CNRS Nantes University UFIP UFIP
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***  test1  ***

elNémo ID: 22012513052493747

Job options:

ID        	=	 22012513052493747
JOBID     	=	 test1
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 test1

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  5                                   7    
HELIX    2   2 ASN A   15  GLY A   24  1                                  10    
HELIX    3   3 GLY A   26  ALA A   36  1                                  11    
SHEET    1   A10 THR A  60  ILE A  65  0                                        
SHEET    2   A10 VAL A  48  GLU A  54 -1  N  ILE A  49   O  PHE A  64           
SHEET    3   A10 ASN A  39  ASN A  45 -1  N  ILE A  41   O  LYS A  52           
SHEET    4   A10 GLY A   6  GLU A  14 -1  N  TRP A   8   O  MET A  40           
SHEET    5   A10 VAL A 122  ARG A 130 -1  O  VAL A 127   N  VAL A  11           
SHEET    6   A10 LYS A 112  MET A 119 -1  N  VAL A 115   O  ARG A 126           
SHEET    7   A10 LYS A 100  GLU A 109 -1  N  LYS A 107   O  VAL A 114           
SHEET    8   A10 VAL A  90  TRP A  97 -1  N  TRP A  97   O  LYS A 100           
SHEET    9   A10 LYS A  79  ASP A  87 -1  N  THR A  85   O  VAL A  92           
SHEET   10   A10 PHE A  70  VAL A  73 -1  N  GLU A  72   O  VAL A  80           
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   GLN A  -7      -2.205  31.290  -8.712  1.00 34.04           N  
ANISOU    1  N   GLN A  -7     3881   4512   4540     97   -174    166       N  
ATOM      2  CA  GLN A  -7      -1.046  30.439  -8.342  1.00 32.98           C  
ANISOU    2  CA  GLN A  -7     3811   4338   4380     59   -119     87       C  
ATOM      3  C   GLN A  -7      -0.681  29.459  -9.450  1.00 32.12           C  
ANISOU    3  C   GLN A  -7     3636   4239   4328     44   -167     87       C  
ATOM      4  O   GLN A  -7      -1.387  29.301 -10.450  1.00 33.54           O  
ANISOU    4  O   GLN A  -7     3790   4511   4443   -145   -151    -16       O  
ATOM      5  CB  GLN A  -7      -1.326  29.690  -7.029  1.00 33.75           C  
ANISOU    5  CB  GLN A  -7     3902   4470   4449    133   -144    123       C  
ATOM      6  N   GLN A  -6       0.468  28.828  -9.289  1.00 30.52           N  
ANISOU    6  N   GLN A  -6     3434   3943   4219      3   -246     60       N  
ATOM      7  CA  GLN A  -6       0.931  27.873 -10.270  1.00 28.50           C  
ANISOU    7  CA  GLN A  -6     3108   3656   4063     20   -238    108       C  
ATOM      8  C   GLN A  -6       1.242  26.610  -9.547  1.00 26.54           C  
ANISOU    8  C   GLN A  -6     2784   3491   3809     16   -247     97       C  
ATOM      9  O   GLN A  -6       1.173  26.535  -8.314  1.00 28.28           O  
ANISOU    9  O   GLN A  -6     3162   3586   3994     -4   -455     39       O  
ATOM     10  CB  GLN A  -6       2.168  28.350 -10.970  1.00 29.48           C  
ANISOU   10  CB  GLN A  -6     3301   3688   4211      0   -179    101       C  
ATOM     11  N   MET A  -5       1.522  25.611 -10.358  1.00 24.16           N  
ANISOU   11  N   MET A  -5     2307   3183   3689    -80   -319     84       N  
ATOM     12  CA AMET A  -5       1.883  24.331  -9.789  0.50 22.31           C  
ANISOU   12  CA AMET A  -5     2013   3025   3439      6   -208     58       C  
ATOM     13  CA BMET A  -5       1.922  24.304  -9.934  0.50 23.85           C  
ANISOU   13  CA BMET A  -5     2267   3175   3619      6   -194     66       C  
ATOM     14  C   MET A  -5       3.334  24.356  -9.382  1.00 22.78           C  
ANISOU   14  C   MET A  -5     2039   3058   3556    106   -140     87       C  
ATOM     15  O   MET A  -5       4.257  24.602 -10.170  1.00 25.99           O  
ANISOU   15  O   MET A  -5     2376   3566   3932    -65    -86    234       O  
ATOM     16  CB AMET A  -5       1.597  23.104 -10.664  0.50 21.17           C  
ANISOU   16  CB AMET A  -5     1860   2870   3312     45   -185     91       C  
ATOM     17  CB BMET A  -5       1.917  23.407 -11.176  0.50 24.10           C  
ANISOU   17  CB BMET A  -5     2306   3285   3562     82    -78     73       C  
ATOM     18  CG AMET A  -5       1.572  21.843  -9.779  0.50 17.57           C  
ANISOU   18  CG AMET A  -5     1419   2754   2501    267    -71    -36       C  
ATOM     19  CG BMET A  -5       1.913  21.975 -10.864  0.50 26.34           C  
ANISOU   19  CG BMET A  -5     2991   3297   3718     35    -51    -76       C  
ATOM     20  SD AMET A  -5       1.223  20.356 -10.644  0.50 18.37           S  
ANISOU   20  SD AMET A  -5     1770   2293   2915   -184     32    -63       S  
ATOM     21  SD BMET A  -5       0.227  21.678 -10.392  0.50 28.63           S  
ANISOU   21  SD BMET A  -5     3446   3582   3849     85    182    191       S  
ATOM     22  CE AMET A  -5      -0.506  20.556 -10.635  0.50 11.69           C  
ANISOU   22  CE AMET A  -5      555   1478   2407   -130   -142   -158       C  
ATOM     23  CE BMET A  -5       0.155  19.901 -10.460  0.50 24.92           C  
ANISOU   23  CE BMET A  -5     3211   3246   3009    454      2   -111       C  
ATOM     24  N   GLY A  -4       3.489  24.093  -8.094  1.00 23.65           N  
ANISOU   24  N   GLY A  -4     2078   3216   3690    257   -234    -26       N  
ATOM     25  CA  GLY A  -4       4.789  24.137  -7.495  1.00 23.88           C  
ANISOU   25  CA  GLY A  -4     2088   3240   3744    277   -308     17       C  
ATOM     26  C   GLY A  -4       5.603  22.926  -7.872  1.00 22.97           C  
ANISOU   26  C   GLY A  -4     1776   3175   3775    228   -391     32       C  
ATOM     27  O   GLY A  -4       5.097  21.898  -8.367  1.00 24.81           O  
ANISOU   27  O   GLY A  -4     1994   3210   4220    208   -245   -180       O  
ATOM     28  N   ARG A  -3       6.889  23.039  -7.612  1.00 23.30           N  
ANISOU   28  N   ARG A  -3     1830   3208   3812    156   -377    171       N  
ATOM     29  CA  ARG A  -3       7.837  21.973  -7.855  1.00 22.56           C  
ANISOU   29  CA  ARG A  -3     1896   3063   3611    269   -391    406       C  
ATOM     30  C   ARG A  -3       7.786  20.944  -6.712  1.00 21.81           C  
ANISOU   30  C   ARG A  -3     1883   2941   3461    215   -253    357       C  
ATOM     31  O   ARG A  -3       7.221  21.169  -5.627  1.00 25.02           O  
ANISOU   31  O   ARG A  -3     2441   3241   3822    326   -325    468       O  
ATOM     32  CB  ARG A  -3       9.265  22.506  -8.049  1.00 25.20           C  
ANISOU   32  CB  ARG A  -3     2060   3504   4008     77   -307    305       C  
ATOM     33  N   GLY A  -2       8.373  19.799  -7.005  1.00 19.62           N  
ANISOU   33  N   GLY A  -2     1312   2808   3332    119   -313    360       N  
ATOM     34  CA  GLY A  -2       8.599  18.765  -6.012  1.00 19.56           C  
ANISOU   34  CA  GLY A  -2     1338   2765   3327      3   -238    367       C  
ATOM     35  C   GLY A  -2       9.737  19.084  -5.100  1.00 19.23           C  
ANISOU   35  C   GLY A  -2     1367   2759   3178   -148   -268    448       C  
ATOM     36  O   GLY A  -2      10.470  20.064  -5.257  1.00 21.93           O  
ANISOU   36  O   GLY A  -2     2102   2857   3373    -62   -422    675       O  
ATOM     37  N   SER A  -1       9.928  18.184  -4.151  1.00 17.09           N  
ANISOU   37  N   SER A  -1      589   2817   3086   -183    -60    399       N  
ATOM     38  CA  SER A  -1      11.033  18.269  -3.312  1.00 17.15           C  
ANISOU   38  CA  SER A  -1      817   2506   3193   -104    -14    331       C  
ATOM     39  C   SER A  -1      11.525  16.891  -2.883  1.00 16.50           C  
ANISOU   39  C   SER A  -1     1046   2406   2816   -191     34    439       C  
ATOM     40  O   SER A  -1      10.851  15.873  -3.041  1.00 17.47           O  
ANISOU   40  O   SER A  -1     1285   2469   2882   -454   -127    652       O  
ATOM     41  CB  SER A  -1      10.738  19.108  -2.081  1.00 19.67           C  
ANISOU   41  CB  SER A  -1     1409   2770   3294    -25     59    345       C  
ATOM     42  OG  SER A  -1      10.000  18.365  -1.170  1.00 27.01           O  
ANISOU   42  OG  SER A  -1     2686   3636   3938   -268    559    -10       O  
ATOM     43  N   MET A   0      12.704  16.858  -2.320  1.00 17.24           N  
ANISOU   43  N   MET A   0     1276   2414   2858   -119      8    337       N  
ATOM     44  CA AMET A   0      13.225  15.568  -1.916  0.50 16.38           C  
ANISOU   44  CA AMET A   0     1080   2376   2767   -265     24    321       C  
ATOM     45  CA BMET A   0      13.275  15.607  -1.828  0.50 16.83           C  
ANISOU   45  CA BMET A   0     1158   2425   2811   -189     24    312       C  
ATOM     46  C   MET A   0      12.293  14.915  -0.880  1.00 16.76           C  
ANISOU   46  C   MET A   0     1029   2460   2876   -149     31    287       C  
ATOM     47  O   MET A   0      12.187  13.721  -0.859  1.00 17.16           O  
ANISOU   47  O   MET A   0     1015   2472   3032   -211    174    481       O  
ATOM     48  CB AMET A   0      14.672  15.677  -1.465  0.50 16.14           C  
ANISOU   48  CB AMET A   0      879   2523   2728   -267    -62    209       C  
ATOM     49  CB BMET A   0      14.610  15.874  -1.133  0.50 17.09           C  
ANISOU   49  CB BMET A   0     1006   2619   2868   -144      4    183       C  
ATOM     50  CG AMET A   0      15.218  14.379  -0.921  0.50 17.00           C  
ANISOU   50  CG AMET A   0      891   2610   2958   -254   -184    158       C  
ATOM     51  CG BMET A   0      15.509  14.648  -1.105  0.50 19.46           C  
ANISOU   51  CG BMET A   0     1617   2729   3047    189    -96    231       C  
ATOM     52  SD AMET A   0      14.934  14.269   0.838  0.50 19.20           S  
ANISOU   52  SD AMET A   0     1406   2792   3097    384   -394    268       S  
ATOM     53  SD BMET A   0      16.488  14.404   0.395  0.50 24.27           S  
ANISOU   53  SD BMET A   0     2604   3082   3534    640   -745    -76       S  
ATOM     54  CE AMET A   0      15.023  12.512   1.083  0.50 20.43           C  
ANISOU   54  CE AMET A   0     1953   2616   3191   -129   -479    124       C  
ATOM     55  CE BMET A   0      15.464  15.229   1.565  0.50 25.01           C  
ANISOU   55  CE BMET A   0     2384   3237   3880    294   -542   -188       C  
ATOM     56  N   CYS A   1      11.647  15.708  -0.038  1.00 17.25           N  
ANISOU   56  N   CYS A   1     1326   2443   2783   -101     31    316       N  
ATOM     57  CA ACYS A   1      10.692  15.212   0.988  0.50 17.46           C  
ANISOU   57  CA ACYS A   1     1266   2612   2756    -52    110    287       C  
ATOM     58  CA BCYS A   1      10.717  15.164   0.998  0.50 18.78           C  
ANISOU   58  CA BCYS A   1     1536   2663   2937    -57    116    333       C  
ATOM     59  C   CYS A   1       9.466  14.468   0.432  1.00 16.13           C  
ANISOU   59  C   CYS A   1      930   2468   2729     85    220    385       C  
ATOM     60  O   CYS A   1       8.758  13.741   1.150  1.00 16.46           O  
ANISOU   60  O   CYS A   1     1411   2110   2731    130    350    538       O  
ATOM     61  CB ACYS A   1      10.282  16.350   1.910  0.50 18.26           C  
ANISOU   61  CB ACYS A   1     1316   2732   2888     45    -10    243       C  
ATOM     62  CB BCYS A   1      10.330  16.218   2.033  0.50 20.41           C  
ANISOU   62  CB BCYS A   1     1691   2922   3141    -39     66    234       C  
ATOM     63  SG ACYS A   1      11.612  16.709   3.059  0.50 22.19           S  
ANISOU   63  SG ACYS A   1     1377   3807   3247   -303     18   -325       S  
ATOM     64  SG BCYS A   1       9.432  17.594   1.381  0.50 30.72           S  
ANISOU   64  SG BCYS A   1     3348   3824   4501    202     48    119       S  
ATOM     65  N   ASP A   2       9.277  14.590  -0.871  1.00 16.33           N  
ANISOU   65  N   ASP A   2      857   2547   2799   -409    -78    497       N  
ATOM     66  CA  ASP A   2       8.335  13.784  -1.539  1.00 17.32           C  
ANISOU   66  CA  ASP A   2      978   2742   2861   -553    -30    549       C  
ATOM     67  C   ASP A   2       8.524  12.279  -1.360  1.00 16.04           C  
ANISOU   67  C   ASP A   2      628   2810   2657   -498    -79    356       C  
ATOM     68  O   ASP A   2       7.528  11.605  -1.414  1.00 17.46           O  
ANISOU   68  O   ASP A   2     1074   2794   2766   -634   -128    370       O  
ATOM     69  CB  ASP A   2       8.175  14.146  -3.016  1.00 18.52           C  
ANISOU   69  CB  ASP A   2     1110   2901   3023   -752   -174    440       C  
ATOM     70  CG  ASP A   2       7.552  15.532  -3.229  1.00 22.90           C  
ANISOU   70  CG  ASP A   2     1997   3506   3197   -181   -258    687       C  
ATOM     71  OD1 ASP A   2       6.857  16.103  -2.358  1.00 27.50           O  
ANISOU   71  OD1 ASP A   2     2380   4130   3939    171   -171   1145       O  
ATOM     72  OD2 ASP A   2       7.752  16.059  -4.313  1.00 26.59           O  
ANISOU   72  OD2 ASP A   2     1334   4662   4104   -718   -197    829       O  
ATOM     73  N   ALA A   3       9.736  11.827  -1.079  1.00 16.33           N  
ANISOU   73  N   ALA A   3      965   2678   2559   -381    126    349       N  
ATOM     74  CA  ALA A   3       9.958  10.403  -0.813  1.00 17.33           C  
ANISOU   74  CA  ALA A   3     1453   2586   2546    -52    194    219       C  
ATOM     75  C   ALA A   3       9.212   9.916   0.418  1.00 15.04           C  
ANISOU   75  C   ALA A   3     1177   2134   2402   -174    113    187       C  
ATOM     76  O   ALA A   3       8.994   8.724   0.552  1.00 16.05           O  
ANISOU   76  O   ALA A   3     1500   2037   2558     33    368    -25       O  
ATOM     77  CB  ALA A   3      11.449  10.135  -0.639  1.00 19.24           C  
ANISOU   77  CB  ALA A   3     1404   2916   2991   -181    389    459       C  
ATOM     78  N   PHE A   4       8.863  10.823   1.340  1.00 13.25           N  
ANISOU   78  N   PHE A   4      781   1879   2371   -130    131     74       N  
ATOM     79  CA  PHE A   4       8.179  10.432   2.576  1.00 12.20           C  
ANISOU   79  CA  PHE A   4      638   1722   2273    -30    174     47       C  
ATOM     80  C   PHE A   4       6.666  10.495   2.399  1.00 11.59           C  
ANISOU   80  C   PHE A   4      847   1378   2178    -62    135    -11       C  
ATOM     81  O   PHE A   4       5.929   9.924   3.195  1.00 12.46           O  
ANISOU   81  O   PHE A   4      785   1585   2364    -92     45    201       O  
ATOM     82  CB  PHE A   4       8.568  11.409   3.703  1.00 11.77           C  
ANISOU   82  CB  PHE A   4      355   1674   2443   -138     94    155       C  
ATOM     83  CG  PHE A   4       9.947  11.304   4.123  1.00 12.75           C  
ANISOU   83  CG  PHE A   4      400   2073   2371    -92     54   -100       C  
ATOM     84  CD1 PHE A   4      10.354  10.229   4.965  1.00 14.34           C  
ANISOU   84  CD1 PHE A   4      261   2455   2731   -129     35    151       C  
ATOM     85  CD2 PHE A   4      10.914  12.208   3.765  1.00 14.41           C  
ANISOU   85  CD2 PHE A   4      346   2394   2734   -131    -29   -175       C  
ATOM     86  CE1 PHE A   4      11.588  10.101   5.328  1.00 15.34           C  
ANISOU   86  CE1 PHE A   4      781   2551   2494    -96    272     22       C  
ATOM     87  CE2 PHE A   4      12.151  12.056   4.111  1.00 15.52           C  
ANISOU   87  CE2 PHE A   4      369   2684   2841   -484    214     56       C  
ATOM     88  CZ  PHE A   4      12.530  10.976   4.942  1.00 15.54           C  
ANISOU   88  CZ  PHE A   4      709   2538   2658     89    107   -164       C  
ATOM     89  N   VAL A   5       6.142  11.178   1.370  1.00 11.36           N  
ANISOU   89  N   VAL A   5      662   1482   2172   -101     38     77       N  
ATOM     90  CA  VAL A   5       4.734  11.440   1.264  1.00 11.94           C  
ANISOU   90  CA  VAL A   5      672   1528   2335    -53     46    -31       C  
ATOM     91  C   VAL A   5       3.971  10.181   0.963  1.00 13.26           C  
ANISOU   91  C   VAL A   5      942   1677   2420   -120     70   -155       C  
ATOM     92  O   VAL A   5       4.364   9.394   0.089  1.00 15.74           O  
ANISOU   92  O   VAL A   5     1267   1910   2804   -352    411   -404       O  
ATOM     93  CB  VAL A   5       4.473  12.505   0.168  1.00 12.96           C  
ANISOU   93  CB  VAL A   5      699   1490   2733     34     24    151       C  
ATOM     94  CG1 VAL A   5       3.001  12.587  -0.211  1.00 15.23           C  
ANISOU   94  CG1 VAL A   5     1251   1814   2721    129    132    198       C  
ATOM     95  CG2 VAL A   5       5.023  13.878   0.740  1.00 14.03           C  
ANISOU   95  CG2 VAL A   5      924   1602   2805     20    -57    -38       C  
ATOM     96  N   GLY A   6       2.856   9.996   1.625  1.00 12.36           N  
ANISOU   96  N   GLY A   6      884   1555   2254   -127    123   -180       N  
ATOM     97  CA  GLY A   6       1.993   8.906   1.362  1.00 13.60           C  
ANISOU   97  CA  GLY A   6     1063   1813   2291   -104    -92   -118       C  
ATOM     98  C   GLY A   6       1.363   8.391   2.622  1.00 12.34           C  
ANISOU   98  C   GLY A   6      845   1711   2132   -189    -35    -73       C  
ATOM     99  O   GLY A   6       1.263   9.091   3.593  1.00 12.71           O  
ANISOU   99  O   GLY A   6      749   1666   2413   -204    174    -64       O  
ATOM    100  N   THR A   7       0.879   7.161   2.533  1.00 12.24           N  
ANISOU  100  N   THR A   7      684   1619   2347   -102    -16    -72       N  
ATOM    101  CA  THR A   7       0.137   6.488   3.574  1.00 12.81           C  
ANISOU  101  CA  THR A   7      835   1627   2402     12     67     23       C  
ATOM    102  C   THR A   7       0.932   5.224   3.959  1.00 11.96           C  
ANISOU  102  C   THR A   7      795   1386   2361    -26    -37     66       C  
ATOM    103  O   THR A   7       1.180   4.380   3.107  1.00 13.46           O  
ANISOU  103  O   THR A   7      851   1770   2494     60   -233   -133       O  
ATOM    104  CB  THR A   7      -1.291   6.161   3.127  1.00 13.65           C  
ANISOU  104  CB  THR A   7      573   1643   2968    -52    -16    222       C  
ATOM    105  OG1 THR A   7      -1.861   7.276   2.447  1.00 17.08           O  
ANISOU  105  OG1 THR A   7     1101   2011   3378     77   -169    170       O  
ATOM    106  CG2 THR A   7      -2.127   5.701   4.300  1.00 18.06           C  
ANISOU  106  CG2 THR A   7     1303   2238   3321   -172    262    178       C  
ATOM    107  N   TRP A   8       1.232   5.132   5.238  1.00 11.53           N  
ANISOU  107  N   TRP A   8      544   1536   2299    -54    168     83       N  
ATOM    108  CA  TRP A   8       2.152   4.130   5.756  1.00 12.28           C  
ANISOU  108  CA  TRP A   8      858   1458   2348     36     25    127       C  
ATOM    109  C   TRP A   8       1.499   3.373   6.899  1.00 12.35           C  
ANISOU  109  C   TRP A   8      772   1525   2395      0    111     80       C  
ATOM    110  O   TRP A   8       0.671   3.940   7.596  1.00 16.20           O  
ANISOU  110  O   TRP A   8     1870   1597   2684     18    665    271       O  
ATOM    111  CB  TRP A   8       3.393   4.819   6.299  1.00 12.14           C  
ANISOU  111  CB  TRP A   8      914   1448   2247    -94      5    226       C  
ATOM    112  CG  TRP A   8       4.142   5.635   5.266  1.00 12.11           C  
ANISOU  112  CG  TRP A   8     1004   1339   2258    -18     53     97       C  
ATOM    113  CD1 TRP A   8       4.013   6.964   4.999  1.00 12.14           C  
ANISOU  113  CD1 TRP A   8      656   1495   2461     18     -3   -114       C  
ATOM    114  CD2 TRP A   8       5.132   5.148   4.370  1.00 10.99           C  
ANISOU  114  CD2 TRP A   8      503   1427   2243     26    -44    157       C  
ATOM    115  NE1 TRP A   8       4.873   7.340   4.012  1.00 11.89           N  
ANISOU  115  NE1 TRP A   8      637   1440   2441   -234    178     59       N  
ATOM    116  CE2 TRP A   8       5.576   6.234   3.604  1.00 11.81           C  
ANISOU  116  CE2 TRP A   8      546   1707   2233   -117    106     18       C  
ATOM    117  CE3 TRP A   8       5.690   3.899   4.115  1.00 12.66           C  
ANISOU  117  CE3 TRP A   8      920   1615   2276    -65   -126     34       C  
ATOM    118  CZ2 TRP A   8       6.559   6.085   2.652  1.00 12.97           C  
ANISOU  118  CZ2 TRP A   8      988   1606   2331   -158     87    198       C  
ATOM    119  CZ3 TRP A   8       6.658   3.759   3.154  1.00 13.40           C  
ANISOU  119  CZ3 TRP A   8      877   1715   2498    218    -71    -12       C  
ATOM    120  CH2 TRP A   8       7.061   4.829   2.426  1.00 12.98           C  
ANISOU  120  CH2 TRP A   8      903   1831   2196     -4    142     -7       C  
ATOM    121  N   LYS A   9       1.800   2.110   7.032  1.00 11.95           N  
ANISOU  121  N   LYS A   9      735   1532   2272   -100    -32    264       N  
ATOM    122  CA  LYS A   9       1.274   1.271   8.130  1.00 12.54           C  
ANISOU  122  CA  LYS A   9      603   1746   2415   -248    -18    284       C  
ATOM    123  C   LYS A   9       2.399   0.596   8.890  1.00 11.89           C  
ANISOU  123  C   LYS A   9      662   1597   2257   -175    108     89       C  
ATOM    124  O   LYS A   9       3.316   0.094   8.303  1.00 12.57           O  
ANISOU  124  O   LYS A   9     1021   1578   2173   -118     36    127       O  
ATOM    125  CB  LYS A   9       0.347   0.224   7.549  1.00 14.50           C  
ANISOU  125  CB  LYS A   9      659   2192   2656   -352     93    479       C  
ATOM    126  CG  LYS A   9       0.860  -0.762   6.648  1.00 22.01           C  
ANISOU  126  CG  LYS A   9     2274   2808   3282   -395    -55    181       C  
ATOM    127  CD  LYS A   9      -0.196  -1.731   6.232  1.00 27.33           C  
ANISOU  127  CD  LYS A   9     3361   3167   3855   -595   -112     69       C  
ATOM    128  CE  LYS A   9       0.443  -2.768   5.363  1.00 30.07           C  
ANISOU  128  CE  LYS A   9     3743   3433   4249   -472    -43   -123       C  
ATOM    129  NZ  LYS A   9       0.463  -2.358   3.942  1.00 33.85           N  
ANISOU  129  NZ  LYS A   9     4189   4020   4651   -200    211    269       N  
ATOM    130  N   LEU A  10       2.331   0.646  10.222  1.00 12.20           N  
ANISOU  130  N   LEU A  10      359   1858   2419    -39     37    190       N  
ATOM    131  CA  LEU A  10       3.364   0.014  11.028  1.00 12.57           C  
ANISOU  131  CA  LEU A  10      304   1936   2535   -290     43     46       C  
ATOM    132  C   LEU A  10       3.376  -1.537  10.862  1.00 12.29           C  
ANISOU  132  C   LEU A  10      542   1790   2337   -446    -16    303       C  
ATOM    133  O   LEU A  10       2.354  -2.131  11.027  1.00 15.60           O  
ANISOU  133  O   LEU A  10     1000   2006   2919   -544   -155    423       O  
ATOM    134  CB  LEU A  10       3.181   0.350  12.512  1.00 13.80           C  
ANISOU  134  CB  LEU A  10      478   2136   2625   -208     76    159       C  
ATOM    135  CG  LEU A  10       4.261  -0.169  13.437  1.00 13.75           C  
ANISOU  135  CG  LEU A  10      358   2301   2564    -41    -50     89       C  
ATOM    136  CD1 LEU A  10       5.568   0.486  13.196  1.00 14.90           C  
ANISOU  136  CD1 LEU A  10      698   2314   2648    -94   -129    121       C  
ATOM    137  CD2 LEU A  10       3.918   0.015  14.901  1.00 19.86           C  
ANISOU  137  CD2 LEU A  10     1246   3956   2344    179    -31     10       C  
ATOM    138  N   VAL A  11       4.518  -2.106  10.523  1.00 13.46           N  
ANISOU  138  N   VAL A  11     1033   1597   2484   -249   -189    273       N  
ATOM    139  CA  VAL A  11       4.621  -3.566  10.386  1.00 16.14           C  
ANISOU  139  CA  VAL A  11     1549   1733   2850   -309   -489    156       C  
ATOM    140  C   VAL A  11       5.526  -4.247  11.352  1.00 16.15           C  
ANISOU  140  C   VAL A  11     1497   1699   2940   -320   -508    368       C  
ATOM    141  O   VAL A  11       5.426  -5.455  11.519  1.00 19.83           O  
ANISOU  141  O   VAL A  11     2362   1773   3398   -326   -904    463       O  
ATOM    142  CB  VAL A  11       4.969  -3.968   8.965  1.00 17.69           C  
ANISOU  142  CB  VAL A  11     1819   1726   3175    -23   -483     16       C  
ATOM    143  CG1 VAL A  11       3.865  -3.535   8.032  1.00 19.29           C  
ANISOU  143  CG1 VAL A  11     1805   2239   3282     47   -449     16       C  
ATOM    144  CG2 VAL A  11       6.387  -3.508   8.526  1.00 19.70           C  
ANISOU  144  CG2 VAL A  11     2225   2136   3122   -129   -387   -178       C  
ATOM    145  N   SER A  12       6.469  -3.527  11.961  1.00 15.19           N  
ANISOU  145  N   SER A  12     1433   1576   2762   -171   -475    301       N  
ATOM    146  CA  SER A  12       7.307  -4.116  12.976  1.00 16.58           C  
ANISOU  146  CA  SER A  12     1726   1739   2831     35   -391    284       C  
ATOM    147  C   SER A  12       7.792  -3.085  13.912  1.00 15.00           C  
ANISOU  147  C   SER A  12     1195   1827   2675   -423   -471    334       C  
ATOM    148  O   SER A  12       7.943  -1.901  13.571  1.00 14.86           O  
ANISOU  148  O   SER A  12     1280   1703   2664   -328   -260    376       O  
ATOM    149  CB  SER A  12       8.426  -4.878  12.332  1.00 18.82           C  
ANISOU  149  CB  SER A  12     1883   2189   3076     43   -452    187       C  
ATOM    150  OG  SER A  12       9.405  -4.069  11.761  1.00 21.52           O  
ANISOU  150  OG  SER A  12     1974   2936   3264     64   -266    373       O  
ATOM    151  N   SER A  13       8.070  -3.539  15.122  1.00 16.05           N  
ANISOU  151  N   SER A  13     1694   1662   2740   -612   -416    380       N  
ATOM    152  CA  SER A  13       8.626  -2.653  16.159  1.00 16.13           C  
ANISOU  152  CA  SER A  13     1669   1849   2611   -485   -495    515       C  
ATOM    153  C   SER A  13       9.591  -3.483  17.005  1.00 16.02           C  
ANISOU  153  C   SER A  13     1518   1927   2639   -447   -465    477       C  
ATOM    154  O   SER A  13       9.289  -4.654  17.325  1.00 19.47           O  
ANISOU  154  O   SER A  13     2170   2068   3156   -684   -753    674       O  
ATOM    155  CB  SER A  13       7.427  -2.216  17.023  1.00 17.62           C  
ANISOU  155  CB  SER A  13     1715   2164   2814   -465   -571    363       C  
ATOM    156  OG  SER A  13       7.730  -1.309  18.062  1.00 20.15           O  
ANISOU  156  OG  SER A  13     2248   2455   2952   -678   -855    369       O  
ATOM    157  N   GLU A  14      10.705  -2.898  17.337  1.00 14.40           N  
ANISOU  157  N   GLU A  14     1481   1543   2445   -233   -326    260       N  
ATOM    158  CA  GLU A  14      11.666  -3.494  18.238  1.00 14.66           C  
ANISOU  158  CA  GLU A  14     1548   1511   2509     94   -313     50       C  
ATOM    159  C   GLU A  14      12.047  -2.519  19.346  1.00 12.41           C  
ANISOU  159  C   GLU A  14      962   1528   2222    117   -254    152       C  
ATOM    160  O   GLU A  14      12.314  -1.349  19.068  1.00 12.52           O  
ANISOU  160  O   GLU A  14     1072   1363   2320     65    -56     27       O  
ATOM    161  CB  GLU A  14      12.931  -3.844  17.465  1.00 17.09           C  
ANISOU  161  CB  GLU A  14     1962   1926   2603    217   -378     45       C  
ATOM    162  CG  GLU A  14      12.755  -5.026  16.503  1.00 23.14           C  
ANISOU  162  CG  GLU A  14     3025   2401   3366    178   -282   -266       C  
ATOM    163  CD  GLU A  14      12.709  -6.405  17.176  1.00 26.42           C  
ANISOU  163  CD  GLU A  14     3884   2433   3721    -90   -379   -408       C  
ATOM    164  OE1 GLU A  14      12.945  -6.551  18.392  1.00 28.83           O  
ANISOU  164  OE1 GLU A  14     4010   2636   4305    103   -750   -328       O  
ATOM    165  OE2 GLU A  14      12.367  -7.390  16.493  1.00 30.74           O  
ANISOU  165  OE2 GLU A  14     4283   3029   4367    -78    -54   -908       O  
ATOM    166  N   ASN A  15      12.027  -3.003  20.559  1.00 12.06           N  
ANISOU  166  N   ASN A  15      862   1453   2266     71    -96     81       N  
ATOM    167  CA AASN A  15      12.534  -2.279  21.745  0.50 11.13           C  
ANISOU  167  CA AASN A  15      489   1470   2268    144   -143    172       C  
ATOM    168  CA BASN A  15      12.516  -2.267  21.735  0.50 12.36           C  
ANISOU  168  CA BASN A  15      719   1613   2362    114    -76    133       C  
ATOM    169  C   ASN A  15      11.714  -1.041  22.085  1.00 11.19           C  
ANISOU  169  C   ASN A  15      300   1609   2342    245    116    202       C  
ATOM    170  O   ASN A  15      12.166  -0.183  22.832  1.00 12.26           O  
ANISOU  170  O   ASN A  15      639   1556   2463     55   -113     57       O  
ATOM    171  CB AASN A  15      14.003  -1.940  21.607  0.50 11.01           C  
ANISOU  171  CB AASN A  15      497   1411   2274    292   -201    108       C  
ATOM    172  CB BASN A  15      13.977  -1.937  21.591  0.50 13.40           C  
ANISOU  172  CB BASN A  15      925   1733   2432    124   -111     62       C  
ATOM    173  CG AASN A  15      14.745  -1.950  22.930  0.50 11.53           C  
ANISOU  173  CG AASN A  15      763   1403   2215    168   -272    265       C  
ATOM    174  CG BASN A  15      14.790  -3.154  21.349  0.50 16.50           C  
ANISOU  174  CG BASN A  15      848   2497   2921    173     97    -31       C  
ATOM    175  OD1AASN A  15      14.563  -2.847  23.731  0.50 11.87           O  
ANISOU  175  OD1AASN A  15     1022   1465   2022    -29   -332    253       O  
ATOM    176  OD1BASN A  15      14.953  -3.941  22.256  0.50 21.20           O  
ANISOU  176  OD1BASN A  15     2466   2230   3359    166   -104   -190       O  
ATOM    177  ND2AASN A  15      15.566  -0.928  23.173  0.50 10.51           N  
ANISOU  177  ND2AASN A  15      266   1422   2304    116    -21    285       N  
ATOM    178  ND2BASN A  15      15.246  -3.368  20.126  0.50 22.55           N  
ANISOU  178  ND2BASN A  15     2387   2799   3381     79    364   -323       N  
ATOM    179  N   PHE A  16      10.493  -0.969  21.642  1.00 11.60           N  
ANISOU  179  N   PHE A  16      388   1409   2610    134    141     44       N  
ATOM    180  CA  PHE A  16       9.686   0.200  21.892  1.00 12.25           C  
ANISOU  180  CA  PHE A  16      567   1657   2430     18   -135     33       C  
ATOM    181  C   PHE A  16       9.307   0.347  23.354  1.00 12.83           C  
ANISOU  181  C   PHE A  16      302   1868   2704   -191    -46     66       C  
ATOM    182  O   PHE A  16       9.205   1.480  23.871  1.00 12.38           O  
ANISOU  182  O   PHE A  16      823   1534   2344    -45     29     -1       O  
ATOM    183  CB  PHE A  16       8.474   0.223  20.964  1.00 13.19           C  
ANISOU  183  CB  PHE A  16      964   1544   2502    171     95    100       C  
ATOM    184  CG  PHE A  16       7.690   1.551  20.930  1.00 13.44           C  
ANISOU  184  CG  PHE A  16      988   2113   2004    241    -97    -16       C  
ATOM    185  CD1 PHE A  16       8.320   2.711  20.573  1.00 14.25           C  
ANISOU  185  CD1 PHE A  16      983   1859   2571    463     51    137       C  
ATOM    186  CD2 PHE A  16       6.350   1.599  21.179  1.00 14.77           C  
ANISOU  186  CD2 PHE A  16      862   2267   2483    361   -182    -93       C  
ATOM    187  CE1 PHE A  16       7.646   3.920  20.451  1.00 17.01           C  
ANISOU  187  CE1 PHE A  16     1952   2081   2430    477   -412    -10       C  
ATOM    188  CE2 PHE A  16       5.645   2.838  21.073  1.00 16.11           C  
ANISOU  188  CE2 PHE A  16      759   2689   2671    625   -454   -251       C  
ATOM    189  CZ  PHE A  16       6.299   3.965  20.703  1.00 17.15           C  
ANISOU  189  CZ  PHE A  16     2007   1924   2584    620   -503   -127       C  
ATOM    190  N   ASP A  17       9.040  -0.758  24.040  1.00 13.09           N  
ANISOU  190  N   ASP A  17      914   1533   2525     39     93    163       N  
ATOM    191  CA  ASP A  17       8.763  -0.678  25.480  1.00 13.83           C  
ANISOU  191  CA  ASP A  17      810   1755   2688   -132    204    321       C  
ATOM    192  C   ASP A  17       9.922  -0.077  26.237  1.00 12.57           C  
ANISOU  192  C   ASP A  17      450   1738   2587   -276    -86    337       C  
ATOM    193  O   ASP A  17       9.705   0.795  27.080  1.00 13.98           O  
ANISOU  193  O   ASP A  17     1093   1816   2401   -111    154    235       O  
ATOM    194  CB  ASP A  17       8.320  -2.048  26.047  1.00 15.71           C  
ANISOU  194  CB  ASP A  17     1351   1814   2801   -210    107    216       C  
ATOM    195  CG  ASP A  17       7.803  -1.925  27.442  1.00 19.02           C  
ANISOU  195  CG  ASP A  17     2019   2213   2993   -222    214    617       C  
ATOM    196  OD1 ASP A  17       8.486  -2.473  28.311  1.00 24.41           O  
ANISOU  196  OD1 ASP A  17     2670   3480   3121    119   -263    411       O  
ATOM    197  OD2 ASP A  17       6.760  -1.314  27.642  1.00 20.83           O  
ANISOU  197  OD2 ASP A  17     2720   2456   2735    229    246    319       O  
ATOM    198  N   ASP A  18      11.135  -0.501  25.957  1.00 12.77           N  
ANISOU  198  N   ASP A  18      297   1728   2824     29    125    478       N  
ATOM    199  CA  ASP A  18      12.290   0.018  26.589  1.00 13.64           C  
ANISOU  199  CA  ASP A  18      338   2113   2731   -223     10    465       C  
ATOM    200  C   ASP A  18      12.506   1.506  26.272  1.00 12.89           C  
ANISOU  200  C   ASP A  18      586   1751   2559    -75    -75    193       C  
ATOM    201  O   ASP A  18      12.903   2.264  27.151  1.00 13.40           O  
ANISOU  201  O   ASP A  18      715   1915   2459    -29    -48    193       O  
ATOM    202  CB  ASP A  18      13.562  -0.742  26.272  1.00 15.53           C  
ANISOU  202  CB  ASP A  18      275   2312   3313   -206   -109    386       C  
ATOM    203  CG  ASP A  18      13.793  -1.918  27.273  1.00 24.43           C  
ANISOU  203  CG  ASP A  18     1857   3616   3807     22     99    748       C  
ATOM    204  OD1 ASP A  18      14.904  -2.021  27.837  1.00 32.80           O  
ANISOU  204  OD1 ASP A  18     3494   4345   4622    523   -165   1109       O  
ATOM    205  OD2 ASP A  18      12.879  -2.692  27.444  1.00 30.24           O  
ANISOU  205  OD2 ASP A  18     3236   3602   4651    247      8   1654       O  
ATOM    206  N   TYR A  19      12.275   1.902  25.031  1.00 12.01           N  
ANISOU  206  N   TYR A  19      630   1549   2383      3     95     16       N  
ATOM    207  CA  TYR A  19      12.282   3.326  24.683  1.00 11.60           C  
ANISOU  207  CA  TYR A  19      594   1471   2340     29    -22    144       C  
ATOM    208  C   TYR A  19      11.323   4.136  25.496  1.00 11.08           C  
ANISOU  208  C   TYR A  19      504   1566   2139     75    -36    118       C  
ATOM    209  O   TYR A  19      11.658   5.160  26.059  1.00 11.70           O  
ANISOU  209  O   TYR A  19      586   1658   2200     37     58     32       O  
ATOM    210  CB  TYR A  19      12.073   3.447  23.167  1.00 11.91           C  
ANISOU  210  CB  TYR A  19      610   1634   2278    -75    116     13       C  
ATOM    211  CG  TYR A  19      11.839   4.898  22.754  1.00 10.99           C  
ANISOU  211  CG  TYR A  19      348   1614   2211   -239    325    -23       C  
ATOM    212  CD1 TYR A  19      12.900   5.753  22.668  1.00 11.30           C  
ANISOU  212  CD1 TYR A  19      439   1801   2051    -10     18     16       C  
ATOM    213  CD2 TYR A  19      10.567   5.355  22.503  1.00 12.18           C  
ANISOU  213  CD2 TYR A  19      296   2023   2307   -153    158    -98       C  
ATOM    214  CE1 TYR A  19      12.719   7.120  22.357  1.00 11.45           C  
ANISOU  214  CE1 TYR A  19      671   1655   2022    -10    -27     56       C  
ATOM    215  CE2 TYR A  19      10.420   6.788  22.168  1.00 13.18           C  
ANISOU  215  CE2 TYR A  19      788   1926   2294    114   -109     -3       C  
ATOM    216  CZ  TYR A  19      11.489   7.595  22.117  1.00 11.98           C  
ANISOU  216  CZ  TYR A  19      782   1746   2023   -246    -16    -76       C  
ATOM    217  OH  TYR A  19      11.227   8.906  21.778  1.00 13.35           O  
ANISOU  217  OH  TYR A  19     1313   1512   2246      9    -87     99       O  
ATOM    218  N   MET A  20      10.088   3.694  25.542  1.00 11.65           N  
ANISOU  218  N   MET A  20      774   1554   2096      8    -24    177       N  
ATOM    219  CA  MET A  20       9.054   4.403  26.276  1.00 12.35           C  
ANISOU  219  CA  MET A  20      592   1816   2283    -42    164    153       C  
ATOM    220  C   MET A  20       9.436   4.463  27.773  1.00 12.08           C  
ANISOU  220  C   MET A  20      521   1898   2168    -84    184    178       C  
ATOM    221  O   MET A  20       9.204   5.494  28.413  1.00 13.19           O  
ANISOU  221  O   MET A  20     1009   1802   2199     40     63    -37       O  
ATOM    222  CB  MET A  20       7.693   3.743  26.105  1.00 12.61           C  
ANISOU  222  CB  MET A  20      814   1851   2124     37     93    199       C  
ATOM    223  CG  MET A  20       7.011   4.004  24.725  1.00 13.32           C  
ANISOU  223  CG  MET A  20     1037   1775   2247    199    182     72       C  
ATOM    224  SD  MET A  20       5.354   3.522  24.665  1.00 14.55           S  
ANISOU  224  SD  MET A  20      715   2317   2495     60     33     52       S  
ATOM    225  CE  MET A  20       5.567   1.719  24.683  1.00 15.78           C  
ANISOU  225  CE  MET A  20     1176   2088   2729   -341     69     -5       C  
ATOM    226  N   LYS A  21       9.994   3.391  28.356  1.00 13.08           N  
ANISOU  226  N   LYS A  21      901   1911   2157    -15    139    123       N  
ATOM    227  CA  LYS A  21      10.386   3.422  29.764  1.00 14.16           C  
ANISOU  227  CA  LYS A  21      935   2232   2213      8    269    159       C  
ATOM    228  C   LYS A  21      11.460   4.497  29.928  1.00 14.49           C  
ANISOU  228  C   LYS A  21     1049   2211   2246    -83    -67    206       C  
ATOM    229  O   LYS A  21      11.429   5.245  30.916  1.00 16.52           O  
ANISOU  229  O   LYS A  21     1594   2520   2161   -376    126     19       O  
ATOM    230  CB  LYS A  21      10.974   2.052  30.167  1.00 15.51           C  
ANISOU  230  CB  LYS A  21     1238   2325   2329    117    113    295       C  
ATOM    231  CG  LYS A  21      10.015   0.996  30.452  1.00 18.86           C  
ANISOU  231  CG  LYS A  21     1969   2670   2526    -91    -53    239       C  
ATOM    232  CD  LYS A  21      10.688  -0.279  30.949  1.00 23.01           C  
ANISOU  232  CD  LYS A  21     2685   2976   3079    220    -15    325       C  
ATOM    233  CE  LYS A  21       9.701  -1.331  31.334  1.00 26.35           C  
ANISOU  233  CE  LYS A  21     2808   3418   3786    344   -307    544       C  
ATOM    234  NZ  LYS A  21      10.267  -2.621  31.749  1.00 31.50           N  
ANISOU  234  NZ  LYS A  21     3478   4059   4429    920   -565    860       N  
ATOM    235  N   GLU A  22      12.410   4.616  29.001  1.00 14.73           N  
ANISOU  235  N   GLU A  22     1027   2371   2199   -179    -91     63       N  
ATOM    236  CA  GLU A  22      13.488   5.565  29.109  1.00 15.49           C  
ANISOU  236  CA  GLU A  22     1086   2499   2301   -227   -138     91       C  
ATOM    237  C   GLU A  22      12.962   6.978  29.027  1.00 14.53           C  
ANISOU  237  C   GLU A  22     1048   2187   2285   -258   -137     -3       C  
ATOM    238  O   GLU A  22      13.433   7.882  29.725  1.00 16.44           O  
ANISOU  238  O   GLU A  22     1268   2462   2516   -446   -254    -42       O  
ATOM    239  CB  GLU A  22      14.555   5.292  28.055  1.00 15.20           C  
ANISOU  239  CB  GLU A  22      822   2462   2489     -8    -42    126       C  
ATOM    240  CG  GLU A  22      15.928   5.815  28.337  1.00 18.24           C  
ANISOU  240  CG  GLU A  22     1144   2864   2921   -174   -120    226       C  
ATOM    241  CD  GLU A  22      16.676   5.031  29.441  1.00 20.76           C  
ANISOU  241  CD  GLU A  22     1487   3281   3117    -36   -177    468       C  
ATOM    242  OE1 GLU A  22      16.180   4.018  29.938  1.00 23.73           O  
ANISOU  242  OE1 GLU A  22     1736   3853   3425    -60   -434    294       O  
ATOM    243  OE2 GLU A  22      17.821   5.384  29.787  1.00 26.08           O  
ANISOU  243  OE2 GLU A  22     2389   3957   3561      5   -570    140       O  
ATOM    244  N   VAL A  23      11.930   7.199  28.213  1.00 14.28           N  
ANISOU  244  N   VAL A  23     1215   1864   2346   -122    -86     14       N  
ATOM    245  CA  VAL A  23      11.245   8.468  28.066  1.00 14.21           C  
ANISOU  245  CA  VAL A  23     1203   1941   2254   -225     55     30       C  
ATOM    246  C   VAL A  23      10.493   8.839  29.342  1.00 15.81           C  
ANISOU  246  C   VAL A  23     1655   1973   2378   -229     89    -73       C  
ATOM    247  O   VAL A  23      10.405   9.998  29.646  1.00 18.57           O  
ANISOU  247  O   VAL A  23     2559   2082   2415   -205    232   -156       O  
ATOM    248  CB  VAL A  23      10.316   8.440  26.822  1.00 14.69           C  
ANISOU  248  CB  VAL A  23     1395   1877   2309    -28    131     95       C  
ATOM    249  CG1 VAL A  23       9.344   9.589  26.741  1.00 16.31           C  
ANISOU  249  CG1 VAL A  23     1845   1859   2491    145     -1     -7       C  
ATOM    250  CG2 VAL A  23      11.132   8.388  25.556  1.00 15.24           C  
ANISOU  250  CG2 VAL A  23     1739   1735   2314    -90    110     20       C  
ATOM    251  N   GLY A  24      10.031   7.857  30.107  1.00 15.28           N  
ANISOU  251  N   GLY A  24     1796   1861   2148   -196    -40    -77       N  
ATOM    252  CA  GLY A  24       9.269   8.082  31.339  1.00 15.59           C  
ANISOU  252  CA  GLY A  24     1619   1949   2356   -367     10    -76       C  
ATOM    253  C   GLY A  24       7.804   7.753  31.233  1.00 14.65           C  
ANISOU  253  C   GLY A  24     1455   1784   2327   -369     64    -99       C  
ATOM    254  O   GLY A  24       7.017   8.168  32.081  1.00 17.74           O  
ANISOU  254  O   GLY A  24     2057   2193   2491   -295    263   -220       O  
ATOM    255  N   VAL A  25       7.377   6.996  30.223  1.00 14.28           N  
ANISOU  255  N   VAL A  25     1510   1704   2210   -176     70    -47       N  
ATOM    256  CA  VAL A  25       5.958   6.664  30.034  1.00 13.56           C  
ANISOU  256  CA  VAL A  25     1256   1640   2256    -87    103     -3       C  
ATOM    257  C   VAL A  25       5.598   5.651  31.106  1.00 14.07           C  
ANISOU  257  C   VAL A  25     1271   1878   2196   -364     36    -50       C  
ATOM    258  O   VAL A  25       6.310   4.674  31.353  1.00 15.40           O  
ANISOU  258  O   VAL A  25     1769   1845   2238   -379    -88    164       O  
ATOM    259  CB  VAL A  25       5.779   6.052  28.666  1.00 12.30           C  
ANISOU  259  CB  VAL A  25      573   1728   2371   -205    -50    166       C  
ATOM    260  CG1 VAL A  25       4.359   5.766  28.451  1.00 14.16           C  
ANISOU  260  CG1 VAL A  25     1260   1691   2427    -80    104    162       C  
ATOM    261  CG2 VAL A  25       6.234   6.981  27.510  1.00 13.77           C  
ANISOU  261  CG2 VAL A  25      860   1865   2505     23     76    352       C  
ATOM    262  N   GLY A  26       4.456   5.864  31.709  1.00 15.29           N  
ANISOU  262  N   GLY A  26     1327   2235   2245   -524    142    -24       N  
ATOM    263  CA  GLY A  26       3.959   4.949  32.738  1.00 15.91           C  
ANISOU  263  CA  GLY A  26     1433   2301   2310   -459    181   -129       C  
ATOM    264  C   GLY A  26       3.415   3.623  32.236  1.00 15.18           C  
ANISOU  264  C   GLY A  26     1291   2214   2262   -437     94    -10       C  
ATOM    265  O   GLY A  26       3.171   3.455  31.072  1.00 15.28           O  
ANISOU  265  O   GLY A  26     1352   2220   2232   -541     -2   -103       O  
ATOM    266  N   PHE A  27       3.309   2.671  33.139  1.00 15.99           N  
ANISOU  266  N   PHE A  27     1785   2253   2036   -463    -26    -83       N  
ATOM    267  CA  PHE A  27       2.968   1.295  32.798  1.00 14.90           C  
ANISOU  267  CA  PHE A  27     1348   2157   2153   -378     81    114       C  
ATOM    268  C   PHE A  27       1.752   1.153  31.922  1.00 13.89           C  
ANISOU  268  C   PHE A  27     1195   1776   2307   -415    -21    183       C  
ATOM    269  O   PHE A  27       1.836   0.558  30.847  1.00 14.01           O  
ANISOU  269  O   PHE A  27     1234   1851   2236   -414     74     58       O  
ATOM    270  CB  PHE A  27       2.790   0.467  34.078  1.00 16.06           C  
ANISOU  270  CB  PHE A  27     1572   2345   2183   -194   -165    180       C  
ATOM    271  CG  PHE A  27       2.423  -0.975  33.805  1.00 17.69           C  
ANISOU  271  CG  PHE A  27     1984   2404   2334   -710   -141    298       C  
ATOM    272  CD1 PHE A  27       3.345  -1.965  33.644  1.00 20.49           C  
ANISOU  272  CD1 PHE A  27     2642   2692   2451   -694   -106    335       C  
ATOM    273  CD2 PHE A  27       1.107  -1.317  33.677  1.00 18.66           C  
ANISOU  273  CD2 PHE A  27     2409   2211   2470   -591   -319    583       C  
ATOM    274  CE1 PHE A  27       2.901  -3.311  33.382  1.00 21.25           C  
ANISOU  274  CE1 PHE A  27     2750   2689   2636   -705    -98    407       C  
ATOM    275  CE2 PHE A  27       0.682  -2.611  33.434  1.00 20.71           C  
ANISOU  275  CE2 PHE A  27     2567   2646   2653   -903   -311    723       C  
ATOM    276  CZ  PHE A  27       1.550  -3.603  33.279  1.00 20.48           C  
ANISOU  276  CZ  PHE A  27     2760   2435   2583   -912   -469    228       C  
ATOM    277  N   ALA A  28       0.614   1.691  32.325  1.00 15.37           N  
ANISOU  277  N   ALA A  28     1519   1999   2322   -266     63     56       N  
ATOM    278  CA  ALA A  28      -0.624   1.428  31.580  1.00 15.38           C  
ANISOU  278  CA  ALA A  28     1376   2060   2406   -240     67    158       C  
ATOM    279  C   ALA A  28      -0.540   2.046  30.188  1.00 14.36           C  
ANISOU  279  C   ALA A  28     1108   1924   2423   -287     -7     59       C  
ATOM    280  O   ALA A  28      -0.966   1.447  29.207  1.00 15.81           O  
ANISOU  280  O   ALA A  28     1530   2038   2436   -309    -31     14       O  
ATOM    281  CB  ALA A  28      -1.820   1.926  32.298  1.00 17.58           C  
ANISOU  281  CB  ALA A  28     1665   2379   2635    -28    176    146       C  
ATOM    282  N   THR A  29       0.015   3.251  30.088  1.00 14.11           N  
ANISOU  282  N   THR A  29     1147   1920   2292   -290     21    -77       N  
ATOM    283  CA  THR A  29       0.175   3.899  28.825  1.00 14.67           C  
ANISOU  283  CA  THR A  29     1315   1861   2399   -217   -211     73       C  
ATOM    284  C   THR A  29       1.090   3.098  27.946  1.00 13.33           C  
ANISOU  284  C   THR A  29      827   1863   2372   -438   -254     41       C  
ATOM    285  O   THR A  29       0.858   2.962  26.710  1.00 14.78           O  
ANISOU  285  O   THR A  29     1157   2092   2366   -321   -204    146       O  
ATOM    286  CB  THR A  29       0.702   5.341  29.007  1.00 15.24           C  
ANISOU  286  CB  THR A  29     1516   1713   2560    -79   -192     70       C  
ATOM    287  OG1 THR A  29      -0.279   6.048  29.752  1.00 18.13           O  
ANISOU  287  OG1 THR A  29     1667   2237   2982     78    -25     68       O  
ATOM    288  CG2 THR A  29       0.848   6.039  27.677  1.00 16.45           C  
ANISOU  288  CG2 THR A  29     1710   1954   2585   -119   -165    383       C  
ATOM    289  N   ARG A  30       2.216   2.636  28.473  1.00 13.17           N  
ANISOU  289  N   ARG A  30      946   1872   2185   -466   -199     93       N  
ATOM    290  CA  ARG A  30       3.139   1.810  27.673  1.00 13.38           C  
ANISOU  290  CA  ARG A  30      859   1966   2257   -222    -32    255       C  
ATOM    291  C   ARG A  30       2.467   0.584  27.119  1.00 13.48           C  
ANISOU  291  C   ARG A  30      953   1941   2227   -201   -156    238       C  
ATOM    292  O   ARG A  30       2.699   0.183  25.961  1.00 13.73           O  
ANISOU  292  O   ARG A  30      938   2008   2269   -122      1    173       O  
ATOM    293  CB  ARG A  30       4.387   1.345  28.471  1.00 14.87           C  
ANISOU  293  CB  ARG A  30      984   2219   2447   -273    -79    262       C  
ATOM    294  CG  ARG A  30       5.437   2.328  28.718  1.00 14.28           C  
ANISOU  294  CG  ARG A  30     1214   2086   2124   -341    304     48       C  
ATOM    295  CD  ARG A  30       6.775   1.732  29.018  1.00 14.12           C  
ANISOU  295  CD  ARG A  30      755   2347   2263    -85    -25    137       C  
ATOM    296  NE  ARG A  30       6.687   0.569  29.920  1.00 14.85           N  
ANISOU  296  NE  ARG A  30      975   2156   2510     43    -66    144       N  
ATOM    297  CZ  ARG A  30       6.557   0.628  31.241  1.00 15.05           C  
ANISOU  297  CZ  ARG A  30     1150   1928   2637     18    133    131       C  
ATOM    298  NH1 ARG A  30       6.481   1.791  31.898  1.00 15.99           N  
ANISOU  298  NH1 ARG A  30     1682   1981   2409    -78   -112    391       N  
ATOM    299  NH2 ARG A  30       6.520  -0.526  31.920  1.00 17.62           N  
ANISOU  299  NH2 ARG A  30     2104   2024   2565    187     72    257       N  
ATOM    300  N   LYS A  31       1.692  -0.104  27.938  1.00 13.49           N  
ANISOU  300  N   LYS A  31     1057   1877   2190   -166      8    149       N  
ATOM    301  CA  LYS A  31       1.087  -1.349  27.472  1.00 14.31           C  
ANISOU  301  CA  LYS A  31     1224   1826   2385   -199      0     10       C  
ATOM    302  C   LYS A  31       0.128  -1.052  26.344  1.00 14.06           C  
ANISOU  302  C   LYS A  31      824   2016   2499   -145    -12    -84       C  
ATOM    303  O   LYS A  31       0.115  -1.774  25.331  1.00 15.62           O  
ANISOU  303  O   LYS A  31      983   2291   2659   -131     69   -362       O  
ATOM    304  CB  LYS A  31       0.343  -2.040  28.620  1.00 15.25           C  
ANISOU  304  CB  LYS A  31     1135   2092   2567   -335     94     36       C  
ATOM    305  CG  LYS A  31       1.220  -2.515  29.698  1.00 19.15           C  
ANISOU  305  CG  LYS A  31     2092   2259   2923   -400   -121    203       C  
ATOM    306  CD  LYS A  31       2.210  -3.520  29.251  1.00 24.45           C  
ANISOU  306  CD  LYS A  31     3001   3054   3234    140    -42    475       C  
ATOM    307  CE  LYS A  31       3.571  -2.934  29.060  1.00 28.31           C  
ANISOU  307  CE  LYS A  31     3423   3435   3895     24     70     22       C  
ATOM    308  NZ  LYS A  31       4.571  -4.057  28.993  1.00 32.27           N  
ANISOU  308  NZ  LYS A  31     4322   3598   4340    359   -275    232       N  
ATOM    309  N   VAL A  32      -0.736  -0.065  26.494  1.00 13.69           N  
ANISOU  309  N   VAL A  32      629   2118   2454   -199   -212   -114       N  
ATOM    310  CA AVAL A  32      -1.685   0.273  25.442  0.50 14.56           C  
ANISOU  310  CA AVAL A  32      699   2169   2664   -285   -138   -193       C  
ATOM    311  CA BVAL A  32      -1.663   0.167  25.419  0.50 14.54           C  
ANISOU  311  CA BVAL A  32      626   2270   2626   -277   -143   -101       C  
ATOM    312  C   VAL A  32      -0.983   0.855  24.200  1.00 13.15           C  
ANISOU  312  C   VAL A  32      284   2292   2418    -70   -249    -25       C  
ATOM    313  O   VAL A  32      -1.316   0.507  23.035  1.00 14.59           O  
ANISOU  313  O   VAL A  32      605   2418   2519   -178   -216   -166       O  
ATOM    314  CB AVAL A  32      -2.767   1.262  25.973  0.50 15.29           C  
ANISOU  314  CB AVAL A  32     1017   2079   2712   -219   -167   -264       C  
ATOM    315  CB BVAL A  32      -2.926   0.906  25.909  0.50 14.81           C  
ANISOU  315  CB BVAL A  32      496   2565   2564   -218   -266     14       C  
ATOM    316  CG1AVAL A  32      -3.746   1.653  24.854  0.50 14.11           C  
ANISOU  316  CG1AVAL A  32      253   2123   2984     23     -1   -598       C  
ATOM    317  CG1BVAL A  32      -3.731   0.054  26.979  0.50 15.13           C  
ANISOU  317  CG1BVAL A  32      769   2187   2792   -337    290   -136       C  
ATOM    318  CG2AVAL A  32      -3.556   0.599  27.130  0.50 17.21           C  
ANISOU  318  CG2AVAL A  32     1288   2222   3026   -304     20   -346       C  
ATOM    319  CG2BVAL A  32      -2.543   2.312  26.419  0.50 17.59           C  
ANISOU  319  CG2BVAL A  32     1358   2431   2893     62   -198   -118       C  
ATOM    320  N   ALA A  33      -0.022   1.732  24.407  1.00 13.48           N  
ANISOU  320  N   ALA A  33      546   2265   2309   -241   -231    -28       N  
ATOM    321  CA  ALA A  33       0.697   2.356  23.273  1.00 14.10           C  
ANISOU  321  CA  ALA A  33      899   2273   2183    -46   -156    209       C  
ATOM    322  C   ALA A  33       1.461   1.307  22.506  1.00 14.78           C  
ANISOU  322  C   ALA A  33      960   2386   2268   -209     31    286       C  
ATOM    323  O   ALA A  33       1.578   1.405  21.289  1.00 15.32           O  
ANISOU  323  O   ALA A  33     1224   2394   2201   -110   -149    271       O  
ATOM    324  CB  ALA A  33       1.638   3.461  23.776  1.00 15.26           C  
ANISOU  324  CB  ALA A  33     1006   2246   2545   -286   -326    255       C  
ATOM    325  N   GLY A  34       2.002   0.315  23.204  1.00 14.18           N  
ANISOU  325  N   GLY A  34      902   2335   2149     13     52    225       N  
ATOM    326  CA  GLY A  34       2.853  -0.679  22.522  1.00 15.34           C  
ANISOU  326  CA  GLY A  34     1040   2349   2439    163    118    217       C  
ATOM    327  C   GLY A  34       2.049  -1.613  21.653  1.00 15.32           C  
ANISOU  327  C   GLY A  34     1348   2068   2402    400    138    117       C  
ATOM    328  O   GLY A  34       2.620  -2.196  20.735  1.00 16.79           O  
ANISOU  328  O   GLY A  34     1064   2608   2706    219    127   -145       O  
ATOM    329  N   MET A  35       0.736  -1.744  21.872  1.00 14.18           N  
ANISOU  329  N   MET A  35     1102   1975   2308    203    229    216       N  
ATOM    330  CA  MET A  35      -0.112  -2.562  20.991  1.00 14.60           C  
ANISOU  330  CA  MET A  35     1255   1885   2407     -4    208    166       C  
ATOM    331  C   MET A  35      -0.461  -1.886  19.642  1.00 13.31           C  
ANISOU  331  C   MET A  35      721   1919   2416    -73    297    232       C  
ATOM    332  O   MET A  35      -0.737  -2.539  18.626  1.00 14.73           O  
ANISOU  332  O   MET A  35      768   2133   2695    -89     60    229       O  
ATOM    333  CB  MET A  35      -1.430  -2.920  21.639  1.00 14.77           C  
ANISOU  333  CB  MET A  35     1299   1681   2631    -77    393    202       C  
ATOM    334  CG  MET A  35      -1.257  -3.796  22.872  1.00 15.60           C  
ANISOU  334  CG  MET A  35     1490   1825   2609   -103    381     79       C  
ATOM    335  SD  MET A  35      -0.625  -5.414  22.512  1.00 15.63           S  
ANISOU  335  SD  MET A  35     1423   1811   2702     74    198    281       S  
ATOM    336  CE  MET A  35      -1.840  -6.108  21.395  1.00 22.31           C  
ANISOU  336  CE  MET A  35     3030   2344   3102   -489   -539    529       C  
ATOM    337  N   ALA A  36      -0.380  -0.570  19.609  1.00 13.83           N  
ANISOU  337  N   ALA A  36      877   1871   2506    -39     66    326       N  
ATOM    338  CA  ALA A  36      -0.908   0.131  18.439  1.00 14.32           C  
ANISOU  338  CA  ALA A  36      967   1990   2482   -112      0    372       C  
ATOM    339  C   ALA A  36      -0.110  -0.145  17.190  1.00 12.69           C  
ANISOU  339  C   ALA A  36      393   1856   2571   -470     -9    294       C  
ATOM    340  O   ALA A  36       1.119  -0.245  17.239  1.00 13.61           O  
ANISOU  340  O   ALA A  36      550   2216   2403   -271    -93    261       O  
ATOM    341  CB  ALA A  36      -1.002   1.633  18.686  1.00 16.22           C  
ANISOU  341  CB  ALA A  36     1479   2028   2653    143     66     83       C  
ATOM    342  N   LYS A  37      -0.811  -0.211  16.085  1.00 13.67           N  
ANISOU  342  N   LYS A  37      707   1887   2599    -93   -115    272       N  
ATOM    343  CA  LYS A  37      -0.235  -0.367  14.740  1.00 14.73           C  
ANISOU  343  CA  LYS A  37     1114   1979   2503   -242     25    108       C  
ATOM    344  C   LYS A  37      -0.714   0.785  13.885  1.00 13.66           C  
ANISOU  344  C   LYS A  37      588   2105   2494   -394    116    248       C  
ATOM    345  O   LYS A  37      -1.663   0.619  13.131  1.00 15.73           O  
ANISOU  345  O   LYS A  37     1120   2304   2552   -579   -123    255       O  
ATOM    346  CB  LYS A  37      -0.605  -1.722  14.118  1.00 15.82           C  
ANISOU  346  CB  LYS A  37     1166   2073   2771   -154     -2    122       C  
ATOM    347  CG  LYS A  37       0.021  -2.854  14.905  1.00 19.04           C  
ANISOU  347  CG  LYS A  37     1410   2486   3335    158    -43     -5       C  
ATOM    348  CD  LYS A  37       1.443  -2.971  14.621  1.00 22.55           C  
ANISOU  348  CD  LYS A  37     2216   2874   3478    220   -219     44       C  
ATOM    349  CE  LYS A  37       2.037  -4.312  14.944  1.00 25.17           C  
ANISOU  349  CE  LYS A  37     2611   3206   3744    335    132    -72       C  
ATOM    350  NZ  LYS A  37       2.086  -4.522  16.412  1.00 29.22           N  
ANISOU  350  NZ  LYS A  37     3125   4268   3709    299     89    279       N  
ATOM    351  N   PRO A  38      -0.149   1.988  14.106  1.00 13.33           N  
ANISOU  351  N   PRO A  38      728   1939   2398   -313     90    202       N  
ATOM    352  CA  PRO A  38      -0.734   3.142  13.458  1.00 14.64           C  
ANISOU  352  CA  PRO A  38     1310   1925   2327   -218    222    277       C  
ATOM    353  C   PRO A  38      -0.640   3.160  11.954  1.00 14.26           C  
ANISOU  353  C   PRO A  38     1205   1875   2336   -351    399    228       C  
ATOM    354  O   PRO A  38       0.290   2.567  11.382  1.00 14.51           O  
ANISOU  354  O   PRO A  38     1090   1947   2476   -329    331    199       O  
ATOM    355  CB  PRO A  38       0.008   4.316  14.062  1.00 17.08           C  
ANISOU  355  CB  PRO A  38     1995   2054   2438   -193    174     65       C  
ATOM    356  CG  PRO A  38       0.888   3.766  15.077  1.00 19.44           C  
ANISOU  356  CG  PRO A  38     2157   2217   3011   -447   -120     49       C  
ATOM    357  CD  PRO A  38       0.944   2.326  15.003  1.00 13.89           C  
ANISOU  357  CD  PRO A  38      847   1952   2479   -449    182    237       C  
ATOM    358  N  AASN A  39      -1.533   3.893  11.328  0.50 14.81           N  
ANISOU  358  N  AASN A  39     1457   1930   2237   -290    275    197       N  
ATOM    359  N  BASN A  39      -1.504   3.994  11.372  0.50 14.27           N  
ANISOU  359  N  BASN A  39     1308   1837   2277   -304    320    183       N  
ATOM    360  CA AASN A  39      -1.234   4.423  10.025  0.50 15.54           C  
ANISOU  360  CA AASN A  39     1793   1839   2272   -162    238    154       C  
ATOM    361  CA BASN A  39      -1.581   4.428   9.958  0.50 14.42           C  
ANISOU  361  CA BASN A  39     1459   1694   2325   -119    362     89       C  
ATOM    362  C  AASN A  39      -0.641   5.768  10.244  0.50 15.02           C  
ANISOU  362  C  AASN A  39     1699   1756   2250   -172    263     97       C  
ATOM    363  C  BASN A  39      -0.972   5.883   9.945  0.50 13.53           C  
ANISOU  363  C  BASN A  39     1321   1561   2256   -178    286     63       C  
ATOM    364  O  AASN A  39      -0.824   6.434  11.270  0.50 15.73           O  
ANISOU  364  O  AASN A  39     1751   2024   2201   -118    163     89       O  
ATOM    365  O  BASN A  39      -1.586   6.780  10.568  0.50 15.07           O  
ANISOU  365  O  BASN A  39     2184   1585   1957    -37    484    199       O  
ATOM    366  CB AASN A  39      -2.419   4.532   9.111  0.50 15.74           C  
ANISOU  366  CB AASN A  39     1815   2019   2144   -182    221    193       C  
ATOM    367  CB BASN A  39      -3.082   4.394   9.548  0.50 15.27           C  
ANISOU  367  CB BASN A  39     1525   1800   2474    -76    384    157       C  
ATOM    368  CG AASN A  39      -2.793   3.207   8.494  0.50 16.69           C  
ANISOU  368  CG AASN A  39     1437   2215   2689   -504   -125    332       C  
ATOM    369  CG BASN A  39      -3.339   4.780   8.080  0.50 19.75           C  
ANISOU  369  CG BASN A  39     2164   2470   2868     48    151    169       C  
ATOM    370  OD1AASN A  39      -2.468   2.136   9.032  0.50 22.71           O  
ANISOU  370  OD1AASN A  39     3171   2536   2918   -522   -639     82       O  
ATOM    371  OD1BASN A  39      -3.965   5.812   7.781  0.50 21.91           O  
ANISOU  371  OD1BASN A  39     1646   2722   3958   -225    211    223       O  
ATOM    372  ND2AASN A  39      -3.505   3.261   7.365  0.50 22.48           N  
ANISOU  372  ND2AASN A  39     2361   3286   2892   -183    -85    264       N  
ATOM    373  ND2BASN A  39      -2.851   3.958   7.165  0.50 19.56           N  
ANISOU  373  ND2BASN A  39     2509   2344   2579   -265   -298    -42       N  
ATOM    374  N   MET A  40       0.205   6.098   9.318  1.00 14.75           N  
ANISOU  374  N   MET A  40     1535   1650   2418   -156    372    117       N  
ATOM    375  CA  MET A  40       0.842   7.395   9.318  1.00 13.89           C  
ANISOU  375  CA  MET A  40     1548   1503   2226   -159    233     31       C  
ATOM    376  C   MET A  40       0.736   7.981   7.943  1.00 13.87           C  
ANISOU  376  C   MET A  40     1310   1692   2268   -246    243     58       C  
ATOM    377  O   MET A  40       1.060   7.334   6.951  1.00 15.01           O  
ANISOU  377  O   MET A  40     1675   1624   2402     39    281    142       O  
ATOM    378  CB  MET A  40       2.304   7.220   9.666  1.00 15.66           C  
ANISOU  378  CB  MET A  40     2134   1516   2299   -229    118     86       C  
ATOM    379  CG  MET A  40       3.161   8.525   9.620  1.00 15.51           C  
ANISOU  379  CG  MET A  40     1584   1765   2545   -115    -48     27       C  
ATOM    380  SD  MET A  40       4.813   8.422  10.154  1.00 20.18           S  
ANISOU  380  SD  MET A  40     2842   1896   2930   -243   -213    -24       S  
ATOM    381  CE  MET A  40       5.395   7.000   9.246  1.00 19.29           C  
ANISOU  381  CE  MET A  40     1429   2642   3256   -195    177     54       C  
ATOM    382  N   ILE A  41       0.197   9.186   7.891  1.00 13.39           N  
ANISOU  382  N   ILE A  41     1240   1617   2231   -207    191    -31       N  
ATOM    383  CA  ILE A  41      -0.056   9.884   6.648  1.00 12.37           C  
ANISOU  383  CA  ILE A  41      639   1717   2342   -329    182     41       C  
ATOM    384  C   ILE A  41       0.865  11.079   6.644  1.00 12.57           C  
ANISOU  384  C   ILE A  41     1066   1549   2158    -82    166    -27       C  
ATOM    385  O   ILE A  41       0.823  11.949   7.543  1.00 13.27           O  
ANISOU  385  O   ILE A  41     1240   1611   2190   -328    247    -92       O  
ATOM    386  CB  ILE A  41      -1.506  10.332   6.504  1.00 14.61           C  
ANISOU  386  CB  ILE A  41      939   2089   2521   -245    205   -175       C  
ATOM    387  CG1 ILE A  41      -2.476   9.177   6.637  1.00 17.77           C  
ANISOU  387  CG1 ILE A  41      778   2941   3033   -651    151   -201       C  
ATOM    388  CG2 ILE A  41      -1.733  11.052   5.188  1.00 18.49           C  
ANISOU  388  CG2 ILE A  41     1276   2824   2924   -282    -69     46       C  
ATOM    389  CD1 ILE A  41      -3.783   9.605   6.698  1.00 23.94           C  
ANISOU  389  CD1 ILE A  41      735   4048   4312  -1107    146   -241       C  
ATOM    390  N   ILE A  42       1.676  11.189   5.613  1.00 11.62           N  
ANISOU  390  N   ILE A  42      998   1322   2095    -91    123   -116       N  
ATOM    391  CA  ILE A  42       2.626  12.292   5.485  1.00 11.39           C  
ANISOU  391  CA  ILE A  42      851   1524   1953     -7    -39    -73       C  
ATOM    392  C   ILE A  42       2.274  13.032   4.221  1.00 11.34           C  
ANISOU  392  C   ILE A  42      741   1439   2126     -4     30    -80       C  
ATOM    393  O   ILE A  42       2.158  12.435   3.138  1.00 12.10           O  
ANISOU  393  O   ILE A  42     1003   1494   2100    -90    -44     27       O  
ATOM    394  CB  ILE A  42       4.090  11.768   5.429  1.00 11.56           C  
ANISOU  394  CB  ILE A  42     1010   1505   1877   -127     45      4       C  
ATOM    395  CG1 ILE A  42       4.419  11.006   6.707  1.00 12.30           C  
ANISOU  395  CG1 ILE A  42     1009   1576   2088    190      8   -102       C  
ATOM    396  CG2 ILE A  42       5.059  12.960   5.220  1.00 13.08           C  
ANISOU  396  CG2 ILE A  42      870   1797   2301    133     76    -67       C  
ATOM    397  CD1 ILE A  42       5.816  10.467   6.805  1.00 14.26           C  
ANISOU  397  CD1 ILE A  42     1253   1940   2224    187    -80    119       C  
ATOM    398  N   SER A  43       2.153  14.344   4.326  1.00 11.59           N  
ANISOU  398  N   SER A  43      936   1416   2049   -170   -175    -65       N  
ATOM    399  CA  SER A  43       1.836  15.198   3.173  1.00 12.76           C  
ANISOU  399  CA  SER A  43     1273   1447   2128    -44   -174     23       C  
ATOM    400  C   SER A  43       2.709  16.445   3.243  1.00 12.63           C  
ANISOU  400  C   SER A  43     1258   1450   2089    187   -137    -48       C  
ATOM    401  O   SER A  43       3.179  16.855   4.296  1.00 12.48           O  
ANISOU  401  O   SER A  43     1207   1490   2043    -59    -29     28       O  
ATOM    402  CB  SER A  43       0.372  15.501   3.124  1.00 15.16           C  
ANISOU  402  CB  SER A  43     1371   1866   2522    -31   -310     65       C  
ATOM    403  OG  SER A  43      -0.011  16.168   4.266  1.00 18.22           O  
ANISOU  403  OG  SER A  43     1723   2305   2894    217   -134    -90       O  
ATOM    404  N   VAL A  44       2.870  17.063   2.091  1.00 13.63           N  
ANISOU  404  N   VAL A  44     1670   1476   2032    -12   -154    -67       N  
ATOM    405  CA  VAL A  44       3.578  18.310   1.940  1.00 14.55           C  
ANISOU  405  CA  VAL A  44     1645   1588   2294   -110   -231     80       C  
ATOM    406  C   VAL A  44       2.732  19.306   1.143  1.00 15.44           C  
ANISOU  406  C   VAL A  44     1957   1681   2226   -104   -327      5       C  
ATOM    407  O   VAL A  44       2.094  18.953   0.174  1.00 19.38           O  
ANISOU  407  O   VAL A  44     3335   1644   2383    -48   -679     68       O  
ATOM    408  CB  VAL A  44       4.955  18.110   1.271  1.00 15.55           C  
ANISOU  408  CB  VAL A  44     1852   1577   2476   -130   -199    104       C  
ATOM    409  CG1 VAL A  44       5.720  19.430   1.153  1.00 20.56           C  
ANISOU  409  CG1 VAL A  44     2083   2224   3503   -506    -53    163       C  
ATOM    410  CG2 VAL A  44       5.828  17.152   2.015  1.00 18.78           C  
ANISOU  410  CG2 VAL A  44     1899   2223   3011    -38   -173   -137       C  
ATOM    411  N   ASN A  45       2.667  20.535   1.619  1.00 14.12           N  
ANISOU  411  N   ASN A  45     1750   1505   2106   -126   -141     66       N  
ATOM    412  CA  ASN A  45       1.957  21.625   0.940  1.00 13.89           C  
ANISOU  412  CA  ASN A  45     1594   1609   2074   -139   -308     81       C  
ATOM    413  C   ASN A  45       2.847  22.846   1.085  1.00 14.69           C  
ANISOU  413  C   ASN A  45     1744   1635   2201    -58   -187    144       C  
ATOM    414  O   ASN A  45       2.961  23.410   2.140  1.00 13.09           O  
ANISOU  414  O   ASN A  45     1279   1514   2180     49   -155     39       O  
ATOM    415  CB  ASN A  45       0.581  21.783   1.528  1.00 14.12           C  
ANISOU  415  CB  ASN A  45     1464   1638   2261     17   -220      3       C  
ATOM    416  CG  ASN A  45      -0.274  22.789   0.821  1.00 13.27           C  
ANISOU  416  CG  ASN A  45     1099   1859   2081   -367   -429    -87       C  
ATOM    417  OD1 ASN A  45      -1.513  22.593   0.745  1.00 15.25           O  
ANISOU  417  OD1 ASN A  45     1342   1921   2529   -283   -185    -91       O  
ATOM    418  ND2 ASN A  45       0.292  23.827   0.350  1.00 14.35           N  
ANISOU  418  ND2 ASN A  45     1239   1571   2640   -313   -535    248       N  
ATOM    419  N   GLY A  46       3.520  23.201   0.006  1.00 16.02           N  
ANISOU  419  N   GLY A  46     2286   1709   2089   -177   -215    140       N  
ATOM    420  CA  GLY A  46       4.486  24.271   0.075  1.00 16.63           C  
ANISOU  420  CA  GLY A  46     2140   1979   2199   -215     82    199       C  
ATOM    421  C   GLY A  46       5.621  23.927   1.042  1.00 15.57           C  
ANISOU  421  C   GLY A  46     1599   1953   2361   -216    247    170       C  
ATOM    422  O   GLY A  46       6.210  22.872   0.957  1.00 17.54           O  
ANISOU  422  O   GLY A  46     1929   2034   2701   -203    174    -70       O  
ATOM    423  N   ASP A  47       5.865  24.802   2.002  1.00 14.90           N  
ANISOU  423  N   ASP A  47     1416   1819   2425   -177    160    206       N  
ATOM    424  CA  ASP A  47       6.871  24.573   3.028  1.00 16.17           C  
ANISOU  424  CA  ASP A  47     1511   2017   2614   -221    -96    225       C  
ATOM    425  C   ASP A  47       6.359  23.758   4.208  1.00 13.72           C  
ANISOU  425  C   ASP A  47     1151   1754   2308     85    109     58       C  
ATOM    426  O   ASP A  47       7.177  23.441   5.088  1.00 14.86           O  
ANISOU  426  O   ASP A  47      987   2063   2596     95   -166     81       O  
ATOM    427  CB  ASP A  47       7.365  25.934   3.583  1.00 18.45           C  
ANISOU  427  CB  ASP A  47     2113   2228   2666   -403   -100    212       C  
ATOM    428  CG  ASP A  47       8.035  26.811   2.543  1.00 22.87           C  
ANISOU  428  CG  ASP A  47     2687   2664   3337   -536   -133    177       C  
ATOM    429  OD1 ASP A  47       8.619  26.282   1.592  1.00 26.78           O  
ANISOU  429  OD1 ASP A  47     3089   3833   3251  -1059    603    437       O  
ATOM    430  OD2 ASP A  47       8.021  28.047   2.716  1.00 30.52           O  
ANISOU  430  OD2 ASP A  47     4176   3109   4311   -729   -139    598       O  
ATOM    431  N   VAL A  48       5.059  23.472   4.244  1.00 11.63           N  
ANISOU  431  N   VAL A  48      768   1525   2122    167    -73    128       N  
ATOM    432  CA  VAL A  48       4.508  22.836   5.415  1.00 11.42           C  
ANISOU  432  CA  VAL A  48      691   1571   2077     50    -90     66       C  
ATOM    433  C   VAL A  48       4.424  21.325   5.200  1.00 11.52           C  
ANISOU  433  C   VAL A  48      902   1459   2016   -143    -68     65       C  
ATOM    434  O   VAL A  48       3.786  20.829   4.279  1.00 12.39           O  
ANISOU  434  O   VAL A  48     1065   1491   2149     51   -236    100       O  
ATOM    435  CB  VAL A  48       3.138  23.382   5.716  1.00 12.57           C  
ANISOU  435  CB  VAL A  48      928   1646   2202     34    -51     91       C  
ATOM    436  CG1 VAL A  48       2.605  22.715   6.990  1.00 14.57           C  
ANISOU  436  CG1 VAL A  48     1440   1714   2382    144    355    133       C  
ATOM    437  CG2 VAL A  48       3.185  24.925   5.885  1.00 15.12           C  
ANISOU  437  CG2 VAL A  48     1307   1720   2715    309     29     55       C  
ATOM    438  N   ILE A  49       4.978  20.598   6.130  1.00 10.79           N  
ANISOU  438  N   ILE A  49      685   1446   1966   -136    -72      1       N  
ATOM    439  CA  ILE A  49       4.886  19.148   6.154  1.00 10.70           C  
ANISOU  439  CA  ILE A  49      263   1599   2203   -104     77   -100       C  
ATOM    440  C   ILE A  49       3.942  18.792   7.264  1.00 10.43           C  
ANISOU  440  C   ILE A  49      263   1457   2242    -88    -30     52       C  
ATOM    441  O   ILE A  49       3.973  19.349   8.380  1.00 11.05           O  
ANISOU  441  O   ILE A  49      429   1602   2166   -103     -2    -61       O  
ATOM    442  CB  ILE A  49       6.254  18.506   6.428  1.00 11.76           C  
ANISOU  442  CB  ILE A  49      332   1779   2358   -285    251   -111       C  
ATOM    443  CG1 ILE A  49       7.318  18.955   5.482  1.00 12.28           C  
ANISOU  443  CG1 ILE A  49      261   1833   2568   -110     48   -136       C  
ATOM    444  CG2 ILE A  49       6.191  16.996   6.544  1.00 12.72           C  
ANISOU  444  CG2 ILE A  49      974   1631   2226     87    -81     -6       C  
ATOM    445  CD1 ILE A  49       8.656  18.721   5.843  1.00 17.03           C  
ANISOU  445  CD1 ILE A  49      345   2968   3157   -490     34    408       C  
ATOM    446  N   THR A  50       3.036  17.859   7.004  1.00 10.85           N  
ANISOU  446  N   THR A  50      479   1516   2125    -28     86    -32       N  
ATOM    447  CA  THR A  50       2.074  17.325   7.972  1.00 11.29           C  
ANISOU  447  CA  THR A  50      633   1484   2173   -284     18    -72       C  
ATOM    448  C   THR A  50       2.346  15.807   8.164  1.00 11.15           C  
ANISOU  448  C   THR A  50      624   1469   2142    -61     72    -86       C  
ATOM    449  O   THR A  50       2.434  15.064   7.188  1.00 12.41           O  
ANISOU  449  O   THR A  50     1155   1443   2116   -193     19      5       O  
ATOM    450  CB  THR A  50       0.638  17.596   7.609  1.00 12.16           C  
ANISOU  450  CB  THR A  50      388   1717   2515   -444     -4    -36       C  
ATOM    451  OG1 THR A  50       0.441  19.014   7.481  1.00 13.67           O  
ANISOU  451  OG1 THR A  50      789   1812   2591    -62    -82    -27       O  
ATOM    452  CG2 THR A  50      -0.347  17.044   8.598  1.00 14.93           C  
ANISOU  452  CG2 THR A  50      370   2109   3194   -374    166   -294       C  
ATOM    453  N   ILE A  51       2.444  15.391   9.407  1.00 10.76           N  
ANISOU  453  N   ILE A  51      700   1312   2075   -177     24    -44       N  
ATOM    454  CA  ILE A  51       2.579  13.958   9.788  1.00 11.41           C  
ANISOU  454  CA  ILE A  51      580   1483   2271   -341     63    -82       C  
ATOM    455  C   ILE A  51       1.393  13.653  10.704  1.00 11.36           C  
ANISOU  455  C   ILE A  51      503   1532   2279   -127    -33    -16       C  
ATOM    456  O   ILE A  51       1.300  14.213  11.830  1.00 12.48           O  
ANISOU  456  O   ILE A  51     1103   1490   2148    -69    164   -111       O  
ATOM    457  CB  ILE A  51       3.906  13.656  10.437  1.00 11.56           C  
ANISOU  457  CB  ILE A  51      572   1377   2440    -83    -65   -157       C  
ATOM    458  CG1 ILE A  51       5.100  14.039   9.595  1.00 13.19           C  
ANISOU  458  CG1 ILE A  51      663   1609   2738   -411    267   -264       C  
ATOM    459  CG2 ILE A  51       3.966  12.162  10.857  1.00 13.65           C  
ANISOU  459  CG2 ILE A  51      905   1566   2713     55    142    137       C  
ATOM    460  CD1 ILE A  51       6.461  13.786  10.189  1.00 14.63           C  
ANISOU  460  CD1 ILE A  51      255   2263   3038    -61    -18   -181       C  
ATOM    461  N   LYS A  52       0.450  12.837  10.245  1.00 11.62           N  
ANISOU  461  N   LYS A  52      450   1667   2297   -249    199    -76       N  
ATOM    462  CA ALYS A  52      -0.723  12.420  10.950  0.50 13.02           C  
ANISOU  462  CA ALYS A  52      811   1663   2473   -173    271   -167       C  
ATOM    463  CA BLYS A  52      -0.689  12.364  11.032  0.50 13.38           C  
ANISOU  463  CA BLYS A  52      930   1697   2456   -141    347   -161       C  
ATOM    464  C   LYS A  52      -0.499  10.931  11.347  1.00 13.96           C  
ANISOU  464  C   LYS A  52     1271   1615   2417   -245    330   -105       C  
ATOM    465  O   LYS A  52      -0.115  10.133  10.502  1.00 16.77           O  
ANISOU  465  O   LYS A  52     2427   1623   2319   -359    483      3       O  
ATOM    466  CB ALYS A  52      -1.958  12.635  10.055  0.50 14.10           C  
ANISOU  466  CB ALYS A  52      745   1938   2671   -306    149    -30       C  
ATOM    467  CB BLYS A  52      -2.035  12.377  10.338  0.50 13.65           C  
ANISOU  467  CB BLYS A  52      568   2010   2605   -123    311    -60       C  
ATOM    468  CG ALYS A  52      -3.305  12.395  10.693  0.50 14.93           C  
ANISOU  468  CG ALYS A  52      581   2051   3039    -33    -36     22       C  
ATOM    469  CG BLYS A  52      -2.409  13.649   9.822  0.50 17.38           C  
ANISOU  469  CG BLYS A  52     1429   2201   2972    -68    327    -85       C  
ATOM    470  CD ALYS A  52      -4.403  12.486   9.663  0.50 18.60           C  
ANISOU  470  CD ALYS A  52     1133   2584   3348     98    -95    271       C  
ATOM    471  CD BLYS A  52      -3.685  13.562   9.105  0.50 20.56           C  
ANISOU  471  CD BLYS A  52     1906   2964   2941   -108    -52     26       C  
ATOM    472  CE ALYS A  52      -5.765  12.558  10.304  0.50 20.42           C  
ANISOU  472  CE ALYS A  52     1170   3100   3485    260    -16    226       C  
ATOM    473  CE BLYS A  52      -3.936  14.878   8.469  0.50 22.45           C  
ANISOU  473  CE BLYS A  52     2217   3195   3116   -147   -122    216       C  
ATOM    474  NZ ALYS A  52      -6.823  12.603   9.287  0.50 24.12           N  
ANISOU  474  NZ ALYS A  52      995   3844   4324     63   -266    201       N  
ATOM    475  NZ BLYS A  52      -3.088  15.017   7.272  0.50 22.34           N  
ANISOU  475  NZ BLYS A  52     1928   3436   3123     85     -2    385       N  
ATOM    476  N   SER A  53      -0.766  10.595  12.601  1.00 13.40           N  
ANISOU  476  N   SER A  53     1208   1604   2279   -251    286      3       N  
ATOM    477  CA  SER A  53      -0.790   9.234  13.059  1.00 14.25           C  
ANISOU  477  CA  SER A  53     1281   1742   2390   -226    433    -49       C  
ATOM    478  C   SER A  53      -2.194   8.872  13.492  1.00 14.41           C  
ANISOU  478  C   SER A  53     1374   1723   2376   -378    364    -79       C  
ATOM    479  O   SER A  53      -2.751   9.519  14.362  1.00 17.03           O  
ANISOU  479  O   SER A  53     1789   2031   2648   -556    622    -61       O  
ATOM    480  CB  SER A  53       0.159   9.070  14.224  1.00 16.16           C  
ANISOU  480  CB  SER A  53     1730   1782   2625   -260    333     33       C  
ATOM    481  OG  SER A  53       0.128   7.725  14.700  1.00 17.99           O  
ANISOU  481  OG  SER A  53     1961   2088   2784   -225    239     84       O  
ATOM    482  N   GLU A  54      -2.741   7.852  12.850  1.00 15.35           N  
ANISOU  482  N   GLU A  54     1420   2035   2375   -418    370   -142       N  
ATOM    483  CA  GLU A  54      -4.116   7.376  13.120  1.00 15.22           C  
ANISOU  483  CA  GLU A  54     1101   2108   2572   -232    318     63       C  
ATOM    484  C   GLU A  54      -3.999   6.045  13.791  1.00 15.14           C  
ANISOU  484  C   GLU A  54      902   2228   2622   -168    355    189       C  
ATOM    485  O   GLU A  54      -3.388   5.096  13.257  1.00 15.09           O  
ANISOU  485  O   GLU A  54     1150   2008   2573     14    207    347       O  
ATOM    486  CB  GLU A  54      -4.899   7.225  11.822  1.00 17.48           C  
ANISOU  486  CB  GLU A  54     1459   2364   2818   -278    299    132       C  
ATOM    487  CG  GLU A  54      -5.103   8.496  11.033  1.00 22.65           C  
ANISOU  487  CG  GLU A  54     2503   2814   3286   -204    257    332       C  
ATOM    488  CD  GLU A  54      -6.147   8.336   9.949  1.00 27.27           C  
ANISOU  488  CD  GLU A  54     2903   3557   3900    -19    -16    420       C  
ATOM    489  OE1 GLU A  54      -6.123   7.301   9.257  1.00 29.08           O  
ANISOU  489  OE1 GLU A  54     3178   4327   3542    -69   -585     33       O  
ATOM    490  OE2 GLU A  54      -7.024   9.225   9.780  1.00 33.54           O  
ANISOU  490  OE2 GLU A  54     3333   4209   5200    129    -72    225       O  
ATOM    491  N   SER A  55      -4.410   6.010  15.039  1.00 15.09           N  
ANISOU  491  N   SER A  55      545   2461   2728    -12     49    235       N  
ATOM    492  CA  SER A  55      -4.103   4.958  15.942  1.00 16.94           C  
ANISOU  492  CA  SER A  55      954   2513   2969     90    262    265       C  
ATOM    493  C   SER A  55      -5.243   4.541  16.824  1.00 17.00           C  
ANISOU  493  C   SER A  55     1327   2352   2779    231    346    291       C  
ATOM    494  O   SER A  55      -6.061   5.320  17.166  1.00 16.69           O  
ANISOU  494  O   SER A  55     1293   2228   2820    502    565    564       O  
ATOM    495  CB  SER A  55      -2.970   5.523  16.782  1.00 18.30           C  
ANISOU  495  CB  SER A  55     1249   2546   3155   -144    324    393       C  
ATOM    496  OG  SER A  55      -2.639   4.584  17.764  1.00 17.67           O  
ANISOU  496  OG  SER A  55     1059   2681   2973    168    174    691       O  
ATOM    497  N   THR A  56      -5.297   3.271  17.184  1.00 17.32           N  
ANISOU  497  N   THR A  56     1633   2142   2804    407    335    214       N  
ATOM    498  CA  THR A  56      -6.181   2.781  18.224  1.00 18.81           C  
ANISOU  498  CA  THR A  56     2187   2040   2919   -106    344     97       C  
ATOM    499  C   THR A  56      -5.800   3.289  19.602  1.00 17.33           C  
ANISOU  499  C   THR A  56     2124   1834   2627    -49    502    139       C  
ATOM    500  O   THR A  56      -6.586   3.204  20.520  1.00 21.25           O  
ANISOU  500  O   THR A  56     2501   2637   2934   -647    690    -10       O  
ATOM    501  CB  THR A  56      -6.114   1.221  18.234  1.00 18.02           C  
ANISOU  501  CB  THR A  56     1489   2268   3089   -131    353   -152       C  
ATOM    502  OG1 THR A  56      -4.718   0.853  18.241  1.00 18.54           O  
ANISOU  502  OG1 THR A  56     1988   2232   2821    -50    255    -20       O  
ATOM    503  CG2 THR A  56      -6.837   0.685  16.944  1.00 20.24           C  
ANISOU  503  CG2 THR A  56     1569   2721   3397   -288   -236   -297       C  
ATOM    504  N  APHE A  57      -4.581   3.755  19.787  0.50 17.53           N  
ANISOU  504  N  APHE A  57     2188   1890   2581    -53    468    214       N  
ATOM    505  N  BPHE A  57      -4.577   3.760  19.780  0.50 17.48           N  
ANISOU  505  N  BPHE A  57     2188   1893   2560    -68    441    190       N  
ATOM    506  CA APHE A  57      -4.174   4.342  21.070  0.50 17.81           C  
ANISOU  506  CA APHE A  57     2218   1939   2610     92    417    280       C  
ATOM    507  CA BPHE A  57      -4.128   4.331  21.064  0.50 17.69           C  
ANISOU  507  CA BPHE A  57     2214   1941   2564     51    358    238       C  
ATOM    508  C  APHE A  57      -4.548   5.817  21.047  0.50 17.97           C  
ANISOU  508  C  APHE A  57     2109   1952   2764    122    501    296       C  
ATOM    509  C  BPHE A  57      -4.477   5.809  21.079  0.50 17.45           C  
ANISOU  509  C  BPHE A  57     2087   1884   2657     49    408    192       C  
ATOM    510  O  APHE A  57      -5.350   6.261  21.830  0.50 19.16           O  
ANISOU  510  O  APHE A  57     2051   2157   3071     34    752    400       O  
ATOM    511  O  BPHE A  57      -5.500   6.183  21.597  0.50 18.52           O  
ANISOU  511  O  BPHE A  57     2035   2101   2901    -24    600    203       O  
ATOM    512  CB APHE A  57      -2.673   4.131  21.303  0.50 18.22           C  
ANISOU  512  CB APHE A  57     2310   1924   2685    267    326    362       C  
ATOM    513  CB BPHE A  57      -2.627   4.091  21.262  0.50 18.46           C  
ANISOU  513  CB BPHE A  57     2361   1989   2664    212    284    349       C  
ATOM    514  CG APHE A  57      -2.109   4.900  22.449  0.50 20.99           C  
ANISOU  514  CG APHE A  57     2913   2130   2931    251    102    397       C  
ATOM    515  CG BPHE A  57      -1.990   4.944  22.311  0.50 21.40           C  
ANISOU  515  CG BPHE A  57     2948   2252   2929    197     95    384       C  
ATOM    516  CD1APHE A  57      -2.626   4.773  23.712  0.50 22.76           C  
ANISOU  516  CD1APHE A  57     3554   2196   2896    131     89    349       C  
ATOM    517  CD1BPHE A  57      -0.830   5.632  22.029  0.50 21.80           C  
ANISOU  517  CD1BPHE A  57     3050   2267   2965    227    140    378       C  
ATOM    518  CD2APHE A  57      -1.031   5.735  22.260  0.50 20.11           C  
ANISOU  518  CD2APHE A  57     2665   2045   2931    352      2    421       C  
ATOM    519  CD2BPHE A  57      -2.532   5.054  23.569  0.50 22.64           C  
ANISOU  519  CD2BPHE A  57     3393   2374   2834    100     81    431       C  
ATOM    520  CE1APHE A  57      -2.081   5.509  24.780  0.50 24.51           C  
ANISOU  520  CE1APHE A  57     3646   2648   3016    -12    -82    343       C  
ATOM    521  CE1BPHE A  57      -0.206   6.418  22.973  0.50 24.27           C  
ANISOU  521  CE1BPHE A  57     3516   2534   3168    130     63    364       C  
ATOM    522  CE2APHE A  57      -0.488   6.449  23.310  0.50 24.17           C  
ANISOU  522  CE2APHE A  57     3515   2486   3183    291   -117    398       C  
ATOM    523  CE2BPHE A  57      -1.919   5.869  24.539  0.50 23.00           C  
ANISOU  523  CE2BPHE A  57     3408   2423   2908   -159    -22    502       C  
ATOM    524  CZ APHE A  57      -1.023   6.342  24.563  0.50 24.60           C  
ANISOU  524  CZ APHE A  57     3563   2607   3176    193   -166    393       C  
ATOM    525  CZ BPHE A  57      -0.755   6.547  24.226  0.50 22.93           C  
ANISOU  525  CZ BPHE A  57     3519   2227   2966     99     20    515       C  
ATOM    526  N  ALYS A  58      -3.972   6.585  20.140  0.50 17.70           N  
ANISOU  526  N  ALYS A  58     1959   2093   2674    151    620    303       N  
ATOM    527  N  BLYS A  58      -3.637   6.666  20.518  0.50 16.19           N  
ANISOU  527  N  BLYS A  58     1877   1886   2387     -5    314    117       N  
ATOM    528  CA ALYS A  58      -4.166   8.045  20.116  0.50 17.23           C  
ANISOU  528  CA ALYS A  58     1768   2137   2638    211    469    215       C  
ATOM    529  CA BLYS A  58      -3.936   8.104  20.509  0.50 15.20           C  
ANISOU  529  CA BLYS A  58     1543   1902   2329      9    233    -64       C  
ATOM    530  C  ALYS A  58      -3.896   8.519  18.706  0.50 17.03           C  
ANISOU  530  C  ALYS A  58     1649   2226   2592    195    611    256       C  
ATOM    531  C  BLYS A  58      -3.596   8.739  19.168  0.50 14.48           C  
ANISOU  531  C  BLYS A  58     1452   1748   2302    -87    225    -54       C  
ATOM    532  O  ALYS A  58      -2.868   8.145  18.142  0.50 20.31           O  
ANISOU  532  O  ALYS A  58     1875   2854   2988    362    569    292       O  
ATOM    533  O  BLYS A  58      -2.465   8.645  18.726  0.50 13.37           O  
ANISOU  533  O  BLYS A  58     1348   1739   1994   -186    165   -185       O  
ATOM    534  CB ALYS A  58      -3.189   8.724  21.100  0.50 17.38           C  
ANISOU  534  CB ALYS A  58     1638   2190   2773    142    387    172       C  
ATOM    535  CB BLYS A  58      -3.193   8.798  21.668  0.50 14.72           C  
ANISOU  535  CB BLYS A  58     1201   1878   2513      1    225   -169       C  
ATOM    536  CG ALYS A  58      -3.413  10.214  21.435  0.50 17.96           C  
ANISOU  536  CG ALYS A  58     1812   2250   2763      7    122    113       C  
ATOM    537  CG BLYS A  58      -3.854   8.578  23.000  0.50 20.14           C  
ANISOU  537  CG BLYS A  58     2078   2743   2827    -91    251     27       C  
ATOM    538  CD ALYS A  58      -4.770  10.577  22.007  0.50 19.76           C  
ANISOU  538  CD ALYS A  58     1743   2860   2904    114   -105    -63       C  
ATOM    539  CD BLYS A  58      -3.375   9.549  24.051  0.50 23.04           C  
ANISOU  539  CD BLYS A  58     2613   2930   3210     -4    408   -117       C  
ATOM    540  CE ALYS A  58      -4.819  12.036  22.383  0.50 21.09           C  
ANISOU  540  CE ALYS A  58     1848   3145   3018    230    136   -160       C  
ATOM    541  CE BLYS A  58      -2.947   8.791  25.312  0.50 23.37           C  
ANISOU  541  CE BLYS A  58     2608   3156   3114     -1    438   -127       C  
ATOM    542  NZ ALYS A  58      -6.180  12.549  22.335  0.50 24.91           N  
ANISOU  542  NZ ALYS A  58     2331   3684   3448    232    151   -112       N  
ATOM    543  NZ BLYS A  58      -1.974   9.457  26.214  0.50 21.78           N  
ANISOU  543  NZ BLYS A  58     2435   2730   3108   -277    869   -136       N  
ATOM    544  N  AASN A  59      -4.763   9.363  18.157  0.50 16.28           N  
ANISOU  544  N  AASN A  59     1456   2124   2603     67    635    202       N  
ATOM    545  N  BASN A  59      -4.581   9.344  18.513  0.50 13.79           N  
ANISOU  545  N  BASN A  59     1251   1731   2256    -35    341     70       N  
ATOM    546  CA AASN A  59      -4.535  10.050  16.887  0.50 16.02           C  
ANISOU  546  CA AASN A  59     1529   1930   2625    -23    558     75       C  
ATOM    547  CA BASN A  59      -4.400  10.060  17.259  0.50 14.78           C  
ANISOU  547  CA BASN A  59     1523   1663   2427     37    329    -31       C  
ATOM    548  C  AASN A  59      -3.774  11.354  17.179  0.50 16.67           C  
ANISOU  548  C  AASN A  59     1692   1930   2710    -87    453     21       C  
ATOM    549  C  BASN A  59      -3.497  11.259  17.476  0.50 15.15           C  
ANISOU  549  C  BASN A  59     1521   1730   2503     15    324     55       C  
ATOM    550  O  AASN A  59      -4.201  12.134  18.045  0.50 17.25           O  
ANISOU  550  O  AASN A  59     1753   1946   2853    -26    527    -65       O  
ATOM    551  O  BASN A  59      -3.613  11.944  18.525  0.50 14.92           O  
ANISOU  551  O  BASN A  59     1535   1674   2458    151    238     75       O  
ATOM    552  CB AASN A  59      -5.856  10.308  16.167  0.50 16.66           C  
ANISOU  552  CB AASN A  59     1685   1995   2648   -139    478    118       C  
ATOM    553  CB BASN A  59      -5.737  10.583  16.748  0.50 15.16           C  
ANISOU  553  CB BASN A  59     1686   1670   2402     46    195    112       C  
ATOM    554  CG AASN A  59      -6.678   9.055  15.976  0.50 17.91           C  
ANISOU  554  CG AASN A  59     1374   2320   3109   -226    483     83       C  
ATOM    555  CG BASN A  59      -6.613   9.517  16.157  0.50 16.77           C  
ANISOU  555  CG BASN A  59     1373   2116   2880    -28    283   -103       C  
ATOM    556  OD1AASN A  59      -6.242   8.090  15.347  0.50 19.12           O  
ANISOU  556  OD1AASN A  59     1648   2605   3010    278    448    153       O  
ATOM    557  OD1BASN A  59      -6.162   8.416  15.842  0.50 14.70           O  
ANISOU  557  OD1BASN A  59      869   1929   2787   -182    146    -16       O  
ATOM    558  ND2AASN A  59      -7.906   9.075  16.495  0.50 19.33           N  
ANISOU  558  ND2AASN A  59     1125   2931   3285   -679    351    517       N  
ATOM    559  ND2BASN A  59      -7.892   9.838  15.996  0.50 21.16           N  
ANISOU  559  ND2BASN A  59     1545   2641   3853    722    346      0       N  
ATOM    560  N   THR A  60      -2.651  11.569  16.488  1.00 14.67           N  
ANISOU  560  N   THR A  60     1327   1742   2503    -14    477    -27       N  
ATOM    561  CA  THR A  60      -1.828  12.781  16.586  1.00 15.23           C  
ANISOU  561  CA  THR A  60     1649   1653   2481    -67    369    -47       C  
ATOM    562  C   THR A  60      -1.707  13.391  15.191  1.00 14.53           C  
ANISOU  562  C   THR A  60     1379   1661   2480     13    410    -10       C  
ATOM    563  O   THR A  60      -1.804  12.710  14.170  1.00 14.11           O  
ANISOU  563  O   THR A  60     1098   1721   2542   -164    347     20       O  
ATOM    564  CB  THR A  60      -0.440  12.526  17.150  1.00 15.74           C  
ANISOU  564  CB  THR A  60     1676   1873   2431    -18    226     56       C  
ATOM    565  OG1 THR A  60       0.291  11.680  16.281  1.00 16.41           O  
ANISOU  565  OG1 THR A  60     1691   1885   2656    -73    214     84       O  
ATOM    566  CG2 THR A  60      -0.444  11.948  18.576  1.00 16.95           C  
ANISOU  566  CG2 THR A  60     1469   2359   2611    190    159    199       C  
ATOM    567  N   GLU A  61      -1.432  14.685  15.148  1.00 14.45           N  
ANISOU  567  N   GLU A  61     1458   1559   2470   -109    537    -56       N  
ATOM    568  CA  GLU A  61      -1.190  15.394  13.869  1.00 13.96           C  
ANISOU  568  CA  GLU A  61      945   1746   2611    -58    402    -19       C  
ATOM    569  C   GLU A  61      -0.264  16.541  14.188  1.00 13.94           C  
ANISOU  569  C   GLU A  61     1066   1607   2623   -249    355   -152       C  
ATOM    570  O   GLU A  61      -0.509  17.342  15.156  1.00 16.28           O  
ANISOU  570  O   GLU A  61     1671   1708   2805   -208    647   -221       O  
ATOM    571  CB  GLU A  61      -2.482  15.863  13.285  1.00 15.15           C  
ANISOU  571  CB  GLU A  61      902   1991   2862    -74    233    -55       C  
ATOM    572  CG  GLU A  61      -2.340  16.632  11.999  1.00 19.49           C  
ANISOU  572  CG  GLU A  61      758   3105   3540    -86    518    316       C  
ATOM    573  CD  GLU A  61      -3.605  17.159  11.438  1.00 25.79           C  
ANISOU  573  CD  GLU A  61      647   4501   4648     99    482    237       C  
ATOM    574  OE1 GLU A  61      -3.498  18.001  10.530  1.00 33.86           O  
ANISOU  574  OE1 GLU A  61     2671   4783   5410   -626    127    626       O  
ATOM    575  OE2 GLU A  61      -4.688  16.778  11.877  1.00 31.84           O  
ANISOU  575  OE2 GLU A  61     1209   5229   5659   -125   -163    553       O  
ATOM    576  N   ILE A  62       0.844  16.630  13.481  1.00 12.11           N  
ANISOU  576  N   ILE A  62      741   1520   2339   -143    195   -123       N  
ATOM    577  CA  ILE A  62       1.761  17.745  13.570  1.00 12.25           C  
ANISOU  577  CA  ILE A  62      854   1560   2237   -274    102   -145       C  
ATOM    578  C   ILE A  62       1.915  18.327  12.171  1.00 12.04           C  
ANISOU  578  C   ILE A  62      960   1573   2040   -190     51   -124       C  
ATOM    579  O   ILE A  62       2.024  17.610  11.193  1.00 13.31           O  
ANISOU  579  O   ILE A  62     1655   1391   2009   -200     88      4       O  
ATOM    580  CB  ILE A  62       3.122  17.383  14.210  1.00 12.73           C  
ANISOU  580  CB  ILE A  62      903   1741   2192   -349     66   -106       C  
ATOM    581  CG1 ILE A  62       3.832  16.278  13.452  1.00 12.93           C  
ANISOU  581  CG1 ILE A  62      780   1819   2311   -344    -23   -132       C  
ATOM    582  CG2 ILE A  62       2.903  16.978  15.681  1.00 15.20           C  
ANISOU  582  CG2 ILE A  62     1616   2020   2138     97     49    100       C  
ATOM    583  CD1 ILE A  62       5.291  16.006  13.929  1.00 15.91           C  
ANISOU  583  CD1 ILE A  62     1039   2169   2834   -349    -74   -223       C  
ATOM    584  N   SER A  63       1.993  19.646  12.110  1.00 11.28           N  
ANISOU  584  N   SER A  63      798   1475   2011    -22    -33    -75       N  
ATOM    585  CA  SER A  63       2.323  20.383  10.898  1.00 11.06           C  
ANISOU  585  CA  SER A  63      566   1550   2085    -63     49    -87       C  
ATOM    586  C   SER A  63       3.456  21.333  11.229  1.00 10.88           C  
ANISOU  586  C   SER A  63      261   1566   2305    -53    111   -109       C  
ATOM    587  O   SER A  63       3.462  21.949  12.307  1.00 12.66           O  
ANISOU  587  O   SER A  63      872   1658   2279   -212    306   -247       O  
ATOM    588  CB  SER A  63       1.190  21.154  10.299  1.00 12.26           C  
ANISOU  588  CB  SER A  63      918   1602   2137     91     15    -74       C  
ATOM    589  OG  SER A  63       0.123  20.311   9.864  1.00 14.06           O  
ANISOU  589  OG  SER A  63      795   1993   2553     47   -134     49       O  
ATOM    590  N   PHE A  64       4.453  21.442  10.381  1.00 10.04           N  
ANISOU  590  N   PHE A  64      332   1393   2088    -10    -88   -125       N  
ATOM    591  CA  PHE A  64       5.657  22.143  10.686  1.00 10.64           C  
ANISOU  591  CA  PHE A  64      294   1550   2195   -113    -10    -17       C  
ATOM    592  C   PHE A  64       6.376  22.579   9.407  1.00 10.64           C  
ANISOU  592  C   PHE A  64      378   1511   2153    178    -84     27       C  
ATOM    593  O   PHE A  64       6.164  22.035   8.329  1.00 11.05           O  
ANISOU  593  O   PHE A  64      623   1498   2077   -132     22    -20       O  
ATOM    594  CB  PHE A  64       6.598  21.322  11.589  1.00 11.23           C  
ANISOU  594  CB  PHE A  64      480   1521   2263    -82   -153      0       C  
ATOM    595  CG  PHE A  64       6.945  19.989  10.967  1.00 11.39           C  
ANISOU  595  CG  PHE A  64      568   1563   2193   -114   -190     39       C  
ATOM    596  CD1 PHE A  64       6.164  18.912  11.134  1.00 11.61           C  
ANISOU  596  CD1 PHE A  64      473   1710   2227   -141    -36    -20       C  
ATOM    597  CD2 PHE A  64       8.081  19.862  10.232  1.00 11.38           C  
ANISOU  597  CD2 PHE A  64      588   1624   2111   -119    -18     42       C  
ATOM    598  CE1 PHE A  64       6.399  17.712  10.493  1.00 12.38           C  
ANISOU  598  CE1 PHE A  64      579   1754   2371    -11   -200     81       C  
ATOM    599  CE2 PHE A  64       8.343  18.657   9.613  1.00 12.87           C  
ANISOU  599  CE2 PHE A  64      821   1837   2228    189     15     46       C  
ATOM    600  CZ  PHE A  64       7.528  17.558   9.826  1.00 12.97           C  
ANISOU  600  CZ  PHE A  64     1017   1500   2409    110   -357    -31       C  
ATOM    601  N   ILE A  65       7.284  23.532   9.573  1.00 11.18           N  
ANISOU  601  N   ILE A  65      313   1542   2393   -188    -89   -191       N  
ATOM    602  CA  ILE A  65       8.267  23.958   8.594  1.00 11.23           C  
ANISOU  602  CA  ILE A  65      258   1468   2541    -38     95   -142       C  
ATOM    603  C   ILE A  65       9.641  23.535   9.074  1.00 10.73           C  
ANISOU  603  C   ILE A  65      421   1296   2359   -103    271      5       C  
ATOM    604  O   ILE A  65       9.918  23.658  10.263  1.00 10.75           O  
ANISOU  604  O   ILE A  65      466   1385   2232   -109     -8    -57       O  
ATOM    605  CB  ILE A  65       8.149  25.471   8.358  1.00 12.32           C  
ANISOU  605  CB  ILE A  65      706   1428   2544    -75     81    -54       C  
ATOM    606  CG1 ILE A  65       6.743  25.795   7.801  1.00 13.37           C  
ANISOU  606  CG1 ILE A  65      553   1693   2832    -69     92    -14       C  
ATOM    607  CG2 ILE A  65       9.216  25.959   7.448  1.00 12.94           C  
ANISOU  607  CG2 ILE A  65      557   1669   2688    -79   -135    157       C  
ATOM    608  CD1 ILE A  65       6.499  27.334   7.708  1.00 16.08           C  
ANISOU  608  CD1 ILE A  65      895   1853   3361    220   -155    156       C  
ATOM    609  N   LEU A  66      10.441  22.974   8.212  1.00 11.11           N  
ANISOU  609  N   LEU A  66      668   1404   2149    116    -32     65       N  
ATOM    610  CA  LEU A  66      11.733  22.503   8.591  1.00 11.64           C  
ANISOU  610  CA  LEU A  66      808   1316   2295    166     -7     37       C  
ATOM    611  C   LEU A  66      12.560  23.611   9.255  1.00 11.49           C  
ANISOU  611  C   LEU A  66      651   1297   2416    -51     -1     10       C  
ATOM    612  O   LEU A  66      12.625  24.743   8.736  1.00 12.05           O  
ANISOU  612  O   LEU A  66      765   1361   2452    -57    -86    112       O  
ATOM    613  CB  LEU A  66      12.496  21.895   7.383  1.00 12.33           C  
ANISOU  613  CB  LEU A  66      571   1489   2624    126    -46     80       C  
ATOM    614  CG  LEU A  66      11.896  20.658   6.741  1.00 13.11           C  
ANISOU  614  CG  LEU A  66     1155   1482   2343    158    -89   -155       C  
ATOM    615  CD1 LEU A  66      12.542  20.342   5.391  1.00 18.02           C  
ANISOU  615  CD1 LEU A  66     2084   2197   2563     74     85   -238       C  
ATOM    616  CD2 LEU A  66      11.939  19.505   7.700  1.00 13.85           C  
ANISOU  616  CD2 LEU A  66      851   1663   2745     16   -425   -211       C  
ATOM    617  N   GLY A  67      13.214  23.288  10.356  1.00 11.35           N  
ANISOU  617  N   GLY A  67      654   1361   2297   -145    -94    140       N  
ATOM    618  CA  GLY A  67      14.049  24.216  11.084  1.00 11.99           C  
ANISOU  618  CA  GLY A  67      787   1436   2330   -125    -45     18       C  
ATOM    619  C   GLY A  67      13.287  25.121  12.043  1.00 11.29           C  
ANISOU  619  C   GLY A  67      510   1439   2338   -164     62    210       C  
ATOM    620  O   GLY A  67      14.023  25.875  12.744  1.00 12.31           O  
ANISOU  620  O   GLY A  67      403   1607   2666   -194   -125     32       O  
ATOM    621  N   GLN A  68      11.990  25.078  12.090  1.00 10.75           N  
ANISOU  621  N   GLN A  68      283   1354   2448   -180     18    -75       N  
ATOM    622  CA  GLN A  68      11.195  26.051  12.863  1.00 11.37           C  
ANISOU  622  CA  GLN A  68      482   1194   2643   -148    -34   -153       C  
ATOM    623  C   GLN A  68      10.501  25.329  14.001  1.00 10.65           C  
ANISOU  623  C   GLN A  68      254   1276   2516    -33     20    -44       C  
ATOM    624  O   GLN A  68       9.594  24.529  13.819  1.00 11.28           O  
ANISOU  624  O   GLN A  68      269   1416   2600   -132    -25   -163       O  
ATOM    625  CB  GLN A  68      10.191  26.746  11.930  1.00 12.60           C  
ANISOU  625  CB  GLN A  68      943   1111   2731     40   -215   -157       C  
ATOM    626  CG  GLN A  68      11.003  27.447  10.796  1.00 14.91           C  
ANISOU  626  CG  GLN A  68     1212   1567   2885   -266   -566    -39       C  
ATOM    627  CD  GLN A  68      10.266  28.435  10.006  1.00 15.87           C  
ANISOU  627  CD  GLN A  68     1171   1603   3255    -28   -543     44       C  
ATOM    628  OE1 GLN A  68       9.085  28.729  10.229  1.00 19.24           O  
ANISOU  628  OE1 GLN A  68     1429   1799   4080     91  -1058    172       O  
ATOM    629  NE2 GLN A  68      10.994  28.981   9.015  1.00 18.22           N  
ANISOU  629  NE2 GLN A  68     2239   1671   3010   -246   -474    232       N  
ATOM    630  N   GLU A  69      10.833  25.712  15.237  1.00 11.58           N  
ANISOU  630  N   GLU A  69      777   1254   2367     40    -95    -77       N  
ATOM    631  CA  GLU A  69      10.326  25.056  16.419  1.00 11.85           C  
ANISOU  631  CA  GLU A  69      730   1363   2408     30   -266     39       C  
ATOM    632  C   GLU A  69       8.845  25.230  16.573  1.00 11.07           C  
ANISOU  632  C   GLU A  69      507   1433   2263     25   -161    -74       C  
ATOM    633  O   GLU A  69       8.296  26.284  16.220  1.00 12.25           O  
ANISOU  633  O   GLU A  69      571   1434   2648     81   -102    -50       O  
ATOM    634  CB  GLU A  69      11.070  25.658  17.628  1.00 13.76           C  
ANISOU  634  CB  GLU A  69      468   2163   2594    -56   -123    230       C  
ATOM    635  CG  GLU A  69      10.707  25.090  18.992  1.00 18.64           C  
ANISOU  635  CG  GLU A  69     1613   2575   2891    -14   -189     43       C  
ATOM    636  CD  GLU A  69      11.564  25.744  20.054  1.00 26.19           C  
ANISOU  636  CD  GLU A  69     3240   3562   3146   -431   -340    -88       C  
ATOM    637  OE1 GLU A  69      11.488  27.004  20.241  1.00 31.72           O  
ANISOU  637  OE1 GLU A  69     3845   4214   3991   -610   -754   -732       O  
ATOM    638  OE2 GLU A  69      12.313  24.986  20.682  1.00 29.57           O  
ANISOU  638  OE2 GLU A  69     3297   4710   3225   -472   -627      4       O  
ATOM    639  N   PHE A  70       8.188  24.213  17.133  1.00 10.68           N  
ANISOU  639  N   PHE A  70      549   1329   2179    149   -188   -113       N  
ATOM    640  CA  PHE A  70       6.782  24.209  17.365  1.00 10.46           C  
ANISOU  640  CA  PHE A  70      351   1408   2213    131    -66    -22       C  
ATOM    641  C   PHE A  70       6.499  23.467  18.660  1.00 10.89           C  
ANISOU  641  C   PHE A  70      322   1448   2365    223   -245    -26       C  
ATOM    642  O   PHE A  70       7.280  22.698  19.136  1.00 12.27           O  
ANISOU  642  O   PHE A  70      686   1656   2320    229      5   -138       O  
ATOM    643  CB  PHE A  70       6.024  23.629  16.165  1.00 10.90           C  
ANISOU  643  CB  PHE A  70      418   1498   2227     82     62      2       C  
ATOM    644  CG  PHE A  70       6.405  22.197  15.810  1.00 10.66           C  
ANISOU  644  CG  PHE A  70      267   1586   2196     33   -164    -39       C  
ATOM    645  CD1 PHE A  70       7.505  21.929  15.071  1.00 10.61           C  
ANISOU  645  CD1 PHE A  70      283   1438   2308    187    -23     13       C  
ATOM    646  CD2 PHE A  70       5.585  21.148  16.221  1.00 13.03           C  
ANISOU  646  CD2 PHE A  70      795   1766   2388   -286    287   -302       C  
ATOM    647  CE1 PHE A  70       7.814  20.600  14.702  1.00 11.33           C  
ANISOU  647  CE1 PHE A  70      395   1653   2256     62    -94     54       C  
ATOM    648  CE2 PHE A  70       5.859  19.853  15.888  1.00 14.10           C  
ANISOU  648  CE2 PHE A  70     1365   1658   2332   -301    378   -113       C  
ATOM    649  CZ  PHE A  70       6.969  19.577  15.169  1.00 12.83           C  
ANISOU  649  CZ  PHE A  70     1091   1659   2124    -39   -139    -40       C  
ATOM    650  N   ASP A  71       5.270  23.644  19.103  1.00 12.06           N  
ANISOU  650  N   ASP A  71      593   1653   2334    367    -86     57       N  
ATOM    651  CA  ASP A  71       4.741  22.913  20.276  1.00 13.22           C  
ANISOU  651  CA  ASP A  71      900   1780   2343    294     55     93       C  
ATOM    652  C   ASP A  71       4.036  21.670  19.808  1.00 13.97           C  
ANISOU  652  C   ASP A  71      889   1930   2489     18    -26    144       C  
ATOM    653  O   ASP A  71       3.303  21.678  18.810  1.00 14.91           O  
ANISOU  653  O   ASP A  71     1200   1834   2628    131    -57    132       O  
ATOM    654  CB  ASP A  71       3.635  23.752  20.943  1.00 14.54           C  
ANISOU  654  CB  ASP A  71     1272   2041   2211    364    144     80       C  
ATOM    655  CG  ASP A  71       4.160  24.933  21.627  1.00 16.41           C  
ANISOU  655  CG  ASP A  71     1013   2538   2683    597      7      3       C  
ATOM    656  OD1 ASP A  71       5.097  24.759  22.416  1.00 18.78           O  
ANISOU  656  OD1 ASP A  71     1696   2431   3007    484   -485   -279       O  
ATOM    657  OD2 ASP A  71       3.631  26.040  21.401  1.00 15.78           O  
ANISOU  657  OD2 ASP A  71      806   2299   2891    149   -145   -128       O  
ATOM    658  N   GLU A  72       4.236  20.571  20.546  1.00 13.43           N  
ANISOU  658  N   GLU A  72      668   1911   2522    -10     37    234       N  
ATOM    659  CA  GLU A  72       3.687  19.257  20.191  1.00 14.61           C  
ANISOU  659  CA  GLU A  72      949   2047   2554    -74     89    337       C  
ATOM    660  C   GLU A  72       3.206  18.627  21.506  1.00 14.36           C  
ANISOU  660  C   GLU A  72      683   2170   2602     48    227    312       C  
ATOM    661  O   GLU A  72       3.843  18.643  22.527  1.00 15.84           O  
ANISOU  661  O   GLU A  72      949   2455   2614   -195    200    315       O  
ATOM    662  CB  GLU A  72       4.788  18.388  19.524  1.00 13.86           C  
ANISOU  662  CB  GLU A  72      959   1825   2482     63    254    337       C  
ATOM    663  CG  GLU A  72       4.386  16.926  19.214  1.00 14.77           C  
ANISOU  663  CG  GLU A  72      572   2304   2736     42   -126    636       C  
ATOM    664  CD  GLU A  72       5.476  16.146  18.556  1.00 13.29           C  
ANISOU  664  CD  GLU A  72      536   2192   2319   -133     51    261       C  
ATOM    665  OE1 GLU A  72       6.606  16.538  18.495  1.00 14.70           O  
ANISOU  665  OE1 GLU A  72      912   2118   2554     30    127   -136       O  
ATOM    666  OE2 GLU A  72       5.131  15.005  18.069  1.00 17.33           O  
ANISOU  666  OE2 GLU A  72     1713   1918   2952   -139     73     70       O  
ATOM    667  N   VAL A  73       2.041  18.045  21.429  1.00 15.29           N  
ANISOU  667  N   VAL A  73      980   2093   2735    141    165    546       N  
ATOM    668  CA  VAL A  73       1.481  17.190  22.518  1.00 15.81           C  
ANISOU  668  CA  VAL A  73      790   2235   2981   -119     76    478       C  
ATOM    669  C   VAL A  73       1.608  15.754  22.005  1.00 16.00           C  
ANISOU  669  C   VAL A  73     1075   2293   2711      3     68    312       C  
ATOM    670  O   VAL A  73       1.017  15.374  21.025  1.00 18.14           O  
ANISOU  670  O   VAL A  73     1690   2042   3158   -126   -374    567       O  
ATOM    671  CB  VAL A  73       0.100  17.523  22.898  1.00 16.76           C  
ANISOU  671  CB  VAL A  73      590   2474   3304    -28    299    505       C  
ATOM    672  CG1 VAL A  73      -0.343  16.507  23.970  1.00 20.99           C  
ANISOU  672  CG1 VAL A  73     1302   2990   3684     50    627    686       C  
ATOM    673  CG2 VAL A  73       0.043  18.980  23.411  1.00 20.16           C  
ANISOU  673  CG2 VAL A  73      913   2633   4113    125    562    347       C  
ATOM    674  N   THR A  74       2.535  14.977  22.578  1.00 14.27           N  
ANISOU  674  N   THR A  74      707   2169   2543     51     77    201       N  
ATOM    675  CA  THR A  74       2.806  13.620  22.065  1.00 14.01           C  
ANISOU  675  CA  THR A  74      743   2236   2342   -246    -16    162       C  
ATOM    676  C   THR A  74       1.697  12.640  22.409  1.00 14.29           C  
ANISOU  676  C   THR A  74      583   2272   2572     10    -19    294       C  
ATOM    677  O   THR A  74       0.815  12.919  23.204  1.00 15.85           O  
ANISOU  677  O   THR A  74      922   2198   2899    -69    387    400       O  
ATOM    678  CB  THR A  74       4.153  13.115  22.575  1.00 13.58           C  
ANISOU  678  CB  THR A  74      606   2222   2331   -149     63    -16       C  
ATOM    679  OG1 THR A  74       4.008  12.901  23.992  1.00 14.73           O  
ANISOU  679  OG1 THR A  74     1301   2045   2249    271    183    230       O  
ATOM    680  CG2 THR A  74       5.195  14.069  22.327  1.00 13.80           C  
ANISOU  680  CG2 THR A  74      323   2218   2702     -9   -130    -90       C  
ATOM    681  N   ALA A  75       1.744  11.478  21.783  1.00 15.21           N  
ANISOU  681  N   ALA A  75      877   2252   2648     73    108    301       N  
ATOM    682  CA  ALA A  75       0.657  10.487  21.948  1.00 16.11           C  
ANISOU  682  CA  ALA A  75     1258   2315   2546   -107     25    316       C  
ATOM    683  C   ALA A  75       0.567  10.084  23.431  1.00 16.55           C  
ANISOU  683  C   ALA A  75     1241   2370   2675     13    233    325       C  
ATOM    684  O   ALA A  75      -0.504   9.802  23.914  1.00 18.73           O  
ANISOU  684  O   ALA A  75     1338   2660   3117   -275    283    373       O  
ATOM    685  CB  ALA A  75       0.989   9.289  21.091  1.00 17.66           C  
ANISOU  685  CB  ALA A  75     1616   2302   2790     13     86    348       C  
ATOM    686  N   ASP A  76       1.684  10.015  24.111  1.00 16.52           N  
ANISOU  686  N   ASP A  76     1433   2230   2613     37    271    384       N  
ATOM    687  CA  ASP A  76       1.748   9.738  25.563  1.00 16.94           C  
ANISOU  687  CA  ASP A  76     1541   2393   2502    -68    196    348       C  
ATOM    688  C   ASP A  76       1.534  10.988  26.442  1.00 18.39           C  
ANISOU  688  C   ASP A  76     1827   2560   2600     16    315    300       C  
ATOM    689  O   ASP A  76       1.731  10.929  27.660  1.00 21.39           O  
ANISOU  689  O   ASP A  76     2591   2993   2543    197    244    341       O  
ATOM    690  CB  ASP A  76       3.089   9.040  25.919  1.00 17.49           C  
ANISOU  690  CB  ASP A  76     1744   2191   2708    -12    181    333       C  
ATOM    691  CG  ASP A  76       4.289   9.869  25.633  1.00 15.62           C  
ANISOU  691  CG  ASP A  76     1413   2040   2481    101    -17    424       C  
ATOM    692  OD1 ASP A  76       4.448  10.303  24.465  1.00 16.15           O  
ANISOU  692  OD1 ASP A  76     1207   2382   2546    254     22    459       O  
ATOM    693  OD2 ASP A  76       5.091  10.106  26.552  1.00 17.88           O  
ANISOU  693  OD2 ASP A  76     1912   2093   2786    110   -157    511       O  
ATOM    694  N   ASP A  77       1.113  12.102  25.835  1.00 18.35           N  
ANISOU  694  N   ASP A  77     1898   2423   2649     41    432    348       N  
ATOM    695  CA  ASP A  77       0.695  13.337  26.545  1.00 20.02           C  
ANISOU  695  CA  ASP A  77     2152   2745   2708    -46    517    214       C  
ATOM    696  C   ASP A  77       1.831  14.132  27.181  1.00 18.94           C  
ANISOU  696  C   ASP A  77     1836   2615   2745    -49    414    128       C  
ATOM    697  O   ASP A  77       1.641  14.864  28.169  1.00 20.81           O  
ANISOU  697  O   ASP A  77     1866   2958   3083   -123    648   -127       O  
ATOM    698  CB  ASP A  77      -0.429  13.078  27.552  1.00 21.13           C  
ANISOU  698  CB  ASP A  77     2095   2989   2941   -125    464    187       C  
ATOM    699  CG  ASP A  77      -1.348  14.268  27.750  1.00 26.30           C  
ANISOU  699  CG  ASP A  77     3026   3595   3371    136    807    244       C  
ATOM    700  OD1 ASP A  77      -2.003  14.301  28.809  1.00 31.46           O  
ANISOU  700  OD1 ASP A  77     3534   4452   3966    349   1158     23       O  
ATOM    701  OD2 ASP A  77      -1.463  15.157  26.868  1.00 29.80           O  
ANISOU  701  OD2 ASP A  77     3340   3950   4032    426    855    597       O  
ATOM    702  N   ARG A  78       3.032  14.032  26.627  1.00 17.58           N  
ANISOU  702  N   ARG A  78     1826   2408   2445    123    275    202       N  
ATOM    703  CA  ARG A  78       4.064  15.008  26.963  1.00 15.73           C  
ANISOU  703  CA  ARG A  78     1391   2207   2375    279    278    249       C  
ATOM    704  C   ARG A  78       3.793  16.280  26.149  1.00 14.59           C  
ANISOU  704  C   ARG A  78     1008   2139   2396    138    273    138       C  
ATOM    705  O   ARG A  78       3.517  16.223  24.952  1.00 16.74           O  
ANISOU  705  O   ARG A  78     1759   2112   2489    425    261    147       O  
ATOM    706  CB  ARG A  78       5.427  14.509  26.657  1.00 15.82           C  
ANISOU  706  CB  ARG A  78     1538   1928   2543    257    226    353       C  
ATOM    707  CG  ARG A  78       6.009  13.395  27.598  1.00 16.60           C  
ANISOU  707  CG  ARG A  78     1718   2061   2527    247     32    364       C  
ATOM    708  CD  ARG A  78       7.353  12.845  27.040  1.00 15.79           C  
ANISOU  708  CD  ARG A  78     1639   1766   2593    192   -235    254       C  
ATOM    709  NE  ARG A  78       7.064  11.974  25.899  1.00 15.78           N  
ANISOU  709  NE  ARG A  78     1750   1777   2468    176     19    195       N  
ATOM    710  CZ  ARG A  78       7.633  12.027  24.700  1.00 14.86           C  
ANISOU  710  CZ  ARG A  78     1088   1996   2561    240   -174    -91       C  
ATOM    711  NH1 ARG A  78       8.702  12.786  24.440  1.00 15.50           N  
ANISOU  711  NH1 ARG A  78     1249   1884   2754     59    -41    -87       N  
ATOM    712  NH2 ARG A  78       7.144  11.223  23.782  1.00 15.52           N  
ANISOU  712  NH2 ARG A  78     1277   2022   2596    140    -71     33       N  
ATOM    713  N   LYS A  79       4.075  17.415  26.784  1.00 16.37           N  
ANISOU  713  N   LYS A  79     1767   2049   2400     81    486    163       N  
ATOM    714  CA  LYS A  79       4.068  18.710  26.118  1.00 16.01           C  
ANISOU  714  CA  LYS A  79     1401   2194   2486    409    360    113       C  
ATOM    715  C   LYS A  79       5.510  19.034  25.822  1.00 15.19           C  
ANISOU  715  C   LYS A  79     1278   2053   2438    320    262    122       C  
ATOM    716  O   LYS A  79       6.295  19.302  26.725  1.00 18.20           O  
ANISOU  716  O   LYS A  79     2058   2422   2434    189    308    -55       O  
ATOM    717  CB  LYS A  79       3.370  19.744  27.015  1.00 18.11           C  
ANISOU  717  CB  LYS A  79     1825   2310   2746    294    541    123       C  
ATOM    718  CG  LYS A  79       1.887  19.498  27.221  1.00 23.79           C  
ANISOU  718  CG  LYS A  79     2595   3087   3354    382    511   -121       C  
ATOM    719  CD  LYS A  79       1.554  18.367  28.106  1.00 29.46           C  
ANISOU  719  CD  LYS A  79     3324   3595   4273    311    359    112       C  
ATOM    720  CE  LYS A  79       0.144  18.453  28.613  1.00 31.91           C  
ANISOU  720  CE  LYS A  79     3627   3949   4547    177    525    242       C  
ATOM    721  NZ  LYS A  79      -0.415  17.096  28.708  1.00 32.97           N  
ANISOU  721  NZ  LYS A  79     3783   3476   5265    550    486    177       N  
ATOM    722  N   VAL A  80       5.827  19.003  24.537  1.00 13.67           N  
ANISOU  722  N   VAL A  80      937   1983   2272    214    159     36       N  
ATOM    723  CA  VAL A  80       7.231  19.120  24.136  1.00 13.93           C  
ANISOU  723  CA  VAL A  80     1236   1789   2267    132    -38     87       C  
ATOM    724  C   VAL A  80       7.432  20.314  23.157  1.00 13.13           C  
ANISOU  724  C   VAL A  80     1098   1825   2065    411    284   -105       C  
ATOM    725  O   VAL A  80       6.452  20.766  22.559  1.00 14.26           O  
ANISOU  725  O   VAL A  80     1143   1835   2441    244     94     44       O  
ATOM    726  CB  VAL A  80       7.774  17.796  23.498  1.00 13.11           C  
ANISOU  726  CB  VAL A  80      763   1796   2420     64    140     88       C  
ATOM    727  CG1 VAL A  80       7.520  16.575  24.439  1.00 15.33           C  
ANISOU  727  CG1 VAL A  80     1316   1913   2594    233     78    273       C  
ATOM    728  CG2 VAL A  80       7.224  17.553  22.128  1.00 15.76           C  
ANISOU  728  CG2 VAL A  80     1680   2013   2294    357    135    122       C  
ATOM    729  N   LYS A  81       8.682  20.743  23.064  1.00 12.97           N  
ANISOU  729  N   LYS A  81     1215   1736   1977    208    168    -53       N  
ATOM    730  CA  LYS A  81       9.070  21.717  22.060  1.00 12.77           C  
ANISOU  730  CA  LYS A  81      833   1747   2272     60    -33    -57       C  
ATOM    731  C   LYS A  81       9.847  20.889  21.046  1.00 12.00           C  
ANISOU  731  C   LYS A  81      811   1643   2103    228     27   -128       C  
ATOM    732  O   LYS A  81      10.856  20.283  21.381  1.00 13.20           O  
ANISOU  732  O   LYS A  81      871   1909   2235    266    -47    -90       O  
ATOM    733  CB  LYS A  81       9.977  22.804  22.667  1.00 15.59           C  
ANISOU  733  CB  LYS A  81     1574   1910   2439    -32    -24    -41       C  
ATOM    734  CG  LYS A  81       9.375  23.593  23.740  1.00 22.12           C  
ANISOU  734  CG  LYS A  81     2606   2813   2985    -82    210   -119       C  
ATOM    735  CD  LYS A  81       8.420  24.594  23.216  1.00 26.62           C  
ANISOU  735  CD  LYS A  81     3312   3371   3432    101     63    -73       C  
ATOM    736  CE  LYS A  81       8.008  25.596  24.288  1.00 29.43           C  
ANISOU  736  CE  LYS A  81     3707   3779   3692     93    -97   -422       C  
ATOM    737  NZ  LYS A  81       6.705  26.226  24.022  1.00 30.66           N  
ANISOU  737  NZ  LYS A  81     3984   3992   3672    125   -627   -451       N  
ATOM    738  N   SER A  82       9.446  20.961  19.795  1.00 11.47           N  
ANISOU  738  N   SER A  82      443   1605   2310    383     62    -22       N  
ATOM    739  CA  SER A  82       9.973  20.117  18.726  1.00 11.45           C  
ANISOU  739  CA  SER A  82      663   1414   2271    153     10     87       C  
ATOM    740  C   SER A  82      10.576  20.925  17.602  1.00 10.12           C  
ANISOU  740  C   SER A  82      299   1307   2237    188   -133    118       C  
ATOM    741  O   SER A  82      10.057  21.971  17.237  1.00 11.42           O  
ANISOU  741  O   SER A  82      597   1415   2326    188     -5    -24       O  
ATOM    742  CB  SER A  82       8.840  19.299  18.162  1.00 11.89           C  
ANISOU  742  CB  SER A  82      549   1683   2284    174    276     77       C  
ATOM    743  OG  SER A  82       8.458  18.298  19.098  1.00 13.82           O  
ANISOU  743  OG  SER A  82     1036   1624   2590    202    281    340       O  
ATOM    744  N   THR A  83      11.653  20.425  17.078  1.00 10.57           N  
ANISOU  744  N   THR A  83      461   1409   2143    237   -114     75       N  
ATOM    745  CA  THR A  83      12.274  20.979  15.849  1.00 10.96           C  
ANISOU  745  CA  THR A  83      672   1319   2173     33    -61     68       C  
ATOM    746  C   THR A  83      12.570  19.847  14.903  1.00 10.50           C  
ANISOU  746  C   THR A  83      651   1343   1996    109     24    102       C  
ATOM    747  O   THR A  83      13.198  18.865  15.327  1.00 12.49           O  
ANISOU  747  O   THR A  83     1268   1488   1988    217    -27     10       O  
ATOM    748  CB  THR A  83      13.500  21.771  16.159  1.00 13.26           C  
ANISOU  748  CB  THR A  83     1048   1604   2382   -102     44     15       C  
ATOM    749  OG1 THR A  83      13.254  22.719  17.187  1.00 14.60           O  
ANISOU  749  OG1 THR A  83      916   1830   2801   -211      7   -373       O  
ATOM    750  CG2 THR A  83      13.928  22.512  14.916  1.00 15.12           C  
ANISOU  750  CG2 THR A  83     1357   1675   2713   -403    -51   -127       C  
ATOM    751  N   ILE A  84      12.160  19.953  13.648  1.00 10.89           N  
ANISOU  751  N   ILE A  84      712   1252   2172    215     49     44       N  
ATOM    752  CA  ILE A  84      12.385  18.899  12.658  1.00 10.82           C  
ANISOU  752  CA  ILE A  84      735   1228   2147    157    221     74       C  
ATOM    753  C   ILE A  84      13.206  19.507  11.541  1.00 11.26           C  
ANISOU  753  C   ILE A  84      657   1519   2102     98     -4     38       C  
ATOM    754  O   ILE A  84      12.837  20.583  11.012  1.00 11.61           O  
ANISOU  754  O   ILE A  84      827   1386   2195     90     20    105       O  
ATOM    755  CB  ILE A  84      11.046  18.321  12.149  1.00 10.89           C  
ANISOU  755  CB  ILE A  84      714   1400   2023     56    198     94       C  
ATOM    756  CG1 ILE A  84      10.266  17.690  13.315  1.00 11.22           C  
ANISOU  756  CG1 ILE A  84      354   1567   2339    358    105     83       C  
ATOM    757  CG2 ILE A  84      11.374  17.224  11.103  1.00 11.96           C  
ANISOU  757  CG2 ILE A  84      777   1462   2304    107    146    -11       C  
ATOM    758  CD1 ILE A  84       8.917  17.142  13.009  1.00 12.26           C  
ANISOU  758  CD1 ILE A  84      522   1738   2395    169    104    179       C  
ATOM    759  N   THR A  85      14.322  18.856  11.204  1.00 11.08           N  
ANISOU  759  N   THR A  85      748   1231   2228     17    119    135       N  
ATOM    760  CA  THR A  85      15.185  19.260  10.119  1.00 11.97           C  
ANISOU  760  CA  THR A  85      688   1477   2382     27    199    116       C  
ATOM    761  C   THR A  85      15.444  18.052   9.197  1.00 12.96           C  
ANISOU  761  C   THR A  85     1199   1466   2258   -101    206     38       C  
ATOM    762  O   THR A  85      15.114  16.930   9.521  1.00 14.11           O  
ANISOU  762  O   THR A  85     1731   1520   2109    -18    346    -30       O  
ATOM    763  CB  THR A  85      16.469  19.795  10.641  1.00 13.38           C  
ANISOU  763  CB  THR A  85      885   1621   2576    -75    186     44       C  
ATOM    764  OG1 THR A  85      17.146  18.805  11.463  1.00 15.91           O  
ANISOU  764  OG1 THR A  85     1150   1992   2902    150   -183   -150       O  
ATOM    765  CG2 THR A  85      16.233  21.115  11.419  1.00 15.99           C  
ANISOU  765  CG2 THR A  85     1410   1833   2830   -106    -15   -430       C  
ATOM    766  N  ALEU A  86      15.740  18.372   7.939  0.50 13.14           N  
ANISOU  766  N  ALEU A  86     1111   1509   2371   -120    207     66       N  
ATOM    767  N  BLEU A  86      16.205  18.259   8.137  0.50 12.93           N  
ANISOU  767  N  BLEU A  86     1380   1344   2185   -183    292     42       N  
ATOM    768  CA ALEU A  86      16.188  17.406   6.958  0.50 13.84           C  
ANISOU  768  CA ALEU A  86     1247   1729   2282   -243    217     37       C  
ATOM    769  CA BLEU A  86      16.801  17.166   7.378  0.50 12.57           C  
ANISOU  769  CA BLEU A  86     1355   1350   2071   -193    194     62       C  
ATOM    770  C  ALEU A  86      17.709  17.409   6.908  0.50 14.32           C  
ANISOU  770  C  ALEU A  86     1224   1814   2402   -324    311     42       C  
ATOM    771  C  BLEU A  86      18.285  17.077   7.656  0.50 12.90           C  
ANISOU  771  C  BLEU A  86     1232   1534   2132   -265    206     85       C  
ATOM    772  O  ALEU A  86      18.359  18.419   6.566  0.50 16.54           O  
ANISOU  772  O  ALEU A  86     1059   2248   2976   -374    739    -28       O  
ATOM    773  O  BLEU A  86      18.951  18.123   7.664  0.50 15.21           O  
ANISOU  773  O  BLEU A  86     1760   1719   2299   -378    292     78       O  
ATOM    774  CB ALEU A  86      15.626  17.755   5.587  0.50 15.24           C  
ANISOU  774  CB ALEU A  86     1573   1850   2367   -197    103     25       C  
ATOM    775  CB BLEU A  86      16.587  17.334   5.888  0.50 13.29           C  
ANISOU  775  CB BLEU A  86     1380   1511   2157   -171    213     92       C  
ATOM    776  CG ALEU A  86      14.470  16.916   5.040  0.50 18.62           C  
ANISOU  776  CG ALEU A  86     1891   2404   2777   -169   -106    -76       C  
ATOM    777  CG BLEU A  86      15.181  17.068   5.407  0.50 13.19           C  
ANISOU  777  CG BLEU A  86      890   1758   2361   -726    -22    194       C  
ATOM    778  CD1ALEU A  86      14.159  17.455   3.657  0.50 16.30           C  
ANISOU  778  CD1ALEU A  86      917   2583   2692    165     16    104       C  
ATOM    779  CD1BLEU A  86      15.054  17.605   3.978  0.50 16.43           C  
ANISOU  779  CD1BLEU A  86     1502   2461   2280      6   -296     11       C  
ATOM    780  CD2ALEU A  86      14.769  15.416   4.963  0.50 16.77           C  
ANISOU  780  CD2ALEU A  86     2001   2135   2234    -47    -15   -253       C  
ATOM    781  CD2BLEU A  86      14.892  15.555   5.448  0.50 14.68           C  
ANISOU  781  CD2BLEU A  86     1082   2108   2387    -89    165   -208       C  
ATOM    782  N  AASP A  87      18.309  16.286   7.264  0.50 14.04           N  
ANISOU  782  N  AASP A  87      987   1976   2368   -319    357    102       N  
ATOM    783  N  BASP A  87      18.781  15.846   7.836  0.50 12.76           N  
ANISOU  783  N  BASP A  87     1050   1681   2115   -270    167    157       N  
ATOM    784  CA AASP A  87      19.746  16.170   7.311  0.50 14.82           C  
ANISOU  784  CA AASP A  87     1225   1954   2449   -284    220     29       C  
ATOM    785  CA BASP A  87      20.192  15.498   7.809  0.50 14.07           C  
ANISOU  785  CA BASP A  87     1139   1852   2352   -184     70    139       C  
ATOM    786  C  AASP A  87      20.086  15.061   6.323  0.50 14.28           C  
ANISOU  786  C  AASP A  87     1061   1932   2433   -207    214     44       C  
ATOM    787  C  BASP A  87      20.391  14.529   6.664  0.50 13.55           C  
ANISOU  787  C  BASP A  87     1015   1759   2374     16    155    232       C  
ATOM    788  O  AASP A  87      19.860  13.887   6.616  0.50 15.04           O  
ANISOU  788  O  AASP A  87     1259   1866   2587   -321    -34     68       O  
ATOM    789  O  BASP A  87      20.057  13.333   6.753  0.50 13.37           O  
ANISOU  789  O  BASP A  87      700   1738   2640      3     44    334       O  
ATOM    790  CB AASP A  87      20.200  15.845   8.744  0.50 16.47           C  
ANISOU  790  CB AASP A  87     1350   2229   2675   -304    164     60       C  
ATOM    791  CB BASP A  87      20.570  14.780   9.093  0.50 14.55           C  
ANISOU  791  CB BASP A  87      990   2023   2514    -76    -15    158       C  
ATOM    792  CG AASP A  87      21.712  15.596   8.856  0.50 21.48           C  
ANISOU  792  CG AASP A  87     2071   2913   3176   -190    -53   -100       C  
ATOM    793  CG BASP A  87      22.010  14.353   9.135  0.50 16.99           C  
ANISOU  793  CG BASP A  87     1521   2269   2663    -76   -119    -25       C  
ATOM    794  OD1AASP A  87      22.160  14.957   9.832  0.50 27.50           O  
ANISOU  794  OD1AASP A  87     3450   3406   3589     -1    -24     52       O  
ATOM    795  OD1BASP A  87      22.820  14.791   8.298  0.50 23.05           O  
ANISOU  795  OD1BASP A  87     2243   3114   3397   -438     40    368       O  
ATOM    796  OD2AASP A  87      22.474  16.044   7.983  0.50 27.29           O  
ANISOU  796  OD2AASP A  87     3218   3369   3781   -260     88      5       O  
ATOM    797  OD2BASP A  87      22.359  13.572  10.054  0.50 22.31           O  
ANISOU  797  OD2BASP A  87     2526   2812   3136     79    -48    372       O  
ATOM    798  N  AGLY A  88      20.559  15.420   5.135  0.50 13.96           N  
ANISOU  798  N  AGLY A  88     1037   1963   2304   -207    109     52       N  
ATOM    799  N  BGLY A  88      20.934  15.033   5.572  0.50 13.71           N  
ANISOU  799  N  BGLY A  88     1023   1686   2498    -36    213    251       N  
ATOM    800  CA AGLY A  88      20.685  14.420   4.124  0.50 14.50           C  
ANISOU  800  CA AGLY A  88     1224   2025   2258     11    121     18       C  
ATOM    801  CA BGLY A  88      21.168  14.195   4.417  0.50 15.04           C  
ANISOU  801  CA BGLY A  88     1314   2010   2390     36     92    130       C  
ATOM    802  C  AGLY A  88      19.269  14.032   3.815  0.50 13.73           C  
ANISOU  802  C  AGLY A  88      985   1991   2241    -75     98    -39       C  
ATOM    803  C  BGLY A  88      19.981  13.298   4.089  0.50 15.28           C  
ANISOU  803  C  BGLY A  88     1374   2077   2354     54    231    126       C  
ATOM    804  O  AGLY A  88      18.450  14.905   3.639  0.50 15.25           O  
ANISOU  804  O  AGLY A  88     1504   1986   2303    -38    176     73       O  
ATOM    805  O  BGLY A  88      20.061  12.084   4.030  0.50 16.00           O  
ANISOU  805  O  BGLY A  88     1255   2234   2590    177    229     -5       O  
ATOM    806  N  AGLY A  89      18.981  12.742   3.747  0.50 13.28           N  
ANISOU  806  N  AGLY A  89      969   2006   2071    -33    212   -117       N  
ATOM    807  N  BGLY A  89      18.839  13.893   3.867  0.50 14.79           N  
ANISOU  807  N  BGLY A  89     1213   2136   2271     -3    407     84       N  
ATOM    808  CA AGLY A  89      17.644  12.248   3.471  0.50 13.15           C  
ANISOU  808  CA AGLY A  89      951   1887   2155   -209    -51   -216       C  
ATOM    809  CA BGLY A  89      17.656  13.100   3.534  0.50 14.54           C  
ANISOU  809  CA BGLY A  89     1174   2075   2273    110    205     -1       C  
ATOM    810  C  AGLY A  89      17.000  11.780   4.726  0.50 12.86           C  
ANISOU  810  C  AGLY A  89      804   1876   2203   -108    -13   -238       C  
ATOM    811  C  BGLY A  89      16.914  12.300   4.625  0.50 13.59           C  
ANISOU  811  C  BGLY A  89      868   2034   2260   -172     97    -43       C  
ATOM    812  O  AGLY A  89      16.090  10.990   4.679  0.50 13.25           O  
ANISOU  812  O  AGLY A  89      783   1918   2331     21    -83   -300       O  
ATOM    813  O  BGLY A  89      15.867  11.716   4.334  0.50 12.79           O  
ANISOU  813  O  BGLY A  89      825   1826   2207    -85   -341     88       O  
ATOM    814  N   VAL A  90      17.391  12.293   5.877  1.00 14.19           N  
ANISOU  814  N   VAL A  90      899   2198   2295   -291    130   -191       N  
ATOM    815  CA  VAL A  90      16.736  11.811   7.087  1.00 13.59           C  
ANISOU  815  CA  VAL A  90     1046   1776   2339   -207    218    -88       C  
ATOM    816  C   VAL A  90      15.996  12.961   7.754  1.00 12.12           C  
ANISOU  816  C   VAL A  90      926   1583   2094   -170    -28    -84       C  
ATOM    817  O   VAL A  90      16.618  14.013   7.982  1.00 12.65           O  
ANISOU  817  O   VAL A  90      896   1710   2199   -253    106    -53       O  
ATOM    818  CB  VAL A  90      17.800  11.249   8.080  1.00 13.94           C  
ANISOU  818  CB  VAL A  90     1039   1721   2535    -28    306   -221       C  
ATOM    819  CG1 VAL A  90      17.191  10.762   9.375  1.00 14.45           C  
ANISOU  819  CG1 VAL A  90      887   2023   2581   -198    180     80       C  
ATOM    820  CG2 VAL A  90      18.626  10.144   7.441  1.00 16.31           C  
ANISOU  820  CG2 VAL A  90     1173   1911   3113     91    407   -229       C  
ATOM    821  N   LEU A  91      14.735  12.774   8.062  1.00 11.24           N  
ANISOU  821  N   LEU A  91      574   1559   2135   -332     65   -102       N  
ATOM    822  CA  LEU A  91      14.013  13.750   8.876  1.00 11.41           C  
ANISOU  822  CA  LEU A  91      880   1438   2015   -132    158     28       C  
ATOM    823  C   LEU A  91      14.433  13.505  10.306  1.00 11.10           C  
ANISOU  823  C   LEU A  91      785   1519   1912     82    272    -11       C  
ATOM    824  O   LEU A  91      14.238  12.404  10.837  1.00 11.96           O  
ANISOU  824  O   LEU A  91     1199   1346   1996      4    193     30       O  
ATOM    825  CB  LEU A  91      12.519  13.585   8.735  1.00 12.92           C  
ANISOU  825  CB  LEU A  91     1162   1578   2168    -82    189     56       C  
ATOM    826  CG  LEU A  91      11.878  14.140   7.462  1.00 14.85           C  
ANISOU  826  CG  LEU A  91     1378   1776   2488   -142     28     27       C  
ATOM    827  CD1 LEU A  91      10.458  13.620   7.315  1.00 17.05           C  
ANISOU  827  CD1 LEU A  91     1560   1988   2929   -284   -165     85       C  
ATOM    828  CD2 LEU A  91      11.896  15.662   7.502  1.00 14.45           C  
ANISOU  828  CD2 LEU A  91     1531   1399   2559    145    -39    152       C  
ATOM    829  N   VAL A  92      14.945  14.525  10.962  1.00 11.02           N  
ANISOU  829  N   VAL A  92      725   1399   2063    144    150      3       N  
ATOM    830  CA  VAL A  92      15.398  14.450  12.355  1.00 10.97           C  
ANISOU  830  CA  VAL A  92      534   1542   2089    236    168     50       C  
ATOM    831  C   VAL A  92      14.529  15.324  13.217  1.00 11.73           C  
ANISOU  831  C   VAL A  92      868   1415   2173    325     50     25       C  
ATOM    832  O   VAL A  92      14.485  16.540  13.035  1.00 12.86           O  
ANISOU  832  O   VAL A  92     1314   1313   2256    219    216    104       O  
ATOM    833  CB  VAL A  92      16.861  14.890  12.440  1.00 12.12           C  
ANISOU  833  CB  VAL A  92      922   1601   2080    415    144    -38       C  
ATOM    834  CG1 VAL A  92      17.352  14.788  13.877  1.00 15.15           C  
ANISOU  834  CG1 VAL A  92     1174   2264   2316    141    133    -67       C  
ATOM    835  CG2 VAL A  92      17.766  14.058  11.495  1.00 14.88           C  
ANISOU  835  CG2 VAL A  92      922   2131   2599     54    266    -53       C  
ATOM    836  N   HIS A  93      13.854  14.694  14.163  1.00 11.23           N  
ANISOU  836  N   HIS A  93      944   1269   2054    422     41     57       N  
ATOM    837  CA  HIS A  93      12.808  15.318  14.984  1.00 11.14           C  
ANISOU  837  CA  HIS A  93      741   1367   2123    278     33    137       C  
ATOM    838  C   HIS A  93      13.271  15.279  16.410  1.00 11.56           C  
ANISOU  838  C   HIS A  93      892   1505   1994    357     48     30       C  
ATOM    839  O   HIS A  93      13.349  14.196  17.003  1.00 12.72           O  
ANISOU  839  O   HIS A  93     1470   1334   2025    211    -63     66       O  
ATOM    840  CB  HIS A  93      11.530  14.546  14.778  1.00 11.54           C  
ANISOU  840  CB  HIS A  93     1018   1362   2003    326    -97    174       C  
ATOM    841  CG  HIS A  93      10.328  14.974  15.535  1.00 11.89           C  
ANISOU  841  CG  HIS A  93      989   1531   1995    367     40    199       C  
ATOM    842  ND1 HIS A  93       9.141  14.317  15.369  1.00 14.60           N  
ANISOU  842  ND1 HIS A  93     1259   1902   2383    414    -14    350       N  
ATOM    843  CD2 HIS A  93      10.139  15.946  16.462  1.00 13.46           C  
ANISOU  843  CD2 HIS A  93     1270   1784   2058    451    342    300       C  
ATOM    844  CE1 HIS A  93       8.253  14.905  16.146  1.00 14.71           C  
ANISOU  844  CE1 HIS A  93      831   2121   2635    412     82    490       C  
ATOM    845  NE2 HIS A  93       8.830  15.877  16.840  1.00 14.68           N  
ANISOU  845  NE2 HIS A  93     1266   1982   2326    496    269    480       N  
ATOM    846  N   VAL A  94      13.614  16.431  16.979  1.00 10.96           N  
ANISOU  846  N   VAL A  94      672   1477   2014    184     88     86       N  
ATOM    847  CA  VAL A  94      14.066  16.531  18.369  1.00 10.91           C  
ANISOU  847  CA  VAL A  94      559   1406   2178    308     41     41       C  
ATOM    848  C   VAL A  94      12.968  17.079  19.205  1.00 11.50           C  
ANISOU  848  C   VAL A  94      901   1377   2089    269     48    -13       C  
ATOM    849  O   VAL A  94      12.396  18.122  18.879  1.00 13.18           O  
ANISOU  849  O   VAL A  94     1238   1572   2195    396    149     91       O  
ATOM    850  CB  VAL A  94      15.373  17.341  18.440  1.00 12.79           C  
ANISOU  850  CB  VAL A  94      812   1610   2435    241   -147     37       C  
ATOM    851  CG1 VAL A  94      15.836  17.375  19.890  1.00 16.31           C  
ANISOU  851  CG1 VAL A  94     1320   2253   2621   -397   -385    134       C  
ATOM    852  CG2 VAL A  94      16.408  16.819  17.461  1.00 16.09           C  
ANISOU  852  CG2 VAL A  94      679   2434   2997    493    243     64       C  
ATOM    853  N   GLN A  95      12.635  16.396  20.277  1.00 11.49           N  
ANISOU  853  N   GLN A  95     1037   1256   2072    243   -131     42       N  
ATOM    854  CA  GLN A  95      11.638  16.824  21.247  1.00 11.66           C  
ANISOU  854  CA  GLN A  95     1025   1312   2093    208    -15     23       C  
ATOM    855  C   GLN A  95      12.291  17.146  22.572  1.00 12.53           C  
ANISOU  855  C   GLN A  95     1160   1459   2141    202     58      6       C  
ATOM    856  O   GLN A  95      13.060  16.316  23.101  1.00 13.24           O  
ANISOU  856  O   GLN A  95     1306   1572   2149    253    -94    -59       O  
ATOM    857  CB  GLN A  95      10.613  15.693  21.521  1.00 12.00           C  
ANISOU  857  CB  GLN A  95     1089   1358   2111    214     -8     52       C  
ATOM    858  CG  GLN A  95       9.845  15.269  20.274  1.00 12.52           C  
ANISOU  858  CG  GLN A  95     1002   1523   2230    -48    101     23       C  
ATOM    859  CD  GLN A  95       8.903  14.070  20.470  1.00 12.31           C  
ANISOU  859  CD  GLN A  95      470   1663   2541    -28    119     84       C  
ATOM    860  OE1 GLN A  95       7.833  13.990  19.823  1.00 14.64           O  
ANISOU  860  OE1 GLN A  95      721   2023   2820    -27     97     68       O  
ATOM    861  NE2 GLN A  95       9.155  13.253  21.447  1.00 12.36           N  
ANISOU  861  NE2 GLN A  95      838   1493   2365   -129   -261    266       N  
ATOM    862  N   LYS A  96      12.011  18.323  23.102  1.00 12.95           N  
ANISOU  862  N   LYS A  96     1315   1518   2088    192      7    -33       N  
ATOM    863  CA  LYS A  96      12.563  18.777  24.372  1.00 14.35           C  
ANISOU  863  CA  LYS A  96     1456   1796   2199     96    -57    -23       C  
ATOM    864  C   LYS A  96      11.463  19.013  25.380  1.00 13.88           C  
ANISOU  864  C   LYS A  96     1423   1621   2229    184   -181    -93       C  
ATOM    865  O   LYS A  96      10.472  19.659  25.096  1.00 14.47           O  
ANISOU  865  O   LYS A  96     1529   1797   2169    334    -84   -122       O  
ATOM    866  CB  LYS A  96      13.337  20.103  24.200  1.00 15.23           C  
ANISOU  866  CB  LYS A  96     1385   1959   2440    -96   -138    -45       C  
ATOM    867  CG  LYS A  96      14.355  20.139  23.167  1.00 19.13           C  
ANISOU  867  CG  LYS A  96     2076   2316   2874    -26    -60    -97       C  
ATOM    868  CD  LYS A  96      15.522  19.256  23.462  1.00 20.33           C  
ANISOU  868  CD  LYS A  96     2371   2483   2870     29   -111   -298       C  
ATOM    869  CE  LYS A  96      16.721  19.616  22.636  1.00 20.69           C  
ANISOU  869  CE  LYS A  96     2218   2419   3223   -271   -294   -287       C  
ATOM    870  NZ  LYS A  96      17.908  18.738  22.855  1.00 22.84           N  
ANISOU  870  NZ  LYS A  96     2645   2259   3771    -86     73    -45       N  
ATOM    871  N   TRP A  97      11.599  18.511  26.604  1.00 14.54           N  
ANISOU  871  N   TRP A  97     1616   1619   2289    182   -125    -95       N  
ATOM    872  CA  TRP A  97      10.634  18.737  27.667  1.00 16.73           C  
ANISOU  872  CA  TRP A  97     2121   1977   2257    445     34    -64       C  
ATOM    873  C   TRP A  97      11.292  18.411  29.009  1.00 18.11           C  
ANISOU  873  C   TRP A  97     2449   2158   2272    502     32   -165       C  
ATOM    874  O   TRP A  97      12.110  17.491  29.086  1.00 19.00           O  
ANISOU  874  O   TRP A  97     2768   2215   2236    580   -180   -143       O  
ATOM    875  CB  TRP A  97       9.351  17.884  27.486  1.00 16.05           C  
ANISOU  875  CB  TRP A  97     1842   2095   2158    459    103    -47       C  
ATOM    876  CG  TRP A  97       9.540  16.424  27.893  1.00 16.32           C  
ANISOU  876  CG  TRP A  97     1515   2124   2560    319    268     81       C  
ATOM    877  CD1 TRP A  97       9.072  15.839  29.022  1.00 17.66           C  
ANISOU  877  CD1 TRP A  97     2288   2163   2256    432    402     64       C  
ATOM    878  CD2 TRP A  97      10.329  15.426  27.238  1.00 15.00           C  
ANISOU  878  CD2 TRP A  97     1542   1815   2341    210    335    -77       C  
ATOM    879  NE1 TRP A  97       9.445  14.552  29.091  1.00 17.66           N  
ANISOU  879  NE1 TRP A  97     2422   1991   2296    419    379    146       N  
ATOM    880  CE2 TRP A  97      10.229  14.259  28.015  1.00 15.54           C  
ANISOU  880  CE2 TRP A  97     1688   2002   2212     36    288     89       C  
ATOM    881  CE3 TRP A  97      11.081  15.386  26.054  1.00 15.17           C  
ANISOU  881  CE3 TRP A  97     1721   1703   2339     -8     79   -113       C  
ATOM    882  CZ2 TRP A  97      10.909  13.081  27.697  1.00 16.32           C  
ANISOU  882  CZ2 TRP A  97     1893   1970   2335    115    -43    247       C  
ATOM    883  CZ3 TRP A  97      11.725  14.196  25.749  1.00 14.90           C  
ANISOU  883  CZ3 TRP A  97     1315   1871   2473   -127    125    -96       C  
ATOM    884  CH2 TRP A  97      11.618  13.077  26.547  1.00 16.01           C  
ANISOU  884  CH2 TRP A  97     1877   1674   2530     36    131   -180       C  
ATOM    885  N   ASP A  98      11.019  19.226  30.035  1.00 19.21           N  
ANISOU  885  N   ASP A  98     2721   2348   2228    632      3   -182       N  
ATOM    886  CA  ASP A  98      11.423  18.863  31.423  1.00 21.52           C  
ANISOU  886  CA  ASP A  98     3123   2681   2371    412    -76   -270       C  
ATOM    887  C   ASP A  98      12.939  18.637  31.523  1.00 21.81           C  
ANISOU  887  C   ASP A  98     3235   2724   2325    382   -137   -366       C  
ATOM    888  O   ASP A  98      13.385  17.788  32.293  1.00 24.73           O  
ANISOU  888  O   ASP A  98     3782   3091   2522    396   -203   -178       O  
ATOM    889  CB  ASP A  98      10.651  17.624  31.877  1.00 23.83           C  
ANISOU  889  CB  ASP A  98     3385   3153   2513    448    -30    -52       C  
ATOM    890  N   GLY A  99      13.743  19.353  30.732  1.00 21.29           N  
ANISOU  890  N   GLY A  99     3127   2529   2430    355   -319   -437       N  
ATOM    891  CA  GLY A  99      15.190  19.181  30.744  1.00 21.48           C  
ANISOU  891  CA  GLY A  99     2945   2545   2668    308   -427   -372       C  
ATOM    892  C   GLY A  99      15.710  17.946  30.017  1.00 20.36           C  
ANISOU  892  C   GLY A  99     2596   2471   2667    386   -480   -337       C  
ATOM    893  O   GLY A  99      16.935  17.679  30.055  1.00 23.12           O  
ANISOU  893  O   GLY A  99     2792   2871   3120    340   -599   -466       O  
ATOM    894  N   LYS A 100      14.795  17.211  29.357  1.00 19.09           N  
ANISOU  894  N   LYS A 100     2479   2310   2464    341   -445   -310       N  
ATOM    895  CA  LYS A 100      15.041  15.936  28.665  1.00 16.08           C  
ANISOU  895  CA  LYS A 100     1605   2124   2379    407   -471   -186       C  
ATOM    896  C   LYS A 100      14.986  16.179  27.171  1.00 15.53           C  
ANISOU  896  C   LYS A 100     1678   1980   2240    286   -401     -8       C  
ATOM    897  O   LYS A 100      14.399  17.135  26.725  1.00 15.77           O  
ANISOU  897  O   LYS A 100     1913   1844   2235    329   -304   -181       O  
ATOM    898  CB  LYS A 100      14.044  14.856  29.082  1.00 17.74           C  
ANISOU  898  CB  LYS A 100     2373   2077   2289    413   -345    -42       C  
ATOM    899  CG  LYS A 100      13.968  14.621  30.592  1.00 22.92           C  
ANISOU  899  CG  LYS A 100     3181   2929   2596    264   -207   -149       C  
ATOM    900  CD  LYS A 100      12.931  13.605  30.988  1.00 25.73           C  
ANISOU  900  CD  LYS A 100     3526   3317   2934    329    -20    135       C  
ATOM    901  CE  LYS A 100      12.802  13.547  32.501  1.00 29.47           C  
ANISOU  901  CE  LYS A 100     3962   3980   3253    289    -21    -38       C  
ATOM    902  NZ  LYS A 100      12.721  14.955  33.039  1.00 35.64           N  
ANISOU  902  NZ  LYS A 100     4997   4208   4334     78   -125    -41       N  
ATOM    903  N   SER A 101      15.564  15.240  26.404  1.00 14.22           N  
ANISOU  903  N   SER A 101     1482   1711   2209     70   -240    -44       N  
ATOM    904  CA  SER A 101      15.527  15.289  24.955  1.00 14.59           C  
ANISOU  904  CA  SER A 101     1499   1742   2302     90   -196      7       C  
ATOM    905  C   SER A 101      15.393  13.884  24.420  1.00 13.43           C  
ANISOU  905  C   SER A 101     1292   1555   2254    173   -182      7       C  
ATOM    906  O   SER A 101      16.026  12.978  24.911  1.00 14.35           O  
ANISOU  906  O   SER A 101     1578   1521   2351    156   -453     45       O  
ATOM    907  CB  SER A 101      16.840  15.879  24.465  1.00 16.78           C  
ANISOU  907  CB  SER A 101     2022   1789   2564   -202    -87    -63       C  
ATOM    908  OG  SER A 101      16.809  16.126  23.086  1.00 19.52           O  
ANISOU  908  OG  SER A 101     2467   2048   2901   -451    -40    -79       O  
ATOM    909  N   THR A 102      14.653  13.735  23.313  1.00 12.66           N  
ANISOU  909  N   THR A 102     1137   1516   2157     88   -198     55       N  
ATOM    910  CA  THR A 102      14.610  12.478  22.537  1.00 11.62           C  
ANISOU  910  CA  THR A 102      632   1461   2320    258    -17    -77       C  
ATOM    911  C   THR A 102      14.567  12.863  21.067  1.00 11.70           C  
ANISOU  911  C   THR A 102      944   1453   2047    196   -109     60       C  
ATOM    912  O   THR A 102      14.089  13.943  20.706  1.00 12.67           O  
ANISOU  912  O   THR A 102     1183   1418   2212    154    -62     70       O  
ATOM    913  CB  THR A 102      13.386  11.654  22.938  1.00 12.48           C  
ANISOU  913  CB  THR A 102     1011   1615   2112    -44    -72   -152       C  
ATOM    914  OG1 THR A 102      13.485  10.354  22.303  1.00 13.29           O  
ANISOU  914  OG1 THR A 102     1060   1464   2523     75     -9   -109       O  
ATOM    915  CG2 THR A 102      12.087  12.231  22.603  1.00 13.38           C  
ANISOU  915  CG2 THR A 102      396   1992   2696     70      3     75       C  
ATOM    916  N   THR A 103      15.180  11.994  20.239  1.00 12.19           N  
ANISOU  916  N   THR A 103     1328   1264   2038    210   -136     79       N  
ATOM    917  CA  THR A 103      15.265  12.212  18.807  1.00 12.45           C  
ANISOU  917  CA  THR A 103     1145   1409   2176    224   -137     18       C  
ATOM    918  C   THR A 103      14.571  11.088  18.059  1.00 12.56           C  
ANISOU  918  C   THR A 103     1370   1372   2030    222    -35    -29       C  
ATOM    919  O   THR A 103      14.811   9.902  18.357  1.00 14.14           O  
ANISOU  919  O   THR A 103     1966   1356   2050    283   -316     12       O  
ATOM    920  CB  THR A 103      16.699  12.367  18.384  1.00 13.30           C  
ANISOU  920  CB  THR A 103     1039   1673   2340    134    -81    -34       C  
ATOM    921  OG1 THR A 103      17.277  13.510  19.044  1.00 17.56           O  
ANISOU  921  OG1 THR A 103     1673   2285   2713   -221    182   -114       O  
ATOM    922  CG2 THR A 103      16.798  12.572  16.901  1.00 15.94           C  
ANISOU  922  CG2 THR A 103     1608   2129   2318     11     87     77       C  
ATOM    923  N   ILE A 104      13.760  11.434  17.100  1.00 11.67           N  
ANISOU  923  N   ILE A 104     1209   1229   1997    216    -64     29       N  
ATOM    924  CA  ILE A 104      13.092  10.497  16.223  1.00 11.71           C  
ANISOU  924  CA  ILE A 104     1075   1262   2110    276    -27     30       C  
ATOM    925  C   ILE A 104      13.563  10.768  14.836  1.00 11.93           C  
ANISOU  925  C   ILE A 104     1193   1405   1934    237     48    110       C  
ATOM    926  O   ILE A 104      13.427  11.872  14.331  1.00 12.61           O  
ANISOU  926  O   ILE A 104     1378   1366   2045    240     53     48       O  
ATOM    927  CB  ILE A 104      11.552  10.673  16.263  1.00 13.49           C  
ANISOU  927  CB  ILE A 104     1680   1426   2019    126    109    100       C  
ATOM    928  CG1 ILE A 104      10.975  10.499  17.702  1.00 14.22           C  
ANISOU  928  CG1 ILE A 104     1597   1669   2134     49    220    -39       C  
ATOM    929  CG2 ILE A 104      10.824   9.702  15.288  1.00 14.34           C  
ANISOU  929  CG2 ILE A 104     1355   1886   2206     44    -93      0       C  
ATOM    930  CD1 ILE A 104       9.521  10.917  17.804  1.00 18.69           C  
ANISOU  930  CD1 ILE A 104     1536   2767   2796    404    445     60       C  
ATOM    931  N   LYS A 105      14.165   9.763  14.207  1.00 11.41           N  
ANISOU  931  N   LYS A 105      840   1402   2094    145     79     46       N  
ATOM    932  CA  LYS A 105      14.677   9.860  12.838  1.00 11.57           C  
ANISOU  932  CA  LYS A 105      944   1414   2035    -94     -9    122       C  
ATOM    933  C   LYS A 105      13.759   9.074  11.939  1.00 11.48           C  
ANISOU  933  C   LYS A 105      939   1314   2106    -66     73    111       C  
ATOM    934  O   LYS A 105      13.373   7.959  12.273  1.00 12.93           O  
ANISOU  934  O   LYS A 105     1391   1393   2126   -170    -85     92       O  
ATOM    935  CB  LYS A 105      16.138   9.369  12.744  1.00 11.71           C  
ANISOU  935  CB  LYS A 105      460   1774   2214    138     64     19       C  
ATOM    936  CG  LYS A 105      17.123  10.280  13.506  1.00 16.42           C  
ANISOU  936  CG  LYS A 105     1085   2347   2804    316   -418     -3       C  
ATOM    937  CD  LYS A 105      18.568   9.890  13.333  1.00 19.94           C  
ANISOU  937  CD  LYS A 105     1229   3166   3178    244   -305      4       C  
ATOM    938  CE  LYS A 105      19.457  10.866  14.052  1.00 23.97           C  
ANISOU  938  CE  LYS A 105     1748   3347   4011    167   -461     -2       C  
ATOM    939  NZ  LYS A 105      20.913  10.576  13.888  1.00 28.05           N  
ANISOU  939  NZ  LYS A 105     2276   3725   4655    224   -130     64       N  
ATOM    940  N   ARG A 106      13.461   9.613  10.770  1.00 10.57           N  
ANISOU  940  N   ARG A 106      760   1205   2050    -86     -9     25       N  
ATOM    941  CA  ARG A 106      12.611   8.949   9.793  1.00 11.21           C  
ANISOU  941  CA  ARG A 106      842   1409   2006    -55     18     19       C  
ATOM    942  C   ARG A 106      13.392   8.903   8.482  1.00 11.50           C  
ANISOU  942  C   ARG A 106      870   1520   1980   -235     13    -42       C  
ATOM    943  O   ARG A 106      13.900   9.938   8.006  1.00 11.56           O  
ANISOU  943  O   ARG A 106      728   1489   2175    -27    102    -75       O  
ATOM    944  CB  ARG A 106      11.287   9.652   9.614  1.00 12.26           C  
ANISOU  944  CB  ARG A 106      818   1712   2126    -64    -30     84       C  
ATOM    945  CG  ARG A 106      10.497   9.680  10.925  1.00 12.57           C  
ANISOU  945  CG  ARG A 106      751   1680   2344      1    114     65       C  
ATOM    946  CD  ARG A 106       9.215  10.477  10.830  1.00 16.63           C  
ANISOU  946  CD  ARG A 106      847   2777   2691   -404    212    -52       C  
ATOM    947  NE  ARG A 106       8.331  10.416  12.015  1.00 16.90           N  
ANISOU  947  NE  ARG A 106     1339   2420   2658   -297    388    -98       N  
ATOM    948  CZ  ARG A 106       8.321  11.295  13.008  1.00 16.01           C  
ANISOU  948  CZ  ARG A 106      472   2706   2904   -271    -63   -238       C  
ATOM    949  NH1 ARG A 106       9.098  12.287  13.071  1.00 15.58           N  
ANISOU  949  NH1 ARG A 106      757   2698   2462    369     34    -27       N  
ATOM    950  NH2 ARG A 106       7.395  11.140  13.965  1.00 19.43           N  
ANISOU  950  NH2 ARG A 106      715   3697   2969     51    359   -136       N  
ATOM    951  N   LYS A 107      13.527   7.725   7.864  1.00 11.04           N  
ANISOU  951  N   LYS A 107      718   1492   1984   -189     49    -38       N  
ATOM    952  CA  LYS A 107      14.371   7.518   6.677  1.00 12.60           C  
ANISOU  952  CA  LYS A 107      853   1666   2265   -213    241    -23       C  
ATOM    953  C   LYS A 107      13.771   6.483   5.772  1.00 12.41           C  
ANISOU  953  C   LYS A 107      725   1776   2212   -414    143    -48       C  
ATOM    954  O   LYS A 107      13.209   5.494   6.236  1.00 14.50           O  
ANISOU  954  O   LYS A 107     1509   1914   2086   -587    157    -32       O  
ATOM    955  CB  LYS A 107      15.762   7.102   7.062  1.00 13.44           C  
ANISOU  955  CB  LYS A 107      487   2154   2463    -37    205   -199       C  
ATOM    956  CG  LYS A 107      16.814   7.012   5.975  1.00 16.86           C  
ANISOU  956  CG  LYS A 107     1187   2163   3055    -70    238   -325       C  
ATOM    957  CD  LYS A 107      18.180   6.651   6.441  1.00 18.66           C  
ANISOU  957  CD  LYS A 107      952   2712   3426    431    454   -647       C  
ATOM    958  CE  LYS A 107      19.214   7.154   5.417  1.00 24.41           C  
ANISOU  958  CE  LYS A 107     2211   3282   3779    361    454   -524       C  
ATOM    959  NZ  LYS A 107      18.699   8.362   4.647  1.00 30.13           N  
ANISOU  959  NZ  LYS A 107     2607   4110   4730    252    385   -264       N  
ATOM    960  N   ARG A 108      13.810   6.717   4.475  1.00 11.39           N  
ANISOU  960  N   ARG A 108      460   1667   2198   -281    123     -4       N  
ATOM    961  CA  ARG A 108      13.418   5.684   3.497  1.00 13.19           C  
ANISOU  961  CA  ARG A 108      724   2013   2272   -255    101     34       C  
ATOM    962  C   ARG A 108      14.501   4.631   3.368  1.00 11.22           C  
ANISOU  962  C   ARG A 108      267   1900   2093     83    126   -153       C  
ATOM    963  O   ARG A 108      15.656   4.948   3.192  1.00 14.18           O  
ANISOU  963  O   ARG A 108      693   1971   2721    -72    314   -299       O  
ATOM    964  CB  ARG A 108      13.125   6.341   2.137  1.00 13.58           C  
ANISOU  964  CB  ARG A 108      748   2157   2253   -363    213     34       C  
ATOM    965  CG  ARG A 108      11.807   7.033   2.115  1.00 15.01           C  
ANISOU  965  CG  ARG A 108     1052   2552   2098   -126    -34    287       C  
ATOM    966  CD  ARG A 108      10.573   6.143   2.191  1.00 17.70           C  
ANISOU  966  CD  ARG A 108      485   3385   2854    118    454    203       C  
ATOM    967  NE  ARG A 108      10.649   5.041   1.207  1.00 18.21           N  
ANISOU  967  NE  ARG A 108      934   2652   3331   -195    189    398       N  
ATOM    968  CZ  ARG A 108      10.418   5.158  -0.088  1.00 17.20           C  
ANISOU  968  CZ  ARG A 108     1130   2119   3283   -130    -92    134       C  
ATOM    969  NH1 ARG A 108       9.876   6.252  -0.563  1.00 16.92           N  
ANISOU  969  NH1 ARG A 108      971   2471   2985    -92   -389    123       N  
ATOM    970  NH2 ARG A 108      10.615   4.129  -0.911  1.00 21.27           N  
ANISOU  970  NH2 ARG A 108     1611   2828   3641    302   -327   -100       N  
ATOM    971  N   GLU A 109      14.098   3.359   3.400  1.00 12.97           N  
ANISOU  971  N   GLU A 109      734   1759   2433   -237    197   -262       N  
ATOM    972  CA  GLU A 109      15.009   2.233   3.156  1.00 14.30           C  
ANISOU  972  CA  GLU A 109     1085   1934   2411    103    247   -191       C  
ATOM    973  C   GLU A 109      14.260   1.233   2.320  1.00 13.13           C  
ANISOU  973  C   GLU A 109      867   1809   2310     81    139   -155       C  
ATOM    974  O   GLU A 109      13.220   0.705   2.730  1.00 13.99           O  
ANISOU  974  O   GLU A 109     1027   2003   2285     -6    325   -207       O  
ATOM    975  CB  GLU A 109      15.360   1.544   4.471  1.00 16.19           C  
ANISOU  975  CB  GLU A 109     1403   2092   2655    191     78   -209       C  
ATOM    976  CG  GLU A 109      16.063   2.397   5.483  1.00 20.13           C  
ANISOU  976  CG  GLU A 109     1873   2840   2933    377   -215   -280       C  
ATOM    977  CD  GLU A 109      17.494   2.651   5.126  1.00 24.52           C  
ANISOU  977  CD  GLU A 109     2350   3496   3470    -78    -12   -550       C  
ATOM    978  OE1 GLU A 109      18.158   3.421   5.832  1.00 28.46           O  
ANISOU  978  OE1 GLU A 109     2749   3924   4138   -521   -162   -415       O  
ATOM    979  OE2 GLU A 109      17.978   2.110   4.109  1.00 30.68           O  
ANISOU  979  OE2 GLU A 109     3010   4438   4208     12     88   -798       O  
ATOM    980  N   ASP A 110      14.662   1.084   1.054  1.00 12.86           N  
ANISOU  980  N   ASP A 110      768   1864   2254    112    146    -16       N  
ATOM    981  CA  ASP A 110      13.943   0.281   0.076  1.00 13.72           C  
ANISOU  981  CA  ASP A 110     1368   1670   2173      9    169    -10       C  
ATOM    982  C   ASP A 110      12.517   0.823   0.017  1.00 12.97           C  
ANISOU  982  C   ASP A 110      940   2040   1948   -112      0    -51       C  
ATOM    983  O   ASP A 110      12.354   2.062  -0.070  1.00 14.07           O  
ANISOU  983  O   ASP A 110     1223   1841   2281    216     92     36       O  
ATOM    984  CB  ASP A 110      14.044  -1.214   0.407  1.00 15.08           C  
ANISOU  984  CB  ASP A 110     1622   1919   2185    300    261    -77       C  
ATOM    985  CG  ASP A 110      15.452  -1.682   0.406  1.00 18.27           C  
ANISOU  985  CG  ASP A 110     1900   2305   2734    103    298    296       C  
ATOM    986  OD1 ASP A 110      16.257  -1.207  -0.400  1.00 21.75           O  
ANISOU  986  OD1 ASP A 110     2030   2747   3488    659    576    198       O  
ATOM    987  OD2 ASP A 110      15.788  -2.576   1.184  1.00 26.56           O  
ANISOU  987  OD2 ASP A 110     3559   3166   3366    645    436    691       O  
ATOM    988  N   ASP A 111      11.450   0.019   0.067  1.00 13.16           N  
ANISOU  988  N   ASP A 111      940   1991   2069    -74    -11   -200       N  
ATOM    989  CA  ASP A 111      10.113   0.455  -0.008  1.00 13.73           C  
ANISOU  989  CA  ASP A 111      710   2182   2323   -152      1   -168       C  
ATOM    990  C   ASP A 111       9.564   0.867   1.363  1.00 13.79           C  
ANISOU  990  C   ASP A 111      691   2173   2373   -116     -6   -146       C  
ATOM    991  O   ASP A 111       8.399   1.111   1.439  1.00 16.21           O  
ANISOU  991  O   ASP A 111      904   2689   2566    -54    -99   -500       O  
ATOM    992  CB  ASP A 111       9.223  -0.571  -0.735  1.00 14.68           C  
ANISOU  992  CB  ASP A 111      938   2279   2359    -93   -131   -167       C  
ATOM    993  CG  ASP A 111       9.514  -0.636  -2.199  1.00 15.90           C  
ANISOU  993  CG  ASP A 111     1412   2207   2421   -203   -140   -168       C  
ATOM    994  OD1 ASP A 111       9.755   0.416  -2.814  1.00 19.52           O  
ANISOU  994  OD1 ASP A 111     2609   2541   2264   -268    -36    -99       O  
ATOM    995  OD2 ASP A 111       9.612  -1.759  -2.730  1.00 19.20           O  
ANISOU  995  OD2 ASP A 111     2490   2257   2548    -96    204   -292       O  
ATOM    996  N   LYS A 112      10.322   0.799   2.404  1.00 13.46           N  
ANISOU  996  N   LYS A 112     1032   1768   2314    -77    111    -57       N  
ATOM    997  CA  LYS A 112       9.914   1.092   3.776  1.00 12.67           C  
ANISOU  997  CA  LYS A 112      902   1776   2136    -85    163   -132       C  
ATOM    998  C   LYS A 112      10.238   2.479   4.201  1.00 12.09           C  
ANISOU  998  C   LYS A 112      667   1625   2301    -98     86    -64       C  
ATOM    999  O   LYS A 112      11.107   3.159   3.657  1.00 12.97           O  
ANISOU  999  O   LYS A 112     1094   1643   2191   -151    208    -95       O  
ATOM   1000  CB  LYS A 112      10.552   0.066   4.699  1.00 14.27           C  
ANISOU 1000  CB  LYS A 112     1379   1717   2326    151    319   -163       C  
ATOM   1001  CG  LYS A 112      10.301  -1.386   4.322  1.00 18.90           C  
ANISOU 1001  CG  LYS A 112     2139   2200   2842    147    414   -191       C  
ATOM   1002  CD  LYS A 112       8.914  -1.844   4.487  1.00 24.11           C  
ANISOU 1002  CD  LYS A 112     2543   2916   3699    114    -15   -308       C  
ATOM   1003  CE  LYS A 112       8.833  -3.395   4.405  1.00 29.20           C  
ANISOU 1003  CE  LYS A 112     3371   3301   4421    227     58    -38       C  
ATOM   1004  NZ  LYS A 112      10.138  -4.026   4.197  1.00 33.55           N  
ANISOU 1004  NZ  LYS A 112     3606   4094   5047    463    -22   -220       N  
ATOM   1005  N   LEU A 113       9.589   2.865   5.272  1.00 11.69           N  
ANISOU 1005  N   LEU A 113      649   1649   2143   -227      5    -90       N  
ATOM   1006  CA ALEU A 113       9.917   4.087   5.996  0.50 11.47           C  
ANISOU 1006  CA ALEU A 113      482   1661   2212   -173    158    -57       C  
ATOM   1007  CA BLEU A 113       9.916   4.087   6.007  0.50 11.77           C  
ANISOU 1007  CA BLEU A 113      614   1688   2170   -185    125    -69       C  
ATOM   1008  C   LEU A 113      10.329   3.605   7.417  1.00 11.36           C  
ANISOU 1008  C   LEU A 113      474   1628   2212   -307    356   -104       C  
ATOM   1009  O   LEU A 113       9.482   3.008   8.096  1.00 12.70           O  
ANISOU 1009  O   LEU A 113      661   1804   2357   -222     58    -93       O  
ATOM   1010  CB ALEU A 113       8.707   5.033   5.989  0.50 12.40           C  
ANISOU 1010  CB ALEU A 113      475   1950   2285   -153     66    -64       C  
ATOM   1011  CB BLEU A 113       8.699   5.016   6.040  0.50 12.96           C  
ANISOU 1011  CB BLEU A 113      752   1925   2245   -168     46    -71       C  
ATOM   1012  CG ALEU A 113       8.971   6.472   6.438  0.50 12.90           C  
ANISOU 1012  CG ALEU A 113      418   1956   2524    169    251   -131       C  
ATOM   1013  CG BLEU A 113       8.845   6.335   6.809  0.50 14.14           C  
ANISOU 1013  CG BLEU A 113     1040   2136   2196      3      0   -217       C  
ATOM   1014  CD1ALEU A 113       7.860   7.357   5.936  0.50 13.09           C  
ANISOU 1014  CD1ALEU A 113      777   1850   2346     10    366      1       C  
ATOM   1015  CD1BLEU A 113      10.093   7.025   6.373  0.50 16.31           C  
ANISOU 1015  CD1BLEU A 113     1614   1803   2777     82    -29    120       C  
ATOM   1016  CD2ALEU A 113       9.120   6.568   7.961  0.50 15.06           C  
ANISOU 1016  CD2ALEU A 113      533   2421   2768    538    -45    320       C  
ATOM   1017  CD2BLEU A 113       7.654   7.226   6.531  0.50 16.17           C  
ANISOU 1017  CD2BLEU A 113     1694   2353   2095     81    124   -109       C  
ATOM   1018  N   VAL A 114      11.566   3.792   7.761  1.00 10.50           N  
ANISOU 1018  N   VAL A 114      410   1506   2074   -196    188     24       N  
ATOM   1019  CA  VAL A 114      12.099   3.305   9.055  1.00 11.88           C  
ANISOU 1019  CA  VAL A 114      666   1707   2140   -260    127     99       C  
ATOM   1020  C   VAL A 114      12.150   4.481  10.003  1.00 12.20           C  
ANISOU 1020  C   VAL A 114      897   1646   2091   -192     67     65       C  
ATOM   1021  O   VAL A 114      12.582   5.593   9.639  1.00 12.68           O  
ANISOU 1021  O   VAL A 114     1122   1615   2079   -176    162     69       O  
ATOM   1022  CB  VAL A 114      13.448   2.689   8.865  1.00 12.65           C  
ANISOU 1022  CB  VAL A 114      780   1870   2155    -82    -28     89       C  
ATOM   1023  CG1 VAL A 114      13.982   2.152  10.202  1.00 16.03           C  
ANISOU 1023  CG1 VAL A 114     1578   2230   2280    167    -20    114       C  
ATOM   1024  CG2 VAL A 114      13.344   1.536   7.864  1.00 16.40           C  
ANISOU 1024  CG2 VAL A 114     1395   2150   2685    300    229   -191       C  
ATOM   1025  N   VAL A 115      11.641   4.261  11.201  1.00 12.14           N  
ANISOU 1025  N   VAL A 115     1102   1369   2140   -315     56     47       N  
ATOM   1026  CA  VAL A 115      11.624   5.235  12.278  1.00 12.26           C  
ANISOU 1026  CA  VAL A 115     1094   1426   2138   -109     51     98       C  
ATOM   1027  C   VAL A 115      12.447   4.770  13.420  1.00 13.17           C  
ANISOU 1027  C   VAL A 115     1511   1533   1959   -257    -57    106       C  
ATOM   1028  O   VAL A 115      12.195   3.717  13.985  1.00 16.44           O  
ANISOU 1028  O   VAL A 115     2036   1839   2368   -456   -370    323       O  
ATOM   1029  CB  VAL A 115      10.219   5.493  12.719  1.00 13.61           C  
ANISOU 1029  CB  VAL A 115     1385   1554   2230   -204      4    -31       C  
ATOM   1030  CG1 VAL A 115      10.154   6.617  13.797  1.00 16.03           C  
ANISOU 1030  CG1 VAL A 115     1377   2109   2604    -79    340   -277       C  
ATOM   1031  CG2 VAL A 115       9.288   5.829  11.541  1.00 15.32           C  
ANISOU 1031  CG2 VAL A 115      706   2016   3097   -499   -190     41       C  
ATOM   1032  N  AGLU A 116      13.494   5.507  13.761  0.50 12.85           N  
ANISOU 1032  N  AGLU A 116     1487   1409   1986   -167     21    127       N  
ATOM   1033  N  BGLU A 116      13.461   5.555  13.767  0.50 12.15           N  
ANISOU 1033  N  BGLU A 116     1402   1300   1911   -147     13     21       N  
ATOM   1034  CA AGLU A 116      14.342   5.136  14.885  0.50 14.12           C  
ANISOU 1034  CA AGLU A 116     1673   1523   2166    -22    -47    112       C  
ATOM   1035  CA BGLU A 116      14.379   5.257  14.858  0.50 13.01           C  
ANISOU 1035  CA BGLU A 116     1574   1283   2085     36    -52     -3       C  
ATOM   1036  C  AGLU A 116      14.202   6.198  15.962  0.50 12.95           C  
ANISOU 1036  C  AGLU A 116     1352   1452   2115      5   -145     45       C  
ATOM   1037  C  BGLU A 116      14.155   6.248  15.971  0.50 12.21           C  
ANISOU 1037  C  BGLU A 116     1282   1310   2046     34   -157    -50       C  
ATOM   1038  O  AGLU A 116      14.430   7.387  15.729  0.50 14.29           O  
ANISOU 1038  O  AGLU A 116     1861   1374   2192     -7   -192     99       O  
ATOM   1039  O  BGLU A 116      14.320   7.452  15.783  0.50 13.85           O  
ANISOU 1039  O  BGLU A 116     1893   1256   2112     26   -202     56       O  
ATOM   1040  CB AGLU A 116      15.808   4.937  14.429  0.50 16.51           C  
ANISOU 1040  CB AGLU A 116     2064   1848   2360     22    -47    254       C  
ATOM   1041  CB BGLU A 116      15.830   5.410  14.377  0.50 14.02           C  
ANISOU 1041  CB BGLU A 116     1924   1240   2162    116    -55    -10       C  
ATOM   1042  CG AGLU A 116      16.027   3.655  13.538  0.50 20.51           C  
ANISOU 1042  CG AGLU A 116     2369   2652   2771   -116    164    100       C  
ATOM   1043  CG BGLU A 116      16.841   4.993  15.416  0.50 15.45           C  
ANISOU 1043  CG BGLU A 116     1633   2032   2203     81    171     53       C  
ATOM   1044  CD AGLU A 116      17.350   2.852  13.761  0.50 25.53           C  
ANISOU 1044  CD AGLU A 116     2881   3231   3588   -162     91    204       C  
ATOM   1045  CD BGLU A 116      18.223   5.562  15.160  0.50 20.03           C  
ANISOU 1045  CD BGLU A 116     2205   2809   2596    -25     36    128       C  
ATOM   1046  OE1AGLU A 116      18.390   3.501  14.008  0.50 27.31           O  
ANISOU 1046  OE1AGLU A 116     2885   3734   3756   -458      2    359       O  
ATOM   1047  OE1BGLU A 116      18.420   6.802  15.075  0.50 24.33           O  
ANISOU 1047  OE1BGLU A 116     3181   3059   3005   -124    115    248       O  
ATOM   1048  OE2AGLU A 116      17.358   1.569  13.644  0.50 27.03           O  
ANISOU 1048  OE2AGLU A 116     2580   3693   3996   -724    225    611       O  
ATOM   1049  OE2BGLU A 116      19.152   4.774  15.092  0.50 20.88           O  
ANISOU 1049  OE2BGLU A 116     1996   2979   2956   -140    462   -112       O  
ATOM   1050  N   CYS A 117      13.789   5.758  17.136  1.00 12.48           N  
ANISOU 1050  N   CYS A 117     1393   1328   2020    254   -167    103       N  
ATOM   1051  CA  CYS A 117      13.509   6.582  18.312  1.00 13.41           C  
ANISOU 1051  CA  CYS A 117     1314   1543   2235    258   -253   -111       C  
ATOM   1052  C   CYS A 117      14.646   6.389  19.289  1.00 12.62           C  
ANISOU 1052  C   CYS A 117     1087   1559   2146    240   -141      5       C  
ATOM   1053  O   CYS A 117      14.849   5.259  19.712  1.00 13.62           O  
ANISOU 1053  O   CYS A 117     1459   1419   2295    166   -490     23       O  
ATOM   1054  CB  CYS A 117      12.152   6.173  18.924  1.00 14.95           C  
ANISOU 1054  CB  CYS A 117     1049   2136   2496    579   -240    -72       C  
ATOM   1055  SG  CYS A 117      10.781   6.186  17.749  1.00 18.42           S  
ANISOU 1055  SG  CYS A 117     1465   2920   2612    293   -357    111       S  
ATOM   1056  N   VAL A 118      15.247   7.468  19.748  1.00 12.06           N  
ANISOU 1056  N   VAL A 118     1002   1458   2120    242   -118     25       N  
ATOM   1057  CA  VAL A 118      16.438   7.379  20.563  1.00 12.97           C  
ANISOU 1057  CA  VAL A 118     1010   1487   2430    126     12     19       C  
ATOM   1058  C   VAL A 118      16.266   8.210  21.834  1.00 13.33           C  
ANISOU 1058  C   VAL A 118     1164   1614   2286    130    -88    107       C  
ATOM   1059  O   VAL A 118      15.944   9.415  21.763  1.00 12.98           O  
ANISOU 1059  O   VAL A 118     1100   1423   2408    250     -7     53       O  
ATOM   1060  CB  VAL A 118      17.711   7.785  19.811  1.00 14.76           C  
ANISOU 1060  CB  VAL A 118     1091   1900   2616     70    242    -35       C  
ATOM   1061  CG1 VAL A 118      18.881   7.821  20.683  1.00 19.47           C  
ANISOU 1061  CG1 VAL A 118     1374   2445   3575    310    -43     72       C  
ATOM   1062  CG2 VAL A 118      17.916   6.872  18.620  1.00 19.85           C  
ANISOU 1062  CG2 VAL A 118     2044   2540   2956   -124    455   -268       C  
ATOM   1063  N   MET A 119      16.458   7.618  22.979  1.00 13.23           N  
ANISOU 1063  N   MET A 119     1259   1382   2385    305   -189     12       N  
ATOM   1064  CA  MET A 119      16.487   8.318  24.258  1.00 15.04           C  
ANISOU 1064  CA  MET A 119     1504   1713   2497    271   -220     -8       C  
ATOM   1065  C   MET A 119      17.719   7.777  24.992  1.00 15.14           C  
ANISOU 1065  C   MET A 119     1392   1917   2440    157   -305    -39       C  
ATOM   1066  O   MET A 119      17.728   6.630  25.402  1.00 13.93           O  
ANISOU 1066  O   MET A 119     1274   1658   2360    261   -205     91       O  
ATOM   1067  CB  MET A 119      15.159   8.056  25.001  1.00 15.94           C  
ANISOU 1067  CB  MET A 119     1421   2077   2555    682   -257   -167       C  
ATOM   1068  CG  MET A 119      15.038   8.546  26.433  1.00 17.94           C  
ANISOU 1068  CG  MET A 119     2103   2008   2703    198   -236     35       C  
ATOM   1069  SD  MET A 119      14.736  10.255  26.353  1.00 22.97           S  
ANISOU 1069  SD  MET A 119     3033   2303   3391   1004   -855   -571       S  
ATOM   1070  CE  MET A 119      14.813  10.907  28.026  1.00 19.06           C  
ANISOU 1070  CE  MET A 119     2515   1943   2781   -108   -217   -491       C  
ATOM   1071  N  ALYS A 120      18.703   8.655  25.145  0.50 16.58           N  
ANISOU 1071  N  ALYS A 120     1744   1939   2616    107   -139     81       N  
ATOM   1072  N  BLYS A 120      18.785   8.559  25.182  0.50 16.87           N  
ANISOU 1072  N  BLYS A 120     1751   1982   2677     94   -195     36       N  
ATOM   1073  CA ALYS A 120      19.960   8.322  25.683  0.50 15.72           C  
ANISOU 1073  CA ALYS A 120     1464   1878   2630     91   -152    147       C  
ATOM   1074  CA BLYS A 120      19.910   8.156  26.017  0.50 17.14           C  
ANISOU 1074  CA BLYS A 120     1569   2075   2868    -22   -216     24       C  
ATOM   1075  C  ALYS A 120      20.526   7.102  24.964  0.50 11.99           C  
ANISOU 1075  C  ALYS A 120      787   1447   2318     76     -9    207       C  
ATOM   1076  C  BLYS A 120      20.440   6.730  25.873  0.50 16.03           C  
ANISOU 1076  C  BLYS A 120     1183   2161   2745     -6   -207     32       C  
ATOM   1077  O  ALYS A 120      20.649   7.112  23.762  0.50 12.61           O  
ANISOU 1077  O  ALYS A 120      703   1562   2527    202     49    431       O  
ATOM   1078  O  BLYS A 120      20.471   6.012  26.860  0.50 18.35           O  
ANISOU 1078  O  BLYS A 120     1363   2488   3122   -217   -182     70       O  
ATOM   1079  CB ALYS A 120      19.834   8.062  27.185  0.50 15.71           C  
ANISOU 1079  CB ALYS A 120     1464   1893   2610    121   -216    147       C  
ATOM   1080  CB BLYS A 120      19.546   8.244  27.490  0.50 16.68           C  
ANISOU 1080  CB BLYS A 120     1646   1871   2821    173   -351      1       C  
ATOM   1081  CG ALYS A 120      19.402   9.294  27.999  0.50 20.68           C  
ANISOU 1081  CG ALYS A 120     2279   2492   3088    254   -212    -84       C  
ATOM   1082  CG BLYS A 120      19.159   9.593  27.974  0.50 19.49           C  
ANISOU 1082  CG BLYS A 120     2210   2075   3117    359   -322    -56       C  
ATOM   1083  CD ALYS A 120      18.667   8.871  29.249  0.50 25.61           C  
ANISOU 1083  CD ALYS A 120     3069   3230   3430    177   -104   -172       C  
ATOM   1084  CD BLYS A 120      18.821   9.442  29.407  0.50 23.96           C  
ANISOU 1084  CD BLYS A 120     3036   2699   3365    249    -54   -170       C  
ATOM   1085  CE ALYS A 120      18.593   9.955  30.311  0.50 28.22           C  
ANISOU 1085  CE ALYS A 120     3573   3427   3720    106    -50   -212       C  
ATOM   1086  CE BLYS A 120      18.455  10.735  30.060  0.50 26.43           C  
ANISOU 1086  CE BLYS A 120     3338   2942   3763    137      0   -260       C  
ATOM   1087  NZ ALYS A 120      17.794   9.438  31.460  0.50 30.66           N  
ANISOU 1087  NZ ALYS A 120     3694   3883   4070   -132     -4   -155       N  
ATOM   1088  NZ BLYS A 120      18.307  10.565  31.532  0.50 29.79           N  
ANISOU 1088  NZ BLYS A 120     4049   3307   3960     -5    -49   -208       N  
ATOM   1089  N  AGLY A 121      20.856   6.034  25.706  0.50 10.19           N  
ANISOU 1089  N  AGLY A 121      349   1571   1952     93     91    299       N  
ATOM   1090  N  BGLY A 121      20.881   6.294  24.704  0.50 14.54           N  
ANISOU 1090  N  BGLY A 121      304   2383   2835   -279   -195     -4       N  
ATOM   1091  CA AGLY A 121      21.380   4.797  25.197  0.50 11.81           C  
ANISOU 1091  CA AGLY A 121      377   1842   2267     35    115    298       C  
ATOM   1092  CA BGLY A 121      21.361   4.930  24.555  0.50 13.58           C  
ANISOU 1092  CA BGLY A 121      253   2222   2685    -15     11    170       C  
ATOM   1093  C  AGLY A 121      20.375   3.814  24.632  0.50 11.74           C  
ANISOU 1093  C  AGLY A 121      312   1797   2352    254    -99    343       C  
ATOM   1094  C  BGLY A 121      20.343   3.861  24.315  0.50 12.58           C  
ANISOU 1094  C  BGLY A 121      271   1942   2564    137   -100    329       C  
ATOM   1095  O  AGLY A 121      20.761   2.716  24.253  0.50 14.79           O  
ANISOU 1095  O  AGLY A 121     1210   1845   2562    472    -44    221       O  
ATOM   1096  O  BGLY A 121      20.654   2.772  23.845  0.50 13.89           O  
ANISOU 1096  O  BGLY A 121      838   1929   2511    418     39    400       O  
ATOM   1097  N   VAL A 122      19.096   4.172  24.600  1.00 12.00           N  
ANISOU 1097  N   VAL A 122      326   1667   2566    -33   -104    292       N  
ATOM   1098  CA  VAL A 122      17.968   3.286  24.220  1.00 12.60           C  
ANISOU 1098  CA  VAL A 122      423   1786   2577    423     98    238       C  
ATOM   1099  C   VAL A 122      17.393   3.661  22.878  1.00 12.08           C  
ANISOU 1099  C   VAL A 122      594   1627   2369     43   -105     67       C  
ATOM   1100  O   VAL A 122      16.948   4.800  22.707  1.00 14.42           O  
ANISOU 1100  O   VAL A 122     1609   1407   2461    406   -405     25       O  
ATOM   1101  CB  VAL A 122      16.946   3.201  25.257  1.00 12.85           C  
ANISOU 1101  CB  VAL A 122      539   1602   2738      6     98    134       C  
ATOM   1102  CG1 VAL A 122      15.848   2.254  24.855  1.00 15.40           C  
ANISOU 1102  CG1 VAL A 122      924   1909   3016    287    375    114       C  
ATOM   1103  CG2 VAL A 122      17.478   2.761  26.640  1.00 16.14           C  
ANISOU 1103  CG2 VAL A 122     1232   2272   2628    379     46    398       C  
ATOM   1104  N   THR A 123      17.386   2.721  21.946  1.00 12.50           N  
ANISOU 1104  N   THR A 123      924   1475   2351    157   -133    120       N  
ATOM   1105  CA  THR A 123      16.865   2.920  20.601  1.00 13.70           C  
ANISOU 1105  CA  THR A 123     1318   1466   2419     36   -106     84       C  
ATOM   1106  C   THR A 123      15.705   1.960  20.339  1.00 13.46           C  
ANISOU 1106  C   THR A 123     1393   1319   2402    170   -270    110       C  
ATOM   1107  O   THR A 123      15.771   0.796  20.725  1.00 16.98           O  
ANISOU 1107  O   THR A 123     1775   1678   2998    -60   -520    429       O  
ATOM   1108  CB  THR A 123      17.907   2.668  19.572  1.00 15.83           C  
ANISOU 1108  CB  THR A 123     1538   1917   2559      0    -35     80       C  
ATOM   1109  OG1 THR A 123      18.976   3.589  19.794  1.00 18.88           O  
ANISOU 1109  OG1 THR A 123     2145   2192   2834   -156    283    -23       O  
ATOM   1110  CG2 THR A 123      17.386   2.845  18.152  1.00 17.44           C  
ANISOU 1110  CG2 THR A 123     1609   2462   2555     33    -63    -15       C  
ATOM   1111  N   SER A 124      14.662   2.424  19.712  1.00 12.75           N  
ANISOU 1111  N   SER A 124     1347   1311   2184      8   -225    184       N  
ATOM   1112  CA  SER A 124      13.617   1.598  19.176  1.00 13.03           C  
ANISOU 1112  CA  SER A 124     1142   1395   2413     14   -218    271       C  
ATOM   1113  C   SER A 124      13.542   1.798  17.702  1.00 12.34           C  
ANISOU 1113  C   SER A 124      910   1507   2269     93    -62    187       C  
ATOM   1114  O   SER A 124      13.613   2.933  17.216  1.00 14.97           O  
ANISOU 1114  O   SER A 124     2054   1441   2193      4    -43    149       O  
ATOM   1115  CB  SER A 124      12.261   1.902  19.802  1.00 13.50           C  
ANISOU 1115  CB  SER A 124     1201   1593   2336   -163   -116    348       C  
ATOM   1116  OG  SER A 124      11.207   1.240  19.185  1.00 14.05           O  
ANISOU 1116  OG  SER A 124     1072   1625   2639      0     23     78       O  
ATOM   1117  N   THR A 125      13.369   0.729  16.952  1.00 11.64           N  
ANISOU 1117  N   THR A 125      736   1378   2307     58    -60    185       N  
ATOM   1118  CA  THR A 125      13.211   0.772  15.499  1.00 11.89           C  
ANISOU 1118  CA  THR A 125      646   1555   2315    106     36    243       C  
ATOM   1119  C   THR A 125      11.827   0.334  15.117  1.00 12.10           C  
ANISOU 1119  C   THR A 125      793   1596   2207    -66      0    186       C  
ATOM   1120  O   THR A 125      11.416  -0.774  15.487  1.00 14.60           O  
ANISOU 1120  O   THR A 125     1505   1643   2397   -332   -152    201       O  
ATOM   1121  CB  THR A 125      14.255  -0.080  14.807  1.00 13.78           C  
ANISOU 1121  CB  THR A 125      672   1964   2598    182    288    223       C  
ATOM   1122  OG1 THR A 125      15.540   0.361  15.189  1.00 18.11           O  
ANISOU 1122  OG1 THR A 125      964   2699   3217    361    381    126       O  
ATOM   1123  CG2 THR A 125      14.151  -0.005  13.310  1.00 17.79           C  
ANISOU 1123  CG2 THR A 125     1634   2707   2416    217    251     69       C  
ATOM   1124  N   ARG A 126      11.136   1.169  14.366  1.00 12.44           N  
ANISOU 1124  N   ARG A 126     1050   1538   2137   -332   -129    102       N  
ATOM   1125  CA  ARG A 126       9.761   0.926  13.957  1.00 13.70           C  
ANISOU 1125  CA  ARG A 126     1349   1713   2141   -391    -11    235       C  
ATOM   1126  C   ARG A 126       9.737   0.991  12.429  1.00 12.52           C  
ANISOU 1126  C   ARG A 126      749   1854   2152   -293      9    169       C  
ATOM   1127  O   ARG A 126      10.170   1.976  11.851  1.00 16.67           O  
ANISOU 1127  O   ARG A 126     1960   2037   2335   -825    -44    196       O  
ATOM   1128  CB  ARG A 126       8.842   1.938  14.589  1.00 14.61           C  
ANISOU 1128  CB  ARG A 126     1127   2233   2189   -389   -130    161       C  
ATOM   1129  CG  ARG A 126       8.663   1.525  16.057  1.00 18.37           C  
ANISOU 1129  CG  ARG A 126     1322   3191   2467     70   -184    -45       C  
ATOM   1130  CD  ARG A 126       8.080   2.483  16.903  1.00 19.66           C  
ANISOU 1130  CD  ARG A 126     1301   3565   2604    -70   -254      1       C  
ATOM   1131  NE  ARG A 126       6.684   2.757  16.752  1.00 19.40           N  
ANISOU 1131  NE  ARG A 126     1251   3682   2434   -126   -278   -312       N  
ATOM   1132  CZ  ARG A 126       5.616   2.173  17.319  1.00 17.92           C  
ANISOU 1132  CZ  ARG A 126      726   3609   2474   -299    -45   -306       C  
ATOM   1133  NH1 ARG A 126       5.726   0.982  17.923  1.00 21.23           N  
ANISOU 1133  NH1 ARG A 126     1638   3908   2518   -141    298    -50       N  
ATOM   1134  NH2 ARG A 126       4.445   2.719  17.181  1.00 21.06           N  
ANISOU 1134  NH2 ARG A 126     1329   3725   2947   -100     35   -191       N  
ATOM   1135  N   VAL A 127       9.182  -0.014  11.780  1.00 11.78           N  
ANISOU 1135  N   VAL A 127      662   1607   2204   -108    -30    121       N  
ATOM   1136  CA  VAL A 127       9.206  -0.083  10.350  1.00 11.21           C  
ANISOU 1136  CA  VAL A 127      332   1666   2261   -267    216    106       C  
ATOM   1137  C   VAL A 127       7.802   0.016   9.842  1.00 10.59           C  
ANISOU 1137  C   VAL A 127      309   1530   2182   -243    146    -39       C  
ATOM   1138  O   VAL A 127       6.920  -0.708  10.230  1.00 11.63           O  
ANISOU 1138  O   VAL A 127      458   1698   2263   -273    -82    102       O  
ATOM   1139  CB  VAL A 127       9.875  -1.404   9.876  1.00 13.20           C  
ANISOU 1139  CB  VAL A 127      807   1840   2369    204     53     74       C  
ATOM   1140  CG1 VAL A 127       9.839  -1.499   8.333  1.00 15.71           C  
ANISOU 1140  CG1 VAL A 127     1512   2137   2317    343     64    -41       C  
ATOM   1141  CG2 VAL A 127      11.263  -1.552  10.412  1.00 15.35           C  
ANISOU 1141  CG2 VAL A 127     1006   1979   2845    330     52     51       C  
ATOM   1142  N   TYR A 128       7.621   0.943   8.869  1.00 11.54           N  
ANISOU 1142  N   TYR A 128      356   1660   2366   -216     87    145       N  
ATOM   1143  CA  TYR A 128       6.393   1.153   8.215  1.00 11.23           C  
ANISOU 1143  CA  TYR A 128      323   1606   2335   -141     63     82       C  
ATOM   1144  C   TYR A 128       6.491   0.727   6.743  1.00 10.92           C  
ANISOU 1144  C   TYR A 128      277   1485   2387   -171     34      7       C  
ATOM   1145  O   TYR A 128       7.516   0.950   6.138  1.00 12.60           O  
ANISOU 1145  O   TYR A 128      741   1714   2330   -190     51    -18       O  
ATOM   1146  CB  TYR A 128       5.957   2.641   8.255  1.00 11.56           C  
ANISOU 1146  CB  TYR A 128      279   1846   2266   -160    -94     61       C  
ATOM   1147  CG  TYR A 128       5.536   3.159   9.616  1.00 11.40           C  
ANISOU 1147  CG  TYR A 128      487   1486   2358   -201   -358     48       C  
ATOM   1148  CD1 TYR A 128       6.482   3.424  10.552  1.00 11.79           C  
ANISOU 1148  CD1 TYR A 128      330   1701   2448   -174    -90     25       C  
ATOM   1149  CD2 TYR A 128       4.198   3.348   9.918  1.00 10.97           C  
ANISOU 1149  CD2 TYR A 128      309   1580   2278   -184   -248      3       C  
ATOM   1150  CE1 TYR A 128       6.116   3.889  11.848  1.00 13.23           C  
ANISOU 1150  CE1 TYR A 128      644   1840   2542   -118   -223    -30       C  
ATOM   1151  CE2 TYR A 128       3.834   3.870  11.158  1.00 12.70           C  
ANISOU 1151  CE2 TYR A 128      447   1803   2575   -217     48     27       C  
ATOM   1152  CZ  TYR A 128       4.773   4.100  12.088  1.00 13.52           C  
ANISOU 1152  CZ  TYR A 128     1004   1661   2470   -310   -156    -43       C  
ATOM   1153  OH  TYR A 128       4.313   4.604  13.316  1.00 16.40           O  
ANISOU 1153  OH  TYR A 128     1455   2449   2324    253     65    -95       O  
ATOM   1154  N   GLU A 129       5.410   0.184   6.243  1.00 12.32           N  
ANISOU 1154  N   GLU A 129      519   1781   2381    -86     28     87       N  
ATOM   1155  CA AGLU A 129       5.231  -0.208   4.847  0.50 13.25           C  
ANISOU 1155  CA AGLU A 129      982   1717   2335    -75     57    -85       C  
ATOM   1156  CA BGLU A 129       5.325  -0.085   4.797  0.50 13.35           C  
ANISOU 1156  CA BGLU A 129     1062   1674   2333      7     16   -125       C  
ATOM   1157  C   GLU A 129       4.163   0.670   4.199  1.00 12.67           C  
ANISOU 1157  C   GLU A 129     1062   1533   2218   -218    -12   -126       C  
ATOM   1158  O   GLU A 129       3.338   1.207   4.881  1.00 12.86           O  
ANISOU 1158  O   GLU A 129     1026   1597   2262    -63    -16     39       O  
ATOM   1159  CB AGLU A 129       4.810  -1.686   4.794  0.50 14.62           C  
ANISOU 1159  CB AGLU A 129     1278   1878   2396   -138     26    -37       C  
ATOM   1160  CB BGLU A 129       5.224  -1.580   4.473  0.50 14.30           C  
ANISOU 1160  CB BGLU A 129     1272   1794   2365    144    -34    -58       C  
ATOM   1161  CG AGLU A 129       5.973  -2.627   5.090  0.50 19.47           C  
ANISOU 1161  CG AGLU A 129     2296   2402   2699    153     30     -7       C  
ATOM   1162  CG BGLU A 129       3.867  -2.206   4.785  0.50 19.61           C  
ANISOU 1162  CG BGLU A 129     2161   2399   2889   -118    -75   -110       C  
ATOM   1163  CD AGLU A 129       5.703  -4.054   4.656  0.50 23.08           C  
ANISOU 1163  CD AGLU A 129     2906   2667   3193   -312     17      5       C  
ATOM   1164  CD BGLU A 129       3.826  -3.747   4.616  0.50 23.92           C  
ANISOU 1164  CD BGLU A 129     2909   2757   3419   -310   -165   -186       C  
ATOM   1165  OE1AGLU A 129       4.750  -4.291   3.885  0.50 26.19           O  
ANISOU 1165  OE1AGLU A 129     3916   2880   3154   -176   -334   -182       O  
ATOM   1166  OE1BGLU A 129       2.760  -4.255   4.279  0.50 25.81           O  
ANISOU 1166  OE1BGLU A 129     3550   2441   3815   -615   -453    -72       O  
ATOM   1167  OE2AGLU A 129       6.427  -4.948   5.120  0.50 25.00           O  
ANISOU 1167  OE2AGLU A 129     2828   3036   3632   -118    109   -153       O  
ATOM   1168  OE2BGLU A 129       4.831  -4.451   4.840  0.50 26.20           O  
ANISOU 1168  OE2BGLU A 129     3290   3161   3503   -172   -311   -126       O  
ATOM   1169  N   ARG A 130       4.133   0.794   2.864  1.00 12.92           N  
ANISOU 1169  N   ARG A 130      848   1776   2285    -72    -80   -325       N  
ATOM   1170  CA  ARG A 130       3.045   1.485   2.240  1.00 13.89           C  
ANISOU 1170  CA  ARG A 130      949   1917   2411   -117   -141   -240       C  
ATOM   1171  C   ARG A 130       1.755   0.819   2.528  1.00 15.01           C  
ANISOU 1171  C   ARG A 130     1150   1888   2665   -221   -292   -253       C  
ATOM   1172  O   ARG A 130       1.622  -0.409   2.426  1.00 17.07           O  
ANISOU 1172  O   ARG A 130     1590   1844   3049   -169   -425   -170       O  
ATOM   1173  CB  ARG A 130       3.275   1.551   0.714  1.00 16.05           C  
ANISOU 1173  CB  ARG A 130     1252   2444   2401    -34   -339   -197       C  
ATOM   1174  CG  ARG A 130       4.490   2.279   0.286  1.00 17.25           C  
ANISOU 1174  CG  ARG A 130     1537   2426   2588    -75   -198     81       C  
ATOM   1175  CD  ARG A 130       4.213   3.698   0.031  1.00 21.38           C  
ANISOU 1175  CD  ARG A 130     1691   2746   3684     92   -261   -122       C  
ATOM   1176  NE  ARG A 130       5.378   4.398  -0.448  1.00 19.85           N  
ANISOU 1176  NE  ARG A 130     1362   2396   3781    110   -422    179       N  
ATOM   1177  CZ  ARG A 130       5.452   5.707  -0.585  1.00 17.60           C  
ANISOU 1177  CZ  ARG A 130     1252   2368   3064    -86   -259    218       C  
ATOM   1178  NH1 ARG A 130       4.421   6.419  -0.343  1.00 17.83           N  
ANISOU 1178  NH1 ARG A 130     1639   2290   2846   -251   -111    237       N  
ATOM   1179  NH2 ARG A 130       6.593   6.265  -0.932  1.00 19.78           N  
ANISOU 1179  NH2 ARG A 130     1789   2455   3271   -276    311    219       N  
ATOM   1180  N   ALA A 131       0.730   1.589   2.824  1.00 15.57           N  
ANISOU 1180  N   ALA A 131     1008   1932   2973   -271   -252    -67       N  
ATOM   1181  CA  ALA A 131      -0.569   1.035   3.146  1.00 19.28           C  
ANISOU 1181  CA  ALA A 131     1521   2385   3417   -312   -250    -58       C  
ATOM   1182  C   ALA A 131      -1.316   0.536   1.889  1.00 22.18           C  
ANISOU 1182  C   ALA A 131     1962   2782   3683   -448   -266    -46       C  
ATOM   1183  O   ALA A 131      -0.892   0.916   0.779  1.00 24.91           O  
ANISOU 1183  O   ALA A 131     2533   2999   3930   -360   -431     39       O  
ATOM   1184  CB  ALA A 131      -1.390   2.042   3.925  1.00 21.25           C  
ANISOU 1184  CB  ALA A 131     1636   2793   3644   -236    -82   -115       C  
TER    1185      ALA A 131                                                      
HETATM 1186  C1 AZGC A 133       3.984   6.315  22.766  0.50 20.67           C  
ANISOU 1186  C1 AZGC A 133     1921   2556   3375   -305    515    668       C  
HETATM 1187  C1 BZGC A 133       5.352   7.074  23.236  0.50 22.84           C  
ANISOU 1187  C1 BZGC A 133     2640   2116   3922    171    763    388       C  
HETATM 1188  O1 AZGC A 133       3.319   6.837  21.590  0.50 24.30           O  
ANISOU 1188  O1 AZGC A 133     2312   3633   3286     -7     17    428       O  
HETATM 1189  O1 BZGC A 133       4.247   7.059  22.326  0.50 29.65           O  
ANISOU 1189  O1 BZGC A 133     3906   3523   3833    111    196     24       O  
HETATM 1190  C2 AZGC A 133       4.233   7.054  20.610  0.50 22.65           C  
ANISOU 1190  C2 AZGC A 133     2562   2960   3082    316    122    127       C  
HETATM 1191  C2 BZGC A 133       4.800   7.294  21.112  0.50 26.18           C  
ANISOU 1191  C2 BZGC A 133     3298   3206   3441    240    182    -99       C  
HETATM 1192  O2 AZGC A 133       5.844   4.973  15.285  0.50 17.92           O  
ANISOU 1192  O2 AZGC A 133     1681   2520   2608    588   -471   -298       O  
HETATM 1193  O2 BZGC A 133       6.222   4.925  15.360  0.50 24.03           O  
ANISOU 1193  O2 BZGC A 133     2745   3204   3180    286   -131   -376       O  
HETATM 1194  C3 AZGC A 133       3.965   6.649  19.298  0.50 24.87           C  
ANISOU 1194  C3 AZGC A 133     2911   3451   3085     36      3     34       C  
HETATM 1195  C3 BZGC A 133       4.047   7.212  19.942  0.50 27.10           C  
ANISOU 1195  C3 BZGC A 133     3463   3357   3476    230    132   -112       C  
HETATM 1196  O3 AZGC A 133       5.547   7.175  15.252  0.50 23.86           O  
ANISOU 1196  O3 AZGC A 133     3056   2647   3360    458   -187   -107       O  
HETATM 1197  O3 BZGC A 133       5.515   7.000  15.006  0.50 26.97           O  
ANISOU 1197  O3 BZGC A 133     3356   3267   3623     29   -237    125       O  
HETATM 1198  C4 AZGC A 133       4.919   6.824  18.296  0.50 25.04           C  
ANISOU 1198  C4 AZGC A 133     2933   3478   3102     79    102   -171       C  
HETATM 1199  C4 BZGC A 133       4.666   7.429  18.712  0.50 26.16           C  
ANISOU 1199  C4 BZGC A 133     3335   3200   3402    199     73   -163       C  
HETATM 1200  C5 AZGC A 133       5.454   7.644  20.901  0.50 21.92           C  
ANISOU 1200  C5 AZGC A 133     2188   2744   3397    373     12    140       C  
HETATM 1201  C5 BZGC A 133       6.159   7.580  21.052  0.50 27.77           C  
ANISOU 1201  C5 BZGC A 133     3639   3380   3533   -128      1     -1       C  
HETATM 1202  C6 AZGC A 133       6.425   7.786  19.892  0.50 23.35           C  
ANISOU 1202  C6 AZGC A 133     2839   2890   3141    391    121    -50       C  
HETATM 1203  C6 BZGC A 133       6.781   7.799  19.826  0.50 26.13           C  
ANISOU 1203  C6 BZGC A 133     3202   3307   3417    171    -29    -41       C  
HETATM 1204  C7 AZGC A 133       6.161   7.398  18.571  0.50 23.96           C  
ANISOU 1204  C7 AZGC A 133     2818   3049   3235    287   -257    -81       C  
HETATM 1205  C7 BZGC A 133       6.023   7.732  18.652  0.50 26.75           C  
ANISOU 1205  C7 BZGC A 133     3361   3347   3453     -1    -96   -196       C  
HETATM 1206  C8 AZGC A 133       7.237   7.595  17.441  0.50 20.56           C  
ANISOU 1206  C8 AZGC A 133     1777   2430   3605    531   -564   -295       C  
HETATM 1207  C8 BZGC A 133       6.692   7.980  17.283  0.50 26.88           C  
ANISOU 1207  C8 BZGC A 133     3237   3214   3758   -126    -55   -176       C  
HETATM 1208  C9 AZGC A 133       7.388   6.345  16.529  0.50 22.06           C  
ANISOU 1208  C9 AZGC A 133     2056   2775   3550      6   -361   -472       C  
HETATM 1209  C9 BZGC A 133       7.200   6.673  16.648  0.50 26.05           C  
ANISOU 1209  C9 BZGC A 133     2853   3265   3777    -31   -188   -323       C  
HETATM 1210  C10AZGC A 133       6.177   6.146  15.593  0.50 20.34           C  
ANISOU 1210  C10AZGC A 133     1401   2488   3838    113   -398    -28       C  
HETATM 1211  C10BZGC A 133       6.246   6.155  15.568  0.50 23.10           C  
ANISOU 1211  C10BZGC A 133     1739   2953   4085   -186   -222      5       C  
HETATM 1212  O   HOH A 134       6.475  23.367  26.487  1.00 51.30           O  
ANISOU 1212  O   HOH A 134     7180   8411   3899    558     48   1512       O  
HETATM 1213  O   HOH A 135      -3.571   3.273  29.177  1.00 30.34           O  
ANISOU 1213  O   HOH A 135     2820   3507   5200   -167   -763   -538       O  
HETATM 1214  O   HOH A 136       9.588  32.950   8.161  1.00 33.86           O  
ANISOU 1214  O   HOH A 136     3843   3103   5919    -22  -1512   -556       O  
HETATM 1215  O   HOH A 137      10.354  22.054  12.708  1.00 11.15           O  
ANISOU 1215  O   HOH A 137      463   1403   2368     89     30    -27       O  
HETATM 1216  O   HOH A 138       7.273  -3.139   1.600  1.00 41.67           O  
ANISOU 1216  O   HOH A 138     6176   3139   6517    263   1092    274       O  
HETATM 1217  O   HOH A 139      12.373  10.335  31.837  1.00 41.92           O  
ANISOU 1217  O   HOH A 139     4483   6644   4798  -2031   -168   -834       O  
HETATM 1218  O   HOH A 140      -2.783   0.726  -1.212  1.00 40.82           O  
ANISOU 1218  O   HOH A 140     4075   6168   5266   -560  -1570    242       O  
HETATM 1219  O   HOH A 141      18.454  11.802  21.537  1.00 39.90           O  
ANISOU 1219  O   HOH A 141     5314   5426   4420   1143   -122   -705       O  
HETATM 1220  O   HOH A 142      -3.397  14.522  19.577  1.00 33.51           O  
ANISOU 1220  O   HOH A 142     2362   5546   4821   -568    512   -261       O  
HETATM 1221  O   HOH A 143      13.648  26.660  15.279  1.00 13.37           O  
ANISOU 1221  O   HOH A 143      643   1632   2805   -301   -135    -59       O  
HETATM 1222  O   HOH A 144       7.180  24.885  12.250  1.00 12.86           O  
ANISOU 1222  O   HOH A 144      310   1874   2701     37    108   -354       O  
HETATM 1223  O   HOH A 145      -3.782  -0.494  22.407  1.00 13.43           O  
ANISOU 1223  O   HOH A 145      878   1692   2532   -214   -111     30       O  
HETATM 1224  O   HOH A 146       4.645  24.333  13.139  1.00 13.11           O  
ANISOU 1224  O   HOH A 146      523   1832   2626    -58    -94   -344       O  
HETATM 1225  O   HOH A 147       2.276  30.196  -7.100  1.00 39.11           O  
ANISOU 1225  O   HOH A 147     6904   4621   3332    124   -124     11       O  
HETATM 1226  O   HOH A 148       2.867  -2.374   1.103  1.00 39.41           O  
ANISOU 1226  O   HOH A 148     5793   3996   5183    726   -114  -2063       O  
HETATM 1227  O   HOH A 149       8.875  28.750  16.942  1.00 25.64           O  
ANISOU 1227  O   HOH A 149     2445   2468   4829     -6    466   -557       O  
HETATM 1228  O   HOH A 150      13.110  -4.002   2.583  1.00 45.32           O  
ANISOU 1228  O   HOH A 150     7366   3732   6120    730  -1007   1610       O  
HETATM 1229  O   HOH A 151      11.746  12.410  12.127  1.00 13.90           O  
ANISOU 1229  O   HOH A 151     1483   1529   2266    224    186    -12       O  
HETATM 1230  O   HOH A 152       9.756  22.932   5.347  1.00 16.30           O  
ANISOU 1230  O   HOH A 152     1110   2691   2391    280   -138   -133       O  
HETATM 1231  O   HOH A 153       9.570  -9.045  20.493  1.00 43.40           O  
ANISOU 1231  O   HOH A 153     2983   8025   5480    626  -1065  -2046       O  
HETATM 1232  O   HOH A 154      -1.853  -3.966  11.846  1.00 42.16           O  
ANISOU 1232  O   HOH A 154     6414   4942   4662  -2859   -526   -107       O  
HETATM 1233  O   HOH A 155      19.085  19.656  25.150  1.00 46.57           O  
ANISOU 1233  O   HOH A 155     6619   5824   5252    222  -1330  -1823       O  
HETATM 1234  O   HOH A 156       7.612  25.771  -0.994  1.00 39.22           O  
ANISOU 1234  O   HOH A 156     2978   6908   5015  -1820    -62   -316       O  
HETATM 1235  O   HOH A 157      15.215   9.027   3.246  1.00 18.17           O  
ANISOU 1235  O   HOH A 157     2188   1992   2722   -333    573    177       O  
HETATM 1236  O   HOH A 158       1.043  20.154   5.046  1.00 17.16           O  
ANISOU 1236  O   HOH A 158      983   2713   2825   -136    -76    288       O  
HETATM 1237  O   HOH A 159      12.814  12.160  -3.124  1.00 43.71           O  
ANISOU 1237  O   HOH A 159     5170   5793   5641  -1973   1766  -1154       O  
HETATM 1238  O   HOH A 160       5.745  -6.794   6.425  1.00 59.18           O  
ANISOU 1238  O   HOH A 160     9558   3504   9421    499    960  -1114       O  
HETATM 1239  O   HOH A 161      22.542   9.224   8.861  1.00 38.52           O  
ANISOU 1239  O   HOH A 161     5220   4681   4731   -367   -197    495       O  
HETATM 1240  O   HOH A 162       4.096   9.339  15.485  1.00 31.09           O  
ANISOU 1240  O   HOH A 162     4050   3429   4331    616   1654    652       O  
HETATM 1241  O   HOH A 163      -3.668  -1.011  19.710  1.00 16.18           O  
ANISOU 1241  O   HOH A 163      939   2359   2847   -680    -78    182       O  
HETATM 1242  O   HOH A 164      -4.865   3.512   5.329  1.00 53.96           O  
ANISOU 1242  O   HOH A 164     4093   7694   8716    869  -2218   -412       O  
HETATM 1243  O   HOH A 165       9.988  -7.142  15.635  1.00 42.25           O  
ANISOU 1243  O   HOH A 165     3964   3449   8640    651    190    412       O  
HETATM 1244  O   HOH A 166      24.006   7.533  24.660  1.00 44.66           O  
ANISOU 1244  O   HOH A 166     3032   6940   6997    -68    368    577       O  
HETATM 1245  O   HOH A 167       3.426  11.369  19.361  1.00 17.45           O  
ANISOU 1245  O   HOH A 167     1606   2324   2700   -437    241     19       O  
HETATM 1246  O   HOH A 168       4.138  27.103   2.316  1.00 20.66           O  
ANISOU 1246  O   HOH A 168     1579   2533   3736    279   -260     68       O  
HETATM 1247  O   HOH A 169       1.616   5.730   0.123  1.00 18.26           O  
ANISOU 1247  O   HOH A 169     1958   2265   2713   -217      3   -329       O  
HETATM 1248  O   HOH A 170      13.939  -2.132  31.474  1.00 38.26           O  
ANISOU 1248  O   HOH A 170     3912   5386   5239   1493   -450    973       O  
HETATM 1249  O   HOH A 171      16.232  21.123   7.185  1.00 19.91           O  
ANISOU 1249  O   HOH A 171     2464   1846   3255   -248    113    128       O  
HETATM 1250  O   HOH A 172       9.556  -3.859  23.294  1.00 37.04           O  
ANISOU 1250  O   HOH A 172     5514   4738   3820   -577   -378    982       O  
HETATM 1251  O   HOH A 173      14.641  25.101  17.377  1.00 18.29           O  
ANISOU 1251  O   HOH A 173     1372   2168   3409   -127   -256   -171       O  
HETATM 1252  O   HOH A 174       1.817  12.891  14.366  1.00 20.33           O  
ANISOU 1252  O   HOH A 174     2077   2747   2900   -325     69    887       O  
HETATM 1253  O   HOH A 175      -5.938   3.352  27.278  1.00 32.66           O  
ANISOU 1253  O   HOH A 175     1419   3691   7299   -102    223   -574       O  
HETATM 1254  O   HOH A 176       2.898  31.924  -9.144  1.00 24.80           O  
ANISOU 1254  O   HOH A 176     3209   2751   3463      3    126    110       O  
HETATM 1255  O   HOH A 177      14.243   0.703  31.729  1.00 33.30           O  
ANISOU 1255  O   HOH A 177     3513   5081   4056    104    136    188       O  
HETATM 1256  O   HOH A 178      25.248   5.330  23.846  1.00 41.93           O  
ANISOU 1256  O   HOH A 178     6261   5174   4496  -1517   1426    381       O  
HETATM 1257  O   HOH A 179      18.990  17.935  14.786  1.00 30.74           O  
ANISOU 1257  O   HOH A 179     2291   4083   5303    -85     59    598       O  
HETATM 1258  O   HOH A 180      16.428   0.655  32.763  1.00 43.73           O  
ANISOU 1258  O   HOH A 180     5503   5802   5308    -76  -1021   2519       O  
HETATM 1259  O   HOH A 181       8.786  10.502  21.474  1.00 17.59           O  
ANISOU 1259  O   HOH A 181     1916   1934   2831   -159    282    -40       O  
HETATM 1260  O   HOH A 182      19.109  19.154  17.542  1.00 35.77           O  
ANISOU 1260  O   HOH A 182     3425   4426   5736  -1240    727   -151       O  
HETATM 1261  O   HOH A 183      16.205  18.803  14.197  1.00 21.84           O  
ANISOU 1261  O   HOH A 183     2811   2469   3017   -690   -315    220       O  
HETATM 1262  O   HOH A 184      15.962  21.114  19.420  1.00 30.81           O  
ANISOU 1262  O   HOH A 184     2279   3351   6074     58   -348    799       O  
HETATM 1263  O   HOH A 185      -7.602   6.657  19.051  1.00 32.91           O  
ANISOU 1263  O   HOH A 185     2723   4797   4982   1018    412  -1029       O  
HETATM 1264  O   HOH A 186       6.043  27.577  15.296  1.00 18.20           O  
ANISOU 1264  O   HOH A 186     1035   2193   3687     61   -543    -89       O  
HETATM 1265  O   HOH A 187       7.951   2.513  -2.755  1.00 37.18           O  
ANISOU 1265  O   HOH A 187     6159   3678   4288   1303   -681    496       O  
HETATM 1266  O   HOH A 188      14.270  18.841   0.372  1.00 29.90           O  
ANISOU 1266  O   HOH A 188     4383   4214   2763   1565   -389     45       O  
HETATM 1267  O   HOH A 189      16.844  19.308   1.898  1.00 28.62           O  
ANISOU 1267  O   HOH A 189     3440   4014   3420    154    472    758       O  
HETATM 1268  O   HOH A 190      21.230   7.367   8.236  1.00 38.81           O  
ANISOU 1268  O   HOH A 190     3596   5919   5228   1470   -886  -1092       O  
HETATM 1269  O   HOH A 191      16.084  21.339   4.146  1.00 38.12           O  
ANISOU 1269  O   HOH A 191     5066   5408   4009  -2004     -1   1036       O  
HETATM 1270  O   HOH A 192       8.691  -3.033  20.227  1.00 20.80           O  
ANISOU 1270  O   HOH A 192     1357   2506   4040    293   -310   -305       O  
HETATM 1271  O   HOH A 193      20.563   1.237  32.528  1.00 44.66           O  
ANISOU 1271  O   HOH A 193     6574   4223   6170    487   1612  -1483       O  
HETATM 1272  O   HOH A 194       8.790  21.178   2.941  1.00 42.14           O  
ANISOU 1272  O   HOH A 194     4287   4346   7379   -992   1212  -1241       O  
HETATM 1273  O   HOH A 195      15.735  -3.276  15.868  1.00 35.85           O  
ANISOU 1273  O   HOH A 195     3395   2293   7932     84   1007   -484       O  
HETATM 1274  O   HOH A 196      13.495  22.164   0.167  1.00 42.62           O  
ANISOU 1274  O   HOH A 196     7036   4673   4482   1024   1357    893       O  
HETATM 1275  O   HOH A 197      -2.177  30.140 -12.894  1.00 35.03           O  
ANISOU 1275  O   HOH A 197     2942   4995   5370  -1097   -204   -423       O  
HETATM 1276  O   HOH A 198       2.993  21.303  23.676  1.00 42.04           O  
ANISOU 1276  O   HOH A 198     7589   3438   4947   1338   2260    -92       O  
HETATM 1277  O   HOH A 199      12.191 -10.258  16.948  1.00 44.00           O  
ANISOU 1277  O   HOH A 199     6953   3414   6349   -740  -1101    144       O  
HETATM 1278  O   HOH A 200      20.856  11.185  10.704  1.00 43.52           O  
ANISOU 1278  O   HOH A 200     2714   7993   5825    375     63    385       O  
HETATM 1279  O   HOH A 201      11.145   6.777  -3.155  1.00 44.24           O  
ANISOU 1279  O   HOH A 201     4649   7548   4612   2497    712   1703       O  
HETATM 1280  O   HOH A 202       2.739  -7.946  17.101  1.00 43.40           O  
ANISOU 1280  O   HOH A 202     2109   6149   8231     19   -908   -663       O  
HETATM 1281  O   HOH A 203       5.885  -2.421  22.947  1.00 35.60           O  
ANISOU 1281  O   HOH A 203     2687   6679   4158    422   -686   -363       O  
HETATM 1282  O   HOH A 204      -1.154  16.693  -0.596  1.00 39.00           O  
ANISOU 1282  O   HOH A 204     2904   6905   5009    952   -165   2206       O  
HETATM 1283  O   HOH A 205      -0.674  14.321   6.376  1.00 18.45           O  
ANISOU 1283  O   HOH A 205     1744   2144   3123    311   -145     29       O  
HETATM 1284  O   HOH A 206      -5.353  13.931  14.873  1.00 41.79           O  
ANISOU 1284  O   HOH A 206     3754   3909   8215    800    662   1063       O  
HETATM 1285  O   HOH A 207      20.137   5.020  28.461  1.00 23.28           O  
ANISOU 1285  O   HOH A 207     2596   2487   3761    566   -649     26       O  
HETATM 1286  O   HOH A 208      -6.657  11.923   6.020  1.00 42.58           O  
ANISOU 1286  O   HOH A 208     3984   7112   5080    669   1339   1848       O  
HETATM 1287  O   HOH A 209       6.169  -8.434  18.604  1.00 47.84           O  
ANISOU 1287  O   HOH A 209     6858   5883   5434  -1828   -588    212       O  
HETATM 1288  O   HOH A 210       6.325  11.373  19.531  1.00 19.65           O  
ANISOU 1288  O   HOH A 210     1510   2259   3694   -476    168   -193       O  
HETATM 1289  O   HOH A 211      19.091  20.561   7.035  1.00 41.11           O  
ANISOU 1289  O   HOH A 211     4052   3642   7926  -1020   2552  -1362       O  
HETATM 1290  O   HOH A 212      14.360  -5.377  22.605  1.00 31.35           O  
ANISOU 1290  O   HOH A 212     5252   2399   4261    250  -1681    224       O  
HETATM 1291  O   HOH A 213      16.901  20.663  17.294  1.00 37.02           O  
ANISOU 1291  O   HOH A 213     2221   4981   6862   1204    509   1620       O  
HETATM 1292  O   HOH A 214      16.229  -3.260  29.378  1.00 42.24           O  
ANISOU 1292  O   HOH A 214     2173   4969   8908    845   1333   1820       O  
HETATM 1293  O   HOH A 215      -4.451   1.996  12.440  1.00 60.82           O  
ANISOU 1293  O   HOH A 215     7659   8810   6636  -1629  -6475   3354       O  
HETATM 1294  O   HOH A 216       1.610  26.150   2.071  1.00 23.19           O  
ANISOU 1294  O   HOH A 216     2100   1995   4713     17     69   -373       O  
HETATM 1295  O   HOH A 217      19.733   1.725  15.087  1.00 36.76           O  
ANISOU 1295  O   HOH A 217     4279   5318   4369     -6   -508    784       O  
HETATM 1296  O   HOH A 218      -8.737  11.899  18.012  1.00 46.07           O  
ANISOU 1296  O   HOH A 218     4187   5336   7979   1331    442  -1999       O  
HETATM 1297  O   HOH A 219       2.639   6.796  13.673  1.00 22.55           O  
ANISOU 1297  O   HOH A 219     2164   2476   3925   -361    781   -291       O  
HETATM 1298  O   HOH A 220      -1.682  -0.105  10.131  1.00 53.09           O  
ANISOU 1298  O   HOH A 220     7496   5593   7082   -630  -2671   2544       O  
HETATM 1299  O   HOH A 221      12.623  -5.278  27.905  1.00 48.54           O  
ANISOU 1299  O   HOH A 221     3763   3777  10901    758   2769   1383       O  
HETATM 1300  O   HOH A 222       2.146   9.794  17.381  1.00 17.90           O  
ANISOU 1300  O   HOH A 222     1778   2330   2690   -473   -123     15       O  
HETATM 1301  O   HOH A 223      11.288  -3.087  13.799  1.00 21.10           O  
ANISOU 1301  O   HOH A 223     2282   2448   3284   -117    -61    -32       O  
HETATM 1302  O   HOH A 224      11.299  -2.859   0.911  1.00 21.95           O  
ANISOU 1302  O   HOH A 224     3045   2121   3173   -374     15     36       O  
HETATM 1303  O   HOH A 225       1.643  15.744  -0.234  1.00 21.86           O  
ANISOU 1303  O   HOH A 225     3329   2641   2335    423   -596   -307       O  
HETATM 1304  O   HOH A 226      11.433  -5.734  21.142  1.00 24.74           O  
ANISOU 1304  O   HOH A 226     3489   1670   4240   -287    521    529       O  
HETATM 1305  O   HOH A 227       7.031  27.712  11.874  1.00 20.55           O  
ANISOU 1305  O   HOH A 227     1254   2271   4282    374   -495   -164       O  
HETATM 1306  O   HOH A 228       9.055  -4.107  -1.816  1.00 40.08           O  
ANISOU 1306  O   HOH A 228     7135   3556   4536   -667    942    684       O  
HETATM 1307  O   HOH A 229       3.375  -7.068  10.834  1.00 70.83           O  
ANISOU 1307  O   HOH A 229     7230   6671  13009  -3739  -2714   2160       O  
HETATM 1308  O   HOH A 230       6.268   9.014  -1.778  1.00 22.41           O  
ANISOU 1308  O   HOH A 230     2114   2833   3566   -532    307   -358       O  
HETATM 1309  O   HOH A 231      17.523  13.219  30.588  1.00 45.29           O  
ANISOU 1309  O   HOH A 231     5922   7061   4225    568  -1023    973       O  
HETATM 1310  O   HOH A 232       1.812   3.953  19.880  1.00 38.46           O  
ANISOU 1310  O   HOH A 232     3133   5010   6470   -633   -666   1078       O  
HETATM 1311  O   HOH A 233      -8.555   5.703  17.553  1.00 38.30           O  
ANISOU 1311  O   HOH A 233     1600   5455   7497    766   1024   -384       O  
HETATM 1312  O   HOH A 234       6.178  -0.565   1.381  1.00 20.17           O  
ANISOU 1312  O   HOH A 234     1061   3039   3562    140    143   -377       O  
HETATM 1313  O   HOH A 235       0.426  18.530  18.942  1.00 31.96           O  
ANISOU 1313  O   HOH A 235     3230   3455   5458   -741  -1771   1576       O  
HETATM 1314  O   HOH A 236      12.986  21.683  19.849  1.00 22.10           O  
ANISOU 1314  O   HOH A 236     2056   3868   2472   -901    -49   -283       O  
HETATM 1315  O   HOH A 237       9.204   7.240  -3.101  1.00 48.59           O  
ANISOU 1315  O   HOH A 237     5582   7035   5844    128    136    500       O  
HETATM 1316  O   HOH A 238      -2.573  19.936   1.478  1.00 25.17           O  
ANISOU 1316  O   HOH A 238     2914   3502   3145  -1501   -245    333       O  
HETATM 1317  O   HOH A 239      21.030   7.826  15.063  1.00 41.20           O  
ANISOU 1317  O   HOH A 239     4594   4400   6657    582    214   1278       O  
HETATM 1318  O   HOH A 240      14.663   1.602  29.261  1.00 22.88           O  
ANISOU 1318  O   HOH A 240     1728   3788   3176    942   -148    516       O  
HETATM 1319  O   HOH A 241      17.374  13.350  28.012  1.00 27.85           O  
ANISOU 1319  O   HOH A 241     2223   3685   4671    901   -397    986       O  
HETATM 1320  O   HOH A 242      10.776   9.883  -4.114  1.00 45.62           O  
ANISOU 1320  O   HOH A 242     5336   7589   4407   -388    805   -247       O  
HETATM 1321  O   HOH A 243      15.841  -3.057  -2.624  1.00 29.05           O  
ANISOU 1321  O   HOH A 243     5181   3188   2667    373    381    380       O  
HETATM 1322  O   HOH A 244       2.855  13.800  18.210  1.00 22.58           O  
ANISOU 1322  O   HOH A 244     2545   2397   3637   -406    349     20       O  
HETATM 1323  O   HOH A 245       0.160   3.421  -0.268  1.00 24.88           O  
ANISOU 1323  O   HOH A 245     2798   2675   3980   -240   -915    -63       O  
HETATM 1324  O   HOH A 246       2.891   1.043  18.828  1.00 22.20           O  
ANISOU 1324  O   HOH A 246     1765   3769   2898   -566     94    -87       O  
HETATM 1325  O   HOH A 247       0.384   5.195  32.413  1.00 25.09           O  
ANISOU 1325  O   HOH A 247     3276   3534   2720   -236    -69   -232       O  
HETATM 1326  O   HOH A 248       4.740  10.197  29.309  1.00 26.70           O  
ANISOU 1326  O   HOH A 248     4606   2559   2978   -205     69    555       O  
HETATM 1327  O   HOH A 249       5.045  22.663  24.072  1.00 30.90           O  
ANISOU 1327  O   HOH A 249     3914   4033   3791   1855    497    -93       O  
HETATM 1328  O   HOH A 250      -2.081  15.931  17.757  1.00 26.85           O  
ANISOU 1328  O   HOH A 250     4714   2658   2828    -86    622   -388       O  
HETATM 1329  O   HOH A 251      -0.771  18.681   3.742  1.00 21.61           O  
ANISOU 1329  O   HOH A 251     2003   2810   3395      3   -564    148       O  
HETATM 1330  O   HOH A 252      -0.052   5.206  18.491  1.00 31.26           O  
ANISOU 1330  O   HOH A 252     2641   3692   5542   -728  -1503   1580       O  
HETATM 1331  O   HOH A 253      18.763  17.147   2.574  1.00 26.13           O  
ANISOU 1331  O   HOH A 253     2727   3765   3434    165    592   -408       O  
HETATM 1332  O   HOH A 254       0.840  15.753  18.493  1.00 24.06           O  
ANISOU 1332  O   HOH A 254     2474   3249   3418    -79    507   -147       O  
HETATM 1333  O   HOH A 255      20.675   5.072  21.590  1.00 23.49           O  
ANISOU 1333  O   HOH A 255     2018   2889   4015    233     -6    152       O  
HETATM 1334  O   HOH A 256      -7.244   9.528  19.703  1.00 28.32           O  
ANISOU 1334  O   HOH A 256     1889   5167   3702     -1    389    -89       O  
HETATM 1335  O   HOH A 257      17.706  13.865  21.733  1.00 24.56           O  
ANISOU 1335  O   HOH A 257     2212   3897   3222   -324    -28   -666       O  
HETATM 1336  O   HOH A 258       2.163  -3.677  24.856  1.00 25.20           O  
ANISOU 1336  O   HOH A 258     2684   3459   3429    625   -193   -537       O  
HETATM 1337  O   HOH A 259       6.029  12.275  16.545  1.00 30.44           O  
ANISOU 1337  O   HOH A 259      974   7202   3389  -1094    387    332       O  
HETATM 1338  O   HOH A 260       8.968  12.101  30.770  1.00 27.94           O  
ANISOU 1338  O   HOH A 260     4569   2889   3156   -247    738    357       O  
HETATM 1339  O   HOH A 261       4.985  -1.596  25.593  1.00 27.70           O  
ANISOU 1339  O   HOH A 261     2631   3580   4314    759   -559   -459       O  
HETATM 1340  O   HOH A 262      18.230  11.370  24.291  1.00 29.13           O  
ANISOU 1340  O   HOH A 262     1107   2533   7427    304    369    780       O  
HETATM 1341  O   HOH A 263      18.253   4.407   2.529  1.00 26.54           O  
ANISOU 1341  O   HOH A 263     2216   4737   3128    385    -37   -345       O  
HETATM 1342  O   HOH A 264      -8.163   6.394  15.069  1.00 33.10           O  
ANISOU 1342  O   HOH A 264     2419   4846   5311   -311   -196   1118       O  
HETATM 1343  O   HOH A 265       5.155  29.021   3.988  1.00 35.96           O  
ANISOU 1343  O   HOH A 265     4463   3356   5843  -1258    464  -1205       O  
HETATM 1344  O   HOH A 266       9.080  21.323  29.566  1.00 29.06           O  
ANISOU 1344  O   HOH A 266     3660   3617   3760   1407   -278   -794       O  
HETATM 1345  O   HOH A 267      16.981   7.126   2.184  1.00 32.49           O  
ANISOU 1345  O   HOH A 267     4438   3273   4632  -1234   1228   -198       O  
HETATM 1346  O   HOH A 268      15.394  19.815  27.268  1.00 29.08           O  
ANISOU 1346  O   HOH A 268     4745   2897   3404   -459   -953   -195       O  
HETATM 1347  O   HOH A 269      -2.050  20.290  11.414  1.00 29.69           O  
ANISOU 1347  O   HOH A 269     2475   2934   5870   -464   1671   -255       O  
HETATM 1348  O   HOH A 270       6.368   8.538  12.881  1.00 25.14           O  
ANISOU 1348  O   HOH A 270     1778   4345   3430   -734    497   -223       O  
HETATM 1349  O   HOH A 271      16.171  -0.884  17.640  1.00 35.64           O  
ANISOU 1349  O   HOH A 271     6460   3656   3424   2134  -1692   -648       O  
HETATM 1350  O   HOH A 272      22.664   2.219  22.237  1.00 21.55           O  
ANISOU 1350  O   HOH A 272     2747   1947   3491    -79    728    -90       O  
HETATM 1351  O   HOH A 273      -0.032   7.893  17.528  1.00 21.91           O  
ANISOU 1351  O   HOH A 273     2211   2781   3331   -330     68    100       O  
HETATM 1352  O   HOH A 274      -0.393  -5.010  17.750  1.00 29.00           O  
ANISOU 1352  O   HOH A 274     2547   2676   5792     49    133    611       O  
HETATM 1353  O   HOH A 275      -4.738  11.955  13.398  1.00 33.46           O  
ANISOU 1353  O   HOH A 275     2525   6411   3776    420   -337    708       O  
HETATM 1354  O   HOH A 276       8.327  -3.315  22.654  1.00 32.06           O  
ANISOU 1354  O   HOH A 276     3841   2623   5714   -390   -119     61       O  
HETATM 1355  O   HOH A 277       8.624  -6.024  20.264  1.00 35.82           O  
ANISOU 1355  O   HOH A 277     4470   4601   4539    771    407   -295       O  
HETATM 1356  O   HOH A 278       4.762  17.131  29.637  1.00 33.21           O  
ANISOU 1356  O   HOH A 278     6467   3282   2867   -682    186     74       O  
HETATM 1357  O   HOH A 279       8.842   4.902  32.833  1.00 27.49           O  
ANISOU 1357  O   HOH A 279     2783   3631   4031     22   -962   -288       O  
HETATM 1358  O   HOH A 280       2.702  12.267  29.975  1.00 36.16           O  
ANISOU 1358  O   HOH A 280     6579   3293   3864    638    -30   -118       O  
HETATM 1359  O   HOH A 281       7.065  -3.000  30.597  1.00 27.63           O  
ANISOU 1359  O   HOH A 281     4890   2364   3243    487    392     12       O  
HETATM 1360  O   HOH A 282      -6.947   2.794  23.709  1.00 29.41           O  
ANISOU 1360  O   HOH A 282     1533   4543   5096   -415   -224    -43       O  
HETATM 1361  O   HOH A 283      19.572  14.722  18.296  1.00 26.89           O  
ANISOU 1361  O   HOH A 283     2264   3547   4404   -555    -94    895       O  
HETATM 1362  O   HOH A 284       2.385  -5.465  20.068  1.00 38.13           O  
ANISOU 1362  O   HOH A 284     2844   5142   6500   1196    591  -1492       O  
HETATM 1363  O   HOH A 285      11.051  22.305  26.493  1.00 32.39           O  
ANISOU 1363  O   HOH A 285     5585   3653   3067   1097    -13   -343       O  
HETATM 1364  O   HOH A 286      22.709   4.103  20.748  1.00 19.35           O  
ANISOU 1364  O   HOH A 286     2251   2056   3046    406    245    146       O  
HETATM 1365  O   HOH A 287      10.130  29.192  19.392  1.00 43.28           O  
ANISOU 1365  O   HOH A 287     3398   5837   7208   1734  -1323  -3058       O  
HETATM 1366  O   HOH A 288       3.500   3.791  35.875  1.00 29.56           O  
ANISOU 1366  O   HOH A 288     5460   3167   2603  -1567   -589    356       O  
HETATM 1367  O   HOH A 289       7.252  -6.305  15.611  1.00 36.54           O  
ANISOU 1367  O   HOH A 289     5671   3308   4904  -1703  -1684   1304       O  
HETATM 1368  O   HOH A 290      21.845  11.421   7.434  1.00 47.15           O  
ANISOU 1368  O   HOH A 290     3078   5915   8919  -1216  -1353   3616       O  
HETATM 1369  O   HOH A 291      -2.340  19.475  14.857  1.00 35.98           O  
ANISOU 1369  O   HOH A 291     2890   3316   7462    360   -358  -1080       O  
HETATM 1370  O   HOH A 292       6.006  23.304  -3.947  1.00 43.97           O  
ANISOU 1370  O   HOH A 292     2944   7306   6454   1221   -199   -394       O  
HETATM 1371  O   HOH A 293      -2.141  12.917  23.551  1.00 43.17           O  
ANISOU 1371  O   HOH A 293     1731   4936   9733     42    119    526       O  
HETATM 1372  O   HOH A 294      18.268   0.898   1.911  1.00 49.99           O  
ANISOU 1372  O   HOH A 294     3646   7771   7577   -495    521  -1264       O  
HETATM 1373  O   HOH A 295      -0.492   9.288  29.234  1.00 43.84           O  
ANISOU 1373  O   HOH A 295     7756   5142   3757     95   2030    416       O  
HETATM 1374  O   HOH A 296      12.657  25.463   5.948  1.00 37.27           O  
ANISOU 1374  O   HOH A 296     6578   3516   4067    556   2155   1094       O  
HETATM 1375  O   HOH A 297      17.244   8.945  16.373  1.00 31.44           O  
ANISOU 1375  O   HOH A 297     4392   3838   3714   1062    -37    191       O  
HETATM 1376  O   HOH A 298      10.414  22.448  -3.469  1.00 42.99           O  
ANISOU 1376  O   HOH A 298     2817   5915   7600     81    613   -817       O  
HETATM 1377  O   HOH A 299       2.996  -2.234  17.857  1.00 30.82           O  
ANISOU 1377  O   HOH A 299     3510   4321   3878   1560    355   1072       O  
HETATM 1378  O   HOH A 300      10.305  -5.250   9.462  1.00 39.42           O  
ANISOU 1378  O   HOH A 300     6666   3278   5032   -177    541   -829       O  
HETATM 1379  O   HOH A 301      12.216  24.750 -14.990  1.00 25.56           O  
ANISOU 1379  O   HOH A 301     2653   2664   4394   -557   -916    192       O  
HETATM 1380  O   HOH A 302      19.933  10.178   2.198  1.00 33.18           O  
ANISOU 1380  O   HOH A 302     3438   3291   5877    890    868     73       O  
HETATM 1381  O   HOH A 303      20.459   4.489  17.558  1.00 29.77           O  
ANISOU 1381  O   HOH A 303     3611   3288   4412     94   1295   1031       O  
HETATM 1382  O   HOH A 304      -1.652  14.168  21.908  1.00 32.87           O  
ANISOU 1382  O   HOH A 304     3354   5261   3872   -544    207   -849       O  
HETATM 1383  O  AHOH A 305      12.170   7.173  33.098  0.50 30.19           O  
ANISOU 1383  O  AHOH A 305     1902   5077   4492      4   -247  -1129       O  
HETATM 1384  O  BHOH A 305      12.699   5.070  33.173  0.50 37.42           O  
ANISOU 1384  O  BHOH A 305     6871   4984   2361  -1092   -599    327       O  
HETATM 1385  O   HOH A 306       7.685   3.136  -0.607  1.00 28.81           O  
ANISOU 1385  O   HOH A 306     2436   3765   4745   1006    523    768       O  
HETATM 1386  O   HOH A 307       7.375  21.643  -1.219  1.00 39.26           O  
ANISOU 1386  O   HOH A 307     8023   3752   3142    620    993    575       O  
HETATM 1387  O   HOH A 308      16.451  -0.431  28.917  1.00 31.96           O  
ANISOU 1387  O   HOH A 308     3397   4479   4266   1941    132     42       O  
HETATM 1388  O   HOH A 309      20.955   2.320  21.693  1.00 31.18           O  
ANISOU 1388  O   HOH A 309     1319   5994   4533    -96   -188     68       O  
HETATM 1389  O   HOH A 310       5.338  -1.814  19.957  1.00 36.64           O  
ANISOU 1389  O   HOH A 310     3250   4414   6255  -1466   2021  -1732       O  
HETATM 1390  O   HOH A 311       9.224  21.009   0.837  1.00 42.50           O  
ANISOU 1390  O   HOH A 311     3938   7536   4674    423    506  -2449       O  
HETATM 1391  O   HOH A 312      21.522  17.864   4.726  1.00 45.81           O  
ANISOU 1391  O   HOH A 312     5901   3834   7670  -1414   3225  -1209       O  
HETATM 1392  O   HOH A 313      19.337  19.680   4.508  1.00 45.05           O  
ANISOU 1392  O   HOH A 313     2889   5751   8476    135     79   1320       O  
HETATM 1393  O   HOH A 314       6.109  19.165  -2.951  1.00 39.70           O  
ANISOU 1393  O   HOH A 314     5579   5562   3942   1206    476    389       O  
HETATM 1394  O   HOH A 315       8.596  21.701  26.628  1.00 39.52           O  
ANISOU 1394  O   HOH A 315     5942   4612   4462   2214  -1245  -1497       O  
HETATM 1395  O   HOH A 316       2.984   8.425  31.083  1.00 29.20           O  
ANISOU 1395  O   HOH A 316     3537   3247   4308    559     82   -454       O  
HETATM 1396  O   HOH A 317       9.701  29.982   6.580  1.00 49.99           O  
ANISOU 1396  O   HOH A 317     8382   5813   4796  -1876  -2911   1912       O  
HETATM 1397  O   HOH A 318       3.028  -4.660  22.486  1.00 35.68           O  
ANISOU 1397  O   HOH A 318     3947   4865   4744    778    594    482       O  
HETATM 1398  O   HOH A 319      18.804   1.742  29.718  1.00 42.44           O  
ANISOU 1398  O   HOH A 319     5786   6946   3391    -25   -512    578       O  
HETATM 1399  O   HOH A 320      11.386  24.764   4.200  1.00 33.48           O  
ANISOU 1399  O   HOH A 320     2125   5797   4798   -852    499   1278       O  
HETATM 1400  O   HOH A 321       6.164  -7.477  13.045  1.00 49.50           O  
ANISOU 1400  O   HOH A 321     4633   5169   9006  -1575   -569    895       O  
HETATM 1401  O   HOH A 322      -2.302  19.466   6.668  1.00 31.91           O  
ANISOU 1401  O   HOH A 322     2681   4003   5439   -728  -1021    758       O  
HETATM 1402  O   HOH A 323       7.771  30.704   8.343  1.00 34.13           O  
ANISOU 1402  O   HOH A 323     2300   2910   7755    501   -813    839       O  
HETATM 1403  O   HOH A 324      -2.937   5.904  28.880  1.00 36.85           O  
ANISOU 1403  O   HOH A 324     3226   4267   6508   -128   -264   -413       O  
HETATM 1404  O   HOH A 325      11.773  -3.115  25.008  1.00 31.28           O  
ANISOU 1404  O   HOH A 325     4857   2247   4777     16   1775    372       O  
HETATM 1405  O   HOH A 326      11.903  -6.453  23.206  1.00 25.81           O  
ANISOU 1405  O   HOH A 326     3353   2597   3854   -127      1   -120       O  
HETATM 1406  O   HOH A 327       4.323  -6.962  14.519  1.00 51.28           O  
ANISOU 1406  O   HOH A 327     3411   7554   8518   1028  -1535    441       O  
HETATM 1407  O   HOH A 328      21.306   9.540  22.582  1.00 37.94           O  
ANISOU 1407  O   HOH A 328     4157   4795   5463   -364     -6   -458       O  
HETATM 1408  O   HOH A 329       7.948  -6.531  17.801  1.00 37.31           O  
ANISOU 1408  O   HOH A 329     4877   3554   5742  -1105  -1409   1534       O  
CONECT 1186 1188                                                                
CONECT 1187 1189                                                                
CONECT 1188 1186 1190                                                           
CONECT 1189 1187 1191                                                           
CONECT 1190 1188 1194 1200                                                      
CONECT 1191 1189 1195 1201                                                      
CONECT 1192 1210                                                                
CONECT 1193 1211                                                                
CONECT 1194 1190 1198                                                           
CONECT 1195 1191 1199                                                           
CONECT 1196 1210                                                                
CONECT 1197 1211                                                                
CONECT 1198 1194 1204                                                           
CONECT 1199 1195 1205                                                           
CONECT 1200 1190 1202                                                           
CONECT 1201 1191 1203                                                           
CONECT 1202 1200 1204                                                           
CONECT 1203 1201 1205                                                           
CONECT 1204 1198 1202 1206                                                      
CONECT 1205 1199 1203 1207                                                      
CONECT 1206 1204 1208                                                           
CONECT 1207 1205 1209                                                           
CONECT 1208 1206 1210                                                           
CONECT 1209 1207 1211                                                           
CONECT 1210 1192 1196 1208                                                      
CONECT 1211 1193 1197 1209                                                      
MASTER      347    0    1    3   10    0    3    6 1272    1   26   11          
END                                                                             



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