CNRS Nantes University US2B US2B
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***  HYDROLASE 30-JUN-04 1TW7  ***

elNémo ID: 2406051500211198616

Job options:

ID        	=	 2406051500211198616
JOBID     	=	 HYDROLASE 30-JUN-04 1TW7
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                               30-JUN-04   1TW7              
TITLE     WIDE OPEN 1.3A STRUCTURE OF A MULTI-DRUG RESISTANT HIV-1 PROTEASE     
TITLE    2 REPRESENTS A NOVEL DRUG TARGET                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEASE;                                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.4.23.16;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE   3 ORGANISM_TAXID: 11676;                                               
SOURCE   4 GENE: HIV-1;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PJFV769NOHISKO                            
KEYWDS    HIV PROTEASE, AIDS, POLYPROTEIN, HYDROLASE, ASPARTYL PROTEASE, MULTI- 
KEYWDS   2 DRUG RESISTANCE                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.MARTIN,J.F.VICKREY,G.PROTEASA,Y.L.JIMENEZ,Z.WAWRZAK,M.A.WINTERS,    
AUTHOR   2 T.C.MERIGAN,L.C.KOVARI                                               
REVDAT   5   23-AUG-23 1TW7    1       REMARK                                   
REVDAT   4   27-OCT-21 1TW7    1       REMARK SEQADV                            
REVDAT   3   24-FEB-09 1TW7    1       VERSN                                    
REVDAT   2   17-JAN-06 1TW7    1       JRNL                                     
REVDAT   1   19-JUL-05 1TW7    0                                                
JRNL        AUTH   P.MARTIN,J.F.VICKREY,G.PROTEASA,Y.L.JIMENEZ,Z.WAWRZAK,       
JRNL        AUTH 2 M.A.WINTERS,T.C.MERIGAN,L.C.KOVARI                           
JRNL        TITL   WIDE OPEN 1.3A STRUCTURE OF A MULTI-DRUG RESISTANT HIV-1     
JRNL        TITL 2 PROTEASE REPRESENTS A NOVEL DRUG TARGET                      
JRNL        REF    STRUCTURE                     V.  13  1887 2005              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   16338417                                                     
JRNL        DOI    10.1016/J.STR.2005.11.005                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   B.C.LOGSDON,J.F.VICKREY,P.MARTIN,G.PROTEASA,J.I.KOPEKE,      
REMARK   1  AUTH 2 S.R.TERLECKY,Z.WAWRZAK,M.A.WINTERS,T.C.MERIGAN,L.C.KOVARI    
REMARK   1  TITL   CRYSTAL STRUCTURES OF A MULTIDRUG-RESISTANT HUMAN            
REMARK   1  TITL 2 IMMUNODEFICIENCY VIRUS TYPE 1 PROTEASE REVEAL AN EXPANDED    
REMARK   1  TITL 3 ACTIVE-SITE CAVITY                                           
REMARK   1  REF    J.VIROL.                      V.  78  3123 2004              
REMARK   1  REFN                   ISSN 0022-538X                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.F.VICKREY,B.C.LOGSDON,G.PROTEASA,S.PALMER,M.A.WINTERS,     
REMARK   1  AUTH 2 T.C.MERIGAN,L.C.KOVARI                                       
REMARK   1  TITL   HIV-1 PROTEASE VARIANTS FROM 100-FOLD DRUG RESISTANT         
REMARK   1  TITL 2 CLINICAL ISOLATES: EXPRESSION, PURIFICATION, AND             
REMARK   1  TITL 3 CRYSTALLIZATION.                                             
REMARK   1  REF    PROTEIN EXPR.PURIF.           V.  28   165 2003              
REMARK   1  REFN                   ISSN 1046-5928                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.500                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 74.7                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.142                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.211                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.400                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2071                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 38356                  
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)) : 0.136                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.204                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.400                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 1814                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 33686                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1508                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 2                                             
REMARK   3   SOLVENT ATOMS      : 380                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1889.3                  
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 11                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 17519                   
REMARK   3   NUMBER OF RESTRAINTS                     : 20756                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.011                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.029                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.029                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.054                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.069                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.011                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.004                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.054                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.076                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: ANISOTROPIC REFINEMENT REDUCED FREE R     
REMARK   3  (NO CUTOFF) BY 0.035                                                
REMARK   4                                                                      
REMARK   4 1TW7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000022960.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JUL-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SILCON                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38356                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 74.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04300                            
REMARK 200   FOR THE DATA SET  : 30.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 0.3                                
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CCP4                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1RQ9                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CHLORIDE, MES, PH 6.5, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 295K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
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       52.87200            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       26.43600            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       79.30800            
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: 3270 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 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 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    GLU A  34   CB  -  CG  -  CD  ANGL. DEV. =  17.4 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    CYS A  67       59.30     38.43                                   
REMARK 500    CYS B  67       52.58     39.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 402                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1RPI   RELATED DB: PDB                                   
REMARK 900 MDR 769 UNCOMPLEXED                                                  
REMARK 900 RELATED ID: 1RQ9   RELATED DB: PDB                                   
REMARK 900 MDR 769 COMPLEXED WITH DMP450 (MOZENAVIR)                            
REMARK 900 RELATED ID: 1RV7   RELATED DB: PDB                                   
REMARK 900 MDR 769 COMPLEXED WITH LOPINAVIR                                     
DBREF  1TW7 A    1    99  GB     30142908 AAP15109         1     99             
DBREF  1TW7 B    1    99  GB     30142908 AAP15109         1     99             
SEQADV 1TW7 ILE A   10  GB   30142908  LEU    10 ENGINEERED MUTATION            
SEQADV 1TW7 ASN A   25  GB   30142908  ASP    25 ENGINEERED MUTATION            
SEQADV 1TW7 VAL A   36  GB   30142908  MET    36 ENGINEERED MUTATION            
SEQADV 1TW7 LEU A   46  GB   30142908  MET    46 ENGINEERED MUTATION            
SEQADV 1TW7 VAL A   54  GB   30142908  ILE    54 ENGINEERED MUTATION            
SEQADV 1TW7 VAL A   62  GB   30142908  ILE    62 ENGINEERED MUTATION            
SEQADV 1TW7 PRO A   63  GB   30142908  LEU    63 ENGINEERED MUTATION            
SEQADV 1TW7 VAL A   71  GB   30142908  ALA    71 ENGINEERED MUTATION            
SEQADV 1TW7 ALA A   82  GB   30142908  VAL    82 ENGINEERED MUTATION            
SEQADV 1TW7 VAL A   84  GB   30142908  ILE    84 ENGINEERED MUTATION            
SEQADV 1TW7 MET A   90  GB   30142908  LEU    90 ENGINEERED MUTATION            
SEQADV 1TW7 ILE B   10  GB   30142908  LEU    10 ENGINEERED MUTATION            
SEQADV 1TW7 ASN B   25  GB   30142908  ASP    25 ENGINEERED MUTATION            
SEQADV 1TW7 VAL B   36  GB   30142908  MET    36 ENGINEERED MUTATION            
SEQADV 1TW7 LEU B   46  GB   30142908  MET    46 ENGINEERED MUTATION            
SEQADV 1TW7 VAL B   54  GB   30142908  ILE    54 ENGINEERED MUTATION            
SEQADV 1TW7 VAL B   62  GB   30142908  ILE    62 ENGINEERED MUTATION            
SEQADV 1TW7 PRO B   63  GB   30142908  LEU    63 ENGINEERED MUTATION            
SEQADV 1TW7 VAL B   71  GB   30142908  ALA    71 ENGINEERED MUTATION            
SEQADV 1TW7 ALA B   82  GB   30142908  VAL    82 ENGINEERED MUTATION            
SEQADV 1TW7 VAL B   84  GB   30142908  ILE    84 ENGINEERED MUTATION            
SEQADV 1TW7 MET B   90  GB   30142908  LEU    90 ENGINEERED MUTATION            
SEQRES   1 A   99  PRO GLN ILE THR LEU TRP GLN ARG PRO ILE VAL THR ILE          
SEQRES   2 A   99  LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASN THR          
SEQRES   3 A   99  GLY ALA ASP ASP THR VAL LEU GLU GLU VAL ASN LEU PRO          
SEQRES   4 A   99  GLY ARG TRP LYS PRO LYS LEU ILE GLY GLY ILE GLY GLY          
SEQRES   5 A   99  PHE VAL LYS VAL ARG GLN TYR ASP GLN VAL PRO ILE GLU          
SEQRES   6 A   99  ILE CYS GLY HIS LYS VAL ILE GLY THR VAL LEU VAL GLY          
SEQRES   7 A   99  PRO THR PRO ALA ASN VAL ILE GLY ARG ASN LEU MET THR          
SEQRES   8 A   99  GLN ILE GLY CYS THR LEU ASN PHE                              
SEQRES   1 B   99  PRO GLN ILE THR LEU TRP GLN ARG PRO ILE VAL THR ILE          
SEQRES   2 B   99  LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASN THR          
SEQRES   3 B   99  GLY ALA ASP ASP THR VAL LEU GLU GLU VAL ASN LEU PRO          
SEQRES   4 B   99  GLY ARG TRP LYS PRO LYS LEU ILE GLY GLY ILE GLY GLY          
SEQRES   5 B   99  PHE VAL LYS VAL ARG GLN TYR ASP GLN VAL PRO ILE GLU          
SEQRES   6 B   99  ILE CYS GLY HIS LYS VAL ILE GLY THR VAL LEU VAL GLY          
SEQRES   7 B   99  PRO THR PRO ALA ASN VAL ILE GLY ARG ASN LEU MET THR          
SEQRES   8 B   99  GLN ILE GLY CYS THR LEU ASN PHE                              
HET     NA  A 402       1                                                       
HET     NA  B 401       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   3   NA    2(NA 1+)                                                     
FORMUL   5  HOH   *380(H2 O)                                                    
HELIX    1   1 GLY A   86  GLY A   94  1                                   9    
HELIX    2   2 GLY B   86  GLY B   94  1                                   9    
SHEET    1   A 4 GLN A   2  ILE A   3  0                                        
SHEET    2   A 4 THR B  96  ASN B  98 -1  O  LEU B  97   N  ILE A   3           
SHEET    3   A 4 THR A  96  ASN A  98 -1  N  THR A  96   O  ASN B  98           
SHEET    4   A 4 GLN B   2  ILE B   3 -1  O  ILE B   3   N  LEU A  97           
SHEET    1   B 8 LYS A  43  GLY A  49  0                                        
SHEET    2   B 8 GLY A  52  ILE A  66 -1  O  GLN A  58   N  LYS A  43           
SHEET    3   B 8 HIS A  69  VAL A  77 -1  O  VAL A  71   N  ILE A  64           
SHEET    4   B 8 VAL A  32  LEU A  33  1  N  LEU A  33   O  LEU A  76           
SHEET    5   B 8 VAL A  84  ILE A  85 -1  O  VAL A  84   N  VAL A  32           
SHEET    6   B 8 GLN A  18  LEU A  24  1  N  LEU A  23   O  ILE A  85           
SHEET    7   B 8 ILE A  10  ILE A  15 -1  N  ILE A  13   O  LYS A  20           
SHEET    8   B 8 GLY A  52  ILE A  66 -1  O  GLU A  65   N  LYS A  14           
SHEET    1   C 8 LYS B  43  GLY B  49  0                                        
SHEET    2   C 8 GLY B  52  ILE B  66 -1  O  GLN B  58   N  LYS B  43           
SHEET    3   C 8 HIS B  69  VAL B  77 -1  O  VAL B  77   N  ARG B  57           
SHEET    4   C 8 VAL B  32  LEU B  33  1  N  LEU B  33   O  LEU B  76           
SHEET    5   C 8 VAL B  84  ILE B  85 -1  O  VAL B  84   N  VAL B  32           
SHEET    6   C 8 GLN B  18  LEU B  24  1  N  LEU B  23   O  ILE B  85           
SHEET    7   C 8 ILE B  10  ILE B  15 -1  N  ILE B  13   O  LYS B  20           
SHEET    8   C 8 GLY B  52  ILE B  66 -1  O  GLU B  65   N  LYS B  14           
SITE     1 AC1  4 PRO A  79  GLY B  73  THR B  74  ASN B  88                    
SITE     1 AC2  4 GLY A  73  THR A  74  ASN A  88  PRO B  79                    
CRYST1   45.043   45.043  105.744  90.00  90.00  90.00 P 41          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      0.022201  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.022201  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009457        0.00000                         
ATOM      1  N   PRO A   1      -4.555  33.477  -5.326  1.00 31.58           N  
ANISOU    1  N   PRO A   1     5119   4378   2503    282    731    365       N  
ATOM      2  CA  PRO A   1      -3.735  34.160  -6.330  1.00 26.25           C  
ANISOU    2  CA  PRO A   1     4512   2958   2504    107    439   -119       C  
ATOM      3  C   PRO A   1      -4.001  33.684  -7.755  1.00 24.44           C  
ANISOU    3  C   PRO A   1     3856   2935   2496   -106    772   -147       C  
ATOM      4  O   PRO A   1      -4.665  32.692  -8.038  1.00 28.21           O  
ANISOU    4  O   PRO A   1     4815   3375   2528   -711    997   -287       O  
ATOM      5  CB  PRO A   1      -2.303  33.774  -5.922  1.00 31.57           C  
ANISOU    5  CB  PRO A   1     4774   4219   3002    150     34    524       C  
ATOM      6  CG  PRO A   1      -2.430  32.548  -5.075  1.00 36.31           C  
ANISOU    6  CG  PRO A   1     5542   4607   3647    641    228   1097       C  
ATOM      7  CD  PRO A   1      -3.771  32.631  -4.405  1.00 35.70           C  
ANISOU    7  CD  PRO A   1     6030   3950   3583    498    744    985       C  
ATOM      8  N   GLN A   2      -3.445  34.411  -8.725  1.00 25.19           N  
ANISOU    8  N   GLN A   2     4369   2494   2709    260   1128    -89       N  
ATOM      9  CA  GLN A   2      -3.377  33.951 -10.109  1.00 21.15           C  
ANISOU    9  CA  GLN A   2     3247   2038   2752    352   1109    -26       C  
ATOM     10  C   GLN A   2      -1.894  33.847 -10.423  1.00 22.72           C  
ANISOU   10  C   GLN A   2     3120   2112   3401    177    874   -276       C  
ATOM     11  O   GLN A   2      -1.173  34.847 -10.292  1.00 27.69           O  
ANISOU   11  O   GLN A   2     3395   2238   4886    -56    657   -268       O  
ATOM     12  CB  GLN A   2      -4.054  34.903 -11.086  1.00 24.78           C  
ANISOU   12  CB  GLN A   2     3774   2581   3061    691    688     14       C  
ATOM     13  CG  GLN A   2      -3.799  34.492 -12.528  1.00 26.10           C  
ANISOU   13  CG  GLN A   2     4168   2865   2883   -459    350   -189       C  
ATOM     14  CD  GLN A   2      -4.661  35.198 -13.552  1.00 32.25           C  
ANISOU   14  CD  GLN A   2     5640   3149   3465   -827    -44    951       C  
ATOM     15  OE1 GLN A   2      -4.249  36.162 -14.201  1.00 46.29           O  
ANISOU   15  OE1 GLN A   2     7485   4660   5443   -931   1198   2411       O  
ATOM     16  NE2 GLN A   2      -5.895  34.712 -13.727  1.00 35.81           N  
ANISOU   16  NE2 GLN A   2     4562   3615   5429    438   -375   1534       N  
ATOM     17  N   ILE A   3      -1.469  32.654 -10.771  1.00 18.57           N  
ANISOU   17  N   ILE A   3     2641   2203   2214    424    111   -121       N  
ATOM     18  CA  ILE A   3      -0.032  32.405 -10.981  1.00 17.72           C  
ANISOU   18  CA  ILE A   3     2569   2374   1790    266     70     27       C  
ATOM     19  C   ILE A   3       0.240  32.106 -12.435  1.00 17.59           C  
ANISOU   19  C   ILE A   3     2877   1926   1880   -247    327     43       C  
ATOM     20  O   ILE A   3      -0.300  31.144 -13.000  1.00 17.50           O  
ANISOU   20  O   ILE A   3     2670   1958   2021   -235    418    -50       O  
ATOM     21  CB  ILE A   3       0.397  31.219 -10.091  1.00 19.24           C  
ANISOU   21  CB  ILE A   3     2883   2583   1845    835    423     52       C  
ATOM     22  CG1 ILE A   3       0.124  31.508  -8.602  1.00 22.10           C  
ANISOU   22  CG1 ILE A   3     3373   3325   1699   -155    477    180       C  
ATOM     23  CG2 ILE A   3       1.859  30.848 -10.318  1.00 20.96           C  
ANISOU   23  CG2 ILE A   3     2667   2501   2795    629    102   -382       C  
ATOM     24  CD1 ILE A   3       0.394  30.383  -7.639  1.00 24.93           C  
ANISOU   24  CD1 ILE A   3     3853   3739   1880    608    152    188       C  
ATOM     25  N   THR A   4       1.065  32.956 -13.047  1.00 16.71           N  
ANISOU   25  N   THR A   4     2546   1748   2054    -29    278     70       N  
ATOM     26  CA  THR A   4       1.446  32.654 -14.428  1.00 16.60           C  
ANISOU   26  CA  THR A   4     2576   1628   2104    -14    476     47       C  
ATOM     27  C   THR A   4       2.564  31.625 -14.415  1.00 15.85           C  
ANISOU   27  C   THR A   4     2559   1681   1782    -54    156     95       C  
ATOM     28  O   THR A   4       3.133  31.257 -13.372  1.00 18.15           O  
ANISOU   28  O   THR A   4     2696   2364   1835   -172    -81    -60       O  
ATOM     29  CB  THR A   4       1.865  33.933 -15.174  1.00 18.05           C  
ANISOU   29  CB  THR A   4     2643   1831   2386    -65    150    438       C  
ATOM     30  OG1 THR A   4       2.877  34.644 -14.448  1.00 19.36           O  
ANISOU   30  OG1 THR A   4     2862   1901   2592   -234    205    224       O  
ATOM     31  CG2 THR A   4       0.676  34.882 -15.297  1.00 20.75           C  
ANISOU   31  CG2 THR A   4     3016   2011   2855    259     90    438       C  
ATOM     32  N   LEU A   5       2.891  31.175 -15.635  1.00 14.47           N  
ANISOU   32  N   LEU A   5     1858   1903   1737    -89    259    165       N  
ATOM     33  CA  LEU A   5       3.748  30.014 -15.709  1.00 12.74           C  
ANISOU   33  CA  LEU A   5     1638   1752   1452   -227    -63    221       C  
ATOM     34  C   LEU A   5       5.033  30.261 -16.458  1.00 12.35           C  
ANISOU   34  C   LEU A   5     1875   1487   1328   -279    196    208       C  
ATOM     35  O   LEU A   5       5.639  29.330 -16.989  1.00 13.18           O  
ANISOU   35  O   LEU A   5     2041   1481   1486   -272    206    217       O  
ATOM     36  CB  LEU A   5       2.941  28.838 -16.303  1.00 14.61           C  
ANISOU   36  CB  LEU A   5     2142   1899   1511   -667     73    261       C  
ATOM     37  CG  LEU A   5       1.835  28.341 -15.346  1.00 13.51           C  
ANISOU   37  CG  LEU A   5     1954   1846   1335   -394     13    234       C  
ATOM     38  CD1 LEU A   5       0.859  27.431 -16.059  1.00 15.47           C  
ANISOU   38  CD1 LEU A   5     1807   1813   2258   -380   -463    384       C  
ATOM     39  CD2 LEU A   5       2.451  27.646 -14.129  1.00 14.58           C  
ANISOU   39  CD2 LEU A   5     2055   2172   1312   -424    -10    305       C  
ATOM     40  N   TRP A   6       5.479  31.531 -16.500  1.00 13.78           N  
ANISOU   40  N   TRP A   6     2067   1560   1610   -414    -14    161       N  
ATOM     41  CA  TRP A   6       6.746  31.825 -17.181  1.00 14.87           C  
ANISOU   41  CA  TRP A   6     2148   1820   1682   -651    -53    523       C  
ATOM     42  C   TRP A   6       7.960  31.342 -16.391  1.00 14.91           C  
ANISOU   42  C   TRP A   6     1995   2075   1595   -656     94    517       C  
ATOM     43  O   TRP A   6       9.046  31.133 -16.955  1.00 19.63           O  
ANISOU   43  O   TRP A   6     2222   3258   1977   -250    409    894       O  
ATOM     44  CB  TRP A   6       6.926  33.315 -17.420  1.00 16.55           C  
ANISOU   44  CB  TRP A   6     2842   1783   1663   -657    -99    422       C  
ATOM     45  CG  TRP A   6       5.832  33.907 -18.247  1.00 18.32           C  
ANISOU   45  CG  TRP A   6     3277   1928   1755   -292   -118    533       C  
ATOM     46  CD1 TRP A   6       4.677  34.487 -17.833  1.00 17.69           C  
ANISOU   46  CD1 TRP A   6     3191   1706   1824   -372   -428    138       C  
ATOM     47  CD2 TRP A   6       5.812  33.957 -19.696  1.00 18.74           C  
ANISOU   47  CD2 TRP A   6     3299   2094   1729   -524   -140    645       C  
ATOM     48  NE1 TRP A   6       3.927  34.911 -18.940  1.00 19.21           N  
ANISOU   48  NE1 TRP A   6     3016   2471   1811   -564   -391    505       N  
ATOM     49  CE2 TRP A   6       4.618  34.590 -20.082  1.00 18.50           C  
ANISOU   49  CE2 TRP A   6     3255   1932   1841   -677   -425    287       C  
ATOM     50  CE3 TRP A   6       6.706  33.526 -20.689  1.00 20.20           C  
ANISOU   50  CE3 TRP A   6     3237   2779   1660   -586   -302    210       C  
ATOM     51  CZ2 TRP A   6       4.302  34.797 -21.434  1.00 18.33           C  
ANISOU   51  CZ2 TRP A   6     3208   1932   1823   -525   -192    535       C  
ATOM     52  CZ3 TRP A   6       6.388  33.739 -22.038  1.00 19.36           C  
ANISOU   52  CZ3 TRP A   6     3331   2288   1738   -296   -285    467       C  
ATOM     53  CH2 TRP A   6       5.191  34.369 -22.381  1.00 19.07           C  
ANISOU   53  CH2 TRP A   6     2938   2313   1996   -569   -187    408       C  
ATOM     54  N   GLN A   7       7.761  31.149 -15.091  1.00 14.70           N  
ANISOU   54  N   GLN A   7     2035   2010   1541   -596     22    388       N  
ATOM     55  CA  GLN A   7       8.722  30.636 -14.144  1.00 16.10           C  
ANISOU   55  CA  GLN A   7     2220   2185   1712   -482    -95    487       C  
ATOM     56  C   GLN A   7       8.119  29.448 -13.407  1.00 14.54           C  
ANISOU   56  C   GLN A   7     2040   1709   1777   -304   -117    260       C  
ATOM     57  O   GLN A   7       6.891  29.285 -13.424  1.00 15.36           O  
ANISOU   57  O   GLN A   7     2055   2190   1592   -330    -36    462       O  
ATOM     58  CB  GLN A   7       9.161  31.738 -13.141  1.00 22.87           C  
ANISOU   58  CB  GLN A   7     3178   2262   3249  -1026  -1454    432       C  
ATOM     59  CG  GLN A   7       9.786  32.885 -13.948  1.00 29.38           C  
ANISOU   59  CG  GLN A   7     4640   2140   4384  -1003  -1445   1003       C  
ATOM     60  CD  GLN A   7      10.258  34.093 -13.198  1.00 37.65           C  
ANISOU   60  CD  GLN A   7     6252   3137   4917  -2552   -746    521       C  
ATOM     61  OE1 GLN A   7      10.794  35.054 -13.796  1.00 42.08           O  
ANISOU   61  OE1 GLN A   7     6290   3331   6368  -2683  -2189   1731       O  
ATOM     62  NE2 GLN A   7      10.076  34.022 -11.873  1.00 48.11           N  
ANISOU   62  NE2 GLN A   7     8741   5007   4532  -2882  -1748    391       N  
ATOM     63  N   ARG A   8       8.944  28.630 -12.769  1.00 14.48           N  
ANISOU   63  N   ARG A   8     2045   1903   1553   -305    -92    226       N  
ATOM     64  CA  ARG A   8       8.399  27.493 -12.032  1.00 14.21           C  
ANISOU   64  CA  ARG A   8     2083   1716   1602    -91      1    238       C  
ATOM     65  C   ARG A   8       7.497  28.005 -10.938  1.00 13.36           C  
ANISOU   65  C   ARG A   8     1948   1675   1454    -67   -142    233       C  
ATOM     66  O   ARG A   8       7.882  28.935 -10.201  1.00 15.28           O  
ANISOU   66  O   ARG A   8     2442   1675   1689   -417    131    197       O  
ATOM     67  CB  ARG A   8       9.557  26.674 -11.419  1.00 15.69           C  
ANISOU   67  CB  ARG A   8     2047   2242   1674     91     53    342       C  
ATOM     68  CG  ARG A   8      10.384  25.994 -12.510  1.00 18.18           C  
ANISOU   68  CG  ARG A   8     2216   2631   2058    336    150    202       C  
ATOM     69  CD  ARG A   8      11.510  25.148 -11.911  1.00 22.13           C  
ANISOU   69  CD  ARG A   8     2595   3348   2466    857   -162     25       C  
ATOM     70  NE  ARG A   8      12.207  24.385 -12.970  1.00 24.83           N  
ANISOU   70  NE  ARG A   8     2979   3565   2891   1109     29    -63       N  
ATOM     71  CZ  ARG A   8      13.344  23.733 -12.781  1.00 26.74           C  
ANISOU   71  CZ  ARG A   8     3333   3948   2879   1486   -398   -592       C  
ATOM     72  NH1 ARG A   8      13.902  23.784 -11.560  1.00 33.47           N  
ANISOU   72  NH1 ARG A   8     3680   5889   3146   1259   -804   -657       N  
ATOM     73  NH2 ARG A   8      13.944  23.054 -13.757  1.00 28.55           N  
ANISOU   73  NH2 ARG A   8     2366   4575   3908    479    -47  -1585       N  
ATOM     74  N   PRO A   9       6.326  27.440 -10.756  1.00 14.18           N  
ANISOU   74  N   PRO A   9     1924   1807   1656    -49   -110    -17       N  
ATOM     75  CA  PRO A   9       5.403  27.958  -9.716  1.00 13.08           C  
ANISOU   75  CA  PRO A   9     1998   1706   1267    -81   -160    196       C  
ATOM     76  C   PRO A   9       5.718  27.420  -8.328  1.00 15.23           C  
ANISOU   76  C   PRO A   9     2254   2054   1479   -516   -365    475       C  
ATOM     77  O   PRO A   9       5.054  26.519  -7.805  1.00 15.52           O  
ANISOU   77  O   PRO A   9     2640   1785   1472   -467    -99    268       O  
ATOM     78  CB  PRO A   9       4.034  27.504 -10.231  1.00 13.38           C  
ANISOU   78  CB  PRO A   9     1969   1832   1284    -85    -99      5       C  
ATOM     79  CG  PRO A   9       4.309  26.220 -10.947  1.00 13.94           C  
ANISOU   79  CG  PRO A   9     2040   1749   1508   -158    130     10       C  
ATOM     80  CD  PRO A   9       5.675  26.403 -11.586  1.00 14.88           C  
ANISOU   80  CD  PRO A   9     1765   2250   1639   -114    -88   -216       C  
ATOM     81  N   ILE A  10       6.766  28.041  -7.761  1.00 15.95           N  
ANISOU   81  N   ILE A  10     2152   2430   1477   -442   -301    110       N  
ATOM     82  CA  ILE A  10       7.243  27.642  -6.429  1.00 17.02           C  
ANISOU   82  CA  ILE A  10     2372   2764   1333   -600   -259    -16       C  
ATOM     83  C   ILE A  10       6.526  28.520  -5.410  1.00 17.97           C  
ANISOU   83  C   ILE A  10     3295   1950   1585   -733     71    119       C  
ATOM     84  O   ILE A  10       6.459  29.750  -5.600  1.00 22.97           O  
ANISOU   84  O   ILE A  10     4884   1890   1955  -1128    -20    118       O  
ATOM     85  CB  ILE A  10       8.774  27.727  -6.342  1.00 21.21           C  
ANISOU   85  CB  ILE A  10     2428   3714   1918   -527   -722    373       C  
ATOM     86  CG1 ILE A  10       9.396  26.700  -7.287  1.00 28.02           C  
ANISOU   86  CG1 ILE A  10     2681   5506   2458    556   -105    215       C  
ATOM     87  CG2 ILE A  10       9.213  27.566  -4.897  1.00 21.90           C  
ANISOU   87  CG2 ILE A  10     2976   3307   2036  -1048   -870    951       C  
ATOM     88  CD1 ILE A  10      10.874  26.816  -7.588  1.00 32.09           C  
ANISOU   88  CD1 ILE A  10     3220   5651   3321   -894    769    -47       C  
ATOM     89  N   VAL A  11       5.956  27.866  -4.394  1.00 16.86           N  
ANISOU   89  N   VAL A  11     2615   2227   1562   -497     31    283       N  
ATOM     90  CA  VAL A  11       5.222  28.615  -3.386  1.00 17.62           C  
ANISOU   90  CA  VAL A  11     2551   2412   1733   -252   -104    239       C  
ATOM     91  C   VAL A  11       5.727  28.198  -1.998  1.00 16.66           C  
ANISOU   91  C   VAL A  11     2476   2229   1627   -657    -94    130       C  
ATOM     92  O   VAL A  11       6.372  27.176  -1.847  1.00 17.94           O  
ANISOU   92  O   VAL A  11     2361   2884   1570   -241   -213    291       O  
ATOM     93  CB  VAL A  11       3.698  28.434  -3.424  1.00 21.28           C  
ANISOU   93  CB  VAL A  11     2466   3128   2490    177   -256    100       C  
ATOM     94  CG1 VAL A  11       3.131  28.890  -4.782  1.00 22.90           C  
ANISOU   94  CG1 VAL A  11     2943   3065   2691    982   -537   -178       C  
ATOM     95  CG2 VAL A  11       3.290  26.998  -3.140  1.00 20.10           C  
ANISOU   95  CG2 VAL A  11     2385   3652   1598   -683    400   -120       C  
ATOM     96  N   THR A  12       5.390  29.047  -1.025  1.00 21.01           N  
ANISOU   96  N   THR A  12     3241   2915   1825   -570    196   -209       N  
ATOM     97  CA  THR A  12       5.740  28.767   0.348  1.00 22.12           C  
ANISOU   97  CA  THR A  12     3242   3416   1747   -208    294   -166       C  
ATOM     98  C   THR A  12       4.618  27.954   0.978  1.00 23.09           C  
ANISOU   98  C   THR A  12     2992   3805   1974    -63    107    338       C  
ATOM     99  O   THR A  12       3.433  28.289   0.873  1.00 24.33           O  
ANISOU   99  O   THR A  12     3091   3417   2738     56    209    307       O  
ATOM    100  CB  THR A  12       5.920  30.036   1.196  1.00 25.99           C  
ANISOU  100  CB  THR A  12     3977   3896   2004   -269    -24   -600       C  
ATOM    101  OG1 THR A  12       7.002  30.827   0.665  1.00 32.31           O  
ANISOU  101  OG1 THR A  12     4671   4790   2815  -1423   -186  -1016       O  
ATOM    102  CG2 THR A  12       6.293  29.670   2.623  1.00 35.00           C  
ANISOU  102  CG2 THR A  12     4306   7222   1771   -168    -94   -791       C  
ATOM    103  N   ILE A  13       5.022  26.890   1.650  1.00 22.39           N  
ANISOU  103  N   ILE A  13     2926   3828   1752    -93     -6    271       N  
ATOM    104  CA  ILE A  13       4.043  26.156   2.434  1.00 22.38           C  
ANISOU  104  CA  ILE A  13     2696   4013   1796    197     57    475       C  
ATOM    105  C   ILE A  13       4.441  26.127   3.894  1.00 25.97           C  
ANISOU  105  C   ILE A  13     2799   5272   1795   -172    -14    507       C  
ATOM    106  O   ILE A  13       5.628  26.181   4.220  1.00 38.88           O  
ANISOU  106  O   ILE A  13     2790  10165   1819   -259      2   1088       O  
ATOM    107  CB  ILE A  13       3.958  24.718   1.904  1.00 24.37           C  
ANISOU  107  CB  ILE A  13     2850   3978   2432   -139     55    495       C  
ATOM    108  CG1 ILE A  13       5.286  23.976   2.073  1.00 29.11           C  
ANISOU  108  CG1 ILE A  13     3768   4250   3041    747   -284    247       C  
ATOM    109  CG2 ILE A  13       3.553  24.791   0.463  1.00 30.32           C  
ANISOU  109  CG2 ILE A  13     3689   5282   2550    959   -393   -586       C  
ATOM    110  CD1 ILE A  13       5.312  22.597   1.502  1.00 32.03           C  
ANISOU  110  CD1 ILE A  13     4346   4216   3609    174   1326    162       C  
ATOM    111  N   LYS A  14       3.459  26.067   4.749  1.00 19.34           N  
ANISOU  111  N   LYS A  14     2738   2905   1703   -715   -126    293       N  
ATOM    112  CA  LYS A  14       3.714  25.898   6.173  1.00 18.37           C  
ANISOU  112  CA  LYS A  14     2848   2424   1708   -227      7     82       C  
ATOM    113  C   LYS A  14       3.235  24.531   6.607  1.00 19.30           C  
ANISOU  113  C   LYS A  14     3001   2459   1873   -247    -27    205       C  
ATOM    114  O   LYS A  14       2.051  24.238   6.427  1.00 20.48           O  
ANISOU  114  O   LYS A  14     3189   2736   1856   -553   -266    376       O  
ATOM    115  CB  LYS A  14       2.989  27.019   6.927  1.00 22.92           C  
ANISOU  115  CB  LYS A  14     3431   2606   2671   -372   1093   -121       C  
ATOM    116  CG  LYS A  14       3.752  27.331   8.213  1.00 32.36           C  
ANISOU  116  CG  LYS A  14     4587   4072   3637    681    370  -1858       C  
ATOM    117  CD  LYS A  14       3.275  28.618   8.874  1.00 45.06           C  
ANISOU  117  CD  LYS A  14     6806   5705   4610   2120    565  -2878       C  
ATOM    118  CE  LYS A  14       2.246  28.339   9.952  1.00 51.63           C  
ANISOU  118  CE  LYS A  14     6982   6730   5905   3559   1483  -2004       C  
ATOM    119  NZ  LYS A  14       2.357  29.286  11.114  1.00 61.25           N  
ANISOU  119  NZ  LYS A  14     8656   9879   4737   2283   1822  -2153       N  
ATOM    120  N   ILE A  15       4.166  23.762   7.165  1.00 21.51           N  
ANISOU  120  N   ILE A  15     3196   2636   2339   -117    -47    373       N  
ATOM    121  CA  ILE A  15       3.912  22.391   7.550  1.00 21.37           C  
ANISOU  121  CA  ILE A  15     3531   2816   1772   -110   -103    589       C  
ATOM    122  C   ILE A  15       4.981  21.868   8.520  1.00 24.91           C  
ANISOU  122  C   ILE A  15     3580   3378   2506   -473   -638    905       C  
ATOM    123  O   ILE A  15       6.196  22.116   8.453  1.00 23.82           O  
ANISOU  123  O   ILE A  15     3616   2535   2899   -556   -624    122       O  
ATOM    124  CB  ILE A  15       3.913  21.441   6.339  1.00 21.79           C  
ANISOU  124  CB  ILE A  15     2893   2879   2507   -220   -214    113       C  
ATOM    125  CG1 ILE A  15       3.526  20.024   6.748  1.00 21.12           C  
ANISOU  125  CG1 ILE A  15     2967   3013   2046   -221   -399    332       C  
ATOM    126  CG2 ILE A  15       5.259  21.565   5.615  1.00 20.22           C  
ANISOU  126  CG2 ILE A  15     2823   2488   2372      9   -258    107       C  
ATOM    127  CD1 ILE A  15       3.468  19.025   5.638  1.00 24.78           C  
ANISOU  127  CD1 ILE A  15     3980   3017   2420   -642   -310    144       C  
ATOM    128  N   GLY A  16       4.478  21.064   9.467  1.00 22.92           N  
ANISOU  128  N   GLY A  16     3587   3122   1999     56   -471    666       N  
ATOM    129  CA  GLY A  16       5.405  20.524  10.460  1.00 23.66           C  
ANISOU  129  CA  GLY A  16     3132   3554   2304   -341   -612    755       C  
ATOM    130  C   GLY A  16       6.182  21.574  11.225  1.00 28.85           C  
ANISOU  130  C   GLY A  16     3466   4080   3414   -510   -882    247       C  
ATOM    131  O   GLY A  16       7.317  21.284  11.644  1.00 30.90           O  
ANISOU  131  O   GLY A  16     3142   5068   3531   -497   -696   -136       O  
ATOM    132  N   GLY A  17       5.567  22.748  11.395  1.00 28.48           N  
ANISOU  132  N   GLY A  17     3777   4210   2832   -455   -625   -143       N  
ATOM    133  CA  GLY A  17       6.183  23.847  12.116  1.00 28.62           C  
ANISOU  133  CA  GLY A  17     3544   5000   2332   -494   -213   -738       C  
ATOM    134  C   GLY A  17       7.283  24.508  11.315  1.00 32.65           C  
ANISOU  134  C   GLY A  17     4494   5218   2691  -1355    -40   -860       C  
ATOM    135  O   GLY A  17       8.038  25.319  11.846  1.00 32.78           O  
ANISOU  135  O   GLY A  17     5470   3706   3277  -1198   -163   -672       O  
ATOM    136  N   GLN A  18       7.431  24.172  10.039  1.00 28.61           N  
ANISOU  136  N   GLN A  18     3929   4806   2134   -820   -518     75       N  
ATOM    137  CA  GLN A  18       8.487  24.717   9.235  1.00 25.62           C  
ANISOU  137  CA  GLN A  18     3092   4003   2640    -19   -550    204       C  
ATOM    138  C   GLN A  18       7.860  25.519   8.087  1.00 22.92           C  
ANISOU  138  C   GLN A  18     3103   3332   2273     80   -376   -219       C  
ATOM    139  O   GLN A  18       6.730  25.227   7.691  1.00 22.45           O  
ANISOU  139  O   GLN A  18     3094   3265   2169    199   -358   -191       O  
ATOM    140  CB  GLN A  18       9.342  23.596   8.628  1.00 35.74           C  
ANISOU  140  CB  GLN A  18     4155   4862   4561   1358   -212    534       C  
ATOM    141  CG  GLN A  18      10.451  22.949   9.431  1.00 40.55           C  
ANISOU  141  CG  GLN A  18     3965   5556   5884   1078   -170   1801       C  
ATOM    142  CD  GLN A  18      11.219  21.934   8.584  1.00 41.71           C  
ANISOU  142  CD  GLN A  18     3987   5264   6596   1461    406   2455       C  
ATOM    143  OE1 GLN A  18      11.804  22.281   7.548  1.00 48.47           O  
ANISOU  143  OE1 GLN A  18     5318   5311   7785   -355   1916   1390       O  
ATOM    144  NE2 GLN A  18      11.215  20.664   8.976  1.00 39.64           N  
ANISOU  144  NE2 GLN A  18     4550   4812   5699    227  -1639   1608       N  
ATOM    145  N   LEU A  19       8.587  26.484   7.549  1.00 27.94           N  
ANISOU  145  N   LEU A  19     3582   4322   2712   -486   -499    411       N  
ATOM    146  CA  LEU A  19       8.258  27.046   6.237  1.00 28.12           C  
ANISOU  146  CA  LEU A  19     4521   3756   2409   -247   -483    -15       C  
ATOM    147  C   LEU A  19       9.123  26.340   5.188  1.00 29.02           C  
ANISOU  147  C   LEU A  19     3693   4566   2766    112   -564     32       C  
ATOM    148  O   LEU A  19      10.335  26.227   5.321  1.00 36.96           O  
ANISOU  148  O   LEU A  19     3427   7174   3441   -632   -249    746       O  
ATOM    149  CB  LEU A  19       8.435  28.562   6.198  1.00 31.05           C  
ANISOU  149  CB  LEU A  19     4496   3775   3528   -343  -1067    177       C  
ATOM    150  CG  LEU A  19       7.408  29.349   7.026  1.00 36.61           C  
ANISOU  150  CG  LEU A  19     5677   3837   4394   -369   -799   -943       C  
ATOM    151  CD1 LEU A  19       7.717  30.845   6.987  1.00 47.86           C  
ANISOU  151  CD1 LEU A  19     8711   3712   5763   -454  -2519  -1282       C  
ATOM    152  CD2 LEU A  19       5.983  29.114   6.567  1.00 36.56           C  
ANISOU  152  CD2 LEU A  19     4922   4840   4129     61     -4   -450       C  
ATOM    153  N   LYS A  20       8.453  25.827   4.154  1.00 25.38           N  
ANISOU  153  N   LYS A  20     3862   3914   1868    155   -181    475       N  
ATOM    154  CA  LYS A  20       9.131  25.123   3.084  1.00 24.04           C  
ANISOU  154  CA  LYS A  20     3118   3766   2248    322    -65    711       C  
ATOM    155  C   LYS A  20       8.742  25.712   1.739  1.00 20.17           C  
ANISOU  155  C   LYS A  20     2387   3441   1837   -306   -455     21       C  
ATOM    156  O   LYS A  20       7.702  26.340   1.632  1.00 24.65           O  
ANISOU  156  O   LYS A  20     2879   4375   2111    440     62    786       O  
ATOM    157  CB  LYS A  20       8.785  23.637   3.125  1.00 26.78           C  
ANISOU  157  CB  LYS A  20     3929   3717   2530    316  -1076    421       C  
ATOM    158  CG  LYS A  20       9.212  22.966   4.439  1.00 35.61           C  
ANISOU  158  CG  LYS A  20     5372   4828   3331    938   -488   1842       C  
ATOM    159  CD  LYS A  20       9.663  21.545   4.187  1.00 39.84           C  
ANISOU  159  CD  LYS A  20     5502   4916   4720   1191   -560   1901       C  
ATOM    160  CE  LYS A  20      11.164  21.429   4.004  1.00 41.38           C  
ANISOU  160  CE  LYS A  20     5600   5661   4463   1137   -135   1069       C  
ATOM    161  NZ  LYS A  20      11.952  21.116   5.223  1.00 34.18           N  
ANISOU  161  NZ  LYS A  20     4433   4706   3848    954    536    728       N  
ATOM    162  N   GLU A  21       9.612  25.485   0.757  1.00 20.33           N  
ANISOU  162  N   GLU A  21     2802   3105   1817     41   -461   -285       N  
ATOM    163  CA  GLU A  21       9.244  25.829  -0.627  1.00 20.93           C  
ANISOU  163  CA  GLU A  21     2990   3238   1724   -617   -442   -209       C  
ATOM    164  C   GLU A  21       8.845  24.593  -1.394  1.00 19.62           C  
ANISOU  164  C   GLU A  21     2652   2865   1937   -623   -746    161       C  
ATOM    165  O   GLU A  21       9.507  23.570  -1.216  1.00 21.38           O  
ANISOU  165  O   GLU A  21     2945   2887   2290   -608   -893    311       O  
ATOM    166  CB  GLU A  21      10.433  26.462  -1.372  1.00 28.10           C  
ANISOU  166  CB  GLU A  21     4316   3710   2652  -1791    125   -279       C  
ATOM    167  CG  GLU A  21      11.084  27.637  -0.685  1.00 37.15           C  
ANISOU  167  CG  GLU A  21     5548   4271   4296  -2409    465  -1118       C  
ATOM    168  CD  GLU A  21      10.156  28.833  -0.815  1.00 44.43           C  
ANISOU  168  CD  GLU A  21     7564   3884   5432  -1897    234  -1041       C  
ATOM    169  OE1 GLU A  21      10.180  29.408  -1.929  1.00 53.71           O  
ANISOU  169  OE1 GLU A  21    10887   5559   3961    397   -444  -1855       O  
ATOM    170  OE2 GLU A  21       9.470  29.080   0.213  1.00 38.46           O  
ANISOU  170  OE2 GLU A  21     5106   4030   5477  -1601   -381   -254       O  
ATOM    171  N   ALA A  22       7.832  24.685  -2.264  1.00 17.71           N  
ANISOU  171  N   ALA A  22     2225   2747   1758   -582   -337     85       N  
ATOM    172  CA  ALA A  22       7.456  23.527  -3.042  1.00 15.91           C  
ANISOU  172  CA  ALA A  22     2241   2456   1348   -653   -364    459       C  
ATOM    173  C   ALA A  22       6.815  23.967  -4.367  1.00 14.01           C  
ANISOU  173  C   ALA A  22     1978   2119   1226   -404     11    393       C  
ATOM    174  O   ALA A  22       6.248  25.048  -4.471  1.00 16.32           O  
ANISOU  174  O   ALA A  22     2515   2132   1555   -262   -212    293       O  
ATOM    175  CB  ALA A  22       6.481  22.650  -2.275  1.00 16.10           C  
ANISOU  175  CB  ALA A  22     2143   2604   1372   -456   -306    705       C  
ATOM    176  N   LEU A  23       6.962  23.075  -5.344  1.00 14.76           N  
ANISOU  176  N   LEU A  23     2292   1927   1388   -574   -265    276       N  
ATOM    177  CA  LEU A  23       6.498  23.306  -6.701  1.00 13.46           C  
ANISOU  177  CA  LEU A  23     1921   1872   1320   -255    -41    129       C  
ATOM    178  C   LEU A  23       5.024  22.926  -6.828  1.00 13.37           C  
ANISOU  178  C   LEU A  23     1955   1733   1393   -290    -88    144       C  
ATOM    179  O   LEU A  23       4.729  21.754  -6.543  1.00 14.82           O  
ANISOU  179  O   LEU A  23     2068   1835   1728   -326    107    272       O  
ATOM    180  CB  LEU A  23       7.384  22.445  -7.611  1.00 15.16           C  
ANISOU  180  CB  LEU A  23     2091   1932   1737     97   -165    -78       C  
ATOM    181  CG  LEU A  23       7.100  22.524  -9.103  1.00 17.02           C  
ANISOU  181  CG  LEU A  23     2752   2188   1528   -232    298    -64       C  
ATOM    182  CD1 LEU A  23       7.371  23.934  -9.593  1.00 20.03           C  
ANISOU  182  CD1 LEU A  23     3158   2395   2058   -795   -492    270       C  
ATOM    183  CD2 LEU A  23       7.929  21.543  -9.948  1.00 21.34           C  
ANISOU  183  CD2 LEU A  23     3034   3215   1859    659    245   -116       C  
ATOM    184  N   LEU A  24       4.148  23.816  -7.252  1.00 13.97           N  
ANISOU  184  N   LEU A  24     1917   1905   1487   -226    -24    244       N  
ATOM    185  CA  LEU A  24       2.783  23.419  -7.615  1.00 13.91           C  
ANISOU  185  CA  LEU A  24     2004   1600   1682   -200   -161   -125       C  
ATOM    186  C   LEU A  24       2.831  22.607  -8.905  1.00 13.69           C  
ANISOU  186  C   LEU A  24     2225   1545   1431   -223    157    144       C  
ATOM    187  O   LEU A  24       3.102  23.159  -9.991  1.00 15.93           O  
ANISOU  187  O   LEU A  24     2386   2126   1539   -723   -142    469       O  
ATOM    188  CB  LEU A  24       1.865  24.622  -7.829  1.00 14.03           C  
ANISOU  188  CB  LEU A  24     1763   1831   1738   -109    293      3       C  
ATOM    189  CG  LEU A  24       1.613  25.461  -6.563  1.00 14.35           C  
ANISOU  189  CG  LEU A  24     2036   1782   1634    -41    219     83       C  
ATOM    190  CD1 LEU A  24       0.868  26.745  -6.918  1.00 16.96           C  
ANISOU  190  CD1 LEU A  24     2570   1879   1994    270    -36    -89       C  
ATOM    191  CD2 LEU A  24       0.882  24.654  -5.525  1.00 16.29           C  
ANISOU  191  CD2 LEU A  24     2260   2197   1731   -373    306     64       C  
ATOM    192  N   ASN A  25       2.543  21.303  -8.793  1.00 12.74           N  
ANISOU  192  N   ASN A  25     2152   1404   1285    -89    -33     95       N  
ATOM    193  CA  ASN A  25       2.863  20.410  -9.905  1.00 12.18           C  
ANISOU  193  CA  ASN A  25     1512   1704   1411   -149     57     -5       C  
ATOM    194  C   ASN A  25       1.621  19.646 -10.329  1.00 12.60           C  
ANISOU  194  C   ASN A  25     1852   1753   1181   -409     10    163       C  
ATOM    195  O   ASN A  25       1.250  18.637  -9.718  1.00 12.53           O  
ANISOU  195  O   ASN A  25     1809   1618   1335   -214    176    172       O  
ATOM    196  CB  ASN A  25       3.994  19.461  -9.478  1.00 13.06           C  
ANISOU  196  CB  ASN A  25     1920   1390   1651    -87    -40    238       C  
ATOM    197  CG  ASN A  25       4.520  18.631 -10.643  1.00 14.85           C  
ANISOU  197  CG  ASN A  25     1849   2005   1787    224    195    236       C  
ATOM    198  OD1 ASN A  25       3.826  18.551 -11.662  1.00 16.60           O  
ANISOU  198  OD1 ASN A  25     2038   2610   1658    -79    236    -39       O  
ATOM    199  ND2 ASN A  25       5.701  18.030 -10.493  1.00 19.46           N  
ANISOU  199  ND2 ASN A  25     2141   2465   2789    640    378    523       N  
ATOM    200  N   THR A  26       0.977  20.121 -11.402  1.00 11.75           N  
ANISOU  200  N   THR A  26     1493   1736   1234   -284    101    241       N  
ATOM    201  CA  THR A  26      -0.257  19.476 -11.876  1.00 11.38           C  
ANISOU  201  CA  THR A  26     1400   1547   1379   -217    185    293       C  
ATOM    202  C   THR A  26       0.057  18.137 -12.523  1.00 12.36           C  
ANISOU  202  C   THR A  26     1570   1655   1472   -209    136    181       C  
ATOM    203  O   THR A  26      -0.895  17.387 -12.790  1.00 13.24           O  
ANISOU  203  O   THR A  26     1710   1739   1581   -342    367     35       O  
ATOM    204  CB  THR A  26      -1.034  20.361 -12.861  1.00 11.01           C  
ANISOU  204  CB  THR A  26     1514   1656   1015   -149    211     95       C  
ATOM    205  OG1 THR A  26      -0.213  20.645 -13.997  1.00 11.56           O  
ANISOU  205  OG1 THR A  26     1445   1678   1271   -149    268    293       O  
ATOM    206  CG2 THR A  26      -1.470  21.656 -12.187  1.00 12.49           C  
ANISOU  206  CG2 THR A  26     1755   1700   1291     61    110     39       C  
ATOM    207  N   GLY A  27       1.342  17.843 -12.766  1.00 12.85           N  
ANISOU  207  N   GLY A  27     1574   1893   1416    -52    120     24       N  
ATOM    208  CA  GLY A  27       1.706  16.542 -13.281  1.00 13.79           C  
ANISOU  208  CA  GLY A  27     2062   1914   1264    -11    326    122       C  
ATOM    209  C   GLY A  27       1.965  15.527 -12.169  1.00 15.05           C  
ANISOU  209  C   GLY A  27     2352   1983   1383    300    484    158       C  
ATOM    210  O   GLY A  27       2.316  14.383 -12.505  1.00 18.03           O  
ANISOU  210  O   GLY A  27     3236   1837   1776    204    361    -80       O  
ATOM    211  N   ALA A  28       1.794  15.911 -10.913  1.00 13.21           N  
ANISOU  211  N   ALA A  28     1958   1803   1257     20    385    277       N  
ATOM    212  CA  ALA A  28       2.049  15.037  -9.776  1.00 13.18           C  
ANISOU  212  CA  ALA A  28     1932   1636   1440   -397    360    341       C  
ATOM    213  C   ALA A  28       0.730  14.667  -9.109  1.00 12.45           C  
ANISOU  213  C   ALA A  28     1721   1498   1509   -178    276    353       C  
ATOM    214  O   ALA A  28      -0.031  15.554  -8.781  1.00 13.55           O  
ANISOU  214  O   ALA A  28     1931   1838   1381      7     89     91       O  
ATOM    215  CB  ALA A  28       3.011  15.686  -8.796  1.00 13.95           C  
ANISOU  215  CB  ALA A  28     1545   1991   1764     77     26    238       C  
ATOM    216  N   ASP A  29       0.499  13.383  -8.927  1.00 12.38           N  
ANISOU  216  N   ASP A  29     1720   1604   1379   -461     33    315       N  
ATOM    217  CA  ASP A  29      -0.740  12.955  -8.281  1.00 12.73           C  
ANISOU  217  CA  ASP A  29     1881   1679   1277   -621     48    151       C  
ATOM    218  C   ASP A  29      -0.702  13.348  -6.812  1.00 12.85           C  
ANISOU  218  C   ASP A  29     1818   1774   1289     34     23     48       C  
ATOM    219  O   ASP A  29      -1.696  13.749  -6.221  1.00 15.00           O  
ANISOU  219  O   ASP A  29     1877   2237   1583     23    252    253       O  
ATOM    220  CB  ASP A  29      -0.894  11.421  -8.342  1.00 15.44           C  
ANISOU  220  CB  ASP A  29     2649   1735   1483   -905    420     85       C  
ATOM    221  CG  ASP A  29      -1.054  10.867  -9.740  1.00 17.44           C  
ANISOU  221  CG  ASP A  29     3018   1950   1659    -34     66   -275       C  
ATOM    222  OD1 ASP A  29      -0.874   9.631  -9.881  1.00 28.02           O  
ANISOU  222  OD1 ASP A  29     5828   2115   2703    463  -1005   -594       O  
ATOM    223  OD2 ASP A  29      -1.364  11.643 -10.681  1.00 16.73           O  
ANISOU  223  OD2 ASP A  29     2437   2286   1632   -437    131    -61       O  
ATOM    224  N   ASP A  30       0.475  13.179  -6.218  1.00 12.43           N  
ANISOU  224  N   ASP A  30     1831   1680   1212   -180     -1    282       N  
ATOM    225  CA  ASP A  30       0.680  13.272  -4.770  1.00 12.66           C  
ANISOU  225  CA  ASP A  30     1730   1833   1248   -193     -2    104       C  
ATOM    226  C   ASP A  30       1.635  14.364  -4.365  1.00 12.34           C  
ANISOU  226  C   ASP A  30     1463   1818   1406    -99    291   -113       C  
ATOM    227  O   ASP A  30       2.416  14.866  -5.165  1.00 14.49           O  
ANISOU  227  O   ASP A  30     1955   1936   1613   -264    449    136       O  
ATOM    228  CB  ASP A  30       1.257  11.950  -4.246  1.00 15.48           C  
ANISOU  228  CB  ASP A  30     2537   1888   1456   -149   -367    294       C  
ATOM    229  CG  ASP A  30       0.360  10.786  -4.576  1.00 18.49           C  
ANISOU  229  CG  ASP A  30     3167   1833   2025   -320   -218    -63       C  
ATOM    230  OD1 ASP A  30       0.940   9.822  -5.087  1.00 24.72           O  
ANISOU  230  OD1 ASP A  30     4491   1808   3092    254   -253    -70       O  
ATOM    231  OD2 ASP A  30      -0.865  10.831  -4.342  1.00 22.14           O  
ANISOU  231  OD2 ASP A  30     3275   2662   2477  -1077    304     30       O  
ATOM    232  N   THR A  31       1.561  14.729  -3.090  1.00 12.41           N  
ANISOU  232  N   THR A  31     1628   1742   1346    -21     -5    -62       N  
ATOM    233  CA  THR A  31       2.462  15.731  -2.498  1.00 11.95           C  
ANISOU  233  CA  THR A  31     1404   1531   1603    177   -106     -6       C  
ATOM    234  C   THR A  31       3.617  15.042  -1.799  1.00 11.54           C  
ANISOU  234  C   THR A  31     1343   1842   1201    137    144    219       C  
ATOM    235  O   THR A  31       3.366  14.149  -0.972  1.00 13.39           O  
ANISOU  235  O   THR A  31     1552   2202   1334    153    292    495       O  
ATOM    236  CB  THR A  31       1.638  16.594  -1.518  1.00 11.29           C  
ANISOU  236  CB  THR A  31     1429   1536   1324    137   -173     19       C  
ATOM    237  OG1 THR A  31       0.711  17.356  -2.286  1.00 11.86           O  
ANISOU  237  OG1 THR A  31     1378   1779   1351    227     -4    188       O  
ATOM    238  CG2 THR A  31       2.507  17.515  -0.671  1.00 12.92           C  
ANISOU  238  CG2 THR A  31     1576   1728   1603   -146   -141    -80       C  
ATOM    239  N   VAL A  32       4.848  15.378  -2.141  1.00 12.49           N  
ANISOU  239  N   VAL A  32     1243   2218   1284    -83    -68    285       N  
ATOM    240  CA  VAL A  32       6.010  14.710  -1.534  1.00 13.48           C  
ANISOU  240  CA  VAL A  32     1423   1900   1800    -15   -222    432       C  
ATOM    241  C   VAL A  32       6.959  15.785  -1.035  1.00 12.68           C  
ANISOU  241  C   VAL A  32     1264   2035   1520   -143   -129    605       C  
ATOM    242  O   VAL A  32       7.362  16.662  -1.842  1.00 13.81           O  
ANISOU  242  O   VAL A  32     1767   2025   1455   -257    -83    514       O  
ATOM    243  CB  VAL A  32       6.791  13.815  -2.502  1.00 17.93           C  
ANISOU  243  CB  VAL A  32     1918   1918   2976    218     58     95       C  
ATOM    244  CG1 VAL A  32       7.865  13.044  -1.710  1.00 19.32           C  
ANISOU  244  CG1 VAL A  32     2403   2984   1953    969    554    203       C  
ATOM    245  CG2 VAL A  32       5.842  12.928  -3.288  1.00 19.95           C  
ANISOU  245  CG2 VAL A  32     2639   2384   2558   -149    304   -240       C  
ATOM    246  N   LEU A  33       7.286  15.778   0.249  1.00 13.19           N  
ANISOU  246  N   LEU A  33     1797   1757   1456    -61    -70    426       N  
ATOM    247  CA  LEU A  33       8.195  16.748   0.852  1.00 15.73           C  
ANISOU  247  CA  LEU A  33     1821   2120   2037      8   -364     65       C  
ATOM    248  C   LEU A  33       9.323  16.035   1.571  1.00 15.32           C  
ANISOU  248  C   LEU A  33     1637   2214   1970   -294   -109    544       C  
ATOM    249  O   LEU A  33       9.038  14.980   2.154  1.00 14.81           O  
ANISOU  249  O   LEU A  33     1849   2045   1735   -432   -135    307       O  
ATOM    250  CB  LEU A  33       7.448  17.625   1.855  1.00 17.25           C  
ANISOU  250  CB  LEU A  33     2399   1987   2171    -18   -201    -30       C  
ATOM    251  CG  LEU A  33       6.179  18.277   1.220  1.00 17.60           C  
ANISOU  251  CG  LEU A  33     2524   1958   2205    315    188    195       C  
ATOM    252  CD1 LEU A  33       5.312  18.938   2.289  1.00 21.94           C  
ANISOU  252  CD1 LEU A  33     2269   2985   3084   -198    942   -137       C  
ATOM    253  CD2 LEU A  33       6.592  19.262   0.169  1.00 20.80           C  
ANISOU  253  CD2 LEU A  33     2615   2978   2309    192    285    625       C  
ATOM    254  N   GLU A  34      10.511  16.607   1.512  1.00 15.96           N  
ANISOU  254  N   GLU A  34     1601   2344   2118   -386   -103    505       N  
ATOM    255  CA  GLU A  34      11.683  16.113   2.212  1.00 21.17           C  
ANISOU  255  CA  GLU A  34     1755   3728   2561    434   -374   -373       C  
ATOM    256  C   GLU A  34      11.879  16.833   3.536  1.00 19.52           C  
ANISOU  256  C   GLU A  34     1662   3532   2223    219   -155      2       C  
ATOM    257  O   GLU A  34      11.497  18.023   3.591  1.00 24.66           O  
ANISOU  257  O   GLU A  34     3583   3250   2537     83   -453   -103       O  
ATOM    258  CB AGLU A  34      12.905  16.489   1.337  0.45 25.19           C  
ANISOU  258  CB AGLU A  34     1783   4610   3177    942    395  -1208       C  
ATOM    259  CB BGLU A  34      12.958  16.246   1.382  0.55 26.22           C  
ANISOU  259  CB BGLU A  34     1961   5399   2602    973    -68   -460       C  
ATOM    260  CG AGLU A  34      13.588  17.752   1.759  0.45 30.80           C  
ANISOU  260  CG AGLU A  34     2298   4092   5311    268    835   -210       C  
ATOM    261  CG BGLU A  34      13.271  14.962   0.626  0.55 29.05           C  
ANISOU  261  CG BGLU A  34     2396   5241   3401    545    583   -540       C  
ATOM    262  CD AGLU A  34      13.330  19.183   1.412  0.45 33.75           C  
ANISOU  262  CD AGLU A  34     3826   4565   4432    579   1120    588       C  
ATOM    263  CD BGLU A  34      14.669  15.084   0.029  0.55 25.54           C  
ANISOU  263  CD BGLU A  34     1482   5550   2672    793   -462   -867       C  
ATOM    264  OE1AGLU A  34      13.824  19.619   0.328  0.45 39.59           O  
ANISOU  264  OE1AGLU A  34     4815   6210   4017   1299   1286    756       O  
ATOM    265  OE1BGLU A  34      15.299  14.024  -0.124  0.55 46.81           O  
ANISOU  265  OE1BGLU A  34     3804   6070   7913   1753   2331     53       O  
ATOM    266  OE2AGLU A  34      12.704  19.997   2.164  0.45 18.58           O  
ANISOU  266  OE2AGLU A  34     2243   2922   1894   -708  -1048    393       O  
ATOM    267  OE2BGLU A  34      15.073  16.215  -0.245  0.55 24.53           O  
ANISOU  267  OE2BGLU A  34     1587   5882   1851    737   -162   -380       O  
ATOM    268  N   GLU A  35      12.476  16.214   4.521  1.00 23.44           N  
ANISOU  268  N   GLU A  35     1951   4397   2558    374   -530    203       N  
ATOM    269  CA  GLU A  35      12.964  16.866   5.742  1.00 24.12           C  
ANISOU  269  CA  GLU A  35     2422   4426   2315    100   -295    157       C  
ATOM    270  C   GLU A  35      11.907  17.723   6.434  1.00 25.90           C  
ANISOU  270  C   GLU A  35     2679   4337   2826    289   -189    146       C  
ATOM    271  O   GLU A  35      12.026  18.930   6.703  1.00 30.05           O  
ANISOU  271  O   GLU A  35     2629   4936   3851   -359    104  -1038       O  
ATOM    272  CB AGLU A  35      14.220  17.702   5.484  0.56 26.70           C  
ANISOU  272  CB AGLU A  35     2879   3757   3509    -68    217   -670       C  
ATOM    273  CB BGLU A  35      14.199  17.710   5.429  0.44 26.71           C  
ANISOU  273  CB BGLU A  35     2796   3859   3492    -53     71   -429       C  
ATOM    274  CG AGLU A  35      14.038  19.016   4.767  0.56 31.73           C  
ANISOU  274  CG AGLU A  35     3709   4145   4200   -348    159    -83       C  
ATOM    275  CG BGLU A  35      15.289  17.001   4.629  0.44 27.47           C  
ANISOU  275  CG BGLU A  35     2732   4011   3695    -93    386    -97       C  
ATOM    276  CD AGLU A  35      15.278  19.851   4.540  0.56 38.29           C  
ANISOU  276  CD AGLU A  35     4186   4499   5863   -854    -87    340       C  
ATOM    277  CD BGLU A  35      16.530  17.869   4.507  0.44 36.19           C  
ANISOU  277  CD BGLU A  35     2847   5264   5638   -665    478   -641       C  
ATOM    278  OE1AGLU A  35      16.406  19.314   4.553  0.56 47.97           O  
ANISOU  278  OE1AGLU A  35     3734   6972   7518   -392    801  -1220       O  
ATOM    279  OE1BGLU A  35      16.581  18.702   3.574  0.44 38.01           O  
ANISOU  279  OE1BGLU A  35     3620   5056   5767  -2134    509   -746       O  
ATOM    280  OE2AGLU A  35      15.121  21.084   4.345  0.56 53.00           O  
ANISOU  280  OE2AGLU A  35     7754   4441   7943  -1864  -1326    943       O  
ATOM    281  OE2BGLU A  35      17.441  17.705   5.354  0.44 46.40           O  
ANISOU  281  OE2BGLU A  35     2164   6634   8831    111   -303    306       O  
ATOM    282  N   VAL A  36      10.833  17.021   6.759  1.00 23.89           N  
ANISOU  282  N   VAL A  36     2852   3856   2369    454     68     51       N  
ATOM    283  CA  VAL A  36       9.785  17.502   7.638  1.00 24.03           C  
ANISOU  283  CA  VAL A  36     3124   3408   2598    394    211   -124       C  
ATOM    284  C   VAL A  36       9.506  16.347   8.605  1.00 21.80           C  
ANISOU  284  C   VAL A  36     2455   3092   2735   -443     49   -469       C  
ATOM    285  O   VAL A  36       9.497  15.165   8.241  1.00 25.32           O  
ANISOU  285  O   VAL A  36     3590   3142   2887    159   -555   -601       O  
ATOM    286  CB  VAL A  36       8.504  17.915   6.902  1.00 28.25           C  
ANISOU  286  CB  VAL A  36     3397   3686   3650   1081   -122   -573       C  
ATOM    287  CG1 VAL A  36       8.049  16.662   6.174  1.00 32.62           C  
ANISOU  287  CG1 VAL A  36     2566   5294   4533    -84    503  -1659       C  
ATOM    288  CG2 VAL A  36       7.363  18.453   7.756  1.00 35.37           C  
ANISOU  288  CG2 VAL A  36     3125   6443   3872   1000   -426  -1954       C  
ATOM    289  N   ASN A  37       9.295  16.746   9.848  1.00 20.02           N  
ANISOU  289  N   ASN A  37     2261   2682   2662   -189    -58   -256       N  
ATOM    290  CA  ASN A  37       8.929  15.795  10.894  1.00 20.54           C  
ANISOU  290  CA  ASN A  37     1523   3536   2745   -392   -573    266       C  
ATOM    291  C   ASN A  37       7.456  15.988  11.205  1.00 20.98           C  
ANISOU  291  C   ASN A  37     1783   2882   3308   -375   -146   -454       C  
ATOM    292  O   ASN A  37       7.030  17.020  11.714  1.00 26.85           O  
ANISOU  292  O   ASN A  37     2844   2771   4587   -268    297   -542       O  
ATOM    293  CB AASN A  37       9.786  15.929  12.142  0.45 28.79           C  
ANISOU  293  CB AASN A  37     2527   5486   2925   -526  -1001     60       C  
ATOM    294  CB BASN A  37       9.801  16.016  12.121  0.55 28.46           C  
ANISOU  294  CB BASN A  37     2488   5444   2881   -632   -927     39       C  
ATOM    295  CG AASN A  37       9.391  15.067  13.324  0.45 34.15           C  
ANISOU  295  CG AASN A  37     3523   6628   2826    482   -829    714       C  
ATOM    296  CG BASN A  37      11.257  15.991  11.679  0.55 29.76           C  
ANISOU  296  CG BASN A  37     2042   5716   3550   -278  -1559    329       C  
ATOM    297  OD1AASN A  37       8.903  13.929  13.221  0.45 27.74           O  
ANISOU  297  OD1AASN A  37     3372   5539   1628   1616    113   1154       O  
ATOM    298  OD1BASN A  37      11.963  16.976  11.866  0.55 46.39           O  
ANISOU  298  OD1BASN A  37     3066   6606   7953  -1443   -473    125       O  
ATOM    299  ND2AASN A  37       9.611  15.620  14.522  0.45 39.87           N  
ANISOU  299  ND2AASN A  37     5445   6703   3002   1083    455   -234       N  
ATOM    300  ND2BASN A  37      11.647  14.860  11.118  0.55 40.98           N  
ANISOU  300  ND2BASN A  37     3150   8132   4289    -93  -1095  -2369       N  
ATOM    301  N   LEU A  38       6.697  14.954  10.889  1.00 16.82           N  
ANISOU  301  N   LEU A  38     1718   2530   2145   -413    -88    399       N  
ATOM    302  CA  LEU A  38       5.267  14.990  11.195  1.00 16.51           C  
ANISOU  302  CA  LEU A  38     1721   2861   1689   -301   -166    356       C  
ATOM    303  C   LEU A  38       5.006  13.982  12.303  1.00 14.58           C  
ANISOU  303  C   LEU A  38     1257   2629   1653    157   -173    365       C  
ATOM    304  O   LEU A  38       5.596  12.909  12.353  1.00 17.51           O  
ANISOU  304  O   LEU A  38     1907   2704   2042    394     60    150       O  
ATOM    305  CB  LEU A  38       4.435  14.661   9.951  1.00 14.69           C  
ANISOU  305  CB  LEU A  38     1789   2229   1562    284   -181    239       C  
ATOM    306  CG  LEU A  38       4.612  15.677   8.796  1.00 14.40           C  
ANISOU  306  CG  LEU A  38     1950   1832   1689     69   -154    117       C  
ATOM    307  CD1 LEU A  38       3.720  15.244   7.627  1.00 14.69           C  
ANISOU  307  CD1 LEU A  38     1901   2193   1487     96   -109    193       C  
ATOM    308  CD2 LEU A  38       4.285  17.067   9.256  1.00 21.22           C  
ANISOU  308  CD2 LEU A  38     3699   1841   2523    149   -176   -159       C  
ATOM    309  N   PRO A  39       4.084  14.307  13.197  1.00 15.61           N  
ANISOU  309  N   PRO A  39     1757   2295   1881    -34    131    146       N  
ATOM    310  CA  PRO A  39       3.751  13.391  14.286  1.00 15.34           C  
ANISOU  310  CA  PRO A  39     2033   2287   1509     27     53      3       C  
ATOM    311  C   PRO A  39       2.757  12.294  13.952  1.00 15.26           C  
ANISOU  311  C   PRO A  39     1866   2453   1480   -111    203    136       C  
ATOM    312  O   PRO A  39       1.961  12.413  13.021  1.00 16.15           O  
ANISOU  312  O   PRO A  39     1717   2973   1444     71    204    -96       O  
ATOM    313  CB  PRO A  39       3.006  14.311  15.291  1.00 18.26           C  
ANISOU  313  CB  PRO A  39     2624   2677   1637    360    100   -188       C  
ATOM    314  CG  PRO A  39       2.375  15.338  14.395  1.00 18.03           C  
ANISOU  314  CG  PRO A  39     2666   2129   2054    154    461      3       C  
ATOM    315  CD  PRO A  39       3.339  15.579  13.266  1.00 17.74           C  
ANISOU  315  CD  PRO A  39     2182   2296   2262    163    367    117       C  
ATOM    316  N   GLY A  40       2.817  11.230  14.754  1.00 16.69           N  
ANISOU  316  N   GLY A  40     2496   2196   1649    -14    184    -21       N  
ATOM    317  CA  GLY A  40       1.781  10.224  14.721  1.00 16.51           C  
ANISOU  317  CA  GLY A  40     2784   2247   1240   -235    217     -2       C  
ATOM    318  C   GLY A  40       2.016   9.113  13.732  1.00 14.66           C  
ANISOU  318  C   GLY A  40     2195   2221   1155     15    163    127       C  
ATOM    319  O   GLY A  40       3.089   8.887  13.175  1.00 17.32           O  
ANISOU  319  O   GLY A  40     2171   2782   1626    398     48    178       O  
ATOM    320  N   ARG A  41       0.965   8.348  13.493  1.00 15.06           N  
ANISOU  320  N   ARG A  41     2480   2078   1164    -92    160     73       N  
ATOM    321  CA  ARG A  41       1.072   7.154  12.692  1.00 18.29           C  
ANISOU  321  CA  ARG A  41     3721   2046   1182   -265    402     87       C  
ATOM    322  C   ARG A  41       1.175   7.497  11.199  1.00 14.75           C  
ANISOU  322  C   ARG A  41     2285   2123   1197    225    180     82       C  
ATOM    323  O   ARG A  41       0.691   8.526  10.705  1.00 14.92           O  
ANISOU  323  O   ARG A  41     1970   2196   1505    217    220    233       O  
ATOM    324  CB  ARG A  41      -0.133   6.272  12.981  1.00 22.10           C  
ANISOU  324  CB  ARG A  41     4424   2102   1870   -694   1016   -215       C  
ATOM    325  CG  ARG A  41      -1.393   6.861  12.391  1.00 29.42           C  
ANISOU  325  CG  ARG A  41     3915   4703   2561  -1165    492    150       C  
ATOM    326  CD  ARG A  41      -1.912   5.836  11.378  1.00 41.24           C  
ANISOU  326  CD  ARG A  41     5574   5711   4386  -2120   -398   -523       C  
ATOM    327  NE  ARG A  41      -3.342   5.691  11.579  1.00 45.31           N  
ANISOU  327  NE  ARG A  41     5596   6639   4983  -2675   -683    222       N  
ATOM    328  CZ  ARG A  41      -3.928   5.249  12.686  1.00 44.23           C  
ANISOU  328  CZ  ARG A  41     5715   5366   5726  -2420   -400    793       C  
ATOM    329  NH1 ARG A  41      -3.197   4.892  13.728  1.00 43.79           N  
ANISOU  329  NH1 ARG A  41     6355   5999   4284  -1768   -250   -830       N  
ATOM    330  NH2 ARG A  41      -5.245   5.181  12.708  1.00 45.48           N  
ANISOU  330  NH2 ARG A  41     5615   4448   7216  -1215    249   1202       N  
ATOM    331  N   TRP A  42       1.825   6.573  10.514  1.00 14.97           N  
ANISOU  331  N   TRP A  42     2223   2156   1310    280    339    168       N  
ATOM    332  CA  TRP A  42       2.016   6.683   9.055  1.00 14.26           C  
ANISOU  332  CA  TRP A  42     2213   1963   1242   -185    308    105       C  
ATOM    333  C   TRP A  42       2.002   5.286   8.509  1.00 14.72           C  
ANISOU  333  C   TRP A  42     2311   1934   1348   -324    161    132       C  
ATOM    334  O   TRP A  42       2.073   4.284   9.245  1.00 16.35           O  
ANISOU  334  O   TRP A  42     2590   2007   1615    211    326    212       O  
ATOM    335  CB  TRP A  42       3.342   7.391   8.701  1.00 16.34           C  
ANISOU  335  CB  TRP A  42     2355   1991   1863   -433    297    370       C  
ATOM    336  CG  TRP A  42       4.495   6.823   9.483  1.00 19.51           C  
ANISOU  336  CG  TRP A  42     2190   2712   2510    -48    310    110       C  
ATOM    337  CD1 TRP A  42       4.958   7.280  10.713  1.00 19.13           C  
ANISOU  337  CD1 TRP A  42     1491   2679   3100   -223   -152      9       C  
ATOM    338  CD2 TRP A  42       5.325   5.726   9.152  1.00 21.12           C  
ANISOU  338  CD2 TRP A  42     2209   2756   3061    -85    632    178       C  
ATOM    339  NE1 TRP A  42       6.019   6.516  11.141  1.00 21.24           N  
ANISOU  339  NE1 TRP A  42     1969   3172   2928    363    356    388       N  
ATOM    340  CE2 TRP A  42       6.266   5.560  10.196  1.00 20.73           C  
ANISOU  340  CE2 TRP A  42     2202   2802   2872     89    857    668       C  
ATOM    341  CE3 TRP A  42       5.393   4.844   8.067  1.00 21.68           C  
ANISOU  341  CE3 TRP A  42     2890   2485   2860    391    872    478       C  
ATOM    342  CZ2 TRP A  42       7.256   4.577  10.226  1.00 22.02           C  
ANISOU  342  CZ2 TRP A  42     2411   2722   3233    110    765    429       C  
ATOM    343  CZ3 TRP A  42       6.372   3.861   8.080  1.00 21.90           C  
ANISOU  343  CZ3 TRP A  42     2601   2558   3163    342    617    675       C  
ATOM    344  CH2 TRP A  42       7.292   3.727   9.137  1.00 23.36           C  
ANISOU  344  CH2 TRP A  42     2412   3089   3376    141    479     89       C  
ATOM    345  N   LYS A  43       1.938   5.147   7.194  1.00 16.37           N  
ANISOU  345  N   LYS A  43     2665   2226   1331     43    356    -74       N  
ATOM    346  CA  LYS A  43       2.161   3.830   6.594  1.00 18.54           C  
ANISOU  346  CA  LYS A  43     2937   2098   2008   -585    881   -310       C  
ATOM    347  C   LYS A  43       3.150   3.965   5.436  1.00 18.23           C  
ANISOU  347  C   LYS A  43     3203   1755   1967     94   1011    130       C  
ATOM    348  O   LYS A  43       3.175   5.040   4.808  1.00 15.77           O  
ANISOU  348  O   LYS A  43     2395   1806   1791    -31    290    108       O  
ATOM    349  CB ALYS A  43       0.884   3.223   6.045  0.59 22.41           C  
ANISOU  349  CB ALYS A  43     3233   3023   2259   -789    529   -428       C  
ATOM    350  CB BLYS A  43       0.873   3.227   6.061  0.41 22.68           C  
ANISOU  350  CB BLYS A  43     3248   3043   2327   -828    527   -445       C  
ATOM    351  CG ALYS A  43       0.134   4.039   5.014  0.59 26.15           C  
ANISOU  351  CG ALYS A  43     3450   3756   2728   -689    275    -51       C  
ATOM    352  CG BLYS A  43       0.244   3.976   4.897  0.41 26.29           C  
ANISOU  352  CG BLYS A  43     3369   3801   2821   -661    289    -72       C  
ATOM    353  CD ALYS A  43      -1.373   3.760   5.068  0.59 31.00           C  
ANISOU  353  CD ALYS A  43     3511   4768   3498  -1002   -232   -181       C  
ATOM    354  CD BLYS A  43      -1.013   3.262   4.406  0.41 31.51           C  
ANISOU  354  CD BLYS A  43     4008   4559   3405   -880   -387   -431       C  
ATOM    355  CE ALYS A  43      -2.111   4.535   3.983  0.59 33.04           C  
ANISOU  355  CE ALYS A  43     3806   5049   3699   -720   -468   -248       C  
ATOM    356  CE BLYS A  43      -2.234   4.172   4.438  0.41 32.10           C  
ANISOU  356  CE BLYS A  43     3570   5076   3551   -984   -435     44       C  
ATOM    357  NZ ALYS A  43      -3.439   3.931   3.659  0.59 37.03           N  
ANISOU  357  NZ ALYS A  43     4603   5687   3778  -1643  -1104    834       N  
ATOM    358  NZ BLYS A  43      -3.512   3.409   4.349  0.41 34.39           N  
ANISOU  358  NZ BLYS A  43     4026   5898   3142  -1531  -1703    885       N  
ATOM    359  N   PRO A  44       3.929   2.929   5.132  1.00 17.35           N  
ANISOU  359  N   PRO A  44     3047   1777   1767    135    483     25       N  
ATOM    360  CA  PRO A  44       4.818   3.030   3.992  1.00 17.55           C  
ANISOU  360  CA  PRO A  44     3086   2189   1393    632    343    -61       C  
ATOM    361  C   PRO A  44       4.001   3.117   2.691  1.00 19.17           C  
ANISOU  361  C   PRO A  44     2680   2848   1756   -191    225    188       C  
ATOM    362  O   PRO A  44       2.902   2.586   2.532  1.00 20.99           O  
ANISOU  362  O   PRO A  44     3065   3021   1887   -647    574   -244       O  
ATOM    363  CB  PRO A  44       5.644   1.740   4.060  1.00 22.73           C  
ANISOU  363  CB  PRO A  44     3764   2403   2469    985    683    224       C  
ATOM    364  CG  PRO A  44       4.737   0.786   4.783  1.00 25.85           C  
ANISOU  364  CG  PRO A  44     4761   1926   3135    533   1065   -167       C  
ATOM    365  CD  PRO A  44       4.069   1.639   5.847  1.00 22.49           C  
ANISOU  365  CD  PRO A  44     4394   1908   2244    480    820    235       C  
ATOM    366  N   LYS A  45       4.558   3.812   1.689  1.00 15.74           N  
ANISOU  366  N   LYS A  45     2664   2072   1242   -175    115   -251       N  
ATOM    367  CA  LYS A  45       3.943   3.889   0.353  1.00 15.74           C  
ANISOU  367  CA  LYS A  45     2008   2529   1444    -60     73   -431       C  
ATOM    368  C   LYS A  45       5.057   3.785  -0.661  1.00 14.69           C  
ANISOU  368  C   LYS A  45     2201   2166   1216   -499    117   -165       C  
ATOM    369  O   LYS A  45       6.100   4.408  -0.458  1.00 15.45           O  
ANISOU  369  O   LYS A  45     2027   2444   1401   -318    -49   -374       O  
ATOM    370  CB  LYS A  45       3.208   5.204   0.145  1.00 17.31           C  
ANISOU  370  CB  LYS A  45     1726   2462   2390   -312    -90     65       C  
ATOM    371  CG  LYS A  45       2.409   5.201  -1.177  1.00 20.31           C  
ANISOU  371  CG  LYS A  45     2695   2829   2194    -92   -209    223       C  
ATOM    372  CD  LYS A  45       1.691   6.528  -1.337  1.00 23.66           C  
ANISOU  372  CD  LYS A  45     2723   3473   2793    502   -231    291       C  
ATOM    373  CE  LYS A  45       1.175   6.750  -2.749  1.00 26.48           C  
ANISOU  373  CE  LYS A  45     2851   4230   2979    873   -366    447       C  
ATOM    374  NZ  LYS A  45       0.014   5.874  -3.026  1.00 40.44           N  
ANISOU  374  NZ  LYS A  45     3198   6674   5493    508  -1155  -2050       N  
ATOM    375  N   LEU A  46       4.833   3.035  -1.723  1.00 15.76           N  
ANISOU  375  N   LEU A  46     2099   2691   1199   -396     66   -441       N  
ATOM    376  CA  LEU A  46       5.787   2.999  -2.834  1.00 14.99           C  
ANISOU  376  CA  LEU A  46     2148   2071   1475     15    291    -49       C  
ATOM    377  C   LEU A  46       5.367   3.963  -3.934  1.00 14.63           C  
ANISOU  377  C   LEU A  46     1681   2375   1503   -127    -62    -30       C  
ATOM    378  O   LEU A  46       4.202   3.891  -4.345  1.00 21.61           O  
ANISOU  378  O   LEU A  46     1720   4593   1898   -484   -239    314       O  
ATOM    379  CB  LEU A  46       5.871   1.580  -3.403  1.00 17.69           C  
ANISOU  379  CB  LEU A  46     2451   2202   2067    288     45   -401       C  
ATOM    380  CG  LEU A  46       6.453   0.549  -2.420  1.00 18.85           C  
ANISOU  380  CG  LEU A  46     3051   1982   2128   -117    -37   -191       C  
ATOM    381  CD1 LEU A  46       6.300  -0.836  -3.044  1.00 27.48           C  
ANISOU  381  CD1 LEU A  46     4626   1851   3964   -381   -567   -389       C  
ATOM    382  CD2 LEU A  46       7.908   0.824  -2.106  1.00 20.89           C  
ANISOU  382  CD2 LEU A  46     3113   2582   2242    105   -527   -155       C  
ATOM    383  N   ILE A  47       6.283   4.832  -4.343  1.00 12.86           N  
ANISOU  383  N   ILE A  47     1714   1990   1184     94     63   -104       N  
ATOM    384  CA  ILE A  47       5.994   5.770  -5.416  1.00 14.32           C  
ANISOU  384  CA  ILE A  47     2157   2244   1040    231     80    -99       C  
ATOM    385  C   ILE A  47       7.034   5.617  -6.529  1.00 15.23           C  
ANISOU  385  C   ILE A  47     2364   2153   1269    411    265     62       C  
ATOM    386  O   ILE A  47       8.034   4.894  -6.376  1.00 15.78           O  
ANISOU  386  O   ILE A  47     2130   2701   1164    433   -102   -240       O  
ATOM    387  CB  ILE A  47       5.951   7.205  -4.887  1.00 16.22           C  
ANISOU  387  CB  ILE A  47     2609   2052   1503    248    642    104       C  
ATOM    388  CG1 ILE A  47       7.282   7.722  -4.309  1.00 18.12           C  
ANISOU  388  CG1 ILE A  47     3477   1924   1484    105   -149   -173       C  
ATOM    389  CG2 ILE A  47       4.864   7.414  -3.823  1.00 25.89           C  
ANISOU  389  CG2 ILE A  47     3668   3853   2315   1247   1263   -437       C  
ATOM    390  CD1 ILE A  47       7.136   9.193  -3.937  1.00 21.96           C  
ANISOU  390  CD1 ILE A  47     4854   1872   1618    391   -496    -36       C  
ATOM    391  N   GLY A  48       6.775   6.305  -7.658  1.00 16.16           N  
ANISOU  391  N   GLY A  48     2815   2054   1272    330    300    165       N  
ATOM    392  CA  GLY A  48       7.719   6.198  -8.779  1.00 15.56           C  
ANISOU  392  CA  GLY A  48     2665   2032   1215    498    227      3       C  
ATOM    393  C   GLY A  48       7.390   4.942  -9.556  1.00 16.04           C  
ANISOU  393  C   GLY A  48     2469   2190   1434    370      0    -62       C  
ATOM    394  O   GLY A  48       6.228   4.663  -9.870  1.00 22.15           O  
ANISOU  394  O   GLY A  48     2522   3435   2459    335   -168   -667       O  
ATOM    395  N   GLY A  49       8.404   4.150  -9.838  1.00 16.59           N  
ANISOU  395  N   GLY A  49     2632   2266   1404    417     71   -368       N  
ATOM    396  CA  GLY A  49       8.147   2.873 -10.506  1.00 16.03           C  
ANISOU  396  CA  GLY A  49     2664   2056   1373    -26    480    -70       C  
ATOM    397  C   GLY A  49       9.088   2.649 -11.689  1.00 16.18           C  
ANISOU  397  C   GLY A  49     2737   2221   1190    213    324   -166       C  
ATOM    398  O   GLY A  49       9.454   1.495 -11.931  1.00 16.96           O  
ANISOU  398  O   GLY A  49     2762   2169   1513    -47    283   -390       O  
ATOM    399  N   ILE A  50       9.465   3.714 -12.372  1.00 15.06           N  
ANISOU  399  N   ILE A  50     2103   2365   1255    215    271     24       N  
ATOM    400  CA  ILE A  50      10.366   3.505 -13.524  1.00 17.33           C  
ANISOU  400  CA  ILE A  50     2404   2628   1555    610    493    139       C  
ATOM    401  C   ILE A  50      11.783   3.268 -13.024  1.00 15.21           C  
ANISOU  401  C   ILE A  50     2163   1969   1647     -4    529   -327       C  
ATOM    402  O   ILE A  50      12.442   4.150 -12.457  1.00 20.13           O  
ANISOU  402  O   ILE A  50     3436   2137   2076   -336    127   -469       O  
ATOM    403  CB  ILE A  50      10.267   4.688 -14.511  1.00 18.44           C  
ANISOU  403  CB  ILE A  50     3155   2423   1427    537    832     29       C  
ATOM    404  CG1 ILE A  50       8.832   4.860 -15.024  1.00 21.86           C  
ANISOU  404  CG1 ILE A  50     3769   2482   2055    603    -18    583       C  
ATOM    405  CG2 ILE A  50      11.256   4.558 -15.646  1.00 23.28           C  
ANISOU  405  CG2 ILE A  50     4513   2897   1437    195   1408   -537       C  
ATOM    406  CD1 ILE A  50       8.620   6.104 -15.869  1.00 24.28           C  
ANISOU  406  CD1 ILE A  50     4473   2404   2349    467    166    687       C  
ATOM    407  N   GLY A  51      12.251   2.037 -13.228  1.00 14.16           N  
ANISOU  407  N   GLY A  51     2208   1926   1246    179    234   -188       N  
ATOM    408  CA  GLY A  51      13.528   1.566 -12.730  1.00 14.53           C  
ANISOU  408  CA  GLY A  51     1857   2338   1327    -76    391   -123       C  
ATOM    409  C   GLY A  51      13.428   1.009 -11.318  1.00 13.35           C  
ANISOU  409  C   GLY A  51     1875   1850   1347   -273     70   -179       C  
ATOM    410  O   GLY A  51      14.460   0.625 -10.737  1.00 16.90           O  
ANISOU  410  O   GLY A  51     2253   2557   1611    215   -247   -526       O  
ATOM    411  N   GLY A  52      12.194   1.004 -10.787  1.00 15.19           N  
ANISOU  411  N   GLY A  52     2179   2361   1231   -136    441   -105       N  
ATOM    412  CA  GLY A  52      12.049   0.578  -9.393  1.00 17.81           C  
ANISOU  412  CA  GLY A  52     2759   2823   1183    569    511    -81       C  
ATOM    413  C   GLY A  52      11.234   1.646  -8.652  1.00 14.60           C  
ANISOU  413  C   GLY A  52     2236   2042   1270   -113    297   -274       C  
ATOM    414  O   GLY A  52      10.928   2.726  -9.161  1.00 17.80           O  
ANISOU  414  O   GLY A  52     3056   2258   1450    112    314    -33       O  
ATOM    415  N   PHE A  53      10.863   1.301  -7.434  1.00 14.30           N  
ANISOU  415  N   PHE A  53     1906   2359   1166     59    209   -263       N  
ATOM    416  CA  PHE A  53      10.021   2.183  -6.628  1.00 14.42           C  
ANISOU  416  CA  PHE A  53     1638   2441   1401    -61    183   -528       C  
ATOM    417  C   PHE A  53      10.806   2.805  -5.489  1.00 14.96           C  
ANISOU  417  C   PHE A  53     1869   2457   1358    107    -44   -375       C  
ATOM    418  O   PHE A  53      11.836   2.227  -5.111  1.00 16.79           O  
ANISOU  418  O   PHE A  53     1917   3116   1347    432     34   -485       O  
ATOM    419  CB  PHE A  53       8.843   1.395  -6.034  1.00 14.50           C  
ANISOU  419  CB  PHE A  53     1755   2309   1444     68    144    -45       C  
ATOM    420  CG  PHE A  53       7.810   1.030  -7.104  1.00 16.65           C  
ANISOU  420  CG  PHE A  53     1896   2532   1898   -391     18   -104       C  
ATOM    421  CD1 PHE A  53       6.707   1.852  -7.346  1.00 16.96           C  
ANISOU  421  CD1 PHE A  53     1990   2951   1503   -233   -147    103       C  
ATOM    422  CD2 PHE A  53       7.986  -0.119  -7.834  1.00 17.99           C  
ANISOU  422  CD2 PHE A  53     2979   2332   1525   -346   -174    153       C  
ATOM    423  CE1 PHE A  53       5.737   1.508  -8.295  1.00 18.37           C  
ANISOU  423  CE1 PHE A  53     2327   2537   2114   -493   -413      0       C  
ATOM    424  CE2 PHE A  53       7.034  -0.477  -8.790  1.00 19.16           C  
ANISOU  424  CE2 PHE A  53     2499   2759   2023   -471     -9   -292       C  
ATOM    425  CZ  PHE A  53       5.955   0.348  -9.038  1.00 18.55           C  
ANISOU  425  CZ  PHE A  53     2461   2568   2018   -649    -14     48       C  
ATOM    426  N   VAL A  54      10.326   3.934  -5.008  1.00 13.97           N  
ANISOU  426  N   VAL A  54     1810   2410   1086     60   -122   -369       N  
ATOM    427  CA  VAL A  54      10.896   4.630  -3.831  1.00 14.67           C  
ANISOU  427  CA  VAL A  54     1374   3054   1147     56    -82   -560       C  
ATOM    428  C   VAL A  54       9.907   4.455  -2.693  1.00 14.68           C  
ANISOU  428  C   VAL A  54     1618   2744   1214    496    124   -311       C  
ATOM    429  O   VAL A  54       8.699   4.658  -2.884  1.00 15.48           O  
ANISOU  429  O   VAL A  54     1534   2851   1496    419     89   -325       O  
ATOM    430  CB  VAL A  54      11.146   6.101  -4.107  1.00 17.99           C  
ANISOU  430  CB  VAL A  54     1888   3201   1745   -735    478  -1024       C  
ATOM    431  CG1 VAL A  54      11.471   6.897  -2.848  1.00 18.08           C  
ANISOU  431  CG1 VAL A  54     2388   3109   1372   -240      5   -620       C  
ATOM    432  CG2 VAL A  54      12.369   6.190  -5.053  1.00 23.93           C  
ANISOU  432  CG2 VAL A  54     2736   4259   2096   -876   1145   -962       C  
ATOM    433  N   LYS A  55      10.352   4.091  -1.524  1.00 13.10           N  
ANISOU  433  N   LYS A  55     1527   2158   1293    109     42   -307       N  
ATOM    434  CA  LYS A  55       9.474   4.037  -0.358  1.00 12.82           C  
ANISOU  434  CA  LYS A  55     1632   1945   1293    346    118   -154       C  
ATOM    435  C   LYS A  55       9.489   5.337   0.395  1.00 12.62           C  
ANISOU  435  C   LYS A  55     1505   1906   1382    282     77   -142       C  
ATOM    436  O   LYS A  55      10.539   5.918   0.688  1.00 14.76           O  
ANISOU  436  O   LYS A  55     1612   2520   1475    103    -43   -342       O  
ATOM    437  CB  LYS A  55       9.983   2.921   0.558  1.00 14.39           C  
ANISOU  437  CB  LYS A  55     2093   1895   1480    302    -48    -91       C  
ATOM    438  CG  LYS A  55       9.015   2.580   1.669  1.00 17.70           C  
ANISOU  438  CG  LYS A  55     2172   2597   1956    197     69    529       C  
ATOM    439  CD  LYS A  55       9.604   1.530   2.611  1.00 17.66           C  
ANISOU  439  CD  LYS A  55     2612   2323   1775    148   -184    288       C  
ATOM    440  CE  LYS A  55      10.126   0.284   1.895  1.00 17.85           C  
ANISOU  440  CE  LYS A  55     2152   2486   2142    143   -708    -79       C  
ATOM    441  NZ  LYS A  55      10.791  -0.638   2.876  1.00 21.76           N  
ANISOU  441  NZ  LYS A  55     2947   2603   2719    389   -550    440       N  
ATOM    442  N   VAL A  56       8.287   5.800   0.707  1.00 11.92           N  
ANISOU  442  N   VAL A  56     1603   1847   1080    296     25   -203       N  
ATOM    443  CA  VAL A  56       8.097   7.008   1.512  1.00 11.53           C  
ANISOU  443  CA  VAL A  56     1690   1752    938    214     29   -174       C  
ATOM    444  C   VAL A  56       7.126   6.729   2.644  1.00 10.69           C  
ANISOU  444  C   VAL A  56     1409   1664    990    154   -124   -190       C  
ATOM    445  O   VAL A  56       6.500   5.672   2.682  1.00 12.86           O  
ANISOU  445  O   VAL A  56     1650   1908   1329    -98     58   -310       O  
ATOM    446  CB  VAL A  56       7.611   8.171   0.634  1.00 12.35           C  
ANISOU  446  CB  VAL A  56     1664   1938   1090    465    172    -78       C  
ATOM    447  CG1 VAL A  56       8.653   8.505  -0.427  1.00 15.31           C  
ANISOU  447  CG1 VAL A  56     2201   2418   1199    -28    291     36       C  
ATOM    448  CG2 VAL A  56       6.238   7.882   0.012  1.00 15.33           C  
ANISOU  448  CG2 VAL A  56     1766   2417   1641    455   -180    103       C  
ATOM    449  N   ARG A  57       7.001   7.686   3.552  1.00 11.55           N  
ANISOU  449  N   ARG A  57     1483   1721   1185    214    215   -263       N  
ATOM    450  CA  ARG A  57       6.013   7.558   4.640  1.00 10.79           C  
ANISOU  450  CA  ARG A  57     1253   1668   1177     80     89   -108       C  
ATOM    451  C   ARG A  57       4.765   8.382   4.266  1.00 10.27           C  
ANISOU  451  C   ARG A  57     1366   1494   1043     74    172    182       C  
ATOM    452  O   ARG A  57       4.859   9.575   4.000  1.00 11.43           O  
ANISOU  452  O   ARG A  57     1485   1577   1281    -69     65    195       O  
ATOM    453  CB  ARG A  57       6.566   8.049   5.984  1.00 11.74           C  
ANISOU  453  CB  ARG A  57     1630   1746   1084     79    -63    128       C  
ATOM    454  CG  ARG A  57       7.647   7.119   6.539  1.00 13.95           C  
ANISOU  454  CG  ARG A  57     1586   2387   1329    351     38    360       C  
ATOM    455  CD  ARG A  57       8.065   7.568   7.940  1.00 14.91           C  
ANISOU  455  CD  ARG A  57     2120   2208   1338    801   -154    271       C  
ATOM    456  NE  ARG A  57       8.951   8.714   7.822  1.00 17.08           N  
ANISOU  456  NE  ARG A  57     2034   2067   2387    811   -286   -305       N  
ATOM    457  CZ  ARG A  57       9.433   9.441   8.827  1.00 21.74           C  
ANISOU  457  CZ  ARG A  57     2294   2968   3000    851   -516   -854       C  
ATOM    458  NH1 ARG A  57      10.222  10.455   8.540  1.00 31.08           N  
ANISOU  458  NH1 ARG A  57     2428   2648   6732    558   -885  -1293       N  
ATOM    459  NH2 ARG A  57       9.109   9.122  10.047  1.00 30.61           N  
ANISOU  459  NH2 ARG A  57     2919   6281   2429   2353  -1066   -622       N  
ATOM    460  N   GLN A  58       3.602   7.710   4.277  1.00 11.18           N  
ANISOU  460  N   GLN A  58     1221   1768   1258      8    175    175       N  
ATOM    461  CA  GLN A  58       2.346   8.393   4.018  1.00 11.29           C  
ANISOU  461  CA  GLN A  58     1378   1617   1295     44    161     11       C  
ATOM    462  C   GLN A  58       1.679   8.852   5.326  1.00 11.52           C  
ANISOU  462  C   GLN A  58     1601   1500   1276     99    262    116       C  
ATOM    463  O   GLN A  58       1.341   8.029   6.185  1.00 11.76           O  
ANISOU  463  O   GLN A  58     1702   1676   1090    -50     10    177       O  
ATOM    464  CB  GLN A  58       1.409   7.492   3.245  1.00 12.03           C  
ANISOU  464  CB  GLN A  58     1593   1469   1507     22   -151     19       C  
ATOM    465  CG  GLN A  58       0.027   8.126   3.046  1.00 12.76           C  
ANISOU  465  CG  GLN A  58     1563   2002   1281     43    -44    -93       C  
ATOM    466  CD  GLN A  58      -0.896   7.284   2.213  1.00 14.42           C  
ANISOU  466  CD  GLN A  58     1570   2365   1544   -122    -17   -338       C  
ATOM    467  OE1 GLN A  58      -0.475   6.479   1.357  1.00 22.14           O  
ANISOU  467  OE1 GLN A  58     2310   3581   2523   -399    442  -1453       O  
ATOM    468  NE2 GLN A  58      -2.185   7.427   2.473  1.00 17.51           N  
ANISOU  468  NE2 GLN A  58     1517   3006   2131     25   -131   -150       N  
ATOM    469  N   TYR A  59       1.525  10.152   5.453  1.00 11.71           N  
ANISOU  469  N   TYR A  59     1755   1546   1148    257    155    153       N  
ATOM    470  CA  TYR A  59       0.803  10.742   6.550  1.00 10.91           C  
ANISOU  470  CA  TYR A  59     1362   1569   1213     65    149     48       C  
ATOM    471  C   TYR A  59      -0.545  11.260   6.096  1.00 10.99           C  
ANISOU  471  C   TYR A  59     1387   1612   1178    -54    -26     37       C  
ATOM    472  O   TYR A  59      -0.595  12.042   5.127  1.00 12.18           O  
ANISOU  472  O   TYR A  59     1430   1997   1201    205    136    192       O  
ATOM    473  CB  TYR A  59       1.593  11.912   7.156  1.00 11.46           C  
ANISOU  473  CB  TYR A  59     1327   1763   1263     83   -175     68       C  
ATOM    474  CG  TYR A  59       2.836  11.484   7.913  1.00 11.80           C  
ANISOU  474  CG  TYR A  59     1308   2171   1006    381     16    194       C  
ATOM    475  CD1 TYR A  59       4.048  11.306   7.270  1.00 12.05           C  
ANISOU  475  CD1 TYR A  59     1237   2016   1325    203     34    150       C  
ATOM    476  CD2 TYR A  59       2.831  11.234   9.293  1.00 12.46           C  
ANISOU  476  CD2 TYR A  59     1502   2153   1080    156    -90    204       C  
ATOM    477  CE1 TYR A  59       5.194  10.907   7.950  1.00 11.74           C  
ANISOU  477  CE1 TYR A  59     1263   1863   1334    271     38     78       C  
ATOM    478  CE2 TYR A  59       3.959  10.840   9.966  1.00 12.07           C  
ANISOU  478  CE2 TYR A  59     1734   1961    893    422    -92     70       C  
ATOM    479  CZ  TYR A  59       5.152  10.668   9.316  1.00 13.73           C  
ANISOU  479  CZ  TYR A  59     1414   2525   1277    108   -196    -13       C  
ATOM    480  OH  TYR A  59       6.301  10.286   9.980  1.00 15.39           O  
ANISOU  480  OH  TYR A  59     1675   2317   1854    184   -545    125       O  
ATOM    481  N   ASP A  60      -1.625  10.873   6.761  1.00 12.70           N  
ANISOU  481  N   ASP A  60     1311   2334   1180    208     43    251       N  
ATOM    482  CA  ASP A  60      -2.940  11.319   6.322  1.00 12.98           C  
ANISOU  482  CA  ASP A  60     1383   1906   1644    140   -160    247       C  
ATOM    483  C   ASP A  60      -3.454  12.521   7.084  1.00 12.26           C  
ANISOU  483  C   ASP A  60     1425   1898   1336     67     99    368       C  
ATOM    484  O   ASP A  60      -3.065  12.739   8.235  1.00 14.39           O  
ANISOU  484  O   ASP A  60     1837   2194   1436    137      0    254       O  
ATOM    485  CB  ASP A  60      -3.922  10.147   6.497  1.00 16.78           C  
ANISOU  485  CB  ASP A  60     1869   2215   2291   -404   -507    -37       C  
ATOM    486  CG  ASP A  60      -3.644   9.115   5.396  1.00 18.58           C  
ANISOU  486  CG  ASP A  60     2434   2340   2286   -254   -514    -65       C  
ATOM    487  OD1 ASP A  60      -3.256   9.475   4.256  1.00 22.21           O  
ANISOU  487  OD1 ASP A  60     2308   3595   2536    -14    103    -19       O  
ATOM    488  OD2 ASP A  60      -3.842   7.925   5.715  1.00 26.26           O  
ANISOU  488  OD2 ASP A  60     4752   2098   3127    261   -763     36       O  
ATOM    489  N   GLN A  61      -4.325  13.300   6.457  1.00 13.16           N  
ANISOU  489  N   GLN A  61     1263   2049   1689    233     77    286       N  
ATOM    490  CA  GLN A  61      -5.043  14.363   7.123  1.00 13.48           C  
ANISOU  490  CA  GLN A  61     1307   2148   1667    103    235    142       C  
ATOM    491  C   GLN A  61      -4.112  15.346   7.826  1.00 13.69           C  
ANISOU  491  C   GLN A  61     1482   2273   1446     62    139    186       C  
ATOM    492  O   GLN A  61      -4.336  15.744   8.986  1.00 16.09           O  
ANISOU  492  O   GLN A  61     1732   2932   1450    328      7     39       O  
ATOM    493  CB  GLN A  61      -6.064  13.775   8.143  1.00 15.72           C  
ANISOU  493  CB  GLN A  61     1725   2608   1639   -122    384    150       C  
ATOM    494  CG  GLN A  61      -7.098  12.909   7.434  1.00 17.22           C  
ANISOU  494  CG  GLN A  61     1487   2707   2349   -182    419    115       C  
ATOM    495  CD  GLN A  61      -8.176  12.342   8.318  1.00 21.52           C  
ANISOU  495  CD  GLN A  61     1796   3923   2458   -560    505    373       C  
ATOM    496  OE1 GLN A  61      -8.040  12.257   9.544  1.00 32.51           O  
ANISOU  496  OE1 GLN A  61     2624   7245   2484   -996    548    795       O  
ATOM    497  NE2 GLN A  61      -9.311  11.944   7.723  1.00 25.23           N  
ANISOU  497  NE2 GLN A  61     2493   4005   3086  -1467    544    -20       N  
ATOM    498  N   VAL A  62      -3.047  15.736   7.135  1.00 13.77           N  
ANISOU  498  N   VAL A  62     1657   1690   1887    -46    220    397       N  
ATOM    499  CA  VAL A  62      -2.046  16.666   7.686  1.00 12.65           C  
ANISOU  499  CA  VAL A  62     1736   1633   1437     56    243    241       C  
ATOM    500  C   VAL A  62      -2.512  18.114   7.469  1.00 12.85           C  
ANISOU  500  C   VAL A  62     1874   1699   1309    246    -29     25       C  
ATOM    501  O   VAL A  62      -2.908  18.463   6.341  1.00 12.93           O  
ANISOU  501  O   VAL A  62     1813   1752   1348    148    -79     85       O  
ATOM    502  CB  VAL A  62      -0.690  16.451   6.998  1.00 12.93           C  
ANISOU  502  CB  VAL A  62     1535   1842   1535     87    -12   -220       C  
ATOM    503  CG1 VAL A  62       0.367  17.407   7.588  1.00 14.66           C  
ANISOU  503  CG1 VAL A  62     1698   2098   1775    -44   -109   -341       C  
ATOM    504  CG2 VAL A  62      -0.185  15.026   7.136  1.00 14.91           C  
ANISOU  504  CG2 VAL A  62     1992   1852   1820    215    135   -144       C  
ATOM    505  N   PRO A  63      -2.482  18.952   8.496  1.00 15.24           N  
ANISOU  505  N   PRO A  63     2438   1861   1493    150   -132   -117       N  
ATOM    506  CA  PRO A  63      -2.773  20.378   8.293  1.00 16.90           C  
ANISOU  506  CA  PRO A  63     3089   1684   1648   -161    363   -143       C  
ATOM    507  C   PRO A  63      -1.624  21.058   7.573  1.00 16.10           C  
ANISOU  507  C   PRO A  63     2608   2015   1495     90    260   -140       C  
ATOM    508  O   PRO A  63      -0.459  20.937   7.970  1.00 20.22           O  
ANISOU  508  O   PRO A  63     2934   2751   1996   -283   -295    514       O  
ATOM    509  CB  PRO A  63      -2.950  20.950   9.714  1.00 19.74           C  
ANISOU  509  CB  PRO A  63     3703   2113   1685    306    723   -129       C  
ATOM    510  CG  PRO A  63      -2.640  19.854  10.672  1.00 22.11           C  
ANISOU  510  CG  PRO A  63     4395   2389   1615    730    733   -111       C  
ATOM    511  CD  PRO A  63      -2.232  18.619   9.917  1.00 15.41           C  
ANISOU  511  CD  PRO A  63     2649   1883   1322   -274     96   -234       C  
ATOM    512  N   ILE A  64      -1.925  21.790   6.498  1.00 15.34           N  
ANISOU  512  N   ILE A  64     2197   1969   1664   -224    116    -28       N  
ATOM    513  CA  ILE A  64      -0.837  22.448   5.771  1.00 16.54           C  
ANISOU  513  CA  ILE A  64     2243   1922   2119   -146    322     65       C  
ATOM    514  C   ILE A  64      -1.446  23.793   5.314  1.00 19.28           C  
ANISOU  514  C   ILE A  64     2723   2380   2222   -154    -70    599       C  
ATOM    515  O   ILE A  64      -2.666  23.902   5.113  1.00 24.20           O  
ANISOU  515  O   ILE A  64     2912   2424   3859    -73   -632    908       O  
ATOM    516  CB  ILE A  64      -0.272  21.545   4.649  1.00 18.69           C  
ANISOU  516  CB  ILE A  64     2168   3174   1758   -317     42   -535       C  
ATOM    517  CG1 ILE A  64       0.849  22.195   3.827  1.00 22.53           C  
ANISOU  517  CG1 ILE A  64     2984   3178   2397   -329    760   -481       C  
ATOM    518  CG2 ILE A  64      -1.370  21.026   3.737  1.00 25.33           C  
ANISOU  518  CG2 ILE A  64     2708   4984   1931   -393   -583   -412       C  
ATOM    519  CD1 ILE A  64       1.612  21.319   2.837  1.00 26.97           C  
ANISOU  519  CD1 ILE A  64     3175   3910   3162    137   1075   -676       C  
ATOM    520  N   GLU A  65      -0.589  24.807   5.176  1.00 17.52           N  
ANISOU  520  N   GLU A  65     2935   1984   1735    -84     44    203       N  
ATOM    521  CA  GLU A  65      -1.060  26.096   4.708  1.00 18.36           C  
ANISOU  521  CA  GLU A  65     3182   1969   1827    117    -52    -51       C  
ATOM    522  C   GLU A  65      -0.300  26.487   3.456  1.00 18.44           C  
ANISOU  522  C   GLU A  65     3009   1992   2007   -494   -282    239       C  
ATOM    523  O   GLU A  65       0.930  26.434   3.543  1.00 22.18           O  
ANISOU  523  O   GLU A  65     3043   3529   1855   -224   -288    253       O  
ATOM    524  CB  GLU A  65      -0.847  27.176   5.785  1.00 23.46           C  
ANISOU  524  CB  GLU A  65     4353   2301   2260    100   -458   -378       C  
ATOM    525  CG  GLU A  65      -1.786  28.354   5.585  1.00 31.75           C  
ANISOU  525  CG  GLU A  65     5523   3018   3522   1255    411   -939       C  
ATOM    526  CD  GLU A  65      -1.548  29.370   6.697  1.00 40.36           C  
ANISOU  526  CD  GLU A  65     7027   3252   5054   1197   -782  -1633       C  
ATOM    527  OE1 GLU A  65      -0.942  28.958   7.720  1.00 42.59           O  
ANISOU  527  OE1 GLU A  65     6991   3826   5365    540  -1457  -1725       O  
ATOM    528  OE2 GLU A  65      -1.974  30.536   6.505  1.00 53.42           O  
ANISOU  528  OE2 GLU A  65    10791   3035   6471   1446  -1609  -1624       O  
ATOM    529  N   ILE A  66      -1.020  26.817   2.388  1.00 19.39           N  
ANISOU  529  N   ILE A  66     2812   2733   1822   -365    -91    196       N  
ATOM    530  CA  ILE A  66      -0.440  27.235   1.114  1.00 23.72           C  
ANISOU  530  CA  ILE A  66     3478   3650   1886   -818     43    305       C  
ATOM    531  C   ILE A  66      -0.992  28.596   0.722  1.00 26.84           C  
ANISOU  531  C   ILE A  66     4323   3575   2299  -1124    107    861       C  
ATOM    532  O   ILE A  66      -2.202  28.709   0.525  1.00 30.10           O  
ANISOU  532  O   ILE A  66     4600   3673   3166   -460   -361   1023       O  
ATOM    533  CB  ILE A  66      -0.759  26.196   0.019  1.00 23.28           C  
ANISOU  533  CB  ILE A  66     2855   4236   1754   -413   -112     71       C  
ATOM    534  CG1 ILE A  66      -0.183  24.825   0.396  1.00 28.50           C  
ANISOU  534  CG1 ILE A  66     3767   4324   2738    264   -604   -664       C  
ATOM    535  CG2 ILE A  66      -0.305  26.703  -1.331  1.00 30.43           C  
ANISOU  535  CG2 ILE A  66     2826   7044   1690   -351     50    423       C  
ATOM    536  CD1 ILE A  66      -0.826  23.634  -0.282  1.00 35.01           C  
ANISOU  536  CD1 ILE A  66     3886   4520   4896     71   -128  -1514       C  
ATOM    537  N   CYS A  67      -0.146  29.602   0.642  1.00 34.61           N  
ANISOU  537  N   CYS A  67     5847   3622   3682  -1906     59   -113       N  
ATOM    538  CA  CYS A  67      -0.537  30.987   0.403  1.00 36.00           C  
ANISOU  538  CA  CYS A  67     6024   3518   4136  -1931   -442   -282       C  
ATOM    539  C   CYS A  67      -1.818  31.406   1.109  1.00 40.30           C  
ANISOU  539  C   CYS A  67     6707   3811   4793  -1461     84   -398       C  
ATOM    540  O   CYS A  67      -2.804  31.801   0.472  1.00 47.29           O  
ANISOU  540  O   CYS A  67     6988   5757   5224   -248    899   1175       O  
ATOM    541  CB  CYS A  67      -0.738  31.248  -1.095  1.00 35.09           C  
ANISOU  541  CB  CYS A  67     5470   3718   4144    341  -1054   -982       C  
ATOM    542  SG  CYS A  67       0.544  30.603  -2.146  1.00 40.05           S  
ANISOU  542  SG  CYS A  67     4290   5827   5100   -822    366    196       S  
ATOM    543  N   GLY A  68      -1.864  31.321   2.438  1.00 40.87           N  
ANISOU  543  N   GLY A  68     6579   4058   4893  -2031    501    170       N  
ATOM    544  CA  GLY A  68      -3.044  31.798   3.127  1.00 42.47           C  
ANISOU  544  CA  GLY A  68     7013   4039   5084  -1660    311   -800       C  
ATOM    545  C   GLY A  68      -4.184  30.818   3.240  1.00 36.82           C  
ANISOU  545  C   GLY A  68     6202   3204   4583   -754    788   -487       C  
ATOM    546  O   GLY A  68      -5.134  31.063   3.980  1.00 41.93           O  
ANISOU  546  O   GLY A  68     6761   4110   5062   -257   1133   -629       O  
ATOM    547  N   HIS A  69      -4.136  29.697   2.519  1.00 30.04           N  
ANISOU  547  N   HIS A  69     5542   2529   3341   -278    -62    429       N  
ATOM    548  CA  HIS A  69      -5.177  28.706   2.568  1.00 26.18           C  
ANISOU  548  CA  HIS A  69     4435   2371   3144    373    118    264       C  
ATOM    549  C   HIS A  69      -4.752  27.524   3.433  1.00 23.44           C  
ANISOU  549  C   HIS A  69     3376   2481   3049     96     42    319       C  
ATOM    550  O   HIS A  69      -3.809  26.818   3.060  1.00 22.30           O  
ANISOU  550  O   HIS A  69     3131   2736   2607     44    -53    340       O  
ATOM    551  CB  HIS A  69      -5.476  28.127   1.181  1.00 28.35           C  
ANISOU  551  CB  HIS A  69     4491   3119   3162    346   -324    256       C  
ATOM    552  CG  HIS A  69      -6.098  29.123   0.270  1.00 30.85           C  
ANISOU  552  CG  HIS A  69     5470   3313   2939   1727    216   -175       C  
ATOM    553  ND1 HIS A  69      -5.467  30.300  -0.078  1.00 35.18           N  
ANISOU  553  ND1 HIS A  69     6311   3969   3085   1527    448    914       N  
ATOM    554  CD2 HIS A  69      -7.291  29.116  -0.343  1.00 34.77           C  
ANISOU  554  CD2 HIS A  69     5622   4300   3290   2149     -7    387       C  
ATOM    555  CE1 HIS A  69      -6.233  30.997  -0.877  1.00 35.77           C  
ANISOU  555  CE1 HIS A  69     6660   4199   2734   2149    488    475       C  
ATOM    556  NE2 HIS A  69      -7.346  30.304  -1.058  1.00 40.13           N  
ANISOU  556  NE2 HIS A  69     6305   5202   3738   2016    293   1316       N  
ATOM    557  N   LYS A  70      -5.482  27.355   4.513  1.00 21.50           N  
ANISOU  557  N   LYS A  70     3414   2067   2686    384   -107   -130       N  
ATOM    558  CA  LYS A  70      -5.300  26.267   5.443  1.00 19.97           C  
ANISOU  558  CA  LYS A  70     3263   1617   2706    271    310   -287       C  
ATOM    559  C   LYS A  70      -6.159  25.087   5.005  1.00 19.99           C  
ANISOU  559  C   LYS A  70     2470   2173   2953    167    635   -548       C  
ATOM    560  O   LYS A  70      -7.369  25.236   4.981  1.00 21.23           O  
ANISOU  560  O   LYS A  70     2589   2737   2740    495    436    123       O  
ATOM    561  CB  LYS A  70      -5.725  26.646   6.852  1.00 23.16           C  
ANISOU  561  CB  LYS A  70     3825   2379   2596    329    250   -366       C  
ATOM    562  CG  LYS A  70      -4.786  27.638   7.517  1.00 29.08           C  
ANISOU  562  CG  LYS A  70     4501   3618   2929   -753   1266  -1287       C  
ATOM    563  CD  LYS A  70      -5.186  27.749   8.997  1.00 32.86           C  
ANISOU  563  CD  LYS A  70     4092   5455   2936  -1214   1208  -1553       C  
ATOM    564  CE  LYS A  70      -4.720  29.052   9.599  1.00 38.18           C  
ANISOU  564  CE  LYS A  70     5438   5699   3368   -871    993  -2301       C  
ATOM    565  NZ  LYS A  70      -4.890  29.006  11.084  1.00 53.07           N  
ANISOU  565  NZ  LYS A  70     9733   7453   2979     95   -337  -2034       N  
ATOM    566  N   VAL A  71      -5.524  23.981   4.699  1.00 16.79           N  
ANISOU  566  N   VAL A  71     2499   1733   2149      9    227   -259       N  
ATOM    567  CA  VAL A  71      -6.209  22.789   4.204  1.00 15.44           C  
ANISOU  567  CA  VAL A  71     2325   1821   1722    -85   -147    164       C  
ATOM    568  C   VAL A  71      -5.658  21.549   4.897  1.00 14.07           C  
ANISOU  568  C   VAL A  71     1805   1737   1803    228   -145   -168       C  
ATOM    569  O   VAL A  71      -4.741  21.654   5.712  1.00 15.44           O  
ANISOU  569  O   VAL A  71     2157   2081   1628     54   -263   -188       O  
ATOM    570  CB  VAL A  71      -6.099  22.616   2.681  1.00 16.76           C  
ANISOU  570  CB  VAL A  71     2662   1872   1835    465   -210    -47       C  
ATOM    571  CG1 VAL A  71      -6.893  23.774   2.073  1.00 19.95           C  
ANISOU  571  CG1 VAL A  71     3460   2198   1922    804   -351    105       C  
ATOM    572  CG2 VAL A  71      -4.644  22.514   2.276  1.00 20.08           C  
ANISOU  572  CG2 VAL A  71     2950   2665   2015    607    190   -176       C  
ATOM    573  N   ILE A  72      -6.287  20.424   4.587  1.00 14.05           N  
ANISOU  573  N   ILE A  72     1976   1713   1650    112   -121    -55       N  
ATOM    574  CA  ILE A  72      -5.943  19.136   5.173  1.00 14.18           C  
ANISOU  574  CA  ILE A  72     2009   1776   1601    300      8     31       C  
ATOM    575  C   ILE A  72      -5.776  18.110   4.080  1.00 13.04           C  
ANISOU  575  C   ILE A  72     1377   1745   1831    106    -42    -58       C  
ATOM    576  O   ILE A  72      -6.592  18.029   3.180  1.00 15.06           O  
ANISOU  576  O   ILE A  72     1705   2427   1591    430    -73   -110       O  
ATOM    577  CB  ILE A  72      -7.076  18.690   6.142  1.00 14.04           C  
ANISOU  577  CB  ILE A  72     1997   1760   1578    137    -42   -112       C  
ATOM    578  CG1 ILE A  72      -7.164  19.652   7.324  1.00 19.62           C  
ANISOU  578  CG1 ILE A  72     3247   2200   2008    306    511   -451       C  
ATOM    579  CG2 ILE A  72      -6.922  17.233   6.534  1.00 14.72           C  
ANISOU  579  CG2 ILE A  72     2311   1874   1407     -2   -148    -47       C  
ATOM    580  CD1 ILE A  72      -8.417  19.415   8.120  1.00 29.43           C  
ANISOU  580  CD1 ILE A  72     2925   6041   2218    153    536  -1232       C  
ATOM    581  N   GLY A  73      -4.682  17.339   4.095  1.00 13.09           N  
ANISOU  581  N   GLY A  73     1554   1747   1674    258    263    274       N  
ATOM    582  CA  GLY A  73      -4.577  16.301   3.092  1.00 14.99           C  
ANISOU  582  CA  GLY A  73     1892   2407   1398    798   -219     13       C  
ATOM    583  C   GLY A  73      -3.395  15.399   3.358  1.00 11.85           C  
ANISOU  583  C   GLY A  73     1359   1853   1291    231     11    128       C  
ATOM    584  O   GLY A  73      -2.632  15.589   4.293  1.00 12.77           O  
ANISOU  584  O   GLY A  73     1375   1978   1498    -20   -137    230       O  
ATOM    585  N   THR A  74      -3.241  14.453   2.467  1.00 12.41           N  
ANISOU  585  N   THR A  74     1596   1948   1171    175    476     95       N  
ATOM    586  CA  THR A  74      -2.149  13.493   2.592  1.00 11.83           C  
ANISOU  586  CA  THR A  74     1333   1861   1303    -15    132   -190       C  
ATOM    587  C   THR A  74      -0.833  14.101   2.166  1.00 11.13           C  
ANISOU  587  C   THR A  74     1403   1683   1144    -46    -64    125       C  
ATOM    588  O   THR A  74      -0.739  14.759   1.125  1.00 12.36           O  
ANISOU  588  O   THR A  74     1637   1847   1212    124    -93    273       O  
ATOM    589  CB  THR A  74      -2.467  12.250   1.707  1.00 12.05           C  
ANISOU  589  CB  THR A  74     1621   1770   1186   -146     56    -33       C  
ATOM    590  OG1 THR A  74      -3.666  11.644   2.184  1.00 17.22           O  
ANISOU  590  OG1 THR A  74     1992   2335   2215   -646    273    -18       O  
ATOM    591  CG2 THR A  74      -1.370  11.224   1.769  1.00 13.98           C  
ANISOU  591  CG2 THR A  74     2348   1553   1411    175    190    258       C  
ATOM    592  N   VAL A  75       0.198  13.888   2.986  1.00 11.55           N  
ANISOU  592  N   VAL A  75     1260   2023   1105    125     47     48       N  
ATOM    593  CA  VAL A  75       1.548  14.293   2.664  1.00 11.26           C  
ANISOU  593  CA  VAL A  75     1257   1568   1452    171    242      3       C  
ATOM    594  C   VAL A  75       2.442  13.067   2.682  1.00 10.61           C  
ANISOU  594  C   VAL A  75     1414   1461   1155    105    318    212       C  
ATOM    595  O   VAL A  75       2.447  12.353   3.691  1.00 12.95           O  
ANISOU  595  O   VAL A  75     1734   1865   1324    190    355    431       O  
ATOM    596  CB  VAL A  75       2.062  15.359   3.652  1.00 12.45           C  
ANISOU  596  CB  VAL A  75     1541   1465   1724     49     55     60       C  
ATOM    597  CG1 VAL A  75       3.506  15.740   3.371  1.00 15.24           C  
ANISOU  597  CG1 VAL A  75     1755   2183   1852   -419    144      5       C  
ATOM    598  CG2 VAL A  75       1.174  16.605   3.549  1.00 15.39           C  
ANISOU  598  CG2 VAL A  75     2287   1416   2145    253   -105     45       C  
ATOM    599  N   LEU A  76       3.208  12.876   1.603  1.00 10.87           N  
ANISOU  599  N   LEU A  76     1231   1592   1308    193    335    183       N  
ATOM    600  CA  LEU A  76       4.228  11.836   1.585  1.00 11.28           C  
ANISOU  600  CA  LEU A  76     1237   1707   1343    276   -144   -141       C  
ATOM    601  C   LEU A  76       5.537  12.482   2.014  1.00 11.46           C  
ANISOU  601  C   LEU A  76     1295   1767   1295     39     25    142       C  
ATOM    602  O   LEU A  76       5.874  13.548   1.501  1.00 14.36           O  
ANISOU  602  O   LEU A  76     1410   2044   2001    -24     12    538       O  
ATOM    603  CB  LEU A  76       4.377  11.188   0.196  1.00 11.34           C  
ANISOU  603  CB  LEU A  76     1223   1685   1402     92    157    -98       C  
ATOM    604  CG  LEU A  76       3.046  10.718  -0.415  1.00 11.23           C  
ANISOU  604  CG  LEU A  76     1626   1479   1163   -106    -17      1       C  
ATOM    605  CD1 LEU A  76       3.294  10.073  -1.766  1.00 13.08           C  
ANISOU  605  CD1 LEU A  76     1790   1937   1244    455    -36   -188       C  
ATOM    606  CD2 LEU A  76       2.282   9.766   0.506  1.00 13.60           C  
ANISOU  606  CD2 LEU A  76     1552   1987   1627   -254     68    310       C  
ATOM    607  N   VAL A  77       6.253  11.841   2.947  1.00 11.41           N  
ANISOU  607  N   VAL A  77     1270   1885   1181     61    -61     71       N  
ATOM    608  CA  VAL A  77       7.502  12.402   3.402  1.00 11.60           C  
ANISOU  608  CA  VAL A  77     1286   1907   1213    -28     74     39       C  
ATOM    609  C   VAL A  77       8.611  11.445   3.000  1.00 12.20           C  
ANISOU  609  C   VAL A  77     1272   1848   1515     21    -44     53       C  
ATOM    610  O   VAL A  77       8.584  10.269   3.349  1.00 13.70           O  
ANISOU  610  O   VAL A  77     1818   1938   1450    205   -158    192       O  
ATOM    611  CB  VAL A  77       7.500  12.615   4.929  1.00 12.93           C  
ANISOU  611  CB  VAL A  77     1685   2009   1219     57   -126     -2       C  
ATOM    612  CG1 VAL A  77       8.838  13.138   5.386  1.00 16.13           C  
ANISOU  612  CG1 VAL A  77     1909   2717   1503   -297   -290     24       C  
ATOM    613  CG2 VAL A  77       6.360  13.547   5.328  1.00 16.82           C  
ANISOU  613  CG2 VAL A  77     2068   2282   2038    108    608   -333       C  
ATOM    614  N   GLY A  78       9.584  11.962   2.242  1.00 13.41           N  
ANISOU  614  N   GLY A  78     1370   2321   1403    -17    160    -98       N  
ATOM    615  CA  GLY A  78      10.650  11.070   1.791  1.00 17.21           C  
ANISOU  615  CA  GLY A  78     1938   2647   1955    216    604    -82       C  
ATOM    616  C   GLY A  78      11.528  11.890   0.853  1.00 16.99           C  
ANISOU  616  C   GLY A  78     1596   2818   2041    316    509    116       C  
ATOM    617  O   GLY A  78      11.237  13.041   0.547  1.00 17.08           O  
ANISOU  617  O   GLY A  78     1862   2909   1720    354    272    170       O  
ATOM    618  N   PRO A  79      12.583  11.227   0.434  1.00 24.47           N  
ANISOU  618  N   PRO A  79     2189   4273   2834   1379   1090   1169       N  
ATOM    619  CA  PRO A  79      13.533  11.869  -0.486  1.00 26.15           C  
ANISOU  619  CA  PRO A  79     1644   5139   3153   1113    915   1207       C  
ATOM    620  C   PRO A  79      12.837  12.200  -1.793  1.00 25.97           C  
ANISOU  620  C   PRO A  79     2859   4762   2245    828   1051    555       C  
ATOM    621  O   PRO A  79      12.085  11.448  -2.404  1.00 29.72           O  
ANISOU  621  O   PRO A  79     4262   4091   2939    792    377    501       O  
ATOM    622  CB  PRO A  79      14.591  10.787  -0.679  1.00 30.80           C  
ANISOU  622  CB  PRO A  79     2189   5313   4201   1324   1347    580       C  
ATOM    623  CG  PRO A  79      13.968   9.499  -0.262  1.00 30.08           C  
ANISOU  623  CG  PRO A  79     2442   4780   4208   1089   1100   -389       C  
ATOM    624  CD  PRO A  79      12.952   9.841   0.785  1.00 26.97           C  
ANISOU  624  CD  PRO A  79     2371   4214   3663   1625   1002    894       C  
ATOM    625  N   THR A  80      13.121  13.424  -2.207  1.00 22.42           N  
ANISOU  625  N   THR A  80     1983   4382   2156   1159    495    178       N  
ATOM    626  CA  THR A  80      12.560  13.872  -3.469  1.00 22.40           C  
ANISOU  626  CA  THR A  80     1789   4633   2091    784    549    352       C  
ATOM    627  C   THR A  80      13.539  14.897  -4.049  1.00 23.53           C  
ANISOU  627  C   THR A  80     2124   4580   2235    559    677     70       C  
ATOM    628  O   THR A  80      14.080  15.718  -3.313  1.00 25.07           O  
ANISOU  628  O   THR A  80     2696   4681   2148    386    131    399       O  
ATOM    629  CB  THR A  80      11.122  14.405  -3.312  1.00 19.07           C  
ANISOU  629  CB  THR A  80     2046   3200   1999    841    514    266       C  
ATOM    630  OG1 THR A  80      10.722  14.965  -4.563  1.00 21.45           O  
ANISOU  630  OG1 THR A  80     2159   4015   1976    610    182    219       O  
ATOM    631  CG2 THR A  80      11.002  15.534  -2.296  1.00 18.96           C  
ANISOU  631  CG2 THR A  80     2085   3014   2107    460   -111    202       C  
ATOM    632  N   PRO A  81      13.814  14.819  -5.349  1.00 22.31           N  
ANISOU  632  N   PRO A  81     1807   4558   2113    681    538    317       N  
ATOM    633  CA  PRO A  81      14.726  15.801  -5.941  1.00 25.94           C  
ANISOU  633  CA  PRO A  81     2721   4638   2495    200    856     61       C  
ATOM    634  C   PRO A  81      14.255  17.218  -5.701  1.00 27.05           C  
ANISOU  634  C   PRO A  81     2447   4592   3240   -184   1109   -584       C  
ATOM    635  O   PRO A  81      15.056  18.142  -5.598  1.00 35.73           O  
ANISOU  635  O   PRO A  81     2831   4780   5965   -581    886    335       O  
ATOM    636  CB  PRO A  81      14.701  15.474  -7.440  1.00 26.24           C  
ANISOU  636  CB  PRO A  81     3341   4157   2472    267   1264    164       C  
ATOM    637  CG  PRO A  81      14.391  14.008  -7.480  1.00 28.53           C  
ANISOU  637  CG  PRO A  81     4186   4476   2178   -558   1336    300       C  
ATOM    638  CD  PRO A  81      13.394  13.804  -6.339  1.00 25.05           C  
ANISOU  638  CD  PRO A  81     2766   4831   1921      9    676    391       C  
ATOM    639  N   ALA A  82      12.943  17.424  -5.605  1.00 26.00           N  
ANISOU  639  N   ALA A  82     2478   4088   3311     32    739   1095       N  
ATOM    640  CA  ALA A  82      12.390  18.751  -5.334  1.00 27.83           C  
ANISOU  640  CA  ALA A  82     2986   4363   3227    352   1312   1152       C  
ATOM    641  C   ALA A  82      11.080  18.569  -4.565  1.00 21.47           C  
ANISOU  641  C   ALA A  82     2038   4134   1985   -501     84    210       C  
ATOM    642  O   ALA A  82      10.372  17.638  -4.892  1.00 23.73           O  
ANISOU  642  O   ALA A  82     3352   3307   2359   -411    -15    234       O  
ATOM    643  CB  ALA A  82      12.163  19.524  -6.619  1.00 32.56           C  
ANISOU  643  CB  ALA A  82     4924   4136   3311    863   1775   1254       C  
ATOM    644  N   ASN A  83      10.773  19.388  -3.557  1.00 18.41           N  
ANISOU  644  N   ASN A  83     1799   2703   2493    -73    113    588       N  
ATOM    645  CA  ASN A  83       9.475  19.306  -2.889  1.00 15.83           C  
ANISOU  645  CA  ASN A  83     1725   2380   1908   -492   -174    432       C  
ATOM    646  C   ASN A  83       8.369  19.639  -3.884  1.00 15.28           C  
ANISOU  646  C   ASN A  83     1894   2030   1880   -509   -350    285       C  
ATOM    647  O   ASN A  83       8.498  20.579  -4.690  1.00 18.16           O  
ANISOU  647  O   ASN A  83     2268   2342   2291   -479   -320    671       O  
ATOM    648  CB  ASN A  83       9.362  20.310  -1.758  1.00 17.70           C  
ANISOU  648  CB  ASN A  83     2305   2838   1584   -266   -399    329       C  
ATOM    649  CG  ASN A  83      10.294  20.033  -0.583  1.00 17.41           C  
ANISOU  649  CG  ASN A  83     2009   2283   2324   -308   -714    309       C  
ATOM    650  OD1 ASN A  83      10.641  18.897  -0.332  1.00 18.47           O  
ANISOU  650  OD1 ASN A  83     2253   2309   2455   -319   -378    563       O  
ATOM    651  ND2 ASN A  83      10.685  21.107   0.131  1.00 19.49           N  
ANISOU  651  ND2 ASN A  83     2876   2689   1840   -124   -488   -185       N  
ATOM    652  N   VAL A  84       7.291  18.863  -3.813  1.00 15.20           N  
ANISOU  652  N   VAL A  84     1591   2459   1724   -394    -38    193       N  
ATOM    653  CA  VAL A  84       6.225  18.938  -4.793  1.00 15.65           C  
ANISOU  653  CA  VAL A  84     1529   2820   1598   -371     90     38       C  
ATOM    654  C   VAL A  84       4.854  19.003  -4.113  1.00 13.75           C  
ANISOU  654  C   VAL A  84     1540   2028   1659   -431     65    227       C  
ATOM    655  O   VAL A  84       4.569  18.153  -3.230  1.00 14.33           O  
ANISOU  655  O   VAL A  84     1789   2219   1435   -376     -4    293       O  
ATOM    656  CB  VAL A  84       6.297  17.694  -5.723  1.00 20.83           C  
ANISOU  656  CB  VAL A  84     1955   4003   1958   -437    171   -844       C  
ATOM    657  CG1 VAL A  84       5.125  17.735  -6.656  1.00 21.54           C  
ANISOU  657  CG1 VAL A  84     2304   3264   2617   -240   -395   -605       C  
ATOM    658  CG2 VAL A  84       7.612  17.638  -6.495  1.00 27.07           C  
ANISOU  658  CG2 VAL A  84     2145   5209   2931    -68    561  -1264       C  
ATOM    659  N   ILE A  85       4.027  19.980  -4.480  1.00 13.94           N  
ANISOU  659  N   ILE A  85     1642   2121   1534   -349    -83    165       N  
ATOM    660  CA  ILE A  85       2.608  19.995  -4.125  1.00 12.70           C  
ANISOU  660  CA  ILE A  85     1719   1786   1320   -302   -121    229       C  
ATOM    661  C   ILE A  85       1.840  19.388  -5.286  1.00 11.68           C  
ANISOU  661  C   ILE A  85     1619   1569   1250   -242    -48    278       C  
ATOM    662  O   ILE A  85       1.857  19.956  -6.402  1.00 14.04           O  
ANISOU  662  O   ILE A  85     2237   1868   1231   -493   -123    351       O  
ATOM    663  CB AILE A  85       2.138  21.412  -3.779  0.47 13.69           C  
ANISOU  663  CB AILE A  85     1955   1838   1410   -258   -160     75       C  
ATOM    664  CB BILE A  85       2.039  21.407  -3.891  0.53 13.24           C  
ANISOU  664  CB BILE A  85     1898   1840   1293   -233   -247     85       C  
ATOM    665  CG1AILE A  85       2.927  21.999  -2.594  0.47 14.83           C  
ANISOU  665  CG1AILE A  85     2129   1893   1611   -405   -309     82       C  
ATOM    666  CG1BILE A  85       2.717  22.230  -2.788  0.53 14.50           C  
ANISOU  666  CG1BILE A  85     2217   1881   1410   -504   -302    134       C  
ATOM    667  CG2AILE A  85       0.638  21.470  -3.523  0.47 13.58           C  
ANISOU  667  CG2AILE A  85     1933   1869   1357   -195   -140    121       C  
ATOM    668  CG2BILE A  85       0.534  21.312  -3.632  0.53 14.74           C  
ANISOU  668  CG2BILE A  85     1811   2102   1686   -128   -280    136       C  
ATOM    669  CD1AILE A  85       2.732  23.480  -2.447  0.47 14.70           C  
ANISOU  669  CD1AILE A  85     2111   1924   1552   -422    267    -76       C  
ATOM    670  CD1BILE A  85       2.895  21.402  -1.535  0.53 15.18           C  
ANISOU  670  CD1BILE A  85     2480   1931   1358   -467   -484     57       C  
ATOM    671  N   GLY A  86       1.243  18.238  -5.069  1.00 12.28           N  
ANISOU  671  N   GLY A  86     1723   1506   1437   -202   -108    224       N  
ATOM    672  CA  GLY A  86       0.539  17.541  -6.144  1.00 12.24           C  
ANISOU  672  CA  GLY A  86     1379   1762   1511   -227    120    -31       C  
ATOM    673  C   GLY A  86      -0.934  17.915  -6.195  1.00 11.06           C  
ANISOU  673  C   GLY A  86     1510   1276   1418    -42    -17    117       C  
ATOM    674  O   GLY A  86      -1.449  18.771  -5.459  1.00 11.67           O  
ANISOU  674  O   GLY A  86     1625   1530   1280   -112     99     41       O  
ATOM    675  N   ARG A  87      -1.605  17.233  -7.122  1.00 11.56           N  
ANISOU  675  N   ARG A  87     1478   1502   1411      8     10     18       N  
ATOM    676  CA  ARG A  87      -3.021  17.510  -7.333  1.00 11.53           C  
ANISOU  676  CA  ARG A  87     1514   1900    967    -24    -16     69       C  
ATOM    677  C   ARG A  87      -3.843  17.274  -6.080  1.00 12.20           C  
ANISOU  677  C   ARG A  87     1553   2034   1049    104     81    166       C  
ATOM    678  O   ARG A  87      -4.844  17.973  -5.880  1.00 13.68           O  
ANISOU  678  O   ARG A  87     1756   2090   1350    219    113    -60       O  
ATOM    679  CB  ARG A  87      -3.574  16.642  -8.459  1.00 12.42           C  
ANISOU  679  CB  ARG A  87     1745   1916   1059   -317    107     11       C  
ATOM    680  CG  ARG A  87      -2.949  16.994  -9.796  1.00 12.49           C  
ANISOU  680  CG  ARG A  87     1889   1943    915   -297    -34    161       C  
ATOM    681  CD  ARG A  87      -3.709  16.281 -10.931  1.00 13.83           C  
ANISOU  681  CD  ARG A  87     2245   1870   1138   -392    -74    -86       C  
ATOM    682  NE  ARG A  87      -3.493  14.852 -10.842  1.00 13.59           N  
ANISOU  682  NE  ARG A  87     1988   1934   1241   -389     -8    101       N  
ATOM    683  CZ  ARG A  87      -4.327  13.948 -10.334  1.00 14.03           C  
ANISOU  683  CZ  ARG A  87     2231   1841   1259   -321    367   -119       C  
ATOM    684  NH1 ARG A  87      -3.943  12.660 -10.315  1.00 15.96           N  
ANISOU  684  NH1 ARG A  87     2666   1847   1553   -198   -146     22       N  
ATOM    685  NH2 ARG A  87      -5.526  14.307  -9.889  1.00 14.88           N  
ANISOU  685  NH2 ARG A  87     2041   2397   1216   -313    177   -109       N  
ATOM    686  N   ASN A  88      -3.457  16.333  -5.220  1.00 11.77           N  
ANISOU  686  N   ASN A  88     1500   1837   1136   -141    116    189       N  
ATOM    687  CA  ASN A  88      -4.246  16.068  -4.011  1.00 11.97           C  
ANISOU  687  CA  ASN A  88     1735   1425   1387   -264    348    166       C  
ATOM    688  C   ASN A  88      -4.415  17.308  -3.143  1.00 12.39           C  
ANISOU  688  C   ASN A  88     1523   1723   1460   -261    375    -52       C  
ATOM    689  O   ASN A  88      -5.488  17.513  -2.578  1.00 16.79           O  
ANISOU  689  O   ASN A  88     1516   2759   2104    -36    426   -509       O  
ATOM    690  CB  ASN A  88      -3.668  14.910  -3.181  1.00 12.52           C  
ANISOU  690  CB  ASN A  88     1683   1702   1372   -272     -4    241       C  
ATOM    691  CG  ASN A  88      -2.424  15.313  -2.410  1.00 13.92           C  
ANISOU  691  CG  ASN A  88     1748   2274   1269   -470    139    -68       C  
ATOM    692  OD1 ASN A  88      -1.430  15.728  -3.026  1.00 13.44           O  
ANISOU  692  OD1 ASN A  88     1531   1938   1640   -136    171    180       O  
ATOM    693  ND2 ASN A  88      -2.483  15.214  -1.099  1.00 13.14           N  
ANISOU  693  ND2 ASN A  88     2157   1613   1224     37      5     91       N  
ATOM    694  N   LEU A  89      -3.383  18.139  -3.022  1.00 11.21           N  
ANISOU  694  N   LEU A  89     1591   1476   1192   -106    -30    113       N  
ATOM    695  CA  LEU A  89      -3.570  19.337  -2.202  1.00 12.69           C  
ANISOU  695  CA  LEU A  89     1830   1587   1406     88   -238    -49       C  
ATOM    696  C   LEU A  89      -4.109  20.497  -3.021  1.00 11.80           C  
ANISOU  696  C   LEU A  89     1603   1547   1332     29    177     78       C  
ATOM    697  O   LEU A  89      -4.798  21.382  -2.467  1.00 12.99           O  
ANISOU  697  O   LEU A  89     1702   1839   1395    291     64    -26       O  
ATOM    698  CB  LEU A  89      -2.272  19.741  -1.508  1.00 12.27           C  
ANISOU  698  CB  LEU A  89     1590   1782   1290   -152     58     -8       C  
ATOM    699  CG  LEU A  89      -1.847  18.806  -0.371  1.00 15.31           C  
ANISOU  699  CG  LEU A  89     1598   2309   1911    113   -260    327       C  
ATOM    700  CD1 LEU A  89      -0.606  19.380   0.296  1.00 17.68           C  
ANISOU  700  CD1 LEU A  89     1783   2812   2123    226   -458   -386       C  
ATOM    701  CD2 LEU A  89      -2.982  18.605   0.619  1.00 18.46           C  
ANISOU  701  CD2 LEU A  89     2400   3112   1502   -605   -145    635       C  
ATOM    702  N   MET A  90      -3.786  20.518  -4.323  1.00 11.75           N  
ANISOU  702  N   MET A  90     1552   1691   1223    -72    -48    -61       N  
ATOM    703  CA  MET A  90      -4.406  21.560  -5.142  1.00 12.50           C  
ANISOU  703  CA  MET A  90     1734   1834   1181    -75   -134    -33       C  
ATOM    704  C   MET A  90      -5.902  21.470  -5.150  1.00 12.98           C  
ANISOU  704  C   MET A  90     1762   1840   1329    -34   -223    174       C  
ATOM    705  O   MET A  90      -6.531  22.540  -5.175  1.00 14.86           O  
ANISOU  705  O   MET A  90     1981   2050   1614    244    -42    274       O  
ATOM    706  CB  MET A  90      -3.820  21.529  -6.581  1.00 14.10           C  
ANISOU  706  CB  MET A  90     2297   1826   1233    -68    133   -107       C  
ATOM    707  CG  MET A  90      -2.395  22.082  -6.528  1.00 17.41           C  
ANISOU  707  CG  MET A  90     1811   3165   1640    175    174    155       C  
ATOM    708  SD  MET A  90      -1.602  22.340  -8.146  1.00 22.30           S  
ANISOU  708  SD  MET A  90     2698   4046   1728   -544    389     43       S  
ATOM    709  CE  MET A  90      -0.912  20.726  -8.347  1.00 23.07           C  
ANISOU  709  CE  MET A  90     3244   4210   1312   -309    735   -325       C  
ATOM    710  N   THR A  91      -6.508  20.278  -5.146  1.00 13.09           N  
ANISOU  710  N   THR A  91     1637   2037   1300   -175   -207   -164       N  
ATOM    711  CA  THR A  91      -7.982  20.252  -5.075  1.00 14.32           C  
ANISOU  711  CA  THR A  91     1636   2225   1581    -56   -260   -368       C  
ATOM    712  C   THR A  91      -8.502  20.810  -3.763  1.00 14.19           C  
ANISOU  712  C   THR A  91     1775   2209   1409     33    -57     56       C  
ATOM    713  O   THR A  91      -9.583  21.411  -3.750  1.00 16.75           O  
ANISOU  713  O   THR A  91     2313   2429   1622    600     -2    161       O  
ATOM    714  CB  THR A  91      -8.535  18.833  -5.248  1.00 14.84           C  
ANISOU  714  CB  THR A  91     1795   2333   1513   -428    -67    -29       C  
ATOM    715  OG1 THR A  91      -7.988  17.974  -4.241  1.00 18.16           O  
ANISOU  715  OG1 THR A  91     2380   2513   2007   -312   -385    100       O  
ATOM    716  CG2 THR A  91      -8.088  18.260  -6.598  1.00 17.41           C  
ANISOU  716  CG2 THR A  91     2805   1913   1899   -436     95   -305       C  
ATOM    717  N   GLN A  92      -7.743  20.599  -2.687  1.00 14.00           N  
ANISOU  717  N   GLN A  92     1611   2363   1347   -148     39      6       N  
ATOM    718  CA  GLN A  92      -8.207  21.050  -1.365  1.00 14.06           C  
ANISOU  718  CA  GLN A  92     1675   2338   1331    -29    209    163       C  
ATOM    719  C   GLN A  92      -8.197  22.582  -1.325  1.00 14.93           C  
ANISOU  719  C   GLN A  92     2004   2297   1374    185    233    243       C  
ATOM    720  O   GLN A  92      -9.120  23.185  -0.747  1.00 18.01           O  
ANISOU  720  O   GLN A  92     2189   2566   2090    329    489    170       O  
ATOM    721  CB  GLN A  92      -7.318  20.503  -0.253  1.00 13.77           C  
ANISOU  721  CB  GLN A  92     1892   2065   1276    107    268    111       C  
ATOM    722  CG  GLN A  92      -7.325  18.986  -0.112  1.00 12.88           C  
ANISOU  722  CG  GLN A  92     1559   2042   1293   -184    213     -1       C  
ATOM    723  CD  GLN A  92      -8.745  18.502   0.107  1.00 13.46           C  
ANISOU  723  CD  GLN A  92     1318   2115   1681     93     50   -336       C  
ATOM    724  OE1 GLN A  92      -9.403  18.917   1.054  1.00 15.20           O  
ANISOU  724  OE1 GLN A  92     1446   2908   1423    -99    202   -184       O  
ATOM    725  NE2 GLN A  92      -9.247  17.633  -0.752  1.00 19.64           N  
ANISOU  725  NE2 GLN A  92     2003   2954   2503   -616    316  -1014       N  
ATOM    726  N   ILE A  93      -7.190  23.259  -1.932  1.00 15.13           N  
ANISOU  726  N   ILE A  93     2053   2344   1350   -304     70   -116       N  
ATOM    727  CA  ILE A  93      -7.176  24.726  -1.939  1.00 15.12           C  
ANISOU  727  CA  ILE A  93     1768   2348   1630    -92    279   -208       C  
ATOM    728  C   ILE A  93      -8.055  25.318  -3.055  1.00 15.60           C  
ANISOU  728  C   ILE A  93     1738   2344   1844    -30    340    -73       C  
ATOM    729  O   ILE A  93      -8.181  26.557  -3.159  1.00 19.50           O  
ANISOU  729  O   ILE A  93     2998   2311   2101    265    284   -158       O  
ATOM    730  CB  ILE A  93      -5.759  25.312  -2.080  1.00 17.25           C  
ANISOU  730  CB  ILE A  93     1958   2514   2082   -390     -9   -290       C  
ATOM    731  CG1 ILE A  93      -5.114  25.097  -3.439  1.00 20.49           C  
ANISOU  731  CG1 ILE A  93     2088   3108   2590   -494    683     48       C  
ATOM    732  CG2 ILE A  93      -4.832  24.745  -1.007  1.00 24.30           C  
ANISOU  732  CG2 ILE A  93     2034   4247   2952   -253   -307    507       C  
ATOM    733  CD1 ILE A  93      -3.623  25.482  -3.444  1.00 22.60           C  
ANISOU  733  CD1 ILE A  93     2493   3037   3055  -1236    629   -261       C  
ATOM    734  N   GLY A  94      -8.661  24.454  -3.874  1.00 15.64           N  
ANISOU  734  N   GLY A  94     1859   2454   1628   -146    174     99       N  
ATOM    735  CA  GLY A  94      -9.508  24.945  -4.939  1.00 15.34           C  
ANISOU  735  CA  GLY A  94     1828   2213   1788    -19    246    373       C  
ATOM    736  C   GLY A  94      -8.755  25.511  -6.140  1.00 16.77           C  
ANISOU  736  C   GLY A  94     1871   2341   2161   -109    347    611       C  
ATOM    737  O   GLY A  94      -9.269  26.388  -6.838  1.00 20.19           O  
ANISOU  737  O   GLY A  94     2618   2974   2077    702    899    877       O  
ATOM    738  N   CYS A  95      -7.570  24.969  -6.377  1.00 15.92           N  
ANISOU  738  N   CYS A  95     2087   2256   1706     11    392    298       N  
ATOM    739  CA  CYS A  95      -6.718  25.410  -7.464  1.00 17.47           C  
ANISOU  739  CA  CYS A  95     2446   2695   1498    421    552    310       C  
ATOM    740  C   CYS A  95      -7.172  24.811  -8.792  1.00 17.73           C  
ANISOU  740  C   CYS A  95     2632   2376   1728   -483    683    422       C  
ATOM    741  O   CYS A  95      -7.346  23.589  -8.830  1.00 20.17           O  
ANISOU  741  O   CYS A  95     3209   2302   2154   -235    730    475       O  
ATOM    742  CB  CYS A  95      -5.281  24.999  -7.129  1.00 19.91           C  
ANISOU  742  CB  CYS A  95     2261   3216   2087    396    698    429       C  
ATOM    743  SG  CYS A  95      -4.079  25.637  -8.314  1.00 20.26           S  
ANISOU  743  SG  CYS A  95     2587   2879   2230   -180    624    266       S  
ATOM    744  N   THR A  96      -7.318  25.686  -9.787  1.00 15.89           N  
ANISOU  744  N   THR A  96     2206   2221   1610     41    393    249       N  
ATOM    745  CA  THR A  96      -7.681  25.193 -11.127  1.00 15.59           C  
ANISOU  745  CA  THR A  96     1652   2514   1756    202    494     25       C  
ATOM    746  C   THR A  96      -6.688  25.713 -12.156  1.00 14.81           C  
ANISOU  746  C   THR A  96     1920   1998   1710    186    492    188       C  
ATOM    747  O   THR A  96      -5.987  26.680 -11.892  1.00 16.63           O  
ANISOU  747  O   THR A  96     2140   2296   1884     21    319    131       O  
ATOM    748  CB  THR A  96      -9.112  25.615 -11.530  1.00 16.73           C  
ANISOU  748  CB  THR A  96     1784   2466   2105    363    384    -45       C  
ATOM    749  OG1 THR A  96      -9.220  27.048 -11.385  1.00 18.30           O  
ANISOU  749  OG1 THR A  96     2408   2533   2011    491    283     -2       O  
ATOM    750  CG2 THR A  96     -10.135  24.922 -10.636  1.00 18.25           C  
ANISOU  750  CG2 THR A  96     1528   2842   2566    225    476   -146       C  
ATOM    751  N   LEU A  97      -6.618  25.056 -13.325  1.00 14.38           N  
ANISOU  751  N   LEU A  97     1801   1979   1686    209    464    253       N  
ATOM    752  CA  LEU A  97      -5.971  25.618 -14.520  1.00 15.40           C  
ANISOU  752  CA  LEU A  97     2052   2299   1499    399    298    400       C  
ATOM    753  C   LEU A  97      -7.007  26.386 -15.336  1.00 16.06           C  
ANISOU  753  C   LEU A  97     1982   2016   2103    173     60    439       C  
ATOM    754  O   LEU A  97      -8.125  25.864 -15.509  1.00 18.85           O  
ANISOU  754  O   LEU A  97     2089   2792   2282   -213    -74    615       O  
ATOM    755  CB  LEU A  97      -5.368  24.524 -15.377  1.00 14.93           C  
ANISOU  755  CB  LEU A  97     1663   2408   1603    269    264    226       C  
ATOM    756  CG  LEU A  97      -4.135  23.803 -14.790  1.00 13.65           C  
ANISOU  756  CG  LEU A  97     1635   1888   1661    -19    -46    -11       C  
ATOM    757  CD1 LEU A  97      -3.959  22.452 -15.509  1.00 16.55           C  
ANISOU  757  CD1 LEU A  97     2776   2114   1398    431    129    -67       C  
ATOM    758  CD2 LEU A  97      -2.894  24.642 -14.904  1.00 16.54           C  
ANISOU  758  CD2 LEU A  97     1661   2532   2091   -187    266    550       C  
ATOM    759  N   ASN A  98      -6.609  27.551 -15.840  1.00 15.26           N  
ANISOU  759  N   ASN A  98     2238   1678   1880    278    190    136       N  
ATOM    760  CA  ASN A  98      -7.573  28.393 -16.561  1.00 18.00           C  
ANISOU  760  CA  ASN A  98     2417   2181   2240    535    388    588       C  
ATOM    761  C   ASN A  98      -6.936  29.008 -17.801  1.00 18.76           C  
ANISOU  761  C   ASN A  98     2549   2555   2026    -92     65    560       C  
ATOM    762  O   ASN A  98      -5.849  29.564 -17.702  1.00 18.18           O  
ANISOU  762  O   ASN A  98     2270   2415   2223    182    -40    594       O  
ATOM    763  CB  ASN A  98      -8.073  29.557 -15.686  1.00 17.91           C  
ANISOU  763  CB  ASN A  98     2112   1926   2768    415    498    581       C  
ATOM    764  CG  ASN A  98      -8.842  29.017 -14.491  1.00 19.94           C  
ANISOU  764  CG  ASN A  98     2607   2672   2299     85    501    205       C  
ATOM    765  OD1 ASN A  98      -8.234  28.617 -13.505  1.00 22.50           O  
ANISOU  765  OD1 ASN A  98     2983   2930   2637    705    686    646       O  
ATOM    766  ND2 ASN A  98     -10.146  29.038 -14.631  1.00 23.55           N  
ANISOU  766  ND2 ASN A  98     2551   4009   2389   -416    634    318       N  
ATOM    767  N   PHE A  99      -7.617  28.904 -18.950  1.00 23.39           N  
ANISOU  767  N   PHE A  99     2864   3979   2044   -522     63    149       N  
ATOM    768  CA  PHE A  99      -7.152  29.622 -20.141  1.00 22.35           C  
ANISOU  768  CA  PHE A  99     2349   4160   1983    538     31    618       C  
ATOM    769  C   PHE A  99      -8.292  29.862 -21.148  1.00 26.26           C  
ANISOU  769  C   PHE A  99     2032   4813   3132     20   -510    574       C  
ATOM    770  O   PHE A  99      -9.392  29.390 -20.779  1.00 27.36           O  
ANISOU  770  O   PHE A  99     2562   4500   3332   -135   -273   1297       O  
ATOM    771  CB  PHE A  99      -5.992  28.882 -20.789  1.00 20.88           C  
ANISOU  771  CB  PHE A  99     2393   3220   2320    248     33    456       C  
ATOM    772  CG  PHE A  99      -6.242  27.505 -21.362  1.00 22.84           C  
ANISOU  772  CG  PHE A  99     2641   3456   2581    -72   -284    389       C  
ATOM    773  CD1 PHE A  99      -6.202  26.411 -20.527  1.00 23.35           C  
ANISOU  773  CD1 PHE A  99     2637   3222   3013     -3    251    427       C  
ATOM    774  CD2 PHE A  99      -6.477  27.330 -22.721  1.00 27.89           C  
ANISOU  774  CD2 PHE A  99     3896   4004   2696    143   -388    -18       C  
ATOM    775  CE1 PHE A  99      -6.397  25.143 -21.027  1.00 27.26           C  
ANISOU  775  CE1 PHE A  99     3606   3395   3358     -9    107    114       C  
ATOM    776  CE2 PHE A  99      -6.704  26.056 -23.236  1.00 28.32           C  
ANISOU  776  CE2 PHE A  99     3533   4187   3040   -115   -220   -212       C  
ATOM    777  CZ  PHE A  99      -6.656  24.976 -22.370  1.00 29.69           C  
ANISOU  777  CZ  PHE A  99     3715   3984   3584    -60   -269   -108       C  
TER     778      PHE A  99                                                      
ATOM    779  N   PRO B   1     -11.069  27.133 -20.955  1.00 27.63           N  
ANISOU  779  N   PRO B   1     3312   4638   2549    323    -65    249       N  
ATOM    780  CA  PRO B   1     -11.648  26.223 -19.958  1.00 26.07           C  
ANISOU  780  CA  PRO B   1     2658   4413   2835    -83   -142      2       C  
ATOM    781  C   PRO B   1     -11.114  26.481 -18.561  1.00 25.16           C  
ANISOU  781  C   PRO B   1     2562   4335   2662    288   -100    481       C  
ATOM    782  O   PRO B   1     -10.076  27.121 -18.367  1.00 25.78           O  
ANISOU  782  O   PRO B   1     2899   4620   2275     44   -398    509       O  
ATOM    783  CB  PRO B   1     -11.163  24.840 -20.422  1.00 31.26           C  
ANISOU  783  CB  PRO B   1     4018   4498   3361    227     35     21       C  
ATOM    784  CG  PRO B   1      -9.943  25.095 -21.244  1.00 34.88           C  
ANISOU  784  CG  PRO B   1     4296   5066   3889    786    655   -203       C  
ATOM    785  CD  PRO B   1      -9.930  26.530 -21.676  1.00 33.90           C  
ANISOU  785  CD  PRO B   1     3925   5547   3409    660    825    580       C  
ATOM    786  N   GLN B   2     -11.861  25.955 -17.595  1.00 28.36           N  
ANISOU  786  N   GLN B   2     2801   4880   3096    484     83   1084       N  
ATOM    787  CA  GLN B   2     -11.420  25.915 -16.207  1.00 22.59           C  
ANISOU  787  CA  GLN B   2     2229   3275   3080    410    227   1006       C  
ATOM    788  C   GLN B   2     -11.304  24.441 -15.853  1.00 22.82           C  
ANISOU  788  C   GLN B   2     2076   2992   3601    211   -122    503       C  
ATOM    789  O   GLN B   2     -12.308  23.712 -15.929  1.00 28.00           O  
ANISOU  789  O   GLN B   2     2065   3442   5132     24   -495    894       O  
ATOM    790  CB  GLN B   2     -12.387  26.629 -15.259  1.00 23.19           C  
ANISOU  790  CB  GLN B   2     2057   3329   3426    640     20    756       C  
ATOM    791  CG  GLN B   2     -11.922  26.405 -13.832  1.00 25.30           C  
ANISOU  791  CG  GLN B   2     2931   3547   3136    155    223    824       C  
ATOM    792  CD  GLN B   2     -12.583  27.219 -12.759  1.00 30.73           C  
ANISOU  792  CD  GLN B   2     2820   5109   3748   -264    900    124       C  
ATOM    793  OE1 GLN B   2     -13.470  26.764 -12.025  1.00 45.79           O  
ANISOU  793  OE1 GLN B   2     5595   6069   5732   -454   3028    855       O  
ATOM    794  NE2 GLN B   2     -12.157  28.466 -12.592  1.00 34.27           N  
ANISOU  794  NE2 GLN B   2     3808   4194   5020    784   1918     43       N  
ATOM    795  N   ILE B   3     -10.098  24.014 -15.520  1.00 17.91           N  
ANISOU  795  N   ILE B   3     2061   2573   2173    107   -121     88       N  
ATOM    796  CA  ILE B   3      -9.872  22.576 -15.357  1.00 17.05           C  
ANISOU  796  CA  ILE B   3     2157   2496   1825     34    -22     36       C  
ATOM    797  C   ILE B   3      -9.574  22.294 -13.903  1.00 16.68           C  
ANISOU  797  C   ILE B   3     1867   2605   1866   -286     60    122       C  
ATOM    798  O   ILE B   3      -8.624  22.851 -13.330  1.00 16.14           O  
ANISOU  798  O   ILE B   3     1728   2318   2087    -90   -125    218       O  
ATOM    799  CB  ILE B   3      -8.711  22.100 -16.249  1.00 18.87           C  
ANISOU  799  CB  ILE B   3     2569   2785   1815    471    175    419       C  
ATOM    800  CG1 ILE B   3      -8.976  22.363 -17.746  1.00 22.90           C  
ANISOU  800  CG1 ILE B   3     3246   3711   1743   -207    224    546       C  
ATOM    801  CG2 ILE B   3      -8.396  20.633 -15.982  1.00 19.49           C  
ANISOU  801  CG2 ILE B   3     2386   2580   2439    309   -314    -18       C  
ATOM    802  CD1 ILE B   3      -7.862  22.062 -18.721  1.00 22.62           C  
ANISOU  802  CD1 ILE B   3     2934   3871   1791   -152    149    830       C  
ATOM    803  N   THR B   4     -10.431  21.467 -13.285  1.00 16.16           N  
ANISOU  803  N   THR B   4     1843   2169   2129    -48    187    157       N  
ATOM    804  CA  THR B   4     -10.125  21.095 -11.907  1.00 17.41           C  
ANISOU  804  CA  THR B   4     1981   2458   2178    -68     43    395       C  
ATOM    805  C   THR B   4      -9.097  19.978 -11.901  1.00 16.53           C  
ANISOU  805  C   THR B   4     1856   2531   1894   -132    -21     95       C  
ATOM    806  O   THR B   4      -8.740  19.423 -12.946  1.00 18.00           O  
ANISOU  806  O   THR B   4     2372   2737   1732     16    -31    261       O  
ATOM    807  CB  THR B   4     -11.402  20.686 -11.149  1.00 17.99           C  
ANISOU  807  CB  THR B   4     2240   2283   2313    -41    455     84       C  
ATOM    808  OG1 THR B   4     -12.094  19.656 -11.852  1.00 21.38           O  
ANISOU  808  OG1 THR B   4     2336   3119   2670   -493    449   -224       O  
ATOM    809  CG2 THR B   4     -12.376  21.855 -11.087  1.00 21.94           C  
ANISOU  809  CG2 THR B   4     2227   2674   3436    252    401    537       C  
ATOM    810  N   LEU B   5      -8.643  19.627 -10.706  1.00 14.62           N  
ANISOU  810  N   LEU B   5     1709   2123   1725   -122    253    112       N  
ATOM    811  CA  LEU B   5      -7.465  18.757 -10.621  1.00 13.36           C  
ANISOU  811  CA  LEU B   5     1681   1819   1576   -271    170   -163       C  
ATOM    812  C   LEU B   5      -7.740  17.478  -9.881  1.00 13.03           C  
ANISOU  812  C   LEU B   5     1582   1977   1391   -358    280      4       C  
ATOM    813  O   LEU B   5      -6.801  16.861  -9.379  1.00 14.11           O  
ANISOU  813  O   LEU B   5     1558   2251   1553   -565     78    190       O  
ATOM    814  CB  LEU B   5      -6.266  19.546 -10.017  1.00 14.44           C  
ANISOU  814  CB  LEU B   5     1754   2403   1329   -729    286    -34       C  
ATOM    815  CG  LEU B   5      -5.811  20.679 -10.976  1.00 12.92           C  
ANISOU  815  CG  LEU B   5     1714   2013   1180   -349    119   -100       C  
ATOM    816  CD1 LEU B   5      -4.930  21.691 -10.294  1.00 14.64           C  
ANISOU  816  CD1 LEU B   5     1599   1849   2116   -265    257   -547       C  
ATOM    817  CD2 LEU B   5      -5.110  20.092 -12.227  1.00 15.86           C  
ANISOU  817  CD2 LEU B   5     2454   2347   1227   -502    456   -208       C  
ATOM    818  N   TRP B   6      -9.016  17.050  -9.818  1.00 14.00           N  
ANISOU  818  N   TRP B   6     1572   2300   1448   -353    208      8       N  
ATOM    819  CA  TRP B   6      -9.318  15.773  -9.160  1.00 14.76           C  
ANISOU  819  CA  TRP B   6     1633   2325   1648   -638    380    -71       C  
ATOM    820  C   TRP B   6      -8.842  14.567  -9.966  1.00 15.14           C  
ANISOU  820  C   TRP B   6     1816   2232   1702   -677    664     97       C  
ATOM    821  O   TRP B   6      -8.658  13.467  -9.427  1.00 19.51           O  
ANISOU  821  O   TRP B   6     3007   2336   2069   -367    818    229       O  
ATOM    822  CB  TRP B   6     -10.825  15.634  -8.951  1.00 16.05           C  
ANISOU  822  CB  TRP B   6     1592   2715   1790   -537    351   -129       C  
ATOM    823  CG  TRP B   6     -11.392  16.724  -8.104  1.00 17.49           C  
ANISOU  823  CG  TRP B   6     1990   2987   1669   -218    549     61       C  
ATOM    824  CD1 TRP B   6     -11.962  17.897  -8.505  1.00 15.74           C  
ANISOU  824  CD1 TRP B   6     1402   2860   1718   -414    -31   -326       C  
ATOM    825  CD2 TRP B   6     -11.428  16.730  -6.651  1.00 17.46           C  
ANISOU  825  CD2 TRP B   6     1911   3056   1668   -526    405    -33       C  
ATOM    826  NE1 TRP B   6     -12.356  18.622  -7.406  1.00 17.08           N  
ANISOU  826  NE1 TRP B   6     2051   2675   1764   -699    201   -379       N  
ATOM    827  CE2 TRP B   6     -12.038  17.921  -6.264  1.00 17.45           C  
ANISOU  827  CE2 TRP B   6     2042   2852   1737   -815    300   -277       C  
ATOM    828  CE3 TRP B   6     -10.997  15.805  -5.686  1.00 18.04           C  
ANISOU  828  CE3 TRP B   6     2382   2941   1531   -837   -179   -236       C  
ATOM    829  CZ2 TRP B   6     -12.227  18.223  -4.909  1.00 19.66           C  
ANISOU  829  CZ2 TRP B   6     2013   3706   1750   -248    565    -97       C  
ATOM    830  CZ3 TRP B   6     -11.181  16.085  -4.332  1.00 18.64           C  
ANISOU  830  CZ3 TRP B   6     2122   3314   1646   -643    467   -152       C  
ATOM    831  CH2 TRP B   6     -11.793  17.298  -3.990  1.00 20.19           C  
ANISOU  831  CH2 TRP B   6     2448   3375   1849   -454    522    -48       C  
ATOM    832  N   GLN B   7      -8.662  14.792 -11.262  1.00 15.35           N  
ANISOU  832  N   GLN B   7     1626   2573   1632   -594    526     17       N  
ATOM    833  CA  GLN B   7      -8.095  13.803 -12.176  1.00 16.20           C  
ANISOU  833  CA  GLN B   7     1795   2511   1851   -735    548   -248       C  
ATOM    834  C   GLN B   7      -6.916  14.412 -12.922  1.00 14.00           C  
ANISOU  834  C   GLN B   7     1683   2031   1604   -451    439   -163       C  
ATOM    835  O   GLN B   7      -6.750  15.646 -12.944  1.00 16.51           O  
ANISOU  835  O   GLN B   7     2352   2045   1877   -504    470     36       O  
ATOM    836  CB AGLN B   7      -9.165  13.303 -13.154  0.56 19.13           C  
ANISOU  836  CB AGLN B   7     1649   3068   2553   -599    382   -686       C  
ATOM    837  CB BGLN B   7      -9.122  13.265 -13.157  0.44 18.51           C  
ANISOU  837  CB BGLN B   7     1839   2714   2479   -682    183   -405       C  
ATOM    838  CG AGLN B   7     -10.464  12.989 -12.447  0.56 23.75           C  
ANISOU  838  CG AGLN B   7     1682   4064   3277   -804    585   -443       C  
ATOM    839  CG BGLN B   7      -9.760  14.234 -14.125  0.44 17.43           C  
ANISOU  839  CG BGLN B   7     1673   2412   2536  -1102    104   -338       C  
ATOM    840  CD AGLN B   7     -11.248  11.768 -12.802  0.56 28.80           C  
ANISOU  840  CD AGLN B   7     2822   4553   3567  -1661   1705   -967       C  
ATOM    841  CD BGLN B   7     -10.673  13.517 -15.107  0.44 20.69           C  
ANISOU  841  CD BGLN B   7     2157   3388   2315   -982     13   -819       C  
ATOM    842  OE1AGLN B   7     -12.129  11.280 -12.056  0.56 30.95           O  
ANISOU  842  OE1AGLN B   7     2735   5144   3880  -1597   1535   -211       O  
ATOM    843  OE1BGLN B   7     -10.734  13.852 -16.292  0.44 31.21           O  
ANISOU  843  OE1BGLN B   7     3216   6419   2222  -1402     85   -433       O  
ATOM    844  NE2AGLN B   7     -10.991  11.214 -13.983  0.56 32.95           N  
ANISOU  844  NE2AGLN B   7     4685   4879   2954  -1717   1244   -767       N  
ATOM    845  NE2BGLN B   7     -11.388  12.499 -14.648  0.44 27.41           N  
ANISOU  845  NE2BGLN B   7     3000   3549   3863  -1881  -1829    -11       N  
ATOM    846  N   ARG B   8      -6.093  13.585 -13.547  1.00 14.70           N  
ANISOU  846  N   ARG B   8     1635   2307   1643   -243    369    -71       N  
ATOM    847  CA  ARG B   8      -4.981  14.130 -14.306  1.00 13.91           C  
ANISOU  847  CA  ARG B   8     1775   1984   1527   -142    476     73       C  
ATOM    848  C   ARG B   8      -5.504  15.023 -15.417  1.00 13.90           C  
ANISOU  848  C   ARG B   8     1966   1784   1531   -166     94   -200       C  
ATOM    849  O   ARG B   8      -6.421  14.640 -16.142  1.00 15.31           O  
ANISOU  849  O   ARG B   8     1694   2402   1722   -427    264    -98       O  
ATOM    850  CB  ARG B   8      -4.178  12.946 -14.876  1.00 15.25           C  
ANISOU  850  CB  ARG B   8     2070   2057   1665     17    566    104       C  
ATOM    851  CG  ARG B   8      -3.458  12.108 -13.848  1.00 16.50           C  
ANISOU  851  CG  ARG B   8     2565   1843   1862     11    136    -40       C  
ATOM    852  CD  ARG B   8      -2.640  10.959 -14.415  1.00 20.50           C  
ANISOU  852  CD  ARG B   8     3109   2012   2667    369     -9   -303       C  
ATOM    853  NE  ARG B   8      -1.826  10.289 -13.385  1.00 24.42           N  
ANISOU  853  NE  ARG B   8     3379   2739   3159    926   -436   -626       N  
ATOM    854  CZ  ARG B   8      -1.269   9.099 -13.495  1.00 26.99           C  
ANISOU  854  CZ  ARG B   8     3705   2918   3631   1196  -1265   -987       C  
ATOM    855  NH1 ARG B   8      -1.424   8.376 -14.609  1.00 39.42           N  
ANISOU  855  NH1 ARG B   8     6744   4081   4152   2227  -1541  -1909       N  
ATOM    856  NH2 ARG B   8      -0.545   8.571 -12.518  1.00 28.65           N  
ANISOU  856  NH2 ARG B   8     4193   2876   3819    373   -970    428       N  
ATOM    857  N   PRO B   9      -4.953  16.216 -15.583  1.00 14.30           N  
ANISOU  857  N   PRO B   9     1923   2028   1483   -305     17     73       N  
ATOM    858  CA  PRO B   9      -5.434  17.145 -16.622  1.00 13.41           C  
ANISOU  858  CA  PRO B   9     1840   2073   1181   -321    150    -32       C  
ATOM    859  C   PRO B   9      -4.897  16.813 -18.009  1.00 15.18           C  
ANISOU  859  C   PRO B   9     2210   2236   1321   -733    375   -238       C  
ATOM    860  O   PRO B   9      -4.007  17.500 -18.524  1.00 16.25           O  
ANISOU  860  O   PRO B   9     1889   2759   1526   -703    369   -115       O  
ATOM    861  CB  PRO B   9      -4.942  18.504 -16.121  1.00 13.72           C  
ANISOU  861  CB  PRO B   9     1817   1908   1488    149    -68   -200       C  
ATOM    862  CG  PRO B   9      -3.697  18.176 -15.367  1.00 13.49           C  
ANISOU  862  CG  PRO B   9     2040   1791   1296   -140   -228    223       C  
ATOM    863  CD  PRO B   9      -3.939  16.826 -14.715  1.00 14.11           C  
ANISOU  863  CD  PRO B   9     1901   1964   1496   -479    -11    336       C  
ATOM    864  N   ILE B  10      -5.496  15.746 -18.565  1.00 15.18           N  
ANISOU  864  N   ILE B  10     2205   2053   1508   -352   -102   -217       N  
ATOM    865  CA  ILE B  10      -5.106  15.286 -19.894  1.00 16.83           C  
ANISOU  865  CA  ILE B  10     2652   2355   1389   -493   -168   -263       C  
ATOM    866  C   ILE B  10      -5.991  15.994 -20.919  1.00 17.38           C  
ANISOU  866  C   ILE B  10     1944   3184   1474   -565     97     19       C  
ATOM    867  O   ILE B  10      -7.221  16.064 -20.794  1.00 23.31           O  
ANISOU  867  O   ILE B  10     1850   5275   1732  -1038    -68    183       O  
ATOM    868  CB  ILE B  10      -5.185  13.748 -19.961  1.00 20.09           C  
ANISOU  868  CB  ILE B  10     3267   2422   1943   -435     73   -707       C  
ATOM    869  CG1 ILE B  10      -4.153  13.131 -19.000  1.00 24.25           C  
ANISOU  869  CG1 ILE B  10     4527   2590   2096    444    218   -141       C  
ATOM    870  CG2 ILE B  10      -5.037  13.283 -21.397  1.00 23.26           C  
ANISOU  870  CG2 ILE B  10     3228   3449   2162   -451    175  -1216       C  
ATOM    871  CD1 ILE B  10      -4.277  11.646 -18.779  1.00 31.37           C  
ANISOU  871  CD1 ILE B  10     5687   2753   3479   -112    -28    144       C  
ATOM    872  N   VAL B  11      -5.367  16.580 -21.939  1.00 17.91           N  
ANISOU  872  N   VAL B  11     2302   2756   1749   -424    313    204       N  
ATOM    873  CA  VAL B  11      -6.073  17.334 -22.957  1.00 17.69           C  
ANISOU  873  CA  VAL B  11     2235   2805   1681   -502    131     19       C  
ATOM    874  C   VAL B  11      -5.691  16.810 -24.343  1.00 18.14           C  
ANISOU  874  C   VAL B  11     2321   2802   1771   -665    -18   -205       C  
ATOM    875  O   VAL B  11      -4.686  16.128 -24.505  1.00 18.68           O  
ANISOU  875  O   VAL B  11     3146   2264   1688   -257    157    -73       O  
ATOM    876  CB  VAL B  11      -5.802  18.845 -22.910  1.00 21.67           C  
ANISOU  876  CB  VAL B  11     3371   2551   2311    196    310   -152       C  
ATOM    877  CG1 VAL B  11      -6.244  19.446 -21.559  1.00 25.30           C  
ANISOU  877  CG1 VAL B  11     3962   3410   2240    844    -82   -429       C  
ATOM    878  CG2 VAL B  11      -4.330  19.155 -23.169  1.00 22.30           C  
ANISOU  878  CG2 VAL B  11     3977   2799   1698  -1339    138     30       C  
ATOM    879  N   THR B  12      -6.553  17.160 -25.312  1.00 20.15           N  
ANISOU  879  N   THR B  12     2842   3035   1779   -714   -218    121       N  
ATOM    880  CA  THR B  12      -6.206  16.794 -26.674  1.00 21.24           C  
ANISOU  880  CA  THR B  12     3017   3273   1780    102    -90    321       C  
ATOM    881  C   THR B  12      -5.469  17.934 -27.342  1.00 22.58           C  
ANISOU  881  C   THR B  12     3426   3248   1906     53    249    198       C  
ATOM    882  O   THR B  12      -5.846  19.099 -27.271  1.00 25.24           O  
ANISOU  882  O   THR B  12     3225   3241   3124     25    330    292       O  
ATOM    883  CB  THR B  12      -7.437  16.523 -27.552  1.00 25.31           C  
ANISOU  883  CB  THR B  12     4212   3424   1982   -411   -781    -26       C  
ATOM    884  OG1 THR B  12      -8.194  15.468 -26.928  1.00 31.15           O  
ANISOU  884  OG1 THR B  12     4963   3926   2947  -1322   -678   -217       O  
ATOM    885  CG2 THR B  12      -6.967  16.090 -28.930  1.00 35.97           C  
ANISOU  885  CG2 THR B  12     5486   5796   2386   -895   -343   -865       C  
ATOM    886  N   ILE B  13      -4.398  17.541 -28.022  1.00 22.22           N  
ANISOU  886  N   ILE B  13     3385   3360   1697    -97    161     35       N  
ATOM    887  CA  ILE B  13      -3.646  18.513 -28.807  1.00 21.61           C  
ANISOU  887  CA  ILE B  13     3571   2942   1698     44    260    -24       C  
ATOM    888  C   ILE B  13      -3.609  18.081 -30.254  1.00 23.74           C  
ANISOU  888  C   ILE B  13     4473   2800   1746    151    494    -54       C  
ATOM    889  O   ILE B  13      -3.664  16.893 -30.598  1.00 31.95           O  
ANISOU  889  O   ILE B  13     7285   2781   2074    560   1121   -185       O  
ATOM    890  CB  ILE B  13      -2.228  18.600 -28.212  1.00 24.54           C  
ANISOU  890  CB  ILE B  13     3655   2956   2713   -248     -6    396       C  
ATOM    891  CG1 ILE B  13      -1.439  17.332 -28.488  1.00 27.77           C  
ANISOU  891  CG1 ILE B  13     3418   3935   3197    230    232   -193       C  
ATOM    892  CG2 ILE B  13      -2.372  18.893 -26.734  1.00 27.11           C  
ANISOU  892  CG2 ILE B  13     4270   3210   2820    603   -918   -273       C  
ATOM    893  CD1 ILE B  13      -0.035  17.243 -28.007  1.00 32.11           C  
ANISOU  893  CD1 ILE B  13     3559   5335   3305    278     83   1351       C  
ATOM    894  N   LYS B  14      -3.564  19.079 -31.103  1.00 18.78           N  
ANISOU  894  N   LYS B  14     2464   2954   1720   -644    242     -3       N  
ATOM    895  CA  LYS B  14      -3.391  18.770 -32.525  1.00 18.02           C  
ANISOU  895  CA  LYS B  14     2175   2955   1718   -265     51     74       C  
ATOM    896  C   LYS B  14      -2.032  19.267 -32.961  1.00 18.77           C  
ANISOU  896  C   LYS B  14     2368   2949   1814   -401    272   -124       C  
ATOM    897  O   LYS B  14      -1.722  20.445 -32.784  1.00 18.88           O  
ANISOU  897  O   LYS B  14     2675   2871   1628   -450    300     57       O  
ATOM    898  CB  LYS B  14      -4.545  19.413 -33.286  1.00 21.07           C  
ANISOU  898  CB  LYS B  14     2632   2991   2384   -168   -427    233       C  
ATOM    899  CG  LYS B  14      -4.829  18.640 -34.567  1.00 36.06           C  
ANISOU  899  CG  LYS B  14     4622   5192   3888    -83  -2210  -1073       C  
ATOM    900  CD  LYS B  14      -6.082  19.170 -35.271  1.00 45.18           C  
ANISOU  900  CD  LYS B  14     5745   6731   4692   -219  -3188    308       C  
ATOM    901  CE  LYS B  14      -5.688  19.726 -36.630  1.00 51.02           C  
ANISOU  901  CE  LYS B  14     7118   7200   5069  -1150  -3090    685       C  
ATOM    902  NZ  LYS B  14      -5.501  18.656 -37.656  1.00 72.71           N  
ANISOU  902  NZ  LYS B  14    11419  10554   5652  -1147  -1241  -1126       N  
ATOM    903  N   ILE B  15      -1.256  18.352 -33.511  1.00 18.86           N  
ANISOU  903  N   ILE B  15     2514   3075   1579   -410    389   -147       N  
ATOM    904  CA  ILE B  15       0.113  18.654 -33.903  1.00 20.98           C  
ANISOU  904  CA  ILE B  15     2591   3241   2141   -378    608   -446       C  
ATOM    905  C   ILE B  15       0.639  17.633 -34.926  1.00 25.13           C  
ANISOU  905  C   ILE B  15     3354   3578   2617   -441   1077   -847       C  
ATOM    906  O   ILE B  15       0.368  16.410 -34.862  1.00 22.87           O  
ANISOU  906  O   ILE B  15     2417   3430   2840   -158    269   -757       O  
ATOM    907  CB  ILE B  15       1.072  18.605 -32.700  1.00 21.69           C  
ANISOU  907  CB  ILE B  15     2604   2700   2936   -430    111   -592       C  
ATOM    908  CG1 ILE B  15       2.521  18.915 -33.077  1.00 23.44           C  
ANISOU  908  CG1 ILE B  15     2573   3458   2876    -20    306    -63       C  
ATOM    909  CG2 ILE B  15       0.919  17.254 -32.005  1.00 21.31           C  
ANISOU  909  CG2 ILE B  15     2677   2648   2771    -89     66   -609       C  
ATOM    910  CD1 ILE B  15       3.501  19.012 -31.939  1.00 25.32           C  
ANISOU  910  CD1 ILE B  15     2611   3622   3388   -575    144   -951       C  
ATOM    911  N   GLY B  16       1.443  18.138 -35.870  1.00 22.53           N  
ANISOU  911  N   GLY B  16     2728   3961   1871   -146    364   -556       N  
ATOM    912  CA  GLY B  16       1.992  17.198 -36.860  1.00 24.20           C  
ANISOU  912  CA  GLY B  16     3269   3929   1998   -706    701   -842       C  
ATOM    913  C   GLY B  16       0.950  16.372 -37.593  1.00 26.95           C  
ANISOU  913  C   GLY B  16     3506   3757   2975   -727    335   -825       C  
ATOM    914  O   GLY B  16       1.206  15.219 -37.996  1.00 28.50           O  
ANISOU  914  O   GLY B  16     4182   3366   3280   -908    260   -556       O  
ATOM    915  N   GLY B  17      -0.230  16.974 -37.772  1.00 27.52           N  
ANISOU  915  N   GLY B  17     3660   3898   2898   -732    -57   -238       N  
ATOM    916  CA  GLY B  17      -1.370  16.382 -38.445  1.00 29.84           C  
ANISOU  916  CA  GLY B  17     4375   4069   2893   -883   -778    101       C  
ATOM    917  C   GLY B  17      -2.004  15.259 -37.649  1.00 31.39           C  
ANISOU  917  C   GLY B  17     4227   4911   2788  -1569   -626      4       C  
ATOM    918  O   GLY B  17      -2.777  14.478 -38.210  1.00 34.95           O  
ANISOU  918  O   GLY B  17     4520   5441   3317  -1887  -1004     48       O  
ATOM    919  N   GLN B  18      -1.710  15.114 -36.364  1.00 27.40           N  
ANISOU  919  N   GLN B  18     3917   4160   2335   -964    191   -591       N  
ATOM    920  CA  GLN B  18      -2.260  14.015 -35.598  1.00 25.81           C  
ANISOU  920  CA  GLN B  18     3743   3382   2681   -144    254   -524       C  
ATOM    921  C   GLN B  18      -3.038  14.615 -34.434  1.00 21.76           C  
ANISOU  921  C   GLN B  18     3065   2854   2349   -441   -107   -429       C  
ATOM    922  O   GLN B  18      -2.735  15.732 -33.999  1.00 22.68           O  
ANISOU  922  O   GLN B  18     3356   2765   2496   -406   -328   -291       O  
ATOM    923  CB  GLN B  18      -1.163  13.124 -35.016  1.00 34.81           C  
ANISOU  923  CB  GLN B  18     4526   4455   4246   1054    310   -451       C  
ATOM    924  CG  GLN B  18      -0.426  12.182 -35.958  1.00 41.03           C  
ANISOU  924  CG  GLN B  18     5473   4531   5586   1156   1078   -719       C  
ATOM    925  CD  GLN B  18       0.566  11.295 -35.218  1.00 43.87           C  
ANISOU  925  CD  GLN B  18     5462   4190   7018   1293   1617    139       C  
ATOM    926  OE1 GLN B  18       0.237  10.665 -34.198  1.00 49.16           O  
ANISOU  926  OE1 GLN B  18     4485   5130   9062   -446    726   1922       O  
ATOM    927  NE2 GLN B  18       1.811  11.212 -35.672  1.00 39.64           N  
ANISOU  927  NE2 GLN B  18     4589   4916   5557     15    292  -1034       N  
ATOM    928  N   LEU B  19      -4.002  13.898 -33.913  1.00 24.89           N  
ANISOU  928  N   LEU B  19     3901   3152   2403   -840    176   -239       N  
ATOM    929  CA  LEU B  19      -4.570  14.262 -32.614  1.00 26.31           C  
ANISOU  929  CA  LEU B  19     3618   3806   2572   -324    209   -301       C  
ATOM    930  C   LEU B  19      -3.853  13.432 -31.547  1.00 27.26           C  
ANISOU  930  C   LEU B  19     4680   3320   2359    -24    242   -484       C  
ATOM    931  O   LEU B  19      -3.827  12.188 -31.672  1.00 34.11           O  
ANISOU  931  O   LEU B  19     6225   3258   3478   -128    157   -536       O  
ATOM    932  CB  LEU B  19      -6.077  14.025 -32.571  1.00 29.48           C  
ANISOU  932  CB  LEU B  19     3728   3383   4092   -638    583   -191       C  
ATOM    933  CG  LEU B  19      -6.899  15.047 -33.359  1.00 33.98           C  
ANISOU  933  CG  LEU B  19     3803   5033   4073   -821  -1067   -289       C  
ATOM    934  CD1 LEU B  19      -8.379  14.692 -33.241  1.00 44.54           C  
ANISOU  934  CD1 LEU B  19     3611   8187   5124   -920   -927  -2405       C  
ATOM    935  CD2 LEU B  19      -6.661  16.475 -32.882  1.00 37.00           C  
ANISOU  935  CD2 LEU B  19     4255   4000   5804    325   -779    327       C  
ATOM    936  N   LYS B  20      -3.300  14.143 -30.553  1.00 26.11           N  
ANISOU  936  N   LYS B  20     4200   3602   2118   -523    371   -172       N  
ATOM    937  CA  LYS B  20      -2.626  13.435 -29.464  1.00 23.67           C  
ANISOU  937  CA  LYS B  20     3721   3082   2189    -70    706   -411       C  
ATOM    938  C   LYS B  20      -3.188  13.801 -28.090  1.00 21.53           C  
ANISOU  938  C   LYS B  20     3371   2806   2003   -219    388   -501       C  
ATOM    939  O   LYS B  20      -3.843  14.827 -27.953  1.00 25.78           O  
ANISOU  939  O   LYS B  20     4755   2823   2218    219   1068   -140       O  
ATOM    940  CB  LYS B  20      -1.117  13.695 -29.499  1.00 27.67           C  
ANISOU  940  CB  LYS B  20     3702   4034   2776     29    920   -129       C  
ATOM    941  CG  LYS B  20      -0.496  13.342 -30.856  1.00 33.44           C  
ANISOU  941  CG  LYS B  20     4462   4873   3370    413   1667   -292       C  
ATOM    942  CD  LYS B  20       1.005  13.193 -30.683  1.00 36.75           C  
ANISOU  942  CD  LYS B  20     4623   4909   4431   1292   1747    123       C  
ATOM    943  CE  LYS B  20       1.307  11.788 -30.184  1.00 39.58           C  
ANISOU  943  CE  LYS B  20     5090   4390   5560    599   1702     31       C  
ATOM    944  NZ  LYS B  20       1.534  10.813 -31.289  1.00 39.17           N  
ANISOU  944  NZ  LYS B  20     3752   5091   6042   1258   1553   -408       N  
ATOM    945  N   GLU B  21      -2.933  12.935 -27.102  1.00 20.92           N  
ANISOU  945  N   GLU B  21     3165   2854   1930   -193   -105   -686       N  
ATOM    946  CA  GLU B  21      -3.317  13.284 -25.726  1.00 20.69           C  
ANISOU  946  CA  GLU B  21     3064   2985   1810   -552   -201   -671       C  
ATOM    947  C   GLU B  21      -2.071  13.657 -24.953  1.00 19.52           C  
ANISOU  947  C   GLU B  21     2767   2378   2273   -502     11   -880       C  
ATOM    948  O   GLU B  21      -1.052  12.983 -25.133  1.00 20.56           O  
ANISOU  948  O   GLU B  21     2830   2830   2151   -349    271   -736       O  
ATOM    949  CB  GLU B  21      -4.007  12.111 -25.030  1.00 26.28           C  
ANISOU  949  CB  GLU B  21     3287   4382   2315  -1611   -515   -119       C  
ATOM    950  CG  GLU B  21      -5.292  11.543 -25.581  1.00 35.63           C  
ANISOU  950  CG  GLU B  21     3718   5419   4400  -2041  -1231    -79       C  
ATOM    951  CD  GLU B  21      -6.520  12.313 -25.168  1.00 42.22           C  
ANISOU  951  CD  GLU B  21     3443   6770   5829  -1348  -1575    438       C  
ATOM    952  OE1 GLU B  21      -7.101  12.036 -24.088  1.00 57.10           O  
ANISOU  952  OE1 GLU B  21     6227   9984   5485   -459      1  -1410       O  
ATOM    953  OE2 GLU B  21      -6.890  13.194 -25.986  1.00 60.49           O  
ANISOU  953  OE2 GLU B  21     6340   5932  10713  -1232  -2233   2327       O  
ATOM    954  N   ALA B  22      -2.162  14.687 -24.098  1.00 17.70           N  
ANISOU  954  N   ALA B  22     2604   2215   1907   -867    357   -612       N  
ATOM    955  CA  ALA B  22      -0.993  15.043 -23.312  1.00 15.62           C  
ANISOU  955  CA  ALA B  22     2470   2102   1363   -794    468   -311       C  
ATOM    956  C   ALA B  22      -1.434  15.677 -21.989  1.00 14.84           C  
ANISOU  956  C   ALA B  22     1939   2416   1285   -436    424    -99       C  
ATOM    957  O   ALA B  22      -2.504  16.259 -21.871  1.00 16.74           O  
ANISOU  957  O   ALA B  22     2062   2535   1762   -280    301   -159       O  
ATOM    958  CB  ALA B  22      -0.100  16.028 -24.058  1.00 15.44           C  
ANISOU  958  CB  ALA B  22     2219   2026   1620   -502    798   -355       C  
ATOM    959  N   LEU B  23      -0.541  15.548 -21.017  1.00 15.29           N  
ANISOU  959  N   LEU B  23     2073   2304   1431   -350    252   -293       N  
ATOM    960  CA  LEU B  23      -0.800  16.028 -19.658  1.00 13.70           C  
ANISOU  960  CA  LEU B  23     1887   1903   1415   -233     94   -133       C  
ATOM    961  C   LEU B  23      -0.407  17.496 -19.539  1.00 13.14           C  
ANISOU  961  C   LEU B  23     1573   1946   1473   -230     72   -105       C  
ATOM    962  O   LEU B  23       0.756  17.811 -19.830  1.00 14.77           O  
ANISOU  962  O   LEU B  23     1809   2048   1754   -322    481    -89       O  
ATOM    963  CB  LEU B  23      -0.013  15.121 -18.718  1.00 14.30           C  
ANISOU  963  CB  LEU B  23     1760   1909   1763    -19    -60   -233       C  
ATOM    964  CG  LEU B  23      -0.029  15.382 -17.232  1.00 16.41           C  
ANISOU  964  CG  LEU B  23     2388   2254   1593   -294    160    367       C  
ATOM    965  CD1 LEU B  23      -1.409  15.134 -16.684  1.00 19.30           C  
ANISOU  965  CD1 LEU B  23     2441   2894   1997   -681    320   -136       C  
ATOM    966  CD2 LEU B  23       1.000  14.527 -16.447  1.00 21.49           C  
ANISOU  966  CD2 LEU B  23     3058   3241   1865    442     18    389       C  
ATOM    967  N   LEU B  24      -1.288  18.387 -19.115  1.00 13.41           N  
ANISOU  967  N   LEU B  24     1744   1898   1455   -243    249    -43       N  
ATOM    968  CA  LEU B  24      -0.916  19.745 -18.734  1.00 13.33           C  
ANISOU  968  CA  LEU B  24     1640   1989   1435   -173   -124   -160       C  
ATOM    969  C   LEU B  24      -0.109  19.707 -17.430  1.00 13.94           C  
ANISOU  969  C   LEU B  24     1522   2532   1243   -355    123     82       C  
ATOM    970  O   LEU B  24      -0.688  19.438 -16.350  1.00 16.07           O  
ANISOU  970  O   LEU B  24     2008   2754   1343   -512    395      0       O  
ATOM    971  CB  LEU B  24      -2.145  20.629 -18.522  1.00 14.38           C  
ANISOU  971  CB  LEU B  24     1853   1874   1736    -79     42     71       C  
ATOM    972  CG  LEU B  24      -2.956  20.845 -19.797  1.00 14.03           C  
ANISOU  972  CG  LEU B  24     1469   2139   1721    -69    182    149       C  
ATOM    973  CD1 LEU B  24      -4.259  21.570 -19.478  1.00 19.15           C  
ANISOU  973  CD1 LEU B  24     1569   3510   2197    333    277    -55       C  
ATOM    974  CD2 LEU B  24      -2.116  21.591 -20.808  1.00 17.13           C  
ANISOU  974  CD2 LEU B  24     1764   2985   1760   -501    223    254       C  
ATOM    975  N   ASN B  25       1.192  19.976 -17.536  1.00 12.21           N  
ANISOU  975  N   ASN B  25     1368   1836   1434   -128     67    -27       N  
ATOM    976  CA  ASN B  25       2.100  19.658 -16.416  1.00 12.16           C  
ANISOU  976  CA  ASN B  25     1517   1589   1515   -182     36    -48       C  
ATOM    977  C   ASN B  25       2.871  20.886 -15.990  1.00 13.07           C  
ANISOU  977  C   ASN B  25     1802   1983   1182   -526    188   -110       C  
ATOM    978  O   ASN B  25       3.900  21.268 -16.590  1.00 12.66           O  
ANISOU  978  O   ASN B  25     1556   1821   1435   -325     48    103       O  
ATOM    979  CB  ASN B  25       3.053  18.537 -16.870  1.00 13.89           C  
ANISOU  979  CB  ASN B  25     1697   1784   1797    124    161    165       C  
ATOM    980  CG  ASN B  25       3.890  18.005 -15.718  1.00 14.58           C  
ANISOU  980  CG  ASN B  25     2211   1640   1689     91    161    333       C  
ATOM    981  OD1 ASN B  25       3.970  18.672 -14.693  1.00 18.09           O  
ANISOU  981  OD1 ASN B  25     2956   2246   1672   -211     47    220       O  
ATOM    982  ND2 ASN B  25       4.512  16.842 -15.832  1.00 18.95           N  
ANISOU  982  ND2 ASN B  25     2408   2144   2647    633    341    584       N  
ATOM    983  N   THR B  26       2.383  21.564 -14.944  1.00 12.04           N  
ANISOU  983  N   THR B  26     1885   1501   1191    -56     64    101       N  
ATOM    984  CA  THR B  26       3.049  22.782 -14.480  1.00 11.64           C  
ANISOU  984  CA  THR B  26     1547   1466   1410    -37    235    111       C  
ATOM    985  C   THR B  26       4.403  22.466 -13.831  1.00 12.79           C  
ANISOU  985  C   THR B  26     1677   1698   1485    -75    119    207       C  
ATOM    986  O   THR B  26       5.184  23.407 -13.579  1.00 13.69           O  
ANISOU  986  O   THR B  26     1882   1823   1494   -153   -100    121       O  
ATOM    987  CB  THR B  26       2.179  23.559 -13.475  1.00 11.01           C  
ANISOU  987  CB  THR B  26     1705   1578    899     37     -3    198       C  
ATOM    988  OG1 THR B  26       1.883  22.701 -12.364  1.00 11.68           O  
ANISOU  988  OG1 THR B  26     1611   1595   1234    -46    157    361       O  
ATOM    989  CG2 THR B  26       0.863  23.995 -14.123  1.00 12.04           C  
ANISOU  989  CG2 THR B  26     1659   1695   1221    166     32    341       C  
ATOM    990  N   GLY B  27       4.656  21.179 -13.562  1.00 12.59           N  
ANISOU  990  N   GLY B  27     1782   1736   1266      9    -35    357       N  
ATOM    991  CA  GLY B  27       5.967  20.815 -13.065  1.00 12.74           C  
ANISOU  991  CA  GLY B  27     1626   2063   1152   -141    115    533       C  
ATOM    992  C   GLY B  27       6.959  20.512 -14.176  1.00 14.28           C  
ANISOU  992  C   GLY B  27     1862   2197   1365     54    204    327       C  
ATOM    993  O   GLY B  27       8.107  20.131 -13.880  1.00 19.35           O  
ANISOU  993  O   GLY B  27     2020   3267   2064    546    234    352       O  
ATOM    994  N   ALA B  28       6.611  20.701 -15.442  1.00 14.87           N  
ANISOU  994  N   ALA B  28     2266   2152   1230    -99    455    429       N  
ATOM    995  CA  ALA B  28       7.525  20.461 -16.551  1.00 13.46           C  
ANISOU  995  CA  ALA B  28     1886   1788   1438   -355    412    297       C  
ATOM    996  C   ALA B  28       7.883  21.777 -17.223  1.00 11.34           C  
ANISOU  996  C   ALA B  28     1367   1589   1354   -181    276    164       C  
ATOM    997  O   ALA B  28       6.981  22.522 -17.578  1.00 14.25           O  
ANISOU  997  O   ALA B  28     1588   2142   1685     44     83    387       O  
ATOM    998  CB  ALA B  28       6.876  19.545 -17.569  1.00 13.86           C  
ANISOU  998  CB  ALA B  28     1931   1421   1913    -63    382     -6       C  
ATOM    999  N   ASP B  29       9.153  22.064 -17.389  1.00 12.22           N  
ANISOU  999  N   ASP B  29     1420   1848   1375   -348    220    157       N  
ATOM   1000  CA  ASP B  29       9.559  23.295 -18.082  1.00 13.24           C  
ANISOU 1000  CA  ASP B  29     1691   2085   1254   -813     70     84       C  
ATOM   1001  C   ASP B  29       9.153  23.244 -19.552  1.00 12.91           C  
ANISOU 1001  C   ASP B  29     1800   1894   1209   -139     35     44       C  
ATOM   1002  O   ASP B  29       8.734  24.227 -20.154  1.00 16.26           O  
ANISOU 1002  O   ASP B  29     2358   2137   1683    150    244    311       O  
ATOM   1003  CB  ASP B  29      11.095  23.487 -18.035  1.00 14.40           C  
ANISOU 1003  CB  ASP B  29     1626   2325   1520   -705    143     15       C  
ATOM   1004  CG  ASP B  29      11.649  23.618 -16.628  1.00 16.06           C  
ANISOU 1004  CG  ASP B  29     1711   2630   1761    -14   -191   -436       C  
ATOM   1005  OD1 ASP B  29      12.891  23.472 -16.471  1.00 26.63           O  
ANISOU 1005  OD1 ASP B  29     1846   5508   2764    349   -462   -487       O  
ATOM   1006  OD2 ASP B  29      10.892  23.879 -15.664  1.00 16.30           O  
ANISOU 1006  OD2 ASP B  29     2366   2305   1522    -56     46     -6       O  
ATOM   1007  N   ASP B  30       9.328  22.065 -20.156  1.00 12.61           N  
ANISOU 1007  N   ASP B  30     1581   2008   1201   -179    166     -3       N  
ATOM   1008  CA  ASP B  30       9.271  21.844 -21.601  1.00 12.44           C  
ANISOU 1008  CA  ASP B  30     1846   1780   1101   -406    328    122       C  
ATOM   1009  C   ASP B  30       8.165  20.888 -21.974  1.00 11.42           C  
ANISOU 1009  C   ASP B  30     1709   1310   1319    -51      3    239       C  
ATOM   1010  O   ASP B  30       7.674  20.096 -21.151  1.00 14.54           O  
ANISOU 1010  O   ASP B  30     2105   1823   1596   -439    336    395       O  
ATOM   1011  CB  ASP B  30      10.591  21.248 -22.120  1.00 14.31           C  
ANISOU 1011  CB  ASP B  30     1873   2100   1463   -291    387    -57       C  
ATOM   1012  CG  ASP B  30      11.737  22.180 -21.798  1.00 17.75           C  
ANISOU 1012  CG  ASP B  30     1804   2958   1980   -450   -188    -28       C  
ATOM   1013  OD1 ASP B  30      12.745  21.626 -21.320  1.00 25.81           O  
ANISOU 1013  OD1 ASP B  30     1803   5186   2816    241    -97    254       O  
ATOM   1014  OD2 ASP B  30      11.644  23.412 -21.988  1.00 21.11           O  
ANISOU 1014  OD2 ASP B  30     2686   2857   2477  -1293    316    276       O  
ATOM   1015  N   THR B  31       7.791  20.962 -23.252  1.00 13.40           N  
ANISOU 1015  N   THR B  31     1763   1926   1401   -255    -91    179       N  
ATOM   1016  CA  THR B  31       6.797  20.054 -23.836  1.00 11.92           C  
ANISOU 1016  CA  THR B  31     1786   1297   1448     27     10     51       C  
ATOM   1017  C   THR B  31       7.495  18.896 -24.519  1.00 12.50           C  
ANISOU 1017  C   THR B  31     2012   1373   1366    194    395    382       C  
ATOM   1018  O   THR B  31       8.347  19.152 -25.369  1.00 12.94           O  
ANISOU 1018  O   THR B  31     1903   1635   1378    -43    297    264       O  
ATOM   1019  CB  THR B  31       5.915  20.860 -24.831  1.00 10.94           C  
ANISOU 1019  CB  THR B  31     1421   1395   1342     13     54    -38       C  
ATOM   1020  OG1 THR B  31       5.162  21.814 -24.078  1.00 12.14           O  
ANISOU 1020  OG1 THR B  31     1857   1560   1198    162    221     63       O  
ATOM   1021  CG2 THR B  31       4.978  19.986 -25.640  1.00 13.45           C  
ANISOU 1021  CG2 THR B  31     1958   1768   1386   -422     -9    -88       C  
ATOM   1022  N   VAL B  32       7.184  17.671 -24.152  1.00 12.42           N  
ANISOU 1022  N   VAL B  32     2275   1224   1219    -23    314     48       N  
ATOM   1023  CA  VAL B  32       7.827  16.504 -24.796  1.00 13.42           C  
ANISOU 1023  CA  VAL B  32     1770   1467   1863     21    269   -245       C  
ATOM   1024  C   VAL B  32       6.745  15.571 -25.320  1.00 12.77           C  
ANISOU 1024  C   VAL B  32     1882   1421   1548   -156    508   -145       C  
ATOM   1025  O   VAL B  32       5.853  15.183 -24.520  1.00 14.63           O  
ANISOU 1025  O   VAL B  32     2013   1937   1607   -284    508     -6       O  
ATOM   1026  CB  VAL B  32       8.729  15.735 -23.823  1.00 17.16           C  
ANISOU 1026  CB  VAL B  32     2016   1945   2558    353     15    -93       C  
ATOM   1027  CG1 VAL B  32       9.467  14.606 -24.561  1.00 20.11           C  
ANISOU 1027  CG1 VAL B  32     3126   2088   2426    958    600    464       C  
ATOM   1028  CG2 VAL B  32       9.663  16.716 -23.135  1.00 19.85           C  
ANISOU 1028  CG2 VAL B  32     2402   2497   2645   -147   -470    379       C  
ATOM   1029  N   LEU B  33       6.792  15.208 -26.595  1.00 13.57           N  
ANISOU 1029  N   LEU B  33     1865   1830   1463   -119    294   -111       N  
ATOM   1030  CA  LEU B  33       5.805  14.341 -27.233  1.00 15.89           C  
ANISOU 1030  CA  LEU B  33     2186   1849   2000    -13    -42   -295       C  
ATOM   1031  C   LEU B  33       6.509  13.172 -27.919  1.00 14.48           C  
ANISOU 1031  C   LEU B  33     2334   1641   1525   -299    445      5       C  
ATOM   1032  O   LEU B  33       7.602  13.460 -28.484  1.00 15.17           O  
ANISOU 1032  O   LEU B  33     2162   1803   1801   -446    289    -61       O  
ATOM   1033  CB  LEU B  33       4.929  15.105 -28.225  1.00 18.15           C  
ANISOU 1033  CB  LEU B  33     2198   2459   2240     63   -292   -226       C  
ATOM   1034  CG  LEU B  33       4.256  16.369 -27.632  1.00 17.78           C  
ANISOU 1034  CG  LEU B  33     2174   2062   2520      8     -9    293       C  
ATOM   1035  CD1 LEU B  33       3.577  17.182 -28.732  1.00 20.52           C  
ANISOU 1035  CD1 LEU B  33     3072   2208   2517   -116    -88    621       C  
ATOM   1036  CD2 LEU B  33       3.241  15.992 -26.594  1.00 20.65           C  
ANISOU 1036  CD2 LEU B  33     3254   2653   1940    105    296    152       C  
ATOM   1037  N   GLU B  34       5.919  12.005 -27.890  1.00 16.08           N  
ANISOU 1037  N   GLU B  34     2381   1668   2060   -413    568    -78       N  
ATOM   1038  CA  GLU B  34       6.405  10.797 -28.531  1.00 20.36           C  
ANISOU 1038  CA  GLU B  34     3107   1820   2808    -42    -49   -470       C  
ATOM   1039  C   GLU B  34       5.693  10.583 -29.868  1.00 19.73           C  
ANISOU 1039  C   GLU B  34     3442   1386   2669     59    -28   -305       C  
ATOM   1040  O   GLU B  34       4.511  10.961 -29.952  1.00 24.83           O  
ANISOU 1040  O   GLU B  34     3162   3216   3056    -41   -200   -657       O  
ATOM   1041  CB AGLU B  34       6.026   9.595 -27.646  0.51 26.06           C  
ANISOU 1041  CB AGLU B  34     4998   1720   3185    453   -655    110       C  
ATOM   1042  CB BGLU B  34       6.181   9.560 -27.674  0.49 25.78           C  
ANISOU 1042  CB BGLU B  34     4919   1828   3048    520   -558    -91       C  
ATOM   1043  CG AGLU B  34       4.792   8.887 -28.125  0.51 30.17           C  
ANISOU 1043  CG AGLU B  34     4489   2141   4831   -436    389    708       C  
ATOM   1044  CG BGLU B  34       7.262   8.488 -27.704  0.49 24.78           C  
ANISOU 1044  CG BGLU B  34     4858   2087   2472    554    332   -267       C  
ATOM   1045  CD AGLU B  34       3.373   9.255 -27.816  0.51 34.81           C  
ANISOU 1045  CD AGLU B  34     4814   3921   4490    396    525   1155       C  
ATOM   1046  CD BGLU B  34       7.117   7.673 -26.428  0.49 24.09           C  
ANISOU 1046  CD BGLU B  34     5954    310   2889    171    151   -484       C  
ATOM   1047  OE1AGLU B  34       2.926   8.791 -26.720  0.51 43.73           O  
ANISOU 1047  OE1AGLU B  34     5842   6570   4202   2764   1233   1953       O  
ATOM   1048  OE1BGLU B  34       5.983   7.347 -26.047  0.49 26.76           O  
ANISOU 1048  OE1BGLU B  34     5854   2742   1572     -6   -246    -52       O  
ATOM   1049  OE2AGLU B  34       2.606   9.910 -28.580  0.51 21.97           O  
ANISOU 1049  OE2AGLU B  34     4268   2070   2008   -689    -86   -990       O  
ATOM   1050  OE2BGLU B  34       8.119   7.379 -25.772  0.49 30.39           O  
ANISOU 1050  OE2BGLU B  34     5775   2564   3206  -1059      7   1136       O  
ATOM   1051  N   GLU B  35       6.297   9.997 -30.852  1.00 23.42           N  
ANISOU 1051  N   GLU B  35     4188   1826   2886    261    124   -628       N  
ATOM   1052  CA  GLU B  35       5.658   9.505 -32.065  1.00 24.59           C  
ANISOU 1052  CA  GLU B  35     4453   2522   2370    -35    122   -173       C  
ATOM   1053  C   GLU B  35       4.806  10.571 -32.758  1.00 25.88           C  
ANISOU 1053  C   GLU B  35     3849   2847   3137     37    228     29       C  
ATOM   1054  O   GLU B  35       3.601  10.459 -33.042  1.00 28.88           O  
ANISOU 1054  O   GLU B  35     4246   2813   3916   -637   -456    170       O  
ATOM   1055  CB AGLU B  35       4.851   8.231 -31.853  0.52 26.86           C  
ANISOU 1055  CB AGLU B  35     3871   2834   3500   -240   -879     41       C  
ATOM   1056  CB BGLU B  35       4.775   8.290 -31.725  0.48 25.88           C  
ANISOU 1056  CB BGLU B  35     3601   2795   3436    -81   -654     21       C  
ATOM   1057  CG AGLU B  35       3.548   8.264 -31.113  0.52 30.01           C  
ANISOU 1057  CG AGLU B  35     3650   3691   4063   -907   -918   -379       C  
ATOM   1058  CG BGLU B  35       5.505   7.194 -30.976  0.48 25.10           C  
ANISOU 1058  CG BGLU B  35     4254   2061   3222    162   -337   -358       C  
ATOM   1059  CD AGLU B  35       2.820   6.930 -31.073  0.52 35.65           C  
ANISOU 1059  CD AGLU B  35     4396   4139   5010  -1519   -923   -540       C  
ATOM   1060  CD BGLU B  35       4.703   6.024 -30.464  0.48 27.66           C  
ANISOU 1060  CD BGLU B  35     5089   1866   3557   -405   -585   -807       C  
ATOM   1061  OE1AGLU B  35       3.472   5.865 -31.120  0.52 42.89           O  
ANISOU 1061  OE1AGLU B  35     6709   3683   5905  -1154  -1213   -548       O  
ATOM   1062  OE1BGLU B  35       5.311   4.929 -30.341  0.48 31.92           O  
ANISOU 1062  OE1BGLU B  35     6614   2107   3409     72   -996   -173       O  
ATOM   1063  OE2AGLU B  35       1.575   6.955 -30.991  0.52 40.39           O  
ANISOU 1063  OE2AGLU B  35     4651   6643   4053  -2606    982  -2218       O  
ATOM   1064  OE2BGLU B  35       3.494   6.138 -30.158  0.48 34.83           O  
ANISOU 1064  OE2BGLU B  35     4662   3112   5459  -1032   -812    119       O  
ATOM   1065  N   VAL B  36       5.524  11.644 -33.065  1.00 22.10           N  
ANISOU 1065  N   VAL B  36     3273   2758   2365    178   -249    -48       N  
ATOM   1066  CA  VAL B  36       5.025  12.682 -33.953  1.00 23.76           C  
ANISOU 1066  CA  VAL B  36     3302   3007   2718    138   -374    183       C  
ATOM   1067  C   VAL B  36       6.137  12.984 -34.947  1.00 21.04           C  
ANISOU 1067  C   VAL B  36     2920   2264   2810   -413   -690     48       C  
ATOM   1068  O   VAL B  36       7.342  12.973 -34.677  1.00 25.56           O  
ANISOU 1068  O   VAL B  36     2900   3553   3259    686   -636   -594       O  
ATOM   1069  CB  VAL B  36       4.593  13.939 -33.193  1.00 25.87           C  
ANISOU 1069  CB  VAL B  36     3459   2771   3601    221   -182    213       C  
ATOM   1070  CG1 VAL B  36       5.820  14.567 -32.582  1.00 29.29           C  
ANISOU 1070  CG1 VAL B  36     3746   3126   4257   -228     37   -462       C  
ATOM   1071  CG2 VAL B  36       3.876  14.937 -34.083  1.00 35.92           C  
ANISOU 1071  CG2 VAL B  36     6061   3656   3930   1432   -800    179       C  
ATOM   1072  N   ASN B  37       5.736  13.252 -36.182  1.00 20.90           N  
ANISOU 1072  N   ASN B  37     3023   2098   2819   -192   -548    223       N  
ATOM   1073  CA  ASN B  37       6.757  13.591 -37.176  1.00 21.67           C  
ANISOU 1073  CA  ASN B  37     3611   1737   2887   -402   -103   -328       C  
ATOM   1074  C   ASN B  37       6.534  15.059 -37.560  1.00 23.37           C  
ANISOU 1074  C   ASN B  37     3139   2235   3508   -642   -942    505       C  
ATOM   1075  O   ASN B  37       5.480  15.452 -38.061  1.00 24.49           O  
ANISOU 1075  O   ASN B  37     2866   2665   3773   -480   -709    245       O  
ATOM   1076  CB  ASN B  37       6.751  12.674 -38.390  1.00 35.66           C  
ANISOU 1076  CB  ASN B  37     7135   3541   2873    -97   -214  -1016       C  
ATOM   1077  CG  ASN B  37       7.973  12.799 -39.284  1.00 47.82           C  
ANISOU 1077  CG  ASN B  37     8131   5700   4340     87   1214  -2654       C  
ATOM   1078  OD1 ASN B  37       8.821  13.709 -39.200  1.00 55.22           O  
ANISOU 1078  OD1 ASN B  37     8100   5426   7454   -106   2546  -1257       O  
ATOM   1079  ND2 ASN B  37       8.120  11.852 -40.215  1.00 74.15           N  
ANISOU 1079  ND2 ASN B  37    13532   7176   7465   1089   3084  -4538       N  
ATOM   1080  N   LEU B  38       7.566  15.848 -37.275  1.00 16.69           N  
ANISOU 1080  N   LEU B  38     2584   1974   1781   -421     96    129       N  
ATOM   1081  CA  LEU B  38       7.542  17.274 -37.571  1.00 16.49           C  
ANISOU 1081  CA  LEU B  38     2746   1893   1625   -156    350    -92       C  
ATOM   1082  C   LEU B  38       8.563  17.549 -38.671  1.00 15.41           C  
ANISOU 1082  C   LEU B  38     2594   1436   1826    234    437     36       C  
ATOM   1083  O   LEU B  38       9.640  16.957 -38.670  1.00 16.28           O  
ANISOU 1083  O   LEU B  38     2481   1792   1913    221     70     13       O  
ATOM   1084  CB  LEU B  38       7.872  18.145 -36.350  1.00 15.52           C  
ANISOU 1084  CB  LEU B  38     2123   2151   1623    -82    153    -97       C  
ATOM   1085  CG  LEU B  38       6.882  17.946 -35.185  1.00 14.26           C  
ANISOU 1085  CG  LEU B  38     1863   1878   1677     59    159   -267       C  
ATOM   1086  CD1 LEU B  38       7.382  18.723 -33.958  1.00 15.54           C  
ANISOU 1086  CD1 LEU B  38     2385   1936   1584    -71    -89   -118       C  
ATOM   1087  CD2 LEU B  38       5.490  18.379 -35.595  1.00 19.56           C  
ANISOU 1087  CD2 LEU B  38     1868   3593   1972    -73    -95    137       C  
ATOM   1088  N   PRO B  39       8.216  18.452 -39.569  1.00 15.38           N  
ANISOU 1088  N   PRO B  39     2363   1695   1786     14    179    124       N  
ATOM   1089  CA  PRO B  39       9.136  18.780 -40.653  1.00 15.15           C  
ANISOU 1089  CA  PRO B  39     2257   1992   1506     38     25     50       C  
ATOM   1090  C   PRO B  39      10.246  19.757 -40.299  1.00 15.39           C  
ANISOU 1090  C   PRO B  39     2434   1792   1621    -44    248     20       C  
ATOM   1091  O   PRO B  39      10.133  20.545 -39.358  1.00 15.29           O  
ANISOU 1091  O   PRO B  39     2623   1874   1314    133   -127     59       O  
ATOM   1092  CB  PRO B  39       8.183  19.504 -41.650  1.00 17.16           C  
ANISOU 1092  CB  PRO B  39     2817   2186   1515    390    -88     -7       C  
ATOM   1093  CG  PRO B  39       7.163  20.130 -40.774  1.00 17.49           C  
ANISOU 1093  CG  PRO B  39     2120   2678   1848    203    125    480       C  
ATOM   1094  CD  PRO B  39       6.911  19.149 -39.640  1.00 16.18           C  
ANISOU 1094  CD  PRO B  39     2356   1725   2067    103    189    164       C  
ATOM   1095  N   GLY B  40      11.320  19.709 -41.115  1.00 15.69           N  
ANISOU 1095  N   GLY B  40     2392   2091   1477   -102    157    185       N  
ATOM   1096  CA  GLY B  40      12.338  20.710 -41.060  1.00 16.51           C  
ANISOU 1096  CA  GLY B  40     2400   2442   1432   -298     -3    200       C  
ATOM   1097  C   GLY B  40      13.445  20.514 -40.067  1.00 14.87           C  
ANISOU 1097  C   GLY B  40     2513   1862   1274     55     66     84       C  
ATOM   1098  O   GLY B  40      13.661  19.427 -39.517  1.00 17.51           O  
ANISOU 1098  O   GLY B  40     3008   1969   1676    333    324    172       O  
ATOM   1099  N   ARG B  41      14.190  21.587 -39.840  1.00 15.20           N  
ANISOU 1099  N   ARG B  41     2227   2174   1375     -8    -26     29       N  
ATOM   1100  CA  ARG B  41      15.378  21.601 -39.009  1.00 16.38           C  
ANISOU 1100  CA  ARG B  41     2258   2785   1181     -7    -22    443       C  
ATOM   1101  C   ARG B  41      15.041  21.387 -37.522  1.00 14.59           C  
ANISOU 1101  C   ARG B  41     2123   2188   1234    374    143    154       C  
ATOM   1102  O   ARG B  41      14.012  21.842 -37.023  1.00 14.88           O  
ANISOU 1102  O   ARG B  41     1989   2015   1651    140    233    174       O  
ATOM   1103  CB AARG B  41      16.189  22.887 -39.162  0.53 20.20           C  
ANISOU 1103  CB AARG B  41     2115   3669   1892   -655    101    480       C  
ATOM   1104  CB BARG B  41      16.091  22.949 -39.145  0.47 20.17           C  
ANISOU 1104  CB BARG B  41     2396   3550   1718   -748   -329    676       C  
ATOM   1105  CG AARG B  41      15.595  24.099 -38.475  0.53 24.38           C  
ANISOU 1105  CG AARG B  41     3808   3069   2387   -992     -9    148       C  
ATOM   1106  CG BARG B  41      17.353  23.160 -38.338  0.47 22.95           C  
ANISOU 1106  CG BARG B  41     2513   4417   1790   -704   -488    604       C  
ATOM   1107  CD AARG B  41      16.665  25.156 -38.237  0.53 27.17           C  
ANISOU 1107  CD AARG B  41     3231   4307   2785  -1336    514   -233       C  
ATOM   1108  CD BARG B  41      18.465  23.739 -39.190  0.47 28.81           C  
ANISOU 1108  CD BARG B  41     2733   5084   3129  -1483   -247    599       C  
ATOM   1109  NE AARG B  41      17.064  25.757 -39.526  0.53 31.07           N  
ANISOU 1109  NE AARG B  41     2833   5348   3625  -1268    349   1030       N  
ATOM   1110  NE BARG B  41      18.183  24.991 -39.881  0.47 31.87           N  
ANISOU 1110  NE BARG B  41     3710   4972   3427  -1673    371    830       N  
ATOM   1111  CZ AARG B  41      17.287  27.055 -39.653  0.53 29.69           C  
ANISOU 1111  CZ AARG B  41     2540   5115   3627   -634    201    959       C  
ATOM   1112  CZ BARG B  41      18.624  25.328 -41.091  0.47 34.46           C  
ANISOU 1112  CZ BARG B  41     4667   5507   2919  -1185    183    644       C  
ATOM   1113  NH1AARG B  41      17.151  27.847 -38.596  0.53 28.15           N  
ANISOU 1113  NH1AARG B  41     1892   5345   3459   -355    157   1000       N  
ATOM   1114  NH1BARG B  41      19.391  24.532 -41.830  0.47 29.67           N  
ANISOU 1114  NH1BARG B  41     2956   5880   2436  -1436   -908    202       N  
ATOM   1115  NH2AARG B  41      17.646  27.600 -40.808  0.53 31.83           N  
ANISOU 1115  NH2AARG B  41     4489   4467   3137   -620   -375    858       N  
ATOM   1116  NH2BARG B  41      18.312  26.501 -41.619  0.47 36.10           N  
ANISOU 1116  NH2BARG B  41     5819   6004   1892   -533   -334    531       N  
ATOM   1117  N   TRP B  42      15.952  20.716 -36.858  1.00 14.02           N  
ANISOU 1117  N   TRP B  42     2083   1998   1245    199    212    419       N  
ATOM   1118  CA  TRP B  42      15.855  20.513 -35.403  1.00 13.14           C  
ANISOU 1118  CA  TRP B  42     1852   1965   1177   -125    197    253       C  
ATOM   1119  C   TRP B  42      17.265  20.530 -34.862  1.00 13.85           C  
ANISOU 1119  C   TRP B  42     1839   2144   1279    -60    207    207       C  
ATOM   1120  O   TRP B  42      18.274  20.473 -35.582  1.00 15.65           O  
ANISOU 1120  O   TRP B  42     1880   2424   1643    116    384    374       O  
ATOM   1121  CB  TRP B  42      15.131  19.187 -35.067  1.00 15.30           C  
ANISOU 1121  CB  TRP B  42     2328   1989   1495   -367    240    315       C  
ATOM   1122  CG  TRP B  42      15.706  18.038 -35.838  1.00 18.07           C  
ANISOU 1122  CG  TRP B  42     2854   1951   2060    -86    148    365       C  
ATOM   1123  CD1 TRP B  42      15.250  17.567 -37.065  1.00 18.18           C  
ANISOU 1123  CD1 TRP B  42     2610   2006   2290     76    423   -184       C  
ATOM   1124  CD2 TRP B  42      16.804  17.229 -35.488  1.00 19.91           C  
ANISOU 1124  CD2 TRP B  42     2689   2093   2783   -121    224    480       C  
ATOM   1125  NE1 TRP B  42      16.012  16.526 -37.469  1.00 20.06           N  
ANISOU 1125  NE1 TRP B  42     2976   1843   2804    379    266    192       N  
ATOM   1126  CE2 TRP B  42      16.971  16.292 -36.520  1.00 19.76           C  
ANISOU 1126  CE2 TRP B  42     2811   2349   2349    184    648    736       C  
ATOM   1127  CE3 TRP B  42      17.664  17.206 -34.385  1.00 19.88           C  
ANISOU 1127  CE3 TRP B  42     2588   2296   2669    253    317    687       C  
ATOM   1128  CZ2 TRP B  42      17.961  15.306 -36.540  1.00 21.42           C  
ANISOU 1128  CZ2 TRP B  42     2714   2713   2712    334    298    495       C  
ATOM   1129  CZ3 TRP B  42      18.664  16.224 -34.391  1.00 20.26           C  
ANISOU 1129  CZ3 TRP B  42     2363   2611   2725    296    730    278       C  
ATOM   1130  CH2 TRP B  42      18.803  15.302 -35.442  1.00 22.75           C  
ANISOU 1130  CH2 TRP B  42     3288   2619   2737    433     21    196       C  
ATOM   1131  N   LYS B  43      17.371  20.579 -33.529  1.00 16.06           N  
ANISOU 1131  N   LYS B  43     2155   2660   1289   -113     36    364       N  
ATOM   1132  CA  LYS B  43      18.707  20.324 -32.958  1.00 18.76           C  
ANISOU 1132  CA  LYS B  43     2296   2882   1952   -619   -420    866       C  
ATOM   1133  C   LYS B  43      18.548  19.388 -31.766  1.00 19.15           C  
ANISOU 1133  C   LYS B  43     2314   3030   1931    716    525    916       C  
ATOM   1134  O   LYS B  43      17.467  19.370 -31.119  1.00 15.42           O  
ANISOU 1134  O   LYS B  43     1872   2144   1842    117    142    198       O  
ATOM   1135  CB  LYS B  43      19.395  21.585 -32.524  1.00 21.43           C  
ANISOU 1135  CB  LYS B  43     2793   2902   2446   -365   -441     93       C  
ATOM   1136  CG  LYS B  43      18.669  22.405 -31.477  1.00 21.99           C  
ANISOU 1136  CG  LYS B  43     2864   2512   2979    -18    404    819       C  
ATOM   1137  CD  LYS B  43      19.340  23.803 -31.396  1.00 37.55           C  
ANISOU 1137  CD  LYS B  43     5257   2985   6027   -817   -625   -916       C  
ATOM   1138  CE  LYS B  43      18.408  24.786 -30.712  1.00 45.69           C  
ANISOU 1138  CE  LYS B  43     7047   3244   7070   -369    238  -1206       C  
ATOM   1139  NZ  LYS B  43      18.869  26.188 -30.549  1.00 57.76           N  
ANISOU 1139  NZ  LYS B  43     8553   3931   9463  -1004   -254  -3006       N  
ATOM   1140  N   PRO B  44      19.572  18.595 -31.474  1.00 18.01           N  
ANISOU 1140  N   PRO B  44     1900   3108   1834    434    231    560       N  
ATOM   1141  CA  PRO B  44      19.462  17.712 -30.311  1.00 16.88           C  
ANISOU 1141  CA  PRO B  44     2167   2724   1523    882     97    252       C  
ATOM   1142  C   PRO B  44      19.400  18.566 -29.036  1.00 17.26           C  
ANISOU 1142  C   PRO B  44     2233   2586   1738   -137    107    169       C  
ATOM   1143  O   PRO B  44      19.942  19.647 -28.920  1.00 20.77           O  
ANISOU 1143  O   PRO B  44     2886   3096   1910   -858   -207    452       O  
ATOM   1144  CB  PRO B  44      20.734  16.854 -30.385  1.00 21.07           C  
ANISOU 1144  CB  PRO B  44     1915   3730   2360   1019    273    585       C  
ATOM   1145  CG  PRO B  44      21.705  17.708 -31.156  1.00 24.25           C  
ANISOU 1145  CG  PRO B  44     1915   4394   2903    589      0    973       C  
ATOM   1146  CD  PRO B  44      20.850  18.412 -32.190  1.00 22.62           C  
ANISOU 1146  CD  PRO B  44     2118   4402   2073    850    398    701       C  
ATOM   1147  N   LYS B  45      18.727  18.028 -28.027  1.00 15.70           N  
ANISOU 1147  N   LYS B  45     2129   2587   1248   -312   -231     96       N  
ATOM   1148  CA  LYS B  45      18.610  18.600 -26.692  1.00 14.57           C  
ANISOU 1148  CA  LYS B  45     2428   1717   1390   -266   -401     81       C  
ATOM   1149  C   LYS B  45      18.729  17.470 -25.689  1.00 14.09           C  
ANISOU 1149  C   LYS B  45     1974   2073   1305   -552   -250    292       C  
ATOM   1150  O   LYS B  45      18.170  16.399 -25.877  1.00 15.38           O  
ANISOU 1150  O   LYS B  45     2558   1719   1567   -232   -454    171       O  
ATOM   1151  CB ALYS B  45      17.269  19.312 -26.530  0.64 18.04           C  
ANISOU 1151  CB ALYS B  45     2786   1694   2373     -9    -84    -68       C  
ATOM   1152  CB BLYS B  45      17.291  19.348 -26.495  0.36 18.71           C  
ANISOU 1152  CB BLYS B  45     2873   1953   2284    108    -60    -18       C  
ATOM   1153  CG ALYS B  45      17.181  20.125 -25.242  0.64 21.87           C  
ANISOU 1153  CG ALYS B  45     3395   2677   2236    284    250   -165       C  
ATOM   1154  CG BLYS B  45      17.270  20.230 -25.249  0.36 21.43           C  
ANISOU 1154  CG BLYS B  45     3325   2484   2335    266    124   -202       C  
ATOM   1155  CD ALYS B  45      15.865  20.873 -25.125  0.64 23.25           C  
ANISOU 1155  CD ALYS B  45     3509   2691   2635    362    530   -114       C  
ATOM   1156  CD BLYS B  45      15.875  20.715 -24.900  0.36 22.64           C  
ANISOU 1156  CD BLYS B  45     3471   2680   2451    316    569    137       C  
ATOM   1157  CE ALYS B  45      15.661  21.381 -23.712  0.64 22.05           C  
ANISOU 1157  CE ALYS B  45     3656   2148   2574     12    933    200       C  
ATOM   1158  CE BLYS B  45      15.896  22.084 -24.248  0.36 24.14           C  
ANISOU 1158  CE BLYS B  45     3223   3141   2807    181    972   -405       C  
ATOM   1159  NZ ALYS B  45      16.623  22.465 -23.371  0.64 27.28           N  
ANISOU 1159  NZ ALYS B  45     2581   3129   4655    533    453  -1351       N  
ATOM   1160  NZ BLYS B  45      15.072  22.158 -23.011  0.36 22.68           N  
ANISOU 1160  NZ BLYS B  45     2494   3502   2621   1237    589    270       N  
ATOM   1161  N   LEU B  46      19.469  17.708 -24.616  1.00 14.98           N  
ANISOU 1161  N   LEU B  46     2193   2303   1197   -119   -293     -4       N  
ATOM   1162  CA  LEU B  46      19.510  16.743 -23.522  1.00 14.22           C  
ANISOU 1162  CA  LEU B  46     1862   2301   1238     28   -135     80       C  
ATOM   1163  C   LEU B  46      18.534  17.162 -22.435  1.00 14.50           C  
ANISOU 1163  C   LEU B  46     2403   1529   1577    -12    163    -32       C  
ATOM   1164  O   LEU B  46      18.601  18.327 -22.029  1.00 20.73           O  
ANISOU 1164  O   LEU B  46     3850   1767   2259   -422    300   -497       O  
ATOM   1165  CB  LEU B  46      20.927  16.658 -22.930  1.00 17.38           C  
ANISOU 1165  CB  LEU B  46     1939   2541   2124   -139   -471    392       C  
ATOM   1166  CG  LEU B  46      21.974  16.049 -23.881  1.00 20.56           C  
ANISOU 1166  CG  LEU B  46     1847   3002   2964    120   -244    351       C  
ATOM   1167  CD1 LEU B  46      23.378  16.186 -23.298  1.00 25.56           C  
ANISOU 1167  CD1 LEU B  46     1902   4060   3750    -13   -455     59       C  
ATOM   1168  CD2 LEU B  46      21.663  14.600 -24.199  1.00 20.44           C  
ANISOU 1168  CD2 LEU B  46     2947   3101   1717    -17   -222    144       C  
ATOM   1169  N   ILE B  47      17.683  16.259 -22.007  1.00 12.93           N  
ANISOU 1169  N   ILE B  47     1911   1714   1286     87    -20    120       N  
ATOM   1170  CA  ILE B  47      16.748  16.534 -20.926  1.00 13.58           C  
ANISOU 1170  CA  ILE B  47     2137   1942   1080    235    -53      7       C  
ATOM   1171  C   ILE B  47      16.899  15.491 -19.823  1.00 14.13           C  
ANISOU 1171  C   ILE B  47     1928   1984   1455    107    145    210       C  
ATOM   1172  O   ILE B  47      17.603  14.487 -19.961  1.00 15.82           O  
ANISOU 1172  O   ILE B  47     2789   1928   1291    376   -279    -49       O  
ATOM   1173  CB  ILE B  47      15.301  16.554 -21.432  1.00 16.03           C  
ANISOU 1173  CB  ILE B  47     1921   2439   1730    261    111    368       C  
ATOM   1174  CG1 ILE B  47      14.795  15.239 -22.028  1.00 17.98           C  
ANISOU 1174  CG1 ILE B  47     1940   3054   1837     92   -341     -4       C  
ATOM   1175  CG2 ILE B  47      15.083  17.656 -22.460  1.00 21.02           C  
ANISOU 1175  CG2 ILE B  47     2765   3041   2180   1012   -214    627       C  
ATOM   1176  CD1 ILE B  47      13.341  15.320 -22.435  1.00 21.82           C  
ANISOU 1176  CD1 ILE B  47     1906   4866   1519    200   -133   -516       C  
ATOM   1177  N   GLY B  48      16.201  15.760 -18.702  1.00 16.36           N  
ANISOU 1177  N   GLY B  48     2361   2643   1212    241    144    287       N  
ATOM   1178  CA  GLY B  48      16.334  14.792 -17.591  1.00 16.21           C  
ANISOU 1178  CA  GLY B  48     2426   2629   1105    394   -346    193       C  
ATOM   1179  C   GLY B  48      17.595  15.128 -16.804  1.00 16.57           C  
ANISOU 1179  C   GLY B  48     2213   2404   1677    144   -193     77       C  
ATOM   1180  O   GLY B  48      17.804  16.286 -16.437  1.00 20.97           O  
ANISOU 1180  O   GLY B  48     2903   2459   2606     40   -467    -31       O  
ATOM   1181  N   GLY B  49      18.407  14.120 -16.560  1.00 16.23           N  
ANISOU 1181  N   GLY B  49     2222   2620   1324    269   -353    -91       N  
ATOM   1182  CA  GLY B  49      19.665  14.301 -15.928  1.00 15.97           C  
ANISOU 1182  CA  GLY B  49     1935   2546   1587   -254    -52    494       C  
ATOM   1183  C   GLY B  49      19.857  13.406 -14.711  1.00 16.84           C  
ANISOU 1183  C   GLY B  49     2279   2818   1301     85   -199    393       C  
ATOM   1184  O   GLY B  49      21.014  13.082 -14.480  1.00 17.16           O  
ANISOU 1184  O   GLY B  49     2263   2857   1399    -81   -241    204       O  
ATOM   1185  N   ILE B  50      18.800  13.031 -14.008  1.00 15.03           N  
ANISOU 1185  N   ILE B  50     2364   2219   1128    396    -40    342       N  
ATOM   1186  CA  ILE B  50      18.995  12.167 -12.841  1.00 16.89           C  
ANISOU 1186  CA  ILE B  50     2573   2598   1247    591    -38    486       C  
ATOM   1187  C   ILE B  50      19.271  10.748 -13.312  1.00 15.25           C  
ANISOU 1187  C   ILE B  50     1902   2142   1750   -137   -307    639       C  
ATOM   1188  O   ILE B  50      18.363  10.104 -13.849  1.00 19.87           O  
ANISOU 1188  O   ILE B  50     2109   3316   2127   -317   -677    355       O  
ATOM   1189  CB  ILE B  50      17.830  12.228 -11.836  1.00 17.54           C  
ANISOU 1189  CB  ILE B  50     2351   2830   1483    126     -8    752       C  
ATOM   1190  CG1 ILE B  50      17.644  13.638 -11.284  1.00 20.32           C  
ANISOU 1190  CG1 ILE B  50     2449   3542   1729    253    229   -158       C  
ATOM   1191  CG2 ILE B  50      18.044  11.217 -10.714  1.00 24.65           C  
ANISOU 1191  CG2 ILE B  50     3337   4321   1708    235   -130   1498       C  
ATOM   1192  CD1 ILE B  50      16.438  13.894 -10.431  1.00 23.14           C  
ANISOU 1192  CD1 ILE B  50     2604   4014   2173   -106    576    -98       C  
ATOM   1193  N   GLY B  51      20.500  10.275 -13.088  1.00 13.66           N  
ANISOU 1193  N   GLY B  51     1836   2205   1149     15   -113    116       N  
ATOM   1194  CA  GLY B  51      20.963   9.002 -13.604  1.00 15.61           C  
ANISOU 1194  CA  GLY B  51     2649   2028   1255      7   -176     77       C  
ATOM   1195  C   GLY B  51      21.528   9.073 -15.013  1.00 14.78           C  
ANISOU 1195  C   GLY B  51     2440   1947   1229    128   -293    -58       C  
ATOM   1196  O   GLY B  51      21.925   8.027 -15.599  1.00 15.70           O  
ANISOU 1196  O   GLY B  51     2308   2093   1564    248   -389   -223       O  
ATOM   1197  N   GLY B  52      21.524  10.301 -15.566  1.00 14.90           N  
ANISOU 1197  N   GLY B  52     2497   2039   1125    -32   -303     81       N  
ATOM   1198  CA  GLY B  52      21.970  10.479 -16.944  1.00 16.78           C  
ANISOU 1198  CA  GLY B  52     2490   2693   1193    540   -217    225       C  
ATOM   1199  C   GLY B  52      20.909  11.283 -17.691  1.00 14.40           C  
ANISOU 1199  C   GLY B  52     2023   2136   1312     37   -316    187       C  
ATOM   1200  O   GLY B  52      19.818  11.567 -17.178  1.00 17.71           O  
ANISOU 1200  O   GLY B  52     2006   3102   1622    143   -202    305       O  
ATOM   1201  N   PHE B  53      21.230  11.661 -18.897  1.00 14.15           N  
ANISOU 1201  N   PHE B  53     2527   1774   1074    145   -358   -121       N  
ATOM   1202  CA  PHE B  53      20.355  12.502 -19.707  1.00 13.95           C  
ANISOU 1202  CA  PHE B  53     2299   1696   1304    -49   -451     47       C  
ATOM   1203  C   PHE B  53      19.720  11.701 -20.850  1.00 14.11           C  
ANISOU 1203  C   PHE B  53     2149   1935   1278    130   -281   -242       C  
ATOM   1204  O   PHE B  53      20.279  10.660 -21.224  1.00 16.56           O  
ANISOU 1204  O   PHE B  53     3238   1843   1211    549   -330    -47       O  
ATOM   1205  CB  PHE B  53      21.118  13.694 -20.311  1.00 15.65           C  
ANISOU 1205  CB  PHE B  53     2486   1764   1695    -88   -155     71       C  
ATOM   1206  CG  PHE B  53      21.498  14.712 -19.244  1.00 16.92           C  
ANISOU 1206  CG  PHE B  53     2704   1873   1852   -423    -40     48       C  
ATOM   1207  CD1 PHE B  53      20.734  15.847 -19.037  1.00 17.86           C  
ANISOU 1207  CD1 PHE B  53     3512   1633   1642   -325    124    118       C  
ATOM   1208  CD2 PHE B  53      22.623  14.489 -18.469  1.00 19.36           C  
ANISOU 1208  CD2 PHE B  53     2339   3163   1855   -474     66   -316       C  
ATOM   1209  CE1 PHE B  53      21.104  16.784 -18.069  1.00 19.02           C  
ANISOU 1209  CE1 PHE B  53     3030   2158   2037   -340    -54   -226       C  
ATOM   1210  CE2 PHE B  53      23.021  15.419 -17.517  1.00 20.21           C  
ANISOU 1210  CE2 PHE B  53     2657   2793   2228   -373   -158   -280       C  
ATOM   1211  CZ  PHE B  53      22.261  16.556 -17.319  1.00 19.82           C  
ANISOU 1211  CZ  PHE B  53     2704   2486   2342   -513    116    134       C  
ATOM   1212  N   VAL B  54      18.582  12.192 -21.339  1.00 14.05           N  
ANISOU 1212  N   VAL B  54     2298   2074    967    263   -311   -280       N  
ATOM   1213  CA  VAL B  54      17.903  11.632 -22.510  1.00 13.73           C  
ANISOU 1213  CA  VAL B  54     2662   1550   1003     87   -447    -54       C  
ATOM   1214  C   VAL B  54      18.059  12.632 -23.646  1.00 13.19           C  
ANISOU 1214  C   VAL B  54     2299   1551   1160    227   -382     32       C  
ATOM   1215  O   VAL B  54      17.829  13.832 -23.419  1.00 14.73           O  
ANISOU 1215  O   VAL B  54     2718   1551   1326    173   -287     16       O  
ATOM   1216  CB  VAL B  54      16.419  11.350 -22.266  1.00 16.79           C  
ANISOU 1216  CB  VAL B  54     2804   1995   1582   -423   -723    564       C  
ATOM   1217  CG1 VAL B  54      15.632  11.033 -23.539  1.00 16.73           C  
ANISOU 1217  CG1 VAL B  54     2828   1838   1691   -230   -694    217       C  
ATOM   1218  CG2 VAL B  54      16.344  10.151 -21.298  1.00 22.52           C  
ANISOU 1218  CG2 VAL B  54     3651   2661   2246   -673   -878   1246       C  
ATOM   1219  N   LYS B  55      18.398  12.177 -24.827  1.00 12.97           N  
ANISOU 1219  N   LYS B  55     2242   1607   1080    100   -385     56       N  
ATOM   1220  CA  LYS B  55      18.502  13.038 -25.995  1.00 12.93           C  
ANISOU 1220  CA  LYS B  55     1942   1665   1306    175   -192    202       C  
ATOM   1221  C   LYS B  55      17.197  13.034 -26.772  1.00 13.37           C  
ANISOU 1221  C   LYS B  55     2088   1616   1375    -56   -366    417       C  
ATOM   1222  O   LYS B  55      16.613  11.976 -27.045  1.00 15.33           O  
ANISOU 1222  O   LYS B  55     2690   1702   1434    -63   -408   -181       O  
ATOM   1223  CB  LYS B  55      19.626  12.545 -26.918  1.00 15.21           C  
ANISOU 1223  CB  LYS B  55     2174   2248   1356     89    -84   -241       C  
ATOM   1224  CG  LYS B  55      19.944  13.540 -28.025  1.00 17.19           C  
ANISOU 1224  CG  LYS B  55     2585   2391   1558    344    390   -107       C  
ATOM   1225  CD  LYS B  55      21.014  12.955 -28.959  1.00 18.63           C  
ANISOU 1225  CD  LYS B  55     2729   2870   1479    514    296   -317       C  
ATOM   1226  CE  LYS B  55      22.247  12.400 -28.232  1.00 18.95           C  
ANISOU 1226  CE  LYS B  55     2484   2352   2364    328    -61   -881       C  
ATOM   1227  NZ  LYS B  55      23.221  11.781 -29.190  1.00 22.28           N  
ANISOU 1227  NZ  LYS B  55     2770   2908   2787    429    637   -478       N  
ATOM   1228  N   VAL B  56      16.732  14.239 -27.083  1.00 12.21           N  
ANISOU 1228  N   VAL B  56     2017   1712    910    160   -250    176       N  
ATOM   1229  CA  VAL B  56      15.502  14.416 -27.874  1.00 12.67           C  
ANISOU 1229  CA  VAL B  56     1981   1927    907    166   -280    147       C  
ATOM   1230  C   VAL B  56      15.793  15.384 -29.005  1.00 11.07           C  
ANISOU 1230  C   VAL B  56     1742   1399   1063    265   -262     -7       C  
ATOM   1231  O   VAL B  56      16.864  16.014 -29.041  1.00 13.67           O  
ANISOU 1231  O   VAL B  56     1961   1890   1342    -66   -237    -65       O  
ATOM   1232  CB  VAL B  56      14.361  14.909 -26.963  1.00 13.18           C  
ANISOU 1232  CB  VAL B  56     2071   1825   1112    246   -180    180       C  
ATOM   1233  CG1 VAL B  56      14.049  13.890 -25.862  1.00 14.62           C  
ANISOU 1233  CG1 VAL B  56     2336   1966   1251    217     24    229       C  
ATOM   1234  CG2 VAL B  56      14.668  16.285 -26.385  1.00 15.38           C  
ANISOU 1234  CG2 VAL B  56     2353   1740   1752    410   -193     15       C  
ATOM   1235  N   ARG B  57      14.833  15.522 -29.910  1.00 11.67           N  
ANISOU 1235  N   ARG B  57     1836   1539   1059    233   -251    267       N  
ATOM   1236  CA  ARG B  57      14.968  16.513 -30.980  1.00 10.89           C  
ANISOU 1236  CA  ARG B  57     1729   1260   1150    169    -76    153       C  
ATOM   1237  C   ARG B  57      14.153  17.758 -30.600  1.00 11.23           C  
ANISOU 1237  C   ARG B  57     1716   1369   1182    154    306    211       C  
ATOM   1238  O   ARG B  57      12.964  17.652 -30.329  1.00 11.58           O  
ANISOU 1238  O   ARG B  57     1714   1522   1164     41    152    -30       O  
ATOM   1239  CB  ARG B  57      14.461  15.963 -32.318  1.00 12.16           C  
ANISOU 1239  CB  ARG B  57     1900   1749    972    340     48     53       C  
ATOM   1240  CG  ARG B  57      15.404  14.886 -32.856  1.00 14.57           C  
ANISOU 1240  CG  ARG B  57     2529   1618   1390    475    275     23       C  
ATOM   1241  CD  ARG B  57      14.959  14.442 -34.239  1.00 15.78           C  
ANISOU 1241  CD  ARG B  57     2556   2142   1298    723    378    -91       C  
ATOM   1242  NE  ARG B  57      13.777  13.612 -34.204  1.00 16.98           N  
ANISOU 1242  NE  ARG B  57     2412   2150   1888    752   -100   -281       N  
ATOM   1243  CZ  ARG B  57      13.146  13.164 -35.300  1.00 21.59           C  
ANISOU 1243  CZ  ARG B  57     3365   2317   2519   1148   -657   -867       C  
ATOM   1244  NH1 ARG B  57      12.071  12.418 -35.181  1.00 29.45           N  
ANISOU 1244  NH1 ARG B  57     3438   2015   5736   1003  -1843  -1046       N  
ATOM   1245  NH2 ARG B  57      13.650  13.501 -36.480  1.00 30.88           N  
ANISOU 1245  NH2 ARG B  57     6337   3461   1934   2371   -500   -543       N  
ATOM   1246  N   GLN B  58      14.798  18.915 -30.632  1.00 11.83           N  
ANISOU 1246  N   GLN B  58     2041   1214   1240     70     73    236       N  
ATOM   1247  CA  GLN B  58      14.100  20.169 -30.371  1.00 11.81           C  
ANISOU 1247  CA  GLN B  58     1779   1445   1263    152    -75    120       C  
ATOM   1248  C   GLN B  58      13.650  20.849 -31.666  1.00 11.02           C  
ANISOU 1248  C   GLN B  58     1530   1514   1142    255    162    167       C  
ATOM   1249  O   GLN B  58      14.491  21.184 -32.520  1.00 12.63           O  
ANISOU 1249  O   GLN B  58     1795   1816   1189   -185    178     40       O  
ATOM   1250  CB  GLN B  58      15.004  21.141 -29.632  1.00 11.32           C  
ANISOU 1250  CB  GLN B  58     1647   1609   1044    -73    269     -7       C  
ATOM   1251  CG  GLN B  58      14.356  22.506 -29.419  1.00 12.56           C  
ANISOU 1251  CG  GLN B  58     1944   1526   1304    -95     38     -9       C  
ATOM   1252  CD  GLN B  58      15.215  23.411 -28.562  1.00 13.79           C  
ANISOU 1252  CD  GLN B  58     2253   1551   1435   -227   -190     53       C  
ATOM   1253  OE1 GLN B  58      15.983  22.976 -27.710  1.00 20.43           O  
ANISOU 1253  OE1 GLN B  58     3305   2320   2138   -229  -1049    220       O  
ATOM   1254  NE2 GLN B  58      15.100  24.704 -28.814  1.00 18.65           N  
ANISOU 1254  NE2 GLN B  58     3240   1467   2381    -55   -267   -148       N  
ATOM   1255  N   TYR B  59      12.364  20.996 -31.816  1.00 11.10           N  
ANISOU 1255  N   TYR B  59     1565   1596   1056    295     53    -94       N  
ATOM   1256  CA  TYR B  59      11.786  21.724 -32.923  1.00 11.61           C  
ANISOU 1256  CA  TYR B  59     1569   1513   1328    185    -20     85       C  
ATOM   1257  C   TYR B  59      11.262  23.062 -32.430  1.00 11.05           C  
ANISOU 1257  C   TYR B  59     1405   1458   1337     17    101     92       C  
ATOM   1258  O   TYR B  59      10.464  23.073 -31.474  1.00 12.82           O  
ANISOU 1258  O   TYR B  59     2055   1532   1284    242    314    142       O  
ATOM   1259  CB  TYR B  59      10.608  20.972 -33.526  1.00 10.91           C  
ANISOU 1259  CB  TYR B  59     1657   1483   1004    101     81     16       C  
ATOM   1260  CG  TYR B  59      11.031  19.707 -34.249  1.00 11.13           C  
ANISOU 1260  CG  TYR B  59     1711   1521    998    255    150     85       C  
ATOM   1261  CD1 TYR B  59      11.210  18.496 -33.575  1.00 11.33           C  
ANISOU 1261  CD1 TYR B  59     1721   1385   1200     92    232     59       C  
ATOM   1262  CD2 TYR B  59      11.271  19.686 -35.627  1.00 11.52           C  
ANISOU 1262  CD2 TYR B  59     1870   1511    995     83     13   -105       C  
ATOM   1263  CE1 TYR B  59      11.595  17.362 -34.269  1.00 12.68           C  
ANISOU 1263  CE1 TYR B  59     1925   1531   1362    328    278     97       C  
ATOM   1264  CE2 TYR B  59      11.661  18.550 -36.299  1.00 12.04           C  
ANISOU 1264  CE2 TYR B  59     1838   1656   1081    399    159    -47       C  
ATOM   1265  CZ  TYR B  59      11.836  17.381 -35.626  1.00 13.41           C  
ANISOU 1265  CZ  TYR B  59     2421   1400   1273    120    230   -134       C  
ATOM   1266  OH  TYR B  59      12.206  16.219 -36.294  1.00 16.66           O  
ANISOU 1266  OH  TYR B  59     2686   1659   1985    357    191   -530       O  
ATOM   1267  N   ASP B  60      11.667  24.144 -33.076  1.00 12.47           N  
ANISOU 1267  N   ASP B  60     2070   1469   1199    148    248    121       N  
ATOM   1268  CA  ASP B  60      11.226  25.451 -32.651  1.00 12.42           C  
ANISOU 1268  CA  ASP B  60     1853   1459   1408    145    225     19       C  
ATOM   1269  C   ASP B  60      10.010  25.969 -33.411  1.00 12.43           C  
ANISOU 1269  C   ASP B  60     1892   1629   1203    116    206    160       C  
ATOM   1270  O   ASP B  60       9.771  25.590 -34.561  1.00 14.13           O  
ANISOU 1270  O   ASP B  60     2471   1685   1212     83    195    204       O  
ATOM   1271  CB  ASP B  60      12.375  26.460 -32.794  1.00 15.23           C  
ANISOU 1271  CB  ASP B  60     2144   1801   1842   -251     -6   -235       C  
ATOM   1272  CG  ASP B  60      13.411  26.178 -31.699  1.00 18.45           C  
ANISOU 1272  CG  ASP B  60     2334   2672   2006   -220   -233   -381       C  
ATOM   1273  OD1 ASP B  60      13.043  25.794 -30.579  1.00 19.76           O  
ANISOU 1273  OD1 ASP B  60     2864   2553   2091    323   -258     45       O  
ATOM   1274  OD2 ASP B  60      14.604  26.349 -31.989  1.00 25.49           O  
ANISOU 1274  OD2 ASP B  60     2220   4364   3101     83   -184    188       O  
ATOM   1275  N   GLN B  61       9.241  26.865 -32.796  1.00 13.15           N  
ANISOU 1275  N   GLN B  61     1997   1455   1546    241    247    244       N  
ATOM   1276  CA  GLN B  61       8.165  27.587 -33.458  1.00 14.07           C  
ANISOU 1276  CA  GLN B  61     2208   1302   1836    113    -10    453       C  
ATOM   1277  C   GLN B  61       7.184  26.657 -34.151  1.00 14.43           C  
ANISOU 1277  C   GLN B  61     2214   1759   1512    -82    165    332       C  
ATOM   1278  O   GLN B  61       6.753  26.912 -35.309  1.00 15.84           O  
ANISOU 1278  O   GLN B  61     2701   1779   1540    394     42     90       O  
ATOM   1279  CB  GLN B  61       8.758  28.587 -34.492  1.00 15.44           C  
ANISOU 1279  CB  GLN B  61     2359   1573   1935     68    120    533       C  
ATOM   1280  CG  GLN B  61       9.574  29.651 -33.762  1.00 17.63           C  
ANISOU 1280  CG  GLN B  61     2774   1345   2578    -60    251    393       C  
ATOM   1281  CD  GLN B  61      10.161  30.722 -34.638  1.00 22.02           C  
ANISOU 1281  CD  GLN B  61     4381   1591   2395   -621    402    322       C  
ATOM   1282  OE1 GLN B  61      10.161  30.614 -35.856  1.00 35.79           O  
ANISOU 1282  OE1 GLN B  61     8837   2307   2455  -1499   1164     -1       O  
ATOM   1283  NE2 GLN B  61      10.625  31.803 -34.041  1.00 24.34           N  
ANISOU 1283  NE2 GLN B  61     4132   2117   3000  -1065    299    135       N  
ATOM   1284  N   VAL B  62       6.796  25.568 -33.503  1.00 13.90           N  
ANISOU 1284  N   VAL B  62     1898   1759   1623   -185    400    153       N  
ATOM   1285  CA  VAL B  62       5.858  24.580 -34.038  1.00 13.05           C  
ANISOU 1285  CA  VAL B  62     1799   1733   1428     17    126    171       C  
ATOM   1286  C   VAL B  62       4.401  25.032 -33.804  1.00 12.78           C  
ANISOU 1286  C   VAL B  62     1846   1735   1275    223    -38     93       C  
ATOM   1287  O   VAL B  62       4.050  25.406 -32.667  1.00 13.16           O  
ANISOU 1287  O   VAL B  62     1951   1709   1342     59     65     -6       O  
ATOM   1288  CB  VAL B  62       6.076  23.211 -33.335  1.00 12.73           C  
ANISOU 1288  CB  VAL B  62     1767   1497   1572    160   -104    -87       C  
ATOM   1289  CG1 VAL B  62       5.155  22.136 -33.960  1.00 13.41           C  
ANISOU 1289  CG1 VAL B  62     1858   1591   1647    153   -131   -137       C  
ATOM   1290  CG2 VAL B  62       7.539  22.791 -33.383  1.00 13.86           C  
ANISOU 1290  CG2 VAL B  62     1706   2013   1550     96    130     46       C  
ATOM   1291  N   PRO B  63       3.558  25.021 -34.821  1.00 15.22           N  
ANISOU 1291  N   PRO B  63     1894   2611   1276    151      3    101       N  
ATOM   1292  CA  PRO B  63       2.139  25.316 -34.633  1.00 16.77           C  
ANISOU 1292  CA  PRO B  63     1815   2933   1624    157    -60    447       C  
ATOM   1293  C   PRO B  63       1.456  24.148 -33.923  1.00 16.14           C  
ANISOU 1293  C   PRO B  63     1736   2666   1730     51   -214    180       C  
ATOM   1294  O   PRO B  63       1.573  22.998 -34.357  1.00 20.29           O  
ANISOU 1294  O   PRO B  63     2771   2968   1972   -387    548   -256       O  
ATOM   1295  CB  PRO B  63       1.588  25.539 -36.046  1.00 18.65           C  
ANISOU 1295  CB  PRO B  63     2010   3404   1672     45   -200    368       C  
ATOM   1296  CG  PRO B  63       2.616  25.047 -37.004  1.00 21.57           C  
ANISOU 1296  CG  PRO B  63     2445   4156   1595    622   -433    -46       C  
ATOM   1297  CD  PRO B  63       3.890  24.774 -36.244  1.00 16.35           C  
ANISOU 1297  CD  PRO B  63     1907   3121   1185   -229    -98    163       C  
ATOM   1298  N   ILE B  64       0.768  24.419 -32.820  1.00 15.25           N  
ANISOU 1298  N   ILE B  64     2031   2093   1673   -286   -114     83       N  
ATOM   1299  CA  ILE B  64       0.085  23.336 -32.105  1.00 16.84           C  
ANISOU 1299  CA  ILE B  64     2395   1872   2133   -121    175    133       C  
ATOM   1300  C   ILE B  64      -1.238  23.947 -31.626  1.00 20.45           C  
ANISOU 1300  C   ILE B  64     2629   2409   2731   -303    706   -165       C  
ATOM   1301  O   ILE B  64      -1.292  25.149 -31.339  1.00 23.52           O  
ANISOU 1301  O   ILE B  64     2621   2600   3716   -137    979   -686       O  
ATOM   1302  CB  ILE B  64       0.998  22.749 -31.003  1.00 20.34           C  
ANISOU 1302  CB  ILE B  64     3508   2056   2164   -502   -600    201       C  
ATOM   1303  CG1 ILE B  64       0.313  21.719 -30.088  1.00 22.00           C  
ANISOU 1303  CG1 ILE B  64     3188   2823   2348   -468   -518    588       C  
ATOM   1304  CG2 ILE B  64       1.686  23.835 -30.192  1.00 26.35           C  
ANISOU 1304  CG2 ILE B  64     4356   2324   3332   -567  -1065   -228       C  
ATOM   1305  CD1 ILE B  64       1.221  20.995 -29.087  1.00 24.12           C  
ANISOU 1305  CD1 ILE B  64     3582   2846   2735    173   -348    722       C  
ATOM   1306  N   GLU B  65      -2.290  23.126 -31.570  1.00 17.07           N  
ANISOU 1306  N   GLU B  65     2283   2455   1750   -108     -5    484       N  
ATOM   1307  CA  GLU B  65      -3.578  23.599 -31.076  1.00 18.85           C  
ANISOU 1307  CA  GLU B  65     2311   2926   1924   -257    -45   -316       C  
ATOM   1308  C   GLU B  65      -3.967  22.842 -29.816  1.00 19.37           C  
ANISOU 1308  C   GLU B  65     2413   2870   2075   -655    247   -491       C  
ATOM   1309  O   GLU B  65      -3.913  21.603 -29.882  1.00 20.46           O  
ANISOU 1309  O   GLU B  65     2949   2873   1954   -403    297   -423       O  
ATOM   1310  CB  GLU B  65      -4.656  23.420 -32.157  1.00 21.94           C  
ANISOU 1310  CB  GLU B  65     2278   3859   2200    -77   -156   -738       C  
ATOM   1311  CG  GLU B  65      -5.854  24.327 -31.981  1.00 27.30           C  
ANISOU 1311  CG  GLU B  65     2894   4736   2742    767   -183     41       C  
ATOM   1312  CD  GLU B  65      -6.860  24.143 -33.099  1.00 35.51           C  
ANISOU 1312  CD  GLU B  65     3259   5771   4464    711  -1241   -240       C  
ATOM   1313  OE1 GLU B  65      -6.474  23.537 -34.126  1.00 40.64           O  
ANISOU 1313  OE1 GLU B  65     4003   6526   4913   -311  -1805  -1659       O  
ATOM   1314  OE2 GLU B  65      -8.017  24.615 -32.919  1.00 49.74           O  
ANISOU 1314  OE2 GLU B  65     2820   9189   6891    868  -1015   -249       O  
ATOM   1315  N   ILE B  66      -4.288  23.581 -28.755  1.00 19.81           N  
ANISOU 1315  N   ILE B  66     2597   2928   2001   -523    248   -469       N  
ATOM   1316  CA  ILE B  66      -4.698  23.007 -27.478  1.00 24.22           C  
ANISOU 1316  CA  ILE B  66     3876   3133   2192  -1135    591   -466       C  
ATOM   1317  C   ILE B  66      -6.060  23.554 -27.062  1.00 27.01           C  
ANISOU 1317  C   ILE B  66     3673   4463   2129  -1248    868    -27       C  
ATOM   1318  O   ILE B  66      -6.222  24.758 -26.872  1.00 27.18           O  
ANISOU 1318  O   ILE B  66     2540   4610   3176   -523    476    134       O  
ATOM   1319  CB  ILE B  66      -3.681  23.312 -26.363  1.00 23.55           C  
ANISOU 1319  CB  ILE B  66     4488   2314   2146    -81    -50     20       C  
ATOM   1320  CG1 ILE B  66      -2.279  22.832 -26.716  1.00 27.16           C  
ANISOU 1320  CG1 ILE B  66     4524   3117   2679    243   -197      7       C  
ATOM   1321  CG2 ILE B  66      -4.155  22.764 -25.019  1.00 29.71           C  
ANISOU 1321  CG2 ILE B  66     5680   3227   2383   -835    266    165       C  
ATOM   1322  CD1 ILE B  66      -1.181  23.405 -25.845  1.00 31.97           C  
ANISOU 1322  CD1 ILE B  66     4925   3864   3358    973  -1377     96       C  
ATOM   1323  N   CYS B  67      -7.018  22.643 -26.953  1.00 33.46           N  
ANISOU 1323  N   CYS B  67     3453   5535   3727  -1824   -480   -315       N  
ATOM   1324  CA  CYS B  67      -8.426  22.976 -26.777  1.00 35.03           C  
ANISOU 1324  CA  CYS B  67     3287   5927   4096  -1718  -1129   -650       C  
ATOM   1325  C   CYS B  67      -8.840  24.184 -27.618  1.00 41.49           C  
ANISOU 1325  C   CYS B  67     3894   6748   5123  -1366  -1052    182       C  
ATOM   1326  O   CYS B  67      -9.379  25.135 -27.048  1.00 47.31           O  
ANISOU 1326  O   CYS B  67     3555   8174   6245    578     -3   1169       O  
ATOM   1327  CB  CYS B  67      -8.756  23.263 -25.315  1.00 35.05           C  
ANISOU 1327  CB  CYS B  67     3426   5485   4407     25  -1121  -1041       C  
ATOM   1328  SG  CYS B  67      -8.276  21.950 -24.219  1.00 41.51           S  
ANISOU 1328  SG  CYS B  67     5633   5618   4520   -265    742     76       S  
ATOM   1329  N   GLY B  68      -8.555  24.138 -28.916  1.00 42.44           N  
ANISOU 1329  N   GLY B  68     3955   7176   4995  -1910  -1193    524       N  
ATOM   1330  CA  GLY B  68      -8.998  25.183 -29.821  1.00 42.98           C  
ANISOU 1330  CA  GLY B  68     3595   7603   5132  -1149  -1422    313       C  
ATOM   1331  C   GLY B  68      -8.184  26.449 -29.743  1.00 37.35           C  
ANISOU 1331  C   GLY B  68     2938   7122   4131   -652   -707    757       C  
ATOM   1332  O   GLY B  68      -8.526  27.459 -30.357  1.00 40.36           O  
ANISOU 1332  O   GLY B  68     2894   7526   4915    116   -552    937       O  
ATOM   1333  N   HIS B  69      -7.094  26.414 -28.969  1.00 31.14           N  
ANISOU 1333  N   HIS B  69     2339   6037   3456   -295    -70    131       N  
ATOM   1334  CA  HIS B  69      -6.200  27.539 -28.917  1.00 26.29           C  
ANISOU 1334  CA  HIS B  69     2246   4761   2981    527     47     28       C  
ATOM   1335  C   HIS B  69      -5.004  27.249 -29.820  1.00 22.70           C  
ANISOU 1335  C   HIS B  69     2571   3186   2869    326    211    -76       C  
ATOM   1336  O   HIS B  69      -4.245  26.350 -29.436  1.00 21.11           O  
ANISOU 1336  O   HIS B  69     2773   2858   2391    222     56   -283       O  
ATOM   1337  CB  HIS B  69      -5.635  27.776 -27.519  1.00 28.41           C  
ANISOU 1337  CB  HIS B  69     2669   5112   3014    690    121   -578       C  
ATOM   1338  CG  HIS B  69      -6.559  28.452 -26.594  1.00 32.18           C  
ANISOU 1338  CG  HIS B  69     3283   5887   3057   1738    175    -95       C  
ATOM   1339  ND1 HIS B  69      -7.728  27.842 -26.208  1.00 34.81           N  
ANISOU 1339  ND1 HIS B  69     3772   6658   2796   1577    874     10       N  
ATOM   1340  CD2 HIS B  69      -6.519  29.652 -25.982  1.00 33.66           C  
ANISOU 1340  CD2 HIS B  69     3951   5930   2909   2134    596   -146       C  
ATOM   1341  CE1 HIS B  69      -8.394  28.628 -25.391  1.00 35.42           C  
ANISOU 1341  CE1 HIS B  69     4072   6608   2778   1935    652     14       C  
ATOM   1342  NE2 HIS B  69      -7.685  29.735 -25.228  1.00 36.56           N  
ANISOU 1342  NE2 HIS B  69     4710   6227   2955   1870   1266    359       N  
ATOM   1343  N   LYS B  70      -4.871  27.967 -30.913  1.00 21.24           N  
ANISOU 1343  N   LYS B  70     2347   3096   2627    458   -169   -243       N  
ATOM   1344  CA  LYS B  70      -3.735  27.803 -31.814  1.00 20.56           C  
ANISOU 1344  CA  LYS B  70     1992   3512   2308    179   -440    -40       C  
ATOM   1345  C   LYS B  70      -2.571  28.666 -31.342  1.00 20.62           C  
ANISOU 1345  C   LYS B  70     2301   2675   2860    322   -482    -88       C  
ATOM   1346  O   LYS B  70      -2.768  29.862 -31.325  1.00 21.28           O  
ANISOU 1346  O   LYS B  70     2432   2761   2891    491    203    289       O  
ATOM   1347  CB  LYS B  70      -4.080  28.196 -33.242  1.00 25.17           C  
ANISOU 1347  CB  LYS B  70     2844   4156   2566   -498   -555    662       C  
ATOM   1348  CG  LYS B  70      -5.166  27.348 -33.885  1.00 31.66           C  
ANISOU 1348  CG  LYS B  70     3982   5007   3043   -993  -1905   1303       C  
ATOM   1349  CD  LYS B  70      -5.202  27.617 -35.395  1.00 39.18           C  
ANISOU 1349  CD  LYS B  70     6457   5301   3130   -885  -2408   1516       C  
ATOM   1350  CE  LYS B  70      -6.426  26.973 -36.023  1.00 44.56           C  
ANISOU 1350  CE  LYS B  70     6996   6394   3540   -633  -3213    854       C  
ATOM   1351  NZ  LYS B  70      -6.345  27.068 -37.516  1.00 63.10           N  
ANISOU 1351  NZ  LYS B  70    10220  10307   3448  -1524  -3165    225       N  
ATOM   1352  N   VAL B  71      -1.463  28.047 -31.015  1.00 16.92           N  
ANISOU 1352  N   VAL B  71     1710   2531   2188     25     87    -40       N  
ATOM   1353  CA  VAL B  71      -0.266  28.733 -30.547  1.00 16.41           C  
ANISOU 1353  CA  VAL B  71     1890   2598   1747    -59    275   -594       C  
ATOM   1354  C   VAL B  71       0.968  28.193 -31.264  1.00 15.07           C  
ANISOU 1354  C   VAL B  71     1758   2207   1762     58     96   -439       C  
ATOM   1355  O   VAL B  71       0.882  27.266 -32.079  1.00 15.66           O  
ANISOU 1355  O   VAL B  71     2014   2261   1673    142      2   -448       O  
ATOM   1356  CB  VAL B  71      -0.073  28.606 -29.023  1.00 17.99           C  
ANISOU 1356  CB  VAL B  71     2125   2923   1786    240    322   -335       C  
ATOM   1357  CG1 VAL B  71      -1.269  29.318 -28.360  1.00 21.40           C  
ANISOU 1357  CG1 VAL B  71     2522   3807   1801    704    392   -447       C  
ATOM   1358  CG2 VAL B  71       0.014  27.213 -28.614  1.00 29.69           C  
ANISOU 1358  CG2 VAL B  71     4861   3415   3006   1302   -128    263       C  
ATOM   1359  N   ILE B  72       2.088  28.841 -30.947  1.00 14.36           N  
ANISOU 1359  N   ILE B  72     1709   2263   1485     84   -110    -79       N  
ATOM   1360  CA  ILE B  72       3.373  28.500 -31.535  1.00 13.72           C  
ANISOU 1360  CA  ILE B  72     1739   1877   1598    247    -56     23       C  
ATOM   1361  C   ILE B  72       4.382  28.299 -30.419  1.00 13.88           C  
ANISOU 1361  C   ILE B  72     1845   1630   1798    266   -197    -34       C  
ATOM   1362  O   ILE B  72       4.481  29.106 -29.507  1.00 15.03           O  
ANISOU 1362  O   ILE B  72     2121   1776   1815    260   -184   -115       O  
ATOM   1363  CB  ILE B  72       3.845  29.601 -32.514  1.00 13.44           C  
ANISOU 1363  CB  ILE B  72     1653   1897   1556    102   -130    -84       C  
ATOM   1364  CG1 ILE B  72       2.915  29.676 -33.723  1.00 19.62           C  
ANISOU 1364  CG1 ILE B  72     2307   3595   1554    -19   -310    448       C  
ATOM   1365  CG2 ILE B  72       5.303  29.418 -32.906  1.00 14.62           C  
ANISOU 1365  CG2 ILE B  72     1891   1704   1959    148    232   -318       C  
ATOM   1366  CD1 ILE B  72       3.148  30.922 -34.543  1.00 27.56           C  
ANISOU 1366  CD1 ILE B  72     5179   3183   2109    274   -859    584       C  
ATOM   1367  N   GLY B  73       5.128  27.194 -30.451  1.00 12.88           N  
ANISOU 1367  N   GLY B  73     1700   1561   1632    180    214    312       N  
ATOM   1368  CA  GLY B  73       6.171  27.061 -29.466  1.00 15.08           C  
ANISOU 1368  CA  GLY B  73     2586   1842   1299    856    -43     97       C  
ATOM   1369  C   GLY B  73       7.082  25.890 -29.737  1.00 12.19           C  
ANISOU 1369  C   GLY B  73     2149   1360   1124    341     56    219       C  
ATOM   1370  O   GLY B  73       6.891  25.134 -30.684  1.00 12.35           O  
ANISOU 1370  O   GLY B  73     1770   1486   1435     11    210     -9       O  
ATOM   1371  N   THR B  74       8.049  25.752 -28.830  1.00 11.89           N  
ANISOU 1371  N   THR B  74     1862   1507   1149    171    129    416       N  
ATOM   1372  CA  THR B  74       9.014  24.665 -28.941  1.00 11.89           C  
ANISOU 1372  CA  THR B  74     1831   1356   1331     69   -120     46       C  
ATOM   1373  C   THR B  74       8.417  23.342 -28.513  1.00 10.47           C  
ANISOU 1373  C   THR B  74     1478   1413   1087    107     49     36       C  
ATOM   1374  O   THR B  74       7.753  23.270 -27.483  1.00 12.29           O  
ANISOU 1374  O   THR B  74     1775   1744   1151    100    200   -129       O  
ATOM   1375  CB  THR B  74      10.270  24.968 -28.080  1.00 13.02           C  
ANISOU 1375  CB  THR B  74     1879   1523   1546   -139   -230    208       C  
ATOM   1376  OG1 THR B  74      10.909  26.146 -28.594  1.00 17.01           O  
ANISOU 1376  OG1 THR B  74     2469   1792   2200   -533     44    279       O  
ATOM   1377  CG2 THR B  74      11.278  23.851 -28.129  1.00 13.90           C  
ANISOU 1377  CG2 THR B  74     1539   2062   1680     37    109    302       C  
ATOM   1378  N   VAL B  75       8.663  22.318 -29.348  1.00 11.11           N  
ANISOU 1378  N   VAL B  75     1704   1364   1155    -44    125     -5       N  
ATOM   1379  CA  VAL B  75       8.233  20.973 -29.026  1.00 12.27           C  
ANISOU 1379  CA  VAL B  75     1679   1290   1693     76    -84    120       C  
ATOM   1380  C   VAL B  75       9.448  20.066 -29.040  1.00 11.02           C  
ANISOU 1380  C   VAL B  75     1492   1536   1159     23     32    195       C  
ATOM   1381  O   VAL B  75      10.149  20.044 -30.058  1.00 13.23           O  
ANISOU 1381  O   VAL B  75     2144   1658   1225    197    334    298       O  
ATOM   1382  CB  VAL B  75       7.161  20.473 -30.009  1.00 11.41           C  
ANISOU 1382  CB  VAL B  75     1451   1357   1528    -39     30    247       C  
ATOM   1383  CG1 VAL B  75       6.782  19.026 -29.759  1.00 15.21           C  
ANISOU 1383  CG1 VAL B  75     2328   1513   1940   -424     18    191       C  
ATOM   1384  CG2 VAL B  75       5.920  21.349 -29.859  1.00 14.41           C  
ANISOU 1384  CG2 VAL B  75     1551   2109   1815    254    171    108       C  
ATOM   1385  N   LEU B  76       9.657  19.332 -27.966  1.00 11.37           N  
ANISOU 1385  N   LEU B  76     1825   1191   1304    123    258    253       N  
ATOM   1386  CA  LEU B  76      10.696  18.312 -27.964  1.00 11.30           C  
ANISOU 1386  CA  LEU B  76     1749   1212   1332    108    -59    -57       C  
ATOM   1387  C   LEU B  76      10.034  16.998 -28.391  1.00 10.86           C  
ANISOU 1387  C   LEU B  76     1543   1226   1356     68    138     73       C  
ATOM   1388  O   LEU B  76       8.970  16.627 -27.886  1.00 13.49           O  
ANISOU 1388  O   LEU B  76     1975   1302   1848    -92    553    135       O  
ATOM   1389  CB  LEU B  76      11.311  18.169 -26.574  1.00 12.16           C  
ANISOU 1389  CB  LEU B  76     2122   1190   1308   -123    -89    256       C  
ATOM   1390  CG  LEU B  76      11.811  19.485 -25.941  1.00 11.01           C  
ANISOU 1390  CG  LEU B  76     1637   1478   1069    -54     42     95       C  
ATOM   1391  CD1 LEU B  76      12.465  19.178 -24.603  1.00 12.53           C  
ANISOU 1391  CD1 LEU B  76     1832   1820   1108    389    -47     -5       C  
ATOM   1392  CD2 LEU B  76      12.762  20.252 -26.844  1.00 13.43           C  
ANISOU 1392  CD2 LEU B  76     2066   1614   1422   -496    235      8       C  
ATOM   1393  N   VAL B  77      10.698  16.301 -29.308  1.00 12.17           N  
ANISOU 1393  N   VAL B  77     1965   1328   1333    169    216   -107       N  
ATOM   1394  CA  VAL B  77      10.152  15.012 -29.765  1.00 12.67           C  
ANISOU 1394  CA  VAL B  77     2119   1298   1396    169     17     52       C  
ATOM   1395  C   VAL B  77      11.121  13.912 -29.373  1.00 11.87           C  
ANISOU 1395  C   VAL B  77     1765   1250   1494      2     16    -58       C  
ATOM   1396  O   VAL B  77      12.280  13.968 -29.724  1.00 13.61           O  
ANISOU 1396  O   VAL B  77     1773   1703   1697     57     96   -134       O  
ATOM   1397  CB  VAL B  77       9.936  15.014 -31.284  1.00 13.54           C  
ANISOU 1397  CB  VAL B  77     2056   1654   1434    104   -125    -34       C  
ATOM   1398  CG1 VAL B  77       9.419  13.680 -31.760  1.00 17.12           C  
ANISOU 1398  CG1 VAL B  77     3016   1878   1611   -251    426   -406       C  
ATOM   1399  CG2 VAL B  77       8.959  16.136 -31.654  1.00 16.23           C  
ANISOU 1399  CG2 VAL B  77     2158   2037   1972    242   -220    449       C  
ATOM   1400  N   GLY B  78      10.590  12.934 -28.617  1.00 13.33           N  
ANISOU 1400  N   GLY B  78     2236   1580   1249    168     90    260       N  
ATOM   1401  CA  GLY B  78      11.430  11.837 -28.218  1.00 17.36           C  
ANISOU 1401  CA  GLY B  78     2160   1883   2553     83     19    831       C  
ATOM   1402  C   GLY B  78      10.664  10.995 -27.210  1.00 17.43           C  
ANISOU 1402  C   GLY B  78     2849   1859   1914    212    213    642       C  
ATOM   1403  O   GLY B  78       9.512  11.273 -26.892  1.00 16.32           O  
ANISOU 1403  O   GLY B  78     2944   1696   1563    152    391    360       O  
ATOM   1404  N   PRO B  79      11.354   9.962 -26.744  1.00 23.14           N  
ANISOU 1404  N   PRO B  79     4056   2147   2591   1039    875    961       N  
ATOM   1405  CA  PRO B  79      10.788   9.037 -25.742  1.00 25.80           C  
ANISOU 1405  CA  PRO B  79     5463   1811   2529   1234   1222    856       C  
ATOM   1406  C   PRO B  79      10.339   9.783 -24.492  1.00 24.87           C  
ANISOU 1406  C   PRO B  79     4816   2441   2191   1224    694    686       C  
ATOM   1407  O   PRO B  79      11.043  10.635 -23.929  1.00 28.84           O  
ANISOU 1407  O   PRO B  79     4964   3617   2378    660    699    329       O  
ATOM   1408  CB  PRO B  79      11.962   8.143 -25.388  1.00 30.07           C  
ANISOU 1408  CB  PRO B  79     6486   2014   2925   1915    878    745       C  
ATOM   1409  CG  PRO B  79      12.935   8.258 -26.507  1.00 32.72           C  
ANISOU 1409  CG  PRO B  79     5790   2599   4042   2088   1227    878       C  
ATOM   1410  CD  PRO B  79      12.728   9.592 -27.142  1.00 30.00           C  
ANISOU 1410  CD  PRO B  79     4642   2889   3870   1907   1391   1197       C  
ATOM   1411  N   THR B  80       9.116   9.428 -24.109  1.00 23.32           N  
ANISOU 1411  N   THR B  80     4773   1798   2292   1340    643    507       N  
ATOM   1412  CA  THR B  80       8.602   9.979 -22.865  1.00 22.72           C  
ANISOU 1412  CA  THR B  80     4657   1832   2143    811    636    449       C  
ATOM   1413  C   THR B  80       7.592   8.966 -22.319  1.00 23.70           C  
ANISOU 1413  C   THR B  80     4673   2069   2260    623    335    629       C  
ATOM   1414  O   THR B  80       6.774   8.438 -23.070  1.00 25.87           O  
ANISOU 1414  O   THR B  80     5162   2433   2234    270    430    307       O  
ATOM   1415  CB  THR B  80       8.023  11.406 -23.013  1.00 19.91           C  
ANISOU 1415  CB  THR B  80     3323   1918   2323    743    635    230       C  
ATOM   1416  OG1 THR B  80       7.458  11.816 -21.761  1.00 23.49           O  
ANISOU 1416  OG1 THR B  80     4406   2395   2125    714    419   -164       O  
ATOM   1417  CG2 THR B  80       6.906  11.503 -24.054  1.00 19.84           C  
ANISOU 1417  CG2 THR B  80     3595   1893   2051    425    554    117       C  
ATOM   1418  N   PRO B  81       7.681   8.676 -21.016  1.00 23.28           N  
ANISOU 1418  N   PRO B  81     4673   1973   2202    506    395    582       N  
ATOM   1419  CA  PRO B  81       6.721   7.742 -20.435  1.00 24.01           C  
ANISOU 1419  CA  PRO B  81     4406   2521   2195    299    136    656       C  
ATOM   1420  C   PRO B  81       5.299   8.236 -20.670  1.00 25.81           C  
ANISOU 1420  C   PRO B  81     4443   2255   3107   -184  -1136    572       C  
ATOM   1421  O   PRO B  81       4.397   7.397 -20.787  1.00 33.06           O  
ANISOU 1421  O   PRO B  81     4774   2892   4894   -814    123     44       O  
ATOM   1422  CB  PRO B  81       7.077   7.740 -18.944  1.00 24.26           C  
ANISOU 1422  CB  PRO B  81     3811   3063   2342    175   -156   1249       C  
ATOM   1423  CG  PRO B  81       8.563   8.025 -18.960  1.00 25.62           C  
ANISOU 1423  CG  PRO B  81     4045   3683   2006   -355    453    854       C  
ATOM   1424  CD  PRO B  81       8.674   9.107 -20.016  1.00 23.53           C  
ANISOU 1424  CD  PRO B  81     3905   2826   2209    434    652    578       C  
ATOM   1425  N   ALA B  82       5.069   9.544 -20.738  1.00 23.85           N  
ANISOU 1425  N   ALA B  82     3794   2374   2894     80    888    503       N  
ATOM   1426  CA  ALA B  82       3.759  10.147 -20.982  1.00 26.06           C  
ANISOU 1426  CA  ALA B  82     3933   2942   3025    323   1128   1199       C  
ATOM   1427  C   ALA B  82       3.940  11.425 -21.797  1.00 20.77           C  
ANISOU 1427  C   ALA B  82     3475   2282   2135   -362    508    361       C  
ATOM   1428  O   ALA B  82       4.895  12.129 -21.504  1.00 23.67           O  
ANISOU 1428  O   ALA B  82     3520   2977   2497   -373    138     28       O  
ATOM   1429  CB  ALA B  82       3.058  10.442 -19.654  1.00 30.92           C  
ANISOU 1429  CB  ALA B  82     4358   4075   3317   1004   1650   1734       C  
ATOM   1430  N   ASN B  83       3.114  11.765 -22.782  1.00 17.87           N  
ANISOU 1430  N   ASN B  83     2528   1779   2484   -118    791    249       N  
ATOM   1431  CA  ASN B  83       3.202  13.051 -23.454  1.00 15.31           C  
ANISOU 1431  CA  ASN B  83     2306   1687   1825   -485    443   -115       C  
ATOM   1432  C   ASN B  83       2.884  14.171 -22.471  1.00 14.41           C  
ANISOU 1432  C   ASN B  83     1974   1841   1660   -439    317   -143       C  
ATOM   1433  O   ASN B  83       1.973  14.059 -21.657  1.00 18.34           O  
ANISOU 1433  O   ASN B  83     2387   2417   2163   -598    749   -327       O  
ATOM   1434  CB  ASN B  83       2.197  13.161 -24.585  1.00 17.52           C  
ANISOU 1434  CB  ASN B  83     2778   2025   1856   -242    128   -478       C  
ATOM   1435  CG  ASN B  83       2.513  12.235 -25.764  1.00 18.33           C  
ANISOU 1435  CG  ASN B  83     2339   2297   2328   -251    249   -826       C  
ATOM   1436  OD1 ASN B  83       3.656  11.872 -26.000  1.00 19.11           O  
ANISOU 1436  OD1 ASN B  83     2375   2402   2482   -251    539   -300       O  
ATOM   1437  ND2 ASN B  83       1.437  11.868 -26.490  1.00 19.86           N  
ANISOU 1437  ND2 ASN B  83     2726   3150   1668   -189    -16   -606       N  
ATOM   1438  N   VAL B  84       3.653  15.245 -22.552  1.00 15.27           N  
ANISOU 1438  N   VAL B  84     2365   1684   1755   -470    186   -121       N  
ATOM   1439  CA  VAL B  84       3.512  16.312 -21.590  1.00 15.64           C  
ANISOU 1439  CA  VAL B  84     2781   1618   1543   -256    108     75       C  
ATOM   1440  C   VAL B  84       3.490  17.680 -22.247  1.00 12.94           C  
ANISOU 1440  C   VAL B  84     1950   1684   1283   -263    326      1       C  
ATOM   1441  O   VAL B  84       4.361  17.981 -23.085  1.00 14.50           O  
ANISOU 1441  O   VAL B  84     2148   1793   1567   -367    581   -203       O  
ATOM   1442  CB  VAL B  84       4.698  16.250 -20.592  1.00 20.72           C  
ANISOU 1442  CB  VAL B  84     4228   1730   1913   -445   -881    175       C  
ATOM   1443  CG1 VAL B  84       4.583  17.448 -19.701  1.00 19.69           C  
ANISOU 1443  CG1 VAL B  84     3004   2172   2305   -250   -277   -298       C  
ATOM   1444  CG2 VAL B  84       4.672  14.960 -19.803  1.00 30.08           C  
ANISOU 1444  CG2 VAL B  84     6196   1994   3239   -748  -2029    829       C  
ATOM   1445  N   ILE B  85       2.513  18.507 -21.903  1.00 13.48           N  
ANISOU 1445  N   ILE B  85     1682   1704   1734   -326    268   -105       N  
ATOM   1446  CA  ILE B  85       2.504  19.925 -22.244  1.00 12.63           C  
ANISOU 1446  CA  ILE B  85     1672   1715   1412   -387    183    -41       C  
ATOM   1447  C   ILE B  85       3.111  20.698 -21.078  1.00 12.22           C  
ANISOU 1447  C   ILE B  85     1702   1712   1231   -387    217     56       C  
ATOM   1448  O   ILE B  85       2.541  20.684 -19.981  1.00 14.24           O  
ANISOU 1448  O   ILE B  85     1963   2053   1395   -315    447   -106       O  
ATOM   1449  CB AILE B  85       1.089  20.409 -22.577  0.61 14.38           C  
ANISOU 1449  CB AILE B  85     1877   2052   1536   -213    -51    -12       C  
ATOM   1450  CB BILE B  85       1.088  20.471 -22.472  0.39 14.26           C  
ANISOU 1450  CB BILE B  85     1875   1995   1548   -169    -58   -128       C  
ATOM   1451  CG1AILE B  85       0.469  19.653 -23.767  0.61 17.63           C  
ANISOU 1451  CG1AILE B  85     2097   2629   1974   -494   -258   -305       C  
ATOM   1452  CG1BILE B  85       0.294  19.754 -23.576  0.39 15.69           C  
ANISOU 1452  CG1BILE B  85     1901   2631   1428   -515     34   -131       C  
ATOM   1453  CG2AILE B  85       1.058  21.911 -22.799  0.61 15.13           C  
ANISOU 1453  CG2AILE B  85     2106   2047   1596     -8    196     18       C  
ATOM   1454  CG2BILE B  85       1.137  21.970 -22.736  0.39 15.85           C  
ANISOU 1454  CG2BILE B  85     2414   1965   1645    111    264   -130       C  
ATOM   1455  CD1AILE B  85      -1.033  19.736 -23.844  0.61 17.62           C  
ANISOU 1455  CD1AILE B  85     2167   2432   2097    -70   -687    440       C  
ATOM   1456  CD1BILE B  85       1.081  19.724 -24.874  0.39 16.24           C  
ANISOU 1456  CD1BILE B  85     1490   3035   1644   -625    100   -468       C  
ATOM   1457  N   GLY B  86       4.279  21.269 -21.288  1.00 12.29           N  
ANISOU 1457  N   GLY B  86     1611   1665   1394   -315    126    -66       N  
ATOM   1458  CA  GLY B  86       5.011  21.978 -20.204  1.00 12.54           C  
ANISOU 1458  CA  GLY B  86     1748   1444   1572    -85    -44   -134       C  
ATOM   1459  C   GLY B  86       4.643  23.442 -20.139  1.00 11.63           C  
ANISOU 1459  C   GLY B  86     1536   1536   1348      0   -108    -89       C  
ATOM   1460  O   GLY B  86       3.786  23.959 -20.882  1.00 11.77           O  
ANISOU 1460  O   GLY B  86     1636   1747   1090     18     -4     57       O  
ATOM   1461  N   ARG B  87       5.302  24.125 -19.182  1.00 10.84           N  
ANISOU 1461  N   ARG B  87     1401   1412   1305   -207     15     13       N  
ATOM   1462  CA  ARG B  87       4.988  25.548 -19.025  1.00 11.66           C  
ANISOU 1462  CA  ARG B  87     1932   1501    998   -148     87    -42       C  
ATOM   1463  C   ARG B  87       5.237  26.389 -20.280  1.00 12.02           C  
ANISOU 1463  C   ARG B  87     1805   1543   1219     51    131    160       C  
ATOM   1464  O   ARG B  87       4.543  27.396 -20.503  1.00 13.60           O  
ANISOU 1464  O   ARG B  87     2180   1666   1322    235    -70     32       O  
ATOM   1465  CB  ARG B  87       5.854  26.115 -17.894  1.00 12.68           C  
ANISOU 1465  CB  ARG B  87     1918   1808   1092   -328     62   -140       C  
ATOM   1466  CG  ARG B  87       5.476  25.532 -16.528  1.00 12.76           C  
ANISOU 1466  CG  ARG B  87     1879   1956   1013   -289     41    -80       C  
ATOM   1467  CD  ARG B  87       6.208  26.295 -15.412  1.00 14.49           C  
ANISOU 1467  CD  ARG B  87     1857   2529   1119   -513     72   -263       C  
ATOM   1468  NE  ARG B  87       7.648  25.995 -15.438  1.00 14.50           N  
ANISOU 1468  NE  ARG B  87     1839   2304   1367   -566    118      9       N  
ATOM   1469  CZ  ARG B  87       8.564  26.828 -15.983  1.00 14.69           C  
ANISOU 1469  CZ  ARG B  87     1695   2264   1624   -409   -167    368       C  
ATOM   1470  NH1 ARG B  87       9.869  26.492 -16.000  1.00 15.19           N  
ANISOU 1470  NH1 ARG B  87     1679   2598   1497   -280   -106     49       N  
ATOM   1471  NH2 ARG B  87       8.216  28.015 -16.485  1.00 14.58           N  
ANISOU 1471  NH2 ARG B  87     2079   2002   1461   -317   -213     17       N  
ATOM   1472  N   ASN B  88       6.178  25.986 -21.151  1.00 11.73           N  
ANISOU 1472  N   ASN B  88     1731   1597   1130   -208    156     10       N  
ATOM   1473  CA  ASN B  88       6.461  26.783 -22.324  1.00 12.16           C  
ANISOU 1473  CA  ASN B  88     1644   1651   1326   -112    133    185       C  
ATOM   1474  C   ASN B  88       5.226  26.962 -23.202  1.00 12.65           C  
ANISOU 1474  C   ASN B  88     1773   1467   1567    -58    -67    209       C  
ATOM   1475  O   ASN B  88       5.029  28.027 -23.773  1.00 18.58           O  
ANISOU 1475  O   ASN B  88     3105   1689   2266   -125   -779    557       O  
ATOM   1476  CB  ASN B  88       7.606  26.191 -23.178  1.00 12.43           C  
ANISOU 1476  CB  ASN B  88     1720   1597   1404   -168    243     31       C  
ATOM   1477  CG  ASN B  88       7.216  24.924 -23.920  1.00 13.60           C  
ANISOU 1477  CG  ASN B  88     2356   1483   1328   -158    120    175       C  
ATOM   1478  OD1 ASN B  88       6.759  23.946 -23.307  1.00 13.17           O  
ANISOU 1478  OD1 ASN B  88     1895   1569   1538   -254    163    148       O  
ATOM   1479  ND2 ASN B  88       7.351  24.966 -25.243  1.00 12.76           N  
ANISOU 1479  ND2 ASN B  88     1877   1696   1277   -104    -99    162       N  
ATOM   1480  N   LEU B  89       4.393  25.926 -23.305  1.00 12.36           N  
ANISOU 1480  N   LEU B  89     1532   1690   1474    -30    193    -36       N  
ATOM   1481  CA  LEU B  89       3.177  26.089 -24.132  1.00 12.43           C  
ANISOU 1481  CA  LEU B  89     1586   1506   1632    -39    109    -97       C  
ATOM   1482  C   LEU B  89       2.032  26.622 -23.282  1.00 11.59           C  
ANISOU 1482  C   LEU B  89     1534   1631   1237     26      0    107       C  
ATOM   1483  O   LEU B  89       1.150  27.323 -23.835  1.00 12.29           O  
ANISOU 1483  O   LEU B  89     1827   1609   1234    250     54    214       O  
ATOM   1484  CB  LEU B  89       2.773  24.800 -24.836  1.00 12.56           C  
ANISOU 1484  CB  LEU B  89     2215   1291   1266   -196     73    168       C  
ATOM   1485  CG  LEU B  89       3.688  24.365 -25.995  1.00 16.08           C  
ANISOU 1485  CG  LEU B  89     2551   1867   1693   -234    375   -223       C  
ATOM   1486  CD1 LEU B  89       3.132  23.097 -26.599  1.00 17.61           C  
ANISOU 1486  CD1 LEU B  89     2480   2161   2048    238   -580   -648       C  
ATOM   1487  CD2 LEU B  89       3.863  25.511 -26.989  1.00 19.26           C  
ANISOU 1487  CD2 LEU B  89     3418   2639   1259   -160    534     50       C  
ATOM   1488  N   MET B  90       2.010  26.301 -21.990  1.00 11.49           N  
ANISOU 1488  N   MET B  90     1670   1426   1270    -10    -69    141       N  
ATOM   1489  CA  MET B  90       0.960  26.938 -21.169  1.00 12.91           C  
ANISOU 1489  CA  MET B  90     1966   1793   1145    -70     13   -128       C  
ATOM   1490  C   MET B  90       1.059  28.439 -21.166  1.00 13.40           C  
ANISOU 1490  C   MET B  90     1834   1833   1423     66    268   -206       C  
ATOM   1491  O   MET B  90       0.001  29.065 -21.140  1.00 14.28           O  
ANISOU 1491  O   MET B  90     1874   1996   1555    174    274     82       O  
ATOM   1492  CB  MET B  90       1.009  26.323 -19.752  1.00 15.24           C  
ANISOU 1492  CB  MET B  90     2134   2412   1244   -270     62    141       C  
ATOM   1493  CG  MET B  90       0.452  24.896 -19.848  1.00 17.12           C  
ANISOU 1493  CG  MET B  90     2977   2017   1511    -25     87    178       C  
ATOM   1494  SD  MET B  90       0.169  24.125 -18.219  1.00 21.54           S  
ANISOU 1494  SD  MET B  90     3828   2657   1701   -611     42    383       S  
ATOM   1495  CE  MET B  90       1.823  23.574 -17.976  1.00 21.86           C  
ANISOU 1495  CE  MET B  90     3795   3576    934   -507    -32    788       C  
ATOM   1496  N   THR B  91       2.278  29.023 -21.210  1.00 12.75           N  
ANISOU 1496  N   THR B  91     1905   1730   1209    -50     14   -181       N  
ATOM   1497  CA  THR B  91       2.280  30.496 -21.278  1.00 14.49           C  
ANISOU 1497  CA  THR B  91     2292   1723   1490    -22   -146   -318       C  
ATOM   1498  C   THR B  91       1.721  31.007 -22.592  1.00 14.46           C  
ANISOU 1498  C   THR B  91     2471   1515   1508   -178   -102   -172       C  
ATOM   1499  O   THR B  91       1.100  32.098 -22.607  1.00 16.03           O  
ANISOU 1499  O   THR B  91     2473   1936   1683    206     24   -226       O  
ATOM   1500  CB  THR B  91       3.696  31.045 -21.081  1.00 15.52           C  
ANISOU 1500  CB  THR B  91     2393   1811   1694   -247    -94    -17       C  
ATOM   1501  OG1 THR B  91       4.546  30.502 -22.097  1.00 18.74           O  
ANISOU 1501  OG1 THR B  91     2430   2408   2281   -293    152   -350       O  
ATOM   1502  CG2 THR B  91       4.218  30.591 -19.709  1.00 17.25           C  
ANISOU 1502  CG2 THR B  91     1888   2521   2144    -74   -211    438       C  
ATOM   1503  N   GLN B  92       1.937  30.229 -23.670  1.00 13.89           N  
ANISOU 1503  N   GLN B  92     2486   1409   1380   -196    -20      1       N  
ATOM   1504  CA  GLN B  92       1.461  30.681 -24.988  1.00 15.02           C  
ANISOU 1504  CA  GLN B  92     2533   1847   1326    119    200     98       C  
ATOM   1505  C   GLN B  92      -0.064  30.658 -25.043  1.00 15.41           C  
ANISOU 1505  C   GLN B  92     2518   2041   1294    294    207    147       C  
ATOM   1506  O   GLN B  92      -0.685  31.578 -25.628  1.00 17.97           O  
ANISOU 1506  O   GLN B  92     2827   2209   1793    480    180    312       O  
ATOM   1507  CB  GLN B  92       2.034  29.801 -26.105  1.00 14.17           C  
ANISOU 1507  CB  GLN B  92     2328   1600   1455      3    214     44       C  
ATOM   1508  CG  GLN B  92       3.550  29.850 -26.210  1.00 13.01           C  
ANISOU 1508  CG  GLN B  92     2245   1395   1304   -173     29     84       C  
ATOM   1509  CD  GLN B  92       4.038  31.261 -26.440  1.00 14.12           C  
ANISOU 1509  CD  GLN B  92     2445   1338   1580   -108   -347    139       C  
ATOM   1510  OE1 GLN B  92       3.637  31.918 -27.405  1.00 14.54           O  
ANISOU 1510  OE1 GLN B  92     2672   1358   1495    -17   -108    156       O  
ATOM   1511  NE2 GLN B  92       4.865  31.815 -25.569  1.00 19.89           N  
ANISOU 1511  NE2 GLN B  92     3061   1724   2772   -626  -1201    482       N  
ATOM   1512  N   ILE B  93      -0.721  29.652 -24.417  1.00 15.60           N  
ANISOU 1512  N   ILE B  93     2485   1974   1468    -87     -7    -38       N  
ATOM   1513  CA  ILE B  93      -2.183  29.670 -24.398  1.00 15.84           C  
ANISOU 1513  CA  ILE B  93     2470   1989   1560    217   -128    328       C  
ATOM   1514  C   ILE B  93      -2.787  30.563 -23.303  1.00 16.48           C  
ANISOU 1514  C   ILE B  93     2468   2278   1517    193     73    398       C  
ATOM   1515  O   ILE B  93      -4.040  30.678 -23.246  1.00 20.30           O  
ANISOU 1515  O   ILE B  93     2442   3125   2146    595   -119    281       O  
ATOM   1516  CB  ILE B  93      -2.768  28.258 -24.227  1.00 18.58           C  
ANISOU 1516  CB  ILE B  93     2432   2313   2314   -174   -208    135       C  
ATOM   1517  CG1 ILE B  93      -2.433  27.547 -22.934  1.00 19.07           C  
ANISOU 1517  CG1 ILE B  93     2842   1909   2492   -198    294    450       C  
ATOM   1518  CG2 ILE B  93      -2.327  27.391 -25.396  1.00 24.83           C  
ANISOU 1518  CG2 ILE B  93     4449   2404   2582   -832    365   -247       C  
ATOM   1519  CD1 ILE B  93      -2.983  26.116 -22.827  1.00 21.62           C  
ANISOU 1519  CD1 ILE B  93     3060   2226   2929   -719    145    133       C  
ATOM   1520  N   GLY B  94      -1.940  31.182 -22.487  1.00 16.09           N  
ANISOU 1520  N   GLY B  94     2481   2013   1618     82    315    192       N  
ATOM   1521  CA  GLY B  94      -2.407  32.034 -21.409  1.00 16.61           C  
ANISOU 1521  CA  GLY B  94     2476   1953   1883    146    577    192       C  
ATOM   1522  C   GLY B  94      -3.011  31.274 -20.234  1.00 17.57           C  
ANISOU 1522  C   GLY B  94     2888   2019   1770    253    564    220       C  
ATOM   1523  O   GLY B  94      -3.919  31.760 -19.541  1.00 21.80           O  
ANISOU 1523  O   GLY B  94     3479   2660   2144    847   1143    889       O  
ATOM   1524  N   CYS B  95      -2.493  30.083 -19.997  1.00 16.10           N  
ANISOU 1524  N   CYS B  95     2409   2033   1676     69     71    217       N  
ATOM   1525  CA  CYS B  95      -2.913  29.244 -18.880  1.00 17.20           C  
ANISOU 1525  CA  CYS B  95     2256   2511   1770    591    366    517       C  
ATOM   1526  C   CYS B  95      -2.274  29.673 -17.563  1.00 18.04           C  
ANISOU 1526  C   CYS B  95     2233   2805   1816    171    269    772       C  
ATOM   1527  O   CYS B  95      -1.043  29.890 -17.496  1.00 20.42           O  
ANISOU 1527  O   CYS B  95     2279   3171   2310     30    376    440       O  
ATOM   1528  CB  CYS B  95      -2.557  27.795 -19.234  1.00 18.65           C  
ANISOU 1528  CB  CYS B  95     2416   2296   2376    498    377    761       C  
ATOM   1529  SG  CYS B  95      -3.141  26.592 -18.035  1.00 20.18           S  
ANISOU 1529  SG  CYS B  95     2807   2664   2196    -99     99    669       S  
ATOM   1530  N   THR B  96      -3.123  29.799 -16.541  1.00 15.94           N  
ANISOU 1530  N   THR B  96     2251   1996   1810    130    268    452       N  
ATOM   1531  CA  THR B  96      -2.638  30.188 -15.216  1.00 15.38           C  
ANISOU 1531  CA  THR B  96     2082   1818   1945    311    112    515       C  
ATOM   1532  C   THR B  96      -3.174  29.209 -14.183  1.00 15.00           C  
ANISOU 1532  C   THR B  96     1974   1914   1812    251    280    394       C  
ATOM   1533  O   THR B  96      -4.146  28.502 -14.426  1.00 16.75           O  
ANISOU 1533  O   THR B  96     2305   2214   1845    -31    155    360       O  
ATOM   1534  CB  THR B  96      -3.076  31.618 -14.813  1.00 16.94           C  
ANISOU 1534  CB  THR B  96     2556   1895   1986    572   -131    452       C  
ATOM   1535  OG1 THR B  96      -4.519  31.752 -14.893  1.00 17.83           O  
ANISOU 1535  OG1 THR B  96     2608   1912   2256    640    -10    341       O  
ATOM   1536  CG2 THR B  96      -2.446  32.656 -15.727  1.00 19.45           C  
ANISOU 1536  CG2 THR B  96     2913   1742   2736    353    -48    570       C  
ATOM   1537  N   LEU B  97      -2.528  29.158 -13.016  1.00 14.56           N  
ANISOU 1537  N   LEU B  97     2121   1765   1646    124    406    198       N  
ATOM   1538  CA  LEU B  97      -3.122  28.508 -11.846  1.00 14.48           C  
ANISOU 1538  CA  LEU B  97     1845   1932   1725    303    544    292       C  
ATOM   1539  C   LEU B  97      -3.864  29.544 -11.006  1.00 15.31           C  
ANISOU 1539  C   LEU B  97     1754   1995   2066    124    482    -60       C  
ATOM   1540  O   LEU B  97      -3.348  30.656 -10.817  1.00 18.75           O  
ANISOU 1540  O   LEU B  97     2419   2373   2334   -337    525   -450       O  
ATOM   1541  CB  LEU B  97      -2.035  27.858 -11.010  1.00 15.00           C  
ANISOU 1541  CB  LEU B  97     2308   1629   1763    284    128     44       C  
ATOM   1542  CG  LEU B  97      -1.271  26.659 -11.584  1.00 14.06           C  
ANISOU 1542  CG  LEU B  97     2079   1430   1833     93    -54    -96       C  
ATOM   1543  CD1 LEU B  97       0.106  26.520 -10.914  1.00 16.76           C  
ANISOU 1543  CD1 LEU B  97     2377   2341   1650    556   -213     19       C  
ATOM   1544  CD2 LEU B  97      -2.086  25.403 -11.440  1.00 16.90           C  
ANISOU 1544  CD2 LEU B  97     2870   1622   1928   -242    726    119       C  
ATOM   1545  N   ASN B  98      -5.044  29.165 -10.512  1.00 15.03           N  
ANISOU 1545  N   ASN B  98     1634   2108   1967    345    436    273       N  
ATOM   1546  CA  ASN B  98      -5.868  30.120  -9.779  1.00 16.94           C  
ANISOU 1546  CA  ASN B  98     1923   2226   2286    548    664    335       C  
ATOM   1547  C   ASN B  98      -6.453  29.463  -8.531  1.00 18.15           C  
ANISOU 1547  C   ASN B  98     2532   2220   2145    370    788    178       C  
ATOM   1548  O   ASN B  98      -7.012  28.383  -8.685  1.00 18.86           O  
ANISOU 1548  O   ASN B  98     2730   2491   1945     79    654    198       O  
ATOM   1549  CB  ASN B  98      -7.043  30.619 -10.631  1.00 17.73           C  
ANISOU 1549  CB  ASN B  98     1862   2380   2497    561    599    355       C  
ATOM   1550  CG  ASN B  98      -6.506  31.352 -11.854  1.00 20.01           C  
ANISOU 1550  CG  ASN B  98     2391   2933   2280    198    279    460       C  
ATOM   1551  OD1 ASN B  98      -6.136  30.721 -12.861  1.00 22.99           O  
ANISOU 1551  OD1 ASN B  98     2776   3506   2454    284    675    398       O  
ATOM   1552  ND2 ASN B  98      -6.488  32.668 -11.760  1.00 24.81           N  
ANISOU 1552  ND2 ASN B  98     3943   2896   2587   -478    232    542       N  
ATOM   1553  N   PHE B  99      -6.346  30.119  -7.369  1.00 22.16           N  
ANISOU 1553  N   PHE B  99     3602   2737   2082      5     89    230       N  
ATOM   1554  CA  PHE B  99      -7.083  29.677  -6.183  1.00 21.12           C  
ANISOU 1554  CA  PHE B  99     3743   2250   2032    386    571   -164       C  
ATOM   1555  C   PHE B  99      -7.357  30.798  -5.156  1.00 23.94           C  
ANISOU 1555  C   PHE B  99     4069   2206   2821    -24   -132   -859       C  
ATOM   1556  O   PHE B  99      -6.871  31.904  -5.481  1.00 28.24           O  
ANISOU 1556  O   PHE B  99     5024   2478   3227   -118    656   -478       O  
ATOM   1557  CB  PHE B  99      -6.347  28.538  -5.496  1.00 20.27           C  
ANISOU 1557  CB  PHE B  99     3240   2365   2097    112    588     64       C  
ATOM   1558  CG  PHE B  99      -4.964  28.791  -4.954  1.00 22.10           C  
ANISOU 1558  CG  PHE B  99     3436   2545   2415    -88    416     22       C  
ATOM   1559  CD1 PHE B  99      -3.884  28.715  -5.818  1.00 23.76           C  
ANISOU 1559  CD1 PHE B  99     3199   2574   3255     16    595   -182       C  
ATOM   1560  CD2 PHE B  99      -4.772  29.069  -3.612  1.00 27.72           C  
ANISOU 1560  CD2 PHE B  99     4229   3553   2749   -349     64   -573       C  
ATOM   1561  CE1 PHE B  99      -2.607  28.901  -5.329  1.00 26.16           C  
ANISOU 1561  CE1 PHE B  99     3371   3062   3505    232    278   -752       C  
ATOM   1562  CE2 PHE B  99      -3.484  29.282  -3.112  1.00 27.59           C  
ANISOU 1562  CE2 PHE B  99     4259   3130   3093   -463     43   -845       C  
ATOM   1563  CZ  PHE B  99      -2.411  29.199  -3.993  1.00 30.66           C  
ANISOU 1563  CZ  PHE B  99     4143   4016   3489    290     99   -711       C  
TER    1564      PHE B  99                                                      
HETATM 1565 NA    NA A 402      -5.288  14.627   0.129  0.64 14.27          NA  
ANISOU 1565 NA    NA A 402     1026   3490    907   -495     31     55      NA  
HETATM 1566 NA    NA B 401       7.908  27.787 -26.455  0.65 14.83          NA  
ANISOU 1566 NA    NA B 401     3787   1075    774   -535     90    -15      NA  
HETATM 1567  O   HOH A 403       5.559  33.677 -14.120  1.00 16.23           O  
ANISOU 1567  O   HOH A 403     2122   2290   1756   -269   -198   -635       O  
HETATM 1568  O   HOH A 404       0.261  13.176  -1.076  1.00 13.84           O  
ANISOU 1568  O   HOH A 404     1872   2006   1381    215    417    248       O  
HETATM 1569  O   HOH A 405       0.100  10.953  11.734  1.00 14.59           O  
ANISOU 1569  O   HOH A 405     2002   2287   1253    433    200    211       O  
HETATM 1570  O   HOH A 406      -8.861  20.617   3.142  1.00 14.13           O  
ANISOU 1570  O   HOH A 406     1617   2246   1507    131     37     76       O  
HETATM 1571  O   HOH A 407       1.173  36.334 -19.644  1.00 16.77           O  
ANISOU 1571  O   HOH A 407     2226   1726   2419     39   -527    113       O  
HETATM 1572  O   HOH A 408      12.306  23.979   1.308  1.00 17.84           O  
ANISOU 1572  O   HOH A 408     1915   2570   2295   -111   -171    232       O  
HETATM 1573  O   HOH A 409      -1.461  14.635 -12.807  1.00 16.93           O  
ANISOU 1573  O   HOH A 409     2245   2193   1996   -621    358   -109       O  
HETATM 1574  O   HOH A 410      -7.730  15.960   1.775  1.00 19.20           O  
ANISOU 1574  O   HOH A 410     2039   2740   2515     -8    -58    381       O  
HETATM 1575  O   HOH A 411       2.358   1.040  -1.708  1.00 21.54           O  
ANISOU 1575  O   HOH A 411     2711   3242   2231   -960    523   -427       O  
HETATM 1576  O   HOH A 412      10.131   9.801   5.627  1.00 18.85           O  
ANISOU 1576  O   HOH A 412     2294   2618   2249     62   -263    681       O  
HETATM 1577  O   HOH A 413      -9.076  21.443  -8.602  1.00 18.36           O  
ANISOU 1577  O   HOH A 413     2607   2448   1922     18    284   -181       O  
HETATM 1578  O   HOH A 414       2.441  11.329 -10.358  1.00 19.91           O  
ANISOU 1578  O   HOH A 414     3203   2159   2204    369    151    -52       O  
HETATM 1579  O   HOH A 415       8.825   6.764 -11.953  1.00 24.79           O  
ANISOU 1579  O   HOH A 415     5154   2353   1913    823   1026   -351       O  
HETATM 1580  O   HOH A 416      12.901  13.042   4.122  1.00 19.94           O  
ANISOU 1580  O   HOH A 416     2177   2437   2962    250   -183   1005       O  
HETATM 1581  O   HOH A 417      -0.974  12.744   9.905  1.00 17.63           O  
ANISOU 1581  O   HOH A 417     2038   2836   1826   -142   -136    409       O  
HETATM 1582  O   HOH A 418      -5.478  12.514   3.983  1.00 15.60           O  
ANISOU 1582  O   HOH A 418     2000   2592   1333    -30    -59     52       O  
HETATM 1583  O   HOH A 419      15.000   8.367  -3.851  1.00 20.14           O  
ANISOU 1583  O   HOH A 419     2336   3292   2025    141   -337    784       O  
HETATM 1584  O   HOH A 420      15.433  12.173  -4.562  1.00 20.58           O  
ANISOU 1584  O   HOH A 420     2237   3133   2449    646    673    544       O  
HETATM 1585  O   HOH A 421       5.053  30.404 -11.695  1.00 20.27           O  
ANISOU 1585  O   HOH A 421     2763   2573   2366   -242     86     83       O  
HETATM 1586  O   HOH A 422       1.078  14.305  11.046  1.00 16.69           O  
ANISOU 1586  O   HOH A 422     1850   2908   1584   -146    122    -31       O  
HETATM 1587  O   HOH A 423      -1.429   9.146   9.014  1.00 17.44           O  
ANISOU 1587  O   HOH A 423     2434   2792   1401    -94     98    606       O  
HETATM 1588  O   HOH A 424      11.938  29.274 -13.031  1.00 26.06           O  
ANISOU 1588  O   HOH A 424     1762   2865   5276   -683    395   -130       O  
HETATM 1589  O   HOH A 425      15.187  -0.740  -8.474  1.00 22.34           O  
ANISOU 1589  O   HOH A 425     3287   2635   2567     -1   -552   -133       O  
HETATM 1590  O   HOH A 426      -1.763  11.592  -1.963  1.00 27.23           O  
ANISOU 1590  O   HOH A 426     3709   3635   3002  -1459    846   -586       O  
HETATM 1591  O   HOH A 427      -4.725  23.403   7.886  1.00 19.99           O  
ANISOU 1591  O   HOH A 427     2940   2607   2050    198    -22   -316       O  
HETATM 1592  O   HOH A 428       6.867  15.225  14.965  1.00 26.16           O  
ANISOU 1592  O   HOH A 428     2778   4483   2679    -81   -119   -734       O  
HETATM 1593  O   HOH A 429       0.308  12.568 -12.779  1.00 23.06           O  
ANISOU 1593  O   HOH A 429     3269   2934   2558     18    417   -344       O  
HETATM 1594  O   HOH A 430      -4.250  12.945  -6.514  1.00 25.23           O  
ANISOU 1594  O   HOH A 430     2398   4337   2853   -801    221  -1374       O  
HETATM 1595  O   HOH A 431      13.165  10.296  -4.637  1.00 24.60           O  
ANISOU 1595  O   HOH A 431     2793   3856   2697    467     52    243       O  
HETATM 1596  O   HOH A 432       0.072  16.708  11.538  1.00 26.15           O  
ANISOU 1596  O   HOH A 432     3570   4230   2135   1394   -130    120       O  
HETATM 1597  O   HOH A 433       4.437  13.220  -6.398  1.00 27.37           O  
ANISOU 1597  O   HOH A 433     3148   4207   3043   1046    549   1061       O  
HETATM 1598  O   HOH A 434     -10.414  22.499   1.635  1.00 26.41           O  
ANISOU 1598  O   HOH A 434     2922   4147   2967   1054    861    788       O  
HETATM 1599  O   HOH A 435       8.014  12.619  10.095  1.00 23.87           O  
ANISOU 1599  O   HOH A 435     2388   2410   4272     40    236   -174       O  
HETATM 1600  O   HOH A 436      -1.074   6.640   6.341  1.00 21.62           O  
ANISOU 1600  O   HOH A 436     2476   2780   2957    123     92    388       O  
HETATM 1601  O   HOH A 437      -7.305  15.776  -2.102  1.00 28.07           O  
ANISOU 1601  O   HOH A 437     2913   3193   4560   -455   1211  -1645       O  
HETATM 1602  O   HOH A 438       5.744  10.275  12.847  1.00 26.63           O  
ANISOU 1602  O   HOH A 438     4260   3434   2423    353   -771   -405       O  
HETATM 1603  O   HOH A 439      -4.501  11.813  -1.404  1.00 24.07           O  
ANISOU 1603  O   HOH A 439     3199   3489   2459   -358   -131    297       O  
HETATM 1604  O   HOH A 440      13.397   0.003  -6.029  1.00 27.40           O  
ANISOU 1604  O   HOH A 440     3826   4099   2486    620    194    205       O  
HETATM 1605  O   HOH A 441      10.210  32.268 -21.272  1.00 25.15           O  
ANISOU 1605  O   HOH A 441     3495   2509   3551    144    534    -58       O  
HETATM 1606  O   HOH A 442      -7.310  29.436  11.535  1.00 27.90           O  
ANISOU 1606  O   HOH A 442     4887   2831   2885   -488   1285    -80       O  
HETATM 1607  O   HOH A 443       7.439  29.105 -19.609  1.00 23.76           O  
ANISOU 1607  O   HOH A 443     3126   2864   3038   -255    226    324       O  
HETATM 1608  O   HOH A 444       2.828  11.762  -7.523  1.00 24.62           O  
ANISOU 1608  O   HOH A 444     2572   3749   3035    771    265    256       O  
HETATM 1609  O   HOH A 445      -2.761  14.802  11.081  1.00 24.57           O  
ANISOU 1609  O   HOH A 445     4389   3361   1585    160   -257    335       O  
HETATM 1610  O   HOH A 446      17.192   1.014 -12.365  1.00 27.16           O  
ANISOU 1610  O   HOH A 446     4304   3353   2663    -97  -1038   -773       O  
HETATM 1611  O   HOH A 447      -7.737  14.288  -4.172  1.00 26.00           O  
ANISOU 1611  O   HOH A 447     2185   4299   3395   -418     74      2       O  
HETATM 1612  O   HOH A 448      -9.989  28.060  -8.945  1.00 22.14           O  
ANISOU 1612  O   HOH A 448     2992   3124   2296    602    387    466       O  
HETATM 1613  O   HOH A 449      11.126  -3.322   1.734  1.00 28.53           O  
ANISOU 1613  O   HOH A 449     4071   2654   4114    237   -892   -141       O  
HETATM 1614  O   HOH A 450       9.116  19.590  10.297  1.00 31.87           O  
ANISOU 1614  O   HOH A 450     4912   3404   3792   -339    494   -646       O  
HETATM 1615  O   HOH A 451       1.702  18.723  11.740  1.00 28.98           O  
ANISOU 1615  O   HOH A 451     3989   3211   3812     41    447    802       O  
HETATM 1616  O   HOH A 452     -10.725  21.879  -6.279  1.00 30.00           O  
ANISOU 1616  O   HOH A 452     3189   5383   2827     61   -279    331       O  
HETATM 1617  O   HOH A 453      10.161  30.278  -9.660  1.00 30.70           O  
ANISOU 1617  O   HOH A 453     4668   3360   3635  -1438   -469   -352       O  
HETATM 1618  O   HOH A 454       2.855  34.697 -10.917  1.00 30.91           O  
ANISOU 1618  O   HOH A 454     4793   3234   3717   -511    328    365       O  
HETATM 1619  O   HOH A 455      -8.902  26.751   0.539  1.00 29.51           O  
ANISOU 1619  O   HOH A 455     3828   3845   3540   1527   -394   -415       O  
HETATM 1620  O   HOH A 456       1.516  20.703   9.869  1.00 27.39           O  
ANISOU 1620  O   HOH A 456     3142   4238   3028   -690   -859   1092       O  
HETATM 1621  O   HOH A 457       3.840   7.293  -7.960  1.00 36.12           O  
ANISOU 1621  O   HOH A 457     4640   5769   3315   2366  -1430     49       O  
HETATM 1622  O   HOH A 458      -9.772  28.694  -3.729  1.00 30.80           O  
ANISOU 1622  O   HOH A 458     3324   3927   4450   -238    695    687       O  
HETATM 1623  O   HOH A 459       9.022  -1.255   4.763  1.00 29.59           O  
ANISOU 1623  O   HOH A 459     4159   3517   3568   -581    481    114       O  
HETATM 1624  O   HOH A 460      11.189   5.458  -9.093  1.00 27.89           O  
ANISOU 1624  O   HOH A 460     3938   3343   3316    784   -122   -101       O  
HETATM 1625  O   HOH A 461       3.155   4.353  12.287  1.00 39.96           O  
ANISOU 1625  O   HOH A 461     6263   4564   4356   1964   -733    401       O  
HETATM 1626  O   HOH A 462      -5.724  12.000  -3.890  1.00 27.05           O  
ANISOU 1626  O   HOH A 462     3526   4307   2446   -292    114   -284       O  
HETATM 1627  O   HOH A 463       5.406  10.966  16.524  1.00 32.61           O  
ANISOU 1627  O   HOH A 463     4711   4591   3087    215   -958    423       O  
HETATM 1628  O   HOH A 464      11.003  27.396   8.922  1.00 35.11           O  
ANISOU 1628  O   HOH A 464     3612   5549   4180  -2252   -491    295       O  
HETATM 1629  O   HOH A 465       3.608  18.934  13.415  1.00 38.93           O  
ANISOU 1629  O   HOH A 465     4453   4232   6106    -51  -1065   1161       O  
HETATM 1630  O   HOH A 466       2.283  37.079 -13.280  1.00 33.03           O  
ANISOU 1630  O   HOH A 466     5297   3160   4092   -277   1208   -796       O  
HETATM 1631  O   HOH A 467      13.431  24.938  -8.856  1.00 45.07           O  
ANISOU 1631  O   HOH A 467     5431   7181   4512   -824  -1010   -661       O  
HETATM 1632  O   HOH A 468       8.400  17.974  -9.273  1.00 38.52           O  
ANISOU 1632  O   HOH A 468     4411   5677   4546    201   -806    350       O  
HETATM 1633  O   HOH A 469      -4.725   6.007   4.190  1.00 27.80           O  
ANISOU 1633  O   HOH A 469     2535   3750   4279   -465    616   -881       O  
HETATM 1634  O   HOH A 470       5.739  16.679 -13.132  1.00 32.28           O  
ANISOU 1634  O   HOH A 470     4255   5105   2903   -915   -365   -533       O  
HETATM 1635  O   HOH A 471      11.517  22.684  -8.393  1.00 33.26           O  
ANISOU 1635  O   HOH A 471     3698   4708   4232   -332    919    283       O  
HETATM 1636  O   HOH A 472      10.293  22.459  -5.336  1.00 37.71           O  
ANISOU 1636  O   HOH A 472     4761   3883   5683    -84     79    698       O  
HETATM 1637  O   HOH A 473       5.741  31.892  -9.716  1.00 31.48           O  
ANISOU 1637  O   HOH A 473     4529   3350   4082   -589   -189     81       O  
HETATM 1638  O   HOH A 474       0.271  24.341   8.576  1.00 31.86           O  
ANISOU 1638  O   HOH A 474     3732   4069   4305   -326   -227   -921       O  
HETATM 1639  O   HOH A 475      -1.519   8.681  -1.015  1.00 35.05           O  
ANISOU 1639  O   HOH A 475     5328   5233   2755   -849   -729    820       O  
HETATM 1640  O   HOH A 476      -4.577   9.680   0.404  1.00 31.15           O  
ANISOU 1640  O   HOH A 476     3890   3712   4231  -1351   -104    568       O  
HETATM 1641  O   HOH A 477      11.664  13.659   7.358  1.00 35.88           O  
ANISOU 1641  O   HOH A 477     3449   5040   5142     85  -1495   -386       O  
HETATM 1642  O   HOH A 478       2.984  23.852  11.105  1.00 39.30           O  
ANISOU 1642  O   HOH A 478     5676   5111   4146   1005   1480    188       O  
HETATM 1643  O   HOH A 479      -3.215   9.869  -5.488  1.00 35.65           O  
ANISOU 1643  O   HOH A 479     4936   4703   3908   -837    955   -522       O  
HETATM 1644  O   HOH A 480     -11.881  30.027 -16.398  1.00 30.14           O  
ANISOU 1644  O   HOH A 480     3403   3544   4505    720   -377   -134       O  
HETATM 1645  O   HOH A 481      -6.252  16.712  10.570  1.00 33.69           O  
ANISOU 1645  O   HOH A 481     4191   5913   2697    872    360   -633       O  
HETATM 1646  O   HOH A 482      17.914  12.858  -0.346  1.00 29.44           O  
ANISOU 1646  O   HOH A 482     4072   3417   3696   1264   -355    156       O  
HETATM 1647  O   HOH A 483      -2.536  24.730   8.552  1.00 34.08           O  
ANISOU 1647  O   HOH A 483     3601   3519   5830    328    527   -149       O  
HETATM 1648  O   HOH A 484      -5.470  18.966  13.155  1.00 35.59           O  
ANISOU 1648  O   HOH A 484     3934   4227   5362   -136  -1177   1583       O  
HETATM 1649  O   HOH A 485      16.784  14.207  -2.393  1.00 41.41           O  
ANISOU 1649  O   HOH A 485     4169   6692   4872  -1112   1388   1951       O  
HETATM 1650  O   HOH A 486      -0.640  37.074 -12.250  1.00 38.59           O  
ANISOU 1650  O   HOH A 486     4841   4039   5783    -32    642   -519       O  
HETATM 1651  O   HOH A 487       5.608  14.197 -11.550  1.00 45.26           O  
ANISOU 1651  O   HOH A 487     5709   5783   5703   1632   -416  -1634       O  
HETATM 1652  O   HOH A 488      11.570  23.279  -2.840  1.00 41.36           O  
ANISOU 1652  O   HOH A 488     3798   5450   6466   -277   -156   -932       O  
HETATM 1653  O   HOH A 489      12.139  30.857 -15.806  1.00 48.01           O  
ANISOU 1653  O   HOH A 489     5349   6997   5896  -1521   1645   -293       O  
HETATM 1654  O   HOH A 490      -0.902  22.273  12.542  1.00 39.65           O  
ANISOU 1654  O   HOH A 490     3945   6613   4507   -729   -642  -1434       O  
HETATM 1655  O   HOH A 491       3.214  10.176  17.789  1.00 37.95           O  
ANISOU 1655  O   HOH A 491     3804   7576   3038   1208  -1487     30       O  
HETATM 1656  O   HOH A 492      -3.623   7.204   8.465  1.00 37.03           O  
ANISOU 1656  O   HOH A 492     5276   4222   4569   -839   1313    -32       O  
HETATM 1657  O   HOH A 493      -3.356  23.172  12.262  1.00 35.82           O  
ANISOU 1657  O   HOH A 493     3651   5125   4832   -508   1067  -1798       O  
HETATM 1658  O   HOH A 494      -6.043  11.482  -8.259  1.00 42.93           O  
ANISOU 1658  O   HOH A 494     4454   5615   6241  -1158   1075    982       O  
HETATM 1659  O   HOH A 495      10.120  30.979 -19.193  1.00 41.79           O  
ANISOU 1659  O   HOH A 495     6054   4308   5516    240    631     90       O  
HETATM 1660  O   HOH A 496      12.799  21.304  -3.019  1.00 32.41           O  
ANISOU 1660  O   HOH A 496     3132   4152   5028   -719    973    286       O  
HETATM 1661  O   HOH A 497      11.212  -1.299  -6.433  1.00 38.95           O  
ANISOU 1661  O   HOH A 497     4660   5327   4813    733   -204    327       O  
HETATM 1662  O   HOH A 498       9.565  12.825  -6.053  1.00 36.50           O  
ANISOU 1662  O   HOH A 498     3872   5225   4772   -225    169   -355       O  
HETATM 1663  O   HOH A 499      -7.689  29.240   5.392  1.00 38.15           O  
ANISOU 1663  O   HOH A 499     5815   3646   5035   1030    797   -113       O  
HETATM 1664  O   HOH A 500       0.417   3.538   1.544  1.00 43.02           O  
ANISOU 1664  O   HOH A 500     5164   6877   4306  -1012    286   2027       O  
HETATM 1665  O   HOH A 501       1.930  29.344   3.616  1.00 40.37           O  
ANISOU 1665  O   HOH A 501     4570   4748   6022    868   -823   -646       O  
HETATM 1666  O   HOH A 502       9.492  19.499  -7.407  1.00 38.81           O  
ANISOU 1666  O   HOH A 502     6032   4792   3923  -1646     22    551       O  
HETATM 1667  O   HOH A 503       9.163   7.185  12.199  1.00 28.79           O  
ANISOU 1667  O   HOH A 503     3259   3771   3907   1153    139     78       O  
HETATM 1668  O   HOH A 504      -1.528   5.246   8.591  1.00 33.29           O  
ANISOU 1668  O   HOH A 504     3405   5235   4007    518    436   1108       O  
HETATM 1669  O   HOH A 505      10.472  28.546   3.103  1.00 43.91           O  
ANISOU 1669  O   HOH A 505     7112   5133   4441    172    687   -627       O  
HETATM 1670  O   HOH A 506       3.153   9.812  -6.136  1.00 36.69           O  
ANISOU 1670  O   HOH A 506     4754   4343   4843   1099    170   -189       O  
HETATM 1671  O   HOH A 507      -2.149  37.034  -7.722  1.00 49.67           O  
ANISOU 1671  O   HOH A 507     6415   5470   6988    -25    858    217       O  
HETATM 1672  O   HOH A 508      11.106  21.195 -10.709  1.00 61.63           O  
ANISOU 1672  O   HOH A 508     7451   8376   7591   -728   -172   -284       O  
HETATM 1673  O   HOH A 509      12.716  28.154 -10.058  1.00 39.31           O  
ANISOU 1673  O   HOH A 509     4526   4871   5537  -1476     12   -342       O  
HETATM 1674  O   HOH A 510      -1.795   6.167  -4.993  1.00 40.86           O  
ANISOU 1674  O   HOH A 510     4156   6135   5232   -510   -934   1187       O  
HETATM 1675  O   HOH A 511      -2.424   3.314  15.497  1.00 49.02           O  
ANISOU 1675  O   HOH A 511     7170   6171   5284  -1862    384  -1204       O  
HETATM 1676  O   HOH A 512     -11.417  10.018   8.696  1.00 42.66           O  
ANISOU 1676  O   HOH A 512     4791   5850   5569  -1166   1241   1054       O  
HETATM 1677  O   HOH A 513       5.292  32.030  -2.014  1.00 37.94           O  
ANISOU 1677  O   HOH A 513     5782   4482   4149    610    215   -611       O  
HETATM 1678  O   HOH A 514      10.185  10.481  -4.834  1.00 57.27           O  
ANISOU 1678  O   HOH A 514     7439   7631   6691    619    710    481       O  
HETATM 1679  O   HOH A 515       4.146   2.187  10.348  1.00 48.44           O  
ANISOU 1679  O   HOH A 515     5118   6366   6923   -172   -265   2491       O  
HETATM 1680  O   HOH A 516     -11.233  28.454  -5.689  1.00 47.74           O  
ANISOU 1680  O   HOH A 516     4971   6734   6432    121  -1074    105       O  
HETATM 1681  O   HOH A 517       4.641  31.364  -7.699  1.00 41.17           O  
ANISOU 1681  O   HOH A 517     5232   5685   4724    356   -505   -513       O  
HETATM 1682  O   HOH A 518       7.139  12.714  -6.821  1.00 57.29           O  
ANISOU 1682  O   HOH A 518     7170   8349   6249    814    985  -1779       O  
HETATM 1683  O   HOH A 519       8.312  -2.561  -0.223  1.00 42.68           O  
ANISOU 1683  O   HOH A 519     7155   4232   4828    -91  -1249     18       O  
HETATM 1684  O   HOH A 520      12.872  26.411  -4.332  1.00 50.15           O  
ANISOU 1684  O   HOH A 520     4704   6740   7611   -533   -854   -274       O  
HETATM 1685  O   HOH A 521      -4.359   5.706   1.348  1.00 36.82           O  
ANISOU 1685  O   HOH A 521     3421   4508   6061   -135   -366  -1075       O  
HETATM 1686  O   HOH A 522      17.669  14.416   3.756  1.00 47.43           O  
ANISOU 1686  O   HOH A 522     5952   5285   6785   -832    270    935       O  
HETATM 1687  O   HOH A 523      10.046  16.078  -7.640  1.00 59.78           O  
ANISOU 1687  O   HOH A 523     8123   6578   8014   -434  -1106   -556       O  
HETATM 1688  O   HOH A 524       6.948  -1.921   3.430  1.00 39.01           O  
ANISOU 1688  O   HOH A 524     5634   4496   4694    622     84   -484       O  
HETATM 1689  O   HOH A 525       6.549  -0.693   1.290  1.00 39.55           O  
ANISOU 1689  O   HOH A 525     5783   4961   4285  -1269   -606   -204       O  
HETATM 1690  O   HOH A 526       9.556   8.713  -7.132  1.00 43.57           O  
ANISOU 1690  O   HOH A 526     6505   5303   4745   -562    428   -822       O  
HETATM 1691  O   HOH A 527       1.494   3.307  -3.583  1.00 45.01           O  
ANISOU 1691  O   HOH A 527     5868   5301   5933   -655    -84   -841       O  
HETATM 1692  O   HOH A 528      -8.972  25.445   7.552  1.00 34.11           O  
ANISOU 1692  O   HOH A 528     4707   6258   1996    -55    107    675       O  
HETATM 1693  O   HOH A 529     -12.915  13.301   7.752  1.00 49.20           O  
ANISOU 1693  O   HOH A 529     5779   6072   6842    914   -374  -1276       O  
HETATM 1694  O   HOH A 530      11.257  19.652  12.356  1.00 41.95           O  
ANISOU 1694  O   HOH A 530     5613   5057   5271   -958   -227    709       O  
HETATM 1695  O   HOH A 531       3.126  31.812  -1.311  1.00 52.46           O  
ANISOU 1695  O   HOH A 531     8693   5413   5826    874   -246   -757       O  
HETATM 1696  O   HOH A 532       3.637  13.222 -14.868  1.00 36.92           O  
ANISOU 1696  O   HOH A 532     5223   5110   3695    816    409    803       O  
HETATM 1697  O   HOH A 533       3.828  31.082   9.938  1.00 84.08           O  
ANISOU 1697  O   HOH A 533    11024  10576  10346   -143   -236   -142       O  
HETATM 1698  O   HOH A 534       0.707   0.281   4.036  1.00 64.83           O  
ANISOU 1698  O   HOH A 534     9042   7582   8008   -596   -266  -1706       O  
HETATM 1699  O   HOH A 535      -4.784  35.638  -3.486  1.00 49.20           O  
ANISOU 1699  O   HOH A 535     6841   6147   5705     13   1063  -1996       O  
HETATM 1700  O   HOH A 536       6.732   9.963  -8.174  1.00 45.57           O  
ANISOU 1700  O   HOH A 536     6849   5901   4565   1526    492    -14       O  
HETATM 1701  O   HOH A 537      -6.014  33.039  -2.770  1.00 54.58           O  
ANISOU 1701  O   HOH A 537     8280   6940   5518  -2144   -153    897       O  
HETATM 1702  O   HOH A 538       3.481  32.743  -6.050  1.00 47.55           O  
ANISOU 1702  O   HOH A 538     5996   5204   6867   -385    359   -493       O  
HETATM 1703  O   HOH A 539       4.255  -0.705   0.960  1.00 45.40           O  
ANISOU 1703  O   HOH A 539     5518   6353   5376    710    632    437       O  
HETATM 1704  O   HOH A 540      13.472   6.194 -12.407  1.00 40.42           O  
ANISOU 1704  O   HOH A 540     4943   4975   5438   -230    227   -128       O  
HETATM 1705  O   HOH A 541      11.793  -1.486  -3.241  1.00 48.11           O  
ANISOU 1705  O   HOH A 541     6803   6024   5453   1449  -1141    669       O  
HETATM 1706  O   HOH A 542      -9.670  26.326   3.301  1.00 55.29           O  
ANISOU 1706  O   HOH A 542     7358   5634   8016    752   -478    422       O  
HETATM 1707  O   HOH A 543      -1.812  30.985  10.388  1.00 86.78           O  
ANISOU 1707  O   HOH A 543    11050  11092  10828   -331   -251   -793       O  
HETATM 1708  O   HOH A 544     -12.442  22.649  -8.197  1.00 66.07           O  
ANISOU 1708  O   HOH A 544     8850   8470   7783   -410   -120  -1500       O  
HETATM 1709  O   HOH A 545       1.304  35.276  -8.630  1.00 44.69           O  
ANISOU 1709  O   HOH A 545     6792   4317   5871   -595    340   -233       O  
HETATM 1710  O   HOH A 546     -13.192  10.505  10.480  1.00 44.67           O  
ANISOU 1710  O   HOH A 546     5165   5692   6115   1382    284  -1008       O  
HETATM 1711  O   HOH A 547      13.032  16.184   8.938  1.00 72.01           O  
ANISOU 1711  O   HOH A 547     8869   9696   8796   -701    459    247       O  
HETATM 1712  O   HOH A 548       7.480  10.241 -10.575  1.00100.81           O  
ANISOU 1712  O   HOH A 548    13082  12683  12540    597    305    242       O  
HETATM 1713  O   HOH A 549       5.155  33.608 -11.423  1.00 39.59           O  
ANISOU 1713  O   HOH A 549     4917   5487   4638   -854   -514   1246       O  
HETATM 1714  O   HOH A 550     -10.251  30.729  -8.524  1.00 48.85           O  
ANISOU 1714  O   HOH A 550     5914   5114   7533    483    911   1442       O  
HETATM 1715  O   HOH A 551       2.441  -2.137   2.793  1.00 59.02           O  
ANISOU 1715  O   HOH A 551     7380   6610   8436   -609   -661   -128       O  
HETATM 1716  O   HOH A 552       5.421  36.820  -9.952  1.00 49.53           O  
ANISOU 1716  O   HOH A 552     6937   6558   5323    873    372    932       O  
HETATM 1717  O   HOH A 553       7.795  15.050 -10.178  1.00 70.12           O  
ANISOU 1717  O   HOH A 553     8506   8386   9752   1532   -343    249       O  
HETATM 1718  O   HOH A 554      -2.170  40.311 -14.273  1.00 51.17           O  
ANISOU 1718  O   HOH A 554     6322   6016   7103    375   1397   1578       O  
HETATM 1719  O   HOH A 555      12.158   8.023 -12.857  1.00 53.98           O  
ANISOU 1719  O   HOH A 555     7251   6199   7060   -503     96  -1985       O  
HETATM 1720  O   HOH A 556      -5.412   5.523  10.203  1.00 45.03           O  
ANISOU 1720  O   HOH A 556     5008   5657   6444    433  -2265   1398       O  
HETATM 1721  O   HOH A 557      -9.891  10.259  10.652  1.00 46.36           O  
ANISOU 1721  O   HOH A 557     6686   5654   5276   -574   1252   2314       O  
HETATM 1722  O   HOH A 558      15.637  17.596  -2.352  1.00 57.94           O  
ANISOU 1722  O   HOH A 558     6845   8649   6521   -937    686    264       O  
HETATM 1723  O   HOH A 559      -0.771   3.414  10.560  1.00 49.61           O  
ANISOU 1723  O   HOH A 559     5631   6573   6645  -1821    935   1391       O  
HETATM 1724  O   HOH A 560      -6.900   6.608  13.908  1.00 41.29           O  
ANISOU 1724  O   HOH A 560     5954   5770   3962    721    125    389       O  
HETATM 1725  O   HOH A 561      13.592  20.092 -12.079  1.00 46.46           O  
ANISOU 1725  O   HOH A 561     5907   4583   7164   1294   -187     -9       O  
HETATM 1726  O   HOH A 562      -1.198   8.319  -7.310  1.00 47.99           O  
ANISOU 1726  O   HOH A 562     7390   4664   6182    110   1227   -515       O  
HETATM 1727  O   HOH A 563       0.056  30.705   3.908  1.00 45.13           O  
ANISOU 1727  O   HOH A 563     5887   5639   5620   -620    893    364       O  
HETATM 1728  O   HOH A 564       1.627   2.212  10.579  1.00 38.01           O  
ANISOU 1728  O   HOH A 564     5354   4526   4563    558    468   1032       O  
HETATM 1729  O   HOH A 565     -11.988  24.873  -7.847  1.00 53.30           O  
ANISOU 1729  O   HOH A 565     7972   6983   5294    434   1675    956       O  
HETATM 1730  O   HOH A 566      14.913  22.018  -4.503  1.00 48.64           O  
ANISOU 1730  O   HOH A 566     3920   6805   7757     -5    273    235       O  
HETATM 1731  O   HOH A 567      -0.269  27.213   9.449  1.00 47.77           O  
ANISOU 1731  O   HOH A 567     6623   7301   4227   -611   1393  -1230       O  
HETATM 1732  O   HOH A 568       1.094   3.639  15.106  1.00 55.32           O  
ANISOU 1732  O   HOH A 568     7689   6853   6477   1448    616  -2193       O  
HETATM 1733  O   HOH A 569      -4.413  40.232 -16.975  1.00 45.30           O  
ANISOU 1733  O   HOH A 569     5801   6297   5114    714    936   -437       O  
HETATM 1734  O   HOH A 570      -5.502  10.205 -10.090  1.00 55.80           O  
ANISOU 1734  O   HOH A 570     6773   6703   7726  -2049   -230   -520       O  
HETATM 1735  O   HOH A 571       8.376  31.121  -7.214  1.00 36.96           O  
ANISOU 1735  O   HOH A 571     4978   4180   4885    355   1230    888       O  
HETATM 1736  O   HOH A 572       4.564  -3.795  -8.899  1.00 53.74           O  
ANISOU 1736  O   HOH A 572     6894   6778   6747   -849   -711  -1396       O  
HETATM 1737  O   HOH A 573      -7.880   5.553  10.862  1.00 48.47           O  
ANISOU 1737  O   HOH A 573     6294   5347   6774    673   1211    603       O  
HETATM 1738  O   HOH A 574       7.457   8.906 -14.796  1.00 46.16           O  
ANISOU 1738  O   HOH A 574     4980   6192   6365   -752    400   -573       O  
HETATM 1739  O   HOH A 575       6.799  33.758  -2.008  1.00 57.47           O  
ANISOU 1739  O   HOH A 575     8400   6644   6792   -508    668   -107       O  
HETATM 1740  O   HOH A 576       3.654  -2.077   6.385  1.00 61.89           O  
ANISOU 1740  O   HOH A 576     7950   7985   7580    425   -203    194       O  
HETATM 1741  O   HOH A 577       5.474  -3.695  -6.405  1.00 62.79           O  
ANISOU 1741  O   HOH A 577     8532   8528   6799    252   1924   -315       O  
HETATM 1742  O   HOH A 578       5.604   1.627  12.441  1.00 71.23           O  
ANISOU 1742  O   HOH A 578     9370   9141   8556   -348    192   1263       O  
HETATM 1743  O   HOH A 579       2.560  34.399  -4.399  1.00 64.47           O  
ANISOU 1743  O   HOH A 579     7090   9222   8184    248   1122    -85       O  
HETATM 1744  O   HOH A 580       3.854  -0.103  13.651  1.00 48.88           O  
ANISOU 1744  O   HOH A 580     6295   6374   5903   1047   1889   -176       O  
HETATM 1745  O   HOH A 581      13.191   5.884 -10.152  1.00 55.87           O  
ANISOU 1745  O   HOH A 581     6960   7547   6719    -85    245  -1062       O  
HETATM 1746  O   HOH A 582      15.830  13.924   2.287  1.00 67.36           O  
ANISOU 1746  O   HOH A 582     7322   9470   8800    836   -863   -647       O  
HETATM 1747  O   HOH A 583       4.271  -2.999  -0.861  1.00 50.62           O  
ANISOU 1747  O   HOH A 583     6630   6237   6366  -1678    160    428       O  
HETATM 1748  O   HOH A 584       3.679  -0.771  -6.226  1.00 46.59           O  
ANISOU 1748  O   HOH A 584     6341   6813   4549   -449   1348    -40       O  
HETATM 1749  O   HOH A 585       3.589  38.239 -11.432  1.00 55.00           O  
ANISOU 1749  O   HOH A 585     6793   7120   6984   -147    721    112       O  
HETATM 1750  O   HOH A 586      14.945  20.226   7.907  1.00 58.22           O  
ANISOU 1750  O   HOH A 586     7714   7625   6782  -1494    421   -701       O  
HETATM 1751  O   HOH A 587       2.464  32.676   3.003  1.00 46.59           O  
ANISOU 1751  O   HOH A 587     7071   5027   5605  -1213    188   -145       O  
HETATM 1752  O   HOH A 588       1.956  -0.173   8.090  1.00 54.35           O  
ANISOU 1752  O   HOH A 588     6570   5988   8091     24    240    835       O  
HETATM 1753  O   HOH A 589      18.185  20.287   6.331  1.00 64.63           O  
ANISOU 1753  O   HOH A 589     8875   8654   7028   -364   -570  -2062       O  
HETATM 1754  O   HOH A 590      14.756   4.955 -13.852  1.00 54.64           O  
ANISOU 1754  O   HOH A 590     6450   7358   6952  -2283    -88  -1197       O  
HETATM 1755  O   HOH A 591      18.831  17.011   8.109  1.00 65.59           O  
ANISOU 1755  O   HOH A 591     9265   7078   8578   -581   1479   1337       O  
HETATM 1756  O   HOH A 592       2.324   5.355  -6.003  1.00 40.96           O  
ANISOU 1756  O   HOH A 592     5588   5163   4811   -149   -346   -843       O  
HETATM 1757  O   HOH A 593      -8.413  31.804  -2.734  1.00 48.51           O  
ANISOU 1757  O   HOH A 593     8079   5663   4690   -756   1527    259       O  
HETATM 1758  O   HOH A 594       5.463  35.170  -6.388  1.00 55.75           O  
ANISOU 1758  O   HOH A 594     7730   7406   6046    230    349   -898       O  
HETATM 1759  O   HOH A 595      11.116  36.879 -10.456  1.00 55.20           O  
ANISOU 1759  O   HOH A 595     7041   7407   6524   -442   -595   -306       O  
HETATM 1760  O   HOH B 402     -11.203  16.934 -12.207  1.00 14.81           O  
ANISOU 1760  O   HOH B 402     1933   1992   1702   -321   -585     -1       O  
HETATM 1761  O   HOH B 403       6.593  30.208 -28.106  1.00 18.90           O  
ANISOU 1761  O   HOH B 403     2267   2207   2706    130    342    -24       O  
HETATM 1762  O   HOH B 404       9.312  22.261 -25.306  1.00 13.82           O  
ANISOU 1762  O   HOH B 404     2079   1795   1377    156    350    200       O  
HETATM 1763  O   HOH B 405       1.913  31.393 -29.483  1.00 14.39           O  
ANISOU 1763  O   HOH B 405     1995   1910   1563     -3    126     12       O  
HETATM 1764  O   HOH B 406     -13.850  21.367  -6.733  1.00 16.63           O  
ANISOU 1764  O   HOH B 406     1454   2471   2394    -69    280   -636       O  
HETATM 1765  O   HOH B 407      -1.477  10.214 -27.698  1.00 17.39           O  
ANISOU 1765  O   HOH B 407     2585   1971   2052   -160    208   -105       O  
HETATM 1766  O   HOH B 408       9.495   9.581 -30.448  1.00 20.11           O  
ANISOU 1766  O   HOH B 408     2432   2420   2788    -35    978   -450       O  
HETATM 1767  O   HOH B 409       8.268  21.426 -37.426  1.00 16.30           O  
ANISOU 1767  O   HOH B 409     2455   1992   1747    -91     41    208       O  
HETATM 1768  O   HOH B 410      21.513  20.165 -24.673  1.00 21.63           O  
ANISOU 1768  O   HOH B 410     3322   2381   2514  -1149   -712    426       O  
HETATM 1769  O   HOH B 411      11.598  22.449 -38.062  1.00 14.02           O  
ANISOU 1769  O   HOH B 411     2318   1914   1094    422    255    121       O  
HETATM 1770  O   HOH B 412       7.849  23.970 -13.578  1.00 17.59           O  
ANISOU 1770  O   HOH B 412     2320   2345   2018   -381   -178    528       O  
HETATM 1771  O   HOH B 413      13.378  23.964 -35.361  1.00 16.60           O  
ANISOU 1771  O   HOH B 413     2460   2196   1653     34    592    155       O  
HETATM 1772  O   HOH B 414      10.006  28.012 -30.368  1.00 17.05           O  
ANISOU 1772  O   HOH B 414     2942   2240   1296   -273     41     -4       O  
HETATM 1773  O   HOH B 415      14.212   7.531 -22.472  1.00 19.63           O  
ANISOU 1773  O   HOH B 415     3117   2111   2230    -73    641   -179       O  
HETATM 1774  O   HOH B 416      11.140  20.109 -15.981  1.00 18.31           O  
ANISOU 1774  O   HOH B 416     2230   2597   2130    197    -28    411       O  
HETATM 1775  O   HOH B 417       9.733  23.519 -36.300  1.00 17.43           O  
ANISOU 1775  O   HOH B 417     2704   2148   1772    -47    388   -134       O  
HETATM 1776  O   HOH B 418      -7.954  17.492 -14.631  1.00 20.96           O  
ANISOU 1776  O   HOH B 418     2919   2853   2191   -247    443    -67       O  
HETATM 1777  O   HOH B 419       1.080  31.578 -17.756  1.00 17.61           O  
ANISOU 1777  O   HOH B 419     2466   2316   1908    133   -284    139       O  
HETATM 1778  O   HOH B 420      -6.701  10.526 -13.400  1.00 25.62           O  
ANISOU 1778  O   HOH B 420     3058   1835   4842   -835    -66    133       O  
HETATM 1779  O   HOH B 421      12.659  12.404 -32.017  1.00 20.53           O  
ANISOU 1779  O   HOH B 421     2847   2395   2559   -268    799   -485       O  
HETATM 1780  O   HOH B 422      15.780  13.722 -14.496  1.00 24.64           O  
ANISOU 1780  O   HOH B 422     2404   5083   1876    385   -399   1239       O  
HETATM 1781  O   HOH B 423      10.362   7.117 -21.735  1.00 21.34           O  
ANISOU 1781  O   HOH B 423     3019   2317   2772    756    402    828       O  
HETATM 1782  O   HOH B 424      23.284   7.256 -17.900  1.00 23.96           O  
ANISOU 1782  O   HOH B 424     2879   3676   2548    318     -9   -879       O  
HETATM 1783  O   HOH B 425      10.951  24.296 -24.347  1.00 24.51           O  
ANISOU 1783  O   HOH B 425     3287   3607   2419  -1366   -506    526       O  
HETATM 1784  O   HOH B 426       9.909  22.145 -13.585  1.00 21.32           O  
ANISOU 1784  O   HOH B 426     2309   3135   2656    277    118    391       O  
HETATM 1785  O   HOH B 427      16.590  27.216 -30.585  1.00 25.87           O  
ANISOU 1785  O   HOH B 427     3733   2447   3651    -75   -827    379       O  
HETATM 1786  O   HOH B 428      10.650  27.081 -24.994  1.00 23.81           O  
ANISOU 1786  O   HOH B 428     3551   3125   2370   -703    384   -140       O  
HETATM 1787  O   HOH B 429       5.942  22.474 -37.924  1.00 26.13           O  
ANISOU 1787  O   HOH B 429     3640   3907   2381   1667    133     47       O  
HETATM 1788  O   HOH B 430       9.500  26.810 -19.871  1.00 26.34           O  
ANISOU 1788  O   HOH B 430     4368   2652   2987   -966  -1032    328       O  
HETATM 1789  O   HOH B 431       0.152  32.970 -27.990  1.00 26.41           O  
ANISOU 1789  O   HOH B 431     3962   3100   2971    772    328    914       O  
HETATM 1790  O   HOH B 432      -5.580  32.527 -17.368  1.00 22.53           O  
ANISOU 1790  O   HOH B 432     2996   2982   2583    456    554    750       O  
HETATM 1791  O   HOH B 433      -7.741  12.363 -16.726  1.00 28.07           O  
ANISOU 1791  O   HOH B 433     3068   4197   3401  -1030   -224   -323       O  
HETATM 1792  O   HOH B 434       9.139  18.045 -19.974  1.00 28.34           O  
ANISOU 1792  O   HOH B 434     4450   2489   3829    406   1534   -201       O  
HETATM 1793  O   HOH B 435      -0.824  27.295 -34.302  1.00 20.80           O  
ANISOU 1793  O   HOH B 435     2937   2688   2278    129   -377   -246       O  
HETATM 1794  O   HOH B 436       9.924  14.495 -36.393  1.00 24.58           O  
ANISOU 1794  O   HOH B 436     2633   2206   4500   -122   -583    777       O  
HETATM 1795  O   HOH B 437      12.223   9.317 -21.729  1.00 25.12           O  
ANISOU 1795  O   HOH B 437     3801   2623   3121    459    311     99       O  
HETATM 1796  O   HOH B 438      22.507   9.058 -20.317  1.00 24.72           O  
ANISOU 1796  O   HOH B 438     3203   3357   2832     16   -283     46       O  
HETATM 1797  O   HOH B 439      -6.609  15.098  -6.760  1.00 24.35           O  
ANISOU 1797  O   HOH B 439     2895   3460   2896   -286    -42    159       O  
HETATM 1798  O   HOH B 440       8.266  30.218 -22.195  1.00 28.90           O  
ANISOU 1798  O   HOH B 440     5184   2302   3494   -166    376    462       O  
HETATM 1799  O   HOH B 441      10.631  19.556 -18.898  1.00 25.34           O  
ANISOU 1799  O   HOH B 441     3472   2972   3185    977    664    381       O  
HETATM 1800  O   HOH B 442      18.328  19.631 -38.686  1.00 39.04           O  
ANISOU 1800  O   HOH B 442     4765   5842   4226   1297    112   -323       O  
HETATM 1801  O   HOH B 443      21.544   5.444 -14.076  1.00 28.47           O  
ANISOU 1801  O   HOH B 443     3497   4079   3241   -394   -541  -1272       O  
HETATM 1802  O   HOH B 444      15.884  23.663 -32.597  1.00 22.95           O  
ANISOU 1802  O   HOH B 444     3285   2545   2890     37    520    205       O  
HETATM 1803  O   HOH B 445       0.632  33.261 -20.063  1.00 26.36           O  
ANISOU 1803  O   HOH B 445     3897   3196   2922   -805     24   -139       O  
HETATM 1804  O   HOH B 446       6.739  29.796 -24.253  1.00 29.58           O  
ANISOU 1804  O   HOH B 446     3852   2627   4759   -605  -1527   1171       O  
HETATM 1805  O   HOH B 447      -6.152  32.356 -22.593  1.00 28.39           O  
ANISOU 1805  O   HOH B 447     3509   3227   4052    651    676   1005       O  
HETATM 1806  O   HOH B 448      12.227  16.686 -39.079  1.00 27.84           O  
ANISOU 1806  O   HOH B 448     3120   4788   2670   -378    409  -1236       O  
HETATM 1807  O   HOH B 449       2.899  13.306 -36.710  1.00 38.17           O  
ANISOU 1807  O   HOH B 449     4220   5703   4580   -315   -579   1068       O  
HETATM 1808  O   HOH B 450       7.798  25.387 -37.388  1.00 26.47           O  
ANISOU 1808  O   HOH B 450     3770   4392   1895    226   -273   -663       O  
HETATM 1809  O   HOH B 451      25.836  11.419 -28.183  1.00 31.78           O  
ANISOU 1809  O   HOH B 451     3505   4424   4145   -222   -163  -1042       O  
HETATM 1810  O   HOH B 452       3.808  20.814 -38.117  1.00 27.76           O  
ANISOU 1810  O   HOH B 452     3244   3696   3607    263     87    584       O  
HETATM 1811  O   HOH B 453     -12.099  19.856 -15.431  1.00 31.66           O  
ANISOU 1811  O   HOH B 453     3752   4892   3384  -1085   -489    410       O  
HETATM 1812  O   HOH B 454      -4.163  31.550 -26.907  1.00 30.85           O  
ANISOU 1812  O   HOH B 454     3386   4355   3979    646     46   -138       O  
HETATM 1813  O   HOH B 455       1.937  20.957 -36.144  1.00 26.41           O  
ANISOU 1813  O   HOH B 455     3861   3227   2947   -500    348   -684       O  
HETATM 1814  O   HOH B 456      -9.787  12.289  -4.952  1.00 24.32           O  
ANISOU 1814  O   HOH B 456     2732   3303   3206    -86    -17     69       O  
HETATM 1815  O   HOH B 457      23.784  13.559 -31.011  1.00 28.18           O  
ANISOU 1815  O   HOH B 457     3508   3552   3648   -287    223    149       O  
HETATM 1816  O   HOH B 458      15.365  13.447 -38.548  1.00 31.69           O  
ANISOU 1816  O   HOH B 458     5064   3103   3871   1733    713    130       O  
HETATM 1817  O   HOH B 459       3.521  18.838 -39.525  1.00 37.28           O  
ANISOU 1817  O   HOH B 459     3916   5129   5120   -475    875    111       O  
HETATM 1818  O   HOH B 460      11.608  17.035 -42.769  1.00 30.44           O  
ANISOU 1818  O   HOH B 460     4238   4250   3078    272     83   -815       O  
HETATM 1819  O   HOH B 461      -9.462  16.951 -16.606  1.00 31.01           O  
ANISOU 1819  O   HOH B 461     3211   4743   3826   -483   -315   -190       O  
HETATM 1820  O   HOH B 462      17.089  11.301 -16.987  1.00 35.87           O  
ANISOU 1820  O   HOH B 462     3499   4898   5231   1309    146   -181       O  
HETATM 1821  O   HOH B 463      10.592  28.257 -22.500  1.00 24.18           O  
ANISOU 1821  O   HOH B 463     3499   3185   2503   -979    469   -239       O  
HETATM 1822  O   HOH B 464      15.335  18.897 -18.495  1.00 30.61           O  
ANISOU 1822  O   HOH B 464     4978   3858   2794   1739   -529   -942       O  
HETATM 1823  O   HOH B 465      -0.552  25.960 -38.616  1.00 40.29           O  
ANISOU 1823  O   HOH B 465     6113   3681   5513    181  -2651    392       O  
HETATM 1824  O   HOH B 466       8.658   5.780 -23.702  1.00 35.91           O  
ANISOU 1824  O   HOH B 466     6057   3454   4132   -202    550    806       O  
HETATM 1825  O   HOH B 467      -1.477  19.886 -37.245  1.00 38.80           O  
ANISOU 1825  O   HOH B 467     4680   6450   3614    367    402   1206       O  
HETATM 1826  O   HOH B 468       5.476  28.705 -36.985  1.00 36.22           O  
ANISOU 1826  O   HOH B 468     6042   4252   3468   1179   -135   -368       O  
HETATM 1827  O   HOH B 469      13.976  23.963 -25.369  1.00 31.90           O  
ANISOU 1827  O   HOH B 469     4064   4790   3267   -150     83   -101       O  
HETATM 1828  O   HOH B 470     -14.448  20.316 -13.143  1.00 35.96           O  
ANISOU 1828  O   HOH B 470     4584   5309   3769    263   -690   1064       O  
HETATM 1829  O   HOH B 471       3.390  28.037 -39.609  1.00 41.74           O  
ANISOU 1829  O   HOH B 471     4893   5746   5220   1024   1603  -1362       O  
HETATM 1830  O   HOH B 472      -1.927  22.298 -34.984  1.00 34.71           O  
ANISOU 1830  O   HOH B 472     4934   3438   4815   -273  -1406   -614       O  
HETATM 1831  O   HOH B 473       0.154  12.151 -20.787  1.00 36.55           O  
ANISOU 1831  O   HOH B 473     4268   4411   5209   -885    517   -611       O  
HETATM 1832  O   HOH B 474       8.672  10.689 -33.549  1.00 43.43           O  
ANISOU 1832  O   HOH B 474     5771   4592   6137   1272    -76   -884       O  
HETATM 1833  O   HOH B 475     -14.604  24.899 -18.773  1.00 40.59           O  
ANISOU 1833  O   HOH B 475     3689   5975   5758    -62    330   1020       O  
HETATM 1834  O   HOH B 476      12.752  25.864 -20.764  1.00 43.26           O  
ANISOU 1834  O   HOH B 476     6176   5348   4914  -1355     38    573       O  
HETATM 1835  O   HOH B 477      -2.329  25.156 -35.363  1.00 39.36           O  
ANISOU 1835  O   HOH B 477     4465   4584   5907    655    256   -766       O  
HETATM 1836  O   HOH B 478      10.013  28.741 -18.653  1.00 38.34           O  
ANISOU 1836  O   HOH B 478     5847   4200   4520   -877   1956  -1097       O  
HETATM 1837  O   HOH B 479      -0.193  11.057 -17.852  1.00 30.28           O  
ANISOU 1837  O   HOH B 479     4775   3811   2918   -474    620   -136       O  
HETATM 1838  O   HOH B 480      12.116  19.347 -44.245  1.00 34.07           O  
ANISOU 1838  O   HOH B 480     6702   3346   2897   1162     74   -573       O  
HETATM 1839  O   HOH B 481       1.348   9.634 -23.663  1.00 32.30           O  
ANISOU 1839  O   HOH B 481     4163   3334   4777   -446    -15     67       O  
HETATM 1840  O   HOH B 482     -14.553  23.051 -13.956  1.00 34.89           O  
ANISOU 1840  O   HOH B 482     3491   4837   4930  -1149   -319    195       O  
HETATM 1841  O   HOH B 483      23.988  11.452 -19.983  1.00 35.83           O  
ANISOU 1841  O   HOH B 483     4807   4586   4220   1194   1017   -412       O  
HETATM 1842  O   HOH B 484      -7.527  34.306  -9.745  1.00 33.59           O  
ANISOU 1842  O   HOH B 484     5274   3791   3697    534    438   -222       O  
HETATM 1843  O   HOH B 485      -0.663  10.941 -23.822  1.00 39.37           O  
ANISOU 1843  O   HOH B 485     5007   4104   5846    -43    225    439       O  
HETATM 1844  O   HOH B 486      -8.506  10.765 -10.167  1.00 48.17           O  
ANISOU 1844  O   HOH B 486     6633   5420   6249  -1448    897   2608       O  
HETATM 1845  O   HOH B 487      -9.286  17.837 -24.430  1.00 36.66           O  
ANISOU 1845  O   HOH B 487     3697   6342   3889    304  -1021   -779       O  
HETATM 1846  O   HOH B 488       9.538  18.868 -11.489  1.00 38.86           O  
ANISOU 1846  O   HOH B 488     5153   4945   4667    815   1044    437       O  
HETATM 1847  O   HOH B 489       8.295  16.915 -15.123  1.00 44.35           O  
ANISOU 1847  O   HOH B 489     4132   6342   6377   1918   -792    543       O  
HETATM 1848  O   HOH B 490      15.289  26.021 -35.078  1.00 36.61           O  
ANISOU 1848  O   HOH B 490     4372   4431   5108   -858    242   1488       O  
HETATM 1849  O   HOH B 491      20.058  18.527 -37.661  1.00 37.53           O  
ANISOU 1849  O   HOH B 491     4638   4055   5565    710   1006   -323       O  
HETATM 1850  O   HOH B 492      -2.556   9.389 -17.343  1.00 40.07           O  
ANISOU 1850  O   HOH B 492     6113   5922   3190    216   -804   -987       O  
HETATM 1851  O   HOH B 493      19.045  22.351 -27.903  1.00 40.64           O  
ANISOU 1851  O   HOH B 493     6382   4385   4674  -1693   1132    -13       O  
HETATM 1852  O   HOH B 494      -4.608  11.445 -35.158  1.00 37.33           O  
ANISOU 1852  O   HOH B 494     5068   3275   5843  -1867    365   -704       O  
HETATM 1853  O   HOH B 495      -7.203  20.217 -30.233  1.00 46.75           O  
ANISOU 1853  O   HOH B 495     4808   5573   7383    338   -198    582       O  
HETATM 1854  O   HOH B 496       0.943  11.215 -15.227  1.00 43.89           O  
ANISOU 1854  O   HOH B 496     5891   5509   5275   -996    327    208       O  
HETATM 1855  O   HOH B 497       8.873  16.601 -43.756  1.00 50.03           O  
ANISOU 1855  O   HOH B 497     5500   7644   5864    138  -1690  -2074       O  
HETATM 1856  O   HOH B 498      16.524  24.208 -20.910  1.00 48.87           O  
ANISOU 1856  O   HOH B 498     6796   4592   7180    477     76   -465       O  
HETATM 1857  O   HOH B 499      -6.469  31.308 -35.586  1.00 46.01           O  
ANISOU 1857  O   HOH B 499     6451   4280   6749   1933   1676    873       O  
HETATM 1858  O   HOH B 500       4.722  14.222 -16.831  1.00 38.87           O  
ANISOU 1858  O   HOH B 500     4480   4900   5388    396    426  -1037       O  
HETATM 1859  O   HOH B 501      17.480  24.146 -34.900  1.00 35.00           O  
ANISOU 1859  O   HOH B 501     5129   4243   3925     24   1173   -125       O  
HETATM 1860  O   HOH B 502      -2.942  31.662 -33.938  1.00 32.24           O  
ANISOU 1860  O   HOH B 502     5040   4575   2635   -367   1181    362       O  
HETATM 1861  O   HOH B 503      19.730  23.266 -36.406  1.00 58.24           O  
ANISOU 1861  O   HOH B 503     7866   6444   7820  -1721    645    578       O  
HETATM 1862  O   HOH B 504       9.453  15.504 -19.172  1.00 41.67           O  
ANISOU 1862  O   HOH B 504     6624   4686   4521    519   -378    432       O  
HETATM 1863  O   HOH B 505      16.713  26.823 -27.572  1.00 38.16           O  
ANISOU 1863  O   HOH B 505     5481   2704   6313   -295  -1239   -113       O  
HETATM 1864  O   HOH B 506      10.938  30.842 -39.698  1.00 47.29           O  
ANISOU 1864  O   HOH B 506     6981   5838   5150    758   1249   -193       O  
HETATM 1865  O   HOH B 507      25.154  14.220 -26.161  1.00 41.40           O  
ANISOU 1865  O   HOH B 507     4003   6653   5076     38     16   -600       O  
HETATM 1866  O   HOH B 508      21.764  16.462 -37.256  1.00 44.46           O  
ANISOU 1866  O   HOH B 508     5749   5992   5152  -2482    821   1031       O  
HETATM 1867  O   HOH B 509       9.472  13.212 -20.452  1.00 49.30           O  
ANISOU 1867  O   HOH B 509     6900   5734   6097    785   -901    -84       O  
HETATM 1868  O   HOH B 510     -10.059  17.217 -21.519  1.00 50.28           O  
ANISOU 1868  O   HOH B 510     6358   7000   5745    540   -421    357       O  
HETATM 1869  O   HOH B 511      -8.963  17.712 -18.790  1.00 55.19           O  
ANISOU 1869  O   HOH B 511     6738   7127   7105    201   -293    182       O  
HETATM 1870  O   HOH B 512      17.420   7.669 -12.468  1.00 49.69           O  
ANISOU 1870  O   HOH B 512     7235   6211   5434   -772   -355   -787       O  
HETATM 1871  O   HOH B 513      11.933  12.089 -21.724  1.00 41.31           O  
ANISOU 1871  O   HOH B 513     5099   4565   6033   -453   1260    964       O  
HETATM 1872  O   HOH B 514      -2.303  35.031 -18.856  1.00 60.45           O  
ANISOU 1872  O   HOH B 514     8278   7380   7312  -1559    473    435       O  
HETATM 1873  O   HOH B 515      16.383   9.689 -15.223  1.00 52.55           O  
ANISOU 1873  O   HOH B 515     5123   7621   7224    500    857    627       O  
HETATM 1874  O   HOH B 516      -5.887  33.809 -20.684  1.00 41.14           O  
ANISOU 1874  O   HOH B 516     5121   4640   5869    360   -399   -933       O  
HETATM 1875  O   HOH B 517      -6.809  30.213 -31.576  1.00 41.29           O  
ANISOU 1875  O   HOH B 517     4618   5891   5181   1098   -909   1587       O  
HETATM 1876  O   HOH B 518      -8.562  32.606 -18.114  1.00 40.94           O  
ANISOU 1876  O   HOH B 518     6000   3843   5712    224    490    858       O  
HETATM 1877  O   HOH B 519      22.948  15.936 -27.677  1.00 36.23           O  
ANISOU 1877  O   HOH B 519     5080   4950   3735  -1161    -43    838       O  
HETATM 1878  O   HOH B 520      -5.974  10.018 -16.251  1.00 42.01           O  
ANISOU 1878  O   HOH B 520     5354   5211   5398  -1679    442     41       O  
HETATM 1879  O   HOH B 521      12.237  15.229 -18.203  1.00 42.89           O  
ANISOU 1879  O   HOH B 521     5662   5196   5439   -207   -915  -1095       O  
HETATM 1880  O   HOH B 522      19.530  20.979 -22.691  1.00 48.44           O  
ANISOU 1880  O   HOH B 522     5131   7003   6272  -1200  -1876    724       O  
HETATM 1881  O   HOH B 523       2.881  11.203 -39.143  1.00 47.21           O  
ANISOU 1881  O   HOH B 523     6201   5770   5966   -700   -302   -480       O  
HETATM 1882  O   HOH B 524      -6.225  11.873 -29.305  1.00 47.83           O  
ANISOU 1882  O   HOH B 524     6176   7016   4982   -418   -366    431       O  
HETATM 1883  O   HOH B 525      21.990  21.085 -29.851  1.00 46.74           O  
ANISOU 1883  O   HOH B 525     4117   8162   5481   -345    571   1083       O  
HETATM 1884  O   HOH B 526      11.905  28.295 -15.753  1.00 46.55           O  
ANISOU 1884  O   HOH B 526     4485   5522   7679  -1027    172    754       O  
HETATM 1885  O   HOH B 527      18.982  26.999 -44.362  1.00 48.69           O  
ANISOU 1885  O   HOH B 527     5026   6826   6647   -941      6   1008       O  
HETATM 1886  O   HOH B 528      12.750  19.668 -20.113  1.00 43.90           O  
ANISOU 1886  O   HOH B 528     6299   4523   5857     71  -1144   -575       O  
HETATM 1887  O   HOH B 529      -8.433  12.164  -7.309  1.00 39.80           O  
ANISOU 1887  O   HOH B 529     4691   5170   5263    643    758   1650       O  
HETATM 1888  O   HOH B 530       8.416   4.668 -29.829  1.00 48.75           O  
ANISOU 1888  O   HOH B 530     5044   6425   7056   1001   1624   -722       O  
HETATM 1889  O   HOH B 531       7.312  14.660 -16.956  1.00 55.44           O  
ANISOU 1889  O   HOH B 531     6708   7682   6675    448    610   1523       O  
HETATM 1890  O   HOH B 532     -10.540  19.239 -19.874  1.00 48.91           O  
ANISOU 1890  O   HOH B 532     5630   6847   6105   -816   -959  -2122       O  
HETATM 1891  O   HOH B 533      12.083  15.304 -15.914  1.00 85.80           O  
ANISOU 1891  O   HOH B 533    11202  10642  10757   -375    396    591       O  
HETATM 1892  O   HOH B 534      24.200  11.211 -23.476  1.00 48.48           O  
ANISOU 1892  O   HOH B 534     5838   6845   5738    334    706   -474       O  
HETATM 1893  O   HOH B 535      23.056  18.508 -27.114  1.00 53.73           O  
ANISOU 1893  O   HOH B 535     7329   6292   6793   -115  -1182   -160       O  
HETATM 1894  O   HOH B 536       9.473   7.000 -28.559  1.00 44.52           O  
ANISOU 1894  O   HOH B 536     5536   5335   6045    109   -194     14       O  
HETATM 1895  O   HOH B 537      16.887  18.939 -41.428  1.00 51.16           O  
ANISOU 1895  O   HOH B 537     7264   5813   6359     -2   1354  -1829       O  
HETATM 1896  O   HOH B 538      16.120  29.543 -40.438  1.00 42.40           O  
ANISOU 1896  O   HOH B 538     6226   5283   4600    781     -7  -1138       O  
HETATM 1897  O   HOH B 539      -3.786  32.368 -29.880  1.00 50.25           O  
ANISOU 1897  O   HOH B 539     5807   7109   6175    944   1787  -1292       O  
HETATM 1898  O   HOH B 540       0.628  19.531 -40.111  1.00 42.45           O  
ANISOU 1898  O   HOH B 540     5978   5396   4756   -969   1100   -141       O  
HETATM 1899  O   HOH B 541      12.516  34.080 -34.733  1.00 44.40           O  
ANISOU 1899  O   HOH B 541     5972   4847   6052  -1689    692    261       O  
HETATM 1900  O   HOH B 542     -15.513  19.521 -15.556  1.00 69.05           O  
ANISOU 1900  O   HOH B 542     9270   8543   8423    -58    136    -40       O  
HETATM 1901  O   HOH B 543      -5.548  23.533 -38.020  1.00 41.58           O  
ANISOU 1901  O   HOH B 543     6427   6276   3094   -907  -1054  -1082       O  
HETATM 1902  O   HOH B 544       2.418   7.571 -22.297  1.00 51.32           O  
ANISOU 1902  O   HOH B 544     7192   6194   6115   -512  -1287   -188       O  
HETATM 1903  O   HOH B 545      -3.897   9.706 -22.516  1.00 42.60           O  
ANISOU 1903  O   HOH B 545     5366   4955   5865   -270    149  -1083       O  
HETATM 1904  O   HOH B 546       8.165  29.777 -37.927  1.00 50.67           O  
ANISOU 1904  O   HOH B 546     6859   7062   5333  -1190   -230   1401       O  
HETATM 1905  O   HOH B 547      -5.143  34.273 -23.349  1.00 56.72           O  
ANISOU 1905  O   HOH B 547     7639   7412   6500    848   -372    357       O  
HETATM 1906  O   HOH B 548      -9.273  15.085 -22.999  1.00 56.42           O  
ANISOU 1906  O   HOH B 548     7122   7072   7245  -1609    478    338       O  
HETATM 1907  O   HOH B 549      24.597  15.807 -30.495  1.00 46.56           O  
ANISOU 1907  O   HOH B 549     4713   6380   6599   1010   -467  -1066       O  
HETATM 1908  O   HOH B 550      -3.709  35.386 -21.538  1.00 53.59           O  
ANISOU 1908  O   HOH B 550     6770   6152   7438   -127  -2504   1492       O  
HETATM 1909  O   HOH B 551     -12.043  15.634 -18.935  1.00 55.01           O  
ANISOU 1909  O   HOH B 551     6164   7737   7002   -472   -983  -1219       O  
HETATM 1910  O   HOH B 552      16.241  15.052 -40.523  1.00 55.94           O  
ANISOU 1910  O   HOH B 552     7165   6697   7392  -1108    357   -965       O  
HETATM 1911  O   HOH B 553     -12.911  27.644  -8.988  1.00 47.04           O  
ANISOU 1911  O   HOH B 553     6821   5315   5737   -637   2278    189       O  
HETATM 1912  O   HOH B 554     -15.271  14.390 -16.299  1.00 48.85           O  
ANISOU 1912  O   HOH B 554     7757   6356   4447   -885    414   -278       O  
HETATM 1913  O   HOH B 555     -16.523  23.639 -16.364  1.00 82.87           O  
ANISOU 1913  O   HOH B 555    10333  10653  10500    435    697   -586       O  
HETATM 1914  O   HOH B 556      -2.180  36.885 -17.069  1.00 56.98           O  
ANISOU 1914  O   HOH B 556     7875   6827   6947    694   -944   -434       O  
HETATM 1915  O   HOH B 557      11.287  16.068 -11.290  1.00 94.02           O  
ANISOU 1915  O   HOH B 557    12053  11749  11922    -51    126    165       O  
HETATM 1916  O   HOH B 558      20.122  20.894 -36.913  1.00 33.12           O  
ANISOU 1916  O   HOH B 558     3445   5469   3672    217    481    713       O  
HETATM 1917  O   HOH B 559      20.035  22.129 -41.281  1.00 60.71           O  
ANISOU 1917  O   HOH B 559     7229   7549   8287   -301   1274   -442       O  
HETATM 1918  O   HOH B 560       0.789   6.140 -15.798  1.00 42.93           O  
ANISOU 1918  O   HOH B 560     5035   4994   6282   -116   -915    134       O  
HETATM 1919  O   HOH B 561      16.736  24.448 -25.477  1.00 42.56           O  
ANISOU 1919  O   HOH B 561     6200   5352   4619   -402   -261    362       O  
HETATM 1920  O   HOH B 562      17.211  19.911 -20.060  1.00 42.19           O  
ANISOU 1920  O   HOH B 562     6269   5221   4539   -219    477   -743       O  
HETATM 1921  O   HOH B 563      -6.594  35.548  -7.352  1.00 47.07           O  
ANISOU 1921  O   HOH B 563     6138   5552   6195    716   1323  -2783       O  
HETATM 1922  O   HOH B 564      10.733  17.835 -15.865  1.00 74.77           O  
ANISOU 1922  O   HOH B 564     8964  10074   9369    634    674      3       O  
HETATM 1923  O   HOH B 565      -8.035  19.454 -38.117  1.00 55.60           O  
ANISOU 1923  O   HOH B 565     6682   7734   6708   -685   -825   -567       O  
HETATM 1924  O   HOH B 566       2.842   8.348 -12.347  1.00 87.03           O  
ANISOU 1924  O   HOH B 566    10553  11173  11343    461    113  -1162       O  
HETATM 1925  O   HOH B 567      23.012  15.155 -34.502  1.00 57.25           O  
ANISOU 1925  O   HOH B 567     5930   7747   8077  -1444  -1087    323       O  
HETATM 1926  O   HOH B 568      -4.918  37.922 -19.889  1.00 44.74           O  
ANISOU 1926  O   HOH B 568     5256   6564   5178    608    829   -444       O  
HETATM 1927  O   HOH B 569     -12.758  20.626 -17.960  1.00 53.79           O  
ANISOU 1927  O   HOH B 569     5578   7027   7831   -531   1664    257       O  
HETATM 1928  O   HOH B 570      22.530  20.853 -34.487  1.00 50.98           O  
ANISOU 1928  O   HOH B 570     6056   7628   5687    -79    629   2043       O  
HETATM 1929  O   HOH B 571     -13.035  30.592 -10.307  1.00 48.22           O  
ANISOU 1929  O   HOH B 571     6431   5805   6085   1403  -1004    746       O  
HETATM 1930  O   HOH B 572      -9.609  25.347 -34.444  1.00 65.77           O  
ANISOU 1930  O   HOH B 572     7864   8223   8904     87    161    747       O  
HETATM 1931  O   HOH B 573       6.616  12.227 -18.390  1.00 59.11           O  
ANISOU 1931  O   HOH B 573     7176   7447   7837   -143   -289  -1011       O  
HETATM 1932  O   HOH B 574       0.668  14.030 -40.037  1.00 52.38           O  
ANISOU 1932  O   HOH B 574     7713   7879   4310   1230   -751   -680       O  
HETATM 1933  O   HOH B 575       7.609  13.469 -15.027  1.00 50.45           O  
ANISOU 1933  O   HOH B 575     6177   7418   5573    317    361    831       O  
HETATM 1934  O   HOH B 576      27.990  15.735 -17.857  1.00 86.73           O  
ANISOU 1934  O   HOH B 576    10637  11500  10818   -348    444   -282       O  
HETATM 1935  O   HOH B 577      -9.434  30.511 -23.618  1.00 37.43           O  
ANISOU 1935  O   HOH B 577     5020   5905   3298    698  -1411    620       O  
HETATM 1936  O   HOH B 578      -0.216  23.431 -38.447  1.00 42.16           O  
ANISOU 1936  O   HOH B 578     5417   4468   6135  -1086   -473  -1426       O  
HETATM 1937  O   HOH B 579      13.837  26.034 -16.417  1.00 58.54           O  
ANISOU 1937  O   HOH B 579     7544   7829   6870   -949   -887   -563       O  
HETATM 1938  O   HOH B 580      13.754  17.287 -18.058  1.00 38.96           O  
ANISOU 1938  O   HOH B 580     5554   5615   3632   1191   -978    194       O  
HETATM 1939  O   HOH B 581       4.281   7.082 -24.531  1.00 50.69           O  
ANISOU 1939  O   HOH B 581     6278   5617   7364    494   -842      1       O  
HETATM 1940  O   HOH B 582      -2.402  10.648 -37.455  1.00 92.59           O  
ANISOU 1940  O   HOH B 582    11562  12054  11564   -365    295   -281       O  
HETATM 1941  O   HOH B 583      15.097  26.784 -14.648  1.00 62.91           O  
ANISOU 1941  O   HOH B 583     7938   7877   8088    478   -788  -1907       O  
HETATM 1942  O   HOH B 584      -0.408  24.208 -28.407  1.00 48.45           O  
ANISOU 1942  O   HOH B 584     6330   4791   7287   1318    -99   1349       O  
HETATM 1943  O   HOH B 585     -17.728  25.080 -11.415  1.00 73.98           O  
ANISOU 1943  O   HOH B 585     9544   9120   9446   -230   1832   1865       O  
HETATM 1944  O   HOH B 586      12.623  32.367 -36.897  1.00 50.85           O  
ANISOU 1944  O   HOH B 586     6476   6561   6285    610   2035   1407       O  
HETATM 1945  O   HOH B 587      27.247  14.770 -28.998  1.00 50.85           O  
ANISOU 1945  O   HOH B 587     6850   6218   6254   -437   1534    -33       O  
HETATM 1946  O   HOH B 588      12.165  29.255 -18.054  1.00 58.37           O  
ANISOU 1946  O   HOH B 588     7461   7776   6941   1022  -2419    -84       O  
MASTER      253    0    2    2   20    0    2    6 1890    2    0   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: April 25th, 2023.