANISOU  570  CG1 ILE A  65      553   1693   2832    -69     92    -14       C
ATOM    571  CG2 ILE A  65       9.216  25.959   7.448  1.00 12.94           C
ANISOU  571  CG2 ILE A  65      557   1669   2688    -79   -135    157       C
ATOM    572  CD1 ILE A  65       6.499  27.334   7.708  1.00 16.08           C
ANISOU  572  CD1 ILE A  65      895   1853   3361    220   -155    156       C
ATOM    573  N   LEU A  66      10.441  22.974   8.212  1.00 11.11           N
ANISOU  573  N   LEU A  66      668   1404   2149    116    -32     65       N
ATOM    574  CA  LEU A  66      11.733  22.503   8.591  1.00 11.64           C
ANISOU  574  CA  LEU A  66      808   1316   2295    166     -7     37       C
ATOM    575  C   LEU A  66      12.560  23.611   9.255  1.00 11.49           C
ANISOU  575  C   LEU A  66      651   1297   2416    -51     -1     10       C
ATOM    576  O   LEU A  66      12.625  24.743   8.736  1.00 12.05           O
ANISOU  576  O   LEU A  66      765   1361   2452    -57    -86    112       O
ATOM    577  CB  LEU A  66      12.496  21.895   7.383  1.00 12.33           C
ANISOU  577  CB  LEU A  66      571   1489   2624    126    -46     80       C
ATOM    578  CG  LEU A  66      11.896  20.658   6.741  1.00 13.11           C
ANISOU  578  CG  LEU A  66     1155   1482   2343    158    -89   -155       C
ATOM    579  CD1 LEU A  66      12.542  20.342   5.391  1.00 18.02           C
ANISOU  579  CD1 LEU A  66     2084   2197   2563     74     85   -238       C
ATOM    580  CD2 LEU A  66      11.939  19.505   7.700  1.00 13.85           C
ANISOU  580  CD2 LEU A  66      851   1663   2745     16   -425   -211       C
ATOM    581  N   GLY A  67      13.214  23.288  10.356  1.00 11.35           N
ANISOU  581  N   GLY A  67      654   1361   2297   -145    -94    140       N
ATOM    582  CA  GLY A  67      14.049  24.216  11.084  1.00 11.99           C
ANISOU  582  CA  GLY A  67      787   1436   2330   -125    -45     18       C
ATOM    583  C   GLY A  67      13.287  25.121  12.043  1.00 11.29           C
ANISOU  583  C   GLY A  67      510   1439   2338   -164     62    210       C
ATOM    584  O   GLY A  67      14.023  25.875  12.744  1.00 12.31           O
ANISOU  584  O   GLY A  67      403   1607   2666   -194   -125     32       O
ATOM    585  N   GLN A  68      11.990  25.078  12.090  1.00 10.75           N
ANISOU  585  N   GLN A  68      283   1354   2448   -180     18    -75       N
ATOM    586  CA  GLN A  68      11.195  26.051  12.863  1.00 11.37           C
ANISOU  586  CA  GLN A  68      482   1194   2643   -148    -34   -153       C
ATOM    587  C   GLN A  68      10.501  25.329  14.001  1.00 10.65           C
ANISOU  587  C   GLN A  68      254   1276   2516    -33     20    -44       C
ATOM    588  O   GLN A  68       9.594  24.529  13.819  1.00 11.28           O
ANISOU  588  O   GLN A  68      269   1416   2600   -132    -25   -163       O
ATOM    589  CB  GLN A  68      10.191  26.746  11.930  1.00 12.60           C
ANISOU  589  CB  GLN A  68      943   1111   2731     40   -215   -157       C
ATOM    590  CG  GLN A  68      11.003  27.447  10.796  1.00 14.91           C
ANISOU  590  CG  GLN A  68     1212   1567   2885   -266   -566    -39       C
ATOM    591  CD  GLN A  68      10.266  28.435  10.006  1.00 15.87           C
ANISOU  591  CD  GLN A  68     1171   1603   3255    -28   -543     44       C
ATOM    592  OE1 GLN A  68       9.085  28.729  10.229  1.00 19.24           O
ANISOU  592  OE1 GLN A  68     1429   1799   4080     91  -1058    172       O
ATOM    593  NE2 GLN A  68      10.994  28.981   9.015  1.00 18.22           N
ANISOU  593  NE2 GLN A  68     2239   1671   3010   -246   -474    232       N
ATOM    594  N   GLU A  69      10.833  25.712  15.237  1.00 11.58           N
ANISOU  594  N   GLU A  69      777   1254   2367     40    -95    -77       N
ATOM    595  CA  GLU A  69      10.326  25.056  16.419  1.00 11.85           C
ANISOU  595  CA  GLU A  69      730   1363   2408     30   -266     39       C
ATOM    596  C   GLU A  69       8.845  25.230  16.573  1.00 11.07           C
ANISOU  596  C   GLU A  69      507   1433   2263     25   -161    -74       C
ATOM    597  O   GLU A  69       8.296  26.284  16.220  1.00 12.25           O
ANISOU  597  O   GLU A  69      571   1434   2648     81   -102    -50       O
ATOM    598  CB  GLU A  69      11.070  25.658  17.628  1.00 13.76           C
ANISOU  598  CB  GLU A  69      468   2163   2594    -56   -123    230       C
ATOM    599  CG  GLU A  69      10.707  25.090  18.992  1.00 18.64           C
ANISOU  599  CG  GLU A  69     1613   2575   2891    -14   -189     43       C
ATOM    600  CD  GLU A  69      11.564  25.744  20.054  1.00 26.19           C
ANISOU  600  CD  GLU A  69     3240   3562   3146   -431   -340    -88       C
ATOM    601  OE1 GLU A  69      11.488  27.004  20.241  1.00 31.72           O
ANISOU  601  OE1 GLU A  69     3845   4214   3991   -610   -754   -732       O
ATOM    602  OE2 GLU A  69      12.313  24.986  20.682  1.00 29.57           O
ANISOU  602  OE2 GLU A  69     3297   4710   3225   -472   -627      4       O
ATOM    603  N   PHE A  70       8.188  24.213  17.133  1.00 10.68           N
ANISOU  603  N   PHE A  70      549   1329   2179    149   -188   -113       N
ATOM    604  CA  PHE A  70       6.782  24.209  17.365  1.00 10.46           C
ANISOU  604  CA  PHE A  70      351   1408   2213    131    -66    -22       C
ATOM    605  C   PHE A  70       6.499  23.467  18.660  1.00 10.89           C
ANISOU  605  C   PHE A  70      322   1448   2365    223   -245    -26       C
ATOM    606  O   PHE A  70       7.280  22.698  19.136  1.00 12.27           O
ANISOU  606  O   PHE A  70      686   1656   2320    229      5   -138       O
ATOM    607  CB  PHE A  70       6.024  23.629  16.165  1.00 10.90           C
ANISOU  607  CB  PHE A  70      418   1498   2227     82     62      2       C
ATOM    608  CG  PHE A  70       6.405  22.197  15.810  1.00 10.66           C
ANISOU  608  CG  PHE A  70      267   1586   2196     33   -164    -39       C
ATOM    609  CD1 PHE A  70       7.505  21.929  15.071  1.00 10.61           C
ANISOU  609  CD1 PHE A  70      283   1438   2308    187    -23     13       C
ATOM    610  CD2 PHE A  70       5.585  21.148  16.221  1.00 13.03           C
ANISOU  610  CD2 PHE A  70      795   1766   2388   -286    287   -302       C
ATOM    611  CE1 PHE A  70       7.814  20.600  14.702  1.00 11.33           C
ANISOU  611  CE1 PHE A  70      395   1653   2256     62    -94     54       C
ATOM    612  CE2 PHE A  70       5.859  19.853  15.888  1.00 14.10           C
ANISOU  612  CE2 PHE A  70     1365   1658   2332   -301    378   -113       C
ATOM    613  CZ  PHE A  70       6.969  19.577  15.169  1.00 12.83           C
ANISOU  613  CZ  PHE A  70     1091   1659   2124    -39   -139    -40       C
ATOM    614  N   ASP A  71       5.270  23.644  19.103  1.00 12.06           N
ANISOU  614  N   ASP A  71      593   1653   2334    367    -86     57       N
ATOM    615  CA  ASP A  71       4.741  22.913  20.276  1.00 13.22           C
ANISOU  615  CA  ASP A  71      900   1780   2343    294     55     93       C
ATOM    616  C   ASP A  71       4.036  21.670  19.808  1.00 13.97           C
ANISOU  616  C   ASP A  71      889   1930   2489     18    -26    144       C
ATOM    617  O   ASP A  71       3.303  21.678  18.810  1.00 14.91           O
ANISOU  617  O   ASP A  71     1200   1834   2628    131    -57    132       O
ATOM    618  CB  ASP A  71       3.635  23.752  20.943  1.00 14.54           C
ANISOU  618  CB  ASP A  71     1272   2041   2211    364    144     80       C
ATOM    619  CG  ASP A  71       4.160  24.933  21.627  1.00 16.41           C
ANISOU  619  CG  ASP A  71     1013   2538   2683    597      7      3       C
ATOM    620  OD1 ASP A  71       5.097  24.759  22.416  1.00 18.78           O
ANISOU  620  OD1 ASP A  71     1696   2431   3007    484   -485   -279       O
ATOM    621  OD2 ASP A  71       3.631  26.040  21.401  1.00 15.78           O
ANISOU  621  OD2 ASP A  71      806   2299   2891    149   -145   -128       O
ATOM    622  N   GLU A  72       4.236  20.571  20.546  1.00 13.43           N
ANISOU  622  N   GLU A  72      668   1911   2522    -10     37    234       N
ATOM    623  CA  GLU A  72       3.687  19.257  20.191  1.00 14.61           C
ANISOU  623  CA  GLU A  72      949   2047   2554    -74     89    337       C
ATOM    624  C   GLU A  72       3.206  18.627  21.506  1.00 14.36           C
ANISOU  624  C   GLU A  72      683   2170   2602     48    227    312       C
ATOM    625  O   GLU A  72       3.843  18.643  22.527  1.00 15.84           O
ANISOU  625  O   GLU A  72      949   2455   2614   -195    200    315       O
ATOM    626  CB  GLU A  72       4.788  18.388  19.524  1.00 13.86           C
ANISOU  626  CB  GLU A  72      959   1825   2482     63    254    337       C
ATOM    627  CG  GLU A  72       4.386  16.926  19.214  1.00 14.77           C
ANISOU  627  CG  GLU A  72      572   2304   2736     42   -126    636       C
ATOM    628  CD  GLU A  72       5.476  16.146  18.556  1.00 13.29           C
ANISOU  628  CD  GLU A  72      536   2192   2319   -133     51    261       C
ATOM    629  OE1 GLU A  72       6.606  16.538  18.495  1.00 14.70           O
ANISOU  629  OE1 GLU A  72      912   2118   2554     30    127   -136       O
ATOM    630  OE2 GLU A  72       5.131  15.005  18.069  1.00 17.33           O
ANISOU  630  OE2 GLU A  72     1713   1918   2952   -139     73     70       O
ATOM    631  N   VAL A  73       2.041  18.045  21.429  1.00 15.29           N
ANISOU  631  N   VAL A  73      980   2093   2735    141    165    546       N
ATOM    632  CA  VAL A  73       1.481  17.190  22.518  1.00 15.81           C
ANISOU  632  CA  VAL A  73      790   2235   2981   -119     76    478       C
ATOM    633  C   VAL A  73       1.608  15.754  22.005  1.00 16.00           C
ANISOU  633  C   VAL A  73     1075   2293   2711      3     68    312       C
ATOM    634  O   VAL A  73       1.017  15.374  21.025  1.00 18.14           O
ANISOU  634  O   VAL A  73     1690   2042   3158   -126   -374    567       O
ATOM    635  CB  VAL A  73       0.100  17.523  22.898  1.00 16.76           C
ANISOU  635  CB  VAL A  73      590   2474   3304    -28    299    505       C
ATOM    636  CG1 VAL A  73      -0.343  16.507  23.970  1.00 20.99           C
ANISOU  636  CG1 VAL A  73     1302   2990   3684     50    627    686       C
ATOM    637  CG2 VAL A  73       0.043  18.980  23.411  1.00 20.16           C
ANISOU  637  CG2 VAL A  73      913   2633   4113    125    562    347       C
ATOM    638  N   THR A  74       2.535  14.977  22.578  1.00 14.27           N
ANISOU  638  N   THR A  74      707   2169   2543     51     77    201       N
ATOM    639  CA  THR A  74       2.806  13.620  22.065  1.00 14.01           C
ANISOU  639  CA  THR A  74      743   2236   2342   -246    -16    162       C
ATOM    640  C   THR A  74       1.697  12.640  22.409  1.00 14.29           C
ANISOU  640  C   THR A  74      583   2272   2572     10    -19    294       C
ATOM    641  O   THR A  74       0.815  12.919  23.204  1.00 15.85           O
ANISOU  641  O   THR A  74      922   2198   2899    -69    387    400       O
ATOM    642  CB  THR A  74       4.153  13.115  22.575  1.00 13.58           C
ANISOU  642  CB  THR A  74      606   2222   2331   -149     63    -16       C
ATOM    643  OG1 THR A  74       4.008  12.901  23.992  1.00 14.73           O
ANISOU  643  OG1 THR A  74     1301   2045   2249    271    183    230       O
ATOM    644  CG2 THR A  74       5.195  14.069  22.327  1.00 13.80           C
ANISOU  644  CG2 THR A  74      323   2218   2702     -9   -130    -90       C
ATOM    645  N   ALA A  75       1.744  11.478  21.783  1.00 15.21           N
ANISOU  645  N   ALA A  75      877   2252   2648     73    108    301       N
ATOM    646  CA  ALA A  75       0.657  10.487  21.948  1.00 16.11           C
ANISOU  646  CA  ALA A  75     1258   2315   2546   -107     25    316       C
ATOM    647  C   ALA A  75       0.567  10.084  23.431  1.00 16.55           C
ANISOU  647  C   ALA A  75     1241   2370   2675     13    233    325       C
ATOM    648  O   ALA A  75      -0.504   9.802  23.914  1.00 18.73           O
ANISOU  648  O   ALA A  75     1338   2660   3117   -275    283    373       O
ATOM    649  CB  ALA A  75       0.989   9.289  21.091  1.00 17.66           C
ANISOU  649  CB  ALA A  75     1616   2302   2790     13     86    348       C
ATOM    650  N   ASP A  76       1.684  10.015  24.111  1.00 16.52           N
ANISOU  650  N   ASP A  76     1433   2230   2613     37    271    384       N
ATOM    651  CA  ASP A  76       1.748   9.738  25.563  1.00 16.94           C
ANISOU  651  CA  ASP A  76     1541   2393   2502    -68    196    348       C
ATOM    652  C   ASP A  76       1.534  10.988  26.442  1.00 18.39           C
ANISOU  652  C   ASP A  76     1827   2560   2600     16    315    300       C
ATOM    653  O   ASP A  76       1.731  10.929  27.660  1.00 21.39           O
ANISOU  653  O   ASP A  76     2591   2993   2543    197    244    341       O
ATOM    654  CB  ASP A  76       3.089   9.040  25.919  1.00 17.49           C
ANISOU  654  CB  ASP A  76     1744   2191   2708    -12    181    333       C
ATOM    655  CG  ASP A  76       4.289   9.869  25.633  1.00 15.62           C
ANISOU  655  CG  ASP A  76     1413   2040   2481    101    -17    424       C
ATOM    656  OD1 ASP A  76       4.448  10.303  24.465  1.00 16.15           O
ANISOU  656  OD1 ASP A  76     1207   2382   2546    254     22    459       O
ATOM    657  OD2 ASP A  76       5.091  10.106  26.552  1.00 17.88           O
ANISOU  657  OD2 ASP A  76     1912   2093   2786    110   -157    511       O
ATOM    658  N   ASP A  77       1.113  12.102  25.835  1.00 18.35           N
ANISOU  658  N   ASP A  77     1898   2423   2649     41    432    348       N
ATOM    659  CA  ASP A  77       0.695  13.337  26.545  1.00 20.02           C
ANISOU  659  CA  ASP A  77     2152   2745   2708    -46    517    214       C
ATOM    660  C   ASP A  77       1.831  14.132  27.181  1.00 18.94           C
ANISOU  660  C   ASP A  77     1836   2615   2745    -49    414    128       C
ATOM    661  O   ASP A  77       1.641  14.864  28.169  1.00 20.81           O
ANISOU  661  O   ASP A  77     1866   2958   3083   -123    648   -127       O
ATOM    662  CB  ASP A  77      -0.429  13.078  27.552  1.00 21.13           C
ANISOU  662  CB  ASP A  77     2095   2989   2941   -125    464    187       C
ATOM    663  CG  ASP A  77      -1.348  14.268  27.750  1.00 26.30           C
ANISOU  663  CG  ASP A  77     3026   3595   3371    136    807    244       C
ATOM    664  OD1 ASP A  77      -2.003  14.301  28.809  1.00 31.46           O
ANISOU  664  OD1 ASP A  77     3534   4452   3966    349   1158     23       O
ATOM    665  OD2 ASP A  77      -1.463  15.157  26.868  1.00 29.80           O
ANISOU  665  OD2 ASP A  77     3340   3950   4032    426    855    597       O
ATOM    666  N   ARG A  78       3.032  14.032  26.627  1.00 17.58           N
ANISOU  666  N   ARG A  78     1826   2408   2445    123    275    202       N
ATOM    667  CA  ARG A  78       4.064  15.008  26.963  1.00 15.73           C
ANISOU  667  CA  ARG A  78     1391   2207   2375    279    278    249       C
ATOM    668  C   ARG A  78       3.793  16.280  26.149  1.00 14.59           C
ANISOU  668  C   ARG A  78     1008   2139   2396    138    273    138       C
ATOM    669  O   ARG A  78       3.517  16.223  24.952  1.00 16.74           O
ANISOU  669  O   ARG A  78     1759   2112   2489    425    261    147       O
ATOM    670  CB  ARG A  78       5.427  14.509  26.657  1.00 15.82           C
ANISOU  670  CB  ARG A  78     1538   1928   2543    257    226    353       C
ATOM    671  CG  ARG A  78       6.009  13.395  27.598  1.00 16.60           C
ANISOU  671  CG  ARG A  78     1718   2061   2527    247     32    364       C
ATOM    672  CD  ARG A  78       7.353  12.845  27.040  1.00 15.79           C
ANISOU  672  CD  ARG A  78     1639   1766   2593    192   -235    254       C
ATOM    673  NE  ARG A  78       7.064  11.974  25.899  1.00 15.78           N
ANISOU  673  NE  ARG A  78     1750   1777   2468    176     19    195       N
ATOM    674  CZ  ARG A  78       7.633  12.027  24.700  1.00 14.86           C
ANISOU  674  CZ  ARG A  78     1088   1996   2561    240   -174    -91       C
ATOM    675  NH1 ARG A  78       8.702  12.786  24.440  1.00 15.50           N
ANISOU  675  NH1 ARG A  78     1249   1884   2754     59    -41    -87       N
ATOM    676  NH2 ARG A  78       7.144  11.223  23.782  1.00 15.52           N
ANISOU  676  NH2 ARG A  78     1277   2022   2596    140    -71     33       N
ATOM    677  N   LYS A  79       4.075  17.415  26.784  1.00 16.37           N
ANISOU  677  N   LYS A  79     1767   2049   2400     81    486    163       N
ATOM    678  CA  LYS A  79       4.068  18.710  26.118  1.00 16.01           C
ANISOU  678  CA  LYS A  79     1401   2194   2486    409    360    113       C
ATOM    679  C   LYS A  79       5.510  19.034  25.822  1.00 15.19           C
ANISOU  679  C   LYS A  79     1278   2053   2438    320    262    122       C
ATOM    680  O   LYS A  79       6.295  19.302  26.725  1.00 18.20           O
ANISOU  680  O   LYS A  79     2058   2422   2434    189    308    -55       O
ATOM    681  CB  LYS A  79       3.370  19.744  27.015  1.00 18.11           C
ANISOU  681  CB  LYS A  79     1825   2310   2746    294    541    123       C
ATOM    682  CG  LYS A  79       1.887  19.498  27.221  1.00 23.79           C
ANISOU  682  CG  LYS A  79     2595   3087   3354    382    511   -121       C
ATOM    683  CD  LYS A  79       1.554  18.367  28.106  1.00 29.46           C
ANISOU  683  CD  LYS A  79     3324   3595   4273    311    359    112       C
ATOM    684  CE  LYS A  79       0.144  18.453  28.613  1.00 31.91           C
ANISOU  684  CE  LYS A  79     3627   3949   4547    177    525    242       C
ATOM    685  NZ  LYS A  79      -0.415  17.096  28.708  1.00 32.97           N
ANISOU  685  NZ  LYS A  79     3783   3476   5265    550    486    177       N
ATOM    686  N   VAL A  80       5.827  19.003  24.537  1.00 13.67           N
ANISOU  686  N   VAL A  80      937   1983   2272    214    159     36       N
ATOM    687  CA  VAL A  80       7.231  19.120  24.136  1.00 13.93           C
ANISOU  687  CA  VAL A  80     1236   1789   2267    132    -38     87       C
ATOM    688  C   VAL A  80       7.432  20.314  23.157  1.00 13.13           C
ANISOU  688  C   VAL A  80     1098   1825   2065    411    284   -105       C
ATOM    689  O   VAL A  80       6.452  20.766  22.559  1.00 14.26           O
ANISOU  689  O   VAL A  80     1143   1835   2441    244     94     44       O
ATOM    690  CB  VAL A  80       7.774  17.796  23.498  1.00 13.11           C
ANISOU  690  CB  VAL A  80      763   1796   2420     64    140     88       C
ATOM    691  CG1 VAL A  80       7.520  16.575  24.439  1.00 15.33           C
ANISOU  691  CG1 VAL A  80     1316   1913   2594    233     78    273       C
ATOM    692  CG2 VAL A  80       7.224  17.553  22.128  1.00 15.76           C
ANISOU  692  CG2 VAL A  80     1680   2013   2294    357    135    122       C
ATOM    693  N   LYS A  81       8.682  20.743  23.064  1.00 12.97           N
ANISOU  693  N   LYS A  81     1215   1736   1977    208    168    -53       N
ATOM    694  CA  LYS A  81       9.070  21.717  22.060  1.00 12.77           C
ANISOU  694  CA  LYS A  81      833   1747   2272     60    -33    -57       C
ATOM    695  C   LYS A  81       9.847  20.889  21.046  1.00 12.00           C
ANISOU  695  C   LYS A  81      811   1643   2103    228     27   -128       C
ATOM    696  O   LYS A  81      10.856  20.283  21.381  1.00 13.20           O
ANISOU  696  O   LYS A  81      871   1909   2235    266    -47    -90       O
ATOM    697  CB  LYS A  81       9.977  22.804  22.667  1.00 15.59           C
ANISOU  697  CB  LYS A  81     1574   1910   2439    -32    -24    -41       C
ATOM    698  CG  LYS A  81       9.375  23.593  23.740  1.00 22.12           C
ANISOU  698  CG  LYS A  81     2606   2813   2985    -82    210   -119       C
ATOM    699  CD  LYS A  81       8.420  24.594  23.216  1.00 26.62           C
ANISOU  699  CD  LYS A  81     3312   3371   3432    101     63    -73       C
ATOM    700  CE  LYS A  81       8.008  25.596  24.288  1.00 29.43           C
ANISOU  700  CE  LYS A  81     3707   3779   3692     93    -97   -422       C
ATOM    701  NZ  LYS A  81       6.705  26.226  24.022  1.00 30.66           N
ANISOU  701  NZ  LYS A  81     3984   3992   3672    125   -627   -451       N
ATOM    702  N   SER A  82       9.446  20.961  19.795  1.00 11.47           N
ANISOU  702  N   SER A  82      443   1605   2310    383     62    -22       N
ATOM    703  CA  SER A  82       9.973  20.117  18.726  1.00 11.45           C
ANISOU  703  CA  SER A  82      663   1414   2271    153     10     87       C
ATOM    704  C   SER A  82      10.576  20.925  17.602  1.00 10.12           C
ANISOU  704  C   SER A  82      299   1307   2237    188   -133    118       C
ATOM    705  O   SER A  82      10.057  21.971  17.237  1.00 11.42           O
ANISOU  705  O   SER A  82      597   1415   2326    188     -5    -24       O
ATOM    706  CB  SER A  82       8.840  19.299  18.162  1.00 11.89           C
ANISOU  706  CB  SER A  82      549   1683   2284    174    276     77       C
ATOM    707  OG  SER A  82       8.458  18.298  19.098  1.00 13.82           O
ANISOU  707  OG  SER A  82     1036   1624   2590    202    281    340       O
ATOM    708  N   THR A  83      11.653  20.425  17.078  1.00 10.57           N
ANISOU  708  N   THR A  83      461   1409   2143    237   -114     75       N
ATOM    709  CA  THR A  83      12.274  20.979  15.849  1.00 10.96           C
ANISOU  709  CA  THR A  83      672   1319   2173     33    -61     68       C
ATOM    710  C   THR A  83      12.570  19.847  14.903  1.00 10.50           C
ANISOU  710  C   THR A  83      651   1343   1996    109     24    102       C
ATOM    711  O   THR A  83      13.198  18.865  15.327  1.00 12.49           O
ANISOU  711  O   THR A  83     1268   1488   1988    217    -27     10       O
ATOM    712  CB  THR A  83      13.500  21.771  16.159  1.00 13.26           C
ANISOU  712  CB  THR A  83     1048   1604   2382   -102     44     15       C
ATOM    713  OG1 THR A  83      13.254  22.719  17.187  1.00 14.60           O
ANISOU  713  OG1 THR A  83      916   1830   2801   -211      7   -373       O
ATOM    714  CG2 THR A  83      13.928  22.512  14.916  1.00 15.12           C
ANISOU  714  CG2 THR A  83     1357   1675   2713   -403    -51   -127       C
ATOM    715  N   ILE A  84      12.160  19.953  13.648  1.00 10.89           N
ANISOU  715  N   ILE A  84      712   1252   2172    215     49     44       N
ATOM    716  CA  ILE A  84      12.385  18.899  12.658  1.00 10.82           C
ANISOU  716  CA  ILE A  84      735   1228   2147    157    221     74       C
ATOM    717  C   ILE A  84      13.206  19.507  11.541  1.00 11.26           C
ANISOU  717  C   ILE A  84      657   1519   2102     98     -4     38       C
ATOM    718  O   ILE A  84      12.837  20.583  11.012  1.00 11.61           O
ANISOU  718  O   ILE A  84      827   1386   2195     90     20    105       O
ATOM    719  CB  ILE A  84      11.046  18.321  12.149  1.00 10.89           C
ANISOU  719  CB  ILE A  84      714   1400   2023     56    198     94       C
ATOM    720  CG1 ILE A  84      10.266  17.690  13.315  1.00 11.22           C
ANISOU  720  CG1 ILE A  84      354   1567   2339    358    105     83       C
ATOM    721  CG2 ILE A  84      11.374  17.224  11.103  1.00 11.96           C
ANISOU  721  CG2 ILE A  84      777   1462   2304    107    146    -11       C
ATOM    722  CD1 ILE A  84       8.917  17.142  13.009  1.00 12.26           C
ANISOU  722  CD1 ILE A  84      522   1738   2395    169    104    179       C
ATOM    723  N   THR A  85      14.322  18.856  11.204  1.00 11.08           N
ANISOU  723  N   THR A  85      748   1231   2228     17    119    135       N
ATOM    724  CA  THR A  85      15.185  19.260  10.119  1.00 11.97           C
ANISOU  724  CA  THR A  85      688   1477   2382     27    199    116       C
ATOM    725  C   THR A  85      15.444  18.052   9.197  1.00 12.96           C
ANISOU  725  C   THR A  85     1199   1466   2258   -101    206     38       C
ATOM    726  O   THR A  85      15.114  16.930   9.521  1.00 14.11           O
ANISOU  726  O   THR A  85     1731   1520   2109    -18    346    -30       O
ATOM    727  CB  THR A  85      16.469  19.795  10.641  1.00 13.38           C
ANISOU  727  CB  THR A  85      885   1621   2576    -75    186     44       C
ATOM    728  OG1 THR A  85      17.146  18.805  11.463  1.00 15.91           O
ANISOU  728  OG1 THR A  85     1150   1992   2902    150   -183   -150       O
ATOM    729  CG2 THR A  85      16.233  21.115  11.419  1.00 15.99           C
ANISOU  729  CG2 THR A  85     1410   1833   2830   -106    -15   -430       C
ATOM    730  N  ALEU A  86      15.740  18.372   7.939  0.50 13.14           N
ANISOU  730  N  ALEU A  86     1111   1509   2371   -120    207     66       N
ATOM    731  N  BLEU A  86      16.205  18.259   8.137  0.50 12.93           N
ANISOU  731  N  BLEU A  86     1380   1344   2185   -183    292     42       N
ATOM    732  CA ALEU A  86      16.188  17.406   6.958  0.50 13.84           C
ANISOU  732  CA ALEU A  86     1247   1729   2282   -243    217     37       C
ATOM    733  CA BLEU A  86      16.801  17.166   7.378  0.50 12.57           C
ANISOU  733  CA BLEU A  86     1355   1350   2071   -193    194     62       C
ATOM    734  C  ALEU A  86      17.709  17.409   6.908  0.50 14.32           C
ANISOU  734  C  ALEU A  86     1224   1814   2402   -324    311     42       C
ATOM    735  C  BLEU A  86      18.285  17.077   7.656  0.50 12.90           C
ANISOU  735  C  BLEU A  86     1232   1534   2132   -265    206     85       C
ATOM    736  O  ALEU A  86      18.359  18.419   6.566  0.50 16.54           O
ANISOU  736  O  ALEU A  86     1059   2248   2976   -374    739    -28       O
ATOM    737  O  BLEU A  86      18.951  18.123   7.664  0.50 15.21           O
ANISOU  737  O  BLEU A  86     1760   1719   2299   -378    292     78       O
ATOM    738  CB ALEU A  86      15.626  17.755   5.587  0.50 15.24           C
ANISOU  738  CB ALEU A  86     1573   1850   2367   -197    103     25       C
ATOM    739  CB BLEU A  86      16.587  17.334   5.888  0.50 13.29           C
ANISOU  739  CB BLEU A  86     1380   1511   2157   -171    213     92       C
ATOM    740  CG ALEU A  86      14.470  16.916   5.040  0.50 18.62           C
ANISOU  740  CG ALEU A  86     1891   2404   2777   -169   -106    -76       C
ATOM    741  CG BLEU A  86      15.181  17.068   5.407  0.50 13.19           C
ANISOU  741  CG BLEU A  86      890   1758   2361   -726    -22    194       C
ATOM    742  CD1ALEU A  86      14.159  17.455   3.657  0.50 16.30           C
ANISOU  742  CD1ALEU A  86      917   2583   2692    165     16    104       C
ATOM    743  CD1BLEU A  86      15.054  17.605   3.978  0.50 16.43           C
ANISOU  743  CD1BLEU A  86     1502   2461   2280      6   -296     11       C
ATOM    744  CD2ALEU A  86      14.769  15.416   4.963  0.50 16.77           C
ANISOU  744  CD2ALEU A  86     2001   2135   2234    -47    -15   -253       C
ATOM    745  CD2BLEU A  86      14.892  15.555   5.448  0.50 14.68           C
ANISOU  745  CD2BLEU A  86     1082   2108   2387    -89    165   -208       C
ATOM    746  N  AASP A  87      18.309  16.286   7.264  0.50 14.04           N
ANISOU  746  N  AASP A  87      987   1976   2368   -319    357    102       N
ATOM    747  N  BASP A  87      18.781  15.846   7.836  0.50 12.76           N
ANISOU  747  N  BASP A  87     1050   1681   2115   -270    167    157       N
ATOM    748  CA AASP A  87      19.746  16.170   7.311  0.50 14.82           C
ANISOU  748  CA AASP A  87     1225   1954   2449   -284    220     29       C
ATOM    749  CA BASP A  87      20.192  15.498   7.809  0.50 14.07           C
ANISOU  749  CA BASP A  87     1139   1852   2352   -184     70    139       C
ATOM    750  C  AASP A  87      20.086  15.061   6.323  0.50 14.28           C
ANISOU  750  C  AASP A  87     1061   1932   2433   -207    214     44       C
ATOM    751  C  BASP A  87      20.391  14.529   6.664  0.50 13.55           C
ANISOU  751  C  BASP A  87     1015   1759   2374     16    155    232       C
ATOM    752  O  AASP A  87      19.860  13.887   6.616  0.50 15.04           O
ANISOU  752  O  AASP A  87     1259   1866   2587   -321    -34     68       O
ATOM    753  O  BASP A  87      20.057  13.333   6.753  0.50 13.37           O
ANISOU  753  O  BASP A  87      700   1738   2640      3     44    334       O
ATOM    754  CB AASP A  87      20.200  15.845   8.744  0.50 16.47           C
ANISOU  754  CB AASP A  87     1350   2229   2675   -304    164     60       C
ATOM    755  CB BASP A  87      20.570  14.780   9.093  0.50 14.55           C
ANISOU  755  CB BASP A  87      990   2023   2514    -76    -15    158       C
ATOM    756  CG AASP A  87      21.712  15.596   8.856  0.50 21.48           C
ANISOU  756  CG AASP A  87     2071   2913   3176   -190    -53   -100       C
ATOM    757  CG BASP A  87      22.010  14.353   9.135  0.50 16.99           C
ANISOU  757  CG BASP A  87     1521   2269   2663    -76   -119    -25       C
ATOM    758  OD1AASP A  87      22.160  14.957   9.832  0.50 27.50           O
ANISOU  758  OD1AASP A  87     3450   3406   3589     -1    -24     52       O
ATOM    759  OD1BASP A  87      22.820  14.791   8.298  0.50 23.05           O
ANISOU  759  OD1BASP A  87     2243   3114   3397   -438     40    368       O
ATOM    760  OD2AASP A  87      22.474  16.044   7.983  0.50 27.29           O
ANISOU  760  OD2AASP A  87     3218   3369   3781   -260     88      5       O
ATOM    761  OD2BASP A  87      22.359  13.572  10.054  0.50 22.31           O
ANISOU  761  OD2BASP A  87     2526   2812   3136     79    -48    372       O
ATOM    762  N  AGLY A  88      20.559  15.420   5.135  0.50 13.96           N
ANISOU  762  N  AGLY A  88     1037   1963   2304   -207    109     52       N
ATOM    763  N  BGLY A  88      20.934  15.033   5.572  0.50 13.71           N
ANISOU  763  N  BGLY A  88     1023   1686   2498    -36    213    251       N
ATOM    764  CA AGLY A  88      20.685  14.420   4.124  0.50 14.50           C
ANISOU  764  CA AGLY A  88     1224   2025   2258     11    121     18       C
ATOM    765  CA BGLY A  88      21.168  14.195   4.417  0.50 15.04           C
ANISOU  765  CA BGLY A  88     1314   2010   2390     36     92    130       C
ATOM    766  C  AGLY A  88      19.269  14.032   3.815  0.50 13.73           C
ANISOU  766  C  AGLY A  88      985   1991   2241    -75     98    -39       C
ATOM    767  C  BGLY A  88      19.981  13.298   4.089  0.50 15.28           C
ANISOU  767  C  BGLY A  88     1374   2077   2354     54    231    126       C
ATOM    768  O  AGLY A  88      18.450  14.905   3.639  0.50 15.25           O
ANISOU  768  O  AGLY A  88     1504   1986   2303    -38    176     73       O
ATOM    769  O  BGLY A  88      20.061  12.084   4.030  0.50 16.00           O
ANISOU  769  O  BGLY A  88     1255   2234   2590    177    229     -5       O
ATOM    770  N  AGLY A  89      18.981  12.742   3.747  0.50 13.28           N
ANISOU  770  N  AGLY A  89      969   2006   2071    -33    212   -117       N
ATOM    771  N  BGLY A  89      18.839  13.893   3.867  0.50 14.79           N
ANISOU  771  N  BGLY A  89     1213   2136   2271     -3    407     84       N
ATOM    772  CA AGLY A  89      17.644  12.248   3.471  0.50 13.15           C
ANISOU  772  CA AGLY A  89      951   1887   2155   -209    -51   -216       C
ATOM    773  CA BGLY A  89      17.656  13.100   3.534  0.50 14.54           C
ANISOU  773  CA BGLY A  89     1174   2075   2273    110    205     -1       C
ATOM    774  C  AGLY A  89      17.000  11.780   4.726  0.50 12.86           C
ANISOU  774  C  AGLY A  89      804   1876   2203   -108    -13   -238       C
ATOM    775  C  BGLY A  89      16.914  12.300   4.625  0.50 13.59           C
ANISOU  775  C  BGLY A  89      868   2034   2260   -172     97    -43       C
ATOM    776  O  AGLY A  89      16.090  10.990   4.679  0.50 13.25           O
ANISOU  776  O  AGLY A  89      783   1918   2331     21    -83   -300       O
ATOM    777  O  BGLY A  89      15.867  11.716   4.334  0.50 12.79           O
ANISOU  777  O  BGLY A  89      825   1826   2207    -85   -341     88       O
ATOM    778  N   VAL A  90      17.391  12.293   5.877  1.00 14.19           N
ANISOU  778  N   VAL A  90      899   2198   2295   -291    130   -191       N
ATOM    779  CA  VAL A  90      16.736  11.811   7.087  1.00 13.59           C
ANISOU  779  CA  VAL A  90     1046   1776   2339   -207    218    -88       C
ATOM    780  C   VAL A  90      15.996  12.961   7.754  1.00 12.12           C
ANISOU  780  C   VAL A  90      926   1583   2094   -170    -28    -84       C
ATOM    781  O   VAL A  90      16.618  14.013   7.982  1.00 12.65           O
ANISOU  781  O   VAL A  90      896   1710   2199   -253    106    -53       O
ATOM    782  CB  VAL A  90      17.800  11.249   8.080  1.00 13.94           C
ANISOU  782  CB  VAL A  90     1039   1721   2535    -28    306   -221       C
ATOM    783  CG1 VAL A  90      17.191  10.762   9.375  1.00 14.45           C
ANISOU  783  CG1 VAL A  90      887   2023   2581   -198    180     80       C
ATOM    784  CG2 VAL A  90      18.626  10.144   7.441  1.00 16.31           C
ANISOU  784  CG2 VAL A  90     1173   1911   3113     91    407   -229       C
ATOM    785  N   LEU A  91      14.735  12.774   8.062  1.00 11.24           N
ANISOU  785  N   LEU A  91      574   1559   2135   -332     65   -102       N
ATOM    786  CA  LEU A  91      14.013  13.750   8.876  1.00 11.41           C
ANISOU  786  CA  LEU A  91      880   1438   2015   -132    158     28       C
ATOM    787  C   LEU A  91      14.433  13.505  10.306  1.00 11.10           C
ANISOU  787  C   LEU A  91      785   1519   1912     82    272    -11       C
ATOM    788  O   LEU A  91      14.238  12.404  10.837  1.00 11.96           O
ANISOU  788  O   LEU A  91     1199   1346   1996      4    193     30       O
ATOM    789  CB  LEU A  91      12.519  13.585   8.735  1.00 12.92           C
ANISOU  789  CB  LEU A  91     1162   1578   2168    -82    189     56       C
ATOM    790  CG  LEU A  91      11.878  14.140   7.462  1.00 14.85           C
ANISOU  790  CG  LEU A  91     1378   1776   2488   -142     28     27       C
ATOM    791  CD1 LEU A  91      10.458  13.620   7.315  1.00 17.05           C
ANISOU  791  CD1 LEU A  91     1560   1988   2929   -284   -165     85       C
ATOM    792  CD2 LEU A  91      11.896  15.662   7.502  1.00 14.45           C
ANISOU  792  CD2 LEU A  91     1531   1399   2559    145    -39    152       C
ATOM    793  N   VAL A  92      14.945  14.525  10.962  1.00 11.02           N
ANISOU  793  N   VAL A  92      725   1399   2063    144    150      3       N
ATOM    794  CA  VAL A  92      15.398  14.450  12.355  1.00 10.97           C
ANISOU  794  CA  VAL A  92      534   1542   2089    236    168     50       C
ATOM    795  C   VAL A  92      14.529  15.324  13.217  1.00 11.73           C
ANISOU  795  C   VAL A  92      868   1415   2173    325     50     25       C
ATOM    796  O   VAL A  92      14.485  16.540  13.035  1.00 12.86           O
ANISOU  796  O   VAL A  92     1314   1313   2256    219    216    104       O
ATOM    797  CB  VAL A  92      16.861  14.890  12.440  1.00 12.12           C
ANISOU  797  CB  VAL A  92      922   1601   2080    415    144    -38       C
ATOM    798  CG1 VAL A  92      17.352  14.788  13.877  1.00 15.15           C
ANISOU  798  CG1 VAL A  92     1174   2264   2316    141    133    -67       C
ATOM    799  CG2 VAL A  92      17.766  14.058  11.495  1.00 14.88           C
ANISOU  799  CG2 VAL A  92      922   2131   2599     54    266    -53       C
ATOM    800  N   HIS A  93      13.854  14.694  14.163  1.00 11.23           N
ANISOU  800  N   HIS A  93      944   1269   2054    422     41     57       N
ATOM    801  CA  HIS A  93      12.808  15.318  14.984  1.00 11.14           C
ANISOU  801  CA  HIS A  93      741   1367   2123    278     33    137       C
ATOM    802  C   HIS A  93      13.271  15.279  16.410  1.00 11.56           C
ANISOU  802  C   HIS A  93      892   1505   1994    357     48     30       C
ATOM    803  O   HIS A  93      13.349  14.196  17.003  1.00 12.72           O
ANISOU  803  O   HIS A  93     1470   1334   2025    211    -63     66       O
ATOM    804  CB  HIS A  93      11.530  14.546  14.778  1.00 11.54           C
ANISOU  804  CB  HIS A  93     1018   1362   2003    326    -97    174       C
ATOM    805  CG  HIS A  93      10.328  14.974  15.535  1.00 11.89           C
ANISOU  805  CG  HIS A  93      989   1531   1995    367     40    199       C
ATOM    806  ND1 HIS A  93       9.141  14.317  15.369  1.00 14.60           N
ANISOU  806  ND1 HIS A  93     1259   1902   2383    414    -14    350       N
ATOM    807  CD2 HIS A  93      10.139  15.946  16.462  1.00 13.46           C
ANISOU  807  CD2 HIS A  93     1270   1784   2058    451    342    300       C
ATOM    808  CE1 HIS A  93       8.253  14.905  16.146  1.00 14.71           C
ANISOU  808  CE1 HIS A  93      831   2121   2635    412     82    490       C
ATOM    809  NE2 HIS A  93       8.830  15.877  16.840  1.00 14.68           N
ANISOU  809  NE2 HIS A  93     1266   1982   2326    496    269    480       N
ATOM    810  N   VAL A  94      13.614  16.431  16.979  1.00 10.96           N
ANISOU  810  N   VAL A  94      672   1477   2014    184     88     86       N
ATOM    811  CA  VAL A  94      14.066  16.531  18.369  1.00 10.91           C
ANISOU  811  CA  VAL A  94      559   1406   2178    308     41     41       C
ATOM    812  C   VAL A  94      12.968  17.079  19.205  1.00 11.50           C
ANISOU  812  C   VAL A  94      901   1377   2089    269     48    -13       C
ATOM    813  O   VAL A  94      12.396  18.122  18.879  1.00 13.18           O
ANISOU  813  O   VAL A  94     1238   1572   2195    396    149     91       O
ATOM    814  CB  VAL A  94      15.373  17.341  18.440  1.00 12.79           C
ANISOU  814  CB  VAL A  94      812   1610   2435    241   -147     37       C
ATOM    815  CG1 VAL A  94      15.836  17.375  19.890  1.00 16.31           C
ANISOU  815  CG1 VAL A  94     1320   2253   2621   -397   -385    134       C
ATOM    816  CG2 VAL A  94      16.408  16.819  17.461  1.00 16.09           C
ANISOU  816  CG2 VAL A  94      679   2434   2997    493    243     64       C
ATOM    817  N   GLN A  95      12.635  16.396  20.277  1.00 11.49           N
ANISOU  817  N   GLN A  95     1037   1256   2072    243   -131     42       N
ATOM    818  CA  GLN A  95      11.638  16.824  21.247  1.00 11.66           C
ANISOU  818  CA  GLN A  95     1025   1312   2093    208    -15     23       C
ATOM    819  C   GLN A  95      12.291  17.146  22.572  1.00 12.53           C
ANISOU  819  C   GLN A  95     1160   1459   2141    202     58      6       C
ATOM    820  O   GLN A  95      13.060  16.316  23.101  1.00 13.24           O
ANISOU  820  O   GLN A  95     1306   1572   2149    253    -94    -59       O
ATOM    821  CB  GLN A  95      10.613  15.693  21.521  1.00 12.00           C
ANISOU  821  CB  GLN A  95     1089   1358   2111    214     -8     52       C
ATOM    822  CG  GLN A  95       9.845  15.269  20.274  1.00 12.52           C
ANISOU  822  CG  GLN A  95     1002   1523   2230    -48    101     23       C
ATOM    823  CD  GLN A  95       8.903  14.070  20.470  1.00 12.31           C
ANISOU  823  CD  GLN A  95      470   1663   2541    -28    119     84       C
ATOM    824  OE1 GLN A  95       7.833  13.990  19.823  1.00 14.64           O
ANISOU  824  OE1 GLN A  95      721   2023   2820    -27     97     68       O
ATOM    825  NE2 GLN A  95       9.155  13.253  21.447  1.00 12.36           N
ANISOU  825  NE2 GLN A  95      838   1493   2365   -129   -261    266       N
ATOM    826  N   LYS A  96      12.011  18.323  23.102  1.00 12.95           N
ANISOU  826  N   LYS A  96     1315   1518   2088    192      7    -33       N
ATOM    827  CA  LYS A  96      12.563  18.777  24.372  1.00 14.35           C
ANISOU  827  CA  LYS A  96     1456   1796   2199     96    -57    -23       C
ATOM    828  C   LYS A  96      11.463  19.013  25.380  1.00 13.88           C
ANISOU  828  C   LYS A  96     1423   1621   2229    184   -181    -93       C
ATOM    829  O   LYS A  96      10.472  19.659  25.096  1.00 14.47           O
ANISOU  829  O   LYS A  96     1529   1797   2169    334    -84   -122       O
ATOM    830  CB  LYS A  96      13.337  20.103  24.200  1.00 15.23           C
ANISOU  830  CB  LYS A  96     1385   1959   2440    -96   -138    -45       C
ATOM    831  CG  LYS A  96      14.355  20.139  23.167  1.00 19.13           C
ANISOU  831  CG  LYS A  96     2076   2316   2874    -26    -60    -97       C
ATOM    832  CD  LYS A  96      15.522  19.256  23.462  1.00 20.33           C
ANISOU  832  CD  LYS A  96     2371   2483   2870     29   -111   -298       C
ATOM    833  CE  LYS A  96      16.721  19.616  22.636  1.00 20.69           C
ANISOU  833  CE  LYS A  96     2218   2419   3223   -271   -294   -287       C
ATOM    834  NZ  LYS A  96      17.908  18.738  22.855  1.00 22.84           N
ANISOU  834  NZ  LYS A  96     2645   2259   3771    -86     73    -45       N
ATOM    835  N   TRP A  97      11.599  18.511  26.604  1.00 14.54           N
ANISOU  835  N   TRP A  97     1616   1619   2289    182   -125    -95       N
ATOM    836  CA  TRP A  97      10.634  18.737  27.667  1.00 16.73           C
ANISOU  836  CA  TRP A  97     2121   1977   2257    445     34    -64       C
ATOM    837  C   TRP A  97      11.292  18.411  29.009  1.00 18.11           C
ANISOU  837  C   TRP A  97     2449   2158   2272    502     32   -165       C
ATOM    838  O   TRP A  97      12.110  17.491  29.086  1.00 19.00           O
ANISOU  838  O   TRP A  97     2768   2215   2236    580   -180   -143       O
ATOM    839  CB  TRP A  97       9.351  17.884  27.486  1.00 16.05           C
ANISOU  839  CB  TRP A  97     1842   2095   2158    459    103    -47       C
ATOM    840  CG  TRP A  97       9.540  16.424  27.893  1.00 16.32           C
ANISOU  840  CG  TRP A  97     1515   2124   2560    319    268     81       C
ATOM    841  CD1 TRP A  97       9.072  15.839  29.022  1.00 17.66           C
ANISOU  841  CD1 TRP A  97     2288   2163   2256    432    402     64       C
ATOM    842  CD2 TRP A  97      10.329  15.426  27.238  1.00 15.00           C
ANISOU  842  CD2 TRP A  97     1542   1815   2341    210    335    -77       C
ATOM    843  NE1 TRP A  97       9.445  14.552  29.091  1.00 17.66           N
ANISOU  843  NE1 TRP A  97     2422   1991   2296    419    379    146       N
ATOM    844  CE2 TRP A  97      10.229  14.259  28.015  1.00 15.54           C
ANISOU  844  CE2 TRP A  97     1688   2002   2212     36    288     89       C
ATOM    845  CE3 TRP A  97      11.081  15.386  26.054  1.00 15.17           C
ANISOU  845  CE3 TRP A  97     1721   1703   2339     -8     79   -113       C
ATOM    846  CZ2 TRP A  97      10.909  13.081  27.697  1.00 16.32           C
ANISOU  846  CZ2 TRP A  97     1893   1970   2335    115    -43    247       C
ATOM    847  CZ3 TRP A  97      11.725  14.196  25.749  1.00 14.90           C
ANISOU  847  CZ3 TRP A  97     1315   1871   2473   -127    125    -96       C
ATOM    848  CH2 TRP A  97      11.618  13.077  26.547  1.00 16.01           C
ANISOU  848  CH2 TRP A  97     1877   1674   2530     36    131   -180       C
ATOM    849  N   ASP A  98      11.019  19.226  30.035  1.00 19.21           N
ANISOU  849  N   ASP A  98     2721   2348   2228    632      3   -182       N
ATOM    850  CA  ASP A  98      11.423  18.863  31.423  1.00 21.52           C
ANISOU  850  CA  ASP A  98     3123   2681   2371    412    -76   -270       C
ATOM    851  C   ASP A  98      12.939  18.637  31.523  1.00 21.81           C
ANISOU  851  C   ASP A  98     3235   2724   2325    382   -137   -366       C
ATOM    852  O   ASP A  98      13.385  17.788  32.293  1.00 24.73           O
ANISOU  852  O   ASP A  98     3782   3091   2522    396   -203   -178       O
ATOM    853  CB  ASP A  98      10.651  17.624  31.877  1.00 23.83           C
ANISOU  853  CB  ASP A  98     3385   3153   2513    448    -30    -52       C
ATOM    854  N   GLY A  99      13.743  19.353  30.732  1.00 21.29           N
ANISOU  854  N   GLY A  99     3127   2529   2430    355   -319   -437       N
ATOM    855  CA  GLY A  99      15.190  19.181  30.744  1.00 21.48           C
ANISOU  855  CA  GLY A  99     2945   2545   2668    308   -427   -372       C
ATOM    856  C   GLY A  99      15.710  17.946  30.017  1.00 20.36           C
ANISOU  856  C   GLY A  99     2596   2471   2667    386   -480   -337       C
ATOM    857  O   GLY A  99      16.935  17.679  30.055  1.00 23.12           O
ANISOU  857  O   GLY A  99     2792   2871   3120    340   -599   -466       O
ATOM    858  N   LYS A 100      14.795  17.211  29.357  1.00 19.09           N
ANISOU  858  N   LYS A 100     2479   2310   2464    341   -445   -310       N
ATOM    859  CA  LYS A 100      15.041  15.936  28.665  1.00 16.08           C
ANISOU  859  CA  LYS A 100     1605   2124   2379    407   -471   -186       C
ATOM    860  C   LYS A 100      14.986  16.179  27.171  1.00 15.53           C
ANISOU  860  C   LYS A 100     1678   1980   2240    286   -401     -8       C
ATOM    861  O   LYS A 100      14.399  17.135  26.725  1.00 15.77           O
ANISOU  861  O   LYS A 100     1913   1844   2235    329   -304   -181       O
ATOM    862  CB  LYS A 100      14.044  14.856  29.082  1.00 17.74           C
ANISOU  862  CB  LYS A 100     2373   2077   2289    413   -345    -42       C
ATOM    863  CG  LYS A 100      13.968  14.621  30.592  1.00 22.92           C
ANISOU  863  CG  LYS A 100     3181   2929   2596    264   -207   -149       C
ATOM    864  CD  LYS A 100      12.931  13.605  30.988  1.00 25.73           C
ANISOU  864  CD  LYS A 100     3526   3317   2934    329    -20    135       C
ATOM    865  CE  LYS A 100      12.802  13.547  32.501  1.00 29.47           C
ANISOU  865  CE  LYS A 100     3962   3980   3253    289    -21    -38       C
ATOM    866  NZ  LYS A 100      12.721  14.955  33.039  1.00 35.64           N
ANISOU  866  NZ  LYS A 100     4997   4208   4334     78   -125    -41       N
ATOM    867  N   SER A 101      15.564  15.240  26.404  1.00 14.22           N
ANISOU  867  N   SER A 101     1482   1711   2209     70   -240    -44       N
ATOM    868  CA  SER A 101      15.527  15.289  24.955  1.00 14.59           C
ANISOU  868  CA  SER A 101     1499   1742   2302     90   -196      7       C
ATOM    869  C   SER A 101      15.393  13.884  24.420  1.00 13.43           C
ANISOU  869  C   SER A 101     1292   1555   2254    173   -182      7       C
ATOM    870  O   SER A 101      16.026  12.978  24.911  1.00 14.35           O
ANISOU  870  O   SER A 101     1578   1521   2351    156   -453     45       O
ATOM    871  CB  SER A 101      16.840  15.879  24.465  1.00 16.78           C
ANISOU  871  CB  SER A 101     2022   1789   2564   -202    -87    -63       C
ATOM    872  OG  SER A 101      16.809  16.126  23.086  1.00 19.52           O
ANISOU  872  OG  SER A 101     2467   2048   2901   -451    -40    -79       O
ATOM    873  N   THR A 102      14.653  13.735  23.313  1.00 12.66           N
ANISOU  873  N   THR A 102     1137   1516   2157     88   -198     55       N
ATOM    874  CA  THR A 102      14.610  12.478  22.537  1.00 11.62           C
ANISOU  874  CA  THR A 102      632   1461   2320    258    -17    -77       C
ATOM    875  C   THR A 102      14.567  12.863  21.067  1.00 11.70           C
ANISOU  875  C   THR A 102      944   1453   2047    196   -109     60       C
ATOM    876  O   THR A 102      14.089  13.943  20.706  1.00 12.67           O
ANISOU  876  O   THR A 102     1183   1418   2212    154    -62     70       O
ATOM    877  CB  THR A 102      13.386  11.654  22.938  1.00 12.48           C
ANISOU  877  CB  THR A 102     1011   1615   2112    -44    -72   -152       C
ATOM    878  OG1 THR A 102      13.485  10.354  22.303  1.00 13.29           O
ANISOU  878  OG1 THR A 102     1060   1464   2523     75     -9   -109       O
ATOM    879  CG2 THR A 102      12.087  12.231  22.603  1.00 13.38           C
ANISOU  879  CG2 THR A 102      396   1992   2696     70      3     75       C
ATOM    880  N   THR A 103      15.180  11.994  20.239  1.00 12.19           N
ANISOU  880  N   THR A 103     1328   1264   2038    210   -136     79       N
ATOM    881  CA  THR A 103      15.265  12.212  18.807  1.00 12.45           C
ANISOU  881  CA  THR A 103     1145   1409   2176    224   -137     18       C
ATOM    882  C   THR A 103      14.571  11.088  18.059  1.00 12.56           C
ANISOU  882  C   THR A 103     1370   1372   2030    222    -35    -29       C
ATOM    883  O   THR A 103      14.811   9.902  18.357  1.00 14.14           O
ANISOU  883  O   THR A 103     1966   1356   2050    283   -316     12       O
ATOM    884  CB  THR A 103      16.699  12.367  18.384  1.00 13.30           C
ANISOU  884  CB  THR A 103     1039   1673   2340    134    -81    -34       C
ATOM    885  OG1 THR A 103      17.277  13.510  19.044  1.00 17.56           O
ANISOU  885  OG1 THR A 103     1673   2285   2713   -221    182   -114       O
ATOM    886  CG2 THR A 103      16.798  12.572  16.901  1.00 15.94           C
ANISOU  886  CG2 THR A 103     1608   2129   2318     11     87     77       C
ATOM    887  N   ILE A 104      13.760  11.434  17.100  1.00 11.67           N
ANISOU  887  N   ILE A 104     1209   1229   1997    216    -64     29       N
ATOM    888  CA  ILE A 104      13.092  10.497  16.223  1.00 11.71           C
ANISOU  888  CA  ILE A 104     1075   1262   2110    276    -27     30       C
ATOM    889  C   ILE A 104      13.563  10.768  14.836  1.00 11.93           C
ANISOU  889  C   ILE A 104     1193   1405   1934    237     48    110       C
ATOM    890  O   ILE A 104      13.427  11.872  14.331  1.00 12.61           O
ANISOU  890  O   ILE A 104     1378   1366   2045    240     53     48       O
ATOM    891  CB  ILE A 104      11.552  10.673  16.263  1.00 13.49           C
ANISOU  891  CB  ILE A 104     1680   1426   2019    126    109    100       C
ATOM    892  CG1 ILE A 104      10.975  10.499  17.702  1.00 14.22           C
ANISOU  892  CG1 ILE A 104     1597   1669   2134     49    220    -39       C
ATOM    893  CG2 ILE A 104      10.824   9.702  15.288  1.00 14.34           C
ANISOU  893  CG2 ILE A 104     1355   1886   2206     44    -93      0       C
ATOM    894  CD1 ILE A 104       9.521  10.917  17.804  1.00 18.69           C
ANISOU  894  CD1 ILE A 104     1536   2767   2796    404    445     60       C
ATOM    895  N   LYS A 105      14.165   9.763  14.207  1.00 11.41           N
ANISOU  895  N   LYS A 105      840   1402   2094    145     79     46       N
ATOM    896  CA  LYS A 105      14.677   9.860  12.838  1.00 11.57           C
ANISOU  896  CA  LYS A 105      944   1414   2035    -94     -9    122       C
ATOM    897  C   LYS A 105      13.759   9.074  11.939  1.00 11.48           C
ANISOU  897  C   LYS A 105      939   1314   2106    -66     73    111       C
ATOM    898  O   LYS A 105      13.373   7.959  12.273  1.00 12.93           O
ANISOU  898  O   LYS A 105     1391   1393   2126   -170    -85     92       O
ATOM    899  CB  LYS A 105      16.138   9.369  12.744  1.00 11.71           C
ANISOU  899  CB  LYS A 105      460   1774   2214    138     64     19       C
ATOM    900  CG  LYS A 105      17.123  10.280  13.506  1.00 16.42           C
ANISOU  900  CG  LYS A 105     1085   2347   2804    316   -418     -3       C
ATOM    901  CD  LYS A 105      18.568   9.890  13.333  1.00 19.94           C
ANISOU  901  CD  LYS A 105     1229   3166   3178    244   -305      4       C
ATOM    902  CE  LYS A 105      19.457  10.866  14.052  1.00 23.97           C
ANISOU  902  CE  LYS A 105     1748   3347   4011    167   -461     -2       C
ATOM    903  NZ  LYS A 105      20.913  10.576  13.888  1.00 28.05           N
ANISOU  903  NZ  LYS A 105     2276   3725   4655    224   -130     64       N
ATOM    904  N   ARG A 106      13.461   9.613  10.770  1.00 10.57           N
ANISOU  904  N   ARG A 106      760   1205   2050    -86     -9     25       N
ATOM    905  CA  ARG A 106      12.611   8.949   9.793  1.00 11.21           C
ANISOU  905  CA  ARG A 106      842   1409   2006    -55     18     19       C
ATOM    906  C   ARG A 106      13.392   8.903   8.482  1.00 11.50           C
ANISOU  906  C   ARG A 106      870   1520   1980   -235     13    -42       C
ATOM    907  O   ARG A 106      13.900   9.938   8.006  1.00 11.56           O
ANISOU  907  O   ARG A 106      728   1489   2175    -27    102    -75       O
ATOM    908  CB  ARG A 106      11.287   9.652   9.614  1.00 12.26           C
ANISOU  908  CB  ARG A 106      818   1712   2126    -64    -30     84       C
ATOM    909  CG  ARG A 106      10.497   9.680  10.925  1.00 12.57           C
ANISOU  909  CG  ARG A 106      751   1680   2344      1    114     65       C
ATOM    910  CD  ARG A 106       9.215  10.477  10.830  1.00 16.63           C
ANISOU  910  CD  ARG A 106      847   2777   2691   -404    212    -52       C
ATOM    911  NE  ARG A 106       8.331  10.416  12.015  1.00 16.90           N
ANISOU  911  NE  ARG A 106     1339   2420   2658   -297    388    -98       N
ATOM    912  CZ  ARG A 106       8.321  11.295  13.008  1.00 16.01           C
ANISOU  912  CZ  ARG A 106      472   2706   2904   -271    -63   -238       C
ATOM    913  NH1 ARG A 106       9.098  12.287  13.071  1.00 15.58           N
ANISOU  913  NH1 ARG A 106      757   2698   2462    369     34    -27       N
ATOM    914  NH2 ARG A 106       7.395  11.140  13.965  1.00 19.43           N
ANISOU  914  NH2 ARG A 106      715   3697   2969     51    359   -136       N
ATOM    915  N   LYS A 107      13.527   7.725   7.864  1.00 11.04           N
ANISOU  915  N   LYS A 107      718   1492   1984   -189     49    -38       N
ATOM    916  CA  LYS A 107      14.371   7.518   6.677  1.00 12.60           C
ANISOU  916  CA  LYS A 107      853   1666   2265   -213    241    -23       C
ATOM    917  C   LYS A 107      13.771   6.483   5.772  1.00 12.41           C
ANISOU  917  C   LYS A 107      725   1776   2212   -414    143    -48       C
ATOM    918  O   LYS A 107      13.209   5.494   6.236  1.00 14.50           O
ANISOU  918  O   LYS A 107     1509   1914   2086   -587    157    -32       O
ATOM    919  CB  LYS A 107      15.762   7.102   7.062  1.00 13.44           C
ANISOU  919  CB  LYS A 107      487   2154   2463    -37    205   -199       C
ATOM    920  CG  LYS A 107      16.814   7.012   5.975  1.00 16.86           C
ANISOU  920  CG  LYS A 107     1187   2163   3055    -70    238   -325       C
ATOM    921  CD  LYS A 107      18.180   6.651   6.441  1.00 18.66           C
ANISOU  921  CD  LYS A 107      952   2712   3426    431    454   -647       C
ATOM    922  CE  LYS A 107      19.214   7.154   5.417  1.00 24.41           C
ANISOU  922  CE  LYS A 107     2211   3282   3779    361    454   -524       C
ATOM    923  NZ  LYS A 107      18.699   8.362   4.647  1.00 30.13           N
ANISOU  923  NZ  LYS A 107     2607   4110   4730    252    385   -264       N
ATOM    924  N   ARG A 108      13.810   6.717   4.475  1.00 11.39           N
ANISOU  924  N   ARG A 108      460   1667   2198   -281    123     -4       N
ATOM    925  CA  ARG A 108      13.418   5.684   3.497  1.00 13.19           C
ANISOU  925  CA  ARG A 108      724   2013   2272   -255    101     34       C
ATOM    926  C   ARG A 108      14.501   4.631   3.368  1.00 11.22           C
ANISOU  926  C   ARG A 108      267   1900   2093     83    126   -153       C
ATOM    927  O   ARG A 108      15.656   4.948   3.192  1.00 14.18           O
ANISOU  927  O   ARG A 108      693   1971   2721    -72    314   -299       O
ATOM    928  CB  ARG A 108      13.125   6.341   2.137  1.00 13.58           C
ANISOU  928  CB  ARG A 108      748   2157   2253   -363    213     34       C
ATOM    929  CG  ARG A 108      11.807   7.033   2.115  1.00 15.01           C
ANISOU  929  CG  ARG A 108     1052   2552   2098   -126    -34    287       C
ATOM    930  CD  ARG A 108      10.573   6.143   2.191  1.00 17.70           C
ANISOU  930  CD  ARG A 108      485   3385   2854    118    454    203       C
ATOM    931  NE  ARG A 108      10.649   5.041   1.207  1.00 18.21           N
ANISOU  931  NE  ARG A 108      934   2652   3331   -195    189    398       N
ATOM    932  CZ  ARG A 108      10.418   5.158  -0.088  1.00 17.20           C
ANISOU  932  CZ  ARG A 108     1130   2119   3283   -130    -92    134       C
ATOM    933  NH1 ARG A 108       9.876   6.252  -0.563  1.00 16.92           N
ANISOU  933  NH1 ARG A 108      971   2471   2985    -92   -389    123       N
ATOM    934  NH2 ARG A 108      10.615   4.129  -0.911  1.00 21.27           N
ANISOU  934  NH2 ARG A 108     1611   2828   3641    302   -327   -100       N
ATOM    935  N   GLU A 109      14.098   3.359   3.400  1.00 12.97           N
ANISOU  935  N   GLU A 109      734   1759   2433   -237    197   -262       N
ATOM    936  CA  GLU A 109      15.009   2.233   3.156  1.00 14.30           C
ANISOU  936  CA  GLU A 109     1085   1934   2411    103    247   -191       C
ATOM    937  C   GLU A 109      14.260   1.233   2.320  1.00 13.13           C
ANISOU  937  C   GLU A 109      867   1809   2310     81    139   -155       C
ATOM    938  O   GLU A 109      13.220   0.705   2.730  1.00 13.99           O
ANISOU  938  O   GLU A 109     1027   2003   2285     -6    325   -207       O
ATOM    939  CB  GLU A 109      15.360   1.544   4.471  1.00 16.19           C
ANISOU  939  CB  GLU A 109     1403   2092   2655    191     78   -209       C
ATOM    940  CG  GLU A 109      16.063   2.397   5.483  1.00 20.13           C
ANISOU  940  CG  GLU A 109     1873   2840   2933    377   -215   -280       C
ATOM    941  CD  GLU A 109      17.494   2.651   5.126  1.00 24.52           C
ANISOU  941  CD  GLU A 109     2350   3496   3470    -78    -12   -550       C
ATOM    942  OE1 GLU A 109      18.158   3.421   5.832  1.00 28.46           O
ANISOU  942  OE1 GLU A 109     2749   3924   4138   -521   -162   -415       O
ATOM    943  OE2 GLU A 109      17.978   2.110   4.109  1.00 30.68           O
ANISOU  943  OE2 GLU A 109     3010   4438   4208     12     88   -798       O
ATOM    944  N   ASP A 110      14.662   1.084   1.054  1.00 12.86           N
ANISOU  944  N   ASP A 110      768   1864   2254    112    146    -16       N
ATOM    945  CA  ASP A 110      13.943   0.281   0.076  1.00 13.72           C
ANISOU  945  CA  ASP A 110     1368   1670   2173      9    169    -10       C
ATOM    946  C   ASP A 110      12.517   0.823   0.017  1.00 12.97           C
ANISOU  946  C   ASP A 110      940   2040   1948   -112      0    -51       C
ATOM    947  O   ASP A 110      12.354   2.062  -0.070  1.00 14.07           O
ANISOU  947  O   ASP A 110     1223   1841   2281    216     92     36       O
ATOM    948  CB  ASP A 110      14.044  -1.214   0.407  1.00 15.08           C
ANISOU  948  CB  ASP A 110     1622   1919   2185    300    261    -77       C
ATOM    949  CG  ASP A 110      15.452  -1.682   0.406  1.00 18.27           C
ANISOU  949  CG  ASP A 110     1900   2305   2734    103    298    296       C
ATOM    950  OD1 ASP A 110      16.257  -1.207  -0.400  1.00 21.75           O
ANISOU  950  OD1 ASP A 110     2030   2747   3488    659    576    198       O
ATOM    951  OD2 ASP A 110      15.788  -2.576   1.184  1.00 26.56           O
ANISOU  951  OD2 ASP A 110     3559   3166   3366    645    436    691       O
ATOM    952  N   ASP A 111      11.450   0.019   0.067  1.00 13.16           N
ANISOU  952  N   ASP A 111      940   1991   2069    -74    -11   -200       N
ATOM    953  CA  ASP A 111      10.113   0.455  -0.008  1.00 13.73           C
ANISOU  953  CA  ASP A 111      710   2182   2323   -152      1   -168       C
ATOM    954  C   ASP A 111       9.564   0.867   1.363  1.00 13.79           C
ANISOU  954  C   ASP A 111      691   2173   2373   -116     -6   -146       C
ATOM    955  O   ASP A 111       8.399   1.111   1.439  1.00 16.21           O
ANISOU  955  O   ASP A 111      904   2689   2566    -54    -99   -500       O
ATOM    956  CB  ASP A 111       9.223  -0.571  -0.735  1.00 14.68           C
ANISOU  956  CB  ASP A 111      938   2279   2359    -93   -131   -167       C
ATOM    957  CG  ASP A 111       9.514  -0.636  -2.199  1.00 15.90           C
ANISOU  957  CG  ASP A 111     1412   2207   2421   -203   -140   -168       C
ATOM    958  OD1 ASP A 111       9.755   0.416  -2.814  1.00 19.52           O
ANISOU  958  OD1 ASP A 111     2609   2541   2264   -268    -36    -99       O
ATOM    959  OD2 ASP A 111       9.612  -1.759  -2.730  1.00 19.20           O
ANISOU  959  OD2 ASP A 111     2490   2257   2548    -96    204   -292       O
ATOM    960  N   LYS A 112      10.322   0.799   2.404  1.00 13.46           N
ANISOU  960  N   LYS A 112     1032   1768   2314    -77    111    -57       N
ATOM    961  CA  LYS A 112       9.914   1.092   3.776  1.00 12.67           C
ANISOU  961  CA  LYS A 112      902   1776   2136    -85    163   -132       C
ATOM    962  C   LYS A 112      10.238   2.479   4.201  1.00 12.09           C
ANISOU  962  C   LYS A 112      667   1625   2301    -98     86    -64       C
ATOM    963  O   LYS A 112      11.107   3.159   3.657  1.00 12.97           O
ANISOU  963  O   LYS A 112     1094   1643   2191   -151    208    -95       O
ATOM    964  CB  LYS A 112      10.552   0.066   4.699  1.00 14.27           C
ANISOU  964  CB  LYS A 112     1379   1717   2326    151    319   -163       C
ATOM    965  CG  LYS A 112      10.301  -1.386   4.322  1.00 18.90           C
ANISOU  965  CG  LYS A 112     2139   2200   2842    147    414   -191       C
ATOM    966  CD  LYS A 112       8.914  -1.844   4.487  1.00 24.11           C
ANISOU  966  CD  LYS A 112     2543   2916   3699    114    -15   -308       C
ATOM    967  CE  LYS A 112       8.833  -3.395   4.405  1.00 29.20           C
ANISOU  967  CE  LYS A 112     3371   3301   4421    227     58    -38       C
ATOM    968  NZ  LYS A 112      10.138  -4.026   4.197  1.00 33.55           N
ANISOU  968  NZ  LYS A 112     3606   4094   5047    463    -22   -220       N
ATOM    969  N   LEU A 113       9.589   2.865   5.272  1.00 11.69           N
ANISOU  969  N   LEU A 113      649   1649   2143   -227      5    -90       N
ATOM    970  CA ALEU A 113       9.917   4.087   5.996  0.50 11.47           C
ANISOU  970  CA ALEU A 113      482   1661   2212   -173    158    -57       C
ATOM    971  CA BLEU A 113       9.916   4.087   6.007  0.50 11.77           C
ANISOU  971  CA BLEU A 113      614   1688   2170   -185    125    -69       C
ATOM    972  C   LEU A 113      10.329   3.605   7.417  1.00 11.36           C
ANISOU  972  C   LEU A 113      474   1628   2212   -307    356   -104       C
ATOM    973  O   LEU A 113       9.482   3.008   8.096  1.00 12.70           O
ANISOU  973  O   LEU A 113      661   1804   2357   -222     58    -93       O
ATOM    974  CB ALEU A 113       8.707   5.033   5.989  0.50 12.40           C
ANISOU  974  CB ALEU A 113      475   1950   2285   -153     66    -64       C
ATOM    975  CB BLEU A 113       8.699   5.016   6.040  0.50 12.96           C
ANISOU  975  CB BLEU A 113      752   1925   2245   -168     46    -71       C
ATOM    976  CG ALEU A 113       8.971   6.472   6.438  0.50 12.90           C
ANISOU  976  CG ALEU A 113      418   1956   2524    169    251   -131       C
ATOM    977  CG BLEU A 113       8.845   6.335   6.809  0.50 14.14           C
ANISOU  977  CG BLEU A 113     1040   2136   2196      3      0   -217       C
ATOM    978  CD1ALEU A 113       7.860   7.357   5.936  0.50 13.09           C
ANISOU  978  CD1ALEU A 113      777   1850   2346     10    366      1       C
ATOM    979  CD1BLEU A 113      10.093   7.025   6.373  0.50 16.31           C
ANISOU  979  CD1BLEU A 113     1614   1803   2777     82    -29    120       C
ATOM    980  CD2ALEU A 113       9.120   6.568   7.961  0.50 15.06           C
ANISOU  980  CD2ALEU A 113      533   2421   2768    538    -45    320       C
ATOM    981  CD2BLEU A 113       7.654   7.226   6.531  0.50 16.17           C
ANISOU  981  CD2BLEU A 113     1694   2353   2095     81    124   -109       C
ATOM    982  N   VAL A 114      11.566   3.792   7.761  1.00 10.50           N
ANISOU  982  N   VAL A 114      410   1506   2074   -196    188     24       N
ATOM    983  CA  VAL A 114      12.099   3.305   9.055  1.00 11.88           C
ANISOU  983  CA  VAL A 114      666   1707   2140   -260    127     99       C
ATOM    984  C   VAL A 114      12.150   4.481  10.003  1.00 12.20           C
ANISOU  984  C   VAL A 114      897   1646   2091   -192     67     65       C
ATOM    985  O   VAL A 114      12.582   5.593   9.639  1.00 12.68           O
ANISOU  985  O   VAL A 114     1122   1615   2079   -176    162     69       O
ATOM    986  CB  VAL A 114      13.448   2.689   8.865  1.00 12.65           C
ANISOU  986  CB  VAL A 114      780   1870   2155    -82    -28     89       C
ATOM    987  CG1 VAL A 114      13.982   2.152  10.202  1.00 16.03           C
ANISOU  987  CG1 VAL A 114     1578   2230   2280    167    -20    114       C
ATOM    988  CG2 VAL A 114      13.344   1.536   7.864  1.00 16.40           C
ANISOU  988  CG2 VAL A 114     1395   2150   2685    300    229   -191       C
ATOM    989  N   VAL A 115      11.641   4.261  11.201  1.00 12.14           N
ANISOU  989  N   VAL A 115     1102   1369   2140   -315     56     47       N
ATOM    990  CA  VAL A 115      11.624   5.235  12.278  1.00 12.26           C
ANISOU  990  CA  VAL A 115     1094   1426   2138   -109     51     98       C
ATOM    991  C   VAL A 115      12.447   4.770  13.420  1.00 13.17           C
ANISOU  991  C   VAL A 115     1511   1533   1959   -257    -57    106       C
ATOM    992  O   VAL A 115      12.195   3.717  13.985  1.00 16.44           O
ANISOU  992  O   VAL A 115     2036   1839   2368   -456   -370    323       O
ATOM    993  CB  VAL A 115      10.219   5.493  12.719  1.00 13.61           C
ANISOU  993  CB  VAL A 115     1385   1554   2230   -204      4    -31       C
ATOM    994  CG1 VAL A 115      10.154   6.617  13.797  1.00 16.03           C
ANISOU  994  CG1 VAL A 115     1377   2109   2604    -79    340   -277       C
ATOM    995  CG2 VAL A 115       9.288   5.829  11.541  1.00 15.32           C
ANISOU  995  CG2 VAL A 115      706   2016   3097   -499   -190     41       C
ATOM    996  N  AGLU A 116      13.494   5.507  13.761  0.50 12.85           N
ANISOU  996  N  AGLU A 116     1487   1409   1986   -167     21    127       N
ATOM    997  N  BGLU A 116      13.461   5.555  13.767  0.50 12.15           N
ANISOU  997  N  BGLU A 116     1402   1300   1911   -147     13     21       N
ATOM    998  CA AGLU A 116      14.342   5.136  14.885  0.50 14.12           C
ANISOU  998  CA AGLU A 116     1673   1523   2166    -22    -47    112       C
ATOM    999  CA BGLU A 116      14.379   5.257  14.858  0.50 13.01           C
ANISOU  999  CA BGLU A 116     1574   1283   2085     36    -52     -3       C
ATOM   1000  C  AGLU A 116      14.202   6.198  15.962  0.50 12.95           C
ANISOU 1000  C  AGLU A 116     1352   1452   2115      5   -145     45       C
ATOM   1001  C  BGLU A 116      14.155   6.248  15.971  0.50 12.21           C
ANISOU 1001  C  BGLU A 116     1282   1310   2046     34   -157    -50       C
ATOM   1002  O  AGLU A 116      14.430   7.387  15.729  0.50 14.29           O
ANISOU 1002  O  AGLU A 116     1861   1374   2192     -7   -192     99       O
ATOM   1003  O  BGLU A 116      14.320   7.452  15.783  0.50 13.85           O
ANISOU 1003  O  BGLU A 116     1893   1256   2112     26   -202     56       O
ATOM   1004  CB AGLU A 116      15.808   4.937  14.429  0.50 16.51           C
ANISOU 1004  CB AGLU A 116     2064   1848   2360     22    -47    254       C
ATOM   1005  CB BGLU A 116      15.830   5.410  14.377  0.50 14.02           C
ANISOU 1005  CB BGLU A 116     1924   1240   2162    116    -55    -10       C
ATOM   1006  CG AGLU A 116      16.027   3.655  13.538  0.50 20.51           C
ANISOU 1006  CG AGLU A 116     2369   2652   2771   -116    164    100       C
ATOM   1007  CG BGLU A 116      16.841   4.993  15.416  0.50 15.45           C
ANISOU 1007  CG BGLU A 116     1633   2032   2203     81    171     53       C
ATOM   1008  CD AGLU A 116      17.350   2.852  13.761  0.50 25.53           C
ANISOU 1008  CD AGLU A 116     2881   3231   3588   -162     91    204       C
ATOM   1009  CD BGLU A 116      18.223   5.562  15.160  0.50 20.03           C
ANISOU 1009  CD BGLU A 116     2205   2809   2596    -25     36    128       C
ATOM   1010  OE1AGLU A 116      18.390   3.501  14.008  0.50 27.31           O
ANISOU 1010  OE1AGLU A 116     2885   3734   3756   -458      2    359       O
ATOM   1011  OE1BGLU A 116      18.420   6.802  15.075  0.50 24.33           O
ANISOU 1011  OE1BGLU A 116     3181   3059   3005   -124    115    248       O
ATOM   1012  OE2AGLU A 116      17.358   1.569  13.644  0.50 27.03           O
ANISOU 1012  OE2AGLU A 116     2580   3693   3996   -724    225    611       O
ATOM   1013  OE2BGLU A 116      19.152   4.774  15.092  0.50 20.88           O
ANISOU 1013  OE2BGLU A 116     1996   2979   2956   -140    462   -112       O
ATOM   1014  N   CYS A 117      13.789   5.758  17.136  1.00 12.48           N
ANISOU 1014  N   CYS A 117     1393   1328   2020    254   -167    103       N
ATOM   1015  CA  CYS A 117      13.509   6.582  18.312  1.00 13.41           C
ANISOU 1015  CA  CYS A 117     1314   1543   2235    258   -253   -111       C
ATOM   1016  C   CYS A 117      14.646   6.389  19.289  1.00 12.62           C
ANISOU 1016  C   CYS A 117     1087   1559   2146    240   -141      5       C
ATOM   1017  O   CYS A 117      14.849   5.259  19.712  1.00 13.62           O
ANISOU 1017  O   CYS A 117     1459   1419   2295    166   -490     23       O
ATOM   1018  CB  CYS A 117      12.152   6.173  18.924  1.00 14.95           C
ANISOU 1018  CB  CYS A 117     1049   2136   2496    579   -240    -72       C
ATOM   1019  SG  CYS A 117      10.781   6.186  17.749  1.00 18.42           S
ANISOU 1019  SG  CYS A 117     1465   2920   2612    293   -357    111       S
ATOM   1020  N   VAL A 118      15.247   7.468  19.748  1.00 12.06           N
ANISOU 1020  N   VAL A 118     1002   1458   2120    242   -118     25       N
ATOM   1021  CA  VAL A 118      16.438   7.379  20.563  1.00 12.97           C
ANISOU 1021  CA  VAL A 118     1010   1487   2430    126     12     19       C
ATOM   1022  C   VAL A 118      16.266   8.210  21.834  1.00 13.33           C
ANISOU 1022  C   VAL A 118     1164   1614   2286    130    -88    107       C
ATOM   1023  O   VAL A 118      15.944   9.415  21.763  1.00 12.98           O
ANISOU 1023  O   VAL A 118     1100   1423   2408    250     -7     53       O
ATOM   1024  CB  VAL A 118      17.711   7.785  19.811  1.00 14.76           C
ANISOU 1024  CB  VAL A 118     1091   1900   2616     70    242    -35       C
ATOM   1025  CG1 VAL A 118      18.881   7.821  20.683  1.00 19.47           C
ANISOU 1025  CG1 VAL A 118     1374   2445   3575    310    -43     72       C
ATOM   1026  CG2 VAL A 118      17.916   6.872  18.620  1.00 19.85           C
ANISOU 1026  CG2 VAL A 118     2044   2540   2956   -124    455   -268       C
ATOM   1027  N   MET A 119      16.458   7.618  22.979  1.00 13.23           N
ANISOU 1027  N   MET A 119     1259   1382   2385    305   -189     12       N
ATOM   1028  CA  MET A 119      16.487   8.318  24.258  1.00 15.04           C
ANISOU 1028  CA  MET A 119     1504   1713   2497    271   -220     -8       C
ATOM   1029  C   MET A 119      17.719   7.777  24.992  1.00 15.14           C
ANISOU 1029  C   MET A 119     1392   1917   2440    157   -305    -39       C
ATOM   1030  O   MET A 119      17.728   6.630  25.402  1.00 13.93           O
ANISOU 1030  O   MET A 119     1274   1658   2360    261   -205     91       O
ATOM   1031  CB  MET A 119      15.159   8.056  25.001  1.00 15.94           C
ANISOU 1031  CB  MET A 119     1421   2077   2555    682   -257   -167       C
ATOM   1032  CG  MET A 119      15.038   8.546  26.433  1.00 17.94           C
ANISOU 1032  CG  MET A 119     2103   2008   2703    198   -236     35       C
ATOM   1033  SD  MET A 119      14.736  10.255  26.353  1.00 22.97           S
ANISOU 1033  SD  MET A 119     3033   2303   3391   1004   -855   -571       S
ATOM   1034  CE  MET A 119      14.813  10.907  28.026  1.00 19.06           C
ANISOU 1034  CE  MET A 119     2515   1943   2781   -108   -217   -491       C
ATOM   1035  N  ALYS A 120      18.703   8.655  25.145  0.50 16.58           N
ANISOU 1035  N  ALYS A 120     1744   1939   2616    107   -139     81       N
ATOM   1036  N  BLYS A 120      18.785   8.559  25.182  0.50 16.87           N
ANISOU 1036  N  BLYS A 120     1751   1982   2677     94   -195     36       N
ATOM   1037  CA ALYS A 120      19.960   8.322  25.683  0.50 15.72           C
ANISOU 1037  CA ALYS A 120     1464   1878   2630     91   -152    147       C
ATOM   1038  CA BLYS A 120      19.910   8.156  26.017  0.50 17.14           C
ANISOU 1038  CA BLYS A 120     1569   2075   2868    -22   -216     24       C
ATOM   1039  C  ALYS A 120      20.526   7.102  24.964  0.50 11.99           C
ANISOU 1039  C  ALYS A 120      787   1447   2318     76     -9    207       C
ATOM   1040  C  BLYS A 120      20.440   6.730  25.873  0.50 16.03           C
ANISOU 1040  C  BLYS A 120     1183   2161   2745     -6   -207     32       C
ATOM   1041  O  ALYS A 120      20.649   7.112  23.762  0.50 12.61           O
ANISOU 1041  O  ALYS A 120      703   1562   2527    202     49    431       O
ATOM   1042  O  BLYS A 120      20.471   6.012  26.860  0.50 18.35           O
ANISOU 1042  O  BLYS A 120     1363   2488   3122   -217   -182     70       O
ATOM   1043  CB ALYS A 120      19.834   8.062  27.185  0.50 15.71           C
ANISOU 1043  CB ALYS A 120     1464   1893   2610    121   -216    147       C
ATOM   1044  CB BLYS A 120      19.546   8.244  27.490  0.50 16.68           C
ANISOU 1044  CB BLYS A 120     1646   1871   2821    173   -351      1       C
ATOM   1045  CG ALYS A 120      19.402   9.294  27.999  0.50 20.68           C
ANISOU 1045  CG ALYS A 120     2279   2492   3088    254   -212    -84       C
ATOM   1046  CG BLYS A 120      19.159   9.593  27.974  0.50 19.49           C
ANISOU 1046  CG BLYS A 120     2210   2075   3117    359   -322    -56       C
ATOM   1047  CD ALYS A 120      18.667   8.871  29.249  0.50 25.61           C
ANISOU 1047  CD ALYS A 120     3069   3230   3430    177   -104   -172       C
ATOM   1048  CD BLYS A 120      18.821   9.442  29.407  0.50 23.96           C
ANISOU 1048  CD BLYS A 120     3036   2699   3365    249    -54   -170       C
ATOM   1049  CE ALYS A 120      18.593   9.955  30.311  0.50 28.22           C
ANISOU 1049  CE ALYS A 120     3573   3427   3720    106    -50   -212       C
ATOM   1050  CE BLYS A 120      18.455  10.735  30.060  0.50 26.43           C
ANISOU 1050  CE BLYS A 120     3338   2942   3763    137      0   -260       C
ATOM   1051  NZ ALYS A 120      17.794   9.438  31.460  0.50 30.66           N
ANISOU 1051  NZ ALYS A 120     3694   3883   4070   -132     -4   -155       N
ATOM   1052  NZ BLYS A 120      18.307  10.565  31.532  0.50 29.79           N
ANISOU 1052  NZ BLYS A 120     4049   3307   3960     -5    -49   -208       N
ATOM   1053  N  AGLY A 121      20.856   6.034  25.706  0.50 10.19           N
ANISOU 1053  N  AGLY A 121      349   1571   1952     93     91    299       N
ATOM   1054  N  BGLY A 121      20.881   6.294  24.704  0.50 14.54           N
ANISOU 1054  N  BGLY A 121      304   2383   2835   -279   -195     -4       N
ATOM   1055  CA AGLY A 121      21.380   4.797  25.197  0.50 11.81           C
ANISOU 1055  CA AGLY A 121      377   1842   2267     35    115    298       C
ATOM   1056  CA BGLY A 121      21.361   4.930  24.555  0.50 13.58           C
ANISOU 1056  CA BGLY A 121      253   2222   2685    -15     11    170       C
ATOM   1057  C  AGLY A 121      20.375   3.814  24.632  0.50 11.74           C
ANISOU 1057  C  AGLY A 121      312   1797   2352    254    -99    343       C
ATOM   1058  C  BGLY A 121      20.343   3.861  24.315  0.50 12.58           C
ANISOU 1058  C  BGLY A 121      271   1942   2564    137   -100    329       C
ATOM   1059  O  AGLY A 121      20.761   2.716  24.253  0.50 14.79           O
ANISOU 1059  O  AGLY A 121     1210   1845   2562    472    -44    221       O
ATOM   1060  O  BGLY A 121      20.654   2.772  23.845  0.50 13.89           O
ANISOU 1060  O  BGLY A 121      838   1929   2511    418     39    400       O
ATOM   1061  N   VAL A 122      19.096   4.172  24.600  1.00 12.00           N
ANISOU 1061  N   VAL A 122      326   1667   2566    -33   -104    292       N
ATOM   1062  CA  VAL A 122      17.968   3.286  24.220  1.00 12.60           C
ANISOU 1062  CA  VAL A 122      423   1786   2577    423     98    238       C
ATOM   1063  C   VAL A 122      17.393   3.661  22.878  1.00 12.08           C
ANISOU 1063  C   VAL A 122      594   1627   2369     43   -105     67       C
ATOM   1064  O   VAL A 122      16.948   4.800  22.707  1.00 14.42           O
ANISOU 1064  O   VAL A 122     1609   1407   2461    406   -405     25       O
ATOM   1065  CB  VAL A 122      16.946   3.201  25.257  1.00 12.85           C
ANISOU 1065  CB  VAL A 122      539   1602   2738      6     98    134       C
ATOM   1066  CG1 VAL A 122      15.848   2.254  24.855  1.00 15.40           C
ANISOU 1066  CG1 VAL A 122      924   1909   3016    287    375    114       C
ATOM   1067  CG2 VAL A 122      17.478   2.761  26.640  1.00 16.14           C
ANISOU 1067  CG2 VAL A 122     1232   2272   2628    379     46    398       C
ATOM   1068  N   THR A 123      17.386   2.721  21.946  1.00 12.50           N
ANISOU 1068  N   THR A 123      924   1475   2351    157   -133    120       N
ATOM   1069  CA  THR A 123      16.865   2.920  20.601  1.00 13.70           C
ANISOU 1069  CA  THR A 123     1318   1466   2419     36   -106     84       C
ATOM   1070  C   THR A 123      15.705   1.960  20.339  1.00 13.46           C
ANISOU 1070  C   THR A 123     1393   1319   2402    170   -270    110       C
ATOM   1071  O   THR A 123      15.771   0.796  20.725  1.00 16.98           O
ANISOU 1071  O   THR A 123     1775   1678   2998    -60   -520    429       O
ATOM   1072  CB  THR A 123      17.907   2.668  19.572  1.00 15.83           C
ANISOU 1072  CB  THR A 123     1538   1917   2559      0    -35     80       C
ATOM   1073  OG1 THR A 123      18.976   3.589  19.794  1.00 18.88           O
ANISOU 1073  OG1 THR A 123     2145   2192   2834   -156    283    -23       O
ATOM   1074  CG2 THR A 123      17.386   2.845  18.152  1.00 17.44           C
ANISOU 1074  CG2 THR A 123     1609   2462   2555     33    -63    -15       C
ATOM   1075  N   SER A 124      14.662   2.424  19.712  1.00 12.75           N
ANISOU 1075  N   SER A 124     1347   1311   2184      8   -225    184       N
ATOM   1076  CA  SER A 124      13.617   1.598  19.176  1.00 13.03           C
ANISOU 1076  CA  SER A 124     1142   1395   2413     14   -218    271       C
ATOM   1077  C   SER A 124      13.542   1.798  17.702  1.00 12.34           C
ANISOU 1077  C   SER A 124      910   1507   2269     93    -62    187       C
ATOM   1078  O   SER A 124      13.613   2.933  17.216  1.00 14.97           O
ANISOU 1078  O   SER A 124     2054   1441   2193      4    -43    149       O
ATOM   1079  CB  SER A 124      12.261   1.902  19.802  1.00 13.50           C
ANISOU 1079  CB  SER A 124     1201   1593   2336   -163   -116    348       C
ATOM   1080  OG  SER A 124      11.207   1.240  19.185  1.00 14.05           O
ANISOU 1080  OG  SER A 124     1072   1625   2639      0     23     78       O
ATOM   1081  N   THR A 125      13.369   0.729  16.952  1.00 11.64           N
ANISOU 1081  N   THR A 125      736   1378   2307     58    -60    185       N
ATOM   1082  CA  THR A 125      13.211   0.772  15.499  1.00 11.89           C
ANISOU 1082  CA  THR A 125      646   1555   2315    106     36    243       C
ATOM   1083  C   THR A 125      11.827   0.334  15.117  1.00 12.10           C
ANISOU 1083  C   THR A 125      793   1596   2207    -66      0    186       C
ATOM   1084  O   THR A 125      11.416  -0.774  15.487  1.00 14.60           O
ANISOU 1084  O   THR A 125     1505   1643   2397   -332   -152    201       O
ATOM   1085  CB  THR A 125      14.255  -0.080  14.807  1.00 13.78           C
ANISOU 1085  CB  THR A 125      672   1964   2598    182    288    223       C
ATOM   1086  OG1 THR A 125      15.540   0.361  15.189  1.00 18.11           O
ANISOU 1086  OG1 THR A 125      964   2699   3217    361    381    126       O
ATOM   1087  CG2 THR A 125      14.151  -0.005  13.310  1.00 17.79           C
ANISOU 1087  CG2 THR A 125     1634   2707   2416    217    251     69       C
ATOM   1088  N   ARG A 126      11.136   1.169  14.366  1.00 12.44           N
ANISOU 1088  N   ARG A 126     1050   1538   2137   -332   -129    102       N
ATOM   1089  CA  ARG A 126       9.761   0.926  13.957  1.00 13.70           C
ANISOU 1089  CA  ARG A 126     1349   1713   2141   -391    -11    235       C
ATOM   1090  C   ARG A 126       9.737   0.991  12.429  1.00 12.52           C
ANISOU 1090  C   ARG A 126      749   1854   2152   -293      9    169       C
ATOM   1091  O   ARG A 126      10.170   1.976  11.851  1.00 16.67           O
ANISOU 1091  O   ARG A 126     1960   2037   2335   -825    -44    196       O
ATOM   1092  CB  ARG A 126       8.842   1.938  14.589  1.00 14.61           C
ANISOU 1092  CB  ARG A 126     1127   2233   2189   -389   -130    161       C
ATOM   1093  CG  ARG A 126       8.663   1.525  16.057  1.00 18.37           C
ANISOU 1093  CG  ARG A 126     1322   3191   2467     70   -184    -45       C
ATOM   1094  CD  ARG A 126       8.080   2.483  16.903  1.00 19.66           C
ANISOU 1094  CD  ARG A 126     1301   3565   2604    -70   -254      1       C
ATOM   1095  NE  ARG A 126       6.684   2.757  16.752  1.00 19.40           N
ANISOU 1095  NE  ARG A 126     1251   3682   2434   -126   -278   -312       N
ATOM   1096  CZ  ARG A 126       5.616   2.173  17.319  1.00 17.92           C
ANISOU 1096  CZ  ARG A 126      726   3609   2474   -299    -45   -306       C
ATOM   1097  NH1 ARG A 126       5.726   0.982  17.923  1.00 21.23           N
ANISOU 1097  NH1 ARG A 126     1638   3908   2518   -141    298    -50       N
ATOM   1098  NH2 ARG A 126       4.445   2.719  17.181  1.00 21.06           N
ANISOU 1098  NH2 ARG A 126     1329   3725   2947   -100     35   -191       N
ATOM   1099  N   VAL A 127       9.182  -0.014  11.780  1.00 11.78           N
ANISOU 1099  N   VAL A 127      662   1607   2204   -108    -30    121       N
ATOM   1100  CA  VAL A 127       9.206  -0.083  10.350  1.00 11.21           C
ANISOU 1100  CA  VAL A 127      332   1666   2261   -267    216    106       C
ATOM   1101  C   VAL A 127       7.802   0.016   9.842  1.00 10.59           C
ANISOU 1101  C   VAL A 127      309   1530   2182   -243    146    -39       C
ATOM   1102  O   VAL A 127       6.920  -0.708  10.230  1.00 11.63           O
ANISOU 1102  O   VAL A 127      458   1698   2263   -273    -82    102       O
ATOM   1103  CB  VAL A 127       9.875  -1.404   9.876  1.00 13.20           C
ANISOU 1103  CB  VAL A 127      807   1840   2369    204     53     74       C
ATOM   1104  CG1 VAL A 127       9.839  -1.499   8.333  1.00 15.71           C
ANISOU 1104  CG1 VAL A 127     1512   2137   2317    343     64    -41       C
ATOM   1105  CG2 VAL A 127      11.263  -1.552  10.412  1.00 15.35           C
ANISOU 1105  CG2 VAL A 127     1006   1979   2845    330     52     51       C
ATOM   1106  N   TYR A 128       7.621   0.943   8.869  1.00 11.54           N
ANISOU 1106  N   TYR A 128      356   1660   2366   -216     87    145       N
ATOM   1107  CA  TYR A 128       6.393   1.153   8.215  1.00 11.23           C
ANISOU 1107  CA  TYR A 128      323   1606   2335   -141     63     82       C
ATOM   1108  C   TYR A 128       6.491   0.727   6.743  1.00 10.92           C
ANISOU 1108  C   TYR A 128      277   1485   2387   -171     34      7       C
ATOM   1109  O   TYR A 128       7.516   0.950   6.138  1.00 12.60           O
ANISOU 1109  O   TYR A 128      741   1714   2330   -190     51    -18       O
ATOM   1110  CB  TYR A 128       5.957   2.641   8.255  1.00 11.56           C
ANISOU 1110  CB  TYR A 128      279   1846   2266   -160    -94     61       C
ATOM   1111  CG  TYR A 128       5.536   3.159   9.616  1.00 11.40           C
ANISOU 1111  CG  TYR A 128      487   1486   2358   -201   -358     48       C
ATOM   1112  CD1 TYR A 128       6.482   3.424  10.552  1.00 11.79           C
ANISOU 1112  CD1 TYR A 128      330   1701   2448   -174    -90     25       C
ATOM   1113  CD2 TYR A 128       4.198   3.348   9.918  1.00 10.97           C
ANISOU 1113  CD2 TYR A 128      309   1580   2278   -184   -248      3       C
ATOM   1114  CE1 TYR A 128       6.116   3.889  11.848  1.00 13.23           C
ANISOU 1114  CE1 TYR A 128      644   1840   2542   -118   -223    -30       C
ATOM   1115  CE2 TYR A 128       3.834   3.870  11.158  1.00 12.70           C
ANISOU 1115  CE2 TYR A 128      447   1803   2575   -217     48     27       C
ATOM   1116  CZ  TYR A 128       4.773   4.100  12.088  1.00 13.52           C
ANISOU 1116  CZ  TYR A 128     1004   1661   2470   -310   -156    -43       C
ATOM   1117  OH  TYR A 128       4.313   4.604  13.316  1.00 16.40           O
ANISOU 1117  OH  TYR A 128     1455   2449   2324    253     65    -95       O
ATOM   1118  N   GLU A 129       5.410   0.184   6.243  1.00 12.32           N
ANISOU 1118  N   GLU A 129      519   1781   2381    -86     28     87       N
ATOM   1119  CA AGLU A 129       5.231  -0.208   4.847  0.50 13.25           C
ANISOU 1119  CA AGLU A 129      982   1717   2335    -75     57    -85       C
ATOM   1120  CA BGLU A 129       5.325  -0.085   4.797  0.50 13.35           C
ANISOU 1120  CA BGLU A 129     1062   1674   2333      7     16   -125       C
ATOM   1121  C   GLU A 129       4.163   0.670   4.199  1.00 12.67           C
ANISOU 1121  C   GLU A 129     1062   1533   2218   -218    -12   -126       C
ATOM   1122  O   GLU A 129       3.338   1.207   4.881  1.00 12.86           O
ANISOU 1122  O   GLU A 129     1026   1597   2262    -63    -16     39       O
ATOM   1123  CB AGLU A 129       4.810  -1.686   4.794  0.50 14.62           C
ANISOU 1123  CB AGLU A 129     1278   1878   2396   -138     26    -37       C
ATOM   1124  CB BGLU A 129       5.224  -1.580   4.473  0.50 14.30           C
ANISOU 1124  CB BGLU A 129     1272   1794   2365    144    -34    -58       C
ATOM   1125  CG AGLU A 129       5.973  -2.627   5.090  0.50 19.47           C
ANISOU 1125  CG AGLU A 129     2296   2402   2699    153     30     -7       C
ATOM   1126  CG BGLU A 129       3.867  -2.206   4.785  0.50 19.61           C
ANISOU 1126  CG BGLU A 129     2161   2399   2889   -118    -75   -110       C
ATOM   1127  CD AGLU A 129       5.703  -4.054   4.656  0.50 23.08           C
ANISOU 1127  CD AGLU A 129     2906   2667   3193   -312     17      5       C
ATOM   1128  CD BGLU A 129       3.826  -3.747   4.616  0.50 23.92           C
ANISOU 1128  CD BGLU A 129     2909   2757   3419   -310   -165   -186       C
ATOM   1129  OE1AGLU A 129       4.750  -4.291   3.885  0.50 26.19           O
ANISOU 1129  OE1AGLU A 129     3916   2880   3154   -176   -334   -182       O
ATOM   1130  OE1BGLU A 129       2.760  -4.255   4.279  0.50 25.81           O
ANISOU 1130  OE1BGLU A 129     3550   2441   3815   -615   -453    -72       O
ATOM   1131  OE2AGLU A 129       6.427  -4.948   5.120  0.50 25.00           O
ANISOU 1131  OE2AGLU A 129     2828   3036   3632   -118    109   -153       O
ATOM   1132  OE2BGLU A 129       4.831  -4.451   4.840  0.50 26.20           O
ANISOU 1132  OE2BGLU A 129     3290   3161   3503   -172   -311   -126       O
ATOM   1133  N   ARG A 130       4.133   0.794   2.864  1.00 12.92           N
ANISOU 1133  N   ARG A 130      848   1776   2285    -72    -80   -325       N
ATOM   1134  CA  ARG A 130       3.045   1.485   2.240  1.00 13.89           C
ANISOU 1134  CA  ARG A 130      949   1917   2411   -117   -141   -240       C
ATOM   1135  C   ARG A 130       1.755   0.819   2.528  1.00 15.01           C
ANISOU 1135  C   ARG A 130     1150   1888   2665   -221   -292   -253       C
ATOM   1136  O   ARG A 130       1.622  -0.409   2.426  1.00 17.07           O
ANISOU 1136  O   ARG A 130     1590   1844   3049   -169   -425   -170       O
ATOM   1137  CB  ARG A 130       3.275   1.551   0.714  1.00 16.05           C
ANISOU 1137  CB  ARG A 130     1252   2444   2401    -34   -339   -197       C
ATOM   1138  CG  ARG A 130       4.490   2.279   0.286  1.00 17.25           C
ANISOU 1138  CG  ARG A 130     1537   2426   2588    -75   -198     81       C
ATOM   1139  CD  ARG A 130       4.213   3.698   0.031  1.00 21.38           C
ANISOU 1139  CD  ARG A 130     1691   2746   3684     92   -261   -122       C
ATOM   1140  NE  ARG A 130       5.378   4.398  -0.448  1.00 19.85           N
ANISOU 1140  NE  ARG A 130     1362   2396   3781    110   -422    179       N
ATOM   1141  CZ  ARG A 130       5.452   5.707  -0.585  1.00 17.60           C
ANISOU 1141  CZ  ARG A 130     1252   2368   3064    -86   -259    218       C
ATOM   1142  NH1 ARG A 130       4.421   6.419  -0.343  1.00 17.83           N
ANISOU 1142  NH1 ARG A 130     1639   2290   2846   -251   -111    237       N
ATOM   1143  NH2 ARG A 130       6.593   6.265  -0.932  1.00 19.78           N
ANISOU 1143  NH2 ARG A 130     1789   2455   3271   -276    311    219       N
ATOM   1144  N   ALA A 131       0.730   1.589   2.824  1.00 15.57           N
ANISOU 1144  N   ALA A 131     1008   1932   2973   -271   -252    -67       N
ATOM   1145  CA  ALA A 131      -0.569   1.035   3.146  1.00 19.28           C
ANISOU 1145  CA  ALA A 131     1521   2385   3417   -312   -250    -58       C
ATOM   1146  C   ALA A 131      -1.316   0.536   1.889  1.00 22.18           C
ANISOU 1146  C   ALA A 131     1962   2782   3683   -448   -266    -46       C
ATOM   1147  O   ALA A 131      -0.892   0.916   0.779  1.00 24.91           O
ANISOU 1147  O   ALA A 131     2533   2999   3930   -360   -431     39       O
ATOM   1148  CB  ALA A 131      -1.390   2.042   3.925  1.00 21.25           C
ANISOU 1148  CB  ALA A 131     1636   2793   3644   -236    -82   -115       C
TER    1149      ALA A 131
HETATM 1150  C1 AZGC A 133       3.984   6.315  22.766  0.50 20.67           C
ANISOU 1150  C1 AZGC A 133     1921   2556   3375   -305    515    668       C
HETATM 1151  C1 BZGC A 133       5.352   7.074  23.236  0.50 22.84           C
ANISOU 1151  C1 BZGC A 133     2640   2116   3922    171    763    388       C
HETATM 1152  O1 AZGC A 133       3.319   6.837  21.590  0.50 24.30           O
ANISOU 1152  O1 AZGC A 133     2312   3633   3286     -7     17    428       O
HETATM 1153  O1 BZGC A 133       4.247   7.059  22.326  0.50 29.65           O
ANISOU 1153  O1 BZGC A 133     3906   3523   3833    111    196     24       O
HETATM 1154  C2 AZGC A 133       4.233   7.054  20.610  0.50 22.65           C
ANISOU 1154  C2 AZGC A 133     2562   2960   3082    316    122    127       C
HETATM 1155  C2 BZGC A 133       4.800   7.294  21.112  0.50 26.18           C
ANISOU 1155  C2 BZGC A 133     3298   3206   3441    240    182    -99       C
HETATM 1156  O2 AZGC A 133       5.844   4.973  15.285  0.50 17.92           O
ANISOU 1156  O2 AZGC A 133     1681   2520   2608    588   -471   -298       O
HETATM 1157  O2 BZGC A 133       6.222   4.925  15.360  0.50 24.03           O
ANISOU 1157  O2 BZGC A 133     2745   3204   3180    286   -131   -376       O
HETATM 1158  C3 AZGC A 133       3.965   6.649  19.298  0.50 24.87           C
ANISOU 1158  C3 AZGC A 133     2911   3451   3085     36      3     34       C
HETATM 1159  C3 BZGC A 133       4.047   7.212  19.942  0.50 27.10           C
ANISOU 1159  C3 BZGC A 133     3463   3357   3476    230    132   -112       C
HETATM 1160  O3 AZGC A 133       5.547   7.175  15.252  0.50 23.86           O
ANISOU 1160  O3 AZGC A 133     3056   2647   3360    458   -187   -107       O
HETATM 1161  O3 BZGC A 133       5.515   7.000  15.006  0.50 26.97           O
ANISOU 1161  O3 BZGC A 133     3356   3267   3623     29   -237    125       O
HETATM 1162  C4 AZGC A 133       4.919   6.824  18.296  0.50 25.04           C
ANISOU 1162  C4 AZGC A 133     2933   3478   3102     79    102   -171       C
HETATM 1163  C4 BZGC A 133       4.666   7.429  18.712  0.50 26.16           C
ANISOU 1163  C4 BZGC A 133     3335   3200   3402    199     73   -163       C
HETATM 1164  C5 AZGC A 133       5.454   7.644  20.901  0.50 21.92           C
ANISOU 1164  C5 AZGC A 133     2188   2744   3397    373     12    140       C
HETATM 1165  C5 BZGC A 133       6.159   7.580  21.052  0.50 27.77           C
ANISOU 1165  C5 BZGC A 133     3639   3380   3533   -128      1     -1       C
HETATM 1166  C6 AZGC A 133       6.425   7.786  19.892  0.50 23.35           C
ANISOU 1166  C6 AZGC A 133     2839   2890   3141    391    121    -50       C
HETATM 1167  C6 BZGC A 133       6.781   7.799  19.826  0.50 26.13           C
ANISOU 1167  C6 BZGC A 133     3202   3307   3417    171    -29    -41       C
HETATM 1168  C7 AZGC A 133       6.161   7.398  18.571  0.50 23.96           C
ANISOU 1168  C7 AZGC A 133     2818   3049   3235    287   -257    -81       C
HETATM 1169  C7 BZGC A 133       6.023   7.732  18.652  0.50 26.75           C
ANISOU 1169  C7 BZGC A 133     3361   3347   3453     -1    -96   -196       C
HETATM 1170  C8 AZGC A 133       7.237   7.595  17.441  0.50 20.56           C
ANISOU 1170  C8 AZGC A 133     1777   2430   3605    531   -564   -295       C
HETATM 1171  C8 BZGC A 133       6.692   7.980  17.283  0.50 26.88           C
ANISOU 1171  C8 BZGC A 133     3237   3214   3758   -126    -55   -176       C
HETATM 1172  C9 AZGC A 133       7.388   6.345  16.529  0.50 22.06           C
ANISOU 1172  C9 AZGC A 133     2056   2775   3550      6   -361   -472       C
HETATM 1173  C9 BZGC A 133       7.200   6.673  16.648  0.50 26.05           C
ANISOU 1173  C9 BZGC A 133     2853   3265   3777    -31   -188   -323       C
HETATM 1174  C10AZGC A 133       6.177   6.146  15.593  0.50 20.34           C
ANISOU 1174  C10AZGC A 133     1401   2488   3838    113   -398    -28       C
HETATM 1175  C10BZGC A 133       6.246   6.155  15.568  0.50 23.10           C
ANISOU 1175  C10BZGC A 133     1739   2953   4085   -186   -222      5       C
HETATM 1176  O   HOH A 134       6.475  23.367  26.487  1.00 51.30           O
ANISOU 1176  O   HOH A 134     7180   8411   3899    558     48   1512       O
HETATM 1177  O   HOH A 135      -3.571   3.273  29.177  1.00 30.34           O
ANISOU 1177  O   HOH A 135     2820   3507   5200   -167   -763   -538       O
HETATM 1178  O   HOH A 136       9.588  32.950   8.161  1.00 33.86           O
ANISOU 1178  O   HOH A 136     3843   3103   5919    -22  -1512   -556       O
HETATM 1179  O   HOH A 137      10.354  22.054  12.708  1.00 11.15           O
ANISOU 1179  O   HOH A 137      463   1403   2368     89     30    -27       O
HETATM 1180  O   HOH A 138       7.273  -3.139   1.600  1.00 41.67           O
ANISOU 1180  O   HOH A 138     6176   3139   6517    263   1092    274       O
HETATM 1181  O   HOH A 139      12.373  10.335  31.837  1.00 41.92           O
ANISOU 1181  O   HOH A 139     4483   6644   4798  -2031   -168   -834       O
HETATM 1182  O   HOH A 140      -2.783   0.726  -1.212  1.00 40.82           O
ANISOU 1182  O   HOH A 140     4075   6168   5266   -560  -1570    242       O
HETATM 1183  O   HOH A 141      18.454  11.802  21.537  1.00 39.90           O
ANISOU 1183  O   HOH A 141     5314   5426   4420   1143   -122   -705       O
HETATM 1184  O   HOH A 142      -3.397  14.522  19.577  1.00 33.51           O
ANISOU 1184  O   HOH A 142     2362   5546   4821   -568    512   -261       O
HETATM 1185  O   HOH A 143      13.648  26.660  15.279  1.00 13.37           O
ANISOU 1185  O   HOH A 143      643   1632   2805   -301   -135    -59       O
HETATM 1186  O   HOH A 144       7.180  24.885  12.250  1.00 12.86           O
ANISOU 1186  O   HOH A 144      310   1874   2701     37    108   -354       O
HETATM 1187  O   HOH A 145      -3.782  -0.494  22.407  1.00 13.43           O
ANISOU 1187  O   HOH A 145      878   1692   2532   -214   -111     30       O
HETATM 1188  O   HOH A 146       4.645  24.333  13.139  1.00 13.11           O
ANISOU 1188  O   HOH A 146      523   1832   2626    -58    -94   -344       O
HETATM 1189  O   HOH A 147       2.276  30.196  -7.100  1.00 39.11           O
ANISOU 1189  O   HOH A 147     6904   4621   3332    124   -124     11       O
HETATM 1190  O   HOH A 148       2.867  -2.374   1.103  1.00 39.41           O
ANISOU 1190  O   HOH A 148     5793   3996   5183    726   -114  -2063       O
HETATM 1191  O   HOH A 149       8.875  28.750  16.942  1.00 25.64           O
ANISOU 1191  O   HOH A 149     2445   2468   4829     -6    466   -557       O
HETATM 1192  O   HOH A 150      13.110  -4.002   2.583  1.00 45.32           O
ANISOU 1192  O   HOH A 150     7366   3732   6120    730  -1007   1610       O
HETATM 1193  O   HOH A 151      11.746  12.410  12.127  1.00 13.90           O
ANISOU 1193  O   HOH A 151     1483   1529   2266    224    186    -12       O
HETATM 1194  O   HOH A 152       9.756  22.932   5.347  1.00 16.30           O
ANISOU 1194  O   HOH A 152     1110   2691   2391    280   -138   -133       O
HETATM 1195  O   HOH A 153       9.570  -9.045  20.493  1.00 43.40           O
ANISOU 1195  O   HOH A 153     2983   8025   5480    626  -1065  -2046       O
HETATM 1196  O   HOH A 154      -1.853  -3.966  11.846  1.00 42.16           O
ANISOU 1196  O   HOH A 154     6414   4942   4662  -2859   -526   -107       O
HETATM 1197  O   HOH A 155      19.085  19.656  25.150  1.00 46.57           O
ANISOU 1197  O   HOH A 155     6619   5824   5252    222  -1330  -1823       O
HETATM 1198  O   HOH A 156       7.612  25.771  -0.994  1.00 39.22           O
ANISOU 1198  O   HOH A 156     2978   6908   5015  -1820    -62   -316       O
HETATM 1199  O   HOH A 157      15.215   9.027   3.246  1.00 18.17           O
ANISOU 1199  O   HOH A 157     2188   1992   2722   -333    573    177       O
HETATM 1200  O   HOH A 158       1.043  20.154   5.046  1.00 17.16           O
ANISOU 1200  O   HOH A 158      983   2713   2825   -136    -76    288       O
HETATM 1201  O   HOH A 159      12.814  12.160  -3.124  1.00 43.71           O
ANISOU 1201  O   HOH A 159     5170   5793   5641  -1973   1766  -1154       O
HETATM 1202  O   HOH A 160       5.745  -6.794   6.425  1.00 59.18           O
ANISOU 1202  O   HOH A 160     9558   3504   9421    499    960  -1114       O
HETATM 1203  O   HOH A 161      22.542   9.224   8.861  1.00 38.52           O
ANISOU 1203  O   HOH A 161     5220   4681   4731   -367   -197    495       O
HETATM 1204  O   HOH A 162       4.096   9.339  15.485  1.00 31.09           O
ANISOU 1204  O   HOH A 162     4050   3429   4331    616   1654    652       O
HETATM 1205  O   HOH A 163      -3.668  -1.011  19.710  1.00 16.18           O
ANISOU 1205  O   HOH A 163      939   2359   2847   -680    -78    182       O
HETATM 1206  O   HOH A 164      -4.865   3.512   5.329  1.00 53.96           O
ANISOU 1206  O   HOH A 164     4093   7694   8716    869  -2218   -412       O
HETATM 1207  O   HOH A 165       9.988  -7.142  15.635  1.00 42.25           O
ANISOU 1207  O   HOH A 165     3964   3449   8640    651    190    412       O
HETATM 1208  O   HOH A 166      24.006   7.533  24.660  1.00 44.66           O
ANISOU 1208  O   HOH A 166     3032   6940   6997    -68    368    577       O
HETATM 1209  O   HOH A 167       3.426  11.369  19.361  1.00 17.45           O
ANISOU 1209  O   HOH A 167     1606   2324   2700   -437    241     19       O
HETATM 1210  O   HOH A 168       4.138  27.103   2.316  1.00 20.66           O
ANISOU 1210  O   HOH A 168     1579   2533   3736    279   -260     68       O
HETATM 1211  O   HOH A 169       1.616   5.730   0.123  1.00 18.26           O
ANISOU 1211  O   HOH A 169     1958   2265   2713   -217      3   -329       O
HETATM 1212  O   HOH A 170      13.939  -2.132  31.474  1.00 38.26           O
ANISOU 1212  O   HOH A 170     3912   5386   5239   1493   -450    973       O
HETATM 1213  O   HOH A 171      16.232  21.123   7.185  1.00 19.91           O
ANISOU 1213  O   HOH A 171     2464   1846   3255   -248    113    128       O
HETATM 1214  O   HOH A 172       9.556  -3.859  23.294  1.00 37.04           O
ANISOU 1214  O   HOH A 172     5514   4738   3820   -577   -378    982       O
HETATM 1215  O   HOH A 173      14.641  25.101  17.377  1.00 18.29           O
ANISOU 1215  O   HOH A 173     1372   2168   3409   -127   -256   -171       O
HETATM 1216  O   HOH A 174       1.817  12.891  14.366  1.00 20.33           O
ANISOU 1216  O   HOH A 174     2077   2747   2900   -325     69    887       O
HETATM 1217  O   HOH A 175      -5.938   3.352  27.278  1.00 32.66           O
ANISOU 1217  O   HOH A 175     1419   3691   7299   -102    223   -574       O
HETATM 1218  O   HOH A 176       2.898  31.924  -9.144  1.00 24.80           O
ANISOU 1218  O   HOH A 176     3209   2751   3463      3    126    110       O
HETATM 1219  O   HOH A 177      14.243   0.703  31.729  1.00 33.30           O
ANISOU 1219  O   HOH A 177     3513   5081   4056    104    136    188       O
HETATM 1220  O   HOH A 178      25.248   5.330  23.846  1.00 41.93           O
ANISOU 1220  O   HOH A 178     6261   5174   4496  -1517   1426    381       O
HETATM 1221  O   HOH A 179      18.990  17.935  14.786  1.00 30.74           O
ANISOU 1221  O   HOH A 179     2291   4083   5303    -85     59    598       O
HETATM 1222  O   HOH A 180      16.428   0.655  32.763  1.00 43.73           O
ANISOU 1222  O   HOH A 180     5503   5802   5308    -76  -1021   2519       O
HETATM 1223  O   HOH A 181       8.786  10.502  21.474  1.00 17.59           O
ANISOU 1223  O   HOH A 181     1916   1934   2831   -159    282    -40       O
HETATM 1224  O   HOH A 182      19.109  19.154  17.542  1.00 35.77           O
ANISOU 1224  O   HOH A 182     3425   4426   5736  -1240    727   -151       O
HETATM 1225  O   HOH A 183      16.205  18.803  14.197  1.00 21.84           O
ANISOU 1225  O   HOH A 183     2811   2469   3017   -690   -315    220       O
HETATM 1226  O   HOH A 184      15.962  21.114  19.420  1.00 30.81           O
ANISOU 1226  O   HOH A 184     2279   3351   6074     58   -348    799       O
HETATM 1227  O   HOH A 185      -7.602   6.657  19.051  1.00 32.91           O
ANISOU 1227  O   HOH A 185     2723   4797   4982   1018    412  -1029       O
HETATM 1228  O   HOH A 186       6.043  27.577  15.296  1.00 18.20           O
ANISOU 1228  O   HOH A 186     1035   2193   3687     61   -543    -89       O
HETATM 1229  O   HOH A 187       7.951   2.513  -2.755  1.00 37.18           O
ANISOU 1229  O   HOH A 187     6159   3678   4288   1303   -681    496       O
HETATM 1230  O   HOH A 188      14.270  18.841   0.372  1.00 29.90           O
ANISOU 1230  O   HOH A 188     4383   4214   2763   1565   -389     45       O
HETATM 1231  O   HOH A 189      16.844  19.308   1.898  1.00 28.62           O
ANISOU 1231  O   HOH A 189     3440   4014   3420    154    472    758       O
HETATM 1232  O   HOH A 190      21.230   7.367   8.236  1.00 38.81           O
ANISOU 1232  O   HOH A 190     3596   5919   5228   1470   -886  -1092       O
HETATM 1233  O   HOH A 191      16.084  21.339   4.146  1.00 38.12           O
ANISOU 1233  O   HOH A 191     5066   5408   4009  -2004     -1   1036       O
HETATM 1234  O   HOH A 192       8.691  -3.033  20.227  1.00 20.80           O
ANISOU 1234  O   HOH A 192     1357   2506   4040    293   -310   -305       O
HETATM 1235  O   HOH A 193      20.563   1.237  32.528  1.00 44.66           O
ANISOU 1235  O   HOH A 193     6574   4223   6170    487   1612  -1483       O
HETATM 1236  O   HOH A 194       8.790  21.178   2.941  1.00 42.14           O
ANISOU 1236  O   HOH A 194     4287   4346   7379   -992   1212  -1241       O
HETATM 1237  O   HOH A 195      15.735  -3.276  15.868  1.00 35.85           O
ANISOU 1237  O   HOH A 195     3395   2293   7932     84   1007   -484       O
HETATM 1238  O   HOH A 196      13.495  22.164   0.167  1.00 42.62           O
ANISOU 1238  O   HOH A 196     7036   4673   4482   1024   1357    893       O
HETATM 1239  O   HOH A 197      -2.177  30.140 -12.894  1.00 35.03           O
ANISOU 1239  O   HOH A 197     2942   4995   5370  -1097   -204   -423       O
HETATM 1240  O   HOH A 198       2.993  21.303  23.676  1.00 42.04           O
ANISOU 1240  O   HOH A 198     7589   3438   4947   1338   2260    -92       O
HETATM 1241  O   HOH A 199      12.191 -10.258  16.948  1.00 44.00           O
ANISOU 1241  O   HOH A 199     6953   3414   6349   -740  -1101    144       O
HETATM 1242  O   HOH A 200      20.856  11.185  10.704  1.00 43.52           O
ANISOU 1242  O   HOH A 200     2714   7993   5825    375     63    385       O
HETATM 1243  O   HOH A 201      11.145   6.777  -3.155  1.00 44.24           O
ANISOU 1243  O   HOH A 201     4649   7548   4612   2497    712   1703       O
HETATM 1244  O   HOH A 202       2.739  -7.946  17.101  1.00 43.40           O
ANISOU 1244  O   HOH A 202     2109   6149   8231     19   -908   -663       O
HETATM 1245  O   HOH A 203       5.885  -2.421  22.947  1.00 35.60           O
ANISOU 1245  O   HOH A 203     2687   6679   4158    422   -686   -363       O
HETATM 1246  O   HOH A 204      -1.154  16.693  -0.596  1.00 39.00           O
ANISOU 1246  O   HOH A 204     2904   6905   5009    952   -165   2206       O
HETATM 1247  O   HOH A 205      -0.674  14.321   6.376  1.00 18.45           O
ANISOU 1247  O   HOH A 205     1744   2144   3123    311   -145     29       O
HETATM 1248  O   HOH A 206      -5.353  13.931  14.873  1.00 41.79           O
ANISOU 1248  O   HOH A 206     3754   3909   8215    800    662   1063       O
HETATM 1249  O   HOH A 207      20.137   5.020  28.461  1.00 23.28           O
ANISOU 1249  O   HOH A 207     2596   2487   3761    566   -649     26       O
HETATM 1250  O   HOH A 208      -6.657  11.923   6.020  1.00 42.58           O
ANISOU 1250  O   HOH A 208     3984   7112   5080    669   1339   1848       O
HETATM 1251  O   HOH A 209       6.169  -8.434  18.604  1.00 47.84           O
ANISOU 1251  O   HOH A 209     6858   5883   5434  -1828   -588    212       O
HETATM 1252  O   HOH A 210       6.325  11.373  19.531  1.00 19.65           O
ANISOU 1252  O   HOH A 210     1510   2259   3694   -476    168   -193       O
HETATM 1253  O   HOH A 211      19.091  20.561   7.035  1.00 41.11           O
ANISOU 1253  O   HOH A 211     4052   3642   7926  -1020   2552  -1362       O
HETATM 1254  O   HOH A 212      14.360  -5.377  22.605  1.00 31.35           O
ANISOU 1254  O   HOH A 212     5252   2399   4261    250  -1681    224       O
HETATM 1255  O   HOH A 213      16.901  20.663  17.294  1.00 37.02           O
ANISOU 1255  O   HOH A 213     2221   4981   6862   1204    509   1620       O
HETATM 1256  O   HOH A 214      16.229  -3.260  29.378  1.00 42.24           O
ANISOU 1256  O   HOH A 214     2173   4969   8908    845   1333   1820       O
HETATM 1257  O   HOH A 215      -4.451   1.996  12.440  1.00 60.82           O
ANISOU 1257  O   HOH A 215     7659   8810   6636  -1629  -6475   3354       O
HETATM 1258  O   HOH A 216       1.610  26.150   2.071  1.00 23.19           O
ANISOU 1258  O   HOH A 216     2100   1995   4713     17     69   -373       O
HETATM 1259  O   HOH A 217      19.733   1.725  15.087  1.00 36.76           O
ANISOU 1259  O   HOH A 217     4279   5318   4369     -6   -508    784       O
HETATM 1260  O   HOH A 218      -8.737  11.899  18.012  1.00 46.07           O
ANISOU 1260  O   HOH A 218     4187   5336   7979   1331    442  -1999       O
HETATM 1261  O   HOH A 219       2.639   6.796  13.673  1.00 22.55           O
ANISOU 1261  O   HOH A 219     2164   2476   3925   -361    781   -291       O
HETATM 1262  O   HOH A 220      -1.682  -0.105  10.131  1.00 53.09           O
ANISOU 1262  O   HOH A 220     7496   5593   7082   -630  -2671   2544       O
HETATM 1263  O   HOH A 221      12.623  -5.278  27.905  1.00 48.54           O
ANISOU 1263  O   HOH A 221     3763   3777  10901    758   2769   1383       O
HETATM 1264  O   HOH A 222       2.146   9.794  17.381  1.00 17.90           O
ANISOU 1264  O   HOH A 222     1778   2330   2690   -473   -123     15       O
HETATM 1265  O   HOH A 223      11.288  -3.087  13.799  1.00 21.10           O
ANISOU 1265  O   HOH A 223     2282   2448   3284   -117    -61    -32       O
HETATM 1266  O   HOH A 224      11.299  -2.859   0.911  1.00 21.95           O
ANISOU 1266  O   HOH A 224     3045   2121   3173   -374     15     36       O
HETATM 1267  O   HOH A 225       1.643  15.744  -0.234  1.00 21.86           O
ANISOU 1267  O   HOH A 225     3329   2641   2335    423   -596   -307       O
HETATM 1268  O   HOH A 226      11.433  -5.734  21.142  1.00 24.74           O
ANISOU 1268  O   HOH A 226     3489   1670   4240   -287    521    529       O
HETATM 1269  O   HOH A 227       7.031  27.712  11.874  1.00 20.55           O
ANISOU 1269  O   HOH A 227     1254   2271   4282    374   -495   -164       O
HETATM 1270  O   HOH A 228       9.055  -4.107  -1.816  1.00 40.08           O
ANISOU 1270  O   HOH A 228     7135   3556   4536   -667    942    684       O
HETATM 1271  O   HOH A 229       3.375  -7.068  10.834  1.00 70.83           O
ANISOU 1271  O   HOH A 229     7230   6671  13009  -3739  -2714   2160       O
HETATM 1272  O   HOH A 230       6.268   9.014  -1.778  1.00 22.41           O
ANISOU 1272  O   HOH A 230     2114   2833   3566   -532    307   -358       O
HETATM 1273  O   HOH A 231      17.523  13.219  30.588  1.00 45.29           O
ANISOU 1273  O   HOH A 231     5922   7061   4225    568  -1023    973       O
HETATM 1274  O   HOH A 232       1.812   3.953  19.880  1.00 38.46           O
ANISOU 1274  O   HOH A 232     3133   5010   6470   -633   -666   1078       O
HETATM 1275  O   HOH A 233      -8.555   5.703  17.553  1.00 38.30           O
ANISOU 1275  O   HOH A 233     1600   5455   7497    766   1024   -384       O
HETATM 1276  O   HOH A 234       6.178  -0.565   1.381  1.00 20.17           O
ANISOU 1276  O   HOH A 234     1061   3039   3562    140    143   -377       O
HETATM 1277  O   HOH A 235       0.426  18.530  18.942  1.00 31.96           O
ANISOU 1277  O   HOH A 235     3230   3455   5458   -741  -1771   1576       O
HETATM 1278  O   HOH A 236      12.986  21.683  19.849  1.00 22.10           O
ANISOU 1278  O   HOH A 236     2056   3868   2472   -901    -49   -283       O
HETATM 1279  O   HOH A 237       9.204   7.240  -3.101  1.00 48.59           O
ANISOU 1279  O   HOH A 237     5582   7035   5844    128    136    500       O
HETATM 1280  O   HOH A 238      -2.573  19.936   1.478  1.00 25.17           O
ANISOU 1280  O   HOH A 238     2914   3502   3145  -1501   -245    333       O
HETATM 1281  O   HOH A 239      21.030   7.826  15.063  1.00 41.20           O
ANISOU 1281  O   HOH A 239     4594   4400   6657    582    214   1278       O
HETATM 1282  O   HOH A 240      14.663   1.602  29.261  1.00 22.88           O
ANISOU 1282  O   HOH A 240     1728   3788   3176    942   -148    516       O
HETATM 1283  O   HOH A 241      17.374  13.350  28.012  1.00 27.85           O
ANISOU 1283  O   HOH A 241     2223   3685   4671    901   -397    986       O
HETATM 1284  O   HOH A 242      10.776   9.883  -4.114  1.00 45.62           O
ANISOU 1284  O   HOH A 242     5336   7589   4407   -388    805   -247       O
HETATM 1285  O   HOH A 243      15.841  -3.057  -2.624  1.00 29.05           O
ANISOU 1285  O   HOH A 243     5181   3188   2667    373    381    380       O
HETATM 1286  O   HOH A 244       2.855  13.800  18.210  1.00 22.58           O
ANISOU 1286  O   HOH A 244     2545   2397   3637   -406    349     20       O
HETATM 1287  O   HOH A 245       0.160   3.421  -0.268  1.00 24.88           O
ANISOU 1287  O   HOH A 245     2798   2675   3980   -240   -915    -63       O
HETATM 1288  O   HOH A 246       2.891   1.043  18.828  1.00 22.20           O
ANISOU 1288  O   HOH A 246     1765   3769   2898   -566     94    -87       O
HETATM 1289  O   HOH A 247       0.384   5.195  32.413  1.00 25.09           O
ANISOU 1289  O   HOH A 247     3276   3534   2720   -236    -69   -232       O
HETATM 1290  O   HOH A 248       4.740  10.197  29.309  1.00 26.70           O
ANISOU 1290  O   HOH A 248     4606   2559   2978   -205     69    555       O
HETATM 1291  O   HOH A 249       5.045  22.663  24.072  1.00 30.90           O
ANISOU 1291  O   HOH A 249     3914   4033   3791   1855    497    -93       O
HETATM 1292  O   HOH A 250      -2.081  15.931  17.757  1.00 26.85           O
ANISOU 1292  O   HOH A 250     4714   2658   2828    -86    622   -388       O
HETATM 1293  O   HOH A 251      -0.771  18.681   3.742  1.00 21.61           O
ANISOU 1293  O   HOH A 251     2003   2810   3395      3   -564    148       O
HETATM 1294  O   HOH A 252      -0.052   5.206  18.491  1.00 31.26           O
ANISOU 1294  O   HOH A 252     2641   3692   5542   -728  -1503   1580       O
HETATM 1295  O   HOH A 253      18.763  17.147   2.574  1.00 26.13           O
ANISOU 1295  O   HOH A 253     2727   3765   3434    165    592   -408       O
HETATM 1296  O   HOH A 254       0.840  15.753  18.493  1.00 24.06           O
ANISOU 1296  O   HOH A 254     2474   3249   3418    -79    507   -147       O
HETATM 1297  O   HOH A 255      20.675   5.072  21.590  1.00 23.49           O
ANISOU 1297  O   HOH A 255     2018   2889   4015    233     -6    152       O
HETATM 1298  O   HOH A 256      -7.244   9.528  19.703  1.00 28.32           O
ANISOU 1298  O   HOH A 256     1889   5167   3702     -1    389    -89       O
HETATM 1299  O   HOH A 257      17.706  13.865  21.733  1.00 24.56           O
ANISOU 1299  O   HOH A 257     2212   3897   3222   -324    -28   -666       O
HETATM 1300  O   HOH A 258       2.163  -3.677  24.856  1.00 25.20           O
ANISOU 1300  O   HOH A 258     2684   3459   3429    625   -193   -537       O
HETATM 1301  O   HOH A 259       6.029  12.275  16.545  1.00 30.44           O
ANISOU 1301  O   HOH A 259      974   7202   3389  -1094    387    332       O
HETATM 1302  O   HOH A 260       8.968  12.101  30.770  1.00 27.94           O
ANISOU 1302  O   HOH A 260     4569   2889   3156   -247    738    357       O
HETATM 1303  O   HOH A 261       4.985  -1.596  25.593  1.00 27.70           O
ANISOU 1303  O   HOH A 261     2631   3580   4314    759   -559   -459       O
HETATM 1304  O   HOH A 262      18.230  11.370  24.291  1.00 29.13           O
ANISOU 1304  O   HOH A 262     1107   2533   7427    304    369    780       O
HETATM 1305  O   HOH A 263      18.253   4.407   2.529  1.00 26.54           O
ANISOU 1305  O   HOH A 263     2216   4737   3128    385    -37   -345       O
HETATM 1306  O   HOH A 264      -8.163   6.394  15.069  1.00 33.10           O
ANISOU 1306  O   HOH A 264     2419   4846   5311   -311   -196   1118       O
HETATM 1307  O   HOH A 265       5.155  29.021   3.988  1.00 35.96           O
ANISOU 1307  O   HOH A 265     4463   3356   5843  -1258    464  -1205       O
HETATM 1308  O   HOH A 266       9.080  21.323  29.566  1.00 29.06           O
ANISOU 1308  O   HOH A 266     3660   3617   3760   1407   -278   -794       O
HETATM 1309  O   HOH A 267      16.981   7.126   2.184  1.00 32.49           O
ANISOU 1309  O   HOH A 267     4438   3273   4632  -1234   1228   -198       O
HETATM 1310  O   HOH A 268      15.394  19.815  27.268  1.00 29.08           O
ANISOU 1310  O   HOH A 268     4745   2897   3404   -459   -953   -195       O
HETATM 1311  O   HOH A 269      -2.050  20.290  11.414  1.00 29.69           O
ANISOU 1311  O   HOH A 269     2475   2934   5870   -464   1671   -255       O
HETATM 1312  O   HOH A 270       6.368   8.538  12.881  1.00 25.14           O
ANISOU 1312  O   HOH A 270     1778   4345   3430   -734    497   -223       O
HETATM 1313  O   HOH A 271      16.171  -0.884  17.640  1.00 35.64           O
ANISOU 1313  O   HOH A 271     6460   3656   3424   2134  -1692   -648       O
HETATM 1314  O   HOH A 272      22.664   2.219  22.237  1.00 21.55           O
ANISOU 1314  O   HOH A 272     2747   1947   3491    -79    728    -90       O
HETATM 1315  O   HOH A 273      -0.032   7.893  17.528  1.00 21.91           O
ANISOU 1315  O   HOH A 273     2211   2781   3331   -330     68    100       O
HETATM 1316  O   HOH A 274      -0.393  -5.010  17.750  1.00 29.00           O
ANISOU 1316  O   HOH A 274     2547   2676   5792     49    133    611       O
HETATM 1317  O   HOH A 275      -4.738  11.955  13.398  1.00 33.46           O
ANISOU 1317  O   HOH A 275     2525   6411   3776    420   -337    708       O
HETATM 1318  O   HOH A 276       8.327  -3.315  22.654  1.00 32.06           O
ANISOU 1318  O   HOH A 276     3841   2623   5714   -390   -119     61       O
HETATM 1319  O   HOH A 277       8.624  -6.024  20.264  1.00 35.82           O
ANISOU 1319  O   HOH A 277     4470   4601   4539    771    407   -295       O
HETATM 1320  O   HOH A 278       4.762  17.131  29.637  1.00 33.21           O
ANISOU 1320  O   HOH A 278     6467   3282   2867   -682    186     74       O
HETATM 1321  O   HOH A 279       8.842   4.902  32.833  1.00 27.49           O
ANISOU 1321  O   HOH A 279     2783   3631   4031     22   -962   -288       O
HETATM 1322  O   HOH A 280       2.702  12.267  29.975  1.00 36.16           O
ANISOU 1322  O   HOH A 280     6579   3293   3864    638    -30   -118       O
HETATM 1323  O   HOH A 281       7.065  -3.000  30.597  1.00 27.63           O
ANISOU 1323  O   HOH A 281     4890   2364   3243    487    392     12       O
HETATM 1324  O   HOH A 282      -6.947   2.794  23.709  1.00 29.41           O
ANISOU 1324  O   HOH A 282     1533   4543   5096   -415   -224    -43       O
HETATM 1325  O   HOH A 283      19.572  14.722  18.296  1.00 26.89           O
ANISOU 1325  O   HOH A 283     2264   3547   4404   -555    -94    895       O
HETATM 1326  O   HOH A 284       2.385  -5.465  20.068  1.00 38.13           O
ANISOU 1326  O   HOH A 284     2844   5142   6500   1196    591  -1492       O
HETATM 1327  O   HOH A 285      11.051  22.305  26.493  1.00 32.39           O
ANISOU 1327  O   HOH A 285     5585   3653   3067   1097    -13   -343       O
HETATM 1328  O   HOH A 286      22.709   4.103  20.748  1.00 19.35           O
ANISOU 1328  O   HOH A 286     2251   2056   3046    406    245    146       O
HETATM 1329  O   HOH A 287      10.130  29.192  19.392  1.00 43.28           O
ANISOU 1329  O   HOH A 287     3398   5837   7208   1734  -1323  -3058       O
HETATM 1330  O   HOH A 288       3.500   3.791  35.875  1.00 29.56           O
ANISOU 1330  O   HOH A 288     5460   3167   2603  -1567   -589    356       O
HETATM 1331  O   HOH A 289       7.252  -6.305  15.611  1.00 36.54           O
ANISOU 1331  O   HOH A 289     5671   3308   4904  -1703  -1684   1304       O
HETATM 1332  O   HOH A 290      21.845  11.421   7.434  1.00 47.15           O
ANISOU 1332  O   HOH A 290     3078   5915   8919  -1216  -1353   3616       O
HETATM 1333  O   HOH A 291      -2.340  19.475  14.857  1.00 35.98           O
ANISOU 1333  O   HOH A 291     2890   3316   7462    360   -358  -1080       O
HETATM 1334  O   HOH A 292       6.006  23.304  -3.947  1.00 43.97           O
ANISOU 1334  O   HOH A 292     2944   7306   6454   1221   -199   -394       O
HETATM 1335  O   HOH A 293      -2.141  12.917  23.551  1.00 43.17           O
ANISOU 1335  O   HOH A 293     1731   4936   9733     42    119    526       O
HETATM 1336  O   HOH A 294      18.268   0.898   1.911  1.00 49.99           O
ANISOU 1336  O   HOH A 294     3646   7771   7577   -495    521  -1264       O
HETATM 1337  O   HOH A 295      -0.492   9.288  29.234  1.00 43.84           O
ANISOU 1337  O   HOH A 295     7756   5142   3757     95   2030    416       O
HETATM 1338  O   HOH A 296      12.657  25.463   5.948  1.00 37.27           O
ANISOU 1338  O   HOH A 296     6578   3516   4067    556   2155   1094       O
HETATM 1339  O   HOH A 297      17.244   8.945  16.373  1.00 31.44           O
ANISOU 1339  O   HOH A 297     4392   3838   3714   1062    -37    191       O
HETATM 1340  O   HOH A 298      10.414  22.448  -3.469  1.00 42.99           O
ANISOU 1340  O   HOH A 298     2817   5915   7600     81    613   -817       O
HETATM 1341  O   HOH A 299       2.996  -2.234  17.857  1.00 30.82           O
ANISOU 1341  O   HOH A 299     3510   4321   3878   1560    355   1072       O
HETATM 1342  O   HOH A 300      10.305  -5.250   9.462  1.00 39.42           O
ANISOU 1342  O   HOH A 300     6666   3278   5032   -177    541   -829       O
HETATM 1343  O   HOH A 301      12.216  24.750 -14.990  1.00 25.56           O
ANISOU 1343  O   HOH A 301     2653   2664   4394   -557   -916    192       O
HETATM 1344  O   HOH A 302      19.933  10.178   2.198  1.00 33.18           O
ANISOU 1344  O   HOH A 302     3438   3291   5877    890    868     73       O
HETATM 1345  O   HOH A 303      20.459   4.489  17.558  1.00 29.77           O
ANISOU 1345  O   HOH A 303     3611   3288   4412     94   1295   1031       O
HETATM 1346  O   HOH A 304      -1.652  14.168  21.908  1.00 32.87           O
ANISOU 1346  O   HOH A 304     3354   5261   3872   -544    207   -849       O
HETATM 1347  O  AHOH A 305      12.170   7.173  33.098  0.50 30.19           O
ANISOU 1347  O  AHOH A 305     1902   5077   4492      4   -247  -1129       O
HETATM 1348  O  BHOH A 305      12.699   5.070  33.173  0.50 37.42           O
ANISOU 1348  O  BHOH A 305     6871   4984   2361  -1092   -599    327       O
HETATM 1349  O   HOH A 306       7.685   3.136  -0.607  1.00 28.81           O
ANISOU 1349  O   HOH A 306     2436   3765   4745   1006    523    768       O
HETATM 1350  O   HOH A 307       7.375  21.643  -1.219  1.00 39.26           O
ANISOU 1350  O   HOH A 307     8023   3752   3142    620    993    575       O
HETATM 1351  O   HOH A 308      16.451  -0.431  28.917  1.00 31.96           O
ANISOU 1351  O   HOH A 308     3397   4479   4266   1941    132     42       O
HETATM 1352  O   HOH A 309      20.955   2.320  21.693  1.00 31.18           O
ANISOU 1352  O   HOH A 309     1319   5994   4533    -96   -188     68       O
HETATM 1353  O   HOH A 310       5.338  -1.814  19.957  1.00 36.64           O
ANISOU 1353  O   HOH A 310     3250   4414   6255  -1466   2021  -1732       O
HETATM 1354  O   HOH A 311       9.224  21.009   0.837  1.00 42.50           O
ANISOU 1354  O   HOH A 311     3938   7536   4674    423    506  -2449       O
HETATM 1355  O   HOH A 312      21.522  17.864   4.726  1.00 45.81           O
ANISOU 1355  O   HOH A 312     5901   3834   7670  -1414   3225  -1209       O
HETATM 1356  O   HOH A 313      19.337  19.680   4.508  1.00 45.05           O
ANISOU 1356  O   HOH A 313     2889   5751   8476    135     79   1320       O
HETATM 1357  O   HOH A 314       6.109  19.165  -2.951  1.00 39.70           O
ANISOU 1357  O   HOH A 314     5579   5562   3942   1206    476    389       O
HETATM 1358  O   HOH A 315       8.596  21.701  26.628  1.00 39.52           O
ANISOU 1358  O   HOH A 315     5942   4612   4462   2214  -1245  -1497       O
HETATM 1359  O   HOH A 316       2.984   8.425  31.083  1.00 29.20           O
ANISOU 1359  O   HOH A 316     3537   3247   4308    559     82   -454       O
HETATM 1360  O   HOH A 317       9.701  29.982   6.580  1.00 49.99           O
ANISOU 1360  O   HOH A 317     8382   5813   4796  -1876  -2911   1912       O
HETATM 1361  O   HOH A 318       3.028  -4.660  22.486  1.00 35.68           O
ANISOU 1361  O   HOH A 318     3947   4865   4744    778    594    482       O
HETATM 1362  O   HOH A 319      18.804   1.742  29.718  1.00 42.44           O
ANISOU 1362  O   HOH A 319     5786   6946   3391    -25   -512    578       O
HETATM 1363  O   HOH A 320      11.386  24.764   4.200  1.00 33.48           O
ANISOU 1363  O   HOH A 320     2125   5797   4798   -852    499   1278       O
HETATM 1364  O   HOH A 321       6.164  -7.477  13.045  1.00 49.50           O
ANISOU 1364  O   HOH A 321     4633   5169   9006  -1575   -569    895       O
HETATM 1365  O   HOH A 322      -2.302  19.466   6.668  1.00 31.91           O
ANISOU 1365  O   HOH A 322     2681   4003   5439   -728  -1021    758       O
HETATM 1366  O   HOH A 323       7.771  30.704   8.343  1.00 34.13           O
ANISOU 1366  O   HOH A 323     2300   2910   7755    501   -813    839       O
HETATM 1367  O   HOH A 324      -2.937   5.904  28.880  1.00 36.85           O
ANISOU 1367  O   HOH A 324     3226   4267   6508   -128   -264   -413       O
HETATM 1368  O   HOH A 325      11.773  -3.115  25.008  1.00 31.28           O
ANISOU 1368  O   HOH A 325     4857   2247   4777     16   1775    372       O
HETATM 1369  O   HOH A 326      11.903  -6.453  23.206  1.00 25.81           O
ANISOU 1369  O   HOH A 326     3353   2597   3854   -127      1   -120       O
HETATM 1370  O   HOH A 327       4.323  -6.962  14.519  1.00 51.28           O
ANISOU 1370  O   HOH A 327     3411   7554   8518   1028  -1535    441       O
HETATM 1371  O   HOH A 328      21.306   9.540  22.582  1.00 37.94           O
ANISOU 1371  O   HOH A 328     4157   4795   5463   -364     -6   -458       O
HETATM 1372  O   HOH A 329       7.948  -6.531  17.801  1.00 37.31           O
ANISOU 1372  O   HOH A 329     4877   3554   5742  -1105  -1409   1534       O
CONECT 1150 1152
CONECT 1151 1153
CONECT 1174 1156 1160 1172
CONECT 1175 1157 1161 1173
CONECT 1154 1152 1158 1164
CONECT 1155 1153 1159 1165
CONECT 1158 1154 1162
CONECT 1159 1155 1163
CONECT 1162 1158 1168
CONECT 1163 1159 1169
CONECT 1164 1154 1166
CONECT 1165 1155 1167
CONECT 1166 1164 1168
CONECT 1167 1165 1169
CONECT 1168 1162 1166 1170
CONECT 1169 1163 1167 1171
CONECT 1170 1168 1172
CONECT 1171 1169 1173
CONECT 1172 1170 1174
CONECT 1173 1171 1175
CONECT 1152 1150 1154
CONECT 1153 1151 1155
CONECT 1156 1174
CONECT 1157 1175
CONECT 1160 1174
CONECT 1161 1175
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.