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***  HYDROLASE/HYDROLASE INHIBITOR 29-OCT-17 5YOK  ***

elNémo ID: 210618153738117753

Job options:

ID        	=	 210618153738117753
JOBID     	=	 HYDROLASE/HYDROLASE INHIBITOR 29-OCT-17 5YOK
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    HYDROLASE/HYDROLASE INHIBITOR           29-OCT-17   5YOK              
TITLE     STRUCTURE OF HIV-1 PROTEASE IN COMPLEX WITH INHIBITOR KNI-1657        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HIV-1 PROTEASE;                                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE   3 ORGANISM_TAXID: 11676;                                               
SOURCE   4 GENE: POL;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    INHIBITOR, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.ADACHI,K.HIDAKA,R.KUROKI,Y.KISO                                     
REVDAT   1   18-JUL-18 5YOK    0                                                
JRNL        AUTH   K.HIDAKA,T.KIMURA,R.SANKARANARAYANAN,J.WANG,K.F.MCDANIEL,    
JRNL        AUTH 2 D.J.KEMPF,M.KAMEOKA,M.ADACHI,R.KUROKI,J.T.NGUYEN,Y.HAYASHI,  
JRNL        AUTH 3 Y.KISO                                                       
JRNL        TITL   IDENTIFICATION OF HIGHLY POTENT HUMAN IMMUNODEFICIENCY VIRUS 
JRNL        TITL 2 TYPE-1 PROTEASE INHIBITORS AGAINST LOPINAVIR AND DARUNAVIR   
JRNL        TITL 3 RESISTANT VIRUSES FROM ALLOPHENYLNORSTATINE-BASED            
JRNL        TITL 4 PEPTIDOMIMETICS WITH P2 TETRAHYDROFURANYLGLYCINE.            
JRNL        REF    J. MED. CHEM.                 V.  61  5138 2018              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   29852069                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.7B01709                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    0.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL                                               
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 0.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.60                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R-VALUE                   
REMARK   3   FREE R VALUE TEST SET SELECTION   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.103                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.103                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.125                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 10024                  
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 200529                 
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.097                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.118                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 9062                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 181768                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1512                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 66                                            
REMARK   3   SOLVENT ATOMS      : 537                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL                    
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL                    
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL                    
REMARK   3   NUMBER OF RESTRAINTS                     : NULL                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.016                   
REMARK   3   ANGLE DISTANCES                      (A) : 2.130                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : NULL                    
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : NULL                    
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : NULL                    
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL                    
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL                    
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL                    
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL                    
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : NULL                                
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5YOK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-NOV-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300005635.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUL-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.800                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 200529                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 11.10                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 50.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 0.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 126MM PHOSPHATE BUFFER AT PH 5.0, 63MM   
REMARK 280  SODIUM CITRATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       29.12500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.97400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.12500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.97400            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9550 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 393  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 413  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     MET B     0                                                      
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   OD1  ASP B    30     O    HOH B   201              1.37            
REMARK 500   HE3  LYS B    43     O    HOH B   247              1.54            
REMARK 500   O    HOH A   290     O    HOH A   428              1.58            
REMARK 500   O    HOH B   266     O    HOH B   340              1.59            
REMARK 500   O    HOH B   416     O    HOH B   418              1.74            
REMARK 500   O    ILE A    50     O    HOH A   203              1.80            
REMARK 500   O    HOH B   208     O    HOH B   349              1.84            
REMARK 500   CG   ASP B    30     O    HOH B   201              2.03            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   237     O    HOH B   416     3556     1.58            
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    ARG A  57   CZ    ARG A  57   NH1     0.115                       
REMARK 500    GLU A  65   CD    GLU A  65   OE2    -0.067                       
REMARK 500    ILE B  33   CB    ILE B  33   CG1    -0.196                       
REMARK 500    GLU B  65   CB    GLU B  65   CG     -0.164                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  41   NE  -  CZ  -  NH2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    LYS A  45   CD  -  CE  -  NZ  ANGL. DEV. =  17.2 DEGREES          
REMARK 500    ARG A  57   CD  -  NE  -  CZ  ANGL. DEV. =  13.5 DEGREES          
REMARK 500    ILE A  62   O   -  C   -  N   ANGL. DEV. = -13.5 DEGREES          
REMARK 500    LEU A  97   CB  -  CA  -  C   ANGL. DEV. = -13.7 DEGREES          
REMARK 500    LEU A  97   CB  -  CA  -  C   ANGL. DEV. =  12.8 DEGREES          
REMARK 500    GLN B   2   CG  -  CD  -  NE2 ANGL. DEV. =  17.2 DEGREES          
REMARK 500    ASP B  25   CB  -  CG  -  OD1 ANGL. DEV. =  -8.4 DEGREES          
REMARK 500    LYS B  43   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES          
REMARK 500    LYS B  45   CB  -  CG  -  CD  ANGL. DEV. =  17.8 DEGREES          
REMARK 500    LYS B  45   CG  -  CD  -  CE  ANGL. DEV. =  23.8 DEGREES          
REMARK 500    MET B  46   CG  -  SD  -  CE  ANGL. DEV. = -10.4 DEGREES          
REMARK 500    GLY B  49   C   -  N   -  CA  ANGL. DEV. =  17.4 DEGREES          
REMARK 500    GLU B  65   OE1 -  CD  -  OE2 ANGL. DEV. =   7.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU B  35      125.98    -38.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ILE A  62        -15.20                                           
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 491        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH A 492        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH A 493        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH A 494        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH A 495        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH A 496        DISTANCE =  6.64 ANGSTROMS                       
REMARK 525    HOH A 497        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH A 498        DISTANCE =  6.85 ANGSTROMS                       
REMARK 525    HOH A 499        DISTANCE =  7.00 ANGSTROMS                       
REMARK 525    HOH A 500        DISTANCE =  7.16 ANGSTROMS                       
REMARK 525    HOH A 501        DISTANCE =  7.42 ANGSTROMS                       
REMARK 525    HOH A 502        DISTANCE =  7.48 ANGSTROMS                       
REMARK 525    HOH A 503        DISTANCE =  7.66 ANGSTROMS                       
REMARK 525    HOH A 504        DISTANCE =  7.80 ANGSTROMS                       
REMARK 525    HOH A 505        DISTANCE =  8.43 ANGSTROMS                       
REMARK 525    HOH B 425        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH B 426        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH B 427        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH B 428        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH B 429        DISTANCE =  6.52 ANGSTROMS                       
REMARK 525    HOH B 430        DISTANCE =  7.30 ANGSTROMS                       
REMARK 525    HOH B 431        DISTANCE =  7.48 ANGSTROMS                       
REMARK 525    HOH B 432        DISTANCE =  9.61 ANGSTROMS                       
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: (4R)-N-[(2,6-DIMETHYLPHENYL)METHYL]-3-[(2S,3S)-3-     
REMARK 630 [[(2S)-2-[(7-METHOXY-1-BENZOFURAN-2-YL)CARBONYLAMINO]-2-[(3R)-       
REMARK 630 OXOLAN-3-YL]ETHANOYL]AMINO]-2-OXIDANYL-4-PHENYL-BUTANOYL]-5,5-       
REMARK 630 DIMETHYL-1,3-THIAZOLIDINE-4-CARBOXAMIDE                              
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     8Z0 A   101                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    8YO 8YR 005 00B 8YU                                      
REMARK 630 DETAILS: NULL                                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8Z0 A 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 102                 
DBREF  5YOK A    0    99  PDB    5YOK     5YOK             0     99             
DBREF  5YOK B    0    99  PDB    5YOK     5YOK             0     99             
SEQRES   1 A  100  MET PRO GLN ILE THR LEU TRP LYS ARG PRO LEU VAL THR          
SEQRES   2 A  100  ILE LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP          
SEQRES   3 A  100  THR GLY ALA ASP ASP THR VAL ILE GLU GLU MET SER LEU          
SEQRES   4 A  100  PRO GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY          
SEQRES   5 A  100  GLY PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE ILE ILE          
SEQRES   6 A  100  GLU ILE ALA GLY HIS LYS ALA ILE GLY THR VAL LEU VAL          
SEQRES   7 A  100  GLY PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU          
SEQRES   8 A  100  THR GLN ILE GLY ALA THR LEU ASN PHE                          
SEQRES   1 B  100  MET PRO GLN ILE THR LEU TRP LYS ARG PRO LEU VAL THR          
SEQRES   2 B  100  ILE LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP          
SEQRES   3 B  100  THR GLY ALA ASP ASP THR VAL ILE GLU GLU MET SER LEU          
SEQRES   4 B  100  PRO GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY          
SEQRES   5 B  100  GLY PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE ILE ILE          
SEQRES   6 B  100  GLU ILE ALA GLY HIS LYS ALA ILE GLY THR VAL LEU VAL          
SEQRES   7 B  100  GLY PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU          
SEQRES   8 B  100  THR GLN ILE GLY ALA THR LEU ASN PHE                          
HET    8Z0  A 101     204                                                       
HET    GOL  B 101      12                                                       
HET    GOL  B 102       6                                                       
HETNAM     8Z0 (4R)-N-[(2,6-DIMETHYLPHENYL)METHYL]-3-[(2S,3S)-3-                
HETNAM   2 8Z0  [[(2S)-2-[(7-METHOXY-1-BENZOFURAN-2-YL)CARBONYLAMINO]-          
HETNAM   3 8Z0  2-[(3R)-OXOLAN-3-YL]ETHANOYL]AMINO]-2-OXIDANYL-4-               
HETNAM   4 8Z0  PHENYL-BUTANOYL]-5,5-DIMETHYL-1,3-THIAZOLIDINE-4-               
HETNAM   5 8Z0  CARBOXAMIDE                                                     
HETNAM     GOL GLYCEROL                                                         
HETSYN     8Z0 KNI-1657                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  8Z0    C41 H48 N4 O8 S                                              
FORMUL   4  GOL    2(C3 H8 O3)                                                  
FORMUL   6  HOH   *537(H2 O)                                                    
HELIX    1 AA1 GLY A   86  THR A   91  1                                   6    
HELIX    2 AA2 GLY B   86  THR B   91  1                                   6    
SHEET    1 AA1 4 GLN A   2  ILE A   3  0                                        
SHEET    2 AA1 4 THR B  96  ASN B  98 -1  O  LEU B  97   N  ILE A   3           
SHEET    3 AA1 4 THR A  96  ASN A  98 -1  N  ASN A  98   O  THR B  96           
SHEET    4 AA1 4 GLN B   2  ILE B   3 -1  O  ILE B   3   N  LEU A  97           
SHEET    1 AA2 8 TRP A  42  GLY A  49  0                                        
SHEET    2 AA2 8 GLY A  52  ILE A  66 -1  O  GLN A  58   N  LYS A  43           
SHEET    3 AA2 8 HIS A  69  VAL A  77 -1  O  HIS A  69   N  ILE A  66           
SHEET    4 AA2 8 VAL A  32  ILE A  33  1  N  ILE A  33   O  LEU A  76           
SHEET    5 AA2 8 ILE A  84  ILE A  85 -1  O  ILE A  84   N  VAL A  32           
SHEET    6 AA2 8 GLN A  18  LEU A  24  1  N  LEU A  23   O  ILE A  85           
SHEET    7 AA2 8 LEU A  10  ILE A  15 -1  N  ILE A  13   O  LYS A  20           
SHEET    8 AA2 8 GLY A  52  ILE A  66 -1  O  GLU A  65   N  LYS A  14           
SHEET    1 AA3 8 LYS B  43  GLY B  49  0                                        
SHEET    2 AA3 8 GLY B  52  ILE B  66 -1  O  GLY B  52   N  GLY B  49           
SHEET    3 AA3 8 HIS B  69  VAL B  77 -1  O  HIS B  69   N  ILE B  66           
SHEET    4 AA3 8 VAL B  32  ILE B  33  1  N  ILE B  33   O  LEU B  76           
SHEET    5 AA3 8 ILE B  84  ILE B  85 -1  O  ILE B  84   N  VAL B  32           
SHEET    6 AA3 8 GLN B  18  LEU B  24  1  N  LEU B  23   O  ILE B  85           
SHEET    7 AA3 8 LEU B  10  ILE B  15 -1  N  ILE B  13   O  LYS B  20           
SHEET    8 AA3 8 GLY B  52  ILE B  66 -1  O  GLU B  65   N  LYS B  14           
SITE     1 AC1 44 TRP A   6  ARG A   8  LEU A  23  ASP A  25                    
SITE     2 AC1 44 GLY A  27  ALA A  28  ASP A  29  ASP A  30                    
SITE     3 AC1 44 GLY A  48  GLY A  49  ILE A  50  PRO A  81                    
SITE     4 AC1 44 VAL A  82  ILE A  84  HOH A 202  HOH A 207                    
SITE     5 AC1 44 HOH A 212  HOH A 220  HOH A 247  HOH A 248                    
SITE     6 AC1 44 HOH A 282  HOH A 288  HOH A 308  HOH A 367                    
SITE     7 AC1 44 HOH A 442  HOH A 499  ARG B   8  LEU B  23                    
SITE     8 AC1 44 ASP B  25  GLY B  27  ALA B  28  ASP B  29                    
SITE     9 AC1 44 ASP B  30  VAL B  32  GLY B  48  GLY B  49                    
SITE    10 AC1 44 ILE B  50  PRO B  81  VAL B  82  ILE B  84                    
SITE    11 AC1 44 HOH B 210  HOH B 354  HOH B 399  HOH B 429                    
SITE     1 AC2 12 GLN A  18  MET A  36  SER A  37  THR B  12                    
SITE     2 AC2 12 ILE B  13  LYS B  14  LEU B  19  GLU B  65                    
SITE     3 AC2 12 ALA B  67  GLY B  68  HOH B 232  HOH B 260                    
SITE     1 AC3  8 HOH A 407  GLU B  35  LYS B  55  ARG B  57                    
SITE     2 AC3  8 VAL B  77  GLY B  78  HOH B 206  HOH B 278                    
CRYST1   58.250   85.948   46.529  90.00  90.00  90.00 P 21 21 2     8          
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      0.017167  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011635  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021492        0.00000                         
ATOM      1  N   PRO A   1       0.866  39.939  17.570  1.00 18.58           N  
ANISOU    1  N   PRO A   1     1535   2595   2509   -520   -586   1615       N  
ATOM      2  CA  PRO A   1      -0.106  39.029  18.151  1.00 14.12           C  
ANISOU    2  CA  PRO A   1     1139   1837   2070    -96   -385    852       C  
ATOM      3  C   PRO A   1       0.457  38.346  19.413  1.00 11.74           C  
ANISOU    3  C   PRO A   1      986   1372   1837     82    -66    679       C  
ATOM      4  O   PRO A   1       1.636  38.495  19.706  1.00 14.15           O  
ANISOU    4  O   PRO A   1      982   1933   2143   -139   -249   1138       O  
ATOM      5  CB  PRO A   1      -0.242  37.954  17.022  1.00 17.36           C  
ANISOU    5  CB  PRO A   1     1887   2349   1967    -52   -432    694       C  
ATOM      6  CG  PRO A   1       1.142  37.868  16.397  1.00 26.45           C  
ANISOU    6  CG  PRO A   1     2491   3828   3132   1021    548    736       C  
ATOM      7  CD  PRO A   1       1.602  39.337  16.380  1.00 27.14           C  
ANISOU    7  CD  PRO A   1     2640   5065   1993  -1069    -38   1562       C  
ATOM      8  HA  PRO A   1      -0.959  39.476  18.331  1.00 16.94           H  
ATOM      9  HB2 PRO A   1      -0.507  37.098  17.392  1.00 20.83           H  
ATOM     10  HB3 PRO A   1      -0.900  38.228  16.364  1.00 20.83           H  
ATOM     11  HG2 PRO A   1       1.736  37.321  16.935  1.00 31.74           H  
ATOM     12  HG3 PRO A   1       1.100  37.503  15.499  1.00 31.74           H  
ATOM     13  HD2 PRO A   1       2.563  39.405  16.492  1.00 32.57           H  
ATOM     14  HD3 PRO A   1       1.347  39.774  15.552  1.00 32.57           H  
ATOM     15  N   GLN A   2      -0.405  37.606  20.077  1.00 10.08           N  
ANISOU   15  N   GLN A   2      884   1047   1672    115    -96    392       N  
ATOM     16  CA  GLN A   2      -0.023  36.678  21.151  1.00  9.15           C  
ANISOU   16  CA  GLN A   2      839    951   1480     89     16    232       C  
ATOM     17  C   GLN A   2      -0.187  35.271  20.581  1.00  9.20           C  
ANISOU   17  C   GLN A   2      883   1053   1351     79   -114    167       C  
ATOM     18  O   GLN A   2      -1.286  34.918  20.149  1.00 11.95           O  
ANISOU   18  O   GLN A   2      925   1336   2010    -55   -255      9       O  
ATOM     19  CB  GLN A   2      -0.877  36.836  22.372  1.00 10.20           C  
ANISOU   19  CB  GLN A   2      857   1154   1632    140    126    159       C  
ATOM     20  CG  GLN A   2      -0.528  35.819  23.456  1.00 10.99           C  
ANISOU   20  CG  GLN A   2     1172   1176   1578     -2    182    183       C  
ATOM     21  CD  GLN A   2      -1.066  36.179  24.793  1.00 12.20           C  
ANISOU   21  CD  GLN A   2     1113   1569   1678    -29    279    128       C  
ATOM     22  OE1 GLN A   2      -2.116  35.635  25.246  1.00 18.15           O  
ANISOU   22  OE1 GLN A   2     1530   2355   2599   -348    779    225       O  
ATOM     23  NE2 GLN A   2      -0.431  37.103  25.459  1.00 12.54           N  
ANISOU   23  NE2 GLN A   2     1188   1668   1624    -51    603   -104       N  
ATOM     24  H   GLN A   2      -1.238  37.669  19.871  1.00 12.10           H  
ATOM     25  HA  GLN A   2       0.916  36.825  21.389  1.00 10.98           H  
ATOM     26  HB2 GLN A   2      -0.763  37.732  22.727  1.00 12.23           H  
ATOM     27  HB3 GLN A   2      -1.809  36.731  22.125  1.00 12.23           H  
ATOM     28  HG2 GLN A   2      -0.878  34.952  23.199  1.00 13.18           H  
ATOM     29  HG3 GLN A   2       0.438  35.742  23.516  1.00 13.18           H  
ATOM     30 HE21 GLN A   2      -0.723  37.358  26.226  1.00 15.05           H  
ATOM     31 HE22 GLN A   2       0.280  37.458  25.130  1.00 15.05           H  
ATOM     32  N   ILE A   3       0.903  34.517  20.577  1.00  8.81           N  
ANISOU   32  N   ILE A   3      918    882   1347     71    -75    191       N  
ATOM     33  CA  ILE A   3       0.910  33.153  20.006  1.00  9.58           C  
ANISOU   33  CA  ILE A   3     1135    940   1349     31   -120    179       C  
ATOM     34  C   ILE A   3       1.127  32.187  21.185  1.00  8.26           C  
ANISOU   34  C   ILE A   3      859    855   1236     22    -63     66       C  
ATOM     35  O   ILE A   3       2.122  32.233  21.895  1.00  8.32           O  
ANISOU   35  O   ILE A   3      831    949   1193    -48    -16    124       O  
ATOM     36  CB  ILE A   3       1.955  33.014  18.928  1.00 11.08           C  
ANISOU   36  CB  ILE A   3     1650   1012   1297    214    134    148       C  
ATOM     37  CG1 ILE A   3       1.619  34.018  17.790  1.00 13.05           C  
ANISOU   37  CG1 ILE A   3     1839   1234   1591    196    283    281       C  
ATOM     38  CG2 ILE A   3       2.104  31.592  18.441  1.00 13.27           C  
ANISOU   38  CG2 ILE A   3     2207   1147   1388    185    124     72       C  
ATOM     39  CD1 ILE A   3       2.642  33.992  16.684  1.00 17.04           C  
ANISOU   39  CD1 ILE A   3     2399   1645   2043    297    783    653       C  
ATOM     40  H   ILE A   3       1.628  34.830  20.916  1.00 10.57           H  
ATOM     41  HA  ILE A   3       0.030  32.974  19.614  1.00 11.50           H  
ATOM     42  HB  ILE A   3       2.814  33.284  19.315  1.00 13.30           H  
ATOM     43 HG12 ILE A   3       0.748  33.801  17.422  1.00 15.66           H  
ATOM     44 HG13 ILE A   3       1.572  34.913  18.159  1.00 15.66           H  
ATOM     45 HG21 ILE A   3       2.778  31.556  17.759  1.00 19.91           H  
ATOM     46 HG22 ILE A   3       2.361  31.027  19.174  1.00 19.91           H  
ATOM     47 HG23 ILE A   3       1.268  31.288  18.081  1.00 19.91           H  
ATOM     48 HD11 ILE A   3       2.395  34.624  16.005  1.00 25.55           H  
ATOM     49 HD12 ILE A   3       3.503  34.223  17.040  1.00 25.55           H  
ATOM     50 HD13 ILE A   3       2.679  33.111  16.303  1.00 25.55           H  
ATOM     51  N   THR A   4       0.132  31.294  21.348  1.00  9.56           N  
ANISOU   51  N   THR A   4      860   1039   1517    -31   -213    288       N  
ATOM     52  CA  THR A   4       0.232  30.247  22.324  1.00  9.19           C  
ANISOU   52  CA  THR A   4      830    996   1459   -109   -122    127       C  
ATOM     53  C   THR A   4       1.106  29.107  21.761  1.00  8.13           C  
ANISOU   53  C   THR A   4      731    952   1221    -99   -163    122       C  
ATOM     54  O   THR A   4       1.517  29.092  20.604  1.00  9.37           O  
ANISOU   54  O   THR A   4     1396    996    956    -41   -221    148       O  
ATOM     55  CB  THR A   4      -1.162  29.739  22.721  1.00 10.77           C  
ANISOU   55  CB  THR A   4      755   1235   1857    -63    -30    183       C  
ATOM     56  OG1 THR A   4      -1.874  29.301  21.582  1.00 13.77           O  
ANISOU   56  OG1 THR A   4     1012   1728   2178   -422   -211   -158       O  
ATOM     57  CG2 THR A   4      -1.933  30.841  23.456  1.00 12.58           C  
ANISOU   57  CG2 THR A   4      865   1635   1997     14     66    102       C  
ATOM     58  H   THR A   4      -0.574  31.352  20.861  1.00 11.47           H  
ATOM     59  HA  THR A   4       0.670  30.608  23.123  1.00 11.03           H  
ATOM     60  HB  THR A   4      -1.052  28.979  23.329  1.00 12.92           H  
ATOM     61  HG1 THR A   4      -1.421  29.427  20.911  1.00 20.65           H  
ATOM     62 HG21 THR A   4      -1.432  31.124  24.224  1.00 18.88           H  
ATOM     63 HG22 THR A   4      -2.064  31.587  22.866  1.00 18.88           H  
ATOM     64 HG23 THR A   4      -2.786  30.501  23.736  1.00 18.88           H  
ATOM     65  N   LEU A   5       1.381  28.143  22.653  1.00  7.53           N  
ANISOU   65  N   LEU A   5      652    989   1048    -69    -17    175       N  
ATOM     66  CA  LEU A   5       2.356  27.103  22.378  1.00  6.47           C  
ANISOU   66  CA  LEU A   5      629    874    810    -87      7     93       C  
ATOM     67  C   LEU A   5       1.763  25.709  22.447  1.00  6.37           C  
ANISOU   67  C   LEU A   5      619    989    668   -106     -7    101       C  
ATOM     68  O   LEU A   5       2.475  24.715  22.538  1.00  6.37           O  
ANISOU   68  O   LEU A   5      652    925    698    -81      9     98       O  
ATOM     69  CB  LEU A   5       3.590  27.265  23.266  1.00  6.47           C  
ANISOU   69  CB  LEU A   5      638    962    712    -97     28     73       C  
ATOM     70  CG  LEU A   5       4.336  28.586  23.033  1.00  6.72           C  
ANISOU   70  CG  LEU A   5      691    958    752   -162      4     46       C  
ATOM     71  CD1 LEU A   5       5.385  28.780  24.132  1.00  7.62           C  
ANISOU   71  CD1 LEU A   5      789   1173    761   -133    -35    -67       C  
ATOM     72  CD2 LEU A   5       4.990  28.630  21.675  1.00  7.73           C  
ANISOU   72  CD2 LEU A   5      809   1189    764   -295    -18    153       C  
ATOM     73  H   LEU A   5       0.969  28.142  23.408  1.00  9.03           H  
ATOM     74  HA  LEU A   5       2.655  27.236  21.454  1.00  7.77           H  
ATOM     75  HB2 LEU A   5       3.317  27.217  24.195  1.00  7.77           H  
ATOM     76  HB3 LEU A   5       4.197  26.527  23.098  1.00  7.77           H  
ATOM     77  HG  LEU A   5       3.689  29.320  23.090  1.00  8.06           H  
ATOM     78 HD11 LEU A   5       4.958  28.750  24.991  1.00 11.43           H  
ATOM     79 HD12 LEU A   5       6.040  28.081  24.075  1.00 11.43           H  
ATOM     80 HD13 LEU A   5       5.814  29.631  24.017  1.00 11.43           H  
ATOM     81 HD21 LEU A   5       4.324  28.507  20.995  1.00 11.59           H  
ATOM     82 HD22 LEU A   5       5.419  29.481  21.554  1.00 11.59           H  
ATOM     83 HD23 LEU A   5       5.645  27.930  21.612  1.00 11.59           H  
ATOM     84  N   TRP A   6       0.437  25.597  22.321  1.00  7.16           N  
ANISOU   84  N   TRP A   6      568    919   1071   -103      7    135       N  
ATOM     85  CA  TRP A   6      -0.241  24.323  22.256  1.00  7.04           C  
ANISOU   85  CA  TRP A   6      595   1032    890   -158     40    134       C  
ATOM     86  C   TRP A   6       0.164  23.519  21.034  1.00  7.65           C  
ANISOU   86  C   TRP A   6      685   1092    957   -231     93    124       C  
ATOM     87  O   TRP A   6       0.148  22.285  21.063  1.00 10.32           O  
ANISOU   87  O   TRP A   6     1594   1086   1007   -239    468     17       O  
ATOM     88  CB  TRP A   6      -1.764  24.503  22.269  1.00  7.50           C  
ANISOU   88  CB  TRP A   6      635   1153    893   -141     25     52       C  
ATOM     89  CG  TRP A   6      -2.270  25.299  23.435  1.00  7.60           C  
ANISOU   89  CG  TRP A   6      582   1144    988    -62    -73     22       C  
ATOM     90  CD1 TRP A   6      -2.886  26.518  23.391  1.00  8.77           C  
ANISOU   90  CD1 TRP A   6      800   1126   1208     35     63     24       C  
ATOM     91  CD2 TRP A   6      -2.192  24.942  24.818  1.00  8.94           C  
ANISOU   91  CD2 TRP A   6      911   1238   1044    218    -29    -17       C  
ATOM     92  NE1 TRP A   6      -3.198  26.935  24.659  1.00 11.25           N  
ANISOU   92  NE1 TRP A   6     1267   1279   1472    389    -61    -35       N  
ATOM     93  CE2 TRP A   6      -2.796  25.996  25.551  1.00 11.45           C  
ANISOU   93  CE2 TRP A   6     1333   1567   1193    430   -139   -193       C  
ATOM     94  CE3 TRP A   6      -1.710  23.837  25.479  1.00 10.70           C  
ANISOU   94  CE3 TRP A   6     1344   1491    989    498      4     -4       C  
ATOM     95  CZ2 TRP A   6      -2.897  25.959  26.913  1.00 15.31           C  
ANISOU   95  CZ2 TRP A   6     2022   2233   1216   1057   -284   -374       C  
ATOM     96  CZ3 TRP A   6      -1.799  23.855  26.838  1.00 14.45           C  
ANISOU   96  CZ3 TRP A   6     2140   2019   1004   1009     13    125       C  
ATOM     97  CH2 TRP A   6      -2.383  24.896  27.556  1.00 15.41           C  
ANISOU   97  CH2 TRP A   6     2158   2180   1166    873     99    -94       C  
ATOM     98  H   TRP A   6      -0.033  26.316  22.277  1.00  8.59           H  
ATOM     99  HA  TRP A   6       0.008  23.808  23.052  1.00  8.45           H  
ATOM    100  HB2 TRP A   6      -2.033  24.944  21.448  1.00  9.00           H  
ATOM    101  HB3 TRP A   6      -2.182  23.627  22.284  1.00  9.00           H  
ATOM    102  HD1 TRP A   6      -3.068  26.995  22.613  1.00 10.53           H  
ATOM    103  HE1 TRP A   6      -3.586  27.676  24.858  1.00 13.49           H  
ATOM    104  HE3 TRP A   6      -1.342  23.115  25.022  1.00 12.84           H  
ATOM    105  HZ2 TRP A   6      -3.309  26.649  27.381  1.00 18.37           H  
ATOM    106  HZ3 TRP A   6      -1.452  23.134  27.312  1.00 17.34           H  
ATOM    107  HH2 TRP A   6      -2.418  24.856  28.484  1.00 18.49           H  
ATOM    108  N   LYS A   7       0.509  24.194  19.952  1.00  8.08           N  
ANISOU  108  N   LYS A   7      768   1257    862   -210    -40    192       N  
ATOM    109  CA  LYS A   7       1.001  23.568  18.718  1.00  8.29           C  
ANISOU  109  CA  LYS A   7      815   1424    724   -332    -84    101       C  
ATOM    110  C   LYS A   7       2.256  24.359  18.321  1.00  6.90           C  
ANISOU  110  C   LYS A   7      721   1041    704   -179   -145    213       C  
ATOM    111  O   LYS A   7       2.573  25.420  18.851  1.00  7.14           O  
ANISOU  111  O   LYS A   7      774   1050    727   -135    -52    149       O  
ATOM    112  CB  LYS A   7      -0.004  23.496  17.588  1.00 11.26           C  
ANISOU  112  CB  LYS A   7      894   2142    989   -277   -182    155       C  
ATOM    113  CG ALYS A   7      -0.484  24.708  17.067  0.59 10.00           C  
ANISOU  113  CG ALYS A   7      759   1781   1033    -19   -163    -81       C  
ATOM    114  CG BLYS A   7      -1.428  23.120  17.912  0.41 23.58           C  
ANISOU  114  CG BLYS A   7     1267   4744   2413  -1383   -585    317       C  
ATOM    115  CD ALYS A   7      -1.544  24.458  15.992  0.59  9.93           C  
ANISOU  115  CD ALYS A   7      978   1684    886     40   -213     55       C  
ATOM    116  CD BLYS A   7      -1.508  21.646  18.231  0.41 35.35           C  
ANISOU  116  CD BLYS A   7     2840   4710   5082  -2722    403    129       C  
ATOM    117  CE ALYS A   7      -2.121  25.742  15.470  0.59 12.25           C  
ANISOU  117  CE ALYS A   7     1141   1855   1381   -204   -380    519       C  
ATOM    118  CE BLYS A   7      -2.132  20.653  17.322  0.41 44.28           C  
ANISOU  118  CE BLYS A   7     3168   5657   6999  -3094   -635   -445       C  
ATOM    119  NZ ALYS A   7      -3.245  25.563  14.547  0.59 12.31           N  
ANISOU  119  NZ ALYS A   7     1282   1625   1492     86   -473    344       N  
ATOM    120  NZ BLYS A   7      -2.930  21.088  16.131  0.41 50.11           N  
ANISOU  120  NZ BLYS A   7     5181   5872   6851  -4000  -1335     99       N  
ATOM    121  H   LYS A   7       0.441  25.051  19.971  1.00  9.70           H  
ATOM    122  HA  LYS A   7       1.277  22.653  18.934  1.00  9.95           H  
ATOM    123  HB2ALYS A   7       0.400  22.997  16.861  1.00 13.52           H  
ATOM    124  HB3ALYS A   7      -0.766  22.982  17.899  1.00 13.52           H  
ATOM    125  HG2ALYS A   7      -0.868  25.239  17.783  0.59 12.00           H  
ATOM    126  HG2BLYS A   7      -1.738  23.636  18.672  0.41 28.29           H  
ATOM    127  HG3ALYS A   7       0.253  25.209  16.684  0.59 12.00           H  
ATOM    128  HG3BLYS A   7      -1.999  23.322  17.155  0.41 28.29           H  
ATOM    129  HD2ALYS A   7      -1.146  23.964  15.259  0.59 11.92           H  
ATOM    130  HD2BLYS A   7      -0.598  21.347  18.385  0.41 42.43           H  
ATOM    131  HD3ALYS A   7      -2.257  23.915  16.366  0.59 11.92           H  
ATOM    132  HD3BLYS A   7      -1.970  21.572  19.081  0.41 42.43           H  
ATOM    133  HE2ALYS A   7      -2.418  26.279  16.221  0.59 14.70           H  
ATOM    134  HE2BLYS A   7      -1.421  20.081  16.994  0.41 53.14           H  
ATOM    135  HE3ALYS A   7      -1.421  26.236  15.015  0.59 14.70           H  
ATOM    136  HE3BLYS A   7      -2.712  20.096  17.864  0.41 53.14           H  
ATOM    137  HZ1ALYS A   7      -3.537  26.359  14.277  0.59 18.47           H  
ATOM    138  HZ1BLYS A   7      -3.231  20.371  15.697  0.41 75.16           H  
ATOM    139  HZ2ALYS A   7      -2.978  25.090  13.842  0.59 18.47           H  
ATOM    140  HZ2BLYS A   7      -3.619  21.582  16.400  0.41 75.16           H  
ATOM    141  HZ3ALYS A   7      -3.903  25.130  14.962  0.59 18.47           H  
ATOM    142  HZ3BLYS A   7      -2.414  21.568  15.587  0.41 75.16           H  
ATOM    143  N   ARG A   8       2.975  23.822  17.332  1.00  7.13           N  
ANISOU  143  N   ARG A   8      891   1018    639   -286   -108    141       N  
ATOM    144  CA  ARG A   8       4.162  24.521  16.848  1.00  6.48           C  
ANISOU  144  CA  ARG A   8      784    952    581   -207   -109    109       C  
ATOM    145  C   ARG A   8       3.797  25.919  16.377  1.00  6.56           C  
ANISOU  145  C   ARG A   8      819    953    573   -188    -88    124       C  
ATOM    146  O   ARG A   8       2.819  26.086  15.623  1.00  7.74           O  
ANISOU  146  O   ARG A   8      851   1210    705   -200   -221    242       O  
ATOM    147  CB  ARG A   8       4.790  23.746  15.680  1.00  7.17           C  
ANISOU  147  CB  ARG A   8      953   1031    578   -234   -110     74       C  
ATOM    148  CG  ARG A   8       5.436  22.415  16.119  1.00  7.82           C  
ANISOU  148  CG  ARG A   8     1103   1062    628    -81    -25     -2       C  
ATOM    149  CD AARG A   8       6.384  21.891  15.045  0.39  7.50           C  
ANISOU  149  CD AARG A   8     1095    968    616   -146     23     39       C  
ATOM    150  CD BARG A   8       5.695  21.464  14.920  0.61  9.58           C  
ANISOU  150  CD BARG A   8     1518   1256    650     12   -138    -69       C  
ATOM    151  NE AARG A   8       7.195  20.819  15.564  0.39  7.68           N  
ANISOU  151  NE AARG A   8     1036   1012    698    -38    124    -22       N  
ATOM    152  NE BARG A   8       6.153  20.179  15.377  0.61  9.66           N  
ANISOU  152  NE BARG A   8     1667   1058    726   -234   -405   -169       N  
ATOM    153  CZ AARG A   8       8.105  20.117  14.894  0.39  8.25           C  
ANISOU  153  CZ AARG A   8     1147    911    891   -188    304   -219       C  
ATOM    154  CZ BARG A   8       6.156  19.055  14.656  0.61  9.98           C  
ANISOU  154  CZ BARG A   8     1406   1269    891     -8   -336   -255       C  
ATOM    155  NH1AARG A   8       8.296  20.394  13.616  0.39 10.74           N  
ANISOU  155  NH1AARG A   8     1518   1284   1037    -22    406   -114       N  
ATOM    156  NH1BARG A   8       5.739  19.099  13.404  0.61 13.94           N  
ANISOU  156  NH1BARG A   8     2542   1590    850     92   -656   -438       N  
ATOM    157  NH2AARG A   8       8.766  19.151  15.550  0.39  9.29           N  
ANISOU  157  NH2AARG A   8     1212    894   1214    -88    450   -235       N  
ATOM    158  NH2BARG A   8       6.556  17.948  15.179  0.61 11.89           N  
ANISOU  158  NH2BARG A   8     2038   1117   1092    -16   -702   -336       N  
ATOM    159  H   ARG A   8       2.741  23.071  16.983  1.00  8.56           H  
ATOM    160  HA  ARG A   8       4.814  24.588  17.576  1.00  7.78           H  
ATOM    161  HB2 ARG A   8       4.105  23.561  15.019  1.00  8.61           H  
ATOM    162  HB3 ARG A   8       5.466  24.301  15.260  1.00  8.61           H  
ATOM    163  HG2AARG A   8       5.927  22.550  16.945  1.00  9.38           H  
ATOM    164  HG3AARG A   8       4.742  21.758  16.286  1.00  9.38           H  
ATOM    165  HD2AARG A   8       5.870  21.571  14.287  0.39  9.00           H  
ATOM    166  HD2BARG A   8       4.877  21.355  14.411  0.61 11.50           H  
ATOM    167  HD3AARG A   8       6.957  22.611  14.738  0.39  9.00           H  
ATOM    168  HD3BARG A   8       6.362  21.856  14.335  0.61 11.50           H  
ATOM    169  HE AARG A   8       7.079  20.612  16.390  0.39  9.22           H  
ATOM    170  HE BARG A   8       6.449  20.130  16.182  0.61 11.59           H  
ATOM    171 HH11AARG A   8       7.838  21.015  13.237  0.39 12.89           H  
ATOM    172 HH11BARG A   8       5.731  18.383  12.928  0.61 16.73           H  
ATOM    173 HH12AARG A   8       8.879  19.953  13.163  0.39 12.89           H  
ATOM    174 HH12BARG A   8       5.474  19.844  13.065  0.61 16.73           H  
ATOM    175 HH21AARG A   8       9.349  18.673  15.137  0.39 11.15           H  
ATOM    176 HH21BARG A   8       6.553  17.226  14.712  0.61 14.26           H  
ATOM    177 HH22AARG A   8       8.605  19.009  16.383  0.39 11.15           H  
ATOM    178 HH22BARG A   8       6.826  17.931  15.995  0.61 14.26           H  
ATOM    179  N   PRO A   9       4.586  26.948  16.739  1.00  6.23           N  
ANISOU  179  N   PRO A   9      778    912    536   -141   -110    140       N  
ATOM    180  CA  PRO A   9       4.261  28.343  16.348  1.00  6.59           C  
ANISOU  180  CA  PRO A   9      836    964    556    -22    -40    149       C  
ATOM    181  C   PRO A   9       4.776  28.639  14.932  1.00  6.37           C  
ANISOU  181  C   PRO A   9      776    920    581      2    -79    139       C  
ATOM    182  O   PRO A   9       5.810  29.246  14.730  1.00  7.12           O  
ANISOU  182  O   PRO A   9      802   1107    636   -135    -77    123       O  
ATOM    183  CB  PRO A   9       4.940  29.179  17.421  1.00  7.34           C  
ANISOU  183  CB  PRO A   9     1084    970    570    -50    -68    113       C  
ATOM    184  CG  PRO A   9       6.133  28.339  17.840  1.00  7.14           C  
ANISOU  184  CG  PRO A   9      950    989    611   -173   -155    142       C  
ATOM    185  CD  PRO A   9       5.587  26.915  17.837  1.00  6.54           C  
ANISOU  185  CD  PRO A   9      854    976    509   -128   -139    129       C  
ATOM    186  HA  PRO A   9       3.291  28.481  16.384  1.00  7.91           H  
ATOM    187  HB2 PRO A   9       5.227  30.035  17.064  1.00  8.81           H  
ATOM    188  HB3 PRO A   9       4.344  29.334  18.170  1.00  8.81           H  
ATOM    189  HG2 PRO A   9       6.864  28.433  17.209  1.00  8.57           H  
ATOM    190  HG3 PRO A   9       6.443  28.591  18.724  1.00  8.57           H  
ATOM    191  HD2 PRO A   9       6.288  26.271  17.653  1.00  7.85           H  
ATOM    192  HD3 PRO A   9       5.170  26.698  18.685  1.00  7.85           H  
ATOM    193  N   LEU A  10       4.002  28.168  13.963  1.00  7.92           N  
ANISOU  193  N   LEU A  10      930   1342    559   -279   -130    221       N  
ATOM    194  CA  LEU A  10       4.297  28.342  12.551  1.00  7.59           C  
ANISOU  194  CA  LEU A  10      886   1284    541   -162   -133    161       C  
ATOM    195  C   LEU A  10       3.631  29.608  12.021  1.00  7.69           C  
ANISOU  195  C   LEU A  10      789   1397    561    -38    -74    165       C  
ATOM    196  O   LEU A  10       2.452  29.889  12.358  1.00 10.48           O  
ANISOU  196  O   LEU A  10      759   2132    854     69    -32    481       O  
ATOM    197  CB  LEU A  10       3.794  27.121  11.755  1.00  9.51           C  
ANISOU  197  CB  LEU A  10     1222   1488    689   -290   -205     39       C  
ATOM    198  CG  LEU A  10       4.513  25.802  12.072  1.00 12.03           C  
ANISOU  198  CG  LEU A  10     2044   1272    982   -425   -373     78       C  
ATOM    199  CD1 LEU A  10       3.806  24.653  11.395  1.00 18.34           C  
ANISOU  199  CD1 LEU A  10     2185   1653   2715   -561   -487   -597       C  
ATOM    200  CD2 LEU A  10       5.983  25.823  11.623  1.00 15.17           C  
ANISOU  200  CD2 LEU A  10     1555   1301   2565     13  -1028   -268       C  
ATOM    201  H   LEU A  10       3.290  27.739  14.182  1.00  9.51           H  
ATOM    202  HA  LEU A  10       5.267  28.420  12.436  1.00  9.11           H  
ATOM    203  HB2 LEU A  10       2.847  27.006  11.931  1.00 11.42           H  
ATOM    204  HB3 LEU A  10       3.894  27.307  10.808  1.00 11.42           H  
ATOM    205  HG  LEU A  10       4.485  25.657  13.041  1.00 14.43           H  
ATOM    206 HD11 LEU A  10       4.261  23.833  11.598  1.00 27.51           H  
ATOM    207 HD12 LEU A  10       2.901  24.603  11.711  1.00 27.51           H  
ATOM    208 HD13 LEU A  10       3.806  24.792  10.445  1.00 27.51           H  
ATOM    209 HD21 LEU A  10       6.438  26.552  12.051  1.00 22.75           H  
ATOM    210 HD22 LEU A  10       6.404  24.996  11.867  1.00 22.75           H  
ATOM    211 HD23 LEU A  10       6.025  25.935  10.670  1.00 22.75           H  
ATOM    212  N   VAL A  11       4.334  30.341  11.189  1.00  7.28           N  
ANISOU  212  N   VAL A  11      805   1247    550    108    -12    111       N  
ATOM    213  CA  VAL A  11       3.836  31.535  10.544  1.00  7.65           C  
ANISOU  213  CA  VAL A  11      785   1365    585    232      3    189       C  
ATOM    214  C   VAL A  11       4.256  31.541   9.080  1.00  7.40           C  
ANISOU  214  C   VAL A  11      859   1151    632    150    -44    151       C  
ATOM    215  O   VAL A  11       5.135  30.796   8.666  1.00  8.67           O  
ANISOU  215  O   VAL A  11     1110   1397    591    372     11    173       O  
ATOM    216  CB  VAL A  11       4.336  32.810  11.229  1.00  9.15           C  
ANISOU  216  CB  VAL A  11     1397   1129    745    249   -109    108       C  
ATOM    217  CG1 VAL A  11       3.858  32.893  12.677  1.00 11.16           C  
ANISOU  217  CG1 VAL A  11     1828   1357    804    317    -71    -71       C  
ATOM    218  CG2 VAL A  11       5.823  32.998  11.105  1.00 10.68           C  
ANISOU  218  CG2 VAL A  11     1551   1318    946   -223   -169    279       C  
ATOM    219  H   VAL A  11       5.141  30.097  11.018  1.00  8.74           H  
ATOM    220  HA  VAL A  11       2.857  31.524  10.586  1.00  9.18           H  
ATOM    221  HB  VAL A  11       3.921  33.561  10.756  1.00 10.98           H  
ATOM    222 HG11 VAL A  11       2.907  32.768  12.708  1.00 16.75           H  
ATOM    223 HG12 VAL A  11       4.287  32.209  13.196  1.00 16.75           H  
ATOM    224 HG13 VAL A  11       4.079  33.755  13.038  1.00 16.75           H  
ATOM    225 HG21 VAL A  11       6.077  32.939  10.181  1.00 16.01           H  
ATOM    226 HG22 VAL A  11       6.066  33.861  11.449  1.00 16.01           H  
ATOM    227 HG23 VAL A  11       6.275  32.315  11.606  1.00 16.01           H  
ATOM    228  N   THR A  12       3.622  32.427   8.306  1.00  8.82           N  
ANISOU  228  N   THR A  12      971   1530    652    354     -8    293       N  
ATOM    229  CA  THR A  12       4.022  32.660   6.922  1.00  8.87           C  
ANISOU  229  CA  THR A  12     1060   1475    635    274    -70    175       C  
ATOM    230  C   THR A  12       5.106  33.726   6.883  1.00  8.09           C  
ANISOU  230  C   THR A  12     1151   1160    581    304    -29    132       C  
ATOM    231  O   THR A  12       5.014  34.769   7.529  1.00  9.88           O  
ANISOU  231  O   THR A  12     1326   1322    881    336    130     28       O  
ATOM    232  CB  THR A  12       2.812  33.084   6.086  1.00 11.44           C  
ANISOU  232  CB  THR A  12     1208   1996    883    210   -229    459       C  
ATOM    233  OG1 THR A  12       1.808  32.071   6.191  1.00 14.39           O  
ANISOU  233  OG1 THR A  12     1249   2763   1128    -63   -346    510       O  
ATOM    234  CG2 THR A  12       3.214  33.286   4.619  1.00 14.27           C  
ANISOU  234  CG2 THR A  12     1490   2795    814    150   -329    577       C  
ATOM    235  H   THR A  12       2.961  32.871   8.632  1.00 10.59           H  
ATOM    236  HA  THR A  12       4.384  31.828   6.553  1.00 10.65           H  
ATOM    237  HB  THR A  12       2.457  33.926   6.440  1.00 13.72           H  
ATOM    238  HG1 THR A  12       1.604  31.969   6.978  1.00 21.58           H  
ATOM    239 HG21 THR A  12       3.888  33.967   4.562  1.00 21.41           H  
ATOM    240 HG22 THR A  12       3.560  32.463   4.266  1.00 21.41           H  
ATOM    241 HG23 THR A  12       2.444  33.554   4.111  1.00 21.41           H  
ATOM    242  N   ILE A  13       6.117  33.452   6.076  1.00  7.98           N  
ANISOU  242  N   ILE A  13     1170   1101    582    218    -21     93       N  
ATOM    243  CA  ILE A  13       7.185  34.377   5.810  1.00  8.11           C  
ANISOU  243  CA  ILE A  13     1263   1047    588    260     45    127       C  
ATOM    244  C   ILE A  13       7.247  34.637   4.296  1.00  8.21           C  
ANISOU  244  C   ILE A  13     1199   1144    590    240     -9     59       C  
ATOM    245  O   ILE A  13       6.813  33.818   3.485  1.00  9.15           O  
ANISOU  245  O   ILE A  13     1415   1224    631    243    -39    135       O  
ATOM    246  CB  ILE A  13       8.544  33.877   6.318  1.00  7.90           C  
ANISOU  246  CB  ILE A  13     1131   1093    597     98    -40     67       C  
ATOM    247  CG1 ILE A  13       9.069  32.640   5.544  1.00  8.64           C  
ANISOU  247  CG1 ILE A  13     1154   1307    626    272   -103    -48       C  
ATOM    248  CG2 ILE A  13       8.431  33.586   7.811  1.00  8.54           C  
ANISOU  248  CG2 ILE A  13     1355   1116    581    276    -77     88       C  
ATOM    249  CD1 ILE A  13      10.497  32.278   5.831  1.00  8.61           C  
ANISOU  249  CD1 ILE A  13     1114   1251    714    158   -112     86       C  
ATOM    250  H   ILE A  13       6.137  32.683   5.691  1.00  9.58           H  
ATOM    251  HA  ILE A  13       6.980  35.223   6.260  1.00  9.73           H  
ATOM    252  HB  ILE A  13       9.193  34.602   6.202  1.00  9.47           H  
ATOM    253 HG12 ILE A  13       8.508  31.879   5.761  1.00 10.37           H  
ATOM    254 HG13 ILE A  13       8.978  32.809   4.593  1.00 10.37           H  
ATOM    255 HG21 ILE A  13       9.277  33.272   8.141  1.00 12.81           H  
ATOM    256 HG22 ILE A  13       8.185  34.388   8.276  1.00 12.81           H  
ATOM    257 HG23 ILE A  13       7.762  32.913   7.956  1.00 12.81           H  
ATOM    258 HD11 ILE A  13      10.741  31.507   5.314  1.00 12.92           H  
ATOM    259 HD12 ILE A  13      11.067  33.014   5.596  1.00 12.92           H  
ATOM    260 HD13 ILE A  13      10.596  32.083   6.765  1.00 12.92           H  
ATOM    261  N   LYS A  14       7.822  35.798   3.974  1.00  8.72           N  
ANISOU  261  N   LYS A  14     1243   1207    664    138     20    230       N  
ATOM    262  CA  LYS A  14       8.135  36.134   2.578  1.00  9.88           C  
ANISOU  262  CA  LYS A  14     1183   1611    736    147    -31    377       C  
ATOM    263  C   LYS A  14       9.641  36.389   2.555  1.00  9.01           C  
ANISOU  263  C   LYS A  14     1215   1348    655    105     -9    300       C  
ATOM    264  O   LYS A  14      10.160  37.238   3.266  1.00  9.83           O  
ANISOU  264  O   LYS A  14     1268   1381    865    162     30    109       O  
ATOM    265  CB  LYS A  14       7.363  37.287   2.057  1.00 13.47           C  
ANISOU  265  CB  LYS A  14     1334   2089   1390    373    -37    917       C  
ATOM    266  CG  LYS A  14       7.519  37.354   0.498  1.00 19.97           C  
ANISOU  266  CG  LYS A  14     2319   3422   1396    835    -53   1150       C  
ATOM    267  CD  LYS A  14       6.581  38.398  -0.108  1.00 32.68           C  
ANISOU  267  CD  LYS A  14     4483   5265   1929   2523    168   1742       C  
ATOM    268  CE  LYS A  14       6.654  38.433  -1.623  1.00 43.77           C  
ANISOU  268  CE  LYS A  14     7646   6129   1865   3785     18   1695       C  
ATOM    269  NZ  LYS A  14       5.341  38.818  -2.224  1.00 63.82           N  
ANISOU  269  NZ  LYS A  14     9690  10162   2950   5483  -1973    747       N  
ATOM    270  H   LYS A  14       8.012  36.361   4.596  1.00 10.46           H  
ATOM    271  HA  LYS A  14       7.942  35.352   2.019  1.00 11.85           H  
ATOM    272  HB2 LYS A  14       6.427  37.188   2.291  1.00 16.16           H  
ATOM    273  HB3 LYS A  14       7.691  38.108   2.456  1.00 16.16           H  
ATOM    274  HG2 LYS A  14       8.436  37.578   0.275  1.00 23.97           H  
ATOM    275  HG3 LYS A  14       7.321  36.484   0.117  1.00 23.97           H  
ATOM    276  HD2 LYS A  14       5.670  38.201   0.162  1.00 39.22           H  
ATOM    277  HD3 LYS A  14       6.811  39.273   0.242  1.00 39.22           H  
ATOM    278  HE2 LYS A  14       7.332  39.069  -1.897  1.00 52.52           H  
ATOM    279  HE3 LYS A  14       6.914  37.558  -1.952  1.00 52.52           H  
ATOM    280  HZ1 LYS A  14       5.413  38.830  -3.111  1.00 95.72           H  
ATOM    281  HZ2 LYS A  14       4.720  38.226  -1.985  1.00 95.72           H  
ATOM    282  HZ3 LYS A  14       5.107  39.626  -1.934  1.00 95.72           H  
ATOM    283  N   ILE A  15      10.334  35.637   1.683  1.00  9.42           N  
ANISOU  283  N   ILE A  15     1183   1525    657     45      0    127       N  
ATOM    284  CA  ILE A  15      11.761  35.731   1.592  1.00  9.68           C  
ANISOU  284  CA  ILE A  15     1164   1507    787    -50     28     41       C  
ATOM    285  C   ILE A  15      12.120  35.483   0.138  1.00  9.91           C  
ANISOU  285  C   ILE A  15     1300   1457    784     92     81     -2       C  
ATOM    286  O   ILE A  15      11.656  34.500  -0.463  1.00  9.80           O  
ANISOU  286  O   ILE A  15     1329   1465    709     12      6    128       O  
ATOM    287  CB  ILE A  15      12.466  34.725   2.521  1.00 10.93           C  
ANISOU  287  CB  ILE A  15     1210   1974    720    163    -28     51       C  
ATOM    288  CG1 ILE A  15      13.975  34.906   2.370  1.00 13.81           C  
ANISOU  288  CG1 ILE A  15     1206   2549   1179    291    -67     71       C  
ATOM    289  CG2 ILE A  15      12.010  33.284   2.353  1.00 11.81           C  
ANISOU  289  CG2 ILE A  15     1597   1780    844    377     12    237       C  
ATOM    290  CD1 ILE A  15      14.785  34.063   3.288  1.00 15.31           C  
ANISOU  290  CD1 ILE A  15     1608   2550   1313    507    -87    247       C  
ATOM    291  H   ILE A  15       9.913  35.089   1.171  1.00 11.30           H  
ATOM    292  HA  ILE A  15      12.037  36.639   1.838  1.00 11.61           H  
ATOM    293  HB  ILE A  15      12.242  34.986   3.439  1.00 13.11           H  
ATOM    294 HG12 ILE A  15      14.223  34.698   1.456  1.00 16.57           H  
ATOM    295 HG13 ILE A  15      14.194  35.838   2.529  1.00 16.57           H  
ATOM    296 HG21 ILE A  15      11.057  33.236   2.458  1.00 17.72           H  
ATOM    297 HG22 ILE A  15      12.251  32.973   1.477  1.00 17.72           H  
ATOM    298 HG23 ILE A  15      12.433  32.735   3.016  1.00 17.72           H  
ATOM    299 HD11 ILE A  15      15.718  34.231   3.135  1.00 22.97           H  
ATOM    300 HD12 ILE A  15      14.566  34.278   4.197  1.00 22.97           H  
ATOM    301 HD13 ILE A  15      14.595  33.137   3.123  1.00 22.97           H  
ATOM    302  N   GLY A  16      12.978  36.324  -0.451  1.00 11.06           N  
ANISOU  302  N   GLY A  16     1555   1535    862    -78    189      8       N  
ATOM    303  CA  GLY A  16      13.438  36.045  -1.782  1.00 11.87           C  
ANISOU  303  CA  GLY A  16     1750   1602    891   -181    334     34       C  
ATOM    304  C   GLY A  16      12.317  35.979  -2.776  1.00 12.03           C  
ANISOU  304  C   GLY A  16     1942   1512    844   -304    237    107       C  
ATOM    305  O   GLY A  16      12.423  35.271  -3.795  1.00 15.09           O  
ANISOU  305  O   GLY A  16     2584   1958    849   -350    335    -63       O  
ATOM    306  H   GLY A  16      13.251  37.026  -0.036  1.00 13.27           H  
ATOM    307  HA2 GLY A  16      14.062  36.736  -2.054  1.00 14.25           H  
ATOM    308  HA3 GLY A  16      13.913  35.199  -1.783  1.00 14.25           H  
ATOM    309  N   GLY A  17      11.224  36.699  -2.569  1.00 12.63           N  
ANISOU  309  N   GLY A  17     2071   1450    991   -141    -65    312       N  
ATOM    310  CA  GLY A  17      10.108  36.687  -3.457  1.00 14.85           C  
ANISOU  310  CA  GLY A  17     2402   1614   1290   -173   -398    517       C  
ATOM    311  C   GLY A  17       9.184  35.500  -3.264  1.00 13.54           C  
ANISOU  311  C   GLY A  17     2102   1470   1265     38   -439    388       C  
ATOM    312  O   GLY A  17       8.226  35.341  -4.062  1.00 19.68           O  
ANISOU  312  O   GLY A  17     2823   2205   2005   -415  -1250    908       O  
ATOM    313  H   GLY A  17      11.186  37.195  -1.868  1.00 15.15           H  
ATOM    314  HA2 GLY A  17       9.600  37.503  -3.331  1.00 17.82           H  
ATOM    315  HA3 GLY A  17      10.435  36.682  -4.370  1.00 17.82           H  
ATOM    316  N   GLN A  18       9.458  34.609  -2.316  1.00 10.30           N  
ANISOU  316  N   GLN A  18     1508   1404    769    122   -101    147       N  
ATOM    317  CA  GLN A  18       8.732  33.386  -2.101  1.00 10.02           C  
ANISOU  317  CA  GLN A  18     1466   1486    629    151    -79     43       C  
ATOM    318  C   GLN A  18       8.000  33.398  -0.767  1.00 10.15           C  
ANISOU  318  C   GLN A  18     1261   1687    680    169    -72     87       C  
ATOM    319  O   GLN A  18       8.487  33.924   0.206  1.00 15.96           O  
ANISOU  319  O   GLN A  18     1700   3070    934   -594    270   -612       O  
ATOM    320  CB  GLN A  18       9.720  32.199  -2.073  1.00  9.54           C  
ANISOU  320  CB  GLN A  18     1397   1397    614    -12    -68     71       C  
ATOM    321  CG  GLN A  18      10.453  32.017  -3.413  1.00 10.41           C  
ANISOU  321  CG  GLN A  18     1358   1612    751     95     -8    127       C  
ATOM    322  CD  GLN A  18      11.517  30.985  -3.403  1.00 11.85           C  
ANISOU  322  CD  GLN A  18     1403   1983    847    227     69    241       C  
ATOM    323  OE1 GLN A  18      12.622  31.273  -3.841  1.00 20.68           O  
ANISOU  323  OE1 GLN A  18     1485   2837   3066    502    834   1079       O  
ATOM    324  NE2 GLN A  18      11.242  29.792  -2.920  1.00 11.14           N  
ANISOU  324  NE2 GLN A  18     1417   1663    900    283     19     43       N  
ATOM    325  H   GLN A  18      10.119  34.777  -1.792  1.00 12.36           H  
ATOM    326  HA  GLN A  18       8.087  33.257  -2.827  1.00 12.03           H  
ATOM    327  HB2 GLN A  18      10.373  32.346  -1.371  1.00 11.45           H  
ATOM    328  HB3 GLN A  18       9.235  31.386  -1.863  1.00 11.45           H  
ATOM    329  HG2 GLN A  18       9.801  31.782  -4.092  1.00 12.50           H  
ATOM    330  HG3 GLN A  18      10.847  32.866  -3.667  1.00 12.50           H  
ATOM    331 HE21 GLN A  18      11.849  29.184  -2.904  1.00 13.36           H  
ATOM    332 HE22 GLN A  18      10.455  29.622  -2.619  1.00 13.36           H  
ATOM    333  N   LEU A  19       6.883  32.726  -0.702  1.00  9.60           N  
ANISOU  333  N   LEU A  19     1394   1467    569    172   -161    147       N  
ATOM    334  CA  LEU A  19       6.160  32.481   0.528  1.00  9.52           C  
ANISOU  334  CA  LEU A  19     1239   1491    673    188    -64     84       C  
ATOM    335  C   LEU A  19       6.545  31.110   1.062  1.00  9.32           C  
ANISOU  335  C   LEU A  19     1327   1451    550    221    -23     52       C  
ATOM    336  O   LEU A  19       6.603  30.117   0.304  1.00 10.73           O  
ANISOU  336  O   LEU A  19     1746   1495    594    118   -105     43       O  
ATOM    337  CB  LEU A  19       4.658  32.497   0.317  1.00 11.25           C  
ANISOU  337  CB  LEU A  19     1227   1786   1008    308   -129    131       C  
ATOM    338  CG  LEU A  19       4.121  33.885  -0.094  1.00 13.19           C  
ANISOU  338  CG  LEU A  19     1489   2095   1130    492   -155    306       C  
ATOM    339  CD1 LEU A  19       2.654  33.706  -0.524  1.00 20.97           C  
ANISOU  339  CD1 LEU A  19     1702   2983   2809    868   -849   -180       C  
ATOM    340  CD2 LEU A  19       4.285  34.877   1.024  1.00 16.90           C  
ANISOU  340  CD2 LEU A  19     2273   1846   1920    761   -582    -65       C  
ATOM    341  H   LEU A  19       6.557  32.410  -1.433  1.00 11.52           H  
ATOM    342  HA  LEU A  19       6.402  33.165   1.187  1.00 11.43           H  
ATOM    343  HB2 LEU A  19       4.429  31.853  -0.371  1.00 13.50           H  
ATOM    344  HB3 LEU A  19       4.221  32.221   1.138  1.00 13.50           H  
ATOM    345  HG  LEU A  19       4.634  34.200  -0.867  1.00 15.83           H  
ATOM    346 HD11 LEU A  19       2.605  33.065  -1.237  1.00 31.46           H  
ATOM    347 HD12 LEU A  19       2.138  33.393   0.223  1.00 31.46           H  
ATOM    348 HD13 LEU A  19       2.304  34.547  -0.825  1.00 31.46           H  
ATOM    349 HD21 LEU A  19       5.215  34.950   1.252  1.00 25.35           H  
ATOM    350 HD22 LEU A  19       3.956  35.734   0.743  1.00 25.35           H  
ATOM    351 HD23 LEU A  19       3.790  34.580   1.791  1.00 25.35           H  
ATOM    352  N   LYS A  20       6.826  31.039   2.366  1.00  8.46           N  
ANISOU  352  N   LYS A  20     1226   1238    560    250    -35     18       N  
ATOM    353  CA  LYS A  20       7.162  29.826   3.040  1.00  8.25           C  
ANISOU  353  CA  LYS A  20     1199   1178    570    135     25     54       C  
ATOM    354  C   LYS A  20       6.479  29.814   4.425  1.00  8.00           C  
ANISOU  354  C   LYS A  20     1069   1247    545     46    -52     -7       C  
ATOM    355  O   LYS A  20       6.156  30.854   4.966  1.00 10.25           O  
ANISOU  355  O   LYS A  20     1560   1273    830     23    384    -88       O  
ATOM    356  CB  LYS A  20       8.664  29.635   3.206  1.00  8.31           C  
ANISOU  356  CB  LYS A  20     1171   1156    642    161     57     57       C  
ATOM    357  CG  LYS A  20       9.393  29.377   1.888  1.00  8.67           C  
ANISOU  357  CG  LYS A  20     1230   1272    597    121     17    -35       C  
ATOM    358  CD  LYS A  20      10.847  29.106   2.028  1.00  8.91           C  
ANISOU  358  CD  LYS A  20     1103   1393    688     49     66    -59       C  
ATOM    359  CE  LYS A  20      11.577  28.735   0.746  1.00 10.05           C  
ANISOU  359  CE  LYS A  20     1191   1730    670     30     92   -180       C  
ATOM    360  NZ  LYS A  20      11.016  27.525   0.117  1.00  9.49           N  
ANISOU  360  NZ  LYS A  20     1214   1626    552    238     -3   -151       N  
ATOM    361  H   LYS A  20       6.803  31.765   2.827  1.00 10.16           H  
ATOM    362  HA  LYS A  20       6.811  29.075   2.516  1.00  9.90           H  
ATOM    363  HB2 LYS A  20       9.037  30.428   3.621  1.00  9.97           H  
ATOM    364  HB3 LYS A  20       8.821  28.887   3.804  1.00  9.97           H  
ATOM    365  HG2 LYS A  20       8.978  28.618   1.448  1.00 10.41           H  
ATOM    366  HG3 LYS A  20       9.276  30.149   1.313  1.00 10.41           H  
ATOM    367  HD2 LYS A  20      11.270  29.895   2.403  1.00 10.69           H  
ATOM    368  HD3 LYS A  20      10.963  28.384   2.665  1.00 10.69           H  
ATOM    369  HE2 LYS A  20      11.519  29.475   0.121  1.00 12.06           H  
ATOM    370  HE3 LYS A  20      12.514  28.585   0.945  1.00 12.06           H  
ATOM    371  HZ1 LYS A  20      11.468  27.341  -0.627  1.00 14.24           H  
ATOM    372  HZ2 LYS A  20      11.082  26.840   0.681  1.00 14.24           H  
ATOM    373  HZ3 LYS A  20      10.160  27.664  -0.082  1.00 14.24           H  
ATOM    374  N   GLU A  21       6.347  28.634   4.988  1.00  7.96           N  
ANISOU  374  N   GLU A  21     1076   1254    514     67    -58     55       N  
ATOM    375  CA  GLU A  21       5.943  28.464   6.382  1.00  7.88           C  
ANISOU  375  CA  GLU A  21      881   1382    553     63    -88    116       C  
ATOM    376  C   GLU A  21       7.205  28.281   7.211  1.00  6.91           C  
ANISOU  376  C   GLU A  21      802   1084    583     47    -70     43       C  
ATOM    377  O   GLU A  21       8.100  27.531   6.814  1.00  8.73           O  
ANISOU  377  O   GLU A  21      955   1491    674    154   -127   -251       O  
ATOM    378  CB  GLU A  21       5.040  27.239   6.509  1.00 10.85           C  
ANISOU  378  CB  GLU A  21      950   2065    864   -317   -225    343       C  
ATOM    379  CG  GLU A  21       4.556  26.905   7.849  1.00 22.10           C  
ANISOU  379  CG  GLU A  21     2440   4382   1074  -1599     46    474       C  
ATOM    380  CD  GLU A  21       3.758  25.591   7.904  1.00 28.07           C  
ANISOU  380  CD  GLU A  21     3271   4779   1979  -2143    387    757       C  
ATOM    381  OE1 GLU A  21       4.277  24.427   7.925  1.00 34.12           O  
ANISOU  381  OE1 GLU A  21     5700   4424   2069  -2067    136    255       O  
ATOM    382  OE2 GLU A  21       2.520  25.677   8.016  1.00 42.32           O  
ANISOU  382  OE2 GLU A  21     2730   7986   4405  -2574  -1618   3681       O  
ATOM    383  H   GLU A  21       6.506  27.932   4.516  1.00  9.55           H  
ATOM    384  HA  GLU A  21       5.461  29.262   6.685  1.00  9.46           H  
ATOM    385  HB2 GLU A  21       4.269  27.373   5.936  1.00 13.03           H  
ATOM    386  HB3 GLU A  21       5.524  26.472   6.165  1.00 13.03           H  
ATOM    387  HG2 GLU A  21       5.315  26.836   8.449  1.00 26.52           H  
ATOM    388  HG3 GLU A  21       3.993  27.627   8.168  1.00 26.52           H  
ATOM    389  N   ALA A  22       7.259  28.915   8.371  1.00  6.39           N  
ANISOU  389  N   ALA A  22      775   1031    478    104    -19     93       N  
ATOM    390  CA  ALA A  22       8.455  28.816   9.214  1.00  5.84           C  
ANISOU  390  CA  ALA A  22      767    885    433     55    -16     69       C  
ATOM    391  C   ALA A  22       8.059  28.865  10.687  1.00  5.91           C  
ANISOU  391  C   ALA A  22      805    848    460     72     12     78       C  
ATOM    392  O   ALA A  22       7.028  29.385  11.082  1.00  7.73           O  
ANISOU  392  O   ALA A  22      955   1250    556    321     90    195       O  
ATOM    393  CB  ALA A  22       9.451  29.919   8.890  1.00  6.55           C  
ANISOU  393  CB  ALA A  22      955    861    525    -25     17     76       C  
ATOM    394  H   ALA A  22       6.589  29.386   8.633  1.00  7.67           H  
ATOM    395  HA  ALA A  22       8.884  27.953   9.039  1.00  7.00           H  
ATOM    396  HB1 ALA A  22      10.222  29.830   9.455  1.00  9.83           H  
ATOM    397  HB2 ALA A  22       9.719  29.849   7.970  1.00  9.83           H  
ATOM    398  HB3 ALA A  22       9.042  30.775   9.039  1.00  9.83           H  
ATOM    399  N   LEU A  23       8.958  28.307  11.498  1.00  5.60           N  
ANISOU  399  N   LEU A  23      747    867    388     16     11     63       N  
ATOM    400  CA  LEU A  23       8.771  28.131  12.944  1.00  5.41           C  
ANISOU  400  CA  LEU A  23      731    805    397    -74     14     49       C  
ATOM    401  C   LEU A  23       9.425  29.271  13.710  1.00  5.55           C  
ANISOU  401  C   LEU A  23      745    811    428    -85     26     69       C  
ATOM    402  O   LEU A  23      10.624  29.524  13.536  1.00  6.37           O  
ANISOU  402  O   LEU A  23      696    986    594   -127    116    -36       O  
ATOM    403  CB  LEU A  23       9.417  26.796  13.289  1.00  5.93           C  
ANISOU  403  CB  LEU A  23      836    780    502    -65    -37     57       C  
ATOM    404  CG  LEU A  23       9.336  26.319  14.741  1.00  7.05           C  
ANISOU  404  CG  LEU A  23     1175    888    458   -164    -69     59       C  
ATOM    405  CD1 LEU A  23       7.927  26.033  15.136  1.00  9.26           C  
ANISOU  405  CD1 LEU A  23     1248   1201    862   -119    233    269       C  
ATOM    406  CD2 LEU A  23      10.229  25.111  14.907  1.00  8.15           C  
ANISOU  406  CD2 LEU A  23     1356    995    560     16   -114    127       C  
ATOM    407  H   LEU A  23       9.696  28.032  11.152  1.00  6.72           H  
ATOM    408  HA  LEU A  23       7.814  28.099  13.153  1.00  6.49           H  
ATOM    409  HB2 LEU A  23       9.012  26.115  12.729  1.00  7.11           H  
ATOM    410  HB3 LEU A  23      10.355  26.846  13.045  1.00  7.11           H  
ATOM    411  HG  LEU A  23       9.677  27.034  15.318  1.00  8.47           H  
ATOM    412 HD11 LEU A  23       7.394  26.823  15.017  1.00 13.90           H  
ATOM    413 HD12 LEU A  23       7.578  25.326  14.588  1.00 13.90           H  
ATOM    414 HD13 LEU A  23       7.901  25.765  16.058  1.00 13.90           H  
ATOM    415 HD21 LEU A  23      11.124  25.336  14.643  1.00 12.22           H  
ATOM    416 HD22 LEU A  23      10.226  24.834  15.826  1.00 12.22           H  
ATOM    417 HD23 LEU A  23       9.903  24.395  14.356  1.00 12.22           H  
ATOM    418  N   LEU A  24       8.684  29.898  14.617  1.00  5.40           N  
ANISOU  418  N   LEU A  24      659    798    472    -38      0     56       N  
ATOM    419  CA  LEU A  24       9.245  30.914  15.512  1.00  5.42           C  
ANISOU  419  CA  LEU A  24      648    784    506    -44    -22     41       C  
ATOM    420  C   LEU A  24       9.964  30.186  16.656  1.00  5.17           C  
ANISOU  420  C   LEU A  24      675    713    461    -45      4      6       C  
ATOM    421  O   LEU A  24       9.300  29.582  17.506  1.00  6.40           O  
ANISOU  421  O   LEU A  24      672   1095    522   -120      0    184       O  
ATOM    422  CB  LEU A  24       8.145  31.821  16.049  1.00  6.35           C  
ANISOU  422  CB  LEU A  24      765    859    644     32    -84    -55       C  
ATOM    423  CG  LEU A  24       7.305  32.565  15.000  1.00  7.17           C  
ANISOU  423  CG  LEU A  24      837    859    867     92   -148     20       C  
ATOM    424  CD1 LEU A  24       6.257  33.386  15.747  1.00 11.09           C  
ANISOU  424  CD1 LEU A  24     1309   1224   1431    552   -320   -188       C  
ATOM    425  CD2 LEU A  24       8.164  33.413  14.079  1.00 10.19           C  
ANISOU  425  CD2 LEU A  24     1190   1117   1335   -149   -524    482       C  
ATOM    426  H   LEU A  24       7.849  29.701  14.680  1.00  6.48           H  
ATOM    427  HA  LEU A  24       9.895  31.455  15.017  1.00  6.51           H  
ATOM    428  HB2 LEU A  24       7.547  31.284  16.592  1.00  7.62           H  
ATOM    429  HB3 LEU A  24       8.553  32.479  16.634  1.00  7.62           H  
ATOM    430  HG  LEU A  24       6.838  31.899  14.454  1.00  8.61           H  
ATOM    431 HD11 LEU A  24       5.742  32.807  16.314  1.00 16.64           H  
ATOM    432 HD12 LEU A  24       6.695  34.051  16.283  1.00 16.64           H  
ATOM    433 HD13 LEU A  24       5.676  33.815  15.115  1.00 16.64           H  
ATOM    434 HD21 LEU A  24       8.805  32.854  13.633  1.00 15.29           H  
ATOM    435 HD22 LEU A  24       7.606  33.843  13.426  1.00 15.29           H  
ATOM    436 HD23 LEU A  24       8.625  34.079  14.594  1.00 15.29           H  
ATOM    437  N   ASP A  25      11.283  30.228  16.627  1.00  4.65           N  
ANISOU  437  N   ASP A  25      654    569    438    -26     29     71       N  
ATOM    438  CA  ASP A  25      12.097  29.299  17.428  1.00  4.67           C  
ANISOU  438  CA  ASP A  25      671    518    481     17     36     63       C  
ATOM    439  C   ASP A  25      13.077  30.042  18.331  1.00  4.37           C  
ANISOU  439  C   ASP A  25      618    489    454     75     60     84       C  
ATOM    440  O   ASP A  25      14.167  30.442  17.936  1.00  4.73           O  
ANISOU  440  O   ASP A  25      647    577    466      3     44     35       O  
ATOM    441  CB  ASP A  25      12.853  28.387  16.471  1.00  5.20           C  
ANISOU  441  CB  ASP A  25      748    606    504     15    100    -12       C  
ATOM    442  CG AASP A  25      13.452  27.163  17.133  0.49  6.36           C  
ANISOU  442  CG AASP A  25      981    602    690    122    359    113       C  
ATOM    443  CG BASP A  25      13.767  27.417  17.249  0.52  6.34           C  
ANISOU  443  CG BASP A  25     1034    493    738    120    307    215       C  
ATOM    444  OD1AASP A  25      13.680  27.331  18.358  0.49  7.13           O  
ANISOU  444  OD1AASP A  25     1324    624    601    231    118    154       O  
ATOM    445  OD1BASP A  25      13.708  27.362  18.480  0.52  5.35           O  
ANISOU  445  OD1BASP A  25      747    595    569    113    155    124       O  
ATOM    446  OD2AASP A  25      13.671  26.196  16.356  0.49  5.60           O  
ANISOU  446  OD2AASP A  25      851    527    622     79   -106    -39       O  
ATOM    447  OD2BASP A  25      14.517  26.604  16.591  0.52  5.08           O  
ANISOU  447  OD2BASP A  25      788    488    538     63     76     11       O  
ATOM    448  H   ASP A  25      11.675  30.810  16.129  1.00  5.58           H  
ATOM    449  HA  ASP A  25      11.503  28.754  17.985  1.00  5.61           H  
ATOM    450  HB2AASP A  25      12.247  28.099  15.770  1.00  6.24           H  
ATOM    451  HB3AASP A  25      13.566  28.896  16.052  1.00  6.24           H  
ATOM    452  N   THR A  26      12.676  30.207  19.613  1.00  4.48           N  
ANISOU  452  N   THR A  26      650    531    421     15     65     22       N  
ATOM    453  CA  THR A  26      13.530  30.894  20.571  1.00  4.61           C  
ANISOU  453  CA  THR A  26      707    505    435     -2     65     14       C  
ATOM    454  C   THR A  26      14.788  30.119  20.928  1.00  4.65           C  
ANISOU  454  C   THR A  26      692    576    393     38     42      6       C  
ATOM    455  O   THR A  26      15.721  30.713  21.495  1.00  5.41           O  
ANISOU  455  O   THR A  26      735    634    564     70    -73    -76       O  
ATOM    456  CB  THR A  26      12.761  31.242  21.858  1.00  4.62           C  
ANISOU  456  CB  THR A  26      741    429    482    -26     95    -38       C  
ATOM    457  OG1 THR A  26      12.294  30.039  22.486  1.00  4.77           O  
ANISOU  457  OG1 THR A  26      771    479    453    -10     50     26       O  
ATOM    458  CG2 THR A  26      11.570  32.133  21.583  1.00  5.23           C  
ANISOU  458  CG2 THR A  26      737    530    601     62    105    -19       C  
ATOM    459  H   THR A  26      11.910  29.905  19.864  1.00  5.38           H  
ATOM    460  HA  THR A  26      13.812  31.738  20.161  1.00  5.53           H  
ATOM    461  HB  THR A  26      13.367  31.705  22.473  1.00  5.55           H  
ATOM    462  HG1 THR A  26      12.931  29.548  22.644  1.00  7.15           H  
ATOM    463 HG21 THR A  26      11.867  32.943  21.162  1.00  7.84           H  
ATOM    464 HG22 THR A  26      10.956  31.678  21.002  1.00  7.84           H  
ATOM    465 HG23 THR A  26      11.131  32.345  22.410  1.00  7.84           H  
ATOM    466  N   GLY A  27      14.823  28.814  20.635  1.00  4.75           N  
ANISOU  466  N   GLY A  27      711    539    448     65     35     29       N  
ATOM    467  CA  GLY A  27      15.995  28.013  20.873  1.00  5.05           C  
ANISOU  467  CA  GLY A  27      810    539    453     94    -14     27       C  
ATOM    468  C   GLY A  27      17.053  28.092  19.798  1.00  5.21           C  
ANISOU  468  C   GLY A  27      808    606    447    191    -42    -45       C  
ATOM    469  O   GLY A  27      18.126  27.510  19.956  1.00  8.84           O  
ANISOU  469  O   GLY A  27     1142   1540    477    806     27     96       O  
ATOM    470  H   GLY A  27      14.126  28.444  20.294  1.00  5.70           H  
ATOM    471  HA2 GLY A  27      16.390  28.289  21.715  1.00  6.06           H  
ATOM    472  HA3 GLY A  27      15.721  27.088  20.969  1.00  6.06           H  
ATOM    473  N   ALA A  28      16.767  28.774  18.702  1.00  4.37           N  
ANISOU  473  N   ALA A  28      600    481    480     34      5     17       N  
ATOM    474  CA  ALA A  28      17.678  28.864  17.566  1.00  4.52           C  
ANISOU  474  CA  ALA A  28      625    480    511     59    -12    -17       C  
ATOM    475  C   ALA A  28      18.386  30.205  17.592  1.00  4.30           C  
ANISOU  475  C   ALA A  28      671    472    394     60     34     -6       C  
ATOM    476  O   ALA A  28      17.757  31.263  17.588  1.00  4.74           O  
ANISOU  476  O   ALA A  28      651    493    550     60     29     52       O  
ATOM    477  CB  ALA A  28      16.932  28.701  16.260  1.00  5.48           C  
ANISOU  477  CB  ALA A  28      768    663    527     -5    -19   -122       C  
ATOM    478  H   ALA A  28      16.011  29.182  18.656  1.00  5.24           H  
ATOM    479  HA  ALA A  28      18.347  28.152  17.640  1.00  5.42           H  
ATOM    480  HB1 ALA A  28      17.550  28.764  15.528  1.00  8.22           H  
ATOM    481  HB2 ALA A  28      16.501  27.843  16.242  1.00  8.22           H  
ATOM    482  HB3 ALA A  28      16.271  29.393  16.180  1.00  8.22           H  
ATOM    483  N   ASP A  29      19.731  30.176  17.556  1.00  4.67           N  
ANISOU  483  N   ASP A  29      604    580    485     60    -25      6       N  
ATOM    484  CA  ASP A  29      20.470  31.424  17.527  1.00  5.18           C  
ANISOU  484  CA  ASP A  29      671    689    492    -41    -25    101       C  
ATOM    485  C   ASP A  29      20.230  32.179  16.213  1.00  5.95           C  
ANISOU  485  C   ASP A  29      636    912    579    -36    -13    242       C  
ATOM    486  O   ASP A  29      20.220  33.416  16.194  1.00  7.43           O  
ANISOU  486  O   ASP A  29      982    940    733    -59    -60    326       O  
ATOM    487  CB  ASP A  29      21.972  31.140  17.653  1.00  6.36           C  
ANISOU  487  CB  ASP A  29      655    992    624    -18    -10    173       C  
ATOM    488  CG  ASP A  29      22.425  30.554  18.969  1.00  5.95           C  
ANISOU  488  CG  ASP A  29      718    794    613    -32    -89     37       C  
ATOM    489  OD1 ASP A  29      21.722  30.675  19.995  1.00  6.18           O  
ANISOU  489  OD1 ASP A  29      804    819    583     33    -68     58       O  
ATOM    490  OD2 ASP A  29      23.550  29.975  18.949  1.00  7.99           O  
ANISOU  490  OD2 ASP A  29      836   1236    784    257    -31    116       O  
ATOM    491  H   ASP A  29      20.148  29.424  17.551  1.00  5.61           H  
ATOM    492  HA  ASP A  29      20.185  31.986  18.277  1.00  6.22           H  
ATOM    493  HB2 ASP A  29      22.227  30.529  16.944  1.00  7.63           H  
ATOM    494  HB3 ASP A  29      22.453  31.970  17.507  1.00  7.63           H  
ATOM    495  N  AASP A  30      20.146  31.361  15.142  0.58  6.80           N  
ANISOU  495  N  AASP A  30      734   1279    418    -48     13    183       N  
ATOM    496  N  BASP A  30      20.090  31.472  15.116  0.42  6.40           N  
ANISOU  496  N  BASP A  30      660   1079    548    -21    -78    257       N  
ATOM    497  CA AASP A  30      20.163  31.703  13.724  0.58  6.39           C  
ANISOU  497  CA AASP A  30      840    909    532    -15    -38    225       C  
ATOM    498  CA BASP A  30      20.048  32.187  13.832  0.42  5.39           C  
ANISOU  498  CA BASP A  30      580    842    503    -51    -57    208       C  
ATOM    499  C  AASP A  30      18.829  31.367  13.040  0.58  4.97           C  
ANISOU  499  C  AASP A  30      763    545    466     37     52     72       C  
ATOM    500  C  BASP A  30      18.895  31.527  13.068  0.42  4.40           C  
ANISOU  500  C  BASP A  30      602    532    440     79     80     38       C  
ATOM    501  O  AASP A  30      17.984  30.698  13.608  0.58  5.32           O  
ANISOU  501  O  AASP A  30      709    747    445     67    107    185       O  
ATOM    502  O  BASP A  30      18.136  30.698  13.585  0.42  5.40           O  
ANISOU  502  O  BASP A  30      611    653    666      4     33    119       O  
ATOM    503  CB AASP A  30      21.302  31.001  12.958  0.58  6.29           C  
ANISOU  503  CB AASP A  30      864    730    655     64    123    207       C  
ATOM    504  CB BASP A  30      21.433  32.031  13.177  0.42  5.24           C  
ANISOU  504  CB BASP A  30      641    624    608    -51     72    139       C  
ATOM    505  CG AASP A  30      22.644  31.227  13.530  0.58  8.55           C  
ANISOU  505  CG AASP A  30     1075   1231    750    212    -56    111       C  
ATOM    506  CG BASP A  30      22.339  33.237  13.451  0.42  6.04           C  
ANISOU  506  CG BASP A  30      622    609    927    -43     64     54       C  
ATOM    507  OD1AASP A  30      22.914  32.276  14.105  0.58 10.54           O  
ANISOU  507  OD1AASP A  30     1049   1454   1264   -217    -29    -63       O  
ATOM    508  OD1BASP A  30      21.954  34.380  13.106  0.42  6.25           O  
ANISOU  508  OD1BASP A  30      810    638    784   -162     34    137       O  
ATOM    509  OD2AASP A  30      23.511  30.327  13.317  0.58 11.92           O  
ANISOU  509  OD2AASP A  30     1124   2001   1133    632   -195   -126       O  
ATOM    510  OD2BASP A  30      23.452  33.013  14.022  0.42 13.70           O  
ANISOU  510  OD2BASP A  30     1041    787   3066   -214   -803    435       O  
ATOM    511  H  AASP A  30      20.074  30.523  15.321  0.58  8.16           H  
ATOM    512  HA AASP A  30      20.303  32.670  13.650  0.58  7.66           H  
ATOM    513  HB2AASP A  30      21.127  30.047  12.944  0.58  7.55           H  
ATOM    514  HB3AASP A  30      21.299  31.314  12.040  0.58  7.55           H  
ATOM    515  N   THR A  31      18.734  31.875  11.796  1.00  5.06           N  
ANISOU  515  N   THR A  31      767    616    426    -85     13     53       N  
ATOM    516  CA  THR A  31      17.593  31.586  10.955  1.00  4.76           C  
ANISOU  516  CA  THR A  31      709    582    410    -61     42      7       C  
ATOM    517  C   THR A  31      18.061  30.690   9.821  1.00  4.75           C  
ANISOU  517  C   THR A  31      729    543    427    -27     18     54       C  
ATOM    518  O   THR A  31      19.049  31.031   9.140  1.00  5.61           O  
ANISOU  518  O   THR A  31      762    685    556    -61    148    -26       O  
ATOM    519  CB  THR A  31      17.012  32.913  10.424  1.00  5.03           C  
ANISOU  519  CB  THR A  31      765    586    448    -25     94     -4       C  
ATOM    520  OG1 THR A  31      16.417  33.603  11.537  1.00  5.27           O  
ANISOU  520  OG1 THR A  31      791    600    490      4     59     -9       O  
ATOM    521  CG2 THR A  31      15.984  32.719   9.354  1.00  5.45           C  
ANISOU  521  CG2 THR A  31      801    664    484     23     23     41       C  
ATOM    522  H  ATHR A  31      19.362  32.380  11.497  1.00  6.07           H  
ATOM    523  HA  THR A  31      16.911  31.118  11.480  1.00  5.71           H  
ATOM    524  HB  THR A  31      17.743  33.460  10.066  1.00  6.04           H  
ATOM    525  HG1 THR A  31      16.980  33.715  12.122  1.00  7.90           H  
ATOM    526 HG21 THR A  31      16.379  32.259   8.610  1.00  8.18           H  
ATOM    527 HG22 THR A  31      15.255  32.200   9.701  1.00  8.18           H  
ATOM    528 HG23 THR A  31      15.658  33.575   9.065  1.00  8.18           H  
ATOM    529  N   VAL A  32      17.395  29.555   9.620  1.00  4.61           N  
ANISOU  529  N   VAL A  32      663    588    397    -18     66      3       N  
ATOM    530  CA  VAL A  32      17.807  28.616   8.575  1.00  4.71           C  
ANISOU  530  CA  VAL A  32      689    612    382    -30     45    -27       C  
ATOM    531  C   VAL A  32      16.586  28.171   7.782  1.00  4.60           C  
ANISOU  531  C   VAL A  32      680    577    388     25     42     -5       C  
ATOM    532  O   VAL A  32      15.553  27.780   8.354  1.00  5.22           O  
ANISOU  532  O   VAL A  32      678    757    431    -38     34      9       O  
ATOM    533  CB  VAL A  32      18.616  27.437   9.132  1.00  4.99           C  
ANISOU  533  CB  VAL A  32      641    616    526     -8    -25    -37       C  
ATOM    534  CG1 VAL A  32      17.878  26.588  10.139  1.00  5.63           C  
ANISOU  534  CG1 VAL A  32      782    707    521     10      4     79       C  
ATOM    535  CG2 VAL A  32      19.168  26.578   7.983  1.00  5.49           C  
ANISOU  535  CG2 VAL A  32      711    644    605     37     34    -61       C  
ATOM    536  H   VAL A  32      16.714  29.371  10.111  1.00  5.53           H  
ATOM    537  HA  VAL A  32      18.391  29.104   7.959  1.00  5.65           H  
ATOM    538  HB  VAL A  32      19.390  27.819   9.597  1.00  5.99           H  
ATOM    539 HG11 VAL A  32      18.449  25.876  10.438  1.00  8.44           H  
ATOM    540 HG12 VAL A  32      17.623  27.130  10.889  1.00  8.44           H  
ATOM    541 HG13 VAL A  32      17.092  26.217   9.730  1.00  8.44           H  
ATOM    542 HG21 VAL A  32      19.632  27.139   7.358  1.00  8.23           H  
ATOM    543 HG22 VAL A  32      19.774  25.922   8.336  1.00  8.23           H  
ATOM    544 HG23 VAL A  32      18.442  26.135   7.538  1.00  8.23           H  
ATOM    545  N   ILE A  33      16.723  28.262   6.466  1.00  4.95           N  
ANISOU  545  N   ILE A  33      669    731    368    -10     31    -35       N  
ATOM    546  CA  ILE A  33      15.659  28.003   5.507  1.00  5.26           C  
ANISOU  546  CA  ILE A  33      705    763    412     24    -11    -34       C  
ATOM    547  C   ILE A  33      16.115  26.869   4.593  1.00  5.26           C  
ANISOU  547  C   ILE A  33      749    768    363     28    -18     27       C  
ATOM    548  O   ILE A  33      17.299  26.747   4.274  1.00  5.84           O  
ANISOU  548  O   ILE A  33      791    834    463     73     21    -38       O  
ATOM    549  CB  ILE A  33      15.336  29.286   4.689  1.00  6.38           C  
ANISOU  549  CB  ILE A  33      925    843    510    146     -7     44       C  
ATOM    550  CG1 ILE A  33      15.056  30.489   5.604  1.00  7.15           C  
ANISOU  550  CG1 ILE A  33     1061    785    710    117    -58     26       C  
ATOM    551  CG2 ILE A  33      14.220  29.064   3.705  1.00  7.58           C  
ANISOU  551  CG2 ILE A  33     1138   1000    572    268   -153     26       C  
ATOM    552  CD1 ILE A  33      13.853  30.341   6.504  1.00  7.80           C  
ANISOU  552  CD1 ILE A  33     1126    984    677    195     16    -70       C  
ATOM    553  H   ILE A  33      17.493  28.491   6.158  1.00  5.94           H  
ATOM    554  HA  ILE A  33      14.855  27.720   5.990  1.00  6.31           H  
ATOM    555  HB  ILE A  33      16.137  29.503   4.168  1.00  7.65           H  
ATOM    556 HG12 ILE A  33      15.838  30.643   6.157  1.00  8.58           H  
ATOM    557 HG13 ILE A  33      14.931  31.275   5.049  1.00  8.58           H  
ATOM    558 HG21 ILE A  33      14.427  28.308   3.151  1.00 11.37           H  
ATOM    559 HG22 ILE A  33      13.403  28.899   4.180  1.00 11.37           H  
ATOM    560 HG23 ILE A  33      14.118  29.845   3.155  1.00 11.37           H  
ATOM    561 HD11 ILE A  33      13.753  31.133   7.037  1.00 11.70           H  
ATOM    562 HD12 ILE A  33      13.066  30.215   5.968  1.00 11.70           H  
ATOM    563 HD13 ILE A  33      13.974  29.582   7.078  1.00 11.70           H  
ATOM    564  N   GLU A  34      15.140  26.051   4.176  1.00  5.55           N  
ANISOU  564  N   GLU A  34      761    844    377     27    -45    -43       N  
ATOM    565  CA  GLU A  34      15.363  25.002   3.187  1.00  6.03           C  
ANISOU  565  CA  GLU A  34      916    803    437     39    -36    -61       C  
ATOM    566  C   GLU A  34      15.916  25.606   1.896  1.00  6.11           C  
ANISOU  566  C   GLU A  34      894    871    417     30    -26   -104       C  
ATOM    567  O   GLU A  34      15.852  26.787   1.621  1.00  6.89           O  
ANISOU  567  O   GLU A  34     1172    840    451    122     27    -31       O  
ATOM    568  CB  GLU A  34      14.036  24.294   2.921  1.00  7.03           C  
ANISOU  568  CB  GLU A  34      972    929    610    -30    -64   -172       C  
ATOM    569  CG  GLU A  34      13.012  25.164   2.237  1.00  7.47           C  
ANISOU  569  CG  GLU A  34      955   1167    546     52   -121   -233       C  
ATOM    570  CD  GLU A  34      11.587  24.752   2.390  1.00 10.21           C  
ANISOU  570  CD  GLU A  34     1138   1363   1146    -83   -185   -243       C  
ATOM    571  OE1 GLU A  34      11.331  23.605   2.815  1.00 19.07           O  
ANISOU  571  OE1 GLU A  34     1302   1408   4103   -325   -501    384       O  
ATOM    572  OE2 GLU A  34      10.678  25.581   2.138  1.00  9.75           O  
ANISOU  572  OE2 GLU A  34     1022   1729    733    112   -151   -262       O  
ATOM    573  H   GLU A  34      14.351  26.148   4.504  1.00  6.66           H  
ATOM    574  HA  GLU A  34      16.008  24.355   3.543  1.00  7.24           H  
ATOM    575  HB2 GLU A  34      14.202  23.514   2.369  1.00  8.43           H  
ATOM    576  HB3 GLU A  34      13.670  23.986   3.765  1.00  8.43           H  
ATOM    577  HG2 GLU A  34      13.105  26.067   2.579  1.00  8.96           H  
ATOM    578  HG3 GLU A  34      13.221  25.190   1.290  1.00  8.96           H  
ATOM    579  N   GLU A  35      16.448  24.700   1.034  1.00  6.83           N  
ANISOU  579  N   GLU A  35     1129    881    429    139      4    -93       N  
ATOM    580  CA  GLU A  35      17.167  25.166  -0.132  1.00  6.91           C  
ANISOU  580  CA  GLU A  35     1170    923    376    116      6    -90       C  
ATOM    581  C   GLU A  35      16.325  26.104  -0.976  1.00  7.07           C  
ANISOU  581  C   GLU A  35     1146    951    429    121    -39   -119       C  
ATOM    582  O   GLU A  35      15.176  25.844  -1.353  1.00  7.62           O  
ANISOU  582  O   GLU A  35     1121   1073    529      9    -78    -99       O  
ATOM    583  CB  GLU A  35      17.622  23.975  -0.984  1.00  7.37           C  
ANISOU  583  CB  GLU A  35     1192    980    463    147     -7   -150       C  
ATOM    584  CG  GLU A  35      18.825  23.285  -0.399  1.00  7.89           C  
ANISOU  584  CG  GLU A  35     1206    996    618    165     13    -99       C  
ATOM    585  CD  GLU A  35      20.108  24.092  -0.408  1.00  8.31           C  
ANISOU  585  CD  GLU A  35     1180   1115    673    175     71    -90       C  
ATOM    586  OE1 GLU A  35      20.148  25.132  -1.080  1.00 10.17           O  
ANISOU  586  OE1 GLU A  35     1439   1327    868    -63     49     57       O  
ATOM    587  OE2 GLU A  35      21.077  23.638   0.280  1.00 10.39           O  
ANISOU  587  OE2 GLU A  35     1216   1501    995    119   -130     21       O  
ATOM    588  H   GLU A  35      16.357  23.857   1.180  1.00  8.19           H  
ATOM    589  HA  GLU A  35      17.962  25.652   0.170  1.00  8.29           H  
ATOM    590  HB2 GLU A  35      16.894  23.339  -1.058  1.00  8.85           H  
ATOM    591  HB3 GLU A  35      17.837  24.287  -1.877  1.00  8.85           H  
ATOM    592  HG2 GLU A  35      18.622  23.042   0.518  1.00  9.47           H  
ATOM    593  HG3 GLU A  35      18.976  22.463  -0.891  1.00  9.47           H  
ATOM    594  N   MET A  36      16.951  27.221  -1.327  1.00  7.36           N  
ANISOU  594  N   MET A  36     1129   1028    473     98    -45     18       N  
ATOM    595  CA  MET A  36      16.390  28.305  -2.122  1.00  7.87           C  
ANISOU  595  CA  MET A  36     1192   1102    519     57   -112    111       C  
ATOM    596  C   MET A  36      17.556  29.159  -2.586  1.00  8.42           C  
ANISOU  596  C   MET A  36     1270   1250    488     -2    -94    108       C  
ATOM    597  O   MET A  36      18.643  29.099  -2.007  1.00  9.08           O  
ANISOU  597  O   MET A  36     1260   1371    613    -88   -118    145       O  
ATOM    598  CB  MET A  36      15.355  29.131  -1.349  1.00  8.62           C  
ANISOU  598  CB  MET A  36     1176   1063    842    177    -32    102       C  
ATOM    599  CG  MET A  36      15.976  29.959  -0.238  1.00  9.21           C  
ANISOU  599  CG  MET A  36     1336   1197    757    129     59     62       C  
ATOM    600  SD  MET A  36      14.751  31.044   0.559  1.00 10.92           S  
ANISOU  600  SD  MET A  36     1731   1169   1004    222    331    122       S  
ATOM    601  CE  MET A  36      14.325  32.100  -0.828  1.00 12.44           C  
ANISOU  601  CE  MET A  36     1803   1276   1365    332    457    340       C  
ATOM    602  H   MET A  36      17.763  27.313  -1.060  1.00  8.83           H  
ATOM    603  HA  MET A  36      15.954  27.919  -2.910  1.00  9.44           H  
ATOM    604  HB2 MET A  36      14.897  29.722  -1.966  1.00 10.34           H  
ATOM    605  HB3 MET A  36      14.695  28.532  -0.966  1.00 10.34           H  
ATOM    606  HG2 MET A  36      16.359  29.366   0.427  1.00 11.05           H  
ATOM    607  HG3 MET A  36      16.692  30.500  -0.604  1.00 11.05           H  
ATOM    608  HE1 MET A  36      13.668  32.743  -0.551  1.00 18.65           H  
ATOM    609  HE2 MET A  36      15.111  32.557  -1.135  1.00 18.65           H  
ATOM    610  HE3 MET A  36      13.967  31.564  -1.540  1.00 18.65           H  
ATOM    611  N   SER A  37      17.307  29.976  -3.614  1.00  9.61           N  
ANISOU  611  N   SER A  37     1322   1357    755    -98   -144    325       N  
ATOM    612  CA ASER A  37      18.251  30.981  -4.059  0.71  9.80           C  
ANISOU  612  CA ASER A  37     1322   1593    585   -228     26    183       C  
ATOM    613  CA BSER A  37      18.338  30.943  -4.005  0.29  9.94           C  
ANISOU  613  CA BSER A  37     1559   1366    628   -161   -202    281       C  
ATOM    614  C   SER A  37      18.111  32.267  -3.280  1.00  9.50           C  
ANISOU  614  C   SER A  37     1335   1365    693     41    -16    254       C  
ATOM    615  O   SER A  37      16.989  32.697  -2.982  1.00 12.11           O  
ANISOU  615  O   SER A  37     1350   1686   1292     78     24    407       O  
ATOM    616  CB ASER A  37      17.955  31.405  -5.513  0.71 11.46           C  
ANISOU  616  CB ASER A  37     1697   1752    646   -258      4    257       C  
ATOM    617  CB BSER A  37      18.313  30.979  -5.539  0.29 12.53           C  
ANISOU  617  CB BSER A  37     2978    908    591   -404   -295    331       C  
ATOM    618  OG ASER A  37      18.106  30.259  -6.253  0.71 13.60           O  
ANISOU  618  OG ASER A  37     2128   2151    580   -822    117   -223       O  
ATOM    619  OG BSER A  37      19.372  31.735  -6.058  0.29 26.02           O  
ANISOU  619  OG BSER A  37     5416   2719   1162  -2159    937   -165       O  
ATOM    620  H  ASER A  37      16.557  29.903  -4.028  1.00 11.53           H  
ATOM    621  HA ASER A  37      19.166  30.640  -3.987  0.71 11.75           H  
ATOM    622  HA BSER A  37      19.208  30.589  -3.725  0.29 11.93           H  
ATOM    623  HB2ASER A  37      17.051  31.749  -5.594  0.71 13.75           H  
ATOM    624  HB2BSER A  37      18.368  30.073  -5.881  0.29 15.04           H  
ATOM    625  HB3ASER A  37      18.578  32.088  -5.806  0.71 13.75           H  
ATOM    626  HB3BSER A  37      17.472  31.360  -5.836  0.29 15.04           H  
ATOM    627  HG ASER A  37      18.867  29.970  -6.157  0.71 20.40           H  
ATOM    628  HG BSER A  37      19.295  31.790  -6.872  0.29 39.03           H  
ATOM    629  N   LEU A  38      19.236  32.919  -2.968  1.00  9.25           N  
ANISOU  629  N   LEU A  38     1300   1254    752     29      6    199       N  
ATOM    630  CA  LEU A  38      19.252  34.256  -2.401  1.00 10.05           C  
ANISOU  630  CA  LEU A  38     1465   1045   1081    119    182    314       C  
ATOM    631  C   LEU A  38      20.358  35.075  -3.084  1.00 11.86           C  
ANISOU  631  C   LEU A  38     1647   1304   1285     39    171    558       C  
ATOM    632  O   LEU A  38      21.304  34.478  -3.575  1.00 11.62           O  
ANISOU  632  O   LEU A  38     1591   1473   1088    -35    251    362       O  
ATOM    633  CB  LEU A  38      19.525  34.245  -0.908  1.00  9.06           C  
ANISOU  633  CB  LEU A  38     1347    913    978    -43     62     77       C  
ATOM    634  CG  LEU A  38      18.372  33.734  -0.037  1.00  9.12           C  
ANISOU  634  CG  LEU A  38     1298    899   1060     20    150     46       C  
ATOM    635  CD1 LEU A  38      18.809  33.616   1.409  1.00  9.58           C  
ANISOU  635  CD1 LEU A  38     1457   1089    879    -56    212    -81       C  
ATOM    636  CD2 LEU A  38      17.150  34.637  -0.136  1.00 11.50           C  
ANISOU  636  CD2 LEU A  38     1376   1271   1462    221    162     74       C  
ATOM    637  H   LEU A  38      19.988  32.527  -3.111  1.00 11.10           H  
ATOM    638  HA  LEU A  38      18.386  34.686  -2.566  1.00 12.06           H  
ATOM    639  HB2 LEU A  38      20.304  33.690  -0.742  1.00 10.88           H  
ATOM    640  HB3 LEU A  38      19.745  35.147  -0.628  1.00 10.88           H  
ATOM    641  HG  LEU A  38      18.120  32.842  -0.355  1.00 10.94           H  
ATOM    642 HD11 LEU A  38      19.580  33.046   1.464  1.00 14.38           H  
ATOM    643 HD12 LEU A  38      19.029  34.486   1.749  1.00 14.38           H  
ATOM    644 HD13 LEU A  38      18.095  33.240   1.929  1.00 14.38           H  
ATOM    645 HD21 LEU A  38      16.878  34.708  -1.054  1.00 17.25           H  
ATOM    646 HD22 LEU A  38      16.433  34.263   0.382  1.00 17.25           H  
ATOM    647 HD23 LEU A  38      17.367  35.508   0.202  1.00 17.25           H  
ATOM    648  N   PRO A  39      20.189  36.387  -3.123  1.00 15.53           N  
ANISOU  648  N   PRO A  39     1867   1467   2216    178    631    926       N  
ATOM    649  CA  PRO A  39      21.193  37.227  -3.783  1.00 19.26           C  
ANISOU  649  CA  PRO A  39     2128   1557   3197     96    602   1375       C  
ATOM    650  C   PRO A  39      22.423  37.454  -2.905  1.00 17.81           C  
ANISOU  650  C   PRO A  39     2202   1239   2921   -164    770    974       C  
ATOM    651  O   PRO A  39      22.307  37.406  -1.701  1.00 18.31           O  
ANISOU  651  O   PRO A  39     2531   1173   2838   -282    972    416       O  
ATOM    652  CB  PRO A  39      20.368  38.509  -4.069  1.00 28.70           C  
ANISOU  652  CB  PRO A  39     2544   2205   5506    535   1051   2477       C  
ATOM    653  CG  PRO A  39      19.372  38.582  -2.946  1.00 33.83           C  
ANISOU  653  CG  PRO A  39     2961   1603   7524    597   2344   2100       C  
ATOM    654  CD  PRO A  39      18.979  37.151  -2.656  1.00 22.20           C  
ANISOU  654  CD  PRO A  39     2646   1326   3960    630   1307   1179       C  
ATOM    655  HA  PRO A  39      21.464  36.813  -4.630  1.00 23.11           H  
ATOM    656  HB2 PRO A  39      20.940  39.292  -4.073  1.00 34.44           H  
ATOM    657  HB3 PRO A  39      19.917  38.445  -4.925  1.00 34.44           H  
ATOM    658  HG2 PRO A  39      19.771  38.993  -2.162  1.00 40.60           H  
ATOM    659  HG3 PRO A  39      18.597  39.103  -3.210  1.00 40.60           H  
ATOM    660  HD2 PRO A  39      18.819  37.013  -1.710  1.00 26.64           H  
ATOM    661  HD3 PRO A  39      18.187  36.895  -3.154  1.00 26.64           H  
ATOM    662  N   GLY A  40      23.490  37.821  -3.589  1.00 18.66           N  
ANISOU  662  N   GLY A  40     2201   1607   2860     69    824   1121       N  
ATOM    663  CA  GLY A  40      24.701  38.296  -2.908  1.00 20.44           C  
ANISOU  663  CA  GLY A  40     2074   1610   3619    -74    861   1331       C  
ATOM    664  C   GLY A  40      25.662  37.191  -2.597  1.00 15.74           C  
ANISOU  664  C   GLY A  40     2033   1425   2167   -116    845    918       C  
ATOM    665  O   GLY A  40      25.524  36.007  -3.005  1.00 16.89           O  
ANISOU  665  O   GLY A  40     1837   1678   2522    -73    548    645       O  
ATOM    666  H   GLY A  40      23.476  37.782  -4.448  1.00 22.39           H  
ATOM    667  HA2 GLY A  40      25.143  38.952  -3.469  1.00 24.53           H  
ATOM    668  HA3 GLY A  40      24.447  38.736  -2.082  1.00 24.53           H  
ATOM    669  N   ARG A  41      26.704  37.567  -1.916  1.00 18.20           N  
ANISOU  669  N   ARG A  41     2497   1684   2321   -414    442   1031       N  
ATOM    670  CA  ARG A  41      27.739  36.663  -1.529  1.00 16.62           C  
ANISOU  670  CA  ARG A  41     2452   1552   1936   -340    389    807       C  
ATOM    671  C   ARG A  41      27.254  35.782  -0.390  1.00 14.19           C  
ANISOU  671  C   ARG A  41     2026   1325   1720    -93    718    592       C  
ATOM    672  O   ARG A  41      26.394  36.114   0.387  1.00 16.39           O  
ANISOU  672  O   ARG A  41     2410   1344   2102    197    871    672       O  
ATOM    673  CB  ARG A  41      29.019  37.437  -1.139  1.00 23.95           C  
ANISOU  673  CB  ARG A  41     2479   2287   3791   -794     18   1577       C  
ATOM    674  CG  ARG A  41      29.659  38.186  -2.282  1.00 36.34           C  
ANISOU  674  CG  ARG A  41     3050   4149   5786  -1097     70   3391       C  
ATOM    675  CD  ARG A  41      30.824  39.071  -1.903  1.00 56.10           C  
ANISOU  675  CD  ARG A  41     5048   5032   9965  -3110    309   3240       C  
ATOM    676  NE  ARG A  41      31.688  39.558  -2.981  1.00 70.94           N  
ANISOU  676  NE  ARG A  41     5902   7445  12001  -3480   1363   4508       N  
ATOM    677  CZ  ARG A  41      31.603  40.671  -3.695  1.00 73.21           C  
ANISOU  677  CZ  ARG A  41     6453   8243  11463  -2833   1904   4931       C  
ATOM    678  NH1 ARG A  41      30.593  41.506  -3.448  1.00 90.15           N  
ANISOU  678  NH1 ARG A  41    11072   8640  12501   -266   2976   3967       N  
ATOM    679  NH2 ARG A  41      32.425  41.064  -4.666  1.00 85.49           N  
ANISOU  679  NH2 ARG A  41     7353  12057  11138  -3735   1552   6018       N  
ATOM    680  H   ARG A  41      26.772  38.393  -1.690  1.00 21.84           H  
ATOM    681  HA  ARG A  41      27.949  36.088  -2.294  1.00 19.95           H  
ATOM    682  HB2 ARG A  41      28.799  38.070  -0.437  1.00 28.74           H  
ATOM    683  HB3 ARG A  41      29.664  36.810  -0.777  1.00 28.74           H  
ATOM    684  HG2 ARG A  41      29.964  37.541  -2.939  1.00 43.61           H  
ATOM    685  HG3 ARG A  41      28.982  38.736  -2.707  1.00 43.61           H  
ATOM    686  HD2 ARG A  41      30.472  39.842  -1.432  1.00 67.32           H  
ATOM    687  HD3 ARG A  41      31.379  38.580  -1.276  1.00 67.32           H  
ATOM    688  HE  ARG A  41      32.349  39.045  -3.180  1.00 85.13           H  
ATOM    689 HH11 ARG A  41      30.017  41.316  -2.838  1.00108.18           H  
ATOM    690 HH12 ARG A  41      30.517  42.234  -3.899  1.00108.18           H  
ATOM    691 HH21 ARG A  41      33.097  40.573  -4.886  1.00102.59           H  
ATOM    692 HH22 ARG A  41      32.285  41.808  -5.073  1.00102.59           H  
ATOM    693  N   TRP A  42      27.943  34.611  -0.284  1.00 13.92           N  
ANISOU  693  N   TRP A  42     1907   1441   1625     38    836    603       N  
ATOM    694  CA  TRP A  42      27.689  33.730   0.833  1.00 11.41           C  
ANISOU  694  CA  TRP A  42     1484   1228   1367      6    597    441       C  
ATOM    695  C   TRP A  42      29.000  33.076   1.257  1.00 12.33           C  
ANISOU  695  C   TRP A  42     1351   1264   1792    -53    721    466       C  
ATOM    696  O   TRP A  42      29.990  33.050   0.528  1.00 14.19           O  
ANISOU  696  O   TRP A  42     1371   1710   1988    -45    848    432       O  
ATOM    697  CB  TRP A  42      26.621  32.672   0.488  1.00 11.86           C  
ANISOU  697  CB  TRP A  42     1440   1434   1363     42    521    336       C  
ATOM    698  CG  TRP A  42      27.020  31.789  -0.658  1.00 13.27           C  
ANISOU  698  CG  TRP A  42     1659   1672   1413    -40    533    234       C  
ATOM    699  CD1 TRP A  42      26.785  32.017  -1.957  1.00 16.63           C  
ANISOU  699  CD1 TRP A  42     2650   1847   1444    -53    475    133       C  
ATOM    700  CD2 TRP A  42      27.735  30.560  -0.623  1.00 13.40           C  
ANISOU  700  CD2 TRP A  42     1484   1686   1618   -129    466    -43       C  
ATOM    701  NE1 TRP A  42      27.305  31.048  -2.732  1.00 19.05           N  
ANISOU  701  NE1 TRP A  42     2722   2599   1486    234    670    -67       N  
ATOM    702  CE2 TRP A  42      27.894  30.089  -1.932  1.00 16.78           C  
ANISOU  702  CE2 TRP A  42     2114   2029   1854    -47    774   -100       C  
ATOM    703  CE3 TRP A  42      28.239  29.800   0.425  1.00 14.36           C  
ANISOU  703  CE3 TRP A  42     1696   1451   1985    -12    403    165       C  
ATOM    704  CZ2 TRP A  42      28.547  28.882  -2.222  1.00 19.89           C  
ANISOU  704  CZ2 TRP A  42     2315   2633   2160    382    521   -539       C  
ATOM    705  CZ3 TRP A  42      28.891  28.591   0.162  1.00 16.51           C  
ANISOU  705  CZ3 TRP A  42     1925   1646   2327    127    347   -115       C  
ATOM    706  CH2 TRP A  42      29.019  28.173  -1.158  1.00 18.88           C  
ANISOU  706  CH2 TRP A  42     2384   1901   2462     85    473   -355       C  
ATOM    707  H   TRP A  42      28.526  34.398  -0.879  1.00 16.70           H  
ATOM    708  HA  TRP A  42      27.358  34.270   1.581  1.00 13.70           H  
ATOM    709  HB2 TRP A  42      26.459  32.121   1.270  1.00 14.23           H  
ATOM    710  HB3 TRP A  42      25.790  33.122   0.267  1.00 14.23           H  
ATOM    711  HD1 TRP A  42      26.320  32.753  -2.283  1.00 19.95           H  
ATOM    712  HE1 TRP A  42      27.276  31.030  -3.591  1.00 22.86           H  
ATOM    713  HE3 TRP A  42      28.141  30.094   1.301  1.00 17.23           H  
ATOM    714  HZ2 TRP A  42      28.653  28.581  -3.096  1.00 23.87           H  
ATOM    715  HZ3 TRP A  42      29.234  28.077   0.857  1.00 19.81           H  
ATOM    716  HH2 TRP A  42      29.450  27.366  -1.323  1.00 22.66           H  
ATOM    717  N   LYS A  43      28.978  32.519   2.469  1.00 12.10           N  
ANISOU  717  N   LYS A  43     1224   1223   1878    113    710    583       N  
ATOM    718  CA  LYS A  43      30.108  31.728   2.948  1.00 13.17           C  
ANISOU  718  CA  LYS A  43     1023   1329   2353    -29    545    643       C  
ATOM    719  C   LYS A  43      29.543  30.489   3.656  1.00  9.87           C  
ANISOU  719  C   LYS A  43      828   1130   1568     12    390    277       C  
ATOM    720  O   LYS A  43      28.454  30.515   4.212  1.00  9.95           O  
ANISOU  720  O   LYS A  43      806   1075   1672     49    451    340       O  
ATOM    721  CB  LYS A  43      31.021  32.515   3.785  1.00 16.15           C  
ANISOU  721  CB  LYS A  43     1350   1424   2998   -263    450    422       C  
ATOM    722  CG  LYS A  43      30.375  33.038   5.001  1.00 15.02           C  
ANISOU  722  CG  LYS A  43     1296   1473   2600   -246    276    543       C  
ATOM    723  CD  LYS A  43      31.301  34.015   5.759  1.00 22.91           C  
ANISOU  723  CD  LYS A  43     1725   2638   3823   -622    269   -344       C  
ATOM    724  CE  LYS A  43      30.522  34.773   6.834  1.00 22.13           C  
ANISOU  724  CE  LYS A  43     2638   2325   2945   -777     58   -165       C  
ATOM    725  NZ  LYS A  43      31.415  35.728   7.582  1.00 38.49           N  
ANISOU  725  NZ  LYS A  43     4635   3662   5456  -2312    182  -1405       N  
ATOM    726  H   LYS A  43      28.291  32.627   2.974  1.00 14.52           H  
ATOM    727  HA  LYS A  43      30.611  31.421   2.164  1.00 15.80           H  
ATOM    728  HB2 LYS A  43      31.773  31.958   4.042  1.00 19.38           H  
ATOM    729  HB3 LYS A  43      31.366  33.258   3.266  1.00 19.38           H  
ATOM    730  HG2 LYS A  43      29.555  33.496   4.757  1.00 18.03           H  
ATOM    731  HG3 LYS A  43      30.142  32.299   5.585  1.00 18.03           H  
ATOM    732  HD2 LYS A  43      32.025  33.520   6.173  1.00 27.49           H  
ATOM    733  HD3 LYS A  43      31.687  34.647   5.133  1.00 27.49           H  
ATOM    734  HE2 LYS A  43      29.797  35.267   6.420  1.00 26.56           H  
ATOM    735  HE3 LYS A  43      30.134  34.139   7.458  1.00 26.56           H  
ATOM    736  HZ1 LYS A  43      30.939  36.156   8.200  1.00 57.73           H  
ATOM    737  HZ2 LYS A  43      32.072  35.274   7.974  1.00 57.73           H  
ATOM    738  HZ3 LYS A  43      31.760  36.318   7.012  1.00 57.73           H  
ATOM    739  N   PRO A  44      30.327  29.414   3.709  1.00 10.07           N  
ANISOU  739  N   PRO A  44      858   1257   1482     92    404    336       N  
ATOM    740  CA  PRO A  44      29.814  28.190   4.344  1.00  9.14           C  
ANISOU  740  CA  PRO A  44      883   1112   1271    114    114    193       C  
ATOM    741  C   PRO A  44      29.893  28.309   5.888  1.00  8.54           C  
ANISOU  741  C   PRO A  44      801   1036   1216      0     86    145       C  
ATOM    742  O   PRO A  44      30.737  29.017   6.468  1.00  9.84           O  
ANISOU  742  O   PRO A  44      903   1260   1352   -135    122    104       O  
ATOM    743  CB  PRO A  44      30.753  27.118   3.800  1.00 10.82           C  
ANISOU  743  CB  PRO A  44     1248   1396   1222    302    144     51       C  
ATOM    744  CG  PRO A  44      32.038  27.849   3.536  1.00 12.06           C  
ANISOU  744  CG  PRO A  44      986   1608   1715    359    173     23       C  
ATOM    745  CD  PRO A  44      31.651  29.231   3.071  1.00 12.08           C  
ANISOU  745  CD  PRO A  44      903   1783   1632    203    401    272       C  
ATOM    746  HA  PRO A  44      28.892  28.016   4.060  1.00 10.97           H  
ATOM    747  HB2 PRO A  44      30.885  26.411   4.451  1.00 12.98           H  
ATOM    748  HB3 PRO A  44      30.401  26.732   2.984  1.00 12.98           H  
ATOM    749  HG2 PRO A  44      32.572  27.900   4.344  1.00 14.47           H  
ATOM    750  HG3 PRO A  44      32.553  27.393   2.852  1.00 14.47           H  
ATOM    751  HD2 PRO A  44      32.285  29.898   3.378  1.00 14.50           H  
ATOM    752  HD3 PRO A  44      31.585  29.274   2.104  1.00 14.50           H  
ATOM    753  N   LYS A  45      29.014  27.580   6.525  1.00  8.49           N  
ANISOU  753  N   LYS A  45      870    993   1171    -64     40     99       N  
ATOM    754  CA  LYS A  45      28.900  27.552   7.972  1.00  7.73           C  
ANISOU  754  CA  LYS A  45      780    891   1090    -50     55     17       C  
ATOM    755  C   LYS A  45      28.426  26.153   8.376  1.00  6.84           C  
ANISOU  755  C   LYS A  45      620    834    988     29     25   -118       C  
ATOM    756  O   LYS A  45      27.682  25.536   7.638  1.00  7.55           O  
ANISOU  756  O   LYS A  45      902    929    867    -69    -71    -12       O  
ATOM    757  CB  LYS A  45      27.885  28.615   8.404  1.00  8.17           C  
ANISOU  757  CB  LYS A  45      799    847   1274    -56    -89    110       C  
ATOM    758  CG  LYS A  45      27.769  28.854   9.898  1.00  8.97           C  
ANISOU  758  CG  LYS A  45      883    986   1335    112     83    -76       C  
ATOM    759  CD  LYS A  45      26.798  29.932  10.269  1.00 12.34           C  
ANISOU  759  CD  LYS A  45     1170    889   2350     74    483    -86       C  
ATOM    760  CE  LYS A  45      26.738  30.231  11.791  1.00 20.86           C  
ANISOU  760  CE  LYS A  45     3166   1673   2615    846   1529    110       C  
ATOM    761  NZ  LYS A  45      26.167  31.313  12.445  1.00 25.70           N  
ANISOU  761  NZ  LYS A  45     3091   2794   3299   -168   1045  -1441       N  
ATOM    762  H   LYS A  45      28.476  27.092   6.063  1.00 10.19           H  
ATOM    763  HA  LYS A  45      29.772  27.739   8.378  1.00  9.27           H  
ATOM    764  HB2 LYS A  45      28.123  29.454   7.979  1.00  9.81           H  
ATOM    765  HB3 LYS A  45      27.013  28.357   8.068  1.00  9.81           H  
ATOM    766  HG2 LYS A  45      27.495  28.027  10.325  1.00 10.76           H  
ATOM    767  HG3 LYS A  45      28.644  29.089  10.245  1.00 10.76           H  
ATOM    768  HD2 LYS A  45      27.042  30.745   9.800  1.00 14.80           H  
ATOM    769  HD3 LYS A  45      25.914  29.672   9.967  1.00 14.80           H  
ATOM    770  HE2 LYS A  45      26.320  29.449  12.185  1.00 25.03           H  
ATOM    771  HE3 LYS A  45      27.661  30.216  12.088  1.00 25.03           H  
ATOM    772  HZ1 LYS A  45      26.282  31.223  13.323  1.00 38.55           H  
ATOM    773  HZ2 LYS A  45      26.556  32.064  12.170  1.00 38.55           H  
ATOM    774  HZ3 LYS A  45      25.296  31.344  12.261  1.00 38.55           H  
ATOM    775  N   MET A  46      28.817  25.723   9.575  1.00  6.64           N  
ANISOU  775  N   MET A  46      651    767    953     71    -84    -46       N  
ATOM    776  CA  MET A  46      28.223  24.536  10.192  1.00  6.74           C  
ANISOU  776  CA  MET A  46      705    821    884     45    -53   -115       C  
ATOM    777  C   MET A  46      27.351  24.988  11.358  1.00  7.01           C  
ANISOU  777  C   MET A  46      814    873    817     19    -65   -172       C  
ATOM    778  O   MET A  46      27.802  25.815  12.159  1.00  9.83           O  
ANISOU  778  O   MET A  46     1088   1271   1152   -238     61   -461       O  
ATOM    779  CB AMET A  46      29.335  23.532  10.503  0.08  7.73           C  
ANISOU  779  CB AMET A  46      794    774   1196     58     18     62       C  
ATOM    780  CB BMET A  46      29.292  23.586  10.723  0.66  7.90           C  
ANISOU  780  CB BMET A  46      889    878   1056    125     -7     82       C  
ATOM    781  CB CMET A  46      29.346  23.630  10.708  0.26  6.55           C  
ANISOU  781  CB CMET A  46      897    679    765     35   -207   -168       C  
ATOM    782  CG AMET A  46      30.274  23.262   9.326  0.08  7.01           C  
ANISOU  782  CG AMET A  46      467   1020   1018    -21   -347   -471       C  
ATOM    783  CG BMET A  46      30.149  22.963   9.677  0.66  8.23           C  
ANISOU  783  CG BMET A  46      765   1356    820    210   -131     82       C  
ATOM    784  CG CMET A  46      30.033  22.906   9.549  0.26  7.15           C  
ANISOU  784  CG CMET A  46      760    279   1515   -162    462    -49       C  
ATOM    785  SD AMET A  46      30.761  21.507   9.184  0.08  9.39           S  
ANISOU  785  SD AMET A  46     1018   1007   1329     89    -24   -226       S  
ATOM    786  SD BMET A  46      29.350  21.981   8.420  0.66 14.17           S  
ANISOU  786  SD BMET A  46      909   1825   2330    320   -262  -1076       S  
ATOM    787  SD CMET A  46      29.193  21.399   9.106  0.26  4.70           S  
ANISOU  787  SD CMET A  46      677    457    546    -33    -69     45       S  
ATOM    788  CE AMET A  46      29.008  20.943   9.308  0.08  6.33           C  
ANISOU  788  CE AMET A  46      793    654    814    679    713    734       C  
ATOM    789  CE BMET A  46      29.152  20.583   9.414  0.66 28.18           C  
ANISOU  789  CE BMET A  46     4565   2312   3192  -1517   2721  -1203       C  
ATOM    790  CE CMET A  46      29.924  20.199  10.264  0.26  5.07           C  
ANISOU  790  CE CMET A  46      604    461    747    137    -85    124       C  
ATOM    791  H   MET A  46      29.433  26.153   9.995  1.00  7.96           H  
ATOM    792  HA AMET A  46      27.634  24.124   9.526  1.00  8.09           H  
ATOM    793  HB2AMET A  46      29.857  23.866  11.249  0.08  9.28           H  
ATOM    794  HB2BMET A  46      29.861  24.074  11.339  0.66  9.48           H  
ATOM    795  HB2CMET A  46      29.998  24.164  11.188  0.26  7.86           H  
ATOM    796  HB3AMET A  46      28.931  22.694  10.779  0.08  9.28           H  
ATOM    797  HB3BMET A  46      28.855  22.880  11.226  0.66  9.48           H  
ATOM    798  HB3CMET A  46      28.978  22.978  11.324  0.26  7.86           H  
ATOM    799  HG2AMET A  46      29.836  23.535   8.505  0.08  8.41           H  
ATOM    800  HG2BMET A  46      30.639  23.673   9.233  0.66  9.88           H  
ATOM    801  HG2CMET A  46      30.062  23.494   8.778  0.26  8.58           H  
ATOM    802  HG3AMET A  46      31.072  23.803   9.429  0.08  8.41           H  
ATOM    803  HG3BMET A  46      30.801  22.401  10.124  0.66  9.88           H  
ATOM    804  HG3CMET A  46      30.947  22.699   9.800  0.26  8.58           H  
ATOM    805  HE1AMET A  46      28.975  19.985   9.257  0.08  9.49           H  
ATOM    806  HE1BMET A  46      28.718  19.891   8.910  0.66 42.27           H  
ATOM    807  HE1CMET A  46      29.538  19.333  10.114  0.26  7.61           H  
ATOM    808  HE2AMET A  46      28.637  21.232  10.145  0.08  9.49           H  
ATOM    809  HE2BMET A  46      30.012  20.274   9.707  0.66 42.27           H  
ATOM    810  HE2CMET A  46      30.873  20.156  10.122  0.26  7.61           H  
ATOM    811  HE3AMET A  46      28.499  21.319   8.586  0.08  9.49           H  
ATOM    812  HE3BMET A  46      28.615  20.807  10.177  0.66 42.27           H  
ATOM    813  HE3CMET A  46      29.748  20.476  11.166  0.26  7.61           H  
ATOM    814  N   ILE A  47      26.158  24.461  11.448  1.00  6.62           N  
ANISOU  814  N   ILE A  47      714    899    752    135    -49   -207       N  
ATOM    815  CA  ILE A  47      25.263  24.724  12.575  1.00  6.66           C  
ANISOU  815  CA  ILE A  47      774    874    732    146    -75   -172       C  
ATOM    816  C   ILE A  47      24.909  23.396  13.220  1.00  6.81           C  
ANISOU  816  C   ILE A  47      716    944    773    252   -111   -168       C  
ATOM    817  O   ILE A  47      24.688  22.394  12.557  1.00  7.19           O  
ANISOU  817  O   ILE A  47     1059    769    741    249   -109    -63       O  
ATOM    818  CB  ILE A  47      24.013  25.541  12.212  1.00  6.50           C  
ANISOU  818  CB  ILE A  47      790    913    621    181    -38   -131       C  
ATOM    819  CG1 ILE A  47      23.162  24.845  11.135  1.00  6.66           C  
ANISOU  819  CG1 ILE A  47      805    930    646    161    -68   -103       C  
ATOM    820  CG2 ILE A  47      24.412  26.933  11.840  1.00  8.08           C  
ANISOU  820  CG2 ILE A  47     1023    814   1050    157   -125   -140       C  
ATOM    821  CD1 ILE A  47      21.818  25.509  10.925  1.00  6.69           C  
ANISOU  821  CD1 ILE A  47      751    929    709    148     -5      1       C  
ATOM    822  H   ILE A  47      25.888  23.939  10.820  1.00  7.94           H  
ATOM    823  HA  ILE A  47      25.769  25.243  13.235  1.00  7.99           H  
ATOM    824  HB  ILE A  47      23.463  25.603  13.020  1.00  7.80           H  
ATOM    825 HG12 ILE A  47      23.650  24.848  10.297  1.00  8.00           H  
ATOM    826 HG13 ILE A  47      23.021  23.921  11.393  1.00  8.00           H  
ATOM    827 HG21 ILE A  47      23.629  27.440  11.613  1.00 12.12           H  
ATOM    828 HG22 ILE A  47      24.858  27.347  12.582  1.00 12.12           H  
ATOM    829 HG23 ILE A  47      25.005  26.905  11.085  1.00 12.12           H  
ATOM    830 HD11 ILE A  47      21.331  25.037  10.246  1.00 10.03           H  
ATOM    831 HD12 ILE A  47      21.321  25.492  11.746  1.00 10.03           H  
ATOM    832 HD13 ILE A  47      21.950  26.419  10.649  1.00 10.03           H  
ATOM    833  N  AGLY A  48      24.748  23.310  14.561  0.56  7.43           N  
ANISOU  833  N  AGLY A  48      835   1007    814    -75    274   -278       N  
ATOM    834  N  BGLY A  48      24.919  23.561  14.562  0.44  6.70           N  
ANISOU  834  N  BGLY A  48      585   1097    712    -45     93   -137       N  
ATOM    835  CA AGLY A  48      24.585  22.064  15.315  0.56  7.34           C  
ANISOU  835  CA AGLY A  48      835   1049    739    -18    172   -143       C  
ATOM    836  CA BGLY A  48      24.572  22.477  15.383  0.44  7.56           C  
ANISOU  836  CA BGLY A  48      761   1069    872   -171    327   -254       C  
ATOM    837  C  AGLY A  48      23.478  22.062  16.403  0.56  5.73           C  
ANISOU  837  C  AGLY A  48      816    673    558     31     41     69       C  
ATOM    838  C  BGLY A  48      23.106  22.579  15.801  0.44  4.93           C  
ANISOU  838  C  BGLY A  48      701    475    586     96    105    103       C  
ATOM    839  O  AGLY A  48      23.147  23.094  16.961  0.56  6.77           O  
ANISOU  839  O  AGLY A  48      999    728    692    -20    188    -18       O  
ATOM    840  O  BGLY A  48      22.528  23.634  15.941  0.44  5.90           O  
ANISOU  840  O  BGLY A  48      841    459    807     76    314     27       O  
ATOM    841  H  AGLY A  48      24.740  24.046  15.006  0.56  8.92           H  
ATOM    842  H  BGLY A  48      25.136  24.318  14.907  0.44  8.04           H  
ATOM    843  HA2AGLY A  48      24.394  21.351  14.686  0.56  8.81           H  
ATOM    844  HA2BGLY A  48      24.717  21.646  14.903  0.44  9.07           H  
ATOM    845  HA3AGLY A  48      25.430  21.855  15.743  0.56  8.81           H  
ATOM    846  HA3BGLY A  48      25.136  22.473  16.172  0.44  9.07           H  
ATOM    847  N  AGLY A  49      22.916  20.890  16.659  0.56  5.81           N  
ANISOU  847  N  AGLY A  49      791    716    570     37     92     -6       N  
ATOM    848  N  BGLY A  49      22.602  21.394  16.127  0.44  5.24           N  
ANISOU  848  N  BGLY A  49      673    515    686    130    242    126       N  
ATOM    849  CA AGLY A  49      21.842  20.774  17.656  0.56  5.85           C  
ANISOU  849  CA AGLY A  49      787    760    544    -54    131    -19       C  
ATOM    850  CA BGLY A  49      21.339  21.267  16.831  0.44  5.78           C  
ANISOU  850  CA BGLY A  49      700    509    856     15    268    148       C  
ATOM    851  C  AGLY A  49      21.562  19.290  17.844  0.56  6.00           C  
ANISOU  851  C  AGLY A  49      939    741    465     44     56     61       C  
ATOM    852  C  BGLY A  49      21.269  19.897  17.491  0.44  5.23           C  
ANISOU  852  C  BGLY A  49      748    476    645     89    242     88       C  
ATOM    853  O  AGLY A  49      22.454  18.450  17.839  0.56  6.91           O  
ANISOU  853  O  AGLY A  49      900    865    705     80     83    113       O  
ATOM    854  O  BGLY A  49      22.294  19.281  17.830  0.44  6.10           O  
ANISOU  854  O  BGLY A  49      776    648    757     81    165    151       O  
ATOM    855  H  AGLY A  49      23.183  20.189  16.238  0.56  6.98           H  
ATOM    856  H  BGLY A  49      23.036  20.682  15.916  0.44  6.29           H  
ATOM    857  HA2AGLY A  49      22.118  21.173  18.496  0.56  7.02           H  
ATOM    858  HA2BGLY A  49      21.266  21.961  17.504  0.44  6.94           H  
ATOM    859  HA3AGLY A  49      21.044  21.231  17.346  0.56  7.02           H  
ATOM    860  HA3BGLY A  49      20.603  21.370  16.207  0.44  6.94           H  
ATOM    861  N  AILE A  50      20.262  18.994  18.069  0.56  5.93           N  
ANISOU  861  N  AILE A  50      876    686    557     -3    160    105       N  
ATOM    862  N  BILE A  50      20.040  19.407  17.639  0.44  5.12           N  
ANISOU  862  N  BILE A  50      748    462    617     66    212    160       N  
ATOM    863  CA AILE A  50      19.884  17.583  18.228  0.56  6.10           C  
ANISOU  863  CA AILE A  50      959    632    590     61    106     98       C  
ATOM    864  CA BILE A  50      19.831  18.232  18.474  0.44  5.57           C  
ANISOU  864  CA BILE A  50      839    550    601     47    217     84       C  
ATOM    865  C  AILE A  50      20.246  16.845  16.949  0.56  7.45           C  
ANISOU  865  C  AILE A  50     1283    750    627     47    149     39       C  
ATOM    866  C  BILE A  50      20.552  16.993  17.995  0.44  6.14           C  
ANISOU  866  C  BILE A  50      957    494    744     75    261    105       C  
ATOM    867  O  AILE A  50      19.885  17.226  15.860  0.56  7.29           O  
ANISOU  867  O  AILE A  50     1208    823    574    -54    100     74       O  
ATOM    868  O  BILE A  50      20.977  16.172  18.793  0.44  7.71           O  
ANISOU  868  O  BILE A  50     1348    674    733    110     93    174       O  
ATOM    869  CB AILE A  50      18.379  17.497  18.508  0.56  6.81           C  
ANISOU  869  CB AILE A  50      917    797    719   -110     45    136       C  
ATOM    870  CB BILE A  50      18.307  17.958  18.638  0.44  5.44           C  
ANISOU  870  CB BILE A  50      815    478    650    -10    271      5       C  
ATOM    871  CG1AILE A  50      18.046  18.131  19.864  0.56  7.00           C  
ANISOU  871  CG1AILE A  50      854    812    834   -107    147     98       C  
ATOM    872  CG1BILE A  50      17.977  17.055  19.835  0.44  6.47           C  
ANISOU  872  CG1BILE A  50      922    727    663   -146    190    113       C  
ATOM    873  CG2AILE A  50      17.875  16.083  18.417  0.56  7.53           C  
ANISOU  873  CG2AILE A  50     1127    875    690   -112     16    147       C  
ATOM    874  CG2BILE A  50      17.666  17.458  17.357  0.44  6.48           C  
ANISOU  874  CG2BILE A  50      951    761    603    -91    215     25       C  
ATOM    875  CD1AILE A  50      18.415  17.273  21.057  0.56  8.59           C  
ANISOU  875  CD1AILE A  50     1355   1050    666   -154     42     44       C  
ATOM    876  CD1BILE A  50      18.399  17.572  21.171  0.44  6.16           C  
ANISOU  876  CD1BILE A  50      712    876    612    -80    196    144       C  
ATOM    877  H  AILE A  50      19.671  19.617  18.118  0.56  7.12           H  
ATOM    878  H  BILE A  50      19.374  19.782  17.244  0.44  6.14           H  
ATOM    879  HA AILE A  50      20.379  17.195  18.980  0.56  7.33           H  
ATOM    880  HA BILE A  50      20.184  18.444  19.364  0.44  6.68           H  
ATOM    881  HB AILE A  50      17.920  18.020  17.818  0.56  8.17           H  
ATOM    882  HB BILE A  50      17.893  18.825  18.829  0.44  6.52           H  
ATOM    883 HG12AILE A  50      18.511  18.979  19.934  0.56  8.39           H  
ATOM    884 HG12BILE A  50      17.018  16.910  19.853  0.44  7.76           H  
ATOM    885 HG13AILE A  50      17.094  18.315  19.896  0.56  8.39           H  
ATOM    886 HG13BILE A  50      18.399  16.193  19.694  0.44  7.76           H  
ATOM    887 HG21AILE A  50      16.932  16.067  18.597  0.56 11.30           H  
ATOM    888 HG21BILE A  50      17.895  18.046  16.634  0.44  9.72           H  
ATOM    889 HG22AILE A  50      18.038  15.742  17.534  0.56 11.30           H  
ATOM    890 HG22BILE A  50      17.986  16.573  17.164  0.44  9.72           H  
ATOM    891 HG23AILE A  50      18.333  15.538  19.060  0.56 11.30           H  
ATOM    892 HG23BILE A  50      16.712  17.437  17.463  0.44  9.72           H  
ATOM    893 HD11AILE A  50      18.178  17.732  21.866  0.56 12.89           H  
ATOM    894 HD11BILE A  50      18.150  16.942  21.851  0.44  9.24           H  
ATOM    895 HD12AILE A  50      17.941  16.440  21.011  0.56 12.89           H  
ATOM    896 HD12BILE A  50      19.351  17.695  21.181  0.44  9.24           H  
ATOM    897 HD13AILE A  50      19.360  17.105  21.050  0.56 12.89           H  
ATOM    898 HD13BILE A  50      17.966  18.413  21.340  0.44  9.24           H  
ATOM    899  N  AGLY A  51      20.999  15.740  17.150  0.56  7.24           N  
ANISOU  899  N  AGLY A  51     1223    782    582      9    151     48       N  
ATOM    900  N  BGLY A  51      20.662  16.839  16.656  0.44  6.05           N  
ANISOU  900  N  BGLY A  51      934    530    699     67    201     15       N  
ATOM    901  CA AGLY A  51      21.485  14.950  16.034  0.56  8.21           C  
ANISOU  901  CA AGLY A  51     1187    776    970    146    308    -38       C  
ATOM    902  CA BGLY A  51      21.278  15.665  16.079  0.44  6.91           C  
ANISOU  902  CA BGLY A  51      875    718    877    155    187   -147       C  
ATOM    903  C  AGLY A  51      22.778  15.550  15.454  0.56 10.78           C  
ANISOU  903  C  AGLY A  51     1068   2133    651   -238    138     43       C  
ATOM    904  C  BGLY A  51      22.647  15.660  15.559  0.44  9.31           C  
ANISOU  904  C  BGLY A  51      924   1311   1093    271    374    343       C  
ATOM    905  O  AGLY A  51      23.320  14.909  14.517  0.56 11.66           O  
ANISOU  905  O  AGLY A  51     1144   1862   1160   -367    369   -155       O  
ATOM    906  O  BGLY A  51      23.094  14.736  14.889  0.44 14.69           O  
ANISOU  906  O  BGLY A  51     1356   1137   2756    -44   1378    112       O  
ATOM    907  H  AGLY A  51      21.194  15.502  17.953  0.56  8.69           H  
ATOM    908  H  BGLY A  51      20.358  17.453  16.136  0.44  7.27           H  
ATOM    909  HA2AGLY A  51      21.656  14.043  16.332  0.56  9.85           H  
ATOM    910  HA2BGLY A  51      21.235  14.970  16.753  0.44  8.30           H  
ATOM    911  HA3AGLY A  51      20.806  14.917  15.343  0.56  9.85           H  
ATOM    912  HA3BGLY A  51      20.704  15.380  15.351  0.44  8.30           H  
ATOM    913  N   GLY A  52      23.392  16.673  15.856  1.00  9.37           N  
ANISOU  913  N   GLY A  52      913   1669    767     10    159    183       N  
ATOM    914  CA  GLY A  52      24.671  17.022  15.310  1.00  8.44           C  
ANISOU  914  CA  GLY A  52      962   1194    858    155    124    253       C  
ATOM    915  C   GLY A  52      24.567  18.237  14.408  1.00  7.12           C  
ANISOU  915  C   GLY A  52      882    962    701    193    135     35       C  
ATOM    916  O   GLY A  52      23.738  19.085  14.620  1.00  9.25           O  
ANISOU  916  O   GLY A  52     1177   1238    889    388    332     27       O  
ATOM    917  H  AGLY A  52      23.019  17.182  16.440  1.00 11.25           H  
ATOM    918  HA2 GLY A  52      25.289  17.209  16.033  1.00 10.12           H  
ATOM    919  HA3 GLY A  52      25.020  16.272  14.803  1.00 10.12           H  
ATOM    920  N   PHE A  53      25.411  18.267  13.384  1.00  6.92           N  
ANISOU  920  N   PHE A  53      943    839    689    223    166     65       N  
ATOM    921  CA  PHE A  53      25.645  19.466  12.567  1.00  6.41           C  
ANISOU  921  CA  PHE A  53      890    758    642    173    103     24       C  
ATOM    922  C   PHE A  53      25.217  19.245  11.122  1.00  6.77           C  
ANISOU  922  C   PHE A  53      923    838    659     92    136    -15       C  
ATOM    923  O   PHE A  53      25.286  18.133  10.575  1.00  7.94           O  
ANISOU  923  O   PHE A  53     1316    774    747     47    138    -59       O  
ATOM    924  CB  PHE A  53      27.112  19.861  12.581  1.00  7.08           C  
ANISOU  924  CB  PHE A  53      917    963    650    155    141     99       C  
ATOM    925  CG  PHE A  53      27.604  20.387  13.912  1.00  6.65           C  
ANISOU  925  CG  PHE A  53      724   1014    640    153     77    106       C  
ATOM    926  CD1 PHE A  53      27.888  19.508  14.964  1.00  8.20           C  
ANISOU  926  CD1 PHE A  53      922   1088    920     86    -66    310       C  
ATOM    927  CD2 PHE A  53      27.784  21.731  14.138  1.00  6.77           C  
ANISOU  927  CD2 PHE A  53      621   1028    772    150     22     60       C  
ATOM    928  CE1 PHE A  53      28.304  20.016  16.190  1.00 10.10           C  
ANISOU  928  CE1 PHE A  53     1132   1698    779   -143   -156    362       C  
ATOM    929  CE2 PHE A  53      28.212  22.219  15.358  1.00  8.27           C  
ANISOU  929  CE2 PHE A  53      694   1301    959     24    103   -154       C  
ATOM    930  CZ  PHE A  53      28.465  21.336  16.376  1.00  9.85           C  
ANISOU  930  CZ  PHE A  53     1046   1783    691   -144    -68     72       C  
ATOM    931  H   PHE A  53      25.842  17.549  13.189  1.00  8.30           H  
ATOM    932  HA  PHE A  53      25.119  20.204  12.939  1.00  7.69           H  
ATOM    933  HB2 PHE A  53      27.645  19.088  12.336  1.00  8.50           H  
ATOM    934  HB3 PHE A  53      27.256  20.542  11.905  1.00  8.50           H  
ATOM    935  HD1 PHE A  53      27.800  18.590  14.843  1.00  9.84           H  
ATOM    936  HD2 PHE A  53      27.613  22.330  13.448  1.00  8.13           H  
ATOM    937  HE1 PHE A  53      28.473  19.431  16.894  1.00 12.12           H  
ATOM    938  HE2 PHE A  53      28.326  23.133  15.488  1.00  9.92           H  
ATOM    939  HZ  PHE A  53      28.752  21.653  17.202  1.00 11.82           H  
ATOM    940  N   ILE A  54      24.833  20.354  10.492  1.00  6.57           N  
ANISOU  940  N   ILE A  54      994    795    560     43     25    -26       N  
ATOM    941  CA  ILE A  54      24.650  20.404   9.046  1.00  6.48           C  
ANISOU  941  CA  ILE A  54     1014    773    530    -48     48    -61       C  
ATOM    942  C   ILE A  54      25.444  21.609   8.519  1.00  5.94           C  
ANISOU  942  C   ILE A  54      763    733    627     31     40    -27       C  
ATOM    943  O   ILE A  54      25.663  22.593   9.191  1.00  6.58           O  
ANISOU  943  O   ILE A  54      845    833    673    -21     14    -84       O  
ATOM    944  CB  ILE A  54      23.183  20.501   8.614  1.00  6.99           C  
ANISOU  944  CB  ILE A  54      950   1024    524    -97     54    -46       C  
ATOM    945  CG1 ILE A  54      22.473  21.768   9.112  1.00  8.14           C  
ANISOU  945  CG1 ILE A  54      928   1360    623     91      5   -209       C  
ATOM    946  CG2 ILE A  54      22.419  19.249   8.999  1.00  9.56           C  
ANISOU  946  CG2 ILE A  54     1199   1255    962   -278    136     59       C  
ATOM    947  CD1 ILE A  54      21.114  22.023   8.525  1.00  9.38           C  
ANISOU  947  CD1 ILE A  54      951   1580    821     20      2   -278       C  
ATOM    948  H   ILE A  54      24.689  21.066  10.954  1.00  7.89           H  
ATOM    949  HA  ILE A  54      25.033  19.589   8.658  1.00  7.78           H  
ATOM    950  HB  ILE A  54      23.180  20.543   7.635  1.00  8.39           H  
ATOM    951 HG12 ILE A  54      22.383  21.710  10.076  1.00  9.77           H  
ATOM    952 HG13 ILE A  54      23.038  22.532   8.919  1.00  9.77           H  
ATOM    953 HG21 ILE A  54      21.505  19.334   8.718  1.00 14.34           H  
ATOM    954 HG22 ILE A  54      22.816  18.487   8.571  1.00 14.34           H  
ATOM    955 HG23 ILE A  54      22.452  19.135   9.952  1.00 14.34           H  
ATOM    956 HD11 ILE A  54      20.752  22.831   8.894  1.00 14.07           H  
ATOM    957 HD12 ILE A  54      21.190  22.112   7.572  1.00 14.07           H  
ATOM    958 HD13 ILE A  54      20.533  21.287   8.732  1.00 14.07           H  
ATOM    959  N   LYS A  55      25.804  21.487   7.236  1.00  6.50           N  
ANISOU  959  N   LYS A  55      989    745    587      9     80    -52       N  
ATOM    960  CA  LYS A  55      26.466  22.538   6.511  1.00  6.37           C  
ANISOU  960  CA  LYS A  55      801    784    693     54     80      7       C  
ATOM    961  C   LYS A  55      25.418  23.399   5.778  1.00  6.30           C  
ANISOU  961  C   LYS A  55      791    825    634    -11     64     -9       C  
ATOM    962  O   LYS A  55      24.494  22.863   5.134  1.00  7.95           O  
ANISOU  962  O   LYS A  55      997    967    875    -69    -82      8       O  
ATOM    963  CB  LYS A  55      27.449  21.962   5.485  1.00  7.87           C  
ANISOU  963  CB  LYS A  55      995    993    824    141    272     -3       C  
ATOM    964  CG  LYS A  55      28.330  23.020   4.831  1.00  9.36           C  
ANISOU  964  CG  LYS A  55     1028   1178   1141     57    371    114       C  
ATOM    965  CD  LYS A  55      29.338  22.428   3.906  1.00 14.74           C  
ANISOU  965  CD  LYS A  55     1520   2144   1602    229    815    280       C  
ATOM    966  CE ALYS A  55      28.753  21.962   2.641  0.64 17.87           C  
ANISOU  966  CE ALYS A  55     2678   2360   1346    692    746     -8       C  
ATOM    967  CE BLYS A  55      30.091  23.349   3.010  0.36 15.47           C  
ANISOU  967  CE BLYS A  55     1720   2261   1547   -778    986   -662       C  
ATOM    968  NZ ALYS A  55      29.887  21.666   1.762  0.64 21.85           N  
ANISOU  968  NZ ALYS A  55     3103   2839   1865    516   1184    -84       N  
ATOM    969  NZ BLYS A  55      30.839  22.584   1.942  0.36 19.68           N  
ANISOU  969  NZ BLYS A  55     1915   2568   2550    360   1609   -108       N  
ATOM    970  H   LYS A  55      25.632  20.750   6.828  1.00  7.80           H  
ATOM    971  HA  LYS A  55      26.958  23.102   7.144  1.00  7.65           H  
ATOM    972  HB2 LYS A  55      28.016  21.310   5.925  1.00  9.44           H  
ATOM    973  HB3 LYS A  55      26.948  21.500   4.795  1.00  9.44           H  
ATOM    974  HG2 LYS A  55      27.770  23.638   4.336  1.00 11.24           H  
ATOM    975  HG3 LYS A  55      28.790  23.523   5.521  1.00 11.24           H  
ATOM    976  HD2ALYS A  55      30.018  23.092   3.714  1.00 17.68           H  
ATOM    977  HD3ALYS A  55      29.770  21.680   4.348  1.00 17.68           H  
ATOM    978  HE2ALYS A  55      28.217  21.167   2.786  0.64 21.44           H  
ATOM    979  HE2BLYS A  55      29.472  23.966   2.590  0.36 18.57           H  
ATOM    980  HE3ALYS A  55      28.191  22.650   2.252  0.64 21.44           H  
ATOM    981  HE3BLYS A  55      30.720  23.867   3.536  0.36 18.57           H  
ATOM    982  HZ1ALYS A  55      29.585  21.377   0.976  0.64 32.77           H  
ATOM    983  HZ1BLYS A  55      31.279  23.156   1.421  0.36 29.52           H  
ATOM    984  HZ2ALYS A  55      30.370  22.403   1.642  0.64 32.77           H  
ATOM    985  HZ2BLYS A  55      31.417  22.027   2.326  0.36 29.52           H  
ATOM    986  HZ3ALYS A  55      30.394  21.036   2.134  0.64 32.77           H  
ATOM    987  HZ3BLYS A  55      30.261  22.119   1.450  0.36 29.52           H  
ATOM    988  N   VAL A  56      25.571  24.715   5.883  1.00  6.14           N  
ANISOU  988  N   VAL A  56      711    819    665     32     43     36       N  
ATOM    989  CA  VAL A  56      24.659  25.660   5.292  1.00  6.13           C  
ANISOU  989  CA  VAL A  56      731    808    653     40     52     40       C  
ATOM    990  C   VAL A  56      25.475  26.757   4.575  1.00  6.76           C  
ANISOU  990  C   VAL A  56      716    856    844     38    103     33       C  
ATOM    991  O   VAL A  56      26.681  26.889   4.753  1.00  8.05           O  
ANISOU  991  O   VAL A  56      755    990   1132    -17     95    141       O  
ATOM    992  CB  VAL A  56      23.730  26.281   6.367  1.00  6.85           C  
ANISOU  992  CB  VAL A  56      736   1052    661    159     41     22       C  
ATOM    993  CG1 VAL A  56      22.897  25.185   7.034  1.00  8.14           C  
ANISOU  993  CG1 VAL A  56      886   1369    654     75    144     66       C  
ATOM    994  CG2 VAL A  56      24.509  27.088   7.384  1.00  8.21           C  
ANISOU  994  CG2 VAL A  56      878   1089    968    285     -1   -219       C  
ATOM    995  H   VAL A  56      26.245  25.017   6.323  1.00  7.37           H  
ATOM    996  HA  VAL A  56      24.107  25.194   4.629  1.00  7.36           H  
ATOM    997  HB  VAL A  56      23.113  26.891   5.912  1.00  8.23           H  
ATOM    998 HG11 VAL A  56      22.417  24.694   6.362  1.00 12.21           H  
ATOM    999 HG12 VAL A  56      23.477  24.588   7.512  1.00 12.21           H  
ATOM   1000 HG13 VAL A  56      22.273  25.583   7.645  1.00 12.21           H  
ATOM   1001 HG21 VAL A  56      25.019  27.765   6.933  1.00 12.32           H  
ATOM   1002 HG22 VAL A  56      23.899  27.503   7.999  1.00 12.32           H  
ATOM   1003 HG23 VAL A  56      25.103  26.507   7.866  1.00 12.32           H  
ATOM   1004  N   ARG A  57      24.758  27.546   3.779  1.00  7.26           N  
ANISOU 1004  N   ARG A  57      791    794   1007     64    147    177       N  
ATOM   1005  CA  ARG A  57      25.273  28.746   3.171  1.00  7.41           C  
ANISOU 1005  CA  ARG A  57      806    822   1021     38    340    127       C  
ATOM   1006  C   ARG A  57      24.782  29.958   3.969  1.00  7.23           C  
ANISOU 1006  C   ARG A  57      841    864    880      7    279    179       C  
ATOM   1007  O   ARG A  57      23.563  30.067   4.193  1.00  8.05           O  
ANISOU 1007  O   ARG A  57      810    994   1072     37    288    -56       O  
ATOM   1008  CB  ARG A  57      24.832  28.930   1.726  1.00  8.43           C  
ANISOU 1008  CB  ARG A  57     1128   1005    880     -6    367    189       C  
ATOM   1009  CG  ARG A  57      25.242  27.814   0.786  1.00 11.79           C  
ANISOU 1009  CG  ARG A  57     1573   1661    978    402    286    -75       C  
ATOM   1010  CD AARG A  57      25.057  27.957  -0.683  0.69 12.01           C  
ANISOU 1010  CD AARG A  57     1353   1971    966     70    342     -1       C  
ATOM   1011  CD BARG A  57      24.935  28.437  -0.623  0.31 11.70           C  
ANISOU 1011  CD BARG A  57      931   2438    811    138    361   -142       C  
ATOM   1012  NE AARG A  57      23.766  28.448  -1.092  0.69 12.19           N  
ANISOU 1012  NE AARG A  57     1197   1996   1161    -18    278    209       N  
ATOM   1013  NE BARG A  57      25.580  27.695  -1.702  0.31  9.97           N  
ANISOU 1013  NE BARG A  57     1378   1290    892    -71    281   -186       N  
ATOM   1014  CZ AARG A  57      22.568  27.961  -1.258  0.69 11.40           C  
ANISOU 1014  CZ AARG A  57     1453   1822    798     43    161     95       C  
ATOM   1015  CZ BARG A  57      25.477  28.003  -2.989  0.31 13.91           C  
ANISOU 1015  CZ BARG A  57     2056   2095    818    444    338   -291       C  
ATOM   1016  NH1AARG A  57      21.515  28.843  -1.692  0.69 10.11           N  
ANISOU 1016  NH1AARG A  57     1106   1417   1090    -98    -11    -53       N  
ATOM   1017  NH1BARG A  57      26.110  27.233  -3.847  0.31 13.68           N  
ANISOU 1017  NH1BARG A  57     1739   2085   1066    183    504   -417       N  
ATOM   1018  NH2AARG A  57      22.339  26.682  -1.148  0.69 11.65           N  
ANISOU 1018  NH2AARG A  57     1067   1625   1471     38    221    599       N  
ATOM   1019  NH2BARG A  57      24.793  29.024  -3.367  0.31 12.67           N  
ANISOU 1019  NH2BARG A  57     1822   2080    625    312    411    -86       N  
ATOM   1020  H   ARG A  57      23.942  27.328   3.619  1.00  8.71           H  
ATOM   1021  HA  ARG A  57      26.252  28.722   3.203  1.00  8.90           H  
ATOM   1022  HB2 ARG A  57      23.866  29.011   1.707  1.00 10.12           H  
ATOM   1023  HB3 ARG A  57      25.201  29.763   1.395  1.00 10.12           H  
ATOM   1024  HG2AARG A  57      26.183  27.640   0.940  1.00 14.14           H  
ATOM   1025  HG3AARG A  57      24.760  27.017   1.059  1.00 14.14           H  
ATOM   1026  HD2AARG A  57      25.737  28.560  -1.021  0.69 14.41           H  
ATOM   1027  HD2BARG A  57      23.976  28.441  -0.768  0.31 14.04           H  
ATOM   1028  HD3AARG A  57      25.202  27.092  -1.097  0.69 14.41           H  
ATOM   1029  HD3BARG A  57      25.243  29.356  -0.639  0.31 14.04           H  
ATOM   1030  HE AARG A  57      23.793  29.288  -1.277  0.69 14.62           H  
ATOM   1031  HE BARG A  57      26.059  27.013  -1.489  0.31 11.96           H  
ATOM   1032 HH11AARG A  57      20.738  28.526  -1.878  0.69 12.13           H  
ATOM   1033 HH11BARG A  57      26.073  27.406  -4.689  0.31 16.42           H  
ATOM   1034 HH12AARG A  57      21.665  29.687  -1.766  0.69 12.13           H  
ATOM   1035 HH12BARG A  57      26.561  26.556  -3.567  0.31 16.42           H  
ATOM   1036 HH21AARG A  57      22.984  26.144  -0.962  0.69 13.98           H  
ATOM   1037 HH21BARG A  57      24.739  29.220  -4.203  0.31 15.20           H  
ATOM   1038 HH22AARG A  57      21.543  26.376  -1.260  0.69 13.98           H  
ATOM   1039 HH22BARG A  57      24.389  29.511  -2.784  0.31 15.20           H  
ATOM   1040  N   GLN A  58      25.667  30.855   4.318  1.00  7.16           N  
ANISOU 1040  N   GLN A  58      791    769    999     35    275    157       N  
ATOM   1041  CA  GLN A  58      25.318  32.052   5.091  1.00  6.89           C  
ANISOU 1041  CA  GLN A  58      768    762    933     63    216    184       C  
ATOM   1042  C   GLN A  58      25.229  33.268   4.152  1.00  7.38           C  
ANISOU 1042  C   GLN A  58      824    820    993      1    265    263       C  
ATOM   1043  O   GLN A  58      26.267  33.653   3.579  1.00  8.90           O  
ANISOU 1043  O   GLN A  58      871    963   1348     43    402    389       O  
ATOM   1044  CB  GLN A  58      26.380  32.307   6.148  1.00  7.43           C  
ANISOU 1044  CB  GLN A  58      818    800   1038     13    168    230       C  
ATOM   1045  CG  GLN A  58      26.110  33.565   6.966  1.00  8.15           C  
ANISOU 1045  CG  GLN A  58      883    833   1196     56     98    172       C  
ATOM   1046  CD  GLN A  58      27.148  33.849   7.976  1.00  9.17           C  
ANISOU 1046  CD  GLN A  58      936    969   1373     82      9     70       C  
ATOM   1047  OE1 GLN A  58      27.810  32.951   8.480  1.00 12.74           O  
ANISOU 1047  OE1 GLN A  58     1387   1480   1684    299   -385     90       O  
ATOM   1048  NE2 GLN A  58      27.330  35.106   8.284  1.00 12.23           N  
ANISOU 1048  NE2 GLN A  58     1189   1262   1920   -133   -242     -3       N  
ATOM   1049  H   GLN A  58      26.486  30.739   4.085  1.00  8.60           H  
ATOM   1050  HA  GLN A  58      24.452  31.915   5.528  1.00  8.27           H  
ATOM   1051  HB2 GLN A  58      26.421  31.544   6.746  1.00  8.92           H  
ATOM   1052  HB3 GLN A  58      27.243  32.392   5.715  1.00  8.92           H  
ATOM   1053  HG2 GLN A  58      26.043  34.322   6.363  1.00  9.78           H  
ATOM   1054  HG3 GLN A  58      25.255  33.469   7.414  1.00  9.78           H  
ATOM   1055 HE21 GLN A  58      27.932  35.325   8.859  1.00 14.68           H  
ATOM   1056 HE22 GLN A  58      26.849  35.714   7.912  1.00 14.68           H  
ATOM   1057  N   TYR A  59      24.058  33.852   4.062  1.00  6.72           N  
ANISOU 1057  N   TYR A  59      856    729    816    -18    220    200       N  
ATOM   1058  CA  TYR A  59      23.808  35.077   3.301  1.00  7.50           C  
ANISOU 1058  CA  TYR A  59     1058    739    883     53    257    233       C  
ATOM   1059  C   TYR A  59      23.537  36.196   4.303  1.00  7.49           C  
ANISOU 1059  C   TYR A  59      980    721    976     19    173    212       C  
ATOM   1060  O   TYR A  59      22.721  36.047   5.208  1.00  9.17           O  
ANISOU 1060  O   TYR A  59     1411    863   1001   -144    442     41       O  
ATOM   1061  CB  TYR A  59      22.595  34.917   2.397  1.00  7.82           C  
ANISOU 1061  CB  TYR A  59     1099    840    857    137    173    302       C  
ATOM   1062  CG  TYR A  59      22.772  33.929   1.287  1.00  8.10           C  
ANISOU 1062  CG  TYR A  59     1109    975    812    154    220    279       C  
ATOM   1063  CD1 TYR A  59      22.493  32.574   1.463  1.00  8.60           C  
ANISOU 1063  CD1 TYR A  59     1259   1009    805    103    200    200       C  
ATOM   1064  CD2 TYR A  59      23.184  34.343   0.027  1.00  9.67           C  
ANISOU 1064  CD2 TYR A  59     1371   1194    890    174    230    345       C  
ATOM   1065  CE1 TYR A  59      22.628  31.684   0.456  1.00  9.70           C  
ANISOU 1065  CE1 TYR A  59     1490   1084    893    185    175    131       C  
ATOM   1066  CE2 TYR A  59      23.320  33.422  -1.013  1.00 11.04           C  
ANISOU 1066  CE2 TYR A  59     1795   1379    770    287    310    259       C  
ATOM   1067  CZ  TYR A  59      23.035  32.088  -0.816  1.00 11.48           C  
ANISOU 1067  CZ  TYR A  59     1938   1320    845    497    294    142       C  
ATOM   1068  OH  TYR A  59      23.156  31.191  -1.840  1.00 14.25           O  
ANISOU 1068  OH  TYR A  59     2641   1471    979    502    418     16       O  
ATOM   1069  H   TYR A  59      23.395  33.492   4.476  1.00  8.06           H  
ATOM   1070  HA  TYR A  59      24.596  35.298   2.762  1.00  9.00           H  
ATOM   1071  HB2 TYR A  59      21.839  34.642   2.938  1.00  9.39           H  
ATOM   1072  HB3 TYR A  59      22.381  35.781   2.011  1.00  9.39           H  
ATOM   1073  HD1 TYR A  59      22.206  32.276   2.296  1.00 10.32           H  
ATOM   1074  HD2 TYR A  59      23.370  35.241  -0.125  1.00 11.60           H  
ATOM   1075  HE1 TYR A  59      22.446  30.785   0.613  1.00 11.64           H  
ATOM   1076  HE2 TYR A  59      23.606  33.712  -1.849  1.00 13.25           H  
ATOM   1077  HH  TYR A  59      23.411  31.580  -2.515  1.00 21.37           H  
ATOM   1078  N   ASP A  60      24.173  37.335   4.160  1.00  9.59           N  
ANISOU 1078  N   ASP A  60     1192    812   1424    -85    422    169       N  
ATOM   1079  CA  ASP A  60      23.977  38.449   5.031  1.00  9.70           C  
ANISOU 1079  CA  ASP A  60     1198    826   1441    -74    268    100       C  
ATOM   1080  C   ASP A  60      23.043  39.498   4.380  1.00 10.08           C  
ANISOU 1080  C   ASP A  60     1327    729   1545    -96    349    143       C  
ATOM   1081  O   ASP A  60      22.878  39.584   3.184  1.00 11.12           O  
ANISOU 1081  O   ASP A  60     1667    908   1398     -7    346    247       O  
ATOM   1082  CB  ASP A  60      25.312  39.048   5.483  1.00 12.30           C  
ANISOU 1082  CB  ASP A  60     1461   1025   1911   -303     72    191       C  
ATOM   1083  CG  ASP A  60      26.171  38.000   6.186  1.00 13.64           C  
ANISOU 1083  CG  ASP A  60     1134   1179   2559   -214   -105    246       C  
ATOM   1084  OD1 ASP A  60      25.692  37.266   7.073  1.00 12.76           O  
ANISOU 1084  OD1 ASP A  60     1246   1054   2259   -115    -69    169       O  
ATOM   1085  OD2 ASP A  60      27.397  37.944   5.842  1.00 18.96           O  
ANISOU 1085  OD2 ASP A  60     1503   1833   3437   -115    439    537       O  
ATOM   1086  H   ASP A  60      24.734  37.414   3.513  1.00 11.51           H  
ATOM   1087  HA  ASP A  60      23.523  38.114   5.832  1.00 11.64           H  
ATOM   1088  HB2 ASP A  60      25.789  39.392   4.712  1.00 14.76           H  
ATOM   1089  HB3 ASP A  60      25.145  39.788   6.088  1.00 14.76           H  
ATOM   1090  N   GLN A  61      22.475  40.330   5.263  1.00  9.82           N  
ANISOU 1090  N   GLN A  61     1216    861   1433    -47    153      6       N  
ATOM   1091  CA  GLN A  61      21.684  41.473   4.817  1.00 10.78           C  
ANISOU 1091  CA  GLN A  61     1295    814   1745     21    184     36       C  
ATOM   1092  C   GLN A  61      20.528  41.082   3.927  1.00  9.95           C  
ANISOU 1092  C   GLN A  61     1427    844   1284    150    243    202       C  
ATOM   1093  O   GLN A  61      20.309  41.690   2.871  1.00 14.85           O  
ANISOU 1093  O   GLN A  61     2812   1091   1403    -69   -103    520       O  
ATOM   1094  CB  GLN A  61      22.552  42.580   4.189  1.00 15.46           C  
ANISOU 1094  CB  GLN A  61     1784    880   2858   -191    377    308       C  
ATOM   1095  CG  GLN A  61      23.645  43.116   5.095  1.00 19.77           C  
ANISOU 1095  CG  GLN A  61     2182   1266   3616   -675    142    181       C  
ATOM   1096  CD AGLN A  61      22.999  44.051   6.094  0.57 23.92           C  
ANISOU 1096  CD AGLN A  61     3763   1424   3360  -1077    464   -173       C  
ATOM   1097  CD BGLN A  61      24.286  44.371   4.575  0.43 32.54           C  
ANISOU 1097  CD BGLN A  61     4462   2086   5079  -2024   -481    738       C  
ATOM   1098  OE1AGLN A  61      23.163  43.815   7.308  0.57 37.57           O  
ANISOU 1098  OE1AGLN A  61     7802   2226   3397   -994    303    110       O  
ATOM   1099  OE1BGLN A  61      24.837  45.120   5.376  0.43 44.10           O  
ANISOU 1099  OE1BGLN A  61     7209   2922   5627  -3349   1689  -1359       O  
ATOM   1100  NE2AGLN A  61      22.235  45.037   5.681  0.57 28.26           N  
ANISOU 1100  NE2AGLN A  61     2655   4099   3346    720   -593  -1960       N  
ATOM   1101  NE2BGLN A  61      24.255  44.655   3.291  0.43 41.60           N  
ANISOU 1101  NE2BGLN A  61     5542   3313   6008  -2995  -2160   2773       N  
ATOM   1102  H   GLN A  61      22.579  40.189   6.105  1.00 11.79           H  
ATOM   1103  HA  GLN A  61      21.288  41.862   5.624  1.00 12.94           H  
ATOM   1104  HB2 GLN A  61      22.961  42.232   3.382  1.00 18.55           H  
ATOM   1105  HB3 GLN A  61      21.975  43.316   3.931  1.00 18.55           H  
ATOM   1106  HG2AGLN A  61      24.084  42.385   5.557  1.00 23.72           H  
ATOM   1107  HG3AGLN A  61      24.309  43.592   4.572  1.00 23.72           H  
ATOM   1108 HE21AGLN A  61      21.834  45.538   6.254  0.57 33.92           H  
ATOM   1109 HE21BGLN A  61      24.624  45.376   3.000  0.43 49.91           H  
ATOM   1110 HE22AGLN A  61      22.137  45.181   4.839  0.57 33.92           H  
ATOM   1111 HE22BGLN A  61      23.866  44.120   2.741  0.43 49.91           H  
ATOM   1112  N   ILE A  62      19.768  40.080   4.352  1.00  8.33           N  
ANISOU 1112  N   ILE A  62     1290    779    906    148     55     91       N  
ATOM   1113  CA  ILE A  62      18.624  39.582   3.643  1.00  8.49           C  
ANISOU 1113  CA  ILE A  62     1265    969    801    221     74     24       C  
ATOM   1114  C   ILE A  62      17.355  40.128   4.292  1.00  9.28           C  
ANISOU 1114  C   ILE A  62     1244   1215    858    282    -65   -162       C  
ATOM   1115  O   ILE A  62      17.183  40.020   5.493  1.00  9.88           O  
ANISOU 1115  O   ILE A  62     1180   1441    911    176     33   -216       O  
ATOM   1116  CB  ILE A  62      18.619  38.040   3.622  1.00  8.52           C  
ANISOU 1116  CB  ILE A  62     1297    919    830    182     23     74       C  
ATOM   1117  CG1 ILE A  62      19.864  37.474   2.960  1.00  8.93           C  
ANISOU 1117  CG1 ILE A  62     1304    890    996    198    -48    -52       C  
ATOM   1118  CG2 ILE A  62      17.358  37.503   3.011  1.00 10.19           C  
ANISOU 1118  CG2 ILE A  62     1308   1250   1085    158    -52   -193       C  
ATOM   1119  CD1 ILE A  62      20.010  37.832   1.486  1.00 10.80           C  
ANISOU 1119  CD1 ILE A  62     1632   1197   1031    395    214    -51       C  
ATOM   1120  H   ILE A  62      19.973  39.706   5.098  1.00  9.99           H  
ATOM   1121  HA  ILE A  62      18.665  39.906   2.719  1.00 10.19           H  
ATOM   1122  HB  ILE A  62      18.633  37.742   4.556  1.00 10.23           H  
ATOM   1123 HG12 ILE A  62      20.644  37.799   3.436  1.00 10.71           H  
ATOM   1124 HG13 ILE A  62      19.850  36.508   3.045  1.00 10.71           H  
ATOM   1125 HG21 ILE A  62      16.599  37.884   3.458  1.00 15.29           H  
ATOM   1126 HG22 ILE A  62      17.331  37.733   2.080  1.00 15.29           H  
ATOM   1127 HG23 ILE A  62      17.339  36.547   3.106  1.00 15.29           H  
ATOM   1128 HD11 ILE A  62      20.815  37.441   1.139  1.00 16.20           H  
ATOM   1129 HD12 ILE A  62      19.255  37.494   0.998  1.00 16.20           H  
ATOM   1130 HD13 ILE A  62      20.050  38.787   1.390  1.00 16.20           H  
ATOM   1131  N  AILE A  63      16.208  40.274   3.708  0.31  7.57           N  
ANISOU 1131  N  AILE A  63     1146    795    764     20    129    179       N  
ATOM   1132  N  BILE A  63      16.579  40.837   3.378  0.70  8.25           N  
ANISOU 1132  N  BILE A  63     1185    944    817    146     56    148       N  
ATOM   1133  CA AILE A  63      14.946  40.679   4.331  0.31  8.31           C  
ANISOU 1133  CA AILE A  63     1198    994    776    220     73    209       C  
ATOM   1134  CA BILE A  63      15.268  41.342   3.808  0.70  8.66           C  
ANISOU 1134  CA BILE A  63     1211    957    926    208    -10    159       C  
ATOM   1135  C  AILE A  63      13.958  39.527   4.335  0.31  8.10           C  
ANISOU 1135  C  AILE A  63     1130   1070    693    144     60    143       C  
ATOM   1136  C  BILE A  63      14.284  40.214   3.900  0.70  7.96           C  
ANISOU 1136  C  BILE A  63     1168    990    685    183    -23     81       C  
ATOM   1137  O  AILE A  63      13.804  38.860   3.313  0.31  9.33           O  
ANISOU 1137  O  AILE A  63     1472   1159    704    141    159     66       O  
ATOM   1138  O  BILE A  63      14.237  39.334   3.040  0.70 11.49           O  
ANISOU 1138  O  BILE A  63     1855   1297    952   -257    296   -117       O  
ATOM   1139  CB AILE A  63      14.363  41.884   3.568  0.31 10.08           C  
ANISOU 1139  CB AILE A  63     1644    961    997    370    148    258       C  
ATOM   1140  CB BILE A  63      14.795  42.460   2.863  0.70 13.20           C  
ANISOU 1140  CB BILE A  63     1516   1222   1979    383     58    649       C  
ATOM   1141  CG1AILE A  63      15.297  43.090   3.709  0.31 12.92           C  
ANISOU 1141  CG1AILE A  63     1977    973   1665    207    466    305       C  
ATOM   1142  CG1BILE A  63      15.743  43.675   2.937  0.70 14.45           C  
ANISOU 1142  CG1BILE A  63     1817   1041   2304    319     96    426       C  
ATOM   1143  CG2AILE A  63      12.920  42.097   3.999  0.31 14.43           C  
ANISOU 1143  CG2AILE A  63     1532   1967   1658    584    106    891       C  
ATOM   1144  CG2BILE A  63      13.367  42.864   3.152  0.70 19.53           C  
ANISOU 1144  CG2BILE A  63     1559   1950   3468    612     33   1085       C  
ATOM   1145  CD1AILE A  63      15.049  44.190   2.684  0.31 14.96           C  
ANISOU 1145  CD1AILE A  63     2164    809   2373    457    219    503       C  
ATOM   1146  CD1BILE A  63      15.522  44.767   1.980  0.70 21.00           C  
ANISOU 1146  CD1BILE A  63     2715   1951   2839     90    174   1238       C  
ATOM   1147  H  AILE A  63      16.185  40.117   2.863  0.31  9.08           H  
ATOM   1148  H  BILE A  63      16.862  40.977   2.578  0.70  9.89           H  
ATOM   1149  HA AILE A  63      15.123  40.947   5.257  0.31  9.97           H  
ATOM   1150  HA BILE A  63      15.371  41.727   4.703  0.70 10.39           H  
ATOM   1151  HB AILE A  63      14.347  41.643   2.618  0.31 12.10           H  
ATOM   1152  HB BILE A  63      14.827  42.111   1.947  0.70 15.84           H  
ATOM   1153 HG12AILE A  63      15.191  43.463   4.598  0.31 15.50           H  
ATOM   1154 HG12BILE A  63      15.683  44.046   3.832  0.70 17.34           H  
ATOM   1155 HG13AILE A  63      16.214  42.786   3.625  0.31 15.50           H  
ATOM   1156 HG13BILE A  63      16.650  43.354   2.820  0.70 17.34           H  
ATOM   1157 HG21AILE A  63      12.425  41.285   3.870  0.31 21.65           H  
ATOM   1158 HG21BILE A  63      12.799  42.092   3.099  0.70 29.29           H  
ATOM   1159 HG22AILE A  63      12.897  42.343   4.927  0.31 21.65           H  
ATOM   1160 HG22BILE A  63      13.313  43.241   4.033  0.70 29.29           H  
ATOM   1161 HG23AILE A  63      12.529  42.798   3.472  0.31 21.65           H  
ATOM   1162 HG23BILE A  63      13.082  43.515   2.507  0.70 29.29           H  
ATOM   1163 HD11AILE A  63      15.667  44.910   2.831  0.31 22.44           H  
ATOM   1164 HD11BILE A  63      16.172  45.458   2.128  0.70 31.51           H  
ATOM   1165 HD12AILE A  63      15.174  43.837   1.800  0.31 22.44           H  
ATOM   1166 HD12BILE A  63      15.611  44.430   1.085  0.70 31.51           H  
ATOM   1167 HD13AILE A  63      14.151  44.515   2.774  0.31 22.44           H  
ATOM   1168 HD13BILE A  63      14.640  45.125   2.101  0.70 31.51           H  
ATOM   1169  N  AILE A  64      13.309  39.278   5.459  0.31  7.93           N  
ANISOU 1169  N  AILE A  64     1181    953    700    217    149    -21       N  
ATOM   1170  N  BILE A  64      13.466  40.243   4.950  0.70  8.51           N  
ANISOU 1170  N  BILE A  64     1202   1067    774    118     16     35       N  
ATOM   1171  CA AILE A  64      12.233  38.327   5.555  0.31  8.88           C  
ANISOU 1171  CA AILE A  64     1088   1147    937    184    126    166       C  
ATOM   1172  CA BILE A  64      12.457  39.207   5.180  0.70  8.66           C  
ANISOU 1172  CA BILE A  64     1095   1131    869     85   -156    122       C  
ATOM   1173  C  AILE A  64      11.128  39.145   6.176  0.31  8.47           C  
ANISOU 1173  C  AILE A  64     1152   1079    796    154     62    189       C  
ATOM   1174  C  BILE A  64      11.219  39.849   5.775  0.70  8.67           C  
ANISOU 1174  C  BILE A  64     1195   1158    746    180    -67    193       C  
ATOM   1175  O  AILE A  64      11.204  39.854   7.154  0.31  9.41           O  
ANISOU 1175  O  AILE A  64     1372   1103    888    367    -10     14       O  
ATOM   1176  O  BILE A  64      11.281  40.938   6.412  0.70 10.76           O  
ANISOU 1176  O  BILE A  64     1280   1363   1202     50    138   -255       O  
ATOM   1177  CB AILE A  64      12.516  37.101   6.413  0.31  9.37           C  
ANISOU 1177  CB AILE A  64      650   1284   1415    136     57    461       C  
ATOM   1178  CB BILE A  64      13.045  38.140   6.150  0.70  9.99           C  
ANISOU 1178  CB BILE A  64     1396   1044   1130    138   -398     73       C  
ATOM   1179  CG1AILE A  64      13.762  36.361   5.946  0.31  8.04           C  
ANISOU 1179  CG1AILE A  64      989   1089    796    141    -90      9       C  
ATOM   1180  CG1BILE A  64      12.205  36.898   6.247  0.70 10.06           C  
ANISOU 1180  CG1BILE A  64     1600   1127    869     91   -122     54       C  
ATOM   1181  CG2AILE A  64      11.363  36.079   6.478  0.31  9.50           C  
ANISOU 1181  CG2AILE A  64     1073    913   1407    -34     59   -278       C  
ATOM   1182  CG2BILE A  64      13.340  38.782   7.508  0.70 12.92           C  
ANISOU 1182  CG2BILE A  64     2311   1194   1113    161   -760     94       C  
ATOM   1183  CD1AILE A  64      14.014  35.083   6.712  0.31  7.89           C  
ANISOU 1183  CD1AILE A  64      969    972    880    226    -97    -18       C  
ATOM   1184  CD1BILE A  64      12.911  35.719   6.886  0.70 12.92           C  
ANISOU 1184  CD1BILE A  64     2275   1208   1132    209   -374    136       C  
ATOM   1185  H  AILE A  64      13.540  39.706   6.168  0.31  9.52           H  
ATOM   1186  H  BILE A  64      13.532  40.891   5.512  0.70 10.22           H  
ATOM   1187  HA AILE A  64      11.965  38.044   4.656  0.31 10.65           H  
ATOM   1188  HA BILE A  64      12.227  38.781   4.328  0.70 10.39           H  
ATOM   1189  HB AILE A  64      12.684  37.413   7.326  0.31 11.25           H  
ATOM   1190  HB BILE A  64      13.909  37.867   5.776  0.70 11.99           H  
ATOM   1191 HG12AILE A  64      13.670  36.151   5.003  0.31  9.65           H  
ATOM   1192 HG12BILE A  64      11.409  37.101   6.762  0.70 12.08           H  
ATOM   1193 HG13AILE A  64      14.531  36.945   6.044  0.31  9.65           H  
ATOM   1194 HG13BILE A  64      11.921  36.645   5.355  0.70 12.08           H  
ATOM   1195 HG21AILE A  64      10.562  36.519   6.771  0.31 14.24           H  
ATOM   1196 HG21BILE A  64      13.878  39.567   7.381  0.70 19.38           H  
ATOM   1197 HG22AILE A  64      11.221  35.701   5.607  0.31 14.24           H  
ATOM   1198 HG22BILE A  64      12.514  39.026   7.933  0.70 19.38           H  
ATOM   1199 HG23AILE A  64      11.589  35.381   7.097  0.31 14.24           H  
ATOM   1200 HG23BILE A  64      13.812  38.157   8.062  0.70 19.38           H  
ATOM   1201 HD11AILE A  64      14.808  34.660   6.377  0.31 11.84           H  
ATOM   1202 HD11BILE A  64      12.316  34.966   6.913  0.70 19.37           H  
ATOM   1203 HD12AILE A  64      14.128  35.285   7.644  0.31 11.84           H  
ATOM   1204 HD12BILE A  64      13.689  35.494   6.370  0.70 19.37           H  
ATOM   1205 HD13AILE A  64      13.266  34.491   6.602  0.31 11.84           H  
ATOM   1206 HD13BILE A  64      13.176  35.951   7.779  0.70 19.37           H  
ATOM   1207  N   GLU A  65      10.034  39.139   5.549  1.00  9.83           N  
ANISOU 1207  N   GLU A  65     1222   1344    947    288    -26    223       N  
ATOM   1208  CA  GLU A  65       8.776  39.539   6.205  1.00 10.36           C  
ANISOU 1208  CA  GLU A  65     1315   1260   1127    376    140    350       C  
ATOM   1209  C   GLU A  65       8.274  38.354   6.978  1.00  9.98           C  
ANISOU 1209  C   GLU A  65     1479   1206    882     72     57     98       C  
ATOM   1210  O   GLU A  65       8.141  37.277   6.402  1.00 13.67           O  
ANISOU 1210  O   GLU A  65     2646   1474    765   -408    133     98       O  
ATOM   1211  CB  GLU A  65       7.765  40.031   5.180  1.00 13.23           C  
ANISOU 1211  CB  GLU A  65     1382   2260   1085    493    109    578       C  
ATOM   1212  CG  GLU A  65       6.604  40.770   5.852  1.00 20.16           C  
ANISOU 1212  CG  GLU A  65     1794   3773   1636   1252    280    871       C  
ATOM   1213  CD  GLU A  65       5.660  41.440   4.849  1.00 34.70           C  
ANISOU 1213  CD  GLU A  65     3270   6386   2743   2725    -62   1845       C  
ATOM   1214  OE1 GLU A  65       5.877  41.365   3.626  1.00 48.98           O  
ANISOU 1214  OE1 GLU A  65     4828  10135   2537   3963   -100   2645       O  
ATOM   1215  OE2 GLU A  65       4.798  42.121   5.292  1.00 48.89           O  
ANISOU 1215  OE2 GLU A  65     4557   9238   3674   4610   -504   1346       O  
ATOM   1216  H  AGLU A  65      10.021  38.898   4.723  1.00 11.80           H  
ATOM   1217  HA  GLU A  65       8.967  40.267   6.833  1.00 12.43           H  
ATOM   1218  HB2 GLU A  65       8.205  40.627   4.553  1.00 15.88           H  
ATOM   1219  HB3 GLU A  65       7.418  39.275   4.681  1.00 15.88           H  
ATOM   1220  HG2 GLU A  65       6.098  40.141   6.390  1.00 24.19           H  
ATOM   1221  HG3 GLU A  65       6.963  41.447   6.447  1.00 24.19           H  
ATOM   1222  N   ILE A  66       8.065  38.500   8.273  1.00  8.97           N  
ANISOU 1222  N   ILE A  66     1230   1092    881    168     39    111       N  
ATOM   1223  CA  ILE A  66       7.683  37.400   9.144  1.00  8.61           C  
ANISOU 1223  CA  ILE A  66     1253   1015    809    231     36     91       C  
ATOM   1224  C   ILE A  66       6.350  37.764   9.734  1.00  9.37           C  
ANISOU 1224  C   ILE A  66     1219   1144    987    199     77    -42       C  
ATOM   1225  O   ILE A  66       6.252  38.714  10.538  1.00 10.20           O  
ANISOU 1225  O   ILE A  66     1515   1097   1033    311    191    -14       O  
ATOM   1226  CB  ILE A  66       8.724  37.218  10.268  1.00  9.09           C  
ANISOU 1226  CB  ILE A  66     1352    991    907    122     -6     69       C  
ATOM   1227  CG1 ILE A  66      10.117  36.937   9.683  1.00  9.30           C  
ANISOU 1227  CG1 ILE A  66     1296   1075    954    165    -45     21       C  
ATOM   1228  CG2 ILE A  66       8.290  36.162  11.244  1.00  9.69           C  
ANISOU 1228  CG2 ILE A  66     1566   1020    875    -74   -234     52       C  
ATOM   1229  CD1 ILE A  66      11.260  37.272  10.584  1.00 10.54           C  
ANISOU 1229  CD1 ILE A  66     1506   1116   1144   -118   -379    223       C  
ATOM   1230  H   ILE A  66       8.158  39.283   8.617  1.00 10.76           H  
ATOM   1231  HA  ILE A  66       7.604  36.574   8.624  1.00 10.33           H  
ATOM   1232  HB  ILE A  66       8.778  38.066  10.757  1.00 10.91           H  
ATOM   1233 HG12 ILE A  66      10.171  35.996   9.454  1.00 11.16           H  
ATOM   1234 HG13 ILE A  66      10.214  37.443   8.861  1.00 11.16           H  
ATOM   1235 HG21 ILE A  66       7.418  36.378  11.583  1.00 14.53           H  
ATOM   1236 HG22 ILE A  66       8.259  35.311  10.802  1.00 14.53           H  
ATOM   1237 HG23 ILE A  66       8.915  36.123  11.972  1.00 14.53           H  
ATOM   1238 HD11 ILE A  66      12.087  37.066  10.142  1.00 15.81           H  
ATOM   1239 HD12 ILE A  66      11.236  38.207  10.797  1.00 15.81           H  
ATOM   1240 HD13 ILE A  66      11.192  36.757  11.392  1.00 15.81           H  
ATOM   1241  N   ALA A  67       5.310  37.039   9.381  1.00 10.14           N  
ANISOU 1241  N   ALA A  67     1190   1192   1242    163    144    -67       N  
ATOM   1242  CA  ALA A  67       3.958  37.320   9.888  1.00 12.45           C  
ANISOU 1242  CA  ALA A  67     1344   1454   1650    123    391    -84       C  
ATOM   1243  C   ALA A  67       3.636  38.793   9.724  1.00 12.23           C  
ANISOU 1243  C   ALA A  67     1274   1451   1644    120    229     -7       C  
ATOM   1244  O   ALA A  67       3.033  39.408  10.627  1.00 14.79           O  
ANISOU 1244  O   ALA A  67     1504   1664   2116    390    537   -136       O  
ATOM   1245  CB  ALA A  67       3.804  36.860  11.320  1.00 15.38           C  
ANISOU 1245  CB  ALA A  67     2185   1384   1924    131   1042    136       C  
ATOM   1246  H   ALA A  67       5.425  36.381   8.839  1.00 12.17           H  
ATOM   1247  HA  ALA A  67       3.322  36.812   9.342  1.00 14.94           H  
ATOM   1248  HB1 ALA A  67       2.915  37.054  11.625  1.00 23.06           H  
ATOM   1249  HB2 ALA A  67       3.960  35.914  11.371  1.00 23.06           H  
ATOM   1250  HB3 ALA A  67       4.440  37.319  11.874  1.00 23.06           H  
ATOM   1251  N   GLY A  68       4.027  39.369   8.583  1.00 12.70           N  
ANISOU 1251  N   GLY A  68     1277   1608   1653    185     26    106       N  
ATOM   1252  CA  GLY A  68       3.669  40.839   8.340  1.00 14.55           C  
ANISOU 1252  CA  GLY A  68     1112   2045   2041    269   -276    551       C  
ATOM   1253  C   GLY A  68       4.672  41.797   8.837  1.00 13.40           C  
ANISOU 1253  C   GLY A  68     1357   1489   1942    351    -16    511       C  
ATOM   1254  O   GLY A  68       4.458  42.999   8.645  1.00 18.52           O  
ANISOU 1254  O   GLY A  68     2096   1596   2925    653   -459    668       O  
ATOM   1255  H   GLY A  68       4.472  38.923   7.997  1.00 15.24           H  
ATOM   1256  HA2 GLY A  68       3.553  40.977   7.387  1.00 17.46           H  
ATOM   1257  HA3 GLY A  68       2.820  41.027   8.770  1.00 17.46           H  
ATOM   1258  N   HIS A  69       5.718  41.390   9.547  1.00 10.91           N  
ANISOU 1258  N   HIS A  69     1135   1272   1492    382     22    157       N  
ATOM   1259  CA  HIS A  69       6.708  42.311  10.145  1.00 11.03           C  
ANISOU 1259  CA  HIS A  69     1235   1249   1459    264    142    187       C  
ATOM   1260  C   HIS A  69       8.030  42.165   9.374  1.00 10.29           C  
ANISOU 1260  C   HIS A  69     1173   1269   1233    271     15    119       C  
ATOM   1261  O   HIS A  69       8.590  41.099   9.284  1.00 11.08           O  
ANISOU 1261  O   HIS A  69     1179   1381   1398    290    107   -148       O  
ATOM   1262  CB  HIS A  69       6.945  41.935  11.627  1.00 11.46           C  
ANISOU 1262  CB  HIS A  69     1499   1292   1305    405    122     38       C  
ATOM   1263  CG  HIS A  69       5.801  42.209  12.510  1.00 12.81           C  
ANISOU 1263  CG  HIS A  69     1701   1378   1497    494    331    260       C  
ATOM   1264  ND1 HIS A  69       4.560  41.666  12.584  1.00 17.30           N  
ANISOU 1264  ND1 HIS A  69     1892   2195   2092    444    611    617       N  
ATOM   1265  CD2 HIS A  69       5.796  43.181  13.465  1.00 15.83           C  
ANISOU 1265  CD2 HIS A  69     2630   1469   1559    782    679    223       C  
ATOM   1266  CE1 HIS A  69       3.787  42.255  13.488  1.00 21.47           C  
ANISOU 1266  CE1 HIS A  69     2314   2520   2839    923   1492   1070       C  
ATOM   1267  NE2 HIS A  69       4.540  43.191  14.005  1.00 21.16           N  
ANISOU 1267  NE2 HIS A  69     3038   2783   1741   1372   1098    540       N  
ATOM   1268  H   HIS A  69       5.826  40.545   9.665  1.00 13.09           H  
ATOM   1269  HA  HIS A  69       6.385  43.234  10.082  1.00 13.24           H  
ATOM   1270  HB2 HIS A  69       7.157  40.990  11.678  1.00 13.75           H  
ATOM   1271  HB3 HIS A  69       7.714  42.427  11.954  1.00 13.75           H  
ATOM   1272  HD1 HIS A  69       4.300  41.008  12.095  1.00 20.75           H  
ATOM   1273  HD2 HIS A  69       6.508  43.730  13.703  1.00 19.00           H  
ATOM   1274  HE1 HIS A  69       2.907  42.048  13.705  1.00 25.77           H  
ATOM   1275  N   LYS A  70       8.504  43.291   8.847  1.00 13.14           N  
ANISOU 1275  N   LYS A  70     1254   1592   1849    442    325    374       N  
ATOM   1276  CA  LYS A  70       9.757  43.299   8.075  1.00 14.08           C  
ANISOU 1276  CA  LYS A  70     1206   2274   1551    219    131    410       C  
ATOM   1277  C   LYS A  70      10.979  43.392   8.990  1.00 12.59           C  
ANISOU 1277  C   LYS A  70     1260   1775   1466    221     93   -178       C  
ATOM   1278  O   LYS A  70      11.011  44.040  10.047  1.00 14.10           O  
ANISOU 1278  O   LYS A  70     1425   1867   1747    324    300   -432       O  
ATOM   1279  CB  LYS A  70       9.740  44.479   7.097  1.00 19.05           C  
ANISOU 1279  CB  LYS A  70     1826   3018   1964    -17    249    979       C  
ATOM   1280  CG  LYS A  70       8.638  44.372   6.026  1.00 27.13           C  
ANISOU 1280  CG  LYS A  70     2665   4262   2768   -463   -502   2210       C  
ATOM   1281  CD  LYS A  70       8.421  45.627   5.153  1.00 37.76           C  
ANISOU 1281  CD  LYS A  70     4580   4218   4693    836   -995   2520       C  
ATOM   1282  CE  LYS A  70       6.998  45.747   4.579  1.00 40.19           C  
ANISOU 1282  CE  LYS A  70     4710   4878   4773    515  -1214   2866       C  
ATOM   1283  NZ  LYS A  70       6.852  46.518   3.322  1.00 60.73           N  
ANISOU 1283  NZ  LYS A  70     6054  10962   4683   1441   -896   4577       N  
ATOM   1284  H   LYS A  70       8.071  44.026   8.958  1.00 15.77           H  
ATOM   1285  HA  LYS A  70       9.814  42.467   7.560  1.00 16.90           H  
ATOM   1286  HB2 LYS A  70       9.612  45.300   7.598  1.00 22.86           H  
ATOM   1287  HB3 LYS A  70      10.602  44.534   6.656  1.00 22.86           H  
ATOM   1288  HG2 LYS A  70       8.852  43.628   5.441  1.00 32.56           H  
ATOM   1289  HG3 LYS A  70       7.801  44.162   6.469  1.00 32.56           H  
ATOM   1290  HD2 LYS A  70       8.610  46.415   5.687  1.00 45.31           H  
ATOM   1291  HD3 LYS A  70       9.054  45.610   4.419  1.00 45.31           H  
ATOM   1292  HE2 LYS A  70       6.658  44.851   4.426  1.00 48.23           H  
ATOM   1293  HE3 LYS A  70       6.434  46.158   5.253  1.00 48.23           H  
ATOM   1294  HZ1 LYS A  70       5.997  46.526   3.076  1.00 91.09           H  
ATOM   1295  HZ2 LYS A  70       7.132  47.353   3.452  1.00 91.09           H  
ATOM   1296  HZ3 LYS A  70       7.340  46.137   2.682  1.00 91.09           H  
ATOM   1297  N  AALA A  71      11.981  42.501   8.681  0.46 12.27           N  
ANISOU 1297  N  AALA A  71      997   2470    917    204    231   -356       N  
ATOM   1298  N  BALA A  71      12.063  42.902   8.405  0.54  9.51           N  
ANISOU 1298  N  BALA A  71     1144   1318    935     74    151    135       N  
ATOM   1299  CA AALA A  71      13.261  42.354   9.373  0.46 11.63           C  
ANISOU 1299  CA AALA A  71     1099   2004   1053    168    148   -470       C  
ATOM   1300  CA BALA A  71      13.312  42.988   9.129  0.54  8.24           C  
ANISOU 1300  CA BALA A  71     1167    812    964    117    131     -5       C  
ATOM   1301  C  AALA A  71      14.413  42.118   8.377  0.46  9.72           C  
ANISOU 1301  C  AALA A  71     1037   1636    801    364    -83   -282       C  
ATOM   1302  C  BALA A  71      14.391  42.695   8.087  0.54  7.10           C  
ANISOU 1302  C  BALA A  71     1104    685    748    159     31    149       C  
ATOM   1303  O  AALA A  71      14.195  41.433   7.394  0.46 12.38           O  
ANISOU 1303  O  AALA A  71     1127   1939   1359     -7    215   -756       O  
ATOM   1304  O  BALA A  71      14.148  42.377   6.963  0.54  8.01           O  
ANISOU 1304  O  BALA A  71     1104    906    851     45    108    -35       O  
ATOM   1305  CB AALA A  71      13.265  41.194  10.389  0.46 11.41           C  
ANISOU 1305  CB AALA A  71      939   2102   1035     -4    111   -469       C  
ATOM   1306  CB BALA A  71      13.379  41.985  10.275  0.54  8.80           C  
ANISOU 1306  CB BALA A  71     1448    873    824     16    122    -29       C  
ATOM   1307  H  AALA A  71      11.841  41.977   8.014  0.46 14.72           H  
ATOM   1308  H  BALA A  71      12.026  42.547   7.623  0.54 11.41           H  
ATOM   1309  HA AALA A  71      13.443  43.185   9.858  0.46 13.96           H  
ATOM   1310  HA BALA A  71      13.429  43.896   9.478  0.54  9.88           H  
ATOM   1311  HB1AALA A  71      14.125  41.143  10.812  0.46 17.11           H  
ATOM   1312  HB1BALA A  71      14.220  42.074  10.729  0.54 13.20           H  
ATOM   1313  HB2AALA A  71      12.590  41.349  11.054  0.46 17.11           H  
ATOM   1314  HB2BALA A  71      12.663  42.156  10.892  0.54 13.20           H  
ATOM   1315  HB3AALA A  71      13.082  40.369   9.934  0.46 17.11           H  
ATOM   1316  HB3BALA A  71      13.296  41.095   9.927  0.54 13.20           H  
ATOM   1317  N   ILE A  72      15.613  42.650   8.631  1.00  9.18           N  
ANISOU 1317  N   ILE A  72     1088   1240    952    318     -7   -252       N  
ATOM   1318  CA  ILE A  72      16.785  42.323   7.827  1.00  8.21           C  
ANISOU 1318  CA  ILE A  72     1103    913    918    214    -10    -96       C  
ATOM   1319  C   ILE A  72      17.793  41.610   8.698  1.00  7.23           C  
ANISOU 1319  C   ILE A  72     1069    637    876     87     60    -30       C  
ATOM   1320  O   ILE A  72      17.938  41.946   9.893  1.00  8.08           O  
ANISOU 1320  O   ILE A  72     1332    661    894    156     30    -25       O  
ATOM   1321  CB  ILE A  72      17.376  43.573   7.143  1.00  9.81           C  
ANISOU 1321  CB  ILE A  72     1630    840   1037    405    150    129       C  
ATOM   1322  CG1 ILE A  72      18.455  43.243   6.126  1.00 10.42           C  
ANISOU 1322  CG1 ILE A  72     1581    913   1228    232    281    191       C  
ATOM   1323  CG2 ILE A  72      17.838  44.601   8.137  1.00 13.70           C  
ANISOU 1323  CG2 ILE A  72     2668    898   1330   -100    412     52       C  
ATOM   1324  CD1 ILE A  72      18.881  44.406   5.247  1.00 13.81           C  
ANISOU 1324  CD1 ILE A  72     2446   1086   1403    261    470    367       C  
ATOM   1325  H  AILE A  72      15.696  43.201   9.287  1.00 11.02           H  
ATOM   1326  HA  ILE A  72      16.502  41.701   7.125  1.00  9.85           H  
ATOM   1327  HB  ILE A  72      16.642  43.985   6.641  1.00 11.78           H  
ATOM   1328 HG12 ILE A  72      19.234  42.912   6.599  1.00 12.50           H  
ATOM   1329 HG13 ILE A  72      18.133  42.527   5.555  1.00 12.50           H  
ATOM   1330 HG21 ILE A  72      17.132  44.783   8.761  1.00 20.55           H  
ATOM   1331 HG22 ILE A  72      18.604  44.267   8.610  1.00 20.55           H  
ATOM   1332 HG23 ILE A  72      18.074  45.409   7.676  1.00 20.55           H  
ATOM   1333 HD11 ILE A  72      19.562  44.113   4.637  1.00 20.71           H  
ATOM   1334 HD12 ILE A  72      18.124  44.727   4.752  1.00 20.71           H  
ATOM   1335 HD13 ILE A  72      19.227  45.112   5.797  1.00 20.71           H  
ATOM   1336  N   GLY A  73      18.479  40.644   8.130  1.00  7.20           N  
ANISOU 1336  N   GLY A  73     1082    672    821     57     42     28       N  
ATOM   1337  CA  GLY A  73      19.546  39.989   8.874  1.00  7.61           C  
ANISOU 1337  CA  GLY A  73     1227    676    817    198     -2     24       C  
ATOM   1338  C   GLY A  73      20.141  38.854   8.076  1.00  7.02           C  
ANISOU 1338  C   GLY A  73     1150    618    740     62     47     24       C  
ATOM   1339  O   GLY A  73      19.908  38.697   6.874  1.00  8.06           O  
ANISOU 1339  O   GLY A  73     1346    799    735    224    -25    -24       O  
ATOM   1340  H   GLY A  73      18.300  40.401   7.325  1.00  8.64           H  
ATOM   1341  HA2 GLY A  73      20.239  40.636   9.082  1.00  9.13           H  
ATOM   1342  HA3 GLY A  73      19.194  39.647   9.710  1.00  9.13           H  
ATOM   1343  N   THR A  74      20.969  38.081   8.763  1.00  7.04           N  
ANISOU 1343  N   THR A  74     1220    568    728    103     52     44       N  
ATOM   1344  CA  THR A  74      21.597  36.932   8.145  1.00  6.67           C  
ANISOU 1344  CA  THR A  74     1070    641    674     80     53     28       C  
ATOM   1345  C   THR A  74      20.575  35.792   8.022  1.00  6.03           C  
ANISOU 1345  C   THR A  74      959    609    586    100     65     92       C  
ATOM   1346  O   THR A  74      19.811  35.517   8.972  1.00  7.12           O  
ANISOU 1346  O   THR A  74     1165    777    603     16    155     46       O  
ATOM   1347  CB  THR A  74      22.791  36.490   8.995  1.00  7.57           C  
ANISOU 1347  CB  THR A  74      993    763    949     78    -10     17       C  
ATOM   1348  OG1 THR A  74      23.744  37.555   8.955  1.00 10.18           O  
ANISOU 1348  OG1 THR A  74     1155    996   1488    -15   -227    -85       O  
ATOM   1349  CG2 THR A  74      23.399  35.193   8.544  1.00  8.30           C  
ANISOU 1349  CG2 THR A  74     1081    867   1017    148    -10     43       C  
ATOM   1350  H   THR A  74      21.136  38.265   9.586  1.00  8.45           H  
ATOM   1351  HA  THR A  74      21.913  37.179   7.251  1.00  8.01           H  
ATOM   1352  HB  THR A  74      22.487  36.383   9.921  1.00  9.08           H  
ATOM   1353  HG1 THR A  74      24.460  37.270   8.675  1.00 15.28           H  
ATOM   1354 HG21 THR A  74      22.737  34.499   8.582  1.00 12.45           H  
ATOM   1355 HG22 THR A  74      23.715  35.284   7.643  1.00 12.45           H  
ATOM   1356 HG23 THR A  74      24.133  34.967   9.120  1.00 12.45           H  
ATOM   1357  N   VAL A  75      20.594  35.124   6.885  1.00  6.02           N  
ANISOU 1357  N   VAL A  75      980    588    583     39    160     86       N  
ATOM   1358  CA  VAL A  75      19.758  33.957   6.637  1.00  5.88           C  
ANISOU 1358  CA  VAL A  75      942    594    567     40    153    111       C  
ATOM   1359  C   VAL A  75      20.670  32.838   6.161  1.00  5.47           C  
ANISOU 1359  C   VAL A  75      801    612    540     50    118    101       C  
ATOM   1360  O   VAL A  75      21.471  33.022   5.231  1.00  6.56           O  
ANISOU 1360  O   VAL A  75     1008    680    656     57    280    139       O  
ATOM   1361  CB  VAL A  75      18.641  34.255   5.627  1.00  6.69           C  
ANISOU 1361  CB  VAL A  75      956    769    667    108    151    163       C  
ATOM   1362  CG1 VAL A  75      17.870  32.983   5.294  1.00  7.52           C  
ANISOU 1362  CG1 VAL A  75     1008    906    774     84    -32     34       C  
ATOM   1363  CG2 VAL A  75      17.725  35.328   6.186  1.00  7.76           C  
ANISOU 1363  CG2 VAL A  75      953    814   1004    172     95    202       C  
ATOM   1364  H   VAL A  75      21.124  35.389   6.262  1.00  7.22           H  
ATOM   1365  HA  VAL A  75      19.346  33.683   7.483  1.00  7.06           H  
ATOM   1366  HB  VAL A  75      19.050  34.595   4.804  1.00  8.03           H  
ATOM   1367 HG11 VAL A  75      18.475  32.325   4.943  1.00 11.28           H  
ATOM   1368 HG12 VAL A  75      17.454  32.643   6.089  1.00 11.28           H  
ATOM   1369 HG13 VAL A  75      17.196  33.179   4.639  1.00 11.28           H  
ATOM   1370 HG21 VAL A  75      18.237  36.115   6.386  1.00 11.64           H  
ATOM   1371 HG22 VAL A  75      17.050  35.542   5.538  1.00 11.64           H  
ATOM   1372 HG23 VAL A  75      17.307  35.006   6.989  1.00 11.64           H  
ATOM   1373  N   LEU A  76      20.542  31.677   6.797  1.00  5.17           N  
ANISOU 1373  N   LEU A  76      750    605    492     39    122     62       N  
ATOM   1374  CA  LEU A  76      21.256  30.490   6.431  1.00  5.10           C  
ANISOU 1374  CA  LEU A  76      681    598    545     -6    107     34       C  
ATOM   1375  C   LEU A  76      20.359  29.622   5.548  1.00  5.05           C  
ANISOU 1375  C   LEU A  76      748    589    468    -10    113     72       C  
ATOM   1376  O   LEU A  76      19.139  29.574   5.762  1.00  5.82           O  
ANISOU 1376  O   LEU A  76      757    779    543    -37    125    -27       O  
ATOM   1377  CB  LEU A  76      21.645  29.690   7.684  1.00  5.14           C  
ANISOU 1377  CB  LEU A  76      719    580    537      5     83     37       C  
ATOM   1378  CG  LEU A  76      22.328  30.525   8.779  1.00  5.38           C  
ANISOU 1378  CG  LEU A  76      700    603    618     15     14     42       C  
ATOM   1379  CD1 LEU A  76      22.644  29.625   9.974  1.00  6.02           C  
ANISOU 1379  CD1 LEU A  76      784    741    625     52    -17     71       C  
ATOM   1380  CD2 LEU A  76      23.586  31.220   8.276  1.00  7.09           C  
ANISOU 1380  CD2 LEU A  76      887    841    806   -175    -17    133       C  
ATOM   1381  H   LEU A  76      20.002  31.637   7.464  1.00  6.20           H  
ATOM   1382  HA  LEU A  76      22.064  30.734   5.935  1.00  6.12           H  
ATOM   1383  HB2 LEU A  76      20.846  29.284   8.055  1.00  6.17           H  
ATOM   1384  HB3 LEU A  76      22.244  28.973   7.421  1.00  6.17           H  
ATOM   1385  HG  LEU A  76      21.697  31.214   9.074  1.00  6.45           H  
ATOM   1386 HD11 LEU A  76      21.838  29.198  10.274  1.00  9.02           H  
ATOM   1387 HD12 LEU A  76      23.282  28.958   9.713  1.00  9.02           H  
ATOM   1388 HD13 LEU A  76      23.008  30.156  10.686  1.00  9.02           H  
ATOM   1389 HD21 LEU A  76      23.366  31.779   7.527  1.00 10.64           H  
ATOM   1390 HD22 LEU A  76      23.956  31.759   8.979  1.00 10.64           H  
ATOM   1391 HD23 LEU A  76      24.230  30.561   8.006  1.00 10.64           H  
ATOM   1392  N   VAL A  77      20.968  28.927   4.576  1.00  5.37           N  
ANISOU 1392  N   VAL A  77      721    711    487     43     63     33       N  
ATOM   1393  CA  VAL A  77      20.220  28.087   3.652  1.00  5.44           C  
ANISOU 1393  CA  VAL A  77      795    723    426     57     72     28       C  
ATOM   1394  C   VAL A  77      20.850  26.718   3.614  1.00  5.67           C  
ANISOU 1394  C   VAL A  77      868    775    383     35     71     -2       C  
ATOM   1395  O   VAL A  77      22.060  26.590   3.389  1.00  5.98           O  
ANISOU 1395  O   VAL A  77      777    776    583     70    132     23       O  
ATOM   1396  CB  VAL A  77      20.187  28.711   2.238  1.00  6.41           C  
ANISOU 1396  CB  VAL A  77      977    865    447    108     69     88       C  
ATOM   1397  CG1 VAL A  77      19.451  27.800   1.276  1.00  7.33           C  
ANISOU 1397  CG1 VAL A  77     1205    987    428     13    -44     27       C  
ATOM   1398  CG2 VAL A  77      19.532  30.078   2.278  1.00  7.32           C  
ANISOU 1398  CG2 VAL A  77     1145    902    568    128     73    167       C  
ATOM   1399  H   VAL A  77      21.823  28.978   4.496  1.00  6.44           H  
ATOM   1400  HA  VAL A  77      19.300  28.001   3.979  1.00  6.53           H  
ATOM   1401  HB  VAL A  77      21.109  28.816   1.922  1.00  7.69           H  
ATOM   1402 HG11 VAL A  77      19.876  26.939   1.262  1.00 11.00           H  
ATOM   1403 HG12 VAL A  77      18.540  27.702   1.563  1.00 11.00           H  
ATOM   1404 HG13 VAL A  77      19.470  28.182   0.396  1.00 11.00           H  
ATOM   1405 HG21 VAL A  77      20.009  30.643   2.890  1.00 10.98           H  
ATOM   1406 HG22 VAL A  77      19.552  30.468   1.401  1.00 10.98           H  
ATOM   1407 HG23 VAL A  77      18.622  29.988   2.568  1.00 10.98           H  
ATOM   1408  N   GLY A  78      20.060  25.657   3.802  1.00  5.63           N  
ANISOU 1408  N   GLY A  78      787    724    500     59     53      3       N  
ATOM   1409  CA  GLY A  78      20.592  24.326   3.742  1.00  6.31           C  
ANISOU 1409  CA  GLY A  78      889    751    615     61     79      9       C  
ATOM   1410  C   GLY A  78      19.563  23.309   4.146  1.00  6.06           C  
ANISOU 1410  C   GLY A  78      890    757    517     34    -40    -62       C  
ATOM   1411  O   GLY A  78      18.366  23.607   4.167  1.00  6.80           O  
ANISOU 1411  O   GLY A  78      825    845    758     53    -23    -32       O  
ATOM   1412  H   GLY A  78      19.222  25.774   3.960  1.00  6.76           H  
ATOM   1413  HA2 GLY A  78      20.892  24.139   2.839  1.00  7.57           H  
ATOM   1414  HA3 GLY A  78      21.359  24.260   4.332  1.00  7.57           H  
ATOM   1415  N   PRO A  79      20.026  22.087   4.440  1.00  6.32           N  
ANISOU 1415  N   PRO A  79      834    687    737     29     -8   -106       N  
ATOM   1416  CA  PRO A  79      19.092  20.938   4.575  1.00  7.16           C  
ANISOU 1416  CA  PRO A  79     1047    690    821    -24      9   -154       C  
ATOM   1417  C   PRO A  79      18.472  20.839   5.956  1.00  7.40           C  
ANISOU 1417  C   PRO A  79     1015    653    975    -97     96    -83       C  
ATOM   1418  O   PRO A  79      18.565  19.858   6.674  1.00 10.26           O  
ANISOU 1418  O   PRO A  79     1635    737   1294     53    522     77       O  
ATOM   1419  CB  PRO A  79      20.001  19.748   4.216  1.00  8.23           C  
ANISOU 1419  CB  PRO A  79     1188    698   1054      8    154   -176       C  
ATOM   1420  CG  PRO A  79      21.357  20.167   4.744  1.00  8.02           C  
ANISOU 1420  CG  PRO A  79     1061    803   1001    126    114    -48       C  
ATOM   1421  CD  PRO A  79      21.433  21.645   4.396  1.00  6.93           C  
ANISOU 1421  CD  PRO A  79      897    769    810     90     44    -92       C  
ATOM   1422  HA  PRO A  79      18.381  21.017   3.905  1.00  8.59           H  
ATOM   1423  HB2 PRO A  79      19.696  18.934   4.646  1.00  9.87           H  
ATOM   1424  HB3 PRO A  79      20.029  19.608   3.257  1.00  9.87           H  
ATOM   1425  HG2 PRO A  79      21.415  20.031   5.703  1.00  9.62           H  
ATOM   1426  HG3 PRO A  79      22.068  19.670   4.310  1.00  9.62           H  
ATOM   1427  HD2 PRO A  79      21.969  22.127   5.045  1.00  8.31           H  
ATOM   1428  HD3 PRO A  79      21.811  21.775   3.513  1.00  8.31           H  
ATOM   1429  N   THR A  80      17.806  21.916   6.359  1.00  7.35           N  
ANISOU 1429  N   THR A  80     1005    790    833     77     61    -89       N  
ATOM   1430  CA  THR A  80      17.050  21.921   7.605  1.00  6.74           C  
ANISOU 1430  CA  THR A  80      948    784    676    -16    -20     -7       C  
ATOM   1431  C   THR A  80      15.727  21.183   7.437  1.00  7.32           C  
ANISOU 1431  C   THR A  80     1028    789    800      2    -29    -66       C  
ATOM   1432  O   THR A  80      15.068  21.358   6.399  1.00  8.51           O  
ANISOU 1432  O   THR A  80     1160   1037    844   -216   -109   -204       O  
ATOM   1433  CB  THR A  80      16.805  23.366   8.094  1.00  6.29           C  
ANISOU 1433  CB  THR A  80      897    785    567    -29     -9     11       C  
ATOM   1434  OG1 THR A  80      16.080  23.247   9.307  1.00  6.72           O  
ANISOU 1434  OG1 THR A  80      920    918    563     39    -17     40       O  
ATOM   1435  CG2 THR A  80      16.100  24.259   7.078  1.00  6.38           C  
ANISOU 1435  CG2 THR A  80     1000    722    558     -6    -63     10       C  
ATOM   1436  H   THR A  80      17.822  22.626   5.875  1.00  8.83           H  
ATOM   1437  HA  THR A  80      17.578  21.453   8.286  1.00  8.09           H  
ATOM   1438  HB  THR A  80      17.674  23.768   8.299  1.00  7.55           H  
ATOM   1439  HG1 THR A  80      15.388  23.684   9.256  1.00 10.08           H  
ATOM   1440 HG21 THR A  80      16.626  24.309   6.277  1.00  9.57           H  
ATOM   1441 HG22 THR A  80      15.237  23.891   6.873  1.00  9.57           H  
ATOM   1442 HG23 THR A  80      15.992  25.139   7.446  1.00  9.57           H  
ATOM   1443  N   PRO A  81      15.283  20.420   8.412  1.00  8.15           N  
ANISOU 1443  N   PRO A  81     1117    705   1090    -84      7     10       N  
ATOM   1444  CA  PRO A  81      14.012  19.722   8.268  1.00  9.02           C  
ANISOU 1444  CA  PRO A  81     1190    738   1296   -165      3    -32       C  
ATOM   1445  C   PRO A  81      12.800  20.643   8.325  1.00  8.50           C  
ANISOU 1445  C   PRO A  81     1230    702   1105   -161    -75    -50       C  
ATOM   1446  O   PRO A  81      11.714  20.224   7.903  1.00 11.59           O  
ANISOU 1446  O   PRO A  81     1263    970   1909   -228   -349   -164       O  
ATOM   1447  CB  PRO A  81      14.020  18.705   9.422  1.00 11.00           C  
ANISOU 1447  CB  PRO A  81     1388    807   1736     -9    373    275       C  
ATOM   1448  CG  PRO A  81      14.994  19.227  10.344  1.00 18.00           C  
ANISOU 1448  CG  PRO A  81     2120   2027   2286   -757   -500   1377       C  
ATOM   1449  CD  PRO A  81      15.982  20.041   9.644  1.00  9.86           C  
ANISOU 1449  CD  PRO A  81     1343    970   1209    -22   -143    330       C  
ATOM   1450  HA  PRO A  81      14.007  19.239   7.415  1.00 10.82           H  
ATOM   1451  HB2 PRO A  81      13.146  18.647   9.838  1.00 13.20           H  
ATOM   1452  HB3 PRO A  81      14.278  17.825   9.106  1.00 13.20           H  
ATOM   1453  HG2 PRO A  81      14.548  19.765  11.016  1.00 21.60           H  
ATOM   1454  HG3 PRO A  81      15.440  18.492  10.793  1.00 21.60           H  
ATOM   1455  HD2 PRO A  81      16.223  20.823  10.165  1.00 11.83           H  
ATOM   1456  HD3 PRO A  81      16.783  19.530   9.449  1.00 11.83           H  
ATOM   1457  N   VAL A  82      12.947  21.809   8.911  1.00  7.79           N  
ANISOU 1457  N   VAL A  82     1129    696    958   -156    -36    -23       N  
ATOM   1458  CA  VAL A  82      11.910  22.775   9.134  1.00  8.07           C  
ANISOU 1458  CA  VAL A  82      972    814   1098   -136     95    -38       C  
ATOM   1459  C   VAL A  82      12.504  24.169   8.881  1.00  6.54           C  
ANISOU 1459  C   VAL A  82      917    728    693    -71     56    -76       C  
ATOM   1460  O   VAL A  82      13.617  24.418   9.302  1.00  6.86           O  
ANISOU 1460  O   VAL A  82      870    727    852    -11    -81    -50       O  
ATOM   1461  CB  VAL A  82      11.395  22.702  10.638  1.00 10.39           C  
ANISOU 1461  CB  VAL A  82     1273   1077   1361   -125    379    290       C  
ATOM   1462  CG1 VAL A  82      10.377  23.741  10.979  1.00 10.13           C  
ANISOU 1462  CG1 VAL A  82     1531   1089    998   -139    333     16       C  
ATOM   1463  CG2 VAL A  82      10.800  21.302  10.880  1.00 14.25           C  
ANISOU 1463  CG2 VAL A  82     1879    993   2221     12    944    366       C  
ATOM   1464  H   VAL A  82      13.736  22.012   9.186  1.00  9.35           H  
ATOM   1465  HA  VAL A  82      11.165  22.613   8.519  1.00  9.68           H  
ATOM   1466  HB  VAL A  82      12.165  22.817  11.234  1.00 12.46           H  
ATOM   1467 HG11 VAL A  82      10.748  24.614  10.829  1.00 15.19           H  
ATOM   1468 HG12 VAL A  82       9.602  23.623  10.426  1.00 15.19           H  
ATOM   1469 HG13 VAL A  82      10.128  23.654  11.902  1.00 15.19           H  
ATOM   1470 HG21 VAL A  82      11.455  20.634  10.661  1.00 21.38           H  
ATOM   1471 HG22 VAL A  82      10.551  21.215  11.803  1.00 21.38           H  
ATOM   1472 HG23 VAL A  82      10.025  21.184  10.326  1.00 21.38           H  
ATOM   1473  N   ASN A  83      11.762  25.074   8.242  1.00  6.23           N  
ANISOU 1473  N   ASN A  83      779    795    650   -141    -26   -107       N  
ATOM   1474  CA  ASN A  83      12.235  26.446   8.137  1.00  5.50           C  
ANISOU 1474  CA  ASN A  83      695    763    508    -54    -10    -62       C  
ATOM   1475  C   ASN A  83      12.133  27.103   9.508  1.00  5.22           C  
ANISOU 1475  C   ASN A  83      654    708    502     -3    -32     -5       C  
ATOM   1476  O   ASN A  83      11.073  27.034  10.139  1.00  6.05           O  
ANISOU 1476  O   ASN A  83      634   1028    498    -42     34    -59       O  
ATOM   1477  CB  ASN A  83      11.391  27.222   7.141  1.00  6.01           C  
ANISOU 1477  CB  ASN A  83      790    901    458    -10    -24    -51       C  
ATOM   1478  CG  ASN A  83      11.445  26.643   5.739  1.00  6.53           C  
ANISOU 1478  CG  ASN A  83      818   1008    506      9    -36    -58       C  
ATOM   1479  OD1 ASN A  83      12.512  26.240   5.271  1.00  8.99           O  
ANISOU 1479  OD1 ASN A  83      828   1744    640    -20      0   -413       O  
ATOM   1480  ND2 ASN A  83      10.313  26.661   5.059  1.00  7.68           N  
ANISOU 1480  ND2 ASN A  83      970   1288    486     34   -140   -147       N  
ATOM   1481  H   ASN A  83      11.009  24.849   7.894  1.00  7.47           H  
ATOM   1482  HA  ASN A  83      13.170  26.447   7.843  1.00  6.60           H  
ATOM   1483  HB2 ASN A  83      10.470  27.228   7.445  1.00  7.22           H  
ATOM   1484  HB3 ASN A  83      11.700  28.142   7.115  1.00  7.22           H  
ATOM   1485 HD21 ASN A  83      10.295  26.382   4.245  1.00  9.22           H  
ATOM   1486 HD22 ASN A  83       9.593  26.952   5.429  1.00  9.22           H  
ATOM   1487  N   ILE A  84      13.226  27.703   9.970  1.00  4.85           N  
ANISOU 1487  N   ILE A  84      678    642    412    -58     40    -47       N  
ATOM   1488  CA  ILE A  84      13.343  28.182  11.350  1.00  4.91           C  
ANISOU 1488  CA  ILE A  84      710    643    404    -69     51    -29       C  
ATOM   1489  C   ILE A  84      13.690  29.661  11.358  1.00  4.76           C  
ANISOU 1489  C   ILE A  84      665    611    423    -19     14    -42       C  
ATOM   1490  O   ILE A  84      14.704  30.078  10.783  1.00  5.51           O  
ANISOU 1490  O   ILE A  84      740    669    559    -71    145    -28       O  
ATOM   1491  CB  ILE A  84      14.438  27.377  12.065  1.00  5.74           C  
ANISOU 1491  CB  ILE A  84      877    743    431     75     -2    -44       C  
ATOM   1492  CG1 ILE A  84      13.978  25.954  12.300  1.00  8.24           C  
ANISOU 1492  CG1 ILE A  84     1606    753    586      9   -121     47       C  
ATOM   1493  CG2 ILE A  84      14.859  28.057  13.374  1.00  6.67           C  
ANISOU 1493  CG2 ILE A  84      992    914    479     71    -99    -85       C  
ATOM   1494  CD1 ILE A  84      15.050  24.961  12.572  1.00 10.90           C  
ANISOU 1494  CD1 ILE A  84     2208    941    745    373   -396     75       C  
ATOM   1495  H   ILE A  84      13.891  27.815   9.437  1.00  5.81           H  
ATOM   1496  HA  ILE A  84      12.490  28.048  11.812  1.00  5.90           H  
ATOM   1497  HB  ILE A  84      15.221  27.346  11.477  1.00  6.89           H  
ATOM   1498 HG12 ILE A  84      13.364  25.952  13.050  1.00  9.89           H  
ATOM   1499 HG13 ILE A  84      13.482  25.661  11.519  1.00  9.89           H  
ATOM   1500 HG21 ILE A  84      15.145  28.955  13.191  1.00 10.01           H  
ATOM   1501 HG22 ILE A  84      14.114  28.075  13.979  1.00 10.01           H  
ATOM   1502 HG23 ILE A  84      15.582  27.566  13.772  1.00 10.01           H  
ATOM   1503 HD11 ILE A  84      14.658  24.095  12.706  1.00 16.35           H  
ATOM   1504 HD12 ILE A  84      15.652  24.928  11.824  1.00 16.35           H  
ATOM   1505 HD13 ILE A  84      15.533  25.219  13.360  1.00 16.35           H  
ATOM   1506  N   ILE A  85      12.856  30.447  12.052  1.00  4.95           N  
ANISOU 1506  N   ILE A  85      636    624    508    -52     54    -57       N  
ATOM   1507  CA  ILE A  85      13.141  31.844  12.348  1.00  4.92           C  
ANISOU 1507  CA  ILE A  85      715    569    475    -33     35    -44       C  
ATOM   1508  C   ILE A  85      13.729  31.881  13.761  1.00  4.88           C  
ANISOU 1508  C   ILE A  85      763    502    479    -24     51      9       C  
ATOM   1509  O   ILE A  85      13.044  31.586  14.746  1.00  5.86           O  
ANISOU 1509  O   ILE A  85      818    792    485   -151     70     36       O  
ATOM   1510  CB  ILE A  85      11.893  32.738  12.287  1.00  5.83           C  
ANISOU 1510  CB  ILE A  85      833    728    522     64     -9     29       C  
ATOM   1511  CG1 ILE A  85      11.162  32.596  10.950  1.00  7.11           C  
ANISOU 1511  CG1 ILE A  85      822   1032    687    197   -117    -73       C  
ATOM   1512  CG2 ILE A  85      12.259  34.174  12.603  1.00  7.10           C  
ANISOU 1512  CG2 ILE A  85     1152    653    731    131     46     37       C  
ATOM   1513  CD1 ILE A  85      12.025  32.853   9.729  1.00  9.18           C  
ANISOU 1513  CD1 ILE A  85     1071   1670    539    238   -130     55       C  
ATOM   1514  H   ILE A  85      12.117  30.110  12.337  1.00  5.94           H  
ATOM   1515  HA  ILE A  85      13.808  32.179  11.712  1.00  5.91           H  
ATOM   1516  HB  ILE A  85      11.281  32.433  12.989  1.00  7.00           H  
ATOM   1517 HG12 ILE A  85      10.799  31.699  10.890  1.00  8.54           H  
ATOM   1518 HG13 ILE A  85      10.415  33.216  10.938  1.00  8.54           H  
ATOM   1519 HG21 ILE A  85      12.714  34.210  13.448  1.00 10.65           H  
ATOM   1520 HG22 ILE A  85      12.835  34.516  11.915  1.00 10.65           H  
ATOM   1521 HG23 ILE A  85      11.461  34.705  12.646  1.00 10.65           H  
ATOM   1522 HD11 ILE A  85      11.496  32.745   8.935  1.00 13.77           H  
ATOM   1523 HD12 ILE A  85      12.370  33.748   9.763  1.00 13.77           H  
ATOM   1524 HD13 ILE A  85      12.754  32.229   9.715  1.00 13.77           H  
ATOM   1525  N   GLY A  86      15.026  32.213  13.839  1.00  4.61           N  
ANISOU 1525  N   GLY A  86      683    507    457    -10     62     -7       N  
ATOM   1526  CA  GLY A  86      15.707  32.233  15.103  1.00  4.69           C  
ANISOU 1526  CA  GLY A  86      688    465    524     31     23     12       C  
ATOM   1527  C   GLY A  86      15.860  33.637  15.662  1.00  4.53           C  
ANISOU 1527  C   GLY A  86      662    488    469     35     38     24       C  
ATOM   1528  O   GLY A  86      15.318  34.629  15.161  1.00  4.84           O  
ANISOU 1528  O   GLY A  86      758    442    530     29      2     46       O  
ATOM   1529  H   GLY A  86      15.456  32.417  13.123  1.00  5.53           H  
ATOM   1530  HA2 GLY A  86      15.214  31.691  15.737  1.00  5.63           H  
ATOM   1531  HA3 GLY A  86      16.587  31.838  14.995  1.00  5.63           H  
ATOM   1532  N   ARG A  87      16.620  33.719  16.761  1.00  4.63           N  
ANISOU 1532  N   ARG A  87      748    448    458     64    -16     15       N  
ATOM   1533  CA  ARG A  87      16.643  34.934  17.559  1.00  4.76           C  
ANISOU 1533  CA  ARG A  87      747    464    491     36     16     10       C  
ATOM   1534  C   ARG A  87      17.144  36.144  16.792  1.00  4.98           C  
ANISOU 1534  C   ARG A  87      813    488    479     25    -41     14       C  
ATOM   1535  O   ARG A  87      16.715  37.267  17.067  1.00  5.60           O  
ANISOU 1535  O   ARG A  87      967    498    536     36     31    -26       O  
ATOM   1536  CB  ARG A  87      17.476  34.747  18.825  1.00  4.96           C  
ANISOU 1536  CB  ARG A  87      744    537    492      4    -31     11       C  
ATOM   1537  CG  ARG A  87      16.863  33.748  19.802  1.00  5.19           C  
ANISOU 1537  CG  ARG A  87      827    524    504     24    -35     -8       C  
ATOM   1538  CD  ARG A  87      17.611  33.711  21.143  1.00  5.67           C  
ANISOU 1538  CD  ARG A  87      993    583    450     49     14     37       C  
ATOM   1539  NE  ARG A  87      18.984  33.267  20.997  1.00  6.03           N  
ANISOU 1539  NE  ARG A  87      946    617    590    100    -59     63       N  
ATOM   1540  CZ  ARG A  87      20.076  34.020  20.901  1.00  6.17           C  
ANISOU 1540  CZ  ARG A  87      926    727    552     69    -70     80       C  
ATOM   1541  NH1 ARG A  87      20.027  35.348  21.029  1.00  6.69           N  
ANISOU 1541  NH1 ARG A  87      874    767    751      5    -21     37       N  
ATOM   1542  NH2 ARG A  87      21.246  33.438  20.662  1.00  7.18           N  
ANISOU 1542  NH2 ARG A  87      990    845    732    148    -30     71       N  
ATOM   1543  H   ARG A  87      17.099  33.046  16.998  1.00  5.55           H  
ATOM   1544  HA  ARG A  87      15.722  35.122  17.837  1.00  5.72           H  
ATOM   1545  HB2 ARG A  87      18.362  34.443  18.577  1.00  5.95           H  
ATOM   1546  HB3 ARG A  87      17.571  35.604  19.270  1.00  5.95           H  
ATOM   1547  HG2 ARG A  87      15.936  33.986  19.961  1.00  6.23           H  
ATOM   1548  HG3 ARG A  87      16.879  32.863  19.404  1.00  6.23           H  
ATOM   1549  HD2 ARG A  87      17.603  34.597  21.536  1.00  6.80           H  
ATOM   1550  HD3 ARG A  87      17.146  33.113  21.749  1.00  6.80           H  
ATOM   1551  HE  ARG A  87      19.106  32.417  20.970  1.00  7.23           H  
ATOM   1552 HH11 ARG A  87      20.746  35.814  20.957  1.00  8.03           H  
ATOM   1553 HH12 ARG A  87      19.275  35.737  21.184  1.00  8.03           H  
ATOM   1554 HH21 ARG A  87      21.291  32.583  20.571  1.00  8.62           H  
ATOM   1555 HH22 ARG A  87      21.959  33.914  20.598  1.00  8.62           H  
ATOM   1556  N   ASN A  88      18.058  35.937  15.852  1.00  5.01           N  
ANISOU 1556  N   ASN A  88      780    483    525     -1     14     11       N  
ATOM   1557  CA  ASN A  88      18.604  37.078  15.116  1.00  5.51           C  
ANISOU 1557  CA  ASN A  88      841    562    568    -77     20     36       C  
ATOM   1558  C   ASN A  88      17.537  37.885  14.393  1.00  5.25           C  
ANISOU 1558  C   ASN A  88      837    507    534    -38     45     25       C  
ATOM   1559  O   ASN A  88      17.743  39.078  14.164  1.00  6.40           O  
ANISOU 1559  O   ASN A  88     1050    503    733   -122    -51     91       O  
ATOM   1560  CB  ASN A  88      19.683  36.628  14.124  1.00  5.71           C  
ANISOU 1560  CB  ASN A  88      792    688    561   -118     33     36       C  
ATOM   1561  CG  ASN A  88      19.126  35.919  12.914  1.00  5.72           C  
ANISOU 1561  CG  ASN A  88      803    672    571     35    -12    -19       C  
ATOM   1562  OD1 ASN A  88      18.389  34.923  13.045  1.00  6.16           O  
ANISOU 1562  OD1 ASN A  88      850    702    649    -30     33    -89       O  
ATOM   1563  ND2 ASN A  88      19.431  36.459  11.740  1.00  6.70           N  
ANISOU 1563  ND2 ASN A  88      942    899    554     -5     73    -35       N  
ATOM   1564  H   ASN A  88      18.327  35.139  15.678  1.00  6.01           H  
ATOM   1565  HA  ASN A  88      19.032  37.672  15.768  1.00  6.62           H  
ATOM   1566  HB2 ASN A  88      20.183  37.405  13.829  1.00  6.85           H  
ATOM   1567  HB3 ASN A  88      20.300  36.034  14.579  1.00  6.85           H  
ATOM   1568 HD21 ASN A  88      19.115  36.120  11.015  1.00  8.04           H  
ATOM   1569 HD22 ASN A  88      19.945  37.148  11.704  1.00  8.04           H  
ATOM   1570  N   LEU A  89      16.432  37.247  14.014  1.00  5.10           N  
ANISOU 1570  N   LEU A  89      827    448    547     -6     34     46       N  
ATOM   1571  CA  LEU A  89      15.311  37.928  13.396  1.00  5.19           C  
ANISOU 1571  CA  LEU A  89      834    464    557    -10      6     47       C  
ATOM   1572  C   LEU A  89      14.120  38.122  14.354  1.00  5.24           C  
ANISOU 1572  C   LEU A  89      836    492    546     20    -27      7       C  
ATOM   1573  O   LEU A  89      13.386  39.100  14.219  1.00  5.88           O  
ANISOU 1573  O   LEU A  89      937    540    624     83      4     45       O  
ATOM   1574  CB  LEU A  89      14.880  37.266  12.098  1.00  5.94           C  
ANISOU 1574  CB  LEU A  89     1003    559    560     19    -43     50       C  
ATOM   1575  CG  LEU A  89      15.908  37.367  10.991  1.00  8.24           C  
ANISOU 1575  CG  LEU A  89     1090   1289    565    456     35     53       C  
ATOM   1576  CD1 LEU A  89      15.504  36.521   9.805  1.00 12.88           C  
ANISOU 1576  CD1 LEU A  89     3041    965    597    687     42    -53       C  
ATOM   1577  CD2 LEU A  89      16.142  38.777  10.532  1.00 14.70           C  
ANISOU 1577  CD2 LEU A  89     2700   1853    700  -1132    371    -34       C  
ATOM   1578  H   LEU A  89      16.381  36.398  14.141  1.00  6.12           H  
ATOM   1579  HA  LEU A  89      15.627  38.825  13.159  1.00  6.23           H  
ATOM   1580  HB2 LEU A  89      14.696  36.329  12.270  1.00  7.12           H  
ATOM   1581  HB3 LEU A  89      14.054  37.677  11.797  1.00  7.12           H  
ATOM   1582  HG  LEU A  89      16.757  37.017  11.335  1.00  9.89           H  
ATOM   1583 HD11 LEU A  89      15.353  35.617  10.093  1.00 19.32           H  
ATOM   1584 HD12 LEU A  89      14.698  36.873   9.421  1.00 19.32           H  
ATOM   1585 HD13 LEU A  89      16.204  36.534   9.149  1.00 19.32           H  
ATOM   1586 HD21 LEU A  89      16.399  39.319  11.281  1.00 22.05           H  
ATOM   1587 HD22 LEU A  89      16.841  38.788   9.874  1.00 22.05           H  
ATOM   1588 HD23 LEU A  89      15.335  39.126  10.147  1.00 22.05           H  
ATOM   1589  N   LEU A  90      13.929  37.209  15.315  1.00  5.07           N  
ANISOU 1589  N   LEU A  90      783    474    554     39     22     18       N  
ATOM   1590  CA  LEU A  90      12.872  37.405  16.292  1.00  5.16           C  
ANISOU 1590  CA  LEU A  90      735    470    639     46     -3     26       C  
ATOM   1591  C   LEU A  90      13.029  38.717  17.059  1.00  5.17           C  
ANISOU 1591  C   LEU A  90      798    472    578     25     80     54       C  
ATOM   1592  O   LEU A  90      12.051  39.386  17.351  1.00  5.82           O  
ANISOU 1592  O   LEU A  90      793    568    718     69     82     15       O  
ATOM   1593  CB  LEU A  90      12.812  36.232  17.282  1.00  5.21           C  
ANISOU 1593  CB  LEU A  90      746    498    616     19     22     25       C  
ATOM   1594  CG  LEU A  90      12.407  34.883  16.678  1.00  5.68           C  
ANISOU 1594  CG  LEU A  90      844    536    649    -62     22    -13       C  
ATOM   1595  CD1 LEU A  90      12.602  33.770  17.692  1.00  6.88           C  
ANISOU 1595  CD1 LEU A  90     1154    512    793   -108     31    -11       C  
ATOM   1596  CD2 LEU A  90      10.988  34.866  16.186  1.00  7.31           C  
ANISOU 1596  CD2 LEU A  90      967    718    927   -140    -18    -60       C  
ATOM   1597  H   LEU A  90      14.429  36.510  15.353  1.00  6.08           H  
ATOM   1598  HA  LEU A  90      12.018  37.437  15.811  1.00  6.20           H  
ATOM   1599  HB2 LEU A  90      13.685  36.134  17.694  1.00  6.25           H  
ATOM   1600  HB3 LEU A  90      12.182  36.455  17.985  1.00  6.25           H  
ATOM   1601  HG  LEU A  90      12.995  34.704  15.915  1.00  6.81           H  
ATOM   1602 HD11 LEU A  90      13.508  33.779  18.008  1.00 10.33           H  
ATOM   1603 HD12 LEU A  90      12.004  33.903  18.432  1.00 10.33           H  
ATOM   1604 HD13 LEU A  90      12.415  32.924  17.279  1.00 10.33           H  
ATOM   1605 HD21 LEU A  90      10.863  35.569  15.544  1.00 10.96           H  
ATOM   1606 HD22 LEU A  90      10.802  34.020  15.773  1.00 10.96           H  
ATOM   1607 HD23 LEU A  90      10.391  34.999  16.926  1.00 10.96           H  
ATOM   1608  N   THR A  91      14.276  39.091  17.385  1.00  5.10           N  
ANISOU 1608  N   THR A  91      747    454    622      8     23      0       N  
ATOM   1609  CA  THR A  91      14.472  40.367  18.077  1.00  5.60           C  
ANISOU 1609  CA  THR A  91      939    470    593    -16     32    -12       C  
ATOM   1610  C   THR A  91      13.923  41.519  17.261  1.00  5.60           C  
ANISOU 1610  C   THR A  91      859    489    653    -10     45     -6       C  
ATOM   1611  O   THR A  91      13.347  42.468  17.765  1.00  6.59           O  
ANISOU 1611  O   THR A  91     1102    515    738    112     64     -7       O  
ATOM   1612  CB  THR A  91      15.947  40.618  18.388  1.00  5.74           C  
ANISOU 1612  CB  THR A  91      884    508    660    -15      2    -28       C  
ATOM   1613  OG1 THR A  91      16.660  40.661  17.146  1.00  6.39           O  
ANISOU 1613  OG1 THR A  91      916    643    725    -19     41     45       O  
ATOM   1614  CG2 THR A  91      16.529  39.633  19.374  1.00  6.23           C  
ANISOU 1614  CG2 THR A  91      964    572    689    -14    -69    -48       C  
ATOM   1615  H   THR A  91      14.947  38.590  17.191  1.00  6.12           H  
ATOM   1616  HA  THR A  91      13.982  40.332  18.926  1.00  6.72           H  
ATOM   1617  HB  THR A  91      16.012  41.508  18.792  1.00  6.89           H  
ATOM   1618  HG1 THR A  91      17.278  40.124  17.168  1.00  9.59           H  
ATOM   1619 HG21 THR A  91      16.012  39.648  20.183  1.00  9.34           H  
ATOM   1620 HG22 THR A  91      16.507  38.751  18.996  1.00  9.34           H  
ATOM   1621 HG23 THR A  91      17.437  39.875  19.569  1.00  9.34           H  
ATOM   1622  N   GLN A  92      14.165  41.460  15.931  1.00  5.71           N  
ANISOU 1622  N   GLN A  92      878    461    700     66     71     49       N  
ATOM   1623  CA  GLN A  92      13.897  42.586  15.058  1.00  5.88           C  
ANISOU 1623  CA  GLN A  92      934    493    674     -3     56     67       C  
ATOM   1624  C   GLN A  92      12.412  42.818  14.876  1.00  6.19           C  
ANISOU 1624  C   GLN A  92      942    562    709     14     36    106       C  
ATOM   1625  O   GLN A  92      11.994  43.977  14.648  1.00  8.10           O  
ANISOU 1625  O   GLN A  92     1077    610   1207     62    -66    206       O  
ATOM   1626  CB  GLN A  92      14.564  42.351  13.701  1.00  6.46           C  
ANISOU 1626  CB  GLN A  92     1083    531    693    -57     89     77       C  
ATOM   1627  CG  GLN A  92      16.066  42.219  13.765  1.00  6.43           C  
ANISOU 1627  CG  GLN A  92     1055    499    744     19    230     31       C  
ATOM   1628  CD  GLN A  92      16.735  43.462  14.307  1.00  6.08           C  
ANISOU 1628  CD  GLN A  92      891    471    812     57    239     43       C  
ATOM   1629  OE1 GLN A  92      16.842  44.477  13.595  1.00  6.86           O  
ANISOU 1629  OE1 GLN A  92     1150    532    771    -18    214     59       O  
ATOM   1630  NE2 GLN A  92      17.123  43.445  15.571  1.00  6.94           N  
ANISOU 1630  NE2 GLN A  92     1089    602    789      3     82     56       N  
ATOM   1631  H   GLN A  92      14.486  40.736  15.595  1.00  6.85           H  
ATOM   1632  HA  GLN A  92      14.289  43.389  15.460  1.00  7.06           H  
ATOM   1633  HB2 GLN A  92      14.197  41.543  13.310  1.00  7.75           H  
ATOM   1634  HB3 GLN A  92      14.341  43.090  13.113  1.00  7.75           H  
ATOM   1635  HG2 GLN A  92      16.294  41.464  14.329  1.00  7.72           H  
ATOM   1636  HG3 GLN A  92      16.406  42.038  12.875  1.00  7.72           H  
ATOM   1637 HE21 GLN A  92      17.463  44.151  15.927  1.00  8.33           H  
ATOM   1638 HE22 GLN A  92      17.036  42.728  16.038  1.00  8.33           H  
ATOM   1639  N   ILE A  93      11.594  41.778  14.973  1.00  6.48           N  
ANISOU 1639  N   ILE A  93      913    602    799     33    -13    127       N  
ATOM   1640  CA  ILE A  93      10.149  41.911  14.920  1.00  7.12           C  
ANISOU 1640  CA  ILE A  93      923    698    923      9    -19    216       C  
ATOM   1641  C   ILE A  93       9.552  42.199  16.280  1.00  7.23           C  
ANISOU 1641  C   ILE A  93      858    619   1108     38     60    138       C  
ATOM   1642  O   ILE A  93       8.338  42.343  16.402  1.00  9.03           O  
ANISOU 1642  O   ILE A  93      945    860   1421    116     80     82       O  
ATOM   1643  CB  ILE A  93       9.485  40.720  14.206  1.00  7.84           C  
ANISOU 1643  CB  ILE A  93      905    980    916    -55   -157    171       C  
ATOM   1644  CG1 ILE A  93       9.509  39.449  15.049  1.00  8.16           C  
ANISOU 1644  CG1 ILE A  93     1051    741   1123    -13   -205     98       C  
ATOM   1645  CG2 ILE A  93      10.084  40.545  12.839  1.00  9.34           C  
ANISOU 1645  CG2 ILE A  93     1115   1327    894    -97   -126     46       C  
ATOM   1646  CD1 ILE A  93       8.747  38.309  14.478  1.00 10.38           C  
ANISOU 1646  CD1 ILE A  93     1400    958   1352   -256   -141      2       C  
ATOM   1647  H   ILE A  93      11.933  40.993  15.070  1.00  7.77           H  
ATOM   1648  HA  ILE A  93       9.966  42.700  14.368  1.00  8.54           H  
ATOM   1649  HB  ILE A  93       8.543  40.956  14.075  1.00  9.41           H  
ATOM   1650 HG12 ILE A  93      10.432  39.175  15.168  1.00  9.79           H  
ATOM   1651 HG13 ILE A  93       9.149  39.653  15.926  1.00  9.79           H  
ATOM   1652 HG21 ILE A  93      10.039  41.377  12.362  1.00 14.00           H  
ATOM   1653 HG22 ILE A  93      11.002  40.275  12.924  1.00 14.00           H  
ATOM   1654 HG23 ILE A  93       9.596  39.873  12.359  1.00 14.00           H  
ATOM   1655 HD11 ILE A  93       8.813  37.553  15.067  1.00 15.57           H  
ATOM   1656 HD12 ILE A  93       7.825  38.557  14.379  1.00 15.57           H  
ATOM   1657 HD13 ILE A  93       9.110  38.078  13.620  1.00 15.57           H  
ATOM   1658  N   GLY A  94      10.369  42.311  17.324  1.00  7.31           N  
ANISOU 1658  N   GLY A  94     1025    698    890    132    112     79       N  
ATOM   1659  CA  GLY A  94       9.884  42.645  18.652  1.00  8.11           C  
ANISOU 1659  CA  GLY A  94     1072    711   1114     81    196     31       C  
ATOM   1660  C   GLY A  94       9.344  41.488  19.424  1.00  7.57           C  
ANISOU 1660  C   GLY A  94      990    831    883     91    146     -8       C  
ATOM   1661  O   GLY A  94       8.543  41.718  20.345  1.00  9.10           O  
ANISOU 1661  O   GLY A  94     1209    924   1119     61    422    -58       O  
ATOM   1662  H   GLY A  94      11.212  42.182  17.210  1.00  8.78           H  
ATOM   1663  HA2 GLY A  94      10.612  43.041  19.157  1.00  9.73           H  
ATOM   1664  HA3 GLY A  94       9.187  43.314  18.568  1.00  9.73           H  
ATOM   1665  N   ALA A  95       9.744  40.265  19.127  1.00  7.00           N  
ANISOU 1665  N   ALA A  95      929    705    868    108    176    126       N  
ATOM   1666  CA  ALA A  95       9.191  39.104  19.803  1.00  6.90           C  
ANISOU 1666  CA  ALA A  95      810    797    857     49    138    131       C  
ATOM   1667  C   ALA A  95       9.854  38.882  21.146  1.00  7.02           C  
ANISOU 1667  C   ALA A  95      820    719    969     51     74    110       C  
ATOM   1668  O   ALA A  95      11.057  38.864  21.292  1.00  8.46           O  
ANISOU 1668  O   ALA A  95      812   1014   1198     28     -5    220       O  
ATOM   1669  CB  ALA A  95       9.381  37.859  18.962  1.00  7.72           C  
ANISOU 1669  CB  ALA A  95     1039    764    957     -9    208     55       C  
ATOM   1670  H   ALA A  95      10.343  40.154  18.520  1.00  8.40           H  
ATOM   1671  HA  ALA A  95       8.232  39.248  19.944  1.00  8.28           H  
ATOM   1672  HB1 ALA A  95       9.011  37.102  19.423  1.00 11.59           H  
ATOM   1673  HB2 ALA A  95       8.934  37.970  18.120  1.00 11.59           H  
ATOM   1674  HB3 ALA A  95      10.318  37.714  18.811  1.00 11.59           H  
ATOM   1675  N   THR A  96       8.969  38.606  22.149  1.00  6.96           N  
ANISOU 1675  N   THR A  96      851    827    811     38     67    104       N  
ATOM   1676  CA  THR A  96       9.408  38.230  23.480  1.00  7.18           C  
ANISOU 1676  CA  THR A  96     1045    684    836     17    -26     27       C  
ATOM   1677  C   THR A  96       8.614  37.002  23.922  1.00  6.76           C  
ANISOU 1677  C   THR A  96      944    693    780    100    140     21       C  
ATOM   1678  O   THR A  96       7.531  36.698  23.431  1.00  7.69           O  
ANISOU 1678  O   THR A  96      905    798   1045     62     53    188       O  
ATOM   1679  CB  THR A  96       9.182  39.389  24.493  1.00  9.29           C  
ANISOU 1679  CB  THR A  96     1659    724    938    206    -97    -53       C  
ATOM   1680  OG1 THR A  96       7.793  39.729  24.554  1.00 10.49           O  
ANISOU 1680  OG1 THR A  96     1907    824   1018    325    347     60       O  
ATOM   1681  CG2 THR A  96      10.014  40.595  24.073  1.00 11.79           C  
ANISOU 1681  CG2 THR A  96     1874    699   1641    -15   -321    -90       C  
ATOM   1682  H   THR A  96       8.125  38.655  21.987  1.00  8.36           H  
ATOM   1683  HA  THR A  96      10.362  38.006  23.454  1.00  8.62           H  
ATOM   1684  HB  THR A  96       9.475  39.096  25.381  1.00 11.15           H  
ATOM   1685  HG1 THR A  96       7.361  39.073  24.790  1.00 15.74           H  
ATOM   1686 HG21 THR A  96      10.941  40.347  24.038  1.00 17.69           H  
ATOM   1687 HG22 THR A  96       9.730  40.894  23.206  1.00 17.69           H  
ATOM   1688 HG23 THR A  96       9.896  41.303  24.710  1.00 17.69           H  
ATOM   1689  N   LEU A  97       9.214  36.305  24.899  1.00  6.76           N  
ANISOU 1689  N   LEU A  97      902    714    799    125    128     49       N  
ATOM   1690  CA  LEU A  97       8.548  35.210  25.579  1.00  7.56           C  
ANISOU 1690  CA  LEU A  97      885    815   1003    138    156    216       C  
ATOM   1691  C   LEU A  97       8.010  35.738  26.895  1.00  8.33           C  
ANISOU 1691  C   LEU A  97      930   1195    851    131    116    179       C  
ATOM   1692  O   LEU A  97       8.742  36.382  27.651  1.00 16.01           O  
ANISOU 1692  O   LEU A  97     1274   3639    809   -843     78   -188       O  
ATOM   1693  CB ALEU A  97       9.571  34.203  26.197  0.52  6.83           C  
ANISOU 1693  CB ALEU A  97      953    684    802    116    -24      2       C  
ATOM   1694  CB BLEU A  97       9.512  33.973  25.482  0.49  6.31           C  
ANISOU 1694  CB BLEU A  97      920    691    644     91    -82   -121       C  
ATOM   1695  CG ALEU A  97       9.960  33.261  25.111  0.52  7.67           C  
ANISOU 1695  CG ALEU A  97     1261    821    658    223     90   -111       C  
ATOM   1696  CG BLEU A  97       9.004  32.651  26.047  0.49  6.77           C  
ANISOU 1696  CG BLEU A  97     1137    697    586    277     58    -22       C  
ATOM   1697  CD1ALEU A  97      11.223  32.527  25.533  0.52  9.36           C  
ANISOU 1697  CD1ALEU A  97     1425   1103    815    561     35     12       C  
ATOM   1698  CD1BLEU A  97       7.973  32.031  25.126  0.49  6.85           C  
ANISOU 1698  CD1BLEU A  97      942    609    896     75    174    -42       C  
ATOM   1699  CD2ALEU A  97       8.804  32.306  24.796  0.52  9.36           C  
ANISOU 1699  CD2ALEU A  97     1481    841   1023    164     -1   -239       C  
ATOM   1700  CD2BLEU A  97      10.170  31.686  26.218  0.49 10.03           C  
ANISOU 1700  CD2BLEU A  97     1339    730   1514    360   -176     38       C  
ATOM   1701  H   LEU A  97      10.017  36.513  25.128  1.00  8.11           H  
ATOM   1702  HA ALEU A  97       7.863  34.775  25.030  1.00  9.08           H  
ATOM   1703  HB2ALEU A  97      10.351  34.676  26.529  0.52  8.19           H  
ATOM   1704  HB2BLEU A  97       9.729  33.835  24.546  0.49  7.57           H  
ATOM   1705  HB3ALEU A  97       9.166  33.720  26.934  0.52  8.19           H  
ATOM   1706  HB3BLEU A  97      10.337  34.198  25.939  0.49  7.57           H  
ATOM   1707  HG ALEU A  97      10.159  33.782  24.305  0.52  9.20           H  
ATOM   1708  HG BLEU A  97       8.594  32.814  26.922  0.49  8.13           H  
ATOM   1709 HD11ALEU A  97      11.484  31.916  24.841  0.52 14.03           H  
ATOM   1710 HD11BLEU A  97       7.237  32.637  25.017  0.49 10.27           H  
ATOM   1711 HD12ALEU A  97      11.927  33.162  25.682  0.52 14.03           H  
ATOM   1712 HD12BLEU A  97       8.373  31.855  24.271  0.49 10.27           H  
ATOM   1713 HD13ALEU A  97      11.054  32.041  26.343  0.52 14.03           H  
ATOM   1714 HD13BLEU A  97       7.657  31.209  25.507  0.49 10.27           H  
ATOM   1715 HD21ALEU A  97       9.067  31.705  24.096  0.52 14.04           H  
ATOM   1716 HD21BLEU A  97      10.826  32.076  26.801  0.49 15.04           H  
ATOM   1717 HD22ALEU A  97       8.581  31.803  25.583  0.52 14.04           H  
ATOM   1718 HD22BLEU A  97       9.853  30.864  26.598  0.49 15.04           H  
ATOM   1719 HD23ALEU A  97       8.039  32.812  24.513  0.52 14.04           H  
ATOM   1720 HD23BLEU A  97      10.568  31.511  25.362  0.49 15.04           H  
ATOM   1721  N   ASN A  98       6.750  35.470  27.200  1.00  7.71           N  
ANISOU 1721  N   ASN A  98      985    793    979    -19    147     -3       N  
ATOM   1722  CA  ASN A  98       6.085  36.057  28.349  1.00  8.10           C  
ANISOU 1722  CA  ASN A  98     1139    848    906     -2    189    -18       C  
ATOM   1723  C   ASN A  98       5.398  34.975  29.155  1.00  7.94           C  
ANISOU 1723  C   ASN A  98     1171    834    830      7    163    -52       C  
ATOM   1724  O   ASN A  98       4.710  34.141  28.595  1.00  8.69           O  
ANISOU 1724  O   ASN A  98     1236    995    876    -55    106     74       O  
ATOM   1725  CB  ASN A  98       5.033  37.086  27.901  1.00  8.85           C  
ANISOU 1725  CB  ASN A  98     1228   1037    896    185    243    -24       C  
ATOM   1726  CG  ASN A  98       5.707  38.242  27.219  1.00  9.98           C  
ANISOU 1726  CG  ASN A  98     1627    779   1161    279    212    -46       C  
ATOM   1727  OD1 ASN A  98       6.069  38.179  26.058  1.00 13.29           O  
ANISOU 1727  OD1 ASN A  98     1761   1319   1667    318    747    261       O  
ATOM   1728  ND2 ASN A  98       6.135  39.228  27.950  1.00 13.44           N  
ANISOU 1728  ND2 ASN A  98     2232   1069   1503    -43    362    -95       N  
ATOM   1729  H   ASN A  98       6.309  34.927  26.699  1.00  9.26           H  
ATOM   1730  HA  ASN A  98       6.751  36.503  28.912  1.00  9.71           H  
ATOM   1731  HB2 ASN A  98       4.406  36.667  27.290  1.00 10.62           H  
ATOM   1732  HB3 ASN A  98       4.538  37.404  28.671  1.00 10.62           H  
ATOM   1733 HD21 ASN A  98       6.662  39.817  27.611  1.00 16.13           H  
ATOM   1734 HD22 ASN A  98       5.891  39.291  28.772  1.00 16.13           H  
ATOM   1735  N   PHE A  99       5.566  35.042  30.476  1.00  8.87           N  
ANISOU 1735  N   PHE A  99     1277   1015    878   -164    211    -62       N  
ATOM   1736  CA  PHE A  99       4.868  34.142  31.407  1.00 10.02           C  
ANISOU 1736  CA  PHE A  99     1586   1126    867    -45    319    109       C  
ATOM   1737  C   PHE A  99       4.821  34.802  32.794  1.00 12.00           C  
ANISOU 1737  C   PHE A  99     2043   1274    970     -6    427    -36       C  
ATOM   1738  O   PHE A  99       4.294  34.136  33.713  1.00 16.69           O  
ANISOU 1738  O   PHE A  99     3150   1582   1232   -235   1073   -190       O  
ATOM   1739  CB  PHE A  99       5.453  32.734  31.436  1.00  9.50           C  
ANISOU 1739  CB  PHE A  99     1487   1139    767      9    160      7       C  
ATOM   1740  CG  PHE A  99       6.868  32.585  31.820  1.00 10.21           C  
ANISOU 1740  CG  PHE A  99     1501   1300    848      8    208     25       C  
ATOM   1741  CD1 PHE A  99       7.886  32.765  30.892  1.00 12.03           C  
ANISOU 1741  CD1 PHE A  99     1490   1726   1084    204    248    131       C  
ATOM   1742  CD2 PHE A  99       7.236  32.260  33.107  1.00 12.57           C  
ANISOU 1742  CD2 PHE A  99     1618   1966    906     13     40     76       C  
ATOM   1743  CE1 PHE A  99       9.179  32.637  31.276  1.00 15.71           C  
ANISOU 1743  CE1 PHE A  99     1490   2649   1475    310    343    342       C  
ATOM   1744  CE2 PHE A  99       8.529  32.131  33.495  1.00 16.13           C  
ANISOU 1744  CE2 PHE A  99     1809   2800   1156    164   -113    230       C  
ATOM   1745  CZ  PHE A  99       9.507  32.337  32.582  1.00 18.28           C  
ANISOU 1745  CZ  PHE A  99     1516   3245   1772    205      2    620       C  
ATOM   1746  OXT PHE A  99       5.258  35.938  32.926  1.00 15.11           O  
ANISOU 1746  OXT PHE A  99     2759   1554   1086   -401    577   -230       O  
ATOM   1747  H   PHE A  99       6.103  35.633  30.795  1.00 10.65           H  
ATOM   1748  HA  PHE A  99       3.942  34.064  31.094  1.00 12.02           H  
ATOM   1749  HB2 PHE A  99       4.921  32.204  32.050  1.00 11.39           H  
ATOM   1750  HB3 PHE A  99       5.341  32.348  30.554  1.00 11.39           H  
ATOM   1751  HD1 PHE A  99       7.680  32.974  30.009  1.00 14.44           H  
ATOM   1752  HD2 PHE A  99       6.567  32.124  33.738  1.00 15.08           H  
ATOM   1753  HE1 PHE A  99       9.856  32.752  30.649  1.00 18.85           H  
ATOM   1754  HE2 PHE A  99       8.740  31.904  34.372  1.00 19.36           H  
ATOM   1755  HZ  PHE A  99      10.400  32.276  32.834  1.00 21.94           H  
TER    1756      PHE A  99                                                      
ATOM   1757  N   PRO B   1       7.622  36.937  33.734  1.00 19.03           N  
ANISOU 1757  N   PRO B   1     3378   2158   1264   -581    -41     42       N  
ATOM   1758  CA  PRO B   1       8.594  37.868  33.148  1.00 16.53           C  
ANISOU 1758  CA  PRO B   1     2597   1883   1427   -207   -149   -177       C  
ATOM   1759  C   PRO B   1       8.329  38.046  31.654  1.00 12.57           C  
ANISOU 1759  C   PRO B   1     1713   1329   1451    -32    212   -207       C  
ATOM   1760  O   PRO B   1       7.553  37.277  31.073  1.00 13.33           O  
ANISOU 1760  O   PRO B   1     2117   1485   1162   -413    283   -317       O  
ATOM   1761  CB  PRO B   1       9.973  37.227  33.317  1.00 21.72           C  
ANISOU 1761  CB  PRO B   1     2942   2434   2385    182   -741     81       C  
ATOM   1762  CG  PRO B   1       9.659  35.803  33.346  1.00 28.24           C  
ANISOU 1762  CG  PRO B   1     4208   2260   3622    410   -278    161       C  
ATOM   1763  CD  PRO B   1       8.322  35.652  34.003  1.00 28.91           C  
ANISOU 1763  CD  PRO B   1     4529   2939   2862   -174   -383   1609       C  
ATOM   1764  HA  PRO B   1       8.560  38.733  33.607  1.00 19.84           H  
ATOM   1765  HB2 PRO B   1      10.555  37.444  32.572  1.00 26.06           H  
ATOM   1766  HB3 PRO B   1      10.394  37.512  34.143  1.00 26.06           H  
ATOM   1767  HG2 PRO B   1       9.631  35.447  32.444  1.00 33.89           H  
ATOM   1768  HG3 PRO B   1      10.335  35.321  33.847  1.00 33.89           H  
ATOM   1769  HD2 PRO B   1       7.833  34.907  33.622  1.00 34.69           H  
ATOM   1770  HD3 PRO B   1       8.421  35.507  34.957  1.00 34.69           H  
ATOM   1771  N   GLN B   2       8.999  39.031  31.126  1.00 13.53           N  
ANISOU 1771  N   GLN B   2     1813   1271   1750   -238    526   -446       N  
ATOM   1772  CA  GLN B   2       9.071  39.239  29.692  1.00 13.24           C  
ANISOU 1772  CA  GLN B   2     1835   1163   1735   -189    692   -541       C  
ATOM   1773  C   GLN B   2      10.535  39.010  29.296  1.00 14.45           C  
ANISOU 1773  C   GLN B   2     1862   1255   2047   -415    668   -697       C  
ATOM   1774  O   GLN B   2      11.373  39.782  29.735  1.00 24.43           O  
ANISOU 1774  O   GLN B   2     2092   1960   4677   -697    847  -1813       O  
ATOM   1775  CB  GLN B   2       8.668  40.630  29.338  1.00 15.20           C  
ANISOU 1775  CB  GLN B   2     2587   1276   1569    -26    728   -398       C  
ATOM   1776  CG  GLN B   2       8.879  40.893  27.863  1.00 21.28           C  
ANISOU 1776  CG  GLN B   2     4284   1805   1517   -698    664   -297       C  
ATOM   1777  CD  GLN B   2       7.992  42.021  27.365  1.00 27.94           C  
ANISOU 1777  CD  GLN B   2     7195   1015   1774    -61    694    186       C  
ATOM   1778  OE1 GLN B   2       8.414  43.140  27.792  1.00 58.55           O  
ANISOU 1778  OE1 GLN B   2    11716   1314   7890  -1577  -1713    240       O  
ATOM   1779  NE2 GLN B   2       6.910  42.066  26.654  1.00 37.73           N  
ANISOU 1779  NE2 GLN B   2     7790   2449   3244   2086   -315   -934       N  
ATOM   1780  H   GLN B   2       9.413  39.577  31.645  1.00 16.24           H  
ATOM   1781  HA  GLN B   2       8.494  38.595  29.231  1.00 15.89           H  
ATOM   1782  HB2 GLN B   2       7.732  40.762  29.560  1.00 18.24           H  
ATOM   1783  HB3 GLN B   2       9.191  41.261  29.858  1.00 18.24           H  
ATOM   1784  HG2 GLN B   2       9.808  41.124  27.708  1.00 25.54           H  
ATOM   1785  HG3 GLN B   2       8.684  40.086  27.362  1.00 25.54           H  
ATOM   1786 HE21 GLN B   2       6.528  42.821  26.500  1.00 45.28           H  
ATOM   1787 HE22 GLN B   2       6.574  41.341  26.336  1.00 45.28           H  
ATOM   1788  N   ILE B   3      10.793  37.976  28.528  1.00 10.50           N  
ANISOU 1788  N   ILE B   3     1373   1034   1346   -147    532   -222       N  
ATOM   1789  CA  ILE B   3      12.119  37.623  28.165  1.00 10.52           C  
ANISOU 1789  CA  ILE B   3     1382   1234   1143   -228    358   -336       C  
ATOM   1790  C   ILE B   3      12.380  38.026  26.719  1.00  9.01           C  
ANISOU 1790  C   ILE B   3     1099   1000   1120   -173    323   -307       C  
ATOM   1791  O   ILE B   3      11.708  37.564  25.784  1.00  9.26           O  
ANISOU 1791  O   ILE B   3     1054   1001   1253   -120    212   -261       O  
ATOM   1792  CB  ILE B   3      12.375  36.142  28.408  1.00 11.68           C  
ANISOU 1792  CB  ILE B   3     1287   1353   1533    -47    566    -53       C  
ATOM   1793  CG1 ILE B   3      12.187  35.832  29.930  1.00 16.38           C  
ANISOU 1793  CG1 ILE B   3     2123   1719   2013    141   1140    437       C  
ATOM   1794  CG2 ILE B   3      13.770  35.772  27.931  1.00 12.12           C  
ANISOU 1794  CG2 ILE B   3     1409   1530   1392     82    478     66       C  
ATOM   1795  CD1 ILE B   3      12.392  34.416  30.233  1.00 17.53           C  
ANISOU 1795  CD1 ILE B   3     2353   1746   2165     -3    836    301       C  
ATOM   1796  H   ILE B   3      10.140  37.499  28.237  1.00 12.60           H  
ATOM   1797  HA  ILE B   3      12.733  38.132  28.735  1.00 12.62           H  
ATOM   1798  HB  ILE B   3      11.719  35.622  27.898  1.00 14.02           H  
ATOM   1799 HG12 ILE B   3      12.816  36.362  30.444  1.00 19.66           H  
ATOM   1800 HG13 ILE B   3      11.291  36.089  30.200  1.00 19.66           H  
ATOM   1801 HG21 ILE B   3      13.924  34.837  28.087  1.00 18.18           H  
ATOM   1802 HG22 ILE B   3      13.846  35.957  26.992  1.00 18.18           H  
ATOM   1803 HG23 ILE B   3      14.420  36.288  28.412  1.00 18.18           H  
ATOM   1804 HD11 ILE B   3      12.268  34.269  31.173  1.00 26.29           H  
ATOM   1805 HD12 ILE B   3      11.759  33.889  29.740  1.00 26.29           H  
ATOM   1806 HD13 ILE B   3      13.284  34.162  29.984  1.00 26.29           H  
ATOM   1807  N   THR B   4      13.338  38.937  26.525  1.00  9.77           N  
ANISOU 1807  N   THR B   4     1261   1180   1050   -340    304   -339       N  
ATOM   1808  CA  THR B   4      13.767  39.321  25.208  1.00  8.65           C  
ANISOU 1808  CA  THR B   4     1176    928    987   -133    225   -292       C  
ATOM   1809  C   THR B   4      14.780  38.308  24.652  1.00  7.97           C  
ANISOU 1809  C   THR B   4     1013   1029    806   -112     -4   -175       C  
ATOM   1810  O   THR B   4      15.189  37.380  25.366  1.00 10.03           O  
ANISOU 1810  O   THR B   4     1207   1580    796    166     39     70       O  
ATOM   1811  CB  THR B   4      14.357  40.742  25.232  1.00 10.15           C  
ANISOU 1811  CB  THR B   4     1293   1016   1318   -303    398   -289       C  
ATOM   1812  OG1 THR B   4      15.541  40.715  26.019  1.00 11.67           O  
ANISOU 1812  OG1 THR B   4     1542   1425   1202   -550    198   -401       O  
ATOM   1813  CG2 THR B   4      13.359  41.714  25.846  1.00 15.18           C  
ANISOU 1813  CG2 THR B   4     1733   1091   2599   -313    656   -787       C  
ATOM   1814  H   THR B   4      13.709  39.305  27.208  1.00 11.72           H  
ATOM   1815  HA  THR B   4      12.984  39.324  24.619  1.00 10.38           H  
ATOM   1816  HB  THR B   4      14.574  41.025  24.319  1.00 12.18           H  
ATOM   1817  HG1 THR B   4      16.085  40.207  25.676  1.00 17.50           H  
ATOM   1818 HG21 THR B   4      12.560  41.731  25.313  1.00 22.76           H  
ATOM   1819 HG22 THR B   4      13.143  41.431  26.737  1.00 22.76           H  
ATOM   1820 HG23 THR B   4      13.744  42.593  25.873  1.00 22.76           H  
ATOM   1821  N   LEU B   5      15.114  38.465  23.386  1.00  6.74           N  
ANISOU 1821  N   LEU B   5      976    657    773    -75     37   -109       N  
ATOM   1822  CA  LEU B   5      15.821  37.390  22.665  1.00  6.10           C  
ANISOU 1822  CA  LEU B   5      911    602    666    -57    -31    -67       C  
ATOM   1823  C   LEU B   5      17.169  37.827  22.111  1.00  5.73           C  
ANISOU 1823  C   LEU B   5      802    540    704    -34    -97    -19       C  
ATOM   1824  O   LEU B   5      17.748  37.147  21.262  1.00  6.24           O  
ANISOU 1824  O   LEU B   5      879    611    740    -29    -43    -41       O  
ATOM   1825  CB  LEU B   5      14.890  36.816  21.607  1.00  6.14           C  
ANISOU 1825  CB  LEU B   5      886    533    775    -23   -128     -6       C  
ATOM   1826  CG  LEU B   5      13.645  36.149  22.181  1.00  6.52           C  
ANISOU 1826  CG  LEU B   5      914    595    819    -47    -26    -49       C  
ATOM   1827  CD1 LEU B   5      12.655  35.838  21.055  1.00  7.01           C  
ANISOU 1827  CD1 LEU B   5      925    697    882    -58   -101     28       C  
ATOM   1828  CD2 LEU B   5      13.976  34.884  22.967  1.00  7.62           C  
ANISOU 1828  CD2 LEU B   5     1117    766    839   -210   -103    159       C  
ATOM   1829  H   LEU B   5      14.918  39.197  22.979  1.00  8.08           H  
ATOM   1830  HA  LEU B   5      15.995  36.675  23.313  1.00  7.32           H  
ATOM   1831  HB2 LEU B   5      14.616  37.530  21.011  1.00  7.37           H  
ATOM   1832  HB3 LEU B   5      15.379  36.164  21.080  1.00  7.37           H  
ATOM   1833  HG  LEU B   5      13.218  36.783  22.793  1.00  7.82           H  
ATOM   1834 HD11 LEU B   5      11.874  35.418  21.423  1.00 10.51           H  
ATOM   1835 HD12 LEU B   5      12.404  36.653  20.616  1.00 10.51           H  
ATOM   1836 HD13 LEU B   5      13.067  35.247  20.421  1.00 10.51           H  
ATOM   1837 HD21 LEU B   5      13.166  34.498  23.308  1.00 11.43           H  
ATOM   1838 HD22 LEU B   5      14.412  34.253  22.389  1.00 11.43           H  
ATOM   1839 HD23 LEU B   5      14.558  35.104  23.697  1.00 11.43           H  
ATOM   1840  N   TRP B   6      17.700  38.935  22.630  1.00  6.20           N  
ANISOU 1840  N   TRP B   6      936    544    736    -56    -18    -61       N  
ATOM   1841  CA  TRP B   6      19.014  39.397  22.241  1.00  6.39           C  
ANISOU 1841  CA  TRP B   6      916    604    762    -69    -47     35       C  
ATOM   1842  C   TRP B   6      20.117  38.428  22.675  1.00  6.96           C  
ANISOU 1842  C   TRP B   6      912    643    931   -117    -35    112       C  
ATOM   1843  O   TRP B   6      21.155  38.347  22.046  1.00 10.17           O  
ANISOU 1843  O   TRP B   6     1016   1270   1348    172    212    471       O  
ATOM   1844  CB  TRP B   6      19.255  40.817  22.839  1.00  7.28           C  
ANISOU 1844  CB  TRP B   6     1056    617    930   -202   -108     65       C  
ATOM   1845  CG  TRP B   6      18.157  41.754  22.450  1.00  6.95           C  
ANISOU 1845  CG  TRP B   6     1143    541    801   -103      5    -39       C  
ATOM   1846  CD1 TRP B   6      17.097  42.108  23.210  1.00  7.88           C  
ANISOU 1846  CD1 TRP B   6     1319    632    864   -102    150    -15       C  
ATOM   1847  CD2 TRP B   6      17.980  42.423  21.179  1.00  6.63           C  
ANISOU 1847  CD2 TRP B   6     1087    469    812    -73      9    -55       C  
ATOM   1848  NE1 TRP B   6      16.255  42.927  22.515  1.00  8.11           N  
ANISOU 1848  NE1 TRP B   6     1194    677   1026     -9    247   -102       N  
ATOM   1849  CE2 TRP B   6      16.782  43.146  21.277  1.00  7.08           C  
ANISOU 1849  CE2 TRP B   6     1046    546    938    -11    103    -48       C  
ATOM   1850  CE3 TRP B   6      18.729  42.492  19.992  1.00  6.62           C  
ANISOU 1850  CE3 TRP B   6      985    483    898    -53     54    -42       C  
ATOM   1851  CZ2 TRP B   6      16.308  43.929  20.224  1.00  7.68           C  
ANISOU 1851  CZ2 TRP B   6     1207    522   1017     56      2    -82       C  
ATOM   1852  CZ3 TRP B   6      18.250  43.284  18.957  1.00  6.94           C  
ANISOU 1852  CZ3 TRP B   6     1169    510    802    -39     45    -69       C  
ATOM   1853  CH2 TRP B   6      17.068  43.991  19.082  1.00  7.26           C  
ANISOU 1853  CH2 TRP B   6     1126    498    970    -53    -83    -26       C  
ATOM   1854  H   TRP B   6      17.250  39.384  23.209  1.00  7.44           H  
ATOM   1855  HA  TRP B   6      19.037  39.469  21.264  1.00  7.67           H  
ATOM   1856  HB2 TRP B   6      19.301  40.757  23.806  1.00  8.74           H  
ATOM   1857  HB3 TRP B   6      20.103  41.163  22.519  1.00  8.74           H  
ATOM   1858  HD1 TRP B   6      16.960  41.832  24.087  1.00  9.45           H  
ATOM   1859  HE1 TRP B   6      15.515  43.251  22.809  1.00  9.73           H  
ATOM   1860  HE3 TRP B   6      19.525  42.019  19.902  1.00  7.95           H  
ATOM   1861  HZ2 TRP B   6      15.504  44.393  20.293  1.00  9.22           H  
ATOM   1862  HZ3 TRP B   6      18.733  43.339  18.164  1.00  8.33           H  
ATOM   1863  HH2 TRP B   6      16.781  44.523  18.374  1.00  8.71           H  
ATOM   1864  N   LYS B   7      19.859  37.707  23.764  1.00  7.23           N  
ANISOU 1864  N   LYS B   7      993    725    867   -157   -144    190       N  
ATOM   1865  CA  LYS B   7      20.701  36.624  24.243  1.00  7.90           C  
ANISOU 1865  CA  LYS B   7      927    781   1117   -161   -242    261       C  
ATOM   1866  C   LYS B   7      19.841  35.355  24.311  1.00  6.41           C  
ANISOU 1866  C   LYS B   7      853    811    627   -142    -74    145       C  
ATOM   1867  O   LYS B   7      18.627  35.403  24.253  1.00  6.40           O  
ANISOU 1867  O   LYS B   7      795    746    744    -72    -61     92       O  
ATOM   1868  CB  LYS B   7      21.331  36.925  25.577  1.00 12.21           C  
ANISOU 1868  CB  LYS B   7     1854    900   1609   -317   -979    173       C  
ATOM   1869  CG ALYS B   7      22.006  38.220  25.785  0.53 16.79           C  
ANISOU 1869  CG ALYS B   7     2111   1263   2624   -549  -1639    374       C  
ATOM   1870  CG BLYS B   7      20.489  37.092  26.753  0.47 16.43           C  
ANISOU 1870  CG BLYS B   7     3075   1449   1347   -288   -711   -269       C  
ATOM   1871  CD ALYS B   7      22.179  38.678  27.249  0.53 29.60           C  
ANISOU 1871  CD ALYS B   7     4442   2704   3430   -936  -2171   -944       C  
ATOM   1872  CD BLYS B   7      21.442  37.490  27.885  0.47 20.94           C  
ANISOU 1872  CD BLYS B   7     3939   1868   1675   -685  -1268     -4       C  
ATOM   1873  CE ALYS B   7      22.917  40.020  27.220  0.53 42.00           C  
ANISOU 1873  CE ALYS B   7     6881   3225   4902  -2055  -3143   -652       C  
ATOM   1874  CE BLYS B   7      20.694  37.539  29.203  0.47 27.69           C  
ANISOU 1874  CE BLYS B   7     4912   3462   1521    143  -1187   -912       C  
ATOM   1875  NZ ALYS B   7      22.144  41.201  27.660  0.53 51.20           N  
ANISOU 1875  NZ ALYS B   7     7639   2426   8231  -1682  -3985   -499       N  
ATOM   1876  NZ BLYS B   7      21.177  38.615  30.079  0.47 36.05           N  
ANISOU 1876  NZ BLYS B   7     5924   5199   1757  -2685   -605   -918       N  
ATOM   1877  H   LYS B   7      19.149  37.895  24.213  1.00  8.68           H  
ATOM   1878  HA  LYS B   7      21.416  36.478  23.589  1.00  9.48           H  
ATOM   1879  HB2ALYS B   7      20.638  36.847  26.251  1.00 14.65           H  
ATOM   1880  HB3ALYS B   7      21.980  36.227  25.756  1.00 14.65           H  
ATOM   1881  HG2ALYS B   7      22.885  38.172  25.377  0.53 20.14           H  
ATOM   1882  HG3ALYS B   7      21.505  38.902  25.311  0.53 20.14           H  
ATOM   1883  HD2ALYS B   7      21.313  38.780  27.673  0.53 35.52           H  
ATOM   1884  HD3ALYS B   7      22.691  38.023  27.748  0.53 35.52           H  
ATOM   1885  HE2ALYS B   7      23.704  39.945  27.782  0.53 50.40           H  
ATOM   1886  HE3ALYS B   7      23.223  40.178  26.313  0.53 50.40           H  
ATOM   1887  HZ1ALYS B   7      22.655  41.927  27.608  0.53 76.80           H  
ATOM   1888  HZ2ALYS B   7      21.431  41.302  27.137  0.53 76.80           H  
ATOM   1889  HZ3ALYS B   7      21.879  41.085  28.502  0.53 76.80           H  
ATOM   1890  N   ARG B   8      20.505  34.209  24.457  1.00  6.78           N  
ANISOU 1890  N   ARG B   8      811    815    798   -116    -54    243       N  
ATOM   1891  CA  ARG B   8      19.753  32.973  24.622  1.00  6.21           C  
ANISOU 1891  CA  ARG B   8      843    739    636   -119    -56    168       C  
ATOM   1892  C   ARG B   8      18.861  33.070  25.856  1.00  5.90           C  
ANISOU 1892  C   ARG B   8      900    619    590    -72    -66     87       C  
ATOM   1893  O   ARG B   8      19.314  33.512  26.918  1.00  6.81           O  
ANISOU 1893  O   ARG B   8      959    803    672   -255    -87     31       O  
ATOM   1894  CB  ARG B   8      20.701  31.797  24.776  1.00  6.61           C  
ANISOU 1894  CB  ARG B   8      930    765    668    -15    -53    147       C  
ATOM   1895  CG  ARG B   8      21.485  31.457  23.527  1.00  7.59           C  
ANISOU 1895  CG  ARG B   8      884   1086    743     91    -55    218       C  
ATOM   1896  CD  ARG B   8      22.523  30.399  23.742  1.00  9.90           C  
ANISOU 1896  CD  ARG B   8     1189   1598    750    482     42    259       C  
ATOM   1897  NE  ARG B   8      23.254  30.144  22.502  1.00  9.98           N  
ANISOU 1897  NE  ARG B   8     1084   1703    780    372   -105    157       N  
ATOM   1898  CZ  ARG B   8      24.469  29.585  22.466  1.00 11.02           C  
ANISOU 1898  CZ  ARG B   8     1208   1866    862    526   -170     43       C  
ATOM   1899  NH1 ARG B   8      25.109  29.252  23.562  1.00 16.88           N  
ANISOU 1899  NH1 ARG B   8     1516   3565    950   1140   -243     18       N  
ATOM   1900  NH2 ARG B   8      25.021  29.407  21.301  1.00 11.82           N  
ANISOU 1900  NH2 ARG B   8      996   2237    990    454   -121     42       N  
ATOM   1901  H   ARG B   8      21.365  34.199  24.455  1.00  8.14           H  
ATOM   1902  HA  ARG B   8      19.192  32.831  23.831  1.00  7.45           H  
ATOM   1903  HB2 ARG B   8      21.326  31.994  25.491  1.00  7.94           H  
ATOM   1904  HB3 ARG B   8      20.188  31.017  25.042  1.00  7.94           H  
ATOM   1905  HG2 ARG B   8      20.868  31.157  22.841  1.00  9.11           H  
ATOM   1906  HG3 ARG B   8      21.919  32.261  23.202  1.00  9.11           H  
ATOM   1907  HD2 ARG B   8      23.142  30.687  24.431  1.00 11.88           H  
ATOM   1908  HD3 ARG B   8      22.096  29.582  24.042  1.00 11.88           H  
ATOM   1909  HE  ARG B   8      22.883  30.363  21.757  1.00 11.98           H  
ATOM   1910 HH11 ARG B   8      25.898  28.913  23.513  1.00 20.25           H  
ATOM   1911 HH12 ARG B   8      24.740  29.372  24.329  1.00 20.25           H  
ATOM   1912 HH21 ARG B   8      25.810  29.069  21.246  1.00 14.18           H  
ATOM   1913 HH22 ARG B   8      24.597  29.628  20.586  1.00 14.18           H  
ATOM   1914  N   PRO B   9      17.630  32.561  25.765  1.00  5.76           N  
ANISOU 1914  N   PRO B   9      893    640    527   -118    -27     38       N  
ATOM   1915  CA  PRO B   9      16.688  32.633  26.920  1.00  6.00           C  
ANISOU 1915  CA  PRO B   9      879    668    596    -73     14    -17       C  
ATOM   1916  C   PRO B   9      16.929  31.467  27.883  1.00  5.75           C  
ANISOU 1916  C   PRO B   9      912    659    485    -77    -11    -43       C  
ATOM   1917  O   PRO B   9      16.177  30.509  27.978  1.00  6.36           O  
ANISOU 1917  O   PRO B   9     1003    675    594   -194    -40    -46       O  
ATOM   1918  CB  PRO B   9      15.317  32.592  26.254  1.00  7.02           C  
ANISOU 1918  CB  PRO B   9      870    974    666    -50      0     84       C  
ATOM   1919  CG  PRO B   9      15.559  31.790  24.996  1.00  6.77           C  
ANISOU 1919  CG  PRO B   9      932    848    641   -171   -117     88       C  
ATOM   1920  CD  PRO B   9      16.892  32.243  24.526  1.00  6.25           C  
ANISOU 1920  CD  PRO B   9      951    742    539    -90    -68     54       C  
ATOM   1921  HA  PRO B   9      16.803  33.483  27.393  1.00  7.20           H  
ATOM   1922  HB2 PRO B   9      14.664  32.157  26.825  1.00  8.43           H  
ATOM   1923  HB3 PRO B   9      15.005  33.486  26.043  1.00  8.43           H  
ATOM   1924  HG2 PRO B   9      15.564  30.839  25.187  1.00  8.13           H  
ATOM   1925  HG3 PRO B   9      14.876  31.974  24.331  1.00  8.13           H  
ATOM   1926  HD2 PRO B   9      17.340  31.541  24.028  1.00  7.50           H  
ATOM   1927  HD3 PRO B   9      16.812  33.027  23.961  1.00  7.50           H  
ATOM   1928  N   LEU B  10      18.034  31.617  28.625  1.00  6.74           N  
ANISOU 1928  N   LEU B  10     1060    754    596   -269   -132     91       N  
ATOM   1929  CA  LEU B  10      18.446  30.636  29.613  1.00  6.88           C  
ANISOU 1929  CA  LEU B  10     1064    840    555   -218   -146    108       C  
ATOM   1930  C   LEU B  10      17.836  30.991  30.952  1.00  7.05           C  
ANISOU 1930  C   LEU B  10     1237    717    565   -164   -188    -33       C  
ATOM   1931  O   LEU B  10      17.801  32.166  31.371  1.00  9.88           O  
ANISOU 1931  O   LEU B  10     2070    695    764   -287    -66    -76       O  
ATOM   1932  CB  LEU B  10      19.981  30.605  29.718  0.94  8.28           C  
ANISOU 1932  CB  LEU B  10     1057   1083    819   -219   -242    231       C  
ATOM   1933  CG  LEU B  10      20.683  30.144  28.442  0.94 11.12           C  
ANISOU 1933  CG  LEU B  10      985   2001    987    -33      5    427       C  
ATOM   1934  CD1 LEU B  10      22.175  30.387  28.470  0.94 15.64           C  
ANISOU 1934  CD1 LEU B  10     1089   1731   2770    -22    315    312       C  
ATOM   1935  CD2 LEU B  10      20.449  28.653  28.179  0.94 14.20           C  
ANISOU 1935  CD2 LEU B  10     1211   2511   1354   -267    296   -757       C  
ATOM   1936  H   LEU B  10      18.517  32.320  28.512  1.00  8.09           H  
ATOM   1937  HA  LEU B  10      18.125  29.752  29.339  1.00  8.26           H  
ATOM   1938  HB2 LEU B  10      20.296  31.494  29.943  0.94  9.94           H  
ATOM   1939  HB3 LEU B  10      20.231  30.011  30.443  0.94  9.94           H  
ATOM   1940  HG  LEU B  10      20.307  30.648  27.690  0.94 13.34           H  
ATOM   1941 HD11 LEU B  10      22.345  31.317  28.633  0.94 23.46           H  
ATOM   1942 HD12 LEU B  10      22.572  29.861  29.168  0.94 23.46           H  
ATOM   1943 HD13 LEU B  10      22.556  30.136  27.625  0.94 23.46           H  
ATOM   1944 HD21 LEU B  10      19.506  28.476  28.157  0.94 21.31           H  
ATOM   1945 HD22 LEU B  10      20.839  28.412  27.336  0.94 21.31           H  
ATOM   1946 HD23 LEU B  10      20.855  28.137  28.879  0.94 21.31           H  
ATOM   1947  N   VAL B  11      17.351  29.971  31.647  1.00  6.26           N  
ANISOU 1947  N   VAL B  11     1132    602    505    -75    -68    -64       N  
ATOM   1948  CA  VAL B  11      16.801  30.106  32.977  1.00  6.40           C  
ANISOU 1948  CA  VAL B  11     1066    706    514     20    -44    -77       C  
ATOM   1949  C   VAL B  11      17.364  28.984  33.847  1.00  5.91           C  
ANISOU 1949  C   VAL B  11      967    669    474    -46    -51    -88       C  
ATOM   1950  O   VAL B  11      17.946  28.021  33.361  1.00  7.89           O  
ANISOU 1950  O   VAL B  11     1560    791    468    199    -31    -69       O  
ATOM   1951  CB  VAL B  11      15.274  30.071  32.975  1.00  8.20           C  
ANISOU 1951  CB  VAL B  11     1077   1248    604    139    -62     54       C  
ATOM   1952  CG1 VAL B  11      14.699  31.218  32.161  1.00 11.07           C  
ANISOU 1952  CG1 VAL B  11     1429   1617    909    503   -192     15       C  
ATOM   1953  CG2 VAL B  11      14.731  28.749  32.547  1.00 10.13           C  
ANISOU 1953  CG2 VAL B  11     1170   1589    861   -301   -178    271       C  
ATOM   1954  H   VAL B  11      17.363  29.190  31.288  1.00  7.52           H  
ATOM   1955  HA  VAL B  11      17.092  30.964  33.349  1.00  7.68           H  
ATOM   1956  HB  VAL B  11      14.987  30.209  33.902  1.00  9.84           H  
ATOM   1957 HG11 VAL B  11      15.073  32.048  32.467  1.00 16.60           H  
ATOM   1958 HG12 VAL B  11      14.915  31.093  31.234  1.00 16.60           H  
ATOM   1959 HG13 VAL B  11      13.745  31.239  32.267  1.00 16.60           H  
ATOM   1960 HG21 VAL B  11      15.118  28.054  33.085  1.00 15.20           H  
ATOM   1961 HG22 VAL B  11      13.777  28.744  32.657  1.00 15.20           H  
ATOM   1962 HG23 VAL B  11      14.947  28.598  31.624  1.00 15.20           H  
ATOM   1963  N   THR B  12      17.133  29.119  35.153  1.00  6.19           N  
ANISOU 1963  N   THR B  12     1034    691    484    -50    -61   -108       N  
ATOM   1964  CA  THR B  12      17.430  28.032  36.068  1.00  6.14           C  
ANISOU 1964  CA  THR B  12      897    837    459     26    -86    -77       C  
ATOM   1965  C   THR B  12      16.181  27.179  36.248  1.00  5.76           C  
ANISOU 1965  C   THR B  12      846    825    387     49    -33    -51       C  
ATOM   1966  O   THR B  12      15.085  27.717  36.447  1.00  7.05           O  
ANISOU 1966  O   THR B  12      917    924    679     95     51     14       O  
ATOM   1967  CB  THR B  12      17.924  28.582  37.417  1.00  8.46           C  
ANISOU 1967  CB  THR B  12     1320   1070    632   -106   -349   -115       C  
ATOM   1968  OG1 THR B  12      19.073  29.409  37.167  1.00 11.23           O  
ANISOU 1968  OG1 THR B  12     1555   1325   1131   -354   -521   -175       O  
ATOM   1969  CG2 THR B  12      18.287  27.463  38.359  1.00 10.62           C  
ANISOU 1969  CG2 THR B  12     1966   1118    710    -15   -582   -126       C  
ATOM   1970  H   THR B  12      16.807  29.855  35.456  1.00  7.42           H  
ATOM   1971  HA  THR B  12      18.136  27.476  35.677  1.00  7.37           H  
ATOM   1972  HB  THR B  12      17.217  29.127  37.821  1.00 10.15           H  
ATOM   1973  HG1 THR B  12      18.865  30.022  36.664  1.00 16.84           H  
ATOM   1974 HG21 THR B  12      17.514  26.917  38.520  1.00 15.92           H  
ATOM   1975 HG22 THR B  12      18.981  26.928  37.967  1.00 15.92           H  
ATOM   1976 HG23 THR B  12      18.597  27.832  39.189  1.00 15.92           H  
ATOM   1977  N   ILE B  13      16.373  25.879  36.207  1.00  5.68           N  
ANISOU 1977  N   ILE B  13      757    845    428     24      9    -68       N  
ATOM   1978  CA  ILE B  13      15.345  24.890  36.517  1.00  5.74           C  
ANISOU 1978  CA  ILE B  13      805    840    408     20    -53    -13       C  
ATOM   1979  C   ILE B  13      15.779  24.123  37.765  1.00  5.61           C  
ANISOU 1979  C   ILE B  13      769    849    386     39    -30    -64       C  
ATOM   1980  O   ILE B  13      16.937  24.105  38.140  1.00  6.62           O  
ANISOU 1980  O   ILE B  13      816   1080    470    -27    -69     37       O  
ATOM   1981  CB  ILE B  13      15.102  23.936  35.322  1.00  6.01           C  
ANISOU 1981  CB  ILE B  13      823    914    410    -31    -23    -64       C  
ATOM   1982  CG1 ILE B  13      16.300  23.031  35.039  1.00  6.65           C  
ANISOU 1982  CG1 ILE B  13      902    935    537     40    -60   -110       C  
ATOM   1983  CG2 ILE B  13      14.708  24.749  34.093  1.00  6.97           C  
ANISOU 1983  CG2 ILE B  13      950   1134    407    110    -84   -108       C  
ATOM   1984  CD1 ILE B  13      16.037  21.888  34.078  1.00  7.46           C  
ANISOU 1984  CD1 ILE B  13     1115    905    647    -27    -68   -114       C  
ATOM   1985  H   ILE B  13      17.153  25.593  35.984  1.00  6.82           H  
ATOM   1986  HA  ILE B  13      14.509  25.360  36.715  1.00  6.89           H  
ATOM   1987  HB  ILE B  13      14.343  23.360  35.553  1.00  7.21           H  
ATOM   1988 HG12 ILE B  13      17.018  23.575  34.679  1.00  7.97           H  
ATOM   1989 HG13 ILE B  13      16.610  22.659  35.880  1.00  7.97           H  
ATOM   1990 HG21 ILE B  13      13.954  25.305  34.306  1.00 10.46           H  
ATOM   1991 HG22 ILE B  13      15.446  25.300  33.824  1.00 10.46           H  
ATOM   1992 HG23 ILE B  13      14.475  24.154  33.377  1.00 10.46           H  
ATOM   1993 HD11 ILE B  13      16.841  21.376  33.961  1.00 11.20           H  
ATOM   1994 HD12 ILE B  13      15.347  21.323  34.434  1.00 11.20           H  
ATOM   1995 HD13 ILE B  13      15.756  22.241  33.230  1.00 11.20           H  
ATOM   1996  N   LYS B  14      14.795  23.461  38.367  1.00  6.00           N  
ANISOU 1996  N   LYS B  14      793    902    449     32    -27      7       N  
ATOM   1997  CA  LYS B  14      15.082  22.539  39.478  1.00  5.74           C  
ANISOU 1997  CA  LYS B  14      825    830    398     41    -79    -15       C  
ATOM   1998  C   LYS B  14      14.427  21.205  39.164  1.00  6.00           C  
ANISOU 1998  C   LYS B  14      905    836    402     72    -44    -47       C  
ATOM   1999  O   LYS B  14      13.216  21.150  38.905  1.00  6.51           O  
ANISOU 1999  O   LYS B  14      837    878    613     51   -101    -68       O  
ATOM   2000  CB  LYS B  14      14.595  23.066  40.825  1.00  6.13           C  
ANISOU 2000  CB  LYS B  14      949    841    402    -15    -37    -54       C  
ATOM   2001  CG  LYS B  14      14.986  22.146  41.975  1.00  7.08           C  
ANISOU 2001  CG  LYS B  14     1149    942    440     29    -80    -16       C  
ATOM   2002  CD  LYS B  14      14.818  22.779  43.348  1.00  7.52           C  
ANISOU 2002  CD  LYS B  14     1217   1024    445     75    -87    -24       C  
ATOM   2003  CE ALYS B  14      13.407  22.937  43.816  0.30  8.83           C  
ANISOU 2003  CE ALYS B  14     1340   1357    457    116    160    115       C  
ATOM   2004  CE BLYS B  14      13.458  23.220  43.632  0.70  6.91           C  
ANISOU 2004  CE BLYS B  14     1136    864    468     -6   -145    -14       C  
ATOM   2005  NZ ALYS B  14      13.410  23.453  45.233  0.30 14.33           N  
ANISOU 2005  NZ ALYS B  14     1623   2289   1210  -1131    734  -1057       N  
ATOM   2006  NZ BLYS B  14      13.373  23.690  45.083  0.70  7.84           N  
ANISOU 2006  NZ BLYS B  14     1241   1140    422    169   -108    -18       N  
ATOM   2007  H   LYS B  14      13.983  23.573  38.105  1.00  7.20           H  
ATOM   2008  HA  LYS B  14      16.051  22.405  39.528  1.00  6.89           H  
ATOM   2009  HB2 LYS B  14      14.972  23.946  40.979  1.00  7.36           H  
ATOM   2010  HB3 LYS B  14      13.629  23.156  40.803  1.00  7.36           H  
ATOM   2011  HG2 LYS B  14      14.443  21.343  41.932  1.00  8.50           H  
ATOM   2012  HG3 LYS B  14      15.913  21.881  41.863  1.00  8.50           H  
ATOM   2013  HD2ALYS B  14      15.297  22.238  43.995  1.00  9.02           H  
ATOM   2014  HD3ALYS B  14      15.236  23.654  43.334  1.00  9.02           H  
ATOM   2015  HE2ALYS B  14      12.936  23.560  43.240  0.30 10.59           H  
ATOM   2016  HE2BLYS B  14      13.217  23.947  43.036  0.70  8.29           H  
ATOM   2017  HE3ALYS B  14      12.949  22.083  43.778  0.30 10.59           H  
ATOM   2018  HE3BLYS B  14      12.838  22.489  43.486  0.70  8.29           H  
ATOM   2019  HZ1ALYS B  14      12.571  23.548  45.516  0.30 21.50           H  
ATOM   2020  HZ1BLYS B  14      12.543  23.960  45.259  0.70 11.76           H  
ATOM   2021  HZ2ALYS B  14      13.836  22.874  45.758  0.30 21.50           H  
ATOM   2022  HZ2BLYS B  14      13.588  23.018  45.626  0.70 11.76           H  
ATOM   2023  HZ3ALYS B  14      13.824  24.240  45.261  0.30 21.50           H  
ATOM   2024  HZ3BLYS B  14      13.938  24.366  45.210  0.70 11.76           H  
ATOM   2025  N  AILE B  15      15.126  20.100  39.138  0.23  5.85           N  
ANISOU 2025  N  AILE B  15      665    730    697   -150   -231   -122       N  
ATOM   2026  N  BILE B  15      15.243  20.151  39.225  0.77  6.52           N  
ANISOU 2026  N  BILE B  15      992    833    505    102    -94   -102       N  
ATOM   2027  CA AILE B  15      14.680  18.739  38.996  0.23  7.75           C  
ANISOU 2027  CA AILE B  15     1003    691   1075   -139   -340   -231       C  
ATOM   2028  CA BILE B  15      14.736  18.832  38.916  0.77  7.08           C  
ANISOU 2028  CA BILE B  15     1062    867    601    145    -65    -81       C  
ATOM   2029  C  AILE B  15      15.549  17.938  39.944  0.23  8.67           C  
ANISOU 2029  C  AILE B  15     1102    541   1455    152   -341   -249       C  
ATOM   2030  C  BILE B  15      15.524  17.873  39.768  0.77  8.65           C  
ANISOU 2030  C  BILE B  15     1351    875    866     87   -394    -97       C  
ATOM   2031  O  AILE B  15      16.720  18.206  40.129  0.23 10.95           O  
ANISOU 2031  O  AILE B  15      988   1348   1578    313   -440  -1071       O  
ATOM   2032  O  BILE B  15      16.763  18.001  39.878  0.77  8.74           O  
ANISOU 2032  O  BILE B  15     1342    829    953    223   -320   -131       O  
ATOM   2033  CB AILE B  15      14.976  18.004  37.688  0.23  8.99           C  
ANISOU 2033  CB AILE B  15     1011    793   1407    154   -300   -520       C  
ATOM   2034  CB BILE B  15      14.812  18.536  37.397  0.77  6.64           C  
ANISOU 2034  CB BILE B  15     1003    707    661    115    -70   -119       C  
ATOM   2035  CG1AILE B  15      14.676  18.898  36.502  0.23 12.15           C  
ANISOU 2035  CG1AILE B  15     1603   1565   1172    291   -404   -400       C  
ATOM   2036  CG1BILE B  15      14.178  17.193  37.093  0.77  7.48           C  
ANISOU 2036  CG1BILE B  15     1112    829    732     23     22    -71       C  
ATOM   2037  CG2AILE B  15      14.265  16.660  37.555  0.23 12.51           C  
ANISOU 2037  CG2AILE B  15     1448   1306   1716   -412    185   -963       C  
ATOM   2038  CG2BILE B  15      16.217  18.650  36.829  0.77  7.85           C  
ANISOU 2038  CG2BILE B  15     1168   1006    630    -57    -15   -147       C  
ATOM   2039  CD1AILE B  15      15.012  18.200  35.200  0.23 12.13           C  
ANISOU 2039  CD1AILE B  15     1180   1716   1437    350   -158   -471       C  
ATOM   2040  CD1BILE B  15      14.042  16.866  35.619  0.77  7.82           C  
ANISOU 2040  CD1BILE B  15     1069    957    770    -64   -108   -243       C  
ATOM   2041  H  AILE B  15      15.976  20.202  39.218  0.23  7.02           H  
ATOM   2042  H  BILE B  15      16.067  20.256  39.448  0.77  7.83           H  
ATOM   2043  HA AILE B  15      13.734  18.655  39.236  0.23  9.30           H  
ATOM   2044  HA BILE B  15      13.797  18.790  39.192  0.77  8.49           H  
ATOM   2045  HB AILE B  15      15.938  17.821  37.673  0.23 10.78           H  
ATOM   2046  HB BILE B  15      14.267  19.216  36.948  0.77  7.96           H  
ATOM   2047 HG12AILE B  15      13.737  19.138  36.507  0.23 14.58           H  
ATOM   2048 HG12BILE B  15      14.710  16.500  37.514  0.77  8.98           H  
ATOM   2049 HG13AILE B  15      15.195  19.714  36.574  0.23 14.58           H  
ATOM   2050 HG13BILE B  15      13.296  17.170  37.496  0.77  8.98           H  
ATOM   2051 HG21AILE B  15      14.470  16.113  38.317  0.23 18.76           H  
ATOM   2052 HG21BILE B  15      16.580  19.512  37.044  0.77 11.77           H  
ATOM   2053 HG22AILE B  15      13.317  16.802  37.509  0.23 18.76           H  
ATOM   2054 HG22BILE B  15      16.772  17.965  37.209  0.77 11.77           H  
ATOM   2055 HG23AILE B  15      14.561  16.219  36.755  0.23 18.76           H  
ATOM   2056 HG23BILE B  15      16.186  18.544  35.876  0.77 11.77           H  
ATOM   2057 HD11AILE B  15      14.815  18.783  34.463  0.23 18.19           H  
ATOM   2058 HD11BILE B  15      13.633  16.003  35.520  0.77 11.74           H  
ATOM   2059 HD12AILE B  15      15.945  17.974  35.189  0.23 18.19           H  
ATOM   2060 HD12BILE B  15      13.494  17.530  35.193  0.77 11.74           H  
ATOM   2061 HD13AILE B  15      14.489  17.398  35.122  0.23 18.19           H  
ATOM   2062 HD13BILE B  15      14.911  16.858  35.211  0.77 11.74           H  
ATOM   2063  N   GLY B  16      14.887  16.948  40.445  1.00 11.48           N  
ANISOU 2063  N   GLY B  16     1640    913   1550    -73   -693    253       N  
ATOM   2064  CA  GLY B  16      15.610  16.003  41.319  1.00 13.99           C  
ANISOU 2064  CA  GLY B  16     1930    941   2128    -98  -1002    403       C  
ATOM   2065  C   GLY B  16      16.313  16.746  42.444  1.00 12.59           C  
ANISOU 2065  C   GLY B  16     1860   1227   1413   -139   -668    573       C  
ATOM   2066  O   GLY B  16      17.325  16.281  42.958  1.00 15.45           O  
ANISOU 2066  O   GLY B  16     2096   1434   1991    -22   -940    540       O  
ATOM   2067  H  AGLY B  16      14.051  16.842  40.275  1.00 13.78           H  
ATOM   2068  HA2 GLY B  16      14.984  15.364  41.694  1.00 16.79           H  
ATOM   2069  HA3 GLY B  16      16.264  15.512  40.796  1.00 16.79           H  
ATOM   2070  N   GLY B  17      15.822  17.907  42.901  1.00 11.75           N  
ANISOU 2070  N   GLY B  17     1639   1308   1253   -285   -443    481       N  
ATOM   2071  CA  GLY B  17      16.425  18.668  43.955  1.00 11.45           C  
ANISOU 2071  CA  GLY B  17     1546   1588    958   -210   -164    457       C  
ATOM   2072  C   GLY B  17      17.599  19.508  43.584  1.00  9.73           C  
ANISOU 2072  C   GLY B  17     1440   1149    888    -40   -247    167       C  
ATOM   2073  O   GLY B  17      18.227  20.155  44.434  1.00 11.70           O  
ANISOU 2073  O   GLY B  17     1862   1534    783   -224   -295     17       O  
ATOM   2074  H   GLY B  17      15.103  18.213  42.541  1.00 14.11           H  
ATOM   2075  HA2 GLY B  17      15.747  19.248  44.335  1.00 13.74           H  
ATOM   2076  HA3 GLY B  17      16.702  18.052  44.651  1.00 13.74           H  
ATOM   2077  N   GLN B  18      17.973  19.483  42.289  1.00  8.94           N  
ANISOU 2077  N   GLN B  18     1262   1152    782    -16   -217    136       N  
ATOM   2078  CA  GLN B  18      19.175  20.109  41.793  1.00  9.45           C  
ANISOU 2078  CA  GLN B  18     1104   1282    990     62   -263    201       C  
ATOM   2079  C   GLN B  18      18.836  21.230  40.840  1.00  7.60           C  
ANISOU 2079  C   GLN B  18     1024   1123    569    109   -162    -21       C  
ATOM   2080  O   GLN B  18      17.937  21.095  40.009  1.00  8.26           O  
ANISOU 2080  O   GLN B  18     1010   1116    827     62   -251    -11       O  
ATOM   2081  CB  GLN B  18      20.053  19.108  41.033  1.00 15.02           C  
ANISOU 2081  CB  GLN B  18     1428   1629   2312    632    355    540       C  
ATOM   2082  CG  GLN B  18      20.522  17.920  41.842  1.00 29.92           C  
ANISOU 2082  CG  GLN B  18     2992   2160   5537   1214    431   1897       C  
ATOM   2083  CD  GLN B  18      20.927  16.667  41.055  1.00 49.62           C  
ANISOU 2083  CD  GLN B  18     5937   3394   8399   3407   1531   1192       C  
ATOM   2084  OE1 GLN B  18      21.640  16.640  40.047  1.00 53.20           O  
ANISOU 2084  OE1 GLN B  18     3443   5864   9704   1204   1583  -1365       O  
ATOM   2085  NE2 GLN B  18      20.438  15.480  41.532  1.00 63.20           N  
ANISOU 2085  NE2 GLN B  18    10045   2832   9707   1431   2950  -1007       N  
ATOM   2086  H   GLN B  18      17.467  19.072  41.728  1.00 10.73           H  
ATOM   2087  HA  GLN B  18      19.683  20.473  42.548  1.00 11.34           H  
ATOM   2088  HB2 GLN B  18      19.554  18.781  40.267  1.00 18.03           H  
ATOM   2089  HB3 GLN B  18      20.832  19.577  40.695  1.00 18.03           H  
ATOM   2090  HG2 GLN B  18      21.283  18.199  42.375  1.00 35.90           H  
ATOM   2091  HG3 GLN B  18      19.813  17.674  42.457  1.00 35.90           H  
ATOM   2092 HE21 GLN B  18      20.630  14.744  41.132  1.00 75.84           H  
ATOM   2093 HE22 GLN B  18      19.939  15.472  42.233  1.00 75.84           H  
ATOM   2094  N   LEU B  19      19.617  22.284  40.914  1.00  7.62           N  
ANISOU 2094  N   LEU B  19      928   1288    506     43   -178     63       N  
ATOM   2095  CA  LEU B  19      19.501  23.411  39.974  1.00  7.32           C  
ANISOU 2095  CA  LEU B  19      917   1265    434     91   -114    -14       C  
ATOM   2096  C   LEU B  19      20.349  23.153  38.744  1.00  7.70           C  
ANISOU 2096  C   LEU B  19      846   1408    497    101    -84     44       C  
ATOM   2097  O   LEU B  19      21.491  22.701  38.830  1.00 10.19           O  
ANISOU 2097  O   LEU B  19     1006   2007    630    454    -82    129       O  
ATOM   2098  CB  LEU B  19      19.961  24.706  40.622  1.00  7.83           C  
ANISOU 2098  CB  LEU B  19     1009   1301    488    -33   -102     31       C  
ATOM   2099  CG  LEU B  19      19.211  25.135  41.884  1.00  8.33           C  
ANISOU 2099  CG  LEU B  19     1198   1361    418    -30   -102    -23       C  
ATOM   2100  CD1 LEU B  19      19.734  26.462  42.364  1.00  9.84           C  
ANISOU 2100  CD1 LEU B  19     1367   1434    716    -81    -89   -172       C  
ATOM   2101  CD2 LEU B  19      17.698  25.174  41.668  1.00  8.70           C  
ANISOU 2101  CD2 LEU B  19     1147   1458    503    123     29    -36       C  
ATOM   2102  H   LEU B  19      20.214  22.316  41.531  1.00  9.14           H  
ATOM   2103  HA  LEU B  19      18.564  23.505  39.702  1.00  8.79           H  
ATOM   2104  HB2 LEU B  19      20.901  24.617  40.844  1.00  9.40           H  
ATOM   2105  HB3 LEU B  19      19.883  25.417  39.967  1.00  9.40           H  
ATOM   2106  HG  LEU B  19      19.395  24.471  42.582  1.00 10.00           H  
ATOM   2107 HD11 LEU B  19      19.259  26.725  43.156  1.00 14.76           H  
ATOM   2108 HD12 LEU B  19      20.670  26.384  42.563  1.00 14.76           H  
ATOM   2109 HD13 LEU B  19      19.606  27.123  41.680  1.00 14.76           H  
ATOM   2110 HD21 LEU B  19      17.396  24.316  41.363  1.00 13.04           H  
ATOM   2111 HD22 LEU B  19      17.262  25.392  42.495  1.00 13.04           H  
ATOM   2112 HD23 LEU B  19      17.487  25.841  41.010  1.00 13.04           H  
ATOM   2113  N   LYS B  20      19.770  23.472  37.575  1.00  6.72           N  
ANISOU 2113  N   LYS B  20      869   1080    452    132    -53    -14       N  
ATOM   2114  CA  LYS B  20      20.443  23.333  36.295  1.00  6.81           C  
ANISOU 2114  CA  LYS B  20      848   1102    486     93     29      5       C  
ATOM   2115  C   LYS B  20      20.058  24.515  35.432  1.00  6.09           C  
ANISOU 2115  C   LYS B  20      720    958    497    -20    -81    -83       C  
ATOM   2116  O   LYS B  20      19.018  25.123  35.608  1.00  7.41           O  
ANISOU 2116  O   LYS B  20      868    979    800     85    104    120       O  
ATOM   2117  CB  LYS B  20      20.017  22.027  35.570  1.00  8.02           C  
ANISOU 2117  CB  LYS B  20     1263   1021    581    169    142    -27       C  
ATOM   2118  CG  LYS B  20      20.313  20.772  36.353  1.00 10.71           C  
ANISOU 2118  CG  LYS B  20     1773   1105    951    192    131    105       C  
ATOM   2119  CD  LYS B  20      19.769  19.547  35.663  1.00 14.21           C  
ANISOU 2119  CD  LYS B  20     2531   1053   1495    -32    564   -161       C  
ATOM   2120  CE  LYS B  20      19.727  18.280  36.511  1.00 21.46           C  
ANISOU 2120  CE  LYS B  20     2327   1405   3937    -16   -557    907       C  
ATOM   2121  NZ  LYS B  20      21.016  17.637  36.372  1.00 27.49           N  
ANISOU 2121  NZ  LYS B  20     2702   3780   3342    963    602   1849       N  
ATOM   2122  H   LYS B  20      18.964  23.772  37.584  1.00  8.06           H  
ATOM   2123  HA  LYS B  20      21.413  23.330  36.433  1.00  8.18           H  
ATOM   2124  HB2 LYS B  20      19.065  22.066  35.390  1.00  9.62           H  
ATOM   2125  HB3 LYS B  20      20.477  21.979  34.717  1.00  9.62           H  
ATOM   2126  HG2 LYS B  20      21.272  20.680  36.461  1.00 12.86           H  
ATOM   2127  HG3 LYS B  20      19.918  20.844  37.236  1.00 12.86           H  
ATOM   2128  HD2 LYS B  20      18.870  19.741  35.357  1.00 17.06           H  
ATOM   2129  HD3 LYS B  20      20.312  19.371  34.878  1.00 17.06           H  
ATOM   2130  HE2 LYS B  20      19.560  18.503  37.440  1.00 25.75           H  
ATOM   2131  HE3 LYS B  20      19.021  17.691  36.202  1.00 25.75           H  
ATOM   2132  HZ1 LYS B  20      21.029  16.890  36.856  1.00 41.24           H  
ATOM   2133  HZ2 LYS B  20      21.158  17.438  35.516  1.00 41.24           H  
ATOM   2134  HZ3 LYS B  20      21.655  18.187  36.658  1.00 41.24           H  
ATOM   2135  N   GLU B  21      20.881  24.822  34.433  1.00  6.72           N  
ANISOU 2135  N   GLU B  21      811   1079    511    109    -39     20       N  
ATOM   2136  CA  GLU B  21      20.557  25.838  33.440  1.00  6.49           C  
ANISOU 2136  CA  GLU B  21      901    937    481    -38    -90    -32       C  
ATOM   2137  C   GLU B  21      19.841  25.177  32.257  1.00  5.81           C  
ANISOU 2137  C   GLU B  21      836    766    474    -28    -31    -46       C  
ATOM   2138  O   GLU B  21      20.244  24.108  31.829  1.00  7.05           O  
ANISOU 2138  O   GLU B  21      899    926    694    152   -188   -161       O  
ATOM   2139  CB  GLU B  21      21.856  26.482  32.946  1.00  8.77           C  
ANISOU 2139  CB  GLU B  21     1097   1315    721   -379   -184     91       C  
ATOM   2140  CG AGLU B  21      21.671  27.560  31.903  0.58  9.07           C  
ANISOU 2140  CG AGLU B  21     1132   1172    938   -367   -185    329       C  
ATOM   2141  CG BGLU B  21      22.457  27.387  34.060  0.42 18.08           C  
ANISOU 2141  CG BGLU B  21     1673   2560   2229   -726    315  -1522       C  
ATOM   2142  CD AGLU B  21      23.037  28.115  31.451  0.58 10.80           C  
ANISOU 2142  CD AGLU B  21     1268   1485   1105   -590   -214    246       C  
ATOM   2143  CD BGLU B  21      21.680  28.480  34.758  0.42 18.17           C  
ANISOU 2143  CD BGLU B  21     2467   1876   2149   -386    637   -561       C  
ATOM   2144  OE1AGLU B  21      23.322  29.138  32.065  0.58 18.61           O  
ANISOU 2144  OE1AGLU B  21     2706   2620   1325  -1876    248   -366       O  
ATOM   2145  OE1BGLU B  21      21.783  29.648  34.284  0.42 31.17           O  
ANISOU 2145  OE1BGLU B  21     5821   2419   2898    389   1356    403       O  
ATOM   2146  OE2AGLU B  21      23.689  27.621  30.516  0.58 12.45           O  
ANISOU 2146  OE2AGLU B  21     1430   1713   1305   -438    152    314       O  
ATOM   2147  OE2BGLU B  21      21.114  28.192  35.821  0.42 12.72           O  
ANISOU 2147  OE2BGLU B  21     1164   1634   1748   -394    259   -850       O  
ATOM   2148  H   GLU B  21      21.631  24.405  34.371  1.00  8.06           H  
ATOM   2149  HA  GLU B  21      19.978  26.520  33.839  1.00  7.79           H  
ATOM   2150  HB2AGLU B  21      22.319  26.865  33.708  1.00 10.52           H  
ATOM   2151  HB3AGLU B  21      22.424  25.788  32.577  1.00 10.52           H  
ATOM   2152  HG2AGLU B  21      21.200  27.194  31.138  0.58 10.89           H  
ATOM   2153  HG3AGLU B  21      21.134  28.279  32.270  0.58 10.89           H  
ATOM   2154  N   ALA B  22      18.825  25.833  31.726  1.00  5.50           N  
ANISOU 2154  N   ALA B  22      838    673    454      3    -36    -44       N  
ATOM   2155  CA  ALA B  22      18.112  25.290  30.574  1.00  5.11           C  
ANISOU 2155  CA  ALA B  22      794    590    440     11    -31     -3       C  
ATOM   2156  C   ALA B  22      17.600  26.423  29.688  1.00  5.21           C  
ANISOU 2156  C   ALA B  22      826    615    422      2     22     -9       C  
ATOM   2157  O   ALA B  22      17.429  27.560  30.102  1.00  7.70           O  
ANISOU 2157  O   ALA B  22     1681    605    467    112    -14    -77       O  
ATOM   2158  CB  ALA B  22      16.965  24.401  31.013  1.00  5.89           C  
ANISOU 2158  CB  ALA B  22      802    778    525    -18    -16    101       C  
ATOM   2159  H   ALA B  22      18.582  26.586  32.062  1.00  6.60           H  
ATOM   2160  HA  ALA B  22      18.739  24.748  30.050  1.00  6.13           H  
ATOM   2161  HB1 ALA B  22      16.512  24.057  30.240  1.00  8.84           H  
ATOM   2162  HB2 ALA B  22      17.307  23.671  31.535  1.00  8.84           H  
ATOM   2163  HB3 ALA B  22      16.349  24.912  31.544  1.00  8.84           H  
ATOM   2164  N   LEU B  23      17.343  26.067  28.439  1.00  4.91           N  
ANISOU 2164  N   LEU B  23      787    496    471     39    -56    -11       N  
ATOM   2165  CA  LEU B  23      16.946  26.968  27.373  1.00  4.66           C  
ANISOU 2165  CA  LEU B  23      726    485    453    -75    -15      0       C  
ATOM   2166  C   LEU B  23      15.441  26.916  27.159  1.00  4.68           C  
ANISOU 2166  C   LEU B  23      765    510    397    -13    -16      5       C  
ATOM   2167  O   LEU B  23      14.893  25.829  26.900  1.00  5.74           O  
ANISOU 2167  O   LEU B  23      840    496    715    -93    -64     -6       O  
ATOM   2168  CB  LEU B  23      17.695  26.530  26.116  1.00  5.19           C  
ANISOU 2168  CB  LEU B  23      768    573    513    -19     32     14       C  
ATOM   2169  CG  LEU B  23      17.463  27.354  24.865  1.00  5.96           C  
ANISOU 2169  CG  LEU B  23      841    731    555     80     64    110       C  
ATOM   2170  CD1 LEU B  23      18.099  28.732  24.991  1.00  8.02           C  
ANISOU 2170  CD1 LEU B  23     1391    703    772     28    266    178       C  
ATOM   2171  CD2 LEU B  23      18.074  26.602  23.673  1.00  7.02           C  
ANISOU 2171  CD2 LEU B  23     1056    924    531    171     62     90       C  
ATOM   2172  H   LEU B  23      17.417  25.233  28.243  1.00  5.89           H  
ATOM   2173  HA  LEU B  23      17.210  27.883  27.606  1.00  5.59           H  
ATOM   2174  HB2 LEU B  23      18.645  26.540  26.312  1.00  6.23           H  
ATOM   2175  HB3 LEU B  23      17.450  25.612  25.923  1.00  6.23           H  
ATOM   2176  HG  LEU B  23      16.499  27.456  24.721  1.00  7.15           H  
ATOM   2177 HD11 LEU B  23      17.939  29.233  24.188  1.00 12.03           H  
ATOM   2178 HD12 LEU B  23      17.715  29.194  25.739  1.00 12.03           H  
ATOM   2179 HD13 LEU B  23      19.045  28.636  25.125  1.00 12.03           H  
ATOM   2180 HD21 LEU B  23      17.937  27.109  22.870  1.00 10.54           H  
ATOM   2181 HD22 LEU B  23      19.015  26.482  23.819  1.00 10.54           H  
ATOM   2182 HD23 LEU B  23      17.652  25.744  23.586  1.00 10.54           H  
ATOM   2183  N   LEU B  24      14.773  28.061  27.189  1.00  4.65           N  
ANISOU 2183  N   LEU B  24      742    485    433    -45    -59    -40       N  
ATOM   2184  CA  LEU B  24      13.340  28.116  26.869  1.00  4.82           C  
ANISOU 2184  CA  LEU B  24      726    548    446    -17    -63    -38       C  
ATOM   2185  C   LEU B  24      13.199  28.115  25.344  1.00  4.72           C  
ANISOU 2185  C   LEU B  24      728    514    445    -35    -81    -22       C  
ATOM   2186  O   LEU B  24      13.591  29.075  24.687  1.00  5.89           O  
ANISOU 2186  O   LEU B  24     1071    538    494   -191   -132     43       O  
ATOM   2187  CB  LEU B  24      12.695  29.371  27.461  1.00  5.63           C  
ANISOU 2187  CB  LEU B  24      756    652    603     36    -55   -140       C  
ATOM   2188  CG  LEU B  24      12.820  29.515  28.986  1.00  6.67           C  
ANISOU 2188  CG  LEU B  24      845    949    591     19    -29   -246       C  
ATOM   2189  CD1 LEU B  24      12.084  30.790  29.393  1.00 12.82           C  
ANISOU 2189  CD1 LEU B  24     1562   1975   1045    842   -348   -921       C  
ATOM   2190  CD2 LEU B  24      12.283  28.278  29.707  1.00 10.50           C  
ANISOU 2190  CD2 LEU B  24     1397   1879    478   -716     46   -173       C  
ATOM   2191  H   LEU B  24      15.186  28.785  27.401  1.00  5.58           H  
ATOM   2192  HA  LEU B  24      12.896  27.322  27.234  1.00  5.78           H  
ATOM   2193  HB2 LEU B  24      13.098  30.149  27.045  1.00  6.75           H  
ATOM   2194  HB3 LEU B  24      11.753  29.372  27.228  1.00  6.75           H  
ATOM   2195  HG  LEU B  24      13.768  29.619  29.211  1.00  8.01           H  
ATOM   2196 HD11 LEU B  24      12.453  31.538  28.917  1.00 19.23           H  
ATOM   2197 HD12 LEU B  24      11.152  30.704  29.180  1.00 19.23           H  
ATOM   2198 HD13 LEU B  24      12.185  30.930  30.337  1.00 19.23           H  
ATOM   2199 HD21 LEU B  24      12.773  27.503  29.422  1.00 15.76           H  
ATOM   2200 HD22 LEU B  24      12.386  28.390  30.655  1.00 15.76           H  
ATOM   2201 HD23 LEU B  24      11.353  28.164  29.498  1.00 15.76           H  
ATOM   2202  N   ASP B  25      12.639  27.018  24.808  1.00  4.35           N  
ANISOU 2202  N   ASP B  25      678    487    390    -43     10     13       N  
ATOM   2203  CA  ASP B  25      12.768  26.722  23.386  1.00  4.53           C  
ANISOU 2203  CA  ASP B  25      774    468    376    -71      2      2       C  
ATOM   2204  C   ASP B  25      11.388  26.470  22.755  1.00  4.58           C  
ANISOU 2204  C   ASP B  25      814    475    348    -71     12     -4       C  
ATOM   2205  O   ASP B  25      10.854  25.361  22.789  1.00  4.79           O  
ANISOU 2205  O   ASP B  25      801    469    440    -68    -51      6       O  
ATOM   2206  CB  ASP B  25      13.654  25.507  23.227  1.00  4.98           C  
ANISOU 2206  CB  ASP B  25      792    506    481    -16     35      9       C  
ATOM   2207  CG AASP B  25      13.706  25.159  21.742  0.49  4.74           C  
ANISOU 2207  CG AASP B  25      740    508    445    -39     91     46       C  
ATOM   2208  CG BASP B  25      14.229  25.218  21.851  0.52  5.36           C  
ANISOU 2208  CG BASP B  25      918    495    504   -142    129     30       C  
ATOM   2209  OD1AASP B  25      13.229  25.872  20.855  0.49  5.20           O  
ANISOU 2209  OD1AASP B  25      887    649    323   -103     50     62       O  
ATOM   2210  OD1BASP B  25      13.519  25.783  20.956  0.52  6.27           O  
ANISOU 2210  OD1BASP B  25      944    697    601     13     24   -107       O  
ATOM   2211  OD2AASP B  25      14.413  24.140  21.464  0.49  4.56           O  
ANISOU 2211  OD2AASP B  25      682    507    438     22     44    -39       O  
ATOM   2212  OD2BASP B  25      15.246  24.513  21.687  0.52  5.96           O  
ANISOU 2212  OD2BASP B  25      896    700    533    126     85    -68       O  
ATOM   2213  H   ASP B  25      12.197  26.480  25.312  1.00  5.22           H  
ATOM   2214  HA  ASP B  25      13.190  27.485  22.938  1.00  5.43           H  
ATOM   2215  HB2AASP B  25      14.546  25.697  23.557  1.00  5.97           H  
ATOM   2216  HB3AASP B  25      13.292  24.762  23.732  1.00  5.97           H  
ATOM   2217  N   THR B  26      10.841  27.520  22.115  1.00  4.71           N  
ANISOU 2217  N   THR B  26      764    456    464    -68    -49     -2       N  
ATOM   2218  CA  THR B  26       9.560  27.381  21.451  1.00  4.77           C  
ANISOU 2218  CA  THR B  26      746    527    430    -66    -23     -7       C  
ATOM   2219  C   THR B  26       9.603  26.489  20.213  1.00  5.00           C  
ANISOU 2219  C   THR B  26      838    470    478     -3   -105     23       C  
ATOM   2220  O   THR B  26       8.535  26.080  19.739  1.00  6.06           O  
ANISOU 2220  O   THR B  26      862    685    618     28   -185    -97       O  
ATOM   2221  CB  THR B  26       8.984  28.752  21.057  1.00  4.81           C  
ANISOU 2221  CB  THR B  26      655    583    483    -15     63     50       C  
ATOM   2222  OG1 THR B  26       9.898  29.414  20.158  1.00  4.89           O  
ANISOU 2222  OG1 THR B  26      705    536    508     17     56     62       O  
ATOM   2223  CG2 THR B  26       8.764  29.642  22.264  1.00  5.29           C  
ANISOU 2223  CG2 THR B  26      749    576    566    -34    107    -46       C  
ATOM   2224  H   THR B  26      11.253  28.275  22.099  1.00  5.65           H  
ATOM   2225  HA  THR B  26       8.939  26.972  22.089  1.00  5.72           H  
ATOM   2226  HB  THR B  26       8.128  28.618  20.599  1.00  5.78           H  
ATOM   2227  HG1 THR B  26      10.024  28.942  19.499  1.00  7.34           H  
ATOM   2228 HG21 THR B  26       8.157  29.213  22.871  1.00  7.94           H  
ATOM   2229 HG22 THR B  26       9.603  29.796  22.705  1.00  7.94           H  
ATOM   2230 HG23 THR B  26       8.393  30.481  21.980  1.00  7.94           H  
ATOM   2231  N   GLY B  27      10.796  26.220  19.689  1.00  4.91           N  
ANISOU 2231  N   GLY B  27      833    513    409      7    -68    -19       N  
ATOM   2232  CA  GLY B  27      10.946  25.312  18.568  1.00  5.37           C  
ANISOU 2232  CA  GLY B  27      884    594    442     79    -89    -63       C  
ATOM   2233  C   GLY B  27      10.965  23.847  18.932  1.00  5.96           C  
ANISOU 2233  C   GLY B  27     1005    602    521    140   -260   -119       C  
ATOM   2234  O   GLY B  27      10.951  23.009  18.043  1.00 11.15           O  
ANISOU 2234  O   GLY B  27     2727    622    635    415   -681   -202       O  
ATOM   2235  H   GLY B  27      11.495  26.593  20.022  1.00  5.89           H  
ATOM   2236  HA2 GLY B  27      10.217  25.466  17.948  1.00  6.45           H  
ATOM   2237  HA3 GLY B  27      11.772  25.526  18.107  1.00  6.45           H  
ATOM   2238  N   ALA B  28      10.980  23.531  20.232  1.00  4.68           N  
ANISOU 2238  N   ALA B  28      692    486    495    -46      7    -77       N  
ATOM   2239  CA  ALA B  28      11.050  22.150  20.695  1.00  5.00           C  
ANISOU 2239  CA  ALA B  28      709    496    580     -9    -61   -110       C  
ATOM   2240  C   ALA B  28       9.683  21.684  21.134  1.00  4.66           C  
ANISOU 2240  C   ALA B  28      676    466    523    -34   -106     -4       C  
ATOM   2241  O   ALA B  28       9.039  22.294  21.985  1.00  5.20           O  
ANISOU 2241  O   ALA B  28      777    596    486    -76    -21    -10       O  
ATOM   2242  CB  ALA B  28      12.036  22.042  21.874  1.00  5.77           C  
ANISOU 2242  CB  ALA B  28      757    564    741     -9   -212    -49       C  
ATOM   2243  H   ALA B  28      10.948  24.163  20.814  1.00  5.62           H  
ATOM   2244  HA  ALA B  28      11.362  21.580  19.961  1.00  6.00           H  
ATOM   2245  HB1 ALA B  28      12.078  21.131  22.175  1.00  8.66           H  
ATOM   2246  HB2 ALA B  28      12.908  22.325  21.589  1.00  8.66           H  
ATOM   2247  HB3 ALA B  28      11.737  22.603  22.594  1.00  8.66           H  
ATOM   2248  N   ASP B  29       9.240  20.544  20.582  1.00  5.35           N  
ANISOU 2248  N   ASP B  29      697    542    671    -53   -134    -69       N  
ATOM   2249  CA  ASP B  29       7.946  20.005  20.994  1.00  5.97           C  
ANISOU 2249  CA  ASP B  29      859    625    648   -173   -143     43       C  
ATOM   2250  C   ASP B  29       7.993  19.563  22.460  1.00  6.65           C  
ANISOU 2250  C   ASP B  29     1136    601    639   -278   -169     66       C  
ATOM   2251  O   ASP B  29       6.981  19.679  23.164  1.00  8.36           O  
ANISOU 2251  O   ASP B  29     1367    958    661   -321   -151    148       O  
ATOM   2252  CB  ASP B  29       7.583  18.797  20.140  1.00  7.25           C  
ANISOU 2252  CB  ASP B  29     1158    753    679   -358   -207     16       C  
ATOM   2253  CG  ASP B  29       7.383  19.102  18.649  1.00  6.88           C  
ANISOU 2253  CG  ASP B  29      903    863    691   -175   -133    -15       C  
ATOM   2254  OD1 ASP B  29       7.123  20.246  18.265  1.00  7.10           O  
ANISOU 2254  OD1 ASP B  29      948    920    670   -164   -150     51       O  
ATOM   2255  OD2 ASP B  29       7.497  18.099  17.883  1.00 10.06           O  
ANISOU 2255  OD2 ASP B  29     1758   1108    728     64    -49   -119       O  
ATOM   2256  H   ASP B  29       9.713  20.135  19.992  1.00  6.41           H  
ATOM   2257  HA  ASP B  29       7.258  20.695  20.886  1.00  7.16           H  
ATOM   2258  HB2 ASP B  29       8.285  18.133  20.229  1.00  8.70           H  
ATOM   2259  HB3 ASP B  29       6.766  18.406  20.488  1.00  8.70           H  
ATOM   2260  N  AASP B  30       9.053  19.000  22.956  0.49  7.55           N  
ANISOU 2260  N  AASP B  30     1233    752    713   -328   -352    144       N  
ATOM   2261  N  BASP B  30       9.149  18.976  22.786  0.52  7.64           N  
ANISOU 2261  N  BASP B  30     1442    597    691   -142   -484    117       N  
ATOM   2262  CA AASP B  30       9.031  18.418  24.329  0.49  6.20           C  
ANISOU 2262  CA AASP B  30     1045    526    643   -153    -94     73       C  
ATOM   2263  CA BASP B  30       9.499  18.194  23.973  0.52  6.02           C  
ANISOU 2263  CA BASP B  30      999    568    584   -124   -132     56       C  
ATOM   2264  C  AASP B  30      10.339  18.901  24.940  0.49  5.42           C  
ANISOU 2264  C  AASP B  30      996    478    462      3    -10     -4       C  
ATOM   2265  C  BASP B  30      10.549  18.888  24.862  0.52  5.34           C  
ANISOU 2265  C  BASP B  30      757    501    651    -26   -122     83       C  
ATOM   2266  O  AASP B  30      11.093  19.741  24.442  0.49  7.76           O  
ANISOU 2266  O  AASP B  30     1365    783    627   -479     -8     24       O  
ATOM   2267  O  BASP B  30      11.133  19.851  24.421  0.52  5.36           O  
ANISOU 2267  O  BASP B  30     1009    415    492    -18    -89    113       O  
ATOM   2268  CB AASP B  30       8.914  16.888  24.139  0.49  6.91           C  
ANISOU 2268  CB AASP B  30     1121    633    714   -239    -11    110       C  
ATOM   2269  CB BASP B  30       9.944  16.756  23.644  0.52  5.78           C  
ANISOU 2269  CB BASP B  30      961    574    530    -40     63     70       C  
ATOM   2270  CG AASP B  30       7.431  16.421  24.254  0.49 11.80           C  
ANISOU 2270  CG AASP B  30     1508   1192   1515   -611    463   -449       C  
ATOM   2271  CG BASP B  30       8.980  16.022  22.777  0.52  9.00           C  
ANISOU 2271  CG BASP B  30     1488    711   1016    -56   -261    -86       C  
ATOM   2272  OD1AASP B  30       6.810  16.481  25.355  0.49 10.10           O  
ANISOU 2272  OD1AASP B  30      968   1497   1145   -193     48   -199       O  
ATOM   2273  OD1BASP B  30       9.407  15.222  21.989  0.52 17.15           O  
ANISOU 2273  OD1BASP B  30     2216   2263   1649    456   -819  -1229       O  
ATOM   2274  OD2AASP B  30       6.964  15.938  23.268  0.49 17.32           O  
ANISOU 2274  OD2AASP B  30     1744   2947   1499  -1307    111   -545       O  
ATOM   2275  OD2BASP B  30       7.770  16.175  23.004  0.52 10.30           O  
ANISOU 2275  OD2BASP B  30     1284    979   1418   -444   -321     95       O  
ATOM   2276  H  AASP B  30       9.774  18.963  22.489  0.49  9.06           H  
ATOM   2277  H  BASP B  30       9.782  19.072  22.212  0.52  9.17           H  
ATOM   2278  HA AASP B  30       8.267  18.762  24.836  0.49  7.44           H  
ATOM   2279  HA BASP B  30       8.683  18.120  24.510  0.52  7.22           H  
ATOM   2280  HB2AASP B  30       9.262  16.643  23.268  0.49  8.29           H  
ATOM   2281  HB2BASP B  30      10.805  16.787  23.200  0.52  6.93           H  
ATOM   2282  HB3AASP B  30       9.447  16.437  24.813  0.49  8.29           H  
ATOM   2283  HB3BASP B  30      10.056  16.265  24.473  0.52  6.93           H  
ATOM   2284  N   THR B  31      10.666  18.344  26.088  1.00  5.56           N  
ANISOU 2284  N   THR B  31      790    599    599    -90    -26     72       N  
ATOM   2285  CA  THR B  31      11.707  18.793  27.010  1.00  4.93           C  
ANISOU 2285  CA  THR B  31      684    523    553    -99     10     74       C  
ATOM   2286  C   THR B  31      12.757  17.707  27.116  1.00  4.98           C  
ANISOU 2286  C   THR B  31      714    507    559    -54     19     39       C  
ATOM   2287  O   THR B  31      12.399  16.557  27.397  1.00  5.84           O  
ANISOU 2287  O   THR B  31      796    480    812    -52     88    101       O  
ATOM   2288  CB  THR B  31      11.072  19.102  28.369  1.00  5.11           C  
ANISOU 2288  CB  THR B  31      683    580    563    -13     23    105       C  
ATOM   2289  OG1 THR B  31      10.236  20.255  28.228  1.00  5.30           O  
ANISOU 2289  OG1 THR B  31      715    613    565     36     49     98       O  
ATOM   2290  CG2 THR B  31      12.110  19.350  29.458  1.00  5.46           C  
ANISOU 2290  CG2 THR B  31      748    657    548     -9     39     61       C  
ATOM   2291  H  ATHR B  31      10.221  17.645  26.319  1.00  6.67           H  
ATOM   2292  HA  THR B  31      12.121  19.608  26.656  1.00  5.91           H  
ATOM   2293  HB  THR B  31      10.514  18.341  28.635  1.00  6.13           H  
ATOM   2294  HG1 THR B  31      10.270  20.524  27.454  1.00  7.95           H  
ATOM   2295 HG21 THR B  31      12.669  18.575  29.551  1.00  8.19           H  
ATOM   2296 HG22 THR B  31      12.650  20.107  29.219  1.00  8.19           H  
ATOM   2297 HG23 THR B  31      11.665  19.525  30.291  1.00  8.19           H  
ATOM   2298  N  AVAL B  32      14.003  18.039  26.841  0.10  5.86           N  
ANISOU 2298  N  AVAL B  32      749    357    989   -114    -23    -14       N  
ATOM   2299  N  BVAL B  32      14.019  18.052  26.867  0.90  5.08           N  
ANISOU 2299  N  BVAL B  32      685    477    651     -4     49    118       N  
ATOM   2300  CA AVAL B  32      15.146  17.145  26.899  0.10  5.06           C  
ANISOU 2300  CA AVAL B  32      622    305    882   -228    116    408       C  
ATOM   2301  CA BVAL B  32      15.088  17.052  26.925  0.90  5.60           C  
ANISOU 2301  CA BVAL B  32      679    538    783     11     53     16       C  
ATOM   2302  C  AVAL B  32      16.187  17.715  27.852  0.10  5.42           C  
ANISOU 2302  C  AVAL B  32      747    477    711    -99    111     68       C  
ATOM   2303  C  BVAL B  32      16.237  17.625  27.725  0.90  5.61           C  
ANISOU 2303  C  BVAL B  32      676    472    855     11     69     47       C  
ATOM   2304  O  AVAL B  32      16.481  18.907  27.828  0.10  5.46           O  
ANISOU 2304  O  AVAL B  32      620    392    940      2    328    -79       O  
ATOM   2305  O  BVAL B  32      16.705  18.753  27.504  0.90  6.33           O  
ANISOU 2305  O  BVAL B  32      740    478   1042    -45     96    100       O  
ATOM   2306  CB AVAL B  32      15.800  16.915  25.519  0.10  6.50           C  
ANISOU 2306  CB AVAL B  32     1073    347    904   -160     10   -180       C  
ATOM   2307  CB BVAL B  32      15.497  16.550  25.532  0.90  5.88           C  
ANISOU 2307  CB BVAL B  32      755    528    819    -56    126     49       C  
ATOM   2308  CG1AVAL B  32      16.659  15.671  25.498  0.10  9.39           C  
ANISOU 2308  CG1AVAL B  32     1945    725    683    332    668    631       C  
ATOM   2309  CG1BVAL B  32      16.035  17.681  24.624  0.90  6.60           C  
ANISOU 2309  CG1BVAL B  32      817    712    828    -30    179    114       C  
ATOM   2310  CG2AVAL B  32      14.667  16.852  24.514  0.10 10.58           C  
ANISOU 2310  CG2AVAL B  32     1751    753   1274   -242   -524   -255       C  
ATOM   2311  CG2BVAL B  32      16.514  15.414  25.680  0.90  6.77           C  
ANISOU 2311  CG2BVAL B  32      917    588    915     12    265     25       C  
ATOM   2312  H  AVAL B  32      14.152  18.853  26.608  0.10  7.03           H  
ATOM   2313  H  BVAL B  32      14.208  18.868  26.671  0.90  6.09           H  
ATOM   2314  HA AVAL B  32      14.846  16.280  27.248  0.10  6.07           H  
ATOM   2315  HA BVAL B  32      14.741  16.282  27.422  0.90  6.72           H  
ATOM   2316  HB AVAL B  32      16.363  17.688  25.307  0.10  7.80           H  
ATOM   2317  HB BVAL B  32      14.698  16.179  25.103  0.90  7.06           H  
ATOM   2318 HG11AVAL B  32      17.360  15.755  26.148  0.10 14.08           H  
ATOM   2319 HG11BVAL B  32      16.276  17.317  23.769  0.90  9.89           H  
ATOM   2320 HG12AVAL B  32      16.119  14.905  25.708  0.10 14.08           H  
ATOM   2321 HG12BVAL B  32      15.355  18.349  24.508  0.90  9.89           H  
ATOM   2322 HG13AVAL B  32      17.043  15.562  24.625  0.10 14.08           H  
ATOM   2323 HG13BVAL B  32      16.807  18.079  25.032  0.90  9.89           H  
ATOM   2324 HG21AVAL B  32      14.151  17.660  24.563  0.10 15.86           H  
ATOM   2325 HG21BVAL B  32      16.771  15.099  24.811  0.90 10.16           H  
ATOM   2326 HG22AVAL B  32      15.029  16.757  23.630  0.10 15.86           H  
ATOM   2327 HG22BVAL B  32      17.289  15.737  26.145  0.90 10.16           H  
ATOM   2328 HG23AVAL B  32      14.104  16.100  24.712  0.10 15.86           H  
ATOM   2329 HG23BVAL B  32      16.119  14.694  26.178  0.90 10.16           H  
ATOM   2330  N   ILE B  33      16.719  16.820  28.674  1.00  6.11           N  
ANISOU 2330  N   ILE B  33      730    504    950    -73    -32     36       N  
ATOM   2331  CA  ILE B  33      17.770  17.170  29.599  1.00  7.12           C  
ANISOU 2331  CA  ILE B  33      778    557   1209     11   -216    -95       C  
ATOM   2332  C   ILE B  33      18.932  16.204  29.440  1.00  6.50           C  
ANISOU 2332  C   ILE B  33      746    577   1001    -30    -87    -16       C  
ATOM   2333  O   ILE B  33      18.762  15.039  29.071  1.00  7.68           O  
ANISOU 2333  O   ILE B  33      756    600   1387     38   -132    -90       O  
ATOM   2334  CB  ILE B  33      17.231  17.202  31.034  1.00  9.65           C  
ANISOU 2334  CB  ILE B  33     1096   1277   1076    408   -302   -503       C  
ATOM   2335  CG1AILE B  33      16.830  15.997  31.462  0.51 10.45           C  
ANISOU 2335  CG1AILE B  33     1441   1372    920    554     80     15       C  
ATOM   2336  CG1BILE B  33      15.850  17.870  31.353  0.49  6.93           C  
ANISOU 2336  CG1BILE B  33      823    889    763    -37    -77     -9       C  
ATOM   2337  CG2AILE B  33      16.284  18.460  30.942  0.51  9.78           C  
ANISOU 2337  CG2AILE B  33     1269    953   1271    202    -83   -434       C  
ATOM   2338  CG2BILE B  33      18.166  17.369  32.289  0.49  6.85           C  
ANISOU 2338  CG2BILE B  33      801    901    746    108    -68    101       C  
ATOM   2339  CD1AILE B  33      16.559  16.253  32.930  0.51 11.74           C  
ANISOU 2339  CD1AILE B  33     1401   1742   1052    159    -67   -108       C  
ATOM   2340  CD1BILE B  33      16.042  19.378  31.198  0.49  7.35           C  
ANISOU 2340  CD1BILE B  33      939    841    846     71      0   -136       C  
ATOM   2341  H  AILE B  33      16.430  16.010  28.655  1.00  7.34           H  
ATOM   2342  HA  ILE B  33      18.088  18.069  29.373  1.00  8.55           H  
ATOM   2343  HB AILE B  33      17.983  17.462  31.606  1.00 11.58           H  
ATOM   2344 HG12AILE B  33      16.027  15.708  31.001  0.51 12.53           H  
ATOM   2345 HG12BILE B  33      15.171  17.551  30.738  0.49  8.31           H  
ATOM   2346 HG13AILE B  33      17.524  15.330  31.343  0.51 12.53           H  
ATOM   2347 HG13BILE B  33      15.573  17.656  32.257  0.49  8.31           H  
ATOM   2348 HG21AILE B  33      16.782  19.212  30.610  0.51 14.67           H  
ATOM   2349 HG21BILE B  33      17.633  17.363  33.088  0.49 10.28           H  
ATOM   2350 HG22AILE B  33      15.556  18.270  30.345  0.51 14.67           H  
ATOM   2351 HG22BILE B  33      18.795  16.644  32.319  0.49 10.28           H  
ATOM   2352 HG23AILE B  33      15.938  18.665  31.813  0.51 14.67           H  
ATOM   2353 HG23BILE B  33      18.640  18.201  32.227  0.49 10.28           H  
ATOM   2354 HD11AILE B  33      16.259  15.442  33.346  0.51 17.61           H  
ATOM   2355 HD11BILE B  33      15.214  19.827  31.386  0.49 11.02           H  
ATOM   2356 HD12AILE B  33      17.365  16.553  33.356  0.51 17.61           H  
ATOM   2357 HD12BILE B  33      16.716  19.680  31.812  0.49 11.02           H  
ATOM   2358 HD13AILE B  33      15.881  16.927  33.017  0.51 17.61           H  
ATOM   2359 HD13BILE B  33      16.316  19.576  30.300  0.49 11.02           H  
ATOM   2360  N  AGLU B  34      20.118  16.689  29.802  0.24  5.75           N  
ANISOU 2360  N  AGLU B  34      773    699    584    -57   -170    130       N  
ATOM   2361  N  BGLU B  34      20.125  16.727  29.708  0.76  6.99           N  
ANISOU 2361  N  BGLU B  34      737    680   1082     -8     70   -122       N  
ATOM   2362  CA AGLU B  34      21.344  15.923  29.856  0.24 10.70           C  
ANISOU 2362  CA AGLU B  34      769   1524   1529    180    -45    699       C  
ATOM   2363  CA BGLU B  34      21.329  15.935  29.715  0.76  6.83           C  
ANISOU 2363  CA BGLU B  34      683    920    837     26     -7   -157       C  
ATOM   2364  C  AGLU B  34      21.194  14.730  30.796  0.24  7.68           C  
ANISOU 2364  C  AGLU B  34      864   1005    874    185   -168    162       C  
ATOM   2365  C  BGLU B  34      21.252  14.823  30.754  0.76  7.80           C  
ANISOU 2365  C  BGLU B  34      751    877   1160    105    -81   -123       C  
ATOM   2366  O  AGLU B  34      20.357  14.610  31.681  0.24  8.49           O  
ANISOU 2366  O  AGLU B  34     1043    979   1012     14      0     37       O  
ATOM   2367  O  BGLU B  34      20.556  14.908  31.743  0.76  7.87           O  
ANISOU 2367  O  BGLU B  34     1001    828    983     89     -8     65       O  
ATOM   2368  CB AGLU B  34      22.493  16.844  30.310  0.24 10.24           C  
ANISOU 2368  CB AGLU B  34      546   1087   2027    420    142    588       C  
ATOM   2369  CB BGLU B  34      22.538  16.844  30.029  0.76  8.98           C  
ANISOU 2369  CB BGLU B  34      829   1418    961   -260    -47      2       C  
ATOM   2370  CG AGLU B  34      22.282  17.426  31.693  0.24 16.17           C  
ANISOU 2370  CG AGLU B  34     1443   3056   1278   -817   -252    795       C  
ATOM   2371  CG BGLU B  34      22.703  17.984  29.043  0.76  8.86           C  
ANISOU 2371  CG BGLU B  34      666   1492   1007   -177    105     47       C  
ATOM   2372  CD AGLU B  34      23.035  18.681  32.089  0.24 14.31           C  
ANISOU 2372  CD AGLU B  34     1080   2580   1455   -157    105    258       C  
ATOM   2373  CD BGLU B  34      23.579  19.148  29.481  0.76 13.82           C  
ANISOU 2373  CD BGLU B  34     1648   1965   1324   -955    184    113       C  
ATOM   2374  OE1AGLU B  34      24.122  18.886  31.461  0.24 25.53           O  
ANISOU 2374  OE1AGLU B  34     2107   3636   3380  -1667   1539  -2452       O  
ATOM   2375  OE1BGLU B  34      24.013  19.187  30.594  0.76 12.45           O  
ANISOU 2375  OE1BGLU B  34     1360   1487   1601   -359     19   -323       O  
ATOM   2376  OE2AGLU B  34      22.561  19.438  33.002  0.24 13.20           O  
ANISOU 2376  OE2AGLU B  34      955   2383   1379   1082      5    955       O  
ATOM   2377  OE2BGLU B  34      23.589  20.212  28.817  0.76 20.25           O  
ANISOU 2377  OE2BGLU B  34     3457   1728   2052   -593    556    231       O  
ATOM   2378  H  AGLU B  34      20.158  17.520  30.020  0.24  6.90           H  
ATOM   2379  H  BGLU B  34      20.180  17.567  29.884  0.76  8.39           H  
ATOM   2380  HA AGLU B  34      21.546  15.590  28.956  0.24 12.84           H  
ATOM   2381  HA BGLU B  34      21.453  15.535  28.829  0.76  8.19           H  
ATOM   2382  HB2AGLU B  34      23.321  16.340  30.304  0.24 12.29           H  
ATOM   2383  HB2BGLU B  34      22.432  17.212  30.920  0.76 10.77           H  
ATOM   2384  HB3AGLU B  34      22.584  17.570  29.673  0.24 12.29           H  
ATOM   2385  HB3BGLU B  34      23.345  16.306  30.025  0.76 10.77           H  
ATOM   2386  HG2AGLU B  34      21.335  17.611  31.791  0.24 19.40           H  
ATOM   2387  HG2BGLU B  34      23.071  17.621  28.222  0.76 10.63           H  
ATOM   2388  HG3AGLU B  34      22.505  16.737  32.337  0.24 19.40           H  
ATOM   2389  HG3BGLU B  34      21.822  18.332  28.834  0.76 10.63           H  
ATOM   2390  N  AGLU B  35      22.085  13.751  30.604  0.46  8.76           N  
ANISOU 2390  N  AGLU B  35      981   1089   1061    253   -233    -59       N  
ATOM   2391  N  BGLU B  35      22.067  13.765  30.517  0.54 10.85           N  
ANISOU 2391  N  BGLU B  35      956    884   2037    181    383    224       N  
ATOM   2392  CA AGLU B  35      22.060  12.560  31.440  0.46 12.99           C  
ANISOU 2392  CA AGLU B  35     1747   1216   1678    772    360    300       C  
ATOM   2393  CA BGLU B  35      22.101  12.633  31.490  0.54  8.57           C  
ANISOU 2393  CA BGLU B  35      734    798   1529    -79   -214     61       C  
ATOM   2394  C  AGLU B  35      21.968  12.921  32.904  0.46  8.84           C  
ANISOU 2394  C  AGLU B  35      857    930   1370    113   -457    447       C  
ATOM   2395  C  BGLU B  35      22.032  12.945  32.971  0.54 12.41           C  
ANISOU 2395  C  BGLU B  35     1555   1267   1611   -342     43    -41       C  
ATOM   2396  O  AGLU B  35      22.875  13.616  33.307  0.46 16.18           O  
ANISOU 2396  O  AGLU B  35     1054   1283   3446   -198  -1139    607       O  
ATOM   2397  O  BGLU B  35      22.781  13.758  33.496  0.54  9.29           O  
ANISOU 2397  O  BGLU B  35     1202   1248    869    -68      7    156       O  
ATOM   2398  CB AGLU B  35      23.320  11.705  31.239  0.46  8.99           C  
ANISOU 2398  CB AGLU B  35      692    921   1598    -99   -221    279       C  
ATOM   2399  CB BGLU B  35      23.372  11.801  31.145  0.54 17.42           C  
ANISOU 2399  CB BGLU B  35     2106   1446   2673   1033   -151   -420       C  
ATOM   2400  CG AGLU B  35      23.317  10.430  32.092  0.46  9.34           C  
ANISOU 2400  CG AGLU B  35     1147    730   1460    138   -168    201       C  
ATOM   2401  CG BGLU B  35      23.192  11.228  29.748  0.54 21.92           C  
ANISOU 2401  CG BGLU B  35     1561   3227   3046   -340    605  -1413       C  
ATOM   2402  CD AGLU B  35      22.094   9.535  31.763  0.46 10.96           C  
ANISOU 2402  CD AGLU B  35     1569    740   1606   -151    175    -30       C  
ATOM   2403  CD BGLU B  35      22.246  10.034  29.656  0.54 24.19           C  
ANISOU 2403  CD BGLU B  35      907   3321   4417    -78   -356   -975       C  
ATOM   2404  OE1AGLU B  35      21.648   9.446  30.592  0.46 11.56           O  
ANISOU 2404  OE1AGLU B  35     1207   1150   1774   -271     77    -42       O  
ATOM   2405  OE1BGLU B  35      21.839   9.407  30.647  0.54 25.81           O  
ANISOU 2405  OE1BGLU B  35     2005   2157   5060   -324   -812   -544       O  
ATOM   2406  OE2AGLU B  35      21.562   8.944  32.713  0.46 14.98           O  
ANISOU 2406  OE2AGLU B  35     2062   1510   1780   -730    387   -164       O  
ATOM   2407  OE2BGLU B  35      21.879   9.731  28.481  0.54 24.37           O  
ANISOU 2407  OE2BGLU B  35     1602   2216   4890    578  -1208  -1148       O  
ATOM   2408  H  AGLU B  35      22.676  13.825  29.983  0.46 10.52           H  
ATOM   2409  H  BGLU B  35      22.560  13.747  29.813  0.54 13.02           H  
ATOM   2410  HA AGLU B  35      21.276  12.025  31.199  0.46 15.59           H  
ATOM   2411  HA BGLU B  35      21.330  12.064  31.286  0.54 10.28           H  
ATOM   2412  HB2AGLU B  35      23.388  11.458  30.303  0.46 10.78           H  
ATOM   2413  HB2BGLU B  35      24.160  12.367  31.174  0.54 20.91           H  
ATOM   2414  HB3AGLU B  35      24.101  12.234  31.464  0.46 10.78           H  
ATOM   2415  HB3BGLU B  35      23.486  11.083  31.788  0.54 20.91           H  
ATOM   2416  HG2AGLU B  35      24.133   9.932  31.930  0.46 11.21           H  
ATOM   2417  HG2BGLU B  35      22.858  11.930  29.167  0.54 26.31           H  
ATOM   2418  HG3AGLU B  35      23.295  10.672  33.031  0.46 11.21           H  
ATOM   2419  HG3BGLU B  35      24.061  10.958  29.410  0.54 26.31           H  
ATOM   2420  N   MET B  36      21.047  12.283  33.595  1.00 10.98           N  
ANISOU 2420  N   MET B  36     1228   1306   1387   -178   -296    351       N  
ATOM   2421  CA  MET B  36      20.819  12.402  35.010  1.00 11.44           C  
ANISOU 2421  CA  MET B  36     1207   1513   1369    -60   -299    390       C  
ATOM   2422  C   MET B  36      19.948  11.216  35.415  1.00 11.99           C  
ANISOU 2422  C   MET B  36     1246   1485   1554    -93   -361    606       C  
ATOM   2423  O   MET B  36      19.400  10.525  34.550  1.00 14.85           O  
ANISOU 2423  O   MET B  36     1983   1539   1785   -530   -509    644       O  
ATOM   2424  CB  MET B  36      20.141  13.690  35.434  1.00 13.35           C  
ANISOU 2424  CB  MET B  36     1593   1435   1741     -4    -88    361       C  
ATOM   2425  CG  MET B  36      18.756  13.818  34.880  1.00 17.33           C  
ANISOU 2425  CG  MET B  36     1480   1504   3208     -4   -269    718       C  
ATOM   2426  SD  MET B  36      17.866  15.240  35.571  1.00 20.58           S  
ANISOU 2426  SD  MET B  36     2010   1555   3790    299    681    950       S  
ATOM   2427  CE  MET B  36      17.882  14.864  37.326  1.00 23.55           C  
ANISOU 2427  CE  MET B  36     2872   1676   3865    607   1183   1174       C  
ATOM   2428  H  AMET B  36      20.535  11.746  33.161  1.00 13.17           H  
ATOM   2429  HA  MET B  36      21.680  12.333  35.474  1.00 13.73           H  
ATOM   2430  HB2 MET B  36      20.100  13.722  36.403  1.00 16.02           H  
ATOM   2431  HB3 MET B  36      20.674  14.443  35.134  1.00 16.02           H  
ATOM   2432  HG2 MET B  36      18.806  13.912  33.916  1.00 20.79           H  
ATOM   2433  HG3 MET B  36      18.259  13.007  35.074  1.00 20.79           H  
ATOM   2434  HE1 MET B  36      17.429  15.561  37.807  1.00 35.32           H  
ATOM   2435  HE2 MET B  36      17.434  14.028  37.478  1.00 35.32           H  
ATOM   2436  HE3 MET B  36      18.789  14.801  37.632  1.00 35.32           H  
ATOM   2437  N   SER B  37      19.827  11.038  36.711  1.00 14.05           N  
ANISOU 2437  N   SER B  37     1439   2078   1504   -125   -340    745       N  
ATOM   2438  CA  SER B  37      18.970   9.942  37.215  1.00 14.98           C  
ANISOU 2438  CA  SER B  37     1608   1725   2020     24   -195    938       C  
ATOM   2439  C   SER B  37      17.600  10.496  37.584  1.00 12.98           C  
ANISOU 2439  C   SER B  37     1596   1460   1581    -93   -179    465       C  
ATOM   2440  O   SER B  37      17.461  11.557  38.225  1.00 15.41           O  
ANISOU 2440  O   SER B  37     1943   1292   2273   -329   -354    360       O  
ATOM   2441  CB  SER B  37      19.623   9.384  38.480  1.00 24.10           C  
ANISOU 2441  CB  SER B  37     2324   3258   3031    493   -254   2160       C  
ATOM   2442  OG ASER B  37      18.742   8.750  39.351  0.62 28.03           O  
ANISOU 2442  OG ASER B  37     3063   3603   3350    776    504   2344       O  
ATOM   2443  OG BSER B  37      20.864   8.725  38.001  0.38 26.59           O  
ANISOU 2443  OG BSER B  37     1486   3625   4391    133   -226   2761       O  
ATOM   2444  H   SER B  37      20.241  11.553  37.260  1.00 16.86           H  
ATOM   2445  HA  SER B  37      18.882   9.239  36.538  1.00 17.98           H  
ATOM   2446  HB2ASER B  37      20.311   8.751  38.220  1.00 28.92           H  
ATOM   2447  HB3ASER B  37      20.057  10.111  38.952  1.00 28.92           H  
ATOM   2448  HG ASER B  37      18.110   9.249  39.511  0.62 42.05           H  
ATOM   2449  HG BSER B  37      20.669   8.103  37.503  0.38 39.89           H  
ATOM   2450  N   LEU B  38      16.539   9.838  37.073  1.00 12.02           N  
ANISOU 2450  N   LEU B  38     1699   1314   1283    147   -129     69       N  
ATOM   2451  CA  LEU B  38      15.174  10.135  37.397  1.00 10.47           C  
ANISOU 2451  CA  LEU B  38     1498   1042   1203    -21      9   -153       C  
ATOM   2452  C   LEU B  38      14.507   8.861  37.894  1.00 11.26           C  
ANISOU 2452  C   LEU B  38     2005    947   1071   -114    -69    -78       C  
ATOM   2453  O   LEU B  38      14.941   7.771  37.455  1.00 11.98           O  
ANISOU 2453  O   LEU B  38     1922   1042   1317     55     -5      7       O  
ATOM   2454  CB  LEU B  38      14.409  10.735  36.217  1.00  9.61           C  
ANISOU 2454  CB  LEU B  38     1408    977   1048   -141    -28    -86       C  
ATOM   2455  CG  LEU B  38      14.820  12.118  35.806  1.00  9.63           C  
ANISOU 2455  CG  LEU B  38     1169    930   1341    -16    -26   -118       C  
ATOM   2456  CD1 LEU B  38      14.031  12.567  34.566  1.00 10.32           C  
ANISOU 2456  CD1 LEU B  38     1438    988   1261    -72      0     -9       C  
ATOM   2457  CD2 LEU B  38      14.541  13.114  36.958  1.00 12.24           C  
ANISOU 2457  CD2 LEU B  38     2005    885   1485     23   -457   -153       C  
ATOM   2458  H   LEU B  38      16.691   9.199  36.517  1.00 14.43           H  
ATOM   2459  HA  LEU B  38      15.169  10.787  38.128  1.00 12.57           H  
ATOM   2460  HB2 LEU B  38      14.516  10.146  35.453  1.00 11.53           H  
ATOM   2461  HB3 LEU B  38      13.466  10.750  36.441  1.00 11.53           H  
ATOM   2462  HG  LEU B  38      15.778  12.123  35.599  1.00 11.55           H  
ATOM   2463 HD11 LEU B  38      14.305  13.453  34.317  1.00 15.48           H  
ATOM   2464 HD12 LEU B  38      14.204  11.962  33.841  1.00 15.48           H  
ATOM   2465 HD13 LEU B  38      13.092  12.566  34.767  1.00 15.48           H  
ATOM   2466 HD21 LEU B  38      14.806  13.997  36.689  1.00 18.37           H  
ATOM   2467 HD22 LEU B  38      13.604  13.110  37.165  1.00 18.37           H  
ATOM   2468 HD23 LEU B  38      15.042  12.853  37.734  1.00 18.37           H  
ATOM   2469  N   PRO B  39      13.505   8.994  38.715  1.00 12.54           N  
ANISOU 2469  N   PRO B  39     2334   1059   1089   -358    388   -250       N  
ATOM   2470  CA  PRO B  39      12.806   7.829  39.251  1.00 14.11           C  
ANISOU 2470  CA  PRO B  39     2910   1130   1003   -513    346   -236       C  
ATOM   2471  C   PRO B  39      11.853   7.216  38.286  1.00 11.69           C  
ANISOU 2471  C   PRO B  39     2110   1036   1031   -345    557   -249       C  
ATOM   2472  O   PRO B  39      11.326   7.926  37.414  1.00 13.13           O  
ANISOU 2472  O   PRO B  39     2398   1046   1247   -240    479   -129       O  
ATOM   2473  CB  PRO B  39      12.055   8.426  40.455  1.00 15.68           C  
ANISOU 2473  CB  PRO B  39     2928   1458   1218   -694    652   -422       C  
ATOM   2474  CG  PRO B  39      11.727   9.841  40.067  1.00 17.33           C  
ANISOU 2474  CG  PRO B  39     2631   1398   2163   -474   1039   -574       C  
ATOM   2475  CD  PRO B  39      12.944  10.275  39.269  1.00 14.71           C  
ANISOU 2475  CD  PRO B  39     2513   1192   1551   -458    571   -476       C  
ATOM   2476  HA  PRO B  39      13.453   7.159  39.557  1.00 16.93           H  
ATOM   2477  HB2 PRO B  39      11.244   7.925  40.635  1.00 18.82           H  
ATOM   2478  HB3 PRO B  39      12.613   8.410  41.248  1.00 18.82           H  
ATOM   2479  HG2 PRO B  39      10.924   9.877  39.525  1.00 20.79           H  
ATOM   2480  HG3 PRO B  39      11.606  10.399  40.851  1.00 20.79           H  
ATOM   2481  HD2 PRO B  39      12.691  10.880  38.554  1.00 17.65           H  
ATOM   2482  HD3 PRO B  39      13.592  10.717  39.841  1.00 17.65           H  
ATOM   2483  N   GLY B  40      11.607   5.932  38.502  1.00 11.84           N  
ANISOU 2483  N   GLY B  40     2194    922   1114   -213    327   -240       N  
ATOM   2484  CA  GLY B  40      10.518   5.281  37.812  1.00 11.38           C  
ANISOU 2484  CA  GLY B  40     1946    885   1234   -139    439   -344       C  
ATOM   2485  C   GLY B  40      10.925   4.586  36.529  1.00  9.72           C  
ANISOU 2485  C   GLY B  40     1647    789   1039   -154    393   -155       C  
ATOM   2486  O   GLY B  40      12.098   4.409  36.208  1.00 13.24           O  
ANISOU 2486  O   GLY B  40     1658   1769   1304   -200    334   -626       O  
ATOM   2487  H   GLY B  40      12.095   5.487  39.053  1.00 14.21           H  
ATOM   2488  HA2 GLY B  40      10.118   4.628  38.407  1.00 13.65           H  
ATOM   2489  HA3 GLY B  40       9.840   5.944  37.606  1.00 13.65           H  
ATOM   2490  N   ARG B  41       9.946   4.110  35.815  1.00  9.00           N  
ANISOU 2490  N   ARG B  41     1509    721    987    119    420    -55       N  
ATOM   2491  CA  ARG B  41      10.132   3.466  34.536  1.00  8.58           C  
ANISOU 2491  CA  ARG B  41     1451    744    869    118    265    -31       C  
ATOM   2492  C   ARG B  41      10.236   4.500  33.438  1.00  8.57           C  
ANISOU 2492  C   ARG B  41     1431    647    985    227    329     26       C  
ATOM   2493  O   ARG B  41       9.679   5.596  33.532  1.00 12.28           O  
ANISOU 2493  O   ARG B  41     2191    938   1260    629    602    167       O  
ATOM   2494  CB  ARG B  41       9.032   2.503  34.242  1.00 11.96           C  
ANISOU 2494  CB  ARG B  41     2043   1280    949   -362    288   -151       C  
ATOM   2495  CG  ARG B  41       9.206   1.269  35.184  1.00 16.55           C  
ANISOU 2495  CG  ARG B  41     3539   1488    886   -808    562     91       C  
ATOM   2496  CD  ARG B  41       8.401   0.168  34.904  1.00 13.23           C  
ANISOU 2496  CD  ARG B  41     2507    980   1239    525    225   -145       C  
ATOM   2497  NE  ARG B  41       8.563  -0.373  33.579  1.00 13.95           N  
ANISOU 2497  NE  ARG B  41     2640   1195   1151   1012   -125   -182       N  
ATOM   2498  CZ  ARG B  41       9.344  -1.394  33.245  1.00  8.46           C  
ANISOU 2498  CZ  ARG B  41     1377    727    917    189     71    -91       C  
ATOM   2499  NH1 ARG B  41      10.133  -1.982  34.127  1.00  7.35           N  
ANISOU 2499  NH1 ARG B  41     1170    625    832     58     89    -80       N  
ATOM   2500  NH2 ARG B  41       9.313  -1.859  32.021  1.00  9.15           N  
ANISOU 2500  NH2 ARG B  41     1506    861    903    382   -115   -133       N  
ATOM   2501  H   ARG B  41       9.146   4.183  36.122  1.00 10.80           H  
ATOM   2502  HA  ARG B  41      10.974   2.966  34.565  1.00 10.29           H  
ATOM   2503  HB2 ARG B  41       8.171   2.923  34.398  1.00 14.35           H  
ATOM   2504  HB3 ARG B  41       9.073   2.223  33.315  1.00 14.35           H  
ATOM   2505  HG2 ARG B  41      10.133   0.985  35.145  1.00 19.86           H  
ATOM   2506  HG3 ARG B  41       9.027   1.553  36.094  1.00 19.86           H  
ATOM   2507  HD2 ARG B  41       8.596  -0.530  35.549  1.00 15.87           H  
ATOM   2508  HD3 ARG B  41       7.473   0.425  35.022  1.00 15.87           H  
ATOM   2509  HE  ARG B  41       8.115   0.000  32.947  1.00 16.74           H  
ATOM   2510 HH11 ARG B  41      10.613  -2.656  33.891  1.00  8.82           H  
ATOM   2511 HH12 ARG B  41      10.168  -1.691  34.935  1.00  8.82           H  
ATOM   2512 HH21 ARG B  41       9.800  -2.534  31.806  1.00 10.98           H  
ATOM   2513 HH22 ARG B  41       8.806  -1.490  31.433  1.00 10.98           H  
ATOM   2514  N   TRP B  42      10.935   4.139  32.379  1.00  7.13           N  
ANISOU 2514  N   TRP B  42     1168    497    882     64    203    -14       N  
ATOM   2515  CA  TRP B  42      11.039   4.970  31.202  1.00  7.04           C  
ANISOU 2515  CA  TRP B  42     1146    471    898     40    166     29       C  
ATOM   2516  C   TRP B  42      10.603   4.194  29.958  1.00  6.76           C  
ANISOU 2516  C   TRP B  42     1000    497    917    -78    208      1       C  
ATOM   2517  O   TRP B  42      10.580   2.959  29.937  1.00  7.52           O  
ANISOU 2517  O   TRP B  42     1185    498   1003    -11    178    -40       O  
ATOM   2518  CB  TRP B  42      12.398   5.592  31.042  1.00  7.41           C  
ANISOU 2518  CB  TRP B  42     1162    498    989    -76     36    -46       C  
ATOM   2519  CG  TRP B  42      13.532   4.599  30.893  1.00  7.38           C  
ANISOU 2519  CG  TRP B  42     1032    462   1143   -118     90     -4       C  
ATOM   2520  CD1 TRP B  42      14.232   3.994  31.872  1.00  8.09           C  
ANISOU 2520  CD1 TRP B  42     1161    560   1171    -86     74     51       C  
ATOM   2521  CD2 TRP B  42      14.071   4.133  29.640  1.00  7.45           C  
ANISOU 2521  CD2 TRP B  42     1024    427   1211   -154     98    -27       C  
ATOM   2522  NE1 TRP B  42      15.206   3.161  31.344  1.00  8.43           N  
ANISOU 2522  NE1 TRP B  42     1049    564   1401    -60    -39     78       N  
ATOM   2523  CE2 TRP B  42      15.133   3.244  29.978  1.00  8.06           C  
ANISOU 2523  CE2 TRP B  42     1050    453   1378   -103    112    -70       C  
ATOM   2524  CE3 TRP B  42      13.813   4.412  28.305  1.00  7.87           C  
ANISOU 2524  CE3 TRP B  42     1093    503   1214   -141    119    -75       C  
ATOM   2525  CZ2 TRP B  42      15.912   2.640  28.969  1.00  9.11           C  
ANISOU 2525  CZ2 TRP B  42     1153    540   1564    -72    188    -61       C  
ATOM   2526  CZ3 TRP B  42      14.583   3.825  27.326  1.00  8.91           C  
ANISOU 2526  CZ3 TRP B  42     1242    606   1337   -171    196   -151       C  
ATOM   2527  CH2 TRP B  42      15.611   2.958  27.670  1.00  9.29           C  
ANISOU 2527  CH2 TRP B  42     1268    677   1374   -103    202   -265       C  
ATOM   2528  H   TRP B  42      11.344   3.383  32.390  1.00  8.55           H  
ATOM   2529  HA  TRP B  42      10.401   5.705  31.316  1.00  8.44           H  
ATOM   2530  HB2 TRP B  42      12.385   6.167  30.261  1.00  8.90           H  
ATOM   2531  HB3 TRP B  42      12.576   6.151  31.815  1.00  8.90           H  
ATOM   2532  HD1 TRP B  42      14.082   4.119  32.781  1.00  9.71           H  
ATOM   2533  HE1 TRP B  42      15.757   2.678  31.793  1.00 10.12           H  
ATOM   2534  HE3 TRP B  42      13.124   4.992  28.073  1.00  9.44           H  
ATOM   2535  HZ2 TRP B  42      16.602   2.051  29.176  1.00 10.94           H  
ATOM   2536  HZ3 TRP B  42      14.413   4.010  26.431  1.00 10.70           H  
ATOM   2537  HH2 TRP B  42      16.118   2.577  26.990  1.00 11.14           H  
ATOM   2538  N   LYS B  43      10.245   4.958  28.928  1.00  7.34           N  
ANISOU 2538  N   LYS B  43     1133    520    971   -145    128     33       N  
ATOM   2539  CA  LYS B  43       9.821   4.461  27.641  1.00  7.75           C  
ANISOU 2539  CA  LYS B  43     1080    783    906   -241     35     30       C  
ATOM   2540  C   LYS B  43      10.751   5.017  26.563  1.00  6.94           C  
ANISOU 2540  C   LYS B  43     1048    503    931    -90     78     20       C  
ATOM   2541  O   LYS B  43      11.320   6.094  26.734  1.00  7.58           O  
ANISOU 2541  O   LYS B  43     1204    520    983   -128     88    -27       O  
ATOM   2542  CB  LYS B  43       8.380   4.950  27.350  1.00 13.24           C  
ANISOU 2542  CB  LYS B  43      991   2407   1333   -334     71    -81       C  
ATOM   2543  CG ALYS B  43       7.344   4.362  28.242  0.70 17.54           C  
ANISOU 2543  CG ALYS B  43     1183   3687   1397   -829    123    -64       C  
ATOM   2544  CG BLYS B  43       7.936   5.883  26.300  0.30 20.41           C  
ANISOU 2544  CG BLYS B  43     1645   1826   3822    -39   -948    462       C  
ATOM   2545  CD ALYS B  43       5.928   4.851  28.067  0.70 24.39           C  
ANISOU 2545  CD ALYS B  43     1058   5528   2128   -607     61  -1086       C  
ATOM   2546  CD BLYS B  43       6.405   5.929  26.216  0.30 29.70           C  
ANISOU 2546  CD BLYS B  43     1648   3066   5900   1461   -539   -551       C  
ATOM   2547  CE ALYS B  43       5.418   5.551  26.887  0.70 38.17           C  
ANISOU 2547  CE ALYS B  43     2733   6019   4887   1340   -741    149       C  
ATOM   2548  CE BLYS B  43       5.888   6.909  25.175  0.30 28.87           C  
ANISOU 2548  CE BLYS B  43     1379   2129   6807    386  -1590   -577       C  
ATOM   2549  NZ ALYS B  43       3.930   5.832  27.164  0.70 55.76           N  
ANISOU 2549  NZ ALYS B  43     2437  10698   6790   1812  -1974  -2581       N  
ATOM   2550  NZ BLYS B  43       5.292   6.298  23.951  0.30 31.47           N  
ANISOU 2550  NZ BLYS B  43     1121   4567   5557   -445   -399   -584       N  
ATOM   2551  H   LYS B  43      10.269   5.811  29.038  1.00  8.81           H  
ATOM   2552  HA  LYS B  43       9.849   3.481  27.635  1.00  9.30           H  
ATOM   2553  HB2ALYS B  43       8.356   5.916  27.439  1.00 15.89           H  
ATOM   2554  HB3ALYS B  43       8.158   4.735  26.431  1.00 15.89           H  
ATOM   2555  HG2ALYS B  43       7.347   3.401  28.112  0.70 21.05           H  
ATOM   2556  HG2BLYS B  43       8.276   6.771  26.493  0.30 24.49           H  
ATOM   2557  HG3ALYS B  43       7.608   4.530  29.160  0.70 21.05           H  
ATOM   2558  HG3BLYS B  43       8.299   5.602  25.445  0.30 24.49           H  
ATOM   2559  HD2ALYS B  43       5.360   4.073  28.184  0.70 29.26           H  
ATOM   2560  HD2BLYS B  43       6.075   5.041  26.003  0.30 35.65           H  
ATOM   2561  HD3ALYS B  43       5.751   5.433  28.822  0.70 29.26           H  
ATOM   2562  HD3BLYS B  43       6.050   6.176  27.084  0.30 35.65           H  
ATOM   2563  HE2ALYS B  43       5.901   6.381  26.750  0.70 45.80           H  
ATOM   2564  HE2BLYS B  43       5.218   7.472  25.592  0.30 34.64           H  
ATOM   2565  HE3ALYS B  43       5.518   4.999  26.095  0.70 45.80           H  
ATOM   2566  HE3BLYS B  43       6.622   7.482  24.904  0.30 34.64           H  
ATOM   2567  HZ1ALYS B  43       3.575   6.259  26.469  0.70 83.64           H  
ATOM   2568  HZ1BLYS B  43       5.018   6.942  23.401  0.30 47.21           H  
ATOM   2569  HZ2ALYS B  43       3.501   5.062  27.290  0.70 83.64           H  
ATOM   2570  HZ2BLYS B  43       5.904   5.798  23.541  0.30 47.21           H  
ATOM   2571  HZ3ALYS B  43       3.854   6.336  27.893  0.70 83.64           H  
ATOM   2572  HZ3BLYS B  43       4.599   5.789  24.181  0.30 47.21           H  
ATOM   2573  N   PRO B  44      10.914   4.319  25.443  1.00  7.43           N  
ANISOU 2573  N   PRO B  44     1256    501    900   -128     55     16       N  
ATOM   2574  CA  PRO B  44      11.841   4.776  24.427  1.00  8.09           C  
ANISOU 2574  CA  PRO B  44     1345    624    920     15    105     40       C  
ATOM   2575  C   PRO B  44      11.243   5.867  23.581  1.00  7.93           C  
ANISOU 2575  C   PRO B  44     1191    707    936    -67      1     25       C  
ATOM   2576  O   PRO B  44      10.033   5.886  23.323  1.00  9.49           O  
ANISOU 2576  O   PRO B  44     1398    729   1264    -89    -30    261       O  
ATOM   2577  CB  PRO B  44      12.087   3.513  23.599  1.00  9.30           C  
ANISOU 2577  CB  PRO B  44     1580    800    942    207    130     13       C  
ATOM   2578  CG  PRO B  44      10.756   2.805  23.668  1.00  9.72           C  
ANISOU 2578  CG  PRO B  44     1937    615    922     67   -161    -65       C  
ATOM   2579  CD  PRO B  44      10.233   3.048  25.067  1.00  8.38           C  
ANISOU 2579  CD  PRO B  44     1479    554    960   -113   -158     21       C  
ATOM   2580  HA  PRO B  44      12.676   5.083  24.839  1.00  9.70           H  
ATOM   2581  HB2 PRO B  44      12.321   3.733  22.683  1.00 11.16           H  
ATOM   2582  HB3 PRO B  44      12.793   2.971  23.985  1.00 11.16           H  
ATOM   2583  HG2 PRO B  44      10.143   3.165  23.007  1.00 11.67           H  
ATOM   2584  HG3 PRO B  44      10.865   1.855  23.505  1.00 11.67           H  
ATOM   2585  HD2 PRO B  44       9.269   3.151  25.070  1.00 10.05           H  
ATOM   2586  HD3 PRO B  44      10.479   2.326  25.666  1.00 10.05           H  
ATOM   2587  N  ALYS B  45      12.116   6.731  23.077  0.38  7.90           N  
ANISOU 2587  N  ALYS B  45     1260    743    820     10    138     54       N  
ATOM   2588  N  BLYS B  45      12.032   6.835  23.111  0.62  8.65           N  
ANISOU 2588  N  BLYS B  45     1306    797    988   -145    -10    148       N  
ATOM   2589  CA ALYS B  45      11.728   7.833  22.218  0.38  7.53           C  
ANISOU 2589  CA ALYS B  45     1006    671   1015    -79     19     67       C  
ATOM   2590  CA BLYS B  45      11.591   7.802  22.136  0.62  8.95           C  
ANISOU 2590  CA BLYS B  45     1634    652    911   -197     33     97       C  
ATOM   2591  C  ALYS B  45      12.913   8.215  21.326  0.38  7.80           C  
ANISOU 2591  C  ALYS B  45     1089    783    915    -85    103     11       C  
ATOM   2592  C  BLYS B  45      12.827   8.188  21.312  0.62  9.04           C  
ANISOU 2592  C  BLYS B  45     1712    615    903    -95    115     -9       C  
ATOM   2593  O  ALYS B  45      14.061   8.229  21.791  0.38  9.17           O  
ANISOU 2593  O  ALYS B  45     1065    997   1213   -254     83   -320       O  
ATOM   2594  O  BLYS B  45      13.953   8.249  21.805  0.62 10.02           O  
ANISOU 2594  O  BLYS B  45     1583   1130    867     76    289    228       O  
ATOM   2595  CB ALYS B  45      11.256   8.956  23.150  0.38 12.13           C  
ANISOU 2595  CB ALYS B  45     1924    651   1760    -94   1004    161       C  
ATOM   2596  CB BLYS B  45      11.021   9.048  22.811  0.62  8.79           C  
ANISOU 2596  CB BLYS B  45     1297    849    993    -33    -15    124       C  
ATOM   2597  CG ALYS B  45      10.912  10.271  22.600  0.38 15.42           C  
ANISOU 2597  CG ALYS B  45     2174    710   2628    202    763    172       C  
ATOM   2598  CG BLYS B  45      10.214   9.977  21.950  0.62  8.93           C  
ANISOU 2598  CG BLYS B  45     1360    934    895   -150     47    239       C  
ATOM   2599  CD ALYS B  45       9.597  10.939  22.519  0.38 11.22           C  
ANISOU 2599  CD ALYS B  45     1453   1096   1462   -281    480    230       C  
ATOM   2600  CD BLYS B  45       9.760  11.135  22.802  0.62 14.98           C  
ANISOU 2600  CD BLYS B  45     1884   1148   2319    523   -488   -478       C  
ATOM   2601  CE ALYS B  45       8.862  11.694  21.493  0.38 15.21           C  
ANISOU 2601  CE ALYS B  45     2852    722   1860   -103     21    213       C  
ATOM   2602  CE BLYS B  45       9.169  12.269  22.053  0.62 14.09           C  
ANISOU 2602  CE BLYS B  45     2320    935   1780   -136    -25     91       C  
ATOM   2603  NZ ALYS B  45       7.851  12.719  21.945  0.38 14.57           N  
ANISOU 2603  NZ ALYS B  45     2428   1209   1570     90   -377    226       N  
ATOM   2604  NZ BLYS B  45       7.918  11.811  21.379  0.62 15.82           N  
ANISOU 2604  NZ BLYS B  45     2264   1743   1645    718   -470   -184       N  
ATOM   2605  H  ALYS B  45      12.949   6.632  23.268  0.38  9.48           H  
ATOM   2606  H  BLYS B  45      12.840   6.885  23.403  0.62 10.38           H  
ATOM   2607  HA ALYS B  45      10.979   7.550  21.653  0.38  9.04           H  
ATOM   2608  HA BLYS B  45      10.914   7.400  21.552  0.62 10.74           H  
ATOM   2609  HB2ALYS B  45      10.477   8.629  23.625  0.38 14.56           H  
ATOM   2610  HB2BLYS B  45      10.463   8.760  23.550  0.62 10.54           H  
ATOM   2611  HB3ALYS B  45      11.952   9.093  23.812  0.38 14.56           H  
ATOM   2612  HB3BLYS B  45      11.760   9.551  23.187  0.62 10.54           H  
ATOM   2613  HG2ALYS B  45      11.482  10.897  23.074  0.38 18.51           H  
ATOM   2614  HG2BLYS B  45      10.754  10.299  21.212  0.62 10.71           H  
ATOM   2615  HG3ALYS B  45      11.241  10.254  21.687  0.38 18.51           H  
ATOM   2616  HG3BLYS B  45       9.445   9.510  21.587  0.62 10.71           H  
ATOM   2617  HD2ALYS B  45       8.975  10.237  22.766  0.38 13.47           H  
ATOM   2618  HD2BLYS B  45       9.104  10.811  23.438  0.62 17.97           H  
ATOM   2619  HD3ALYS B  45       9.609  11.546  23.276  0.38 13.47           H  
ATOM   2620  HD3BLYS B  45      10.520  11.462  23.307  0.62 17.97           H  
ATOM   2621  HE2ALYS B  45       9.514  12.148  20.936  0.38 18.25           H  
ATOM   2622  HE2BLYS B  45       8.968  12.997  22.662  0.62 16.91           H  
ATOM   2623  HE3ALYS B  45       8.401  11.054  20.929  0.38 18.25           H  
ATOM   2624  HE3BLYS B  45       9.801  12.591  21.391  0.62 16.91           H  
ATOM   2625  HZ1ALYS B  45       7.479  13.103  21.233  0.38 21.85           H  
ATOM   2626  HZ1BLYS B  45       7.559  12.488  20.927  0.62 23.73           H  
ATOM   2627  HZ2ALYS B  45       7.221  12.320  22.430  0.38 21.85           H  
ATOM   2628  HZ2BLYS B  45       8.109  11.148  20.816  0.62 23.73           H  
ATOM   2629  HZ3ALYS B  45       8.257  13.339  22.438  0.38 21.85           H  
ATOM   2630  HZ3BLYS B  45       7.340  11.523  21.991  0.62 23.73           H  
ATOM   2631  N   MET B  46      12.604   8.554  20.078  1.00 10.10           N  
ANISOU 2631  N   MET B  46     1603   1089    917    -78     96     67       N  
ATOM   2632  CA  MET B  46      13.568   9.202  19.216  1.00 11.20           C  
ANISOU 2632  CA  MET B  46     1662   1355    984    -75    187    203       C  
ATOM   2633  C   MET B  46      13.104  10.609  18.929  1.00 11.03           C  
ANISOU 2633  C   MET B  46     1369   1570   1002    103    204    298       C  
ATOM   2634  O   MET B  46      11.922  10.787  18.629  1.00 14.47           O  
ANISOU 2634  O   MET B  46     1532   1691   1947   -203    -88    724       O  
ATOM   2635  CB  MET B  46      13.649   8.427  17.873  1.00 23.50           C  
ANISOU 2635  CB  MET B  46     5101   2099   1198     23   1196   -113       C  
ATOM   2636  CG AMET B  46      14.600   7.249  18.149  0.53 22.74           C  
ANISOU 2636  CG AMET B  46     5300    787   2040   -653   1369   -269       C  
ATOM   2637  CG BMET B  46      14.772   8.738  16.906  0.47 26.97           C  
ANISOU 2637  CG BMET B  46     6240   1643   1754    196   1979    175       C  
ATOM   2638  SD AMET B  46      15.024   6.383  16.652  0.53 30.79           S  
ANISOU 2638  SD AMET B  46     6444   1870   2689     62   1013   -910       S  
ATOM   2639  SD BMET B  46      16.274   7.743  17.209  0.47 32.51           S  
ANISOU 2639  SD BMET B  46     5569   2413   3635    -33   2241    311       S  
ATOM   2640  CE AMET B  46      14.663   7.589  15.427  0.53 29.34           C  
ANISOU 2640  CE AMET B  46     7292   1153   2038  -1052   3047   -564       C  
ATOM   2641  CE BMET B  46      15.322   6.648  18.287  0.47 28.08           C  
ANISOU 2641  CE BMET B  46     7866    550   1619    250   2413   -363       C  
ATOM   2642  H  AMET B  46      11.816   8.384  19.778  1.00 12.12           H  
ATOM   2643  HA  MET B  46      14.447   9.220  19.648  1.00 13.44           H  
ATOM   2644  HB2AMET B  46      12.773   8.106  17.608  1.00 28.20           H  
ATOM   2645  HB3AMET B  46      14.001   8.995  17.170  1.00 28.20           H  
ATOM   2646  HG2AMET B  46      15.409   7.581  18.567  0.53 27.29           H  
ATOM   2647  HG2BMET B  46      14.463   8.575  16.002  0.47 32.36           H  
ATOM   2648  HG3AMET B  46      14.176   6.633  18.766  0.53 27.29           H  
ATOM   2649  HG3BMET B  46      14.997   9.679  16.977  0.47 32.36           H  
ATOM   2650  HE1AMET B  46      14.856   7.231  14.558  0.53 44.01           H  
ATOM   2651  HE1BMET B  46      15.896   5.959  18.630  0.47 42.12           H  
ATOM   2652  HE2AMET B  46      13.734   7.827  15.476  0.53 44.01           H  
ATOM   2653  HE2BMET B  46      14.959   7.155  19.017  0.47 42.12           H  
ATOM   2654  HE3AMET B  46      15.202   8.370  15.578  0.53 44.01           H  
ATOM   2655  HE3BMET B  46      14.607   6.249  17.787  0.47 42.12           H  
ATOM   2656  N   ILE B  47      13.988  11.563  18.995  1.00  9.78           N  
ANISOU 2656  N   ILE B  47     1463   1201    829    145    278     84       N  
ATOM   2657  CA  ILE B  47      13.648  12.954  18.677  1.00  9.62           C  
ANISOU 2657  CA  ILE B  47     1351   1247    841    193    303    100       C  
ATOM   2658  C   ILE B  47      14.604  13.458  17.608  1.00  9.51           C  
ANISOU 2658  C   ILE B  47     1346   1208    843    215    318     45       C  
ATOM   2659  O   ILE B  47      15.811  13.161  17.621  1.00 14.49           O  
ANISOU 2659  O   ILE B  47     1483   2502   1191    761    617    703       O  
ATOM   2660  CB  ILE B  47      13.644  13.842  19.916  1.00  9.03           C  
ANISOU 2660  CB  ILE B  47     1212   1144    871    160    368     85       C  
ATOM   2661  CG1 ILE B  47      15.002  13.843  20.676  1.00  9.47           C  
ANISOU 2661  CG1 ILE B  47     1163   1198   1022    194    312    216       C  
ATOM   2662  CG2 ILE B  47      12.518  13.490  20.856  1.00 10.07           C  
ANISOU 2662  CG2 ILE B  47     1287   1454    856    144    389     75       C  
ATOM   2663  CD1 ILE B  47      15.116  14.883  21.753  1.00  9.37           C  
ANISOU 2663  CD1 ILE B  47     1248    978   1121    116    229    154       C  
ATOM   2664  H   ILE B  47      14.793  11.372  19.232  1.00 11.73           H  
ATOM   2665  HA  ILE B  47      12.743  12.963  18.299  1.00 11.55           H  
ATOM   2666  HB  ILE B  47      13.486  14.760  19.611  1.00 10.84           H  
ATOM   2667 HG12 ILE B  47      15.134  12.968  21.074  1.00 11.36           H  
ATOM   2668 HG13 ILE B  47      15.716  13.983  20.034  1.00 11.36           H  
ATOM   2669 HG21 ILE B  47      12.548  14.068  21.622  1.00 15.10           H  
ATOM   2670 HG22 ILE B  47      11.678  13.600  20.405  1.00 15.10           H  
ATOM   2671 HG23 ILE B  47      12.611  12.578  21.140  1.00 15.10           H  
ATOM   2672 HD11 ILE B  47      15.977  14.818  22.171  1.00 14.05           H  
ATOM   2673 HD12 ILE B  47      15.012  15.756  21.367  1.00 14.05           H  
ATOM   2674 HD13 ILE B  47      14.430  14.740  22.409  1.00 14.05           H  
ATOM   2675  N  AGLY B  48      14.071  14.257  16.697  0.54  8.87           N  
ANISOU 2675  N  AGLY B  48     1237    885   1049    143    374    145       N  
ATOM   2676  N  BGLY B  48      13.986  14.151  16.699  0.46  7.34           N  
ANISOU 2676  N  BGLY B  48     1258    551    813   -115    131   -174       N  
ATOM   2677  CA AGLY B  48      14.680  14.717  15.451  0.54  7.55           C  
ANISOU 2677  CA AGLY B  48     1194    767    736   -146    -11    -42       C  
ATOM   2678  CA BGLY B  48      14.929  14.718  15.707  0.46  6.92           C  
ANISOU 2678  CA BGLY B  48     1276    579    619     58     14    -87       C  
ATOM   2679  C  AGLY B  48      14.861  16.234  15.276  0.54  6.41           C  
ANISOU 2679  C  AGLY B  48     1128    697    466      0    225    -74       C  
ATOM   2680  C  BGLY B  48      14.982  16.190  15.963  0.46  5.33           C  
ANISOU 2680  C  BGLY B  48      916    574    415    -19    162    -90       C  
ATOM   2681  O  AGLY B  48      13.846  16.907  15.524  0.54  7.58           O  
ANISOU 2681  O  AGLY B  48     1023    763    922    -51    272     47       O  
ATOM   2682  O  BGLY B  48      14.302  16.802  16.754  0.46  6.27           O  
ANISOU 2682  O  BGLY B  48     1008    495    738     28    314     57       O  
ATOM   2683  H  AGLY B  48      13.274  14.537  16.857  0.54 10.65           H  
ATOM   2684  H  BGLY B  48      13.134  14.266  16.676  0.46  8.81           H  
ATOM   2685  HA2AGLY B  48      15.552  14.300  15.371  0.54  9.06           H  
ATOM   2686  HA2BGLY B  48      15.809  14.324  15.814  0.46  8.31           H  
ATOM   2687  HA3AGLY B  48      14.138  14.393  14.714  0.54  9.06           H  
ATOM   2688  HA3BGLY B  48      14.618  14.542  14.806  0.46  8.31           H  
ATOM   2689  N  AGLY B  49      16.106  16.606  15.058  0.54  8.87           N  
ANISOU 2689  N  AGLY B  49      917    437   1816    136    296   -251       N  
ATOM   2690  N  BGLY B  49      15.824  16.825  15.013  0.46  7.63           N  
ANISOU 2690  N  BGLY B  49      644    452   1630     44    374    -94       N  
ATOM   2691  CA AGLY B  49      16.301  18.051  15.253  0.54  6.16           C  
ANISOU 2691  CA AGLY B  49     1070    665    464    -82     98    -78       C  
ATOM   2692  CA BGLY B  49      16.014  18.156  14.373  0.46  6.28           C  
ANISOU 2692  CA BGLY B  49      955    596    693   -120    226    -47       C  
ATOM   2693  C  AGLY B  49      17.158  18.438  14.073  0.54  5.62           C  
ANISOU 2693  C  AGLY B  49      975    542    489     67     50   -137       C  
ATOM   2694  C  BGLY B  49      17.193  18.385  13.475  0.46  5.54           C  
ANISOU 2694  C  BGLY B  49      841    628    511    -21    131   -152       C  
ATOM   2695  O  AGLY B  49      17.115  17.790  13.011  0.54  6.16           O  
ANISOU 2695  O  AGLY B  49     1190    609    403    -78    117   -162       O  
ATOM   2696  O  BGLY B  49      17.497  17.592  12.579  0.46  6.54           O  
ANISOU 2696  O  BGLY B  49     1201    624    514     -9    163   -144       O  
ATOM   2697  H  AGLY B  49      16.734  16.065  14.828  0.54 10.65           H  
ATOM   2698  H  BGLY B  49      16.406  16.266  14.714  0.46  9.16           H  
ATOM   2699  HA2AGLY B  49      15.455  18.524  15.242  0.54  7.39           H  
ATOM   2700  HA2BGLY B  49      15.215  18.347  13.858  0.46  7.53           H  
ATOM   2701  HA3AGLY B  49      16.756  18.233  16.091  0.54  7.39           H  
ATOM   2702  HA3BGLY B  49      16.058  18.815  15.083  0.46  7.53           H  
ATOM   2703  N  AILE B  50      17.961  19.489  14.222  0.54  5.20           N  
ANISOU 2703  N  AILE B  50      799    581    478    -41    122   -111       N  
ATOM   2704  N  BILE B  50      17.894  19.520  13.675  0.46  5.88           N  
ANISOU 2704  N  BILE B  50      968    535    600    -97    259   -114       N  
ATOM   2705  CA AILE B  50      18.629  20.065  13.088  0.54  5.52           C  
ANISOU 2705  CA AILE B  50      897    578    497    -10     80     40       C  
ATOM   2706  CA BILE B  50      19.089  19.821  12.891  0.46  6.55           C  
ANISOU 2706  CA BILE B  50     1025    651    663    -76    244     87       C  
ATOM   2707  C  AILE B  50      19.597  19.093  12.384  0.54  5.83           C  
ANISOU 2707  C  AILE B  50      902    588    593    -23    173    -14       C  
ATOM   2708  C  BILE B  50      20.120  18.735  13.129  0.46  6.84           C  
ANISOU 2708  C  BILE B  50      937    787    721    -63    191    140       C  
ATOM   2709  O  AILE B  50      19.776  19.185  11.185  0.54  6.95           O  
ANISOU 2709  O  AILE B  50     1220    735    529     90    178     13       O  
ATOM   2710  O  BILE B  50      20.476  18.401  14.273  0.46  7.85           O  
ANISOU 2710  O  BILE B  50     1177    817    809    -40    178    203       O  
ATOM   2711  CB AILE B  50      19.354  21.372  13.501  0.54  5.30           C  
ANISOU 2711  CB AILE B  50      858    603    432     29     77    -43       C  
ATOM   2712  CB BILE B  50      19.662  21.206  13.278  0.46  7.23           C  
ANISOU 2712  CB BILE B  50     1154    718    711    -54    268      1       C  
ATOM   2713  CG1AILE B  50      19.746  22.246  12.313  0.54  5.86           C  
ANISOU 2713  CG1AILE B  50      870    677    546    -69     69    -34       C  
ATOM   2714  CG1BILE B  50      18.693  22.339  12.922  0.46  7.57           C  
ANISOU 2714  CG1BILE B  50     1232    647    826   -184    286    -65       C  
ATOM   2715  CG2AILE B  50      20.536  21.091  14.397  0.54  5.83           C  
ANISOU 2715  CG2AILE B  50      881    639    565     -4     41    -39       C  
ATOM   2716  CG2BILE B  50      21.049  21.454  12.779  0.46  7.40           C  
ANISOU 2716  CG2BILE B  50     1098    776    771   -228     49     88       C  
ATOM   2717  CD1AILE B  50      18.619  22.717  11.434  0.54  5.52           C  
ANISOU 2717  CD1AILE B  50      820    609    542    -78     45    -75       C  
ATOM   2718  CD1BILE B  50      18.589  22.651  11.454  0.46 11.54           C  
ANISOU 2718  CD1BILE B  50     1844   1091   1188   -194    -84    567       C  
ATOM   2719  H  AILE B  50      18.082  19.826  15.005  0.54  6.24           H  
ATOM   2720  H  BILE B  50      17.633  20.078  14.276  0.46  7.06           H  
ATOM   2721  HA AILE B  50      17.939  20.309  12.437  0.54  6.62           H  
ATOM   2722  HA BILE B  50      18.851  19.831  11.940  0.46  7.86           H  
ATOM   2723  HB AILE B  50      18.715  21.891  14.033  0.54  6.36           H  
ATOM   2724  HB BILE B  50      19.725  21.205  14.256  0.46  8.67           H  
ATOM   2725 HG12AILE B  50      20.213  23.026  12.651  0.54  7.03           H  
ATOM   2726 HG12BILE B  50      17.811  22.105  13.250  0.46  9.08           H  
ATOM   2727 HG13AILE B  50      20.372  21.749  11.764  0.54  7.03           H  
ATOM   2728 HG13BILE B  50      18.974  23.142  13.388  0.46  9.08           H  
ATOM   2729 HG21AILE B  50      20.257  20.541  15.132  0.54  8.75           H  
ATOM   2730 HG21BILE B  50      21.615  20.720  13.026  0.46 11.10           H  
ATOM   2731 HG22AILE B  50      21.216  20.635  13.896  0.54  8.75           H  
ATOM   2732 HG22BILE B  50      21.034  21.539  11.822  0.46 11.10           H  
ATOM   2733 HG23AILE B  50      20.887  21.919  14.732  0.54  8.75           H  
ATOM   2734 HG23BILE B  50      21.388  22.264  13.166  0.46 11.10           H  
ATOM   2735 HD11AILE B  50      18.971  23.255  10.722  0.54  8.27           H  
ATOM   2736 HD11BILE B  50      17.964  23.369  11.323  0.46 17.31           H  
ATOM   2737 HD12AILE B  50      18.162  21.957  11.065  0.54  8.27           H  
ATOM   2738 HD12BILE B  50      19.450  22.912  11.120  0.46 17.31           H  
ATOM   2739 HD13AILE B  50      18.003  23.238  11.955  0.54  8.27           H  
ATOM   2740 HD13BILE B  50      18.284  21.873  10.982  0.46 17.31           H  
ATOM   2741  N  AGLY B  51      20.221  18.217  13.148  0.54  5.97           N  
ANISOU 2741  N  AGLY B  51      984    637    511     24    124    -28       N  
ATOM   2742  N  BGLY B  51      20.626  18.175  12.038  0.46  7.14           N  
ANISOU 2742  N  BGLY B  51      988    751    815    -47    243     48       N  
ATOM   2743  CA AGLY B  51      21.258  17.353  12.654  0.54  6.91           C  
ANISOU 2743  CA AGLY B  51     1038    718    712     57    202     40       C  
ATOM   2744  CA BGLY B  51      21.653  17.169  12.130  0.46  9.30           C  
ANISOU 2744  CA BGLY B  51     1339    904   1081    127    379     97       C  
ATOM   2745  C  AGLY B  51      20.952  15.935  12.288  0.54  8.68           C  
ANISOU 2745  C  AGLY B  51     1601    739    761     65    199      2       C  
ATOM   2746  C  BGLY B  51      21.063  15.780  12.336  0.46 10.29           C  
ANISOU 2746  C  BGLY B  51     1512    851   1313     -2    -14    203       C  
ATOM   2747  O  AGLY B  51      21.712  15.214  11.678  0.54 10.83           O  
ANISOU 2747  O  AGLY B  51     1919    904   1048    -33    598    -41       O  
ATOM   2748  O  BGLY B  51      21.891  14.896  12.115  0.46 12.51           O  
ANISOU 2748  O  BGLY B  51     1645   1107   1719     22    486     97       O  
ATOM   2749  H  AGLY B  51      19.998  18.161  13.977  0.54  7.16           H  
ATOM   2750  H  BGLY B  51      20.337  18.416  11.264  0.46  8.57           H  
ATOM   2751  HA2AGLY B  51      21.636  17.777  11.868  0.54  8.29           H  
ATOM   2752  HA2BGLY B  51      22.181  17.175  11.316  0.46 11.17           H  
ATOM   2753  HA3AGLY B  51      21.958  17.331  13.326  0.54  8.29           H  
ATOM   2754  HA3BGLY B  51      22.242  17.380  12.870  0.46 11.17           H  
ATOM   2755  N   GLY B  52      19.786  15.500  12.660  1.00  8.94           N  
ANISOU 2755  N   GLY B  52     1539    665    991    -12    108    -99       N  
ATOM   2756  CA  GLY B  52      19.344  14.142  12.668  1.00  9.38           C  
ANISOU 2756  CA  GLY B  52     1841    701    810    -97    436   -150       C  
ATOM   2757  C   GLY B  52      18.616  13.847  13.962  1.00  9.01           C  
ANISOU 2757  C   GLY B  52     1550    796    873    192    425    -51       C  
ATOM   2758  O   GLY B  52      17.949  14.714  14.514  1.00 10.70           O  
ANISOU 2758  O   GLY B  52     1691   1017   1115    381    485    -85       O  
ATOM   2759  H  AGLY B  52      19.222  16.090  12.930  1.00 10.73           H  
ATOM   2760  HA2 GLY B  52      18.751  13.987  11.916  1.00 11.26           H  
ATOM   2761  HA3 GLY B  52      20.107  13.549  12.579  1.00 11.26           H  
ATOM   2762  N   PHE B  53      18.762  12.646  14.459  1.00 12.22           N  
ANISOU 2762  N   PHE B  53     2019   1001   1345    405    973    319       N  
ATOM   2763  CA  PHE B  53      17.961  12.148  15.584  1.00 14.41           C  
ANISOU 2763  CA  PHE B  53     1724   1945   1481    552    820    733       C  
ATOM   2764  C   PHE B  53      18.880  11.684  16.709  1.00 13.76           C  
ANISOU 2764  C   PHE B  53     1547   1668   1702    592    872    866       C  
ATOM   2765  O   PHE B  53      20.025  11.216  16.489  1.00 15.41           O  
ANISOU 2765  O   PHE B  53     1635   1996   1876    670    854    900       O  
ATOM   2766  CB  PHE B  53      17.123  10.883  15.121  1.00 24.93           C  
ANISOU 2766  CB  PHE B  53     2692   4130   2087  -1485    668   1041       C  
ATOM   2767  CG  PHE B  53      16.059  11.218  14.056  1.00 22.02           C  
ANISOU 2767  CG  PHE B  53     3579   1706   2584   -744    117   -210       C  
ATOM   2768  CD1 PHE B  53      16.405  11.392  12.708  1.00 28.34           C  
ANISOU 2768  CD1 PHE B  53     4300   3443   2382  -1485   -548    192       C  
ATOM   2769  CD2 PHE B  53      14.720  11.470  14.404  1.00 26.11           C  
ANISOU 2769  CD2 PHE B  53     3386   2013   3931   -686   -324  -1190       C  
ATOM   2770  CE1 PHE B  53      15.484  11.808  11.765  1.00 30.54           C  
ANISOU 2770  CE1 PHE B  53     5104   2716   3093  -1998  -1474     33       C  
ATOM   2771  CE2 PHE B  53      13.744  11.859  13.446  1.00 29.56           C  
ANISOU 2771  CE2 PHE B  53     3839   1524   5201   -770  -1197  -1355       C  
ATOM   2772  CZ  PHE B  53      14.157  12.026  12.133  1.00 36.31           C  
ANISOU 2772  CZ  PHE B  53     5327   2738   4909   -438  -1813   -389       C  
ATOM   2773  H   PHE B  53      19.352  12.126  14.111  1.00 14.66           H  
ATOM   2774  HA  PHE B  53      17.360  12.851  15.908  1.00 17.29           H  
ATOM   2775  HB2 PHE B  53      17.731  10.218  14.761  1.00 29.92           H  
ATOM   2776  HB3 PHE B  53      16.685  10.495  15.894  1.00 29.92           H  
ATOM   2777  HD1 PHE B  53      17.280  11.223  12.440  1.00 34.00           H  
ATOM   2778  HD2 PHE B  53      14.464  11.380  15.293  1.00 31.33           H  
ATOM   2779  HE1 PHE B  53      15.750  11.942  10.884  1.00 36.65           H  
ATOM   2780  HE2 PHE B  53      12.858  11.996  13.692  1.00 35.48           H  
ATOM   2781  HZ  PHE B  53      13.540  12.288  11.488  1.00 43.57           H  
ATOM   2782  N   ILE B  54      18.347  11.720  17.942  1.00 12.79           N  
ANISOU 2782  N   ILE B  54     1384   1620   1564    428    687    761       N  
ATOM   2783  CA  ILE B  54      18.938  11.065  19.070  1.00 11.25           C  
ANISOU 2783  CA  ILE B  54     1105   1330   1584    409    606    665       C  
ATOM   2784  C   ILE B  54      17.862  10.167  19.729  1.00 10.69           C  
ANISOU 2784  C   ILE B  54     1312   1111   1395    314    598    388       C  
ATOM   2785  O   ILE B  54      16.664  10.417  19.672  1.00 11.10           O  
ANISOU 2785  O   ILE B  54     1337   1154   1474    201    536    353       O  
ATOM   2786  CB  ILE B  54      19.612  11.995  20.116  1.00 12.61           C  
ANISOU 2786  CB  ILE B  54     1175   1254   2078    127    241    755       C  
ATOM   2787  CG1 ILE B  54      18.632  12.992  20.777  1.00 11.88           C  
ANISOU 2787  CG1 ILE B  54     1110   1315   1819    135    325    653       C  
ATOM   2788  CG2 ILE B  54      20.804  12.713  19.519  1.00 14.78           C  
ANISOU 2788  CG2 ILE B  54     1272   1519   2491     93    564    723       C  
ATOM   2789  CD1 ILE B  54      19.133  13.780  21.927  1.00 14.71           C  
ANISOU 2789  CD1 ILE B  54     1369   1149   2739    -76   -146    291       C  
ATOM   2790  H   ILE B  54      17.616  12.157  18.060  1.00 15.34           H  
ATOM   2791  HA  ILE B  54      19.635  10.470  18.723  1.00 13.50           H  
ATOM   2792  HB  ILE B  54      19.955  11.418  20.830  1.00 15.13           H  
ATOM   2793 HG12 ILE B  54      18.334  13.615  20.095  1.00 14.25           H  
ATOM   2794 HG13 ILE B  54      17.853  12.495  21.072  1.00 14.25           H  
ATOM   2795 HG21 ILE B  54      21.395  12.072  19.117  1.00 22.17           H  
ATOM   2796 HG22 ILE B  54      20.503  13.333  18.852  1.00 22.17           H  
ATOM   2797 HG23 ILE B  54      21.271  13.187  20.211  1.00 22.17           H  
ATOM   2798 HD11 ILE B  54      18.437  14.358  22.247  1.00 22.07           H  
ATOM   2799 HD12 ILE B  54      19.403  13.184  22.630  1.00 22.07           H  
ATOM   2800 HD13 ILE B  54      19.885  14.308  21.649  1.00 22.07           H  
ATOM   2801  N   LYS B  55      18.369   9.126  20.424  1.00 11.07           N  
ANISOU 2801  N   LYS B  55     1447   1042   1467    275    658    401       N  
ATOM   2802  CA  LYS B  55      17.534   8.261  21.277  1.00 10.00           C  
ANISOU 2802  CA  LYS B  55     1618    829   1124     94    485    197       C  
ATOM   2803  C   LYS B  55      17.570   8.842  22.661  1.00  8.91           C  
ANISOU 2803  C   LYS B  55     1270    663   1251     22    332    163       C  
ATOM   2804  O   LYS B  55      18.623   9.207  23.180  1.00 11.07           O  
ANISOU 2804  O   LYS B  55     1245   1162   1549    -51    428     96       O  
ATOM   2805  CB  LYS B  55      18.113   6.864  21.295  1.00 14.45           C  
ANISOU 2805  CB  LYS B  55     2676    890   1598    253    767    171       C  
ATOM   2806  CG  LYS B  55      18.441   6.204  20.091  1.00 29.48           C  
ANISOU 2806  CG  LYS B  55     6566   1266   2703    332   2460   -253       C  
ATOM   2807  CD  LYS B  55      19.139   4.896  20.028  1.00 52.60           C  
ANISOU 2807  CD  LYS B  55     9904   2379   6513   2118   2981  -1154       C  
ATOM   2808  CE  LYS B  55      19.058   4.347  18.601  1.00 58.78           C  
ANISOU 2808  CE  LYS B  55    10848   2725   7431    336   4649  -2552       C  
ATOM   2809  NZ  LYS B  55      17.892   3.427  18.444  1.00 89.13           N  
ANISOU 2809  NZ  LYS B  55    15910   2628  13310  -2366    126   -934       N  
ATOM   2810  H   LYS B  55      19.211   8.962  20.366  1.00 13.29           H  
ATOM   2811  HA  LYS B  55      16.613   8.242  20.942  1.00 12.00           H  
ATOM   2812  HB2 LYS B  55      18.920   6.896  21.833  1.00 17.34           H  
ATOM   2813  HB3 LYS B  55      17.483   6.299  21.769  1.00 17.34           H  
ATOM   2814  HG2 LYS B  55      17.608   6.092  19.606  1.00 35.38           H  
ATOM   2815  HG3 LYS B  55      18.978   6.826  19.576  1.00 35.38           H  
ATOM   2816  HD2 LYS B  55      20.068   5.007  20.286  1.00 63.12           H  
ATOM   2817  HD3 LYS B  55      18.726   4.272  20.645  1.00 63.12           H  
ATOM   2818  HE2 LYS B  55      18.974   5.084  17.976  1.00 70.54           H  
ATOM   2819  HE3 LYS B  55      19.876   3.869  18.393  1.00 70.54           H  
ATOM   2820  HZ1 LYS B  55      17.866   3.121  17.609  1.00133.70           H  
ATOM   2821  HZ2 LYS B  55      17.975   2.743  19.008  1.00133.70           H  
ATOM   2822  HZ3 LYS B  55      17.140   3.868  18.622  1.00133.70           H  
ATOM   2823  N   VAL B  56      16.414   8.865  23.312  1.00  8.36           N  
ANISOU 2823  N   VAL B  56     1160    664   1163     31    281     52       N  
ATOM   2824  CA  VAL B  56      16.269   9.392  24.639  1.00  7.95           C  
ANISOU 2824  CA  VAL B  56     1137    656   1049     -3    187     44       C  
ATOM   2825  C   VAL B  56      15.367   8.471  25.463  1.00  7.62           C  
ANISOU 2825  C   VAL B  56      994    584   1146    -11    165    -23       C  
ATOM   2826  O   VAL B  56      14.663   7.593  24.944  1.00  9.06           O  
ANISOU 2826  O   VAL B  56     1344    863   1029   -197    197    -85       O  
ATOM   2827  CB  VAL B  56      15.666  10.830  24.618  1.00  8.63           C  
ANISOU 2827  CB  VAL B  56     1319    694   1072     74    169     27       C  
ATOM   2828  CG1 VAL B  56      16.596  11.765  23.845  1.00 11.33           C  
ANISOU 2828  CG1 VAL B  56     1879    684   1486     17    264    214       C  
ATOM   2829  CG2 VAL B  56      14.262  10.835  24.060  1.00 10.84           C  
ANISOU 2829  CG2 VAL B  56     1489   1047   1339    460    -57   -169       C  
ATOM   2830  H   VAL B  56      15.717   8.548  22.920  1.00 10.03           H  
ATOM   2831  HA  VAL B  56      17.152   9.428  25.062  1.00  9.54           H  
ATOM   2832  HB  VAL B  56      15.622  11.150  25.543  1.00 10.36           H  
ATOM   2833 HG11 VAL B  56      17.475  11.733  24.229  1.00 17.00           H  
ATOM   2834 HG12 VAL B  56      16.638  11.487  22.927  1.00 17.00           H  
ATOM   2835 HG13 VAL B  56      16.259  12.663  23.892  1.00 17.00           H  
ATOM   2836 HG21 VAL B  56      13.712  10.238  24.572  1.00 16.27           H  
ATOM   2837 HG22 VAL B  56      13.902  11.724  24.110  1.00 16.27           H  
ATOM   2838 HG23 VAL B  56      14.281  10.548  23.144  1.00 16.27           H  
ATOM   2839  N   ARG B  57      15.414   8.683  26.775  1.00  7.62           N  
ANISOU 2839  N   ARG B  57     1031    627   1064   -121    174    -39       N  
ATOM   2840  CA  ARG B  57      14.569   7.987  27.726  1.00  6.88           C  
ANISOU 2840  CA  ARG B  57      957    511    990    -88    160    -16       C  
ATOM   2841  C   ARG B  57      13.440   8.916  28.136  1.00  6.34           C  
ANISOU 2841  C   ARG B  57      936    450    879    -76    114     43       C  
ATOM   2842  O   ARG B  57      13.699  10.036  28.577  1.00  7.18           O  
ANISOU 2842  O   ARG B  57      929    474   1161    -58     63    -44       O  
ATOM   2843  CB  ARG B  57      15.359   7.563  28.955  1.00  7.54           C  
ANISOU 2843  CB  ARG B  57      997    507   1192    -61     47     75       C  
ATOM   2844  CG  ARG B  57      16.575   6.733  28.701  1.00  9.10           C  
ANISOU 2844  CG  ARG B  57     1070    635   1546     -9     83    -90       C  
ATOM   2845  CD  ARG B  57      17.165   6.078  29.902  1.00 10.85           C  
ANISOU 2845  CD  ARG B  57     1004    730   2143     -3   -198    208       C  
ATOM   2846  NE  ARG B  57      17.418   6.931  31.026  1.00 11.65           N  
ANISOU 2846  NE  ARG B  57     1363    797   2004    -52   -386    271       N  
ATOM   2847  CZ  ARG B  57      18.480   7.671  31.227  1.00 13.69           C  
ANISOU 2847  CZ  ARG B  57     1403    766   2723   -112   -547    258       C  
ATOM   2848  NH1 ARG B  57      19.371   7.759  30.253  1.00 16.45           N  
ANISOU 2848  NH1 ARG B  57     1271   1478   3129   -325   -478    689       N  
ATOM   2849  NH2 ARG B  57      18.572   8.338  32.372  1.00 18.12           N  
ANISOU 2849  NH2 ARG B  57     2518   1000   2958    123  -1245   -134       N  
ATOM   2850  H   ARG B  57      15.974   9.262  27.074  1.00  9.14           H  
ATOM   2851  HA  ARG B  57      14.190   7.192  27.297  1.00  8.26           H  
ATOM   2852  HB2 ARG B  57      15.631   8.362  29.432  1.00  9.05           H  
ATOM   2853  HB3 ARG B  57      14.767   7.064  29.539  1.00  9.05           H  
ATOM   2854  HG2 ARG B  57      16.347   6.044  28.057  1.00 10.92           H  
ATOM   2855  HG3 ARG B  57      17.252   7.298  28.296  1.00 10.92           H  
ATOM   2856  HD2 ARG B  57      16.566   5.370  30.187  1.00 13.02           H  
ATOM   2857  HD3 ARG B  57      18.002   5.662  29.641  1.00 13.02           H  
ATOM   2858  HE  ARG B  57      16.809   6.959  31.632  1.00 13.98           H  
ATOM   2859 HH11 ARG B  57      19.243   7.336  29.515  1.00 19.74           H  
ATOM   2860 HH12 ARG B  57      20.077   8.238  30.358  1.00 19.74           H  
ATOM   2861 HH21 ARG B  57      17.944   8.276  32.957  1.00 21.75           H  
ATOM   2862 HH22 ARG B  57      19.258   8.831  32.529  1.00 21.75           H  
ATOM   2863  N   GLN B  58      12.198   8.466  28.007  1.00  6.24           N  
ANISOU 2863  N   GLN B  58      941    482    807    -93     80     27       N  
ATOM   2864  CA  GLN B  58      11.038   9.272  28.343  1.00  6.11           C  
ANISOU 2864  CA  GLN B  58      923    474    785    -72    112     24       C  
ATOM   2865  C   GLN B  58      10.533   8.919  29.751  1.00  6.04           C  
ANISOU 2865  C   GLN B  58      882    501    775    -37     23    113       C  
ATOM   2866  O   GLN B  58      10.097   7.775  29.972  1.00  7.08           O  
ANISOU 2866  O   GLN B  58     1128    462    939   -102    200     84       O  
ATOM   2867  CB  GLN B  58       9.918   9.075  27.342  1.00  6.41           C  
ANISOU 2867  CB  GLN B  58      980    567    745   -104     62     49       C  
ATOM   2868  CG  GLN B  58       8.657   9.835  27.696  1.00  7.11           C  
ANISOU 2868  CG  GLN B  58      990    677    873    -96     43     65       C  
ATOM   2869  CD  GLN B  58       7.580   9.689  26.698  1.00  9.03           C  
ANISOU 2869  CD  GLN B  58     1132   1132    962   -108    -15     91       C  
ATOM   2870  OE1 GLN B  58       7.824   9.556  25.484  1.00 13.09           O  
ANISOU 2870  OE1 GLN B  58     1341   2461    876     71    -41    124       O  
ATOM   2871  NE2 GLN B  58       6.337   9.782  27.145  1.00 12.63           N  
ANISOU 2871  NE2 GLN B  58     1085   2162   1267   -277    -43    -95       N  
ATOM   2872  H   GLN B  58      12.076   7.667  27.713  1.00  7.49           H  
ATOM   2873  HA  GLN B  58      11.301  10.216  28.334  1.00  7.33           H  
ATOM   2874  HB2 GLN B  58      10.224   9.363  26.467  1.00  7.69           H  
ATOM   2875  HB3 GLN B  58       9.709   8.129  27.285  1.00  7.69           H  
ATOM   2876  HG2 GLN B  58       8.333   9.522  28.555  1.00  8.53           H  
ATOM   2877  HG3 GLN B  58       8.874  10.776  27.787  1.00  8.53           H  
ATOM   2878 HE21 GLN B  58       5.677   9.751  26.594  1.00 15.16           H  
ATOM   2879 HE22 GLN B  58       6.189   9.874  27.988  1.00 15.16           H  
ATOM   2880  N   TYR B  59      10.530   9.896  30.638  1.00  6.10           N  
ANISOU 2880  N   TYR B  59      977    485    717    -64     65    104       N  
ATOM   2881  CA  TYR B  59       9.997   9.787  31.998  1.00  6.32           C  
ANISOU 2881  CA  TYR B  59     1018    530    708    -59     72    152       C  
ATOM   2882  C   TYR B  59       8.752  10.665  32.070  1.00  6.54           C  
ANISOU 2882  C   TYR B  59      978    637    723    -88     77     79       C  
ATOM   2883  O   TYR B  59       8.772  11.820  31.681  1.00  8.75           O  
ANISOU 2883  O   TYR B  59     1097    708   1323     68    363    299       O  
ATOM   2884  CB  TYR B  59      10.990  10.225  33.048  1.00  7.53           C  
ANISOU 2884  CB  TYR B  59     1212    716    764    -22     20     18       C  
ATOM   2885  CG  TYR B  59      12.233   9.365  33.110  1.00  7.27           C  
ANISOU 2885  CG  TYR B  59     1209    591    799     -4    -90     93       C  
ATOM   2886  CD1 TYR B  59      13.325   9.615  32.287  1.00  7.70           C  
ANISOU 2886  CD1 TYR B  59     1180    659    913     31   -123    141       C  
ATOM   2887  CD2 TYR B  59      12.344   8.305  34.016  1.00  8.36           C  
ANISOU 2887  CD2 TYR B  59     1434    734    821    -59   -119    117       C  
ATOM   2888  CE1 TYR B  59      14.464   8.852  32.343  1.00  8.17           C  
ANISOU 2888  CE1 TYR B  59     1133    709   1077     33    -85     69       C  
ATOM   2889  CE2 TYR B  59      13.474   7.536  34.081  1.00  8.70           C  
ANISOU 2889  CE2 TYR B  59     1489    646    975     -7   -290    194       C  
ATOM   2890  CZ  TYR B  59      14.530   7.783  33.249  1.00  9.21           C  
ANISOU 2890  CZ  TYR B  59     1277    660   1355     37   -347    147       C  
ATOM   2891  OH  TYR B  59      15.705   7.058  33.263  1.00 10.80           O  
ANISOU 2891  OH  TYR B  59     1392    856   1610    214   -284    160       O  
ATOM   2892  H   TYR B  59      10.865  10.651  30.401  1.00  7.32           H  
ATOM   2893  HA  TYR B  59       9.742   8.856  32.168  1.00  7.58           H  
ATOM   2894  HB2 TYR B  59      11.253  11.141  32.867  1.00  9.04           H  
ATOM   2895  HB3 TYR B  59      10.556  10.209  33.915  1.00  9.04           H  
ATOM   2896  HD1 TYR B  59      13.282  10.319  31.682  1.00  9.24           H  
ATOM   2897  HD2 TYR B  59      11.634   8.119  34.587  1.00 10.04           H  
ATOM   2898  HE1 TYR B  59      15.184   9.041  31.786  1.00  9.80           H  
ATOM   2899  HE2 TYR B  59      13.524   6.840  34.697  1.00 10.44           H  
ATOM   2900  HH  TYR B  59      15.660   6.475  33.837  1.00 16.19           H  
ATOM   2901  N   ASP B  60       7.667  10.120  32.580  1.00  8.34           N  
ANISOU 2901  N   ASP B  60     1066    721   1193   -158    118    136       N  
ATOM   2902  CA  ASP B  60       6.419  10.860  32.691  1.00  8.38           C  
ANISOU 2902  CA  ASP B  60      967    908   1119   -136     56     41       C  
ATOM   2903  C   ASP B  60       6.210  11.378  34.116  1.00  8.12           C  
ANISOU 2903  C   ASP B  60      930    884   1089   -235    -31    118       C  
ATOM   2904  O   ASP B  60       6.670  10.826  35.111  1.00  9.15           O  
ANISOU 2904  O   ASP B  60     1190    904   1176    -54    -17    160       O  
ATOM   2905  CB  ASP B  60       5.249  10.024  32.215  1.00 10.41           C  
ANISOU 2905  CB  ASP B  60     1154   1113   1452   -343    137    -90       C  
ATOM   2906  CG  ASP B  60       5.385   9.709  30.680  1.00 12.82           C  
ANISOU 2906  CG  ASP B  60     1941   1131   1509   -523   -590      2       C  
ATOM   2907  OD1 ASP B  60       5.783  10.599  29.923  1.00 13.74           O  
ANISOU 2907  OD1 ASP B  60     1968   1611   1331   -437     21    -75       O  
ATOM   2908  OD2 ASP B  60       4.982   8.612  30.359  1.00 25.10           O  
ANISOU 2908  OD2 ASP B  60     5427   1593   1950  -1243   -656   -130       O  
ATOM   2909  H   ASP B  60       7.696   9.306  32.855  1.00 10.00           H  
ATOM   2910  HA  ASP B  60       6.485  11.639  32.100  1.00 10.05           H  
ATOM   2911  HB2 ASP B  60       5.220   9.193  32.715  1.00 12.49           H  
ATOM   2912  HB3 ASP B  60       4.421  10.503  32.377  1.00 12.49           H  
ATOM   2913  N   GLN B  61       5.438  12.458  34.203  1.00  7.78           N  
ANISOU 2913  N   GLN B  61      917    844   1020   -126    -33     68       N  
ATOM   2914  CA  GLN B  61       4.917  12.979  35.476  1.00  8.31           C  
ANISOU 2914  CA  GLN B  61      903   1036   1029   -178     49    148       C  
ATOM   2915  C   GLN B  61       6.046  13.325  36.453  1.00  7.47           C  
ANISOU 2915  C   GLN B  61      896    919    853    -91     79    205       C  
ATOM   2916  O   GLN B  61       5.989  13.042  37.649  1.00  9.65           O  
ANISOU 2916  O   GLN B  61     1120   1388    939   -240     85    334       O  
ATOM   2917  CB  GLN B  61       3.896  11.979  36.014  1.00 10.51           C  
ANISOU 2917  CB  GLN B  61     1002   1255   1499   -368    178    195       C  
ATOM   2918  CG AGLN B  61       2.820  12.615  36.807  0.64  8.91           C  
ANISOU 2918  CG AGLN B  61     1153    946   1084   -344    293   -166       C  
ATOM   2919  CG BGLN B  61       2.481  12.286  35.487  0.36 11.60           C  
ANISOU 2919  CG BGLN B  61      989   1966   1191   -364    185   -199       C  
ATOM   2920  CD AGLN B  61       1.667  11.658  37.029  0.64  9.93           C  
ANISOU 2920  CD AGLN B  61     1161   1110   1278   -347    409   -406       C  
ATOM   2921  CD BGLN B  61       1.454  11.351  36.069  0.36 14.40           C  
ANISOU 2921  CD BGLN B  61      995   1658   2492   -203    567   -195       C  
ATOM   2922  OE1AGLN B  61       1.312  10.865  36.210  0.64 15.62           O  
ANISOU 2922  OE1AGLN B  61     1691   2016   1873  -1126    845  -1047       O  
ATOM   2923  OE1BGLN B  61       1.110  10.335  35.474  0.36 20.32           O  
ANISOU 2923  OE1BGLN B  61     2486   1779   2995   -729    -30    -14       O  
ATOM   2924  NE2AGLN B  61       1.064  11.734  38.202  0.64  8.03           N  
ANISOU 2924  NE2AGLN B  61      871    958   1040    -80    305    -21       N  
ATOM   2925  NE2BGLN B  61       0.960  11.632  37.262  0.36 21.49           N  
ANISOU 2925  NE2BGLN B  61     2576   2675   2426   -750   1262    218       N  
ATOM   2926  H   GLN B  61       5.233  12.873  33.478  1.00  9.34           H  
ATOM   2927  HA  GLN B  61       4.436  13.810  35.278  1.00  9.97           H  
ATOM   2928  HB2AGLN B  61       3.498  11.504  35.268  1.00 12.61           H  
ATOM   2929  HB3AGLN B  61       4.354  11.329  36.569  1.00 12.61           H  
ATOM   2930  HG2AGLN B  61       3.176  12.895  37.665  0.64 10.69           H  
ATOM   2931  HG2BGLN B  61       2.247  13.200  35.713  0.36 13.92           H  
ATOM   2932  HG3AGLN B  61       2.500  13.404  36.343  0.64 10.69           H  
ATOM   2933  HG3BGLN B  61       2.475  12.207  34.521  0.36 13.92           H  
ATOM   2934 HE21AGLN B  61       0.408  11.208  38.383  0.64  9.64           H  
ATOM   2935 HE21BGLN B  61       0.392  11.101  37.628  0.36 25.78           H  
ATOM   2936 HE22AGLN B  61       1.328  12.309  38.785  0.64  9.64           H  
ATOM   2937 HE22BGLN B  61       1.207  12.346  37.672  0.36 25.78           H  
ATOM   2938  N   ILE B  62       7.067  13.985  35.929  1.00  6.60           N  
ANISOU 2938  N   ILE B  62      801    854    705    -64    -21    125       N  
ATOM   2939  CA  ILE B  62       8.240  14.432  36.668  1.00  6.51           C  
ANISOU 2939  CA  ILE B  62      796    828    702    -62    -48    162       C  
ATOM   2940  C   ILE B  62       8.028  15.833  37.176  1.00  6.38           C  
ANISOU 2940  C   ILE B  62      743    824    712   -119     28    126       C  
ATOM   2941  O   ILE B  62       7.633  16.730  36.436  1.00  6.57           O  
ANISOU 2941  O   ILE B  62      801    846    701    -18    -18    102       O  
ATOM   2942  CB  ILE B  62       9.491  14.334  35.780  1.00  7.12           C  
ANISOU 2942  CB  ILE B  62      855    932    758    -18    -20    162       C  
ATOM   2943  CG1 ILE B  62       9.765  12.908  35.346  1.00  8.02           C  
ANISOU 2943  CG1 ILE B  62     1006    977    880     34     36    -20       C  
ATOM   2944  CG2 ILE B  62      10.707  14.976  36.447  1.00  8.28           C  
ANISOU 2944  CG2 ILE B  62      797   1088   1073     18    -57     -7       C  
ATOM   2945  CD1 ILE B  62      10.137  11.944  36.458  1.00 10.06           C  
ANISOU 2945  CD1 ILE B  62     1583    993   1020    283      7     63       C  
ATOM   2946  H   ILE B  62       7.035  14.164  35.088  1.00  7.92           H  
ATOM   2947  HA  ILE B  62       8.363  13.839  37.439  1.00  7.81           H  
ATOM   2948  HB  ILE B  62       9.306  14.850  34.967  1.00  8.54           H  
ATOM   2949 HG12 ILE B  62       8.976  12.568  34.898  1.00  9.62           H  
ATOM   2950 HG13 ILE B  62      10.486  12.920  34.697  1.00  9.62           H  
ATOM   2951 HG21 ILE B  62      10.493  15.875  36.706  1.00 12.42           H  
ATOM   2952 HG22 ILE B  62      10.950  14.468  37.225  1.00 12.42           H  
ATOM   2953 HG23 ILE B  62      11.442  14.987  35.830  1.00 12.42           H  
ATOM   2954 HD11 ILE B  62      10.291  11.072  36.087  1.00 15.09           H  
ATOM   2955 HD12 ILE B  62      10.935  12.251  36.894  1.00 15.09           H  
ATOM   2956 HD13 ILE B  62       9.421  11.899  37.095  1.00 15.09           H  
ATOM   2957  N   ILE B  63       8.290  16.037  38.464  1.00  7.20           N  
ANISOU 2957  N   ILE B  63     1081    820    669   -145      7    176       N  
ATOM   2958  CA  ILE B  63       8.223  17.356  39.094  1.00  7.85           C  
ANISOU 2958  CA  ILE B  63     1190    911    706   -197     90     46       C  
ATOM   2959  C   ILE B  63       9.431  18.186  38.633  1.00  7.16           C  
ANISOU 2959  C   ILE B  63      989    874    695   -180   -186     96       C  
ATOM   2960  O   ILE B  63      10.589  17.751  38.738  1.00  8.43           O  
ANISOU 2960  O   ILE B  63     1106    916    990   -117   -220    189       O  
ATOM   2961  CB  ILE B  63       8.174  17.191  40.616  1.00 10.69           C  
ANISOU 2961  CB  ILE B  63     1902   1195    723   -277    101    109       C  
ATOM   2962  CG1 ILE B  63       6.864  16.488  41.060  1.00 12.90           C  
ANISOU 2962  CG1 ILE B  63     1648   2073    887    102    365    467       C  
ATOM   2963  CG2 ILE B  63       8.374  18.513  41.301  1.00 19.53           C  
ANISOU 2963  CG2 ILE B  63     4489   1690    799   -544    328   -358       C  
ATOM   2964  CD1 ILE B  63       6.937  15.982  42.500  1.00 19.37           C  
ANISOU 2964  CD1 ILE B  63     2470   3477    975   -711    127    671       C  
ATOM   2965  H   ILE B  63       8.509  15.362  38.950  1.00  8.63           H  
ATOM   2966  HA  ILE B  63       7.403  17.804  38.800  1.00  9.42           H  
ATOM   2967  HB  ILE B  63       8.921  16.612  40.873  1.00 12.83           H  
ATOM   2968 HG12 ILE B  63       6.125  17.111  40.979  1.00 15.48           H  
ATOM   2969 HG13 ILE B  63       6.689  15.739  40.469  1.00 15.48           H  
ATOM   2970 HG21 ILE B  63       8.340  18.389  42.252  1.00 29.29           H  
ATOM   2971 HG22 ILE B  63       9.228  18.875  41.055  1.00 29.29           H  
ATOM   2972 HG23 ILE B  63       7.680  19.120  41.032  1.00 29.29           H  
ATOM   2973 HD11 ILE B  63       6.108  15.555  42.732  1.00 29.06           H  
ATOM   2974 HD12 ILE B  63       7.655  15.350  42.582  1.00 29.06           H  
ATOM   2975 HD13 ILE B  63       7.092  16.721  43.092  1.00 29.06           H  
ATOM   2976  N   ILE B  64       9.166  19.373  38.137  1.00  7.30           N  
ANISOU 2976  N   ILE B  64      903    924    782   -162   -123    157       N  
ATOM   2977  CA  ILE B  64      10.207  20.250  37.618  1.00  7.50           C  
ANISOU 2977  CA  ILE B  64      885    920    876   -190   -183    222       C  
ATOM   2978  C   ILE B  64       9.789  21.656  37.818  1.00  8.78           C  
ANISOU 2978  C   ILE B  64      822    924   1391    -93   -231    291       C  
ATOM   2979  O   ILE B  64       8.652  22.004  37.557  1.00 15.90           O  
ANISOU 2979  O   ILE B  64      887   1034   3760   -141   -698    403       O  
ATOM   2980  CB  ILE B  64      10.533  19.896  36.132  1.00  8.26           C  
ANISOU 2980  CB  ILE B  64     1042   1125    784   -223   -228    266       C  
ATOM   2981  CG1 ILE B  64      11.635  20.781  35.589  1.00  8.01           C  
ANISOU 2981  CG1 ILE B  64      956    998    908    -67    -45    130       C  
ATOM   2982  CG2 ILE B  64       9.313  19.883  35.232  1.00 12.53           C  
ANISOU 2982  CG2 ILE B  64     1135   2484    858   -656   -259    658       C  
ATOM   2983  CD1 ILE B  64      12.126  20.386  34.212  1.00  9.33           C  
ANISOU 2983  CD1 ILE B  64     1065   1381    888    -40    -87    138       C  
ATOM   2984  H   ILE B  64       8.349  19.641  38.117  1.00  8.76           H  
ATOM   2985  HA  ILE B  64      11.018  20.100  38.147  1.00  9.00           H  
ATOM   2986  HB  ILE B  64      10.886  18.982  36.135  1.00  9.91           H  
ATOM   2987 HG12 ILE B  64      11.312  21.695  35.553  1.00  9.61           H  
ATOM   2988 HG13 ILE B  64      12.384  20.759  36.204  1.00  9.61           H  
ATOM   2989 HG21 ILE B  64       8.642  19.312  35.612  1.00 18.80           H  
ATOM   2990 HG22 ILE B  64       8.967  20.775  35.150  1.00 18.80           H  
ATOM   2991 HG23 ILE B  64       9.559  19.554  34.365  1.00 18.80           H  
ATOM   2992 HD11 ILE B  64      12.821  20.988  33.935  1.00 14.00           H  
ATOM   2993 HD12 ILE B  64      12.472  19.491  34.240  1.00 14.00           H  
ATOM   2994 HD13 ILE B  64      11.398  20.428  33.588  1.00 14.00           H  
ATOM   2995  N   GLU B  65      10.706  22.532  38.265  1.00  6.90           N  
ANISOU 2995  N   GLU B  65      793    972    700    -56   -114     31       N  
ATOM   2996  CA  GLU B  65      10.451  23.953  38.378  1.00  7.35           C  
ANISOU 2996  CA  GLU B  65      864   1097    666     27    -59   -101       C  
ATOM   2997  C   GLU B  65      11.233  24.683  37.303  1.00  6.59           C  
ANISOU 2997  C   GLU B  65      792    814    747    -18    -56   -137       C  
ATOM   2998  O   GLU B  65      12.391  24.349  37.057  1.00  7.54           O  
ANISOU 2998  O   GLU B  65      745    930   1019     23     32     50       O  
ATOM   2999  CB  GLU B  65      10.884  24.438  39.773  1.00 10.70           C  
ANISOU 2999  CB  GLU B  65     1084   2034    704    218   -170   -427       C  
ATOM   3000  CG AGLU B  65      10.296  25.595  40.355  0.63  9.10           C  
ANISOU 3000  CG AGLU B  65     1305   1206    740     31   -174   -170       C  
ATOM   3001  CG BGLU B  65      10.066  24.391  40.850  0.38  8.63           C  
ANISOU 3001  CG BGLU B  65     1158   1191    733    -66    -65   -109       C  
ATOM   3002  CD AGLU B  65      10.704  25.801  41.810  0.63  8.90           C  
ANISOU 3002  CD AGLU B  65     1153   1279    749    156   -153   -114       C  
ATOM   3003  CD BGLU B  65      10.521  24.882  42.233  0.38  7.04           C  
ANISOU 3003  CD BGLU B  65     1089    829    597    202     92   -161       C  
ATOM   3004  OE1AGLU B  65      11.733  26.434  41.988  0.63 12.33           O  
ANISOU 3004  OE1AGLU B  65     1906   1857    641   -653   -265    -26       O  
ATOM   3005  OE1BGLU B  65       9.814  24.512  43.147  0.38 16.33           O  
ANISOU 3005  OE1BGLU B  65     1691   3433    711  -1119     74   -134       O  
ATOM   3006  OE2AGLU B  65      10.008  25.431  42.758  0.63 17.88           O  
ANISOU 3006  OE2AGLU B  65     1811   3673    907   -852   -182    339       O  
ATOM   3007  OE2BGLU B  65      11.515  25.674  42.212  0.38  8.34           O  
ANISOU 3007  OE2BGLU B  65     1178   1226    577      7     47   -268       O  
ATOM   3008  H   GLU B  65      11.479  22.235  38.494  1.00  8.28           H  
ATOM   3009  HA  GLU B  65       9.493  24.123  38.256  1.00  8.82           H  
ATOM   3010  HB2AGLU B  65      10.739  23.703  40.389  1.00 12.84           H  
ATOM   3011  HB3AGLU B  65      11.841  24.590  39.738  1.00 12.84           H  
ATOM   3012  HG2AGLU B  65      10.557  26.375  39.840  0.63 10.92           H  
ATOM   3013  HG2BGLU B  65       9.269  24.894  40.620  0.38 10.35           H  
ATOM   3014  HG3AGLU B  65       9.331  25.518  40.306  0.63 10.92           H  
ATOM   3015  HG3BGLU B  65       9.791  23.467  40.955  0.38 10.35           H  
ATOM   3016  N   ILE B  66      10.589  25.647  36.652  1.00  6.51           N  
ANISOU 3016  N   ILE B  66      777    860    690     30     20   -101       N  
ATOM   3017  CA  ILE B  66      11.179  26.383  35.528  1.00  6.70           C  
ANISOU 3017  CA  ILE B  66      794    828    771     -3     61   -115       C  
ATOM   3018  C   ILE B  66      11.117  27.848  35.878  1.00  6.30           C  
ANISOU 3018  C   ILE B  66      850    838    562     20    -11    -47       C  
ATOM   3019  O   ILE B  66      10.040  28.420  35.957  1.00  6.70           O  
ANISOU 3019  O   ILE B  66      852    938    603    106    -35    -87       O  
ATOM   3020  CB  ILE B  66      10.429  26.098  34.232  1.00  7.70           C  
ANISOU 3020  CB  ILE B  66      959   1064    729   -106     62   -184       C  
ATOM   3021  CG1 ILE B  66      10.392  24.613  33.925  1.00 10.60           C  
ANISOU 3021  CG1 ILE B  66     1705   1180    903   -438    273   -378       C  
ATOM   3022  CG2 ILE B  66      11.032  26.901  33.100  1.00  8.13           C  
ANISOU 3022  CG2 ILE B  66     1105   1089    711    -47     26   -119       C  
ATOM   3023  CD1AILE B  66       9.391  24.064  33.115  0.68  9.41           C  
ANISOU 3023  CD1AILE B  66     1363   1270    727   -286     45   -131       C  
ATOM   3024  CD1BILE B  66      11.442  23.832  33.460  0.32 10.22           C  
ANISOU 3024  CD1BILE B  66     1834   1128    689    -98     68   -178       C  
ATOM   3025  H   ILE B  66       9.790  25.849  36.902  1.00  7.81           H  
ATOM   3026  HA  ILE B  66      12.116  26.116  35.424  1.00  8.04           H  
ATOM   3027  HB  ILE B  66       9.504  26.400  34.351  1.00  9.24           H  
ATOM   3028 HG12AILE B  66      11.243  24.386  33.519  1.00 12.72           H  
ATOM   3029 HG13AILE B  66      10.356  24.148  34.776  1.00 12.72           H  
ATOM   3030 HG21 ILE B  66      11.036  27.832  33.334  1.00 12.19           H  
ATOM   3031 HG22 ILE B  66      11.933  26.607  32.943  1.00 12.19           H  
ATOM   3032 HG23 ILE B  66      10.511  26.774  32.303  1.00 12.19           H  
ATOM   3033 HD11AILE B  66       9.528  23.118  33.033  0.68 14.11           H  
ATOM   3034 HD11BILE B  66      11.143  22.927  33.352  0.32 15.32           H  
ATOM   3035 HD12AILE B  66       8.532  24.230  33.511  0.68 14.11           H  
ATOM   3036 HD12BILE B  66      11.744  24.173  32.615  0.32 15.32           H  
ATOM   3037 HD13AILE B  66       9.425  24.469  32.245  0.68 14.11           H  
ATOM   3038 HD13BILE B  66      12.164  23.858  34.092  0.32 15.32           H  
ATOM   3039  N   ALA B  67      12.268  28.469  36.167  1.00  6.94           N  
ANISOU 3039  N   ALA B  67      846    837    798     36    -49    -99       N  
ATOM   3040  CA  ALA B  67      12.303  29.865  36.553  1.00  8.03           C  
ANISOU 3040  CA  ALA B  67     1048    927    894    -73    -13   -144       C  
ATOM   3041  C   ALA B  67      11.321  30.141  37.707  1.00  7.76           C  
ANISOU 3041  C   ALA B  67     1091    844    836   -118      7   -223       C  
ATOM   3042  O   ALA B  67      10.641  31.154  37.740  1.00  9.30           O  
ANISOU 3042  O   ALA B  67     1365    836   1123     -2    120   -211       O  
ATOM   3043  CB  ALA B  67      12.064  30.789  35.378  1.00 10.35           C  
ANISOU 3043  CB  ALA B  67     1503    912   1282     36    360    149       C  
ATOM   3044  H   ALA B  67      13.005  28.028  36.122  1.00  8.33           H  
ATOM   3045  HA  ALA B  67      13.205  30.050  36.889  1.00  9.64           H  
ATOM   3046  HB1 ALA B  67      12.095  31.701  35.676  1.00 15.52           H  
ATOM   3047  HB2 ALA B  67      12.743  30.645  34.715  1.00 15.52           H  
ATOM   3048  HB3 ALA B  67      11.202  30.606  34.997  1.00 15.52           H  
ATOM   3049  N   GLY B  68      11.269  29.187  38.666  1.00  7.85           N  
ANISOU 3049  N   GLY B  68     1064   1026    713    -66    -57   -163       N  
ATOM   3050  CA  GLY B  68      10.387  29.317  39.807  1.00  9.24           C  
ANISOU 3050  CA  GLY B  68     1309   1311    683   -187    -64   -272       C  
ATOM   3051  C   GLY B  68       8.989  28.853  39.613  1.00  8.91           C  
ANISOU 3051  C   GLY B  68     1197   1366    620    -69     54   -274       C  
ATOM   3052  O   GLY B  68       8.215  28.836  40.603  1.00 12.89           O  
ANISOU 3052  O   GLY B  68     1369   2584    652   -207     99   -310       O  
ATOM   3053  H   GLY B  68      11.769  28.491  38.597  1.00  9.42           H  
ATOM   3054  HA2 GLY B  68      10.771  28.820  40.546  1.00 11.09           H  
ATOM   3055  HA3 GLY B  68      10.363  30.251  40.068  1.00 11.09           H  
ATOM   3056  N   HIS B  69       8.563  28.525  38.413  1.00  7.07           N  
ANISOU 3056  N   HIS B  69      974    942    609    -13     -4   -151       N  
ATOM   3057  CA  HIS B  69       7.201  28.088  38.111  1.00  7.44           C  
ANISOU 3057  CA  HIS B  69      898   1076    685     -7     66   -196       C  
ATOM   3058  C   HIS B  69       7.134  26.573  38.154  1.00  7.34           C  
ANISOU 3058  C   HIS B  69      875   1032    715      9     29   -204       C  
ATOM   3059  O   HIS B  69       7.911  25.877  37.483  1.00  7.97           O  
ANISOU 3059  O   HIS B  69      856   1067    923     75     66   -101       O  
ATOM   3060  CB  HIS B  69       6.771  28.613  36.727  1.00  8.19           C  
ANISOU 3060  CB  HIS B  69      947   1230    749     22    -53    -81       C  
ATOM   3061  CG  HIS B  69       6.577  30.064  36.723  1.00  8.93           C  
ANISOU 3061  CG  HIS B  69     1119   1205    869    162     34    -57       C  
ATOM   3062  ND1 HIS B  69       7.407  31.089  36.898  1.00 12.84           N  
ANISOU 3062  ND1 HIS B  69     1520   1372   1695     27   -139      6       N  
ATOM   3063  CD2 HIS B  69       5.353  30.659  36.518  1.00  9.43           C  
ANISOU 3063  CD2 HIS B  69     1122   1252    997    239     20    -87       C  
ATOM   3064  CE1 HIS B  69       6.719  32.266  36.847  1.00 10.46           C  
ANISOU 3064  CE1 HIS B  69     1600   1076   1060    104    -38     19       C  
ATOM   3065  NE2 HIS B  69       5.494  31.975  36.615  1.00 13.57           N  
ANISOU 3065  NE2 HIS B  69     1890   1486   1474    371     71     22       N  
ATOM   3066  H   HIS B  69       9.123  28.572  37.762  1.00  8.48           H  
ATOM   3067  HA  HIS B  69       6.594  28.451  38.789  1.00  8.93           H  
ATOM   3068  HB2 HIS B  69       7.450  28.380  36.073  1.00  9.83           H  
ATOM   3069  HB3 HIS B  69       5.944  28.179  36.464  1.00  9.83           H  
ATOM   3070  HD1 HIS B  69       8.254  31.019  37.026  1.00 15.40           H  
ATOM   3071  HD2 HIS B  69       4.557  30.212  36.340  1.00 11.32           H  
ATOM   3072  HE1 HIS B  69       7.074  33.118  36.959  1.00 12.55           H  
ATOM   3073  N   LYS B  70       6.223  26.033  38.925  1.00  9.73           N  
ANISOU 3073  N   LYS B  70     1231   1127   1117    -98    442   -311       N  
ATOM   3074  CA  LYS B  70       6.099  24.604  39.126  1.00 10.92           C  
ANISOU 3074  CA  LYS B  70     1537   1236   1129   -251    509   -272       C  
ATOM   3075  C   LYS B  70       5.363  23.952  37.956  1.00 10.39           C  
ANISOU 3075  C   LYS B  70      979   1138   1594   -254    354   -330       C  
ATOM   3076  O   LYS B  70       4.323  24.399  37.518  1.00 17.31           O  
ANISOU 3076  O   LYS B  70     1046   1652   3489    240   -197  -1079       O  
ATOM   3077  CB  LYS B  70       5.414  24.330  40.479  1.00 17.68           C  
ANISOU 3077  CB  LYS B  70     3080   1631   1605   -682   1289   -275       C  
ATOM   3078  CG  LYS B  70       6.194  24.754  41.694  0.86 22.70           C  
ANISOU 3078  CG  LYS B  70     5144   1831   1137   -236    941   -368       C  
ATOM   3079  CD  LYS B  70       5.355  24.510  42.949  0.83 40.63           C  
ANISOU 3079  CD  LYS B  70     8183   4754   1581  -1143   2100    -64       C  
ATOM   3080  CE  LYS B  70       5.353  23.089  43.463  0.81 53.73           C  
ANISOU 3080  CE  LYS B  70    10331   5949   2918  -1135   2342   1804       C  
ATOM   3081  NZ  LYS B  70       4.100  22.424  43.953  0.78 60.59           N  
ANISOU 3081  NZ  LYS B  70    12841   6123   2688  -4000   2893   -976       N  
ATOM   3082  H   LYS B  70       5.671  26.552  39.331  1.00 11.67           H  
ATOM   3083  HA  LYS B  70       7.002  24.225  39.163  1.00 13.10           H  
ATOM   3084  HB2 LYS B  70       4.559  24.788  40.488  1.00 21.21           H  
ATOM   3085  HB3 LYS B  70       5.235  23.379  40.545  1.00 21.21           H  
ATOM   3086  HG2 LYS B  70       7.019  24.248  41.747  0.86 27.24           H  
ATOM   3087  HG3 LYS B  70       6.419  25.695  41.627  0.86 27.24           H  
ATOM   3088  HD2 LYS B  70       5.683  25.090  43.654  0.83 48.76           H  
ATOM   3089  HD3 LYS B  70       4.440  24.769  42.761  0.83 48.76           H  
ATOM   3090  HE2 LYS B  70       5.708  22.533  42.752  0.81 64.47           H  
ATOM   3091  HE3 LYS B  70       5.994  23.052  44.191  0.81 64.47           H  
ATOM   3092  HZ1 LYS B  70       4.287  21.594  44.215  0.78 90.89           H  
ATOM   3093  HZ2 LYS B  70       3.768  22.884  44.638  0.78 90.89           H  
ATOM   3094  HZ3 LYS B  70       3.501  22.399  43.295  0.78 90.89           H  
ATOM   3095  N   ALA B  71       5.889  22.824  37.510  1.00  8.48           N  
ANISOU 3095  N   ALA B  71      937    895   1198   -186    100    -32       N  
ATOM   3096  CA  ALA B  71       5.292  21.985  36.462  1.00  7.99           C  
ANISOU 3096  CA  ALA B  71      828    855   1171   -192     71     36       C  
ATOM   3097  C   ALA B  71       5.443  20.528  36.885  1.00  7.03           C  
ANISOU 3097  C   ALA B  71      676    896    940    -56    124     15       C  
ATOM   3098  O   ALA B  71       6.300  20.180  37.715  1.00  7.68           O  
ANISOU 3098  O   ALA B  71      830    900   1014   -132     41      0       O  
ATOM   3099  CB  ALA B  71       5.942  22.260  35.111  1.00  8.91           C  
ANISOU 3099  CB  ALA B  71     1102    982   1101   -228     46    119       C  
ATOM   3100  H   ALA B  71       6.632  22.563  37.857  1.00 10.18           H  
ATOM   3101  HA  ALA B  71       4.337  22.195  36.398  1.00  9.58           H  
ATOM   3102  HB1 ALA B  71       5.538  21.703  34.442  1.00 13.37           H  
ATOM   3103  HB2 ALA B  71       5.816  23.183  34.877  1.00 13.37           H  
ATOM   3104  HB3 ALA B  71       6.881  22.068  35.162  1.00 13.37           H  
ATOM   3105  N   ILE B  72       4.635  19.666  36.270  1.00  6.44           N  
ANISOU 3105  N   ILE B  72      691    773    839    -68     99     31       N  
ATOM   3106  CA  ILE B  72       4.767  18.222  36.466  1.00  6.11           C  
ANISOU 3106  CA  ILE B  72      699    809    675    -49     85     61       C  
ATOM   3107  C   ILE B  72       4.467  17.612  35.114  1.00  5.75           C  
ANISOU 3107  C   ILE B  72      639    773    644    -53    117    100       C  
ATOM   3108  O   ILE B  72       3.329  17.710  34.624  1.00  6.73           O  
ANISOU 3108  O   ILE B  72      666   1071    668     15     82    110       O  
ATOM   3109  CB  ILE B  72       3.821  17.641  37.529  1.00  6.62           C  
ANISOU 3109  CB  ILE B  72      739    923    702   -102    165    -12       C  
ATOM   3110  CG1 ILE B  72       3.891  18.418  38.838  1.00  7.28           C  
ANISOU 3110  CG1 ILE B  72      817   1133    652   -194    120    -13       C  
ATOM   3111  CG2 ILE B  72       4.153  16.164  37.705  1.00  7.31           C  
ANISOU 3111  CG2 ILE B  72      960    938    714   -106    139     93       C  
ATOM   3112  CD1 ILE B  72       2.888  17.907  39.877  1.00  8.98           C  
ANISOU 3112  CD1 ILE B  72     1088   1385    736   -284    295    -61       C  
ATOM   3113  H   ILE B  72       4.021  19.964  35.747  1.00  7.73           H  
ATOM   3114  HA  ILE B  72       5.693  18.015  36.712  1.00  7.33           H  
ATOM   3115  HB  ILE B  72       2.905  17.706  37.188  1.00  7.94           H  
ATOM   3116 HG12 ILE B  72       4.788  18.349  39.200  1.00  8.74           H  
ATOM   3117 HG13 ILE B  72       3.714  19.355  38.660  1.00  8.74           H  
ATOM   3118 HG21 ILE B  72       4.095  15.720  36.856  1.00 10.96           H  
ATOM   3119 HG22 ILE B  72       5.044  16.076  38.052  1.00 10.96           H  
ATOM   3120 HG23 ILE B  72       3.530  15.767  38.317  1.00 10.96           H  
ATOM   3121 HD11 ILE B  72       2.969  18.424  40.682  1.00 13.47           H  
ATOM   3122 HD12 ILE B  72       1.997  17.991  39.531  1.00 13.47           H  
ATOM   3123 HD13 ILE B  72       3.070  16.984  40.071  1.00 13.47           H  
ATOM   3124  N   GLY B  73       5.456  17.014  34.447  1.00  5.87           N  
ANISOU 3124  N   GLY B  73      650    780    666    -12     26     77       N  
ATOM   3125  CA  GLY B  73       5.184  16.530  33.114  1.00  6.33           C  
ANISOU 3125  CA  GLY B  73      754    843    663     39     31     80       C  
ATOM   3126  C   GLY B  73       6.325  15.694  32.578  1.00  5.83           C  
ANISOU 3126  C   GLY B  73      716    712    654    -65     29    116       C  
ATOM   3127  O   GLY B  73       7.177  15.197  33.314  1.00  6.74           O  
ANISOU 3127  O   GLY B  73      839    894    673    125     -9     87       O  
ATOM   3128  H   GLY B  73       6.234  16.920  34.801  1.00  7.04           H  
ATOM   3129  HA2 GLY B  73       4.374  15.996  33.127  1.00  7.59           H  
ATOM   3130  HA3 GLY B  73       5.034  17.284  32.523  1.00  7.59           H  
ATOM   3131  N   THR B  74       6.304  15.499  31.253  1.00  5.89           N  
ANISOU 3131  N   THR B  74      778    693    631     29     24     78       N  
ATOM   3132  CA  THR B  74       7.212  14.563  30.635  1.00  5.78           C  
ANISOU 3132  CA  THR B  74      859    571    634     14     25    101       C  
ATOM   3133  C   THR B  74       8.588  15.177  30.432  1.00  5.67           C  
ANISOU 3133  C   THR B  74      885    574    567      8     29     70       C  
ATOM   3134  O   THR B  74       8.701  16.290  29.889  1.00  6.56           O  
ANISOU 3134  O   THR B  74      890    644    810    -16    -50    229       O  
ATOM   3135  CB  THR B  74       6.620  14.080  29.317  1.00  6.83           C  
ANISOU 3135  CB  THR B  74      923    786    731   -127     25     42       C  
ATOM   3136  OG1 THR B  74       5.394  13.420  29.610  1.00  8.80           O  
ANISOU 3136  OG1 THR B  74     1000   1218    926   -300     -8   -107       O  
ATOM   3137  CG2 THR B  74       7.559  13.118  28.580  1.00  7.92           C  
ANISOU 3137  CG2 THR B  74     1294    793    743    -32     46    -74       C  
ATOM   3138  H   THR B  74       5.745  15.935  30.767  1.00  7.06           H  
ATOM   3139  HA  THR B  74       7.306  13.790  31.230  1.00  6.93           H  
ATOM   3140  HB  THR B  74       6.439  14.854  28.744  1.00  8.19           H  
ATOM   3141  HG1 THR B  74       5.054  13.153  28.913  1.00 13.20           H  
ATOM   3142 HG21 THR B  74       8.385  13.566  28.384  1.00 11.88           H  
ATOM   3143 HG22 THR B  74       7.733  12.354  29.134  1.00 11.88           H  
ATOM   3144 HG23 THR B  74       7.147  12.833  27.761  1.00 11.88           H  
ATOM   3145  N   VAL B  75       9.618  14.449  30.839  1.00  5.46           N  
ANISOU 3145  N   VAL B  75      784    577    591    -22     45    119       N  
ATOM   3146  CA  VAL B  75      10.995  14.874  30.693  1.00  5.48           C  
ANISOU 3146  CA  VAL B  75      810    535    613     16     32     99       C  
ATOM   3147  C   VAL B  75      11.735  13.751  29.979  1.00  5.35           C  
ANISOU 3147  C   VAL B  75      765    502    644    -24     -7     87       C  
ATOM   3148  O   VAL B  75      11.702  12.594  30.412  1.00  6.29           O  
ANISOU 3148  O   VAL B  75     1005    496    747    -35    136    139       O  
ATOM   3149  CB  VAL B  75      11.636  15.191  32.054  1.00  6.24           C  
ANISOU 3149  CB  VAL B  75      986    633    611    -60     -2     63       C  
ATOM   3150  CG1 VAL B  75      13.110  15.515  31.898  1.00  7.13           C  
ANISOU 3150  CG1 VAL B  75      960    875    714    -44   -123    -18       C  
ATOM   3151  CG2 VAL B  75      10.902  16.347  32.726  1.00  7.08           C  
ANISOU 3151  CG2 VAL B  75     1084    777    668    -35     27    -66       C  
ATOM   3152  H   VAL B  75       9.462  13.688  31.208  1.00  6.55           H  
ATOM   3153  HA  VAL B  75      11.021  15.678  30.134  1.00  6.57           H  
ATOM   3154  HB  VAL B  75      11.553  14.399  32.626  1.00  7.49           H  
ATOM   3155 HG11 VAL B  75      13.556  14.778  31.474  1.00 10.70           H  
ATOM   3156 HG12 VAL B  75      13.209  16.302  31.359  1.00 10.70           H  
ATOM   3157 HG13 VAL B  75      13.497  15.668  32.763  1.00 10.70           H  
ATOM   3158 HG21 VAL B  75       9.972  16.126  32.817  1.00 10.61           H  
ATOM   3159 HG22 VAL B  75      11.279  16.504  33.595  1.00 10.61           H  
ATOM   3160 HG23 VAL B  75      10.992  17.138  32.190  1.00 10.61           H  
ATOM   3161  N   LEU B  76      12.400  14.104  28.880  1.00  5.19           N  
ANISOU 3161  N   LEU B  76      777    442    636    -35     32     72       N  
ATOM   3162  CA  LEU B  76      13.248  13.201  28.142  1.00  5.23           C  
ANISOU 3162  CA  LEU B  76      719    446    705    -34     49     57       C  
ATOM   3163  C   LEU B  76      14.692  13.372  28.614  1.00  5.65           C  
ANISOU 3163  C   LEU B  76      773    475    771    -30     41     84       C  
ATOM   3164  O   LEU B  76      15.103  14.504  28.915  1.00  6.20           O  
ANISOU 3164  O   LEU B  76      795    484    938    -46    -43     66       O  
ATOM   3165  CB  LEU B  76      13.174  13.494  26.647  1.00  5.55           C  
ANISOU 3165  CB  LEU B  76      793    512    678    -72     83     48       C  
ATOM   3166  CG  LEU B  76      11.770  13.626  26.067  1.00  5.92           C  
ANISOU 3166  CG  LEU B  76      899    549    668    -76     16     93       C  
ATOM   3167  CD1 LEU B  76      11.814  13.999  24.595  1.00  6.96           C  
ANISOU 3167  CD1 LEU B  76     1064    713    711   -109     16    109       C  
ATOM   3168  CD2 LEU B  76      10.946  12.378  26.307  1.00  7.10           C  
ANISOU 3168  CD2 LEU B  76      934    775    828   -245    -36    157       C  
ATOM   3169  H   LEU B  76      12.319  14.911  28.596  1.00  6.23           H  
ATOM   3170  HA  LEU B  76      12.961  12.278  28.306  1.00  6.28           H  
ATOM   3171  HB2 LEU B  76      13.655  14.318  26.474  1.00  6.66           H  
ATOM   3172  HB3 LEU B  76      13.635  12.784  26.173  1.00  6.66           H  
ATOM   3173  HG  LEU B  76      11.328  14.362  26.540  1.00  7.11           H  
ATOM   3174 HD11 LEU B  76      12.343  14.792  24.481  1.00 10.44           H  
ATOM   3175 HD12 LEU B  76      12.204  13.279  24.094  1.00 10.44           H  
ATOM   3176 HD13 LEU B  76      10.922  14.161  24.280  1.00 10.44           H  
ATOM   3177 HD21 LEU B  76      10.941  12.174  27.245  1.00 10.65           H  
ATOM   3178 HD22 LEU B  76      10.046  12.527  26.007  1.00 10.65           H  
ATOM   3179 HD23 LEU B  76      11.328  11.644  25.821  1.00 10.65           H  
ATOM   3180  N   VAL B  77      15.439  12.288  28.673  1.00  6.24           N  
ANISOU 3180  N   VAL B  77      750    481    997    -16    -32     62       N  
ATOM   3181  CA  VAL B  77      16.848  12.321  29.105  1.00  6.72           C  
ANISOU 3181  CA  VAL B  77      783    515   1105    -27    -75     68       C  
ATOM   3182  C   VAL B  77      17.684  11.679  28.031  1.00  7.19           C  
ANISOU 3182  C   VAL B  77      822    532   1217     27     15    182       C  
ATOM   3183  O   VAL B  77      17.419  10.548  27.599  1.00  7.95           O  
ANISOU 3183  O   VAL B  77      937    537   1367     17     77     64       O  
ATOM   3184  CB  VAL B  77      17.034  11.611  30.450  1.00  7.81           C  
ANISOU 3184  CB  VAL B  77      925    648   1217    -85   -146    173       C  
ATOM   3185  CG1 VAL B  77      18.512  11.615  30.851  1.00  9.13           C  
ANISOU 3185  CG1 VAL B  77      970    871   1421    -56   -265    203       C  
ATOM   3186  CG2 VAL B  77      16.179  12.235  31.527  1.00  8.69           C  
ANISOU 3186  CG2 VAL B  77     1060    939   1105    -63   -101    233       C  
ATOM   3187  H   VAL B  77      15.091  11.533  28.451  1.00  7.48           H  
ATOM   3188  HA  VAL B  77      17.126  13.256  29.202  1.00  8.07           H  
ATOM   3189  HB  VAL B  77      16.752  10.679  30.341  1.00  9.37           H  
ATOM   3190 HG11 VAL B  77      19.035  11.214  30.152  1.00 13.69           H  
ATOM   3191 HG12 VAL B  77      18.804  12.518  30.991  1.00 13.69           H  
ATOM   3192 HG13 VAL B  77      18.625  11.113  31.662  1.00 13.69           H  
ATOM   3193 HG21 VAL B  77      15.259  12.221  31.254  1.00 13.03           H  
ATOM   3194 HG22 VAL B  77      16.278  11.737  32.342  1.00 13.03           H  
ATOM   3195 HG23 VAL B  77      16.457  13.142  31.671  1.00 13.03           H  
ATOM   3196  N   GLY B  78      18.760  12.352  27.603  1.00  7.92           N  
ANISOU 3196  N   GLY B  78      831    574   1425     61     79    158       N  
ATOM   3197  CA  GLY B  78      19.636  11.769  26.618  1.00  9.31           C  
ANISOU 3197  CA  GLY B  78      963    681   1682     93    258    109       C  
ATOM   3198  C   GLY B  78      20.686  12.750  26.167  1.00  8.84           C  
ANISOU 3198  C   GLY B  78      725    628   1807     79    137     29       C  
ATOM   3199  O   GLY B  78      20.884  13.783  26.803  1.00  9.54           O  
ANISOU 3199  O   GLY B  78      888    798   1723     32     61     38       O  
ATOM   3200  H   GLY B  78      18.929  13.134  27.918  1.00  9.50           H  
ATOM   3201  HA2 GLY B  78      20.068  10.986  26.994  1.00 11.17           H  
ATOM   3202  HA3 GLY B  78      19.113  11.484  25.852  1.00 11.17           H  
ATOM   3203  N  APRO B  79      21.425  12.380  25.157  0.56 10.18           N  
ANISOU 3203  N  APRO B  79      965    699   1974     97    433     85       N  
ATOM   3204  N  BPRO B  79      21.329  12.497  24.996  0.44  8.60           N  
ANISOU 3204  N  BPRO B  79      609    516   1948    212    175     41       N  
ATOM   3205  CA APRO B  79      22.640  13.150  24.851  0.56  8.89           C  
ANISOU 3205  CA APRO B  79      611    878   1689    246     90    178       C  
ATOM   3206  CA BPRO B  79      22.457  13.241  24.389  0.44  9.07           C  
ANISOU 3206  CA BPRO B  79      717    715   1811    175    128     -6       C  
ATOM   3207  C  APRO B  79      22.313  14.438  24.091  0.56  7.31           C  
ANISOU 3207  C  APRO B  79      596    773   1244     27    191     36       C  
ATOM   3208  C  BPRO B  79      22.116  14.524  23.599  0.44  8.12           C  
ANISOU 3208  C  BPRO B  79      677    906   1319    137    165     47       C  
ATOM   3209  O  APRO B  79      22.787  14.701  22.970  0.56  7.85           O  
ANISOU 3209  O  APRO B  79      763    686   1355     67    351    -10       O  
ATOM   3210  O  BPRO B  79      22.557  14.745  22.473  0.44 10.57           O  
ANISOU 3210  O  BPRO B  79     1053   1643   1080    375    179   -166       O  
ATOM   3211  CB APRO B  79      23.431  12.123  24.049  0.56  9.47           C  
ANISOU 3211  CB APRO B  79      693    938   1752    319    191    227       C  
ATOM   3212  CB BPRO B  79      23.156  12.247  23.444  0.44  9.93           C  
ANISOU 3212  CB BPRO B  79     1007    917   1626    154    235    -46       C  
ATOM   3213  CG APRO B  79      22.372  11.278  23.331  0.56 10.13           C  
ANISOU 3213  CG APRO B  79      723    815   2081    183    421     27       C  
ATOM   3214  CG BPRO B  79      22.013  11.400  22.980  0.44 12.48           C  
ANISOU 3214  CG BPRO B  79      795   1073   2592    115    441   -639       C  
ATOM   3215  CD APRO B  79      21.296  11.135  24.378  0.56  9.56           C  
ANISOU 3215  CD APRO B  79      752    793   1869    251    305     90       C  
ATOM   3216  CD BPRO B  79      21.099  11.269  24.180  0.44 11.05           C  
ANISOU 3216  CD BPRO B  79      960    624   2365    183    312   -190       C  
ATOM   3217  HA APRO B  79      23.117  13.364  25.681  0.56 10.67           H  
ATOM   3218  HA BPRO B  79      23.085  13.479  25.102  0.44 10.89           H  
ATOM   3219  HB2APRO B  79      24.013  12.561  23.409  0.56 11.36           H  
ATOM   3220  HB2BPRO B  79      23.580  12.705  22.701  0.44 11.92           H  
ATOM   3221  HB3APRO B  79      23.971  11.570  24.636  0.56 11.36           H  
ATOM   3222  HB3BPRO B  79      23.819  11.719  23.914  0.44 11.92           H  
ATOM   3223  HG2APRO B  79      22.037  11.732  22.542  0.56 12.15           H  
ATOM   3224  HG2BPRO B  79      21.549  11.825  22.242  0.44 14.98           H  
ATOM   3225  HG3APRO B  79      22.729  10.413  23.073  0.56 12.15           H  
ATOM   3226  HG3BPRO B  79      22.327  10.529  22.692  0.44 14.98           H  
ATOM   3227  HD2APRO B  79      20.418  11.067  23.971  0.56 11.47           H  
ATOM   3228  HD2BPRO B  79      20.172  11.214  23.899  0.44 13.26           H  
ATOM   3229  HD3APRO B  79      21.449  10.356  24.934  0.56 11.47           H  
ATOM   3230  HD3BPRO B  79      21.318  10.473  24.690  0.44 13.26           H  
ATOM   3231  N  ATHR B  80      21.476  15.277  24.704  0.56  6.23           N  
ANISOU 3231  N  ATHR B  80      607    645    973     67    183     96       N  
ATOM   3232  N  BTHR B  80      21.402  15.397  24.296  0.44  7.87           N  
ANISOU 3232  N  BTHR B  80     1230    765    817    233    139     60       N  
ATOM   3233  CA ATHR B  80      21.207  16.569  24.122  0.56  5.70           C  
ANISOU 3233  CA ATHR B  80      559    645    832     16    162    -33       C  
ATOM   3234  CA BTHR B  80      21.147  16.745  23.878  0.44  7.08           C  
ANISOU 3234  CA BTHR B  80      903    830    795    216      9    162       C  
ATOM   3235  C  ATHR B  80      22.380  17.511  24.346  0.56  6.32           C  
ANISOU 3235  C  ATHR B  80      722    606    929     22    152    -41       C  
ATOM   3236  C  BTHR B  80      22.337  17.644  24.144  0.44  7.44           C  
ANISOU 3236  C  BTHR B  80      784    976    900    221     39    153       C  
ATOM   3237  O  ATHR B  80      23.011  17.474  25.398  0.56  6.66           O  
ANISOU 3237  O  ATHR B  80      690    719    971      0     50     23       O  
ATOM   3238  O  BTHR B  80      23.078  17.460  25.121  0.44  9.77           O  
ANISOU 3238  O  BTHR B  80      903   1621    970    326   -138    161       O  
ATOM   3239  CB ATHR B  80      19.879  17.151  24.706  0.56  6.19           C  
ANISOU 3239  CB ATHR B  80      698    717    796    188    135     84       C  
ATOM   3240  CB BTHR B  80      19.917  17.304  24.663  0.44  6.55           C  
ANISOU 3240  CB BTHR B  80      813    621    907    -96     29   -123       C  
ATOM   3241  OG1ATHR B  80      19.714  18.439  24.123  0.56  5.42           O  
ANISOU 3241  OG1ATHR B  80      669    603    665     47    115    -45       O  
ATOM   3242  OG1BTHR B  80      19.664  18.594  24.136  0.44  7.59           O  
ANISOU 3242  OG1BTHR B  80     1193    822    698    331   -162    -98       O  
ATOM   3243  CG2ATHR B  80      19.839  17.226  26.235  0.56  6.09           C  
ANISOU 3243  CG2ATHR B  80      517    893    765     29    197    191       C  
ATOM   3244  CG2BTHR B  80      20.158  17.331  26.166  0.44  6.06           C  
ANISOU 3244  CG2BTHR B  80      622    681    861    -53    204    181       C  
ATOM   3245  H  ATHR B  80      21.099  15.048  25.442  0.56  7.47           H  
ATOM   3246  H  BTHR B  80      21.071  15.138  25.046  0.44  9.44           H  
ATOM   3247  HA ATHR B  80      21.090  16.451  23.157  0.56  6.84           H  
ATOM   3248  HA BTHR B  80      20.947  16.752  22.919  0.44  8.49           H  
ATOM   3249  HB ATHR B  80      19.139  16.583  24.408  0.56  7.43           H  
ATOM   3250  HB BTHR B  80      19.141  16.734  24.479  0.44  7.86           H  
ATOM   3251  HG1ATHR B  80      19.637  19.000  24.716  0.56  8.13           H  
ATOM   3252  HG1BTHR B  80      19.767  19.155  24.726  0.44 11.39           H  
ATOM   3253 HG21ATHR B  80      19.952  16.346  26.601  0.56  9.13           H  
ATOM   3254 HG21BTHR B  80      20.324  16.439  26.479  0.44  9.08           H  
ATOM   3255 HG22ATHR B  80      20.545  17.796  26.546  0.56  9.13           H  
ATOM   3256 HG22BTHR B  80      20.918  17.884  26.359  0.44  9.08           H  
ATOM   3257 HG23ATHR B  80      18.992  17.582  26.515  0.56  9.13           H  
ATOM   3258 HG23BTHR B  80      19.383  17.686  26.608  0.44  9.08           H  
ATOM   3259  N  APRO B  81      22.739  18.424  23.432  0.56  6.87           N  
ANISOU 3259  N  APRO B  81      795    676    985    -30    129     75       N  
ATOM   3260  N  BPRO B  81      22.535  18.611  23.275  0.44  6.50           N  
ANISOU 3260  N  BPRO B  81      590   1053    678    133    153     59       N  
ATOM   3261  CA APRO B  81      23.842  19.344  23.714  0.56  7.14           C  
ANISOU 3261  CA APRO B  81      549    881   1119     19    135    164       C  
ATOM   3262  CA BPRO B  81      23.663  19.525  23.421  0.44  7.42           C  
ANISOU 3262  CA BPRO B  81      626   1296    730     59    115    110       C  
ATOM   3263  C  APRO B  81      23.563  20.378  24.792  0.56  6.93           C  
ANISOU 3263  C  APRO B  81      648    751   1078     56    -58    182       C  
ATOM   3264  C  BPRO B  81      23.509  20.502  24.595  0.44  7.13           C  
ANISOU 3264  C  BPRO B  81      621   1207    719    -25     44    143       C  
ATOM   3265  O  APRO B  81      24.489  20.912  25.412  0.56  8.62           O  
ANISOU 3265  O  APRO B  81      725   1137   1218    -79   -120     46       O  
ATOM   3266  O  BPRO B  81      24.535  21.032  25.049  0.44  8.15           O  
ANISOU 3266  O  BPRO B  81      633   1440    839   -181     62    160       O  
ATOM   3267  CB APRO B  81      24.073  20.043  22.349  0.56  7.31           C  
ANISOU 3267  CB APRO B  81      650    748   1212    125    212    207       C  
ATOM   3268  CB BPRO B  81      23.668  20.313  22.106  0.44  8.75           C  
ANISOU 3268  CB BPRO B  81      912   1464    752    142    366    312       C  
ATOM   3269  CG APRO B  81      23.459  19.119  21.308  0.56  8.11           C  
ANISOU 3269  CG APRO B  81      744   1163    992     55    354     48       C  
ATOM   3270  CG BPRO B  81      22.284  20.158  21.557  0.44 10.39           C  
ANISOU 3270  CG BPRO B  81     1292   1599    821    -82    -74    307       C  
ATOM   3271  CD APRO B  81      22.262  18.520  22.040  0.56  7.64           C  
ANISOU 3271  CD APRO B  81      616   1110   1004     -1    167    166       C  
ATOM   3272  CD BPRO B  81      21.788  18.811  22.009  0.44  8.40           C  
ANISOU 3272  CD BPRO B  81     1142   1419    440    -23     14    -15       C  
ATOM   3273  HA APRO B  81      24.640  18.831  23.955  0.56  8.56           H  
ATOM   3274  HA BPRO B  81      24.497  19.019  23.512  0.44  8.91           H  
ATOM   3275  HB2APRO B  81      23.641  20.911  22.332  0.56  8.77           H  
ATOM   3276  HB2BPRO B  81      23.871  21.248  22.267  0.44 10.51           H  
ATOM   3277  HB3APRO B  81      25.021  20.163  22.183  0.56  8.77           H  
ATOM   3278  HB3BPRO B  81      24.324  19.951  21.491  0.44 10.51           H  
ATOM   3279  HG2APRO B  81      23.177  19.615  20.523  0.56  9.74           H  
ATOM   3280  HG2BPRO B  81      21.706  20.860  21.894  0.44 12.47           H  
ATOM   3281  HG3APRO B  81      24.086  18.429  21.039  0.56  9.74           H  
ATOM   3282  HG3BPRO B  81      22.297  20.205  20.589  0.44 12.47           H  
ATOM   3283  HD2APRO B  81      21.486  19.099  21.976  0.56  9.17           H  
ATOM   3284  HD2BPRO B  81      20.830  18.821  22.162  0.44 10.08           H  
ATOM   3285  HD3APRO B  81      22.036  17.646  21.686  0.56  9.17           H  
ATOM   3286  HD3BPRO B  81      22.001  18.122  21.361  0.44 10.08           H  
ATOM   3287  N  AVAL B  82      22.309  20.754  25.032  0.56  7.59           N  
ANISOU 3287  N  AVAL B  82      621   1368    723     29    -50   -100       N  
ATOM   3288  N  BVAL B  82      22.261  20.715  24.973  0.44  5.39           N  
ANISOU 3288  N  BVAL B  82      609    525    794     94     -1    188       N  
ATOM   3289  CA AVAL B  82      21.968  21.677  26.109  0.56  6.55           C  
ANISOU 3289  CA AVAL B  82      688    961    690     -9    -81    111       C  
ATOM   3290  CA BVAL B  82      21.749  21.760  25.841  0.44  6.46           C  
ANISOU 3290  CA BVAL B  82      863    536    910    -76     57     87       C  
ATOM   3291  C  AVAL B  82      20.662  21.158  26.672  0.56  5.50           C  
ANISOU 3291  C  AVAL B  82      622    607    736     93    -64    -23       C  
ATOM   3292  C  BVAL B  82      20.522  21.292  26.590  0.44  5.38           C  
ANISOU 3292  C  BVAL B  82      649    523    751     68    -28    112       C  
ATOM   3293  O  AVAL B  82      19.918  20.420  26.028  0.56  5.72           O  
ANISOU 3293  O  AVAL B  82      687    624    733    115     26    -86       O  
ATOM   3294  O  BVAL B  82      19.690  20.656  25.941  0.44  6.10           O  
ANISOU 3294  O  BVAL B  82      618    768    795    159    -61   -161       O  
ATOM   3295  CB AVAL B  82      21.901  23.141  25.704  0.56  9.12           C  
ANISOU 3295  CB AVAL B  82     1137   1073   1050   -194   -107    272       C  
ATOM   3296  CB BVAL B  82      21.441  23.060  25.041  0.44  8.64           C  
ANISOU 3296  CB BVAL B  82     1277    515   1295    198    648    232       C  
ATOM   3297  CG1AVAL B  82      20.718  23.355  24.704  0.56  9.59           C  
ANISOU 3297  CG1AVAL B  82     1223    761   1443     11   -150    415       C  
ATOM   3298  CG1BVAL B  82      20.792  24.146  25.863  0.44  8.77           C  
ANISOU 3298  CG1BVAL B  82     1675    672    788    217    224    -11       C  
ATOM   3299  CG2AVAL B  82      21.752  24.102  26.844  0.56 21.61           C  
ANISOU 3299  CG2AVAL B  82     3824   1560   2340   -119   -598   -704       C  
ATOM   3300  CG2BVAL B  82      22.810  23.532  24.525  0.44 15.80           C  
ANISOU 3300  CG2BVAL B  82     1816    610   3222    -88   1422    545       C  
ATOM   3301  H  AVAL B  82      21.680  20.442  24.536  0.56  9.11           H  
ATOM   3302  H  BVAL B  82      21.677  20.163  24.665  0.44  6.47           H  
ATOM   3303  HA AVAL B  82      22.651  21.590  26.806  0.56  7.86           H  
ATOM   3304  HA BVAL B  82      22.442  21.970  26.500  0.44  7.75           H  
ATOM   3305  HB AVAL B  82      22.732  23.359  25.234  0.56 10.95           H  
ATOM   3306  HB BVAL B  82      20.864  22.843  24.278  0.44 10.37           H  
ATOM   3307 HG11AVAL B  82      20.804  22.743  23.970  0.56 14.39           H  
ATOM   3308 HG11BVAL B  82      20.632  24.914  25.309  0.44 13.16           H  
ATOM   3309 HG12AVAL B  82      19.885  23.198  25.155  0.56 14.39           H  
ATOM   3310 HG12BVAL B  82      19.959  23.826  26.215  0.44 13.16           H  
ATOM   3311 HG13AVAL B  82      20.737  24.256  24.373  0.56 14.39           H  
ATOM   3312 HG13BVAL B  82      21.374  24.390  26.587  0.44 13.16           H  
ATOM   3313 HG21AVAL B  82      21.718  24.999  26.503  0.56 32.42           H  
ATOM   3314 HG21BVAL B  82      23.214  22.835  24.004  0.44 23.71           H  
ATOM   3315 HG22AVAL B  82      20.942  23.910  27.321  0.56 32.42           H  
ATOM   3316 HG22BVAL B  82      22.695  24.314  23.979  0.44 23.71           H  
ATOM   3317 HG23AVAL B  82      22.502  24.014  27.437  0.56 32.42           H  
ATOM   3318 HG23BVAL B  82      23.377  23.744  25.270  0.44 23.71           H  
ATOM   3319  N   ASN B  83      20.327  21.605  27.879  1.00  5.58           N  
ANISOU 3319  N   ASN B  83      687    604    702      1    -68     -8       N  
ATOM   3320  CA  ASN B  83      19.030  21.309  28.462  1.00  5.03           C  
ANISOU 3320  CA  ASN B  83      654    557    585     18    -92    -19       C  
ATOM   3321  C   ASN B  83      17.970  22.201  27.812  1.00  4.85           C  
ANISOU 3321  C   ASN B  83      721    496    515     53    -49    -43       C  
ATOM   3322  O   ASN B  83      18.154  23.412  27.761  1.00  6.15           O  
ANISOU 3322  O   ASN B  83      900    501    796      7   -249    -48       O  
ATOM   3323  CB  ASN B  83      19.049  21.567  29.958  1.00  5.82           C  
ANISOU 3323  CB  ASN B  83      796    675    607     60   -147    -36       C  
ATOM   3324  CG  ASN B  83      20.007  20.656  30.709  1.00  6.06           C  
ANISOU 3324  CG  ASN B  83      810    677    679     34   -117     75       C  
ATOM   3325  OD1 ASN B  83      20.134  19.481  30.377  1.00  7.79           O  
ANISOU 3325  OD1 ASN B  83     1049    644   1090     76   -312     52       O  
ATOM   3326  ND2 ASN B  83      20.612  21.179  31.759  1.00  7.74           N  
ANISOU 3326  ND2 ASN B  83     1230    903    631    242   -309    -15       N  
ATOM   3327  H  AASN B  83      20.890  22.079  28.324  1.00  6.69           H  
ATOM   3328  HA  ASN B  83      18.808  20.369  28.297  1.00  6.03           H  
ATOM   3329  HB2 ASN B  83      19.303  22.489  30.116  1.00  6.98           H  
ATOM   3330  HB3 ASN B  83      18.154  21.441  30.310  1.00  6.98           H  
ATOM   3331 HD21 ASN B  83      21.124  20.690  32.247  1.00  9.28           H  
ATOM   3332 HD22 ASN B  83      20.494  22.008  31.955  1.00  9.28           H  
ATOM   3333  N   ILE B  84      16.906  21.587  27.315  1.00  4.59           N  
ANISOU 3333  N   ILE B  84      561    492    586      6    -43     32       N  
ATOM   3334  CA  ILE B  84      15.885  22.258  26.514  1.00  4.82           C  
ANISOU 3334  CA  ILE B  84      608    495    620    -24    -34     99       C  
ATOM   3335  C   ILE B  84      14.521  22.108  27.167  1.00  4.55           C  
ANISOU 3335  C   ILE B  84      622    475    528    -27    -62     12       C  
ATOM   3336  O   ILE B  84      14.066  20.979  27.389  1.00  5.07           O  
ANISOU 3336  O   ILE B  84      669    442    702    -26     68     18       O  
ATOM   3337  CB  ILE B  84      15.868  21.641  25.099  1.00  5.55           C  
ANISOU 3337  CB  ILE B  84      673    764    545     92     -7    155       C  
ATOM   3338  CG1 ILE B  84      17.140  21.949  24.339  1.00  8.87           C  
ANISOU 3338  CG1 ILE B  84      803   1691    674    182    135    507       C  
ATOM   3339  CG2 ILE B  84      14.613  22.062  24.322  1.00  6.88           C  
ANISOU 3339  CG2 ILE B  84      814   1021    624    206   -102     68       C  
ATOM   3340  CD1 ILE B  84      17.395  21.121  23.124  1.00 12.10           C  
ANISOU 3340  CD1 ILE B  84     1098   2602    624    592    229    405       C  
ATOM   3341  H   ILE B  84      16.811  20.747  27.472  1.00  5.51           H  
ATOM   3342  HA  ILE B  84      16.106  23.210  26.447  1.00  5.79           H  
ATOM   3343  HB  ILE B  84      15.826  20.668  25.209  1.00  6.66           H  
ATOM   3344 HG12 ILE B  84      17.117  22.881  24.072  1.00 10.64           H  
ATOM   3345 HG13 ILE B  84      17.890  21.840  24.945  1.00 10.64           H  
ATOM   3346 HG21 ILE B  84      13.831  21.850  24.837  1.00 10.32           H  
ATOM   3347 HG22 ILE B  84      14.641  23.008  24.158  1.00 10.32           H  
ATOM   3348 HG23 ILE B  84      14.582  21.593  23.485  1.00 10.32           H  
ATOM   3349 HD11 ILE B  84      18.221  21.394  22.719  1.00 18.15           H  
ATOM   3350 HD12 ILE B  84      17.452  20.196  23.374  1.00 18.15           H  
ATOM   3351 HD13 ILE B  84      16.677  21.240  22.499  1.00 18.15           H  
ATOM   3352  N   ILE B  85      13.891  23.235  27.448  1.00  4.40           N  
ANISOU 3352  N   ILE B  85      547    468    556    -59    -51     -1       N  
ATOM   3353  CA  ILE B  85      12.507  23.273  27.932  1.00  4.41           C  
ANISOU 3353  CA  ILE B  85      613    510    452     -5    -12    -27       C  
ATOM   3354  C   ILE B  85      11.624  23.575  26.722  1.00  4.22           C  
ANISOU 3354  C   ILE B  85      581    490    437    -40     32    -37       C  
ATOM   3355  O   ILE B  85      11.664  24.670  26.166  1.00  5.02           O  
ANISOU 3355  O   ILE B  85      705    564    524    -86    -47     86       O  
ATOM   3356  CB  ILE B  85      12.294  24.337  29.023  1.00  5.13           C  
ANISOU 3356  CB  ILE B  85      803    584    445      6    -38    -85       C  
ATOM   3357  CG1 ILE B  85      13.327  24.194  30.154  1.00  6.64           C  
ANISOU 3357  CG1 ILE B  85     1092    737    544     24   -218   -177       C  
ATOM   3358  CG2 ILE B  85      10.853  24.278  29.513  1.00  6.17           C  
ANISOU 3358  CG2 ILE B  85      871    849    484     31    127    -89       C  
ATOM   3359  CD1 ILE B  85      13.409  22.816  30.769  1.00  8.71           C  
ANISOU 3359  CD1 ILE B  85     1627    867    618     88   -542    -88       C  
ATOM   3360  H   ILE B  85      14.310  23.978  27.342  1.00  5.27           H  
ATOM   3361  HA  ILE B  85      12.268  22.393  28.291  1.00  5.29           H  
ATOM   3362  HB  ILE B  85      12.429  25.215  28.609  1.00  6.15           H  
ATOM   3363 HG12 ILE B  85      14.201  24.429  29.805  1.00  7.97           H  
ATOM   3364 HG13 ILE B  85      13.110  24.831  30.853  1.00  7.97           H  
ATOM   3365 HG21 ILE B  85      10.257  24.373  28.766  1.00  9.25           H  
ATOM   3366 HG22 ILE B  85      10.695  23.435  29.943  1.00  9.25           H  
ATOM   3367 HG23 ILE B  85      10.698  24.991  30.137  1.00  9.25           H  
ATOM   3368 HD11 ILE B  85      14.074  22.814  31.462  1.00 13.07           H  
ATOM   3369 HD12 ILE B  85      12.556  22.581  31.142  1.00 13.07           H  
ATOM   3370 HD13 ILE B  85      13.649  22.178  30.093  1.00 13.07           H  
ATOM   3371  N   GLY B  86      10.851  22.582  26.306  1.00  4.51           N  
ANISOU 3371  N   GLY B  86      672    482    457    -51    -54     11       N  
ATOM   3372  CA  GLY B  86      10.007  22.694  25.142  1.00  4.73           C  
ANISOU 3372  CA  GLY B  86      693    593    404    -58    -47     11       C  
ATOM   3373  C   GLY B  86       8.575  22.945  25.472  1.00  4.58           C  
ANISOU 3373  C   GLY B  86      691    505    439    -51    -57     11       C  
ATOM   3374  O   GLY B  86       8.167  23.206  26.621  1.00  5.10           O  
ANISOU 3374  O   GLY B  86      706    699    417    -38    -24     23       O  
ATOM   3375  H   GLY B  86      10.853  21.844  26.747  1.00  5.41           H  
ATOM   3376  HA2 GLY B  86      10.334  23.418  24.585  1.00  5.68           H  
ATOM   3377  HA3 GLY B  86      10.072  21.874  24.627  1.00  5.68           H  
ATOM   3378  N   ARG B  87       7.730  22.874  24.425  1.00  4.80           N  
ANISOU 3378  N   ARG B  87      676    616    425    -33    -52      5       N  
ATOM   3379  CA  ARG B  87       6.371  23.371  24.539  1.00  4.99           C  
ANISOU 3379  CA  ARG B  87      721    623    439    -28    -87     76       C  
ATOM   3380  C   ARG B  87       5.527  22.609  25.545  1.00  5.19           C  
ANISOU 3380  C   ARG B  87      658    714    483    -38    -80     73       C  
ATOM   3381  O   ARG B  87       4.610  23.197  26.129  1.00  5.78           O  
ANISOU 3381  O   ARG B  87      712    784    569    -12    -18    102       O  
ATOM   3382  CB  ARG B  87       5.671  23.388  23.168  1.00  5.17           C  
ANISOU 3382  CB  ARG B  87      670    713    465    -48    -89     63       C  
ATOM   3383  CG  ARG B  87       6.300  24.384  22.196  1.00  5.57           C  
ANISOU 3383  CG  ARG B  87      759    751    479    -17    -93    108       C  
ATOM   3384  CD  ARG B  87       5.502  24.522  20.895  1.00  5.74           C  
ANISOU 3384  CD  ARG B  87      734    827    492    -42    -93    133       C  
ATOM   3385  NE  ARG B  87       5.478  23.279  20.125  1.00  6.19           N  
ANISOU 3385  NE  ARG B  87      787    955    469    -71    -62     38       N  
ATOM   3386  CZ  ARG B  87       4.543  22.366  20.164  1.00  6.51           C  
ANISOU 3386  CZ  ARG B  87      866    920    541    -37   -167     71       C  
ATOM   3387  NH1 ARG B  87       3.406  22.515  20.838  1.00  7.05           N  
ANISOU 3387  NH1 ARG B  87      807   1004    707   -111   -104    -17       N  
ATOM   3388  NH2 ARG B  87       4.714  21.224  19.477  1.00  7.64           N  
ANISOU 3388  NH2 ARG B  87     1079    930    719    -30    -85    -67       N  
ATOM   3389  H   ARG B  87       7.998  22.532  23.683  1.00  5.76           H  
ATOM   3390  HA  ARG B  87       6.425  24.299  24.849  1.00  5.99           H  
ATOM   3391  HB2 ARG B  87       5.711  22.500  22.781  1.00  6.21           H  
ATOM   3392  HB3 ARG B  87       4.736  23.615  23.292  1.00  6.21           H  
ATOM   3393  HG2 ARG B  87       6.359  25.252  22.625  1.00  6.68           H  
ATOM   3394  HG3 ARG B  87       7.202  24.095  21.985  1.00  6.68           H  
ATOM   3395  HD2 ARG B  87       4.592  24.784  21.106  1.00  6.89           H  
ATOM   3396  HD3 ARG B  87       5.895  25.224  20.353  1.00  6.89           H  
ATOM   3397  HE  ARG B  87       6.141  23.135  19.597  1.00  7.43           H  
ATOM   3398 HH11 ARG B  87       3.258  23.239  21.277  1.00  8.45           H  
ATOM   3399 HH12 ARG B  87       2.819  21.886  20.836  1.00  8.45           H  
ATOM   3400 HH21 ARG B  87       5.432  21.101  19.019  1.00  9.17           H  
ATOM   3401 HH22 ARG B  87       4.106  20.616  19.495  1.00  9.17           H  
ATOM   3402  N   ASN B  88       5.800  21.325  25.752  1.00  5.39           N  
ANISOU 3402  N   ASN B  88      696    691    539    -98    -45     70       N  
ATOM   3403  CA  ASN B  88       5.000  20.579  26.710  1.00  5.73           C  
ANISOU 3403  CA  ASN B  88      709    760    581   -134    -98    110       C  
ATOM   3404  C   ASN B  88       5.048  21.238  28.109  1.00  5.76           C  
ANISOU 3404  C   ASN B  88      696    798    566    -64     26    151       C  
ATOM   3405  O   ASN B  88       4.055  21.169  28.838  1.00  7.37           O  
ANISOU 3405  O   ASN B  88      767   1193    675   -196     43    104       O  
ATOM   3406  CB  ASN B  88       5.426  19.114  26.785  1.00  6.18           C  
ANISOU 3406  CB  ASN B  88      804    735    670   -180    -77    147       C  
ATOM   3407  CG  ASN B  88       6.760  18.900  27.453  1.00  6.08           C  
ANISOU 3407  CG  ASN B  88      780    674    717    -43    -25    106       C  
ATOM   3408  OD1 ASN B  88       7.775  19.516  27.063  1.00  6.43           O  
ANISOU 3408  OD1 ASN B  88      750    828    720    -83    -50     92       O  
ATOM   3409  ND2 ASN B  88       6.767  18.045  28.466  1.00  6.76           N  
ANISOU 3409  ND2 ASN B  88      842    787    787     29    -83    189       N  
ATOM   3410  H   ASN B  88       6.439  20.940  25.325  1.00  6.47           H  
ATOM   3411  HA  ASN B  88       4.070  20.603  26.403  1.00  6.88           H  
ATOM   3412  HB2 ASN B  88       4.750  18.616  27.272  1.00  7.42           H  
ATOM   3413  HB3 ASN B  88       5.467  18.754  25.886  1.00  7.42           H  
ATOM   3414 HD21 ASN B  88       7.498  17.888  28.891  1.00  8.11           H  
ATOM   3415 HD22 ASN B  88       6.042  17.645  28.696  1.00  8.11           H  
ATOM   3416  N   LEU B  89       6.176  21.811  28.490  1.00  5.26           N  
ANISOU 3416  N   LEU B  89      678    714    489    -51    -15    105       N  
ATOM   3417  CA  LEU B  89       6.297  22.488  29.775  1.00  5.77           C  
ANISOU 3417  CA  LEU B  89      798    777    486     -4     14    109       C  
ATOM   3418  C   LEU B  89       6.118  24.000  29.676  1.00  5.70           C  
ANISOU 3418  C   LEU B  89      709    841    488    -26    -53     68       C  
ATOM   3419  O   LEU B  89       5.634  24.619  30.625  1.00  6.51           O  
ANISOU 3419  O   LEU B  89      949    865    513     54     50     26       O  
ATOM   3420  CB  LEU B  89       7.607  22.124  30.487  1.00  6.20           C  
ANISOU 3420  CB  LEU B  89      793    941    480      6    -57    113       C  
ATOM   3421  CG  LEU B  89       7.779  20.639  30.764  1.00  7.13           C  
ANISOU 3421  CG  LEU B  89      965   1033    552    184     -5    143       C  
ATOM   3422  CD1 LEU B  89       9.093  20.433  31.521  1.00  8.68           C  
ANISOU 3422  CD1 LEU B  89     1153   1382    566    416    -82    120       C  
ATOM   3423  CD2 LEU B  89       6.629  20.012  31.524  1.00  9.36           C  
ANISOU 3423  CD2 LEU B  89     1275   1145    927    163    197    451       C  
ATOM   3424  H   LEU B  89       6.858  21.783  27.965  1.00  6.32           H  
ATOM   3425  HA  LEU B  89       5.568  22.155  30.339  1.00  6.92           H  
ATOM   3426  HB2 LEU B  89       8.350  22.426  29.942  1.00  7.44           H  
ATOM   3427  HB3 LEU B  89       7.646  22.603  31.329  1.00  7.44           H  
ATOM   3428  HG  LEU B  89       7.854  20.179  29.901  1.00  8.56           H  
ATOM   3429 HD11 LEU B  89       9.813  20.835  31.028  1.00 13.02           H  
ATOM   3430 HD12 LEU B  89       9.031  20.843  32.387  1.00 13.02           H  
ATOM   3431 HD13 LEU B  89       9.261  19.494  31.623  1.00 13.02           H  
ATOM   3432 HD21 LEU B  89       6.807  19.079  31.661  1.00 14.05           H  
ATOM   3433 HD22 LEU B  89       6.533  20.448  32.374  1.00 14.05           H  
ATOM   3434 HD23 LEU B  89       5.819  20.113  31.019  1.00 14.05           H  
ATOM   3435  N   LEU B  90       6.470  24.606  28.540  1.00  5.58           N  
ANISOU 3435  N   LEU B  90      777    746    472    -34     10     20       N  
ATOM   3436  CA  LEU B  90       6.188  26.029  28.373  1.00  5.56           C  
ANISOU 3436  CA  LEU B  90      775    693    517    -13     -8    -26       C  
ATOM   3437  C   LEU B  90       4.706  26.298  28.512  1.00  6.02           C  
ANISOU 3437  C   LEU B  90      851    735    563    -51     84     45       C  
ATOM   3438  O   LEU B  90       4.303  27.332  29.072  1.00  6.86           O  
ANISOU 3438  O   LEU B  90      937    784    731     58    119     -1       O  
ATOM   3439  CB  LEU B  90       6.728  26.532  27.029  1.00  5.49           C  
ANISOU 3439  CB  LEU B  90      752    652    556    -30     14      8       C  
ATOM   3440  CG  LEU B  90       8.269  26.506  26.878  1.00  5.87           C  
ANISOU 3440  CG  LEU B  90      690    740    667    -82      5     69       C  
ATOM   3441  CD1 LEU B  90       8.681  26.813  25.452  1.00  6.70           C  
ANISOU 3441  CD1 LEU B  90      766    939    690    -43     41    108       C  
ATOM   3442  CD2 LEU B  90       8.957  27.435  27.827  1.00  7.92           C  
ANISOU 3442  CD2 LEU B  90      929   1028    873   -259    -42    -44       C  
ATOM   3443  H   LEU B  90       6.859  24.164  27.913  1.00  6.70           H  
ATOM   3444  HA  LEU B  90       6.652  26.515  29.087  1.00  6.67           H  
ATOM   3445  HB2 LEU B  90       6.342  25.992  26.322  1.00  6.58           H  
ATOM   3446  HB3 LEU B  90       6.423  27.444  26.898  1.00  6.58           H  
ATOM   3447  HG  LEU B  90       8.570  25.597  27.083  1.00  7.04           H  
ATOM   3448 HD11 LEU B  90       8.233  26.212  24.852  1.00 10.05           H  
ATOM   3449 HD12 LEU B  90       8.440  27.717  25.236  1.00 10.05           H  
ATOM   3450 HD13 LEU B  90       9.631  26.705  25.363  1.00 10.05           H  
ATOM   3451 HD21 LEU B  90       8.688  27.231  28.726  1.00 11.88           H  
ATOM   3452 HD22 LEU B  90       9.908  27.329  27.746  1.00 11.88           H  
ATOM   3453 HD23 LEU B  90       8.717  28.341  27.619  1.00 11.88           H  
ATOM   3454  N   THR B  91       3.853  25.407  27.999  1.00  6.19           N  
ANISOU 3454  N   THR B  91      765    798    648    -42     50     69       N  
ATOM   3455  CA  THR B  91       2.429  25.597  28.157  1.00  6.79           C  
ANISOU 3455  CA  THR B  91      768    895    764     29     65    179       C  
ATOM   3456  C   THR B  91       2.004  25.481  29.622  1.00  7.54           C  
ANISOU 3456  C   THR B  91      805   1032    857    -17    148    176       C  
ATOM   3457  O   THR B  91       1.125  26.220  30.064  1.00  9.51           O  
ANISOU 3457  O   THR B  91      988   1379   1030    281    255    219       O  
ATOM   3458  CB  THR B  91       1.623  24.622  27.290  1.00  7.52           C  
ANISOU 3458  CB  THR B  91      773   1069    847    -83    -27    216       C  
ATOM   3459  OG1 THR B  91       1.990  23.283  27.617  1.00  8.97           O  
ANISOU 3459  OG1 THR B  91      963   1013   1231   -173   -140    290       O  
ATOM   3460  CG2 THR B  91       1.785  24.901  25.797  1.00  8.18           C  
ANISOU 3460  CG2 THR B  91      912   1191    819    -65    -70    170       C  
ATOM   3461  H   THR B  91       4.151  24.721  27.576  1.00  7.42           H  
ATOM   3462  HA  THR B  91       2.216  26.505  27.857  1.00  8.15           H  
ATOM   3463  HB  THR B  91       0.676  24.735  27.515  1.00  9.03           H  
ATOM   3464  HG1 THR B  91       1.552  22.760  27.163  1.00 13.46           H  
ATOM   3465 HG21 THR B  91       1.530  25.807  25.612  1.00 12.27           H  
ATOM   3466 HG22 THR B  91       2.701  24.768  25.544  1.00 12.27           H  
ATOM   3467 HG23 THR B  91       1.225  24.302  25.297  1.00 12.27           H  
ATOM   3468  N   GLN B  92       2.626  24.600  30.405  1.00  7.39           N  
ANISOU 3468  N   GLN B  92      891    995    755     15    159    185       N  
ATOM   3469  CA  GLN B  92       2.299  24.506  31.823  1.00  8.51           C  
ANISOU 3469  CA  GLN B  92     1156   1096    789     -3    319    229       C  
ATOM   3470  C   GLN B  92       2.611  25.761  32.592  1.00 10.11           C  
ANISOU 3470  C   GLN B  92     1634   1152    828    122    452    153       C  
ATOM   3471  O   GLN B  92       1.912  26.021  33.596  1.00 16.01           O  
ANISOU 3471  O   GLN B  92     2630   1617   1476   -108   1332   -129       O  
ATOM   3472  CB  GLN B  92       2.991  23.313  32.497  1.00  7.90           C  
ANISOU 3472  CB  GLN B  92     1010   1149    663   -132    110    209       C  
ATOM   3473  CG  GLN B  92       2.434  21.972  32.061  1.00  7.59           C  
ANISOU 3473  CG  GLN B  92      856   1068    787   -147    -14    292       C  
ATOM   3474  CD  GLN B  92       2.763  20.831  33.034  1.00  7.03           C  
ANISOU 3474  CD  GLN B  92      638   1246    627   -154     46    238       C  
ATOM   3475  OE1 GLN B  92       2.994  21.086  34.235  1.00  8.06           O  
ANISOU 3475  OE1 GLN B  92      908   1196    777   -135     26    259       O  
ATOM   3476  NE2 GLN B  92       2.725  19.621  32.553  1.00  7.87           N  
ANISOU 3476  NE2 GLN B  92      944   1100    769    -75     80    246       N  
ATOM   3477  H   GLN B  92       3.226  24.082  30.071  1.00  8.87           H  
ATOM   3478  HA  GLN B  92       1.332  24.357  31.890  1.00 10.21           H  
ATOM   3479  HB2 GLN B  92       3.939  23.342  32.292  1.00  9.48           H  
ATOM   3480  HB3 GLN B  92       2.894  23.395  33.459  1.00  9.48           H  
ATOM   3481  HG2 GLN B  92       1.471  22.045  31.975  1.00  9.10           H  
ATOM   3482  HG3 GLN B  92       2.793  21.753  31.187  1.00  9.10           H  
ATOM   3483 HE21 GLN B  92       2.864  18.948  33.071  1.00  9.45           H  
ATOM   3484 HE22 GLN B  92       2.561  19.494  31.719  1.00  9.45           H  
ATOM   3485  N   ILE B  93       3.622  26.503  32.207  1.00  8.57           N  
ANISOU 3485  N   ILE B  93     1363   1067    633     52    193    154       N  
ATOM   3486  CA  ILE B  93       3.952  27.717  32.905  1.00  9.82           C  
ANISOU 3486  CA  ILE B  93     1805   1071    634    115    254     -4       C  
ATOM   3487  C   ILE B  93       3.332  28.931  32.314  1.00  9.52           C  
ANISOU 3487  C   ILE B  93     1474   1036    891    184    444     22       C  
ATOM   3488  O   ILE B  93       3.574  30.057  32.746  1.00 11.84           O  
ANISOU 3488  O   ILE B  93     1846   1080   1305    115    528   -178       O  
ATOM   3489  CB  ILE B  93       5.504  27.869  33.069  1.00 10.57           C  
ANISOU 3489  CB  ILE B  93     1822   1256    697    125   -133   -259       C  
ATOM   3490  CG1 ILE B  93       6.188  28.259  31.777  1.00 10.16           C  
ANISOU 3490  CG1 ILE B  93     1387   1426    816    122   -114   -278       C  
ATOM   3491  CG2 ILE B  93       6.075  26.648  33.753  1.00 12.54           C  
ANISOU 3491  CG2 ILE B  93     2266   1331    884    271   -416   -233       C  
ATOM   3492  CD1 ILE B  93       7.663  28.516  31.906  1.00 13.55           C  
ANISOU 3492  CD1 ILE B  93     1411   1927   1502     82   -238   -628       C  
ATOM   3493  H   ILE B  93       4.093  26.260  31.529  1.00 10.29           H  
ATOM   3494  HA  ILE B  93       3.584  27.627  33.809  1.00 11.79           H  
ATOM   3495  HB  ILE B  93       5.640  28.617  33.687  1.00 12.68           H  
ATOM   3496 HG12 ILE B  93       6.052  27.551  31.128  1.00 12.19           H  
ATOM   3497 HG13 ILE B  93       5.763  29.060  31.431  1.00 12.19           H  
ATOM   3498 HG21 ILE B  93       5.583  26.474  34.559  1.00 18.81           H  
ATOM   3499 HG22 ILE B  93       6.006  25.891  33.167  1.00 18.81           H  
ATOM   3500 HG23 ILE B  93       6.997  26.804  33.968  1.00 18.81           H  
ATOM   3501 HD11 ILE B  93       8.021  28.757  31.049  1.00 20.32           H  
ATOM   3502 HD12 ILE B  93       7.810  29.233  32.527  1.00 20.32           H  
ATOM   3503 HD13 ILE B  93       8.099  27.723  32.224  1.00 20.32           H  
ATOM   3504  N   GLY B  94       2.462  28.749  31.300  1.00  9.40           N  
ANISOU 3504  N   GLY B  94     1380   1006    972    205    409    143       N  
ATOM   3505  CA  GLY B  94       1.689  29.849  30.747  1.00 10.49           C  
ANISOU 3505  CA  GLY B  94     1339   1131   1280    246    501    210       C  
ATOM   3506  C   GLY B  94       2.454  30.725  29.772  1.00  8.76           C  
ANISOU 3506  C   GLY B  94     1140    980   1011    239    264    189       C  
ATOM   3507  O   GLY B  94       2.109  31.898  29.615  1.00 11.04           O  
ANISOU 3507  O   GLY B  94     1386   1066   1493    386    534    261       O  
ATOM   3508  H   GLY B  94       2.361  27.961  30.972  1.00 11.28           H  
ATOM   3509  HA2 GLY B  94       0.912  29.486  30.294  1.00 12.59           H  
ATOM   3510  HA3 GLY B  94       1.371  30.403  31.477  1.00 12.59           H  
ATOM   3511  N   ALA B  95       3.494  30.198  29.123  1.00  7.76           N  
ANISOU 3511  N   ALA B  95     1104    766    901    138    178    123       N  
ATOM   3512  CA  ALA B  95       4.316  31.017  28.239  1.00  7.35           C  
ANISOU 3512  CA  ALA B  95     1043    781    803     92    152     55       C  
ATOM   3513  C   ALA B  95       3.670  31.200  26.872  1.00  7.34           C  
ANISOU 3513  C   ALA B  95     1010    778    833     36    141     18       C  
ATOM   3514  O   ALA B  95       3.122  30.279  26.285  1.00  8.84           O  
ANISOU 3514  O   ALA B  95     1327    892    940    -94     53     33       O  
ATOM   3515  CB  ALA B  95       5.677  30.393  28.087  1.00  8.27           C  
ANISOU 3515  CB  ALA B  95     1111    939    906     75    161    105       C  
ATOM   3516  H   ALA B  95       3.682  29.365  29.227  1.00  9.31           H  
ATOM   3517  HA  ALA B  95       4.426  31.900  28.650  1.00  8.82           H  
ATOM   3518  HB1 ALA B  95       6.214  30.935  27.505  1.00 12.41           H  
ATOM   3519  HB2 ALA B  95       6.099  30.331  28.947  1.00 12.41           H  
ATOM   3520  HB3 ALA B  95       5.585  29.514  27.712  1.00 12.41           H  
ATOM   3521  N   THR B  96       3.808  32.431  26.354  1.00  6.98           N  
ANISOU 3521  N   THR B  96      930    769    796     24     93     53       N  
ATOM   3522  CA  THR B  96       3.393  32.790  25.020  1.00  7.36           C  
ANISOU 3522  CA  THR B  96      908    893    828    124    151    105       C  
ATOM   3523  C   THR B  96       4.526  33.585  24.356  1.00  7.06           C  
ANISOU 3523  C   THR B  96      976    668    879    105    174     40       C  
ATOM   3524  O   THR B  96       5.355  34.200  24.992  1.00  8.10           O  
ANISOU 3524  O   THR B  96     1139    961    794   -133    156    -68       O  
ATOM   3525  CB  THR B  96       2.091  33.647  25.027  1.00  8.82           C  
ANISOU 3525  CB  THR B  96     1045   1164    944    286    259    146       C  
ATOM   3526  OG1 THR B  96       2.277  34.790  25.781  1.00  9.66           O  
ANISOU 3526  OG1 THR B  96     1210   1060   1182    259    420    206       O  
ATOM   3527  CG2 THR B  96       0.924  32.869  25.566  1.00 10.43           C  
ANISOU 3527  CG2 THR B  96     1061   1478   1189    185    279     94       C  
ATOM   3528  H   THR B  96       4.164  33.040  26.846  1.00  8.38           H  
ATOM   3529  HA  THR B  96       3.234  31.972  24.505  1.00  8.83           H  
ATOM   3530  HB  THR B  96       1.889  33.912  24.105  1.00 10.59           H  
ATOM   3531  HG1 THR B  96       2.906  35.219  25.476  1.00 14.49           H  
ATOM   3532 HG21 THR B  96       0.797  32.076  25.040  1.00 15.65           H  
ATOM   3533 HG22 THR B  96       1.096  32.624  26.478  1.00 15.65           H  
ATOM   3534 HG23 THR B  96       0.132  33.410  25.524  1.00 15.65           H  
ATOM   3535  N   LEU B  97       4.468  33.586  23.006  1.00  6.98           N  
ANISOU 3535  N   LEU B  97      939    768    787     14    127     20       N  
ATOM   3536  CA  LEU B  97       5.255  34.518  22.214  1.00  7.25           C  
ANISOU 3536  CA  LEU B  97      942    819    830     11    165      2       C  
ATOM   3537  C   LEU B  97       4.420  35.737  21.878  1.00  7.62           C  
ANISOU 3537  C   LEU B  97      881    872    971     26     51    131       C  
ATOM   3538  O   LEU B  97       3.200  35.641  21.604  1.00  9.93           O  
ANISOU 3538  O   LEU B  97     1073   1023   1453    -83   -245    230       O  
ATOM   3539  CB  LEU B  97       5.668  33.874  20.872  1.00  8.64           C  
ANISOU 3539  CB  LEU B  97     1151   1041    896     92    187     -4       C  
ATOM   3540  CG ALEU B  97       6.763  32.930  20.983  0.79  7.45           C  
ANISOU 3540  CG ALEU B  97     1135    866    663    140     43    142       C  
ATOM   3541  CG BLEU B  97       7.108  34.265  20.357  0.21  8.55           C  
ANISOU 3541  CG BLEU B  97     1289   1076    691     99    247    227       C  
ATOM   3542  CD1ALEU B  97       6.870  32.057  19.716  0.79  8.99           C  
ANISOU 3542  CD1ALEU B  97     1440   1076    695    292     62     32       C  
ATOM   3543  CD1BLEU B  97       8.281  34.292  21.294  0.21  8.85           C  
ANISOU 3543  CD1BLEU B  97     1109    654   1400    554    112   -223       C  
ATOM   3544  CD2ALEU B  97       8.080  33.586  21.231  0.79  9.04           C  
ANISOU 3544  CD2ALEU B  97     1185    820   1226    345    107    -79       C  
ATOM   3545  CD2BLEU B  97       7.391  33.332  19.158  0.21 11.44           C  
ANISOU 3545  CD2BLEU B  97     1385   1707    996    414    254   -108       C  
ATOM   3546  H   LEU B  97       3.954  33.023  22.607  1.00  8.38           H  
ATOM   3547  HA  LEU B  97       6.054  34.788  22.714  1.00  8.70           H  
ATOM   3548  HB2ALEU B  97       4.899  33.418  20.496  1.00 10.37           H  
ATOM   3549  HB3ALEU B  97       5.924  34.577  20.255  1.00 10.37           H  
ATOM   3550  HG ALEU B  97       6.574  32.338  21.741  0.79  8.95           H  
ATOM   3551  HG BLEU B  97       7.031  35.170  19.988  0.21 10.26           H  
ATOM   3552 HD11ALEU B  97       7.601  31.441  19.813  0.79 13.48           H  
ATOM   3553 HD11BLEU B  97       8.088  34.876  22.031  0.21 13.28           H  
ATOM   3554 HD12ALEU B  97       6.053  31.568  19.594  0.79 13.48           H  
ATOM   3555 HD12BLEU B  97       8.449  33.406  21.622  0.21 13.28           H  
ATOM   3556 HD13ALEU B  97       7.025  32.618  18.953  0.79 13.48           H  
ATOM   3557 HD13BLEU B  97       9.056  34.613  20.826  0.21 13.28           H  
ATOM   3558 HD21ALEU B  97       8.765  32.915  21.295  0.79 13.56           H  
ATOM   3559 HD21BLEU B  97       6.632  33.326  18.570  0.21 17.16           H  
ATOM   3560 HD22ALEU B  97       8.283  34.181  20.506  0.79 13.56           H  
ATOM   3561 HD22BLEU B  97       8.163  33.648  18.681  0.21 17.16           H  
ATOM   3562 HD23ALEU B  97       8.041  34.082  22.051  0.79 13.56           H  
ATOM   3563 HD23BLEU B  97       7.556  32.441  19.477  0.21 17.16           H  
ATOM   3564  N   ASN B  98       5.017  36.921  21.922  1.00  7.40           N  
ANISOU 3564  N   ASN B  98      850    811    983     72    141     59       N  
ATOM   3565  CA  ASN B  98       4.303  38.156  21.757  1.00  7.46           C  
ANISOU 3565  CA  ASN B  98      793    881    994     41     43    160       C  
ATOM   3566  C   ASN B  98       5.113  39.106  20.902  1.00  8.10           C  
ANISOU 3566  C   ASN B  98      859    937   1097     44     67    151       C  
ATOM   3567  O   ASN B  98       6.303  39.290  21.166  1.00  8.39           O  
ANISOU 3567  O   ASN B  98      809   1029   1160     92    110    281       O  
ATOM   3568  CB  ASN B  98       3.986  38.821  23.086  1.00  8.19           C  
ANISOU 3568  CB  ASN B  98      938    813   1176     79    151    107       C  
ATOM   3569  CG  ASN B  98       3.108  37.960  23.942  1.00  7.90           C  
ANISOU 3569  CG  ASN B  98      961    884    979     70    131     23       C  
ATOM   3570  OD1 ASN B  98       1.870  38.231  23.988  1.00 11.57           O  
ANISOU 3570  OD1 ASN B  98     1045   1423   1664    109    306    138       O  
ATOM   3571  ND2 ASN B  98       3.625  37.021  24.581  1.00  8.13           N  
ANISOU 3571  ND2 ASN B  98      991    921    994    -17    241    117       N  
ATOM   3572  H   ASN B  98       5.866  36.951  22.055  1.00  8.88           H  
ATOM   3573  HA  ASN B  98       3.460  37.967  21.296  1.00  8.96           H  
ATOM   3574  HB2 ASN B  98       4.813  39.004  23.558  1.00  9.83           H  
ATOM   3575  HB3 ASN B  98       3.542  39.668  22.922  1.00  9.83           H  
ATOM   3576 HD21 ASN B  98       3.136  36.522  25.083  1.00  9.76           H  
ATOM   3577 HD22 ASN B  98       4.470  36.873  24.521  1.00  9.76           H  
ATOM   3578  N   PHE B  99       4.469  39.743  19.926  1.00  9.33           N  
ANISOU 3578  N   PHE B  99      878   1197   1260     24     -6    467       N  
ATOM   3579  CA  PHE B  99       5.076  40.780  19.126  1.00  9.48           C  
ANISOU 3579  CA  PHE B  99      939   1027   1421     64     72    397       C  
ATOM   3580  C   PHE B  99       3.991  41.646  18.503  1.00 11.72           C  
ANISOU 3580  C   PHE B  99     1074   1436   1678    231     88    712       C  
ATOM   3581  O   PHE B  99       4.298  42.552  17.750  1.00 15.56           O  
ANISOU 3581  O   PHE B  99     1323   1868   2367    288    156   1224       O  
ATOM   3582  CB  PHE B  99       6.047  40.250  18.064  1.00  9.70           C  
ANISOU 3582  CB  PHE B  99     1035   1243   1187     78     30    453       C  
ATOM   3583  CG  PHE B  99       5.520  39.270  17.048  1.00 10.78           C  
ANISOU 3583  CG  PHE B  99     1256   1230   1367     11    118    386       C  
ATOM   3584  CD1 PHE B  99       5.431  37.921  17.369  1.00 12.66           C  
ANISOU 3584  CD1 PHE B  99     1707   1271   1545    137    280    273       C  
ATOM   3585  CD2 PHE B  99       5.176  39.679  15.784  1.00 13.85           C  
ANISOU 3585  CD2 PHE B  99     1813   1670   1465     45   -366    440       C  
ATOM   3586  CE1 PHE B  99       4.975  37.022  16.433  1.00 14.55           C  
ANISOU 3586  CE1 PHE B  99     1856   1305   2036     48    259    100       C  
ATOM   3587  CE2 PHE B  99       4.710  38.784  14.868  1.00 17.15           C  
ANISOU 3587  CE2 PHE B  99     2368   1856   1903   -199   -669    282       C  
ATOM   3588  CZ  PHE B  99       4.596  37.451  15.193  1.00 17.33           C  
ANISOU 3588  CZ  PHE B  99     2439   1772   1980   -264   -334     38       C  
ATOM   3589  OXT PHE B  99       2.795  41.423  18.782  1.00 15.68           O  
ANISOU 3589  OXT PHE B  99     1089   2087   2427    195    -54   1105       O  
ATOM   3590  H   PHE B  99       3.652  39.526  19.764  1.00 11.20           H  
ATOM   3591  HA  PHE B  99       5.592  41.351  19.732  1.00 11.38           H  
ATOM   3592  HB2 PHE B  99       6.405  41.012  17.582  1.00 11.64           H  
ATOM   3593  HB3 PHE B  99       6.789  39.828  18.525  1.00 11.64           H  
ATOM   3594  HD1 PHE B  99       5.678  37.627  18.216  1.00 15.19           H  
ATOM   3595  HD2 PHE B  99       5.261  40.575  15.550  1.00 16.61           H  
ATOM   3596  HE1 PHE B  99       4.925  36.118  16.645  1.00 17.45           H  
ATOM   3597  HE2 PHE B  99       4.467  39.075  14.019  1.00 20.58           H  
ATOM   3598  HZ  PHE B  99       4.262  36.846  14.571  1.00 20.79           H  
TER    3599      PHE B  99                                                      
HETATM 3600  C1 A8Z0 A 101      24.705  23.336  19.796  0.49  7.42           C  
ANISOU 3600  C1 A8Z0 A 101      456   1104   1093    181     36    275       C  
HETATM 3601  C1 B8Z0 A 101      12.072  17.230  12.864  0.52  9.00           C  
ANISOU 3601  C1 B8Z0 A 101     1471   1126    618     80     -9   -376       C  
HETATM 3602  C2 A8Z0 A 101      25.574  23.284  20.846  0.49  9.16           C  
ANISOU 3602  C2 A8Z0 A 101      782   1220   1269    309    -64    399       C  
HETATM 3603  C2 B8Z0 A 101      11.330  17.013  11.714  0.52  8.69           C  
ANISOU 3603  C2 B8Z0 A 101     1470   1047    589   -252    -32   -161       C  
HETATM 3604  C3 A8Z0 A 101      25.718  24.366  21.809  0.49 10.52           C  
ANISOU 3604  C3 A8Z0 A 101     1078   1650   1033    523   -204    251       C  
HETATM 3605  C3 B8Z0 A 101      10.064  17.570  11.586  0.52 10.84           C  
ANISOU 3605  C3 B8Z0 A 101     1612   1634    627   -327   -244   -306       C  
HETATM 3606  C4 A8Z0 A 101      24.977  25.510  21.722  0.49 10.77           C  
ANISOU 3606  C4 A8Z0 A 101     1255   1246   1346    248   -520     64       C  
HETATM 3607  C4 B8Z0 A 101       9.491  18.255  12.561  0.52  9.47           C  
ANISOU 3607  C4 B8Z0 A 101     1584    912    890     27   -315   -219       C  
HETATM 3608  C5 A8Z0 A 101      24.002  25.569  20.684  0.49  8.12           C  
ANISOU 3608  C5 A8Z0 A 101      814   1002   1087    145   -265    167       C  
HETATM 3609  C5 B8Z0 A 101      10.092  18.356  13.874  0.52  7.97           C  
ANISOU 3609  C5 B8Z0 A 101     1254    876    719   -184   -176   -247       C  
HETATM 3610  C6 A8Z0 A 101      23.904  24.502  19.731  0.49  7.21           C  
ANISOU 3610  C6 A8Z0 A 101      715    847   1015    101    -68    249       C  
HETATM 3611  C6 B8Z0 A 101      11.401  17.856  13.929  0.52  7.33           C  
ANISOU 3611  C6 B8Z0 A 101     1186    823    611   -135     29   -178       C  
HETATM 3612  C7 A8Z0 A 101      25.249  21.263  18.784  0.49  9.42           C  
ANISOU 3612  C7 A8Z0 A 101     1015   1022   1331    481    376    637       C  
HETATM 3613  C7 B8Z0 A 101      13.823  15.878  12.039  0.52 12.13           C  
ANISOU 3613  C7 B8Z0 A 101     2332    852   1152    250   1138    240       C  
HETATM 3614  C8 A8Z0 A 101      23.057  26.566  20.191  0.49  7.46           C  
ANISOU 3614  C8 A8Z0 A 101      904    825    936    109   -303     16       C  
HETATM 3615  C8 B8Z0 A 101       9.877  18.964  15.139  0.52  8.14           C  
ANISOU 3615  C8 B8Z0 A 101     1003   1089    815    -32    -80   -280       C  
HETATM 3616  C9 A8Z0 A 101      22.470  26.017  19.117  0.49  6.20           C  
ANISOU 3616  C9 A8Z0 A 101      752    571    894     79   -211     68       C  
HETATM 3617  C9 B8Z0 A 101      11.001  18.769  15.870  0.52  6.62           C  
ANISOU 3617  C9 B8Z0 A 101      904    823    639    -41     -6   -192       C  
HETATM 3618  C10A8Z0 A 101      21.383  26.500  18.230  0.49  4.76           C  
ANISOU 3618  C10A8Z0 A 101      578    525    598     48    -21     52       C  
HETATM 3619  C10B8Z0 A 101      11.371  19.227  17.240  0.52  5.70           C  
ANISOU 3619  C10B8Z0 A 101      872    580    584    -53     49    -74       C  
HETATM 3620  O1 A8Z0 A 101      24.397  22.367  18.806  0.49  8.44           O  
ANISOU 3620  O1 A8Z0 A 101      889    917   1210    393     40    240       O  
HETATM 3621  O1 B8Z0 A 101      13.333  16.695  13.155  0.52  8.22           O  
ANISOU 3621  O1 B8Z0 A 101     1274   1016    647     -3    148   -243       O  
HETATM 3622  O3 A8Z0 A 101      20.863  27.607  18.418  0.49  5.30           O  
ANISOU 3622  O3 A8Z0 A 101      764    486    644     90     14      4       O  
HETATM 3623  O3 B8Z0 A 101      10.601  19.830  17.972  0.52  6.25           O  
ANISOU 3623  O3 B8Z0 A 101      797    673    765     96     44      0       O  
HETATM 3624  O7 A8Z0 A 101      22.959  24.745  18.807  0.49  6.06           O  
ANISOU 3624  O7 A8Z0 A 101      667    666    834    162    -65    117       O  
HETATM 3625  O7 B8Z0 A 101      11.979  18.073  15.164  0.52  6.89           O  
ANISOU 3625  O7 B8Z0 A 101     1069    784    609    -89     50   -233       O  
HETATM 3626  C11A8Z0 A 101      19.869  25.881  16.404  0.49  4.21           C  
ANISOU 3626  C11A8Z0 A 101      573    390    542     38     42     64       C  
HETATM 3627  C11B8Z0 A 101      13.211  19.419  18.827  0.52  5.11           C  
ANISOU 3627  C11B8Z0 A 101      736    555    535    -95     29    -35       C  
HETATM 3628  N2 A8Z0 A 101      21.041  25.649  17.256  0.49  4.56           N  
ANISOU 3628  N2 A8Z0 A 101      564    498    568     47     42     15       N  
HETATM 3629  N2 B8Z0 A 101      12.620  18.915  17.577  0.52  5.26           N  
ANISOU 3629  N2 B8Z0 A 101      787    554    538    -54    102   -127       N  
HETATM 3630  C12A8Z0 A 101      20.254  25.952  14.944  0.49  4.30           C  
ANISOU 3630  C12A8Z0 A 101      610    389    536    -17    148    -45       C  
HETATM 3631  C12B8Z0 A 101      13.608  18.290  19.770  0.52  5.21           C  
ANISOU 3631  C12B8Z0 A 101      771    485    604     10    169     -8       C  
HETATM 3632  C13A8Z0 A 101      19.016  26.224  14.055  0.49  4.59           C  
ANISOU 3632  C13A8Z0 A 101      705    518    417    -49     79      6       C  
HETATM 3633  C13B8Z0 A 101      14.244  18.855  21.050  0.52  5.46           C  
ANISOU 3633  C13B8Z0 A 101      783    610    560     64    101      2       C  
HETATM 3634  C15A8Z0 A 101      21.105  27.219  14.715  0.49  5.02           C  
ANISOU 3634  C15A8Z0 A 101      665    519    610    -74    119     90       C  
HETATM 3635  C15B8Z0 A 101      12.375  17.588  20.258  0.52  6.01           C  
ANISOU 3635  C15B8Z0 A 101      910    528    709    -58    216     81       C  
HETATM 3636  C16A8Z0 A 101      18.841  24.772  16.758  0.49  4.11           C  
ANISOU 3636  C16A8Z0 A 101      580    451    436     67     66     -2       C  
HETATM 3637  C16B8Z0 A 101      14.369  20.363  18.399  0.52  4.92           C  
ANISOU 3637  C16B8Z0 A 101      745    484    530    -42    109    -46       C  
HETATM 3638  C14A8Z0 A 101      19.275  27.636  13.522  0.49  4.81           C  
ANISOU 3638  C14A8Z0 A 101      817    496    406     77     77    -36       C  
HETATM 3639  C14B8Z0 A 101      13.232  18.471  22.144  0.52  5.80           C  
ANISOU 3639  C14B8Z0 A 101      879    614    580    214     56    122       C  
HETATM 3640  O  A8Z0 A 101      18.705  23.780  16.040  0.49  5.10           O  
ANISOU 3640  O  A8Z0 A 101      782    491    548    -77    195    -85       O  
HETATM 3641  O  B8Z0 A 101      15.540  19.977  18.393  0.52  5.60           O  
ANISOU 3641  O  B8Z0 A 101      698    501    801     -1     93     34       O  
HETATM 3642  O8 A8Z0 A 101      20.154  28.234  14.444  0.49  5.04           O  
ANISOU 3642  O8 A8Z0 A 101      745    502    554    -45     40     18       O  
HETATM 3643  O8 B8Z0 A 101      12.005  18.313  21.451  0.52  6.02           O  
ANISOU 3643  O8 B8Z0 A 101      781    733    637    -13    118     72       O  
HETATM 3644  C26A8Z0 A 101      14.743  23.451  17.990  0.49  4.29           C  
ANISOU 3644  C26A8Z0 A 101      625    552    356     10      0    -66       C  
HETATM 3645  C26B8Z0 A 101      16.446  24.351  18.535  0.52  4.66           C  
ANISOU 3645  C26B8Z0 A 101      631    466    568     83     -7      7       C  
HETATM 3646  N3 A8Z0 A 101      18.166  24.974  17.874  0.49  4.09           N  
ANISOU 3646  N3 A8Z0 A 101      644    448    370      8     42     29       N  
HETATM 3647  N3 B8Z0 A 101      13.964  21.579  18.022  0.52  4.78           N  
ANISOU 3647  N3 B8Z0 A 101      702    497    508      6      9     17       N  
HETATM 3648  O4 A8Z0 A 101      14.151  23.110  19.038  0.49  4.76           O  
ANISOU 3648  O4 A8Z0 A 101      718    546    438   -117    136    -64       O  
HETATM 3649  O4 B8Z0 A 101      16.510  25.391  17.846  0.52  5.16           O  
ANISOU 3649  O4 B8Z0 A 101      701    502    640     -4     33     57       O  
HETATM 3650  C25A8Z0 A 101      15.750  24.582  18.035  0.49  4.24           C  
ANISOU 3650  C25A8Z0 A 101      626    409    481     24     55     -6       C  
HETATM 3651  C25B8Z0 A 101      15.092  23.620  18.705  0.52  4.99           C  
ANISOU 3651  C25B8Z0 A 101      723    506    554      4    121      6       C  
HETATM 3652  C19A8Z0 A 101      18.723  23.306  20.206  0.49  4.55           C  
ANISOU 3652  C19A8Z0 A 101      699    465    462     67     96    108       C  
HETATM 3653  C19B8Z0 A 101      14.124  22.306  15.217  0.52  5.22           C  
ANISOU 3653  C19B8Z0 A 101      839    547    478     -4    124     14       C  
HETATM 3654  C18A8Z0 A 101      17.334  23.783  19.863  0.49  4.78           C  
ANISOU 3654  C18A8Z0 A 101      683    555    469     42     69    122       C  
HETATM 3655  C18B8Z0 A 101      14.448  23.271  16.308  0.52  4.90           C  
ANISOU 3655  C18B8Z0 A 101      773    538    438    -18    122     62       C  
HETATM 3656  C22A8Z0 A 101      21.277  22.486  20.910  0.49  7.84           C  
ANISOU 3656  C22A8Z0 A 101      901    974    925    231   -122    135       C  
HETATM 3657  C22B8Z0 A 101      13.459  20.524  13.167  0.52  8.32           C  
ANISOU 3657  C22B8Z0 A 101     1466    853    653    -81    -92   -104       C  
HETATM 3658  C17A8Z0 A 101      17.155  24.049  18.366  0.49  4.17           C  
ANISOU 3658  C17A8Z0 A 101      595    428    467     -6     53     32       C  
HETATM 3659  C17B8Z0 A 101      14.914  22.606  17.579  0.52  4.73           C  
ANISOU 3659  C17B8Z0 A 101      647    509    535      8    105    -11       C  
HETATM 3660  O2 A8Z0 A 101      15.426  25.564  18.991  0.49  4.61           O  
ANISOU 3660  O2 A8Z0 A 101      649    499    498     25     61    -78       O  
HETATM 3661  O2 B8Z0 A 101      14.036  24.504  18.714  0.52  4.88           O  
ANISOU 3661  O2 B8Z0 A 101      675    556    513     35     74    -78       O  
HETATM 3662  C20A8Z0 A 101      19.576  24.203  20.833  0.49  5.46           C  
ANISOU 3662  C20A8Z0 A 101      776    599    576     31    -38    121       C  
HETATM 3663  C20B8Z0 A 101      12.842  21.958  14.921  0.52  6.28           C  
ANISOU 3663  C20B8Z0 A 101      829    840    575    -15     72     38       C  
HETATM 3664  C24A8Z0 A 101      19.128  22.010  19.931  0.49  6.49           C  
ANISOU 3664  C24A8Z0 A 101      988    624    706    235   -169     71       C  
HETATM 3665  C24B8Z0 A 101      15.133  21.704  14.444  0.52  6.61           C  
ANISOU 3665  C24B8Z0 A 101      923    834    603    195     87    -82       C  
HETATM 3666  C21A8Z0 A 101      20.838  23.770  21.162  0.49  7.24           C  
ANISOU 3666  C21A8Z0 A 101      758    853    976    -90   -220    194       C  
HETATM 3667  C21B8Z0 A 101      12.492  21.102  13.902  0.52  8.38           C  
ANISOU 3667  C21B8Z0 A 101     1077   1282    636   -239    -56     16       C  
HETATM 3668  C23A8Z0 A 101      20.403  21.612  20.296  0.49  6.57           C  
ANISOU 3668  C23A8Z0 A 101      804    705    838    300     30    138       C  
HETATM 3669  C23B8Z0 A 101      14.793  20.804  13.433  0.52  7.27           C  
ANISOU 3669  C23B8Z0 A 101     1262    714    622    190     53    -69       C  
HETATM 3670  C32A8Z0 A 101      14.265  20.454  17.394  0.49  4.44           C  
ANISOU 3670  C32A8Z0 A 101      668    532    386    -26     43    -20       C  
HETATM 3671  C32B8Z0 A 101      19.345  24.154  17.462  0.52  4.56           C  
ANISOU 3671  C32B8Z0 A 101      605    561    465    -19     47    -14       C  
HETATM 3672  N4 A8Z0 A 101      14.542  22.813  16.829  0.49  4.46           N  
ANISOU 3672  N4 A8Z0 A 101      732    498    364    -60     38     68       N  
HETATM 3673  N4 B8Z0 A 101      17.529  23.810  19.079  0.52  4.62           N  
ANISOU 3673  N4 B8Z0 A 101      711    468    473    -39     50     68       N  
HETATM 3674  O5 A8Z0 A 101      15.478  20.243  17.337  0.49  5.38           O  
ANISOU 3674  O5 A8Z0 A 101      702    647    573     33    127    110       O  
HETATM 3675  O5 B8Z0 A 101      19.085  23.100  16.864  0.52  5.42           O  
ANISOU 3675  O5 B8Z0 A 101      896    597    444    -46    108    -17       O  
HETATM 3676  C27A8Z0 A 101      13.628  21.689  16.801  0.49  4.43           C  
ANISOU 3676  C27A8Z0 A 101      668    492    421    -22     84    -37       C  
HETATM 3677  C27B8Z0 A 101      18.836  24.427  18.884  0.52  4.40           C  
ANISOU 3677  C27B8Z0 A 101      648    416    508    -18     67     -4       C  
HETATM 3678  C28A8Z0 A 101      13.218  21.527  15.313  0.49  5.19           C  
ANISOU 3678  C28A8Z0 A 101      813    644    396    -46      6     53       C  
HETATM 3679  C28B8Z0 A 101      19.736  23.929  20.012  0.52  4.82           C  
ANISOU 3679  C28B8Z0 A 101      731    555    435     25     35    -56       C  
HETATM 3680  C31A8Z0 A 101      15.197  23.203  15.584  0.49  5.27           C  
ANISOU 3680  C31A8Z0 A 101      858    555    472    -35    120     -4       C  
HETATM 3681  C31B8Z0 A 101      17.523  22.597  19.941  0.52  5.28           C  
ANISOU 3681  C31B8Z0 A 101      855    510    522     23    108    113       C  
HETATM 3682  C29A8Z0 A 101      12.218  22.621  14.973  0.49  5.59           C  
ANISOU 3682  C29A8Z0 A 101      929    646    422    -97    -38     53       C  
HETATM 3683  C29B8Z0 A 101      19.393  24.685  21.313  0.52  5.85           C  
ANISOU 3683  C29B8Z0 A 101     1014    639    437     90     -9    -81       C  
HETATM 3684  C30A8Z0 A 101      12.670  20.175  14.942  0.49  5.65           C  
ANISOU 3684  C30A8Z0 A 101      942    579    498    -71    -85    -43       C  
HETATM 3685  C30B8Z0 A 101      21.222  24.014  19.719  0.52  5.33           C  
ANISOU 3685  C30B8Z0 A 101      750    606    547    -26     11     30       C  
HETATM 3686  S2 A8Z0 A 101      14.783  21.857  14.431  0.49  5.35           S  
ANISOU 3686  S2 A8Z0 A 101      897    559    455   -107    130    -57       S  
HETATM 3687  S2 B8Z0 A 101      19.272  22.167  20.155  0.52  5.00           S  
ANISOU 3687  S2 B8Z0 A 101      740    542    503      7     71     60       S  
HETATM 3688  C33A8Z0 A 101      13.806  18.327  18.554  0.49  5.42           C  
ANISOU 3688  C33A8Z0 A 101      848    465    626     17    119      8       C  
HETATM 3689  C33B8Z0 A 101      20.746  24.981  15.614  0.52  4.98           C  
ANISOU 3689  C33B8Z0 A 101      678    565    535    -10    125      9       C  
HETATM 3690  N5 A8Z0 A 101      13.407  19.613  17.974  0.49  5.02           N  
ANISOU 3690  N5 A8Z0 A 101      709    485    600    -24     76     17       N  
HETATM 3691  N5 B8Z0 A 101      20.092  25.137  16.941  0.52  4.82           N  
ANISOU 3691  N5 B8Z0 A 101      705    578    439    -10     88    -26       N  
HETATM 3692  C41A8Z0 A 101      14.862  19.624  20.977  0.49  7.95           C  
ANISOU 3692  C41A8Z0 A 101      885    766   1189     -9   -111   -100       C  
HETATM 3693  C41B8Z0 A 101      18.286  25.707  14.166  0.52  6.19           C  
ANISOU 3693  C41B8Z0 A 101      692    765    756    -11     17    -78       C  
HETATM 3694  C35A8Z0 A 101      13.675  18.677  21.049  0.49  6.26           C  
ANISOU 3694  C35A8Z0 A 101      978    578    682     81      9     22       C  
HETATM 3695  C35B8Z0 A 101      19.515  26.590  14.104  0.52  5.25           C  
ANISOU 3695  C35B8Z0 A 101      731    644    501     12     88   -100       C  
HETATM 3696  C36A8Z0 A 101      13.114  18.401  22.294  0.49  7.49           C  
ANISOU 3696  C36A8Z0 A 101     1226    866    585    193     54   -108       C  
HETATM 3697  C36B8Z0 A 101      19.487  27.734  13.348  0.52  6.34           C  
ANISOU 3697  C36B8Z0 A 101      968    776    519     55      9     25       C  
HETATM 3698  C37A8Z0 A 101      12.015  17.561  22.376  0.49  7.47           C  
ANISOU 3698  C37A8Z0 A 101     1269    734    667    261    277    206       C  
HETATM 3699  C37B8Z0 A 101      20.571  28.554  13.298  0.52  5.96           C  
ANISOU 3699  C37B8Z0 A 101      970    637    521    115    192     61       C  
HETATM 3700  C38A8Z0 A 101      11.458  17.039  21.264  0.49  6.51           C  
ANISOU 3700  C38A8Z0 A 101      945    496    886    116    313    197       C  
HETATM 3701  C38B8Z0 A 101      21.697  28.288  14.029  0.52  5.93           C  
ANISOU 3701  C38B8Z0 A 101      907    646    567    -24    204      3       C  
HETATM 3702  C39A8Z0 A 101      11.988  17.295  19.991  0.49  5.81           C  
ANISOU 3702  C39A8Z0 A 101      857    542    678     49    129     73       C  
HETATM 3703  C39B8Z0 A 101      21.761  27.152  14.824  0.52  5.17           C  
ANISOU 3703  C39B8Z0 A 101      686    597    566     -3    133     -8       C  
HETATM 3704  C40A8Z0 A 101      11.318  16.723  18.759  0.49  7.19           C  
ANISOU 3704  C40A8Z0 A 101      798    796    977    -51    -43     22       C  
HETATM 3705  C40B8Z0 A 101      22.995  26.913  15.661  0.52  6.28           C  
ANISOU 3705  C40B8Z0 A 101      717    890    636     -9     57    -12       C  
HETATM 3706  C34A8Z0 A 101      13.119  18.092  19.894  0.49  5.26           C  
ANISOU 3706  C34A8Z0 A 101      741    557    582     63     94     66       C  
HETATM 3707  C34B8Z0 A 101      20.670  26.284  14.848  0.52  4.91           C  
ANISOU 3707  C34B8Z0 A 101      650    645    460     37    137     -3       C  
HETATM 3708  H2 A8Z0 A 101      26.331  24.276  22.502  0.49 12.63           H  
HETATM 3709  H2 B8Z0 A 101       9.603  17.457  10.787  0.52 13.01           H  
HETATM 3710  H1 A8Z0 A 101      26.097  22.522  20.952  0.49 10.99           H  
HETATM 3711  H1 B8Z0 A 101      11.680  16.494  11.027  0.52 10.43           H  
HETATM 3712  H3 A8Z0 A 101      25.103  26.217  22.313  0.49 12.92           H  
HETATM 3713  H3 B8Z0 A 101       8.682  18.683  12.399  0.52 11.37           H  
HETATM 3714  H4 A8Z0 A 101      24.973  20.659  18.090  0.49 14.14           H  
HETATM 3715  H4 B8Z0 A 101      14.687  15.521  12.258  0.52 18.20           H  
HETATM 3716  H5 A8Z0 A 101      26.148  21.555  18.615  0.49 14.14           H  
HETATM 3717  H5 B8Z0 A 101      13.211  15.156  11.877  0.52 18.20           H  
HETATM 3718  H6 A8Z0 A 101      25.213  20.814  19.632  0.49 14.14           H  
HETATM 3719  H6 B8Z0 A 101      13.892  16.421  11.250  0.52 18.20           H  
HETATM 3720  H7 A8Z0 A 101      22.895  27.409  20.548  0.49  8.95           H  
HETATM 3721  H7 B8Z0 A 101       9.109  19.411  15.414  0.52  9.76           H  
HETATM 3722  H8 A8Z0 A 101      19.479  26.745  16.656  0.49  5.06           H  
HETATM 3723  H8 B8Z0 A 101      12.533  19.963  19.281  0.52  6.13           H  
HETATM 3724  H9 A8Z0 A 101      21.521  24.948  17.126  0.49  5.47           H  
HETATM 3725  H9 B8Z0 A 101      13.087  18.414  17.058  0.52  6.31           H  
HETATM 3726  H10A8Z0 A 101      20.730  25.144  14.659  0.49  5.15           H  
HETATM 3727  H10B8Z0 A 101      14.215  17.662  19.327  0.52  6.25           H  
HETATM 3728  H12A8Z0 A 101      18.958  25.582  13.330  0.49  5.51           H  
HETATM 3729  H12B8Z0 A 101      14.348  19.818  20.993  0.52  6.56           H  
HETATM 3730  H13A8Z0 A 101      18.198  26.190  14.575  0.49  5.51           H  
HETATM 3731  H13B8Z0 A 101      15.110  18.451  21.218  0.52  6.56           H  
HETATM 3732  H16A8Z0 A 101      21.625  27.434  15.505  0.49  6.02           H  
HETATM 3733  H16B8Z0 A 101      11.668  17.629  19.595  0.52  7.21           H  
HETATM 3734  H17A8Z0 A 101      21.708  27.099  13.964  0.49  6.02           H  
HETATM 3735  H17B8Z0 A 101      12.563  16.658  20.461  0.52  7.21           H  
HETATM 3736  H20A8Z0 A 101      19.678  27.600  12.641  0.49  5.77           H  
HETATM 3737  H20B8Z0 A 101      13.492  17.645  22.580  0.52  6.96           H  
HETATM 3738  H21A8Z0 A 101      18.447  28.137  13.466  0.49  5.77           H  
HETATM 3739  H21B8Z0 A 101      13.164  19.171  22.812  0.52  6.96           H  
HETATM 3740  H15A8Z0 A 101      18.331  25.683  18.332  0.49  4.91           H  
HETATM 3741  H15B8Z0 A 101      13.124  21.765  18.040  0.52  5.73           H  
HETATM 3742  H39A8Z0 A 101      15.780  25.007  17.152  0.49  5.09           H  
HETATM 3743  H39B8Z0 A 101      15.103  23.138  19.559  0.52  5.99           H  
HETATM 3744  H32A8Z0 A 101      17.148  24.599  20.354  0.49  5.73           H  
HETATM 3745  H32B8Z0 A 101      13.660  23.802  16.503  0.52  5.88           H  
HETATM 3746  H33A8Z0 A 101      16.690  23.114  20.145  0.49  5.73           H  
HETATM 3747  H33B8Z0 A 101      15.141  23.875  15.998  0.52  5.88           H  
HETATM 3748  H36A8Z0 A 101      22.136  22.218  21.146  0.49  9.41           H  
HETATM 3749  H36B8Z0 A 101      13.235  19.937  12.482  0.52  9.98           H  
HETATM 3750  H14A8Z0 A 101      17.272  23.198  17.894  0.49  5.00           H  
HETATM 3751  H14B8Z0 A 101      15.778  22.176  17.407  0.52  5.68           H  
HETATM 3752  H22A8Z0 A 101      14.730  25.355  19.372  0.49  6.91           H  
HETATM 3753  H22B8Z0 A 101      14.138  25.046  19.320  0.52  7.32           H  
HETATM 3754  H31A8Z0 A 101      19.301  25.070  21.026  0.49  6.55           H  
HETATM 3755  H31B8Z0 A 101      12.161  22.321  15.439  0.52  7.54           H  
HETATM 3756  H38A8Z0 A 101      18.552  21.416  19.506  0.49  7.78           H  
HETATM 3757  H38B8Z0 A 101      16.026  21.905  14.607  0.52  7.93           H  
HETATM 3758  H34A8Z0 A 101      21.421  24.368  21.571  0.49  8.69           H  
HETATM 3759  H34B8Z0 A 101      11.597  20.924  13.723  0.52 10.06           H  
HETATM 3760  H37A8Z0 A 101      20.675  20.739  20.125  0.49  7.88           H  
HETATM 3761  H37B8Z0 A 101      15.462  20.391  12.936  0.52  8.72           H  
HETATM 3762  H11A8Z0 A 101      12.831  21.916  17.325  0.49  5.31           H  
HETATM 3763  H11B8Z0 A 101      18.731  25.396  18.986  0.52  5.28           H  
HETATM 3764  H18A8Z0 A 101      16.157  23.273  15.704  0.49  6.33           H  
HETATM 3765  H18B8Z0 A 101      17.041  21.873  19.512  0.52  6.34           H  
HETATM 3766  H19A8Z0 A 101      14.856  24.052  15.263  0.49  6.33           H  
HETATM 3767  H19B8Z0 A 101      17.109  22.786  20.797  0.52  6.34           H  
HETATM 3768  H23A8Z0 A 101      12.583  23.475  15.216  0.49  8.38           H  
HETATM 3769  H23B8Z0 A 101      18.450  24.620  21.481  0.52  8.78           H  
HETATM 3770  H24A8Z0 A 101      12.036  22.607  14.030  0.49  8.38           H  
HETATM 3771  H24B8Z0 A 101      19.876  24.297  22.046  0.52  8.78           H  
HETATM 3772  H25A8Z0 A 101      11.403  22.472  15.458  0.49  8.38           H  
HETATM 3773  H25B8Z0 A 101      19.638  25.608  21.221  0.52  8.78           H  
HETATM 3774  H28A8Z0 A 101      13.313  19.498  15.163  0.49  8.48           H  
HETATM 3775  H28B8Z0 A 101      21.717  23.685  20.473  0.52  7.99           H  
HETATM 3776  H29A8Z0 A 101      11.857  20.015  15.427  0.49  8.48           H  
HETATM 3777  H29B8Z0 A 101      21.427  23.484  18.945  0.52  7.99           H  
HETATM 3778  H30A8Z0 A 101      12.490  20.151  13.999  0.49  8.48           H  
HETATM 3779  H30B8Z0 A 101      21.464  24.929  19.553  0.52  7.99           H  
HETATM 3780  H26A8Z0 A 101      14.768  18.314  18.678  0.49  6.51           H  
HETATM 3781  H26B8Z0 A 101      20.303  24.279  15.112  0.52  5.97           H  
HETATM 3782  H27A8Z0 A 101      13.573  17.611  17.942  0.49  6.51           H  
HETATM 3783  H27B8Z0 A 101      21.674  24.726  15.735  0.52  5.97           H  
HETATM 3784  H35A8Z0 A 101      12.577  19.836  18.009  0.49  6.02           H  
HETATM 3785  H35B8Z0 A 101      20.195  25.869  17.380  0.52  5.78           H  
HETATM 3786  H40A8Z0 A 101      15.140  19.719  20.063  0.49 11.92           H  
HETATM 3787  H40B8Z0 A 101      18.463  24.951  14.732  0.52  9.29           H  
HETATM 3788  H41A8Z0 A 101      14.609  20.482  21.325  0.49 11.92           H  
HETATM 3789  H41B8Z0 A 101      17.549  26.208  14.524  0.52  9.29           H  
HETATM 3790  H42A8Z0 A 101      15.587  19.269  21.496  0.49 11.92           H  
HETATM 3791  H42B8Z0 A 101      18.066  25.401  13.283  0.52  9.29           H  
HETATM 3792  H43A8Z0 A 101      13.475  18.777  23.064  0.49  8.99           H  
HETATM 3793  H43B8Z0 A 101      18.722  27.951  12.867  0.52  7.60           H  
HETATM 3794  H44A8Z0 A 101      11.657  17.354  23.210  0.49  8.97           H  
HETATM 3795  H44B8Z0 A 101      20.547  29.310  12.757  0.52  7.15           H  
HETATM 3796  H45A8Z0 A 101      10.705  16.498  21.343  0.49  7.82           H  
HETATM 3797  H45B8Z0 A 101      22.422  28.870  13.993  0.52  7.12           H  
HETATM 3798  H46A8Z0 A 101      10.556  16.201  19.022  0.49 10.79           H  
HETATM 3799  H46B8Z0 A 101      22.894  26.095  16.153  0.52  9.42           H  
HETATM 3800  H47A8Z0 A 101      11.032  17.440  18.188  0.49 10.79           H  
HETATM 3801  H47B8Z0 A 101      23.763  26.849  15.089  0.52  9.42           H  
HETATM 3802  H48A8Z0 A 101      11.939  16.165  18.286  0.49 10.79           H  
HETATM 3803  H48B8Z0 A 101      23.112  27.642  16.274  0.52  9.42           H  
HETATM 3804  C1 AGOL B 101      14.344  26.975  39.868  0.58  8.18           C  
ANISOU 3804  C1 AGOL B 101     1341    960    620    135    102    -54       C  
HETATM 3805  C1 BGOL B 101      14.056  26.606  39.753  0.42 17.68           C  
ANISOU 3805  C1 BGOL B 101     3275   2046    998    745   -657     69       C  
HETATM 3806  O1 AGOL B 101      12.952  27.062  39.594  0.58 16.06           O  
ANISOU 3806  O1 AGOL B 101     1614   1767   2358   -209   -689    474       O  
HETATM 3807  O1 BGOL B 101      13.487  27.280  38.663  0.42  6.79           O  
ANISOU 3807  O1 BGOL B 101     1066   1042    320    217    279    155       O  
HETATM 3808  C2 AGOL B 101      14.971  28.164  40.464  0.58 10.71           C  
ANISOU 3808  C2 AGOL B 101      996   1669   1160     18    363   -579       C  
HETATM 3809  C2 BGOL B 101      13.937  27.341  41.059  0.42 18.03           C  
ANISOU 3809  C2 BGOL B 101     1989   3554    901     52   -440   -386       C  
HETATM 3810  O2 AGOL B 101      15.909  28.824  39.717  0.58 11.66           O  
ANISOU 3810  O2 AGOL B 101     1686   1567    914    -62    257   -125       O  
HETATM 3811  O2 BGOL B 101      12.572  27.703  41.391  0.42 21.30           O  
ANISOU 3811  O2 BGOL B 101     2402   3425   1782    749     28    457       O  
HETATM 3812  C3 AGOL B 101      14.128  29.018  41.311  0.58  9.28           C  
ANISOU 3812  C3 AGOL B 101     1929    813    572     52    444   -111       C  
HETATM 3813  C3 BGOL B 101      14.666  28.682  40.697  0.42 20.93           C  
ANISOU 3813  C3 BGOL B 101     2321   3411   1746   -413  -1217   -628       C  
HETATM 3814  O3 AGOL B 101      14.680  29.985  41.879  0.58  8.39           O  
ANISOU 3814  O3 AGOL B 101      958   1337    703    110   -186   -207       O  
HETATM 3815  O3 BGOL B 101      15.905  28.133  40.458  0.42 24.25           O  
ANISOU 3815  O3 BGOL B 101     3587   2636   2440   -198   1384    476       O  
HETATM 3816  C1  GOL B 102      18.419   6.029  25.428  0.50 30.78           C  
ANISOU 3816  C1  GOL B 102     2649   3086   5265   1302    736  -1273       C  
HETATM 3817  O1  GOL B 102      18.157   4.716  25.140  0.52 31.43           O  
ANISOU 3817  O1  GOL B 102     2578   3067   5588    602   1133   -596       O  
HETATM 3818  C2  GOL B 102      19.604   6.503  26.238  0.49 25.72           C  
ANISOU 3818  C2  GOL B 102     1932   2338   4922    -85   1284   1282       C  
HETATM 3819  O2  GOL B 102      19.717   6.039  27.565  0.50 22.07           O  
ANISOU 3819  O2  GOL B 102     1731   1431   4726    426   1477    909       O  
HETATM 3820  C3  GOL B 102      19.571   8.039  26.194  0.51 29.02           C  
ANISOU 3820  C3  GOL B 102     2195   2387   5788    416   -650   1783       C  
HETATM 3821  O3  GOL B 102      19.892   8.360  27.476  0.48 50.54           O  
ANISOU 3821  O3  GOL B 102     8108   2317   7635  -2510  -4000   1778       O  
HETATM 3822  O   HOH A 201      25.708  27.954  -4.521  0.50 32.40           O  
ANISOU 3822  O   HOH A 201     3894   4370   3314   -404   -279    330       O  
HETATM 3823  O   HOH A 202      11.080  17.105  15.089  0.49 13.11           O  
ANISOU 3823  O   HOH A 202     1428   1470   1787    -73     53   -374       O  
HETATM 3824  O   HOH A 203      22.362  15.572  19.766  1.00 20.19           O  
ANISOU 3824  O   HOH A 203     2803   2893   1518    304    411    271       O  
HETATM 3825  O   HOH A 204      21.751  45.385   8.204  1.00 64.37           O  
ANISOU 3825  O   HOH A 204     4880  14136   3983   -316   1388   -191       O  
HETATM 3826  O   HOH A 205      22.296  46.014   3.395  1.00 68.52           O  
ANISOU 3826  O   HOH A 205     9464   2424  12594   -764   1739   2403       O  
HETATM 3827  O   HOH A 206      24.381  39.725   1.331  0.50  9.61           O  
ANISOU 3827  O   HOH A 206     1317    820   1296    -16    643    452       O  
HETATM 3828  O   HOH A 207       8.882  22.079  16.804  1.00 11.17           O  
ANISOU 3828  O   HOH A 207     1695   1234   1062   -237     14   -162       O  
HETATM 3829  O   HOH A 208      24.904  32.644  15.974  1.00 45.25           O  
ANISOU 3829  O   HOH A 208     3395   5534   7239  -2742    953  -1977       O  
HETATM 3830  O   HOH A 209       7.603  41.700   1.904  1.00 46.81           O  
ANISOU 3830  O   HOH A 209     4438   9258   3031  -2167   -591    522       O  
HETATM 3831  O   HOH A 210      28.688  20.966  -0.355  1.00 57.37           O  
ANISOU 3831  O   HOH A 210     8809   7401   4291   1038  -1845    360       O  
HETATM 3832  O   HOH A 211      28.477  39.631   4.290  1.00 41.46           O  
ANISOU 3832  O   HOH A 211     3350   4051   7413    430   1659   2492       O  
HETATM 3833  O   HOH A 212      10.472  20.186  18.018  0.49  5.13           O  
ANISOU 3833  O   HOH A 212      694    639    500     -7      5     16       O  
HETATM 3834  O   HOH A 213      23.858  37.724   0.313  0.50 14.15           O  
ANISOU 3834  O   HOH A 213     2078   1058   1921    169    902    486       O  
HETATM 3835  O   HOH A 214       8.200  25.242   1.573  1.00 36.50           O  
ANISOU 3835  O   HOH A 214     1537   5570   5934   -129   -169  -4000       O  
HETATM 3836  O   HOH A 215       2.740  32.143  34.186  1.00 23.88           O  
ANISOU 3836  O   HOH A 215     3103   1770   3661   -614   2130  -1108       O  
HETATM 3837  O   HOH A 216      -2.468  31.364  20.161  1.00 28.14           O  
ANISOU 3837  O   HOH A 216     2334   3524   4197   -918  -1585   1572       O  
HETATM 3838  O   HOH A 217       9.204  20.676   7.547  1.00 49.49           O  
ANISOU 3838  O   HOH A 217     2515   3362  11809    386  -2250  -2836       O  
HETATM 3839  O   HOH A 218      20.961  29.719  -6.309  1.00 26.99           O  
ANISOU 3839  O   HOH A 218     3353   2903   3390  -1011   1196   -409       O  
HETATM 3840  O   HOH A 219      19.490  43.661   1.418  1.00 48.47           O  
ANISOU 3840  O   HOH A 219    10397   4725   2198   4833    905   1108       O  
HETATM 3841  O   HOH A 220      17.955  20.776  16.687  1.00 12.87           O  
ANISOU 3841  O   HOH A 220      808   1160   2633   -220    561  -1206       O  
HETATM 3842  O   HOH A 221      25.325  30.215  17.065  1.00 16.49           O  
ANISOU 3842  O   HOH A 221     1387   3297   1209    257    232    251       O  
HETATM 3843  O   HOH A 222      14.319  38.559   0.560  1.00 14.37           O  
ANISOU 3843  O   HOH A 222     2181   1939   1015   -389      2   -154       O  
HETATM 3844  O   HOH A 223      24.525  22.440   2.566  1.00 45.21           O  
ANISOU 3844  O   HOH A 223     4621   9598   1936  -3482    987  -1247       O  
HETATM 3845  O   HOH A 224       7.696  36.641  -6.270  1.00 54.79           O  
ANISOU 3845  O   HOH A 224     8207   6633   4737    -45  -3024   3394       O  
HETATM 3846  O   HOH A 225      25.946  38.121   2.026  1.00 21.11           O  
ANISOU 3846  O   HOH A 225     2908   1953   2684    123   1692    673       O  
HETATM 3847  O   HOH A 226       1.325  27.822  18.301  1.00 15.62           O  
ANISOU 3847  O   HOH A 226     2875   1726    981    956   -248     29       O  
HETATM 3848  O  BHOH A 227      24.576  30.655  14.472  0.50 14.19           O  
ANISOU 3848  O  BHOH A 227     1673   1463   1934    -31   -394    389       O  
HETATM 3849  O   HOH A 228      20.860  21.092   1.015  1.00 17.53           O  
ANISOU 3849  O   HOH A 228     1875   2212   2176   -339   -876    866       O  
HETATM 3850  O   HOH A 229      15.336  20.778   3.816  1.00 15.39           O  
ANISOU 3850  O   HOH A 229     2573   2146    780   -769    176   -133       O  
HETATM 3851  O   HOH A 230       4.675  35.138  36.150  1.00 37.02           O  
ANISOU 3851  O   HOH A 230     8327   3321   1581   -426    535   -766       O  
HETATM 3852  O   HOH A 231      24.021  32.067  -4.203  1.00 19.51           O  
ANISOU 3852  O   HOH A 231     3105   2546   1322    -27    574    -87       O  
HETATM 3853  O   HOH A 232      23.842  34.663  -4.577  1.00 17.51           O  
ANISOU 3853  O   HOH A 232     1956   2609   1691    -68    617    281       O  
HETATM 3854  O   HOH A 233      28.595  25.771  14.706  0.50 11.19           O  
ANISOU 3854  O   HOH A 233     1257   1683   1057   -399    -82    -81       O  
HETATM 3855  O   HOH A 234      12.531  21.222   2.823  1.00 22.80           O  
ANISOU 3855  O   HOH A 234     2211   1821   4115   -395    244   -255       O  
HETATM 3856  O   HOH A 235      27.143  46.110   6.311  0.50 44.01           O  
ANISOU 3856  O   HOH A 235     2054   5218   8455   -682    472   -585       O  
HETATM 3857  O  BHOH A 236      26.236  25.276  16.144  0.51 10.92           O  
ANISOU 3857  O  BHOH A 236     1361   1212   1328     19    -49   -426       O  
HETATM 3858  O   HOH A 237       9.059  44.992  11.619  1.00 38.12           O  
ANISOU 3858  O   HOH A 237     2147   7033   4443   -376   1043  -3241       O  
HETATM 3859  O   HOH A 238      20.812  33.969  -6.434  1.00 39.33           O  
ANISOU 3859  O   HOH A 238     5434   6960   1660  -2617   -467    906       O  
HETATM 3860  O   HOH A 239      -3.926  35.621  27.230  0.50 39.73           O  
ANISOU 3860  O   HOH A 239     4493   5284   4418  -1826   2493   -445       O  
HETATM 3861  O   HOH A 240      14.938  33.831  -4.301  1.00 28.95           O  
ANISOU 3861  O   HOH A 240     3231   5740   1375   2565   -316   -205       O  
HETATM 3862  O   HOH A 241      -0.525  32.448   4.903  0.50 27.74           O  
ANISOU 3862  O   HOH A 241     1849   4788   3275    773   -386   1319       O  
HETATM 3863  O   HOH A 242      23.129  25.100   1.267  1.00 16.13           O  
ANISOU 3863  O   HOH A 242     1556   2654   1553    -38    271   -891       O  
HETATM 3864  O   HOH A 243      11.118  17.672   7.208  1.00 45.47           O  
ANISOU 3864  O   HOH A 243     3698   3695   8856   -474  -1583  -3128       O  
HETATM 3865  O   HOH A 244      -1.183  27.148  20.076  1.00 13.95           O  
ANISOU 3865  O   HOH A 244     2127   1296   1560   -372   -892    225       O  
HETATM 3866  O   HOH A 245      23.142  36.821  12.965  0.50  9.12           O  
ANISOU 3866  O   HOH A 245     1109    837   1313   -210   -314    165       O  
HETATM 3867  O   HOH A 246       5.220  39.909  30.420  1.00 25.48           O  
ANISOU 3867  O   HOH A 246     3534   2619   2952    218    512   -827       O  
HETATM 3868  O   HOH A 247      25.188  28.845  14.867  1.00 25.64           O  
ANISOU 3868  O   HOH A 247     4106   2617   2440    626   -175   -133       O  
HETATM 3869  O   HOH A 248      26.792  23.641  18.491  0.49 20.85           O  
ANISOU 3869  O   HOH A 248     2494   2264   2694   -466    -94    131       O  
HETATM 3870  O   HOH A 249      19.908  17.487   6.862  1.00 24.69           O  
ANISOU 3870  O   HOH A 249     6191   1484   1146    479   -110     38       O  
HETATM 3871  O   HOH A 250      27.431  17.292   9.104  1.00 32.84           O  
ANISOU 3871  O   HOH A 250     2975   3617   5141   -506   2298  -2096       O  
HETATM 3872  O  BHOH A 251      22.085  35.120  17.253  0.50 21.11           O  
ANISOU 3872  O  BHOH A 251     1767   1915   3860   -369   -215    586       O  
HETATM 3873  O   HOH A 252      19.291  39.900  17.251  1.00  8.42           O  
ANISOU 3873  O   HOH A 252     1089   1015    905     55     47     15       O  
HETATM 3874  O   HOH A 253       7.140  41.715  22.780  1.00 12.92           O  
ANISOU 3874  O   HOH A 253     2098   1186   1331    478    333      7       O  
HETATM 3875  O   HOH A 254      21.265  39.921  -1.333  0.50 22.45           O  
ANISOU 3875  O   HOH A 254     3608   3125   1291    812    526    498       O  
HETATM 3876  O   HOH A 255       3.880  41.485   1.740  1.00 67.66           O  
ANISOU 3876  O   HOH A 255     3406  12036   8733   1289   1387    304       O  
HETATM 3877  O   HOH A 256      13.467  40.105  21.764  1.00  8.94           O  
ANISOU 3877  O   HOH A 256     1056    788   1350     10    -19     99       O  
HETATM 3878  O   HOH A 257      -2.418  34.182  17.746  1.00 35.67           O  
ANISOU 3878  O   HOH A 257     3081   6420   3243   -670   -478  -1064       O  
HETATM 3879  O   HOH A 258      -4.016  28.190  14.183  1.00 21.55           O  
ANISOU 3879  O   HOH A 258     1358   2207   4137    426   -283   -136       O  
HETATM 3880  O   HOH A 259       4.905  16.742  12.221  1.00 72.55           O  
ANISOU 3880  O   HOH A 259    13467   6651   5806  -3458   -857  -3166       O  
HETATM 3881  O   HOH A 260      -3.506  33.729  21.301  1.00 24.77           O  
ANISOU 3881  O   HOH A 260     1663   4450   2739  -1244   -461   1460       O  
HETATM 3882  O   HOH A 261       4.059  39.449   2.784  1.00 70.42           O  
ANISOU 3882  O   HOH A 261     6184  10157   8822    305  -1010   1534       O  
HETATM 3883  O   HOH A 262      18.481  30.642  21.747  1.00  7.28           O  
ANISOU 3883  O   HOH A 262      830    748   1024     10     17    172       O  
HETATM 3884  O   HOH A 263       2.723  29.521   5.592  1.00 25.41           O  
ANISOU 3884  O   HOH A 263     2012   2922   4146   -165     12   -688       O  
HETATM 3885  O   HOH A 264       1.240  24.443  14.031  1.00 18.14           O  
ANISOU 3885  O   HOH A 264     1702   3309   1471   -995   -258   -389       O  
HETATM 3886  O   HOH A 265      15.624  44.621  11.094  1.00  9.87           O  
ANISOU 3886  O   HOH A 265     1400   1268    860    230    153    127       O  
HETATM 3887  O   HOH A 266      20.272  28.571  21.383  1.00  9.34           O  
ANISOU 3887  O   HOH A 266     1068    973   1297    261    308    336       O  
HETATM 3888  O   HOH A 267       0.289  25.308   9.652  0.50 33.20           O  
ANISOU 3888  O   HOH A 267     3181   6283   2399  -1941   -631   1773       O  
HETATM 3889  O   HOH A 268      21.024  35.615  17.731  0.63 12.71           O  
ANISOU 3889  O   HOH A 268     1413   1860   1270    186    -75   -368       O  
HETATM 3890  O   HOH A 269       1.298  38.882  12.762  1.00 27.43           O  
ANISOU 3890  O   HOH A 269     3329   4070   2401    747   1225    167       O  
HETATM 3891  O   HOH A 270      20.850  33.515  10.635  1.00  8.11           O  
ANISOU 3891  O   HOH A 270     1037    954    907    -53    233    206       O  
HETATM 3892  O   HOH A 271      -3.861  33.913  23.882  1.00 16.95           O  
ANISOU 3892  O   HOH A 271     1393   1809   2853   -362    144    618       O  
HETATM 3893  O   HOH A 272      28.068  35.692   4.307  1.00 18.91           O  
ANISOU 3893  O   HOH A 272     1710   1830   3217   -339    783   -194       O  
HETATM 3894  O   HOH A 273      11.307  34.481  -6.258  1.00 28.79           O  
ANISOU 3894  O   HOH A 273     3539   4811   1939   -878   -683    652       O  
HETATM 3895  O   HOH A 274      26.391  31.112  15.254  1.00 65.48           O  
ANISOU 3895  O   HOH A 274    10650   7217   5529   6362  -4000  -3521       O  
HETATM 3896  O   HOH A 275      33.413  29.923   6.393  1.00 23.21           O  
ANISOU 3896  O   HOH A 275     1946   4416   1930  -1456    394     25       O  
HETATM 3897  O   HOH A 276       0.664  28.013  13.489  1.00 21.56           O  
ANISOU 3897  O   HOH A 276     1731   3843   2132   -564    312    126       O  
HETATM 3898  O   HOH A 277      10.286  20.785   5.526  1.00 55.12           O  
ANISOU 3898  O   HOH A 277     6478   8668   4550  -4000  -2708   2958       O  
HETATM 3899  O   HOH A 278      21.522  31.468  -4.238  1.00 22.38           O  
ANISOU 3899  O   HOH A 278     2224   2826   2945   -240    305  -1197       O  
HETATM 3900  O   HOH A 279       7.206  44.211  20.222  1.00 28.87           O  
ANISOU 3900  O   HOH A 279     3780   3328   3207   1439   1215    160       O  
HETATM 3901  O   HOH A 280      17.117  40.997   0.595  1.00 27.96           O  
ANISOU 3901  O   HOH A 280     4083   4544   1364   -307   -619    268       O  
HETATM 3902  O   HOH A 281      31.764  31.098  -0.531  1.00 41.60           O  
ANISOU 3902  O   HOH A 281     4059   4950   5857   1865   2948   1627       O  
HETATM 3903  O   HOH A 282      25.332  26.210  15.518  0.49 11.56           O  
ANISOU 3903  O   HOH A 282     2135   1177    820   -208    241   -118       O  
HETATM 3904  O   HOH A 283       1.810  30.928  14.930  0.50 11.64           O  
ANISOU 3904  O   HOH A 283     1526   1902    731    283    213     31       O  
HETATM 3905  O   HOH A 284       6.804  15.319  14.112  1.00 48.32           O  
ANISOU 3905  O   HOH A 284     8077   3474   5714  -1133   1575  -1799       O  
HETATM 3906  O   HOH A 285       6.979  45.687   9.093  1.00 33.91           O  
ANISOU 3906  O   HOH A 285     2852   1876   7390    927   1318   1076       O  
HETATM 3907  O   HOH A 286      29.174  37.923   8.073  1.00 33.50           O  
ANISOU 3907  O   HOH A 286     2538   2713   6718   -303  -2134    498       O  
HETATM 3908  O   HOH A 287      31.967  35.086   0.836  1.00 55.43           O  
ANISOU 3908  O   HOH A 287     3606   7287   8912  -1422   2355   2643       O  
HETATM 3909  O  BHOH A 288      23.202  27.185  19.448  0.51  9.25           O  
ANISOU 3909  O  BHOH A 288     1112   1230    964   -111   -172     54       O  
HETATM 3910  O   HOH A 289      13.089  42.579  20.619  1.00  9.33           O  
ANISOU 3910  O   HOH A 289     1517    921    895     42     91     17       O  
HETATM 3911  O   HOH A 290      24.721  20.448   3.598  1.00 24.90           O  
ANISOU 3911  O   HOH A 290     2179   3542   3178    275   -590  -1620       O  
HETATM 3912  O   HOH A 291      23.254  40.248   8.026  1.00 14.29           O  
ANISOU 3912  O   HOH A 291     2104   1195   1805   -348   -188    -48       O  
HETATM 3913  O   HOH A 292      27.246  16.075  13.086  1.00 26.45           O  
ANISOU 3913  O   HOH A 292     3519   2126   3808   1903   1373    258       O  
HETATM 3914  O   HOH A 293       4.524  21.114  11.743  1.00 25.74           O  
ANISOU 3914  O   HOH A 293     5009   2459   1728    122  -1135   -216       O  
HETATM 3915  O   HOH A 294       7.313  26.382   3.467  1.00 26.58           O  
ANISOU 3915  O   HOH A 294     5760   2220   1519   1478    295   -187       O  
HETATM 3916  O   HOH A 295      -3.141  37.802  19.184  1.00 21.81           O  
ANISOU 3916  O   HOH A 295     1247   2623   3924     70   -547    885       O  
HETATM 3917  O   HOH A 296      -0.450  20.887  23.518  1.00 26.23           O  
ANISOU 3917  O   HOH A 296     3378   2100   3894    370   2055    375       O  
HETATM 3918  O   HOH A 297       5.931  31.575  -3.174  1.00 33.68           O  
ANISOU 3918  O   HOH A 297     4952   6146    937  -3351   -142   -299       O  
HETATM 3919  O   HOH A 298       2.680  44.048   6.620  1.00 62.28           O  
ANISOU 3919  O   HOH A 298     3886   7077  11292   1472  -1444   5209       O  
HETATM 3920  O   HOH A 299      10.810  39.714   1.920  1.00 26.91           O  
ANISOU 3920  O   HOH A 299     4669   2762   2185   -872    -28    397       O  
HETATM 3921  O   HOH A 300      29.941  25.066   0.753  1.00 48.41           O  
ANISOU 3921  O   HOH A 300     7109   3672   6516    829   4599   -356       O  
HETATM 3922  O   HOH A 301      25.239  30.080  -6.033  1.00 62.53           O  
ANISOU 3922  O   HOH A 301     6037  11789   4516   2861   1798   2616       O  
HETATM 3923  O   HOH A 302      -0.946  20.211  19.352  0.50 22.97           O  
ANISOU 3923  O   HOH A 302     2832   2704   2671   -314    246   -581       O  
HETATM 3924  O   HOH A 303      22.792  36.100  20.556  1.00 38.40           O  
ANISOU 3924  O   HOH A 303     2838   2960   7924  -1284   2755  -1811       O  
HETATM 3925  O   HOH A 304       2.221  21.233  16.251  1.00 17.74           O  
ANISOU 3925  O   HOH A 304     1887   2081   2372   -906     26   -535       O  
HETATM 3926  O   HOH A 305       1.477  34.067   9.379  1.00 21.40           O  
ANISOU 3926  O   HOH A 305     2309   3576   1762   1664    280    331       O  
HETATM 3927  O   HOH A 306       9.004  24.542   7.485  1.00 15.93           O  
ANISOU 3927  O   HOH A 306     1596   2547   1548  -1027   -506    436       O  
HETATM 3928  O   HOH A 307      10.551  38.796  -0.668  1.00 21.51           O  
ANISOU 3928  O   HOH A 307     3169   2255   2262    635   -246   -136       O  
HETATM 3929  O  BHOH A 308      20.702  27.574  18.444  0.51  5.26           O  
ANISOU 3929  O  BHOH A 308      729    613    540     40    -32    -16       O  
HETATM 3930  O   HOH A 309      21.467  38.556  11.601  1.00  9.47           O  
ANISOU 3930  O   HOH A 309     1597    988    800   -159    142     10       O  
HETATM 3931  O   HOH A 310       8.731  28.781  -1.204  1.00 20.45           O  
ANISOU 3931  O   HOH A 310     2558   3559   1191    971   -558   -809       O  
HETATM 3932  O   HOH A 311      25.405  36.934  11.282  1.00 49.80           O  
ANISOU 3932  O   HOH A 311     2769  11770   3256    -87  -1135  -2632       O  
HETATM 3933  O   HOH A 312      23.395  38.085  -6.512  1.00 48.33           O  
ANISOU 3933  O   HOH A 312     5535   7027   4708   -424   1432   4056       O  
HETATM 3934  O   HOH A 313       9.869  45.610  15.849  1.00 27.20           O  
ANISOU 3934  O   HOH A 313     2020   1675   6024    181    851   -287       O  
HETATM 3935  O   HOH A 314      27.348  34.201  -4.434  1.00 44.75           O  
ANISOU 3935  O   HOH A 314     4672   5787   5534    839  -1664   -723       O  
HETATM 3936  O   HOH A 315      12.430  21.410   5.095  0.50 32.62           O  
ANISOU 3936  O   HOH A 315     3220   4461   3976   -149    524   -832       O  
HETATM 3937  O   HOH A 316      25.169  18.947   5.885  1.00 14.13           O  
ANISOU 3937  O   HOH A 316     2568   1276   1204   -187    318   -437       O  
HETATM 3938  O   HOH A 317       6.889  22.216  11.773  1.00 20.85           O  
ANISOU 3938  O   HOH A 317     2730   2552   2167    649    533    225       O  
HETATM 3939  O   HOH A 318      22.474  41.150   0.716  1.00 23.38           O  
ANISOU 3939  O   HOH A 318     3747   2677   1930    541    780    803       O  
HETATM 3940  O   HOH A 319      25.980  13.955  13.663  0.50 37.56           O  
ANISOU 3940  O   HOH A 319     2643   3855   6921   1566  -2577  -2511       O  
HETATM 3941  O   HOH A 320      29.697  35.294  10.056  1.00 40.72           O  
ANISOU 3941  O   HOH A 320     3127   7236   4189    266  -2059  -1292       O  
HETATM 3942  O   HOH A 321       3.686  37.924  31.377  1.00 29.56           O  
ANISOU 3942  O   HOH A 321     5022   2366   3174    888    901      7       O  
HETATM 3943  O   HOH A 322       4.770  37.675   6.260  1.00 22.90           O  
ANISOU 3943  O   HOH A 322     2530   3374   2278    820    270   -463       O  
HETATM 3944  O   HOH A 323       2.878  21.967   8.844  1.00 45.82           O  
ANISOU 3944  O   HOH A 323     3631   7414   5328  -2049   1050  -1285       O  
HETATM 3945  O   HOH A 324      27.794  25.597   2.308  1.00 18.74           O  
ANISOU 3945  O   HOH A 324     2520   2359   1817    967    572    291       O  
HETATM 3946  O   HOH A 325      16.427  21.761   1.567  1.00  8.81           O  
ANISOU 3946  O   HOH A 325     1423    970    756     32      2    -88       O  
HETATM 3947  O   HOH A 326      27.927  32.597  14.491  1.00 58.70           O  
ANISOU 3947  O   HOH A 326     4328  13505   3141  -3526    155  -1513       O  
HETATM 3948  O  BHOH A 327      -3.792  30.631  19.714  0.50 23.41           O  
ANISOU 3948  O  BHOH A 327     2135   3224   3006    719  -1120    611       O  
HETATM 3949  O   HOH A 328      -2.415  23.728  12.335  1.00 55.92           O  
ANISOU 3949  O   HOH A 328     3582  13883   2518   2186   -597   -896       O  
HETATM 3950  O   HOH A 329      27.690  30.602  -5.681  1.00 48.63           O  
ANISOU 3950  O   HOH A 329     9682   5251   2443  -2678    -20    236       O  
HETATM 3951  O   HOH A 330      13.004  45.351  11.899  1.00 12.00           O  
ANISOU 3951  O   HOH A 330     1828   1037   1422    161    281    111       O  
HETATM 3952  O  BHOH A 331      25.885  40.214  -0.695  1.00 32.81           O  
ANISOU 3952  O  BHOH A 331     6322   2488   2911   -480    537    607       O  
HETATM 3953  O   HOH A 332      29.702  34.131  -2.703  1.00 29.61           O  
ANISOU 3953  O   HOH A 332     3804   4108   2668    710   1984   1365       O  
HETATM 3954  O   HOH A 333      22.955  24.846  -3.486  0.50 31.57           O  
ANISOU 3954  O   HOH A 333     3664   3111   4506    268  -1865  -1601       O  
HETATM 3955  O   HOH A 334      -2.235  20.702  22.099  1.00 32.94           O  
ANISOU 3955  O   HOH A 334     2475   5433   3863   1957   1676   2776       O  
HETATM 3956  O   HOH A 335      -3.620  18.655  17.861  1.00 82.22           O  
ANISOU 3956  O   HOH A 335    12331  10231   6818   5484   5734    702       O  
HETATM 3957  O  BHOH A 336      -3.751  29.580  26.111  0.50 21.55           O  
ANISOU 3957  O  BHOH A 336     1757   2405   3539    452  -1360   -839       O  
HETATM 3958  O   HOH A 337      12.400  22.871   5.985  0.50 17.30           O  
ANISOU 3958  O   HOH A 337     2281   2107   1794    552     90    -56       O  
HETATM 3959  O   HOH A 338      32.751  34.335  10.005  1.00 70.03           O  
ANISOU 3959  O   HOH A 338     7219   6511  11294   3759  -2502   1985       O  
HETATM 3960  O  CHOH A 339      34.165  36.947   6.732  0.50 36.22           O  
ANISOU 3960  O  CHOH A 339     4095   3579   5268   -914  -1462   1915       O  
HETATM 3961  O   HOH A 340       2.513  28.798   7.758  1.00 60.66           O  
ANISOU 3961  O   HOH A 340     3653   5792  12229  -2324  -4000   2995       O  
HETATM 3962  O   HOH A 341       8.985  23.449   4.887  1.00 38.58           O  
ANISOU 3962  O   HOH A 341     5384   6004   2397  -3714   -231   -540       O  
HETATM 3963  O   HOH A 342      31.670  37.880   5.283  0.50 34.60           O  
ANISOU 3963  O   HOH A 342     2772   4144   5446   -622    386    774       O  
HETATM 3964  O   HOH A 343      29.767  18.666   2.766  1.00 61.30           O  
ANISOU 3964  O   HOH A 343    11304   3011   7590   1382   1425   -595       O  
HETATM 3965  O   HOH A 344       0.596  30.645   8.790  1.00 43.15           O  
ANISOU 3965  O   HOH A 344     3808   4481   7131  -1014  -1646    -69       O  
HETATM 3966  O   HOH A 345       2.379  21.811  23.951  1.00 31.52           O  
ANISOU 3966  O   HOH A 345     3529   5808   1928    207    891    600       O  
HETATM 3967  O   HOH A 346      23.677  14.318  18.372  1.00 30.71           O  
ANISOU 3967  O   HOH A 346     3044   5011   2918  -2229  -1597   2709       O  
HETATM 3968  O   HOH A 347      -1.243  20.513  13.382  0.50 40.79           O  
ANISOU 3968  O   HOH A 347     2631   4995   6948  -1157  -1728   2486       O  
HETATM 3969  O   HOH A 348      -1.191  31.178  18.319  1.00 38.62           O  
ANISOU 3969  O   HOH A 348     5729   4458   3613  -2337  -1342   1031       O  
HETATM 3970  O   HOH A 349      25.607  24.395  -1.376  1.00 62.42           O  
ANISOU 3970  O   HOH A 349     8765   6822   6718   3456   3293   -702       O  
HETATM 3971  O  BHOH A 350       1.386  42.526  14.843  0.50 25.79           O  
ANISOU 3971  O  BHOH A 350     3677   2170   3369    911   1536   -680       O  
HETATM 3972  O   HOH A 351      33.347  24.410   3.158  1.00 35.32           O  
ANISOU 3972  O   HOH A 351     4127   2502   5991    986    419    153       O  
HETATM 3973  O  CHOH A 352      29.805  26.273  14.814  0.50 17.58           O  
ANISOU 3973  O  CHOH A 352     1772   2250   2259    560   -677    369       O  
HETATM 3974  O   HOH A 353      13.614  39.078  -2.780  0.50 44.69           O  
ANISOU 3974  O   HOH A 353     5263   5592   5114     45  -1077  -2883       O  
HETATM 3975  O   HOH A 354      13.111  32.756  -6.841  1.00 65.89           O  
ANISOU 3975  O   HOH A 354    10146   7989   5410   2595    950  -3996       O  
HETATM 3976  O   HOH A 355      18.649  35.070  -5.837  1.00 66.86           O  
ANISOU 3976  O   HOH A 355    10084   5747   8058  -3728   5544  -3779       O  
HETATM 3977  O   HOH A 356      26.001  14.014  16.512  1.00 45.38           O  
ANISOU 3977  O   HOH A 356     3446   3475   9293   -280  -1005   2739       O  
HETATM 3978  O   HOH A 357       4.796  27.431  -0.784  1.00 54.52           O  
ANISOU 3978  O   HOH A 357     6987   5808   6687   2058   3930   2007       O  
HETATM 3979  O   HOH A 358       3.809  16.153  16.180  1.00 70.43           O  
ANISOU 3979  O   HOH A 358     5606  10361   9198  -3997  -1711    951       O  
HETATM 3980  O   HOH A 359       7.218  23.073   9.067  1.00 29.69           O  
ANISOU 3980  O   HOH A 359     3647   4873   2090  -2491    338   -365       O  
HETATM 3981  O  BHOH A 360       8.762  21.820  13.846  0.51 16.00           O  
ANISOU 3981  O  BHOH A 360     2117   2312   1288   -332    491    -24       O  
HETATM 3982  O   HOH A 361      25.928  41.735   2.562  1.00 52.26           O  
ANISOU 3982  O   HOH A 361     7484   3227   7962    931   4915    388       O  
HETATM 3983  O   HOH A 362       2.882  46.149  14.766  1.00 67.99           O  
ANISOU 3983  O   HOH A 362     8781   6341   9175   3486   3044  -2439       O  
HETATM 3984  O   HOH A 363      12.546  38.573  -5.194  1.00 69.13           O  
ANISOU 3984  O   HOH A 363    12735   5156   6812  -2756   4428    599       O  
HETATM 3985  O   HOH A 364       5.557  45.740  11.837  1.00 74.97           O  
ANISOU 3985  O   HOH A 364    12484   3468  10837    620    475   3360       O  
HETATM 3986  O   HOH A 365       2.650  44.637  11.160  0.50 29.73           O  
ANISOU 3986  O   HOH A 365     5133   3027   2464    713    770    115       O  
HETATM 3987  O   HOH A 366       8.189  44.573  13.700  1.00 25.99           O  
ANISOU 3987  O   HOH A 366     3354   3077   2858    923   -186    162       O  
HETATM 3988  O  BHOH A 367      24.432  24.803  18.664  0.50 14.23           O  
ANISOU 3988  O  BHOH A 367     1329   1976   1779    -32   -230   -637       O  
HETATM 3989  O   HOH A 368      -0.800  41.123  20.618  1.00 36.58           O  
ANISOU 3989  O   HOH A 368     5124   4670   3277    298  -1034    206       O  
HETATM 3990  O   HOH A 369       3.595  29.535   2.816  1.00 30.73           O  
ANISOU 3990  O   HOH A 369     3145   4688   3147      6  -1349    132       O  
HETATM 3991  O   HOH A 370      16.124  18.247   4.553  1.00 59.78           O  
ANISOU 3991  O   HOH A 370     9811   3650   7900   1933    697  -1127       O  
HETATM 3992  O   HOH A 371       7.435  19.066  10.203  0.50 38.11           O  
ANISOU 3992  O   HOH A 371     6172   3877   3569  -1675   1444  -1411       O  
HETATM 3993  O   HOH A 372      25.829  41.512   8.242  1.00 38.34           O  
ANISOU 3993  O   HOH A 372     4591   4648   4462  -2181  -1336    731       O  
HETATM 3994  O  CHOH A 373       1.099  43.268  16.063  0.50  8.46           O  
ANISOU 3994  O  CHOH A 373      795    991   1238    464     35    155       O  
HETATM 3995  O   HOH A 374       3.302  44.635   3.019  0.50 43.01           O  
ANISOU 3995  O   HOH A 374     2817   3880   8673   -423   -199  -1733       O  
HETATM 3996  O   HOH A 375       0.915  41.409  13.430  1.00 36.65           O  
ANISOU 3996  O   HOH A 375     6653   2507   3938    538   3034   -211       O  
HETATM 3997  O   HOH A 376      15.811  33.040  -7.333  1.00 94.05           O  
ANISOU 3997  O   HOH A 376    12666  15266   5674   4519  -4000   3826       O  
HETATM 3998  O   HOH A 377      -1.056  34.072  28.521  1.00 42.20           O  
ANISOU 3998  O   HOH A 377     1981   9040   4056   -459   1039  -1848       O  
HETATM 3999  O   HOH A 378      26.694  41.072  -3.337  0.50 47.42           O  
ANISOU 3999  O   HOH A 378     5513   4553   6879  -2129    140  -2011       O  
HETATM 4000  O   HOH A 379       0.279  28.906  16.079  1.00 19.85           O  
ANISOU 4000  O   HOH A 379     2331   3012   1748    337   -349    999       O  
HETATM 4001  O   HOH A 380      27.512  18.070   6.866  1.00 38.45           O  
ANISOU 4001  O   HOH A 380     3422   5365   4953   1740   -217   1489       O  
HETATM 4002  O   HOH A 381       2.699  37.083   5.475  1.00 73.26           O  
ANISOU 4002  O   HOH A 381    11504  11589   3085   5045   -976   2024       O  
HETATM 4003  O   HOH A 382      -4.389  35.348  17.875  1.00 65.99           O  
ANISOU 4003  O   HOH A 382     6447   7362   9771  -3426  -2622   2578       O  
HETATM 4004  O   HOH A 383      27.541  14.976  10.457  1.00 71.99           O  
ANISOU 4004  O   HOH A 383     5202   7035  13486  -3586   -587   1439       O  
HETATM 4005  O   HOH A 384       2.280  39.238  28.415  1.00 64.43           O  
ANISOU 4005  O   HOH A 384     5319   7460  10242   3275    450  -3227       O  
HETATM 4006  O   HOH A 385      27.402  41.822   5.643  1.00 53.81           O  
ANISOU 4006  O   HOH A 385     5330   7074   6823  -3931   -294   1610       O  
HETATM 4007  O   HOH A 386      16.067  36.185  -4.780  1.00 56.78           O  
ANISOU 4007  O   HOH A 386     8208   7458   4623  -2327  -1312   3352       O  
HETATM 4008  O  DHOH A 387      26.098  27.382  17.564  1.00 38.25           O  
ANISOU 4008  O  DHOH A 387     6191   4337   3141    498  -1624   -139       O  
HETATM 4009  O   HOH A 388      31.893  22.053  -1.804  0.50 41.74           O  
ANISOU 4009  O   HOH A 388     4233   7796   2886    814    457   -360       O  
HETATM 4010  O   HOH A 389      22.754  41.669  -3.251  1.00 40.36           O  
ANISOU 4010  O   HOH A 389     4613   4613   5196   -756     -2   2182       O  
HETATM 4011  O   HOH A 390       9.359  43.974  23.473  1.00 74.22           O  
ANISOU 4011  O   HOH A 390    15373   1154   9995   1053   4437   1144       O  
HETATM 4012  O   HOH A 391       4.166  37.359   3.732  1.00 86.63           O  
ANISOU 4012  O   HOH A 391     5858  10675  14422   1586   5649  -4000       O  
HETATM 4013  O   HOH A 392      -2.805  29.175  16.207  1.00 54.48           O  
ANISOU 4013  O   HOH A 392     7251   7119   5098   3392  -3216   -293       O  
HETATM 4014  O   HOH A 393      29.125  42.974  -0.013  0.50 56.02           O  
ANISOU 4014  O   HOH A 393     3778  10531   5709   -710      0      0       O  
HETATM 4015  O   HOH A 394      20.037  48.375   5.258  1.00 42.89           O  
ANISOU 4015  O   HOH A 394     4134   3570   7622     45   -505   -537       O  
HETATM 4016  O   HOH A 395      27.881  15.883  15.493  1.00 34.37           O  
ANISOU 4016  O   HOH A 395     1895   3258   7127   -826  -1638   1575       O  
HETATM 4017  O  CHOH A 396      22.844  34.362  12.201  0.50 18.20           O  
ANISOU 4017  O  CHOH A 396     2607   1839   2056   -690  -1200    641       O  
HETATM 4018  O   HOH A 397      14.151  21.520   0.096  1.00 14.39           O  
ANISOU 4018  O   HOH A 397     2245   1618   1279   -403   -665    326       O  
HETATM 4019  O   HOH A 398      25.623  24.086   1.450  1.00 30.41           O  
ANISOU 4019  O   HOH A 398     2467   3881   4519    803   -746   -955       O  
HETATM 4020  O   HOH A 399      33.405  22.107   5.053  1.00 25.65           O  
ANISOU 4020  O   HOH A 399     4266   2392   2508   1224    150   -361       O  
HETATM 4021  O   HOH A 400      -0.060  25.618  12.013  1.00 37.24           O  
ANISOU 4021  O   HOH A 400     3372   5725   4211   -641  -1957   1115       O  
HETATM 4022  O   HOH A 401       5.939  46.307  16.235  1.00 51.52           O  
ANISOU 4022  O   HOH A 401     6151   2687   9570   1522   4275   2005       O  
HETATM 4023  O   HOH A 402      11.338  44.394  21.673  1.00 27.60           O  
ANISOU 4023  O   HOH A 402     3334   2264   4265     78   1847  -1244       O  
HETATM 4024  O   HOH A 403      29.836  36.749   2.654  1.00 37.95           O  
ANISOU 4024  O   HOH A 403     3094   5183   5282   -230   1072   2344       O  
HETATM 4025  O   HOH A 404      10.454  48.232   4.263  1.00 77.66           O  
ANISOU 4025  O   HOH A 404     9061   8798   9893   5248   3931    440       O  
HETATM 4026  O   HOH A 405       1.864  36.773  30.036  1.00 37.10           O  
ANISOU 4026  O   HOH A 405     4440   3024   5792   -747   2105  -1670       O  
HETATM 4027  O   HOH A 406      -0.988  29.474  27.027  1.00 33.98           O  
ANISOU 4027  O   HOH A 406     2458   7050   2633   -494   1270   -844       O  
HETATM 4028  O   HOH A 407       9.274  46.215  18.212  1.00 46.68           O  
ANISOU 4028  O   HOH A 407     5817   2082   8783    646   4419     77       O  
HETATM 4029  O   HOH A 408      27.547  25.634  17.025  0.50 14.72           O  
ANISOU 4029  O   HOH A 408     2268   1785   1206    517    318    207       O  
HETATM 4030  O   HOH A 409      29.366  17.480  11.058  1.00 37.86           O  
ANISOU 4030  O   HOH A 409     3227   7228   3075   1968  -1522  -1220       O  
HETATM 4031  O   HOH A 410      31.753  26.033  -0.254  1.00 83.09           O  
ANISOU 4031  O   HOH A 410     7532   9913  12244   3569  -2995   4675       O  
HETATM 4032  O   HOH A 411      16.331  16.312   6.613  1.00 47.80           O  
ANISOU 4032  O   HOH A 411     5103   8477   3500   -413   -612   -434       O  
HETATM 4033  O   HOH A 412       0.087  32.905  14.081  1.00 32.05           O  
ANISOU 4033  O   HOH A 412     3630   5372   2451   2189   -157    -23       O  
HETATM 4034  O   HOH A 413       0.000  42.974  14.784  0.50 40.39           O  
ANISOU 4034  O   HOH A 413     3949   5005   5479   1669      0      0       O  
HETATM 4035  O   HOH A 414      22.451  27.490  -6.532  1.00 50.45           O  
ANISOU 4035  O   HOH A 414     6984   6374   4670  -3927   3334  -3383       O  
HETATM 4036  O   HOH A 415      -6.250  35.350  24.417  1.00 20.90           O  
ANISOU 4036  O   HOH A 415     2226   1699   3543     -6    413    250       O  
HETATM 4037  O   HOH A 416      -0.522  28.681   5.183  1.00 70.64           O  
ANISOU 4037  O   HOH A 416     5401   8528  11314  -2993  -2232  -1453       O  
HETATM 4038  O   HOH A 417      -4.150  31.962  25.820  1.00 15.25           O  
ANISOU 4038  O   HOH A 417     1787   2029   1633   -136    -11   -172       O  
HETATM 4039  O   HOH A 418       9.842  42.034   2.252  1.00 42.60           O  
ANISOU 4039  O   HOH A 418     4749   6662   3809   -996   -500   2188       O  
HETATM 4040  O   HOH A 419      22.500  37.581  15.868  0.50 30.11           O  
ANISOU 4040  O   HOH A 419     3491   3635   3634  -1746  -1198    114       O  
HETATM 4041  O   HOH A 420      16.683  38.402  -0.812  1.00 18.71           O  
ANISOU 4041  O   HOH A 420     2599   1978   2107    457    303    270       O  
HETATM 4042  O   HOH A 421      -4.845  36.960  21.397  1.00 55.01           O  
ANISOU 4042  O   HOH A 421     3831   5379  10447    732   3010   2874       O  
HETATM 4043  O   HOH A 422      29.519  24.461  -1.683  0.50 32.85           O  
ANISOU 4043  O   HOH A 422     3695   2961   5081   -821   -536    304       O  
HETATM 4044  O   HOH A 423      24.767  34.547  -6.984  0.50 45.16           O  
ANISOU 4044  O   HOH A 423     9601   2982   3555  -1856   1825    439       O  
HETATM 4045  O   HOH A 424       0.352  35.330  32.357  1.00 56.96           O  
ANISOU 4045  O   HOH A 424     6790   5842   7723   -199   2961  -1013       O  
HETATM 4046  O   HOH A 425      13.439  40.595  -1.066  1.00 52.16           O  
ANISOU 4046  O   HOH A 425     4752   6615   7273   1963   1680   3360       O  
HETATM 4047  O   HOH A 426      -1.887  31.931  27.496  1.00 33.25           O  
ANISOU 4047  O   HOH A 426     2042   7559   2280   -952    -75   -399       O  
HETATM 4048  O   HOH A 427       1.947  21.822  13.616  1.00 30.83           O  
ANISOU 4048  O   HOH A 427     4814   2828   3373  -1384   -683   -360       O  
HETATM 4049  O  BHOH A 428      25.459  19.151   3.069  1.00 37.46           O  
ANISOU 4049  O  BHOH A 428     5601   4832   2952   -542    139  -1835       O  
HETATM 4050  O   HOH A 429      -3.411  30.996  17.835  1.00 48.22           O  
ANISOU 4050  O   HOH A 429     6680   5761   4787  -2025  -3065    678       O  
HETATM 4051  O   HOH A 430       0.043  33.180   2.325  1.00 44.17           O  
ANISOU 4051  O   HOH A 430     3402   8945   3435   1286   -155   2064       O  
HETATM 4052  O   HOH A 431      -2.072  29.480  12.928  1.00 89.04           O  
ANISOU 4052  O   HOH A 431     3673  12211  15933  -3743   3207   -560       O  
HETATM 4053  O   HOH A 432      24.280  41.648  -1.543  1.00 70.75           O  
ANISOU 4053  O   HOH A 432     8435   6029  10817   3654  -3640  -2375       O  
HETATM 4054  O   HOH A 433       0.852  36.232   7.861  1.00 34.73           O  
ANISOU 4054  O   HOH A 433     4029   4097   4283   1724    -96   1324       O  
HETATM 4055  O   HOH A 434      -4.355  39.155  23.697  1.00 52.06           O  
ANISOU 4055  O   HOH A 434     5033   4448   9122    618    442   1795       O  
HETATM 4056  O   HOH A 435      24.780  21.985  -1.570  1.00 61.22           O  
ANISOU 4056  O   HOH A 435     3442  10701   7731   1787   -209  -2726       O  
HETATM 4057  O   HOH A 436       3.680  30.685  -3.039  1.00 50.30           O  
ANISOU 4057  O   HOH A 436     2867   9453   5653   -510   -524   -471       O  
HETATM 4058  O   HOH A 437      25.885  33.603  17.815  1.00 72.74           O  
ANISOU 4058  O   HOH A 437     6176   8115  11700   1328  -4000  -3360       O  
HETATM 4059  O   HOH A 438      18.740  15.577   5.381  1.00 54.26           O  
ANISOU 4059  O   HOH A 438     9059   5407   4923  -4000   -529  -1620       O  
HETATM 4060  O   HOH A 439      34.731  24.759   1.379  1.00 80.27           O  
ANISOU 4060  O   HOH A 439    11684  11106   5892   4576  -2591  -3202       O  
HETATM 4061  O   HOH A 440      15.744  38.425  -3.331  1.00 32.90           O  
ANISOU 4061  O   HOH A 440     2695   6721   2339   -116    -44   1015       O  
HETATM 4062  O   HOH A 441      26.221  14.073   8.829  0.50 38.21           O  
ANISOU 4062  O   HOH A 441     7641   2713   3301    592  -1171   -900       O  
HETATM 4063  O  CHOH A 442      25.214  26.287  16.893  0.50 21.34           O  
ANISOU 4063  O  CHOH A 442     3576   2623   1427  -1060   -668   -181       O  
HETATM 4064  O   HOH A 443      18.509  40.492  -1.140  1.00 43.60           O  
ANISOU 4064  O   HOH A 443     5324   6807   3447   3055    471   1527       O  
HETATM 4065  O   HOH A 444       1.063  21.968  10.245  1.00 62.50           O  
ANISOU 4065  O   HOH A 444    10646   6272   5413  -3076   3796  -1044       O  
HETATM 4066  O   HOH A 445      12.538  15.216   8.894  1.00 40.92           O  
ANISOU 4066  O   HOH A 445     6436   5541   2646  -2417    454  -1918       O  
HETATM 4067  O   HOH A 446      -5.838  34.408  20.311  1.00 33.23           O  
ANISOU 4067  O   HOH A 446     2332   3066   6476   -555   -819   1174       O  
HETATM 4068  O   HOH A 447      -1.501  41.369  24.135  1.00 53.06           O  
ANISOU 4068  O   HOH A 447     4524   7954   6483   1388    880   -448       O  
HETATM 4069  O   HOH A 448      22.994  40.887  12.034  1.00 37.50           O  
ANISOU 4069  O   HOH A 448     3602   2322   7476   -634   1413   -365       O  
HETATM 4070  O   HOH A 449      23.437  15.383   7.369  1.00 53.84           O  
ANISOU 4070  O   HOH A 449     4816   4226  10197    264  -1959  -3734       O  
HETATM 4071  O   HOH A 450      -3.960  40.391  21.359  1.00 69.01           O  
ANISOU 4071  O   HOH A 450     6582   5753  12325    497  -2955   -736       O  
HETATM 4072  O   HOH A 451      -0.245  36.543  12.411  1.00 61.68           O  
ANISOU 4072  O   HOH A 451     2608  10435   8995   -444   1048   2928       O  
HETATM 4073  O   HOH A 452       9.506  16.071   8.195  0.50 41.16           O  
ANISOU 4073  O   HOH A 452     7279   2228   5200   -690    449   -962       O  
HETATM 4074  O   HOH A 453       0.354  44.429  15.781  0.50 14.78           O  
ANISOU 4074  O   HOH A 453     1451   1984   1849    886   -470   -805       O  
HETATM 4075  O   HOH A 454       1.375  30.846   1.660  1.00 34.70           O  
ANISOU 4075  O   HOH A 454     3323   6032   3043    359   -674     73       O  
HETATM 4076  O   HOH A 455      34.319  32.241   2.334  0.50 34.80           O  
ANISOU 4076  O   HOH A 455     2777   5688   3970    879    109   1866       O  
HETATM 4077  O   HOH A 456      22.971  19.492   1.654  1.00 22.93           O  
ANISOU 4077  O   HOH A 456     2487   3830   1876    995   -423   -346       O  
HETATM 4078  O   HOH A 457      13.115  48.048  11.581  1.00 12.59           O  
ANISOU 4078  O   HOH A 457     1725    879   1894   -170   -205   -217       O  
HETATM 4079  O   HOH A 458      27.858  18.185   4.346  1.00 67.50           O  
ANISOU 4079  O   HOH A 458    12070   4548   7503   2664   5447   1425       O  
HETATM 4080  O   HOH A 459      34.937  30.658   4.355  1.00 30.63           O  
ANISOU 4080  O   HOH A 459     2148   5117   3681  -1140    399   1549       O  
HETATM 4081  O   HOH A 460       4.511  28.156  -3.611  1.00 70.06           O  
ANISOU 4081  O   HOH A 460    12168   6048   6819    -81    869  -3774       O  
HETATM 4082  O   HOH A 461      15.313  42.592  -0.975  1.00 47.95           O  
ANISOU 4082  O   HOH A 461    10350   2977   3808    840  -3339    -20       O  
HETATM 4083  O   HOH A 462      18.593  46.219   2.065  1.00 37.21           O  
ANISOU 4083  O   HOH A 462     7566   2873   2859    537   1090    685       O  
HETATM 4084  O   HOH A 463       7.648  48.052   7.927  1.00 55.26           O  
ANISOU 4084  O   HOH A 463     6520   8935   4290  -1230   -622   1685       O  
HETATM 4085  O   HOH A 464      30.307  18.540   5.588  1.00 33.88           O  
ANISOU 4085  O   HOH A 464     4617   2973   4518    919  -1722   -851       O  
HETATM 4086  O   HOH A 465      14.661  16.557   5.097  1.00 55.30           O  
ANISOU 4086  O   HOH A 465     8461   3710   7590   -948   -495    918       O  
HETATM 4087  O   HOH A 466      32.698  28.476  -0.586  1.00 53.43           O  
ANISOU 4087  O   HOH A 466     3376   7012   8705   1593   2327   -995       O  
HETATM 4088  O   HOH A 467       0.392  34.414  11.838  1.00 33.29           O  
ANISOU 4088  O   HOH A 467     3784   4978   3131    722   1317    204       O  
HETATM 4089  O   HOH A 468      -5.728  33.125  27.642  1.00 19.36           O  
ANISOU 4089  O   HOH A 468     1740   2950   2227    158    -64   -560       O  
HETATM 4090  O   HOH A 469      34.992  29.748   1.907  1.00 43.87           O  
ANISOU 4090  O   HOH A 469     3893   7069   4715   -146    940   3686       O  
HETATM 4091  O  CHOH A 470      -1.469  34.524  15.132  0.50 37.01           O  
ANISOU 4091  O  CHOH A 470     5914   4556   2754   2816   -373    333       O  
HETATM 4092  O   HOH A 471      11.091  44.553   1.307  1.00 60.12           O  
ANISOU 4092  O   HOH A 471    10653   4840   5988   3348  -2544  -1191       O  
HETATM 4093  O   HOH A 472      21.232  49.959   6.610  1.00 83.26           O  
ANISOU 4093  O   HOH A 472    13276   6370  10105    933  -3346  -4000       O  
HETATM 4094  O   HOH A 473       0.991  35.786   2.726  1.00 40.01           O  
ANISOU 4094  O   HOH A 473     4698   4416   5185   1370    432     -9       O  
HETATM 4095  O  BHOH A 474      31.706  20.848   6.746  0.50 16.31           O  
ANISOU 4095  O  BHOH A 474     1807   1644   2377    359    611   -737       O  
HETATM 4096  O   HOH A 475      22.950  17.175   6.025  1.00 21.05           O  
ANISOU 4096  O   HOH A 475     3602   1876   2042   -720     13   -194       O  
HETATM 4097  O  CHOH A 476       0.402  36.879  31.265  0.50 42.95           O  
ANISOU 4097  O  CHOH A 476     5776   3361   6211  -1660   1894   -416       O  
HETATM 4098  O   HOH A 477      26.712  11.215  16.226  1.00 56.64           O  
ANISOU 4098  O   HOH A 477    10597   3408   6232    418  -3310   -522       O  
HETATM 4099  O   HOH A 478      26.243  14.685   6.615  1.00 88.81           O  
ANISOU 4099  O   HOH A 478    10728   9117  11889   2990   4105  -4000       O  
HETATM 4100  O   HOH A 479      12.118  46.690   2.430  1.00 49.02           O  
ANISOU 4100  O   HOH A 479     4526   5737   7254  -1478   -469  -1052       O  
HETATM 4101  O  CHOH A 480      26.979  19.020   2.248  0.50 35.74           O  
ANISOU 4101  O  CHOH A 480     4517   5545   2710  -1107    360   -718       O  
HETATM 4102  O   HOH A 481      17.830  47.627   3.878  1.00 28.90           O  
ANISOU 4102  O   HOH A 481     4846   1981   3499    267    471    615       O  
HETATM 4103  O   HOH A 482      28.302  14.738  17.488  1.00 31.98           O  
ANISOU 4103  O   HOH A 482     3560   3677   4189   -329    341   -512       O  
HETATM 4104  O   HOH A 483       1.249  30.514  -1.053  1.00 75.09           O  
ANISOU 4104  O   HOH A 483    10028   5690  11112   -366   3445   3235       O  
HETATM 4105  O   HOH A 484      29.620  24.285  18.541  1.00 17.20           O  
ANISOU 4105  O   HOH A 484     1608   2077   2460    211    465    -48       O  
HETATM 4106  O   HOH A 485      27.406  12.857  11.318  1.00 61.20           O  
ANISOU 4106  O   HOH A 485     5194  11455   5218    174    307   1875       O  
HETATM 4107  O   HOH A 486      20.093  16.170   2.715  1.00 42.97           O  
ANISOU 4107  O   HOH A 486     6841   4552   3960   1804  -2878   -443       O  
HETATM 4108  O   HOH A 487      -2.124  32.296  14.770  1.00 61.32           O  
ANISOU 4108  O   HOH A 487     3539   6388  11986    502   -205   1292       O  
HETATM 4109  O   HOH A 488      29.631  30.965  16.998  1.00 58.15           O  
ANISOU 4109  O   HOH A 488     8243   5647   6888  -2843   4105  -3303       O  
HETATM 4110  O   HOH A 489      18.019  17.502   1.466  1.00 34.04           O  
ANISOU 4110  O   HOH A 489     4726   1477   5962   -237   -126   1214       O  
HETATM 4111  O   HOH A 490      22.239  16.907   3.105  1.00 41.43           O  
ANISOU 4111  O   HOH A 490     5172   5613   4019   1450    759  -2010       O  
HETATM 4112  O  CHOH A 491      14.994  35.029  -9.002  0.50 34.78           O  
ANISOU 4112  O  CHOH A 491     5884   3212   3331    992   -899  -1527       O  
HETATM 4113  O   HOH A 492      -2.356  36.113  14.309  0.50 43.78           O  
ANISOU 4113  O   HOH A 492     6799   4623   4221   1522   -524  -1202       O  
HETATM 4114  O   HOH A 493      -7.924  34.361  26.512  1.00 17.99           O  
ANISOU 4114  O   HOH A 493     1640   2030   2759   -499   -392    676       O  
HETATM 4115  O   HOH A 494      -2.093  33.945  11.175  1.00 78.97           O  
ANISOU 4115  O   HOH A 494     5738  10943  11537   2989   2834  -1765       O  
HETATM 4116  O   HOH A 495      12.689  34.946 -10.346  0.50 21.75           O  
ANISOU 4116  O   HOH A 495     2790   2292   2690   -170    475    204       O  
HETATM 4117  O   HOH A 496      35.924  21.536   6.080  1.00 21.89           O  
ANISOU 4117  O   HOH A 496     3492   2861   1467   -828    -73     85       O  
HETATM 4118  O   HOH A 497      -8.057  35.933  28.574  1.00 48.52           O  
ANISOU 4118  O   HOH A 497     8181   4085   5072   1267   1951   -769       O  
HETATM 4119  O   HOH A 498      21.343  13.894   4.778  0.50 47.33           O  
ANISOU 4119  O   HOH A 498     5616   6802   4495   3449   -592  -1043       O  
HETATM 4120  O  CHOH A 499      -2.588  17.786  25.679  0.50 50.59           O  
ANISOU 4120  O  CHOH A 499     5365   6010   6702   2175   -880   2147       O  
HETATM 4121  O   HOH A 500      -6.211  31.067  29.671  1.00 29.51           O  
ANISOU 4121  O   HOH A 500     3009   5352   2183   1284     87    863       O  
HETATM 4122  O   HOH A 501      20.708  52.263   4.944  1.00 51.23           O  
ANISOU 4122  O   HOH A 501     4064   5916   8325    357   2225   -343       O  
HETATM 4123  O   HOH A 502      14.307  47.353   0.490  1.00 70.44           O  
ANISOU 4123  O   HOH A 502     8068   5962  11141   2570  -3949   1865       O  
HETATM 4124  O   HOH A 503       2.249  42.280  35.993  0.50 56.73           O  
ANISOU 4124  O   HOH A 503     4708   6955   8610  -3544    636   1741       O  
HETATM 4125  O   HOH A 504      16.889  49.734   2.485  1.00 57.52           O  
ANISOU 4125  O   HOH A 504    13384   4401   2767    342   -763    658       O  
HETATM 4126  O   HOH A 505      32.021  24.179  21.919  1.00 55.19           O  
ANISOU 4126  O   HOH A 505     5454  11200   3065   3090   1932     -1       O  
HETATM 4127  O   HOH B 201       8.365  15.043  21.111  1.00 49.36           O  
ANISOU 4127  O   HOH B 201     4290   4039   9310   -797  -3198   3440       O  
HETATM 4128  O   HOH B 202      24.921  18.788  28.709  0.37 12.54           O  
ANISOU 4128  O   HOH B 202     1154   1939   1389   -356    160   -496       O  
HETATM 4129  O   HOH B 203      18.376  17.237  38.853  0.50 49.13           O  
ANISOU 4129  O   HOH B 203     8865   6033   2657  -1735   -431  -2414       O  
HETATM 4130  O   HOH B 204       6.333  14.600  26.554  1.00 73.12           O  
ANISOU 4130  O   HOH B 204     6915  11047   8167  -2079  -4000  -4000       O  
HETATM 4131  O   HOH B 205       5.631  15.441  21.466  1.00 49.76           O  
ANISOU 4131  O   HOH B 205     8411   6846   2522  -4000  -1748   1496       O  
HETATM 4132  O   HOH B 206      19.442   3.041  26.080  1.00 46.50           O  
ANISOU 4132  O   HOH B 206     4238   2899   9478    139   -714   1732       O  
HETATM 4133  O   HOH B 207      10.796  24.722  45.383  1.00 13.82           O  
ANISOU 4133  O   HOH B 207     1440   2453   1044     62     27   -478       O  
HETATM 4134  O  BHOH B 208      23.914  22.509  29.619  1.00 48.31           O  
ANISOU 4134  O  BHOH B 208     5398   6615   5250   -522   1536   1297       O  
HETATM 4135  O   HOH B 209       9.544   7.659  35.733  1.00 31.21           O  
ANISOU 4135  O   HOH B 209     3973   3786   3391   1140    458   -253       O  
HETATM 4136  O   HOH B 210      16.530  15.803  11.149  0.50 30.19           O  
ANISOU 4136  O   HOH B 210     5790   2114   2883   1938  -2976  -2018       O  
HETATM 4137  O   HOH B 211       3.400   4.250  25.306  1.00 61.74           O  
ANISOU 4137  O   HOH B 211     5545   8183   8334   1937    475  -4000       O  
HETATM 4138  O   HOH B 212      24.360  13.801  21.010  1.00 13.03           O  
ANISOU 4138  O   HOH B 212     1319   1643   1694     26    112     62       O  
HETATM 4139  O   HOH B 213      21.678  12.376  14.997  1.00 62.79           O  
ANISOU 4139  O   HOH B 213     9227   8160   5047  -4000   4133  -1416       O  
HETATM 4140  O   HOH B 214      25.486  21.433  27.663  1.00 37.38           O  
ANISOU 4140  O   HOH B 214     5031   4405   3921  -2232   -724    458       O  
HETATM 4141  O   HOH B 215       8.239  27.149  43.321  1.00 44.37           O  
ANISOU 4141  O   HOH B 215     5043   6294   4518  -2624   1590  -3599       O  
HETATM 4142  O   HOH B 216      22.226  15.193  38.031  1.00 50.79           O  
ANISOU 4142  O   HOH B 216    10583   4582   2983  -3732  -2826    815       O  
HETATM 4143  O   HOH B 217       2.321  23.680  36.101  0.50 17.46           O  
ANISOU 4143  O   HOH B 217     1661   2764   1815   -391     92   -312       O  
HETATM 4144  O   HOH B 218       3.469   8.124  28.213  1.00 32.67           O  
ANISOU 4144  O   HOH B 218     2671   6059   2945  -1345    154  -1847       O  
HETATM 4145  O   HOH B 219      19.946  31.417  34.015  1.00 55.01           O  
ANISOU 4145  O   HOH B 219     4925   9587   5143  -3270  -1971   3615       O  
HETATM 4146  O   HOH B 220       8.473  29.373  43.100  1.00 34.18           O  
ANISOU 4146  O   HOH B 220     3593   7040   1580   -140     73  -1065       O  
HETATM 4147  O   HOH B 221       6.294  10.367  23.575  1.00 50.48           O  
ANISOU 4147  O   HOH B 221     2317  13565   2156    757    -57   1375       O  
HETATM 4148  O   HOH B 222       7.543   5.048  23.772  1.00 52.93           O  
ANISOU 4148  O   HOH B 222     2320   9653   6940    487   -645   3868       O  
HETATM 4149  O   HOH B 223       7.457  15.588  18.580  1.00 21.14           O  
ANISOU 4149  O   HOH B 223     3834   1512   2207    218   -519   -236       O  
HETATM 4150  O   HOH B 224      17.016  35.882  26.468  1.00 15.75           O  
ANISOU 4150  O   HOH B 224     2124   2203   1300    982    526    591       O  
HETATM 4151  O   HOH B 225       2.311  43.905  16.714  0.50 17.23           O  
ANISOU 4151  O   HOH B 225     1595   1807   2756    330   -856    297       O  
HETATM 4152  O   HOH B 226      14.445   5.136  37.132  1.00 14.31           O  
ANISOU 4152  O   HOH B 226     1925   1284   1904    171   -162   -346       O  
HETATM 4153  O   HOH B 227      19.759  41.125  26.560  0.50 18.39           O  
ANISOU 4153  O   HOH B 227     2229   2689   1655  -1122   -525   -408       O  
HETATM 4154  O   HOH B 228      16.848  12.820  40.458  1.00 36.07           O  
ANISOU 4154  O   HOH B 228     5712   3894   3282    775    -87  -1227       O  
HETATM 4155  O   HOH B 229      24.250  15.417  26.515  1.00 27.22           O  
ANISOU 4155  O   HOH B 229     4606   2662   2460   1880   -444    385       O  
HETATM 4156  O  BHOH B 230      16.073  33.886  32.409  0.50 40.51           O  
ANISOU 4156  O  BHOH B 230     7482   2948   4046   1068   3096    532       O  
HETATM 4157  O   HOH B 231       6.502  43.985  17.398  1.00 20.60           O  
ANISOU 4157  O   HOH B 231     1919   1329   4115    347    915     -1       O  
HETATM 4158  O   HOH B 232      12.696  27.110  44.378  1.00 10.38           O  
ANISOU 4158  O   HOH B 232     1271   1880    559    217    -42   -266       O  
HETATM 4159  O   HOH B 233      23.106  20.705  39.549  1.00 65.07           O  
ANISOU 4159  O   HOH B 233     5181   6392  11680   4017    678   3463       O  
HETATM 4160  O   HOH B 234       4.384  15.750  26.188  1.00 52.97           O  
ANISOU 4160  O   HOH B 234     3830   2614  12482  -1672  -2307    542       O  
HETATM 4161  O   HOH B 235       3.874  12.996  27.456  1.00 34.56           O  
ANISOU 4161  O   HOH B 235     3916   4438   3996   -173  -1800   -932       O  
HETATM 4162  O   HOH B 236      12.141  16.226  40.292  1.00 11.10           O  
ANISOU 4162  O   HOH B 236     1558   1170   1239    -40   -330    236       O  
HETATM 4163  O   HOH B 237      18.021   1.014  19.597  1.00 66.38           O  
ANISOU 4163  O   HOH B 237    11068   3524   9127   -583   6820   1112       O  
HETATM 4164  O   HOH B 238      22.716   7.941  39.770  1.00 95.51           O  
ANISOU 4164  O   HOH B 238    10434  12531  11163   5634  -3301   4948       O  
HETATM 4165  O   HOH B 239      16.288  42.833  27.492  1.00 40.40           O  
ANISOU 4165  O   HOH B 239     3119   4514   6804   -845    379  -3788       O  
HETATM 4166  O   HOH B 240      23.045  25.975  28.492  1.00 22.29           O  
ANISOU 4166  O   HOH B 240     3582   2179   2204   -674    303    -15       O  
HETATM 4167  O  BHOH B 241      17.676   8.503  34.964  0.41 18.11           O  
ANISOU 4167  O  BHOH B 241     1736   2645   2091   -450    -88   -825       O  
HETATM 4168  O   HOH B 242       5.512  13.270  20.729  1.00151.28           O  
ANISOU 4168  O   HOH B 242    16395  18689  18972   3060  -1582    229       O  
HETATM 4169  O   HOH B 243       7.996   7.639  34.045  1.00 20.43           O  
ANISOU 4169  O   HOH B 243     2487   1464   3349    603   1365    880       O  
HETATM 4170  O   HOH B 244       2.918  26.648  37.028  1.00 44.77           O  
ANISOU 4170  O   HOH B 244     4869   2654   8474    925   -471    925       O  
HETATM 4171  O   HOH B 245      24.027  20.713  34.877  1.00 27.61           O  
ANISOU 4171  O   HOH B 245     3133   2877   3855    249   -599    402       O  
HETATM 4172  O  BHOH B 246      21.624  23.984  29.510  1.00 45.83           O  
ANISOU 4172  O  BHOH B 246     6909   6079   3387   -169    831   -615       O  
HETATM 4173  O   HOH B 247       7.779   7.358  23.889  1.00 34.74           O  
ANISOU 4173  O   HOH B 247     2261   3892   6261   -483    676  -2407       O  
HETATM 4174  O   HOH B 248      -1.518   9.763  35.182  1.00 29.89           O  
ANISOU 4174  O   HOH B 248     5356   2645   2680    156   -154   -568       O  
HETATM 4175  O   HOH B 249      18.679  32.046  36.689  1.00 38.82           O  
ANISOU 4175  O   HOH B 249     2822   1949   9101   -176   -966    461       O  
HETATM 4176  O   HOH B 250      18.355  20.000  47.136  1.00  9.95           O  
ANISOU 4176  O   HOH B 250     1586   1126    845    155     13    -16       O  
HETATM 4177  O   HOH B 251      22.102  40.121  20.224  1.00 44.42           O  
ANISOU 4177  O   HOH B 251     5614   4622   5638    846   3190   2839       O  
HETATM 4178  O   HOH B 252      25.587  29.220  29.396  1.00 54.70           O  
ANISOU 4178  O   HOH B 252     3483   7649   8413  -1405   2315   2618       O  
HETATM 4179  O   HOH B 253       1.064  28.707  25.432  1.00 12.47           O  
ANISOU 4179  O   HOH B 253     1278   1848   1329   -264    180   -306       O  
HETATM 4180  O   HOH B 254       2.585  19.029  29.681  1.00  8.97           O  
ANISOU 4180  O   HOH B 254     1119   1159    927   -103     80    246       O  
HETATM 4181  O   HOH B 255      13.573  39.526  31.334  1.00 40.33           O  
ANISOU 4181  O   HOH B 255     4169   7087   3155   -507   -326   1307       O  
HETATM 4182  O   HOH B 256       4.311  19.134  22.841  1.00 31.57           O  
ANISOU 4182  O   HOH B 256     2491   5636   3156  -1869   -741    383       O  
HETATM 4183  O   HOH B 257      16.307   9.112  40.573  1.00 39.39           O  
ANISOU 4183  O   HOH B 257     5094   6233   2747    179   -672    900       O  
HETATM 4184  O   HOH B 258      19.294  34.227  30.327  1.00 22.37           O  
ANISOU 4184  O   HOH B 258     3421   2220   2352   -977   -586    565       O  
HETATM 4185  O   HOH B 259       7.587  23.883  18.379  1.00  7.01           O  
ANISOU 4185  O   HOH B 259      829    942    736   -214     26   -211       O  
HETATM 4186  O   HOH B 260      14.797  31.074  38.582  1.00 21.86           O  
ANISOU 4186  O   HOH B 260     2662   3108   2042      8   -326   -517       O  
HETATM 4187  O   HOH B 261      21.795  34.097  27.968  1.00 19.92           O  
ANISOU 4187  O   HOH B 261     2195   2013   2911   -977  -1482    891       O  
HETATM 4188  O   HOH B 262      24.379  15.541  11.058  1.00 27.23           O  
ANISOU 4188  O   HOH B 262     3328   1079   5322    -94   2377   -306       O  
HETATM 4189  O   HOH B 263       1.696  34.499  28.462  1.00 13.94           O  
ANISOU 4189  O   HOH B 263     1649   1778   1555    539    526    191       O  
HETATM 4190  O   HOH B 264      11.232  14.305  16.635  1.00 35.48           O  
ANISOU 4190  O   HOH B 264     1551   2979   8149   -324   -193   2822       O  
HETATM 4191  O   HOH B 265       4.131   6.612  32.061  1.00 43.32           O  
ANISOU 4191  O   HOH B 265     6066   2499   6914    -95   3354    -49       O  
HETATM 4192  O   HOH B 266      22.077  26.281  37.569  1.00 40.62           O  
ANISOU 4192  O   HOH B 266     3959   6492   4063  -1122   1482  -2395       O  
HETATM 4193  O   HOH B 267      15.330   5.258  23.625  1.00 24.10           O  
ANISOU 4193  O   HOH B 267     2618   2086   3906   -503   1117  -1632       O  
HETATM 4194  O   HOH B 268      22.396   9.089  35.347  1.00 39.13           O  
ANISOU 4194  O   HOH B 268     4550   6324   3108   3197    126    784       O  
HETATM 4195  O   HOH B 269      20.321  17.295  33.142  0.50 17.01           O  
ANISOU 4195  O   HOH B 269     1721   2319   2037   -149    -20   -845       O  
HETATM 4196  O   HOH B 270      19.513  16.974   9.520  0.50  9.79           O  
ANISOU 4196  O   HOH B 270     1719   1041    738    -26    204    -24       O  
HETATM 4197  O   HOH B 271       0.711  33.096  31.706  1.00 32.15           O  
ANISOU 4197  O   HOH B 271     5435   2344   3709    906   2292     93       O  
HETATM 4198  O  BHOH B 272      21.526  16.832  33.746  0.50 13.15           O  
ANISOU 4198  O  BHOH B 272     2373   1101   1225      1   -239    -21       O  
HETATM 4199  O   HOH B 273      23.236  15.331  35.763  1.00 33.33           O  
ANISOU 4199  O   HOH B 273     3360   6091   2460  -1953    103  -1188       O  
HETATM 4200  O   HOH B 274      17.908  39.226  25.837  1.00 12.80           O  
ANISOU 4200  O   HOH B 274     1683   1753   1136   -368     12   -103       O  
HETATM 4201  O   HOH B 275       1.962  42.132  21.366  1.00 55.89           O  
ANISOU 4201  O   HOH B 275     5963   7971   6038   -167   4123   -625       O  
HETATM 4202  O   HOH B 276      19.115  16.402  45.119  1.00 29.72           O  
ANISOU 4202  O   HOH B 276     3913   3970   2735    635  -1563    124       O  
HETATM 4203  O   HOH B 277       8.492   1.291  30.821  1.00 18.03           O  
ANISOU 4203  O   HOH B 277     2052   2055   2334   -377    261    302       O  
HETATM 4204  O  CHOH B 278      20.929   7.814  24.010  0.50 24.21           O  
ANISOU 4204  O  CHOH B 278     2894   1169   4589    351  -1817   -245       O  
HETATM 4205  O   HOH B 279       1.552  15.664  35.408  1.00  8.75           O  
ANISOU 4205  O   HOH B 279      890   1005   1232      2    186   -102       O  
HETATM 4206  O   HOH B 280       3.943  13.529  32.028  1.00  9.70           O  
ANISOU 4206  O   HOH B 280      993   1295   1179   -147    -20    209       O  
HETATM 4207  O   HOH B 281      24.677  29.487  26.346  1.00 33.96           O  
ANISOU 4207  O   HOH B 281     3505   7266   1363   2479    206    899       O  
HETATM 4208  O   HOH B 282       2.248  19.939  21.005  1.00 39.43           O  
ANISOU 4208  O   HOH B 282     2059   2034   9995   -688   1223   1141       O  
HETATM 4209  O   HOH B 283       0.608  40.524  22.911  1.00 21.02           O  
ANISOU 4209  O   HOH B 283     2019   1969   3524    887    219    567       O  
HETATM 4210  O   HOH B 284       7.473   6.950  30.648  1.00 27.31           O  
ANISOU 4210  O   HOH B 284     1988   1797   5974   -530   1428   -239       O  
HETATM 4211  O   HOH B 285       7.128  37.911  36.350  1.00 56.70           O  
ANISOU 4211  O   HOH B 285     7446   9386   3430  -1014   2487   -898       O  
HETATM 4212  O   HOH B 286      13.187  18.945  42.760  1.00 15.66           O  
ANISOU 4212  O   HOH B 286     2002   1799   1795   -128   -352    412       O  
HETATM 4213  O   HOH B 287      12.115  42.501  29.325  1.00 33.02           O  
ANISOU 4213  O   HOH B 287     4098   2612   5090  -1354   1033  -1463       O  
HETATM 4214  O   HOH B 288      12.814   4.430  40.605  1.00 20.05           O  
ANISOU 4214  O   HOH B 288     3240   1851   2073   -602   -486    260       O  
HETATM 4215  O   HOH B 289      27.278  27.423  23.865  1.00 50.53           O  
ANISOU 4215  O   HOH B 289     4271   7654   6132   4036   1499   2059       O  
HETATM 4216  O   HOH B 290      21.786  22.262  42.774  1.00 23.50           O  
ANISOU 4216  O   HOH B 290     2320   3792   2285  -1114  -1631   1488       O  
HETATM 4217  O   HOH B 291       9.119  16.064  27.071  1.00  8.60           O  
ANISOU 4217  O   HOH B 291     1199    714   1161   -152    163    219       O  
HETATM 4218  O   HOH B 292       0.392  21.100  26.685  1.00 20.83           O  
ANISOU 4218  O   HOH B 292     3412   1503   2527     69  -1318     70       O  
HETATM 4219  O   HOH B 293      10.423  33.690  36.431  1.00 20.09           O  
ANISOU 4219  O   HOH B 293     3334   1797   2049    515    380    266       O  
HETATM 4220  O   HOH B 294      15.966  34.102  30.332  1.00 22.49           O  
ANISOU 4220  O   HOH B 294     4104   2150   1783    891    -96    221       O  
HETATM 4221  O   HOH B 295      22.941  12.418  13.123  1.00 33.24           O  
ANISOU 4221  O   HOH B 295     3917   1650   6309     59   1718   -670       O  
HETATM 4222  O   HOH B 296      23.376  34.262  24.337  1.00 17.42           O  
ANISOU 4222  O   HOH B 296     1144   1875   3206   -170    -99    -66       O  
HETATM 4223  O  BHOH B 297       8.582   8.435  36.727  0.50 20.66           O  
ANISOU 4223  O  BHOH B 297     2365   2317   2700   -513    543   -554       O  
HETATM 4224  O   HOH B 298      11.667  20.685  41.293  1.00 14.66           O  
ANISOU 4224  O   HOH B 298     1552   2466   1220    153    -37    501       O  
HETATM 4225  O   HOH B 299       3.947   9.462  25.559  1.00 55.18           O  
ANISOU 4225  O   HOH B 299     2588  11991   5139   -895  -2202   1356       O  
HETATM 4226  O   HOH B 300      10.392  40.750  32.981  1.00 32.75           O  
ANISOU 4226  O   HOH B 300     4763   3441   3500  -1913  -1069   -303       O  
HETATM 4227  O   HOH B 301      15.866  31.499  36.190  1.00 16.82           O  
ANISOU 4227  O   HOH B 301     2723   1526   1761    881     34   -572       O  
HETATM 4228  O  BHOH B 302      22.447  19.191  33.030  0.63 13.06           O  
ANISOU 4228  O  BHOH B 302     1825   1610   1232   -130    -68    182       O  
HETATM 4229  O   HOH B 303      24.017  13.856  28.368  1.00 35.57           O  
ANISOU 4229  O   HOH B 303     4410   6472   1828   4092   1394   1374       O  
HETATM 4230  O   HOH B 304       4.537  27.808  40.486  1.00 17.86           O  
ANISOU 4230  O   HOH B 304     2317   1854   2210    -37   1206   -439       O  
HETATM 4231  O   HOH B 305       6.046   0.425  32.367  1.00 43.43           O  
ANISOU 4231  O   HOH B 305     3538   7337   4643   2598  -1907  -1460       O  
HETATM 4232  O   HOH B 306      23.255  23.173  34.135  1.00 21.46           O  
ANISOU 4232  O   HOH B 306     1944   3260   2465   1455    926   1017       O  
HETATM 4233  O   HOH B 307       7.250   4.283  36.887  1.00 30.14           O  
ANISOU 4233  O   HOH B 307     2843   4632   3295   -934   1734  -1576       O  
HETATM 4234  O   HOH B 308       9.281  32.699  39.797  1.00 21.76           O  
ANISOU 4234  O   HOH B 308     3202   3105   1468    318     93   -558       O  
HETATM 4235  O   HOH B 309       9.992   7.714  19.060  1.00 21.21           O  
ANISOU 4235  O   HOH B 309     2407   2990   2183   -854   -821    -16       O  
HETATM 4236  O   HOH B 310      20.695  10.953  13.050  1.00 28.44           O  
ANISOU 4236  O   HOH B 310     4111   1650   4400    980   2584    337       O  
HETATM 4237  O   HOH B 311      13.890  44.473  23.294  1.00 36.39           O  
ANISOU 4237  O   HOH B 311     2654   3524   6827   -354   2288  -1802       O  
HETATM 4238  O   HOH B 312       4.322  16.848  29.563  1.00  8.43           O  
ANISOU 4238  O   HOH B 312     1043   1046    924    -87   -122    285       O  
HETATM 4239  O  BHOH B 313       8.093   1.561  29.214  0.50 16.94           O  
ANISOU 4239  O  BHOH B 313     1833   1629   2590   -370    147    358       O  
HETATM 4240  O   HOH B 314      21.418  12.711  38.550  1.00 25.38           O  
ANISOU 4240  O   HOH B 314     3071   3928   2070  -1125   -777    417       O  
HETATM 4241  O   HOH B 315      21.887  23.613  29.425  0.50  8.30           O  
ANISOU 4241  O   HOH B 315      936   1133    898   -489     -6   -262       O  
HETATM 4242  O   HOH B 316       7.027  10.201  37.989  1.00 31.41           O  
ANISOU 4242  O   HOH B 316     3942   2956   4327    105   -665   1601       O  
HETATM 4243  O   HOH B 317      14.898  39.551  28.983  1.00 20.59           O  
ANISOU 4243  O   HOH B 317     2787   3126   1443  -1253    225   -731       O  
HETATM 4244  O  CHOH B 318      27.868  28.611  20.913  0.50 36.06           O  
ANISOU 4244  O  CHOH B 318     1954   5434   5499   1304  -1735  -1834       O  
HETATM 4245  O   HOH B 319       9.286  21.743  42.114  1.00 29.42           O  
ANISOU 4245  O   HOH B 319     3807   3171   3536   1175   1291    281       O  
HETATM 4246  O   HOH B 320      23.235  23.731  24.830  0.49 24.41           O  
ANISOU 4246  O   HOH B 320     2286   2625   3810  -1166    876    374       O  
HETATM 4247  O   HOH B 321      21.990   6.113  31.794  1.00 54.44           O  
ANISOU 4247  O   HOH B 321     3441   2047  13965   -496  -3377   2299       O  
HETATM 4248  O   HOH B 322       9.375  13.692  40.029  1.00 16.65           O  
ANISOU 4248  O   HOH B 322     3008   1345   1596   -197   -733    495       O  
HETATM 4249  O   HOH B 323      23.598  19.199  36.537  1.00 54.87           O  
ANISOU 4249  O   HOH B 323     4835   3700  11073   1554  -1486   1322       O  
HETATM 4250  O   HOH B 324      24.267  17.988  40.721  1.00 83.71           O  
ANISOU 4250  O   HOH B 324     7037   4659  18216  -2897  -2266   2292       O  
HETATM 4251  O   HOH B 325       7.915  -1.006  29.468  1.00 19.89           O  
ANISOU 4251  O   HOH B 325     1580   2151   3374    173    -78    396       O  
HETATM 4252  O   HOH B 326      21.518  12.520  10.266  1.00 40.46           O  
ANISOU 4252  O   HOH B 326     5775   3152   5529   -248   2482  -1603       O  
HETATM 4253  O   HOH B 327       9.648   4.971  20.445  0.50 31.71           O  
ANISOU 4253  O   HOH B 327     4127   4125   3079  -1782   -458    655       O  
HETATM 4254  O   HOH B 328       4.933  10.628  39.184  1.00 39.93           O  
ANISOU 4254  O   HOH B 328     2221   8124   3925    338    801    321       O  
HETATM 4255  O   HOH B 329       6.759  12.594  24.791  1.00 32.45           O  
ANISOU 4255  O   HOH B 329     5107   3798   2690  -1551   -871   1342       O  
HETATM 4256  O  BHOH B 330      19.106  18.510   9.400  0.46 14.10           O  
ANISOU 4256  O  BHOH B 330      989   2487   1562    -76     79    913       O  
HETATM 4257  O   HOH B 331      19.660  37.744  18.882  0.50  7.41           O  
ANISOU 4257  O   HOH B 331     1044    782    820     29     -3    212       O  
HETATM 4258  O  CHOH B 332      19.366  10.736  11.990  0.50 24.80           O  
ANISOU 4258  O  CHOH B 332     3818   1955   3089   -425    270   -693       O  
HETATM 4259  O   HOH B 333      20.295  14.276   8.944  1.00 51.31           O  
ANISOU 4259  O   HOH B 333    12296   3144   2895   2563    754   -541       O  
HETATM 4260  O   HOH B 334       3.774  41.489  26.190  1.00 53.38           O  
ANISOU 4260  O   HOH B 334     8463   4376   6235   2247  -2164  -1877       O  
HETATM 4261  O   HOH B 335      20.670   6.874  35.359  1.00 50.12           O  
ANISOU 4261  O   HOH B 335     5261   4188   8459    636  -1928  -1520       O  
HETATM 4262  O   HOH B 336      17.727   6.985  35.988  0.59 18.64           O  
ANISOU 4262  O   HOH B 336     2084   1904   2673   -224   -270   -489       O  
HETATM 4263  O   HOH B 337      15.298   1.471  18.158  0.50 37.01           O  
ANISOU 4263  O   HOH B 337     5515   4053   3657  -1404   1104   1724       O  
HETATM 4264  O   HOH B 338       6.235  39.786  32.944  1.00 33.09           O  
ANISOU 4264  O   HOH B 338     3493   4429   3902   1062    244  -1313       O  
HETATM 4265  O   HOH B 339       1.756  11.929  32.693  1.00 46.88           O  
ANISOU 4265  O   HOH B 339     1652   2415  12683   -161   -883   2379       O  
HETATM 4266  O  CHOH B 340      22.362  27.126  36.257  1.00 56.05           O  
ANISOU 4266  O  CHOH B 340     6905   8062   5061  -2352   2456   1015       O  
HETATM 4267  O   HOH B 341       3.041  15.055  27.969  1.00 36.37           O  
ANISOU 4267  O   HOH B 341     5549   3593   3855  -1224  -1687  -1289       O  
HETATM 4268  O   HOH B 342       0.866  29.238  34.505  1.00 38.34           O  
ANISOU 4268  O   HOH B 342     4143   5758   3798  -1864    863    411       O  
HETATM 4269  O   HOH B 343      14.514   5.067  20.842  1.00 25.28           O  
ANISOU 4269  O   HOH B 343     4466   1648   2920     54   1155    234       O  
HETATM 4270  O   HOH B 344       6.868  31.885  40.927  1.00 23.74           O  
ANISOU 4270  O   HOH B 344     3172   3230   2079    199    932   -473       O  
HETATM 4271  O   HOH B 345      19.638   4.744  32.285  1.00 40.17           O  
ANISOU 4271  O   HOH B 345     5455   3019   5880   1627  -3234   -203       O  
HETATM 4272  O   HOH B 346       4.010  17.933  19.525  1.00 74.74           O  
ANISOU 4272  O   HOH B 346     4506   8256  13945  -4000    497  -4000       O  
HETATM 4273  O  BHOH B 347      17.962   4.063  33.243  0.41 42.17           O  
ANISOU 4273  O  BHOH B 347     3736   6786   4546   1609   1405  -1681       O  
HETATM 4274  O   HOH B 348      24.755  33.257  22.111  1.00 73.64           O  
ANISOU 4274  O   HOH B 348     5357   6024  14930  -3533   2548   -377       O  
HETATM 4275  O   HOH B 349      24.293  22.570  31.420  1.00 45.03           O  
ANISOU 4275  O   HOH B 349     6087   6761   3242   -609    863   1321       O  
HETATM 4276  O   HOH B 350       3.131  29.101  36.079  0.50 11.48           O  
ANISOU 4276  O   HOH B 350     1250   1735   1118    -67    123   -112       O  
HETATM 4277  O   HOH B 351      13.926  15.092  43.788  1.00 44.61           O  
ANISOU 4277  O   HOH B 351     6346   4699   4895   1523   1608   -340       O  
HETATM 4278  O   HOH B 352      27.631  27.779  19.613  0.50 31.95           O  
ANISOU 4278  O   HOH B 352     2373   4109   4935   -393  -1961   -873       O  
HETATM 4279  O   HOH B 353      25.722  16.721  27.532  1.00 36.82           O  
ANISOU 4279  O   HOH B 353     4536   2235   6383    -24   4183   -776       O  
HETATM 4280  O  BHOH B 354      23.782  26.153  21.935  0.51 15.37           O  
ANISOU 4280  O  BHOH B 354     2135   2077   1282    297   -194    252       O  
HETATM 4281  O   HOH B 355      11.412  20.498  45.131  1.00 57.07           O  
ANISOU 4281  O   HOH B 355     5777  11285   3331  -3377  -1772   3303       O  
HETATM 4282  O   HOH B 356       4.956  30.391  39.782  1.00 24.75           O  
ANISOU 4282  O   HOH B 356     3968   2881   1995      0    340   -157       O  
HETATM 4283  O   HOH B 357       6.628   4.799  31.828  1.00 40.19           O  
ANISOU 4283  O   HOH B 357     4360   4660   5341  -1759  -1380   1807       O  
HETATM 4284  O   HOH B 358      21.728  27.008  23.331  0.49 10.10           O  
ANISOU 4284  O   HOH B 358     1079    849   1681    116    -79    538       O  
HETATM 4285  O   HOH B 359       8.080  34.586  37.424  1.00 17.82           O  
ANISOU 4285  O   HOH B 359     2664   1783   1922   -166   -218   -171       O  
HETATM 4286  O   HOH B 360       8.063  11.421  40.186  1.00 35.82           O  
ANISOU 4286  O   HOH B 360     2404   3182   7212    186   1567    711       O  
HETATM 4287  O   HOH B 361      17.530  35.899  29.043  1.00 18.39           O  
ANISOU 4287  O   HOH B 361     3452   1655   1464     -3   -268     32       O  
HETATM 4288  O  CHOH B 362       5.055  44.498  20.790  0.50 50.78           O  
ANISOU 4288  O  CHOH B 362     5041   4341   8764   2845     20    954       O  
HETATM 4289  O   HOH B 363      23.020  27.363  25.979  1.00 30.58           O  
ANISOU 4289  O   HOH B 363     6980   2491   1456   1770    938    416       O  
HETATM 4290  O   HOH B 364       1.797  32.408  36.767  1.00 38.58           O  
ANISOU 4290  O   HOH B 364     4971   4875   3941   -326   2687   -726       O  
HETATM 4291  O   HOH B 365      17.282  16.315   9.060  0.50 22.22           O  
ANISOU 4291  O   HOH B 365     2670   3288   1981  -1053   1260   -965       O  
HETATM 4292  O   HOH B 366      21.912  19.640  43.753  1.00 63.49           O  
ANISOU 4292  O   HOH B 366     3848   9385   9454    396  -2402   6213       O  
HETATM 4293  O   HOH B 367      -0.650   8.285  32.805  0.50 50.08           O  
ANISOU 4293  O   HOH B 367     7188   4491   6215   3191   3420   1956       O  
HETATM 4294  O   HOH B 368      21.205  17.876  45.047  1.00 61.64           O  
ANISOU 4294  O   HOH B 368     5309  13466   3252  -1847   -607  -2250       O  
HETATM 4295  O   HOH B 369      11.851   4.660  19.886  1.00 42.37           O  
ANISOU 4295  O   HOH B 369     7495   4963   2682  -3549   1003   -627       O  
HETATM 4296  O   HOH B 370      13.339  19.306  45.463  1.00 29.18           O  
ANISOU 4296  O   HOH B 370     4752   3222   2454   -984   -605   -838       O  
HETATM 4297  O   HOH B 371       4.472  34.653  39.171  1.00 63.96           O  
ANISOU 4297  O   HOH B 371     5070   5399  12384  -1089   3235  -1486       O  
HETATM 4298  O   HOH B 372       5.163  45.449  26.082  0.50 67.58           O  
ANISOU 4298  O   HOH B 372     4745  12540   6862  -3325  -3746    799       O  
HETATM 4299  O   HOH B 373      18.125   5.140  38.140  0.50 27.74           O  
ANISOU 4299  O   HOH B 373     2175   4459   3279   -530   -182   1337       O  
HETATM 4300  O   HOH B 374      24.339  24.609  36.130  1.00 47.93           O  
ANISOU 4300  O   HOH B 374     5562   4726   6838   1415  -3510  -1346       O  
HETATM 4301  O  CHOH B 375      14.706   2.383  20.460  0.50 31.22           O  
ANISOU 4301  O  CHOH B 375     7162   1739   2254   1503   -382     34       O  
HETATM 4302  O   HOH B 376      17.557  38.531  28.570  0.50 16.41           O  
ANISOU 4302  O   HOH B 376     2774   1389   1701   -256     41   -129       O  
HETATM 4303  O   HOH B 377      18.417   4.858  39.657  0.59 33.28           O  
ANISOU 4303  O   HOH B 377     3657   3995   4239  -1535   -628    916       O  
HETATM 4304  O   HOH B 378       1.986  26.715  39.652  1.00 53.21           O  
ANISOU 4304  O   HOH B 378     2055   7690   9267   -540    733   2490       O  
HETATM 4305  O   HOH B 379       4.489  42.407  22.831  1.00 37.65           O  
ANISOU 4305  O   HOH B 379     2604   2218   8633    668   1477    106       O  
HETATM 4306  O   HOH B 380       6.586  23.361  46.865  1.00 59.94           O  
ANISOU 4306  O   HOH B 380     4370   7263   9785  -2809   -976  -3196       O  
HETATM 4307  O   HOH B 381       9.784  22.739  46.683  1.00 47.76           O  
ANISOU 4307  O   HOH B 381     4956   6589   5520   -443   -459  -3430       O  
HETATM 4308  O   HOH B 382       2.151  18.844  17.599  1.00 62.91           O  
ANISOU 4308  O   HOH B 382    12085   5138   5258  -3603  -1710   -639       O  
HETATM 4309  O  BHOH B 383       3.108  28.801  36.639  0.50 27.87           O  
ANISOU 4309  O  BHOH B 383     2325   4823   2810    348   -852    -83       O  
HETATM 4310  O   HOH B 384      23.784  10.953  36.283  0.50 36.74           O  
ANISOU 4310  O   HOH B 384     4429   2909   5792   1001  -2110     -1       O  
HETATM 4311  O   HOH B 385       3.524  46.407  16.955  0.50 34.20           O  
ANISOU 4311  O   HOH B 385     2184   3403   6635    398   1773  -1884       O  
HETATM 4312  O   HOH B 386      14.513  17.386  46.673  1.00 47.32           O  
ANISOU 4312  O   HOH B 386     6043   8159   2708   -895    429   1755       O  
HETATM 4313  O   HOH B 387      15.740   6.930  41.381  0.50 40.58           O  
ANISOU 4313  O   HOH B 387     5838   6053   2608   2123  -1841    -55       O  
HETATM 4314  O   HOH B 388      11.706  16.457  42.962  1.00 22.33           O  
ANISOU 4314  O   HOH B 388     4106   2321   1550   -484   -530    129       O  
HETATM 4315  O   HOH B 389      19.513  43.663  25.685  1.00 39.74           O  
ANISOU 4315  O   HOH B 389     7174   2715   4312   -644  -3086    664       O  
HETATM 4316  O   HOH B 390       5.068  15.070  19.276  1.00 62.73           O  
ANISOU 4316  O   HOH B 390     6145  10481   5788  -1974    586   2241       O  
HETATM 4317  O   HOH B 391      17.290  44.591  26.180  1.00 61.25           O  
ANISOU 4317  O   HOH B 391    14810   3998   3077   2137   3167    450       O  
HETATM 4318  O   HOH B 392      23.321  12.370  41.762  1.00 78.35           O  
ANISOU 4318  O   HOH B 392    12162   5687  10150   1835  -3976   1275       O  
HETATM 4319  O   HOH B 393       9.927  43.318  31.762  0.50 60.10           O  
ANISOU 4319  O   HOH B 393    11566   3718   6192  -3136   2242  -3621       O  
HETATM 4320  O   HOH B 394       2.212  42.456  23.622  1.00 63.47           O  
ANISOU 4320  O   HOH B 394     7678   5532   9470   -724   4464  -2663       O  
HETATM 4321  O   HOH B 395      15.277  35.416  32.594  1.00 38.74           O  
ANISOU 4321  O   HOH B 395     6152   3700   3991   1557    -91  -1410       O  
HETATM 4322  O   HOH B 396      -1.146  30.757  32.788  1.00 72.09           O  
ANISOU 4322  O   HOH B 396     9616   9351   6792   1445   6047   2566       O  
HETATM 4323  O   HOH B 397      24.123  33.010  26.691  1.00 45.87           O  
ANISOU 4323  O   HOH B 397     2587   8970   4835  -2205   -726   3768       O  
HETATM 4324  O   HOH B 398      12.172  13.505  39.854  1.00 16.58           O  
ANISOU 4324  O   HOH B 398     2273   1515   2136     58     33    -98       O  
HETATM 4325  O  BHOH B 399      24.557  23.549  21.403  0.50 17.69           O  
ANISOU 4325  O  BHOH B 399     2045   2115   2161    218    -93    324       O  
HETATM 4326  O   HOH B 400       0.518  14.562  33.073  0.50 18.31           O  
ANISOU 4326  O   HOH B 400     3378   1866   1297   -504   -505   -284       O  
HETATM 4327  O   HOH B 401      14.052  12.672  41.688  1.00 37.71           O  
ANISOU 4327  O   HOH B 401     6206   1589   5680    304  -3935   -630       O  
HETATM 4328  O   HOH B 402       8.766  13.926  16.653  1.00 59.74           O  
ANISOU 4328  O   HOH B 402     4477   8046   8823   1009   1450   -515       O  
HETATM 4329  O   HOH B 403      26.315  25.217  25.286  1.00 47.28           O  
ANISOU 4329  O   HOH B 403     7804   6007   3084  -3886  -2179    526       O  
HETATM 4330  O   HOH B 404      22.159  33.772  30.493  1.00 44.32           O  
ANISOU 4330  O   HOH B 404     5716   6787   3333  -2850     35  -2150       O  
HETATM 4331  O   HOH B 405       6.147   2.571  31.025  1.00 29.26           O  
ANISOU 4331  O   HOH B 405     2895   2374   5187    -27    557    746       O  
HETATM 4332  O   HOH B 406       5.220   2.435  35.309  1.00 75.64           O  
ANISOU 4332  O   HOH B 406     3533  10543  12950   1178   2559   -794       O  
HETATM 4333  O   HOH B 407      16.173   3.313  38.269  1.00 22.51           O  
ANISOU 4333  O   HOH B 407     2571   2448   3024    217     15    -34       O  
HETATM 4334  O   HOH B 408      14.956   2.806  40.084  1.00 34.51           O  
ANISOU 4334  O   HOH B 408     3541   3951   4839  -1413    765  -1425       O  
HETATM 4335  O   HOH B 409      14.372  37.512  32.863  1.00 50.41           O  
ANISOU 4335  O   HOH B 409     8580   4786   4646   1315  -1619  -1566       O  
HETATM 4336  O   HOH B 410      15.459  14.844   9.076  1.00 33.75           O  
ANISOU 4336  O   HOH B 410     5109   4377   2575  -1990    355  -1531       O  
HETATM 4337  O   HOH B 411      14.872  33.676  34.996  1.00 23.54           O  
ANISOU 4337  O   HOH B 411     3721   2172   2520    161    204    592       O  
HETATM 4338  O  CHOH B 412       0.653  13.538  33.792  0.50 28.85           O  
ANISOU 4338  O  CHOH B 412     2452   4376   3480  -1075    640  -2282       O  
HETATM 4339  O   HOH B 413       9.260  14.155  42.908  1.00 52.21           O  
ANISOU 4339  O   HOH B 413     6555   9067   3035  -2839   -832   1445       O  
HETATM 4340  O   HOH B 414      17.913  12.247   9.458  1.00 65.82           O  
ANISOU 4340  O   HOH B 414     9573   5136   8809    569  -3194  -4000       O  
HETATM 4341  O   HOH B 415       6.853   1.155  27.254  0.50 47.56           O  
ANISOU 4341  O   HOH B 415     2897   2566  11531   -651  -1211  -1304       O  
HETATM 4342  O  CHOH B 416      19.503   3.026  33.832  1.00 49.20           O  
ANISOU 4342  O  CHOH B 416     3674   6862   7045   -688   1144    530       O  
HETATM 4343  O   HOH B 417      -3.758   9.254  35.198  1.00 32.14           O  
ANISOU 4343  O   HOH B 417     3000   5606   2880    870    -71   1320       O  
HETATM 4344  O   HOH B 418      20.876   4.039  34.182  1.00 57.11           O  
ANISOU 4344  O   HOH B 418     4196   8426   7784  -2526    639   1349       O  
HETATM 4345  O   HOH B 419      21.403  43.773  23.220  0.50 32.41           O  
ANISOU 4345  O   HOH B 419     2420   1960   7199      2   -810    621       O  
HETATM 4346  O  DHOH B 420      27.021  25.526  18.489  1.00 45.38           O  
ANISOU 4346  O  DHOH B 420     5112   5830   5274  -1837    458     10       O  
HETATM 4347  O   HOH B 421       9.214  19.368  44.186  0.50 75.86           O  
ANISOU 4347  O   HOH B 421     6787  14915   5407  -1346  -4000  -2901       O  
HETATM 4348  O   HOH B 422      12.790  34.311  33.993  1.00 63.33           O  
ANISOU 4348  O   HOH B 422     7788   5102   9740   2564  -4000   1515       O  
HETATM 4349  O   HOH B 423      12.810  37.327  35.394  1.00 52.44           O  
ANISOU 4349  O   HOH B 423     5922   4591   8225   -138  -2263   3081       O  
HETATM 4350  O   HOH B 424      10.480  37.315  38.587  1.00 56.30           O  
ANISOU 4350  O   HOH B 424     7684   4064   8371   -526   -978  -1123       O  
HETATM 4351  O  CHOH B 425      26.043  19.706  27.340  0.50 18.02           O  
ANISOU 4351  O  CHOH B 425     1570   3666   1203    455      6    228       O  
HETATM 4352  O  CHOH B 426       5.604  47.867  25.048  0.50 37.45           O  
ANISOU 4352  O  CHOH B 426     3325   2756   7301   -267  -1611   1452       O  
HETATM 4353  O   HOH B 427       9.264  11.626  42.834  1.00 59.62           O  
ANISOU 4353  O   HOH B 427     9286   9565   2452  -3416   1725  -1502       O  
HETATM 4354  O   HOH B 428       9.681  16.323  44.805  1.00 41.02           O  
ANISOU 4354  O   HOH B 428     3322   7877   3458   -951    451    529       O  
HETATM 4355  O  CHOH B 429      26.162  22.816  23.559  0.50 16.75           O  
ANISOU 4355  O  CHOH B 429     1788   2193   2005   -289   -297    814       O  
HETATM 4356  O   HOH B 430      31.248  25.703  20.378  1.00 36.81           O  
ANISOU 4356  O   HOH B 430     3649   3537   5967   -485  -1690   -629       O  
HETATM 4357  O   HOH B 431       5.590  35.512  43.200  0.50 40.15           O  
ANISOU 4357  O   HOH B 431     4448   6837   3060   1321   1287   2653       O  
HETATM 4358  O  CHOH B 432      14.343  39.546  40.623  0.50 46.43           O  
ANISOU 4358  O  CHOH B 432     3005   6978   6609    748  -2149    144       O  
CONECT 3600 3602 3610 3620                                                      
CONECT 3601 3603 3611 3621                                                      
CONECT 3602 3600 3604 3710                                                      
CONECT 3603 3601 3605 3711                                                      
CONECT 3604 3602 3606 3708                                                      
CONECT 3605 3603 3607 3709                                                      
CONECT 3606 3604 3608 3712                                                      
CONECT 3607 3605 3609 3713                                                      
CONECT 3608 3606 3610 3614                                                      
CONECT 3609 3607 3611 3615                                                      
CONECT 3610 3600 3608 3624                                                      
CONECT 3611 3601 3609 3625                                                      
CONECT 3612 3620 3714 3716 3718                                                 
CONECT 3613 3621 3715 3717 3719                                                 
CONECT 3614 3608 3616 3720                                                      
CONECT 3615 3609 3617 3721                                                      
CONECT 3616 3614 3618 3624                                                      
CONECT 3617 3615 3619 3625                                                      
CONECT 3618 3616 3622 3628                                                      
CONECT 3619 3617 3623 3629                                                      
CONECT 3620 3600 3612                                                           
CONECT 3621 3601 3613                                                           
CONECT 3622 3618                                                                
CONECT 3623 3619                                                                
CONECT 3624 3610 3616                                                           
CONECT 3625 3611 3617                                                           
CONECT 3626 3628 3630 3636 3722                                                 
CONECT 3627 3629 3631 3637 3723                                                 
CONECT 3628 3618 3626 3724                                                      
CONECT 3629 3619 3627 3725                                                      
CONECT 3630 3626 3632 3634 3726                                                 
CONECT 3631 3627 3633 3635 3727                                                 
CONECT 3632 3630 3638 3728 3730                                                 
CONECT 3633 3631 3639 3729 3731                                                 
CONECT 3634 3630 3642 3732 3734                                                 
CONECT 3635 3631 3643 3733 3735                                                 
CONECT 3636 3626 3640 3646                                                      
CONECT 3637 3627 3641 3647                                                      
CONECT 3638 3632 3642 3736 3738                                                 
CONECT 3639 3633 3643 3737 3739                                                 
CONECT 3640 3636                                                                
CONECT 3641 3637                                                                
CONECT 3642 3634 3638                                                           
CONECT 3643 3635 3639                                                           
CONECT 3644 3648 3650 3672                                                      
CONECT 3645 3649 3651 3673                                                      
CONECT 3646 3636 3658 3740                                                      
CONECT 3647 3637 3659 3741                                                      
CONECT 3648 3644                                                                
CONECT 3649 3645                                                                
CONECT 3650 3644 3658 3660 3742                                                 
CONECT 3651 3645 3659 3661 3743                                                 
CONECT 3652 3654 3662 3664                                                      
CONECT 3653 3655 3663 3665                                                      
CONECT 3654 3652 3658 3744 3746                                                 
CONECT 3655 3653 3659 3745 3747                                                 
CONECT 3656 3666 3668 3748                                                      
CONECT 3657 3667 3669 3749                                                      
CONECT 3658 3646 3650 3654 3750                                                 
CONECT 3659 3647 3651 3655 3751                                                 
CONECT 3660 3650 3752                                                           
CONECT 3661 3651 3753                                                           
CONECT 3662 3652 3666 3754                                                      
CONECT 3663 3653 3667 3755                                                      
CONECT 3664 3652 3668 3756                                                      
CONECT 3665 3653 3669 3757                                                      
CONECT 3666 3656 3662 3758                                                      
CONECT 3667 3657 3663 3759                                                      
CONECT 3668 3656 3664 3760                                                      
CONECT 3669 3657 3665 3761                                                      
CONECT 3670 3674 3676 3690                                                      
CONECT 3671 3675 3677 3691                                                      
CONECT 3672 3644 3676 3680                                                      
CONECT 3673 3645 3677 3681                                                      
CONECT 3674 3670                                                                
CONECT 3675 3671                                                                
CONECT 3676 3670 3672 3678 3762                                                 
CONECT 3677 3671 3673 3679 3763                                                 
CONECT 3678 3676 3682 3684 3686                                                 
CONECT 3679 3677 3683 3685 3687                                                 
CONECT 3680 3672 3686 3764 3766                                                 
CONECT 3681 3673 3687 3765 3767                                                 
CONECT 3682 3678 3768 3770 3772                                                 
CONECT 3683 3679 3769 3771 3773                                                 
CONECT 3684 3678 3774 3776 3778                                                 
CONECT 3685 3679 3775 3777 3779                                                 
CONECT 3686 3678 3680                                                           
CONECT 3687 3679 3681                                                           
CONECT 3688 3690 3706 3780 3782                                                 
CONECT 3689 3691 3707 3781 3783                                                 
CONECT 3690 3670 3688 3784                                                      
CONECT 3691 3671 3689 3785                                                      
CONECT 3692 3694 3786 3788 3790                                                 
CONECT 3693 3695 3787 3789 3791                                                 
CONECT 3694 3692 3696 3706                                                      
CONECT 3695 3693 3697 3707                                                      
CONECT 3696 3694 3698 3792                                                      
CONECT 3697 3695 3699 3793                                                      
CONECT 3698 3696 3700 3794                                                      
CONECT 3699 3697 3701 3795                                                      
CONECT 3700 3698 3702 3796                                                      
CONECT 3701 3699 3703 3797                                                      
CONECT 3702 3700 3704 3706                                                      
CONECT 3703 3701 3705 3707                                                      
CONECT 3704 3702 3798 3800 3802                                                 
CONECT 3705 3703 3799 3801 3803                                                 
CONECT 3706 3688 3694 3702                                                      
CONECT 3707 3689 3695 3703                                                      
CONECT 3708 3604                                                                
CONECT 3709 3605                                                                
CONECT 3710 3602                                                                
CONECT 3711 3603                                                                
CONECT 3712 3606                                                                
CONECT 3713 3607                                                                
CONECT 3714 3612                                                                
CONECT 3715 3613                                                                
CONECT 3716 3612                                                                
CONECT 3717 3613                                                                
CONECT 3718 3612                                                                
CONECT 3719 3613                                                                
CONECT 3720 3614                                                                
CONECT 3721 3615                                                                
CONECT 3722 3626                                                                
CONECT 3723 3627                                                                
CONECT 3724 3628                                                                
CONECT 3725 3629                                                                
CONECT 3726 3630                                                                
CONECT 3727 3631                                                                
CONECT 3728 3632                                                                
CONECT 3729 3633                                                                
CONECT 3730 3632                                                                
CONECT 3731 3633                                                                
CONECT 3732 3634                                                                
CONECT 3733 3635                                                                
CONECT 3734 3634                                                                
CONECT 3735 3635                                                                
CONECT 3736 3638                                                                
CONECT 3737 3639                                                                
CONECT 3738 3638                                                                
CONECT 3739 3639                                                                
CONECT 3740 3646                                                                
CONECT 3741 3647                                                                
CONECT 3742 3650                                                                
CONECT 3743 3651                                                                
CONECT 3744 3654                                                                
CONECT 3745 3655                                                                
CONECT 3746 3654                                                                
CONECT 3747 3655                                                                
CONECT 3748 3656                                                                
CONECT 3749 3657                                                                
CONECT 3750 3658                                                                
CONECT 3751 3659                                                                
CONECT 3752 3660                                                                
CONECT 3753 3661                                                                
CONECT 3754 3662                                                                
CONECT 3755 3663                                                                
CONECT 3756 3664                                                                
CONECT 3757 3665                                                                
CONECT 3758 3666                                                                
CONECT 3759 3667                                                                
CONECT 3760 3668                                                                
CONECT 3761 3669                                                                
CONECT 3762 3676                                                                
CONECT 3763 3677                                                                
CONECT 3764 3680                                                                
CONECT 3765 3681                                                                
CONECT 3766 3680                                                                
CONECT 3767 3681                                                                
CONECT 3768 3682                                                                
CONECT 3769 3683                                                                
CONECT 3770 3682                                                                
CONECT 3771 3683                                                                
CONECT 3772 3682                                                                
CONECT 3773 3683                                                                
CONECT 3774 3684                                                                
CONECT 3775 3685                                                                
CONECT 3776 3684                                                                
CONECT 3777 3685                                                                
CONECT 3778 3684                                                                
CONECT 3779 3685                                                                
CONECT 3780 3688                                                                
CONECT 3781 3689                                                                
CONECT 3782 3688                                                                
CONECT 3783 3689                                                                
CONECT 3784 3690                                                                
CONECT 3785 3691                                                                
CONECT 3786 3692                                                                
CONECT 3787 3693                                                                
CONECT 3788 3692                                                                
CONECT 3789 3693                                                                
CONECT 3790 3692                                                                
CONECT 3791 3693                                                                
CONECT 3792 3696                                                                
CONECT 3793 3697                                                                
CONECT 3794 3698                                                                
CONECT 3795 3699                                                                
CONECT 3796 3700                                                                
CONECT 3797 3701                                                                
CONECT 3798 3704                                                                
CONECT 3799 3705                                                                
CONECT 3800 3704                                                                
CONECT 3801 3705                                                                
CONECT 3802 3704                                                                
CONECT 3803 3705                                                                
CONECT 3804 3806 3808                                                           
CONECT 3805 3807 3809                                                           
CONECT 3806 3804                                                                
CONECT 3807 3805                                                                
CONECT 3808 3804 3810 3812                                                      
CONECT 3809 3805 3811 3813                                                      
CONECT 3810 3808                                                                
CONECT 3811 3809                                                                
CONECT 3812 3808 3814                                                           
CONECT 3813 3809 3815                                                           
CONECT 3814 3812                                                                
CONECT 3815 3813                                                                
CONECT 3816 3817 3818                                                           
CONECT 3817 3816                                                                
CONECT 3818 3816 3819 3820                                                      
CONECT 3819 3818                                                                
CONECT 3820 3818 3821                                                           
CONECT 3821 3820                                                                
MASTER      383    0    3    2   20    0   16    6 2115    2  222   16          
END                                                                             



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