CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***  Practical_lesson_jeandi  ***

elNémo ID: 22012513052293587

Job options:

ID        	=	 22012513052293587
JOBID     	=	 Practical_lesson_jeandi
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 Practical_lesson_jeandi

HEADER    LIPID BINDING PROTEIN                   11-OCT-10   3P6G              
TITLE     HUMAN ADIPOCYTE LIPID-BINDING PROTEIN FABP4 IN COMPLEX WITH (R)-      
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, LIPID BINDING     
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.GONZALEZ,E.POZHARSKI                                              
REVDAT   3   25-FEB-15 3P6G    1       JRNL                                     
REVDAT   2   11-FEB-15 3P6G    1       JRNL                                     
REVDAT   1   13-APR-11 3P6G    0                                                
JRNL        AUTH   J.M.GONZALEZ,S.Z.FISHER                                      
JRNL        TITL   STRUCTURAL ANALYSIS OF IBUPROFEN BINDING TO HUMAN ADIPOCYTE  
JRNL        TITL 2 FATTY-ACID BINDING PROTEIN (FABP4).                          
JRNL        REF    ACTA CRYSTALLOGR F STRUCT     V.  71   163 2015              
JRNL        REF  2 BIOL COMMUN                                                  
JRNL        REFN                                                                
JRNL        PMID   25664790                                                     
JRNL        DOI    10.1107/S2053230X14027897                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.56                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 40749                          
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) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.194                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2040                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.23                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2806                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.00                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 140                          
REMARK   3   BIN FREE R VALUE                    : 0.2400                       
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            : 200                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.96000                                              
REMARK   3    B22 (A**2) : -0.90000                                             
REMARK   3    B33 (A**2) : -3.06000                                             
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): 0.040         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.049         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.958                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1260 ; 0.022 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):   861 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1711 ; 2.021 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2114 ; 1.004 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   171 ; 6.579 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    52 ;33.019 ;25.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   246 ;14.293 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;17.743 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   193 ; 0.128 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1445 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   248 ; 0.003 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   788 ; 2.028 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   327 ; 0.858 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1289 ; 3.070 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   472 ; 4.313 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   418 ; 6.147 ; 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):  2121 ; 1.846 ; 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 3P6G 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 RCSB062015.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57520                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.060                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.11500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.1000                            
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) : 1.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 82.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.19                                     
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       16.14500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.46500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.77300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.46500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.14500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.77300            
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   O    HOH A   176     O    HOH A   216              1.85            
REMARK 500   OE2  GLU A    14     O    HOH A   163              1.85            
REMARK 500   OE2  GLU A   116     O    HOH A   134              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD2  ASP A    71     O    HOH A   201     3555     1.58            
REMARK 500   ND2  ASN A    15     O    HOH A   252     3645     1.72            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  14   CB    GLU A  14   CG      0.120                       
REMARK 500    GLU A  14   CG    GLU A  14   CD      0.100                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  77       32.45     71.45                                   
REMARK 500    ASP A 110     -133.52     53.61                                   
REMARK 500    LYS A 120     -119.84     53.81                                   
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 202        DISTANCE =  5.45 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IZP 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: 3P6H   RELATED DB: PDB                                   
DBREF  3P6G A    0   131  UNP    P15090   FABP4_HUMAN      1    132             
SEQADV 3P6G GLN A   -7  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6G GLN A   -6  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6G MET A   -5  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6G GLY A   -4  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6G ARG A   -3  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6G GLY A   -2  UNP  P15090              EXPRESSION TAG                 
SEQADV 3P6G 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    IZP  A 133      15                                                       
HETNAM     IZP (2R)-2-[4-(2-METHYLPROPYL)PHENYL]PROPANOIC ACID                  
HETSYN     IZP (R)-IBUPROFEN                                                    
FORMUL   2  IZP    C13 H18 O2                                                   
FORMUL   3  HOH   *200(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  7 ARG A  78  ILE A 104  ARG A 126  TYR A 128                    
SITE     2 AC1  7 HOH A 145  HOH A 309  HOH A 325                               
CRYST1   32.290   53.546   74.930  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      0.030969  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018676  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013346        0.00000                         
ATOM      1  N   GLN A  -7      -2.320  31.334  -8.596  1.00 33.12           N  
ANISOU    1  N   GLN A  -7     4004   4238   4340    178   -238    -21       N  
ATOM      2  CA  GLN A  -7      -1.477  30.163  -8.199  1.00 31.68           C  
ANISOU    2  CA  GLN A  -7     3696   4132   4208    160   -217    -70       C  
ATOM      3  C   GLN A  -7      -0.795  29.492  -9.403  1.00 30.61           C  
ANISOU    3  C   GLN A  -7     3452   4079   4098    169   -263    -85       C  
ATOM      4  O   GLN A  -7      -1.333  29.450 -10.505  1.00 32.76           O  
ANISOU    4  O   GLN A  -7     3783   4420   4241     24   -221   -180       O  
ATOM      5  CB  GLN A  -7      -2.311  29.147  -7.422  1.00 32.16           C  
ANISOU    5  CB  GLN A  -7     3774   4132   4311    174   -324    -44       C  
ATOM      6  N   GLN A  -6       0.420  28.996  -9.190  1.00 28.60           N  
ANISOU    6  N   GLN A  -6     3070   3838   3956     80   -261   -121       N  
ATOM      7  CA  GLN A  -6       1.078  28.119 -10.160  1.00 25.63           C  
ANISOU    7  CA  GLN A  -6     2407   3537   3791     59   -246    -26       C  
ATOM      8  C   GLN A  -6       1.368  26.819  -9.442  1.00 23.08           C  
ANISOU    8  C   GLN A  -6     1879   3297   3593     58   -216    -31       C  
ATOM      9  O   GLN A  -6       1.371  26.777  -8.203  1.00 24.90           O  
ANISOU    9  O   GLN A  -6     2097   3484   3877     79   -140    -71       O  
ATOM     10  CB  GLN A  -6       2.385  28.731 -10.713  1.00 27.16           C  
ANISOU   10  CB  GLN A  -6     2719   3662   3935     32    -71     43       C  
ATOM     11  N   MET A  -5       1.562  25.765 -10.234  1.00 20.39           N  
ANISOU   11  N   MET A  -5     1361   3026   3357     33   -262     33       N  
ATOM     12  CA AMET A  -5       1.926  24.484  -9.637  0.50 19.16           C  
ANISOU   12  CA AMET A  -5     1236   2872   3172     82    -68     33       C  
ATOM     13  CA BMET A  -5       1.982  24.430  -9.815  0.50 20.95           C  
ANISOU   13  CA BMET A  -5     1594   3013   3350     68   -120     59       C  
ATOM     14  C   MET A  -5       3.405  24.441  -9.295  1.00 19.90           C  
ANISOU   14  C   MET A  -5     1280   2977   3302    -26      2     58       C  
ATOM     15  O   MET A  -5       4.318  24.693 -10.102  1.00 22.95           O  
ANISOU   15  O   MET A  -5     1378   3501   3838    -19    124    203       O  
ATOM     16  CB AMET A  -5       1.507  23.271 -10.472  0.50 18.29           C  
ANISOU   16  CB AMET A  -5     1231   2711   3004    119    -33     63       C  
ATOM     17  CB BMET A  -5       1.957  23.536 -11.068  0.50 21.63           C  
ANISOU   17  CB BMET A  -5     1824   3086   3308    171    -78    107       C  
ATOM     18  CG AMET A  -5       1.640  21.949  -9.690  0.50 14.62           C  
ANISOU   18  CG AMET A  -5      375   2617   2563    518    126    -72       C  
ATOM     19  CG BMET A  -5       1.788  22.068 -10.815  0.50 24.45           C  
ANISOU   19  CG BMET A  -5     2601   3199   3490    146    -82     15       C  
ATOM     20  SD AMET A  -5       1.134  20.520 -10.626  0.50 16.67           S  
ANISOU   20  SD AMET A  -5      551   2664   3117      5    184     76       S  
ATOM     21  SD BMET A  -5       0.076  21.875 -10.342  0.50 30.03           S  
ANISOU   21  SD BMET A  -5     3303   3967   4137    461    294    169       S  
ATOM     22  CE AMET A  -5      -0.564  20.821 -10.732  0.50 12.73           C  
ANISOU   22  CE AMET A  -5      276   1699   2859   -182    -14   -170       C  
ATOM     23  CE BMET A  -5      -0.365  20.204 -10.787  0.50 24.92           C  
ANISOU   23  CE BMET A  -5     2095   3819   3554    390    354    261       C  
ATOM     24  N   GLY A  -4       3.620  24.124  -8.024  1.00 19.77           N  
ANISOU   24  N   GLY A  -4      885   3176   3447     38     56    -14       N  
ATOM     25  CA  GLY A  -4       4.954  24.015  -7.537  1.00 20.93           C  
ANISOU   25  CA  GLY A  -4     1272   3215   3466    103   -172    -52       C  
ATOM     26  C   GLY A  -4       5.660  22.765  -7.999  1.00 21.47           C  
ANISOU   26  C   GLY A  -4     1421   3234   3498    157   -145      1       C  
ATOM     27  O   GLY A  -4       5.077  21.825  -8.472  1.00 22.78           O  
ANISOU   27  O   GLY A  -4     1260   3497   3896     44    -29   -279       O  
ATOM     28  N   ARG A  -3       6.964  22.772  -7.863  1.00 21.30           N  
ANISOU   28  N   ARG A  -3     1257   3432   3403    250   -110    122       N  
ATOM     29  CA  ARG A  -3       7.824  21.633  -8.207  1.00 20.76           C  
ANISOU   29  CA  ARG A  -3     1205   3383   3301     70     47    259       C  
ATOM     30  C   ARG A  -3       7.946  20.700  -7.008  1.00 20.11           C  
ANISOU   30  C   ARG A  -3      929   3339   3373     99   -186    275       C  
ATOM     31  O   ARG A  -3       7.534  21.032  -5.903  1.00 22.35           O  
ANISOU   31  O   ARG A  -3     1241   3759   3489   -189    -25    397       O  
ATOM     32  CB  ARG A  -3       9.153  22.118  -8.701  1.00 22.30           C  
ANISOU   32  CB  ARG A  -3     1390   3607   3474    111     19    285       C  
ATOM     33  CG  ARG A  -3       9.035  22.650 -10.107  1.00 24.75           C  
ANISOU   33  CG  ARG A  -3     1823   3947   3631    202    186    280       C  
ATOM     34  CD  ARG A  -3      10.291  23.250 -10.638  1.00 25.62           C  
ANISOU   34  CD  ARG A  -3     1483   4481   3770    265    366    255       C  
ATOM     35  NE  ARG A  -3       9.983  23.809 -11.954  1.00 29.55           N  
ANISOU   35  NE  ARG A  -3     2710   4669   3849    315    343    244       N  
ATOM     36  CZ  ARG A  -3      10.820  24.518 -12.687  1.00 33.10           C  
ANISOU   36  CZ  ARG A  -3     3793   4608   4176   -168     97    189       C  
ATOM     37  NH1 ARG A  -3      12.047  24.761 -12.237  1.00 33.21           N  
ANISOU   37  NH1 ARG A  -3     3261   5063   4293    -88    340     25       N  
ATOM     38  NH2 ARG A  -3      10.420  24.969 -13.874  1.00 35.03           N  
ANISOU   38  NH2 ARG A  -3     4475   4525   4307    -27     -1    247       N  
ATOM     39  N   GLY A  -2       8.567  19.556  -7.224  1.00 19.86           N  
ANISOU   39  N   GLY A  -2     1162   3070   3313    -23    159    353       N  
ATOM     40  CA  GLY A  -2       8.764  18.568  -6.190  1.00 19.44           C  
ANISOU   40  CA  GLY A  -2     1013   3028   3343     46   -164    347       C  
ATOM     41  C   GLY A  -2       9.894  18.919  -5.271  1.00 19.11           C  
ANISOU   41  C   GLY A  -2     1109   2833   3320    -72   -219    503       C  
ATOM     42  O   GLY A  -2      10.566  19.954  -5.448  1.00 20.65           O  
ANISOU   42  O   GLY A  -2      835   3141   3870     14    -48    476       O  
ATOM     43  N   SER A  -1      10.077  18.091  -4.267  1.00 18.96           N  
ANISOU   43  N   SER A  -1     1034   2952   3218   -251    -47    389       N  
ATOM     44  CA  SER A  -1      11.260  18.194  -3.439  1.00 18.67           C  
ANISOU   44  CA  SER A  -1     1089   2823   3181   -274   -126    255       C  
ATOM     45  C   SER A  -1      11.658  16.824  -2.961  1.00 17.40           C  
ANISOU   45  C   SER A  -1      798   2736   3074   -373   -175    175       C  
ATOM     46  O   SER A  -1      10.978  15.812  -3.126  1.00 18.58           O  
ANISOU   46  O   SER A  -1      936   2893   3228   -492   -293    235       O  
ATOM     47  CB  SER A  -1      10.993  19.070  -2.230  1.00 20.76           C  
ANISOU   47  CB  SER A  -1     1603   3018   3265   -110    -83    252       C  
ATOM     48  OG  SER A  -1      10.168  18.365  -1.311  1.00 26.75           O  
ANISOU   48  OG  SER A  -1     2376   3893   3895   -345    417     -7       O  
ATOM     49  N  AMET A   0      12.823  16.806  -2.330  0.50 17.56           N  
ANISOU   49  N  AMET A   0      821   2705   3146   -271   -191    196       N  
ATOM     50  N  BMET A   0      12.840  16.773  -2.376  0.50 17.62           N  
ANISOU   50  N  BMET A   0      846   2702   3145   -278   -196    196       N  
ATOM     51  CA AMET A   0      13.417  15.565  -1.835  0.50 16.89           C  
ANISOU   51  CA AMET A   0      747   2677   2991   -131      6    200       C  
ATOM     52  CA BMET A   0      13.368  15.480  -1.954  0.50 16.94           C  
ANISOU   52  CA BMET A   0      769   2668   2996   -151    -12    194       C  
ATOM     53  C  AMET A   0      12.472  14.885  -0.823  0.50 17.24           C  
ANISOU   53  C  AMET A   0      810   2640   3098   -209    -36    158       C  
ATOM     54  C  BMET A   0      12.454  14.884  -0.903  0.50 17.33           C  
ANISOU   54  C  BMET A   0      874   2628   3082   -191    -35    152       C  
ATOM     55  O  AMET A   0      12.342  13.685  -0.860  0.50 17.38           O  
ANISOU   55  O  AMET A   0      439   2808   3353   -270    165    416       O  
ATOM     56  O  BMET A   0      12.273  13.686  -0.864  0.50 17.86           O  
ANISOU   56  O  BMET A   0      633   2789   3363   -157    145    405       O  
ATOM     57  CB AMET A   0      14.804  15.897  -1.248  0.50 16.88           C  
ANISOU   57  CB AMET A   0      619   2819   2975   -108     96    162       C  
ATOM     58  CB BMET A   0      14.792  15.636  -1.451  0.50 16.88           C  
ANISOU   58  CB BMET A   0      691   2745   2978   -157     46    126       C  
ATOM     59  CG AMET A   0      15.944  14.877  -1.405  0.50 17.44           C  
ANISOU   59  CG AMET A   0      677   2769   3181    334    -18    207       C  
ATOM     60  CG BMET A   0      15.412  14.342  -1.011  0.50 17.55           C  
ANISOU   60  CG BMET A   0      770   2670   3229   -114     -1    122       C  
ATOM     61  SD AMET A   0      16.647  14.393   0.242  0.50 22.86           S  
ANISOU   61  SD AMET A   0     1427   3447   3811    335   -326    -15       S  
ATOM     62  SD BMET A   0      15.182  14.074   0.732  0.50 25.20           S  
ANISOU   62  SD BMET A   0     2384   3676   3514   -240    -42   -139       S  
ATOM     63  CE AMET A   0      14.989  14.240   0.942  0.50 16.68           C  
ANISOU   63  CE AMET A   0      529   2899   2907    735   -459    -88       C  
ATOM     64  CE BMET A   0      16.294  15.326   1.380  0.50 22.09           C  
ANISOU   64  CE BMET A   0     1548   3602   3243     90    100   -351       C  
ATOM     65  N  ACYS A   1      11.805  15.641   0.049  0.50 18.62           N  
ANISOU   65  N  ACYS A   1     1394   2579   3100   -258     75    163       N  
ATOM     66  N  BCYS A   1      11.874  15.750  -0.084  0.50 18.64           N  
ANISOU   66  N  BCYS A   1     1411   2566   3101   -188     64    151       N  
ATOM     67  CA ACYS A   1      10.852  15.027   1.014  0.50 19.06           C  
ANISOU   67  CA ACYS A   1     1440   2703   3096   -127     13    196       C  
ATOM     68  CA BCYS A   1      10.881  15.367   0.924  0.50 19.09           C  
ANISOU   68  CA BCYS A   1     1495   2690   3067    -71     63    175       C  
ATOM     69  C  ACYS A   1       9.625  14.376   0.387  0.50 17.32           C  
ANISOU   69  C  ACYS A   1     1012   2613   2953   -186    105    175       C  
ATOM     70  C  BCYS A   1       9.680  14.520   0.394  0.50 17.62           C  
ANISOU   70  C  BCYS A   1     1097   2629   2969   -122     69    174       C  
ATOM     71  O  ACYS A   1       8.842  13.690   1.067  0.50 18.67           O  
ANISOU   71  O  ACYS A   1     1307   2603   3182     74    411    194       O  
ATOM     72  O  BCYS A   1       9.018  13.829   1.166  0.50 18.97           O  
ANISOU   72  O  BCYS A   1     1482   2548   3176    117    224    193       O  
ATOM     73  CB ACYS A   1      10.393  16.024   2.072  0.50 19.94           C  
ANISOU   73  CB ACYS A   1     1753   2762   3061   -206    -64    125       C  
ATOM     74  CB BCYS A   1      10.400  16.631   1.632  0.50 20.19           C  
ANISOU   74  CB BCYS A   1     1781   2726   3162    -20    -98    127       C  
ATOM     75  SG ACYS A   1       9.484  17.472   1.462  0.50 27.85           S  
ANISOU   75  SG ACYS A   1     2556   3606   4418     12   -219    241       S  
ATOM     76  SG BCYS A   1       9.891  16.340   3.368  0.50 26.83           S  
ANISOU   76  SG BCYS A   1     2691   3589   3913   -123    706    210       S  
ATOM     77  N   ASP A   2       9.496  14.490  -0.929  1.00 16.83           N  
ANISOU   77  N   ASP A   2      725   2712   2955   -303    -29    370       N  
ATOM     78  CA  ASP A   2       8.420  13.771  -1.559  1.00 16.58           C  
ANISOU   78  CA  ASP A   2      404   2797   3099   -350   -137    330       C  
ATOM     79  C   ASP A   2       8.580  12.266  -1.404  1.00 16.37           C  
ANISOU   79  C   ASP A   2      590   2684   2945   -525     -7    268       C  
ATOM     80  O   ASP A   2       7.614  11.609  -1.460  1.00 18.44           O  
ANISOU   80  O   ASP A   2     1053   2764   3187   -673    -56    209       O  
ATOM     81  CB  ASP A   2       8.304  14.147  -3.017  1.00 19.44           C  
ANISOU   81  CB  ASP A   2     1158   3057   3168   -509   -170    288       C  
ATOM     82  CG  ASP A   2       7.667  15.532  -3.223  1.00 20.21           C  
ANISOU   82  CG  ASP A   2      558   3618   3501    -51      2    512       C  
ATOM     83  OD1 ASP A   2       6.918  16.050  -2.351  1.00 28.46           O  
ANISOU   83  OD1 ASP A   2     1870   4514   4427    487    101    564       O  
ATOM     84  OD2 ASP A   2       7.901  16.093  -4.299  1.00 25.63           O  
ANISOU   84  OD2 ASP A   2      998   4793   3946   -595    -58    667       O  
ATOM     85  N   ALA A   3       9.811  11.776  -1.191  1.00 16.37           N  
ANISOU   85  N   ALA A   3      708   2668   2842   -353    290    209       N  
ATOM     86  CA  ALA A   3      10.030  10.346  -0.910  1.00 16.18           C  
ANISOU   86  CA  ALA A   3      857   2524   2764    -69    449      8       C  
ATOM     87  C   ALA A   3       9.234   9.889   0.333  1.00 14.16           C  
ANISOU   87  C   ALA A   3      396   2267   2714   -190    234     49       C  
ATOM     88  O   ALA A   3       8.986   8.694   0.504  1.00 16.11           O  
ANISOU   88  O   ALA A   3      986   2201   2932   -130    355     60       O  
ATOM     89  CB  ALA A   3      11.510  10.047  -0.735  1.00 18.54           C  
ANISOU   89  CB  ALA A   3     1083   2910   3049     56    529    161       C  
ATOM     90  N   PHE A   4       8.984  10.813   1.231  1.00 13.19           N  
ANISOU   90  N   PHE A   4      273   2058   2678   -172     13     23       N  
ATOM     91  CA  PHE A   4       8.282  10.503   2.486  1.00 12.63           C  
ANISOU   91  CA  PHE A   4      514   1794   2489   -148     98    101       C  
ATOM     92  C   PHE A   4       6.773  10.572   2.357  1.00 12.01           C  
ANISOU   92  C   PHE A   4      388   1767   2409   -261    117     -8       C  
ATOM     93  O   PHE A   4       6.071  10.059   3.207  1.00 13.19           O  
ANISOU   93  O   PHE A   4      502   2030   2476   -116    189    159       O  
ATOM     94  CB  PHE A   4       8.694  11.438   3.633  1.00 12.33           C  
ANISOU   94  CB  PHE A   4      253   1840   2591     16      2    113       C  
ATOM     95  CG  PHE A   4      10.126  11.263   4.056  1.00 13.34           C  
ANISOU   95  CG  PHE A   4      266   2139   2663   -126    113    -44       C  
ATOM     96  CD1 PHE A   4      10.450  10.231   4.917  1.00 14.31           C  
ANISOU   96  CD1 PHE A   4      283   2427   2728     39    270     56       C  
ATOM     97  CD2 PHE A   4      11.117  12.096   3.644  1.00 15.67           C  
ANISOU   97  CD2 PHE A   4      443   2547   2963   -490   -155    216       C  
ATOM     98  CE1 PHE A   4      11.738  10.023   5.304  1.00 14.90           C  
ANISOU   98  CE1 PHE A   4      281   2716   2661    149    126    190       C  
ATOM     99  CE2 PHE A   4      12.418  11.907   4.037  1.00 16.44           C  
ANISOU   99  CE2 PHE A   4      691   2748   2807   -771   -211    130       C  
ATOM    100  CZ  PHE A   4      12.757  10.839   4.854  1.00 15.06           C  
ANISOU  100  CZ  PHE A   4      268   2909   2542   -143   -129    -55       C  
ATOM    101  N   VAL A   5       6.270  11.330   1.367  1.00 12.46           N  
ANISOU  101  N   VAL A   5      349   1965   2417   -375    147    105       N  
ATOM    102  CA  VAL A   5       4.844  11.602   1.273  1.00 12.01           C  
ANISOU  102  CA  VAL A   5      289   1750   2524   -218    100    -15       C  
ATOM    103  C   VAL A   5       4.081  10.364   0.956  1.00 12.97           C  
ANISOU  103  C   VAL A   5      272   1825   2830   -167    -42   -207       C  
ATOM    104  O   VAL A   5       4.436   9.585   0.059  1.00 15.97           O  
ANISOU  104  O   VAL A   5      542   2371   3154   -467    151   -295       O  
ATOM    105  CB  VAL A   5       4.590  12.704   0.204  1.00 14.09           C  
ANISOU  105  CB  VAL A   5      435   1798   3119   -136     52     77       C  
ATOM    106  CG1 VAL A   5       3.124  12.808  -0.286  1.00 17.06           C  
ANISOU  106  CG1 VAL A   5      418   2694   3369     79   -154   -103       C  
ATOM    107  CG2 VAL A   5       5.194  14.074   0.752  1.00 14.97           C  
ANISOU  107  CG2 VAL A   5      682   1995   3011    -94   -160     57       C  
ATOM    108  N   GLY A   6       2.932  10.214   1.615  1.00 12.79           N  
ANISOU  108  N   GLY A   6      274   1990   2594   -191     12    -87       N  
ATOM    109  CA  GLY A   6       2.062   9.132   1.354  1.00 13.20           C  
ANISOU  109  CA  GLY A   6      311   2137   2567   -245    -28   -107       C  
ATOM    110  C   GLY A   6       1.496   8.601   2.651  1.00 12.12           C  
ANISOU  110  C   GLY A   6      281   1928   2393   -190   -117    -34       C  
ATOM    111  O   GLY A   6       1.423   9.282   3.642  1.00 13.34           O  
ANISOU  111  O   GLY A   6      424   2171   2471   -323    155   -178       O  
ATOM    112  N   THR A   7       0.984   7.378   2.555  1.00 12.81           N  
ANISOU  112  N   THR A   7      493   1864   2508   -178   -193      0       N  
ATOM    113  CA  THR A   7       0.252   6.702   3.648  1.00 12.53           C  
ANISOU  113  CA  THR A   7      258   1870   2632     50    -85     64       C  
ATOM    114  C   THR A   7       1.002   5.400   3.985  1.00 12.08           C  
ANISOU  114  C   THR A   7      255   1769   2565     -1     74    -32       C  
ATOM    115  O   THR A   7       1.208   4.578   3.104  1.00 13.90           O  
ANISOU  115  O   THR A   7      518   1940   2821     57   -307   -142       O  
ATOM    116  CB  THR A   7      -1.179   6.363   3.206  1.00 13.82           C  
ANISOU  116  CB  THR A   7      264   1931   3053    -48   -168      0       C  
ATOM    117  OG1 THR A   7      -1.763   7.554   2.653  1.00 18.51           O  
ANISOU  117  OG1 THR A   7      291   2663   4078     57   -367    302       O  
ATOM    118  CG2 THR A   7      -1.996   5.833   4.384  1.00 17.30           C  
ANISOU  118  CG2 THR A   7      473   2589   3509   -202    130    -44       C  
ATOM    119  N   TRP A   8       1.381   5.281   5.250  1.00 11.68           N  
ANISOU  119  N   TRP A   8      286   1765   2384    126    227     91       N  
ATOM    120  CA  TRP A   8       2.285   4.226   5.702  1.00 11.95           C  
ANISOU  120  CA  TRP A   8      312   1753   2474    185     64     86       C  
ATOM    121  C   TRP A   8       1.618   3.479   6.849  1.00 11.92           C  
ANISOU  121  C   TRP A   8      255   1723   2552    -41     39    122       C  
ATOM    122  O   TRP A   8       0.804   4.064   7.575  1.00 14.52           O  
ANISOU  122  O   TRP A   8      924   1910   2679    154    399    169       O  
ATOM    123  CB  TRP A   8       3.596   4.852   6.197  1.00 11.96           C  
ANISOU  123  CB  TRP A   8      281   1799   2463    -87    -16    192       C  
ATOM    124  CG  TRP A   8       4.280   5.683   5.188  1.00 11.30           C  
ANISOU  124  CG  TRP A   8      253   1763   2278     -1     15     89       C  
ATOM    125  CD1 TRP A   8       4.201   7.016   4.991  1.00 11.92           C  
ANISOU  125  CD1 TRP A   8      255   1826   2448    -38     42    -19       C  
ATOM    126  CD2 TRP A   8       5.285   5.200   4.293  1.00 11.53           C  
ANISOU  126  CD2 TRP A   8      255   1559   2565    -43     52     -4       C  
ATOM    127  NE1 TRP A   8       5.054   7.396   3.976  1.00 12.94           N  
ANISOU  127  NE1 TRP A   8      490   1664   2761   -293    175    218       N  
ATOM    128  CE2 TRP A   8       5.691   6.282   3.515  1.00 11.86           C  
ANISOU  128  CE2 TRP A   8      260   1827   2416     42    108    -78       C  
ATOM    129  CE3 TRP A   8       5.748   3.926   4.011  1.00 12.00           C  
ANISOU  129  CE3 TRP A   8      282   1813   2462    -29    248     61       C  
ATOM    130  CZ2 TRP A   8       6.678   6.158   2.544  1.00 12.82           C  
ANISOU  130  CZ2 TRP A   8      308   2011   2551   -281    -24     85       C  
ATOM    131  CZ3 TRP A   8       6.761   3.783   3.056  1.00 12.63           C  
ANISOU  131  CZ3 TRP A   8      260   1957   2578    -21   -128    -80       C  
ATOM    132  CH2 TRP A   8       7.141   4.897   2.293  1.00 13.52           C  
ANISOU  132  CH2 TRP A   8      288   2273   2574    232    129    -99       C  
ATOM    133  N   LYS A   9       1.855   2.200   6.951  1.00 12.13           N  
ANISOU  133  N   LYS A   9      268   1814   2527   -130   -115    155       N  
ATOM    134  CA  LYS A   9       1.315   1.359   8.037  1.00 12.42           C  
ANISOU  134  CA  LYS A   9      290   1993   2434    -22   -285    152       C  
ATOM    135  C   LYS A   9       2.426   0.628   8.756  1.00 11.78           C  
ANISOU  135  C   LYS A   9      269   1855   2353   -156    -55    143       C  
ATOM    136  O   LYS A   9       3.405   0.161   8.154  1.00 12.54           O  
ANISOU  136  O   LYS A   9      266   1984   2514     10    175     29       O  
ATOM    137  CB  LYS A   9       0.311   0.364   7.464  1.00 14.08           C  
ANISOU  137  CB  LYS A   9      547   2189   2612   -334   -216    371       C  
ATOM    138  CG  LYS A   9       0.776  -0.643   6.460  1.00 20.95           C  
ANISOU  138  CG  LYS A   9     1881   2875   3201   -373   -299    213       C  
ATOM    139  CD  LYS A   9      -0.369  -1.487   5.999  1.00 26.86           C  
ANISOU  139  CD  LYS A   9     2991   3294   3917   -668   -328     22       C  
ATOM    140  CE  LYS A   9       0.057  -2.388   4.872  1.00 29.71           C  
ANISOU  140  CE  LYS A   9     3367   3604   4316   -540    -42    -48       C  
ATOM    141  NZ  LYS A   9      -1.099  -3.188   4.339  1.00 33.97           N  
ANISOU  141  NZ  LYS A   9     3821   4199   4888  -1140   -295    100       N  
ATOM    142  N   LEU A  10       2.334   0.593  10.058  1.00 12.57           N  
ANISOU  142  N   LEU A  10      253   2076   2444     -8    -36    145       N  
ATOM    143  CA  LEU A  10       3.355  -0.110  10.874  1.00 12.76           C  
ANISOU  143  CA  LEU A  10      276   2044   2525   -154   -159    124       C  
ATOM    144  C   LEU A  10       3.342  -1.609  10.635  1.00 12.86           C  
ANISOU  144  C   LEU A  10      263   2051   2570    -25   -151     85       C  
ATOM    145  O   LEU A  10       2.286  -2.237  10.739  1.00 15.27           O  
ANISOU  145  O   LEU A  10      354   2193   3254   -407   -268    244       O  
ATOM    146  CB  LEU A  10       3.098   0.133  12.335  1.00 12.87           C  
ANISOU  146  CB  LEU A  10      256   2070   2564    -72      3    120       C  
ATOM    147  CG  LEU A  10       4.194  -0.413  13.265  1.00 13.82           C  
ANISOU  147  CG  LEU A  10      256   2396   2598     28    -74     75       C  
ATOM    148  CD1 LEU A  10       5.492   0.391  13.228  1.00 14.59           C  
ANISOU  148  CD1 LEU A  10      479   2533   2529   -226     19    303       C  
ATOM    149  CD2 LEU A  10       3.699  -0.475  14.731  1.00 16.49           C  
ANISOU  149  CD2 LEU A  10      556   3032   2676     30      8     79       C  
ATOM    150  N   VAL A  11       4.532  -2.134  10.331  1.00 12.39           N  
ANISOU  150  N   VAL A  11      304   1740   2662   -246   -175    103       N  
ATOM    151  CA  VAL A  11       4.697  -3.552  10.178  1.00 14.00           C  
ANISOU  151  CA  VAL A  11      565   1970   2783   -239   -321     78       C  
ATOM    152  C   VAL A  11       5.550  -4.242  11.207  1.00 14.59           C  
ANISOU  152  C   VAL A  11      790   1940   2813   -274   -362    170       C  
ATOM    153  O   VAL A  11       5.432  -5.464  11.379  1.00 16.65           O  
ANISOU  153  O   VAL A  11     1027   2045   3252   -278   -571    231       O  
ATOM    154  CB  VAL A  11       5.033  -3.967   8.769  1.00 16.56           C  
ANISOU  154  CB  VAL A  11     1146   2157   2988    -93   -360     63       C  
ATOM    155  CG1 VAL A  11       3.890  -3.535   7.802  1.00 19.37           C  
ANISOU  155  CG1 VAL A  11     1536   2670   3150    -85   -441    -76       C  
ATOM    156  CG2 VAL A  11       6.351  -3.477   8.340  1.00 18.92           C  
ANISOU  156  CG2 VAL A  11     1543   2438   3205   -294     -3   -186       C  
ATOM    157  N   SER A  12       6.482  -3.541  11.842  1.00 13.84           N  
ANISOU  157  N   SER A  12      576   1919   2761   -144   -321    193       N  
ATOM    158  CA  SER A  12       7.290  -4.139  12.863  1.00 15.29           C  
ANISOU  158  CA  SER A  12     1163   1962   2684    -48   -193    113       C  
ATOM    159  C   SER A  12       7.761  -3.084  13.829  1.00 12.48           C  
ANISOU  159  C   SER A  12      435   1812   2493   -113   -189    154       C  
ATOM    160  O   SER A  12       7.932  -1.933  13.463  1.00 12.86           O  
ANISOU  160  O   SER A  12      343   1837   2705    -95   -152    253       O  
ATOM    161  CB  SER A  12       8.420  -4.962  12.297  1.00 17.19           C  
ANISOU  161  CB  SER A  12     1337   2242   2950    -63   -365    158       C  
ATOM    162  OG  SER A  12       9.370  -4.131  11.714  1.00 18.02           O  
ANISOU  162  OG  SER A  12     1254   2576   3015   -110   -148    199       O  
ATOM    163  N  ASER A  13       7.826  -3.422  15.129  0.50 14.38           N  
ANISOU  163  N  ASER A  13     1061   1893   2507   -262   -127     68       N  
ATOM    164  N  BSER A  13       8.186  -3.632  14.948  0.50 13.00           N  
ANISOU  164  N  BSER A  13      721   1753   2464   -141   -174    141       N  
ATOM    165  CA ASER A  13       8.319  -2.512  16.212  0.50 14.76           C  
ANISOU  165  CA ASER A  13     1281   1923   2402   -209    -47    109       C  
ATOM    166  CA BSER A  13       8.677  -2.833  16.003  0.50 12.34           C  
ANISOU  166  CA BSER A  13      754   1619   2316     52   -190     86       C  
ATOM    167  C  ASER A  13       9.182  -3.333  17.223  0.50 14.93           C  
ANISOU  167  C  ASER A  13     1364   1940   2367   -252    -24     28       C  
ATOM    168  C  BSER A  13       9.626  -3.600  16.840  0.50 11.83           C  
ANISOU  168  C  BSER A  13      388   1819   2287    -81   -117     86       C  
ATOM    169  O  ASER A  13       8.634  -4.298  17.796  0.50 17.04           O  
ANISOU  169  O  ASER A  13     1799   2051   2622   -336    -20    276       O  
ATOM    170  O  BSER A  13       9.402  -4.764  17.174  0.50 11.99           O  
ANISOU  170  O  BSER A  13      269   1789   2497    106   -120    249       O  
ATOM    171  CB ASER A  13       7.099  -1.813  16.904  0.50 14.66           C  
ANISOU  171  CB ASER A  13     1164   1886   2519   -305    -12    113       C  
ATOM    172  CB BSER A  13       7.514  -2.383  16.885  0.50 13.00           C  
ANISOU  172  CB BSER A  13      884   1614   2439     81   -151    130       C  
ATOM    173  OG ASER A  13       7.446  -0.993  18.027  0.50 14.77           O  
ANISOU  173  OG ASER A  13      903   2029   2680    -29     19    116       O  
ATOM    174  OG BSER A  13       7.974  -1.520  17.913  0.50 13.84           O  
ANISOU  174  OG BSER A  13      877   1785   2597    601   -337   -151       O  
ATOM    175  N  AGLU A  14      10.492  -3.005  17.392  0.50 14.76           N  
ANISOU  175  N  AGLU A  14     1301   1879   2425   -241    -26     65       N  
ATOM    176  N  BGLU A  14      10.687  -2.910  17.204  0.50 11.98           N  
ANISOU  176  N  BGLU A  14      274   1806   2470    -30   -101     87       N  
ATOM    177  CA AGLU A  14      11.474  -3.680  18.340  0.50 14.80           C  
ANISOU  177  CA AGLU A  14     1366   1948   2309    -36    -30     80       C  
ATOM    178  CA BGLU A  14      11.711  -3.474  18.034  0.50 12.60           C  
ANISOU  178  CA BGLU A  14      554   1864   2368    118    -27    152       C  
ATOM    179  C  AGLU A  14      11.948  -2.702  19.435  0.50 10.75           C  
ANISOU  179  C  AGLU A  14      306   1657   2120     -3     20    211       C  
ATOM    180  C  BGLU A  14      12.047  -2.501  19.096  0.50 10.97           C  
ANISOU  180  C  BGLU A  14      270   1669   2227    154      0    200       C  
ATOM    181  O  AGLU A  14      12.277  -1.537  19.118  0.50 11.87           O  
ANISOU  181  O  AGLU A  14      368   1596   2544     54    -74     85       O  
ATOM    182  O  BGLU A  14      12.321  -1.338  18.850  0.50 12.12           O  
ANISOU  182  O  BGLU A  14      271   1841   2493    146    -89     92       O  
ATOM    183  CB AGLU A  14      12.734  -4.325  17.624  0.50 16.78           C  
ANISOU  183  CB AGLU A  14     1654   2224   2498     21     17     68       C  
ATOM    184  CB BGLU A  14      12.970  -3.929  17.293  0.50 13.86           C  
ANISOU  184  CB BGLU A  14      626   2064   2574    250   -114    109       C  
ATOM    185  CG AGLU A  14      14.204  -4.145  18.322  0.50 18.53           C  
ANISOU  185  CG AGLU A  14     1693   2584   2763    -37     49     75       C  
ATOM    186  CG BGLU A  14      13.749  -2.960  16.548  0.50 18.66           C  
ANISOU  186  CG BGLU A  14     1872   2307   2910    166     31    -77       C  
ATOM    187  CD AGLU A  14      15.220  -5.382  18.534  0.50 22.32           C  
ANISOU  187  CD AGLU A  14     1862   3173   3445    -46    255    259       C  
ATOM    188  CD BGLU A  14      15.122  -3.513  16.151  0.50 21.60           C  
ANISOU  188  CD BGLU A  14     2175   2633   3399    457     71   -141       C  
ATOM    189  OE1AGLU A  14      16.227  -5.550  17.808  0.50 18.89           O  
ANISOU  189  OE1AGLU A  14      620   2752   3803    170    112    367       O  
ATOM    190  OE1BGLU A  14      15.862  -3.878  17.059  0.50 23.26           O  
ANISOU  190  OE1BGLU A  14     1358   3104   4375    978     18   -578       O  
ATOM    191  OE2AGLU A  14      15.126  -6.123  19.537  0.50 22.74           O  
ANISOU  191  OE2AGLU A  14     1442   3592   3605   -288    245    702       O  
ATOM    192  OE2BGLU A  14      15.446  -3.566  14.964  0.50 23.36           O  
ANISOU  192  OE2BGLU A  14     2344   2631   3898    803    413   -439       O  
ATOM    193  N  AASN A  15      11.971  -3.152  20.699  0.50 10.58           N  
ANISOU  193  N  AASN A  15      370   1623   2025    -14     62    197       N  
ATOM    194  N  BASN A  15      12.028  -2.998  20.301  0.50 10.53           N  
ANISOU  194  N  BASN A  15      259   1712   2029     75     77    262       N  
ATOM    195  CA AASN A  15      12.524  -2.374  21.813  0.50 10.57           C  
ANISOU  195  CA AASN A  15      377   1601   2036     27     -7    214       C  
ATOM    196  CA BASN A  15      12.581  -2.306  21.469  0.50 10.82           C  
ANISOU  196  CA BASN A  15      338   1704   2070    159     73    187       C  
ATOM    197  C  AASN A  15      11.752  -1.040  21.948  0.50 10.64           C  
ANISOU  197  C  AASN A  15      253   1596   2192     17     13    164       C  
ATOM    198  C  BASN A  15      11.737  -1.146  22.016  0.50 11.12           C  
ANISOU  198  C  BASN A  15      256   1736   2232     65     27    146       C  
ATOM    199  O  AASN A  15      12.225  -0.052  22.486  0.50  9.45           O  
ANISOU  199  O  AASN A  15      262   1295   2032     12    127    418       O  
ATOM    200  O  BASN A  15      12.159  -0.434  22.948  0.50 10.02           O  
ANISOU  200  O  BASN A  15      259   1694   1855     88     58    435       O  
ATOM    201  CB AASN A  15      14.050  -2.156  21.613  0.50  9.93           C  
ANISOU  201  CB AASN A  15      266   1545   1962    103    -62    329       C  
ATOM    202  CB BASN A  15      14.009  -1.797  21.223  0.50 11.46           C  
ANISOU  202  CB BASN A  15      362   1694   2298     34     93    210       C  
ATOM    203  CG AASN A  15      14.815  -2.096  22.877  0.50 12.28           C  
ANISOU  203  CG AASN A  15      277   2067   2321    198     84    175       C  
ATOM    204  CG BASN A  15      15.032  -2.901  21.154  0.50 14.52           C  
ANISOU  204  CG BASN A  15      374   2214   2929    450    -52    371       C  
ATOM    205  OD1AASN A  15      14.648  -2.951  23.720  0.50 15.59           O  
ANISOU  205  OD1AASN A  15     1082   2356   2486    225   -138    228       O  
ATOM    206  OD1BASN A  15      14.891  -3.969  21.790  0.50 15.24           O  
ANISOU  206  OD1BASN A  15      281   1992   3516    219     -6   -100       O  
ATOM    207  ND2AASN A  15      15.635  -1.061  23.034  0.50 12.81           N  
ANISOU  207  ND2AASN A  15      257   2200   2407     69    -68    -36       N  
ATOM    208  ND2BASN A  15      16.151  -2.606  20.459  0.50 17.49           N  
ANISOU  208  ND2BASN A  15      446   2764   3435   -106    137   -219       N  
ATOM    209  N   PHE A  16      10.468  -1.028  21.546  1.00 11.23           N  
ANISOU  209  N   PHE A  16      255   1595   2414     44    -44     49       N  
ATOM    210  CA  PHE A  16       9.667   0.196  21.801  1.00 11.32           C  
ANISOU  210  CA  PHE A  16      283   1667   2349     55   -240     26       C  
ATOM    211  C   PHE A  16       9.237   0.352  23.232  1.00 11.36           C  
ANISOU  211  C   PHE A  16      278   1691   2345    112   -179     76       C  
ATOM    212  O   PHE A  16       9.237   1.445  23.763  1.00 11.52           O  
ANISOU  212  O   PHE A  16      254   1658   2463      1     57     -1       O  
ATOM    213  CB  PHE A  16       8.493   0.210  20.875  1.00 12.37           C  
ANISOU  213  CB  PHE A  16      431   1788   2480     12   -220     66       C  
ATOM    214  CG  PHE A  16       7.767   1.536  20.786  1.00 11.75           C  
ANISOU  214  CG  PHE A  16      289   1950   2223    174    -49     74       C  
ATOM    215  CD1 PHE A  16       8.381   2.683  20.401  1.00 12.93           C  
ANISOU  215  CD1 PHE A  16      344   2079   2488    374    -75      9       C  
ATOM    216  CD2 PHE A  16       6.410   1.611  21.017  1.00 12.55           C  
ANISOU  216  CD2 PHE A  16      273   2118   2377    176    -92    -41       C  
ATOM    217  CE1 PHE A  16       7.736   3.889  20.275  1.00 13.82           C  
ANISOU  217  CE1 PHE A  16      463   2106   2681    359    -99     81       C  
ATOM    218  CE2 PHE A  16       5.741   2.855  20.887  1.00 13.67           C  
ANISOU  218  CE2 PHE A  16      367   2333   2490    482     79     11       C  
ATOM    219  CZ  PHE A  16       6.407   3.967  20.511  1.00 14.38           C  
ANISOU  219  CZ  PHE A  16      771   2023   2669    510   -118    -56       C  
ATOM    220  N   ASP A  17       8.967  -0.755  23.898  1.00 11.93           N  
ANISOU  220  N   ASP A  17      271   1705   2556    126   -120     67       N  
ATOM    221  CA  ASP A  17       8.661  -0.635  25.318  1.00 11.95           C  
ANISOU  221  CA  ASP A  17      267   1755   2518   -113   -131    193       C  
ATOM    222  C   ASP A  17       9.831  -0.084  26.107  1.00 11.93           C  
ANISOU  222  C   ASP A  17      260   1783   2488   -101    -22    150       C  
ATOM    223  O   ASP A  17       9.672   0.791  26.911  1.00 12.75           O  
ANISOU  223  O   ASP A  17      266   2006   2572   -106    131    -53       O  
ATOM    224  CB  ASP A  17       8.217  -1.979  25.864  1.00 14.48           C  
ANISOU  224  CB  ASP A  17      693   2035   2771     -1     34    231       C  
ATOM    225  CG  ASP A  17       7.676  -1.870  27.287  1.00 15.08           C  
ANISOU  225  CG  ASP A  17      585   2231   2913   -207    106    480       C  
ATOM    226  OD1 ASP A  17       8.306  -2.363  28.231  1.00 22.39           O  
ANISOU  226  OD1 ASP A  17     1400   3955   3150   -114     20    483       O  
ATOM    227  OD2 ASP A  17       6.617  -1.338  27.467  1.00 19.69           O  
ANISOU  227  OD2 ASP A  17     1145   3224   3113    359    524    266       O  
ATOM    228  N   ASP A  18      11.062  -0.558  25.859  1.00 12.70           N  
ANISOU  228  N   ASP A  18      253   1943   2628     27      5    160       N  
ATOM    229  CA  ASP A  18      12.258  -0.026  26.513  1.00 12.60           C  
ANISOU  229  CA  ASP A  18      254   2055   2476     16    -55    266       C  
ATOM    230  C   ASP A  18      12.502   1.431  26.164  1.00 12.13           C  
ANISOU  230  C   ASP A  18      284   1876   2449    178    163     59       C  
ATOM    231  O   ASP A  18      12.868   2.216  27.049  1.00 12.91           O  
ANISOU  231  O   ASP A  18      255   2046   2604     34    -49     45       O  
ATOM    232  CB  ASP A  18      13.517  -0.869  26.263  1.00 14.28           C  
ANISOU  232  CB  ASP A  18      276   2330   2820    218     26    228       C  
ATOM    233  CG  ASP A  18      13.492  -2.169  27.110  1.00 20.21           C  
ANISOU  233  CG  ASP A  18     1428   2911   3339    288    203    457       C  
ATOM    234  OD1 ASP A  18      12.768  -2.276  28.123  1.00 27.14           O  
ANISOU  234  OD1 ASP A  18     2387   3621   4301    652    455    846       O  
ATOM    235  OD2 ASP A  18      14.215  -3.079  26.793  1.00 26.26           O  
ANISOU  235  OD2 ASP A  18     2511   3010   4455    481     71    430       O  
ATOM    236  N   TYR A  19      12.260   1.813  24.913  1.00 11.52           N  
ANISOU  236  N   TYR A  19      260   1765   2350    -51    110    -10       N  
ATOM    237  CA  TYR A  19      12.334   3.209  24.534  1.00 11.04           C  
ANISOU  237  CA  TYR A  19      260   1663   2269      6    123      0       C  
ATOM    238  C   TYR A  19      11.434   4.041  25.413  1.00 11.06           C  
ANISOU  238  C   TYR A  19      257   1658   2285    -43     72     31       C  
ATOM    239  O   TYR A  19      11.752   5.087  25.965  1.00 11.90           O  
ANISOU  239  O   TYR A  19      257   1881   2381     12     93     -8       O  
ATOM    240  CB  TYR A  19      12.085   3.417  23.069  1.00 11.67           C  
ANISOU  240  CB  TYR A  19      306   1836   2291    -72    321    -39       C  
ATOM    241  CG  TYR A  19      11.913   4.874  22.684  1.00 10.96           C  
ANISOU  241  CG  TYR A  19      258   1756   2147    -76     52    -88       C  
ATOM    242  CD1 TYR A  19      13.016   5.742  22.584  1.00 11.51           C  
ANISOU  242  CD1 TYR A  19      296   1879   2198   -241   -114     -8       C  
ATOM    243  CD2 TYR A  19      10.632   5.365  22.454  1.00 11.29           C  
ANISOU  243  CD2 TYR A  19      253   1846   2188      0      1      0       C  
ATOM    244  CE1 TYR A  19      12.833   7.076  22.314  1.00 11.51           C  
ANISOU  244  CE1 TYR A  19      291   1708   2373   -216    122    -59       C  
ATOM    245  CE2 TYR A  19      10.462   6.701  22.166  1.00 11.77           C  
ANISOU  245  CE2 TYR A  19      299   1932   2242   -242   -165    118       C  
ATOM    246  CZ  TYR A  19      11.512   7.540  22.089  1.00 11.21           C  
ANISOU  246  CZ  TYR A  19      277   1779   2202   -170    114   -117       C  
ATOM    247  OH  TYR A  19      11.311   8.880  21.799  1.00 12.59           O  
ANISOU  247  OH  TYR A  19      270   1841   2672    -80     15    104       O  
ATOM    248  N   MET A  20      10.147   3.632  25.459  1.00 10.75           N  
ANISOU  248  N   MET A  20      258   1647   2178     17     94    -14       N  
ATOM    249  CA  MET A  20       9.109   4.351  26.211  1.00 11.24           C  
ANISOU  249  CA  MET A  20      275   1683   2309    -56    199     87       C  
ATOM    250  C   MET A  20       9.448   4.410  27.706  1.00 11.41           C  
ANISOU  250  C   MET A  20      286   1695   2351   -189    131     20       C  
ATOM    251  O   MET A  20       9.302   5.422  28.329  1.00 11.99           O  
ANISOU  251  O   MET A  20      270   1920   2364   -143   -101     24       O  
ATOM    252  CB  MET A  20       7.715   3.802  26.041  1.00 11.48           C  
ANISOU  252  CB  MET A  20      271   1875   2213    -60    174     49       C  
ATOM    253  CG  MET A  20       7.067   3.937  24.610  1.00 11.21           C  
ANISOU  253  CG  MET A  20      314   1876   2069    267    190     88       C  
ATOM    254  SD  MET A  20       5.442   3.557  24.501  1.00 13.24           S  
ANISOU  254  SD  MET A  20      253   2275   2501     13     25     29       S  
ATOM    255  CE  MET A  20       5.587   1.835  24.632  1.00 15.30           C  
ANISOU  255  CE  MET A  20      335   2934   2542   -371    320   -409       C  
ATOM    256  N   LYS A  21      10.008   3.308  28.245  1.00 11.99           N  
ANISOU  256  N   LYS A  21      298   1909   2349   -152    242    115       N  
ATOM    257  CA  LYS A  21      10.449   3.327  29.639  1.00 13.21           C  
ANISOU  257  CA  LYS A  21      518   2162   2337    -38    217    104       C  
ATOM    258  C   LYS A  21      11.520   4.401  29.846  1.00 13.49           C  
ANISOU  258  C   LYS A  21      553   2234   2336     37     22     87       C  
ATOM    259  O   LYS A  21      11.503   5.140  30.827  1.00 14.75           O  
ANISOU  259  O   LYS A  21      736   2555   2314    -39      0    -12       O  
ATOM    260  CB  LYS A  21      11.051   1.967  30.084  1.00 14.79           C  
ANISOU  260  CB  LYS A  21      800   2351   2466    -96    128    212       C  
ATOM    261  CG  LYS A  21       9.978   0.923  30.369  1.00 16.45           C  
ANISOU  261  CG  LYS A  21      695   2727   2828     30     57    137       C  
ATOM    262  CD  LYS A  21      10.719  -0.361  30.815  1.00 20.16           C  
ANISOU  262  CD  LYS A  21     1700   2861   3096      9    234    316       C  
ATOM    263  CE  LYS A  21       9.762  -1.396  31.220  1.00 22.83           C  
ANISOU  263  CE  LYS A  21     2041   3086   3547   -131     21    280       C  
ATOM    264  NZ  LYS A  21      10.474  -2.538  31.810  1.00 26.33           N  
ANISOU  264  NZ  LYS A  21     2306   3475   4222    113   -253    547       N  
ATOM    265  N   GLU A  22      12.464   4.475  28.905  1.00 13.61           N  
ANISOU  265  N   GLU A  22      351   2405   2412   -216    -31     16       N  
ATOM    266  CA  GLU A  22      13.550   5.409  29.031  1.00 13.86           C  
ANISOU  266  CA  GLU A  22      300   2357   2608   -281   -102     53       C  
ATOM    267  C   GLU A  22      13.066   6.856  28.959  1.00 12.95           C  
ANISOU  267  C   GLU A  22      315   2124   2480   -329    -76   -131       C  
ATOM    268  O   GLU A  22      13.517   7.722  29.693  1.00 15.03           O  
ANISOU  268  O   GLU A  22      513   2400   2796   -352   -122    -39       O  
ATOM    269  CB  GLU A  22      14.663   5.146  27.978  1.00 14.17           C  
ANISOU  269  CB  GLU A  22      277   2457   2650   -228      2    214       C  
ATOM    270  CG  GLU A  22      16.002   5.635  28.278  1.00 15.55           C  
ANISOU  270  CG  GLU A  22      261   2665   2980    -55    132    199       C  
ATOM    271  CD  GLU A  22      16.741   4.814  29.386  1.00 17.00           C  
ANISOU  271  CD  GLU A  22      275   2922   3259     45   -246    395       C  
ATOM    272  OE1 GLU A  22      16.253   3.757  29.829  1.00 20.53           O  
ANISOU  272  OE1 GLU A  22     1281   3187   3331    299   -429    613       O  
ATOM    273  OE2 GLU A  22      17.923   5.136  29.686  1.00 19.65           O  
ANISOU  273  OE2 GLU A  22      421   3581   3463     36   -140     18       O  
ATOM    274  N   VAL A  23      12.014   7.089  28.160  1.00 13.36           N  
ANISOU  274  N   VAL A  23      358   2051   2665   -413   -145    -36       N  
ATOM    275  CA  VAL A  23      11.395   8.385  28.022  1.00 13.26           C  
ANISOU  275  CA  VAL A  23      659   1957   2423   -334     97    -38       C  
ATOM    276  C   VAL A  23      10.657   8.772  29.287  1.00 14.42           C  
ANISOU  276  C   VAL A  23      958   1990   2531    -82    -41     -9       C  
ATOM    277  O   VAL A  23      10.604   9.924  29.624  1.00 16.58           O  
ANISOU  277  O   VAL A  23     1632   2003   2662    -69    179   -102       O  
ATOM    278  CB  VAL A  23      10.446   8.389  26.770  1.00 13.63           C  
ANISOU  278  CB  VAL A  23      666   1881   2629    -52     57     25       C  
ATOM    279  CG1 VAL A  23       9.471   9.592  26.770  1.00 15.09           C  
ANISOU  279  CG1 VAL A  23      785   2224   2724    197     65     -5       C  
ATOM    280  CG2 VAL A  23      11.322   8.329  25.513  1.00 14.24           C  
ANISOU  280  CG2 VAL A  23      606   2172   2633   -321    222    -75       C  
ATOM    281  N   GLY A  24      10.170   7.776  30.009  1.00 13.78           N  
ANISOU  281  N   GLY A  24      680   2028   2524   -215     44    -23       N  
ATOM    282  CA  GLY A  24       9.428   7.978  31.240  1.00 13.48           C  
ANISOU  282  CA  GLY A  24      764   1864   2494    -78     91     62       C  
ATOM    283  C   GLY A  24       7.927   7.697  31.153  1.00 13.85           C  
ANISOU  283  C   GLY A  24      876   1997   2388     44    213    -55       C  
ATOM    284  O   GLY A  24       7.191   8.062  32.044  1.00 15.63           O  
ANISOU  284  O   GLY A  24      896   2343   2697   -281    237   -250       O  
ATOM    285  N   VAL A  25       7.490   6.962  30.130  1.00 12.43           N  
ANISOU  285  N   VAL A  25      271   1981   2469      9    197    -78       N  
ATOM    286  CA  VAL A  25       6.100   6.671  29.956  1.00 11.73           C  
ANISOU  286  CA  VAL A  25      273   1830   2352    132    144     54       C  
ATOM    287  C   VAL A  25       5.718   5.671  31.035  1.00 12.58           C  
ANISOU  287  C   VAL A  25      274   2112   2393    -15    141     27       C  
ATOM    288  O   VAL A  25       6.350   4.679  31.263  1.00 14.45           O  
ANISOU  288  O   VAL A  25      774   2144   2569    -31    -51    143       O  
ATOM    289  CB  VAL A  25       5.862   6.124  28.565  1.00 12.52           C  
ANISOU  289  CB  VAL A  25      369   1907   2480    -35    164     96       C  
ATOM    290  CG1 VAL A  25       4.372   5.840  28.314  1.00 14.25           C  
ANISOU  290  CG1 VAL A  25      374   2274   2766     -8     61     88       C  
ATOM    291  CG2 VAL A  25       6.293   7.071  27.482  1.00 14.26           C  
ANISOU  291  CG2 VAL A  25      323   2143   2951    -39     65    285       C  
ATOM    292  N   GLY A  26       4.526   5.869  31.590  1.00 14.48           N  
ANISOU  292  N   GLY A  26      719   2383   2396   -321     77     74       N  
ATOM    293  CA  GLY A  26       3.991   4.990  32.632  1.00 14.66           C  
ANISOU  293  CA  GLY A  26      814   2401   2354   -425     51    -43       C  
ATOM    294  C   GLY A  26       3.441   3.672  32.096  1.00 13.35           C  
ANISOU  294  C   GLY A  26      322   2363   2384   -382     10     44       C  
ATOM    295  O   GLY A  26       3.168   3.522  30.911  1.00 13.96           O  
ANISOU  295  O   GLY A  26      564   2424   2314   -305     32   -127       O  
ATOM    296  N   PHE A  27       3.239   2.720  33.004  1.00 13.64           N  
ANISOU  296  N   PHE A  27      508   2353   2321   -240     13     67       N  
ATOM    297  CA  PHE A  27       2.851   1.357  32.625  1.00 13.44           C  
ANISOU  297  CA  PHE A  27      355   2289   2461   -202    -12     58       C  
ATOM    298  C   PHE A  27       1.654   1.267  31.704  1.00 12.86           C  
ANISOU  298  C   PHE A  27      320   2140   2425   -348     59    137       C  
ATOM    299  O   PHE A  27       1.773   0.652  30.637  1.00 13.54           O  
ANISOU  299  O   PHE A  27      382   2341   2420   -385     26     63       O  
ATOM    300  CB  PHE A  27       2.646   0.515  33.885  1.00 13.78           C  
ANISOU  300  CB  PHE A  27      301   2346   2586   -145      4    124       C  
ATOM    301  CG  PHE A  27       2.307  -0.927  33.618  1.00 14.24           C  
ANISOU  301  CG  PHE A  27      410   2552   2447   -235   -241    114       C  
ATOM    302  CD1 PHE A  27       3.283  -1.898  33.517  1.00 16.97           C  
ANISOU  302  CD1 PHE A  27      922   2809   2716   -371    104    267       C  
ATOM    303  CD2 PHE A  27       0.988  -1.310  33.506  1.00 15.84           C  
ANISOU  303  CD2 PHE A  27      706   2524   2788   -389   -263    328       C  
ATOM    304  CE1 PHE A  27       2.908  -3.248  33.262  1.00 18.58           C  
ANISOU  304  CE1 PHE A  27     1485   2717   2856   -171    166    130       C  
ATOM    305  CE2 PHE A  27       0.668  -2.628  33.212  1.00 17.79           C  
ANISOU  305  CE2 PHE A  27     1720   2529   2507   -509   -259    355       C  
ATOM    306  CZ  PHE A  27       1.585  -3.567  33.109  1.00 18.24           C  
ANISOU  306  CZ  PHE A  27     1824   2480   2627   -355    -66     85       C  
ATOM    307  N   ALA A  28       0.495   1.786  32.119  1.00 13.61           N  
ANISOU  307  N   ALA A  28      312   2258   2598   -317    126    148       N  
ATOM    308  CA  ALA A  28      -0.721   1.536  31.351  1.00 13.91           C  
ANISOU  308  CA  ALA A  28      274   2227   2781   -202    -51     84       C  
ATOM    309  C   ALA A  28      -0.622   2.184  29.969  1.00 13.27           C  
ANISOU  309  C   ALA A  28      323   2130   2585   -157    -88     40       C  
ATOM    310  O   ALA A  28      -1.043   1.609  28.956  1.00 14.39           O  
ANISOU  310  O   ALA A  28      287   2450   2728   -195   -207     71       O  
ATOM    311  CB  ALA A  28      -1.960   2.020  32.065  1.00 15.52           C  
ANISOU  311  CB  ALA A  28      449   2592   2855    -17    149    199       C  
ATOM    312  N   THR A  29      -0.025   3.377  29.896  1.00 13.43           N  
ANISOU  312  N   THR A  29      297   2196   2609   -172   -215    -25       N  
ATOM    313  CA  THR A  29       0.195   4.012  28.620  1.00 13.21           C  
ANISOU  313  CA  THR A  29      313   2133   2571    -40   -207     35       C  
ATOM    314  C   THR A  29       1.119   3.187  27.746  1.00 13.21           C  
ANISOU  314  C   THR A  29      374   2118   2525   -138     51    -23       C  
ATOM    315  O   THR A  29       0.873   3.037  26.540  1.00 13.01           O  
ANISOU  315  O   THR A  29      320   2171   2450   -117    -70     78       O  
ATOM    316  CB  THR A  29       0.705   5.442  28.781  1.00 13.54           C  
ANISOU  316  CB  THR A  29      567   1995   2581    -62    -91     50       C  
ATOM    317  OG1 THR A  29      -0.264   6.188  29.516  1.00 17.12           O  
ANISOU  317  OG1 THR A  29      909   2403   3192     59     41     81       O  
ATOM    318  CG2 THR A  29       0.946   6.153  27.491  1.00 15.06           C  
ANISOU  318  CG2 THR A  29      410   2529   2780     11   -302     99       C  
ATOM    319  N   ARG A  30       2.254   2.730  28.297  1.00 13.15           N  
ANISOU  319  N   ARG A  30      388   2113   2494   -301   -187    -40       N  
ATOM    320  CA  ARG A  30       3.125   1.897  27.503  1.00 12.57           C  
ANISOU  320  CA  ARG A  30      469   2057   2249   -166    -74     30       C  
ATOM    321  C   ARG A  30       2.458   0.688  26.937  1.00 11.98           C  
ANISOU  321  C   ARG A  30      279   2079   2193   -132   -185    107       C  
ATOM    322  O   ARG A  30       2.673   0.304  25.798  1.00 12.77           O  
ANISOU  322  O   ARG A  30      259   2306   2284    -81    -74     54       O  
ATOM    323  CB  ARG A  30       4.298   1.436  28.340  1.00 14.27           C  
ANISOU  323  CB  ARG A  30      366   2533   2521   -478   -198    130       C  
ATOM    324  CG  ARG A  30       5.375   2.455  28.574  1.00 14.29           C  
ANISOU  324  CG  ARG A  30      271   2623   2533   -190     85      5       C  
ATOM    325  CD  ARG A  30       6.740   1.793  28.930  1.00 13.32           C  
ANISOU  325  CD  ARG A  30      259   2516   2282   -120     21      1       C  
ATOM    326  NE  ARG A  30       6.660   0.612  29.779  1.00 13.69           N  
ANISOU  326  NE  ARG A  30      256   2221   2725    -20    -80    -37       N  
ATOM    327  CZ  ARG A  30       6.499   0.638  31.100  1.00 13.60           C  
ANISOU  327  CZ  ARG A  30      271   2152   2743   -184      6     93       C  
ATOM    328  NH1 ARG A  30       6.420   1.765  31.763  1.00 14.33           N  
ANISOU  328  NH1 ARG A  30      277   2427   2737   -121    197    200       N  
ATOM    329  NH2 ARG A  30       6.440  -0.499  31.760  1.00 15.24           N  
ANISOU  329  NH2 ARG A  30      446   2409   2936     20    188    229       N  
ATOM    330  N   LYS A  31       1.651   0.022  27.769  1.00 11.71           N  
ANISOU  330  N   LYS A  31      257   1929   2261    -49     67     36       N  
ATOM    331  CA  LYS A  31       1.107  -1.233  27.286  1.00 12.76           C  
ANISOU  331  CA  LYS A  31      492   1970   2383   -194    -91    -66       C  
ATOM    332  C   LYS A  31       0.098  -0.950  26.146  1.00 11.78           C  
ANISOU  332  C   LYS A  31      263   1831   2380    -99     95   -115       C  
ATOM    333  O   LYS A  31       0.113  -1.654  25.167  1.00 13.05           O  
ANISOU  333  O   LYS A  31      255   2148   2553     40    -49   -241       O  
ATOM    334  CB  LYS A  31       0.333  -1.925  28.415  1.00 14.48           C  
ANISOU  334  CB  LYS A  31      892   1950   2659   -389     31     18       C  
ATOM    335  CG  LYS A  31       1.211  -2.434  29.534  1.00 17.26           C  
ANISOU  335  CG  LYS A  31     1599   2204   2754   -465    -85    125       C  
ATOM    336  CD  LYS A  31       2.172  -3.513  29.076  1.00 22.66           C  
ANISOU  336  CD  LYS A  31     2629   2877   3101     25   -289    239       C  
ATOM    337  CE  LYS A  31       3.583  -3.164  29.452  1.00 26.11           C  
ANISOU  337  CE  LYS A  31     2952   3522   3447   -406     62   -183       C  
ATOM    338  NZ  LYS A  31       4.591  -4.216  29.054  1.00 29.44           N  
ANISOU  338  NZ  LYS A  31     3674   4031   3478    218   -251    -82       N  
ATOM    339  N   VAL A  32      -0.703   0.083  26.274  1.00 11.95           N  
ANISOU  339  N   VAL A  32      276   1936   2328     50    -25    -34       N  
ATOM    340  CA  VAL A  32      -1.659   0.363  25.186  1.00 12.39           C  
ANISOU  340  CA  VAL A  32      253   2090   2363     10    -14     -7       C  
ATOM    341  C   VAL A  32      -1.067   1.021  23.915  1.00 11.80           C  
ANISOU  341  C   VAL A  32      258   2036   2189     25    100    -45       C  
ATOM    342  O   VAL A  32      -1.297   0.670  22.798  1.00 11.76           O  
ANISOU  342  O   VAL A  32      265   2149   2051   -107    113   -158       O  
ATOM    343  CB  VAL A  32      -2.846   1.214  25.767  1.00 13.07           C  
ANISOU  343  CB  VAL A  32      264   2196   2503     25   -160   -103       C  
ATOM    344  CG1 VAL A  32      -3.817   1.581  24.647  1.00 14.66           C  
ANISOU  344  CG1 VAL A  32      284   2671   2615    253   -117   -108       C  
ATOM    345  CG2 VAL A  32      -3.583   0.387  26.906  1.00 14.66           C  
ANISOU  345  CG2 VAL A  32      451   2422   2695     64    231      5       C  
ATOM    346  N   ALA A  33      -0.052   1.909  24.190  1.00 12.16           N  
ANISOU  346  N   ALA A  33      258   2122   2239    -78    -62      7       N  
ATOM    347  CA  ALA A  33       0.658   2.556  23.096  1.00 13.39           C  
ANISOU  347  CA  ALA A  33      509   2269   2308    -72    -27     67       C  
ATOM    348  C   ALA A  33       1.545   1.523  22.360  1.00 13.17           C  
ANISOU  348  C   ALA A  33      267   2396   2339   -174     -5    103       C  
ATOM    349  O   ALA A  33       1.646   1.576  21.150  1.00 14.22           O  
ANISOU  349  O   ALA A  33      253   2700   2448     -2     16     27       O  
ATOM    350  CB  ALA A  33       1.578   3.654  23.638  1.00 14.51           C  
ANISOU  350  CB  ALA A  33      294   2443   2776   -186   -254     24       C  
ATOM    351  N   GLY A  34       2.102   0.573  23.113  1.00 13.15           N  
ANISOU  351  N   GLY A  34      270   2411   2313     50    180     33       N  
ATOM    352  CA  GLY A  34       2.935  -0.435  22.478  1.00 14.14           C  
ANISOU  352  CA  GLY A  34      436   2538   2396     89     26    -47       C  
ATOM    353  C   GLY A  34       2.189  -1.400  21.607  1.00 13.31           C  
ANISOU  353  C   GLY A  34      393   2306   2356    125    144    -33       C  
ATOM    354  O   GLY A  34       2.673  -1.928  20.624  1.00 15.76           O  
ANISOU  354  O   GLY A  34      278   3011   2697     77    230   -245       O  
ATOM    355  N   MET A  35       0.901  -1.581  21.909  1.00 12.66           N  
ANISOU  355  N   MET A  35      276   2140   2390    148    162     58       N  
ATOM    356  CA  MET A  35      -0.005  -2.434  21.133  1.00 12.44           C  
ANISOU  356  CA  MET A  35      265   2071   2389     54    153    117       C  
ATOM    357  C   MET A  35      -0.513  -1.738  19.859  1.00 12.94           C  
ANISOU  357  C   MET A  35      290   2169   2455     49    282     30       C  
ATOM    358  O   MET A  35      -0.943  -2.426  18.926  1.00 14.19           O  
ANISOU  358  O   MET A  35      265   2284   2842   -127    104     69       O  
ATOM    359  CB  MET A  35      -1.232  -2.819  21.975  1.00 13.83           C  
ANISOU  359  CB  MET A  35      502   2042   2711    122    418     90       C  
ATOM    360  CG  MET A  35      -0.990  -3.954  22.922  1.00 14.91           C  
ANISOU  360  CG  MET A  35      771   2269   2624   -285    482    158       C  
ATOM    361  SD  MET A  35      -0.746  -5.519  22.162  1.00 16.24           S  
ANISOU  361  SD  MET A  35      622   2235   3313     38    167    120       S  
ATOM    362  CE  MET A  35      -2.369  -5.687  21.419  1.00 17.84           C  
ANISOU  362  CE  MET A  35      287   2861   3631   -196    264   -121       C  
ATOM    363  N   ALA A  36      -0.392  -0.438  19.778  1.00 12.85           N  
ANISOU  363  N   ALA A  36      255   2108   2518    -10     71    314       N  
ATOM    364  CA  ALA A  36      -0.921   0.297  18.618  1.00 13.52           C  
ANISOU  364  CA  ALA A  36      341   2252   2544   -192     88    265       C  
ATOM    365  C   ALA A  36      -0.212  -0.102  17.342  1.00 13.60           C  
ANISOU  365  C   ALA A  36      628   2048   2489    -52    -14    292       C  
ATOM    366  O   ALA A  36       1.021  -0.380  17.325  1.00 13.92           O  
ANISOU  366  O   ALA A  36      256   2332   2701    -80    -24    202       O  
ATOM    367  CB  ALA A  36      -0.880   1.774  18.841  1.00 15.46           C  
ANISOU  367  CB  ALA A  36      983   2266   2622    104     44    319       C  
ATOM    368  N   LYS A  37      -0.943  -0.048  16.269  1.00 13.57           N  
ANISOU  368  N   LYS A  37      374   2138   2641   -297    -63    269       N  
ATOM    369  CA  LYS A  37      -0.481  -0.321  14.927  1.00 14.23           C  
ANISOU  369  CA  LYS A  37      558   2238   2610   -267     34    128       C  
ATOM    370  C   LYS A  37      -0.846   0.884  14.053  1.00 13.16           C  
ANISOU  370  C   LYS A  37      440   2044   2514   -204     73    221       C  
ATOM    371  O   LYS A  37      -1.754   0.825  13.268  1.00 15.40           O  
ANISOU  371  O   LYS A  37      358   2585   2907   -253    -64    217       O  
ATOM    372  CB  LYS A  37      -1.101  -1.583  14.339  1.00 17.71           C  
ANISOU  372  CB  LYS A  37     1650   2389   2690   -274    -78    172       C  
ATOM    373  CG  LYS A  37      -1.139  -2.738  15.250  1.00 22.88           C  
ANISOU  373  CG  LYS A  37     2757   2852   3083   -261    -19     -1       C  
ATOM    374  CD  LYS A  37       0.152  -3.287  15.549  1.00 24.11           C  
ANISOU  374  CD  LYS A  37     2745   3113   3301    -63     30     88       C  
ATOM    375  CE  LYS A  37       0.007  -4.748  16.120  1.00 23.09           C  
ANISOU  375  CE  LYS A  37     2184   3015   3573    -80    255    -25       C  
ATOM    376  NZ  LYS A  37      -0.506  -4.826  17.536  1.00 19.67           N  
ANISOU  376  NZ  LYS A  37      849   2856   3769    131     18    242       N  
ATOM    377  N  APRO A  38      -0.161   2.012  14.170  0.50 12.56           N  
ANISOU  377  N  APRO A  38      270   2040   2461   -140    101    197       N  
ATOM    378  N  BPRO A  38      -0.165   2.006  14.263  0.50 12.92           N  
ANISOU  378  N  BPRO A  38      262   2085   2561   -102     74    187       N  
ATOM    379  CA APRO A  38      -0.574   3.212  13.454  0.50 12.28           C  
ANISOU  379  CA APRO A  38      364   2030   2269    -87    192    113       C  
ATOM    380  CA BPRO A  38      -0.539   3.253  13.702  0.50 12.67           C  
ANISOU  380  CA BPRO A  38      307   2094   2412    -66    167    153       C  
ATOM    381  C  APRO A  38      -0.530   3.168  11.921  0.50 11.80           C  
ANISOU  381  C  APRO A  38      467   1789   2227   -236    125     41       C  
ATOM    382  C  BPRO A  38      -0.267   3.357  12.265  0.50 13.51           C  
ANISOU  382  C  BPRO A  38      771   2023   2336    -97     81    128       C  
ATOM    383  O  APRO A  38       0.338   2.491  11.353  0.50 12.11           O  
ANISOU  383  O  APRO A  38      373   1891   2337   -130    152    -76       O  
ATOM    384  O  BPRO A  38       0.688   2.772  11.758  0.50 15.00           O  
ANISOU  384  O  BPRO A  38      659   2270   2770     23    368    237       O  
ATOM    385  CB APRO A  38       0.295   4.307  14.065  0.50 14.41           C  
ANISOU  385  CB APRO A  38      985   2124   2366   -101    174    110       C  
ATOM    386  CB BPRO A  38       0.295   4.259  14.483  0.50 14.37           C  
ANISOU  386  CB BPRO A  38      823   2174   2462    -21    246    109       C  
ATOM    387  CG APRO A  38       1.433   3.590  14.696  0.50 15.81           C  
ANISOU  387  CG APRO A  38      955   2365   2686   -191    -16     77       C  
ATOM    388  CG BPRO A  38       1.465   3.521  14.863  0.50 15.88           C  
ANISOU  388  CG BPRO A  38     1010   2306   2715   -204    -55     87       C  
ATOM    389  CD APRO A  38       0.954   2.253  15.095  0.50 13.31           C  
ANISOU  389  CD APRO A  38      265   2227   2565   -144    -64    156       C  
ATOM    390  CD BPRO A  38       0.993   2.153  15.156  0.50 13.70           C  
ANISOU  390  CD BPRO A  38      263   2262   2677   -139    -48    133       C  
ATOM    391  N  AASN A  39      -1.463   3.869  11.280  0.50 13.27           N  
ANISOU  391  N  AASN A  39     1104   1806   2129   -165     14    -12       N  
ATOM    392  N  BASN A  39      -1.000   4.226  11.616  0.50 11.91           N  
ANISOU  392  N  BASN A  39      551   1778   2194   -183    112     94       N  
ATOM    393  CA AASN A  39      -1.300   4.430   9.950  0.50 14.18           C  
ANISOU  393  CA AASN A  39     1402   1707   2279    -95     48    -35       C  
ATOM    394  CA BASN A  39      -0.578   4.665  10.317  0.50 12.84           C  
ANISOU  394  CA BASN A  39      922   1745   2211   -163    -69      2       C  
ATOM    395  C  AASN A  39      -0.727   5.851  10.066  0.50 13.10           C  
ANISOU  395  C  AASN A  39     1155   1626   2195    -89    380     69       C  
ATOM    396  C  BASN A  39       0.345   5.896  10.457  0.50 12.53           C  
ANISOU  396  C  BASN A  39      880   1761   2119   -123   -131    -43       C  
ATOM    397  O  AASN A  39      -1.218   6.716  10.820  0.50 17.39           O  
ANISOU  397  O  AASN A  39     2631   1653   2321   -363    701    -31       O  
ATOM    398  O  BASN A  39       0.689   6.351  11.572  0.50 15.29           O  
ANISOU  398  O  BASN A  39     1042   2303   2463     18     31    -67       O  
ATOM    399  CB AASN A  39      -2.625   4.413   9.195  0.50 14.80           C  
ANISOU  399  CB AASN A  39     1359   1799   2463    -92     -1    -84       C  
ATOM    400  CB BASN A  39      -1.782   4.870   9.381  0.50 13.08           C  
ANISOU  400  CB BASN A  39     1031   1724   2212   -104    -84     27       C  
ATOM    401  CG AASN A  39      -2.862   3.096   8.449  0.50 16.67           C  
ANISOU  401  CG AASN A  39     1120   2378   2834   -326   -429   -225       C  
ATOM    402  CG BASN A  39      -2.338   3.559   8.810  0.50 18.42           C  
ANISOU  402  CG BASN A  39     1754   2514   2729   -116   -298    -89       C  
ATOM    403  OD1AASN A  39      -3.709   3.058   7.526  0.50 21.94           O  
ANISOU  403  OD1AASN A  39      492   3584   4257   -103   -961    -92       O  
ATOM    404  OD1BASN A  39      -2.965   3.578   7.747  0.50 25.32           O  
ANISOU  404  OD1BASN A  39     2397   3682   3539   -746   -624   -121       O  
ATOM    405  ND2AASN A  39      -2.147   2.045   8.806  0.50 21.90           N  
ANISOU  405  ND2AASN A  39     2604   2810   2907   -146   -600   -285       N  
ATOM    406  ND2BASN A  39      -2.030   2.428   9.451  0.50 24.86           N  
ANISOU  406  ND2BASN A  39     3666   2650   3127    -39    -23    -40       N  
ATOM    407  N  AMET A  40       0.365   6.068   9.345  0.50 13.89           N  
ANISOU  407  N  AMET A  40     1338   1666   2272   -225    423     98       N  
ATOM    408  N  BMET A  40       0.805   6.385   9.328  0.50 12.22           N  
ANISOU  408  N  BMET A  40      693   1757   2192   -145    -37    -25       N  
ATOM    409  CA AMET A  40       1.021   7.359   9.370  0.50 14.09           C  
ANISOU  409  CA AMET A  40     1430   1648   2273   -127    284     42       C  
ATOM    410  CA BMET A  40       1.576   7.604   9.311  0.50 11.05           C  
ANISOU  410  CA BMET A  40      434   1659   2106   -156    225    -36       C  
ATOM    411  C  AMET A  40       0.913   8.020   8.000  0.50 13.44           C  
ANISOU  411  C  AMET A  40     1060   1662   2382   -186    265     22       C  
ATOM    412  C  BMET A  40       1.250   8.216   7.973  0.50 10.94           C  
ANISOU  412  C  BMET A  40      275   1650   2229   -171     53    -53       C  
ATOM    413  O  AMET A  40       1.097   7.328   6.978  0.50 13.49           O  
ANISOU  413  O  AMET A  40     1024   1513   2585   -106    385    115       O  
ATOM    414  O  BMET A  40       1.604   7.691   6.943  0.50 11.11           O  
ANISOU  414  O  BMET A  40      307   1624   2289   -258     85     91       O  
ATOM    415  CB AMET A  40       2.487   7.196   9.756  0.50 15.32           C  
ANISOU  415  CB AMET A  40     1638   1885   2296   -119    258    116       C  
ATOM    416  CB BMET A  40       3.071   7.322   9.416  0.50 11.07           C  
ANISOU  416  CB BMET A  40      343   1764   2099   -144    377    -15       C  
ATOM    417  CG AMET A  40       3.221   8.503   9.839  0.50 17.29           C  
ANISOU  417  CG AMET A  40     1948   2099   2521   -147    295     72       C  
ATOM    418  CG BMET A  40       3.921   8.579   9.554  0.50 12.42           C  
ANISOU  418  CG BMET A  40      606   1762   2351   -259    100     54       C  
ATOM    419  SD AMET A  40       4.964   8.393  10.286  0.50 22.42           S  
ANISOU  419  SD AMET A  40     2442   2566   3509   -483     97   -200       S  
ATOM    420  SD BMET A  40       5.666   8.296   9.482  0.50 14.30           S  
ANISOU  420  SD BMET A  40      383   2126   2923    -28    134     96       S  
ATOM    421  CE AMET A  40       5.522   7.017   9.243  0.50 19.16           C  
ANISOU  421  CE AMET A  40      503   3043   3731     46    665   -133       C  
ATOM    422  CE BMET A  40       5.805   7.061  10.759  0.50 15.13           C  
ANISOU  422  CE BMET A  40      412   2430   2904   -583    -13    369       C  
ATOM    423  N   ILE A  41       0.512   9.308   8.000  1.00 12.70           N  
ANISOU  423  N   ILE A  41      704   1678   2440    -73    198     15       N  
ATOM    424  CA  ILE A  41       0.184  10.036   6.770  1.00 12.32           C  
ANISOU  424  CA  ILE A  41      282   1979   2418   -222     19    -79       C  
ATOM    425  C   ILE A  41       1.113  11.268   6.713  1.00 12.33           C  
ANISOU  425  C   ILE A  41      508   1773   2402   -147     68     35       C  
ATOM    426  O   ILE A  41       1.008  12.123   7.578  1.00 14.06           O  
ANISOU  426  O   ILE A  41      887   1972   2483   -336    149    -29       O  
ATOM    427  CB  ILE A  41      -1.294  10.419   6.691  1.00 13.32           C  
ANISOU  427  CB  ILE A  41      261   2103   2695   -113     58    -85       C  
ATOM    428  CG1 ILE A  41      -2.193   9.193   6.831  1.00 17.15           C  
ANISOU  428  CG1 ILE A  41      754   2630   3131   -356     35    -95       C  
ATOM    429  CG2 ILE A  41      -1.568  11.128   5.372  1.00 16.87           C  
ANISOU  429  CG2 ILE A  41      310   2951   3148    197    -99      5       C  
ATOM    430  CD1 ILE A  41      -3.696   9.602   7.044  1.00 22.24           C  
ANISOU  430  CD1 ILE A  41      501   3889   4059   -944    106     28       C  
ATOM    431  N   ILE A  42       1.906  11.348   5.660  1.00 11.54           N  
ANISOU  431  N   ILE A  42      457   1661   2267   -175     44    -12       N  
ATOM    432  CA  ILE A  42       2.835  12.466   5.502  1.00 11.01           C  
ANISOU  432  CA  ILE A  42      272   1718   2192   -166     31    -40       C  
ATOM    433  C   ILE A  42       2.489  13.226   4.242  1.00 11.53           C  
ANISOU  433  C   ILE A  42      276   1781   2324   -186     16    -91       C  
ATOM    434  O   ILE A  42       2.369  12.639   3.182  1.00 12.36           O  
ANISOU  434  O   ILE A  42      257   1958   2480    -77    -22     28       O  
ATOM    435  CB  ILE A  42       4.288  11.994   5.472  1.00 12.03           C  
ANISOU  435  CB  ILE A  42      287   2062   2220   -132    223    -35       C  
ATOM    436  CG1 ILE A  42       4.638  11.160   6.721  1.00 12.26           C  
ANISOU  436  CG1 ILE A  42      263   1962   2433   -120     63    -37       C  
ATOM    437  CG2 ILE A  42       5.247  13.192   5.271  1.00 13.28           C  
ANISOU  437  CG2 ILE A  42      282   2188   2573   -235      7    105       C  
ATOM    438  CD1 ILE A  42       6.108  10.642   6.744  1.00 13.56           C  
ANISOU  438  CD1 ILE A  42      255   2303   2592    -40    -70    200       C  
ATOM    439  N   SER A  43       2.309  14.527   4.365  1.00 11.94           N  
ANISOU  439  N   SER A  43      296   1826   2412   -106   -183     14       N  
ATOM    440  CA  SER A  43       1.975  15.379   3.248  1.00 11.82           C  
ANISOU  440  CA  SER A  43      346   1814   2329   -136   -287    -24       C  
ATOM    441  C   SER A  43       2.765  16.664   3.316  1.00 12.52           C  
ANISOU  441  C   SER A  43      560   1855   2341     -2    -36     -8       C  
ATOM    442  O   SER A  43       3.232  17.048   4.389  1.00 12.84           O  
ANISOU  442  O   SER A  43      664   1905   2307   -214     74    -93       O  
ATOM    443  CB  SER A  43       0.497  15.636   3.194  1.00 13.29           C  
ANISOU  443  CB  SER A  43      543   1906   2599   -148   -421    146       C  
ATOM    444  OG  SER A  43       0.097  16.304   4.353  1.00 17.31           O  
ANISOU  444  OG  SER A  43      683   2827   3065    -68    -74    132       O  
ATOM    445  N   VAL A  44       2.872  17.291   2.168  1.00 13.58           N  
ANISOU  445  N   VAL A  44      862   1914   2383    -36   -234     -8       N  
ATOM    446  CA  VAL A  44       3.559  18.529   2.017  1.00 14.09           C  
ANISOU  446  CA  VAL A  44     1079   1828   2443    -71    -33     48       C  
ATOM    447  C   VAL A  44       2.701  19.525   1.254  1.00 13.88           C  
ANISOU  447  C   VAL A  44      871   1862   2540   -103   -177     -1       C  
ATOM    448  O   VAL A  44       2.107  19.180   0.244  1.00 16.97           O  
ANISOU  448  O   VAL A  44     1844   2024   2577     78   -429    -49       O  
ATOM    449  CB  VAL A  44       4.933  18.372   1.339  1.00 15.32           C  
ANISOU  449  CB  VAL A  44     1202   1997   2620    -22     27     69       C  
ATOM    450  CG1 VAL A  44       5.675  19.720   1.330  1.00 19.63           C  
ANISOU  450  CG1 VAL A  44     1702   2349   3407   -375    220    171       C  
ATOM    451  CG2 VAL A  44       5.763  17.310   2.036  1.00 16.65           C  
ANISOU  451  CG2 VAL A  44      759   2539   3026    -47      7    118       C  
ATOM    452  N   ASN A  45       2.683  20.757   1.728  1.00 12.30           N  
ANISOU  452  N   ASN A  45      329   1854   2490     -6    -95     -1       N  
ATOM    453  CA  ASN A  45       1.963  21.847   1.055  1.00 13.68           C  
ANISOU  453  CA  ASN A  45      919   1926   2349   -113   -233     14       C  
ATOM    454  C   ASN A  45       2.850  23.075   1.202  1.00 12.64           C  
ANISOU  454  C   ASN A  45      532   1942   2329    115   -118     86       C  
ATOM    455  O   ASN A  45       2.943  23.658   2.258  1.00 13.05           O  
ANISOU  455  O   ASN A  45      258   2157   2542    -73    -79     41       O  
ATOM    456  CB  ASN A  45       0.545  22.012   1.639  1.00 13.60           C  
ANISOU  456  CB  ASN A  45      889   1732   2544    -48    -92    -27       C  
ATOM    457  CG  ASN A  45      -0.296  23.027   0.921  1.00 12.39           C  
ANISOU  457  CG  ASN A  45      575   1812   2320    -91   -204    -43       C  
ATOM    458  OD1 ASN A  45      -1.569  22.868   0.855  1.00 15.26           O  
ANISOU  458  OD1 ASN A  45      409   2485   2902   -267   -183    -50       O  
ATOM    459  ND2 ASN A  45       0.250  24.076   0.496  1.00 12.70           N  
ANISOU  459  ND2 ASN A  45      349   1905   2569     11   -471     86       N  
ATOM    460  N   GLY A  46       3.478  23.445   0.104  1.00 14.61           N  
ANISOU  460  N   GLY A  46     1023   2172   2354   -151   -185     62       N  
ATOM    461  CA  GLY A  46       4.444  24.501   0.164  1.00 14.40           C  
ANISOU  461  CA  GLY A  46     1013   2098   2358   -251   -108     87       C  
ATOM    462  C   GLY A  46       5.591  24.165   1.103  1.00 13.93           C  
ANISOU  462  C   GLY A  46      644   2121   2527   -124     35     47       C  
ATOM    463  O   GLY A  46       6.187  23.105   0.977  1.00 15.62           O  
ANISOU  463  O   GLY A  46      837   2227   2870     -8     56     48       O  
ATOM    464  N   ASP A  47       5.797  25.017   2.079  1.00 14.07           N  
ANISOU  464  N   ASP A  47      676   2087   2581   -139    -38    137       N  
ATOM    465  CA  ASP A  47       6.846  24.768   3.065  1.00 14.44           C  
ANISOU  465  CA  ASP A  47      705   2195   2586    -61     21    198       C  
ATOM    466  C   ASP A  47       6.364  23.937   4.259  1.00 12.55           C  
ANISOU  466  C   ASP A  47      337   2007   2421     94    -76    208       C  
ATOM    467  O   ASP A  47       7.182  23.612   5.145  1.00 13.45           O  
ANISOU  467  O   ASP A  47      254   2266   2589     23     46    254       O  
ATOM    468  CB  ASP A  47       7.388  26.090   3.681  1.00 16.72           C  
ANISOU  468  CB  ASP A  47     1274   2450   2629   -253    -67    248       C  
ATOM    469  CG  ASP A  47       7.991  27.035   2.697  1.00 21.16           C  
ANISOU  469  CG  ASP A  47     1758   3085   3193   -491   -297    196       C  
ATOM    470  OD1 ASP A  47       8.536  26.577   1.706  1.00 24.53           O  
ANISOU  470  OD1 ASP A  47     1651   4377   3290   -736    549    397       O  
ATOM    471  OD2 ASP A  47       7.942  28.267   2.964  1.00 29.15           O  
ANISOU  471  OD2 ASP A  47     3331   3432   4309   -563   -253    528       O  
ATOM    472  N   VAL A  48       5.046  23.689   4.338  1.00 11.67           N  
ANISOU  472  N   VAL A  48      276   1803   2355     90   -178    208       N  
ATOM    473  CA  VAL A  48       4.495  23.047   5.506  1.00 11.10           C  
ANISOU  473  CA  VAL A  48      288   1828   2100    149   -186    102       C  
ATOM    474  C   VAL A  48       4.408  21.559   5.323  1.00 11.47           C  
ANISOU  474  C   VAL A  48      272   1854   2229   -132     84     91       C  
ATOM    475  O   VAL A  48       3.719  21.075   4.413  1.00 12.71           O  
ANISOU  475  O   VAL A  48      372   2058   2398     59   -185     36       O  
ATOM    476  CB  VAL A  48       3.108  23.596   5.832  1.00 11.90           C  
ANISOU  476  CB  VAL A  48      310   1911   2298    239   -189    164       C  
ATOM    477  CG1 VAL A  48       2.654  22.966   7.137  1.00 13.26           C  
ANISOU  477  CG1 VAL A  48      303   2124   2611    103    -91     53       C  
ATOM    478  CG2 VAL A  48       3.209  25.118   5.978  1.00 14.18           C  
ANISOU  478  CG2 VAL A  48      337   2358   2691    333    122    -75       C  
ATOM    479  N   ILE A  49       4.984  20.806   6.254  1.00 10.54           N  
ANISOU  479  N   ILE A  49      253   1577   2172    -27      3     29       N  
ATOM    480  CA  ILE A  49       4.913  19.381   6.293  1.00 10.79           C  
ANISOU  480  CA  ILE A  49      254   1769   2076     17    -49    -44       C  
ATOM    481  C   ILE A  49       3.879  19.010   7.395  1.00 10.94           C  
ANISOU  481  C   ILE A  49      253   1696   2207    -13    -21     60       C  
ATOM    482  O   ILE A  49       3.897  19.579   8.456  1.00 11.55           O  
ANISOU  482  O   ILE A  49      272   1837   2277   -167     68    -80       O  
ATOM    483  CB  ILE A  49       6.266  18.746   6.580  1.00 11.69           C  
ANISOU  483  CB  ILE A  49      293   1832   2315    229   -113     21       C  
ATOM    484  CG1 ILE A  49       7.290  19.125   5.461  1.00 13.09           C  
ANISOU  484  CG1 ILE A  49      260   2203   2509   -118     21      3       C  
ATOM    485  CG2 ILE A  49       6.057  17.258   6.640  1.00 12.61           C  
ANISOU  485  CG2 ILE A  49      316   2070   2405    320   -109     78       C  
ATOM    486  CD1 ILE A  49       8.757  18.763   5.831  1.00 16.31           C  
ANISOU  486  CD1 ILE A  49      260   2739   3197     58    131      8       C  
ATOM    487  N   THR A  50       3.001  18.056   7.051  1.00 11.17           N  
ANISOU  487  N   THR A  50      306   1691   2245   -232    -21    -67       N  
ATOM    488  CA  THR A  50       2.071  17.527   8.049  1.00 11.25           C  
ANISOU  488  CA  THR A  50      268   1775   2229   -146    -51      0       C  
ATOM    489  C   THR A  50       2.297  16.040   8.241  1.00 11.49           C  
ANISOU  489  C   THR A  50      277   1804   2283   -190     44   -149       C  
ATOM    490  O   THR A  50       2.411  15.311   7.259  1.00 12.47           O  
ANISOU  490  O   THR A  50      366   1998   2375   -294    -13     72       O  
ATOM    491  CB  THR A  50       0.605  17.812   7.632  1.00 11.83           C  
ANISOU  491  CB  THR A  50      289   1916   2286   -201   -136   -151       C  
ATOM    492  OG1 THR A  50       0.419  19.239   7.536  1.00 13.24           O  
ANISOU  492  OG1 THR A  50      263   2071   2695   -134    -32     79       O  
ATOM    493  CG2 THR A  50      -0.438  17.243   8.669  1.00 13.71           C  
ANISOU  493  CG2 THR A  50      264   2209   2736   -147     22     81       C  
ATOM    494  N   ILE A  51       2.377  15.599   9.500  1.00 11.29           N  
ANISOU  494  N   ILE A  51      269   1738   2282   -149     46    -96       N  
ATOM    495  CA  ILE A  51       2.501  14.201   9.843  1.00 11.39           C  
ANISOU  495  CA  ILE A  51      260   1695   2370    -65    105   -186       C  
ATOM    496  C   ILE A  51       1.295  13.869  10.721  1.00 11.53           C  
ANISOU  496  C   ILE A  51      278   1730   2370   -185     64    -59       C  
ATOM    497  O   ILE A  51       1.206  14.391  11.807  1.00 12.46           O  
ANISOU  497  O   ILE A  51      268   1925   2540   -125    129   -131       O  
ATOM    498  CB  ILE A  51       3.831  13.835  10.518  1.00 11.70           C  
ANISOU  498  CB  ILE A  51      269   1704   2473    -31    188   -185       C  
ATOM    499  CG1 ILE A  51       5.006  14.190   9.621  1.00 12.50           C  
ANISOU  499  CG1 ILE A  51      268   1675   2805     11    195   -224       C  
ATOM    500  CG2 ILE A  51       3.823  12.367  10.873  1.00 12.65           C  
ANISOU  500  CG2 ILE A  51      262   1893   2651     82    115    137       C  
ATOM    501  CD1 ILE A  51       6.393  13.962  10.252  1.00 13.70           C  
ANISOU  501  CD1 ILE A  51      267   1859   3079    131     97    -53       C  
ATOM    502  N   LYS A  52       0.446  12.955  10.238  1.00 12.39           N  
ANISOU  502  N   LYS A  52      292   1873   2542   -214    172   -139       N  
ATOM    503  CA  LYS A  52      -0.700  12.473  11.015  1.00 12.98           C  
ANISOU  503  CA  LYS A  52      322   1863   2745   -226    324   -136       C  
ATOM    504  C   LYS A  52      -0.463  11.035  11.364  1.00 13.51           C  
ANISOU  504  C   LYS A  52      537   1937   2659   -168    253   -115       C  
ATOM    505  O   LYS A  52       0.093  10.283  10.575  1.00 16.40           O  
ANISOU  505  O   LYS A  52     1458   2077   2694   -211    608   -113       O  
ATOM    506  CB  LYS A  52      -1.999  12.534  10.252  1.00 14.22           C  
ANISOU  506  CB  LYS A  52      362   2080   2960   -332    396   -183       C  
ATOM    507  CG  LYS A  52      -2.347  13.790   9.759  1.00 17.44           C  
ANISOU  507  CG  LYS A  52      612   2675   3339   -560    350     58       C  
ATOM    508  CD  LYS A  52      -3.670  13.776   9.109  1.00 20.63           C  
ANISOU  508  CD  LYS A  52     1305   2997   3534   -223     94     31       C  
ATOM    509  CE  LYS A  52      -4.046  15.115   8.519  1.00 22.02           C  
ANISOU  509  CE  LYS A  52     1210   3200   3954   -360    209    125       C  
ATOM    510  NZ  LYS A  52      -5.365  15.145   7.866  1.00 25.71           N  
ANISOU  510  NZ  LYS A  52     1017   4199   4552    -72    -85    110       N  
ATOM    511  N   SER A  53      -0.786  10.645  12.589  1.00 13.24           N  
ANISOU  511  N   SER A  53      464   1962   2604   -318    348    -44       N  
ATOM    512  CA  SER A  53      -0.751   9.281  12.975  1.00 14.07           C  
ANISOU  512  CA  SER A  53      736   1840   2767   -108    341    -20       C  
ATOM    513  C   SER A  53      -2.134   8.875  13.499  1.00 14.96           C  
ANISOU  513  C   SER A  53      987   1913   2784   -268    442    -58       C  
ATOM    514  O   SER A  53      -2.656   9.519  14.380  1.00 17.85           O  
ANISOU  514  O   SER A  53     1507   2111   3163   -464    776   -154       O  
ATOM    515  CB  SER A  53       0.261   9.049  14.076  1.00 16.03           C  
ANISOU  515  CB  SER A  53     1082   2026   2980    -32    397     50       C  
ATOM    516  OG  SER A  53       0.432   7.693  14.441  1.00 22.67           O  
ANISOU  516  OG  SER A  53     2627   2451   3533   -219    410    102       O  
ATOM    517  N   GLU A  54      -2.649   7.780  12.990  1.00 14.43           N  
ANISOU  517  N   GLU A  54      706   2030   2745   -185    478    -16       N  
ATOM    518  CA  GLU A  54      -3.933   7.318  13.410  1.00 14.11           C  
ANISOU  518  CA  GLU A  54      436   2127   2795    -12    174     97       C  
ATOM    519  C   GLU A  54      -3.835   5.939  13.972  1.00 13.19           C  
ANISOU  519  C   GLU A  54      273   2084   2652   -194    -26    132       C  
ATOM    520  O   GLU A  54      -3.315   5.047  13.306  1.00 13.81           O  
ANISOU  520  O   GLU A  54      350   2075   2821    -78    309    176       O  
ATOM    521  CB  GLU A  54      -4.916   7.317  12.232  1.00 17.29           C  
ANISOU  521  CB  GLU A  54      978   2436   3155     58     24    166       C  
ATOM    522  CG  GLU A  54      -4.979   8.609  11.457  1.00 22.26           C  
ANISOU  522  CG  GLU A  54     2128   2872   3457    119     19    244       C  
ATOM    523  CD  GLU A  54      -6.078   8.599  10.416  1.00 26.93           C  
ANISOU  523  CD  GLU A  54     2790   3683   3757    541   -334    220       C  
ATOM    524  OE1 GLU A  54      -6.085   7.684   9.542  1.00 27.59           O  
ANISOU  524  OE1 GLU A  54     2485   4137   3859     48   -306      9       O  
ATOM    525  OE2 GLU A  54      -6.937   9.505  10.481  1.00 33.22           O  
ANISOU  525  OE2 GLU A  54     3590   4451   4580    797   -290    137       O  
ATOM    526  N   SER A  55      -4.393   5.699  15.167  1.00 13.88           N  
ANISOU  526  N   SER A  55      332   2236   2705    -82    234     83       N  
ATOM    527  CA  SER A  55      -4.374   4.329  15.737  1.00 14.19           C  
ANISOU  527  CA  SER A  55      278   2205   2906    -12    198    122       C  
ATOM    528  C   SER A  55      -5.555   4.199  16.665  1.00 14.91           C  
ANISOU  528  C   SER A  55      571   2148   2943    -15    268    144       C  
ATOM    529  O   SER A  55      -6.199   5.220  16.946  1.00 15.86           O  
ANISOU  529  O   SER A  55      507   2362   3157     42    400    269       O  
ATOM    530  CB  SER A  55      -3.071   4.030  16.467  1.00 14.49           C  
ANISOU  530  CB  SER A  55      273   2119   3110    -72    219    120       C  
ATOM    531  OG  SER A  55      -3.005   4.668  17.710  1.00 17.39           O  
ANISOU  531  OG  SER A  55      852   2755   2998   -206    -25    141       O  
ATOM    532  N   THR A  56      -5.731   3.009  17.266  1.00 14.46           N  
ANISOU  532  N   THR A  56      281   2130   3081     78    210    107       N  
ATOM    533  CA  THR A  56      -6.833   2.878  18.227  1.00 13.66           C  
ANISOU  533  CA  THR A  56      280   2053   2856    101    237     42       C  
ATOM    534  C   THR A  56      -6.448   3.567  19.541  1.00 15.53           C  
ANISOU  534  C   THR A  56      749   2294   2857    -91    560     -7       C  
ATOM    535  O   THR A  56      -7.336   3.800  20.354  1.00 17.47           O  
ANISOU  535  O   THR A  56     1303   2519   2815    -79    587    103       O  
ATOM    536  CB  THR A  56      -7.123   1.378  18.565  1.00 14.75           C  
ANISOU  536  CB  THR A  56      275   2334   2996     55    235    -25       C  
ATOM    537  OG1 THR A  56      -5.904   0.759  18.936  1.00 15.49           O  
ANISOU  537  OG1 THR A  56      275   2436   3173    -36    249     47       O  
ATOM    538  CG2 THR A  56      -7.629   0.648  17.335  1.00 17.14           C  
ANISOU  538  CG2 THR A  56     1134   2367   3011   -197    288    -30       C  
ATOM    539  N   PHE A  57      -5.142   3.789  19.758  1.00 14.71           N  
ANISOU  539  N   PHE A  57      870   2080   2636    -36    495     -1       N  
ATOM    540  CA  PHE A  57      -4.641   4.441  20.990  1.00 15.30           C  
ANISOU  540  CA  PHE A  57     1042   2028   2741   -142    473     12       C  
ATOM    541  C   PHE A  57      -4.883   5.932  20.934  1.00 17.05           C  
ANISOU  541  C   PHE A  57     1409   2206   2861   -109    428    111       C  
ATOM    542  O   PHE A  57      -5.471   6.461  21.821  1.00 18.50           O  
ANISOU  542  O   PHE A  57     1127   2642   3259    -85    721    112       O  
ATOM    543  CB  PHE A  57      -3.188   4.125  21.227  1.00 16.31           C  
ANISOU  543  CB  PHE A  57     1231   2141   2822    -33    308     96       C  
ATOM    544  CG  PHE A  57      -2.487   4.960  22.285  1.00 21.31           C  
ANISOU  544  CG  PHE A  57     2546   2298   3252   -153    -63    243       C  
ATOM    545  CD1 PHE A  57      -2.899   5.006  23.600  1.00 22.71           C  
ANISOU  545  CD1 PHE A  57     2978   2355   3292   -245   -185     37       C  
ATOM    546  CD2 PHE A  57      -1.330   5.639  21.939  1.00 22.42           C  
ANISOU  546  CD2 PHE A  57     2394   2703   3421   -361   -455    179       C  
ATOM    547  CE1 PHE A  57      -2.168   5.798  24.554  1.00 25.20           C  
ANISOU  547  CE1 PHE A  57     3160   3072   3343   -272   -466     81       C  
ATOM    548  CE2 PHE A  57      -0.608   6.419  22.863  1.00 24.35           C  
ANISOU  548  CE2 PHE A  57     2930   2748   3573   -319   -589    349       C  
ATOM    549  CZ  PHE A  57      -1.048   6.504  24.160  1.00 24.78           C  
ANISOU  549  CZ  PHE A  57     3253   2814   3346    -65   -537     93       C  
ATOM    550  N   LYS A  58      -4.403   6.621  19.918  1.00 16.74           N  
ANISOU  550  N   LYS A  58      998   2293   3069   -213    433     91       N  
ATOM    551  CA  LYS A  58      -4.487   8.042  19.867  1.00 15.91           C  
ANISOU  551  CA  LYS A  58      674   2273   3098    172    459    164       C  
ATOM    552  C   LYS A  58      -4.328   8.425  18.411  1.00 16.24           C  
ANISOU  552  C   LYS A  58      922   2211   3037     39    552    222       C  
ATOM    553  O   LYS A  58      -3.624   7.751  17.630  1.00 19.31           O  
ANISOU  553  O   LYS A  58     1509   2386   3439    204    823    180       O  
ATOM    554  CB  LYS A  58      -3.337   8.682  20.671  1.00 18.59           C  
ANISOU  554  CB  LYS A  58     1327   2376   3358   -212    373    164       C  
ATOM    555  CG  LYS A  58      -3.422  10.205  20.930  1.00 24.36           C  
ANISOU  555  CG  LYS A  58     2613   2924   3717     48    128    210       C  
ATOM    556  CD  LYS A  58      -4.542  10.624  21.874  1.00 28.36           C  
ANISOU  556  CD  LYS A  58     3242   3591   3941   -160    165     19       C  
ATOM    557  CE  LYS A  58      -4.707  12.158  21.900  1.00 31.66           C  
ANISOU  557  CE  LYS A  58     3953   3889   4187    -16     31     27       C  
ATOM    558  NZ  LYS A  58      -5.210  12.768  20.600  1.00 34.46           N  
ANISOU  558  NZ  LYS A  58     4403   4327   4361    100     76    184       N  
ATOM    559  N   ASN A  59      -4.922   9.517  18.057  1.00 15.70           N  
ANISOU  559  N   ASN A  59      979   2001   2984     10    603     31       N  
ATOM    560  CA  ASN A  59      -4.740  10.168  16.760  1.00 15.13           C  
ANISOU  560  CA  ASN A  59      839   1953   2956      0    599     39       C  
ATOM    561  C   ASN A  59      -3.993  11.467  17.025  1.00 16.13           C  
ANISOU  561  C   ASN A  59     1152   1985   2992    -80    671    -69       C  
ATOM    562  O   ASN A  59      -4.344  12.237  17.920  1.00 18.79           O  
ANISOU  562  O   ASN A  59     1330   2338   3469   -331    976   -266       O  
ATOM    563  CB  ASN A  59      -6.092  10.407  16.096  1.00 17.02           C  
ANISOU  563  CB  ASN A  59     1166   2246   3051      4    527    104       C  
ATOM    564  CG  ASN A  59      -6.844   9.159  15.882  1.00 16.33           C  
ANISOU  564  CG  ASN A  59      435   2576   3191    107     -6    164       C  
ATOM    565  OD1 ASN A  59      -6.356   8.136  15.486  1.00 17.64           O  
ANISOU  565  OD1 ASN A  59      368   2676   3655     95    401    219       O  
ATOM    566  ND2 ASN A  59      -8.153   9.238  16.188  1.00 22.32           N  
ANISOU  566  ND2 ASN A  59      268   3712   4498   -104    113    341       N  
ATOM    567  N   THR A  60      -2.881  11.658  16.324  1.00 13.93           N  
ANISOU  567  N   THR A  60      678   1959   2655   -134    497     37       N  
ATOM    568  CA  THR A  60      -2.075  12.874  16.458  1.00 14.09           C  
ANISOU  568  CA  THR A  60      824   1913   2615     40    332     69       C  
ATOM    569  C   THR A  60      -1.918  13.514  15.096  1.00 12.39           C  
ANISOU  569  C   THR A  60      434   1837   2437   -112    262    -54       C  
ATOM    570  O   THR A  60      -1.969  12.846  14.084  1.00 13.51           O  
ANISOU  570  O   THR A  60      487   2040   2604   -321    312      9       O  
ATOM    571  CB  THR A  60      -0.728  12.623  17.095  1.00 14.68           C  
ANISOU  571  CB  THR A  60      697   2209   2669    187    123    125       C  
ATOM    572  OG1 THR A  60       0.094  11.794  16.270  1.00 16.26           O  
ANISOU  572  OG1 THR A  60      572   2334   3271    209    143    254       O  
ATOM    573  CG2 THR A  60      -0.901  11.996  18.458  1.00 18.43           C  
ANISOU  573  CG2 THR A  60     1049   2919   3034    153    139    295       C  
ATOM    574  N   GLU A  61      -1.581  14.803  15.127  1.00 12.42           N  
ANISOU  574  N   GLU A  61      412   1747   2559    -41    169    -15       N  
ATOM    575  CA  GLU A  61      -1.330  15.529  13.908  1.00 12.71           C  
ANISOU  575  CA  GLU A  61      308   1947   2573   -149    313    -25       C  
ATOM    576  C   GLU A  61      -0.377  16.644  14.271  1.00 13.37           C  
ANISOU  576  C   GLU A  61      593   1890   2596   -280    360    -40       C  
ATOM    577  O   GLU A  61      -0.635  17.420  15.195  1.00 14.85           O  
ANISOU  577  O   GLU A  61      847   1975   2817   -285    483   -108       O  
ATOM    578  CB  GLU A  61      -2.627  16.093  13.314  1.00 14.65           C  
ANISOU  578  CB  GLU A  61      399   2223   2944     35     66     99       C  
ATOM    579  CG  GLU A  61      -2.375  16.940  12.081  1.00 19.14           C  
ANISOU  579  CG  GLU A  61     1138   2837   3296   -192   -167    446       C  
ATOM    580  CD  GLU A  61      -3.668  17.483  11.460  1.00 23.06           C  
ANISOU  580  CD  GLU A  61      706   3670   4384   -116   -215    775       C  
ATOM    581  OE1 GLU A  61      -3.604  18.558  10.856  1.00 26.79           O  
ANISOU  581  OE1 GLU A  61     1079   4450   4650   -581   -328   1413       O  
ATOM    582  OE2 GLU A  61      -4.746  16.894  11.625  1.00 28.82           O  
ANISOU  582  OE2 GLU A  61     1108   4910   4931   -776   -125    654       O  
ATOM    583  N   ILE A  62       0.735  16.766  13.539  1.00 11.91           N  
ANISOU  583  N   ILE A  62      295   1696   2534   -223    130     34       N  
ATOM    584  CA  ILE A  62       1.642  17.911  13.649  1.00 11.97           C  
ANISOU  584  CA  ILE A  62      466   1677   2402   -179    -39    -47       C  
ATOM    585  C   ILE A  62       1.861  18.539  12.286  1.00 11.00           C  
ANISOU  585  C   ILE A  62      259   1704   2214    -80    -48    -89       C  
ATOM    586  O   ILE A  62       1.944  17.829  11.296  1.00 12.63           O  
ANISOU  586  O   ILE A  62      343   1849   2605   -342     21    -35       O  
ATOM    587  CB  ILE A  62       3.022  17.553  14.335  1.00 12.61           C  
ANISOU  587  CB  ILE A  62      401   1739   2649   -284   -148   -139       C  
ATOM    588  CG1 ILE A  62       3.747  16.463  13.578  1.00 12.78           C  
ANISOU  588  CG1 ILE A  62      326   1964   2566   -353    -14     41       C  
ATOM    589  CG2 ILE A  62       2.765  17.096  15.768  1.00 14.97           C  
ANISOU  589  CG2 ILE A  62      773   2134   2779    -45   -285     72       C  
ATOM    590  CD1 ILE A  62       5.165  16.255  14.036  1.00 14.29           C  
ANISOU  590  CD1 ILE A  62      303   2368   2758   -312   -108     80       C  
ATOM    591  N   SER A  63       1.970  19.849  12.236  1.00 10.52           N  
ANISOU  591  N   SER A  63      256   1651   2089     40    -57      7       N  
ATOM    592  CA  SER A  63       2.330  20.567  11.053  1.00 11.08           C  
ANISOU  592  CA  SER A  63      282   1710   2215    -49   -234     20       C  
ATOM    593  C   SER A  63       3.472  21.504  11.428  1.00 11.10           C  
ANISOU  593  C   SER A  63      263   1717   2237    -93     82     60       C  
ATOM    594  O   SER A  63       3.489  22.071  12.477  1.00 11.74           O  
ANISOU  594  O   SER A  63      269   1904   2287   -125    126    -95       O  
ATOM    595  CB  SER A  63       1.189  21.379  10.423  1.00 11.74           C  
ANISOU  595  CB  SER A  63      253   1969   2238    -12     20    142       C  
ATOM    596  OG  SER A  63       0.138  20.544   9.940  1.00 13.73           O  
ANISOU  596  OG  SER A  63      271   2193   2749   -151   -135     65       O  
ATOM    597  N   PHE A  64       4.442  21.634  10.502  1.00 11.07           N  
ANISOU  597  N   PHE A  64      258   1795   2152    -63    -70     47       N  
ATOM    598  CA  PHE A  64       5.706  22.324  10.795  1.00 10.73           C  
ANISOU  598  CA  PHE A  64      266   1787   2021    -85   -116    -54       C  
ATOM    599  C   PHE A  64       6.360  22.703   9.484  1.00 10.27           C  
ANISOU  599  C   PHE A  64      257   1598   2047     75     22    -42       C  
ATOM    600  O   PHE A  64       6.182  22.184   8.443  1.00 11.00           O  
ANISOU  600  O   PHE A  64      253   1821   2104     -7     20     -6       O  
ATOM    601  CB  PHE A  64       6.601  21.451  11.721  1.00 11.01           C  
ANISOU  601  CB  PHE A  64      271   1721   2189   -102   -147      1       C  
ATOM    602  CG  PHE A  64       6.913  20.151  11.127  1.00 11.83           C  
ANISOU  602  CG  PHE A  64      285   1786   2423   -195   -118    -25       C  
ATOM    603  CD1 PHE A  64       6.054  19.056  11.287  1.00 11.74           C  
ANISOU  603  CD1 PHE A  64      305   1790   2365    -18   -330      6       C  
ATOM    604  CD2 PHE A  64       8.056  19.992  10.362  1.00 12.30           C  
ANISOU  604  CD2 PHE A  64      284   1987   2402    224    -68    -10       C  
ATOM    605  CE1 PHE A  64       6.279  17.881  10.667  1.00 12.67           C  
ANISOU  605  CE1 PHE A  64      319   1856   2638   -107   -382    100       C  
ATOM    606  CE2 PHE A  64       8.266  18.784   9.750  1.00 12.42           C  
ANISOU  606  CE2 PHE A  64      258   2175   2284     94     23     96       C  
ATOM    607  CZ  PHE A  64       7.448  17.733   9.937  1.00 12.83           C  
ANISOU  607  CZ  PHE A  64      325   1861   2689    107   -399    -32       C  
ATOM    608  N   ILE A  65       7.334  23.624   9.717  1.00 10.92           N  
ANISOU  608  N   ILE A  65      262   1773   2114    -78    -93    -95       N  
ATOM    609  CA  ILE A  65       8.322  24.074   8.699  1.00 10.64           C  
ANISOU  609  CA  ILE A  65      268   1581   2192     60    148   -153       C  
ATOM    610  C   ILE A  65       9.726  23.635   9.176  1.00 10.34           C  
ANISOU  610  C   ILE A  65      284   1493   2152    -32    243   -153       C  
ATOM    611  O   ILE A  65       9.981  23.696  10.360  1.00 10.43           O  
ANISOU  611  O   ILE A  65      266   1571   2123    -32    151    -69       O  
ATOM    612  CB  ILE A  65       8.216  25.549   8.480  1.00 11.47           C  
ANISOU  612  CB  ILE A  65      285   1741   2330   -113    226    -92       C  
ATOM    613  CG1 ILE A  65       6.803  25.899   7.937  1.00 12.61           C  
ANISOU  613  CG1 ILE A  65      273   1946   2570    -94   -190     87       C  
ATOM    614  CG2 ILE A  65       9.356  26.064   7.560  1.00 12.26           C  
ANISOU  614  CG2 ILE A  65      262   1729   2665     -5    149     81       C  
ATOM    615  CD1 ILE A  65       6.613  27.375   7.811  1.00 15.44           C  
ANISOU  615  CD1 ILE A  65      303   2096   3466     21   -401     13       C  
ATOM    616  N   LEU A  66      10.443  22.980   8.255  1.00 10.20           N  
ANISOU  616  N   LEU A  66      263   1599   2012   -106    -36   -159       N  
ATOM    617  CA  LEU A  66      11.787  22.499   8.592  1.00 10.62           C  
ANISOU  617  CA  LEU A  66      267   1550   2216     22   -164    -63       C  
ATOM    618  C   LEU A  66      12.636  23.615   9.244  1.00 10.13           C  
ANISOU  618  C   LEU A  66      264   1507   2076     -4    143     26       C  
ATOM    619  O   LEU A  66      12.656  24.703   8.811  1.00 11.24           O  
ANISOU  619  O   LEU A  66      254   1598   2419      1    -43    107       O  
ATOM    620  CB  LEU A  66      12.483  21.912   7.383  1.00 11.79           C  
ANISOU  620  CB  LEU A  66      253   1872   2351     10     29    -90       C  
ATOM    621  CG  LEU A  66      11.862  20.680   6.756  1.00 12.71           C  
ANISOU  621  CG  LEU A  66      298   1877   2652    269    -22   -180       C  
ATOM    622  CD1 LEU A  66      12.401  20.380   5.361  1.00 16.45           C  
ANISOU  622  CD1 LEU A  66     1014   2350   2884    122    125   -327       C  
ATOM    623  CD2 LEU A  66      11.869  19.473   7.689  1.00 13.92           C  
ANISOU  623  CD2 LEU A  66      413   1912   2963    146    -91   -150       C  
ATOM    624  N   GLY A  67      13.229  23.239  10.363  1.00 10.26           N  
ANISOU  624  N   GLY A  67      255   1480   2161    -14     62     77       N  
ATOM    625  CA  GLY A  67      14.100  24.125  11.088  1.00 10.94           C  
ANISOU  625  CA  GLY A  67      295   1628   2231   -240     37    -73       C  
ATOM    626  C   GLY A  67      13.470  25.084  12.068  1.00 10.35           C  
ANISOU  626  C   GLY A  67      263   1465   2202   -111     32   -122       C  
ATOM    627  O   GLY A  67      14.139  25.829  12.775  1.00 11.24           O  
ANISOU  627  O   GLY A  67      262   1642   2364   -111     -9   -192       O  
ATOM    628  N   GLN A  68      12.114  25.055  12.118  1.00 10.64           N  
ANISOU  628  N   GLN A  68      278   1542   2223   -178     -6    -93       N  
ATOM    629  CA  GLN A  68      11.345  26.085  12.859  1.00 10.86           C  
ANISOU  629  CA  GLN A  68      269   1676   2180    -65   -157    -37       C  
ATOM    630  C   GLN A  68      10.656  25.397  14.023  1.00 10.86           C  
ANISOU  630  C   GLN A  68      262   1614   2248     -7      3     36       C  
ATOM    631  O   GLN A  68       9.673  24.602  13.830  1.00 11.00           O  
ANISOU  631  O   GLN A  68      253   1622   2303     -7      6    -73       O  
ATOM    632  CB  GLN A  68      10.392  26.821  11.914  1.00 11.26           C  
ANISOU  632  CB  GLN A  68      262   1661   2352      1   -135   -139       C  
ATOM    633  CG  GLN A  68      11.205  27.459  10.770  1.00 12.07           C  
ANISOU  633  CG  GLN A  68      327   1731   2526   -104    -28     58       C  
ATOM    634  CD  GLN A  68      10.526  28.492   9.924  1.00 13.37           C  
ANISOU  634  CD  GLN A  68      265   1989   2827     50   -167   -121       C  
ATOM    635  OE1 GLN A  68       9.329  28.812  10.090  1.00 15.17           O  
ANISOU  635  OE1 GLN A  68      256   2304   3201     45    -70     54       O  
ATOM    636  NE2 GLN A  68      11.298  29.015   8.954  1.00 13.55           N  
ANISOU  636  NE2 GLN A  68      585   1859   2704   -164   -229    209       N  
ATOM    637  N  AGLU A  69      10.990  25.731  15.238  0.50 10.53           N  
ANISOU  637  N  AGLU A  69      254   1504   2241    -29    -36    -13       N  
ATOM    638  N  BGLU A  69      10.993  25.747  15.241  0.50 11.00           N  
ANISOU  638  N  BGLU A  69      254   1626   2298    -29    -28    -62       N  
ATOM    639  CA AGLU A  69      10.520  24.974  16.360  0.50 10.40           C  
ANISOU  639  CA AGLU A  69      265   1517   2170     69   -125     34       C  
ATOM    640  CA BGLU A  69      10.550  25.094  16.461  0.50 10.88           C  
ANISOU  640  CA BGLU A  69      260   1634   2239     65    -96    -57       C  
ATOM    641  C  AGLU A  69       9.024  25.223  16.586  0.50 10.58           C  
ANISOU  641  C  AGLU A  69      318   1468   2231     96    -37     47       C  
ATOM    642  C  BGLU A  69       9.031  25.238  16.614  0.50 10.93           C  
ANISOU  642  C  BGLU A  69      335   1541   2276     97      0     -3       C  
ATOM    643  O  AGLU A  69       8.496  26.308  16.246  0.50 11.75           O  
ANISOU  643  O  AGLU A  69      258   1698   2508     30    103     34       O  
ATOM    644  O  BGLU A  69       8.487  26.301  16.252  0.50 11.43           O  
ANISOU  644  O  BGLU A  69      260   1637   2445     38    110    -27       O  
ATOM    645  CB AGLU A  69      11.292  25.269  17.644  0.50 10.88           C  
ANISOU  645  CB AGLU A  69      380   1524   2228    -30     33    127       C  
ATOM    646  CB BGLU A  69      11.236  25.757  17.688  0.50 11.92           C  
ANISOU  646  CB BGLU A  69      316   1826   2383    -19     43   -153       C  
ATOM    647  CG AGLU A  69      11.201  26.686  18.081  0.50 10.86           C  
ANISOU  647  CG AGLU A  69      254   1559   2313    -30     -9   -134       C  
ATOM    648  CG BGLU A  69      11.195  24.979  19.021  0.50 15.58           C  
ANISOU  648  CG BGLU A  69     1085   2182   2649   -171   -116    -55       C  
ATOM    649  CD AGLU A  69      11.927  26.922  19.401  0.50 13.21           C  
ANISOU  649  CD AGLU A  69      284   1981   2753     16   -279   -358       C  
ATOM    650  CD BGLU A  69      12.417  25.271  19.945  0.50 20.53           C  
ANISOU  650  CD BGLU A  69     1571   3006   3222   -634     24     80       C  
ATOM    651  OE1AGLU A  69      11.634  27.895  20.093  0.50 15.26           O  
ANISOU  651  OE1AGLU A  69      301   2362   3133    119   -361   -390       O  
ATOM    652  OE1BGLU A  69      12.911  26.415  19.887  0.50 26.68           O  
ANISOU  652  OE1BGLU A  69     2825   3270   4041   -574   -358    -93       O  
ATOM    653  OE2AGLU A  69      12.891  26.163  19.682  0.50 18.42           O  
ANISOU  653  OE2AGLU A  69     1101   2363   3534      7   -836   -492       O  
ATOM    654  OE2BGLU A  69      12.935  24.365  20.661  0.50 24.91           O  
ANISOU  654  OE2BGLU A  69     2470   3750   3242   -870    207    324       O  
ATOM    655  N  APHE A  70       8.426  24.255  17.265  0.50 10.80           N  
ANISOU  655  N  APHE A  70      270   1578   2252    152     13     74       N  
ATOM    656  N  BPHE A  70       8.430  24.250  17.273  0.50 10.84           N  
ANISOU  656  N  BPHE A  70      270   1592   2254    152     18     52       N  
ATOM    657  CA APHE A  70       7.001  24.315  17.563  0.50 11.01           C  
ANISOU  657  CA APHE A  70      273   1621   2290    154     76     52       C  
ATOM    658  CA BPHE A  70       6.996  24.302  17.588  0.50 10.96           C  
ANISOU  658  CA BPHE A  70      272   1616   2275    148     77     44       C  
ATOM    659  C  APHE A  70       6.773  23.588  18.853  0.50 11.88           C  
ANISOU  659  C  APHE A  70      269   1870   2376    150    -61     17       C  
ATOM    660  C  BPHE A  70       6.803  23.574  18.907  0.50 11.61           C  
ANISOU  660  C  BPHE A  70      269   1818   2322    130   -102      3       C  
ATOM    661  O  APHE A  70       7.612  22.819  19.352  0.50 13.19           O  
ANISOU  661  O  APHE A  70      350   2127   2532    311    266    191       O  
ATOM    662  O  BPHE A  70       7.647  22.778  19.334  0.50 13.18           O  
ANISOU  662  O  BPHE A  70      382   2111   2515    303    203    172       O  
ATOM    663  CB APHE A  70       6.200  23.739  16.387  0.50 11.48           C  
ANISOU  663  CB APHE A  70      265   1766   2330    -41    147    100       C  
ATOM    664  CB BPHE A  70       6.193  23.734  16.404  0.50 11.47           C  
ANISOU  664  CB BPHE A  70      264   1763   2328    -47    138     92       C  
ATOM    665  CG  PHE A  70       6.465  22.309  16.063  1.00 11.64           C  
ANISOU  665  CG  PHE A  70      267   1655   2497     81    151     45       C  
ATOM    666  CD1 PHE A  70       5.718  21.254  16.583  1.00 12.18           C  
ANISOU  666  CD1 PHE A  70      557   1552   2520    -25    139     34       C  
ATOM    667  CD2 PHE A  70       7.576  21.984  15.184  1.00 10.99           C  
ANISOU  667  CD2 PHE A  70      255   1468   2453     39     31     17       C  
ATOM    668  CE1 PHE A  70       5.980  19.964  16.236  1.00 13.29           C  
ANISOU  668  CE1 PHE A  70      444   1915   2689   -108    -12    -76       C  
ATOM    669  CE2 PHE A  70       7.791  20.699  14.854  1.00 12.17           C  
ANISOU  669  CE2 PHE A  70      280   1880   2461   -173   -135      5       C  
ATOM    670  CZ  PHE A  70       7.034  19.671  15.368  1.00 12.83           C  
ANISOU  670  CZ  PHE A  70      507   1753   2614    352    -81    122       C  
ATOM    671  N  AASP A  71       5.572  23.858  19.364  0.50 12.59           N  
ANISOU  671  N  AASP A  71      300   1819   2664    162    291    195       N  
ATOM    672  N  BASP A  71       5.688  23.901  19.569  0.50 12.34           N  
ANISOU  672  N  BASP A  71      463   1666   2561    114    242    143       N  
ATOM    673  CA AASP A  71       5.087  23.194  20.574  0.50 13.48           C  
ANISOU  673  CA AASP A  71      428   2038   2653    209    281    125       C  
ATOM    674  CA BASP A  71       5.291  23.172  20.785  0.50 11.86           C  
ANISOU  674  CA BASP A  71      263   1796   2447    120     46     85       C  
ATOM    675  C  AASP A  71       4.319  21.949  20.171  0.50 13.86           C  
ANISOU  675  C  AASP A  71      512   2092   2661     99    187    179       C  
ATOM    676  C  BASP A  71       4.308  22.039  20.334  0.50 12.61           C  
ANISOU  676  C  BASP A  71      389   1896   2505     20    117    146       C  
ATOM    677  O  AASP A  71       3.523  21.980  19.229  0.50 16.13           O  
ANISOU  677  O  AASP A  71      786   2240   3102    187     46    381       O  
ATOM    678  O  BASP A  71       3.416  22.222  19.504  0.50 14.09           O  
ANISOU  678  O  BASP A  71      437   1981   2935    109    -29    344       O  
ATOM    679  CB AASP A  71       4.068  24.065  21.302  0.50 14.75           C  
ANISOU  679  CB AASP A  71      757   2221   2627    319    407     83       C  
ATOM    680  CB BASP A  71       4.669  24.096  21.853  0.50 12.14           C  
ANISOU  680  CB BASP A  71      657   1643   2310     44    -43    109       C  
ATOM    681  CG AASP A  71       4.687  25.237  21.967  0.50 18.53           C  
ANISOU  681  CG AASP A  71     1686   2335   3017    211    347     24       C  
ATOM    682  CG BASP A  71       5.595  25.088  22.406  0.50 12.38           C  
ANISOU  682  CG BASP A  71      285   1861   2555    209   -118   -138       C  
ATOM    683  OD1AASP A  71       5.683  25.080  22.703  0.50 23.49           O  
ANISOU  683  OD1AASP A  71     2326   3214   3383    505    130    108       O  
ATOM    684  OD1BASP A  71       6.692  24.689  22.845  0.50 15.06           O  
ANISOU  684  OD1BASP A  71      765   2089   2868    755   -379     14       O  
ATOM    685  OD2AASP A  71       4.130  26.332  21.741  0.50 22.29           O  
ANISOU  685  OD2AASP A  71     2375   2568   3525    560    485    155       O  
ATOM    686  OD2BASP A  71       5.237  26.278  22.502  0.50 12.52           O  
ANISOU  686  OD2BASP A  71      645   1530   2581    169   -563     47       O  
ATOM    687  N   GLU A  72       4.522  20.859  20.891  1.00 12.75           N  
ANISOU  687  N   GLU A  72      328   1933   2582    138    232    208       N  
ATOM    688  CA  GLU A  72       3.831  19.606  20.557  1.00 14.37           C  
ANISOU  688  CA  GLU A  72      646   2176   2636    157    114    366       C  
ATOM    689  C   GLU A  72       3.374  18.930  21.835  1.00 14.01           C  
ANISOU  689  C   GLU A  72      366   2308   2649    190    129    302       C  
ATOM    690  O   GLU A  72       4.014  19.023  22.855  1.00 15.39           O  
ANISOU  690  O   GLU A  72      805   2333   2708    -29    376    350       O  
ATOM    691  CB  GLU A  72       4.887  18.674  19.845  1.00 14.62           C  
ANISOU  691  CB  GLU A  72      516   2270   2768    116     93    209       C  
ATOM    692  CG  GLU A  72       4.389  17.272  19.484  1.00 16.03           C  
ANISOU  692  CG  GLU A  72      524   2658   2908    228    189    383       C  
ATOM    693  CD  GLU A  72       5.372  16.402  18.833  1.00 15.25           C  
ANISOU  693  CD  GLU A  72      725   2414   2655     57    249    172       C  
ATOM    694  OE1 GLU A  72       6.565  16.717  18.754  1.00 15.70           O  
ANISOU  694  OE1 GLU A  72      471   2374   3117     98    471    -47       O  
ATOM    695  OE2 GLU A  72       4.969  15.276  18.420  1.00 19.55           O  
ANISOU  695  OE2 GLU A  72     1205   2862   3362   -469   -164     26       O  
ATOM    696  N   VAL A  73       2.145  18.389  21.815  1.00 13.60           N  
ANISOU  696  N   VAL A  73      285   2229   2652    242    114    330       N  
ATOM    697  CA  VAL A  73       1.717  17.521  22.871  1.00 13.67           C  
ANISOU  697  CA  VAL A  73      276   2149   2767    152    190    267       C  
ATOM    698  C   VAL A  73       1.749  16.104  22.321  1.00 14.05           C  
ANISOU  698  C   VAL A  73      444   2179   2712    116    130    180       C  
ATOM    699  O   VAL A  73       1.105  15.777  21.337  1.00 15.65           O  
ANISOU  699  O   VAL A  73      593   2394   2957     -7     50    338       O  
ATOM    700  CB  VAL A  73       0.294  17.835  23.331  1.00 15.45           C  
ANISOU  700  CB  VAL A  73      632   2368   2869    -17    309    208       C  
ATOM    701  CG1 VAL A  73      -0.121  16.805  24.408  1.00 18.31           C  
ANISOU  701  CG1 VAL A  73      584   2856   3517    225    708    280       C  
ATOM    702  CG2 VAL A  73       0.182  19.199  23.871  1.00 17.87           C  
ANISOU  702  CG2 VAL A  73      694   2507   3586    168    251    220       C  
ATOM    703  N   THR A  74       2.629  15.282  22.873  1.00 13.83           N  
ANISOU  703  N   THR A  74      258   2158   2837     99      5    212       N  
ATOM    704  CA  THR A  74       2.839  13.967  22.312  1.00 13.94           C  
ANISOU  704  CA  THR A  74      265   2195   2835     15    178    165       C  
ATOM    705  C   THR A  74       1.746  12.977  22.695  1.00 14.99           C  
ANISOU  705  C   THR A  74      469   2254   2973     73     59    168       C  
ATOM    706  O   THR A  74       0.887  13.264  23.516  1.00 16.26           O  
ANISOU  706  O   THR A  74      446   2407   3325     82    306    334       O  
ATOM    707  CB  THR A  74       4.166  13.415  22.798  1.00 14.97           C  
ANISOU  707  CB  THR A  74      454   2308   2923     19    212     53       C  
ATOM    708  OG1 THR A  74       4.126  13.185  24.220  1.00 15.25           O  
ANISOU  708  OG1 THR A  74      454   2273   3063     63    170    214       O  
ATOM    709  CG2 THR A  74       5.346  14.340  22.455  1.00 14.99           C  
ANISOU  709  CG2 THR A  74      285   2482   2927    267     73    359       C  
ATOM    710  N   ALA A  75       1.772  11.804  22.053  1.00 15.07           N  
ANISOU  710  N   ALA A  75      535   2166   3022    -74    -97    146       N  
ATOM    711  CA  ALA A  75       0.684  10.854  22.231  1.00 16.04           C  
ANISOU  711  CA  ALA A  75      605   2390   3098    -25    -59    145       C  
ATOM    712  C   ALA A  75       0.579  10.421  23.694  1.00 16.40           C  
ANISOU  712  C   ALA A  75      653   2425   3151    -75     12    150       C  
ATOM    713  O   ALA A  75      -0.516  10.103  24.144  1.00 19.12           O  
ANISOU  713  O   ALA A  75      927   2788   3548   -189     77    313       O  
ATOM    714  CB  ALA A  75       0.863   9.642  21.370  1.00 18.49           C  
ANISOU  714  CB  ALA A  75     1381   2389   3254   -250   -207    128       C  
ATOM    715  N   ASP A  76       1.735  10.301  24.349  1.00 16.69           N  
ANISOU  715  N   ASP A  76      967   2347   3024    -65    140    235       N  
ATOM    716  CA  ASP A  76       1.839  10.028  25.794  1.00 17.00           C  
ANISOU  716  CA  ASP A  76     1060   2499   2899    -66     90    199       C  
ATOM    717  C   ASP A  76       1.642  11.211  26.740  1.00 17.53           C  
ANISOU  717  C   ASP A  76     1236   2532   2891    -87    249    254       C  
ATOM    718  O   ASP A  76       1.868  11.123  27.938  1.00 20.47           O  
ANISOU  718  O   ASP A  76     1935   2908   2934    221    407    341       O  
ATOM    719  CB  ASP A  76       3.137   9.318  26.109  1.00 16.34           C  
ANISOU  719  CB  ASP A  76      881   2442   2884    -70    188    263       C  
ATOM    720  CG  ASP A  76       4.358  10.123  25.787  1.00 16.17           C  
ANISOU  720  CG  ASP A  76     1200   2246   2697    -17     79    133       C  
ATOM    721  OD1 ASP A  76       4.481  10.600  24.647  1.00 16.50           O  
ANISOU  721  OD1 ASP A  76      684   2482   3102    266     28    331       O  
ATOM    722  OD2 ASP A  76       5.178  10.284  26.694  1.00 17.98           O  
ANISOU  722  OD2 ASP A  76     1715   2324   2791    -19     75    196       O  
ATOM    723  N   ASP A  77       1.242  12.334  26.176  1.00 16.35           N  
ANISOU  723  N   ASP A  77      790   2525   2897     -5    436    335       N  
ATOM    724  CA  ASP A  77       0.902  13.555  26.903  1.00 18.47           C  
ANISOU  724  CA  ASP A  77     1187   2809   3019   -114    359    163       C  
ATOM    725  C   ASP A  77       2.083  14.328  27.538  1.00 17.19           C  
ANISOU  725  C   ASP A  77      973   2674   2882    -18    422    133       C  
ATOM    726  O   ASP A  77       1.928  14.979  28.559  1.00 20.27           O  
ANISOU  726  O   ASP A  77     1030   3397   3271   -126    675   -111       O  
ATOM    727  CB  ASP A  77      -0.204  13.241  27.932  1.00 18.77           C  
ANISOU  727  CB  ASP A  77      883   3042   3204   -145    377    187       C  
ATOM    728  CG  ASP A  77      -1.126  14.433  28.184  1.00 24.94           C  
ANISOU  728  CG  ASP A  77     2171   3666   3636    168    447    353       C  
ATOM    729  OD1 ASP A  77      -1.733  14.452  29.269  1.00 30.37           O  
ANISOU  729  OD1 ASP A  77     2928   4681   3930     58    594    242       O  
ATOM    730  OD2 ASP A  77      -1.225  15.368  27.336  1.00 30.69           O  
ANISOU  730  OD2 ASP A  77     2855   4376   4429    383    656    912       O  
ATOM    731  N   ARG A  78       3.267  14.299  26.917  1.00 15.78           N  
ANISOU  731  N   ARG A  78      763   2474   2757     44    421    176       N  
ATOM    732  CA  ARG A  78       4.342  15.238  27.235  1.00 14.71           C  
ANISOU  732  CA  ARG A  78      899   2180   2509     98    337    213       C  
ATOM    733  C   ARG A  78       4.121  16.521  26.432  1.00 14.38           C  
ANISOU  733  C   ARG A  78      812   2121   2530    118    511     89       C  
ATOM    734  O   ARG A  78       3.690  16.470  25.276  1.00 15.74           O  
ANISOU  734  O   ARG A  78     1166   2161   2653    245    234    108       O  
ATOM    735  CB  ARG A  78       5.682  14.642  26.882  1.00 14.07           C  
ANISOU  735  CB  ARG A  78      574   2171   2598     67    268    181       C  
ATOM    736  CG  ARG A  78       6.181  13.522  27.771  1.00 14.52           C  
ANISOU  736  CG  ARG A  78      916   2116   2484   -119    254    150       C  
ATOM    737  CD  ARG A  78       7.480  12.991  27.222  1.00 15.38           C  
ANISOU  737  CD  ARG A  78     1121   2154   2569     40     28    226       C  
ATOM    738  NE  ARG A  78       7.174  12.164  26.064  1.00 14.41           N  
ANISOU  738  NE  ARG A  78      690   2088   2694     42    -68     11       N  
ATOM    739  CZ  ARG A  78       7.776  12.186  24.870  1.00 14.57           C  
ANISOU  739  CZ  ARG A  78      797   2066   2669    348    199    -91       C  
ATOM    740  NH1 ARG A  78       8.866  12.938  24.627  1.00 14.83           N  
ANISOU  740  NH1 ARG A  78      872   2218   2544    104    187    -34       N  
ATOM    741  NH2 ARG A  78       7.281  11.406  23.889  1.00 14.84           N  
ANISOU  741  NH2 ARG A  78      458   2225   2956     81    260   -105       N  
ATOM    742  N   LYS A  79       4.395  17.633  27.066  1.00 15.34           N  
ANISOU  742  N   LYS A  79     1226   2149   2450    224    468    -33       N  
ATOM    743  CA  LYS A  79       4.443  18.934  26.421  1.00 15.66           C  
ANISOU  743  CA  LYS A  79     1366   2145   2438    371    377     -6       C  
ATOM    744  C   LYS A  79       5.892  19.203  26.085  1.00 15.28           C  
ANISOU  744  C   LYS A  79     1218   2154   2432    167    221    108       C  
ATOM    745  O   LYS A  79       6.736  19.398  26.994  1.00 16.95           O  
ANISOU  745  O   LYS A  79     1344   2580   2516    265    381    -13       O  
ATOM    746  CB  LYS A  79       3.912  19.992  27.367  1.00 17.69           C  
ANISOU  746  CB  LYS A  79     1751   2294   2674    351    390     80       C  
ATOM    747  CG  LYS A  79       2.443  19.913  27.599  1.00 22.46           C  
ANISOU  747  CG  LYS A  79     2288   2908   3338    505    376    -85       C  
ATOM    748  CD  LYS A  79       1.884  18.659  28.184  1.00 27.83           C  
ANISOU  748  CD  LYS A  79     3156   3498   3920    307    346     95       C  
ATOM    749  CE  LYS A  79       0.373  18.814  28.365  1.00 31.07           C  
ANISOU  749  CE  LYS A  79     3444   4051   4311      9    208     68       C  
ATOM    750  NZ  LYS A  79      -0.347  17.515  28.283  1.00 33.43           N  
ANISOU  750  NZ  LYS A  79     4039   3970   4689   -120    199     17       N  
ATOM    751  N   VAL A  80       6.189  19.146  24.790  1.00 14.11           N  
ANISOU  751  N   VAL A  80     1125   1927   2308    146    193     48       N  
ATOM    752  CA  VAL A  80       7.578  19.230  24.337  1.00 13.22           C  
ANISOU  752  CA  VAL A  80      879   1845   2298     66     67     79       C  
ATOM    753  C   VAL A  80       7.760  20.381  23.366  1.00 13.16           C  
ANISOU  753  C   VAL A  80      854   1892   2254    -15    141    -42       C  
ATOM    754  O   VAL A  80       6.825  20.809  22.722  1.00 13.99           O  
ANISOU  754  O   VAL A  80      994   1879   2441     -7     39    156       O  
ATOM    755  CB  VAL A  80       8.049  17.868  23.707  1.00 13.12           C  
ANISOU  755  CB  VAL A  80      379   1979   2625    212    156     44       C  
ATOM    756  CG1 VAL A  80       7.764  16.683  24.661  1.00 14.48           C  
ANISOU  756  CG1 VAL A  80      937   1988   2575     21    122    207       C  
ATOM    757  CG2 VAL A  80       7.463  17.582  22.331  1.00 13.62           C  
ANISOU  757  CG2 VAL A  80      595   2084   2496    -70    257    161       C  
ATOM    758  N   LYS A  81       8.982  20.822  23.247  1.00 12.97           N  
ANISOU  758  N   LYS A  81      875   1742   2311     80    183     61       N  
ATOM    759  CA  LYS A  81       9.376  21.732  22.222  1.00 14.16           C  
ANISOU  759  CA  LYS A  81     1139   1837   2402    107     51    -40       C  
ATOM    760  C   LYS A  81      10.139  20.900  21.171  1.00 11.52           C  
ANISOU  760  C   LYS A  81      363   1770   2242    192    215   -126       C  
ATOM    761  O   LYS A  81      11.157  20.267  21.457  1.00 13.46           O  
ANISOU  761  O   LYS A  81      521   2023   2569    228      5    -48       O  
ATOM    762  CB  LYS A  81      10.348  22.760  22.778  1.00 15.58           C  
ANISOU  762  CB  LYS A  81     1256   2007   2654     26   -137    166       C  
ATOM    763  CG  LYS A  81       9.740  23.660  23.796  1.00 22.79           C  
ANISOU  763  CG  LYS A  81     2687   2821   3150     63    -64   -124       C  
ATOM    764  CD  LYS A  81       9.429  25.027  23.211  1.00 28.54           C  
ANISOU  764  CD  LYS A  81     3641   3362   3840    336   -176     -3       C  
ATOM    765  CE  LYS A  81       8.720  25.914  24.235  1.00 30.30           C  
ANISOU  765  CE  LYS A  81     4001   3581   3931    205   -254   -333       C  
ATOM    766  NZ  LYS A  81       7.753  26.739  23.552  1.00 32.94           N  
ANISOU  766  NZ  LYS A  81     4631   3620   4265    210   -245   -176       N  
ATOM    767  N   SER A  82       9.691  20.992  19.931  1.00 11.10           N  
ANISOU  767  N   SER A  82      293   1672   2250     19    155    -28       N  
ATOM    768  CA  SER A  82      10.094  20.138  18.852  1.00 11.11           C  
ANISOU  768  CA  SER A  82      259   1617   2345     89    -12     59       C  
ATOM    769  C   SER A  82      10.673  20.922  17.709  1.00 10.95           C  
ANISOU  769  C   SER A  82      257   1584   2319     72     33    114       C  
ATOM    770  O   SER A  82      10.226  22.020  17.371  1.00 11.22           O  
ANISOU  770  O   SER A  82      270   1606   2386    134    108    126       O  
ATOM    771  CB  SER A  82       8.945  19.381  18.280  1.00 12.19           C  
ANISOU  771  CB  SER A  82      256   1830   2543    -58     58    -43       C  
ATOM    772  OG  SER A  82       8.566  18.372  19.197  1.00 14.15           O  
ANISOU  772  OG  SER A  82      629   1894   2850     45    441    153       O  
ATOM    773  N   THR A  83      11.771  20.379  17.133  1.00 11.32           N  
ANISOU  773  N   THR A  83      267   1774   2259    128    -79     85       N  
ATOM    774  CA  THR A  83      12.299  20.933  15.893  1.00 10.43           C  
ANISOU  774  CA  THR A  83      273   1626   2063      6   -189      3       C  
ATOM    775  C   THR A  83      12.528  19.759  14.945  1.00 10.43           C  
ANISOU  775  C   THR A  83      265   1632   2064    -43    137     51       C  
ATOM    776  O   THR A  83      13.115  18.735  15.371  1.00 12.09           O  
ANISOU  776  O   THR A  83      329   1862   2400    212    -11     94       O  
ATOM    777  CB  THR A  83      13.626  21.641  16.124  1.00 11.86           C  
ANISOU  777  CB  THR A  83      255   1856   2394    -54    -17     55       C  
ATOM    778  OG1 THR A  83      13.465  22.597  17.165  1.00 13.40           O  
ANISOU  778  OG1 THR A  83      286   1961   2844   -227    -60   -174       O  
ATOM    779  CG2 THR A  83      13.980  22.410  14.864  1.00 14.16           C  
ANISOU  779  CG2 THR A  83      395   2297   2686    -13    132     11       C  
ATOM    780  N   ILE A  84      12.145  19.879  13.685  1.00 10.39           N  
ANISOU  780  N   ILE A  84      268   1630   2047     45    156     74       N  
ATOM    781  CA  ILE A  84      12.295  18.861  12.678  1.00 10.19           C  
ANISOU  781  CA  ILE A  84      262   1475   2133     20   -127    155       C  
ATOM    782  C   ILE A  84      13.063  19.451  11.517  1.00 10.33           C  
ANISOU  782  C   ILE A  84      269   1527   2126     86    150    176       C  
ATOM    783  O   ILE A  84      12.772  20.529  11.082  1.00 11.41           O  
ANISOU  783  O   ILE A  84      414   1639   2282     12    282    103       O  
ATOM    784  CB  ILE A  84      10.939  18.322  12.214  1.00 10.71           C  
ANISOU  784  CB  ILE A  84      285   1561   2220     73   -226    116       C  
ATOM    785  CG1 ILE A  84      10.188  17.658  13.407  1.00 11.08           C  
ANISOU  785  CG1 ILE A  84      255   1791   2163    -40    -47    226       C  
ATOM    786  CG2 ILE A  84      11.218  17.293  11.156  1.00 11.83           C  
ANISOU  786  CG2 ILE A  84      286   1925   2282   -118   -224    -25       C  
ATOM    787  CD1 ILE A  84       8.806  17.110  13.153  1.00 11.81           C  
ANISOU  787  CD1 ILE A  84      257   1922   2305    -57    -67    129       C  
ATOM    788  N   THR A  85      14.131  18.751  11.145  1.00 11.02           N  
ANISOU  788  N   THR A  85      266   1618   2300     97    122     96       N  
ATOM    789  CA  THR A  85      15.062  19.168  10.092  1.00 12.11           C  
ANISOU  789  CA  THR A  85      264   1760   2574    -98    109      5       C  
ATOM    790  C   THR A  85      15.274  17.975   9.195  1.00 11.97           C  
ANISOU  790  C   THR A  85      287   1710   2550    -71    260     69       C  
ATOM    791  O   THR A  85      14.967  16.850   9.495  1.00 13.34           O  
ANISOU  791  O   THR A  85      741   1819   2508     96    440     76       O  
ATOM    792  CB  THR A  85      16.385  19.667  10.639  1.00 13.01           C  
ANISOU  792  CB  THR A  85      297   1998   2645    -43    211     49       C  
ATOM    793  OG1 THR A  85      16.947  18.640  11.468  1.00 15.31           O  
ANISOU  793  OG1 THR A  85      578   2344   2895    182    -82     24       O  
ATOM    794  CG2 THR A  85      16.189  20.946  11.482  1.00 15.13           C  
ANISOU  794  CG2 THR A  85      289   2205   3255    -94   -292   -300       C  
ATOM    795  N   LEU A  86      15.815  18.246   8.023  1.00 14.52           N  
ANISOU  795  N   LEU A  86     1146   1700   2671    -87    544    146       N  
ATOM    796  CA  LEU A  86      16.493  17.226   7.230  1.00 16.59           C  
ANISOU  796  CA  LEU A  86     1524   1865   2913   -174    533     72       C  
ATOM    797  C   LEU A  86      18.005  17.157   7.440  1.00 17.47           C  
ANISOU  797  C   LEU A  86     1102   2255   3278   -499    838     44       C  
ATOM    798  O   LEU A  86      18.723  18.187   7.508  1.00 21.76           O  
ANISOU  798  O   LEU A  86     1454   2635   4176   -423    896    -70       O  
ATOM    799  CB  LEU A  86      16.284  17.404   5.750  1.00 19.58           C  
ANISOU  799  CB  LEU A  86     2287   2138   3012   -205    565     60       C  
ATOM    800  CG  LEU A  86      14.914  17.037   5.220  1.00 20.06           C  
ANISOU  800  CG  LEU A  86     2022   2484   3113    -45    268    392       C  
ATOM    801  CD1 LEU A  86      14.539  17.612   3.843  1.00 23.53           C  
ANISOU  801  CD1 LEU A  86     3324   2816   2797    409    413    -45       C  
ATOM    802  CD2 LEU A  86      14.746  15.485   5.160  1.00 17.86           C  
ANISOU  802  CD2 LEU A  86      848   2567   3371    -29     69    -33       C  
ATOM    803  N   ASP A  87      18.482  15.955   7.629  1.00 17.74           N  
ANISOU  803  N   ASP A  87     1104   2338   3296   -741    744   -177       N  
ATOM    804  CA  ASP A  87      19.926  15.769   7.638  1.00 18.42           C  
ANISOU  804  CA  ASP A  87      982   2748   3269   -778    655    -92       C  
ATOM    805  C   ASP A  87      20.173  14.745   6.564  1.00 16.36           C  
ANISOU  805  C   ASP A  87      660   2515   3039   -510    533   -127       C  
ATOM    806  O   ASP A  87      19.951  13.581   6.778  1.00 17.86           O  
ANISOU  806  O   ASP A  87      731   2751   3303   -564    365   -103       O  
ATOM    807  CB  ASP A  87      20.396  15.254   9.026  1.00 20.88           C  
ANISOU  807  CB  ASP A  87     1260   3232   3441   -893    540   -121       C  
ATOM    808  CG  ASP A  87      21.882  14.897   9.144  1.00 26.98           C  
ANISOU  808  CG  ASP A  87     2150   4098   4004   -569    184    -70       C  
ATOM    809  OD1 ASP A  87      22.715  15.180   8.280  1.00 33.18           O  
ANISOU  809  OD1 ASP A  87     2528   5470   4606  -1195    166   -140       O  
ATOM    810  OD2 ASP A  87      22.218  14.292  10.204  1.00 35.12           O  
ANISOU  810  OD2 ASP A  87     3017   5364   4963   -483   -640    137       O  
ATOM    811  N  AGLY A  88      20.810  15.128   5.461  0.50 15.23           N  
ANISOU  811  N  AGLY A  88      374   2492   2918   -403    364    -36       N  
ATOM    812  N  BGLY A  88      20.667  15.219   5.411  0.50 16.61           N  
ANISOU  812  N  BGLY A  88      995   2404   2909   -395    441   -101       N  
ATOM    813  CA AGLY A  88      21.065  14.157   4.435  0.50 14.27           C  
ANISOU  813  CA AGLY A  88      309   2409   2703   -113    289     59       C  
ATOM    814  CA BGLY A  88      20.746  14.408   4.221  0.50 15.35           C  
ANISOU  814  CA BGLY A  88      873   2280   2679   -283    553    -22       C  
ATOM    815  C  AGLY A  88      19.920  13.229   4.102  0.50 14.15           C  
ANISOU  815  C  AGLY A  88      562   2264   2549   -100     85     64       C  
ATOM    816  C  BGLY A  88      19.345  14.025   3.856  0.50 14.53           C  
ANISOU  816  C  BGLY A  88      882   2161   2477   -186    504    -52       C  
ATOM    817  O  AGLY A  88      20.086  12.025   4.063  0.50 16.46           O  
ANISOU  817  O  AGLY A  88      887   2438   2927     66    -47     16       O  
ATOM    818  O  BGLY A  88      18.507  14.898   3.733  0.50 16.35           O  
ANISOU  818  O  BGLY A  88     1034   2428   2748   -235    590    -51       O  
ATOM    819  N  AGLY A  89      18.756  13.786   3.849  0.50 13.49           N  
ANISOU  819  N  AGLY A  89      528   2136   2459     11     19    106       N  
ATOM    820  N  BGLY A  89      19.109  12.715   3.765  0.50 14.28           N  
ANISOU  820  N  BGLY A  89      939   2105   2380   -172    406   -147       N  
ATOM    821  CA AGLY A  89      17.608  12.978   3.493  0.50 13.02           C  
ANISOU  821  CA AGLY A  89      515   2131   2299    -39     57     27       C  
ATOM    822  CA BGLY A  89      17.820  12.083   3.477  0.50 13.57           C  
ANISOU  822  CA BGLY A  89      763   2096   2294   -211    434   -162       C  
ATOM    823  C  AGLY A  89      16.926  12.193   4.616  0.50 13.24           C  
ANISOU  823  C  AGLY A  89      483   2228   2318    -87    169    -48       C  
ATOM    824  C  BGLY A  89      17.093  11.648   4.736  0.50 12.73           C  
ANISOU  824  C  BGLY A  89      356   2152   2326   -206    429   -196       C  
ATOM    825  O  AGLY A  89      15.924  11.539   4.337  0.50 12.83           O  
ANISOU  825  O  AGLY A  89      343   2171   2359   -218     50    -19       O  
ATOM    826  O  BGLY A  89      16.182  10.798   4.694  0.50 13.94           O  
ANISOU  826  O  BGLY A  89      608   2094   2593   -240   -119   -196       O  
ATOM    827  N   VAL A  90      17.404  12.272   5.867  1.00 13.50           N  
ANISOU  827  N   VAL A  90      331   2400   2397   -298    308   -215       N  
ATOM    828  CA  VAL A  90      16.726  11.773   7.089  1.00 12.84           C  
ANISOU  828  CA  VAL A  90      429   2023   2424   -252    129   -299       C  
ATOM    829  C   VAL A  90      15.982  12.899   7.726  1.00 11.44           C  
ANISOU  829  C   VAL A  90      318   1793   2234   -316     17   -144       C  
ATOM    830  O   VAL A  90      16.512  13.988   7.944  1.00 13.05           O  
ANISOU  830  O   VAL A  90      324   2104   2528   -164    153   -110       O  
ATOM    831  CB  VAL A  90      17.776  11.260   8.110  1.00 13.51           C  
ANISOU  831  CB  VAL A  90      310   2055   2766   -302    145   -138       C  
ATOM    832  CG1 VAL A  90      17.115  10.762   9.368  1.00 13.88           C  
ANISOU  832  CG1 VAL A  90      430   2203   2641     87     49    124       C  
ATOM    833  CG2 VAL A  90      18.705  10.107   7.541  1.00 17.95           C  
ANISOU  833  CG2 VAL A  90      812   2633   3373    344    365   -320       C  
ATOM    834  N   LEU A  91      14.694  12.683   7.973  1.00 11.54           N  
ANISOU  834  N   LEU A  91      324   1855   2204   -293    -17   -112       N  
ATOM    835  CA ALEU A  91      13.932  13.662   8.805  0.50 10.74           C  
ANISOU  835  CA ALEU A  91      273   1631   2174   -160     64    -23       C  
ATOM    836  CA BLEU A  91      13.931  13.602   8.736  0.50 11.21           C  
ANISOU  836  CA BLEU A  91      266   1741   2249   -122     76      9       C  
ATOM    837  C   LEU A  91      14.228  13.413  10.242  1.00 10.89           C  
ANISOU  837  C   LEU A  91      288   1595   2252    112    226     13       C  
ATOM    838  O   LEU A  91      14.009  12.368  10.774  1.00 11.94           O  
ANISOU  838  O   LEU A  91      286   1732   2518     37     34     83       O  
ATOM    839  CB ALEU A  91      12.417  13.613   8.677  0.50 10.89           C  
ANISOU  839  CB ALEU A  91      277   1633   2227   -176     70   -106       C  
ATOM    840  CB BLEU A  91      12.509  13.293   8.378  0.50 12.45           C  
ANISOU  840  CB BLEU A  91      422   1852   2454   -119     40    -26       C  
ATOM    841  CG ALEU A  91      11.779  14.119   7.372  0.50 11.21           C  
ANISOU  841  CG ALEU A  91      512   1672   2076   -130   -139   -136       C  
ATOM    842  CG BLEU A  91      11.521  14.369   8.739  0.50 12.89           C  
ANISOU  842  CG BLEU A  91      256   2449   2193     82      7     23       C  
ATOM    843  CD1ALEU A  91      10.381  13.537   7.173  0.50 12.53           C  
ANISOU  843  CD1ALEU A  91      289   1953   2519   -185   -192     21       C  
ATOM    844  CD1BLEU A  91      11.748  15.641   7.978  0.50 12.09           C  
ANISOU  844  CD1BLEU A  91      308   2550   1733    302    163    109       C  
ATOM    845  CD2ALEU A  91      11.739  15.617   7.257  0.50 10.71           C  
ANISOU  845  CD2ALEU A  91      266   1794   2010    136    -38     43       C  
ATOM    846  CD2BLEU A  91      10.119  13.892   8.513  0.50 15.09           C  
ANISOU  846  CD2BLEU A  91      332   2682   2718   -270    328    164       C  
ATOM    847  N   VAL A  92      14.765  14.432  10.893  1.00 10.80           N  
ANISOU  847  N   VAL A  92      331   1638   2134    129    349    -13       N  
ATOM    848  CA  VAL A  92      15.200  14.324  12.279  1.00 10.72           C  
ANISOU  848  CA  VAL A  92      303   1614   2156    128    277     91       C  
ATOM    849  C   VAL A  92      14.284  15.218  13.137  1.00 10.64           C  
ANISOU  849  C   VAL A  92      301   1577   2165    212    180    113       C  
ATOM    850  O   VAL A  92      14.287  16.403  12.986  1.00 11.82           O  
ANISOU  850  O   VAL A  92      304   1651   2536    217    222    168       O  
ATOM    851  CB  VAL A  92      16.668  14.793  12.398  1.00 12.10           C  
ANISOU  851  CB  VAL A  92      314   1917   2367    188    292     22       C  
ATOM    852  CG1 VAL A  92      17.095  14.677  13.822  1.00 13.93           C  
ANISOU  852  CG1 VAL A  92      320   2416   2555     75    140    -36       C  
ATOM    853  CG2 VAL A  92      17.602  14.027  11.384  1.00 14.31           C  
ANISOU  853  CG2 VAL A  92      261   2263   2913      3    146   -131       C  
ATOM    854  N   HIS A  93      13.656  14.563  14.099  1.00 10.72           N  
ANISOU  854  N   HIS A  93      308   1543   2220    264     68    179       N  
ATOM    855  CA  HIS A  93      12.693  15.220  14.987  1.00 11.04           C  
ANISOU  855  CA  HIS A  93      299   1609   2287    135     62    142       C  
ATOM    856  C   HIS A  93      13.241  15.163  16.411  1.00 10.86           C  
ANISOU  856  C   HIS A  93      285   1575   2264    168    151     54       C  
ATOM    857  O   HIS A  93      13.331  14.098  16.994  1.00 11.65           O  
ANISOU  857  O   HIS A  93      387   1602   2437     76    -33    108       O  
ATOM    858  CB  HIS A  93      11.352  14.511  14.869  1.00 11.49           C  
ANISOU  858  CB  HIS A  93      383   1689   2294    104     40    224       C  
ATOM    859  CG  HIS A  93      10.238  15.035  15.744  1.00 11.75           C  
ANISOU  859  CG  HIS A  93      264   1731   2469    -35    141    262       C  
ATOM    860  ND1 HIS A  93       8.970  14.498  15.688  1.00 14.29           N  
ANISOU  860  ND1 HIS A  93      258   2132   3039     12    117    474       N  
ATOM    861  CD2 HIS A  93      10.176  16.068  16.632  1.00 12.90           C  
ANISOU  861  CD2 HIS A  93      302   1995   2601    249    215    266       C  
ATOM    862  CE1 HIS A  93       8.200  15.161  16.536  1.00 15.00           C  
ANISOU  862  CE1 HIS A  93      644   2085   2969    347    433    437       C  
ATOM    863  NE2 HIS A  93       8.888  16.142  17.091  1.00 15.71           N  
ANISOU  863  NE2 HIS A  93      461   2385   3122    470    476    542       N  
ATOM    864  N   VAL A  94      13.610  16.304  16.933  1.00 11.25           N  
ANISOU  864  N   VAL A  94      275   1683   2314    161    101     61       N  
ATOM    865  CA  VAL A  94      14.153  16.401  18.305  1.00 11.48           C  
ANISOU  865  CA  VAL A  94      263   1791   2307     27    142     35       C  
ATOM    866  C   VAL A  94      13.035  17.009  19.190  1.00 11.14           C  
ANISOU  866  C   VAL A  94      269   1797   2165    149    -39    102       C  
ATOM    867  O   VAL A  94      12.489  18.055  18.842  1.00 12.43           O  
ANISOU  867  O   VAL A  94      451   1812   2458    225    145    126       O  
ATOM    868  CB  VAL A  94      15.428  17.264  18.344  1.00 13.28           C  
ANISOU  868  CB  VAL A  94      257   2273   2516     28     96    -16       C  
ATOM    869  CG1 VAL A  94      15.949  17.333  19.750  1.00 14.41           C  
ANISOU  869  CG1 VAL A  94      256   2601   2617     -4     87      4       C  
ATOM    870  CG2 VAL A  94      16.497  16.675  17.370  1.00 15.15           C  
ANISOU  870  CG2 VAL A  94      341   2507   2905     40    479    -68       C  
ATOM    871  N   GLN A  95      12.815  16.379  20.320  1.00 11.27           N  
ANISOU  871  N   GLN A  95      268   1735   2279    121   -100     63       N  
ATOM    872  CA  GLN A  95      11.854  16.829  21.321  1.00 11.46           C  
ANISOU  872  CA  GLN A  95      309   1736   2308    124    129     80       C  
ATOM    873  C   GLN A  95      12.558  17.109  22.627  1.00 12.97           C  
ANISOU  873  C   GLN A  95      868   1780   2279    152     27      6       C  
ATOM    874  O   GLN A  95      13.314  16.251  23.130  1.00 13.47           O  
ANISOU  874  O   GLN A  95      778   1916   2424    282    -39     58       O  
ATOM    875  CB  GLN A  95      10.782  15.746  21.597  1.00 12.03           C  
ANISOU  875  CB  GLN A  95      631   1688   2251    143    114    166       C  
ATOM    876  CG  GLN A  95       9.926  15.389  20.398  1.00 12.23           C  
ANISOU  876  CG  GLN A  95      563   1673   2410    109    123     95       C  
ATOM    877  CD  GLN A  95       8.975  14.245  20.645  1.00 13.01           C  
ANISOU  877  CD  GLN A  95      293   1844   2804    177    236    102       C  
ATOM    878  OE1 GLN A  95       7.889  14.217  20.021  1.00 15.83           O  
ANISOU  878  OE1 GLN A  95      255   2680   3076      6    -85    243       O  
ATOM    879  NE2 GLN A  95       9.255  13.388  21.581  1.00 12.34           N  
ANISOU  879  NE2 GLN A  95      255   1817   2614    -34     46    103       N  
ATOM    880  N   LYS A  96      12.308  18.286  23.162  1.00 13.17           N  
ANISOU  880  N   LYS A  96      934   1778   2289     89   -158    -85       N  
ATOM    881  CA  LYS A  96      12.905  18.733  24.423  1.00 15.46           C  
ANISOU  881  CA  LYS A  96     1478   2047   2347    113    -94    -53       C  
ATOM    882  C   LYS A  96      11.847  18.989  25.474  1.00 15.47           C  
ANISOU  882  C   LYS A  96     1655   1933   2288    179    -47   -136       C  
ATOM    883  O   LYS A  96      10.881  19.661  25.190  1.00 16.64           O  
ANISOU  883  O   LYS A  96     1868   2032   2420    308   -107      1       O  
ATOM    884  CB  LYS A  96      13.671  20.048  24.236  1.00 17.07           C  
ANISOU  884  CB  LYS A  96     1704   2323   2459     11   -194    -57       C  
ATOM    885  CG  LYS A  96      14.698  20.038  23.172  1.00 19.40           C  
ANISOU  885  CG  LYS A  96     1653   2706   3011     -9   -116   -154       C  
ATOM    886  CD  LYS A  96      15.941  19.162  23.438  1.00 19.58           C  
ANISOU  886  CD  LYS A  96     1192   2943   3302    -80   -204   -199       C  
ATOM    887  CE  LYS A  96      17.123  19.469  22.506  1.00 19.45           C  
ANISOU  887  CE  LYS A  96     1136   2775   3476   -536   -260    -76       C  
ATOM    888  NZ  LYS A  96      18.198  18.532  22.732  1.00 21.06           N  
ANISOU  888  NZ  LYS A  96     1098   3185   3717   -203   -183     97       N  
ATOM    889  N   TRP A  97      12.025  18.484  26.681  1.00 16.00           N  
ANISOU  889  N   TRP A  97     1803   1945   2329    287    -73   -135       N  
ATOM    890  CA  TRP A  97      11.071  18.723  27.769  1.00 16.22           C  
ANISOU  890  CA  TRP A  97     1888   1908   2365    177     -4   -139       C  
ATOM    891  C   TRP A  97      11.768  18.398  29.097  1.00 19.02           C  
ANISOU  891  C   TRP A  97     2563   2251   2411    230     33   -133       C  
ATOM    892  O   TRP A  97      12.535  17.458  29.154  1.00 19.11           O  
ANISOU  892  O   TRP A  97     2544   2319   2399    375   -119     14       O  
ATOM    893  CB  TRP A  97       9.805  17.860  27.597  1.00 17.20           C  
ANISOU  893  CB  TRP A  97     1861   2196   2478    174     84   -154       C  
ATOM    894  CG  TRP A  97       9.946  16.439  27.982  1.00 16.42           C  
ANISOU  894  CG  TRP A  97     1584   2131   2523    271    256    -37       C  
ATOM    895  CD1 TRP A  97       9.416  15.854  29.071  1.00 15.32           C  
ANISOU  895  CD1 TRP A  97      837   2423   2558    129    196    -50       C  
ATOM    896  CD2 TRP A  97      10.681  15.395  27.307  1.00 15.39           C  
ANISOU  896  CD2 TRP A  97     1215   2109   2522     24    191   -118       C  
ATOM    897  NE1 TRP A  97       9.766  14.537  29.136  1.00 16.25           N  
ANISOU  897  NE1 TRP A  97     1228   2287   2657    -47    244     33       N  
ATOM    898  CE2 TRP A  97      10.559  14.235  28.074  1.00 16.75           C  
ANISOU  898  CE2 TRP A  97     1704   2217   2443    215    199     -6       C  
ATOM    899  CE3 TRP A  97      11.400  15.330  26.133  1.00 14.96           C  
ANISOU  899  CE3 TRP A  97      908   2296   2478   -308     25    -77       C  
ATOM    900  CZ2 TRP A  97      11.147  13.039  27.716  1.00 15.30           C  
ANISOU  900  CZ2 TRP A  97      748   2008   3057    -84    193    221       C  
ATOM    901  CZ3 TRP A  97      12.015  14.138  25.796  1.00 15.30           C  
ANISOU  901  CZ3 TRP A  97     1175   2047   2590   -278     26    -83       C  
ATOM    902  CH2 TRP A  97      11.944  13.042  26.602  1.00 13.71           C  
ANISOU  902  CH2 TRP A  97      256   1917   3033    -69    -20   -174       C  
ATOM    903  N   ASP A  98      11.541  19.208  30.138  1.00 20.20           N  
ANISOU  903  N   ASP A  98     2838   2346   2490    262    -41   -274       N  
ATOM    904  CA  ASP A  98      12.006  18.820  31.486  1.00 22.63           C  
ANISOU  904  CA  ASP A  98     3172   2697   2728    204   -154   -240       C  
ATOM    905  C   ASP A  98      13.528  18.555  31.539  1.00 22.33           C  
ANISOU  905  C   ASP A  98     3186   2631   2668    108   -239   -279       C  
ATOM    906  O   ASP A  98      13.996  17.672  32.268  1.00 24.40           O  
ANISOU  906  O   ASP A  98     3603   2745   2920    233   -395   -183       O  
ATOM    907  CB  ASP A  98      11.255  17.552  31.941  1.00 24.41           C  
ANISOU  907  CB  ASP A  98     3383   2943   2946    206   -170   -168       C  
ATOM    908  CG  ASP A  98      11.079  17.447  33.463  1.00 29.60           C  
ANISOU  908  CG  ASP A  98     4205   3588   3451     98    -37    -44       C  
ATOM    909  OD1 ASP A  98      11.143  18.480  34.169  1.00 35.11           O  
ANISOU  909  OD1 ASP A  98     5284   4230   3824    379    185   -423       O  
ATOM    910  OD2 ASP A  98      10.888  16.303  33.952  1.00 36.31           O  
ANISOU  910  OD2 ASP A  98     5131   4240   4422    -56    -53    470       O  
ATOM    911  N   GLY A  99      14.297  19.257  30.717  1.00 21.88           N  
ANISOU  911  N   GLY A  99     3079   2593   2640     16   -242   -286       N  
ATOM    912  CA  GLY A  99      15.754  19.063  30.639  1.00 21.63           C  
ANISOU  912  CA  GLY A  99     2922   2599   2695     20   -352   -242       C  
ATOM    913  C   GLY A  99      16.187  17.774  29.968  1.00 20.97           C  
ANISOU  913  C   GLY A  99     2615   2604   2747    108   -393   -210       C  
ATOM    914  O   GLY A  99      17.373  17.420  30.006  1.00 23.41           O  
ANISOU  914  O   GLY A  99     2704   2964   3226     32   -467   -329       O  
ATOM    915  N   LYS A 100      15.247  17.081  29.332  1.00 18.79           N  
ANISOU  915  N   LYS A 100     2193   2473   2472    -30   -396   -228       N  
ATOM    916  CA  LYS A 100      15.512  15.816  28.624  1.00 17.22           C  
ANISOU  916  CA  LYS A 100     1824   2273   2443    112   -371    -78       C  
ATOM    917  C   LYS A 100      15.356  16.056  27.124  1.00 15.98           C  
ANISOU  917  C   LYS A 100     1584   2046   2438    -58   -350   -203       C  
ATOM    918  O   LYS A 100      14.763  17.067  26.708  1.00 16.38           O  
ANISOU  918  O   LYS A 100     1647   1970   2605      9   -427   -155       O  
ATOM    919  CB  LYS A 100      14.468  14.776  29.023  1.00 18.44           C  
ANISOU  919  CB  LYS A 100     2314   2108   2581     60   -375    -24       C  
ATOM    920  CG  LYS A 100      14.434  14.429  30.500  1.00 23.11           C  
ANISOU  920  CG  LYS A 100     3044   2926   2810    -13     -5   -134       C  
ATOM    921  CD  LYS A 100      13.259  13.555  30.896  1.00 26.82           C  
ANISOU  921  CD  LYS A 100     3742   3505   2941   -237     24    175       C  
ATOM    922  CE  LYS A 100      13.226  13.343  32.396  1.00 30.94           C  
ANISOU  922  CE  LYS A 100     4267   4078   3411   -273    242    102       C  
ATOM    923  NZ  LYS A 100      12.029  12.579  32.768  1.00 34.24           N  
ANISOU  923  NZ  LYS A 100     4776   4365   3869   -316    412    314       N  
ATOM    924  N   SER A 101      15.865  15.102  26.337  1.00 14.55           N  
ANISOU  924  N   SER A 101     1043   1951   2534    -73   -292   -241       N  
ATOM    925  CA  SER A 101      15.748  15.175  24.895  1.00 13.80           C  
ANISOU  925  CA  SER A 101      716   1992   2535    -50   -310    -98       C  
ATOM    926  C   SER A 101      15.637  13.797  24.322  1.00 12.81           C  
ANISOU  926  C   SER A 101      511   1853   2501    -17   -212     35       C  
ATOM    927  O   SER A 101      16.230  12.867  24.824  1.00 14.37           O  
ANISOU  927  O   SER A 101     1016   1868   2574     77   -408     78       O  
ATOM    928  CB  SER A 101      17.004  15.852  24.354  1.00 15.93           C  
ANISOU  928  CB  SER A 101     1189   2034   2830   -408   -247    -52       C  
ATOM    929  OG  SER A 101      16.979  16.050  22.968  1.00 18.70           O  
ANISOU  929  OG  SER A 101     1602   2502   2998   -529   -217   -112       O  
ATOM    930  N   THR A 102      14.836  13.661  23.268  1.00 11.57           N  
ANISOU  930  N   THR A 102      496   1744   2155     -5   -283     16       N  
ATOM    931  CA  THR A 102      14.730  12.430  22.513  1.00 11.61           C  
ANISOU  931  CA  THR A 102      396   1791   2223     99   -226    -62       C  
ATOM    932  C   THR A 102      14.699  12.793  21.033  1.00 11.31           C  
ANISOU  932  C   THR A 102      339   1714   2242    -87   -176    -66       C  
ATOM    933  O   THR A 102      14.250  13.892  20.671  1.00 11.82           O  
ANISOU  933  O   THR A 102      322   1719   2448     72    -66     62       O  
ATOM    934  CB  THR A 102      13.515  11.582  22.975  1.00 11.81           C  
ANISOU  934  CB  THR A 102      269   1823   2395     28   -118   -119       C  
ATOM    935  OG1 THR A 102      13.539  10.316  22.363  1.00 13.21           O  
ANISOU  935  OG1 THR A 102      254   1843   2922    -36    -26   -102       O  
ATOM    936  CG2 THR A 102      12.193  12.203  22.636  1.00 12.34           C  
ANISOU  936  CG2 THR A 102      262   1970   2455    118    -41     24       C  
ATOM    937  N   THR A 103      15.142  11.850  20.199  1.00 11.45           N  
ANISOU  937  N   THR A 103      432   1660   2259     77   -247   -103       N  
ATOM    938  CA  THR A 103      15.228  12.049  18.775  1.00 12.72           C  
ANISOU  938  CA  THR A 103      671   1757   2402    159   -150     28       C  
ATOM    939  C   THR A 103      14.473  10.922  18.071  1.00 12.81           C  
ANISOU  939  C   THR A 103     1130   1636   2099     92    -83     12       C  
ATOM    940  O   THR A 103      14.712   9.770  18.356  1.00 15.72           O  
ANISOU  940  O   THR A 103     1995   1573   2404    216   -405    107       O  
ATOM    941  CB  THR A 103      16.663  12.216  18.282  1.00 14.07           C  
ANISOU  941  CB  THR A 103      807   2000   2538     24     14     -8       C  
ATOM    942  OG1 THR A 103      17.300  13.324  18.964  1.00 17.24           O  
ANISOU  942  OG1 THR A 103      831   2598   3120   -135     28    210       O  
ATOM    943  CG2 THR A 103      16.681  12.468  16.746  1.00 16.07           C  
ANISOU  943  CG2 THR A 103      446   2677   2979    106    167     37       C  
ATOM    944  N   ILE A 104      13.660  11.297  17.099  1.00 12.20           N  
ANISOU  944  N   ILE A 104      918   1540   2178    134   -125     43       N  
ATOM    945  CA AILE A 104      12.952  10.377  16.234  0.50 12.66           C  
ANISOU  945  CA AILE A 104     1078   1528   2201     87    -60     38       C  
ATOM    946  CA BILE A 104      12.928  10.395  16.232  0.50 11.70           C  
ANISOU  946  CA BILE A 104      938   1398   2107     93    -32     22       C  
ATOM    947  C   ILE A 104      13.368  10.656  14.809  1.00 11.13           C  
ANISOU  947  C   ILE A 104      500   1507   2220    -43    -51    -14       C  
ATOM    948  O   ILE A 104      13.160  11.752  14.316  1.00 11.46           O  
ANISOU  948  O   ILE A 104      586   1489   2276     71    117     96       O  
ATOM    949  CB AILE A 104      11.408  10.548  16.325  0.50 14.38           C  
ANISOU  949  CB AILE A 104     1169   1921   2372     32    -39    -18       C  
ATOM    950  CB BILE A 104      11.372  10.612  16.349  0.50 12.73           C  
ANISOU  950  CB BILE A 104      943   1653   2240     85     -4    -34       C  
ATOM    951  CG1AILE A 104      10.737   9.600  15.330  0.50 14.87           C  
ANISOU  951  CG1AILE A 104     1005   2078   2566    -49    -83     12       C  
ATOM    952  CG1BILE A 104      10.943  10.340  17.782  0.50 11.02           C  
ANISOU  952  CG1BILE A 104      789   1361   2035    -90     48   -221       C  
ATOM    953  CG2AILE A 104      11.041  11.971  16.077  0.50 18.91           C  
ANISOU  953  CG2AILE A 104     1837   2438   2910     33   -133     37       C  
ATOM    954  CG2BILE A 104      10.655   9.646  15.448  0.50 13.00           C  
ANISOU  954  CG2BILE A 104      514   2013   2411    -76     54    -66       C  
ATOM    955  CD1AILE A 104       9.299   9.667  15.381  0.50 18.58           C  
ANISOU  955  CD1AILE A 104     1308   2668   3081    117     37    114       C  
ATOM    956  CD1BILE A 104       9.473  10.551  18.021  0.50 15.33           C  
ANISOU  956  CD1BILE A 104     1336   1918   2569   -123    -45   -104       C  
ATOM    957  N   LYS A 105      13.972   9.654  14.167  1.00 11.91           N  
ANISOU  957  N   LYS A 105      643   1590   2291     92    -85     21       N  
ATOM    958  CA  LYS A 105      14.460   9.787  12.808  1.00 11.63           C  
ANISOU  958  CA  LYS A 105      509   1623   2285     48    -72     67       C  
ATOM    959  C   LYS A 105      13.612   8.951  11.886  1.00 11.89           C  
ANISOU  959  C   LYS A 105      758   1556   2202      7     36    -19       C  
ATOM    960  O   LYS A 105      13.230   7.861  12.243  1.00 13.99           O  
ANISOU  960  O   LYS A 105     1338   1656   2321   -170   -157     67       O  
ATOM    961  CB  LYS A 105      15.925   9.341  12.725  1.00 12.74           C  
ANISOU  961  CB  LYS A 105      704   1884   2253     -9     41     47       C  
ATOM    962  CG  LYS A 105      16.870  10.228  13.484  1.00 15.36           C  
ANISOU  962  CG  LYS A 105      440   2389   3006    242   -119     46       C  
ATOM    963  CD  LYS A 105      18.310   9.934  13.219  1.00 19.14           C  
ANISOU  963  CD  LYS A 105      463   3292   3517   -236     11    290       C  
ATOM    964  CE  LYS A 105      19.312  10.931  13.967  1.00 21.68           C  
ANISOU  964  CE  LYS A 105      299   3832   4104    148   -380    255       C  
ATOM    965  NZ  LYS A 105      20.644  10.650  13.753  1.00 25.51           N  
ANISOU  965  NZ  LYS A 105      562   4159   4969     90    -68    114       N  
ATOM    966  N   ARG A 106      13.356   9.491  10.714  1.00 11.61           N  
ANISOU  966  N   ARG A 106      535   1646   2230    -20     86      7       N  
ATOM    967  CA  ARG A 106      12.607   8.827   9.661  1.00 11.74           C  
ANISOU  967  CA  ARG A 106      414   1764   2280    -93     73     12       C  
ATOM    968  C   ARG A 106      13.489   8.782   8.409  1.00 11.05           C  
ANISOU  968  C   ARG A 106      260   1712   2223     60    -94    -61       C  
ATOM    969  O   ARG A 106      13.938   9.846   7.982  1.00 11.81           O  
ANISOU  969  O   ARG A 106      258   1762   2468    -63     71     10       O  
ATOM    970  CB  ARG A 106      11.275   9.512   9.363  1.00 12.71           C  
ANISOU  970  CB  ARG A 106      266   2049   2511   -154     13     58       C  
ATOM    971  CG  ARG A 106      10.285   9.453  10.505  1.00 13.98           C  
ANISOU  971  CG  ARG A 106      641   1888   2782   -142    390     45       C  
ATOM    972  CD  ARG A 106       9.081  10.368  10.193  1.00 16.17           C  
ANISOU  972  CD  ARG A 106      341   2434   3369    -38    520     63       C  
ATOM    973  NE  ARG A 106       7.944  10.245  11.070  1.00 17.53           N  
ANISOU  973  NE  ARG A 106      310   2607   3743    -99    431    -32       N  
ATOM    974  CZ  ARG A 106       7.867  10.856  12.245  1.00 17.42           C  
ANISOU  974  CZ  ARG A 106      453   2914   3252   -202    577    123       C  
ATOM    975  NH1 ARG A 106       8.754  11.733  12.647  1.00 18.06           N  
ANISOU  975  NH1 ARG A 106      394   3146   3320     16    574    306       N  
ATOM    976  NH2 ARG A 106       6.747  10.731  12.934  1.00 20.11           N  
ANISOU  976  NH2 ARG A 106      634   3331   3674   -318    558   -124       N  
ATOM    977  N   LYS A 107      13.577   7.607   7.827  1.00 11.91           N  
ANISOU  977  N   LYS A 107      259   1885   2379    -46    101   -140       N  
ATOM    978  CA  LYS A 107      14.455   7.402   6.646  1.00 12.14           C  
ANISOU  978  CA  LYS A 107      257   1955   2401    -65     69   -173       C  
ATOM    979  C   LYS A 107      13.856   6.363   5.688  1.00 12.33           C  
ANISOU  979  C   LYS A 107      406   1986   2290    -78     66   -161       C  
ATOM    980  O   LYS A 107      13.353   5.352   6.135  1.00 14.37           O  
ANISOU  980  O   LYS A 107     1222   1991   2246   -336     91     36       O  
ATOM    981  CB  LYS A 107      15.865   7.004   7.018  1.00 13.19           C  
ANISOU  981  CB  LYS A 107      257   2140   2613    -79     61   -337       C  
ATOM    982  CG  LYS A 107      16.924   7.090   5.935  1.00 16.95           C  
ANISOU  982  CG  LYS A 107      537   2596   3305    -49    181   -271       C  
ATOM    983  CD  LYS A 107      18.313   6.706   6.430  1.00 17.53           C  
ANISOU  983  CD  LYS A 107      499   2647   3511     95    157   -550       C  
ATOM    984  CE  LYS A 107      19.342   6.939   5.396  1.00 23.72           C  
ANISOU  984  CE  LYS A 107     1946   3428   3636    137    299   -531       C  
ATOM    985  NZ  LYS A 107      19.127   5.854   4.393  1.00 28.00           N  
ANISOU  985  NZ  LYS A 107     2637   3798   4204    143    441   -915       N  
ATOM    986  N   ARG A 108      13.931   6.631   4.405  1.00 11.89           N  
ANISOU  986  N   ARG A 108      385   1770   2359   -199     88    -59       N  
ATOM    987  CA  ARG A 108      13.543   5.654   3.411  1.00 12.57           C  
ANISOU  987  CA  ARG A 108      345   2040   2388    -90    107    -76       C  
ATOM    988  C   ARG A 108      14.576   4.590   3.249  1.00 12.29           C  
ANISOU  988  C   ARG A 108      256   2081   2330     46     57   -128       C  
ATOM    989  O   ARG A 108      15.775   4.893   3.083  1.00 14.44           O  
ANISOU  989  O   ARG A 108      266   2286   2933    -64    173   -142       O  
ATOM    990  CB  ARG A 108      13.289   6.314   2.090  1.00 13.21           C  
ANISOU  990  CB  ARG A 108      277   2357   2385   -199    112    -37       C  
ATOM    991  CG  ARG A 108      12.020   7.083   2.045  1.00 14.70           C  
ANISOU  991  CG  ARG A 108      351   2789   2446    158     49    135       C  
ATOM    992  CD  ARG A 108      10.686   6.255   2.152  1.00 16.26           C  
ANISOU  992  CD  ARG A 108      547   2942   2689    132    236    119       C  
ATOM    993  NE  ARG A 108      10.741   5.112   1.241  1.00 17.64           N  
ANISOU  993  NE  ARG A 108      614   2867   3220   -191    124    237       N  
ATOM    994  CZ  ARG A 108      10.461   5.168  -0.049  1.00 15.71           C  
ANISOU  994  CZ  ARG A 108      277   2403   3286   -221    -42   -157       C  
ATOM    995  NH1 ARG A 108       9.942   6.281  -0.586  1.00 17.52           N  
ANISOU  995  NH1 ARG A 108      735   2514   3407    162    -24    -77       N  
ATOM    996  NH2 ARG A 108      10.645   4.112  -0.808  1.00 20.47           N  
ANISOU  996  NH2 ARG A 108      798   3095   3881     35   -472   -345       N  
ATOM    997  N   GLU A 109      14.225   3.311   3.270  1.00 12.32           N  
ANISOU  997  N   GLU A 109      257   2004   2418     24     93   -146       N  
ATOM    998  CA  GLU A 109      15.098   2.181   3.056  1.00 13.06           C  
ANISOU  998  CA  GLU A 109      554   2056   2353     10    131   -155       C  
ATOM    999  C   GLU A 109      14.325   1.191   2.188  1.00 12.41           C  
ANISOU  999  C   GLU A 109      459   1967   2286    -35    117   -119       C  
ATOM   1000  O   GLU A 109      13.320   0.662   2.606  1.00 13.73           O  
ANISOU 1000  O   GLU A 109      498   2270   2446   -138    234    -59       O  
ATOM   1001  CB  GLU A 109      15.423   1.487   4.372  1.00 13.85           C  
ANISOU 1001  CB  GLU A 109      483   2173   2603     99    143   -154       C  
ATOM   1002  CG  GLU A 109      16.156   2.397   5.377  1.00 18.27           C  
ANISOU 1002  CG  GLU A 109     1359   2691   2889    -33    -70    -45       C  
ATOM   1003  CD  GLU A 109      17.553   2.699   5.007  1.00 21.81           C  
ANISOU 1003  CD  GLU A 109     1661   3401   3224   -320    -65   -526       C  
ATOM   1004  OE1 GLU A 109      18.209   3.490   5.721  1.00 25.53           O  
ANISOU 1004  OE1 GLU A 109     1509   4112   4078   -444     30   -693       O  
ATOM   1005  OE2 GLU A 109      18.023   2.121   4.010  1.00 26.58           O  
ANISOU 1005  OE2 GLU A 109     1671   4213   4212   -255    187   -858       O  
ATOM   1006  N   ASP A 110      14.777   1.014   0.959  1.00 12.48           N  
ANISOU 1006  N   ASP A 110      442   1995   2302    -43    111    -67       N  
ATOM   1007  CA  ASP A 110      14.033   0.221  -0.016  1.00 12.16           C  
ANISOU 1007  CA  ASP A 110      421   1945   2252    -13    176   -134       C  
ATOM   1008  C   ASP A 110      12.609   0.770  -0.097  1.00 11.99           C  
ANISOU 1008  C   ASP A 110      298   2080   2178    -70     59   -189       C  
ATOM   1009  O   ASP A 110      12.463   1.990  -0.207  1.00 12.80           O  
ANISOU 1009  O   ASP A 110      497   1898   2465    -13    246   -116       O  
ATOM   1010  CB  ASP A 110      14.161  -1.269   0.293  1.00 13.64           C  
ANISOU 1010  CB  ASP A 110      789   2079   2312   -125    119   -154       C  
ATOM   1011  CG  ASP A 110      15.555  -1.752   0.238  1.00 17.64           C  
ANISOU 1011  CG  ASP A 110     1634   2390   2676    324    262     33       C  
ATOM   1012  OD1 ASP A 110      16.291  -1.319  -0.659  1.00 17.96           O  
ANISOU 1012  OD1 ASP A 110     1114   2636   3073    287    405    -20       O  
ATOM   1013  OD2 ASP A 110      15.884  -2.617   1.069  1.00 24.07           O  
ANISOU 1013  OD2 ASP A 110     2444   3278   3421    632    157    503       O  
ATOM   1014  N   ASP A 111      11.542  -0.047  -0.072  1.00 12.93           N  
ANISOU 1014  N   ASP A 111      341   2120   2450    -56     59   -210       N  
ATOM   1015  CA  ASP A 111      10.182   0.409  -0.135  1.00 12.44           C  
ANISOU 1015  CA  ASP A 111      397   2133   2195   -123     25   -122       C  
ATOM   1016  C   ASP A 111       9.595   0.804   1.208  1.00 13.36           C  
ANISOU 1016  C   ASP A 111      588   2151   2335   -135    -72   -211       C  
ATOM   1017  O   ASP A 111       8.429   1.124   1.268  1.00 16.18           O  
ANISOU 1017  O   ASP A 111      509   2930   2708     31    178   -428       O  
ATOM   1018  CB  ASP A 111       9.292  -0.571  -0.866  1.00 14.29           C  
ANISOU 1018  CB  ASP A 111      853   2316   2260   -216    -45   -209       C  
ATOM   1019  CG  ASP A 111       9.638  -0.659  -2.326  1.00 14.34           C  
ANISOU 1019  CG  ASP A 111      332   2452   2662   -269    -39   -239       C  
ATOM   1020  OD1 ASP A 111       9.945   0.402  -2.921  1.00 17.92           O  
ANISOU 1020  OD1 ASP A 111     1360   2782   2666   -351    126   -281       O  
ATOM   1021  OD2 ASP A 111       9.653  -1.776  -2.831  1.00 19.51           O  
ANISOU 1021  OD2 ASP A 111     1981   2723   2708   -308    147   -472       O  
ATOM   1022  N  ALYS A 112      10.414   0.801   2.248  0.50 12.52           N  
ANISOU 1022  N  ALYS A 112      263   2148   2346   -118     84   -178       N  
ATOM   1023  N  BLYS A 112      10.406   0.810   2.261  0.50 12.70           N  
ANISOU 1023  N  BLYS A 112      265   2202   2359   -135     88   -183       N  
ATOM   1024  CA ALYS A 112       9.989   1.034   3.605  0.50 12.97           C  
ANISOU 1024  CA ALYS A 112      647   1997   2281   -114     86   -188       C  
ATOM   1025  CA BLYS A 112       9.960   1.057   3.623  0.50 12.98           C  
ANISOU 1025  CA BLYS A 112      550   2094   2284   -158    105   -194       C  
ATOM   1026  C  ALYS A 112      10.351   2.419   4.074  0.50 12.54           C  
ANISOU 1026  C  ALYS A 112      670   1878   2216    -99    100   -138       C  
ATOM   1027  C  BLYS A 112      10.326   2.439   4.120  0.50 12.82           C  
ANISOU 1027  C  BLYS A 112      607   2002   2260   -149    125   -146       C  
ATOM   1028  O  ALYS A 112      11.224   3.101   3.540  0.50 13.01           O  
ANISOU 1028  O  ALYS A 112      349   2037   2557   -225     79   -131       O  
ATOM   1029  O  BLYS A 112      11.212   3.112   3.590  0.50 13.71           O  
ANISOU 1029  O  BLYS A 112      311   2287   2608   -329    133   -126       O  
ATOM   1030  CB ALYS A 112      10.602  -0.011   4.538  0.50 14.46           C  
ANISOU 1030  CB ALYS A 112     1068   2081   2342    -58    208   -108       C  
ATOM   1031  CB BLYS A 112      10.530   0.006   4.577  0.50 13.99           C  
ANISOU 1031  CB BLYS A 112      768   2199   2347   -152    212   -121       C  
ATOM   1032  CG ALYS A 112      10.191  -1.442   4.261  0.50 17.83           C  
ANISOU 1032  CG ALYS A 112     1719   2432   2621    -11    330   -145       C  
ATOM   1033  CG BLYS A 112      10.335  -1.436   4.180  0.50 17.00           C  
ANISOU 1033  CG BLYS A 112     1508   2404   2546    -84    202   -122       C  
ATOM   1034  CD ALYS A 112      11.129  -2.415   4.943  0.50 21.14           C  
ANISOU 1034  CD ALYS A 112     2479   2733   2819    248    285   -148       C  
ATOM   1035  CD BLYS A 112       8.896  -1.870   4.338  0.50 16.92           C  
ANISOU 1035  CD BLYS A 112     1630   2356   2443   -228     77   -159       C  
ATOM   1036  CE ALYS A 112      10.743  -3.857   4.674  0.50 22.94           C  
ANISOU 1036  CE ALYS A 112     2532   2992   3191    114    263   -115       C  
ATOM   1037  CE BLYS A 112       8.793  -3.381   4.402  0.50 18.86           C  
ANISOU 1037  CE BLYS A 112     1970   2551   2643   -274     10    -91       C  
ATOM   1038  NZ ALYS A 112      11.922  -4.570   4.114  0.50 24.89           N  
ANISOU 1038  NZ ALYS A 112     2367   3406   3684    212    208    -73       N  
ATOM   1039  NZ BLYS A 112       7.418  -3.755   4.765  0.50 23.17           N  
ANISOU 1039  NZ BLYS A 112     2216   3083   3503   -247    -97   -236       N  
ATOM   1040  N  ALEU A 113       9.668   2.815   5.124  0.50 11.40           N  
ANISOU 1040  N  ALEU A 113      271   1814   2245   -129    135   -176       N  
ATOM   1041  N  BLEU A 113       9.652   2.840   5.185  0.50 11.76           N  
ANISOU 1041  N  BLEU A 113      269   1921   2277   -119    132   -172       N  
ATOM   1042  CA ALEU A 113      10.018   4.010   5.903  0.50 11.48           C  
ANISOU 1042  CA ALEU A 113      288   1914   2159   -112    232    -91       C  
ATOM   1043  CA BLEU A 113      10.013   4.047   5.962  0.50 11.57           C  
ANISOU 1043  CA BLEU A 113      285   1948   2162    -89    233    -83       C  
ATOM   1044  C  ALEU A 113      10.384   3.524   7.296  0.50 11.40           C  
ANISOU 1044  C  ALEU A 113      293   1822   2215   -215    159   -141       C  
ATOM   1045  C  BLEU A 113      10.385   3.523   7.325  0.50 11.41           C  
ANISOU 1045  C  BLEU A 113      289   1828   2216   -202    157   -140       C  
ATOM   1046  O  ALEU A 113       9.554   2.911   7.989  0.50 12.67           O  
ANISOU 1046  O  ALEU A 113      306   2069   2438   -170     99     -9       O  
ATOM   1047  O  BLEU A 113       9.577   2.869   8.015  0.50 12.48           O  
ANISOU 1047  O  BLEU A 113      258   2034   2448    -86     47    -10       O  
ATOM   1048  CB ALEU A 113       8.803   4.932   5.937  0.50 12.57           C  
ANISOU 1048  CB ALEU A 113      262   2061   2451   -117     72   -194       C  
ATOM   1049  CB BLEU A 113       8.815   5.005   6.038  0.50 12.60           C  
ANISOU 1049  CB BLEU A 113      259   2047   2479    -68     95   -180       C  
ATOM   1050  CG ALEU A 113       9.057   6.244   6.676  0.50 14.60           C  
ANISOU 1050  CG ALEU A 113      621   2234   2690     59      5   -179       C  
ATOM   1051  CG BLEU A 113       9.117   6.446   6.490  0.50 13.54           C  
ANISOU 1051  CG BLEU A 113      279   2256   2609    229      0   -188       C  
ATOM   1052  CD1ALEU A 113       9.091   6.036   8.153  0.50 19.01           C  
ANISOU 1052  CD1ALEU A 113     1451   2713   3057   -424    186      6       C  
ATOM   1053  CD1BLEU A 113       7.962   7.376   6.074  0.50 11.15           C  
ANISOU 1053  CD1BLEU A 113      259   1470   2507     53   -104   -226       C  
ATOM   1054  CD2ALEU A 113      10.336   6.896   6.149  0.50 15.40           C  
ANISOU 1054  CD2ALEU A 113      647   2111   3091   -111   -155   -133       C  
ATOM   1055  CD2BLEU A 113       9.222   6.489   7.931  0.50 13.78           C  
ANISOU 1055  CD2BLEU A 113      283   2332   2621    153    240    482       C  
ATOM   1056  N   VAL A 114      11.673   3.708   7.640  1.00 11.38           N  
ANISOU 1056  N   VAL A 114      282   1831   2210   -204     77    -37       N  
ATOM   1057  CA  VAL A 114      12.179   3.217   8.900  1.00 11.61           C  
ANISOU 1057  CA  VAL A 114      301   1843   2266   -127    272     49       C  
ATOM   1058  C   VAL A 114      12.278   4.375   9.903  1.00 11.38           C  
ANISOU 1058  C   VAL A 114      258   1837   2229    -80     34     -5       C  
ATOM   1059  O   VAL A 114      12.670   5.485   9.577  1.00 12.44           O  
ANISOU 1059  O   VAL A 114      507   1896   2320   -123    132     20       O  
ATOM   1060  CB  VAL A 114      13.506   2.592   8.674  1.00 12.94           C  
ANISOU 1060  CB  VAL A 114      413   1964   2538   -163     75     -6       C  
ATOM   1061  CG1 VAL A 114      14.165   2.067  10.028  1.00 15.53           C  
ANISOU 1061  CG1 VAL A 114      970   2268   2660     82   -235   -108       C  
ATOM   1062  CG2 VAL A 114      13.397   1.494   7.635  1.00 14.79           C  
ANISOU 1062  CG2 VAL A 114      886   2093   2640    146    172   -111       C  
ATOM   1063  N   VAL A 115      11.782   4.118  11.116  1.00 11.74           N  
ANISOU 1063  N   VAL A 115      458   1661   2340   -121   -115    -27       N  
ATOM   1064  CA  VAL A 115      11.752   5.047  12.178  1.00 11.02           C  
ANISOU 1064  CA  VAL A 115      254   1487   2445     18    -34     78       C  
ATOM   1065  C   VAL A 115      12.710   4.555  13.275  1.00 11.70           C  
ANISOU 1065  C   VAL A 115      614   1528   2303    -24    -82     22       C  
ATOM   1066  O   VAL A 115      12.609   3.442  13.703  1.00 13.29           O  
ANISOU 1066  O   VAL A 115      734   1683   2633   -122   -272    125       O  
ATOM   1067  CB  VAL A 115      10.363   5.179  12.727  1.00 11.90           C  
ANISOU 1067  CB  VAL A 115      253   1625   2644     -6    -19   -118       C  
ATOM   1068  CG1 VAL A 115      10.370   6.121  13.896  1.00 16.30           C  
ANISOU 1068  CG1 VAL A 115      320   2679   3193     73     82   -377       C  
ATOM   1069  CG2 VAL A 115       9.349   5.628  11.616  1.00 15.07           C  
ANISOU 1069  CG2 VAL A 115      270   2178   3277    -64   -219    197       C  
ATOM   1070  N  AGLU A 116      13.572   5.457  13.716  0.50 11.44           N  
ANISOU 1070  N  AGLU A 116      480   1607   2256    -37   -124     87       N  
ATOM   1071  N  BGLU A 116      13.658   5.385  13.671  0.50 11.81           N  
ANISOU 1071  N  BGLU A 116      690   1538   2259   -115    -52     75       N  
ATOM   1072  CA AGLU A 116      14.532   5.185  14.761  0.50 10.79           C  
ANISOU 1072  CA AGLU A 116      312   1542   2244     45    -40     43       C  
ATOM   1073  CA BGLU A 116      14.442   5.110  14.861  0.50 11.57           C  
ANISOU 1073  CA BGLU A 116      614   1549   2233    -75     37     37       C  
ATOM   1074  C  AGLU A 116      14.290   6.152  15.936  0.50 11.06           C  
ANISOU 1074  C  AGLU A 116      345   1632   2224      8   -266     54       C  
ATOM   1075  C  BGLU A 116      14.136   6.135  15.907  0.50 11.64           C  
ANISOU 1075  C  BGLU A 116      605   1610   2207    -37   -240     22       C  
ATOM   1076  O  AGLU A 116      14.523   7.343  15.788  0.50 11.51           O  
ANISOU 1076  O  AGLU A 116      353   1615   2406     16   -235     54       O  
ATOM   1077  O  BGLU A 116      14.150   7.321  15.641  0.50 13.06           O  
ANISOU 1077  O  BGLU A 116     1025   1597   2341    103   -293     84       O  
ATOM   1078  CB AGLU A 116      15.970   5.358  14.224  0.50 11.37           C  
ANISOU 1078  CB AGLU A 116      292   1694   2332    126   -236     55       C  
ATOM   1079  CB BGLU A 116      15.917   5.195  14.621  0.50 11.97           C  
ANISOU 1079  CB BGLU A 116      652   1685   2208    -95    -82     92       C  
ATOM   1080  CG AGLU A 116      17.068   4.933  15.268  0.50 12.30           C  
ANISOU 1080  CG AGLU A 116      352   2004   2315    414    -52    -23       C  
ATOM   1081  CG BGLU A 116      16.508   4.036  13.953  0.50 15.42           C  
ANISOU 1081  CG BGLU A 116     1246   2015   2596    -48    176     55       C  
ATOM   1082  CD AGLU A 116      18.487   5.582  15.112  0.50 14.15           C  
ANISOU 1082  CD AGLU A 116      292   2457   2625    283     30   -214       C  
ATOM   1083  CD BGLU A 116      18.033   4.088  13.996  0.50 18.75           C  
ANISOU 1083  CD BGLU A 116     1359   2615   3149   -166    133     -8       C  
ATOM   1084  OE1AGLU A 116      19.498   4.861  15.057  0.50 16.39           O  
ANISOU 1084  OE1AGLU A 116      281   2797   3146    129   -246     81       O  
ATOM   1085  OE1BGLU A 116      18.613   5.064  14.525  0.50 19.24           O  
ANISOU 1085  OE1BGLU A 116     1089   2846   3372    272     27   -377       O  
ATOM   1086  OE2AGLU A 116      18.582   6.824  15.086  0.50 16.88           O  
ANISOU 1086  OE2AGLU A 116      266   2630   3517   -145    120     14       O  
ATOM   1087  OE2BGLU A 116      18.628   3.121  13.534  0.50 20.97           O  
ANISOU 1087  OE2BGLU A 116     1025   3131   3811    299   -284    103       O  
ATOM   1088  N   CYS A 117      13.851   5.640  17.096  1.00 12.29           N  
ANISOU 1088  N   CYS A 117      734   1642   2292     58   -138     32       N  
ATOM   1089  CA  CYS A 117      13.556   6.441  18.273  1.00 11.61           C  
ANISOU 1089  CA  CYS A 117      300   1688   2421    188   -162      9       C  
ATOM   1090  C   CYS A 117      14.708   6.232  19.242  1.00 11.65           C  
ANISOU 1090  C   CYS A 117      449   1596   2382    148   -183    -54       C  
ATOM   1091  O   CYS A 117      14.923   5.106  19.601  1.00 12.30           O  
ANISOU 1091  O   CYS A 117      312   1614   2747    153   -231     29       O  
ATOM   1092  CB  CYS A 117      12.228   6.017  18.895  1.00 13.21           C  
ANISOU 1092  CB  CYS A 117      347   2058   2613    398   -152   -152       C  
ATOM   1093  SG  CYS A 117      10.818   5.999  17.786  1.00 17.50           S  
ANISOU 1093  SG  CYS A 117      389   3227   3032    153   -193    149       S  
ATOM   1094  N   VAL A 118      15.288   7.308  19.701  1.00 11.85           N  
ANISOU 1094  N   VAL A 118      324   1744   2433    126    -42    -80       N  
ATOM   1095  CA  VAL A 118      16.477   7.247  20.506  1.00 11.78           C  
ANISOU 1095  CA  VAL A 118      253   1710   2512    -16     -5     31       C  
ATOM   1096  C   VAL A 118      16.268   8.083  21.758  1.00 11.50           C  
ANISOU 1096  C   VAL A 118      256   1681   2433    -66    -35     -2       C  
ATOM   1097  O   VAL A 118      15.959   9.281  21.702  1.00 11.45           O  
ANISOU 1097  O   VAL A 118      272   1565   2511    147    -68     46       O  
ATOM   1098  CB  VAL A 118      17.791   7.706  19.784  1.00 14.73           C  
ANISOU 1098  CB  VAL A 118      578   2154   2861   -186    144     -5       C  
ATOM   1099  CG1 VAL A 118      18.959   7.849  20.781  1.00 16.19           C  
ANISOU 1099  CG1 VAL A 118      365   2425   3360   -106    199     81       C  
ATOM   1100  CG2 VAL A 118      18.139   6.753  18.696  1.00 17.79           C  
ANISOU 1100  CG2 VAL A 118     1365   2486   2908   -363    259   -152       C  
ATOM   1101  N   MET A 119      16.491   7.457  22.907  1.00 12.32           N  
ANISOU 1101  N   MET A 119      549   1633   2497    142   -124     -7       N  
ATOM   1102  CA AMET A 119      16.484   8.105  24.205  0.50 12.78           C  
ANISOU 1102  CA AMET A 119      398   1895   2563    100   -177     24       C  
ATOM   1103  CA BMET A 119      16.540   8.158  24.175  0.50 13.36           C  
ANISOU 1103  CA BMET A 119      555   1938   2583    169   -177      9       C  
ATOM   1104  C   MET A 119      17.746   7.596  24.917  1.00 13.18           C  
ANISOU 1104  C   MET A 119      302   2156   2549     49   -160    -11       C  
ATOM   1105  O   MET A 119      17.798   6.444  25.279  1.00 12.76           O  
ANISOU 1105  O   MET A 119      275   1900   2669    163   -118     64       O  
ATOM   1106  CB AMET A 119      15.206   7.754  24.963  0.50 13.21           C  
ANISOU 1106  CB AMET A 119      306   2118   2595    205    -15    -27       C  
ATOM   1107  CB BMET A 119      15.240   8.033  24.956  0.50 13.73           C  
ANISOU 1107  CB BMET A 119      485   2101   2631    286    -79    -52       C  
ATOM   1108  CG AMET A 119      15.027   8.469  26.286  0.50 13.77           C  
ANISOU 1108  CG AMET A 119      682   1880   2669    136   -335     -1       C  
ATOM   1109  CG BMET A 119      15.321   8.413  26.421  0.50 15.80           C  
ANISOU 1109  CG BMET A 119      874   2336   2791    537    -85    -34       C  
ATOM   1110  SD AMET A 119      15.161  10.259  26.124  0.50 13.02           S  
ANISOU 1110  SD AMET A 119      612   1832   2503     88    227    121       S  
ATOM   1111  SD BMET A 119      14.525   9.967  26.676  0.50 19.13           S  
ANISOU 1111  SD BMET A 119     1631   2735   2899    650     77   -167       S  
ATOM   1112  CE AMET A 119      14.894  10.803  27.820  0.50 14.60           C  
ANISOU 1112  CE AMET A 119     1244   1692   2610   -166   -534    328       C  
ATOM   1113  CE BMET A 119      15.237  10.502  28.242  0.50 18.58           C  
ANISOU 1113  CE BMET A 119     1946   2365   2749    449   -211     73       C  
ATOM   1114  N   LYS A 120      18.778   8.436  25.067  1.00 14.21           N  
ANISOU 1114  N   LYS A 120      470   2112   2814     33   -220    -31       N  
ATOM   1115  CA  LYS A 120      20.043   8.107  25.650  1.00 14.96           C  
ANISOU 1115  CA  LYS A 120      586   2185   2911    -75   -279   -104       C  
ATOM   1116  C   LYS A 120      20.601   6.880  24.918  1.00 13.95           C  
ANISOU 1116  C   LYS A 120      289   2127   2881   -178   -225      0       C  
ATOM   1117  O   LYS A 120      20.711   6.898  23.683  1.00 15.73           O  
ANISOU 1117  O   LYS A 120      314   2392   3271    137    -65     78       O  
ATOM   1118  CB  LYS A 120      19.917   7.964  27.171  1.00 15.60           C  
ANISOU 1118  CB  LYS A 120      687   2309   2930   -147   -458     -1       C  
ATOM   1119  CG  LYS A 120      19.527   9.295  27.901  1.00 21.19           C  
ANISOU 1119  CG  LYS A 120     2029   2724   3296    279   -434    -72       C  
ATOM   1120  CD  LYS A 120      18.659   9.113  29.129  1.00 27.72           C  
ANISOU 1120  CD  LYS A 120     3352   3462   3717    189   -182   -109       C  
ATOM   1121  CE  LYS A 120      19.286   8.441  30.315  1.00 32.21           C  
ANISOU 1121  CE  LYS A 120     4009   4138   4089    217    -84     76       C  
ATOM   1122  NZ  LYS A 120      18.197   8.235  31.352  1.00 33.45           N  
ANISOU 1122  NZ  LYS A 120     3839   4691   4179    442    -39     18       N  
ATOM   1123  N   GLY A 121      20.832   5.801  25.612  1.00 13.59           N  
ANISOU 1123  N   GLY A 121      270   1935   2956     79   -185    110       N  
ATOM   1124  CA  GLY A 121      21.475   4.653  24.961  1.00 13.72           C  
ANISOU 1124  CA  GLY A 121      279   2004   2928    -42   -259     54       C  
ATOM   1125  C   GLY A 121      20.427   3.668  24.447  1.00 12.41           C  
ANISOU 1125  C   GLY A 121      284   1798   2633   -113   -246    178       C  
ATOM   1126  O   GLY A 121      20.755   2.577  24.004  1.00 13.13           O  
ANISOU 1126  O   GLY A 121      259   1929   2800    -98     32    158       O  
ATOM   1127  N   VAL A 122      19.082   3.980  24.561  1.00 12.42           N  
ANISOU 1127  N   VAL A 122      262   1851   2604      6   -142    272       N  
ATOM   1128  CA  VAL A 122      18.009   3.049  24.131  1.00 12.06           C  
ANISOU 1128  CA  VAL A 122      276   1905   2398   -124    167    100       C  
ATOM   1129  C   VAL A 122      17.513   3.481  22.777  1.00 11.67           C  
ANISOU 1129  C   VAL A 122      261   1828   2341     76    109    165       C  
ATOM   1130  O   VAL A 122      17.087   4.653  22.612  1.00 13.49           O  
ANISOU 1130  O   VAL A 122      699   1747   2678    250   -261     -6       O  
ATOM   1131  CB  VAL A 122      16.891   2.990  25.165  1.00 13.13           C  
ANISOU 1131  CB  VAL A 122      274   2019   2694     90    211    186       C  
ATOM   1132  CG1 VAL A 122      15.786   2.007  24.695  1.00 15.93           C  
ANISOU 1132  CG1 VAL A 122      313   2497   3241   -202    335    171       C  
ATOM   1133  CG2 VAL A 122      17.464   2.537  26.506  1.00 15.22           C  
ANISOU 1133  CG2 VAL A 122      332   2723   2727    167    426    277       C  
ATOM   1134  N   THR A 123      17.504   2.562  21.842  1.00 12.01           N  
ANISOU 1134  N   THR A 123      276   1822   2465    169    -99     66       N  
ATOM   1135  CA  THR A 123      16.981   2.779  20.484  1.00 13.35           C  
ANISOU 1135  CA  THR A 123      559   1897   2615    -58     60     35       C  
ATOM   1136  C   THR A 123      15.878   1.792  20.206  1.00 13.24           C  
ANISOU 1136  C   THR A 123      674   1692   2661    108   -147    -33       C  
ATOM   1137  O   THR A 123      16.016   0.618  20.466  1.00 16.32           O  
ANISOU 1137  O   THR A 123      902   1861   3436    -30   -597    290       O  
ATOM   1138  CB  THR A 123      18.068   2.666  19.454  1.00 15.24           C  
ANISOU 1138  CB  THR A 123      751   2308   2731    -34    139     48       C  
ATOM   1139  OG1 THR A 123      19.085   3.579  19.787  1.00 18.43           O  
ANISOU 1139  OG1 THR A 123      525   3077   3398   -124    330     45       O  
ATOM   1140  CG2 THR A 123      17.581   2.962  18.059  1.00 16.41           C  
ANISOU 1140  CG2 THR A 123      780   2797   2659    134    270   -102       C  
ATOM   1141  N   SER A 124      14.820   2.276  19.599  1.00 12.55           N  
ANISOU 1141  N   SER A 124      426   1723   2618    -31   -209     89       N  
ATOM   1142  CA  SER A 124      13.784   1.470  19.033  1.00 11.47           C  
ANISOU 1142  CA  SER A 124      264   1591   2502     55   -133    216       C  
ATOM   1143  C   SER A 124      13.677   1.679  17.566  1.00 11.16           C  
ANISOU 1143  C   SER A 124      282   1595   2362    190     75     80       C  
ATOM   1144  O   SER A 124      13.731   2.790  17.124  1.00 13.43           O  
ANISOU 1144  O   SER A 124      963   1634   2503     28     14    107       O  
ATOM   1145  CB  SER A 124      12.421   1.761  19.680  1.00 11.77           C  
ANISOU 1145  CB  SER A 124      260   1731   2479     52    -93    275       C  
ATOM   1146  OG  SER A 124      11.291   1.174  19.088  1.00 13.38           O  
ANISOU 1146  OG  SER A 124      271   2138   2673   -116    153    111       O  
ATOM   1147  N   THR A 125      13.478   0.604  16.812  1.00 11.35           N  
ANISOU 1147  N   THR A 125      257   1582   2470     77      6     73       N  
ATOM   1148  CA  THR A 125      13.295   0.642  15.403  1.00 12.00           C  
ANISOU 1148  CA  THR A 125      260   1818   2480     88     81    153       C  
ATOM   1149  C   THR A 125      11.892   0.192  15.041  1.00 11.55           C  
ANISOU 1149  C   THR A 125      254   1775   2357     42    -10    116       C  
ATOM   1150  O   THR A 125      11.481  -0.895  15.413  1.00 12.91           O  
ANISOU 1150  O   THR A 125      485   1816   2602    -96   -127    149       O  
ATOM   1151  CB  THR A 125      14.335  -0.204  14.685  1.00 13.62           C  
ANISOU 1151  CB  THR A 125      310   2215   2648    243    134    130       C  
ATOM   1152  OG1 THR A 125      15.638   0.238  15.046  1.00 15.93           O  
ANISOU 1152  OG1 THR A 125      336   2687   3027    391    216   -141       O  
ATOM   1153  CG2 THR A 125      14.194  -0.150  13.147  1.00 16.72           C  
ANISOU 1153  CG2 THR A 125      402   3022   2926    179    396   -100       C  
ATOM   1154  N   ARG A 126      11.222   1.005  14.235  1.00 11.46           N  
ANISOU 1154  N   ARG A 126      263   1729   2363    -89   -102     99       N  
ATOM   1155  CA  ARG A 126       9.847   0.751  13.798  1.00 11.26           C  
ANISOU 1155  CA  ARG A 126      293   1709   2274   -217   -132     73       C  
ATOM   1156  C   ARG A 126       9.843   0.838  12.296  1.00 12.08           C  
ANISOU 1156  C   ARG A 126      259   1917   2412    -81     75     15       C  
ATOM   1157  O   ARG A 126      10.443   1.744  11.713  1.00 15.62           O  
ANISOU 1157  O   ARG A 126     1182   2103   2648   -618    -39    150       O  
ATOM   1158  CB  ARG A 126       8.883   1.743  14.460  1.00 12.55           C  
ANISOU 1158  CB  ARG A 126      320   2007   2442   -112     -6     -4       C  
ATOM   1159  CG  ARG A 126       8.735   1.451  15.943  1.00 13.90           C  
ANISOU 1159  CG  ARG A 126      286   2295   2700     66   -276    -94       C  
ATOM   1160  CD  ARG A 126       8.159   2.547  16.725  1.00 15.51           C  
ANISOU 1160  CD  ARG A 126      266   2911   2716    -11    181   -208       C  
ATOM   1161  NE  ARG A 126       6.757   2.792  16.479  1.00 16.79           N  
ANISOU 1161  NE  ARG A 126      303   3147   2930     37    355   -367       N  
ATOM   1162  CZ  ARG A 126       5.702   2.150  17.010  1.00 16.14           C  
ANISOU 1162  CZ  ARG A 126      275   3128   2729   -232    121   -377       C  
ATOM   1163  NH1 ARG A 126       5.817   1.017  17.681  1.00 17.35           N  
ANISOU 1163  NH1 ARG A 126      332   3491   2768   -474    173   -105       N  
ATOM   1164  NH2 ARG A 126       4.482   2.600  16.816  1.00 18.28           N  
ANISOU 1164  NH2 ARG A 126      383   3499   3061   -343    228   -213       N  
ATOM   1165  N   VAL A 127       9.235  -0.154  11.620  1.00 11.53           N  
ANISOU 1165  N   VAL A 127      258   1752   2369    -84    -33    -82       N  
ATOM   1166  CA  VAL A 127       9.270  -0.215  10.197  1.00 11.54           C  
ANISOU 1166  CA  VAL A 127      268   1673   2444   -110   -121     51       C  
ATOM   1167  C   VAL A 127       7.840  -0.059   9.688  1.00 10.94           C  
ANISOU 1167  C   VAL A 127      258   1624   2274    -79    -29    -47       C  
ATOM   1168  O   VAL A 127       6.925  -0.726  10.143  1.00 12.43           O  
ANISOU 1168  O   VAL A 127      342   2005   2373   -389     56    108       O  
ATOM   1169  CB  VAL A 127       9.855  -1.557   9.697  1.00 12.49           C  
ANISOU 1169  CB  VAL A 127      258   1937   2550    -85     50    -99       C  
ATOM   1170  CG1 VAL A 127       9.901  -1.577   8.180  1.00 15.14           C  
ANISOU 1170  CG1 VAL A 127      519   2484   2746    264     -6   -247       C  
ATOM   1171  CG2 VAL A 127      11.278  -1.744  10.272  1.00 15.06           C  
ANISOU 1171  CG2 VAL A 127      423   2209   3088     46    315     43       C  
ATOM   1172  N   TYR A 128       7.695   0.832   8.722  1.00 11.40           N  
ANISOU 1172  N   TYR A 128      266   1811   2254   -139    -48     50       N  
ATOM   1173  CA  TYR A 128       6.416   1.064   8.052  1.00 10.87           C  
ANISOU 1173  CA  TYR A 128      257   1676   2196      6    -86    -14       C  
ATOM   1174  C   TYR A 128       6.528   0.732   6.580  1.00 11.70           C  
ANISOU 1174  C   TYR A 128      274   1782   2388   -136   -148     77       C  
ATOM   1175  O   TYR A 128       7.552   0.929   5.939  1.00 12.92           O  
ANISOU 1175  O   TYR A 128      352   2074   2480   -231    105   -132       O  
ATOM   1176  CB  TYR A 128       6.054   2.551   8.154  1.00 11.73           C  
ANISOU 1176  CB  TYR A 128      297   1881   2278   -191   -210      8       C  
ATOM   1177  CG  TYR A 128       5.686   3.065   9.516  1.00 11.27           C  
ANISOU 1177  CG  TYR A 128      276   1699   2304   -118   -162    -18       C  
ATOM   1178  CD1 TYR A 128       6.603   3.318  10.498  1.00 12.61           C  
ANISOU 1178  CD1 TYR A 128      490   1777   2521    -74    -59    -56       C  
ATOM   1179  CD2 TYR A 128       4.329   3.259   9.798  1.00 11.87           C  
ANISOU 1179  CD2 TYR A 128      307   1742   2459    -42    -75    -10       C  
ATOM   1180  CE1 TYR A 128       6.193   3.750  11.765  1.00 14.12           C  
ANISOU 1180  CE1 TYR A 128      782   2014   2569   -168   -416      7       C  
ATOM   1181  CE2 TYR A 128       3.928   3.700  11.021  1.00 13.63           C  
ANISOU 1181  CE2 TYR A 128      712   1907   2559   -148     36     90       C  
ATOM   1182  CZ  TYR A 128       4.836   3.933  12.014  1.00 13.72           C  
ANISOU 1182  CZ  TYR A 128      622   2089   2503   -230     66      8       C  
ATOM   1183  OH  TYR A 128       4.440   4.378  13.266  1.00 16.15           O  
ANISOU 1183  OH  TYR A 128      814   2618   2702     -1    -15    -66       O  
ATOM   1184  N  AGLU A 129       5.421   0.268   6.013  0.50 12.67           N  
ANISOU 1184  N  AGLU A 129      268   2112   2433   -122   -124    -51       N  
ATOM   1185  N  BGLU A 129       5.402   0.234   6.065  0.50 12.52           N  
ANISOU 1185  N  BGLU A 129      273   2054   2426   -171    -92    -15       N  
ATOM   1186  CA AGLU A 129       5.357   0.032   4.578  0.50 13.55           C  
ANISOU 1186  CA AGLU A 129      552   2162   2434     15   -148   -127       C  
ATOM   1187  CA BGLU A 129       5.243  -0.124   4.657  0.50 13.60           C  
ANISOU 1187  CA BGLU A 129      668   2078   2421    -29    -84    -56       C  
ATOM   1188  C  AGLU A 129       4.192   0.816   4.023  0.50 12.63           C  
ANISOU 1188  C  AGLU A 129      259   2181   2357    -58    -94   -162       C  
ATOM   1189  C  BGLU A 129       4.154   0.756   4.034  0.50 12.56           C  
ANISOU 1189  C  BGLU A 129      262   2140   2369    -90    -98   -135       C  
ATOM   1190  O  AGLU A 129       3.349   1.311   4.755  0.50 13.27           O  
ANISOU 1190  O  AGLU A 129      270   2210   2560   -151    103   -105       O  
ATOM   1191  O  BGLU A 129       3.305   1.269   4.750  0.50 14.02           O  
ANISOU 1191  O  BGLU A 129      533   2198   2592    -44     95    -83       O  
ATOM   1192  CB AGLU A 129       5.151  -1.461   4.285  0.50 15.17           C  
ANISOU 1192  CB AGLU A 129     1063   2247   2453    167   -178   -206       C  
ATOM   1193  CB BGLU A 129       4.866  -1.623   4.527  0.50 14.23           C  
ANISOU 1193  CB BGLU A 129      881   2094   2430     94    -66    -55       C  
ATOM   1194  CG AGLU A 129       6.382  -2.242   4.705  0.50 16.76           C  
ANISOU 1194  CG AGLU A 129     1052   2651   2665    144   -241   -200       C  
ATOM   1195  CG BGLU A 129       3.456  -2.053   4.628  0.50 17.77           C  
ANISOU 1195  CG BGLU A 129     1567   2445   2740     32   -104     96       C  
ATOM   1196  CD AGLU A 129       6.399  -3.726   4.353  0.50 19.50           C  
ANISOU 1196  CD AGLU A 129     1092   3233   3084     30   -422   -406       C  
ATOM   1197  CD BGLU A 129       3.389  -3.560   4.327  0.50 21.84           C  
ANISOU 1197  CD BGLU A 129     2468   2737   3091     -2   -117    -41       C  
ATOM   1198  OE1AGLU A 129       5.329  -4.290   4.057  0.50 21.60           O  
ANISOU 1198  OE1AGLU A 129      941   3372   3892   -165   -409   -104       O  
ATOM   1199  OE1BGLU A 129       2.327  -4.173   4.355  0.50 26.91           O  
ANISOU 1199  OE1BGLU A 129     3164   3155   3905   -332    -28    226       O  
ATOM   1200  OE2AGLU A 129       7.512  -4.307   4.399  0.50 26.13           O  
ANISOU 1200  OE2AGLU A 129     2097   3717   4111    310   -354   -477       O  
ATOM   1201  OE2BGLU A 129       4.438  -4.143   4.045  0.50 25.90           O  
ANISOU 1201  OE2BGLU A 129     3177   3018   3645    357    115   -197       O  
ATOM   1202  N   ARG A 130       4.152   0.949   2.718  1.00 13.38           N  
ANISOU 1202  N   ARG A 130      254   2336   2491    -50    -23   -204       N  
ATOM   1203  CA  ARG A 130       3.026   1.659   2.083  1.00 14.20           C  
ANISOU 1203  CA  ARG A 130      270   2497   2626     41   -200   -188       C  
ATOM   1204  C   ARG A 130       1.708   0.976   2.331  1.00 15.04           C  
ANISOU 1204  C   ARG A 130      337   2467   2911    -45   -354   -187       C  
ATOM   1205  O   ARG A 130       1.618  -0.270   2.265  1.00 16.40           O  
ANISOU 1205  O   ARG A 130      390   2398   3440    -38   -287   -265       O  
ATOM   1206  CB  ARG A 130       3.245   1.754   0.582  1.00 16.41           C  
ANISOU 1206  CB  ARG A 130      686   2793   2755     33   -386   -117       C  
ATOM   1207  CG  ARG A 130       4.450   2.449   0.202  1.00 17.07           C  
ANISOU 1207  CG  ARG A 130      882   2889   2712     31   -257     57       C  
ATOM   1208  CD  ARG A 130       4.250   3.898   0.079  1.00 19.70           C  
ANISOU 1208  CD  ARG A 130     1046   2767   3670   -182    -42   -140       C  
ATOM   1209  NE  ARG A 130       5.408   4.594  -0.463  1.00 19.46           N  
ANISOU 1209  NE  ARG A 130     1310   2573   3510    -93     -8   -117       N  
ATOM   1210  CZ  ARG A 130       5.469   5.906  -0.613  1.00 17.12           C  
ANISOU 1210  CZ  ARG A 130      973   2501   3030   -163   -133    222       C  
ATOM   1211  NH1 ARG A 130       4.431   6.635  -0.344  1.00 17.71           N  
ANISOU 1211  NH1 ARG A 130     1161   2433   3135    -40   -292     36       N  
ATOM   1212  NH2 ARG A 130       6.601   6.463  -0.991  1.00 19.43           N  
ANISOU 1212  NH2 ARG A 130     1344   2589   3447   -336     23    -18       N  
ATOM   1213  N   ALA A 131       0.686   1.755   2.607  1.00 15.89           N  
ANISOU 1213  N   ALA A 131      313   2522   3203   -146   -329   -126       N  
ATOM   1214  CA  ALA A 131      -0.643   1.275   2.853  1.00 17.94           C  
ANISOU 1214  CA  ALA A 131      627   2752   3436   -303   -225    -28       C  
ATOM   1215  C   ALA A 131      -1.166   0.764   1.517  1.00 20.87           C  
ANISOU 1215  C   ALA A 131     1181   3137   3611   -621   -288    -14       C  
ATOM   1216  O   ALA A 131      -0.745   1.127   0.423  1.00 24.82           O  
ANISOU 1216  O   ALA A 131     1903   3643   3882   -555   -580     32       O  
ATOM   1217  CB  ALA A 131      -1.422   2.353   3.404  1.00 20.69           C  
ANISOU 1217  CB  ALA A 131     1328   2806   3726   -265     -7    -59       C  
TER    1218      ALA A 131                                                      
HETATM 1219  C1  IZP A 133       5.452   5.863  15.792  1.00 21.68           C  
ANISOU 1219  C1  IZP A 133      899   3506   3830     79    231     67       C  
HETATM 1220  O1  IZP A 133       4.386   5.453  16.325  1.00 24.28           O  
ANISOU 1220  O1  IZP A 133     1589   3815   3818   -386    -94   -433       O  
HETATM 1221  C2  IZP A 133       6.335   8.688  21.600  1.00 25.46           C  
ANISOU 1221  C2  IZP A 133     3430   3134   3109    386   -187     -3       C  
HETATM 1222  O2  IZP A 133       6.260   5.178  15.100  1.00 20.27           O  
ANISOU 1222  O2  IZP A 133      909   3618   3172    379   -230   -207       O  
HETATM 1223  C3  IZP A 133       6.278   7.472  22.505  1.00 25.98           C  
ANISOU 1223  C3  IZP A 133     3561   3112   3196    330    129     -7       C  
HETATM 1224  C4  IZP A 133       4.816   7.056  22.669  1.00 27.43           C  
ANISOU 1224  C4  IZP A 133     3573   3269   3579    428    393    106       C  
HETATM 1225  C5  IZP A 133       6.991   7.759  23.834  1.00 26.91           C  
ANISOU 1225  C5  IZP A 133     3900   2903   3419    495    -14    182       C  
HETATM 1226  C6  IZP A 133       5.731   7.384  15.929  1.00 19.80           C  
ANISOU 1226  C6  IZP A 133     1174   3166   3184    -73     74     59       C  
HETATM 1227  C7  IZP A 133       7.001   7.725  15.128  1.00 25.38           C  
ANISOU 1227  C7  IZP A 133      976   4074   4593    547    451    234       C  
HETATM 1228  C8  IZP A 133       5.950   7.720  17.422  1.00 20.81           C  
ANISOU 1228  C8  IZP A 133     1565   3182   3158    188    109    -32       C  
HETATM 1229  C9  IZP A 133       4.987   8.373  18.114  1.00 21.25           C  
ANISOU 1229  C9  IZP A 133     1822   3178   3070    474   -142      1       C  
HETATM 1230  C10 IZP A 133       5.132   8.678  19.444  1.00 23.46           C  
ANISOU 1230  C10 IZP A 133     2601   3345   2965    475   -182     48       C  
HETATM 1231  C11 IZP A 133       6.262   8.313  20.124  1.00 21.93           C  
ANISOU 1231  C11 IZP A 133     2567   2935   2827    462   -303    -71       C  
HETATM 1232  C12 IZP A 133       7.282   7.627  19.441  1.00 21.01           C  
ANISOU 1232  C12 IZP A 133     1981   2927   3072    257   -352     14       C  
HETATM 1233  C13 IZP A 133       7.112   7.311  18.082  1.00 19.95           C  
ANISOU 1233  C13 IZP A 133     1645   2780   3154    273   -182    114       C  
HETATM 1234  O   HOH A 134      19.622   2.105  15.123  1.00 43.06           O  
ANISOU 1234  O   HOH A 134      455   7917   7989   1146    191  -1860       O  
HETATM 1235  O   HOH A 135       5.916  -7.438  13.112  1.00 33.95           O  
ANISOU 1235  O   HOH A 135     2861   3704   6333   -417   -580    673       O  
HETATM 1236  O   HOH A 136       3.195  -6.869  10.795  1.00 48.70           O  
ANISOU 1236  O   HOH A 136     4477   5135   8889  -1521  -1862   1769       O  
HETATM 1237  O   HOH A 137       9.403  14.789  -6.032  1.00 35.52           O  
ANISOU 1237  O   HOH A 137     3244   4153   6098     88     -5    280       O  
HETATM 1238  O   HOH A 138       7.928  18.242  -1.508  1.00 45.90           O  
ANISOU 1238  O   HOH A 138     3569   7138   6729    -93   3101   -218       O  
HETATM 1239  O   HOH A 139      20.074  16.508  16.423  1.00 38.03           O  
ANISOU 1239  O   HOH A 139      546   6801   7100    694      7   2140       O  
HETATM 1240  O   HOH A 140      13.218  -6.284  30.309  1.00 31.86           O  
ANISOU 1240  O   HOH A 140     2370   3616   6117    -18   1101    657       O  
HETATM 1241  O   HOH A 141       5.408   8.045  34.112  1.00 48.99           O  
ANISOU 1241  O   HOH A 141     7359   7088   4164  -2958   2142  -1625       O  
HETATM 1242  O   HOH A 142      -8.490   5.680  22.080  1.00 39.75           O  
ANISOU 1242  O   HOH A 142      637   6249   8216   -569    518  -2440       O  
HETATM 1243  O   HOH A 143       0.128   5.058  18.227  1.00 43.08           O  
ANISOU 1243  O   HOH A 143     5884   4117   6367     95  -2301    577       O  
HETATM 1244  O   HOH A 144      -2.051  13.376  24.333  1.00 56.55           O  
ANISOU 1244  O   HOH A 144      829   7622  13035   1519   1895    304       O  
HETATM 1245  O   HOH A 145       2.470   6.858  16.362  1.00 35.71           O  
ANISOU 1245  O   HOH A 145     2827   5907   4834    -11    494  -1152       O  
HETATM 1246  O   HOH A 146      20.284  17.057  24.140  1.00 50.46           O  
ANISOU 1246  O   HOH A 146     2629   9080   7461   -656  -1170   2042       O  
HETATM 1247  O   HOH A 147      17.535  -2.908  13.418  1.00 55.40           O  
ANISOU 1247  O   HOH A 147    10472   3150   7425    143   -448   1403       O  
HETATM 1248  O   HOH A 148      21.749  10.139   5.509  1.00 30.64           O  
ANISOU 1248  O   HOH A 148     1520   5327   4792   -116    795   -223       O  
HETATM 1249  O   HOH A 149      -3.408  14.369  19.652  1.00 34.17           O  
ANISOU 1249  O   HOH A 149     2271   4940   5770   -572    558   -686       O  
HETATM 1250  O   HOH A 150       8.323  21.769  26.774  1.00 38.56           O  
ANISOU 1250  O   HOH A 150     7447   2717   4483   -223   -790   -427       O  
HETATM 1251  O   HOH A 151      18.337   0.957   1.599  1.00 37.00           O  
ANISOU 1251  O   HOH A 151     1045   8010   5002    -97    654   -245       O  
HETATM 1252  O   HOH A 152       7.201  25.051  12.314  1.00 12.10           O  
ANISOU 1252  O   HOH A 152      254   1832   2508     13     52   -138       O  
HETATM 1253  O   HOH A 153      18.366  11.617  21.505  1.00 35.88           O  
ANISOU 1253  O   HOH A 153     2387   6598   4645    746      8   -780       O  
HETATM 1254  O   HOH A 154      -1.727  14.500  21.640  1.00 40.90           O  
ANISOU 1254  O   HOH A 154     2354   7008   6175   -431    162  -2111       O  
HETATM 1255  O   HOH A 155      -7.963   8.511  21.420  1.00 44.12           O  
ANISOU 1255  O   HOH A 155     1232   7635   7894    632    841   1779       O  
HETATM 1256  O   HOH A 156      10.403  22.075  12.815  1.00 11.22           O  
ANISOU 1256  O   HOH A 156      253   1625   2382    -19      0    -39       O  
HETATM 1257  O   HOH A 157       8.569  -6.085  20.125  1.00 34.85           O  
ANISOU 1257  O   HOH A 157     1507   5588   6145     -4     14    690       O  
HETATM 1258  O   HOH A 158      11.507  12.210  12.092  1.00 12.68           O  
ANISOU 1258  O   HOH A 158      260   1952   2604   -107      2     20       O  
HETATM 1259  O   HOH A 159      13.785  26.653  15.324  1.00 11.99           O  
ANISOU 1259  O   HOH A 159      269   1775   2508   -140    -85    -23       O  
HETATM 1260  O   HOH A 160       6.849  20.024  29.607  1.00 42.07           O  
ANISOU 1260  O   HOH A 160     5455   7194   3334   1693    116  -1031       O  
HETATM 1261  O   HOH A 161      20.484  10.869  20.053  1.00 37.74           O  
ANISOU 1261  O   HOH A 161     2307   4434   7595   -630   1534  -1499       O  
HETATM 1262  O   HOH A 162      19.621   9.949  17.405  1.00 29.97           O  
ANISOU 1262  O   HOH A 162     2517   3774   5095   -547    -82    720       O  
HETATM 1263  O   HOH A 163      15.395  -6.587  21.305  1.00 31.32           O  
ANISOU 1263  O   HOH A 163     1537   3802   6559   -224     41    103       O  
HETATM 1264  O   HOH A 164      12.405  -7.821  17.039  1.00 37.91           O  
ANISOU 1264  O   HOH A 164     1605   6089   6709   -233    394   -979       O  
HETATM 1265  O   HOH A 165       4.638  24.506  13.376  1.00 12.60           O  
ANISOU 1265  O   HOH A 165      255   2048   2484     51    -49      7       O  
HETATM 1266  O   HOH A 166      14.336   0.600  31.739  1.00 27.76           O  
ANISOU 1266  O   HOH A 166     1452   4998   4097   -242    -72    455       O  
HETATM 1267  O   HOH A 167      14.824  10.407   0.702  1.00 39.57           O  
ANISOU 1267  O   HOH A 167     5715   4390   4927    501    713   -610       O  
HETATM 1268  O   HOH A 168      -1.850   7.905  -0.341  1.00 33.64           O  
ANISOU 1268  O   HOH A 168     5923   3906   2953  -1513    283     -1       O  
HETATM 1269  O   HOH A 169      -3.694  -0.606  21.972  1.00 13.18           O  
ANISOU 1269  O   HOH A 169      321   1978   2705   -290   -235     94       O  
HETATM 1270  O   HOH A 170      -5.549  14.176  15.278  1.00 36.46           O  
ANISOU 1270  O   HOH A 170     2487   4412   6954    468     47   -636       O  
HETATM 1271  O   HOH A 171       0.695   7.645  -1.855  1.00 29.96           O  
ANISOU 1271  O   HOH A 171     3577   3823   3984   -379  -1116    289       O  
HETATM 1272  O   HOH A 172      -2.448  18.930  20.879  1.00 35.17           O  
ANISOU 1272  O   HOH A 172     1884   4884   6593    192    705   1210       O  
HETATM 1273  O   HOH A 173      19.949  20.190  13.919  1.00 30.19           O  
ANISOU 1273  O   HOH A 173     2985   3234   5250   -445    175    -83       O  
HETATM 1274  O   HOH A 174      -0.343  32.004  -4.715  1.00 46.18           O  
ANISOU 1274  O   HOH A 174     8973   4264   4306  -1935  -1532    792       O  
HETATM 1275  O   HOH A 175      14.697  -5.310  -2.186  1.00 34.90           O  
ANISOU 1275  O   HOH A 175     4675   3482   5101    593   -726    365       O  
HETATM 1276  O   HOH A 176       9.291  21.728   1.046  1.00 77.58           O  
ANISOU 1276  O   HOH A 176     4108  17280   8087  -1277    112  -1253       O  
HETATM 1277  O   HOH A 177       5.252  30.570   6.614  1.00 33.64           O  
ANISOU 1277  O   HOH A 177     4835   3756   4189  -1065   1225   -665       O  
HETATM 1278  O   HOH A 178      17.624  12.374  30.357  1.00 40.62           O  
ANISOU 1278  O   HOH A 178     5409   5127   4896   1024  -1280   -332       O  
HETATM 1279  O   HOH A 179      12.999  -7.614  19.971  1.00 32.83           O  
ANISOU 1279  O   HOH A 179     1406   3835   7232    350   -303   -663       O  
HETATM 1280  O   HOH A 180       1.784   8.238  34.464  1.00 49.06           O  
ANISOU 1280  O   HOH A 180     9742   3968   4929  -1345   -919   -969       O  
HETATM 1281  O   HOH A 181       6.212  21.943  -1.418  1.00 39.52           O  
ANISOU 1281  O   HOH A 181     7042   4374   3599    213    456  -1265       O  
HETATM 1282  O   HOH A 182      -3.724  -1.323  19.253  1.00 14.46           O  
ANISOU 1282  O   HOH A 182      313   2347   2835   -347     46    202       O  
HETATM 1283  O   HOH A 183       2.338  -4.988  19.620  1.00 46.87           O  
ANISOU 1283  O   HOH A 183     4328   7104   6373  -1164   1969  -3495       O  
HETATM 1284  O   HOH A 184       9.503   3.082  -3.079  1.00 41.96           O  
ANISOU 1284  O   HOH A 184     5808   4150   5982   1567  -1346  -1411       O  
HETATM 1285  O   HOH A 185       0.975  20.401   5.121  1.00 15.29           O  
ANISOU 1285  O   HOH A 185      357   2673   2780   -309    -50    146       O  
HETATM 1286  O   HOH A 186       8.907  -3.969   0.979  1.00 39.43           O  
ANISOU 1286  O   HOH A 186     3931   5134   5916  -1392   -713   1990       O  
HETATM 1287  O   HOH A 187      -0.102  28.315  -5.760  1.00 44.96           O  
ANISOU 1287  O   HOH A 187     7016   5233   4831  -1170   2085    777       O  
HETATM 1288  O   HOH A 188      13.921  -1.873   4.348  1.00 42.61           O  
ANISOU 1288  O   HOH A 188     2349   6567   7273    934   1148    673       O  
HETATM 1289  O   HOH A 189      23.927  14.347   6.186  1.00 52.42           O  
ANISOU 1289  O   HOH A 189     1507  10318   8092   1391   2903    139       O  
HETATM 1290  O   HOH A 190      14.938  24.861   5.264  1.00 50.63           O  
ANISOU 1290  O   HOH A 190     5262   5488   8486   1196   3750   -322       O  
HETATM 1291  O   HOH A 191       9.804  23.076   5.386  1.00 16.56           O  
ANISOU 1291  O   HOH A 191      338   3145   2805    475   -155   -114       O  
HETATM 1292  O   HOH A 192      15.412   8.941   3.228  1.00 19.29           O  
ANISOU 1292  O   HOH A 192     1622   2488   3218   -512    666   -267       O  
HETATM 1293  O   HOH A 193      20.208  16.313  20.187  1.00 45.87           O  
ANISOU 1293  O   HOH A 193     7177   6197   4053  -1175   -806    131       O  
HETATM 1294  O   HOH A 194       5.798  -5.391  17.930  1.00 42.58           O  
ANISOU 1294  O   HOH A 194     5174   3848   7155   -288     28   1988       O  
HETATM 1295  O   HOH A 195       8.181  17.939  31.983  1.00 54.73           O  
ANISOU 1295  O   HOH A 195     8637   6000   6155   -641   3466  -1140       O  
HETATM 1296  O   HOH A 196      -3.175  33.895 -12.421  1.00 43.39           O  
ANISOU 1296  O   HOH A 196     4349   7292   4843   -877   1286    909       O  
HETATM 1297  O   HOH A 197      15.811  21.953   4.738  1.00 38.01           O  
ANISOU 1297  O   HOH A 197     3948   4988   5505  -1890   -637   2169       O  
HETATM 1298  O   HOH A 198      22.485   1.784  14.383  1.00 41.51           O  
ANISOU 1298  O   HOH A 198     4869   4527   6373   1828    447   1051       O  
HETATM 1299  O   HOH A 199       6.558  11.625  31.088  1.00 33.68           O  
ANISOU 1299  O   HOH A 199     2885   5676   4234   -574    491    258       O  
HETATM 1300  O   HOH A 200      12.627   6.783  32.921  1.00 42.05           O  
ANISOU 1300  O   HOH A 200     2564   9658   3754  -1036   -201   -735       O  
HETATM 1301  O   HOH A 201      -3.842   0.648  16.832  1.00 16.77           O  
ANISOU 1301  O   HOH A 201      263   2915   3192   -158     41     78       O  
HETATM 1302  O   HOH A 202       6.394  -9.166  18.789  1.00 62.47           O  
ANISOU 1302  O   HOH A 202    10043   8033   5657  -4984   4200  -1498       O  
HETATM 1303  O   HOH A 203      13.808  22.700   2.831  1.00 43.42           O  
ANISOU 1303  O   HOH A 203     4890   5852   5755   -662   1258   2365       O  
HETATM 1304  O   HOH A 204      -2.670   5.787  32.396  1.00 49.01           O  
ANISOU 1304  O   HOH A 204     7527   4563   6530   -613     -4    876       O  
HETATM 1305  O   HOH A 205      19.394  12.994  26.120  1.00 45.90           O  
ANISOU 1305  O   HOH A 205     7768   4617   5052   -301  -2003    361       O  
HETATM 1306  O   HOH A 206       4.316  -7.387  28.906  1.00 51.42           O  
ANISOU 1306  O   HOH A 206     5211   9182   5144    366  -1976  -1354       O  
HETATM 1307  O   HOH A 207      -3.251  -1.391   3.387  1.00 46.35           O  
ANISOU 1307  O   HOH A 207     2593   7639   7377  -2020   -421   1467       O  
HETATM 1308  O   HOH A 208      21.689   5.164  16.529  1.00 35.49           O  
ANISOU 1308  O   HOH A 208     1408   6503   5573     51    606    107       O  
HETATM 1309  O   HOH A 209      -2.245   4.902  -0.288  1.00 39.49           O  
ANISOU 1309  O   HOH A 209     2962   5575   6465   -495   -966    656       O  
HETATM 1310  O   HOH A 210       6.536   4.042  35.549  1.00 44.61           O  
ANISOU 1310  O   HOH A 210     7316   5068   4566   1015   -291    230       O  
HETATM 1311  O   HOH A 211      21.096   8.156  15.124  1.00 38.43           O  
ANISOU 1311  O   HOH A 211     2030   4754   7815   -169    909   1037       O  
HETATM 1312  O   HOH A 212      -2.448  19.592  15.068  1.00 41.36           O  
ANISOU 1312  O   HOH A 212     1717   4246   9752    527   -280  -2253       O  
HETATM 1313  O   HOH A 213      -7.191   2.653  23.450  1.00 16.24           O  
ANISOU 1313  O   HOH A 213      259   2365   3543   -107    -59    -68       O  
HETATM 1314  O   HOH A 214      13.606  -9.080  22.831  1.00 52.75           O  
ANISOU 1314  O   HOH A 214     3125   7938   8977    696    203    312       O  
HETATM 1315  O   HOH A 215       4.897  21.582  30.650  1.00 45.83           O  
ANISOU 1315  O   HOH A 215     5890   6820   4701    246   -218  -1375       O  
HETATM 1316  O   HOH A 216       8.677  21.287   2.731  1.00 44.11           O  
ANISOU 1316  O   HOH A 216     7208   3644   5908     70    711  -1255       O  
HETATM 1317  O   HOH A 217       1.550  13.038  14.268  1.00 18.84           O  
ANISOU 1317  O   HOH A 217      798   3195   3164    -21    173    490       O  
HETATM 1318  O   HOH A 218       2.914   1.034  18.646  1.00 18.26           O  
ANISOU 1318  O   HOH A 218      365   3442   3129   -490    134   -245       O  
HETATM 1319  O   HOH A 219      16.239  21.078   7.274  1.00 18.01           O  
ANISOU 1319  O   HOH A 219     1079   2325   3437   -190    201    201       O  
HETATM 1320  O   HOH A 220       8.736  -3.093  20.167  1.00 18.99           O  
ANISOU 1320  O   HOH A 220      570   2897   3748    180   -397   -294       O  
HETATM 1321  O   HOH A 221       6.065  27.574  15.643  1.00 14.44           O  
ANISOU 1321  O   HOH A 221      259   2124   3102     -3   -127    -17       O  
HETATM 1322  O   HOH A 222      22.707   2.050  22.081  1.00 15.50           O  
ANISOU 1322  O   HOH A 222      333   2444   3110   -151    -52   -107       O  
HETATM 1323  O   HOH A 223      -0.525  14.494   6.393  1.00 18.22           O  
ANISOU 1323  O   HOH A 223      612   2631   3677    -79     81    -89       O  
HETATM 1324  O   HOH A 224      13.282  21.589  19.797  1.00 20.60           O  
ANISOU 1324  O   HOH A 224      613   4257   2956   -521    -48    -16       O  
HETATM 1325  O   HOH A 225      -7.179   1.097  25.754  1.00 14.43           O  
ANISOU 1325  O   HOH A 225      268   2418   2794   -181     19    204       O  
HETATM 1326  O   HOH A 226      22.752   4.033  20.688  1.00 13.73           O  
ANISOU 1326  O   HOH A 226      318   1919   2976     65     91    103       O  
HETATM 1327  O   HOH A 227       4.141  27.329   2.473  1.00 18.91           O  
ANISOU 1327  O   HOH A 227     1368   2682   3133     82   -135   -136       O  
HETATM 1328  O   HOH A 228      16.135  18.685  14.153  1.00 21.46           O  
ANISOU 1328  O   HOH A 228      561   3762   3829     -2    -54    384       O  
HETATM 1329  O   HOH A 229       2.857   6.759  13.185  1.00 19.57           O  
ANISOU 1329  O   HOH A 229     1102   2864   3469    -47    501    -15       O  
HETATM 1330  O   HOH A 230      11.272  -3.174  13.660  1.00 18.62           O  
ANISOU 1330  O   HOH A 230     1250   2401   3421   -112   -221    -86       O  
HETATM 1331  O   HOH A 231      20.280   4.869  28.333  1.00 19.37           O  
ANISOU 1331  O   HOH A 231      988   2743   3626    292   -264   -167       O  
HETATM 1332  O   HOH A 232       0.566  18.949  19.257  1.00 23.86           O  
ANISOU 1332  O   HOH A 232     1488   2947   4630   -613   -938    454       O  
HETATM 1333  O   HOH A 233       1.802  15.964  -0.189  1.00 21.35           O  
ANISOU 1333  O   HOH A 233     2577   2788   2745     -4   -802   -227       O  
HETATM 1334  O   HOH A 234       8.918  10.691  21.694  1.00 18.42           O  
ANISOU 1334  O   HOH A 234     1254   2202   3540   -137    336     31       O  
HETATM 1335  O   HOH A 235       1.647   5.956   0.089  1.00 18.16           O  
ANISOU 1335  O   HOH A 235      771   2768   3362   -360     46    -60       O  
HETATM 1336  O   HOH A 236      -0.663  18.857   3.776  1.00 21.16           O  
ANISOU 1336  O   HOH A 236     1595   2737   3706   -235   -912    267       O  
HETATM 1337  O   HOH A 237       2.099  10.114  17.430  1.00 20.23           O  
ANISOU 1337  O   HOH A 237      761   3406   3519     47    224     17       O  
HETATM 1338  O   HOH A 238       6.262  -0.390   1.212  1.00 19.52           O  
ANISOU 1338  O   HOH A 238      860   3039   3516   -104    150   -554       O  
HETATM 1339  O   HOH A 239      20.710   4.881  21.625  1.00 21.12           O  
ANISOU 1339  O   HOH A 239     1000   2917   4105     35   -393    343       O  
HETATM 1340  O   HOH A 240      -2.770  20.307   1.612  1.00 25.47           O  
ANISOU 1340  O   HOH A 240     1970   3982   3723  -1572   -167    321       O  
HETATM 1341  O   HOH A 241      11.310  -5.773  21.073  1.00 21.67           O  
ANISOU 1341  O   HOH A 241     1738   2266   4226   -164    230    466       O  
HETATM 1342  O   HOH A 242      11.338  -2.907   0.779  1.00 23.45           O  
ANISOU 1342  O   HOH A 242     2901   2308   3698   -674     42    -99       O  
HETATM 1343  O   HOH A 243       0.421   5.286  32.226  1.00 23.17           O  
ANISOU 1343  O   HOH A 243     2413   3431   2958   -413   -173     -6       O  
HETATM 1344  O   HOH A 244       3.169  11.808  19.400  1.00 21.35           O  
ANISOU 1344  O   HOH A 244     1805   2844   3461   -511    342     60       O  
HETATM 1345  O   HOH A 245      -0.007   3.106  34.660  1.00 25.56           O  
ANISOU 1345  O   HOH A 245     3580   3421   2710    741    173   -118       O  
HETATM 1346  O   HOH A 246       1.711  26.367   2.114  1.00 22.04           O  
ANISOU 1346  O   HOH A 246     1083   2725   4564   -334   -102   -257       O  
HETATM 1347  O   HOH A 247      -2.133  15.974  17.792  1.00 21.65           O  
ANISOU 1347  O   HOH A 247     1906   2904   3414   -312    387    -70       O  
HETATM 1348  O   HOH A 248       8.471  -3.458  22.754  1.00 27.27           O  
ANISOU 1348  O   HOH A 248     2411   3474   4476   -623    693   -565       O  
HETATM 1349  O   HOH A 249      18.405  11.162  24.129  1.00 22.96           O  
ANISOU 1349  O   HOH A 249     1392   2460   4872   -143    464    404       O  
HETATM 1350  O   HOH A 250      14.586   1.486  29.206  1.00 19.45           O  
ANISOU 1350  O   HOH A 250      908   3164   3318    479   -291    210       O  
HETATM 1351  O   HOH A 251       4.253   9.256  13.080  1.00 20.93           O  
ANISOU 1351  O   HOH A 251      591   3309   4050   -162      0   -135       O  
HETATM 1352  O   HOH A 252      14.761  25.111  17.414  1.00 21.45           O  
ANISOU 1352  O   HOH A 252      864   3375   3909   -161   -383    265       O  
HETATM 1353  O   HOH A 253      17.788  13.834  21.637  1.00 23.36           O  
ANISOU 1353  O   HOH A 253     1452   3859   3561   -421    -23    -51       O  
HETATM 1354  O   HOH A 254      11.078  -3.168  24.544  1.00 21.90           O  
ANISOU 1354  O   HOH A 254     1783   2480   4055    256    437    225       O  
HETATM 1355  O   HOH A 255      18.544   1.444  29.584  1.00 29.88           O  
ANISOU 1355  O   HOH A 255     1571   5725   4055  -1031    -24   1372       O  
HETATM 1356  O   HOH A 256      -4.797  12.348  13.226  1.00 27.93           O  
ANISOU 1356  O   HOH A 256      892   5766   3952   -150   -440    335       O  
HETATM 1357  O   HOH A 257      -7.187  10.378  19.775  1.00 28.61           O  
ANISOU 1357  O   HOH A 257     1664   5306   3899    543   1023    -81       O  
HETATM 1358  O   HOH A 258       6.288   9.266  -1.839  1.00 22.37           O  
ANISOU 1358  O   HOH A 258     1323   2989   4187   -387    106   -273       O  
HETATM 1359  O   HOH A 259      17.643  13.171  27.843  1.00 23.93           O  
ANISOU 1359  O   HOH A 259     1709   3634   3747    750   -268    645       O  
HETATM 1360  O   HOH A 260       6.784  -3.016  30.425  1.00 26.81           O  
ANISOU 1360  O   HOH A 260     3749   2648   3787     19    898     41       O  
HETATM 1361  O   HOH A 261      15.658  19.687  27.384  1.00 26.99           O  
ANISOU 1361  O   HOH A 261     3384   3268   3602   -176   -926   -178       O  
HETATM 1362  O   HOH A 262       2.170  -3.523  24.710  1.00 21.25           O  
ANISOU 1362  O   HOH A 262      698   3555   3820    486   -230   -116       O  
HETATM 1363  O   HOH A 263       5.296  17.239  29.998  1.00 29.54           O  
ANISOU 1363  O   HOH A 263     3894   4535   2792   -153    247     70       O  
HETATM 1364  O   HOH A 264      21.784   3.318  18.684  1.00 23.77           O  
ANISOU 1364  O   HOH A 264     1375   3576   4079   -248      1    338       O  
HETATM 1365  O   HOH A 265       4.902  -1.610  25.469  1.00 27.37           O  
ANISOU 1365  O   HOH A 265     1215   4496   4688    579    -79   -597       O  
HETATM 1366  O   HOH A 266       4.957  14.847  31.064  1.00 39.17           O  
ANISOU 1366  O   HOH A 266     7275   4018   3589    819   1365    -40       O  
HETATM 1367  O   HOH A 267      -3.675   3.273  28.888  1.00 24.65           O  
ANISOU 1367  O   HOH A 267      837   3817   4709    437   -512   -757       O  
HETATM 1368  O   HOH A 268       7.612  12.275  15.176  1.00 28.28           O  
ANISOU 1368  O   HOH A 268     2336   3904   4503  -1118    553  -1476       O  
HETATM 1369  O   HOH A 269       5.144  29.196   4.284  1.00 26.82           O  
ANISOU 1369  O   HOH A 269     2426   3610   4152   -241    276   -656       O  
HETATM 1370  O   HOH A 270       3.151   8.490  30.958  1.00 27.94           O  
ANISOU 1370  O   HOH A 270     2833   3167   4614    816   1072   -247       O  
HETATM 1371  O   HOH A 271       2.424  14.296  18.320  1.00 27.80           O  
ANISOU 1371  O   HOH A 271     1643   4125   4793  -1006   -707   1208       O  
HETATM 1372  O   HOH A 272       7.197  -6.314  15.520  1.00 35.44           O  
ANISOU 1372  O   HOH A 272     5721   3057   4685  -1691  -1013   1437       O  
HETATM 1373  O   HOH A 273       3.403   3.839  35.730  1.00 29.24           O  
ANISOU 1373  O   HOH A 273     5033   3157   2917  -1323    -87    109       O  
HETATM 1374  O   HOH A 274       5.997  -2.090  22.833  1.00 29.55           O  
ANISOU 1374  O   HOH A 274     1251   5164   4812    529   -248    640       O  
HETATM 1375  O   HOH A 275      18.496   4.438   2.438  1.00 25.93           O  
ANISOU 1375  O   HOH A 275     1792   4689   3370    194    235   -354       O  
HETATM 1376  O   HOH A 276       4.851  10.248  29.392  1.00 24.24           O  
ANISOU 1376  O   HOH A 276     3006   2977   3225   -176    245    616       O  
HETATM 1377  O   HOH A 277      17.119   8.909  16.324  1.00 25.81           O  
ANISOU 1377  O   HOH A 277     2667   3135   4002    821     61    205       O  
HETATM 1378  O   HOH A 278      18.672  17.049   2.671  1.00 31.16           O  
ANISOU 1378  O   HOH A 278     3051   4650   4136    500    -95   -594       O  
HETATM 1379  O   HOH A 279       0.215   3.595  -0.367  1.00 27.18           O  
ANISOU 1379  O   HOH A 279     2332   3172   4821   -527  -1405    -38       O  
HETATM 1380  O  AHOH A 280      16.699  -0.450  17.235  0.50 23.05           O  
ANISOU 1380  O  AHOH A 280      307   5260   3191    256   -365   -380       O  
HETATM 1381  O  BHOH A 280      15.415  -1.449  17.861  0.50 23.39           O  
ANISOU 1381  O  BHOH A 280     2744   3076   3066   1975   -151   -159       O  
HETATM 1382  O   HOH A 281       1.841  -6.276  25.759  1.00 32.27           O  
ANISOU 1382  O   HOH A 281     2157   3139   6963    994   3237    600       O  
HETATM 1383  O   HOH A 282      10.436  -3.927  28.154  1.00 37.08           O  
ANISOU 1383  O   HOH A 282     2040   5272   6774    923   1147   1898       O  
HETATM 1384  O   HOH A 283      16.113  23.243   8.686  1.00 27.05           O  
ANISOU 1384  O   HOH A 283     1486   4119   4671    259    528   -650       O  
HETATM 1385  O   HOH A 284       5.285  -1.623  19.908  1.00 33.20           O  
ANISOU 1385  O   HOH A 284     1028   3792   7792   -333   2410   -651       O  
HETATM 1386  O   HOH A 285       8.806   4.950  32.704  1.00 26.52           O  
ANISOU 1386  O   HOH A 285     2487   3804   3784   -112  -1303    438       O  
HETATM 1387  O   HOH A 286      -6.742   5.166  23.921  1.00 31.89           O  
ANISOU 1387  O   HOH A 286     5096   3039   3980  -1109   1368   -219       O  
HETATM 1388  O   HOH A 287       7.691   3.187  -0.730  1.00 27.85           O  
ANISOU 1388  O   HOH A 287     1812   4535   4232    801    667    656       O  
HETATM 1389  O   HOH A 288       9.199  12.024  30.765  1.00 26.78           O  
ANISOU 1389  O   HOH A 288     3192   3027   3955     -7   1097    124       O  
HETATM 1390  O   HOH A 289      17.124   7.035   2.183  1.00 32.66           O  
ANISOU 1390  O   HOH A 289     4040   3479   4890   -703   1937   -800       O  
HETATM 1391  O   HOH A 290      -1.074  18.468   0.830  1.00 27.44           O  
ANISOU 1391  O   HOH A 290     2189   3602   4635    487   -942     28       O  
HETATM 1392  O   HOH A 291       0.769  15.957  18.481  1.00 33.06           O  
ANISOU 1392  O   HOH A 291     5160   3611   3788  -1268   1098   -175       O  
HETATM 1393  O   HOH A 292      13.539  21.351  28.354  1.00 33.01           O  
ANISOU 1393  O   HOH A 292     4835   3978   3726  -1072   -191   -662       O  
HETATM 1394  O   HOH A 293      10.145  -5.318   9.553  1.00 33.62           O  
ANISOU 1394  O   HOH A 293     5381   2960   4430    390   1484   -576       O  
HETATM 1395  O   HOH A 294       9.645  21.378  29.781  1.00 28.68           O  
ANISOU 1395  O   HOH A 294     3783   3044   4068    865    325   -786       O  
HETATM 1396  O  AHOH A 295      12.633  25.446   6.089  0.50 20.98           O  
ANISOU 1396  O  AHOH A 295     2486   2536   2947     64    983    615       O  
HETATM 1397  O  BHOH A 295      11.347  24.931   4.382  0.50 25.97           O  
ANISOU 1397  O  BHOH A 295     1161   4794   3909   -715    143   1512       O  
HETATM 1398  O   HOH A 296      -5.931   3.262  27.163  1.00 25.32           O  
ANISOU 1398  O   HOH A 296     1642   3789   4187     71    152   -207       O  
HETATM 1399  O   HOH A 297      15.788  26.196   8.692  1.00 24.71           O  
ANISOU 1399  O   HOH A 297     1803   3686   3899   -758    -21      0       O  
HETATM 1400  O   HOH A 298       8.029  30.774   8.353  1.00 26.41           O  
ANISOU 1400  O   HOH A 298      939   2987   6109   -334   -485   1021       O  
HETATM 1401  O   HOH A 299       5.945  12.054  19.412  1.00 73.35           O  
ANISOU 1401  O   HOH A 299     5698  11764  10405  -2486    288  -6124       O  
HETATM 1402  O   HOH A 300      -8.117   6.104  14.742  1.00 31.12           O  
ANISOU 1402  O   HOH A 300     1681   4289   5851   -197  -1265    304       O  
HETATM 1403  O   HOH A 301      -2.382  19.851   6.841  1.00 29.91           O  
ANISOU 1403  O   HOH A 301      715   5126   5523    258   -295   1140       O  
HETATM 1404  O   HOH A 302       2.837  -2.152   0.834  1.00 35.11           O  
ANISOU 1404  O   HOH A 302     3156   4537   5646      1    446  -2085       O  
HETATM 1405  O   HOH A 303       8.138  -4.369  32.431  1.00 35.54           O  
ANISOU 1405  O   HOH A 303     4653   4230   4618   -414    256    705       O  
HETATM 1406  O   HOH A 304       3.014  12.294  30.173  1.00 32.42           O  
ANISOU 1406  O   HOH A 304     4412   3951   3955    354    723    958       O  
HETATM 1407  O   HOH A 305       2.258  -2.831  18.077  1.00 35.42           O  
ANISOU 1407  O   HOH A 305     3557   4569   5329   1786  -1924  -1506       O  
HETATM 1408  O   HOH A 306      17.650   0.970  13.305  1.00 31.21           O  
ANISOU 1408  O   HOH A 306     1839   4982   5035   -418   1310   -375       O  
HETATM 1409  O   HOH A 307       4.105  -3.995  16.722  1.00 55.54           O  
ANISOU 1409  O   HOH A 307      755  10875   9469    854  -2108  -1741       O  
HETATM 1410  O   HOH A 308       3.677  21.605  24.243  1.00 29.03           O  
ANISOU 1410  O   HOH A 308     3766   3433   3829    826    365   -116       O  
HETATM 1411  O   HOH A 309       6.562  10.874  17.231  1.00 32.35           O  
ANISOU 1411  O   HOH A 309     1976   4992   5323   -491    350   -158       O  
HETATM 1412  O   HOH A 310      -7.471   6.906  18.709  1.00 41.43           O  
ANISOU 1412  O   HOH A 310     2592   5983   7166    422   -287  -1348       O  
HETATM 1413  O   HOH A 311       9.650  32.910   8.165  1.00 33.84           O  
ANISOU 1413  O   HOH A 311     1987   5242   5627    367  -1425   -144       O  
HETATM 1414  O   HOH A 312       5.936  22.989  24.646  1.00 32.62           O  
ANISOU 1414  O   HOH A 312     3425   3741   5228    381   1515   -272       O  
HETATM 1415  O   HOH A 313      -0.195  -2.388   9.798  1.00 33.02           O  
ANISOU 1415  O   HOH A 313     1134   5477   5933  -1903  -1190    444       O  
HETATM 1416  O   HOH A 314      19.541  14.592  18.096  1.00 29.28           O  
ANISOU 1416  O   HOH A 314      824   4709   5591   -366    251   1336       O  
HETATM 1417  O   HOH A 315       3.877  10.866  15.345  1.00 33.57           O  
ANISOU 1417  O   HOH A 315     3036   5300   4416  -1192   1391  -1592       O  
HETATM 1418  O   HOH A 316       1.466  -4.627  12.009  1.00 27.62           O  
ANISOU 1418  O   HOH A 316     2678   3435   4380   -470    248    623       O  
HETATM 1419  O   HOH A 317      21.545   9.219  22.545  1.00 31.86           O  
ANISOU 1419  O   HOH A 317     2371   4712   5021   -653   -979    111       O  
HETATM 1420  O   HOH A 318      12.814  -5.429  27.942  1.00 37.08           O  
ANISOU 1420  O   HOH A 318     3853   3535   6700    367   1555   1301       O  
HETATM 1421  O   HOH A 319       2.812  -4.756  22.184  1.00 31.30           O  
ANISOU 1421  O   HOH A 319     1815   4317   5759    556   -240   1034       O  
HETATM 1422  O   HOH A 320      21.211  17.971   4.553  1.00 34.21           O  
ANISOU 1422  O   HOH A 320     2450   4019   6529    553   1889    703       O  
HETATM 1423  O   HOH A 321       5.278  19.002  -8.024  1.00 32.11           O  
ANISOU 1423  O   HOH A 321     2283   4833   5083  -1022    453   -981       O  
HETATM 1424  O   HOH A 322      -1.545   9.364  26.666  1.00 34.47           O  
ANISOU 1424  O   HOH A 322     4119   5077   3901   -786    296   -649       O  
HETATM 1425  O   HOH A 323      -2.857   5.833  28.956  1.00 29.64           O  
ANISOU 1425  O   HOH A 323     1060   4122   6081    564   -772   -540       O  
HETATM 1426  O   HOH A 324      20.778  11.391  10.937  1.00 53.58           O  
ANISOU 1426  O   HOH A 324     3469   8768   8119    677   -600   3277       O  
HETATM 1427  O   HOH A 325       3.626   5.746  18.928  1.00 31.08           O  
ANISOU 1427  O   HOH A 325     2595   4907   4305   -506    118    555       O  
HETATM 1428  O   HOH A 326      13.202  10.023  31.422  1.00 39.08           O  
ANISOU 1428  O   HOH A 326     5353   5116   4377  -1280  -1431   -609       O  
HETATM 1429  O   HOH A 327      -1.246   7.004  16.393  1.00 35.39           O  
ANISOU 1429  O   HOH A 327     2224   6045   5174   1639   1138    353       O  
HETATM 1430  O   HOH A 328      11.112  22.301  26.637  1.00 42.08           O  
ANISOU 1430  O   HOH A 328     8088   4115   3785    -11   -636    339       O  
HETATM 1431  O   HOH A 329       6.247  23.513  -4.293  1.00 38.51           O  
ANISOU 1431  O   HOH A 329     3439   6215   4975    506   1058    182       O  
HETATM 1432  O   HOH A 330      21.622  11.948   8.018  1.00 81.30           O  
ANISOU 1432  O   HOH A 330     5810  12737  12341  -8146  -5180   8799       O  
HETATM 1433  O   HOH A 331      20.176  10.196   2.121  1.00 43.57           O  
ANISOU 1433  O   HOH A 331     1797   6151   8605    380    294  -1072       O  
HETATM 1434  O   HOH A 332      10.893  29.461   6.142  1.00 35.35           O  
ANISOU 1434  O   HOH A 332     4000   5219   4210  -1917  -1627    916       O  
HETATM 1435  O   HOH A 333       0.350   9.076  29.554  1.00 39.92           O  
ANISOU 1435  O   HOH A 333     7233   3331   4603   -763   1618   -497       O  
CONECT 1219 1220 1222 1226                                                      
CONECT 1220 1219                                                                
CONECT 1221 1223 1231                                                           
CONECT 1222 1219                                                                
CONECT 1223 1221 1224 1225                                                      
CONECT 1224 1223                                                                
CONECT 1225 1223                                                                
CONECT 1226 1219 1227 1228                                                      
CONECT 1227 1226                                                                
CONECT 1228 1226 1229 1233                                                      
CONECT 1229 1228 1230                                                           
CONECT 1230 1229 1231                                                           
CONECT 1231 1221 1230 1232                                                      
CONECT 1232 1231 1233                                                           
CONECT 1233 1228 1232                                                           
MASTER      339    0    1    3   10    0    2    6 1287    1   15   11          
END                                                                             



If you find results from this site helpful for your research, please cite one of our papers:

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.