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

elNémo ID: 22012513052193569

Job options:

ID        	=	 22012513052193569
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   3P6H              
TITLE     HUMAN ADIPOCYTE LIPID-BINDING PROTEIN FABP4 IN COMPLEX WITH (S)-      
TITLE    2 IBUPROFEN                                                            
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, DRUG,             
KEYWDS   2 NONSTEROIDAL ANTI-INFLAMMATORY DRUG, LIPID BINDING PROTEIN           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.GONZALEZ,E.POZHARSKI                                              
REVDAT   4   25-FEB-15 3P6H    1       JRNL                                     
REVDAT   3   11-FEB-15 3P6H    1       JRNL                                     
REVDAT   2   20-APR-11 3P6H    1       KEYWDS REMARK                            
REVDAT   1   13-APR-11 3P6H    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.    1.15 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) : 1.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 46490                          
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) : 0.160                           
REMARK   3   R VALUE            (WORKING SET) : 0.158                           
REMARK   3   FREE R VALUE                     : 0.191                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2355                            
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) : 1.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3144                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2410                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 157                          
REMARK   3   BIN FREE R VALUE                    : 0.2590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1072                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 172                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.60000                                              
REMARK   3    B22 (A**2) : -0.13000                                             
REMARK   3    B33 (A**2) : -1.47000                                             
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): 0.033         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.636         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.971                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.963                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1227 ; 0.021 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):   854 ; 0.014 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1663 ; 2.010 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2098 ; 1.021 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   166 ; 6.316 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    49 ;34.384 ;24.898       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   247 ;15.520 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;19.104 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   188 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1394 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   239 ; 0.005 ; 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):   761 ; 2.197 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   317 ; 0.734 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1246 ; 3.355 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   466 ; 4.824 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   412 ; 6.770 ; 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):  2081 ; 2.040 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 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 3P6H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-OCT-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062016.                                      
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          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58556                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.060                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.12400                            
REMARK 200   FOR THE DATA SET  : 6.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.06                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.72500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.72500                            
REMARK 200   FOR SHELL         : 1.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M SODIUM CITRATE, PH 6.5, VAPOR      
REMARK 280  DIFFUSION, TEMPERATURE 293K                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       16.16400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.51550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.69000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.51550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.16400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.69000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A  -7    CG   CD   OE1  NE2                                  
REMARK 470     GLN A  -6    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A    14     O    HOH A   206              2.03            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    MET A   0   CG  -  SD  -  CE  ANGL. DEV. = -13.5 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    PHE A  57      -71.11    -78.04                                   
REMARK 500    ASP A  77       31.32     75.14                                   
REMARK 500    ASP A 110     -134.62     53.94                                   
REMARK 500    LYS A 120     -122.97     56.03                                   
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 141        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH A 149        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH A 287        DISTANCE =  5.89 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IBP A 133                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3P6C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P6D   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P6E   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P6F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3P6G   RELATED DB: PDB                                   
DBREF  3P6H A    0   131  UNP    P15090   FABP4_HUMAN      1    132             
SEQADV 3P6H GLN A   -7  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6H GLN A   -6  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6H MET A   -5  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6H GLY A   -4  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6H ARG A   -3  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6H GLY A   -2  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6H 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    IBP  A 133      15                                                       
HETNAM     IBP IBUPROFEN                                                        
HETSYN     IBP 2-(4-ISOBUTYLPHENYL)PROPIONIC ACID                               
FORMUL   2  IBP    C13 H18 O2                                                   
FORMUL   3  HOH   *172(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 ASN A  59  PHE A  64  0                                        
SHEET    2   A10 VAL A  48  GLU A  54 -1  N  ILE A  49   O  PHE A  64           
SHEET    3   A10 ASN A  39  ASN A  45 -1  N  ASN A  39   O  GLU A  54           
SHEET    4   A10 GLY A   6  GLU A  14 -1  N  TRP A   8   O  MET A  40           
SHEET    5   A10 VAL A 122  ARG A 130 -1  O  VAL A 127   N  VAL A  11           
SHEET    6   A10 LYS A 112  MET A 119 -1  N  VAL A 115   O  ARG A 126           
SHEET    7   A10 LYS A 100  GLU A 109 -1  N  LYS A 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  PHE A  70   O  SER A  82           
SITE     1 AC1  5 ASP A  76  ARG A 126  TYR A 128  HOH A 210                    
SITE     2 AC1  5 HOH A 279                                                     
CRYST1   32.328   53.380   75.031  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      0.030933  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018734  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013328        0.00000                         
ATOM      1  N   GLN A  -7      -2.178  31.443  -8.790  1.00 38.04           N  
ANISOU    1  N   GLN A  -7     4801   4747   4903    160   -100     35       N  
ATOM      2  CA  GLN A  -7      -1.473  30.238  -8.245  1.00 37.51           C  
ANISOU    2  CA  GLN A  -7     4732   4713   4806    129    -95    -20       C  
ATOM      3  C   GLN A  -7      -0.896  29.361  -9.364  1.00 36.71           C  
ANISOU    3  C   GLN A  -7     4566   4664   4717    105   -117    -40       C  
ATOM      4  O   GLN A  -7      -1.597  29.028 -10.324  1.00 37.79           O  
ANISOU    4  O   GLN A  -7     4663   4861   4832     54   -163    -93       O  
ATOM      5  CB  GLN A  -7      -2.433  29.418  -7.360  1.00 37.94           C  
ANISOU    5  CB  GLN A  -7     4731   4785   4898    112    -93     19       C  
ATOM      6  N   GLN A  -6       0.384  28.998  -9.245  1.00 35.04           N  
ANISOU    6  N   GLN A  -6     4394   4417   4502     47   -136    -48       N  
ATOM      7  CA  GLN A  -6       1.048  28.077 -10.198  1.00 33.06           C  
ANISOU    7  CA  GLN A  -6     4157   4069   4334     63   -151     14       C  
ATOM      8  C   GLN A  -6       1.344  26.767  -9.488  1.00 31.52           C  
ANISOU    8  C   GLN A  -6     3939   3885   4150     44   -186     10       C  
ATOM      9  O   GLN A  -6       1.348  26.720  -8.241  1.00 31.20           O  
ANISOU    9  O   GLN A  -6     4089   3642   4122     84   -212    -67       O  
ATOM     10  CB  GLN A  -6       2.354  28.680 -10.755  1.00 33.90           C  
ANISOU   10  CB  GLN A  -6     4271   4244   4363    -20   -115      0       C  
ATOM     11  N   MET A  -5       1.566  25.707 -10.279  1.00 28.67           N  
ANISOU   11  N   MET A  -5     3350   3609   3931     -4   -286     49       N  
ATOM     12  CA  MET A  -5       1.936  24.421  -9.702  1.00 27.54           C  
ANISOU   12  CA  MET A  -5     3209   3488   3764    -71   -208     52       C  
ATOM     13  C   MET A  -5       3.384  24.432  -9.294  1.00 26.92           C  
ANISOU   13  C   MET A  -5     3134   3458   3636     19   -199    112       C  
ATOM     14  O   MET A  -5       4.296  24.604 -10.128  1.00 27.43           O  
ANISOU   14  O   MET A  -5     3200   3588   3632     90   -150    289       O  
ATOM     15  CB  MET A  -5       1.718  23.222 -10.624  1.00 27.62           C  
ANISOU   15  CB  MET A  -5     3145   3513   3834    -35   -226     54       C  
ATOM     16  CG  MET A  -5       1.773  21.907  -9.781  1.00 25.80           C  
ANISOU   16  CG  MET A  -5     3032   3378   3393    -51   -335    -72       C  
ATOM     17  SD  MET A  -5       1.198  20.434 -10.599  1.00 25.20           S  
ANISOU   17  SD  MET A  -5     2697   3667   3210   -492    -92   -143       S  
ATOM     18  CE  MET A  -5      -0.529  20.811 -10.686  1.00 20.33           C  
ANISOU   18  CE  MET A  -5     2171   3355   2197   -465    -58    175       C  
ATOM     19  N   GLY A  -4       3.580  24.163  -8.014  1.00 25.92           N  
ANISOU   19  N   GLY A  -4     2878   3439   3529      7   -262     11       N  
ATOM     20  CA  GLY A  -4       4.916  24.164  -7.433  1.00 25.32           C  
ANISOU   20  CA  GLY A  -4     2769   3333   3517     43   -217      0       C  
ATOM     21  C   GLY A  -4       5.624  22.926  -7.908  1.00 25.57           C  
ANISOU   21  C   GLY A  -4     2932   3290   3492     -8   -256     28       C  
ATOM     22  O   GLY A  -4       5.006  21.938  -8.341  1.00 26.24           O  
ANISOU   22  O   GLY A  -4     2952   3282   3733    -34   -166   -141       O  
ATOM     23  N   ARG A  -3       6.934  22.974  -7.808  1.00 26.43           N  
ANISOU   23  N   ARG A  -3     3038   3431   3573    -18    -94    119       N  
ATOM     24  CA  ARG A  -3       7.727  21.813  -8.100  1.00 25.45           C  
ANISOU   24  CA  ARG A  -3     2953   3255   3459     10   -118    283       C  
ATOM     25  C   ARG A  -3       7.837  20.901  -6.862  1.00 24.49           C  
ANISOU   25  C   ARG A  -3     2790   3174   3341    -36   -121    288       C  
ATOM     26  O   ARG A  -3       7.296  21.186  -5.770  1.00 25.22           O  
ANISOU   26  O   ARG A  -3     2727   3375   3479    -70   -258    355       O  
ATOM     27  CB  ARG A  -3       9.100  22.221  -8.648  1.00 27.41           C  
ANISOU   27  CB  ARG A  -3     3239   3532   3644    -29    -30    287       C  
ATOM     28  CG  ARG A  -3       9.151  22.181 -10.204  1.00 32.86           C  
ANISOU   28  CG  ARG A  -3     4021   4384   4079    -27      3    186       C  
ATOM     29  CD  ARG A  -3       8.918  23.548 -10.823  1.00 38.78           C  
ANISOU   29  CD  ARG A  -3     4905   4829   4999   -134    111    270       C  
ATOM     30  NE  ARG A  -3      10.194  24.250 -11.054  1.00 42.26           N  
ANISOU   30  NE  ARG A  -3     4939   5703   5413   -254    264    191       N  
ATOM     31  CZ  ARG A  -3      10.769  24.471 -12.243  1.00 44.47           C  
ANISOU   31  CZ  ARG A  -3     5456   5991   5450   -192    236    159       C  
ATOM     32  NH1 ARG A  -3      11.924  25.123 -12.283  1.00 44.32           N  
ANISOU   32  NH1 ARG A  -3     5366   6050   5423   -273    486    176       N  
ATOM     33  NH2 ARG A  -3      10.203  24.073 -13.391  1.00 46.56           N  
ANISOU   33  NH2 ARG A  -3     5886   6279   5522    -95    347     19       N  
ATOM     34  N   GLY A  -2       8.487  19.772  -7.074  1.00 21.16           N  
ANISOU   34  N   GLY A  -2     2049   2882   3108    -77   -183    394       N  
ATOM     35  CA  GLY A  -2       8.624  18.786  -6.004  1.00 19.73           C  
ANISOU   35  CA  GLY A  -2     1841   2710   2942    -53   -283    390       C  
ATOM     36  C   GLY A  -2       9.800  19.052  -5.107  1.00 19.39           C  
ANISOU   36  C   GLY A  -2     1755   2675   2936    -60   -244    467       C  
ATOM     37  O   GLY A  -2      10.520  20.073  -5.235  1.00 19.89           O  
ANISOU   37  O   GLY A  -2     1882   2498   3175     60   -473    536       O  
ATOM     38  N   SER A  -1       9.983  18.142  -4.172  1.00 17.66           N  
ANISOU   38  N   SER A  -1     1541   2541   2628   -315   -116    446       N  
ATOM     39  CA  SER A  -1      11.140  18.260  -3.298  1.00 19.37           C  
ANISOU   39  CA  SER A  -1     2083   2597   2676   -262   -120    388       C  
ATOM     40  C   SER A  -1      11.626  16.863  -2.933  1.00 18.96           C  
ANISOU   40  C   SER A  -1     2107   2472   2623   -314    -40    455       C  
ATOM     41  O   SER A  -1      10.947  15.862  -3.076  1.00 17.99           O  
ANISOU   41  O   SER A  -1     1875   2341   2620   -696    -10    721       O  
ATOM     42  CB  SER A  -1      10.767  19.065  -2.055  1.00 21.42           C  
ANISOU   42  CB  SER A  -1     2441   2793   2903   -227    -44    327       C  
ATOM     43  OG  SER A  -1      10.093  18.277  -1.101  1.00 27.70           O  
ANISOU   43  OG  SER A  -1     3515   3662   3345   -265    487    147       O  
ATOM     44  N   MET A   0      12.793  16.822  -2.358  1.00 19.93           N  
ANISOU   44  N   MET A   0     2334   2582   2653   -185   -129    472       N  
ATOM     45  CA  MET A   0      13.357  15.551  -1.916  1.00 19.62           C  
ANISOU   45  CA  MET A   0     2335   2544   2575   -137    -63    376       C  
ATOM     46  C   MET A   0      12.413  14.895  -0.874  1.00 18.50           C  
ANISOU   46  C   MET A   0     2092   2444   2490   -346   -112    272       C  
ATOM     47  O   MET A   0      12.284  13.672  -0.863  1.00 19.52           O  
ANISOU   47  O   MET A   0     2429   2408   2579   -283     51    308       O  
ATOM     48  CB  MET A   0      14.754  15.853  -1.353  1.00 20.57           C  
ANISOU   48  CB  MET A   0     2390   2732   2694     -8   -264    251       C  
ATOM     49  CG  MET A   0      15.792  14.735  -1.353  1.00 23.92           C  
ANISOU   49  CG  MET A   0     2655   3039   3393    505   -268    372       C  
ATOM     50  SD  MET A   0      16.601  14.484   0.260  1.00 34.06           S  
ANISOU   50  SD  MET A   0     4034   4735   4171    346   -158    317       S  
ATOM     51  CE  MET A   0      14.984  14.177   0.907  1.00 17.54           C  
ANISOU   51  CE  MET A   0     2123   2809   1733   1016   -226    111       C  
ATOM     52  N  ACYS A   1      11.764  15.742  -0.070  0.50 19.14           N  
ANISOU   52  N  ACYS A   1     2311   2419   2539   -360    -15    281       N  
ATOM     53  N  BCYS A   1      11.742  15.679  -0.031  0.50 18.03           N  
ANISOU   53  N  BCYS A   1     2153   2293   2401   -387    -71    281       N  
ATOM     54  CA ACYS A   1      10.780  15.337   0.962  0.50 19.93           C  
ANISOU   54  CA ACYS A   1     2442   2540   2589   -303    100    221       C  
ATOM     55  CA BCYS A   1      10.810  15.080   0.978  0.50 17.95           C  
ANISOU   55  CA BCYS A   1     2178   2275   2364   -360      4    224       C  
ATOM     56  C  ACYS A   1       9.584  14.504   0.417  0.50 18.24           C  
ANISOU   56  C  ACYS A   1     2232   2245   2452   -333     96    324       C  
ATOM     57  C  BCYS A   1       9.572  14.405   0.398  0.50 16.84           C  
ANISOU   57  C  BCYS A   1     2023   2069   2304   -364     72    327       C  
ATOM     58  O  ACYS A   1       8.893  13.799   1.176  0.50 17.83           O  
ANISOU   58  O  ACYS A   1     2296   1984   2492   -293    213    401       O  
ATOM     59  O  BCYS A   1       8.807  13.730   1.113  0.50 15.97           O  
ANISOU   59  O  BCYS A   1     1978   1786   2302   -320    270    541       O  
ATOM     60  CB ACYS A   1      10.309  16.612   1.703  0.50 21.22           C  
ANISOU   60  CB ACYS A   1     2559   2689   2815   -299     50    173       C  
ATOM     61  CB BCYS A   1      10.356  16.117   1.984  0.50 18.45           C  
ANISOU   61  CB BCYS A   1     2207   2407   2395   -214    -39    162       C  
ATOM     62  SG ACYS A   1      10.132  16.465   3.549  0.50 28.50           S  
ANISOU   62  SG ACYS A   1     3840   3598   3389   -228    715    177       S  
ATOM     63  SG BCYS A   1      11.671  16.735   2.968  0.50 23.37           S  
ANISOU   63  SG BCYS A   1     2849   3076   2955   -444   -204   -147       S  
ATOM     64  N   ASP A   2       9.357  14.563  -0.891  1.00 17.06           N  
ANISOU   64  N   ASP A   2     1972   2133   2374   -411    -10    498       N  
ATOM     65  CA  ASP A   2       8.322  13.780  -1.544  1.00 17.98           C  
ANISOU   65  CA  ASP A   2     2009   2399   2421   -444    -92    482       C  
ATOM     66  C   ASP A   2       8.510  12.268  -1.380  1.00 16.97           C  
ANISOU   66  C   ASP A   2     1946   2309   2191   -545    -11    468       C  
ATOM     67  O   ASP A   2       7.548  11.561  -1.445  1.00 17.09           O  
ANISOU   67  O   ASP A   2     1752   2501   2238   -718     56    485       O  
ATOM     68  CB  ASP A   2       8.160  14.178  -3.004  1.00 19.37           C  
ANISOU   68  CB  ASP A   2     2040   2641   2677   -543   -165    431       C  
ATOM     69  CG  ASP A   2       7.612  15.593  -3.186  1.00 21.56           C  
ANISOU   69  CG  ASP A   2     2403   2922   2866   -379   -368    680       C  
ATOM     70  OD1 ASP A   2       6.954  16.172  -2.281  1.00 27.62           O  
ANISOU   70  OD1 ASP A   2     3090   3572   3831   -418    339    712       O  
ATOM     71  OD2 ASP A   2       7.901  16.149  -4.238  1.00 25.90           O  
ANISOU   71  OD2 ASP A   2     3023   3513   3303  -1405   -204    610       O  
ATOM     72  N   ALA A   3       9.725  11.793  -1.113  1.00 15.87           N  
ANISOU   72  N   ALA A   3     1805   2303   1921   -498    204    456       N  
ATOM     73  CA  ALA A   3       9.971  10.392  -0.845  1.00 16.62           C  
ANISOU   73  CA  ALA A   3     2001   2285   2028   -358    167    270       C  
ATOM     74  C   ALA A   3       9.228   9.902   0.391  1.00 14.50           C  
ANISOU   74  C   ALA A   3     1728   1970   1811   -240    203    225       C  
ATOM     75  O   ALA A   3       9.011   8.692   0.535  1.00 13.67           O  
ANISOU   75  O   ALA A   3     1467   1798   1926   -205    448    -15       O  
ATOM     76  CB  ALA A   3      11.433  10.105  -0.666  1.00 18.46           C  
ANISOU   76  CB  ALA A   3     2057   2632   2322   -296    203    551       C  
ATOM     77  N   PHE A   4       8.927  10.812   1.310  1.00 11.42           N  
ANISOU   77  N   PHE A   4     1098   1608   1633   -144     63    212       N  
ATOM     78  CA  PHE A   4       8.191  10.478   2.537  1.00 10.62           C  
ANISOU   78  CA  PHE A   4     1161   1364   1507    -42     96    105       C  
ATOM     79  C   PHE A   4       6.690  10.526   2.391  1.00  9.73           C  
ANISOU   79  C   PHE A   4     1152   1004   1539      3     75    102       C  
ATOM     80  O   PHE A   4       5.974   9.950   3.181  1.00 11.47           O  
ANISOU   80  O   PHE A   4     1536   1176   1644   -161    160    318       O  
ATOM     81  CB  PHE A   4       8.585  11.435   3.644  1.00 11.14           C  
ANISOU   81  CB  PHE A   4     1106   1474   1653    -91    -47    102       C  
ATOM     82  CG  PHE A   4      10.024  11.274   4.087  1.00 12.02           C  
ANISOU   82  CG  PHE A   4     1055   1868   1644   -154    -35     16       C  
ATOM     83  CD1 PHE A   4      10.429  10.201   4.913  1.00 12.92           C  
ANISOU   83  CD1 PHE A   4     1432   1843   1632     58   -233     24       C  
ATOM     84  CD2 PHE A   4      11.017  12.199   3.748  1.00 13.76           C  
ANISOU   84  CD2 PHE A   4     1103   2052   2073   -235   -158    117       C  
ATOM     85  CE1 PHE A   4      11.721  10.061   5.332  1.00 15.00           C  
ANISOU   85  CE1 PHE A   4     1600   2446   1652    -26   -126    256       C  
ATOM     86  CE2 PHE A   4      12.346  12.014   4.160  1.00 13.60           C  
ANISOU   86  CE2 PHE A   4      907   2255   2003   -622     70    151       C  
ATOM     87  CZ  PHE A   4      12.673  10.959   4.959  1.00 13.58           C  
ANISOU   87  CZ  PHE A   4     1296   2176   1685    154    -22    -85       C  
ATOM     88  N   VAL A   5       6.192  11.234   1.387  1.00 10.11           N  
ANISOU   88  N   VAL A   5     1133   1231   1477     93    103     49       N  
ATOM     89  CA  VAL A   5       4.786  11.513   1.302  1.00 11.18           C  
ANISOU   89  CA  VAL A   5     1295   1304   1646    -21      4     31       C  
ATOM     90  C   VAL A   5       4.039  10.254   0.987  1.00 11.88           C  
ANISOU   90  C   VAL A   5     1496   1275   1740   -145    144    -68       C  
ATOM     91  O   VAL A   5       4.420   9.452   0.130  1.00 14.03           O  
ANISOU   91  O   VAL A   5     1689   1473   2168   -400    354   -310       O  
ATOM     92  CB  VAL A   5       4.475  12.601   0.242  1.00 12.35           C  
ANISOU   92  CB  VAL A   5     1552   1131   2008      9   -170    117       C  
ATOM     93  CG1 VAL A   5       3.001  12.692  -0.169  1.00 15.93           C  
ANISOU   93  CG1 VAL A   5     1691   2021   2340    138   -223    295       C  
ATOM     94  CG2 VAL A   5       5.071  13.959   0.802  1.00 13.01           C  
ANISOU   94  CG2 VAL A   5     1560   1264   2118   -113   -284    184       C  
ATOM     95  N   GLY A   6       2.916  10.089   1.672  1.00 10.94           N  
ANISOU   95  N   GLY A   6     1328   1277   1550   -273     53   -194       N  
ATOM     96  CA  GLY A   6       2.070   8.993   1.421  1.00 11.13           C  
ANISOU   96  CA  GLY A   6      973   1544   1710   -258     81   -167       C  
ATOM     97  C   GLY A   6       1.393   8.479   2.678  1.00 10.57           C  
ANISOU   97  C   GLY A   6     1157   1223   1636   -171     89    -19       C  
ATOM     98  O   GLY A   6       1.335   9.152   3.689  1.00 11.95           O  
ANISOU   98  O   GLY A   6     1513   1360   1664   -372    271   -179       O  
ATOM     99  N   THR A   7       0.918   7.265   2.578  1.00 11.03           N  
ANISOU   99  N   THR A   7     1196   1368   1626   -247   -104    -29       N  
ATOM    100  CA  THR A   7       0.150   6.593   3.640  1.00 11.36           C  
ANISOU  100  CA  THR A   7     1111   1253   1953   -137   -104   -110       C  
ATOM    101  C   THR A   7       0.946   5.319   4.002  1.00 11.19           C  
ANISOU  101  C   THR A   7     1252   1195   1805     78   -161    -37       C  
ATOM    102  O   THR A   7       1.151   4.462   3.141  1.00 12.20           O  
ANISOU  102  O   THR A   7     1613   1351   1670    138   -336    -38       O  
ATOM    103  CB  THR A   7      -1.228   6.245   3.189  1.00 12.31           C  
ANISOU  103  CB  THR A   7     1120   1284   2272   -167   -173    135       C  
ATOM    104  OG1 THR A   7      -1.839   7.380   2.568  1.00 17.59           O  
ANISOU  104  OG1 THR A   7     1387   1750   3544     96   -511    140       O  
ATOM    105  CG2 THR A   7      -2.110   5.792   4.365  1.00 15.54           C  
ANISOU  105  CG2 THR A   7     1576   1736   2592   -655    -70     52       C  
ATOM    106  N   TRP A   8       1.306   5.184   5.268  1.00  9.72           N  
ANISOU  106  N   TRP A   8     1041   1117   1532    167    120    -68       N  
ATOM    107  CA  TRP A   8       2.203   4.159   5.751  1.00  9.14           C  
ANISOU  107  CA  TRP A   8      875    944   1653   -105     34    -49       C  
ATOM    108  C   TRP A   8       1.515   3.415   6.866  1.00 10.62           C  
ANISOU  108  C   TRP A   8     1261   1194   1580    -21    124     -1       C  
ATOM    109  O   TRP A   8       0.752   3.992   7.644  1.00 14.12           O  
ANISOU  109  O   TRP A   8     2209   1322   1831     14    342      0       O  
ATOM    110  CB  TRP A   8       3.457   4.811   6.266  1.00  9.88           C  
ANISOU  110  CB  TRP A   8     1151   1088   1513    -68     76     93       C  
ATOM    111  CG  TRP A   8       4.206   5.641   5.276  1.00  9.18           C  
ANISOU  111  CG  TRP A   8      715   1203   1568   -189    -49    -78       C  
ATOM    112  CD1 TRP A   8       4.070   6.996   5.017  1.00  9.93           C  
ANISOU  112  CD1 TRP A   8      788   1448   1535   -272     37    -82       C  
ATOM    113  CD2 TRP A   8       5.173   5.161   4.337  1.00  8.70           C  
ANISOU  113  CD2 TRP A   8      517   1242   1545    124    -52    153       C  
ATOM    114  NE1 TRP A   8       4.964   7.341   4.042  1.00  9.30           N  
ANISOU  114  NE1 TRP A   8      514   1236   1782   -108    138    130       N  
ATOM    115  CE2 TRP A   8       5.649   6.250   3.589  1.00  9.49           C  
ANISOU  115  CE2 TRP A   8      850   1354   1402     21    169      8       C  
ATOM    116  CE3 TRP A   8       5.737   3.910   4.091  1.00 10.90           C  
ANISOU  116  CE3 TRP A   8     1255   1431   1452    280    121   -100       C  
ATOM    117  CZ2 TRP A   8       6.633   6.111   2.612  1.00 11.42           C  
ANISOU  117  CZ2 TRP A   8     1216   1563   1557     16     10     83       C  
ATOM    118  CZ3 TRP A   8       6.705   3.770   3.134  1.00 10.00           C  
ANISOU  118  CZ3 TRP A   8      614   1407   1778    240   -204   -242       C  
ATOM    119  CH2 TRP A   8       7.154   4.867   2.398  1.00 12.06           C  
ANISOU  119  CH2 TRP A   8     1262   1683   1634     -8      0   -110       C  
ATOM    120  N   LYS A   9       1.868   2.143   7.014  1.00 10.14           N  
ANISOU  120  N   LYS A   9     1031   1248   1572   -228     13    149       N  
ATOM    121  CA  LYS A   9       1.320   1.296   8.108  1.00 10.15           C  
ANISOU  121  CA  LYS A   9      782   1488   1586   -306    -19    100       C  
ATOM    122  C   LYS A   9       2.499   0.635   8.847  1.00  9.84           C  
ANISOU  122  C   LYS A   9      684   1406   1649   -388    -36     78       C  
ATOM    123  O   LYS A   9       3.417   0.144   8.261  1.00 10.69           O  
ANISOU  123  O   LYS A   9     1362   1158   1541   -114     18     44       O  
ATOM    124  CB  LYS A   9       0.308   0.324   7.554  1.00 12.65           C  
ANISOU  124  CB  LYS A   9     1041   1776   1989   -413   -133    358       C  
ATOM    125  CG  LYS A   9       0.836  -0.624   6.614  1.00 19.05           C  
ANISOU  125  CG  LYS A   9     2399   2550   2287   -350   -292    209       C  
ATOM    126  CD  LYS A   9      -0.134  -1.697   6.212  1.00 25.39           C  
ANISOU  126  CD  LYS A   9     3296   2981   3370   -665   -389     64       C  
ATOM    127  CE  LYS A   9       0.562  -2.668   5.247  1.00 27.15           C  
ANISOU  127  CE  LYS A   9     3289   3382   3643   -962   -154    -89       C  
ATOM    128  NZ  LYS A   9       0.302  -2.306   3.809  1.00 33.04           N  
ANISOU  128  NZ  LYS A   9     4235   4080   4237   -660   -406    260       N  
ATOM    129  N   LEU A  10       2.407   0.597  10.176  1.00 11.00           N  
ANISOU  129  N   LEU A  10      904   1702   1572   -190     71    270       N  
ATOM    130  CA  LEU A  10       3.458  -0.022  10.979  1.00 10.74           C  
ANISOU  130  CA  LEU A  10      598   1685   1797    -55    -87    234       C  
ATOM    131  C   LEU A  10       3.411  -1.542  10.747  1.00 11.42           C  
ANISOU  131  C   LEU A  10      956   1615   1765   -135    -82    375       C  
ATOM    132  O   LEU A  10       2.332  -2.166  10.962  1.00 14.83           O  
ANISOU  132  O   LEU A  10     1458   1883   2294   -401    -78    540       O  
ATOM    133  CB  LEU A  10       3.210   0.226  12.483  1.00 12.57           C  
ANISOU  133  CB  LEU A  10      899   2052   1823   -201    -78    179       C  
ATOM    134  CG  LEU A  10       4.328  -0.221  13.395  1.00 11.67           C  
ANISOU  134  CG  LEU A  10      398   2214   1820   -187    -93    346       C  
ATOM    135  CD1 LEU A  10       5.569   0.474  13.243  1.00 12.30           C  
ANISOU  135  CD1 LEU A  10      340   2325   2007   -237    -82    260       C  
ATOM    136  CD2 LEU A  10       3.853  -0.156  14.861  1.00 16.79           C  
ANISOU  136  CD2 LEU A  10     1176   3349   1851    -31   -108    187       C  
ATOM    137  N   VAL A  11       4.568  -2.108  10.453  1.00 11.16           N  
ANISOU  137  N   VAL A  11     1045   1268   1924   -269   -240    298       N  
ATOM    138  CA  VAL A  11       4.668  -3.548  10.279  1.00 14.52           C  
ANISOU  138  CA  VAL A  11     1709   1518   2290   -310   -479    261       C  
ATOM    139  C   VAL A  11       5.585  -4.259  11.258  1.00 15.60           C  
ANISOU  139  C   VAL A  11     2097   1578   2251   -312   -594    425       C  
ATOM    140  O   VAL A  11       5.422  -5.465  11.447  1.00 18.47           O  
ANISOU  140  O   VAL A  11     2432   1709   2876   -357   -939    561       O  
ATOM    141  CB  VAL A  11       5.031  -3.942   8.857  1.00 15.84           C  
ANISOU  141  CB  VAL A  11     1782   1727   2509   -312   -470    137       C  
ATOM    142  CG1 VAL A  11       3.883  -3.528   7.929  1.00 18.01           C  
ANISOU  142  CG1 VAL A  11     2396   2149   2297    -50   -668     61       C  
ATOM    143  CG2 VAL A  11       6.428  -3.478   8.409  1.00 17.26           C  
ANISOU  143  CG2 VAL A  11     1927   2046   2584     64   -494     55       C  
ATOM    144  N   SER A  12       6.508  -3.537  11.900  1.00 13.61           N  
ANISOU  144  N   SER A  12     1793   1418   1961    -77   -526    365       N  
ATOM    145  CA  SER A  12       7.379  -4.143  12.907  1.00 14.20           C  
ANISOU  145  CA  SER A  12     1994   1324   2077   -151   -366    335       C  
ATOM    146  C   SER A  12       7.877  -3.122  13.859  1.00 13.01           C  
ANISOU  146  C   SER A  12     1668   1453   1822   -210   -322    225       C  
ATOM    147  O   SER A  12       8.041  -1.960  13.510  1.00 12.29           O  
ANISOU  147  O   SER A  12     1433   1329   1905   -392   -170    388       O  
ATOM    148  CB  SER A  12       8.506  -4.911  12.297  1.00 16.30           C  
ANISOU  148  CB  SER A  12     1978   1922   2291   -107   -445    234       C  
ATOM    149  OG  SER A  12       9.449  -4.095  11.726  1.00 18.77           O  
ANISOU  149  OG  SER A  12     2542   2244   2344     75   -159    326       O  
ATOM    150  N   SER A  13       8.174  -3.578  15.056  1.00 14.13           N  
ANISOU  150  N   SER A  13     2062   1350   1956   -402   -328    270       N  
ATOM    151  CA  SER A  13       8.705  -2.752  16.098  1.00 14.31           C  
ANISOU  151  CA  SER A  13     2118   1521   1799   -274   -393    315       C  
ATOM    152  C   SER A  13       9.667  -3.579  16.934  1.00 14.12           C  
ANISOU  152  C   SER A  13     1983   1522   1859   -227   -341    269       C  
ATOM    153  O   SER A  13       9.378  -4.728  17.260  1.00 17.31           O  
ANISOU  153  O   SER A  13     2624   1483   2469   -365   -604    585       O  
ATOM    154  CB  SER A  13       7.527  -2.223  16.920  1.00 16.64           C  
ANISOU  154  CB  SER A  13     2542   1794   1984   -405   -327    162       C  
ATOM    155  OG  SER A  13       7.907  -1.353  17.952  1.00 17.18           O  
ANISOU  155  OG  SER A  13     2385   1850   2292   -268   -657    105       O  
ATOM    156  N   GLU A  14      10.767  -2.968  17.300  1.00 12.48           N  
ANISOU  156  N   GLU A  14     1837   1183   1720     25   -329     80       N  
ATOM    157  CA  GLU A  14      11.786  -3.561  18.172  1.00 12.08           C  
ANISOU  157  CA  GLU A  14     1589   1181   1817    248   -312     20       C  
ATOM    158  C   GLU A  14      12.155  -2.593  19.275  1.00 11.84           C  
ANISOU  158  C   GLU A  14     1502   1257   1738    182   -205     48       C  
ATOM    159  O   GLU A  14      12.445  -1.436  19.005  1.00 11.54           O  
ANISOU  159  O   GLU A  14     1609   1109   1664    142    -96     37       O  
ATOM    160  CB  GLU A  14      13.054  -3.925  17.387  1.00 14.14           C  
ANISOU  160  CB  GLU A  14     1646   1622   2102    436   -363    -38       C  
ATOM    161  CG  GLU A  14      12.818  -5.092  16.408  1.00 21.74           C  
ANISOU  161  CG  GLU A  14     2883   2413   2961    317   -319   -343       C  
ATOM    162  CD  GLU A  14      12.837  -6.471  17.091  1.00 26.80           C  
ANISOU  162  CD  GLU A  14     3866   2604   3711    377   -519   -389       C  
ATOM    163  OE1 GLU A  14      13.090  -6.551  18.306  1.00 30.29           O  
ANISOU  163  OE1 GLU A  14     4223   3154   4131    291  -1049   -257       O  
ATOM    164  OE2 GLU A  14      12.573  -7.492  16.417  1.00 32.03           O  
ANISOU  164  OE2 GLU A  14     4453   3063   4654    809   -309  -1091       O  
ATOM    165  N   ASN A  15      12.160  -3.080  20.492  1.00 10.57           N  
ANISOU  165  N   ASN A  15     1249   1076   1691    171    -44    142       N  
ATOM    166  CA  ASN A  15      12.627  -2.349  21.663  1.00 10.47           C  
ANISOU  166  CA  ASN A  15     1136   1255   1585    168    -52     99       C  
ATOM    167  C   ASN A  15      11.798  -1.117  22.032  1.00 10.24           C  
ANISOU  167  C   ASN A  15      871   1433   1583    192     52    143       C  
ATOM    168  O   ASN A  15      12.248  -0.253  22.758  1.00 10.68           O  
ANISOU  168  O   ASN A  15     1104   1235   1718    -48    -58     29       O  
ATOM    169  CB AASN A  15      14.109  -1.961  21.540  0.50 10.98           C  
ANISOU  169  CB AASN A  15     1190   1380   1600    307    -10     71       C  
ATOM    170  CB BASN A  15      14.093  -1.982  21.519  0.50 11.62           C  
ANISOU  170  CB BASN A  15     1317   1408   1687    341     13     29       C  
ATOM    171  CG AASN A  15      14.834  -1.962  22.883  0.50  9.16           C  
ANISOU  171  CG AASN A  15      255   1535   1688      5    -55    197       C  
ATOM    172  CG BASN A  15      14.930  -3.184  21.333  0.50 12.94           C  
ANISOU  172  CG BASN A  15     1244   1714   1958    453   -176   -130       C  
ATOM    173  OD1AASN A  15      14.692  -2.899  23.682  0.50 11.64           O  
ANISOU  173  OD1AASN A  15     1109   1461   1852   -100    158    320       O  
ATOM    174  OD1BASN A  15      15.026  -3.990  22.238  0.50 17.58           O  
ANISOU  174  OD1BASN A  15     2554   1342   2784    109     17     38       O  
ATOM    175  ND2AASN A  15      15.682  -0.974  23.101  0.50 10.36           N  
ANISOU  175  ND2AASN A  15      358   1811   1767   -351   -281    400       N  
ATOM    176  ND2BASN A  15      15.434  -3.391  20.148  0.50 18.01           N  
ANISOU  176  ND2BASN A  15     2016   2346   2478    433    425    -67       N  
ATOM    177  N   PHE A  16      10.565  -1.017  21.558  1.00 10.27           N  
ANISOU  177  N   PHE A  16      951   1204   1747    -20    -25     44       N  
ATOM    178  CA  PHE A  16       9.722   0.161  21.782  1.00 10.78           C  
ANISOU  178  CA  PHE A  16     1045   1363   1688     17    -77     51       C  
ATOM    179  C   PHE A  16       9.325   0.280  23.230  1.00 10.03           C  
ANISOU  179  C   PHE A  16      707   1460   1642    -93    -58     27       C  
ATOM    180  O   PHE A  16       9.283   1.411  23.769  1.00 10.08           O  
ANISOU  180  O   PHE A  16     1114   1207   1507   -103   -129    -37       O  
ATOM    181  CB  PHE A  16       8.511   0.216  20.846  1.00 10.59           C  
ANISOU  181  CB  PHE A  16     1039   1417   1567    149    -88    -51       C  
ATOM    182  CG  PHE A  16       7.810   1.573  20.781  1.00  9.67           C  
ANISOU  182  CG  PHE A  16      559   1560   1554     88    -73    -62       C  
ATOM    183  CD1 PHE A  16       8.509   2.695  20.380  1.00 12.68           C  
ANISOU  183  CD1 PHE A  16     1456   1454   1907     20    -34    -37       C  
ATOM    184  CD2 PHE A  16       6.527   1.686  21.050  1.00 11.02           C  
ANISOU  184  CD2 PHE A  16      466   1948   1770   -110   -176    -95       C  
ATOM    185  CE1 PHE A  16       7.859   3.893  20.238  1.00 15.03           C  
ANISOU  185  CE1 PHE A  16     2428   1462   1821    321    -79   -196       C  
ATOM    186  CE2 PHE A  16       5.862   2.941  20.928  1.00 12.53           C  
ANISOU  186  CE2 PHE A  16     1287   1786   1686    693    -81    -57       C  
ATOM    187  CZ  PHE A  16       6.593   4.019  20.523  1.00 14.01           C  
ANISOU  187  CZ  PHE A  16     2376   1479   1465    361   -191    -74       C  
ATOM    188  N   ASP A  17       9.084  -0.834  23.927  1.00 10.99           N  
ANISOU  188  N   ASP A  17     1221   1209   1746     56     73    135       N  
ATOM    189  CA  ASP A  17       8.706  -0.715  25.348  1.00 12.61           C  
ANISOU  189  CA  ASP A  17     1450   1441   1899   -181      1    307       C  
ATOM    190  C   ASP A  17       9.905  -0.108  26.158  1.00 11.54           C  
ANISOU  190  C   ASP A  17     1096   1426   1860     87     31    453       C  
ATOM    191  O   ASP A  17       9.758   0.773  26.999  1.00 11.78           O  
ANISOU  191  O   ASP A  17     1448   1407   1618    -36    161    264       O  
ATOM    192  CB  ASP A  17       8.332  -2.078  25.918  1.00 13.92           C  
ANISOU  192  CB  ASP A  17     1644   1523   2120    -39     65    383       C  
ATOM    193  CG  ASP A  17       7.829  -1.978  27.322  1.00 15.99           C  
ANISOU  193  CG  ASP A  17     1876   1766   2430   -116    208    747       C  
ATOM    194  OD1 ASP A  17       8.469  -2.518  28.203  1.00 22.25           O  
ANISOU  194  OD1 ASP A  17     3095   3153   2203    202     49    682       O  
ATOM    195  OD2 ASP A  17       6.798  -1.349  27.565  1.00 18.77           O  
ANISOU  195  OD2 ASP A  17     2395   2234   2502    117    299    712       O  
ATOM    196  N   ASP A  18      11.104  -0.580  25.892  1.00 10.98           N  
ANISOU  196  N   ASP A  18      866   1260   2044     33    -72    313       N  
ATOM    197  CA  ASP A  18      12.346  -0.086  26.518  1.00 11.79           C  
ANISOU  197  CA  ASP A  18      745   1690   2044     33     72    327       C  
ATOM    198  C   ASP A  18      12.550   1.404  26.173  1.00 11.81           C  
ANISOU  198  C   ASP A  18     1176   1442   1868     38     31    147       C  
ATOM    199  O   ASP A  18      12.943   2.179  27.049  1.00 10.93           O  
ANISOU  199  O   ASP A  18      923   1465   1766    103   -245    254       O  
ATOM    200  CB  ASP A  18      13.591  -0.918  26.173  1.00 14.49           C  
ANISOU  200  CB  ASP A  18     1065   1966   2475    245     92    344       C  
ATOM    201  CG  ASP A  18      13.633  -2.297  26.941  1.00 22.54           C  
ANISOU  201  CG  ASP A  18     2387   2771   3404    227    221    653       C  
ATOM    202  OD1 ASP A  18      12.853  -2.488  27.872  1.00 29.87           O  
ANISOU  202  OD1 ASP A  18     3316   3438   4594    -48    241   1532       O  
ATOM    203  OD2 ASP A  18      14.464  -3.127  26.632  1.00 30.59           O  
ANISOU  203  OD2 ASP A  18     3583   3834   4205    627   -477    491       O  
ATOM    204  N   TYR A  19      12.257   1.824  24.936  1.00 10.45           N  
ANISOU  204  N   TYR A  19     1147   1268   1553     27    115    116       N  
ATOM    205  CA  TYR A  19      12.381   3.250  24.604  1.00  9.35           C  
ANISOU  205  CA  TYR A  19      632   1400   1521     31     97    120       C  
ATOM    206  C   TYR A  19      11.418   4.085  25.427  1.00  8.29           C  
ANISOU  206  C   TYR A  19      276   1458   1413    131    126    267       C  
ATOM    207  O   TYR A  19      11.746   5.107  26.014  1.00 10.13           O  
ANISOU  207  O   TYR A  19     1145   1360   1342    -21    -55     37       O  
ATOM    208  CB  TYR A  19      12.116   3.413  23.084  1.00 10.58           C  
ANISOU  208  CB  TYR A  19     1168   1409   1441     61    103    163       C  
ATOM    209  CG  TYR A  19      11.910   4.885  22.697  1.00  8.43           C  
ANISOU  209  CG  TYR A  19      326   1391   1485   -289     33   -114       C  
ATOM    210  CD1 TYR A  19      12.968   5.727  22.597  1.00  8.70           C  
ANISOU  210  CD1 TYR A  19      281   1634   1388   -197    -31    117       C  
ATOM    211  CD2 TYR A  19      10.639   5.340  22.446  1.00  9.78           C  
ANISOU  211  CD2 TYR A  19      370   1597   1747   -373   -168     90       C  
ATOM    212  CE1 TYR A  19      12.757   7.077  22.285  1.00  8.66           C  
ANISOU  212  CE1 TYR A  19      362   1342   1586   -326    150   -102       C  
ATOM    213  CE2 TYR A  19      10.409   6.715  22.148  1.00  9.60           C  
ANISOU  213  CE2 TYR A  19      281   1540   1823     63   -179    297       C  
ATOM    214  CZ  TYR A  19      11.490   7.546  22.077  1.00  9.10           C  
ANISOU  214  CZ  TYR A  19      550   1553   1355   -191    124    -58       C  
ATOM    215  OH  TYR A  19      11.246   8.876  21.753  1.00 11.55           O  
ANISOU  215  OH  TYR A  19     1598   1164   1623     57   -139    214       O  
ATOM    216  N   MET A  20      10.199   3.632  25.478  1.00  7.92           N  
ANISOU  216  N   MET A  20      270   1327   1409     31    103    148       N  
ATOM    217  CA  MET A  20       9.144   4.299  26.224  1.00  9.36           C  
ANISOU  217  CA  MET A  20      566   1436   1555     46    297    229       C  
ATOM    218  C   MET A  20       9.490   4.348  27.718  1.00 10.21           C  
ANISOU  218  C   MET A  20      962   1459   1458    177    190    100       C  
ATOM    219  O   MET A  20       9.268   5.390  28.364  1.00 11.42           O  
ANISOU  219  O   MET A  20     1580   1319   1436   -159    -46     -5       O  
ATOM    220  CB  MET A  20       7.805   3.632  26.051  1.00  9.59           C  
ANISOU  220  CB  MET A  20      655   1584   1402    216    370    204       C  
ATOM    221  CG  MET A  20       7.137   3.912  24.677  1.00 11.51           C  
ANISOU  221  CG  MET A  20     1570   1299   1503     34      2     84       C  
ATOM    222  SD  MET A  20       5.400   3.381  24.561  1.00 12.37           S  
ANISOU  222  SD  MET A  20     1103   1953   1642   -192     75     36       S  
ATOM    223  CE  MET A  20       5.627   1.580  24.654  1.00 13.46           C  
ANISOU  223  CE  MET A  20     1458   1675   1979   -488    116    -35       C  
ATOM    224  N   LYS A  21      10.062   3.256  28.267  1.00 11.81           N  
ANISOU  224  N   LYS A  21     1561   1503   1423   -131    105    111       N  
ATOM    225  CA  LYS A  21      10.510   3.313  29.682  1.00 12.48           C  
ANISOU  225  CA  LYS A  21     1391   1809   1540    -19     59    190       C  
ATOM    226  C   LYS A  21      11.531   4.403  29.870  1.00 13.41           C  
ANISOU  226  C   LYS A  21     1779   1846   1468   -101   -126    151       C  
ATOM    227  O   LYS A  21      11.468   5.150  30.853  1.00 15.51           O  
ANISOU  227  O   LYS A  21     2218   2140   1534    -10   -119     81       O  
ATOM    228  CB  LYS A  21      11.110   1.975  30.113  1.00 13.05           C  
ANISOU  228  CB  LYS A  21     1405   1979   1572      9     49    261       C  
ATOM    229  CG  LYS A  21      10.065   0.899  30.350  1.00 15.56           C  
ANISOU  229  CG  LYS A  21     1788   2221   1903     62     39    425       C  
ATOM    230  CD  LYS A  21      10.738  -0.347  30.866  1.00 19.28           C  
ANISOU  230  CD  LYS A  21     2334   2533   2456    165   -220    677       C  
ATOM    231  CE  LYS A  21       9.819  -1.469  31.103  1.00 23.83           C  
ANISOU  231  CE  LYS A  21     2996   2830   3227    111   -294    629       C  
ATOM    232  NZ  LYS A  21      10.399  -2.449  31.967  1.00 27.26           N  
ANISOU  232  NZ  LYS A  21     2909   3414   4031    408   -653    791       N  
ATOM    233  N   GLU A  22      12.487   4.507  28.946  1.00 12.33           N  
ANISOU  233  N   GLU A  22     1415   1708   1559      1   -177    133       N  
ATOM    234  CA  GLU A  22      13.602   5.497  29.053  1.00 13.32           C  
ANISOU  234  CA  GLU A  22     1560   1814   1687    -93   -278     76       C  
ATOM    235  C   GLU A  22      13.029   6.882  28.978  1.00 12.69           C  
ANISOU  235  C   GLU A  22     1739   1689   1391   -181   -234    -31       C  
ATOM    236  O   GLU A  22      13.496   7.766  29.669  1.00 15.74           O  
ANISOU  236  O   GLU A  22     2236   2134   1609   -513   -306    -43       O  
ATOM    237  CB  GLU A  22      14.692   5.217  27.995  1.00 15.07           C  
ANISOU  237  CB  GLU A  22     1783   2089   1851   -102    -98     50       C  
ATOM    238  CG  GLU A  22      16.072   5.721  28.340  1.00 17.96           C  
ANISOU  238  CG  GLU A  22     1965   2441   2416   -196   -427    145       C  
ATOM    239  CD  GLU A  22      16.796   4.879  29.401  1.00 18.57           C  
ANISOU  239  CD  GLU A  22     2160   2427   2468   -363   -381    385       C  
ATOM    240  OE1 GLU A  22      16.263   3.858  29.901  1.00 21.57           O  
ANISOU  240  OE1 GLU A  22     2442   2917   2834   -741   -585    488       O  
ATOM    241  OE2 GLU A  22      17.925   5.266  29.751  1.00 22.85           O  
ANISOU  241  OE2 GLU A  22     3045   2859   2777   -270   -807    136       O  
ATOM    242  N   VAL A  23      11.993   7.074  28.159  1.00 12.43           N  
ANISOU  242  N   VAL A  23     1649   1592   1481   -253   -107     34       N  
ATOM    243  CA  VAL A  23      11.298   8.353  28.021  1.00 11.96           C  
ANISOU  243  CA  VAL A  23     1454   1531   1556   -295     29    -41       C  
ATOM    244  C   VAL A  23      10.564   8.748  29.297  1.00 13.02           C  
ANISOU  244  C   VAL A  23     1717   1629   1599   -362     19    -78       C  
ATOM    245  O   VAL A  23      10.459   9.908  29.606  1.00 15.13           O  
ANISOU  245  O   VAL A  23     2285   1630   1833   -336    265   -138       O  
ATOM    246  CB  VAL A  23      10.338   8.341  26.776  1.00 12.31           C  
ANISOU  246  CB  VAL A  23     1643   1463   1569    -85    -53     87       C  
ATOM    247  CG1 VAL A  23       9.339   9.485  26.767  1.00 13.21           C  
ANISOU  247  CG1 VAL A  23     1844   1482   1691    -77    -44      4       C  
ATOM    248  CG2 VAL A  23      11.187   8.315  25.490  1.00 13.06           C  
ANISOU  248  CG2 VAL A  23     1966   1495   1499   -185    169    -84       C  
ATOM    249  N   GLY A  24      10.135   7.754  30.066  1.00 13.31           N  
ANISOU  249  N   GLY A  24     1881   1591   1585   -379     -6    -42       N  
ATOM    250  CA  GLY A  24       9.369   7.984  31.279  1.00 14.22           C  
ANISOU  250  CA  GLY A  24     1998   1841   1563   -265     40    -58       C  
ATOM    251  C   GLY A  24       7.889   7.644  31.196  1.00 13.75           C  
ANISOU  251  C   GLY A  24     2019   1679   1525   -233     55    -71       C  
ATOM    252  O   GLY A  24       7.098   8.034  32.062  1.00 14.49           O  
ANISOU  252  O   GLY A  24     2015   1800   1689   -220    192   -216       O  
ATOM    253  N   VAL A  25       7.476   6.945  30.161  1.00 12.82           N  
ANISOU  253  N   VAL A  25     1971   1318   1580   -212      0    -45       N  
ATOM    254  CA  VAL A  25       6.081   6.556  29.985  1.00 12.36           C  
ANISOU  254  CA  VAL A  25     1845   1334   1515      8     89     11       C  
ATOM    255  C   VAL A  25       5.678   5.534  31.043  1.00 11.59           C  
ANISOU  255  C   VAL A  25     1400   1475   1527    -78     34   -166       C  
ATOM    256  O   VAL A  25       6.434   4.570  31.272  1.00 12.44           O  
ANISOU  256  O   VAL A  25     1686   1453   1588   -311   -163    152       O  
ATOM    257  CB  VAL A  25       5.826   5.994  28.554  1.00 10.92           C  
ANISOU  257  CB  VAL A  25     1273   1239   1635   -212     41    -72       C  
ATOM    258  CG1 VAL A  25       4.373   5.699  28.356  1.00 12.18           C  
ANISOU  258  CG1 VAL A  25     1525   1462   1637    -38    150     74       C  
ATOM    259  CG2 VAL A  25       6.270   6.984  27.477  1.00 12.68           C  
ANISOU  259  CG2 VAL A  25     1782   1262   1771   -195    169    381       C  
ATOM    260  N   GLY A  26       4.512   5.761  31.652  1.00 12.82           N  
ANISOU  260  N   GLY A  26     1749   1669   1451   -353    -73    -40       N  
ATOM    261  CA  GLY A  26       3.983   4.884  32.670  1.00 13.81           C  
ANISOU  261  CA  GLY A  26     1854   1981   1412   -432    136   -169       C  
ATOM    262  C   GLY A  26       3.484   3.555  32.149  1.00 14.13           C  
ANISOU  262  C   GLY A  26     2034   1860   1475   -565    127     19       C  
ATOM    263  O   GLY A  26       3.181   3.402  30.980  1.00 13.33           O  
ANISOU  263  O   GLY A  26     1900   1769   1396   -737    -44    -28       O  
ATOM    264  N   PHE A  27       3.312   2.601  33.069  1.00 13.33           N  
ANISOU  264  N   PHE A  27     1955   1774   1334   -470      1    -19       N  
ATOM    265  CA  PHE A  27       3.031   1.218  32.712  1.00 13.34           C  
ANISOU  265  CA  PHE A  27     1709   1839   1521   -412     54    170       C  
ATOM    266  C   PHE A  27       1.787   1.117  31.806  1.00 11.08           C  
ANISOU  266  C   PHE A  27     1173   1440   1598   -460    199    271       C  
ATOM    267  O   PHE A  27       1.841   0.507  30.745  1.00 12.18           O  
ANISOU  267  O   PHE A  27     1615   1587   1424   -453     46    121       O  
ATOM    268  CB  PHE A  27       2.827   0.392  33.988  1.00 12.73           C  
ANISOU  268  CB  PHE A  27     1453   1816   1567   -280     14    228       C  
ATOM    269  CG  PHE A  27       2.419  -1.023  33.722  1.00 14.62           C  
ANISOU  269  CG  PHE A  27     2084   1882   1589   -619    -65    333       C  
ATOM    270  CD1 PHE A  27       3.351  -2.039  33.583  1.00 15.14           C  
ANISOU  270  CD1 PHE A  27     1695   2020   2035   -806    -35    377       C  
ATOM    271  CD2 PHE A  27       1.077  -1.393  33.619  1.00 15.46           C  
ANISOU  271  CD2 PHE A  27     2090   1822   1961   -623   -165    605       C  
ATOM    272  CE1 PHE A  27       2.922  -3.378  33.311  1.00 17.05           C  
ANISOU  272  CE1 PHE A  27     1857   2352   2268   -792    180    560       C  
ATOM    273  CE2 PHE A  27       0.703  -2.703  33.328  1.00 15.34           C  
ANISOU  273  CE2 PHE A  27     1528   2145   2154   -603   -142    848       C  
ATOM    274  CZ  PHE A  27       1.635  -3.675  33.210  1.00 16.03           C  
ANISOU  274  CZ  PHE A  27     1925   2160   2003   -499   -325    186       C  
ATOM    275  N   ALA A  28       0.651   1.645  32.236  1.00 12.36           N  
ANISOU  275  N   ALA A  28     1134   1809   1751   -452    258     35       N  
ATOM    276  CA  ALA A  28      -0.619   1.405  31.498  1.00 12.85           C  
ANISOU  276  CA  ALA A  28     1190   1758   1932   -179     -9    119       C  
ATOM    277  C   ALA A  28      -0.569   2.063  30.119  1.00 11.97           C  
ANISOU  277  C   ALA A  28      973   1659   1914   -448     29     64       C  
ATOM    278  O   ALA A  28      -0.989   1.462  29.129  1.00 14.12           O  
ANISOU  278  O   ALA A  28     1682   1903   1779   -510   -154    150       O  
ATOM    279  CB  ALA A  28      -1.845   1.911  32.244  1.00 12.87           C  
ANISOU  279  CB  ALA A  28      818   1690   2381    -16    101    122       C  
ATOM    280  N   THR A  29       0.015   3.263  30.035  1.00 12.23           N  
ANISOU  280  N   THR A  29     1360   1616   1667   -456    -48     21       N  
ATOM    281  CA  THR A  29       0.207   3.900  28.749  1.00 12.24           C  
ANISOU  281  CA  THR A  29     1209   1655   1785   -258   -117     97       C  
ATOM    282  C   THR A  29       1.126   3.088  27.865  1.00 11.25           C  
ANISOU  282  C   THR A  29      868   1616   1787    -83   -108    119       C  
ATOM    283  O   THR A  29       0.874   2.917  26.662  1.00 11.60           O  
ANISOU  283  O   THR A  29     1089   1728   1588   -148   -125     -1       O  
ATOM    284  CB  THR A  29       0.716   5.310  28.914  1.00 12.85           C  
ANISOU  284  CB  THR A  29     1654   1389   1836   -270    -53     22       C  
ATOM    285  OG1 THR A  29      -0.251   6.034  29.664  1.00 14.92           O  
ANISOU  285  OG1 THR A  29     1507   1798   2364    -68     34     36       O  
ATOM    286  CG2 THR A  29       0.947   5.994  27.561  1.00 13.82           C  
ANISOU  286  CG2 THR A  29     1813   1468   1967   -297   -391    278       C  
ATOM    287  N   ARG A  30       2.219   2.576  28.405  1.00 10.61           N  
ANISOU  287  N   ARG A  30      921   1498   1612   -334    -64    184       N  
ATOM    288  CA  ARG A  30       3.169   1.772  27.614  1.00 11.13           C  
ANISOU  288  CA  ARG A  30     1143   1599   1484   -159      2    341       C  
ATOM    289  C   ARG A  30       2.474   0.548  27.026  1.00 11.07           C  
ANISOU  289  C   ARG A  30     1215   1525   1464   -118    -66    313       C  
ATOM    290  O   ARG A  30       2.689   0.160  25.870  1.00 11.96           O  
ANISOU  290  O   ARG A  30     1308   1753   1482    -20    -58    171       O  
ATOM    291  CB  ARG A  30       4.352   1.278  28.391  1.00 11.34           C  
ANISOU  291  CB  ARG A  30      884   1756   1665     25   -122    218       C  
ATOM    292  CG  ARG A  30       5.498   2.277  28.716  1.00 12.04           C  
ANISOU  292  CG  ARG A  30     1168   1809   1598   -448    116    210       C  
ATOM    293  CD  ARG A  30       6.811   1.644  28.990  1.00 10.60           C  
ANISOU  293  CD  ARG A  30      313   1937   1775   -244   -216    146       C  
ATOM    294  NE  ARG A  30       6.730   0.497  29.874  1.00 11.89           N  
ANISOU  294  NE  ARG A  30     1326   1582   1609   -256   -106    144       N  
ATOM    295  CZ  ARG A  30       6.581   0.549  31.179  1.00 12.98           C  
ANISOU  295  CZ  ARG A  30     1620   1690   1620   -164      2    113       C  
ATOM    296  NH1 ARG A  30       6.510   1.716  31.858  1.00 13.75           N  
ANISOU  296  NH1 ARG A  30     2184   1596   1443   -105   -137    326       N  
ATOM    297  NH2 ARG A  30       6.543  -0.596  31.859  1.00 14.76           N  
ANISOU  297  NH2 ARG A  30     2403   1668   1536   -194    102    184       N  
ATOM    298  N   LYS A  31       1.669  -0.113  27.835  1.00 11.29           N  
ANISOU  298  N   LYS A  31     1268   1600   1418   -275    -20    211       N  
ATOM    299  CA  LYS A  31       1.060  -1.356  27.364  1.00 11.82           C  
ANISOU  299  CA  LYS A  31     1430   1467   1593   -382     19     17       C  
ATOM    300  C   LYS A  31       0.110  -1.064  26.222  1.00 11.89           C  
ANISOU  300  C   LYS A  31     1483   1473   1559   -108    -64     40       C  
ATOM    301  O   LYS A  31       0.106  -1.770  25.223  1.00 13.03           O  
ANISOU  301  O   LYS A  31     1610   1650   1688   -101    -87   -224       O  
ATOM    302  CB  LYS A  31       0.340  -2.066  28.496  1.00 12.53           C  
ANISOU  302  CB  LYS A  31     1441   1525   1793   -516     43     99       C  
ATOM    303  CG  LYS A  31       1.217  -2.608  29.581  1.00 16.28           C  
ANISOU  303  CG  LYS A  31     2341   1910   1933   -323   -131    186       C  
ATOM    304  CD  LYS A  31       2.183  -3.675  29.100  1.00 21.65           C  
ANISOU  304  CD  LYS A  31     3054   2759   2412    269   -345    482       C  
ATOM    305  CE  LYS A  31       3.594  -3.420  29.616  1.00 26.71           C  
ANISOU  305  CE  LYS A  31     3372   3494   3281    -31    -40   -251       C  
ATOM    306  NZ  LYS A  31       4.616  -4.407  29.123  1.00 29.44           N  
ANISOU  306  NZ  LYS A  31     3897   3705   3582    548   -416   -155       N  
ATOM    307  N   VAL A  32      -0.730  -0.076  26.382  1.00 11.23           N  
ANISOU  307  N   VAL A  32     1228   1495   1542   -209    -97   -109       N  
ATOM    308  CA  VAL A  32      -1.739   0.262  25.312  1.00 11.62           C  
ANISOU  308  CA  VAL A  32     1061   1718   1635   -203   -179   -157       C  
ATOM    309  C   VAL A  32      -0.999   0.863  24.101  1.00 11.78           C  
ANISOU  309  C   VAL A  32     1328   1547   1598   -199    -75   -148       C  
ATOM    310  O   VAL A  32      -1.358   0.550  22.965  1.00 12.35           O  
ANISOU  310  O   VAL A  32     1319   1899   1474   -398    -76   -111       O  
ATOM    311  CB  VAL A  32      -2.866   1.149  25.884  1.00 12.89           C  
ANISOU  311  CB  VAL A  32     1462   1762   1672    -93    -36   -214       C  
ATOM    312  CG1 VAL A  32      -3.738   1.703  24.804  1.00 16.23           C  
ANISOU  312  CG1 VAL A  32     1773   2251   2140    103    -86   -281       C  
ATOM    313  CG2 VAL A  32      -3.639   0.334  26.937  1.00 14.88           C  
ANISOU  313  CG2 VAL A  32     1525   2158   1968    244     73    -18       C  
ATOM    314  N   ALA A  33      -0.036   1.754  24.328  1.00 11.16           N  
ANISOU  314  N   ALA A  33     1163   1623   1453   -149   -125    -39       N  
ATOM    315  CA  ALA A  33       0.680   2.382  23.215  1.00 10.71           C  
ANISOU  315  CA  ALA A  33      982   1722   1366    -44    -74     82       C  
ATOM    316  C   ALA A  33       1.493   1.353  22.440  1.00 13.06           C  
ANISOU  316  C   ALA A  33     1641   1796   1525      9    -25    125       C  
ATOM    317  O   ALA A  33       1.592   1.437  21.222  1.00 13.42           O  
ANISOU  317  O   ALA A  33     1812   1879   1406    -36     21    185       O  
ATOM    318  CB  ALA A  33       1.529   3.504  23.709  1.00 13.14           C  
ANISOU  318  CB  ALA A  33     1635   1790   1567   -219   -292     93       C  
ATOM    319  N   GLY A  34       2.034   0.347  23.126  1.00 12.11           N  
ANISOU  319  N   GLY A  34     1277   1909   1414    182    153    158       N  
ATOM    320  CA  GLY A  34       2.838  -0.645  22.457  1.00 11.98           C  
ANISOU  320  CA  GLY A  34     1175   1896   1477    259     44    151       C  
ATOM    321  C   GLY A  34       2.067  -1.562  21.571  1.00 12.81           C  
ANISOU  321  C   GLY A  34     1393   1875   1598    149    214    116       C  
ATOM    322  O   GLY A  34       2.592  -2.080  20.622  1.00 14.43           O  
ANISOU  322  O   GLY A  34     1433   2305   1745    117    284   -193       O  
ATOM    323  N   MET A  35       0.789  -1.746  21.857  1.00 11.91           N  
ANISOU  323  N   MET A  35     1319   1543   1663    271    385    193       N  
ATOM    324  CA  MET A  35      -0.079  -2.567  21.029  1.00 12.21           C  
ANISOU  324  CA  MET A  35     1271   1501   1867     51    173    347       C  
ATOM    325  C   MET A  35      -0.494  -1.911  19.696  1.00 12.09           C  
ANISOU  325  C   MET A  35     1349   1417   1826   -225    168    371       C  
ATOM    326  O   MET A  35      -0.812  -2.577  18.738  1.00 14.64           O  
ANISOU  326  O   MET A  35     1922   1507   2133   -343     61    345       O  
ATOM    327  CB  MET A  35      -1.373  -2.912  21.743  1.00 13.40           C  
ANISOU  327  CB  MET A  35     1436   1475   2180    -48    312    426       C  
ATOM    328  CG  MET A  35      -1.200  -3.865  22.865  1.00 14.20           C  
ANISOU  328  CG  MET A  35     1927   1590   1876    146    305     89       C  
ATOM    329  SD  MET A  35      -0.717  -5.479  22.413  1.00 13.73           S  
ANISOU  329  SD  MET A  35     1629   1479   2107     43    103    325       S  
ATOM    330  CE  MET A  35      -2.057  -6.069  21.438  1.00 19.63           C  
ANISOU  330  CE  MET A  35     3026   2180   2252   -434   -750    301       C  
ATOM    331  N   ALA A  36      -0.441  -0.584  19.635  1.00 11.40           N  
ANISOU  331  N   ALA A  36     1151   1419   1760     17    131    392       N  
ATOM    332  CA  ALA A  36      -0.962   0.125  18.482  1.00 13.16           C  
ANISOU  332  CA  ALA A  36     1413   1766   1821     48    135    275       C  
ATOM    333  C   ALA A  36      -0.164  -0.156  17.220  1.00 11.67           C  
ANISOU  333  C   ALA A  36      892   1660   1882   -243     86    171       C  
ATOM    334  O   ALA A  36       1.034  -0.329  17.258  1.00 12.66           O  
ANISOU  334  O   ALA A  36      865   2029   1915    -98     54    195       O  
ATOM    335  CB  ALA A  36      -0.961   1.639  18.769  1.00 13.32           C  
ANISOU  335  CB  ALA A  36     1549   1521   1990    131     23    198       C  
ATOM    336  N   LYS A  37      -0.875  -0.246  16.107  1.00 12.05           N  
ANISOU  336  N   LYS A  37     1054   1613   1911   -250     58    209       N  
ATOM    337  CA ALYS A  37      -0.236  -0.437  14.810  0.50 12.70           C  
ANISOU  337  CA ALYS A  37     1183   1709   1930   -175     35     67       C  
ATOM    338  CA BLYS A  37      -0.272  -0.432  14.782  0.50 12.29           C  
ANISOU  338  CA BLYS A  37     1164   1604   1900   -178     41     60       C  
ATOM    339  C   LYS A  37      -0.754   0.732  13.935  1.00 12.17           C  
ANISOU  339  C   LYS A  37     1169   1636   1818   -370     59    175       C  
ATOM    340  O   LYS A  37      -1.689   0.609  13.146  1.00 13.98           O  
ANISOU  340  O   LYS A  37     1449   1936   1925   -222   -134    189       O  
ATOM    341  CB ALYS A  37      -0.467  -1.876  14.293  0.50 13.70           C  
ANISOU  341  CB ALYS A  37     1298   1819   2087   -221     77     45       C  
ATOM    342  CB BLYS A  37      -0.695  -1.760  14.159  0.50 13.22           C  
ANISOU  342  CB BLYS A  37     1381   1613   2028   -174      8     55       C  
ATOM    343  CG ALYS A  37      -0.388  -2.921  15.463  0.50 16.73           C  
ANISOU  343  CG ALYS A  37     1889   2157   2308    -81    -95     27       C  
ATOM    344  CG BLYS A  37       0.007  -2.930  14.786  0.50 12.67           C  
ANISOU  344  CG BLYS A  37     1401   1377   2033   -155    184     11       C  
ATOM    345  CD ALYS A  37       0.498  -4.114  15.284  0.50 20.03           C  
ANISOU  345  CD ALYS A  37     2321   2545   2745    113   -318    163       C  
ATOM    346  CD BLYS A  37       1.476  -2.935  14.461  0.50 16.54           C  
ANISOU  346  CD BLYS A  37     1650   2289   2342    -67    -47    126       C  
ATOM    347  CE ALYS A  37       0.246  -5.222  16.379  0.50 18.05           C  
ANISOU  347  CE ALYS A  37     1984   2222   2651      6   -114     68       C  
ATOM    348  CE BLYS A  37       2.147  -4.269  14.803  0.50 19.00           C  
ANISOU  348  CE BLYS A  37     2190   2485   2542     87     59    126       C  
ATOM    349  NZ ALYS A  37      -0.633  -4.943  17.609  0.50 14.76           N  
ANISOU  349  NZ ALYS A  37     1309   1584   2715   -606    312    380       N  
ATOM    350  NZ BLYS A  37       1.930  -4.675  16.196  0.50 19.75           N  
ANISOU  350  NZ BLYS A  37     2100   2685   2720    242    149    594       N  
ATOM    351  N   PRO A  38      -0.129   1.907  14.107  1.00 11.58           N  
ANISOU  351  N   PRO A  38     1227   1470   1701   -355     44    117       N  
ATOM    352  CA  PRO A  38      -0.677   3.073  13.469  1.00 12.40           C  
ANISOU  352  CA  PRO A  38     1337   1674   1699   -119    127    159       C  
ATOM    353  C   PRO A  38      -0.515   3.139  11.978  1.00 12.39           C  
ANISOU  353  C   PRO A  38     1405   1558   1743   -321    472     34       C  
ATOM    354  O   PRO A  38       0.347   2.516  11.416  1.00 12.80           O  
ANISOU  354  O   PRO A  38     1469   1633   1760   -293    377    -17       O  
ATOM    355  CB  PRO A  38       0.085   4.240  14.085  1.00 14.80           C  
ANISOU  355  CB  PRO A  38     2026   1739   1856    -51    219    -61       C  
ATOM    356  CG  PRO A  38       0.764   3.736  15.169  1.00 17.63           C  
ANISOU  356  CG  PRO A  38     2077   2088   2531   -229   -145      2       C  
ATOM    357  CD  PRO A  38       0.959   2.264  15.018  1.00 13.59           C  
ANISOU  357  CD  PRO A  38     1506   1859   1799   -284     57    -70       C  
ATOM    358  N   ASN A  39      -1.417   3.922  11.389  1.00 12.41           N  
ANISOU  358  N   ASN A  39     1710   1404   1601    -94    489     92       N  
ATOM    359  CA  ASN A  39      -1.153   4.482  10.063  1.00 15.16           C  
ANISOU  359  CA  ASN A  39     2227   1611   1921   -208    572     45       C  
ATOM    360  C   ASN A  39      -0.546   5.858  10.202  1.00 16.43           C  
ANISOU  360  C   ASN A  39     2791   1548   1903   -264    732    -52       C  
ATOM    361  O   ASN A  39      -0.952   6.672  11.049  1.00 20.22           O  
ANISOU  361  O   ASN A  39     3429   1801   2451   -506   1266   -197       O  
ATOM    362  CB  ASN A  39      -2.387   4.534   9.254  1.00 17.36           C  
ANISOU  362  CB  ASN A  39     2616   1915   2064     39    325    145       C  
ATOM    363  CG  ASN A  39      -2.701   3.232   8.556  1.00 20.49           C  
ANISOU  363  CG  ASN A  39     2896   2412   2475   -215     -8    280       C  
ATOM    364  OD1 ASN A  39      -2.329   2.155   8.995  1.00 27.12           O  
ANISOU  364  OD1 ASN A  39     4560   2674   3071   -251   -263    200       O  
ATOM    365  ND2 ASN A  39      -3.308   3.359   7.368  1.00 28.62           N  
ANISOU  365  ND2 ASN A  39     3937   4205   2733    276   -407    -85       N  
ATOM    366  N   MET A  40       0.429   6.140   9.372  1.00 15.82           N  
ANISOU  366  N   MET A  40     2680   1463   1866   -264    718    -38       N  
ATOM    367  CA  MET A  40       1.088   7.403   9.377  1.00 15.10           C  
ANISOU  367  CA  MET A  40     2615   1373   1750   -207    645   -133       C  
ATOM    368  C   MET A  40       0.928   8.023   8.001  1.00 14.11           C  
ANISOU  368  C   MET A  40     2410   1176   1774   -221    615    -17       C  
ATOM    369  O   MET A  40       1.197   7.390   6.998  1.00 15.06           O  
ANISOU  369  O   MET A  40     2750   1253   1717    114    739    122       O  
ATOM    370  CB  MET A  40       2.543   7.219   9.733  1.00 15.62           C  
ANISOU  370  CB  MET A  40     2674   1424   1837   -537    551     38       C  
ATOM    371  CG  MET A  40       3.275   8.516   9.702  1.00 19.55           C  
ANISOU  371  CG  MET A  40     3191   1810   2427   -691    660      5       C  
ATOM    372  SD  MET A  40       4.975   8.399  10.157  1.00 23.18           S  
ANISOU  372  SD  MET A  40     4186   1736   2882   -687     33   -123       S  
ATOM    373  CE  MET A  40       5.560   7.080   9.125  1.00 25.39           C  
ANISOU  373  CE  MET A  40     3728   3287   2628   -602    492   -217       C  
ATOM    374  N   ILE A  41       0.366   9.211   7.967  1.00 12.82           N  
ANISOU  374  N   ILE A  41     1905   1222   1744   -101    569    -75       N  
ATOM    375  CA  ILE A  41       0.076   9.954   6.722  1.00 12.27           C  
ANISOU  375  CA  ILE A  41     1749   1299   1613   -201    435   -217       C  
ATOM    376  C   ILE A  41       0.985  11.162   6.705  1.00 10.91           C  
ANISOU  376  C   ILE A  41     1448   1105   1592   -293    124    -36       C  
ATOM    377  O   ILE A  41       0.898  12.013   7.601  1.00 12.25           O  
ANISOU  377  O   ILE A  41     1754   1308   1590   -327    409   -116       O  
ATOM    378  CB  ILE A  41      -1.412  10.406   6.578  1.00 13.76           C  
ANISOU  378  CB  ILE A  41     1522   1605   2100   -236    464   -325       C  
ATOM    379  CG1 ILE A  41      -2.410   9.207   6.693  1.00 19.15           C  
ANISOU  379  CG1 ILE A  41     2341   2175   2760   -631    621   -332       C  
ATOM    380  CG2 ILE A  41      -1.639  11.173   5.299  1.00 17.54           C  
ANISOU  380  CG2 ILE A  41     2073   2161   2430    -13    194   -296       C  
ATOM    381  CD1 ILE A  41      -3.879   9.650   6.931  1.00 23.86           C  
ANISOU  381  CD1 ILE A  41     2434   2839   3792   -774    565   -349       C  
ATOM    382  N   ILE A  42       1.810  11.264   5.671  1.00  9.98           N  
ANISOU  382  N   ILE A  42     1187   1124   1477   -126    -19   -115       N  
ATOM    383  CA  ILE A  42       2.803  12.357   5.531  1.00  9.28           C  
ANISOU  383  CA  ILE A  42     1098   1044   1383    -95     -5    -36       C  
ATOM    384  C   ILE A  42       2.427  13.113   4.257  1.00  9.20           C  
ANISOU  384  C   ILE A  42      920   1102   1471      1   -124     -2       C  
ATOM    385  O   ILE A  42       2.269  12.492   3.202  1.00 10.71           O  
ANISOU  385  O   ILE A  42     1545   1155   1370   -148   -159    -43       O  
ATOM    386  CB  ILE A  42       4.238  11.839   5.477  1.00  8.75           C  
ANISOU  386  CB  ILE A  42      847   1163   1312    -87    -21    -61       C  
ATOM    387  CG1 ILE A  42       4.594  11.082   6.777  1.00 11.75           C  
ANISOU  387  CG1 ILE A  42     1919   1043   1499    105    -25    -36       C  
ATOM    388  CG2 ILE A  42       5.199  12.990   5.257  1.00 11.39           C  
ANISOU  388  CG2 ILE A  42     1369   1427   1530   -510    -27   -177       C  
ATOM    389  CD1 ILE A  42       6.020  10.463   6.792  1.00 12.63           C  
ANISOU  389  CD1 ILE A  42     1663   1347   1789    209    -94    108       C  
ATOM    390  N   SER A  43       2.194  14.412   4.368  1.00  9.58           N  
ANISOU  390  N   SER A  43     1170   1086   1383    -83   -284      2       N  
ATOM    391  CA  SER A  43       1.920  15.262   3.254  1.00 11.15           C  
ANISOU  391  CA  SER A  43     1346   1399   1488   -105   -322     75       C  
ATOM    392  C   SER A  43       2.712  16.526   3.330  1.00 10.47           C  
ANISOU  392  C   SER A  43     1378   1157   1440   -238   -144     14       C  
ATOM    393  O   SER A  43       3.232  16.929   4.383  1.00 10.53           O  
ANISOU  393  O   SER A  43     1505   1231   1264   -123    -77     58       O  
ATOM    394  CB  SER A  43       0.450  15.548   3.203  1.00 13.19           C  
ANISOU  394  CB  SER A  43     1590   1526   1896   -167   -232    209       C  
ATOM    395  OG  SER A  43       0.056  16.208   4.359  1.00 15.19           O  
ANISOU  395  OG  SER A  43     1567   2008   2196    283   -181     92       O  
ATOM    396  N   VAL A  44       2.845  17.152   2.175  1.00 11.58           N  
ANISOU  396  N   VAL A  44     1818   1250   1329   -100   -295    -68       N  
ATOM    397  CA  VAL A  44       3.529  18.395   2.028  1.00 11.00           C  
ANISOU  397  CA  VAL A  44     1378   1275   1527   -294   -190     -3       C  
ATOM    398  C   VAL A  44       2.722  19.391   1.243  1.00 12.29           C  
ANISOU  398  C   VAL A  44     1880   1328   1459   -126   -294    -37       C  
ATOM    399  O   VAL A  44       2.061  19.030   0.266  1.00 14.85           O  
ANISOU  399  O   VAL A  44     2621   1302   1718    -27   -716     -8       O  
ATOM    400  CB  VAL A  44       4.894  18.233   1.351  1.00 11.93           C  
ANISOU  400  CB  VAL A  44     1210   1553   1768   -303   -224     94       C  
ATOM    401  CG1 VAL A  44       5.732  19.527   1.244  1.00 16.24           C  
ANISOU  401  CG1 VAL A  44      502   2374   3294   -648    267    122       C  
ATOM    402  CG2 VAL A  44       5.766  17.253   2.096  1.00 14.86           C  
ANISOU  402  CG2 VAL A  44     1512   1727   2406   -131   -270    -80       C  
ATOM    403  N   ASN A  45       2.668  20.627   1.700  1.00 11.07           N  
ANISOU  403  N   ASN A  45     1467   1339   1398   -122   -260     57       N  
ATOM    404  CA  ASN A  45       1.935  21.695   1.010  1.00 11.46           C  
ANISOU  404  CA  ASN A  45     1523   1396   1433   -173   -280    110       C  
ATOM    405  C   ASN A  45       2.818  22.930   1.176  1.00 11.99           C  
ANISOU  405  C   ASN A  45     1800   1358   1398    -75   -245    197       C  
ATOM    406  O   ASN A  45       2.923  23.495   2.241  1.00 11.17           O  
ANISOU  406  O   ASN A  45     1559   1337   1348     84   -173    122       O  
ATOM    407  CB  ASN A  45       0.561  21.844   1.636  1.00 11.41           C  
ANISOU  407  CB  ASN A  45     1342   1443   1547    -89   -382    -92       C  
ATOM    408  CG  ASN A  45      -0.341  22.856   0.930  1.00 12.11           C  
ANISOU  408  CG  ASN A  45     1124   1880   1595    108   -329     26       C  
ATOM    409  OD1 ASN A  45      -1.599  22.690   0.828  1.00 13.63           O  
ANISOU  409  OD1 ASN A  45     1360   1868   1950    124   -228   -159       O  
ATOM    410  ND2 ASN A  45       0.270  23.902   0.450  1.00 11.24           N  
ANISOU  410  ND2 ASN A  45     1089   1403   1775    -85   -547    216       N  
ATOM    411  N   GLY A  46       3.486  23.320   0.102  1.00 13.20           N  
ANISOU  411  N   GLY A  46     1972   1598   1443   -196   -181     89       N  
ATOM    412  CA  GLY A  46       4.462  24.380   0.159  1.00 13.02           C  
ANISOU  412  CA  GLY A  46     1692   1591   1664   -150    -43    222       C  
ATOM    413  C   GLY A  46       5.572  24.017   1.112  1.00 12.54           C  
ANISOU  413  C   GLY A  46     1535   1618   1609    -80    149    267       C  
ATOM    414  O   GLY A  46       6.193  22.965   0.993  1.00 14.72           O  
ANISOU  414  O   GLY A  46     1769   1801   2020    141    298     41       O  
ATOM    415  N   ASP A  47       5.825  24.881   2.086  1.00 12.16           N  
ANISOU  415  N   ASP A  47     1298   1738   1583   -229     63    208       N  
ATOM    416  CA  ASP A  47       6.884  24.644   3.084  1.00 12.99           C  
ANISOU  416  CA  ASP A  47     1511   1652   1772   -128   -110    333       C  
ATOM    417  C   ASP A  47       6.389  23.844   4.276  1.00 11.61           C  
ANISOU  417  C   ASP A  47     1439   1393   1576    -52     -7    162       C  
ATOM    418  O   ASP A  47       7.172  23.498   5.147  1.00 11.08           O  
ANISOU  418  O   ASP A  47      827   1589   1791    -86    -85    223       O  
ATOM    419  CB  ASP A  47       7.446  25.984   3.594  1.00 15.24           C  
ANISOU  419  CB  ASP A  47     1997   1887   1905   -337   -188    293       C  
ATOM    420  CG  ASP A  47       8.063  26.839   2.521  1.00 19.64           C  
ANISOU  420  CG  ASP A  47     2420   2371   2670   -532   -321    320       C  
ATOM    421  OD1 ASP A  47       8.580  26.284   1.543  1.00 26.10           O  
ANISOU  421  OD1 ASP A  47     3088   3825   3001   -532    572    485       O  
ATOM    422  OD2 ASP A  47       8.025  28.078   2.693  1.00 27.47           O  
ANISOU  422  OD2 ASP A  47     4156   2626   3653   -684   -477    402       O  
ATOM    423  N   VAL A  48       5.100  23.530   4.297  1.00 10.42           N  
ANISOU  423  N   VAL A  48     1344   1236   1376     15   -136    190       N  
ATOM    424  CA  VAL A  48       4.468  22.904   5.485  1.00  8.72           C  
ANISOU  424  CA  VAL A  48      742   1185   1384   -246   -101     64       C  
ATOM    425  C   VAL A  48       4.390  21.408   5.295  1.00  9.78           C  
ANISOU  425  C   VAL A  48     1034   1322   1359   -142   -121    -44       C  
ATOM    426  O   VAL A  48       3.717  20.928   4.381  1.00 10.02           O  
ANISOU  426  O   VAL A  48     1116   1286   1405      2   -233     74       O  
ATOM    427  CB  VAL A  48       3.105  23.507   5.807  1.00 10.03           C  
ANISOU  427  CB  VAL A  48      889   1318   1603     16    -66    163       C  
ATOM    428  CG1 VAL A  48       2.580  22.886   7.122  1.00 12.12           C  
ANISOU  428  CG1 VAL A  48     1753   1241   1609     -9    155     64       C  
ATOM    429  CG2 VAL A  48       3.152  25.042   5.961  1.00 13.09           C  
ANISOU  429  CG2 VAL A  48     1830   1210   1933    316     -9    -22       C  
ATOM    430  N   ILE A  49       5.027  20.673   6.201  1.00  8.42           N  
ANISOU  430  N   ILE A  49      830   1076   1291   -211   -130    -23       N  
ATOM    431  CA  ILE A  49       4.939  19.187   6.252  1.00  7.84           C  
ANISOU  431  CA  ILE A  49      376   1146   1454   -324     77      5       C  
ATOM    432  C   ILE A  49       3.956  18.835   7.344  1.00  7.70           C  
ANISOU  432  C   ILE A  49      262   1181   1480    -94    -16    144       C  
ATOM    433  O   ILE A  49       3.967  19.434   8.440  1.00  8.94           O  
ANISOU  433  O   ILE A  49      829   1181   1383   -176    -19    -54       O  
ATOM    434  CB  ILE A  49       6.336  18.567   6.516  1.00  8.21           C  
ANISOU  434  CB  ILE A  49      284   1266   1570   -175     21     66       C  
ATOM    435  CG1 ILE A  49       7.337  19.054   5.474  1.00 10.25           C  
ANISOU  435  CG1 ILE A  49      716   1533   1645     12    136    -93       C  
ATOM    436  CG2 ILE A  49       6.249  17.035   6.610  1.00 10.89           C  
ANISOU  436  CG2 ILE A  49     1339   1122   1676    111   -142     92       C  
ATOM    437  CD1 ILE A  49       8.795  18.733   5.878  1.00 15.19           C  
ANISOU  437  CD1 ILE A  49      777   2499   2496   -421    393    297       C  
ATOM    438  N   THR A  50       3.028  17.923   7.063  1.00  8.20           N  
ANISOU  438  N   THR A  50      632   1142   1341   -126     59     65       N  
ATOM    439  CA  THR A  50       2.052  17.385   8.033  1.00  9.20           C  
ANISOU  439  CA  THR A  50      895   1203   1396   -251     76     65       C  
ATOM    440  C   THR A  50       2.336  15.885   8.212  1.00  9.04           C  
ANISOU  440  C   THR A  50      781   1220   1430    -62      8    -20       C  
ATOM    441  O   THR A  50       2.415  15.131   7.238  1.00  9.47           O  
ANISOU  441  O   THR A  50      978   1169   1448    -93      1    -28       O  
ATOM    442  CB  THR A  50       0.576  17.691   7.645  1.00  8.79           C  
ANISOU  442  CB  THR A  50      387   1384   1568   -217    -84     21       C  
ATOM    443  OG1 THR A  50       0.453  19.107   7.552  1.00 11.83           O  
ANISOU  443  OG1 THR A  50     1446   1303   1745     65   -230     18       O  
ATOM    444  CG2 THR A  50      -0.330  17.126   8.652  1.00 10.85           C  
ANISOU  444  CG2 THR A  50      632   1681   1809   -292     47    -43       C  
ATOM    445  N   ILE A  51       2.454  15.459   9.472  1.00  8.71           N  
ANISOU  445  N   ILE A  51      805   1142   1361    -95      0    -47       N  
ATOM    446  CA  ILE A  51       2.597  14.028   9.831  1.00  7.99           C  
ANISOU  446  CA  ILE A  51      323   1091   1620   -197    183    -12       C  
ATOM    447  C   ILE A  51       1.430  13.709  10.762  1.00  8.60           C  
ANISOU  447  C   ILE A  51      302   1280   1683   -201     90    126       C  
ATOM    448  O   ILE A  51       1.338  14.264  11.883  1.00 10.05           O  
ANISOU  448  O   ILE A  51     1162   1161   1495     36    164    -79       O  
ATOM    449  CB  ILE A  51       3.937  13.726  10.461  1.00  9.09           C  
ANISOU  449  CB  ILE A  51      272   1391   1790    132     78     45       C  
ATOM    450  CG1 ILE A  51       5.096  14.063   9.575  1.00  9.64           C  
ANISOU  450  CG1 ILE A  51      287   1397   1978    -81    233   -154       C  
ATOM    451  CG2 ILE A  51       3.912  12.211  10.834  1.00 11.77           C  
ANISOU  451  CG2 ILE A  51     1519   1226   1726      5    -54    213       C  
ATOM    452  CD1 ILE A  51       6.418  13.824  10.141  1.00 12.18           C  
ANISOU  452  CD1 ILE A  51      259   2020   2348    -55    103   -294       C  
ATOM    453  N  ALYS A  52       0.502  12.874  10.295  0.50  9.58           N  
ANISOU  453  N  ALYS A  52      383   1467   1787   -341    244    -56       N  
ATOM    454  N  BLYS A  52       0.485  12.896  10.310  0.50  9.43           N  
ANISOU  454  N  BLYS A  52      377   1426   1778   -271    316    -48       N  
ATOM    455  CA ALYS A  52      -0.707  12.446  10.964  0.50 10.26           C  
ANISOU  455  CA ALYS A  52      498   1492   1908   -538    202   -156       C  
ATOM    456  CA BLYS A  52      -0.514  12.324  11.152  0.50  9.98           C  
ANISOU  456  CA BLYS A  52      443   1407   1941   -324    431    -88       C  
ATOM    457  C  ALYS A  52      -0.545  10.937  11.365  0.50 11.02           C  
ANISOU  457  C  ALYS A  52      946   1412   1828   -432    305   -151       C  
ATOM    458  C  BLYS A  52      -0.161  10.915  11.511  0.50 10.77           C  
ANISOU  458  C  BLYS A  52      846   1310   1934   -371    503    -44       C  
ATOM    459  O  ALYS A  52      -0.320  10.119  10.504  0.50  9.29           O  
ANISOU  459  O  ALYS A  52      491   1463   1573   -531    130   -123       O  
ATOM    460  O  BLYS A  52       0.551  10.169  10.813  0.50 10.39           O  
ANISOU  460  O  BLYS A  52      562   1363   2022   -510    388    -55       O  
ATOM    461  CB ALYS A  52      -1.961  12.643  10.066  0.50 10.77           C  
ANISOU  461  CB ALYS A  52      553   1495   2043   -592    217    -89       C  
ATOM    462  CB BLYS A  52      -1.922  12.314  10.563  0.50 10.50           C  
ANISOU  462  CB BLYS A  52      514   1588   1885   -355    552   -124       C  
ATOM    463  CG ALYS A  52      -3.257  12.328  10.707  0.50 13.54           C  
ANISOU  463  CG ALYS A  52      560   2111   2473   -722    229     27       C  
ATOM    464  CG BLYS A  52      -2.303  13.619   9.920  0.50 12.20           C  
ANISOU  464  CG BLYS A  52      305   1977   2354   -228    206     36       C  
ATOM    465  CD ALYS A  52      -4.442  12.624   9.709  0.50 17.29           C  
ANISOU  465  CD ALYS A  52     1133   2523   2913   -733    -60    230       C  
ATOM    466  CD BLYS A  52      -3.571  13.570   9.222  0.50 12.45           C  
ANISOU  466  CD BLYS A  52      283   1904   2541   -184    153    -24       C  
ATOM    467  CE ALYS A  52      -5.847  12.622  10.334  0.50 19.75           C  
ANISOU  467  CE ALYS A  52     1576   2889   3039   -270   -118    232       C  
ATOM    468  CE BLYS A  52      -3.783  14.883   8.420  0.50 18.21           C  
ANISOU  468  CE BLYS A  52     1656   2380   2880    -65     58    312       C  
ATOM    469  NZ ALYS A  52      -6.866  13.257   9.460  0.50 22.56           N  
ANISOU  469  NZ ALYS A  52     1964   3191   3413    -18   -258    314       N  
ATOM    470  NZ BLYS A  52      -3.141  14.864   7.064  0.50 20.04           N  
ANISOU  470  NZ BLYS A  52     2182   2574   2858     15    152    634       N  
ATOM    471  N   SER A  53      -0.687  10.580  12.655  1.00 12.37           N  
ANISOU  471  N   SER A  53     1614   1286   1797   -325    414      7       N  
ATOM    472  CA  SER A  53      -0.717   9.195  13.107  1.00 13.55           C  
ANISOU  472  CA  SER A  53     1844   1407   1897   -430    490     48       C  
ATOM    473  C   SER A  53      -2.149   8.856  13.539  1.00 13.51           C  
ANISOU  473  C   SER A  53     1931   1497   1703   -413    593     33       C  
ATOM    474  O   SER A  53      -2.721   9.508  14.391  1.00 14.72           O  
ANISOU  474  O   SER A  53     1887   1647   2058   -505    787   -173       O  
ATOM    475  CB  SER A  53       0.245   9.030  14.275  1.00 14.38           C  
ANISOU  475  CB  SER A  53     1670   1531   2262   -248    587     22       C  
ATOM    476  OG  SER A  53       0.266   7.685  14.774  1.00 17.91           O  
ANISOU  476  OG  SER A  53     2777   1648   2378   -403    129    202       O  
ATOM    477  N   GLU A  54      -2.687   7.851  12.890  1.00 13.48           N  
ANISOU  477  N   GLU A  54     1790   1687   1645   -373    362    -72       N  
ATOM    478  CA  GLU A  54      -4.048   7.356  13.198  1.00 14.29           C  
ANISOU  478  CA  GLU A  54     1680   1830   1918   -304    252     37       C  
ATOM    479  C   GLU A  54      -3.914   6.035  13.873  1.00 13.95           C  
ANISOU  479  C   GLU A  54     1413   2093   1790   -213    227    139       C  
ATOM    480  O   GLU A  54      -3.345   5.095  13.298  1.00 13.38           O  
ANISOU  480  O   GLU A  54     1566   1765   1752   -182    359    280       O  
ATOM    481  CB  GLU A  54      -4.820   7.221  11.903  1.00 16.95           C  
ANISOU  481  CB  GLU A  54     2245   2009   2185   -140    164    110       C  
ATOM    482  CG  GLU A  54      -5.031   8.521  11.175  1.00 22.04           C  
ANISOU  482  CG  GLU A  54     2900   2712   2761    -61    112    298       C  
ATOM    483  CD  GLU A  54      -6.065   8.386  10.095  1.00 28.65           C  
ANISOU  483  CD  GLU A  54     3754   3724   3406    105   -263    157       C  
ATOM    484  OE1 GLU A  54      -5.980   7.430   9.292  1.00 30.18           O  
ANISOU  484  OE1 GLU A  54     4167   3922   3377    -82   -667   -145       O  
ATOM    485  OE2 GLU A  54      -6.985   9.230  10.061  1.00 36.17           O  
ANISOU  485  OE2 GLU A  54     4654   4327   4761    669   -196    149       O  
ATOM    486  N  ASER A  55      -4.333   5.915  15.123  0.50 14.56           N  
ANISOU  486  N  ASER A  55     1490   2209   1833   -120    192    120       N  
ATOM    487  N  BSER A  55      -4.398   5.956  15.106  0.50 15.35           N  
ANISOU  487  N  BSER A  55     1576   2347   1908    -96    158     91       N  
ATOM    488  CA ASER A  55      -4.286   4.576  15.755  0.50 15.85           C  
ANISOU  488  CA ASER A  55     1832   2274   1914     49    297    234       C  
ATOM    489  CA BSER A  55      -4.153   4.764  15.931  0.50 18.05           C  
ANISOU  489  CA BSER A  55     2199   2533   2123     69    227    130       C  
ATOM    490  C  ASER A  55      -5.409   4.401  16.709  0.50 16.59           C  
ANISOU  490  C  ASER A  55     2208   2223   1873     41    403    188       C  
ATOM    491  C  BSER A  55      -5.262   4.495  16.893  0.50 17.81           C  
ANISOU  491  C  BSER A  55     2399   2374   1992     98    328    141       C  
ATOM    492  O  ASER A  55      -6.250   5.249  16.929  0.50 15.92           O  
ANISOU  492  O  ASER A  55     2086   2104   1857    218    486    470       O  
ATOM    493  O  BSER A  55      -5.914   5.420  17.373  0.50 16.46           O  
ANISOU  493  O  BSER A  55     2358   2041   1855    323    261    327       O  
ATOM    494  CB ASER A  55      -2.934   4.114  16.420  0.50 16.30           C  
ANISOU  494  CB ASER A  55     1972   2159   2059     -2    241    122       C  
ATOM    495  CB BSER A  55      -2.871   4.843  16.752  0.50 20.28           C  
ANISOU  495  CB BSER A  55     2343   2943   2419     29    304     63       C  
ATOM    496  OG ASER A  55      -2.684   4.615  17.747  0.50 10.01           O  
ANISOU  496  OG ASER A  55     1007   1546   1249     29    241    702       O  
ATOM    497  OG BSER A  55      -2.449   6.144  16.925  0.50 24.35           O  
ANISOU  497  OG BSER A  55     3390   3152   2710     35   -147    -95       O  
ATOM    498  N   THR A  56      -5.392   3.224  17.248  1.00 17.34           N  
ANISOU  498  N   THR A  56     2553   2028   2008    208    292     63       N  
ATOM    499  CA  THR A  56      -6.317   2.816  18.249  1.00 18.09           C  
ANISOU  499  CA  THR A  56     2760   2010   2103   -117    354    -41       C  
ATOM    500  C   THR A  56      -5.934   3.369  19.601  1.00 17.62           C  
ANISOU  500  C   THR A  56     2787   1934   1974   -123    485    -66       C  
ATOM    501  O   THR A  56      -6.792   3.393  20.469  1.00 20.53           O  
ANISOU  501  O   THR A  56     3146   2608   2046   -681    694   -191       O  
ATOM    502  CB  THR A  56      -6.272   1.266  18.305  1.00 20.19           C  
ANISOU  502  CB  THR A  56     2909   2175   2588    -97    201   -387       C  
ATOM    503  OG1 THR A  56      -4.873   0.836  18.239  1.00 19.99           O  
ANISOU  503  OG1 THR A  56     3127   1932   2533    -52     99    -99       O  
ATOM    504  CG2 THR A  56      -7.093   0.708  17.102  1.00 20.87           C  
ANISOU  504  CG2 THR A  56     3363   2054   2511      0   -239   -407       C  
ATOM    505  N   PHE A  57      -4.671   3.722  19.814  1.00 16.32           N  
ANISOU  505  N   PHE A  57     2729   1649   1822    -14    462     89       N  
ATOM    506  CA  PHE A  57      -4.217   4.356  21.056  1.00 16.82           C  
ANISOU  506  CA  PHE A  57     2646   1789   1954    -25    466    221       C  
ATOM    507  C   PHE A  57      -4.588   5.827  21.061  1.00 16.42           C  
ANISOU  507  C   PHE A  57     2482   1713   2043    -26    513    203       C  
ATOM    508  O   PHE A  57      -5.497   6.245  21.751  1.00 18.82           O  
ANISOU  508  O   PHE A  57     2682   1886   2581    -19    815    280       O  
ATOM    509  CB  PHE A  57      -2.718   4.104  21.293  1.00 17.84           C  
ANISOU  509  CB  PHE A  57     3021   1825   1929     73    269    295       C  
ATOM    510  CG  PHE A  57      -2.105   4.930  22.380  1.00 20.38           C  
ANISOU  510  CG  PHE A  57     3223   1882   2638    182    -39    407       C  
ATOM    511  CD1 PHE A  57      -2.642   4.961  23.639  1.00 21.99           C  
ANISOU  511  CD1 PHE A  57     3512   2173   2667    172   -257     25       C  
ATOM    512  CD2 PHE A  57      -0.955   5.657  22.133  1.00 19.58           C  
ANISOU  512  CD2 PHE A  57     2831   1941   2664    376     77    307       C  
ATOM    513  CE1 PHE A  57      -2.043   5.753  24.649  1.00 23.48           C  
ANISOU  513  CE1 PHE A  57     3445   2568   2908   -289   -528    215       C  
ATOM    514  CE2 PHE A  57      -0.356   6.442  23.153  1.00 22.53           C  
ANISOU  514  CE2 PHE A  57     3118   2370   3073    478   -358    453       C  
ATOM    515  CZ  PHE A  57      -0.920   6.479  24.384  1.00 22.86           C  
ANISOU  515  CZ  PHE A  57     3366   2383   2935    239   -498    464       C  
ATOM    516  N  ALYS A  58      -3.901   6.578  20.227  0.50 17.18           N  
ANISOU  516  N  ALYS A  58     2377   1831   2319     93    670    220       N  
ATOM    517  N  BLYS A  58      -3.847   6.691  20.364  0.50 14.94           N  
ANISOU  517  N  BLYS A  58     2128   1562   1987     69    660    188       N  
ATOM    518  CA ALYS A  58      -4.181   7.961  20.065  0.50 17.21           C  
ANISOU  518  CA ALYS A  58     2213   1926   2398     79    519    146       C  
ATOM    519  CA BLYS A  58      -4.091   8.160  20.401  0.50 13.60           C  
ANISOU  519  CA BLYS A  58     1696   1543   1926     23    456     41       C  
ATOM    520  C  ALYS A  58      -4.092   8.281  18.618  0.50 16.86           C  
ANISOU  520  C  ALYS A  58     2117   1850   2436    107    545    155       C  
ATOM    521  C  BLYS A  58      -3.679   8.767  19.066  0.50 12.76           C  
ANISOU  521  C  BLYS A  58     1503   1366   1977    -58    517    110       C  
ATOM    522  O  ALYS A  58      -3.608   7.541  17.745  0.50 17.76           O  
ANISOU  522  O  ALYS A  58     2370   1940   2437    -41    667    218       O  
ATOM    523  O  BLYS A  58      -2.487   8.579  18.693  0.50 11.55           O  
ANISOU  523  O  BLYS A  58     1277   1365   1747    260    442    110       O  
ATOM    524  CB ALYS A  58      -3.174   8.816  20.825  0.50 17.58           C  
ANISOU  524  CB ALYS A  58     2097   2023   2558     76    524     82       C  
ATOM    525  CB BLYS A  58      -3.262   8.798  21.525  0.50 12.69           C  
ANISOU  525  CB BLYS A  58     1421   1641   1760   -207    544     90       C  
ATOM    526  CG ALYS A  58      -3.239   8.654  22.334  0.50 20.12           C  
ANISOU  526  CG ALYS A  58     2440   2431   2770     31     97     48       C  
ATOM    527  CG BLYS A  58      -3.391  10.313  21.600  0.50 14.41           C  
ANISOU  527  CG BLYS A  58     1471   1960   2043    -56    346    -72       C  
ATOM    528  CD ALYS A  58      -4.529   9.247  22.858  0.50 22.92           C  
ANISOU  528  CD ALYS A  58     2684   3097   2928    -18    128   -178       C  
ATOM    529  CD BLYS A  58      -4.713  10.780  22.026  0.50 16.70           C  
ANISOU  529  CD BLYS A  58     1453   2416   2476   -276    147   -143       C  
ATOM    530  CE ALYS A  58      -4.937   8.705  24.218  0.50 23.55           C  
ANISOU  530  CE ALYS A  58     2848   3084   3015   -212     12    -47       C  
ATOM    531  CE BLYS A  58      -4.803  12.264  21.783  0.50 20.00           C  
ANISOU  531  CE BLYS A  58     2222   2454   2921   -310    176    -24       C  
ATOM    532  NZ ALYS A  58      -6.363   9.073  24.491  0.50 25.39           N  
ANISOU  532  NZ ALYS A  58     2971   3339   3334   -115    -51     19       N  
ATOM    533  NZ BLYS A  58      -5.470  12.556  20.465  0.50 19.64           N  
ANISOU  533  NZ BLYS A  58     2133   2256   3073   -303    -88     53       N  
ATOM    534  N   ASN A  59      -4.667   9.400  18.352  1.00 13.54           N  
ANISOU  534  N   ASN A  59     1481   1485   2176     32    627    145       N  
ATOM    535  CA  ASN A  59      -4.393  10.060  17.072  1.00 13.91           C  
ANISOU  535  CA  ASN A  59     1536   1524   2225   -212    647     85       C  
ATOM    536  C   ASN A  59      -3.566  11.300  17.362  1.00 14.28           C  
ANISOU  536  C   ASN A  59     1819   1486   2119   -109    660      5       C  
ATOM    537  O   ASN A  59      -3.799  11.997  18.371  1.00 18.10           O  
ANISOU  537  O   ASN A  59     2629   1680   2565   -110   1138   -183       O  
ATOM    538  CB  ASN A  59      -5.713  10.427  16.368  1.00 15.42           C  
ANISOU  538  CB  ASN A  59     1775   1878   2204    -94    569    289       C  
ATOM    539  CG  ASN A  59      -6.615   9.255  16.075  1.00 16.26           C  
ANISOU  539  CG  ASN A  59      929   2668   2581   -338     -9     33       C  
ATOM    540  OD1 ASN A  59      -6.199   8.217  15.601  1.00 17.11           O  
ANISOU  540  OD1 ASN A  59     1647   2219   2632     58    470    397       O  
ATOM    541  ND2 ASN A  59      -7.923   9.429  16.342  1.00 24.83           N  
ANISOU  541  ND2 ASN A  59     1428   4021   3984    -36   -282    129       N  
ATOM    542  N   THR A  60      -2.597  11.578  16.505  1.00 13.55           N  
ANISOU  542  N   THR A  60     1817   1470   1859   -239    694     73       N  
ATOM    543  CA  THR A  60      -1.831  12.792  16.606  1.00 13.19           C  
ANISOU  543  CA  THR A  60     1785   1340   1886    -30    576     55       C  
ATOM    544  C   THR A  60      -1.707  13.415  15.222  1.00 12.66           C  
ANISOU  544  C   THR A  60     1620   1389   1802    -97    402     52       C  
ATOM    545  O   THR A  60      -1.802  12.739  14.194  1.00 11.69           O  
ANISOU  545  O   THR A  60     1217   1378   1844   -101    379    -37       O  
ATOM    546  CB  THR A  60      -0.467  12.561  17.192  1.00 13.34           C  
ANISOU  546  CB  THR A  60     1853   1356   1858    -34    438    113       C  
ATOM    547  OG1 THR A  60       0.299  11.699  16.359  1.00 13.96           O  
ANISOU  547  OG1 THR A  60     1748   1533   2021    153    299     96       O  
ATOM    548  CG2 THR A  60      -0.517  11.970  18.604  1.00 15.48           C  
ANISOU  548  CG2 THR A  60     1808   2085   1987     97    334    315       C  
ATOM    549  N   GLU A  61      -1.434  14.704  15.206  1.00 12.24           N  
ANISOU  549  N   GLU A  61     1689   1204   1755    -26    452    -19       N  
ATOM    550  CA  GLU A  61      -1.096  15.409  13.990  1.00 11.57           C  
ANISOU  550  CA  GLU A  61     1177   1342   1874    -74    307    -22       C  
ATOM    551  C   GLU A  61      -0.186  16.549  14.313  1.00 11.59           C  
ANISOU  551  C   GLU A  61     1527   1264   1609   -173    349   -111       C  
ATOM    552  O   GLU A  61      -0.452  17.359  15.210  1.00 13.98           O  
ANISOU  552  O   GLU A  61     1809   1535   1967   -138    601   -183       O  
ATOM    553  CB  GLU A  61      -2.345  15.913  13.322  1.00 13.24           C  
ANISOU  553  CB  GLU A  61     1314   1508   2208   -434    133     62       C  
ATOM    554  CG  GLU A  61      -2.084  16.666  12.039  1.00 16.96           C  
ANISOU  554  CG  GLU A  61     1294   2570   2579   -401     -4    413       C  
ATOM    555  CD  GLU A  61      -3.394  17.147  11.445  1.00 22.23           C  
ANISOU  555  CD  GLU A  61     1209   3720   3513   -653    648    755       C  
ATOM    556  OE1 GLU A  61      -3.408  18.231  10.823  1.00 29.51           O  
ANISOU  556  OE1 GLU A  61     2668   4401   4141   -198   -189   1252       O  
ATOM    557  OE2 GLU A  61      -4.433  16.524  11.675  1.00 27.01           O  
ANISOU  557  OE2 GLU A  61     1177   4934   4150   -431   -209    817       O  
ATOM    558  N   ILE A  62       0.886  16.640  13.544  1.00 10.42           N  
ANISOU  558  N   ILE A  62     1364   1195   1398   -105    208     15       N  
ATOM    559  CA  ILE A  62       1.814  17.766  13.636  1.00 10.31           C  
ANISOU  559  CA  ILE A  62     1367   1190   1361   -199    185    -70       C  
ATOM    560  C   ILE A  62       2.000  18.377  12.240  1.00  9.70           C  
ANISOU  560  C   ILE A  62     1098   1202   1384   -234     35    127       C  
ATOM    561  O   ILE A  62       2.094  17.644  11.248  1.00 10.99           O  
ANISOU  561  O   ILE A  62     1701   1230   1243   -144    138     -7       O  
ATOM    562  CB  ILE A  62       3.179  17.409  14.291  1.00 10.10           C  
ANISOU  562  CB  ILE A  62     1037   1328   1470   -187     53    143       C  
ATOM    563  CG1 ILE A  62       3.983  16.329  13.511  1.00 12.03           C  
ANISOU  563  CG1 ILE A  62     1495   1596   1478   -381    -12     21       C  
ATOM    564  CG2 ILE A  62       2.957  16.977  15.742  1.00 13.59           C  
ANISOU  564  CG2 ILE A  62     2058   1622   1482    156     63    200       C  
ATOM    565  CD1 ILE A  62       5.383  16.082  13.989  1.00 12.48           C  
ANISOU  565  CD1 ILE A  62      838   1887   2015     51   -422     37       C  
ATOM    566  N   SER A  63       1.997  19.682  12.178  1.00  8.72           N  
ANISOU  566  N   SER A  63      793   1137   1382    -29    119    -15       N  
ATOM    567  CA  SER A  63       2.408  20.450  10.991  1.00  8.57           C  
ANISOU  567  CA  SER A  63      872   1089   1295   -113     81    101       C  
ATOM    568  C   SER A  63       3.545  21.389  11.320  1.00  8.22           C  
ANISOU  568  C   SER A  63      574   1074   1474    -33    -54     95       C  
ATOM    569  O   SER A  63       3.521  22.003  12.379  1.00  9.77           O  
ANISOU  569  O   SER A  63      882   1314   1517   -188     58   -195       O  
ATOM    570  CB  SER A  63       1.217  21.221  10.388  1.00  9.79           C  
ANISOU  570  CB  SER A  63     1153   1193   1374     27    -43    -40       C  
ATOM    571  OG  SER A  63       0.193  20.359   9.966  1.00 12.08           O  
ANISOU  571  OG  SER A  63     1304   1479   1806     35   -425    -47       O  
ATOM    572  N   PHE A  64       4.507  21.501  10.441  1.00  8.15           N  
ANISOU  572  N   PHE A  64      876    934   1287     35     35     -7       N  
ATOM    573  CA  PHE A  64       5.681  22.238  10.741  1.00  8.98           C  
ANISOU  573  CA  PHE A  64      995   1047   1367   -200      0    -29       C  
ATOM    574  C   PHE A  64       6.416  22.649   9.463  1.00  7.69           C  
ANISOU  574  C   PHE A  64      509   1052   1359   -114     68    158       C  
ATOM    575  O   PHE A  64       6.210  22.089   8.405  1.00  9.10           O  
ANISOU  575  O   PHE A  64      956   1278   1222     -6    -57     35       O  
ATOM    576  CB  PHE A  64       6.619  21.367  11.658  1.00 10.08           C  
ANISOU  576  CB  PHE A  64     1220   1229   1379    -51    -51    -63       C  
ATOM    577  CG  PHE A  64       6.993  20.042  11.044  1.00  8.95           C  
ANISOU  577  CG  PHE A  64      307   1536   1556    -79   -119     98       C  
ATOM    578  CD1 PHE A  64       6.150  18.961  11.207  1.00  9.45           C  
ANISOU  578  CD1 PHE A  64      720   1484   1384   -313    -97    159       C  
ATOM    579  CD2 PHE A  64       8.123  19.903  10.317  1.00  9.20           C  
ANISOU  579  CD2 PHE A  64      429   1297   1767   -240     28     96       C  
ATOM    580  CE1 PHE A  64       6.409  17.765  10.533  1.00  9.83           C  
ANISOU  580  CE1 PHE A  64      299   1529   1907    -34    -72    114       C  
ATOM    581  CE2 PHE A  64       8.411  18.691   9.705  1.00 11.18           C  
ANISOU  581  CE2 PHE A  64      929   1946   1371    -38    181     68       C  
ATOM    582  CZ  PHE A  64       7.519  17.658   9.870  1.00  9.64           C  
ANISOU  582  CZ  PHE A  64      394   1473   1794    197   -417    -47       C  
ATOM    583  N   ILE A  65       7.360  23.531   9.645  1.00  7.88           N  
ANISOU  583  N   ILE A  65      409   1183   1402   -110      1      8       N  
ATOM    584  CA  ILE A  65       8.318  23.985   8.668  1.00  8.17           C  
ANISOU  584  CA  ILE A  65      605    950   1546    -74    181     88       C  
ATOM    585  C   ILE A  65       9.689  23.568   9.145  1.00  8.93           C  
ANISOU  585  C   ILE A  65      881   1008   1504    -84    162     93       C  
ATOM    586  O   ILE A  65       9.989  23.682  10.322  1.00  8.38           O  
ANISOU  586  O   ILE A  65      691   1059   1435   -221    -87      7       O  
ATOM    587  CB  ILE A  65       8.199  25.516   8.437  1.00  9.58           C  
ANISOU  587  CB  ILE A  65      905   1084   1649    -64    -72    -44       C  
ATOM    588  CG1 ILE A  65       6.816  25.859   7.890  1.00 10.77           C  
ANISOU  588  CG1 ILE A  65      962   1263   1864    189   -203    268       C  
ATOM    589  CG2 ILE A  65       9.342  25.980   7.552  1.00 11.08           C  
ANISOU  589  CG2 ILE A  65     1096   1142   1969   -170      0    119       C  
ATOM    590  CD1 ILE A  65       6.547  27.395   7.823  1.00 14.05           C  
ANISOU  590  CD1 ILE A  65     1206   1374   2758     95   -246    278       C  
ATOM    591  N   LEU A  66      10.490  23.004   8.271  1.00  8.20           N  
ANISOU  591  N   LEU A  66      610    993   1511     72     97     -2       N  
ATOM    592  CA  LEU A  66      11.752  22.511   8.645  1.00  7.73           C  
ANISOU  592  CA  LEU A  66      588    827   1523    132    187    155       C  
ATOM    593  C   LEU A  66      12.608  23.606   9.304  1.00  9.53           C  
ANISOU  593  C   LEU A  66      944   1095   1581    -33     44    115       C  
ATOM    594  O   LEU A  66      12.679  24.725   8.785  1.00 10.13           O  
ANISOU  594  O   LEU A  66     1087   1177   1584     99     70    156       O  
ATOM    595  CB  LEU A  66      12.519  21.913   7.419  1.00  9.53           C  
ANISOU  595  CB  LEU A  66      598   1311   1713     56     45     49       C  
ATOM    596  CG  LEU A  66      11.914  20.659   6.802  1.00 11.29           C  
ANISOU  596  CG  LEU A  66     1390   1270   1630    -85    -53   -126       C  
ATOM    597  CD1 LEU A  66      12.524  20.372   5.407  1.00 14.48           C  
ANISOU  597  CD1 LEU A  66     1704   1775   2021    255    470   -353       C  
ATOM    598  CD2 LEU A  66      12.039  19.521   7.738  1.00 12.49           C  
ANISOU  598  CD2 LEU A  66     1588   1167   1990   -281   -114    -85       C  
ATOM    599  N   GLY A  67      13.291  23.264  10.398  1.00  9.00           N  
ANISOU  599  N   GLY A  67      847   1031   1539    -22     57    193       N  
ATOM    600  CA  GLY A  67      14.120  24.175  11.124  1.00  9.96           C  
ANISOU  600  CA  GLY A  67     1217   1110   1458    -50     37     -6       C  
ATOM    601  C   GLY A  67      13.450  25.083  12.110  1.00  8.99           C  
ANISOU  601  C   GLY A  67      526   1194   1695   -194    183     64       C  
ATOM    602  O   GLY A  67      14.146  25.836  12.806  1.00  9.62           O  
ANISOU  602  O   GLY A  67      712   1119   1823   -142    -57    -89       O  
ATOM    603  N   GLN A  68      12.132  25.064  12.161  1.00  8.61           N  
ANISOU  603  N   GLN A  68      739    923   1608   -190     91    -91       N  
ATOM    604  CA  GLN A  68      11.304  26.044  12.900  1.00  9.37           C  
ANISOU  604  CA  GLN A  68      988    987   1585   -129     60    -67       C  
ATOM    605  C   GLN A  68      10.573  25.360  14.059  1.00  9.12           C  
ANISOU  605  C   GLN A  68      805    968   1691   -195      9    -10       C  
ATOM    606  O   GLN A  68       9.689  24.532  13.879  1.00  9.37           O  
ANISOU  606  O   GLN A  68      862   1027   1670   -207     12    -63       O  
ATOM    607  CB  GLN A  68      10.316  26.750  11.982  1.00 10.47           C  
ANISOU  607  CB  GLN A  68     1351    925   1701    -59    -33   -236       C  
ATOM    608  CG  GLN A  68      11.130  27.404  10.833  1.00 12.59           C  
ANISOU  608  CG  GLN A  68     1490   1475   1817   -431   -440     52       C  
ATOM    609  CD  GLN A  68      10.432  28.427  10.039  1.00 15.00           C  
ANISOU  609  CD  GLN A  68     1894   1319   2486   -289   -666    -66       C  
ATOM    610  OE1 GLN A  68       9.239  28.772  10.274  1.00 17.48           O  
ANISOU  610  OE1 GLN A  68     1848   1609   3182      3   -938    149       O  
ATOM    611  NE2 GLN A  68      11.169  28.981   9.060  1.00 15.42           N  
ANISOU  611  NE2 GLN A  68     2399   1196   2264   -206   -510    396       N  
ATOM    612  N  AGLU A  69      10.965  25.721  15.280  0.50  8.99           N  
ANISOU  612  N  AGLU A  69     1121    861   1431   -102     32    -43       N  
ATOM    613  N  BGLU A  69      11.007  25.731  15.288  0.50  9.85           N  
ANISOU  613  N  BGLU A  69     1148   1100   1493   -122     81      5       N  
ATOM    614  CA AGLU A  69      10.453  24.986  16.429  0.50  9.33           C  
ANISOU  614  CA AGLU A  69     1194    875   1475   -231      3   -104       C  
ATOM    615  CA BGLU A  69      10.443  25.188  16.558  0.50 11.45           C  
ANISOU  615  CA BGLU A  69     1328   1345   1678   -126    100     -5       C  
ATOM    616  C  AGLU A  69       8.973  25.255  16.704  0.50  9.46           C  
ANISOU  616  C  AGLU A  69     1163   1090   1341     40     55   -159       C  
ATOM    617  C  BGLU A  69       8.935  25.238  16.569  0.50 10.05           C  
ANISOU  617  C  BGLU A  69     1185   1287   1344     91    164   -100       C  
ATOM    618  O  AGLU A  69       8.439  26.362  16.501  0.50  8.09           O  
ANISOU  618  O  AGLU A  69      929    942   1202    186   -171   -194       O  
ATOM    619  O  BGLU A  69       8.360  26.214  16.030  0.50  7.53           O  
ANISOU  619  O  BGLU A  69      665    946   1249    142   -135   -292       O  
ATOM    620  CB AGLU A  69      11.341  25.336  17.639  0.50  9.54           C  
ANISOU  620  CB AGLU A  69     1269    898   1457    -82   -109     86       C  
ATOM    621  CB BGLU A  69      10.986  26.021  17.775  0.50 12.11           C  
ANISOU  621  CB BGLU A  69     1405   1711   1484   -108    158    159       C  
ATOM    622  CG AGLU A  69      10.740  25.075  19.078  0.50 12.46           C  
ANISOU  622  CG AGLU A  69     1806   1245   1684   -375   -123    249       C  
ATOM    623  CG BGLU A  69      10.285  27.325  18.010  0.50 17.91           C  
ANISOU  623  CG BGLU A  69     2300   2244   2259    -51     67   -138       C  
ATOM    624  CD AGLU A  69      11.558  25.709  20.172  0.50 19.19           C  
ANISOU  624  CD AGLU A  69     2843   2465   1980   -462   -372    358       C  
ATOM    625  CD BGLU A  69      10.764  28.129  19.228  0.50 19.00           C  
ANISOU  625  CD BGLU A  69     1765   2737   2717    251   -159   -321       C  
ATOM    626  OE1AGLU A  69      11.359  26.907  20.455  0.50 22.75           O  
ANISOU  626  OE1AGLU A  69     3457   2676   2510  -1141   -573    -38       O  
ATOM    627  OE1BGLU A  69      11.731  27.729  19.900  0.50 16.49           O  
ANISOU  627  OE1BGLU A  69     1157   2311   2794     97   -429    -75       O  
ATOM    628  OE2AGLU A  69      12.386  24.988  20.735  0.50 22.91           O  
ANISOU  628  OE2AGLU A  69     2795   3499   2411   -808   -711    441       O  
ATOM    629  OE2BGLU A  69      10.173  29.199  19.489  0.50 24.57           O  
ANISOU  629  OE2BGLU A  69     3192   2901   3241    599   -187  -1252       O  
ATOM    630  N   PHE A  70       8.289  24.225  17.191  1.00  9.00           N  
ANISOU  630  N   PHE A  70      849   1137   1433    130     65   -162       N  
ATOM    631  CA  PHE A  70       6.877  24.209  17.449  1.00  8.68           C  
ANISOU  631  CA  PHE A  70      649   1122   1526    227    213    -39       C  
ATOM    632  C   PHE A  70       6.628  23.427  18.725  1.00  9.33           C  
ANISOU  632  C   PHE A  70      901   1020   1624    156    222   -114       C  
ATOM    633  O   PHE A  70       7.401  22.651  19.222  1.00 10.80           O  
ANISOU  633  O   PHE A  70     1284   1244   1575    417    146    168       O  
ATOM    634  CB  PHE A  70       6.130  23.612  16.239  1.00  9.73           C  
ANISOU  634  CB  PHE A  70      969   1318   1410    293    155    -20       C  
ATOM    635  CG  PHE A  70       6.500  22.196  15.895  1.00  8.79           C  
ANISOU  635  CG  PHE A  70      521   1221   1595     97     36     37       C  
ATOM    636  CD1 PHE A  70       7.571  21.925  15.122  1.00  7.57           C  
ANISOU  636  CD1 PHE A  70      277   1072   1524    121    -99    -44       C  
ATOM    637  CD2 PHE A  70       5.709  21.164  16.335  1.00 11.65           C  
ANISOU  637  CD2 PHE A  70     1434   1375   1614     -9    210   -129       C  
ATOM    638  CE1 PHE A  70       7.932  20.611  14.768  1.00  8.56           C  
ANISOU  638  CE1 PHE A  70      459   1355   1436     94     75     35       C  
ATOM    639  CE2 PHE A  70       6.020  19.848  16.007  1.00 12.07           C  
ANISOU  639  CE2 PHE A  70     1506   1419   1659   -247    261      5       C  
ATOM    640  CZ  PHE A  70       7.083  19.578  15.230  1.00 10.88           C  
ANISOU  640  CZ  PHE A  70     1321   1414   1398     -2   -131   -185       C  
ATOM    641  N   ASP A  71       5.443  23.700  19.237  1.00 10.43           N  
ANISOU  641  N   ASP A  71     1063   1157   1743    283     99    245       N  
ATOM    642  CA  ASP A  71       4.871  22.970  20.384  1.00 11.11           C  
ANISOU  642  CA  ASP A  71      988   1497   1736    239    319     99       C  
ATOM    643  C   ASP A  71       4.125  21.730  19.938  1.00 11.85           C  
ANISOU  643  C   ASP A  71     1081   1646   1774    -92    174    257       C  
ATOM    644  O   ASP A  71       3.393  21.732  18.937  1.00 14.10           O  
ANISOU  644  O   ASP A  71     1360   1766   2229    223    210    449       O  
ATOM    645  CB  ASP A  71       3.788  23.834  21.036  1.00 12.52           C  
ANISOU  645  CB  ASP A  71     1287   1689   1780    397    285    245       C  
ATOM    646  CG  ASP A  71       4.320  25.049  21.656  1.00 15.35           C  
ANISOU  646  CG  ASP A  71     1683   2485   1662    411    178   -269       C  
ATOM    647  OD1 ASP A  71       5.271  24.902  22.430  1.00 17.62           O  
ANISOU  647  OD1 ASP A  71     2210   2403   2080    299   -239   -112       O  
ATOM    648  OD2 ASP A  71       3.701  26.139  21.432  1.00 15.76           O  
ANISOU  648  OD2 ASP A  71     1343   2468   2175    309    -19   -138       O  
ATOM    649  N   GLU A  72       4.366  20.628  20.664  1.00 12.16           N  
ANISOU  649  N   GLU A  72     1167   1647   1803    -31    121    224       N  
ATOM    650  CA  GLU A  72       3.797  19.336  20.319  1.00 12.62           C  
ANISOU  650  CA  GLU A  72     1171   1681   1939    -62    142    292       C  
ATOM    651  C   GLU A  72       3.304  18.707  21.622  1.00 14.15           C  
ANISOU  651  C   GLU A  72     1667   1674   2033    -45    145    346       C  
ATOM    652  O   GLU A  72       3.948  18.736  22.625  1.00 13.95           O  
ANISOU  652  O   GLU A  72     1506   1902   1889    -81    401    437       O  
ATOM    653  CB  GLU A  72       4.886  18.458  19.649  1.00 12.49           C  
ANISOU  653  CB  GLU A  72     1419   1469   1856   -177    223    216       C  
ATOM    654  CG  GLU A  72       4.485  16.998  19.336  1.00 12.77           C  
ANISOU  654  CG  GLU A  72     1293   1732   1826    -13     38    242       C  
ATOM    655  CD  GLU A  72       5.527  16.195  18.634  1.00 12.41           C  
ANISOU  655  CD  GLU A  72     1377   1581   1757     -6     39    104       C  
ATOM    656  OE1 GLU A  72       6.652  16.639  18.556  1.00 13.72           O  
ANISOU  656  OE1 GLU A  72     1629   1628   1953    -39     98   -169       O  
ATOM    657  OE2 GLU A  72       5.158  15.083  18.191  1.00 16.18           O  
ANISOU  657  OE2 GLU A  72     2280   1693   2171   -206    -34     47       O  
ATOM    658  N   VAL A  73       2.137  18.126  21.579  1.00 13.63           N  
ANISOU  658  N   VAL A  73     1439   1587   2152    178     84    480       N  
ATOM    659  CA  VAL A  73       1.621  17.305  22.679  1.00 13.49           C  
ANISOU  659  CA  VAL A  73     1332   1618   2173    151    211    491       C  
ATOM    660  C   VAL A  73       1.684  15.868  22.154  1.00 13.41           C  
ANISOU  660  C   VAL A  73     1320   1754   2020    -54     37    451       C  
ATOM    661  O   VAL A  73       1.015  15.498  21.208  1.00 15.58           O  
ANISOU  661  O   VAL A  73     1609   1806   2504   -178   -313    736       O  
ATOM    662  CB  VAL A  73       0.244  17.718  23.174  1.00 15.87           C  
ANISOU  662  CB  VAL A  73     1660   1992   2377     76    389    283       C  
ATOM    663  CG1 VAL A  73      -0.216  16.734  24.283  1.00 17.44           C  
ANISOU  663  CG1 VAL A  73     1734   2212   2679   -232    690    499       C  
ATOM    664  CG2 VAL A  73       0.273  19.188  23.777  1.00 17.71           C  
ANISOU  664  CG2 VAL A  73     1967   1877   2884    337    703    386       C  
ATOM    665  N   THR A  74       2.590  15.070  22.697  1.00 12.80           N  
ANISOU  665  N   THR A  74     1348   1655   1859    157     42    346       N  
ATOM    666  CA  THR A  74       2.787  13.721  22.192  1.00 12.53           C  
ANISOU  666  CA  THR A  74     1346   1646   1768   -171    125    355       C  
ATOM    667  C   THR A  74       1.649  12.752  22.542  1.00 13.15           C  
ANISOU  667  C   THR A  74     1195   1768   2030     11    105    332       C  
ATOM    668  O   THR A  74       0.780  13.062  23.343  1.00 13.79           O  
ANISOU  668  O   THR A  74     1241   1740   2256    -45    172    391       O  
ATOM    669  CB  THR A  74       4.140  13.167  22.714  1.00 12.69           C  
ANISOU  669  CB  THR A  74     1398   1648   1774    -42   -117    233       C  
ATOM    670  OG1 THR A  74       3.965  13.002  24.126  1.00 13.57           O  
ANISOU  670  OG1 THR A  74     2042   1573   1539    216    249    224       O  
ATOM    671  CG2 THR A  74       5.295  14.106  22.406  1.00 11.57           C  
ANISOU  671  CG2 THR A  74      838   1416   2142   -202      9    249       C  
ATOM    672  N   ALA A  75       1.671  11.572  21.929  1.00 13.76           N  
ANISOU  672  N   ALA A  75     1415   1706   2107   -105    217    302       N  
ATOM    673  CA  ALA A  75       0.580  10.583  22.114  1.00 15.27           C  
ANISOU  673  CA  ALA A  75     1567   1990   2243   -255    178    249       C  
ATOM    674  C   ALA A  75       0.471  10.183  23.591  1.00 14.87           C  
ANISOU  674  C   ALA A  75     1456   1945   2248   -260    170    320       C  
ATOM    675  O   ALA A  75      -0.616   9.890  24.102  1.00 17.27           O  
ANISOU  675  O   ALA A  75     1598   2421   2540   -577    104    336       O  
ATOM    676  CB  ALA A  75       0.809   9.329  21.221  1.00 15.03           C  
ANISOU  676  CB  ALA A  75     1206   2142   2360   -112    211    257       C  
ATOM    677  N   ASP A  76       1.635  10.181  24.270  1.00 14.06           N  
ANISOU  677  N   ASP A  76     1632   1663   2047   -233    178    290       N  
ATOM    678  CA  ASP A  76       1.645   9.888  25.717  1.00 14.28           C  
ANISOU  678  CA  ASP A  76     1821   1776   1827   -244    247    299       C  
ATOM    679  C   ASP A  76       1.475  11.120  26.607  1.00 14.88           C  
ANISOU  679  C   ASP A  76     1814   1875   1963   -103    419    221       C  
ATOM    680  O   ASP A  76       1.623  11.046  27.808  1.00 17.48           O  
ANISOU  680  O   ASP A  76     2561   2148   1929    137    393    302       O  
ATOM    681  CB  ASP A  76       2.904   9.141  26.115  1.00 14.08           C  
ANISOU  681  CB  ASP A  76     1722   1714   1912   -302    151    214       C  
ATOM    682  CG  ASP A  76       4.199   9.933  25.808  1.00 12.79           C  
ANISOU  682  CG  ASP A  76     1387   1484   1985    273    -58     88       C  
ATOM    683  OD1 ASP A  76       4.329  10.438  24.654  1.00 13.77           O  
ANISOU  683  OD1 ASP A  76     1949   1564   1719     27    173    355       O  
ATOM    684  OD2 ASP A  76       5.074  10.129  26.703  1.00 13.70           O  
ANISOU  684  OD2 ASP A  76     1705   1515   1985    -53    185    291       O  
ATOM    685  N   ASP A  77       1.112  12.260  26.026  1.00 14.13           N  
ANISOU  685  N   ASP A  77     1765   1751   1851    -15    561    205       N  
ATOM    686  CA  ASP A  77       0.711  13.487  26.735  1.00 16.50           C  
ANISOU  686  CA  ASP A  77     2112   2046   2109    -25    595    174       C  
ATOM    687  C   ASP A  77       1.890  14.232  27.346  1.00 15.84           C  
ANISOU  687  C   ASP A  77     2165   1944   1906     19    544    191       C  
ATOM    688  O   ASP A  77       1.709  14.944  28.340  1.00 18.12           O  
ANISOU  688  O   ASP A  77     2089   2417   2377     29    787   -212       O  
ATOM    689  CB  ASP A  77      -0.427  13.269  27.743  1.00 16.83           C  
ANISOU  689  CB  ASP A  77     2076   2086   2233    -75    670    181       C  
ATOM    690  CG  ASP A  77      -1.287  14.496  27.907  1.00 22.22           C  
ANISOU  690  CG  ASP A  77     2500   2987   2955    163   1007    291       C  
ATOM    691  OD1 ASP A  77      -1.946  14.600  28.963  1.00 28.90           O  
ANISOU  691  OD1 ASP A  77     3185   3937   3855    137   1551    314       O  
ATOM    692  OD2 ASP A  77      -1.357  15.360  26.994  1.00 27.62           O  
ANISOU  692  OD2 ASP A  77     3256   3565   3669     72   1066    809       O  
ATOM    693  N   ARG A  78       3.077  14.165  26.733  1.00 14.80           N  
ANISOU  693  N   ARG A  78     2164   1721   1735     78    600     74       N  
ATOM    694  CA  ARG A  78       4.139  15.107  27.102  1.00 14.19           C  
ANISOU  694  CA  ARG A  78     2210   1605   1577     49    406    176       C  
ATOM    695  C   ARG A  78       3.947  16.357  26.269  1.00 14.21           C  
ANISOU  695  C   ARG A  78     2127   1714   1557    201    456    160       C  
ATOM    696  O   ARG A  78       3.617  16.301  25.111  1.00 15.03           O  
ANISOU  696  O   ARG A  78     2310   1544   1857    168    472    152       O  
ATOM    697  CB  ARG A  78       5.526  14.561  26.761  1.00 14.54           C  
ANISOU  697  CB  ARG A  78     2333   1537   1653    120    366    185       C  
ATOM    698  CG  ARG A  78       6.130  13.475  27.702  1.00 14.01           C  
ANISOU  698  CG  ARG A  78     2011   1620   1689     48     69    252       C  
ATOM    699  CD  ARG A  78       7.375  12.868  27.128  1.00 12.51           C  
ANISOU  699  CD  ARG A  78     1649   1462   1640    102    -49     28       C  
ATOM    700  NE  ARG A  78       7.000  11.979  26.032  1.00 12.68           N  
ANISOU  700  NE  ARG A  78     1835   1357   1625    209     19     72       N  
ATOM    701  CZ  ARG A  78       7.593  11.963  24.853  1.00 11.44           C  
ANISOU  701  CZ  ARG A  78     1169   1390   1785    -72    146     36       C  
ATOM    702  NH1 ARG A  78       8.620  12.737  24.586  1.00 10.83           N  
ANISOU  702  NH1 ARG A  78      989   1448   1675    -67   -121     94       N  
ATOM    703  NH2 ARG A  78       7.126  11.206  23.906  1.00 13.23           N  
ANISOU  703  NH2 ARG A  78     2130   1213   1683   -112    -37    -20       N  
ATOM    704  N   LYS A  79       4.237  17.480  26.907  1.00 14.49           N  
ANISOU  704  N   LYS A  79     2142   1688   1674     79    464    100       N  
ATOM    705  CA  LYS A  79       4.186  18.779  26.234  1.00 14.58           C  
ANISOU  705  CA  LYS A  79     1953   1688   1896    248    336     77       C  
ATOM    706  C   LYS A  79       5.600  19.143  25.915  1.00 13.38           C  
ANISOU  706  C   LYS A  79     1914   1389   1781    240    331     52       C  
ATOM    707  O   LYS A  79       6.397  19.403  26.821  1.00 16.50           O  
ANISOU  707  O   LYS A  79     2511   2058   1698     58    487    -96       O  
ATOM    708  CB  LYS A  79       3.504  19.835  27.109  1.00 15.80           C  
ANISOU  708  CB  LYS A  79     2208   1653   2140    232    472    170       C  
ATOM    709  CG  LYS A  79       2.028  19.608  27.214  1.00 23.23           C  
ANISOU  709  CG  LYS A  79     2900   2735   3191    262    299    -42       C  
ATOM    710  CD  LYS A  79       1.601  18.462  28.079  1.00 29.98           C  
ANISOU  710  CD  LYS A  79     3780   3570   4038    -46    302    166       C  
ATOM    711  CE  LYS A  79       0.129  18.607  28.515  1.00 33.43           C  
ANISOU  711  CE  LYS A  79     4034   4235   4432     50    273    208       C  
ATOM    712  NZ  LYS A  79      -0.611  17.325  28.423  1.00 34.82           N  
ANISOU  712  NZ  LYS A  79     4389   4187   4651     85    347     83       N  
ATOM    713  N   VAL A  80       5.991  19.037  24.633  1.00 12.30           N  
ANISOU  713  N   VAL A  80     1725   1445   1501    289    243     15       N  
ATOM    714  CA  VAL A  80       7.394  19.138  24.229  1.00 11.71           C  
ANISOU  714  CA  VAL A  80     1597   1422   1428    198    204     40       C  
ATOM    715  C   VAL A  80       7.548  20.298  23.257  1.00 11.07           C  
ANISOU  715  C   VAL A  80     1459   1272   1473    284     41    -23       C  
ATOM    716  O   VAL A  80       6.597  20.784  22.643  1.00 11.56           O  
ANISOU  716  O   VAL A  80     1313   1367   1709     67    145    119       O  
ATOM    717  CB  VAL A  80       7.882  17.810  23.574  1.00 11.15           C  
ANISOU  717  CB  VAL A  80     1413   1209   1614    108    293     32       C  
ATOM    718  CG1 VAL A  80       7.627  16.588  24.519  1.00 12.58           C  
ANISOU  718  CG1 VAL A  80     1632   1260   1886    344    331    351       C  
ATOM    719  CG2 VAL A  80       7.216  17.556  22.233  1.00 12.41           C  
ANISOU  719  CG2 VAL A  80     1983   1417   1314    259    360     60       C  
ATOM    720  N  ALYS A  81       8.795  20.739  23.166  0.50 10.51           N  
ANISOU  720  N  ALYS A  81     1393   1143   1454    305    160    -11       N  
ATOM    721  N  BLYS A  81       8.793  20.725  23.151  0.50 10.72           N  
ANISOU  721  N  BLYS A  81     1464   1158   1449    305    158    -29       N  
ATOM    722  CA ALYS A  81       9.221  21.686  22.136  0.50 10.16           C  
ANISOU  722  CA ALYS A  81     1201   1144   1515    132     96     -8       C  
ATOM    723  CA BLYS A  81       9.188  21.672  22.124  0.50 10.71           C  
ANISOU  723  CA BLYS A  81     1401   1180   1488    150     80    -13       C  
ATOM    724  C  ALYS A  81       9.983  20.883  21.101  0.50 10.42           C  
ANISOU  724  C  ALYS A  81     1223   1288   1449    185    171    -27       C  
ATOM    725  C  BLYS A  81      10.005  20.919  21.094  0.50 10.64           C  
ANISOU  725  C  BLYS A  81     1364   1246   1431    191    150    -46       C  
ATOM    726  O  ALYS A  81      10.929  20.181  21.428  0.50 10.59           O  
ANISOU  726  O  ALYS A  81     1043   1429   1552      7    -36      6       O  
ATOM    727  O  BLYS A  81      11.017  20.306  21.415  0.50 11.05           O  
ANISOU  727  O  BLYS A  81     1537   1258   1403    115    -28    -75       O  
ATOM    728  CB ALYS A  81      10.135  22.769  22.734  0.50 12.47           C  
ANISOU  728  CB ALYS A  81     1653   1355   1728     25     96    -71       C  
ATOM    729  CB BLYS A  81      10.027  22.793  22.722  0.50 13.13           C  
ANISOU  729  CB BLYS A  81     1801   1435   1750     96     92   -124       C  
ATOM    730  CG ALYS A  81       9.490  23.598  23.812  0.50 14.37           C  
ANISOU  730  CG ALYS A  81     1730   1641   2086     95    201   -202       C  
ATOM    731  CG BLYS A  81      10.170  23.933  21.779  0.50 16.29           C  
ANISOU  731  CG BLYS A  81     2275   1935   1979    -90     14    -20       C  
ATOM    732  CD ALYS A  81       8.508  24.588  23.255  0.50 16.59           C  
ANISOU  732  CD ALYS A  81     2142   2088   2072      6    -84    -15       C  
ATOM    733  CD BLYS A  81       9.203  24.987  22.185  0.50 22.02           C  
ANISOU  733  CD BLYS A  81     2861   2573   2930     24    148    -76       C  
ATOM    734  CE ALYS A  81       7.856  25.366  24.406  0.50 17.10           C  
ANISOU  734  CE ALYS A  81     2233   2049   2214    -82   -236   -230       C  
ATOM    735  CE BLYS A  81       9.538  25.513  23.571  0.50 24.06           C  
ANISOU  735  CE BLYS A  81     3210   2786   3145   -159     -2    -49       C  
ATOM    736  NZ ALYS A  81       6.858  26.389  23.958  0.50 17.49           N  
ANISOU  736  NZ ALYS A  81     2216   2280   2148    -88   -671    -20       N  
ATOM    737  NZ BLYS A  81       8.409  26.317  24.055  0.50 25.57           N  
ANISOU  737  NZ BLYS A  81     3236   2709   3770   -180    -10    -36       N  
ATOM    738  N   SER A  82       9.544  20.945  19.854  1.00  9.38           N  
ANISOU  738  N   SER A  82      855   1266   1441    331    115     55       N  
ATOM    739  CA  SER A  82      10.074  20.104  18.795  1.00  9.49           C  
ANISOU  739  CA  SER A  82     1039   1121   1444    157    195      5       C  
ATOM    740  C   SER A  82      10.665  20.950  17.676  1.00  8.43           C  
ANISOU  740  C   SER A  82      704   1154   1342    183   -108    -37       C  
ATOM    741  O   SER A  82      10.141  22.013  17.320  1.00  9.18           O  
ANISOU  741  O   SER A  82      953   1025   1510    325     28     39       O  
ATOM    742  CB  SER A  82       8.895  19.299  18.236  1.00 10.14           C  
ANISOU  742  CB  SER A  82     1143   1201   1506    -12    156    -49       C  
ATOM    743  OG  SER A  82       8.555  18.303  19.185  1.00 12.58           O  
ANISOU  743  OG  SER A  82     1758   1215   1806    -19    349    304       O  
ATOM    744  N   THR A  83      11.732  20.416  17.103  1.00  8.37           N  
ANISOU  744  N   THR A  83      755   1009   1414    117     17     54       N  
ATOM    745  CA  THR A  83      12.310  20.949  15.877  1.00  8.69           C  
ANISOU  745  CA  THR A  83      937    900   1462     83     19     56       C  
ATOM    746  C   THR A  83      12.584  19.782  14.953  1.00  9.18           C  
ANISOU  746  C   THR A  83     1125   1047   1315    242    209     64       C  
ATOM    747  O   THR A  83      13.160  18.778  15.374  1.00  9.92           O  
ANISOU  747  O   THR A  83     1269   1108   1390    287   -104     61       O  
ATOM    748  CB  THR A  83      13.540  21.750  16.136  1.00 10.13           C  
ANISOU  748  CB  THR A  83      837   1194   1816     15    104    -61       C  
ATOM    749  OG1 THR A  83      13.360  22.665  17.200  1.00 13.08           O  
ANISOU  749  OG1 THR A  83     1401   1418   2151   -186    -11   -433       O  
ATOM    750  CG2 THR A  83      13.952  22.478  14.894  1.00 13.49           C  
ANISOU  750  CG2 THR A  83     1480   1532   2113   -440    354    -48       C  
ATOM    751  N   ILE A  84      12.152  19.904  13.697  1.00  9.17           N  
ANISOU  751  N   ILE A  84     1250   1009   1222    159    -35    -26       N  
ATOM    752  CA  ILE A  84      12.393  18.895  12.685  1.00  8.83           C  
ANISOU  752  CA  ILE A  84      969    993   1393    211    165     28       C  
ATOM    753  C   ILE A  84      13.211  19.480  11.560  1.00  8.34           C  
ANISOU  753  C   ILE A  84      781   1128   1257     46    -15     38       C  
ATOM    754  O   ILE A  84      12.867  20.563  11.055  1.00  9.63           O  
ANISOU  754  O   ILE A  84     1264   1097   1298    115     -9     93       O  
ATOM    755  CB  ILE A  84      11.049  18.266  12.175  1.00  8.41           C  
ANISOU  755  CB  ILE A  84      965    919   1311    330    136    137       C  
ATOM    756  CG1 ILE A  84      10.213  17.651  13.330  1.00  8.58           C  
ANISOU  756  CG1 ILE A  84      839    943   1476     92    129    251       C  
ATOM    757  CG2 ILE A  84      11.354  17.200  11.132  1.00  9.86           C  
ANISOU  757  CG2 ILE A  84      931   1283   1532    168     65    -71       C  
ATOM    758  CD1 ILE A  84       8.911  17.077  13.038  1.00  8.98           C  
ANISOU  758  CD1 ILE A  84      398   1315   1700   -207     61    109       C  
ATOM    759  N   THR A  85      14.314  18.817  11.211  1.00  8.48           N  
ANISOU  759  N   THR A  85      788   1030   1404     43     74    184       N  
ATOM    760  CA  THR A  85      15.185  19.204  10.138  1.00 10.01           C  
ANISOU  760  CA  THR A  85     1062   1101   1639      7    228    112       C  
ATOM    761  C   THR A  85      15.408  18.028   9.216  1.00 10.66           C  
ANISOU  761  C   THR A  85     1348   1224   1479    -27    395    102       C  
ATOM    762  O   THR A  85      15.086  16.912   9.541  1.00 10.95           O  
ANISOU  762  O   THR A  85     1503   1157   1499    -57    438     27       O  
ATOM    763  CB  THR A  85      16.479  19.760  10.679  1.00  9.76           C  
ANISOU  763  CB  THR A  85      506   1233   1969    274    214    -82       C  
ATOM    764  OG1 THR A  85      17.087  18.720  11.472  1.00 13.98           O  
ANISOU  764  OG1 THR A  85     1260   1612   2437    188   -229   -142       O  
ATOM    765  CG2 THR A  85      16.295  21.003  11.501  1.00 14.40           C  
ANISOU  765  CG2 THR A  85     1534   1614   2321   -357    178   -536       C  
ATOM    766  N  ALEU A  86      16.208  18.257   8.185  0.50 10.43           N  
ANISOU  766  N  ALEU A  86     1069   1283   1607   -150    331    113       N  
ATOM    767  N  BLEU A  86      15.756  18.334   7.970  0.50 11.44           N  
ANISOU  767  N  BLEU A  86     1606   1190   1549     26    309    122       N  
ATOM    768  CA ALEU A  86      16.745  17.164   7.378  0.50 11.48           C  
ANISOU  768  CA ALEU A  86     1388   1328   1645   -193    124     23       C  
ATOM    769  CA BLEU A  86      16.146  17.338   6.980  0.50 11.87           C  
ANISOU  769  CA BLEU A  86     1502   1373   1634   -119    186     93       C  
ATOM    770  C  ALEU A  86      18.236  17.048   7.628  0.50 11.54           C  
ANISOU  770  C  ALEU A  86     1368   1270   1744   -239     77     10       C  
ATOM    771  C  BLEU A  86      17.645  17.350   6.892  0.50 13.07           C  
ANISOU  771  C  BLEU A  86     1553   1537   1876   -175    311    -17       C  
ATOM    772  O  ALEU A  86      18.921  18.096   7.630  0.50 13.08           O  
ANISOU  772  O  ALEU A  86     1661   1400   1908   -423    207   -105       O  
ATOM    773  O  BLEU A  86      18.267  18.364   6.509  0.50 15.98           O  
ANISOU  773  O  BLEU A  86     1801   1778   2493   -113    519     83       O  
ATOM    774  CB ALEU A  86      16.518  17.383   5.909  0.50 11.85           C  
ANISOU  774  CB ALEU A  86     1330   1513   1660   -210    135      5       C  
ATOM    775  CB BLEU A  86      15.544  17.629   5.591  0.50 13.17           C  
ANISOU  775  CB BLEU A  86     1849   1521   1632   -101    139     38       C  
ATOM    776  CG ALEU A  86      15.120  17.088   5.409  0.50 11.86           C  
ANISOU  776  CG ALEU A  86      937   1718   1851   -483   -260     66       C  
ATOM    777  CG BLEU A  86      14.304  16.892   5.064  0.50 16.13           C  
ANISOU  777  CG BLEU A  86     2064   2012   2051   -134    -90     89       C  
ATOM    778  CD1ALEU A  86      14.873  17.781   4.045  0.50 14.01           C  
ANISOU  778  CD1ALEU A  86     1487   1857   1976    -21    -59     65       C  
ATOM    779  CD1BLEU A  86      13.942  17.403   3.671  0.50 16.42           C  
ANISOU  779  CD1BLEU A  86     2508   2037   1690     49     80   -213       C  
ATOM    780  CD2ALEU A  86      14.928  15.556   5.301  0.50 10.47           C  
ANISOU  780  CD2ALEU A  86      273   1671   2031    -25   -181   -254       C  
ATOM    781  CD2BLEU A  86      14.468  15.374   5.037  0.50 14.89           C  
ANISOU  781  CD2BLEU A  86     2497   1574   1583   -443     65    -71       C  
ATOM    782  N  AASP A  87      18.731  15.811   7.816  0.50 11.45           N  
ANISOU  782  N  AASP A  87     1214   1360   1776   -236    195    -37       N  
ATOM    783  N  BASP A  87      18.244  16.227   7.257  0.50 12.72           N  
ANISOU  783  N  BASP A  87     1281   1708   1842   -233    189     11       N  
ATOM    784  CA AASP A  87      20.162  15.456   7.844  0.50 12.75           C  
ANISOU  784  CA AASP A  87     1234   1611   1996   -234    111      8       C  
ATOM    785  CA BASP A  87      19.668  16.094   7.321  0.50 14.13           C  
ANISOU  785  CA BASP A  87     1462   1863   2044   -197    122    -63       C  
ATOM    786  C  AASP A  87      20.402  14.512   6.687  0.50 12.25           C  
ANISOU  786  C  AASP A  87     1008   1667   1977   -292    130     75       C  
ATOM    787  C  BASP A  87      20.074  14.955   6.413  0.50 13.66           C  
ANISOU  787  C  BASP A  87     1365   1844   1980   -153    244    -17       C  
ATOM    788  O  AASP A  87      20.192  13.302   6.795  0.50 13.26           O  
ANISOU  788  O  AASP A  87      947   1753   2335   -172    -12    -25       O  
ATOM    789  O  BASP A  87      19.761  13.791   6.687  0.50 14.09           O  
ANISOU  789  O  BASP A  87     1715   1644   1991    -56     83     16       O  
ATOM    790  CB AASP A  87      20.606  14.797   9.174  0.50 13.76           C  
ANISOU  790  CB AASP A  87     1260   1820   2148   -200    139    -33       C  
ATOM    791  CB BASP A  87      20.126  15.824   8.756  0.50 15.00           C  
ANISOU  791  CB BASP A  87     1490   2071   2136   -166    131     11       C  
ATOM    792  CG AASP A  87      22.085  14.373   9.175  0.50 17.26           C  
ANISOU  792  CG AASP A  87     1774   2186   2597    -29   -140   -100       C  
ATOM    793  CG BASP A  87      21.650  15.690   8.877  0.50 19.14           C  
ANISOU  793  CG BASP A  87     1943   2604   2723   -188     47   -118       C  
ATOM    794  OD1AASP A  87      22.835  14.798   8.285  0.50 21.11           O  
ANISOU  794  OD1AASP A  87     1957   2922   3141   -295    -74    228       O  
ATOM    795  OD1BASP A  87      22.384  16.270   8.046  0.50 23.57           O  
ANISOU  795  OD1BASP A  87     2261   3417   3276   -385    170   -107       O  
ATOM    796  OD2AASP A  87      22.503  13.618  10.088  0.50 22.85           O  
ANISOU  796  OD2AASP A  87     2404   2851   3423     37   -540    213       O  
ATOM    797  OD2BASP A  87      22.121  15.008   9.807  0.50 23.64           O  
ANISOU  797  OD2BASP A  87     2580   2857   3545   -306   -513   -100       O  
ATOM    798  N  AGLY A  88      20.888  15.074   5.583  0.50 13.79           N  
ANISOU  798  N  AGLY A  88     1334   1858   2045   -171    282      4       N  
ATOM    799  N  BGLY A  88      20.748  15.281   5.309  0.50 14.15           N  
ANISOU  799  N  BGLY A  88     1475   1891   2009    -28    205    -45       N  
ATOM    800  CA AGLY A  88      20.819  14.377   4.320  0.50 14.22           C  
ANISOU  800  CA AGLY A  88     1636   1799   1966   -175    295    -22       C  
ATOM    801  CA BGLY A  88      21.167  14.225   4.421  0.50 14.56           C  
ANISOU  801  CA BGLY A  88     1671   1905   1955    -33     97    -76       C  
ATOM    802  C  AGLY A  88      19.402  14.064   3.899  0.50 13.69           C  
ANISOU  802  C  AGLY A  88     1639   1745   1817   -152    310    -21       C  
ATOM    803  C  BGLY A  88      19.997  13.304   4.094  0.50 13.92           C  
ANISOU  803  C  BGLY A  88     1506   1912   1870     59    153    -73       C  
ATOM    804  O  AGLY A  88      18.577  14.962   3.749  0.50 13.34           O  
ANISOU  804  O  AGLY A  88     1502   1692   1874   -360    382      0       O  
ATOM    805  O  BGLY A  88      20.157  12.098   4.065  0.50 13.61           O  
ANISOU  805  O  BGLY A  88     1347   1812   2009    167     43     35       O  
ATOM    806  N  AGLY A  89      19.138  12.778   3.704  0.50 12.99           N  
ANISOU  806  N  AGLY A  89     1519   1688   1729   -180    305    -83       N  
ATOM    807  N  BGLY A  89      18.815  13.854   3.837  0.50 12.94           N  
ANISOU  807  N  BGLY A  89     1515   1776   1626     68    204     -2       N  
ATOM    808  CA AGLY A  89      17.801  12.247   3.440  0.50 13.41           C  
ANISOU  808  CA AGLY A  89     1584   1792   1718   -138    245   -217       C  
ATOM    809  CA BGLY A  89      17.680  13.039   3.489  0.50 12.62           C  
ANISOU  809  CA BGLY A  89     1337   1825   1634    126    251    -88       C  
ATOM    810  C  AGLY A  89      17.054  11.798   4.680  0.50 12.30           C  
ANISOU  810  C  AGLY A  89     1339   1653   1680   -111    306   -328       C  
ATOM    811  C  BGLY A  89      16.897  12.315   4.610  0.50 12.41           C  
ANISOU  811  C  BGLY A  89     1344   1767   1603   -144    204    -56       C  
ATOM    812  O  AGLY A  89      16.122  10.984   4.603  0.50 12.67           O  
ANISOU  812  O  AGLY A  89     1652   1338   1822     34     57   -502       O  
ATOM    813  O  BGLY A  89      15.815  11.774   4.345  0.50 12.29           O  
ANISOU  813  O  BGLY A  89     1357   1695   1614    -12     90     13       O  
ATOM    814  N   VAL A  90      17.436  12.312   5.852  1.00 12.43           N  
ANISOU  814  N   VAL A  90     1236   1840   1643   -224    202   -222       N  
ATOM    815  CA  VAL A  90      16.771  11.818   7.092  1.00 11.27           C  
ANISOU  815  CA  VAL A  90     1101   1499   1681   -298    224   -230       C  
ATOM    816  C   VAL A  90      16.018  12.979   7.745  1.00  8.87           C  
ANISOU  816  C   VAL A  90      478   1472   1418   -127     14    -89       C  
ATOM    817  O   VAL A  90      16.589  14.049   7.964  1.00 10.53           O  
ANISOU  817  O   VAL A  90     1220   1271   1506   -402    224   -106       O  
ATOM    818  CB  VAL A  90      17.853  11.241   8.069  1.00 11.50           C  
ANISOU  818  CB  VAL A  90     1127   1336   1906   -163    323   -174       C  
ATOM    819  CG1 VAL A  90      17.212  10.718   9.341  1.00 14.08           C  
ANISOU  819  CG1 VAL A  90     1795   1547   2007   -184    410    -39       C  
ATOM    820  CG2 VAL A  90      18.692  10.195   7.388  1.00 14.86           C  
ANISOU  820  CG2 VAL A  90     1582   1599   2462    434    189   -256       C  
ATOM    821  N   LEU A  91      14.758  12.761   8.037  1.00  9.22           N  
ANISOU  821  N   LEU A  91      772   1336   1394    -42     29    -37       N  
ATOM    822  CA  LEU A  91      13.980  13.715   8.837  1.00  9.25           C  
ANISOU  822  CA  LEU A  91     1016   1151   1346     64    156    126       C  
ATOM    823  C   LEU A  91      14.401  13.453  10.282  1.00  9.71           C  
ANISOU  823  C   LEU A  91     1179   1310   1200    241    383    -10       C  
ATOM    824  O   LEU A  91      14.209  12.359  10.816  1.00  9.87           O  
ANISOU  824  O   LEU A  91     1394   1016   1338    109    252    148       O  
ATOM    825  CB  LEU A  91      12.490  13.527   8.649  1.00 11.51           C  
ANISOU  825  CB  LEU A  91     1268   1433   1670      8    252    266       C  
ATOM    826  CG  LEU A  91      11.905  14.123   7.397  1.00 13.13           C  
ANISOU  826  CG  LEU A  91     1654   1605   1727   -264     24     -1       C  
ATOM    827  CD1 LEU A  91      10.555  13.551   7.232  1.00 16.50           C  
ANISOU  827  CD1 LEU A  91     1753   1958   2555   -206    -37    258       C  
ATOM    828  CD2 LEU A  91      11.863  15.662   7.565  1.00 13.84           C  
ANISOU  828  CD2 LEU A  91     2125   1165   1968    412      5    149       C  
ATOM    829  N   VAL A  92      14.903  14.482  10.949  1.00  9.55           N  
ANISOU  829  N   VAL A  92     1334   1035   1257    148    188    -14       N  
ATOM    830  CA  VAL A  92      15.364  14.375  12.327  1.00  9.26           C  
ANISOU  830  CA  VAL A  92     1111   1041   1363    184    178     73       C  
ATOM    831  C   VAL A  92      14.491  15.245  13.200  1.00  9.21           C  
ANISOU  831  C   VAL A  92     1008   1109   1383    404     67    157       C  
ATOM    832  O   VAL A  92      14.436  16.465  13.013  1.00 11.21           O  
ANISOU  832  O   VAL A  92     1615   1176   1465    287    114    151       O  
ATOM    833  CB  VAL A  92      16.831  14.833  12.412  1.00 10.89           C  
ANISOU  833  CB  VAL A  92     1384   1257   1496    141    259      8       C  
ATOM    834  CG1 VAL A  92      17.353  14.745  13.848  1.00 14.02           C  
ANISOU  834  CG1 VAL A  92     1688   2028   1609    218     83    -64       C  
ATOM    835  CG2 VAL A  92      17.735  14.022  11.475  1.00 11.95           C  
ANISOU  835  CG2 VAL A  92     1146   1681   1713    183    216   -171       C  
ATOM    836  N   HIS A  93      13.784  14.608  14.114  1.00  9.02           N  
ANISOU  836  N   HIS A  93     1037   1030   1359    298    151     46       N  
ATOM    837  CA  HIS A  93      12.777  15.226  14.997  1.00  8.07           C  
ANISOU  837  CA  HIS A  93      593   1075   1396    245    149    136       C  
ATOM    838  C   HIS A  93      13.298  15.178  16.402  1.00  9.19           C  
ANISOU  838  C   HIS A  93     1110   1202   1181    244     86      6       C  
ATOM    839  O   HIS A  93      13.416  14.127  17.000  1.00 10.40           O  
ANISOU  839  O   HIS A  93     1671   1020   1259    157    -35     79       O  
ATOM    840  CB  HIS A  93      11.480  14.493  14.794  1.00  8.54           C  
ANISOU  840  CB  HIS A  93      613   1142   1487    302   -144    213       C  
ATOM    841  CG  HIS A  93      10.297  14.929  15.557  1.00  8.38           C  
ANISOU  841  CG  HIS A  93      520   1082   1578    254    249    199       C  
ATOM    842  ND1 HIS A  93       9.137  14.228  15.425  1.00 11.75           N  
ANISOU  842  ND1 HIS A  93      669   1665   2130    131    317    615       N  
ATOM    843  CD2 HIS A  93      10.087  15.908  16.479  1.00 11.66           C  
ANISOU  843  CD2 HIS A  93     1353   1263   1815    197     41    393       C  
ATOM    844  CE1 HIS A  93       8.230  14.757  16.216  1.00 13.51           C  
ANISOU  844  CE1 HIS A  93      767   2066   2299    141    343    820       C  
ATOM    845  NE2 HIS A  93       8.775  15.788  16.855  1.00 13.23           N  
ANISOU  845  NE2 HIS A  93     1264   1574   2186    467    407    898       N  
ATOM    846  N   VAL A  94      13.610  16.350  16.988  1.00  8.55           N  
ANISOU  846  N   VAL A  94      821   1134   1292    215    -36    -19       N  
ATOM    847  CA  VAL A  94      14.079  16.454  18.371  1.00  9.19           C  
ANISOU  847  CA  VAL A  94     1039    996   1455    271    162     31       C  
ATOM    848  C   VAL A  94      13.012  17.035  19.210  1.00  9.02           C  
ANISOU  848  C   VAL A  94      870   1138   1418    159     14   -174       C  
ATOM    849  O   VAL A  94      12.454  18.087  18.902  1.00 10.76           O  
ANISOU  849  O   VAL A  94     1239   1327   1523    596    148     97       O  
ATOM    850  CB  VAL A  94      15.391  17.278  18.445  1.00 10.67           C  
ANISOU  850  CB  VAL A  94     1123   1148   1780    107    147     39       C  
ATOM    851  CG1 VAL A  94      15.892  17.318  19.841  1.00 13.35           C  
ANISOU  851  CG1 VAL A  94     1497   1689   1885     57   -251    -88       C  
ATOM    852  CG2 VAL A  94      16.415  16.687  17.471  1.00 11.19           C  
ANISOU  852  CG2 VAL A  94      264   1701   2287    -49    135     31       C  
ATOM    853  N   GLN A  95      12.701  16.337  20.307  1.00  9.77           N  
ANISOU  853  N   GLN A  95     1556    882   1274    159   -115    -29       N  
ATOM    854  CA  GLN A  95      11.718  16.764  21.283  1.00 10.38           C  
ANISOU  854  CA  GLN A  95     1588    978   1377    313    -97     54       C  
ATOM    855  C   GLN A  95      12.389  17.062  22.589  1.00 10.05           C  
ANISOU  855  C   GLN A  95     1449   1019   1347    136    -31     48       C  
ATOM    856  O   GLN A  95      13.132  16.237  23.115  1.00 11.34           O  
ANISOU  856  O   GLN A  95     1629   1292   1384    211   -172    -12       O  
ATOM    857  CB  GLN A  95      10.673  15.664  21.554  1.00 10.27           C  
ANISOU  857  CB  GLN A  95     1567    976   1358    195     92     35       C  
ATOM    858  CG  GLN A  95       9.817  15.231  20.364  1.00 10.26           C  
ANISOU  858  CG  GLN A  95     1210   1283   1405    -59    105    -96       C  
ATOM    859  CD  GLN A  95       8.909  14.058  20.629  1.00  9.85           C  
ANISOU  859  CD  GLN A  95      550   1396   1794   -116     81     53       C  
ATOM    860  OE1 GLN A  95       9.179  13.234  21.515  1.00 11.78           O  
ANISOU  860  OE1 GLN A  95     1259   1397   1817    -15     40    255       O  
ATOM    861  NE2 GLN A  95       7.829  13.944  19.864  1.00 10.38           N  
ANISOU  861  NE2 GLN A  95      734   1472   1735     19     29    187       N  
ATOM    862  N   LYS A  96      12.092  18.244  23.145  1.00 11.46           N  
ANISOU  862  N   LYS A  96     1798   1177   1377    177   -196    -49       N  
ATOM    863  CA  LYS A  96      12.643  18.720  24.431  1.00 13.12           C  
ANISOU  863  CA  LYS A  96     2049   1393   1540     -5   -186    -59       C  
ATOM    864  C   LYS A  96      11.542  18.970  25.433  1.00 12.66           C  
ANISOU  864  C   LYS A  96     2217   1188   1403    138   -209    -66       C  
ATOM    865  O   LYS A  96      10.560  19.627  25.135  1.00 13.08           O  
ANISOU  865  O   LYS A  96     2204   1285   1479     88    -66    -61       O  
ATOM    866  CB  LYS A  96      13.411  20.031  24.223  1.00 14.15           C  
ANISOU  866  CB  LYS A  96     2067   1630   1680    -86   -249   -238       C  
ATOM    867  CG  LYS A  96      14.453  20.008  23.182  1.00 17.80           C  
ANISOU  867  CG  LYS A  96     2300   2217   2246     81   -253   -147       C  
ATOM    868  CD  LYS A  96      15.648  19.199  23.521  1.00 19.29           C  
ANISOU  868  CD  LYS A  96     2506   2135   2685    207     50    -46       C  
ATOM    869  CE  LYS A  96      16.863  19.453  22.623  1.00 19.90           C  
ANISOU  869  CE  LYS A  96     2129   2523   2909   -299   -120   -157       C  
ATOM    870  NZ  LYS A  96      18.046  18.643  22.945  1.00 21.99           N  
ANISOU  870  NZ  LYS A  96     2603   2059   3691   -353    -89   -109       N  
ATOM    871  N   TRP A  97      11.731  18.445  26.650  1.00 13.48           N  
ANISOU  871  N   TRP A  97     2407   1256   1456    118   -115    -96       N  
ATOM    872  CA  TRP A  97      10.747  18.665  27.728  1.00 14.51           C  
ANISOU  872  CA  TRP A  97     2415   1611   1484    294   -134   -144       C  
ATOM    873  C   TRP A  97      11.409  18.349  29.036  1.00 15.77           C  
ANISOU  873  C   TRP A  97     2664   1881   1444    360   -101    -95       C  
ATOM    874  O   TRP A  97      12.211  17.445  29.128  1.00 16.76           O  
ANISOU  874  O   TRP A  97     3045   1842   1480    537   -309   -119       O  
ATOM    875  CB  TRP A  97       9.490  17.787  27.539  1.00 14.41           C  
ANISOU  875  CB  TRP A  97     2251   1668   1556    216    151      0       C  
ATOM    876  CG  TRP A  97       9.658  16.361  27.936  1.00 14.91           C  
ANISOU  876  CG  TRP A  97     2378   1661   1626    326    283    118       C  
ATOM    877  CD1 TRP A  97       9.149  15.763  29.032  1.00 14.27           C  
ANISOU  877  CD1 TRP A  97     1553   2175   1692    473    491     32       C  
ATOM    878  CD2 TRP A  97      10.447  15.379  27.279  1.00 13.56           C  
ANISOU  878  CD2 TRP A  97     2269   1388   1493    101    285   -143       C  
ATOM    879  NE1 TRP A  97       9.519  14.465  29.093  1.00 14.22           N  
ANISOU  879  NE1 TRP A  97     2017   1617   1767    111    211     -1       N  
ATOM    880  CE2 TRP A  97      10.340  14.197  28.027  1.00 13.97           C  
ANISOU  880  CE2 TRP A  97     2183   1581   1542    -97    228    120       C  
ATOM    881  CE3 TRP A  97      11.175  15.358  26.104  1.00 13.79           C  
ANISOU  881  CE3 TRP A  97     2025   1648   1565   -198    -10    -92       C  
ATOM    882  CZ2 TRP A  97      10.994  13.013  27.657  1.00 14.22           C  
ANISOU  882  CZ2 TRP A  97     2244   1540   1617   -331    -30    177       C  
ATOM    883  CZ3 TRP A  97      11.819  14.181  25.738  1.00 11.88           C  
ANISOU  883  CZ3 TRP A  97     1598   1451   1465   -128     59    -55       C  
ATOM    884  CH2 TRP A  97      11.711  13.026  26.513  1.00 13.84           C  
ANISOU  884  CH2 TRP A  97     2059   1399   1798   -136     32   -242       C  
ATOM    885  N   ASP A  98      11.130  19.154  30.058  1.00 18.37           N  
ANISOU  885  N   ASP A  98     3341   2119   1518    353   -140   -280       N  
ATOM    886  CA  ASP A  98      11.592  18.804  31.434  1.00 20.86           C  
ANISOU  886  CA  ASP A  98     3500   2578   1846    253   -277   -344       C  
ATOM    887  C   ASP A  98      13.092  18.567  31.522  1.00 20.52           C  
ANISOU  887  C   ASP A  98     3493   2471   1832    146   -389   -437       C  
ATOM    888  O   ASP A  98      13.575  17.703  32.280  1.00 23.26           O  
ANISOU  888  O   ASP A  98     4076   2885   1875    178   -489   -393       O  
ATOM    889  CB  ASP A  98      10.840  17.563  31.896  1.00 22.87           C  
ANISOU  889  CB  ASP A  98     3734   3081   1872    203   -296   -226       C  
ATOM    890  CG  ASP A  98       9.773  17.880  32.853  1.00 30.14           C  
ANISOU  890  CG  ASP A  98     4338   4068   3044    199   -126   -350       C  
ATOM    891  OD1 ASP A  98      10.163  18.130  34.028  1.00 35.16           O  
ANISOU  891  OD1 ASP A  98     5484   5005   2869    162   -480     87       O  
ATOM    892  OD2 ASP A  98       8.581  17.863  32.429  1.00 37.63           O  
ANISOU  892  OD2 ASP A  98     4625   5616   4056     71   -429   -435       O  
ATOM    893  N   GLY A  99      13.864  19.313  30.746  1.00 19.97           N  
ANISOU  893  N   GLY A  99     3303   2411   1873     80   -481   -622       N  
ATOM    894  CA  GLY A  99      15.292  19.082  30.701  1.00 20.72           C  
ANISOU  894  CA  GLY A  99     3219   2502   2152     -3   -488   -454       C  
ATOM    895  C   GLY A  99      15.788  17.825  30.024  1.00 20.14           C  
ANISOU  895  C   GLY A  99     3053   2422   2175     28   -518   -419       C  
ATOM    896  O   GLY A  99      16.987  17.581  30.013  1.00 22.96           O  
ANISOU  896  O   GLY A  99     3307   2727   2690     17   -843   -508       O  
ATOM    897  N   LYS A 100      14.884  17.072  29.389  1.00 17.66           N  
ANISOU  897  N   LYS A 100     2776   2173   1758     32   -614   -371       N  
ATOM    898  CA  LYS A 100      15.160  15.808  28.680  1.00 16.27           C  
ANISOU  898  CA  LYS A 100     2548   1988   1646    172   -538   -159       C  
ATOM    899  C   LYS A 100      15.085  16.056  27.175  1.00 14.11           C  
ANISOU  899  C   LYS A 100     2246   1645   1469     58   -551    -46       C  
ATOM    900  O   LYS A 100      14.541  17.059  26.737  1.00 13.56           O  
ANISOU  900  O   LYS A 100     2058   1439   1653     89   -482   -158       O  
ATOM    901  CB  LYS A 100      14.104  14.774  29.083  1.00 16.38           C  
ANISOU  901  CB  LYS A 100     2715   1871   1636    271   -501     11       C  
ATOM    902  CG  LYS A 100      14.098  14.453  30.591  1.00 21.53           C  
ANISOU  902  CG  LYS A 100     3393   2720   2066     63   -338    -59       C  
ATOM    903  CD  LYS A 100      12.903  13.570  30.959  1.00 24.79           C  
ANISOU  903  CD  LYS A 100     3586   3220   2610     43    103    184       C  
ATOM    904  CE  LYS A 100      12.641  13.444  32.459  1.00 28.25           C  
ANISOU  904  CE  LYS A 100     4106   3730   2896     43     72     75       C  
ATOM    905  NZ  LYS A 100      11.237  13.007  32.696  1.00 34.69           N  
ANISOU  905  NZ  LYS A 100     4885   4717   3578   -267    380    470       N  
ATOM    906  N   SER A 101      15.611  15.119  26.402  1.00 13.56           N  
ANISOU  906  N   SER A 101     2244   1480   1428    190   -467    -75       N  
ATOM    907  CA  SER A 101      15.546  15.217  24.948  1.00 13.73           C  
ANISOU  907  CA  SER A 101     2149   1459   1605     39   -321    -19       C  
ATOM    908  C   SER A 101      15.461  13.818  24.374  1.00 11.67           C  
ANISOU  908  C   SER A 101     1705   1272   1457    113   -186     38       C  
ATOM    909  O   SER A 101      16.096  12.920  24.864  1.00 13.04           O  
ANISOU  909  O   SER A 101     2002   1204   1745    118   -606     30       O  
ATOM    910  CB  SER A 101      16.831  15.893  24.452  1.00 15.77           C  
ANISOU  910  CB  SER A 101     2363   1686   1940   -102   -235     19       C  
ATOM    911  OG  SER A 101      16.902  16.052  23.072  1.00 17.66           O  
ANISOU  911  OG  SER A 101     2505   1974   2228   -458   -259     49       O  
ATOM    912  N   THR A 102      14.705  13.662  23.294  1.00 10.41           N  
ANISOU  912  N   THR A 102     1504   1151   1297     55   -245     14       N  
ATOM    913  CA  THR A 102      14.654  12.423  22.527  1.00  9.08           C  
ANISOU  913  CA  THR A 102      984   1060   1404    319    -13    -47       C  
ATOM    914  C   THR A 102      14.639  12.802  21.051  1.00  9.78           C  
ANISOU  914  C   THR A 102     1357   1135   1224    134    -76     44       C  
ATOM    915  O   THR A 102      14.140  13.869  20.685  1.00 10.72           O  
ANISOU  915  O   THR A 102     1523   1101   1447    202    -17     71       O  
ATOM    916  CB  THR A 102      13.417  11.590  22.919  1.00 10.49           C  
ANISOU  916  CB  THR A 102     1357   1289   1339   -282     -5   -123       C  
ATOM    917  OG1 THR A 102      13.512  10.288  22.301  1.00 11.22           O  
ANISOU  917  OG1 THR A 102     1426   1037   1800    -24     -2   -107       O  
ATOM    918  CG2 THR A 102      12.057  12.231  22.567  1.00 10.16           C  
ANISOU  918  CG2 THR A 102      649   1366   1845    -46   -153    -19       C  
ATOM    919  N   THR A 103      15.175  11.902  20.226  1.00  9.77           N  
ANISOU  919  N   THR A 103     1442    944   1325    294   -173     54       N  
ATOM    920  CA  THR A 103      15.286  12.140  18.799  1.00 10.26           C  
ANISOU  920  CA  THR A 103     1346   1060   1491    282   -163     21       C  
ATOM    921  C   THR A 103      14.608  10.970  18.059  1.00 10.20           C  
ANISOU  921  C   THR A 103     1380   1126   1370    356    -78    -13       C  
ATOM    922  O   THR A 103      14.892   9.806  18.345  1.00 12.30           O  
ANISOU  922  O   THR A 103     2180   1035   1455    323   -304    116       O  
ATOM    923  CB  THR A 103      16.765  12.284  18.369  1.00 11.57           C  
ANISOU  923  CB  THR A 103     1228   1467   1699    259    -69    115       C  
ATOM    924  OG1 THR A 103      17.339  13.405  19.047  1.00 15.15           O  
ANISOU  924  OG1 THR A 103     1709   1876   2169    -15   -197      5       O  
ATOM    925  CG2 THR A 103      16.856  12.527  16.885  1.00 13.08           C  
ANISOU  925  CG2 THR A 103     1161   1914   1893     28     60    -29       C  
ATOM    926  N   ILE A 104      13.754  11.333  17.117  1.00  9.52           N  
ANISOU  926  N   ILE A 104     1478    877   1262    247   -182     52       N  
ATOM    927  CA  ILE A 104      13.072  10.417  16.220  1.00 10.89           C  
ANISOU  927  CA  ILE A 104     1758   1029   1351    165    -51     45       C  
ATOM    928  C   ILE A 104      13.578  10.708  14.832  1.00  9.97           C  
ANISOU  928  C   ILE A 104     1670   1014   1104    144     25    -29       C  
ATOM    929  O   ILE A 104      13.448  11.829  14.349  1.00  9.87           O  
ANISOU  929  O   ILE A 104     1538    965   1246    343    100     73       O  
ATOM    930  CB  ILE A 104      11.537  10.617  16.306  1.00 11.48           C  
ANISOU  930  CB  ILE A 104     1800   1252   1308      5    167    104       C  
ATOM    931  CG1 ILE A 104      11.037  10.328  17.731  1.00 11.24           C  
ANISOU  931  CG1 ILE A 104     1278   1457   1533    -87    -18    -21       C  
ATOM    932  CG2 ILE A 104      10.860   9.681  15.308  1.00 12.78           C  
ANISOU  932  CG2 ILE A 104     1770   1533   1551   -115    -83   -133       C  
ATOM    933  CD1 ILE A 104       9.621  10.774  17.930  1.00 16.03           C  
ANISOU  933  CD1 ILE A 104     1384   2575   2129     42   -107    -17       C  
ATOM    934  N   LYS A 105      14.149   9.714  14.178  1.00  9.37           N  
ANISOU  934  N   LYS A 105     1309    936   1315     43     93     18       N  
ATOM    935  CA  LYS A 105      14.609   9.804  12.815  1.00  9.66           C  
ANISOU  935  CA  LYS A 105     1331   1063   1275     97     93     20       C  
ATOM    936  C   LYS A 105      13.763   9.001  11.897  1.00  9.35           C  
ANISOU  936  C   LYS A 105     1246   1025   1280    185     -1    -52       C  
ATOM    937  O   LYS A 105      13.343   7.888  12.257  1.00 11.11           O  
ANISOU  937  O   LYS A 105     1757   1084   1378     31   -117     82       O  
ATOM    938  CB  LYS A 105      16.066   9.306  12.726  1.00 10.55           C  
ANISOU  938  CB  LYS A 105     1236   1406   1365    -36    200    -98       C  
ATOM    939  CG  LYS A 105      17.084  10.219  13.470  1.00 14.19           C  
ANISOU  939  CG  LYS A 105     1422   1949   2020     27   -331   -179       C  
ATOM    940  CD  LYS A 105      18.531   9.781  13.314  1.00 18.35           C  
ANISOU  940  CD  LYS A 105     1065   3113   2792   -228   -350   -164       C  
ATOM    941  CE  LYS A 105      19.472  10.821  14.027  1.00 20.88           C  
ANISOU  941  CE  LYS A 105     1401   3080   3450   -387    -30   -131       C  
ATOM    942  NZ  LYS A 105      20.941  10.563  13.931  1.00 25.97           N  
ANISOU  942  NZ  LYS A 105     2190   3268   4408   -170   -110   -317       N  
ATOM    943  N   ARG A 106      13.418   9.547  10.732  1.00  9.33           N  
ANISOU  943  N   ARG A 106     1328    909   1305     48     13    -26       N  
ATOM    944  CA  ARG A 106      12.612   8.870   9.747  1.00  9.43           C  
ANISOU  944  CA  ARG A 106     1174   1119   1288   -155    111      9       C  
ATOM    945  C   ARG A 106      13.461   8.858   8.458  1.00  9.69           C  
ANISOU  945  C   ARG A 106     1199   1248   1234    -75     35    -14       C  
ATOM    946  O   ARG A 106      13.914   9.894   7.999  1.00 10.33           O  
ANISOU  946  O   ARG A 106     1401   1220   1303    -97     12     14       O  
ATOM    947  CB  ARG A 106      11.286   9.628   9.540  1.00  9.59           C  
ANISOU  947  CB  ARG A 106      719   1218   1706   -173     21     41       C  
ATOM    948  CG  ARG A 106      10.381   9.595  10.802  1.00 11.84           C  
ANISOU  948  CG  ARG A 106     1406   1310   1783   -274    283    150       C  
ATOM    949  CD  ARG A 106       9.154  10.542  10.629  1.00 14.84           C  
ANISOU  949  CD  ARG A 106     1245   2067   2325   -263    457     34       C  
ATOM    950  NE  ARG A 106       8.127  10.473  11.714  1.00 17.76           N  
ANISOU  950  NE  ARG A 106     1647   2203   2897    -51    734    249       N  
ATOM    951  CZ  ARG A 106       8.139  11.262  12.788  1.00 16.06           C  
ANISOU  951  CZ  ARG A 106      998   2541   2562    446    264    531       C  
ATOM    952  NH1 ARG A 106       9.126  12.113  13.027  1.00 15.51           N  
ANISOU  952  NH1 ARG A 106     1221   2559   2110    601    252    428       N  
ATOM    953  NH2 ARG A 106       7.183  11.130  13.689  1.00 20.48           N  
ANISOU  953  NH2 ARG A 106     2359   3038   2385    -50   1002     77       N  
ATOM    954  N   LYS A 107      13.592   7.679   7.846  1.00  9.84           N  
ANISOU  954  N   LYS A 107     1311   1232   1195   -197     58    -34       N  
ATOM    955  CA  LYS A 107      14.414   7.504   6.664  1.00 11.43           C  
ANISOU  955  CA  LYS A 107     1672   1381   1290    -76    -11    -74       C  
ATOM    956  C   LYS A 107      13.790   6.472   5.720  1.00 12.09           C  
ANISOU  956  C   LYS A 107     1716   1503   1372   -338     63    -37       C  
ATOM    957  O   LYS A 107      13.271   5.454   6.151  1.00 12.79           O  
ANISOU  957  O   LYS A 107     1973   1549   1336   -484     22    -10       O  
ATOM    958  CB  LYS A 107      15.800   7.011   7.071  1.00 13.51           C  
ANISOU  958  CB  LYS A 107     1761   1938   1433      1    103   -242       C  
ATOM    959  CG  LYS A 107      16.870   7.105   5.956  1.00 16.52           C  
ANISOU  959  CG  LYS A 107     1969   2107   2201    -73      3   -146       C  
ATOM    960  CD  LYS A 107      18.247   6.659   6.387  1.00 18.80           C  
ANISOU  960  CD  LYS A 107     1799   2759   2584    259     89   -300       C  
ATOM    961  CE  LYS A 107      19.322   7.172   5.392  1.00 22.67           C  
ANISOU  961  CE  LYS A 107     2209   3404   2999     20    545   -597       C  
ATOM    962  NZ  LYS A 107      20.665   6.704   5.708  1.00 28.61           N  
ANISOU  962  NZ  LYS A 107     2493   4495   3882    -66    574   -402       N  
ATOM    963  N   ARG A 108      13.897   6.726   4.424  1.00 10.97           N  
ANISOU  963  N   ARG A 108     1451   1368   1347    -36     32     -5       N  
ATOM    964  CA  ARG A 108      13.480   5.742   3.446  1.00 10.43           C  
ANISOU  964  CA  ARG A 108     1081   1421   1460    -92     62     14       C  
ATOM    965  C   ARG A 108      14.592   4.695   3.285  1.00 10.69           C  
ANISOU  965  C   ARG A 108      936   1568   1557   -117    -35   -204       C  
ATOM    966  O   ARG A 108      15.748   5.037   3.084  1.00 12.95           O  
ANISOU  966  O   ARG A 108     1187   1656   2076    -32    235   -481       O  
ATOM    967  CB  ARG A 108      13.180   6.421   2.105  1.00 11.35           C  
ANISOU  967  CB  ARG A 108      866   1788   1656   -400    127     48       C  
ATOM    968  CG  ARG A 108      11.835   7.076   2.086  1.00 13.56           C  
ANISOU  968  CG  ARG A 108     1345   2077   1727   -167    -15    364       C  
ATOM    969  CD  ARG A 108      10.600   6.132   2.156  1.00 15.61           C  
ANISOU  969  CD  ARG A 108     1017   2721   2193   -240    217    424       C  
ATOM    970  NE  ARG A 108      10.718   5.044   1.158  1.00 17.96           N  
ANISOU  970  NE  ARG A 108     1463   2467   2892   -305   -149    402       N  
ATOM    971  CZ  ARG A 108      10.470   5.179  -0.138  1.00 17.53           C  
ANISOU  971  CZ  ARG A 108     1805   1985   2870   -330   -169    136       C  
ATOM    972  NH1 ARG A 108       9.914   6.276  -0.607  1.00 16.98           N  
ANISOU  972  NH1 ARG A 108     1951   2213   2284    -37   -162    274       N  
ATOM    973  NH2 ARG A 108      10.680   4.183  -0.979  1.00 21.52           N  
ANISOU  973  NH2 ARG A 108     2014   3001   3161    297   -233    -99       N  
ATOM    974  N   GLU A 109      14.195   3.435   3.295  1.00 11.35           N  
ANISOU  974  N   GLU A 109     1410   1374   1526    -38    156   -211       N  
ATOM    975  CA  GLU A 109      15.095   2.313   3.064  1.00 12.30           C  
ANISOU  975  CA  GLU A 109     1394   1642   1637    154     54   -213       C  
ATOM    976  C   GLU A 109      14.349   1.353   2.213  1.00 10.88           C  
ANISOU  976  C   GLU A 109     1072   1439   1623     68    136    -60       C  
ATOM    977  O   GLU A 109      13.374   0.781   2.658  1.00 11.24           O  
ANISOU  977  O   GLU A 109     1107   1573   1589   -194    175    -73       O  
ATOM    978  CB  GLU A 109      15.454   1.610   4.382  1.00 15.35           C  
ANISOU  978  CB  GLU A 109     2006   1866   1959    262     -8   -205       C  
ATOM    979  CG  GLU A 109      16.132   2.475   5.396  1.00 20.36           C  
ANISOU  979  CG  GLU A 109     2986   2507   2241    226   -304   -145       C  
ATOM    980  CD  GLU A 109      17.554   2.702   5.075  1.00 24.23           C  
ANISOU  980  CD  GLU A 109     3309   3117   2777    -34   -151   -467       C  
ATOM    981  OE1 GLU A 109      18.226   3.427   5.846  1.00 29.11           O  
ANISOU  981  OE1 GLU A 109     3589   3677   3794   -111   -772   -799       O  
ATOM    982  OE2 GLU A 109      18.033   2.143   4.054  1.00 30.27           O  
ANISOU  982  OE2 GLU A 109     3778   4117   3604    180     77  -1013       O  
ATOM    983  N   ASP A 110      14.775   1.134   0.982  1.00 11.40           N  
ANISOU  983  N   ASP A 110     1261   1686   1384    -21    112    -77       N  
ATOM    984  CA  ASP A 110      14.025   0.333   0.031  1.00 11.85           C  
ANISOU  984  CA  ASP A 110     1421   1619   1460   -109    244     32       C  
ATOM    985  C   ASP A 110      12.626   0.901  -0.053  1.00 10.96           C  
ANISOU  985  C   ASP A 110     1038   1754   1371   -151     18   -160       C  
ATOM    986  O   ASP A 110      12.458   2.103  -0.161  1.00 11.98           O  
ANISOU  986  O   ASP A 110     1327   1674   1548     -7    183   -137       O  
ATOM    987  CB  ASP A 110      14.156  -1.174   0.348  1.00 12.66           C  
ANISOU  987  CB  ASP A 110     1668   1552   1589    -35    222    -89       C  
ATOM    988  CG  ASP A 110      15.592  -1.666   0.282  1.00 16.74           C  
ANISOU  988  CG  ASP A 110     2095   2330   1934    214    343    239       C  
ATOM    989  OD1 ASP A 110      16.344  -1.172  -0.571  1.00 17.69           O  
ANISOU  989  OD1 ASP A 110     2001   2166   2552    568    589    157       O  
ATOM    990  OD2 ASP A 110      15.955  -2.535   1.102  1.00 21.71           O  
ANISOU  990  OD2 ASP A 110     2465   2923   2858    623    402    660       O  
ATOM    991  N   ASP A 111      11.568   0.078  -0.025  1.00 11.42           N  
ANISOU  991  N   ASP A 111     1132   1819   1386    -20    -87   -204       N  
ATOM    992  CA  ASP A 111      10.201   0.540  -0.089  1.00 11.18           C  
ANISOU  992  CA  ASP A 111      988   1769   1489   -176      3   -192       C  
ATOM    993  C   ASP A 111       9.594   0.868   1.281  1.00 10.94           C  
ANISOU  993  C   ASP A 111      729   1736   1688    -52     12   -304       C  
ATOM    994  O   ASP A 111       8.428   1.169   1.359  1.00 13.22           O  
ANISOU  994  O   ASP A 111      920   2323   1779    188   -118   -635       O  
ATOM    995  CB  ASP A 111       9.300  -0.489  -0.817  1.00 11.88           C  
ANISOU  995  CB  ASP A 111     1212   1884   1418   -184     -1   -212       C  
ATOM    996  CG  ASP A 111       9.634  -0.584  -2.283  1.00 13.73           C  
ANISOU  996  CG  ASP A 111     1766   1775   1674     72    143    -99       C  
ATOM    997  OD1 ASP A 111       9.849   0.478  -2.893  1.00 15.76           O  
ANISOU  997  OD1 ASP A 111     2381   2041   1565   -426     50   -168       O  
ATOM    998  OD2 ASP A 111       9.692  -1.705  -2.816  1.00 16.46           O  
ANISOU  998  OD2 ASP A 111     2623   1954   1677      6    324   -326       O  
ATOM    999  N   LYS A 112      10.457   0.874   2.318  1.00 11.69           N  
ANISOU  999  N   LYS A 112     1345   1608   1487   -127    248   -167       N  
ATOM   1000  CA ALYS A 112      10.043   1.069   3.715  0.50 11.53           C  
ANISOU 1000  CA ALYS A 112     1435   1510   1435   -187    226   -138       C  
ATOM   1001  CA BLYS A 112       9.929   1.119   3.649  0.50 11.52           C  
ANISOU 1001  CA BLYS A 112     1404   1567   1405    -92    210   -143       C  
ATOM   1002  C   LYS A 112      10.332   2.467   4.175  1.00 10.86           C  
ANISOU 1002  C   LYS A 112     1320   1458   1347    -81    142    -68       C  
ATOM   1003  O   LYS A 112      11.163   3.143   3.621  1.00 11.84           O  
ANISOU 1003  O   LYS A 112     1646   1405   1445   -191    307    -22       O  
ATOM   1004  CB ALYS A 112      10.832   0.118   4.630  0.50 11.52           C  
ANISOU 1004  CB ALYS A 112     1410   1458   1507    -96    401   -133       C  
ATOM   1005  CB BLYS A 112      10.403  -0.007   4.550  0.50 12.25           C  
ANISOU 1005  CB BLYS A 112     1565   1657   1431      9    179   -124       C  
ATOM   1006  CG ALYS A 112      10.562  -1.387   4.425  0.50 13.14           C  
ANISOU 1006  CG ALYS A 112     1723   1511   1758   -334    276   -118       C  
ATOM   1007  CG BLYS A 112      10.060  -1.380   3.995  0.50 13.58           C  
ANISOU 1007  CG BLYS A 112     1602   1859   1696      4    245   -195       C  
ATOM   1008  CD ALYS A 112       9.081  -1.741   4.359  0.50 17.07           C  
ANISOU 1008  CD ALYS A 112     2005   2266   2214   -234    214    -41       C  
ATOM   1009  CD BLYS A 112      10.460  -2.488   4.924  0.50 18.53           C  
ANISOU 1009  CD BLYS A 112     2424   2333   2282    265    145    -95       C  
ATOM   1010  CE ALYS A 112       8.892  -3.235   4.622  0.50 19.47           C  
ANISOU 1010  CE ALYS A 112     2139   2504   2752   -270    202     38       C  
ATOM   1011  CE BLYS A 112      10.170  -3.862   4.336  0.50 20.43           C  
ANISOU 1011  CE BLYS A 112     2536   2427   2799    212     19   -147       C  
ATOM   1012  NZ ALYS A 112       7.526  -3.675   4.388  0.50 20.22           N  
ANISOU 1012  NZ ALYS A 112     2215   2390   3078   -824    189     71       N  
ATOM   1013  NZ BLYS A 112      10.305  -4.937   5.373  0.50 22.95           N  
ANISOU 1013  NZ BLYS A 112     2791   2667   3260    457    -90    -46       N  
ATOM   1014  N   LEU A 113       9.619   2.854   5.218  1.00  9.26           N  
ANISOU 1014  N   LEU A 113      888   1248   1379   -182     37   -123       N  
ATOM   1015  CA ALEU A 113       9.949   4.059   5.985  0.50  9.19           C  
ANISOU 1015  CA ALEU A 113      880   1276   1334   -300    -16    -72       C  
ATOM   1016  CA BLEU A 113       9.937   4.037   5.996  0.50  9.78           C  
ANISOU 1016  CA BLEU A 113     1100   1259   1355   -308    -68    -70       C  
ATOM   1017  C   LEU A 113      10.365   3.504   7.371  1.00  9.36           C  
ANISOU 1017  C   LEU A 113     1119   1098   1336   -219    -69   -134       C  
ATOM   1018  O   LEU A 113       9.558   2.920   8.072  1.00 11.23           O  
ANISOU 1018  O   LEU A 113     1434   1386   1446   -132     79    155       O  
ATOM   1019  CB ALEU A 113       8.776   5.057   5.996  0.50 10.41           C  
ANISOU 1019  CB ALEU A 113     1156   1388   1411   -213     65   -136       C  
ATOM   1020  CB BLEU A 113       8.713   4.929   6.078  0.50 11.09           C  
ANISOU 1020  CB BLEU A 113     1379   1338   1493   -255    -49   -159       C  
ATOM   1021  CG ALEU A 113       9.031   6.495   6.481  0.50  9.35           C  
ANISOU 1021  CG ALEU A 113      319   1616   1615     62    239    -95       C  
ATOM   1022  CG BLEU A 113       8.953   6.171   6.906  0.50 12.81           C  
ANISOU 1022  CG BLEU A 113     1916   1350   1599   -159   -212    -77       C  
ATOM   1023  CD1ALEU A 113       7.856   7.376   6.119  0.50 10.07           C  
ANISOU 1023  CD1ALEU A 113      346   1593   1886   -176    290    300       C  
ATOM   1024  CD1BLEU A 113      10.220   6.936   6.328  0.50 13.95           C  
ANISOU 1024  CD1BLEU A 113     1399   1522   2378    -32   -379   -170       C  
ATOM   1025  CD2ALEU A 113       9.271   6.458   7.989  0.50 12.31           C  
ANISOU 1025  CD2ALEU A 113     1281   1645   1748    343    503    220       C  
ATOM   1026  CD2BLEU A 113       7.685   6.982   6.922  0.50 16.96           C  
ANISOU 1026  CD2BLEU A 113     2234   1855   2353   -115   -109   -394       C  
ATOM   1027  N   VAL A 114      11.631   3.731   7.722  1.00  9.00           N  
ANISOU 1027  N   VAL A 114     1020   1122   1275   -338     63      9       N  
ATOM   1028  CA  VAL A 114      12.232   3.232   8.961  1.00 10.12           C  
ANISOU 1028  CA  VAL A 114     1348   1078   1418   -140    128     99       C  
ATOM   1029  C   VAL A 114      12.292   4.389   9.929  1.00 10.02           C  
ANISOU 1029  C   VAL A 114     1256   1248   1301   -206    -11    -32       C  
ATOM   1030  O   VAL A 114      12.722   5.505   9.589  1.00 11.11           O  
ANISOU 1030  O   VAL A 114     1618   1271   1331   -344    206    -10       O  
ATOM   1031  CB  VAL A 114      13.576   2.565   8.719  1.00 10.74           C  
ANISOU 1031  CB  VAL A 114     1234   1189   1655    -76     58     26       C  
ATOM   1032  CG1 VAL A 114      14.151   2.027  10.042  1.00 13.12           C  
ANISOU 1032  CG1 VAL A 114     1540   1763   1681     33    136    113       C  
ATOM   1033  CG2 VAL A 114      13.431   1.431   7.695  1.00 13.44           C  
ANISOU 1033  CG2 VAL A 114     1840   1418   1846    321    117   -268       C  
ATOM   1034  N   VAL A 115      11.830   4.122  11.145  1.00 10.05           N  
ANISOU 1034  N   VAL A 115     1496   1001   1319   -117     53     65       N  
ATOM   1035  CA  VAL A 115      11.769   5.108  12.216  1.00  9.91           C  
ANISOU 1035  CA  VAL A 115     1286   1052   1427   -140    -56     40       C  
ATOM   1036  C   VAL A 115      12.690   4.629  13.335  1.00 10.12           C  
ANISOU 1036  C   VAL A 115     1258   1190   1397    -73   -199    201       C  
ATOM   1037  O   VAL A 115      12.542   3.530  13.846  1.00 13.28           O  
ANISOU 1037  O   VAL A 115     1812   1459   1774   -317   -326    363       O  
ATOM   1038  CB  VAL A 115      10.316   5.346  12.685  1.00 11.13           C  
ANISOU 1038  CB  VAL A 115     1346   1281   1603     27     91   -111       C  
ATOM   1039  CG1 VAL A 115      10.211   6.479  13.734  1.00 14.22           C  
ANISOU 1039  CG1 VAL A 115     1482   1951   1970   -315     94   -440       C  
ATOM   1040  CG2 VAL A 115       9.438   5.695  11.506  1.00 13.58           C  
ANISOU 1040  CG2 VAL A 115     1485   1509   2166   -148   -112     18       C  
ATOM   1041  N  AGLU A 116      13.645   5.459  13.700  0.50  9.09           N  
ANISOU 1041  N  AGLU A 116      977   1122   1353    100   -214    183       N  
ATOM   1042  N  BGLU A 116      13.619   5.466  13.748  0.50  9.98           N  
ANISOU 1042  N  BGLU A 116     1180   1208   1403    -33   -181    178       N  
ATOM   1043  CA AGLU A 116      14.565   5.202  14.815  0.50  8.94           C  
ANISOU 1043  CA AGLU A 116      848    954   1592    294   -107     85       C  
ATOM   1044  CA BGLU A 116      14.539   5.151  14.849  0.50 10.63           C  
ANISOU 1044  CA BGLU A 116     1189   1198   1651     57   -111     93       C  
ATOM   1045  C  AGLU A 116      14.167   6.201  15.918  0.50  9.28           C  
ANISOU 1045  C  AGLU A 116     1091   1102   1330    155   -154    -34       C  
ATOM   1046  C  BGLU A 116      14.364   6.159  15.950  0.50 10.02           C  
ANISOU 1046  C  BGLU A 116     1191   1205   1408     22   -197     -4       C  
ATOM   1047  O  AGLU A 116      13.976   7.388  15.667  0.50  9.49           O  
ANISOU 1047  O  AGLU A 116     1257   1002   1344    243   -245    117       O  
ATOM   1048  O  BGLU A 116      14.691   7.330  15.748  0.50  8.42           O  
ANISOU 1048  O  BGLU A 116      898    939   1360     64   -267    101       O  
ATOM   1049  CB AGLU A 116      16.020   5.321  14.372  0.50 10.70           C  
ANISOU 1049  CB AGLU A 116      900   1404   1760    217   -244     82       C  
ATOM   1050  CB BGLU A 116      15.967   5.245  14.417  0.50 12.57           C  
ANISOU 1050  CB BGLU A 116     1317   1577   1879    -45   -174    109       C  
ATOM   1051  CG AGLU A 116      17.059   4.986  15.431  0.50 11.21           C  
ANISOU 1051  CG AGLU A 116      739   1468   2051    754    -71    170       C  
ATOM   1052  CG BGLU A 116      16.569   4.042  13.908  0.50 16.34           C  
ANISOU 1052  CG BGLU A 116     1706   2085   2417     14     -5     -2       C  
ATOM   1053  CD AGLU A 116      18.467   5.601  15.167  0.50 14.00           C  
ANISOU 1053  CD AGLU A 116     1041   2145   2131    460   -216   -183       C  
ATOM   1054  CD BGLU A 116      18.066   4.111  14.055  0.50 19.18           C  
ANISOU 1054  CD BGLU A 116     1530   2645   3109    495   -157   -174       C  
ATOM   1055  OE1AGLU A 116      18.624   6.844  15.197  0.50 17.67           O  
ANISOU 1055  OE1AGLU A 116     2307   2341   2063    -19     90     51       O  
ATOM   1056  OE1BGLU A 116      18.599   5.125  14.567  0.50 20.86           O  
ANISOU 1056  OE1BGLU A 116     1387   3322   3216    756   -888   -705       O  
ATOM   1057  OE2AGLU A 116      19.433   4.837  14.957  0.50 13.83           O  
ANISOU 1057  OE2AGLU A 116      270   2128   2857    178     -3    163       O  
ATOM   1058  OE2BGLU A 116      18.710   3.146  13.682  0.50 20.25           O  
ANISOU 1058  OE2BGLU A 116      703   3414   3574   1051   -317   -253       O  
ATOM   1059  N   CYS A 117      13.918   5.683  17.105  1.00  9.72           N  
ANISOU 1059  N   CYS A 117     1326   1028   1339    211   -159     34       N  
ATOM   1060  CA  CYS A 117      13.614   6.492  18.268  1.00 10.54           C  
ANISOU 1060  CA  CYS A 117     1432   1042   1529    321   -200     51       C  
ATOM   1061  C   CYS A 117      14.704   6.259  19.277  1.00 10.71           C  
ANISOU 1061  C   CYS A 117     1429   1264   1374    130   -245     45       C  
ATOM   1062  O   CYS A 117      14.942   5.142  19.709  1.00 11.16           O  
ANISOU 1062  O   CYS A 117     1748   1027   1465     99   -306    125       O  
ATOM   1063  CB  CYS A 117      12.237   6.040  18.873  1.00 12.06           C  
ANISOU 1063  CB  CYS A 117     1412   1570   1600    337   -305     -3       C  
ATOM   1064  SG  CYS A 117      10.872   6.014  17.707  1.00 15.75           S  
ANISOU 1064  SG  CYS A 117     1737   2445   1799    386   -192    152       S  
ATOM   1065  N   VAL A 118      15.311   7.345  19.710  1.00 10.36           N  
ANISOU 1065  N   VAL A 118     1289   1096   1550    143   -165     83       N  
ATOM   1066  CA  VAL A 118      16.474   7.278  20.549  1.00 10.36           C  
ANISOU 1066  CA  VAL A 118      975   1200   1760     97   -104      4       C  
ATOM   1067  C   VAL A 118      16.280   8.127  21.813  1.00 10.98           C  
ANISOU 1067  C   VAL A 118     1327   1192   1651    154   -176     56       C  
ATOM   1068  O   VAL A 118      15.929   9.317  21.738  1.00 11.54           O  
ANISOU 1068  O   VAL A 118     1569   1151   1665    434   -183      7       O  
ATOM   1069  CB  VAL A 118      17.800   7.751  19.849  1.00 12.12           C  
ANISOU 1069  CB  VAL A 118     1082   1363   2158   -163   -175    -78       C  
ATOM   1070  CG1 VAL A 118      18.888   7.839  20.794  1.00 15.73           C  
ANISOU 1070  CG1 VAL A 118      498   2321   3158    -80   -102   -229       C  
ATOM   1071  CG2 VAL A 118      18.182   6.871  18.725  1.00 16.34           C  
ANISOU 1071  CG2 VAL A 118     1780   1894   2533    185    331   -217       C  
ATOM   1072  N   MET A 119      16.519   7.498  22.952  1.00 11.35           N  
ANISOU 1072  N   MET A 119     1552   1073   1685    159   -244     53       N  
ATOM   1073  CA AMET A 119      16.561   8.219  24.217  0.50 12.68           C  
ANISOU 1073  CA AMET A 119     1728   1391   1697    242   -338     74       C  
ATOM   1074  CA BMET A 119      16.487   8.175  24.259  0.50 12.57           C  
ANISOU 1074  CA BMET A 119     1726   1338   1710    174   -303    136       C  
ATOM   1075  C   MET A 119      17.751   7.650  24.955  1.00 13.24           C  
ANISOU 1075  C   MET A 119     1749   1512   1768    304   -341     56       C  
ATOM   1076  O   MET A 119      17.795   6.502  25.349  1.00 12.56           O  
ANISOU 1076  O   MET A 119     1496   1543   1730    514   -310    -13       O  
ATOM   1077  CB AMET A 119      15.257   8.032  24.983  0.50 12.55           C  
ANISOU 1077  CB AMET A 119     1503   1536   1728    438   -432    -76       C  
ATOM   1078  CB BMET A 119      15.172   7.788  24.995  0.50 12.40           C  
ANISOU 1078  CB BMET A 119     1443   1484   1784    265   -403     16       C  
ATOM   1079  CG AMET A 119      15.296   8.500  26.427  0.50 14.81           C  
ANISOU 1079  CG AMET A 119     1863   1925   1837    225   -384   -115       C  
ATOM   1080  CG BMET A 119      14.862   8.498  26.328  0.50 13.24           C  
ANISOU 1080  CG BMET A 119     1663   1485   1880     -5   -359    224       C  
ATOM   1081  SD AMET A 119      14.360  10.003  26.582  0.50 16.05           S  
ANISOU 1081  SD AMET A 119     2019   1741   2337    248   -128   -322       S  
ATOM   1082  SD BMET A 119      15.103  10.279  26.176  0.50 12.07           S  
ANISOU 1082  SD BMET A 119     1488   1424   1673     13     70    213       S  
ATOM   1083  CE AMET A 119      15.338  10.869  27.839  0.50 15.38           C  
ANISOU 1083  CE AMET A 119     1148   1895   2799   -547   -579   -284       C  
ATOM   1084  CE BMET A 119      14.629  10.798  27.892  0.50 12.20           C  
ANISOU 1084  CE BMET A 119     1411   1513   1710    -41   -384    151       C  
ATOM   1085  N   LYS A 120      18.737   8.516  25.088  1.00 15.78           N  
ANISOU 1085  N   LYS A 120     2146   1598   2249    259   -334    113       N  
ATOM   1086  CA  LYS A 120      19.979   8.191  25.692  1.00 18.12           C  
ANISOU 1086  CA  LYS A 120     2208   2134   2540     69   -241    109       C  
ATOM   1087  C   LYS A 120      20.554   6.986  24.930  1.00 16.34           C  
ANISOU 1087  C   LYS A 120     1776   2007   2425   -169   -382    124       C  
ATOM   1088  O   LYS A 120      20.728   7.001  23.701  1.00 18.09           O  
ANISOU 1088  O   LYS A 120     1959   2149   2764    -47   -199    326       O  
ATOM   1089  CB  LYS A 120      19.794   8.005  27.214  1.00 17.44           C  
ANISOU 1089  CB  LYS A 120     2260   1875   2491    231   -474    101       C  
ATOM   1090  CG  LYS A 120      19.443   9.318  27.926  1.00 22.82           C  
ANISOU 1090  CG  LYS A 120     3078   2606   2987    210   -148   -131       C  
ATOM   1091  CD  LYS A 120      18.593   9.124  29.160  1.00 27.51           C  
ANISOU 1091  CD  LYS A 120     3684   3412   3353    168      0   -279       C  
ATOM   1092  CE  LYS A 120      19.329   8.414  30.270  1.00 32.21           C  
ANISOU 1092  CE  LYS A 120     4257   4149   3832    214      9    -68       C  
ATOM   1093  NZ  LYS A 120      18.361   7.996  31.345  1.00 35.26           N  
ANISOU 1093  NZ  LYS A 120     4569   4932   3896    372    311   -418       N  
ATOM   1094  N   GLY A 121      20.829   5.908  25.629  1.00 14.75           N  
ANISOU 1094  N   GLY A 121     1260   1847   2496   -224   -321    195       N  
ATOM   1095  CA  GLY A 121      21.447   4.748  24.978  1.00 14.33           C  
ANISOU 1095  CA  GLY A 121     1320   1761   2363   -146   -167    195       C  
ATOM   1096  C   GLY A 121      20.447   3.761  24.475  1.00 13.23           C  
ANISOU 1096  C   GLY A 121     1352   1586   2087   -176   -250    198       C  
ATOM   1097  O   GLY A 121      20.805   2.701  24.020  1.00 13.79           O  
ANISOU 1097  O   GLY A 121     1210   1701   2326    153     29    380       O  
ATOM   1098  N   VAL A 122      19.155   4.079  24.577  1.00 12.36           N  
ANISOU 1098  N   VAL A 122     1441   1254   2000    -44   -217    235       N  
ATOM   1099  CA  VAL A 122      18.103   3.166  24.134  1.00 10.74           C  
ANISOU 1099  CA  VAL A 122     1053   1200   1828    224   -143    168       C  
ATOM   1100  C   VAL A 122      17.555   3.578  22.803  1.00 12.28           C  
ANISOU 1100  C   VAL A 122     1515   1407   1742    239   -247    223       C  
ATOM   1101  O   VAL A 122      17.098   4.721  22.627  1.00 13.43           O  
ANISOU 1101  O   VAL A 122     2067   1216   1819    537   -501     90       O  
ATOM   1102  CB  VAL A 122      16.988   3.053  25.163  1.00 11.46           C  
ANISOU 1102  CB  VAL A 122     1023   1382   1948    238    -17    154       C  
ATOM   1103  CG1 VAL A 122      15.870   2.112  24.689  1.00 13.80           C  
ANISOU 1103  CG1 VAL A 122     1145   1652   2443    107     74    256       C  
ATOM   1104  CG2 VAL A 122      17.538   2.577  26.520  1.00 13.35           C  
ANISOU 1104  CG2 VAL A 122     1171   1847   2054    217     48    491       C  
ATOM   1105  N   THR A 123      17.568   2.661  21.850  1.00 11.41           N  
ANISOU 1105  N   THR A 123     1268   1189   1876    340   -196    204       N  
ATOM   1106  CA  THR A 123      17.057   2.868  20.520  1.00 12.72           C  
ANISOU 1106  CA  THR A 123     1670   1299   1864    164   -143    151       C  
ATOM   1107  C   THR A 123      15.914   1.872  20.255  1.00 11.69           C  
ANISOU 1107  C   THR A 123     1466   1130   1845    233   -432     44       C  
ATOM   1108  O   THR A 123      16.045   0.646  20.534  1.00 16.03           O  
ANISOU 1108  O   THR A 123     2086   1451   2550    240   -437    334       O  
ATOM   1109  CB  THR A 123      18.131   2.668  19.473  1.00 13.62           C  
ANISOU 1109  CB  THR A 123     1524   1649   1999    135   -125    -31       C  
ATOM   1110  OG1 THR A 123      19.202   3.535  19.781  1.00 17.23           O  
ANISOU 1110  OG1 THR A 123     1922   2062   2562   -123    136   -118       O  
ATOM   1111  CG2 THR A 123      17.623   2.925  18.046  1.00 16.59           C  
ANISOU 1111  CG2 THR A 123     2330   2053   1918    171     59    122       C  
ATOM   1112  N   SER A 124      14.871   2.326  19.640  1.00 10.48           N  
ANISOU 1112  N   SER A 124     1204   1159   1618   -132   -319    284       N  
ATOM   1113  CA  SER A 124      13.826   1.491  19.093  1.00 10.04           C  
ANISOU 1113  CA  SER A 124      987   1183   1643     53   -205    288       C  
ATOM   1114  C   SER A 124      13.687   1.727  17.616  1.00 11.10           C  
ANISOU 1114  C   SER A 124     1354   1367   1494    126   -159    242       C  
ATOM   1115  O   SER A 124      13.750   2.853  17.160  1.00 12.60           O  
ANISOU 1115  O   SER A 124     2119   1164   1503     32    -61    256       O  
ATOM   1116  CB  SER A 124      12.468   1.779  19.758  1.00 10.85           C  
ANISOU 1116  CB  SER A 124     1181   1242   1700     51   -222    197       C  
ATOM   1117  OG  SER A 124      11.375   1.187  19.103  1.00 12.01           O  
ANISOU 1117  OG  SER A 124     1259   1557   1744     30     51    121       O  
ATOM   1118  N   THR A 125      13.494   0.657  16.848  1.00  9.73           N  
ANISOU 1118  N   THR A 125     1131   1085   1478    101   -128    245       N  
ATOM   1119  CA  THR A 125      13.352   0.725  15.411  1.00 10.88           C  
ANISOU 1119  CA  THR A 125     1221   1357   1555    266     33    189       C  
ATOM   1120  C   THR A 125      11.986   0.251  15.017  1.00 10.41           C  
ANISOU 1120  C   THR A 125     1197   1353   1402    -32     35    110       C  
ATOM   1121  O   THR A 125      11.534  -0.836  15.420  1.00 11.49           O  
ANISOU 1121  O   THR A 125     1320   1367   1678   -209   -134    251       O  
ATOM   1122  CB  THR A 125      14.381  -0.168  14.704  1.00 12.04           C  
ANISOU 1122  CB  THR A 125      908   1892   1773    302     10     99       C  
ATOM   1123  OG1 THR A 125      15.670   0.297  15.063  1.00 16.37           O  
ANISOU 1123  OG1 THR A 125     1411   2266   2541    608    187      2       O  
ATOM   1124  CG2 THR A 125      14.253  -0.111  13.214  1.00 16.00           C  
ANISOU 1124  CG2 THR A 125     1524   2709   1844    410    160    -32       C  
ATOM   1125  N   ARG A 126      11.273   1.090  14.293  1.00 10.54           N  
ANISOU 1125  N   ARG A 126     1380   1271   1353   -229   -286    149       N  
ATOM   1126  CA  ARG A 126       9.942   0.792  13.839  1.00 11.41           C  
ANISOU 1126  CA  ARG A 126     1534   1426   1374   -342    -71    204       C  
ATOM   1127  C   ARG A 126       9.922   0.847  12.333  1.00 11.01           C  
ANISOU 1127  C   ARG A 126     1333   1507   1343   -304   -207    247       C  
ATOM   1128  O   ARG A 126      10.499   1.728  11.758  1.00 15.21           O  
ANISOU 1128  O   ARG A 126     2380   1916   1481   -986   -119    288       O  
ATOM   1129  CB  ARG A 126       8.963   1.747  14.458  1.00 12.45           C  
ANISOU 1129  CB  ARG A 126     1422   1869   1439   -359    -62     33       C  
ATOM   1130  CG  ARG A 126       8.781   1.420  15.960  1.00 17.05           C  
ANISOU 1130  CG  ARG A 126     2054   2525   1897    232   -285     90       C  
ATOM   1131  CD  ARG A 126       8.161   2.465  16.734  1.00 19.63           C  
ANISOU 1131  CD  ARG A 126     2340   3098   2017    225   -318     25       C  
ATOM   1132  NE  ARG A 126       6.733   2.681  16.577  1.00 20.24           N  
ANISOU 1132  NE  ARG A 126     2313   3517   1858   -201   -178   -218       N  
ATOM   1133  CZ  ARG A 126       5.746   2.055  17.220  1.00 18.10           C  
ANISOU 1133  CZ  ARG A 126     2234   3004   1639   -542   -378    -50       C  
ATOM   1134  NH1 ARG A 126       5.932   0.901  17.837  1.00 18.51           N  
ANISOU 1134  NH1 ARG A 126     2079   3258   1693     76   -363   -196       N  
ATOM   1135  NH2 ARG A 126       4.509   2.482  17.049  1.00 19.96           N  
ANISOU 1135  NH2 ARG A 126     2199   3004   2379   -600     68    118       N  
ATOM   1136  N   VAL A 127       9.227  -0.074  11.687  1.00 10.65           N  
ANISOU 1136  N   VAL A 127     1386   1359   1302   -370   -158    147       N  
ATOM   1137  CA  VAL A 127       9.316  -0.164  10.251  1.00 10.49           C  
ANISOU 1137  CA  VAL A 127     1129   1432   1422   -281   -101     -9       C  
ATOM   1138  C   VAL A 127       7.893  -0.046   9.734  1.00  9.31           C  
ANISOU 1138  C   VAL A 127     1034   1258   1245   -179    -48    -68       C  
ATOM   1139  O   VAL A 127       6.986  -0.770  10.160  1.00  9.95           O  
ANISOU 1139  O   VAL A 127      845   1469   1464   -258    -17    133       O  
ATOM   1140  CB  VAL A 127       9.875  -1.481   9.760  1.00 11.59           C  
ANISOU 1140  CB  VAL A 127     1100   1656   1648    -28      0    -43       C  
ATOM   1141  CG1 VAL A 127       9.867  -1.479   8.213  1.00 13.70           C  
ANISOU 1141  CG1 VAL A 127     1532   2086   1585    490   -106   -179       C  
ATOM   1142  CG2 VAL A 127      11.292  -1.674  10.308  1.00 13.67           C  
ANISOU 1142  CG2 VAL A 127     1140   1846   2205     23      9     69       C  
ATOM   1143  N   TYR A 128       7.693   0.931   8.816  1.00  9.25           N  
ANISOU 1143  N   TYR A 128      907   1279   1327   -225     80    110       N  
ATOM   1144  CA  TYR A 128       6.451   1.140   8.129  1.00  9.22           C  
ANISOU 1144  CA  TYR A 128      754   1275   1472   -207    -64     77       C  
ATOM   1145  C   TYR A 128       6.547   0.730   6.676  1.00  8.41           C  
ANISOU 1145  C   TYR A 128      253   1335   1606     11    -10      1       C  
ATOM   1146  O   TYR A 128       7.582   0.955   6.058  1.00 10.57           O  
ANISOU 1146  O   TYR A 128     1050   1467   1496   -341     95   -100       O  
ATOM   1147  CB  TYR A 128       6.038   2.636   8.192  1.00 10.18           C  
ANISOU 1147  CB  TYR A 128     1105   1232   1529   -104    -55    -31       C  
ATOM   1148  CG  TYR A 128       5.563   3.097   9.572  1.00  9.18           C  
ANISOU 1148  CG  TYR A 128      422   1350   1715   -319   -348     51       C  
ATOM   1149  CD1 TYR A 128       6.506   3.374  10.559  1.00 11.40           C  
ANISOU 1149  CD1 TYR A 128      441   1733   2153   -524    -40    -78       C  
ATOM   1150  CD2 TYR A 128       4.271   3.309   9.836  1.00  9.33           C  
ANISOU 1150  CD2 TYR A 128      306   1442   1796   -173   -218     85       C  
ATOM   1151  CE1 TYR A 128       6.077   3.826  11.870  1.00 13.51           C  
ANISOU 1151  CE1 TYR A 128     1473   1835   1824    -81   -228   -278       C  
ATOM   1152  CE2 TYR A 128       3.823   3.744  11.095  1.00 12.42           C  
ANISOU 1152  CE2 TYR A 128     1534   1530   1653   -180     31    -37       C  
ATOM   1153  CZ  TYR A 128       4.739   4.024  12.075  1.00 12.43           C  
ANISOU 1153  CZ  TYR A 128     1319   1728   1673   -450   -155   -145       C  
ATOM   1154  OH  TYR A 128       4.173   4.384  13.287  1.00 15.69           O  
ANISOU 1154  OH  TYR A 128     2003   2338   1618    140     57   -359       O  
ATOM   1155  N   GLU A 129       5.434   0.225   6.160  1.00  9.80           N  
ANISOU 1155  N   GLU A 129      646   1468   1607   -104    -20    -26       N  
ATOM   1156  CA AGLU A 129       5.299  -0.134   4.759  0.50 10.84           C  
ANISOU 1156  CA AGLU A 129      923   1540   1654   -123    -28   -142       C  
ATOM   1157  CA BGLU A 129       5.350  -0.027   4.721  0.50 11.54           C  
ANISOU 1157  CA BGLU A 129     1038   1618   1726    -13    -76    -91       C  
ATOM   1158  C   GLU A 129       4.203   0.735   4.152  1.00 10.91           C  
ANISOU 1158  C   GLU A 129     1147   1406   1592      1   -153   -182       C  
ATOM   1159  O   GLU A 129       3.336   1.226   4.855  1.00 10.51           O  
ANISOU 1159  O   GLU A 129     1121   1363   1508   -167    -74      2       O  
ATOM   1160  CB AGLU A 129       5.025  -1.665   4.632  0.50 10.28           C  
ANISOU 1160  CB AGLU A 129      469   1675   1762   -246    -54    -97       C  
ATOM   1161  CB BGLU A 129       5.275  -1.527   4.369  0.50 12.59           C  
ANISOU 1161  CB BGLU A 129     1100   1784   1899    143   -184    -54       C  
ATOM   1162  CG AGLU A 129       6.282  -2.526   4.906  0.50 13.56           C  
ANISOU 1162  CG AGLU A 129      995   2053   2102    206   -287   -100       C  
ATOM   1163  CG BGLU A 129       3.914  -2.167   4.386  0.50 14.68           C  
ANISOU 1163  CG BGLU A 129      605   2355   2617    487   -311    231       C  
ATOM   1164  CD AGLU A 129       5.955  -4.045   4.835  0.50 16.47           C  
ANISOU 1164  CD AGLU A 129     1270   2244   2742   -112   -295   -144       C  
ATOM   1165  CD BGLU A 129       4.068  -3.657   4.072  0.50 21.19           C  
ANISOU 1165  CD BGLU A 129     2395   2627   3028    236    -78     17       C  
ATOM   1166  OE1AGLU A 129       4.759  -4.403   4.648  0.50 19.18           O  
ANISOU 1166  OE1AGLU A 129     2187   2016   3084   -403   -369   -100       O  
ATOM   1167  OE1BGLU A 129       3.074  -4.379   4.064  0.50 23.96           O  
ANISOU 1167  OE1BGLU A 129     2766   2686   3651     45   -211     80       O  
ATOM   1168  OE2AGLU A 129       6.867  -4.863   5.025  0.50 23.44           O  
ANISOU 1168  OE2AGLU A 129     2845   2667   3393     61   -260    122       O  
ATOM   1169  OE2BGLU A 129       5.225  -4.100   3.847  0.50 24.22           O  
ANISOU 1169  OE2BGLU A 129     2957   3157   3088    374    282    -23       O  
ATOM   1170  N   ARG A 130       4.194   0.866   2.842  1.00 10.76           N  
ANISOU 1170  N   ARG A 130     1097   1483   1506    -14   -205   -221       N  
ATOM   1171  CA  ARG A 130       3.089   1.570   2.192  1.00 13.21           C  
ANISOU 1171  CA  ARG A 130     1574   1734   1710      8   -318   -156       C  
ATOM   1172  C   ARG A 130       1.766   0.891   2.475  1.00 14.34           C  
ANISOU 1172  C   ARG A 130     1607   1741   2099    -16   -399   -248       C  
ATOM   1173  O   ARG A 130       1.622  -0.358   2.410  1.00 15.66           O  
ANISOU 1173  O   ARG A 130     1869   1603   2478   -197   -544   -289       O  
ATOM   1174  CB  ARG A 130       3.303   1.582   0.701  1.00 14.70           C  
ANISOU 1174  CB  ARG A 130     1805   2082   1696     69   -411    -77       C  
ATOM   1175  CG  ARG A 130       4.465   2.316   0.277  1.00 16.88           C  
ANISOU 1175  CG  ARG A 130     2342   2219   1851     44   -135    187       C  
ATOM   1176  CD  ARG A 130       4.184   3.763   0.142  1.00 18.08           C  
ANISOU 1176  CD  ARG A 130     2013   2260   2595    237   -115     86       C  
ATOM   1177  NE  ARG A 130       5.349   4.478  -0.383  1.00 18.32           N  
ANISOU 1177  NE  ARG A 130     2384   2033   2541    -28    -33    227       N  
ATOM   1178  CZ  ARG A 130       5.411   5.790  -0.544  1.00 16.56           C  
ANISOU 1178  CZ  ARG A 130     2289   1898   2104   -169   -238    185       C  
ATOM   1179  NH1 ARG A 130       4.386   6.540  -0.286  1.00 16.38           N  
ANISOU 1179  NH1 ARG A 130     2218   1943   2063   -238   -314    136       N  
ATOM   1180  NH2 ARG A 130       6.542   6.343  -0.949  1.00 18.46           N  
ANISOU 1180  NH2 ARG A 130     2442   2149   2422   -344    127     42       N  
ATOM   1181  N   ALA A 131       0.768   1.689   2.794  1.00 15.38           N  
ANISOU 1181  N   ALA A 131     1519   1879   2444   -184   -316   -174       N  
ATOM   1182  CA  ALA A 131      -0.516   1.151   3.150  1.00 18.11           C  
ANISOU 1182  CA  ALA A 131     1716   2271   2893   -196   -288    -58       C  
ATOM   1183  C   ALA A 131      -1.245   0.582   1.912  1.00 20.22           C  
ANISOU 1183  C   ALA A 131     1855   2613   3213   -359   -421    -77       C  
ATOM   1184  O   ALA A 131      -0.903   0.943   0.800  1.00 22.45           O  
ANISOU 1184  O   ALA A 131     2227   2975   3328   -392   -800   -114       O  
ATOM   1185  CB  ALA A 131      -1.346   2.232   3.825  1.00 19.20           C  
ANISOU 1185  CB  ALA A 131     1798   2391   3104   -176    -67   -170       C  
TER    1186      ALA A 131                                                      
HETATM 1187  C1  IBP A 133       5.912   6.100  15.533  1.00 23.49           C  
ANISOU 1187  C1  IBP A 133     3022   2729   3173    919   -547   -318       C  
HETATM 1188  C2  IBP A 133       4.998   8.580  21.675  1.00 21.54           C  
ANISOU 1188  C2  IBP A 133     2827   2760   2598   -137    253    245       C  
HETATM 1189  C3  IBP A 133       4.916   7.519  22.769  1.00 24.21           C  
ANISOU 1189  C3  IBP A 133     3530   2628   3038   -210    392    479       C  
HETATM 1190  C4  IBP A 133       6.354   7.260  23.229  1.00 26.19           C  
ANISOU 1190  C4  IBP A 133     3967   2705   3277    340    435    367       C  
HETATM 1191  C5  IBP A 133       4.046   6.332  22.271  1.00 24.79           C  
ANISOU 1191  C5  IBP A 133     3087   2594   3736     34    302    596       C  
HETATM 1192  C6  IBP A 133       6.959   6.541  16.556  1.00 22.44           C  
ANISOU 1192  C6  IBP A 133     3058   2521   2946    488   -142   -584       C  
HETATM 1193  C7  IBP A 133       7.564   7.849  16.044  1.00 21.52           C  
ANISOU 1193  C7  IBP A 133     2304   2934   2937    346   -436    -34       C  
HETATM 1194  C8  IBP A 133       6.383   6.991  17.891  1.00 19.38           C  
ANISOU 1194  C8  IBP A 133     2528   2350   2484    417   -161   -421       C  
HETATM 1195  C9  IBP A 133       7.295   7.487  18.806  1.00 16.50           C  
ANISOU 1195  C9  IBP A 133     1824   1983   2461    196    158      0       C  
HETATM 1196  C10 IBP A 133       6.818   7.993  20.007  1.00 17.91           C  
ANISOU 1196  C10 IBP A 133     2511   2209   2083    412   -343     57       C  
HETATM 1197  C11 IBP A 133       5.466   7.995  20.324  1.00 18.98           C  
ANISOU 1197  C11 IBP A 133     2493   2423   2294    314   -299     15       C  
HETATM 1198  C12 IBP A 133       4.558   7.493  19.381  1.00 20.07           C  
ANISOU 1198  C12 IBP A 133     2004   2946   2675    300   -259   -279       C  
HETATM 1199  C13 IBP A 133       5.011   7.006  18.157  1.00 21.23           C  
ANISOU 1199  C13 IBP A 133     2346   3047   2674    196   -104   -483       C  
HETATM 1200  O1  IBP A 133       5.828   4.891  15.301  1.00 21.01           O  
ANISOU 1200  O1  IBP A 133     3376   2420   2183    550   -544   -155       O  
HETATM 1201  O2  IBP A 133       5.119   6.949  15.023  1.00 25.39           O  
ANISOU 1201  O2  IBP A 133     3606   2662   3379    877  -1068   -531       O  
HETATM 1202  O   HOH A 134      -3.992   6.125   7.622  1.00 34.54           O  
ANISOU 1202  O   HOH A 134     2547   3557   7018   -606    975   -361       O  
HETATM 1203  O   HOH A 135      10.423  22.071  12.751  1.00  8.95           O  
ANISOU 1203  O   HOH A 135      908   1004   1488     89    -50     45       O  
HETATM 1204  O   HOH A 136       7.234  24.913  12.333  1.00 11.14           O  
ANISOU 1204  O   HOH A 136     1125   1580   1527   -138    140   -263       O  
HETATM 1205  O   HOH A 137       4.675  24.380  13.250  1.00 10.77           O  
ANISOU 1205  O   HOH A 137      783   1463   1844    -83    -90   -327       O  
HETATM 1206  O   HOH A 138      -2.667   5.959  32.846  1.00 40.24           O  
ANISOU 1206  O   HOH A 138     6076   3644   5566   -429    936    936       O  
HETATM 1207  O   HOH A 139       1.006  20.272   5.118  1.00 13.35           O  
ANISOU 1207  O   HOH A 139     1144   1946   1981   -288   -175    382       O  
HETATM 1208  O   HOH A 140       5.443  -1.126  -1.029  1.00 65.24           O  
ANISOU 1208  O   HOH A 140     7751   8863   8173  -2620  -1448  -3171       O  
HETATM 1209  O   HOH A 141      -2.744  18.850  20.448  1.00 33.54           O  
ANISOU 1209  O   HOH A 141     2830   4986   4927   -343    583   -393       O  
HETATM 1210  O   HOH A 142       9.184  21.330   2.493  1.00 47.27           O  
ANISOU 1210  O   HOH A 142    10914   2967   4078   1331    490   -961       O  
HETATM 1211  O   HOH A 143      13.731  26.627  15.364  1.00 11.65           O  
ANISOU 1211  O   HOH A 143     1275   1298   1854   -405    -29   -169       O  
HETATM 1212  O   HOH A 144      17.988  27.310   5.841  1.00 28.11           O  
ANISOU 1212  O   HOH A 144     2846   4754   3078    166   -286   -282       O  
HETATM 1213  O   HOH A 145      11.705  12.318  12.131  1.00 11.66           O  
ANISOU 1213  O   HOH A 145     1651   1229   1547     98    234    -64       O  
HETATM 1214  O   HOH A 146       0.800   7.512  -1.831  1.00 29.47           O  
ANISOU 1214  O   HOH A 146     4281   4253   2662   -380   -951    756       O  
HETATM 1215  O   HOH A 147       8.697  -3.773   1.127  1.00 40.87           O  
ANISOU 1215  O   HOH A 147     4975   3849   6705  -1958   -893   2275       O  
HETATM 1216  O   HOH A 148       3.755  25.550  17.914  1.00 15.09           O  
ANISOU 1216  O   HOH A 148     1827   1905   2002    768   -144   -385       O  
HETATM 1217  O   HOH A 149      25.608   5.028  23.797  1.00 38.92           O  
ANISOU 1217  O   HOH A 149     5662   4388   4736  -2178   2092    277       O  
HETATM 1218  O   HOH A 150      16.255  23.270   8.777  1.00 29.96           O  
ANISOU 1218  O   HOH A 150     2388   3297   5698   -107   1403  -1337       O  
HETATM 1219  O   HOH A 151       3.956  10.317  13.579  1.00 34.56           O  
ANISOU 1219  O   HOH A 151     3502   5861   3767   -876    186   2545       O  
HETATM 1220  O   HOH A 152       8.450  21.628  26.746  1.00 46.68           O  
ANISOU 1220  O   HOH A 152     7330   4339   6066  -2734   1903  -3159       O  
HETATM 1221  O   HOH A 153      12.687  10.186  31.674  1.00 43.73           O  
ANISOU 1221  O   HOH A 153     8195   5032   3389  -2315  -1509   -667       O  
HETATM 1222  O   HOH A 154       7.294  26.307  -0.920  1.00 37.20           O  
ANISOU 1222  O   HOH A 154     4509   6540   3085  -1925   -141    684       O  
HETATM 1223  O   HOH A 155       6.366  23.729  -4.256  1.00 40.71           O  
ANISOU 1223  O   HOH A 155     4422   6942   4101    367  -1091    -95       O  
HETATM 1224  O   HOH A 156       6.542  21.629  -1.321  1.00 41.76           O  
ANISOU 1224  O   HOH A 156     9217   4045   2603   1492   1426   -257       O  
HETATM 1225  O   HOH A 157      21.528   7.690   8.286  1.00 38.94           O  
ANISOU 1225  O   HOH A 157     4359   6088   4346   1990   -584    668       O  
HETATM 1226  O   HOH A 158      -3.825  -0.547  22.306  1.00 12.31           O  
ANISOU 1226  O   HOH A 158     1231   1428   2016   -344   -261    276       O  
HETATM 1227  O   HOH A 159      -3.150  14.373  19.842  1.00 36.92           O  
ANISOU 1227  O   HOH A 159     4848   5567   3610   -940   1665   -412       O  
HETATM 1228  O   HOH A 160       9.810  23.002   5.422  1.00 14.24           O  
ANISOU 1228  O   HOH A 160     1402   2434   1574    484    -78     81       O  
HETATM 1229  O   HOH A 161       8.926   6.448  -3.435  1.00 49.79           O  
ANISOU 1229  O   HOH A 161     6084   9073   3759   1640   -648    693       O  
HETATM 1230  O   HOH A 162      -3.588   3.265  29.040  1.00 33.01           O  
ANISOU 1230  O   HOH A 162     4058   3243   5240    628  -2311  -1146       O  
HETATM 1231  O   HOH A 163      10.071  -7.071  15.724  1.00 42.92           O  
ANISOU 1231  O   HOH A 163     4620   2468   9219    113    910    938       O  
HETATM 1232  O   HOH A 164       3.311  21.412  23.987  1.00 35.39           O  
ANISOU 1232  O   HOH A 164     6924   2778   3743    752   -245   -508       O  
HETATM 1233  O   HOH A 165       3.820  16.593  -2.153  1.00 40.96           O  
ANISOU 1233  O   HOH A 165     6885   4478   4200  -3205   1228   -860       O  
HETATM 1234  O   HOH A 166      21.097   7.829  15.270  1.00 57.17           O  
ANISOU 1234  O   HOH A 166     4709   3858  13154   -204   2892   1578       O  
HETATM 1235  O   HOH A 167      15.313   8.986   3.214  1.00 18.51           O  
ANISOU 1235  O   HOH A 167     2871   1831   2331   -578    689     21       O  
HETATM 1236  O   HOH A 168      20.541   4.489  17.500  1.00 40.40           O  
ANISOU 1236  O   HOH A 168     5269   3983   6095    764   3091   1850       O  
HETATM 1237  O   HOH A 169       7.646   3.133  -0.720  1.00 27.85           O  
ANISOU 1237  O   HOH A 169     3477   3700   3402   1272   1171    686       O  
HETATM 1238  O   HOH A 170      20.844  11.472  10.863  1.00 67.95           O  
ANISOU 1238  O   HOH A 170     1301  14509  10004   1256   1482   4976       O  
HETATM 1239  O   HOH A 171       1.574   5.786   0.136  1.00 16.50           O  
ANISOU 1239  O   HOH A 171     2229   1951   2089   -275   -442   -223       O  
HETATM 1240  O   HOH A 172       8.812  10.516  21.631  1.00 14.30           O  
ANISOU 1240  O   HOH A 172     1937   1440   2057   -146    373     89       O  
HETATM 1241  O   HOH A 173       2.180   9.830  17.486  1.00 14.66           O  
ANISOU 1241  O   HOH A 173     1521   1798   2250   -129   -212   -102       O  
HETATM 1242  O   HOH A 174       8.783  -3.053  20.098  1.00 17.94           O  
ANISOU 1242  O   HOH A 174     2634   1901   2279    295   -456   -185       O  
HETATM 1243  O   HOH A 175       1.605  15.783  -0.137  1.00 19.58           O  
ANISOU 1243  O   HOH A 175     3340   2532   1564    215   -593   -280       O  
HETATM 1244  O   HOH A 176       7.141  27.732  11.818  1.00 16.84           O  
ANISOU 1244  O   HOH A 176     1089   2056   3250    226   -225   -242       O  
HETATM 1245  O   HOH A 177       4.081  27.142   2.431  1.00 18.67           O  
ANISOU 1245  O   HOH A 177     2401   1994   2696    216   -482    -22       O  
HETATM 1246  O   HOH A 178      -0.526  14.348   6.471  1.00 15.64           O  
ANISOU 1246  O   HOH A 178     1883   1844   2213    -75     48   -101       O  
HETATM 1247  O   HOH A 179      13.318  21.244  28.359  1.00 22.55           O  
ANISOU 1247  O   HOH A 179     3109   2444   3014     -1   -505   -302       O  
HETATM 1248  O   HOH A 180       1.909  12.782  14.317  1.00 18.70           O  
ANISOU 1248  O   HOH A 180     2864   2126   2114   -194    260    660       O  
HETATM 1249  O   HOH A 181      16.127  18.703  14.205  1.00 20.44           O  
ANISOU 1249  O   HOH A 181     3142   2321   2302   -489   -303    178       O  
HETATM 1250  O   HOH A 182      18.010  -3.727   1.242  1.00 58.32           O  
ANISOU 1250  O   HOH A 182     4620   9405   8131   2964    654   3028       O  
HETATM 1251  O   HOH A 183       7.466   5.197  -4.908  1.00 47.01           O  
ANISOU 1251  O   HOH A 183     3918   8777   5163  -1483  -2004    570       O  
HETATM 1252  O   HOH A 184      16.322  21.104   7.262  1.00 17.56           O  
ANISOU 1252  O   HOH A 184     2600   1348   2723   -316    332    270       O  
HETATM 1253  O   HOH A 185       7.274   3.982  35.526  1.00 39.14           O  
ANISOU 1253  O   HOH A 185     7188   4246   3435  -2687   -789     57       O  
HETATM 1254  O   HOH A 186      21.912  11.752   7.606  1.00 64.78           O  
ANISOU 1254  O   HOH A 186     3742   9358  11514    224  -2284    705       O  
HETATM 1255  O   HOH A 187       1.676  26.193   2.181  1.00 19.36           O  
ANISOU 1255  O   HOH A 187     2364   1596   3392    -75     23   -269       O  
HETATM 1256  O   HOH A 188      15.816  -5.815  18.965  1.00 74.67           O  
ANISOU 1256  O   HOH A 188     6075   1382  20912    212  -8190    663       O  
HETATM 1257  O   HOH A 189       3.351  11.444  19.520  1.00 13.84           O  
ANISOU 1257  O   HOH A 189     1215   1786   2256   -174    134    149       O  
HETATM 1258  O   HOH A 190      21.197   9.414  22.582  1.00 54.10           O  
ANISOU 1258  O   HOH A 190    10056   6567   3929  -4926  -1036   1202       O  
HETATM 1259  O   HOH A 191       8.390   2.651  -3.043  1.00 93.12           O  
ANISOU 1259  O   HOH A 191    25407   5760   4212   4036  -1569   2369       O  
HETATM 1260  O   HOH A 192      11.330  -2.802   0.844  1.00 18.62           O  
ANISOU 1260  O   HOH A 192     2864   1788   2421   -259     76    -90       O  
HETATM 1261  O   HOH A 193      20.366  10.967  20.271  1.00 37.49           O  
ANISOU 1261  O   HOH A 193     4037   3067   7138  -1184    748   -420       O  
HETATM 1262  O   HOH A 194      10.358  29.887   6.556  1.00134.64           O  
ANISOU 1262  O   HOH A 194    21199  15094  14860 -13091 -12638   7689       O  
HETATM 1263  O   HOH A 195      11.322  27.956   4.972  1.00 44.57           O  
ANISOU 1263  O   HOH A 195     7731   3425   5777   -540   3102   -134       O  
HETATM 1264  O   HOH A 196       6.323   8.596  12.540  1.00 98.13           O  
ANISOU 1264  O   HOH A 196     7637  23676   5972  -2283  -1358   5370       O  
HETATM 1265  O   HOH A 197       2.884   1.007  18.772  1.00 18.47           O  
ANISOU 1265  O   HOH A 197     1620   3421   1976   -679    161    -41       O  
HETATM 1266  O   HOH A 198      19.744  10.008  17.616  1.00 35.30           O  
ANISOU 1266  O   HOH A 198     4405   3072   5933    783      0    953       O  
HETATM 1267  O   HOH A 199      20.319   4.935  28.471  1.00 21.46           O  
ANISOU 1267  O   HOH A 199     3342   2019   2791    605   -294    250       O  
HETATM 1268  O   HOH A 200       1.973  30.486  -7.078  1.00 40.95           O  
ANISOU 1268  O   HOH A 200     7950   3982   3626  -2682    575    -25       O  
HETATM 1269  O   HOH A 201      12.184  28.507  22.429  1.00 41.70           O  
ANISOU 1269  O   HOH A 201     7549   5320   2974   -234   -841  -1434       O  
HETATM 1270  O   HOH A 202      13.177  21.556  19.833  1.00 18.21           O  
ANISOU 1270  O   HOH A 202     1625   3231   2061  -1031   -217    119       O  
HETATM 1271  O   HOH A 203      -2.830   0.787  -1.295  1.00 37.83           O  
ANISOU 1271  O   HOH A 203     3913   5224   5236     71  -2113   -572       O  
HETATM 1272  O   HOH A 204       2.819  13.910  18.424  1.00 19.48           O  
ANISOU 1272  O   HOH A 204     2852   2101   2448   -366     16     65       O  
HETATM 1273  O   HOH A 205      13.215  -3.910   2.499  1.00 52.18           O  
ANISOU 1273  O   HOH A 205     9635   4171   6019   -631  -3592   2538       O  
HETATM 1274  O   HOH A 206      13.079  -7.594  20.050  1.00 39.13           O  
ANISOU 1274  O   HOH A 206     4891   3073   6903   1227  -1503   -564       O  
HETATM 1275  O   HOH A 207      11.533  -5.809  21.050  1.00 23.95           O  
ANISOU 1275  O   HOH A 207     3955   1306   3837   -484   -136    845       O  
HETATM 1276  O   HOH A 208       6.266  -0.418   1.370  1.00 18.08           O  
ANISOU 1276  O   HOH A 208     1634   2431   2805    160    270   -350       O  
HETATM 1277  O   HOH A 209       6.179  11.389  19.548  1.00 16.45           O  
ANISOU 1277  O   HOH A 209     1203   2142   2904   -394    -27    139       O  
HETATM 1278  O   HOH A 210       2.575   6.713  13.634  1.00 20.46           O  
ANISOU 1278  O   HOH A 210     2265   2080   3428   -214    -14    -12       O  
HETATM 1279  O   HOH A 211      18.219   0.754   1.603  1.00 46.03           O  
ANISOU 1279  O   HOH A 211     3173  10820   3496  -1839    597    427       O  
HETATM 1280  O   HOH A 212       0.636  18.547  18.968  1.00 27.19           O  
ANISOU 1280  O   HOH A 212     2115   3204   5012  -1067  -1042   2086       O  
HETATM 1281  O   HOH A 213       6.067  27.560  15.398  1.00 18.23           O  
ANISOU 1281  O   HOH A 213     1920   1797   3210    401   -955   -472       O  
HETATM 1282  O   HOH A 214      11.461  -3.150  13.676  1.00 19.07           O  
ANISOU 1282  O   HOH A 214     2791   1993   2461    289     -6    -75       O  
HETATM 1283  O   HOH A 215      17.601  -1.636  20.052  1.00 22.09           O  
ANISOU 1283  O   HOH A 215     2831   2174   3385    551   -694   -205       O  
HETATM 1284  O   HOH A 216      13.993  -1.973   4.255  1.00 48.29           O  
ANISOU 1284  O   HOH A 216     7790   5213   5345  -3056    183   1591       O  
HETATM 1285  O   HOH A 217      -0.710  18.743   3.750  1.00 17.96           O  
ANISOU 1285  O   HOH A 217     2425   1742   2654   -207   -744     92       O  
HETATM 1286  O   HOH A 218      17.754  13.818  21.739  1.00 21.78           O  
ANISOU 1286  O   HOH A 218     2174   3715   2387   -584   -213   -349       O  
HETATM 1287  O   HOH A 219      14.644   1.498  29.177  1.00 18.82           O  
ANISOU 1287  O   HOH A 219     1981   2959   2208    324   -355    323       O  
HETATM 1288  O   HOH A 220       0.484   5.071  32.379  1.00 24.92           O  
ANISOU 1288  O   HOH A 220     4441   2841   2185   -269      8   -151       O  
HETATM 1289  O   HOH A 221       6.346   9.135  -1.814  1.00 21.09           O  
ANISOU 1289  O   HOH A 221     2552   2264   3194   -274    472   -471       O  
HETATM 1290  O   HOH A 222       3.588   3.666  35.764  1.00 27.42           O  
ANISOU 1290  O   HOH A 222     5413   3042   1962  -1939   -722    312       O  
HETATM 1291  O   HOH A 223      12.329 -10.063  16.818  1.00 76.29           O  
ANISOU 1291  O   HOH A 223     9617   9035  10334   2058  -3039  -4026       O  
HETATM 1292  O   HOH A 224      17.441  13.356  27.957  1.00 25.00           O  
ANISOU 1292  O   HOH A 224     2710   2959   3828    -71  -1158    864       O  
HETATM 1293  O  AHOH A 225       8.301  -3.472  22.743  0.50 18.86           O  
ANISOU 1293  O  AHOH A 225     1875   2526   2765  -1464    131   -639       O  
HETATM 1294  O  BHOH A 225       9.578  -3.670  23.125  0.50 25.79           O  
ANISOU 1294  O  BHOH A 225     4157   3213   2429  -2552    358   -425       O  
HETATM 1295  O  AHOH A 226       8.984  28.788  16.689  0.50 18.49           O  
ANISOU 1295  O  AHOH A 226     1745   1424   3854    218    360   -153       O  
HETATM 1296  O  BHOH A 226       9.569  28.810  15.333  0.50 11.64           O  
ANISOU 1296  O  BHOH A 226      436   1357   2629    -31    278    203       O  
HETATM 1297  O   HOH A 227       4.805  -1.710  25.584  1.00 24.44           O  
ANISOU 1297  O   HOH A 227     2623   3076   3585    234    535   -591       O  
HETATM 1298  O   HOH A 228       0.936  15.794  18.524  1.00 29.28           O  
ANISOU 1298  O   HOH A 228     4942   3940   2241  -1190    441    -81       O  
HETATM 1299  O   HOH A 229      18.259  11.294  24.327  1.00 29.49           O  
ANISOU 1299  O   HOH A 229     2975   1769   6460   -120  -1137    498       O  
HETATM 1300  O   HOH A 230      -1.894  15.910  17.823  1.00 27.26           O  
ANISOU 1300  O   HOH A 230     5569   2206   2582   -313   1372   -409       O  
HETATM 1301  O   HOH A 231      15.520  19.709  27.307  1.00 25.63           O  
ANISOU 1301  O   HOH A 231     4693   2352   2690   -700  -1055   -317       O  
HETATM 1302  O   HOH A 232       2.145  -3.552  24.701  1.00 21.51           O  
ANISOU 1302  O   HOH A 232     2376   2961   2835    685   -394   -650       O  
HETATM 1303  O   HOH A 233      -7.183  10.048  19.684  1.00 33.27           O  
ANISOU 1303  O   HOH A 233     2655   7094   2892    999   1020    772       O  
HETATM 1304  O   HOH A 234      11.422  -3.234  24.670  1.00 33.28           O  
ANISOU 1304  O   HOH A 234     6737   1595   4310    501   2397    510       O  
HETATM 1305  O   HOH A 235       5.131  -1.564  19.561  1.00 25.53           O  
ANISOU 1305  O   HOH A 235     1653   3277   4767   -355    644   -294       O  
HETATM 1306  O   HOH A 236      -2.257   3.886  -2.960  1.00 42.17           O  
ANISOU 1306  O   HOH A 236     7039   3903   5079    928  -1998    560       O  
HETATM 1307  O   HOH A 237      -5.246  14.054  14.828  1.00 45.50           O  
ANISOU 1307  O   HOH A 237     3967   3070  10249    402    359  -1077       O  
HETATM 1308  O   HOH A 238      15.440  26.836   5.358  1.00101.85           O  
ANISOU 1308  O   HOH A 238     8165  21803   8728   -114  -1565  -7201       O  
HETATM 1309  O   HOH A 239      18.854  17.712  14.756  1.00 36.19           O  
ANISOU 1309  O   HOH A 239     2970   4066   6715    123  -1612   -183       O  
HETATM 1310  O   HOH A 240      -2.374   4.680  -0.248  1.00 38.97           O  
ANISOU 1310  O   HOH A 240     5071   3855   5878  -1222  -1672    973       O  
HETATM 1311  O   HOH A 241      12.219  -6.532  23.435  1.00 34.99           O  
ANISOU 1311  O   HOH A 241     4163   3892   5239    -32    919  -1311       O  
HETATM 1312  O   HOH A 242      20.016  16.782  16.573  1.00 38.55           O  
ANISOU 1312  O   HOH A 242     3420   4958   6267   -820    738   2208       O  
HETATM 1313  O   HOH A 243      16.009  -3.013  -2.764  1.00 23.44           O  
ANISOU 1313  O   HOH A 243     4518   2534   1852    666    -63    276       O  
HETATM 1314  O   HOH A 244      16.093  25.760  19.903  1.00 46.78           O  
ANISOU 1314  O   HOH A 244     9479   5317   2977  -3226  -2562   1751       O  
HETATM 1315  O   HOH A 245       4.692  14.676  30.993  1.00 48.32           O  
ANISOU 1315  O   HOH A 245    12109   3934   2316  -1026    924   -427       O  
HETATM 1316  O   HOH A 246      17.397  12.417  30.185  1.00 40.43           O  
ANISOU 1316  O   HOH A 246     6023   5214   4123   1555   -757  -1307       O  
HETATM 1317  O   HOH A 247       7.336  -6.308  15.515  1.00 31.73           O  
ANISOU 1317  O   HOH A 247     5685   2508   3862  -1812  -1772   1557       O  
HETATM 1318  O   HOH A 248      -0.211  21.682  29.375  1.00 39.65           O  
ANISOU 1318  O   HOH A 248     6338   4480   4245   3169  -1866   -650       O  
HETATM 1319  O   HOH A 249      11.488  24.737   4.293  1.00 34.53           O  
ANISOU 1319  O   HOH A 249     2073   7082   3965  -1600    -79   2405       O  
HETATM 1320  O   HOH A 250      -1.856  20.273  11.551  1.00 30.53           O  
ANISOU 1320  O   HOH A 250     3182   2791   5627   -674   2070     -7       O  
HETATM 1321  O   HOH A 251      -9.417   4.066  20.751  1.00 18.52           O  
ANISOU 1321  O   HOH A 251     2695   1593   2748    500    782    153       O  
HETATM 1322  O   HOH A 252      20.837   5.062  21.561  1.00 24.38           O  
ANISOU 1322  O   HOH A 252     3748   2405   3110    913    451    372       O  
HETATM 1323  O   HOH A 253       4.790  10.136  29.453  1.00 24.62           O  
ANISOU 1323  O   HOH A 253     4677   2601   2075   -510    332    666       O  
HETATM 1324  O   HOH A 254       0.100   3.438  -0.144  1.00 23.52           O  
ANISOU 1324  O   HOH A 254     2238   2460   4235   -105  -1293   -486       O  
HETATM 1325  O   HOH A 255      17.234   8.923  16.421  1.00 26.74           O  
ANISOU 1325  O   HOH A 255     4231   2892   3035    580   -656    410       O  
HETATM 1326  O   HOH A 256       5.279  22.709  24.138  1.00 29.22           O  
ANISOU 1326  O   HOH A 256     4709   3266   3126   1529    194   -719       O  
HETATM 1327  O   HOH A 257       2.846  12.279  30.066  1.00 28.06           O  
ANISOU 1327  O   HOH A 257     4681   3386   2594    488   -109    130       O  
HETATM 1328  O   HOH A 258       8.996  12.016  30.690  1.00 25.01           O  
ANISOU 1328  O   HOH A 258     4514   2521   2466   -197   1063    363       O  
HETATM 1329  O   HOH A 259      -4.623  12.006  13.313  1.00 33.35           O  
ANISOU 1329  O   HOH A 259     2228   7652   2789   -482   -480    637       O  
HETATM 1330  O   HOH A 260       0.135   7.956  17.689  1.00 25.16           O  
ANISOU 1330  O   HOH A 260     3781   2634   3143   -357    664     57       O  
HETATM 1331  O   HOH A 261       9.252  21.217  29.718  1.00 30.11           O  
ANISOU 1331  O   HOH A 261     5350   2812   3278   1712    238   -878       O  
HETATM 1332  O   HOH A 262       3.133   8.309  30.990  1.00 23.85           O  
ANISOU 1332  O   HOH A 262     3213   2246   3601    124   1217    288       O  
HETATM 1333  O   HOH A 263       6.120  -2.059  22.807  1.00 32.16           O  
ANISOU 1333  O   HOH A 263     3324   4631   4262    248   -610     63       O  
HETATM 1334  O   HOH A 264       8.818   4.901  32.802  1.00 23.88           O  
ANISOU 1334  O   HOH A 264     2365   3110   3595   -666  -1148    544       O  
HETATM 1335  O   HOH A 265       7.084  -3.066  30.469  1.00 26.25           O  
ANISOU 1335  O   HOH A 265     5675   1930   2369   -374    499    -13       O  
HETATM 1336  O   HOH A 266      19.516  14.703  18.187  1.00 31.72           O  
ANISOU 1336  O   HOH A 266     2250   4187   5614   -215    803   1953       O  
HETATM 1337  O   HOH A 267      -1.838   7.861  -0.396  1.00 32.71           O  
ANISOU 1337  O   HOH A 267     7129   3083   2215  -1826    776   -156       O  
HETATM 1338  O   HOH A 268      10.994  22.250  26.587  1.00 29.94           O  
ANISOU 1338  O   HOH A 268     5646   3024   2705    249   -302    103       O  
HETATM 1339  O   HOH A 269       7.174  29.357  13.914  1.00 24.05           O  
ANISOU 1339  O   HOH A 269     3588   2173   3377     36   -150    193       O  
HETATM 1340  O   HOH A 270      12.795  25.544   6.189  1.00 28.88           O  
ANISOU 1340  O   HOH A 270     4717   2629   3628   1031   1592    784       O  
HETATM 1341  O   HOH A 271      10.519  -3.729  28.305  1.00 48.81           O  
ANISOU 1341  O   HOH A 271     4284   4818   9441    884   1009   5315       O  
HETATM 1342  O   HOH A 272      10.225  -5.248   9.287  1.00 36.20           O  
ANISOU 1342  O   HOH A 272     7249   2438   4065   -434   1398   -663       O  
HETATM 1343  O   HOH A 273      18.882  17.172   2.637  1.00 32.00           O  
ANISOU 1343  O   HOH A 273     4497   3929   3730    648    771   -647       O  
HETATM 1344  O   HOH A 274      18.402   4.568   2.415  1.00 24.43           O  
ANISOU 1344  O   HOH A 274     2879   4334   2067     65   -168   -418       O  
HETATM 1345  O   HOH A 275       0.744  19.538  -2.000  1.00 37.61           O  
ANISOU 1345  O   HOH A 275     5903   2937   5447   1705  -3086   -415       O  
HETATM 1346  O   HOH A 276       6.174  11.822  16.636  1.00 35.53           O  
ANISOU 1346  O   HOH A 276     2412   7990   3094  -2271    583   -299       O  
HETATM 1347  O   HOH A 277       8.035  30.717   8.506  1.00 28.04           O  
ANISOU 1347  O   HOH A 277     3209   2344   5101    385   -603    642       O  
HETATM 1348  O   HOH A 278      -3.931   1.782  15.029  1.00 26.55           O  
ANISOU 1348  O   HOH A 278     3198   2688   4202   1050   1604    342       O  
HETATM 1349  O   HOH A 279       4.400   9.395  15.920  1.00 22.84           O  
ANISOU 1349  O   HOH A 279     2744   2534   3399    -94   -223   -140       O  
HETATM 1350  O   HOH A 280       4.958  17.179  29.767  1.00 31.47           O  
ANISOU 1350  O   HOH A 280     6262   3532   2163   -466    547   -312       O  
HETATM 1351  O   HOH A 281       4.210  13.313  15.693  1.00 26.10           O  
ANISOU 1351  O   HOH A 281     4309   2965   2641    376    -24    178       O  
HETATM 1352  O   HOH A 282       0.071   5.226  18.666  1.00 34.88           O  
ANISOU 1352  O   HOH A 282     3940   3727   5585  -1545  -2195   2148       O  
HETATM 1353  O   HOH A 283      -7.686   6.574  19.109  1.00 30.84           O  
ANISOU 1353  O   HOH A 283     2881   4593   4242   1069    326   -774       O  
HETATM 1354  O   HOH A 284       5.948  29.957  10.091  1.00 27.66           O  
ANISOU 1354  O   HOH A 284     2383   3835   4289   -731    327   -897       O  
HETATM 1355  O   HOH A 285      19.427  20.386   7.524  1.00 35.54           O  
ANISOU 1355  O   HOH A 285     3679   3146   6677  -1023   2103  -2005       O  
HETATM 1356  O   HOH A 286      13.392   6.636  -1.554  1.00 24.53           O  
ANISOU 1356  O   HOH A 286     3803   3062   2455   1940     66    205       O  
HETATM 1357  O   HOH A 287      -5.099   2.361  33.319  1.00 30.83           O  
ANISOU 1357  O   HOH A 287     2808   2473   6433     17   -789   1522       O  
HETATM 1358  O   HOH A 288      15.885  26.116   8.695  1.00 26.29           O  
ANISOU 1358  O   HOH A 288     2915   3877   3196  -1531   -209   -226       O  
HETATM 1359  O   HOH A 289       1.565  25.781 -13.149  1.00 27.43           O  
ANISOU 1359  O   HOH A 289     2893   3259   4267    -17  -1218    163       O  
HETATM 1360  O   HOH A 290      -1.089  18.297   0.720  1.00 30.47           O  
ANISOU 1360  O   HOH A 290     3119   2904   5552    755  -1175    514       O  
HETATM 1361  O   HOH A 291      16.500  23.207  21.642  1.00 41.04           O  
ANISOU 1361  O   HOH A 291     3445   2523   9623   -602   2125   1994       O  
HETATM 1362  O   HOH A 292       2.432  -5.391  19.901  1.00 30.93           O  
ANISOU 1362  O   HOH A 292     3123   4561   4066    367    752   -988       O  
HETATM 1363  O   HOH A 293      -7.975   6.242  14.915  1.00 39.00           O  
ANISOU 1363  O   HOH A 293     3091   5496   6228   -217   -990   2942       O  
HETATM 1364  O   HOH A 294       5.475  16.588  -5.323  1.00 38.23           O  
ANISOU 1364  O   HOH A 294     3974   4346   6204    927  -2464  -1380       O  
HETATM 1365  O   HOH A 295      13.558  28.145   7.942  1.00 34.29           O  
ANISOU 1365  O   HOH A 295     3765   6034   3226    908   -542  -1748       O  
HETATM 1366  O   HOH A 296       2.798  -2.394  17.741  1.00 29.61           O  
ANISOU 1366  O   HOH A 296     4165   4224   2860   1925    -89    -72       O  
HETATM 1367  O   HOH A 297      18.350  11.463  21.646  1.00 46.45           O  
ANISOU 1367  O   HOH A 297     1632   9277   6739    698  -1401  -1938       O  
HETATM 1368  O   HOH A 298       8.789  -5.975  20.148  1.00 33.13           O  
ANISOU 1368  O   HOH A 298     3678   4108   4801     27    720   -595       O  
HETATM 1369  O   HOH A 299      -2.253  19.573   6.723  1.00 33.29           O  
ANISOU 1369  O   HOH A 299     3573   3578   5498    881  -1322    710       O  
HETATM 1370  O   HOH A 300      -2.782   5.917  28.952  1.00 41.08           O  
ANISOU 1370  O   HOH A 300     5103   3722   6783   -275  -1885  -1716       O  
HETATM 1371  O   HOH A 301       0.109  -2.634   9.576  1.00 34.90           O  
ANISOU 1371  O   HOH A 301     3135   4372   5752  -1624   -900   1937       O  
HETATM 1372  O   HOH A 302       3.026  -4.579  22.480  1.00 34.92           O  
ANISOU 1372  O   HOH A 302     5209   4462   3596   2654   1589   1553       O  
HETATM 1373  O   HOH A 303      12.922  12.132  -3.047  1.00 44.94           O  
ANISOU 1373  O   HOH A 303     6638   4310   6125  -2010   2374   -176       O  
HETATM 1374  O   HOH A 304      -2.062   9.409  26.363  1.00 43.71           O  
ANISOU 1374  O   HOH A 304     4987   5535   6083  -1083   3226   -462       O  
HETATM 1375  O   HOH A 305       2.894  -2.373   1.131  1.00 35.03           O  
ANISOU 1375  O   HOH A 305     5263   3156   4890    184   -181  -1823       O  
CONECT 1187 1192 1200 1201                                                      
CONECT 1188 1189 1197                                                           
CONECT 1189 1188 1190 1191                                                      
CONECT 1190 1189                                                                
CONECT 1191 1189                                                                
CONECT 1192 1187 1193 1194                                                      
CONECT 1193 1192                                                                
CONECT 1194 1192 1195 1199                                                      
CONECT 1195 1194 1196                                                           
CONECT 1196 1195 1197                                                           
CONECT 1197 1188 1196 1198                                                      
CONECT 1198 1197 1199                                                           
CONECT 1199 1194 1198                                                           
CONECT 1200 1187                                                                
CONECT 1201 1187                                                                
MASTER      319    0    1    3   10    0    2    6 1259    1   15   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.